data_6313
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
1H,13C,and 15N NMR assignments of the Bombyx mori Pheromone-binding Protein
fragment BmPBP(1-128) at pH 6.5.
;
_BMRB_accession_number 6313
_BMRB_flat_file_name bmr6313.str
_Entry_type original
_Submission_date 2004-09-03
_Accession_date 2004-09-03
_Entry_origination author
_NMR_STAR_version 2.1.1
_Experimental_method NMR
_Details
;
Spectral analysis and assignment where performed using the program CARA
(www.cara.ch)
;
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Damberger Fred . .
2 Michel Erich . .
3 Wuthrich Kurt . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 770
"13C chemical shifts" 555
"15N chemical shifts" 145
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2005-02-08 original author .
stop_
loop_
_Related_BMRB_accession_number
_Relationship
4849 'Pheromone-binding Protein of Bombyx mori'
stop_
_Original_release_date 2005-02-08
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Letter to the Editor: Assignments for the Bombyx mori pheromone-binding protein
fragment BmPBP(1-128) at pH 6.5
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Michel Erich . .
2 Damberger Fred F. .
3 Chen Angela M. .
4 Ishida Yuko . .
5 Leal Walter S. .
6 Wuthrich Kurt . .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_volume 31
_Journal_issue 1
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 65
_Page_last 65
_Year 2005
_Details .
loop_
_Keyword
'truncation mutant'
'pH-dependent conformation'
'conformational exchange'
CARA
stop_
save_
#######################################
# Cited references within the entry #
#######################################
save_ref_3
_Saveframe_category citation
_Citation_full
;
Herrmann T, Guntert P, Wuthrich K.
J Biomol NMR. 2002 Nov;24(3):171-89.
;
_Citation_title 'Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 12522306
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Herrmann Torsten . .
2 Guntert Peter . .
3 Wuthrich Kurt . .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_name_full 'Journal of biomolecular NMR'
_Journal_volume 24
_Journal_issue 3
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 171
_Page_last 189
_Year 2002
_Details
;
Novel algorithms are presented for automated NOESY peak picking and NOE signal
identification in homonuclear 2D and heteronuclear-resolved 3D
[(1)H,(1)H]-NOESY spectra during de novo protein structure determination by
NMR, which have been implemented in the new software ATNOS (automated NOESY
peak picking). The input for ATNOS consists of the amino acid sequence of the
protein, chemical shift lists from the sequence-specific resonance assignment,
and one or several 2D or 3D NOESY spectra. In the present implementation, ATNOS
performs multiple cycles of NOE peak identification in concert with automated
NOE assignment with the software CANDID and protein structure calculation with
the program DYANA. In the second and subsequent cycles, the intermediate
protein structures are used as an additional guide for the interpretation of
the NOESY spectra. By incorporating the analysis of the raw NMR data into the
process of automated de novo protein NMR structure determination, ATNOS enables
direct feedback between the protein structure, the NOE assignments and the
experimental NOESY spectra. The main elements of the algorithms for NOESY
spectral analysis are techniques for local baseline correction and evaluation
of local noise level amplitudes, automated determination of spectrum-specific
threshold parameters, the use of symmetry relations, and the inclusion of the
chemical shift information and the intermediate protein structures in the
process of distinguishing between NOE peaks and artifacts. The ATNOS procedure
has been validated with experimental NMR data sets of three proteins, for which
high-quality NMR structures had previously been obtained by interactive
interpretation of the NOESY spectra. The ATNOS-based structures coincide
closely with those obtained with interactive peak picking. Overall, we present
the algorithms used in this paper as a further important step towards objective
and efficient de novo protein structure determination by NMR.
;
save_
save_ref_4
_Saveframe_category citation
_Citation_full
;
Herrmann T, Guntert P, Wuthrich K.
J Mol Biol. 2002 May 24;319(1):209-27.
;
_Citation_title 'Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 12051947
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Herrmann Torsten . .
2 Guntert Peter . .
3 Wuthrich Kurt . .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_name_full 'Journal of molecular biology'
_Journal_volume 319
_Journal_issue 1
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 209
_Page_last 227
_Year 2002
_Details
;
Combined automated NOE assignment and structure determination module (CANDID) is
a new software for efficient NMR structure determination of proteins by
automated assignment of the NOESY spectra. CANDID uses an iterative approach
with multiple cycles of NOE cross-peak assignment and protein structure
calculation using the fast DYANA torsion angle dynamics algorithm, so that the
result from each CANDID cycle consists of exhaustive, possibly ambiguous NOE
cross-peak assignments in all available spectra and a three-dimensional protein
structure represented by a bundle of conformers. The input for the first CANDID
cycle consists of the amino acid sequence, the chemical shift list from the
sequence-specific resonance assignment, and listings of the cross-peak
positions and volumes in one or several two, three or four-dimensional NOESY
spectra. The input for the second and subsequent CANDID cycles contains the
three-dimensional protein structure from the previous cycle, in addition to the
complete input used for the first cycle. CANDID includes two new elements that
make it robust with respect to the presence of artifacts in the input data,
i.e. network-anchoring and constraint-combination, which have a key role in de
novo protein structure determinations for the successful generation of the
correct polypeptide fold by the first CANDID cycle. Network-anchoring makes use
of the fact that any network of correct NOE cross-peak assignments forms a
self-consistent set; the initial, chemical shift-based assignments for each
individual NOE cross-peak are therefore weighted by the extent to which they
can be embedded into the network formed by all other NOE cross-peak
assignments. Constraint-combination reduces the deleterious impact of artifact
NOE upper distance constraints in the input for a protein structure calculation
by combining the assignments for two or several peaks into a single upper limit
distance constraint, which lowers the probability that the presence of an
artifact peak will influence the outcome of the structure calculation. CANDID
test calculations were performed with NMR data sets of four proteins for which
high-quality structures had previously been solved by interactive protocols,
and they yielded comparable results to these reference structure determinations
with regard to both the residual constraint violations, and the precision and
accuracy of the atomic coordinates. The CANDID approach has further been
validated by de novo NMR structure determinations of four additional proteins.
The experience gained in these calculations shows that once nearly complete
sequence-specific resonance assignments are available, the automated CANDID
approach results in greatly enhanced efficiency of the NOESY spectral analysis.
The fact that the correct fold is obtained in cycle 1 of a de novo structure
calculation is the single most important advance achieved with CANDID, when
compared with previously proposed automated NOESY assignment methods that do
not use network-anchoring and constraint-combination.
;
save_
save_ref_5
_Saveframe_category citation
_Citation_full
;
Guntert P, Mumenthaler C, Wuthrich K.
J Mol Biol. 1997 Oct 17;273(1):283-98.
;
_Citation_title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 9367762
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Guntert P. . .
2 Mumenthaler C. . .
3 Wuthrich K. . .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_name_full 'Journal of molecular biology'
_Journal_volume 273
_Journal_issue 1
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 283
_Page_last 298
_Year 1997
_Details
;
The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient
calculation of three-dimensional protein and nucleic acid structures from
distance constraints and torsion angle constraints collected by nuclear
magnetic resonance (NMR) experiments performs simulated annealing by molecular
dynamics in torsion angle space and uses a fast recursive algorithm to
integrate the equations of motions. Torsion angle dynamics can be more
efficient than molecular dynamics in Cartesian coordinate space because of the
reduced number of degrees of freedom and the concomitant absence of
high-frequency bond and angle vibrations, which allows for the use of longer
time-steps and/or higher temperatures in the structure calculation. It also
represents a significant advance over the variable target function method in
torsion angle space with the REDAC strategy used by the predecessor program
DIANA. DYANA computation times per accepted conformer in the "bundle" used to
represent the NMR structure compare favorably with those of other presently
available structure calculation algorithms, and are of the order of 160 seconds
for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300
computer. Test calculations starting from conformers with random torsion angle
values further showed that DYANA is capable of efficient calculation of
high-quality protein structures with up to 400 amino acid residues, and of
nucleic acid structures.
;
save_
##################################
# Molecular system description #
##################################
save_system_PBP
_Saveframe_category molecular_system
_Mol_system_name 'Pheromone-binding protein'
_Abbreviation_common PBP
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
BmPBP $BmPBP
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all disulfide bound'
loop_
_Biological_function
'pheromone transport protein'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_BmPBP
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'Bombyx mori Pheromone-binding protein'
_Name_variant BmPBP(1-128)
_Abbreviation_common BmPBP
_Molecular_mass 14467
_Mol_thiol_state 'all disulfide bound'
_Details
;
MW is given for an unlabeled polypeptide and assuming all six cysteines form
disulfides (consistent with biochemical and structural data).
;
##############################
# Polymer residue sequence #
##############################
_Residue_count 128
_Mol_residue_sequence
;
SQEVMKNLSLNFGKALDECK
KEMTLTDAINEDFYNFWKEG
YEIKNRETGCAIMCLSTKLN
MLDPEGNLHHGNAMEFAKKH
GADETMAQQLIDIVHGCEKS
TPANDDKCIWTLGVATCFKA
EIHKLNWA
;
loop_
_Residue_seq_code
_Residue_label
1 SER 2 GLN 3 GLU 4 VAL 5 MET
6 LYS 7 ASN 8 LEU 9 SER 10 LEU
11 ASN 12 PHE 13 GLY 14 LYS 15 ALA
16 LEU 17 ASP 18 GLU 19 CYS 20 LYS
21 LYS 22 GLU 23 MET 24 THR 25 LEU
26 THR 27 ASP 28 ALA 29 ILE 30 ASN
31 GLU 32 ASP 33 PHE 34 TYR 35 ASN
36 PHE 37 TRP 38 LYS 39 GLU 40 GLY
41 TYR 42 GLU 43 ILE 44 LYS 45 ASN
46 ARG 47 GLU 48 THR 49 GLY 50 CYS
51 ALA 52 ILE 53 MET 54 CYS 55 LEU
56 SER 57 THR 58 LYS 59 LEU 60 ASN
61 MET 62 LEU 63 ASP 64 PRO 65 GLU
66 GLY 67 ASN 68 LEU 69 HIS 70 HIS
71 GLY 72 ASN 73 ALA 74 MET 75 GLU
76 PHE 77 ALA 78 LYS 79 LYS 80 HIS
81 GLY 82 ALA 83 ASP 84 GLU 85 THR
86 MET 87 ALA 88 GLN 89 GLN 90 LEU
91 ILE 92 ASP 93 ILE 94 VAL 95 HIS
96 GLY 97 CYS 98 GLU 99 LYS 100 SER
101 THR 102 PRO 103 ALA 104 ASN 105 ASP
106 ASP 107 LYS 108 CYS 109 ILE 110 TRP
111 THR 112 LEU 113 GLY 114 VAL 115 ALA
116 THR 117 CYS 118 PHE 119 LYS 120 ALA
121 GLU 122 ILE 123 HIS 124 LYS 125 LEU
126 ASN 127 TRP 128 ALA
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 4849 BmPBP 100.00 142 100.00 100.00 1.85e-89
PDB 1DQE "Bombyx Mori Pheromone Binding Protein" 100.00 137 100.00 100.00 3.44e-89
PDB 1GM0 "A Form Of The Pheromone-Binding Protein From Bombyx Mori" 99.22 142 100.00 100.00 1.57e-88
PDB 1LS8 "Nmr Structure Of The Unliganded Bombyx Mori Pheromone- Binding Protein At Physiological Ph" 99.22 142 100.00 100.00 1.57e-88
PDB 1XFR "Solution Structure Of The Bombyx Mori Pheromone-Binding Protein Fragment Bmpbp(1-128) At Ph 6.5" 100.00 128 100.00 100.00 5.74e-89
PDB 2FJY "Crystal Structure Of B-Form Bombyx Mori Pheromone Binding Protein" 100.00 142 100.00 100.00 1.85e-89
PDB 2P70 "Bombyx Mori Pheromone Binding Protein Bound To Bell Pepper Odorant" 100.00 132 100.00 100.00 3.63e-89
PDB 2P71 "Bombyx Mori Pheromone Binding Protein Bound To Iodohexadecane" 100.00 132 100.00 100.00 3.63e-89
EMBL CAA64443 "Pheromone binding protein [Bombyx mori]" 100.00 164 100.00 100.00 5.61e-90
GB ACT34881 "pheromone-binding protein 1 [Bombyx mandarina]" 100.00 164 100.00 100.00 5.73e-90
GB AGR44744 "pheromone binding protein-1 [Bombyx mori]" 102.34 167 96.95 96.95 8.15e-87
GB AGR44745 "pheromone binding protein-1 [Bombyx mori]" 102.34 167 97.71 97.71 7.15e-88
GB AGR44746 "pheromone binding protein-1 [Bombyx mori]" 102.34 167 96.95 96.95 3.40e-87
GB AGR44747 "pheromone binding protein-1 [Bombyx mori]" 102.34 167 96.95 96.95 8.15e-87
REF NP_001037494 "pheromone-binding protein precursor [Bombyx mori]" 100.00 164 100.00 100.00 5.61e-90
SP P34174 "RecName: Full=Pheromone-binding protein; Short=PBP; Flags: Precursor [Bombyx mori]" 100.00 164 100.00 100.00 5.61e-90
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Organ
_Tissue
_Fraction
$BmPBP 'silkworm moth' 7091 Eukaryota Metazoa Bombyx mori antennae 'sensillum lymph' sensillum
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
$BmPBP 'recombinant technology' 'E. coli' Escherichia coli BL21 plasmid .
;
Cells were grown on minimal media with NH4Cl and glucose as 15N and 13C sources
respectively.
;
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
$BmPBP 1.1 mM '[U-99% 13C; U-98% 15N]'
'potassium phosphate buffer' 50 mM .
H2O 95 % .
D2O 5 % .
NaN3 0.2 % .
stop_
save_
############################
# Computer software used #
############################
save_CARA
_Saveframe_category software
_Name CARA
_Version 1.1
loop_
_Task
'computer-aided resonance assignment'
stop_
_Details
;
www.nmr.ch
in-house developed software available at www.nmr.ch
;
save_
save_ATNOS
_Saveframe_category software
_Name ATNOS
_Version .
loop_
_Task
'automated peak-picking'
integration
stop_
_Details 'in-house developed software'
_Citation_label $ref_3
save_
save_CANDID
_Saveframe_category software
_Name CANDID
_Version .
loop_
_Task
'automated NOE crosspeak assignment for structure calculation'
stop_
_Details 'in-house developed software'
_Citation_label $ref_4
save_
save_DYANA
_Saveframe_category software
_Name DYANA
_Version .
loop_
_Task
'automated structure calculation using NMR constraints'
stop_
_Details 'in-house developed software'
_Citation_label $ref_5
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 500
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 900
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_HNCA_1
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_Sample_label $sample_1
save_
save_CBCA(CO)NH_2
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCA(CO)NH
_Sample_label $sample_1
save_
save_HNCACB_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_Sample_label $sample_1
save_
save_HNCO_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_Sample_label $sample_1
save_
save_HN(CA)CO_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CA)CO
_Sample_label $sample_1
save_
save_(H)CCH-COSY_6
_Saveframe_category NMR_applied_experiment
_Experiment_name (H)CCH-COSY
_Sample_label $sample_1
save_
save_15N-resolved_[1H,1H]-TOCSY_7
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N-resolved [1H,1H]-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-resolved_[1H,1H]-NOESY_9
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N-resolved [1H,1H]-NOESY'
_Sample_label $sample_1
save_
save_13C(aliphatic)-resolved_[1H,1H]-NOESY_10
_Saveframe_category NMR_applied_experiment
_Experiment_name '13C(aliphatic)-resolved [1H,1H]-NOESY'
_Sample_label $sample_1
save_
save_13C(aromatic)-resolved_[1H,1H]-NOESY_11
_Saveframe_category NMR_applied_experiment
_Experiment_name '13C(aromatic)-resolved [1H,1H]-NOESY'
_Sample_label $sample_1
save_
#######################
# Sample conditions #
#######################
save_Ex-cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.5 0.05 n/a
temperature 293 0.3 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference
_Saveframe_category chemical_shift_reference
_Details .
loop_
_Mol_common_name
_Atom_type
_Atom_isotope_number
_Atom_group
_Chem_shift_units
_Chem_shift_value
_Reference_method
_Reference_type
_External_reference_sample_geometry
_External_reference_location
_External_reference_axis
_Indirect_shift_ratio
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_BmPBP_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $Ex-cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name BmPBP
_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 SER CA C 56.6 0.4 1
2 . 1 SER HA H 3.25 0.025 1
3 . 1 SER CB C 65.6 0.4 1
4 . 1 SER HB2 H 3.81 0.025 2
5 . 1 SER HB3 H 3.33 0.025 2
6 . 2 GLN CA C 57.6 0.4 1
7 . 2 GLN HA H 4.21 0.025 1
8 . 2 GLN CB C 27.9 0.4 1
9 . 2 GLN HB2 H 1.92 0.025 1
10 . 2 GLN HB3 H 1.92 0.025 1
11 . 2 GLN CG C 33.3 0.4 1
12 . 2 GLN HG2 H 2.40 0.025 2
13 . 2 GLN HG3 H 2.15 0.025 2
14 . 2 GLN NE2 N 110.2 0.4 1
15 . 2 GLN HE21 H 7.24 0.025 2
16 . 2 GLN HE22 H 6.71 0.025 2
17 . 2 GLN C C 179.5 0.4 1
18 . 3 GLU N N 119.4 0.4 1
19 . 3 GLU H H 8.49 0.025 1
20 . 3 GLU CA C 59.1 0.4 1
21 . 3 GLU HA H 3.87 0.025 1
22 . 3 GLU CB C 28.9 0.4 1
23 . 3 GLU HB2 H 1.92 0.025 2
24 . 3 GLU HB3 H 1.83 0.025 2
25 . 3 GLU CG C 35.8 0.4 1
26 . 3 GLU HG2 H 2.20 0.025 1
27 . 3 GLU HG3 H 2.20 0.025 1
28 . 3 GLU C C 178.9 0.4 1
29 . 4 VAL N N 120.0 0.4 1
30 . 4 VAL H H 7.48 0.025 1
31 . 4 VAL CA C 65.6 0.4 1
32 . 4 VAL HA H 3.67 0.025 1
33 . 4 VAL CB C 31.3 0.4 1
34 . 4 VAL HB H 1.55 0.025 1
35 . 4 VAL HG1 H 0.68 0.025 2
36 . 4 VAL HG2 H 0.80 0.025 2
37 . 4 VAL CG1 C 20.4 0.4 1
38 . 4 VAL CG2 C 22.3 0.4 1
39 . 4 VAL C C 178.2 0.4 1
40 . 5 MET N N 118.0 0.4 1
41 . 5 MET H H 8.09 0.025 1
42 . 5 MET CA C 56.2 0.4 1
43 . 5 MET HA H 4.33 0.025 1
44 . 5 MET CB C 29.4 0.4 1
45 . 5 MET HB2 H 1.67 0.025 2
46 . 5 MET HB3 H 1.86 0.025 2
47 . 5 MET CG C 31.6 0.4 1
48 . 5 MET HG2 H 2.35 0.025 2
49 . 5 MET HG3 H 2.16 0.025 2
50 . 5 MET HE H 2.01 0.025 1
51 . 5 MET CE C 16.4 0.4 1
52 . 5 MET C C 179.4 0.4 1
53 . 6 LYS N N 120.2 0.4 1
54 . 6 LYS H H 8.01 0.025 1
55 . 6 LYS CA C 59.2 0.4 1
56 . 6 LYS HA H 4.00 0.025 1
57 . 6 LYS CB C 31.7 0.4 1
58 . 6 LYS HB2 H 1.84 0.025 1
59 . 6 LYS HB3 H 1.84 0.025 1
60 . 6 LYS C C 178.9 0.4 1
61 . 7 ASN N N 119.3 0.4 1
62 . 7 ASN H H 7.68 0.025 1
63 . 7 ASN CA C 56.1 0.4 1
64 . 7 ASN HA H 4.58 0.025 1
65 . 7 ASN CB C 38.7 0.4 1
66 . 7 ASN HB2 H 2.92 0.025 1
67 . 7 ASN HB3 H 2.92 0.025 1
68 . 7 ASN ND2 N 114.6 0.4 1
69 . 7 ASN HD21 H 7.86 0.025 2
70 . 7 ASN HD22 H 7.32 0.025 2
71 . 7 ASN C C 179.5 0.4 1
72 . 8 LEU N N 122.2 0.4 1
73 . 8 LEU H H 9.20 0.025 1
74 . 8 LEU CA C 58.5 0.4 1
75 . 8 LEU HA H 3.87 0.025 1
76 . 8 LEU CB C 41.2 0.4 1
77 . 8 LEU HB2 H 2.17 0.025 2
78 . 8 LEU HB3 H 1.44 0.025 2
79 . 8 LEU CG C 26.6 0.4 1
80 . 8 LEU HG H 1.92 0.025 1
81 . 8 LEU HD1 H 0.87 0.025 2
82 . 8 LEU HD2 H 0.83 0.025 2
83 . 8 LEU CD1 C 26.6 0.4 1
84 . 8 LEU CD2 C 25.0 0.4 1
85 . 8 LEU C C 178.6 0.4 1
86 . 9 SER N N 114.5 0.4 1
87 . 9 SER H H 8.43 0.025 1
88 . 9 SER CA C 62.5 0.4 1
89 . 9 SER HA H 4.08 0.025 1
90 . 9 SER CB C 63.1 0.4 1
91 . 9 SER HB2 H 4.32 0.025 1
92 . 9 SER HB3 H 4.32 0.025 1
93 . 9 SER C C 175.0 0.4 1
94 . 10 LEU N N 122.2 0.4 1
95 . 10 LEU H H 8.16 0.025 1
96 . 10 LEU CA C 57.5 0.4 1
97 . 10 LEU HA H 4.15 0.025 1
98 . 10 LEU CB C 42.0 0.4 1
99 . 10 LEU HB2 H 1.82 0.025 2
100 . 10 LEU HB3 H 1.72 0.025 2
101 . 10 LEU CG C 26.7 0.4 1
102 . 10 LEU HG H 1.56 0.025 1
103 . 10 LEU HD1 H 0.89 0.025 1
104 . 10 LEU HD2 H 0.89 0.025 1
105 . 10 LEU CD1 C 24.2 0.4 1
106 . 10 LEU CD2 C 24.1 0.4 1
107 . 10 LEU C C 179.7 0.4 1
108 . 11 ASN N N 115.0 0.4 1
109 . 11 ASN H H 7.57 0.025 1
110 . 11 ASN CA C 56.9 0.4 1
111 . 11 ASN HA H 4.26 0.025 1
112 . 11 ASN CB C 38.7 0.4 1
113 . 11 ASN HB2 H 2.07 0.025 2
114 . 11 ASN HB3 H 1.91 0.025 2
115 . 11 ASN ND2 N 115.3 0.4 1
116 . 11 ASN HD21 H 7.42 0.025 2
117 . 11 ASN HD22 H 7.07 0.025 2
118 . 11 ASN C C 176.9 0.4 1
119 . 12 PHE N N 123.3 0.4 1
120 . 12 PHE H H 9.02 0.025 1
121 . 12 PHE CA C 60.9 0.4 1
122 . 12 PHE HA H 4.07 0.025 1
123 . 12 PHE CB C 40.0 0.4 1
124 . 12 PHE HB2 H 3.05 0.025 2
125 . 12 PHE HB3 H 3.23 0.025 2
126 . 12 PHE HD1 H 6.65 0.025 1
127 . 12 PHE HD2 H 6.65 0.025 1
128 . 12 PHE HE1 H 6.90 0.025 1
129 . 12 PHE HE2 H 6.90 0.025 1
130 . 12 PHE CD1 C 132.6 0.4 1
131 . 12 PHE CE1 C 131.2 0.4 1
132 . 12 PHE CZ C 131.4 0.4 1
133 . 12 PHE HZ H 7.28 0.025 1
134 . 12 PHE C C 175.6 0.4 1
135 . 13 GLY N N 99.1 0.4 1
136 . 13 GLY H H 7.43 0.025 1
137 . 13 GLY CA C 44.9 0.4 1
138 . 13 GLY HA2 H 3.67 0.025 2
139 . 13 GLY HA3 H 3.93 0.025 2
140 . 13 GLY C C 175.3 0.4 1
141 . 14 LYS N N 121.4 0.4 1
142 . 14 LYS H H 6.92 0.025 1
143 . 14 LYS CA C 59.5 0.4 1
144 . 14 LYS HA H 3.94 0.025 1
145 . 14 LYS CB C 32.2 0.4 1
146 . 14 LYS HB2 H 1.90 0.025 2
147 . 14 LYS HB3 H 1.83 0.025 2
148 . 14 LYS CG C 24.9 0.4 1
149 . 14 LYS HG2 H 1.65 0.025 2
150 . 14 LYS HG3 H 1.50 0.025 2
151 . 14 LYS CD C 28.8 0.4 1
152 . 14 LYS HD2 H 1.70 0.025 1
153 . 14 LYS HD3 H 1.70 0.025 1
154 . 14 LYS CE C 41.6 0.4 1
155 . 14 LYS HE2 H 2.88 0.025 2
156 . 14 LYS HE3 H 2.80 0.025 2
157 . 14 LYS C C 177.8 0.4 1
158 . 15 ALA N N 119.0 0.4 1
159 . 15 ALA H H 8.10 0.025 1
160 . 15 ALA CA C 51.3 0.4 1
161 . 15 ALA HA H 4.67 0.025 1
162 . 15 ALA HB H 1.22 0.025 1
163 . 15 ALA CB C 16.8 0.4 1
164 . 15 ALA C C 176.9 0.4 1
165 . 16 LEU N N 121.3 0.4 1
166 . 16 LEU H H 7.37 0.025 1
167 . 16 LEU CA C 59.1 0.4 1
168 . 16 LEU HA H 3.37 0.025 1
169 . 16 LEU CB C 41.0 0.4 1
170 . 16 LEU HB2 H 1.27 0.025 2
171 . 16 LEU HB3 H 1.57 0.025 2
172 . 16 LEU CG C 26.2 0.4 1
173 . 16 LEU HG H 1.20 0.025 1
174 . 16 LEU HD1 H 0.24 0.025 2
175 . 16 LEU HD2 H 0.35 0.025 2
176 . 16 LEU CD1 C 22.9 0.4 1
177 . 16 LEU CD2 C 24.7 0.4 1
178 . 16 LEU C C 177.6 0.4 1
179 . 17 ASP N N 117.1 0.4 1
180 . 17 ASP H H 8.80 0.025 1
181 . 17 ASP CA C 57.4 0.4 1
182 . 17 ASP HA H 4.21 0.025 1
183 . 17 ASP CB C 39.4 0.4 1
184 . 17 ASP HB2 H 2.51 0.025 2
185 . 17 ASP HB3 H 2.57 0.025 2
186 . 17 ASP C C 178.9 0.4 1
187 . 18 GLU N N 120.4 0.4 1
188 . 18 GLU H H 7.63 0.025 1
189 . 18 GLU CA C 58.9 0.4 1
190 . 18 GLU HA H 4.00 0.025 1
191 . 18 GLU CB C 29.1 0.4 1
192 . 18 GLU HB2 H 2.06 0.025 2
193 . 18 GLU HB3 H 1.96 0.025 2
194 . 18 GLU CG C 35.7 0.4 1
195 . 18 GLU HG2 H 2.26 0.025 2
196 . 18 GLU HG3 H 2.11 0.025 2
197 . 18 GLU C C 178.9 0.4 1
198 . 19 CYS N N 117.1 0.4 1
199 . 19 CYS H H 7.85 0.025 1
200 . 19 CYS CA C 59.4 0.4 1
201 . 19 CYS HA H 4.16 0.025 1
202 . 19 CYS CB C 41.0 0.4 1
203 . 19 CYS HB2 H 3.05 0.025 2
204 . 19 CYS HB3 H 2.51 0.025 2
205 . 19 CYS C C 176.0 0.4 1
206 . 20 LYS N N 119.2 0.4 1
207 . 20 LYS H H 8.72 0.025 1
208 . 20 LYS CA C 60.0 0.4 1
209 . 20 LYS HA H 3.62 0.025 1
210 . 20 LYS CB C 32.2 0.4 1
211 . 20 LYS HB2 H 1.93 0.025 2
212 . 20 LYS HB3 H 1.78 0.025 2
213 . 20 LYS CG C 25.3 0.4 1
214 . 20 LYS HG2 H 1.20 0.025 2
215 . 20 LYS HG3 H 1.42 0.025 2
216 . 20 LYS CD C 29.6 0.4 1
217 . 20 LYS HD2 H 1.58 0.025 2
218 . 20 LYS HD3 H 1.56 0.025 2
219 . 20 LYS CE C 41.3 0.4 1
220 . 20 LYS HE2 H 2.79 0.025 2
221 . 20 LYS HE3 H 2.72 0.025 2
222 . 20 LYS C C 178.3 0.4 1
223 . 21 LYS N N 116.9 0.4 1
224 . 21 LYS H H 7.50 0.025 1
225 . 21 LYS CA C 58.3 0.4 1
226 . 21 LYS HA H 4.09 0.025 1
227 . 21 LYS CB C 32.2 0.4 1
228 . 21 LYS HB2 H 1.89 0.025 1
229 . 21 LYS HB3 H 1.89 0.025 1
230 . 21 LYS CG C 24.6 0.4 1
231 . 21 LYS HG2 H 1.49 0.025 2
232 . 21 LYS HG3 H 1.38 0.025 2
233 . 21 LYS CD C 28.7 0.4 1
234 . 21 LYS HD2 H 1.63 0.025 1
235 . 21 LYS HD3 H 1.63 0.025 1
236 . 21 LYS CE C 41.6 0.4 1
237 . 21 LYS HE2 H 2.91 0.025 2
238 . 21 LYS HE3 H 2.81 0.025 2
239 . 21 LYS C C 179.6 0.4 1
240 . 22 GLU N N 118.8 0.4 1
241 . 22 GLU H H 8.51 0.025 1
242 . 22 GLU CA C 58.8 0.4 1
243 . 22 GLU HA H 3.96 0.025 1
244 . 22 GLU CB C 30.2 0.4 1
245 . 22 GLU HB2 H 2.06 0.025 2
246 . 22 GLU HB3 H 1.97 0.025 2
247 . 22 GLU CG C 35.9 0.4 1
248 . 22 GLU HG2 H 2.21 0.025 2
249 . 22 GLU HG3 H 2.41 0.025 2
250 . 22 GLU C C 178.5 0.4 1
251 . 23 MET N N 113.2 0.4 1
252 . 23 MET H H 7.91 0.025 1
253 . 23 MET CA C 54.9 0.4 1
254 . 23 MET HA H 4.52 0.025 1
255 . 23 MET CB C 32.7 0.4 1
256 . 23 MET HB2 H 1.79 0.025 2
257 . 23 MET HB3 H 2.28 0.025 2
258 . 23 MET CG C 33.0 0.4 1
259 . 23 MET HG2 H 2.45 0.025 2
260 . 23 MET HG3 H 2.64 0.025 2
261 . 23 MET HE H 2.04 0.025 1
262 . 23 MET CE C 17.2 0.4 1
263 . 23 MET C C 174.3 0.4 1
264 . 24 THR N N 114.9 0.4 1
265 . 24 THR H H 7.43 0.025 1
266 . 24 THR CA C 62.0 0.4 1
267 . 24 THR HA H 3.80 0.025 1
268 . 24 THR CB C 67.1 0.4 1
269 . 24 THR HB H 4.39 0.025 1
270 . 24 THR HG2 H 1.19 0.025 1
271 . 24 THR CG2 C 22.2 0.4 1
272 . 24 THR C C 173.7 0.4 1
273 . 25 LEU N N 119.2 0.4 1
274 . 25 LEU H H 8.34 0.025 1
275 . 25 LEU CA C 52.6 0.4 1
276 . 25 LEU HA H 4.69 0.025 1
277 . 25 LEU CB C 42.3 0.4 1
278 . 25 LEU HB2 H 1.61 0.025 2
279 . 25 LEU HB3 H 1.58 0.025 2
280 . 25 LEU CG C 26.6 0.4 1
281 . 25 LEU HG H 1.58 0.025 1
282 . 25 LEU HD1 H 0.74 0.025 2
283 . 25 LEU HD2 H 0.79 0.025 2
284 . 25 LEU CD1 C 24.9 0.4 1
285 . 25 LEU CD2 C 21.7 0.4 1
286 . 25 LEU C C 177.0 0.4 1
287 . 26 THR N N 113.6 0.4 1
288 . 26 THR H H 9.30 0.025 1
289 . 26 THR CA C 60.7 0.4 1
290 . 26 THR HA H 4.47 0.025 1
291 . 26 THR CB C 71.0 0.4 1
292 . 26 THR HB H 4.53 0.025 1
293 . 26 THR HG2 H 1.38 0.025 1
294 . 26 THR CG2 C 20.8 0.4 1
295 . 26 THR C C 174.1 0.4 1
296 . 27 ASP N N 116.4 0.4 1
297 . 27 ASP H H 8.43 0.025 1
298 . 27 ASP CA C 55.5 0.4 1
299 . 27 ASP HA H 4.29 0.025 1
300 . 27 ASP CB C 39.8 0.4 1
301 . 27 ASP HB2 H 2.55 0.025 2
302 . 27 ASP HB3 H 2.83 0.025 2
303 . 27 ASP C C 177.4 0.4 1
304 . 28 ALA N N 124.3 0.4 1
305 . 28 ALA H H 8.23 0.025 1
306 . 28 ALA CA C 54.6 0.4 1
307 . 28 ALA HA H 4.12 0.025 1
308 . 28 ALA HB H 1.32 0.025 1
309 . 28 ALA CB C 17.9 0.4 1
310 . 28 ALA C C 179.8 0.4 1
311 . 29 ILE N N 108.0 0.4 1
312 . 29 ILE H H 7.11 0.025 1
313 . 29 ILE CA C 63.0 0.4 1
314 . 29 ILE HA H 4.16 0.025 1
315 . 29 ILE CB C 37.6 0.4 1
316 . 29 ILE HB H 2.24 0.025 1
317 . 29 ILE HG2 H 0.94 0.025 1
318 . 29 ILE CG2 C 18.0 0.4 1
319 . 29 ILE CG1 C 24.1 0.4 1
320 . 29 ILE HG12 H 1.27 0.025 2
321 . 29 ILE HG13 H 1.57 0.025 2
322 . 29 ILE HD1 H 0.76 0.025 1
323 . 29 ILE CD1 C 15.6 0.4 1
324 . 29 ILE C C 177.4 0.4 1
325 . 30 ASN N N 120.9 0.4 1
326 . 30 ASN H H 7.79 0.025 1
327 . 30 ASN CA C 56.4 0.4 1
328 . 30 ASN HA H 4.14 0.025 1
329 . 30 ASN CB C 36.7 0.4 1
330 . 30 ASN HB2 H 2.86 0.025 2
331 . 30 ASN HB3 H 2.62 0.025 2
332 . 30 ASN ND2 N 110.1 0.4 1
333 . 30 ASN HD21 H 7.54 0.025 2
334 . 30 ASN HD22 H 7.09 0.025 2
335 . 30 ASN C C 177.6 0.4 1
336 . 31 GLU N N 118.3 0.4 1
337 . 31 GLU H H 7.73 0.025 1
338 . 31 GLU CA C 58.8 0.4 1
339 . 31 GLU HA H 3.99 0.025 1
340 . 31 GLU CB C 29.6 0.4 1
341 . 31 GLU HB2 H 2.05 0.025 1
342 . 31 GLU HB3 H 2.05 0.025 1
343 . 31 GLU CG C 35.6 0.4 1
344 . 31 GLU HG2 H 2.27 0.025 2
345 . 31 GLU HG3 H 2.39 0.025 2
346 . 31 GLU C C 178.3 0.4 1
347 . 32 ASP N N 118.3 0.4 1
348 . 32 ASP H H 7.29 0.025 1
349 . 32 ASP CA C 56.5 0.4 1
350 . 32 ASP HA H 4.51 0.025 1
351 . 32 ASP CB C 40.6 0.4 1
352 . 32 ASP HB2 H 3.08 0.025 2
353 . 32 ASP HB3 H 2.39 0.025 2
354 . 32 ASP C C 176.8 0.4 1
355 . 33 PHE N N 114.9 0.4 1
356 . 33 PHE H H 7.73 0.025 1
357 . 33 PHE CA C 62.6 0.4 1
358 . 33 PHE HA H 4.04 0.025 1
359 . 33 PHE CB C 38.4 0.4 1
360 . 33 PHE HB2 H 2.88 0.025 2
361 . 33 PHE HB3 H 3.01 0.025 2
362 . 33 PHE HD1 H 7.22 0.025 1
363 . 33 PHE HD2 H 7.22 0.025 1
364 . 33 PHE HE1 H 6.99 0.025 1
365 . 33 PHE HE2 H 6.99 0.025 1
366 . 33 PHE CD1 C 132.2 0.4 1
367 . 33 PHE CE1 C 131.1 0.4 1
368 . 33 PHE CZ C 129.3 0.4 1
369 . 33 PHE HZ H 7.01 0.025 1
370 . 33 PHE C C 179.1 0.4 1
371 . 34 TYR N N 119.6 0.4 1
372 . 34 TYR H H 8.49 0.025 1
373 . 34 TYR CA C 60.0 0.4 1
374 . 34 TYR HA H 4.34 0.025 1
375 . 34 TYR CB C 37.5 0.4 1
376 . 34 TYR HB2 H 3.08 0.025 2
377 . 34 TYR HB3 H 2.97 0.025 2
378 . 34 TYR HD1 H 7.04 0.025 1
379 . 34 TYR HD2 H 7.04 0.025 1
380 . 34 TYR HE1 H 6.77 0.025 1
381 . 34 TYR HE2 H 6.77 0.025 1
382 . 34 TYR CD1 C 133.5 0.4 1
383 . 34 TYR CE1 C 118.5 0.4 1
384 . 34 TYR C C 177.9 0.4 1
385 . 35 ASN N N 113.7 0.4 1
386 . 35 ASN H H 7.43 0.025 1
387 . 35 ASN CA C 52.7 0.4 1
388 . 35 ASN HA H 4.45 0.025 1
389 . 35 ASN CB C 37.7 0.4 1
390 . 35 ASN HB2 H 1.76 0.025 2
391 . 35 ASN HB3 H 1.39 0.025 2
392 . 35 ASN ND2 N 115.4 0.4 1
393 . 35 ASN HD21 H 6.95 0.025 2
394 . 35 ASN HD22 H 7.22 0.025 2
395 . 35 ASN C C 174.3 0.4 1
396 . 36 PHE N N 120.7 0.4 1
397 . 36 PHE H H 6.88 0.025 1
398 . 36 PHE CA C 62.7 0.4 1
399 . 36 PHE HA H 3.37 0.025 1
400 . 36 PHE CB C 40.0 0.4 1
401 . 36 PHE HB2 H 3.12 0.025 2
402 . 36 PHE HB3 H 2.15 0.025 2
403 . 36 PHE HD1 H 5.47 0.025 1
404 . 36 PHE HD2 H 5.47 0.025 1
405 . 36 PHE HE1 H 6.12 0.025 1
406 . 36 PHE HE2 H 6.12 0.025 1
407 . 36 PHE CD1 C 132.1 0.4 1
408 . 36 PHE CE1 C 130.1 0.4 1
409 . 36 PHE CZ C 128.8 0.4 1
410 . 36 PHE HZ H 6.69 0.025 1
411 . 36 PHE C C 176.1 0.4 1
412 . 37 TRP N N 112.0 0.4 1
413 . 37 TRP H H 8.35 0.025 1
414 . 37 TRP CA C 55.3 0.4 1
415 . 37 TRP HA H 4.69 0.025 1
416 . 37 TRP CB C 29.1 0.4 1
417 . 37 TRP HB2 H 3.77 0.025 2
418 . 37 TRP HB3 H 2.91 0.025 2
419 . 37 TRP CD1 C 128.5 0.4 1
420 . 37 TRP CE3 C 122.2 0.4 1
421 . 37 TRP NE1 N 127.2 0.4 1
422 . 37 TRP HD1 H 7.37 0.025 1
423 . 37 TRP HE3 H 7.38 0.025 1
424 . 37 TRP CZ3 C 122.1 0.4 1
425 . 37 TRP CZ2 C 114.7 0.4 1
426 . 37 TRP HE1 H 9.95 0.025 1
427 . 37 TRP HZ3 H 6.90 0.025 1
428 . 37 TRP CH2 C 123.9 0.4 1
429 . 37 TRP HZ2 H 7.30 0.025 1
430 . 37 TRP HH2 H 6.92 0.025 1
431 . 37 TRP C C 175.6 0.4 1
432 . 38 LYS N N 122.3 0.4 1
433 . 38 LYS H H 7.83 0.025 1
434 . 38 LYS CA C 56.3 0.4 1
435 . 38 LYS HA H 4.19 0.025 1
436 . 38 LYS CB C 32.0 0.4 1
437 . 38 LYS HB2 H 1.82 0.025 2
438 . 38 LYS HB3 H 1.72 0.025 2
439 . 38 LYS CG C 24.6 0.4 1
440 . 38 LYS HG2 H 1.42 0.025 2
441 . 38 LYS HG3 H 1.31 0.025 2
442 . 38 LYS CD C 29.0 0.4 1
443 . 38 LYS HD2 H 1.60 0.025 1
444 . 38 LYS HD3 H 1.60 0.025 1
445 . 38 LYS CE C 41.9 0.4 1
446 . 38 LYS HE2 H 2.97 0.025 1
447 . 38 LYS HE3 H 2.97 0.025 1
448 . 38 LYS C C 178.0 0.4 1
449 . 39 GLU N N 131.7 0.4 1
450 . 39 GLU H H 9.25 0.025 1
451 . 39 GLU CA C 57.9 0.4 1
452 . 39 GLU HA H 3.71 0.025 1
453 . 39 GLU CB C 28.7 0.4 1
454 . 39 GLU HB2 H 1.82 0.025 1
455 . 39 GLU HB3 H 1.82 0.025 1
456 . 39 GLU CG C 35.4 0.4 1
457 . 39 GLU HG2 H 1.96 0.025 2
458 . 39 GLU HG3 H 2.02 0.025 2
459 . 39 GLU C C 177.4 0.4 1
460 . 40 GLY N N 114.3 0.4 1
461 . 40 GLY H H 9.01 0.025 1
462 . 40 GLY CA C 44.9 0.4 1
463 . 40 GLY HA2 H 4.01 0.025 2
464 . 40 GLY HA3 H 3.58 0.025 2
465 . 40 GLY C C 173.2 0.4 1
466 . 41 TYR N N 121.9 0.4 1
467 . 41 TYR H H 7.42 0.025 1
468 . 41 TYR CA C 58.3 0.4 1
469 . 41 TYR HA H 4.16 0.025 1
470 . 41 TYR CB C 39.6 0.4 1
471 . 41 TYR HB2 H 2.55 0.025 2
472 . 41 TYR HB3 H 2.79 0.025 2
473 . 41 TYR HD1 H 6.71 0.025 1
474 . 41 TYR HD2 H 6.71 0.025 1
475 . 41 TYR HE1 H 6.66 0.025 1
476 . 41 TYR HE2 H 6.66 0.025 1
477 . 41 TYR CD1 C 134.0 0.4 1
478 . 41 TYR CE1 C 118.2 0.4 1
479 . 41 TYR C C 174.4 0.4 1
480 . 42 GLU N N 128.9 0.4 1
481 . 42 GLU H H 7.69 0.025 1
482 . 42 GLU CA C 54.2 0.4 1
483 . 42 GLU HA H 4.16 0.025 1
484 . 42 GLU CB C 30.6 0.4 1
485 . 42 GLU HB2 H 1.50 0.025 2
486 . 42 GLU HB3 H 1.55 0.025 2
487 . 42 GLU CG C 35.4 0.4 1
488 . 42 GLU HG2 H 1.78 0.025 2
489 . 42 GLU HG3 H 2.02 0.025 2
490 . 42 GLU C C 173.9 0.4 1
491 . 43 ILE N N 124.4 0.4 1
492 . 43 ILE H H 8.21 0.025 1
493 . 43 ILE CA C 61.0 0.4 1
494 . 43 ILE HA H 3.78 0.025 1
495 . 43 ILE CB C 36.8 0.4 1
496 . 43 ILE HB H 1.51 0.025 1
497 . 43 ILE HG2 H 0.72 0.025 1
498 . 43 ILE CG2 C 18.8 0.4 1
499 . 43 ILE CG1 C 27.2 0.4 1
500 . 43 ILE HG12 H 0.85 0.025 2
501 . 43 ILE HG13 H 1.42 0.025 2
502 . 43 ILE HD1 H 0.42 0.025 1
503 . 43 ILE CD1 C 13.6 0.4 1
504 . 43 ILE C C 175.6 0.4 1
505 . 44 LYS N N 124.5 0.4 1
506 . 44 LYS H H 9.03 0.025 1
507 . 44 LYS CA C 55.8 0.4 1
508 . 44 LYS HA H 4.32 0.025 1
509 . 44 LYS CB C 34.4 0.4 1
510 . 44 LYS HB2 H 1.57 0.025 2
511 . 44 LYS HB3 H 1.72 0.025 2
512 . 44 LYS CG C 24.0 0.4 1
513 . 44 LYS HG2 H 1.16 0.025 1
514 . 44 LYS HG3 H 1.16 0.025 1
515 . 44 LYS CD C 28.5 0.4 1
516 . 44 LYS HD2 H 1.49 0.025 1
517 . 44 LYS HD3 H 1.49 0.025 1
518 . 44 LYS CE C 41.5 0.4 1
519 . 44 LYS HE2 H 2.80 0.025 1
520 . 44 LYS HE3 H 2.80 0.025 1
521 . 44 LYS C C 176.1 0.4 1
522 . 45 ASN N N 118.3 0.4 1
523 . 45 ASN H H 7.56 0.025 1
524 . 45 ASN CA C 53.0 0.4 1
525 . 45 ASN HA H 4.66 0.025 1
526 . 45 ASN CB C 38.6 0.4 1
527 . 45 ASN HB2 H 2.92 0.025 1
528 . 45 ASN HB3 H 2.92 0.025 1
529 . 45 ASN ND2 N 115.8 0.4 1
530 . 45 ASN HD21 H 8.19 0.025 2
531 . 45 ASN HD22 H 7.25 0.025 2
532 . 45 ASN C C 175.5 0.4 1
533 . 46 ARG N N 128.2 0.4 1
534 . 46 ARG H H 9.20 0.025 1
535 . 46 ARG CA C 59.6 0.4 1
536 . 46 ARG HA H 3.72 0.025 1
537 . 46 ARG CB C 29.4 0.4 1
538 . 46 ARG HB2 H 1.89 0.025 2
539 . 46 ARG HB3 H 1.74 0.025 2
540 . 46 ARG CG C 27.5 0.4 1
541 . 46 ARG HG2 H 1.59 0.025 2
542 . 46 ARG HG3 H 1.31 0.025 2
543 . 46 ARG CD C 42.2 0.4 1
544 . 46 ARG HD2 H 3.29 0.025 2
545 . 46 ARG HD3 H 3.07 0.025 2
546 . 46 ARG NE N 84.8 0.4 1
547 . 46 ARG HE H 9.45 0.025 1
548 . 46 ARG HH11 H 6.78 0.025 1
549 . 46 ARG HH12 H 6.78 0.025 1
550 . 46 ARG HH21 H 7.08 0.025 1
551 . 46 ARG HH22 H 7.08 0.025 1
552 . 46 ARG C C 178.3 0.4 1
553 . 47 GLU N N 115.7 0.4 1
554 . 47 GLU H H 8.85 0.025 1
555 . 47 GLU CA C 59.9 0.4 1
556 . 47 GLU HA H 3.93 0.025 1
557 . 47 GLU CB C 30.1 0.4 1
558 . 47 GLU HB2 H 1.93 0.025 2
559 . 47 GLU HB3 H 2.05 0.025 2
560 . 47 GLU CG C 37.3 0.4 1
561 . 47 GLU HG2 H 2.22 0.025 2
562 . 47 GLU HG3 H 2.50 0.025 2
563 . 47 GLU C C 178.2 0.4 1
564 . 48 THR N N 120.5 0.4 1
565 . 48 THR H H 7.84 0.025 1
566 . 48 THR CA C 66.2 0.4 1
567 . 48 THR HA H 4.33 0.025 1
568 . 48 THR CB C 66.4 0.4 1
569 . 48 THR HB H 3.88 0.025 1
570 . 48 THR HG2 H 0.93 0.025 1
571 . 48 THR CG2 C 22.8 0.4 1
572 . 48 THR C C 177.3 0.4 1
573 . 49 GLY N N 108.9 0.4 1
574 . 49 GLY H H 7.55 0.025 1
575 . 49 GLY CA C 47.5 0.4 1
576 . 49 GLY HA2 H 3.51 0.025 2
577 . 49 GLY HA3 H 4.49 0.025 2
578 . 49 GLY C C 175.7 0.4 1
579 . 50 CYS N N 117.9 0.4 1
580 . 50 CYS H H 7.96 0.025 1
581 . 50 CYS CA C 55.4 0.4 1
582 . 50 CYS HA H 4.62 0.025 1
583 . 50 CYS CB C 34.9 0.4 1
584 . 50 CYS HB2 H 3.17 0.025 2
585 . 50 CYS HB3 H 3.33 0.025 2
586 . 50 CYS C C 177.0 0.4 1
587 . 51 ALA N N 123.0 0.4 1
588 . 51 ALA H H 8.72 0.025 1
589 . 51 ALA CA C 55.7 0.4 1
590 . 51 ALA HA H 3.80 0.025 1
591 . 51 ALA HB H 1.56 0.025 1
592 . 51 ALA CB C 17.9 0.4 1
593 . 51 ALA C C 178.4 0.4 1
594 . 52 ILE N N 117.7 0.4 1
595 . 52 ILE H H 8.47 0.025 1
596 . 52 ILE CA C 66.2 0.4 1
597 . 52 ILE HA H 3.74 0.025 1
598 . 52 ILE CB C 37.7 0.4 1
599 . 52 ILE HB H 1.92 0.025 1
600 . 52 ILE HG2 H 0.89 0.025 1
601 . 52 ILE CG2 C 17.7 0.4 1
602 . 52 ILE CG1 C 30.4 0.4 1
603 . 52 ILE HG12 H 0.95 0.025 2
604 . 52 ILE HG13 H 2.27 0.025 2
605 . 52 ILE HD1 H 0.59 0.025 1
606 . 52 ILE CD1 C 13.3 0.4 1
607 . 52 ILE C C 177.5 0.4 1
608 . 53 MET N N 121.3 0.4 1
609 . 53 MET H H 8.03 0.025 1
610 . 53 MET CA C 59.5 0.4 1
611 . 53 MET HA H 4.13 0.025 1
612 . 53 MET CB C 32.7 0.4 1
613 . 53 MET HB2 H 2.41 0.025 2
614 . 53 MET HB3 H 2.34 0.025 2
615 . 53 MET CG C 30.7 0.4 1
616 . 53 MET HG2 H 2.69 0.025 2
617 . 53 MET HG3 H 2.42 0.025 2
618 . 53 MET HE H 2.06 0.025 1
619 . 53 MET CE C 16.2 0.4 1
620 . 53 MET C C 178.0 0.4 1
621 . 54 CYS N N 121.3 0.4 1
622 . 54 CYS H H 8.21 0.025 1
623 . 54 CYS CA C 59.5 0.4 1
624 . 54 CYS HA H 4.21 0.025 1
625 . 54 CYS CB C 43.0 0.4 1
626 . 54 CYS HB2 H 3.72 0.025 2
627 . 54 CYS HB3 H 3.26 0.025 2
628 . 54 CYS C C 175.5 0.4 1
629 . 55 LEU N N 123.9 0.4 1
630 . 55 LEU H H 8.84 0.025 1
631 . 55 LEU CA C 57.2 0.4 1
632 . 55 LEU HA H 3.64 0.025 1
633 . 55 LEU CB C 40.3 0.4 1
634 . 55 LEU HB2 H 1.48 0.025 2
635 . 55 LEU HB3 H 0.42 0.025 2
636 . 55 LEU CG C 25.9 0.4 1
637 . 55 LEU HG H 1.75 0.025 1
638 . 55 LEU HD1 H 0.52 0.025 2
639 . 55 LEU HD2 H 0.44 0.025 2
640 . 55 LEU CD1 C 26.4 0.4 1
641 . 55 LEU CD2 C 21.3 0.4 1
642 . 55 LEU C C 179.5 0.4 1
643 . 56 SER N N 113.7 0.4 1
644 . 56 SER H H 8.26 0.025 1
645 . 56 SER CA C 62.4 0.4 1
646 . 56 SER HA H 3.93 0.025 1
647 . 56 SER CB C 62.9 0.4 1
648 . 56 SER HB2 H 4.08 0.025 2
649 . 56 SER HB3 H 3.60 0.025 2
650 . 56 SER C C 176.3 0.4 1
651 . 57 THR N N 119.7 0.4 1
652 . 57 THR H H 8.14 0.025 1
653 . 57 THR CA C 66.4 0.4 1
654 . 57 THR HA H 4.08 0.025 1
655 . 57 THR CB C 68.2 0.4 1
656 . 57 THR HB H 4.41 0.025 1
657 . 57 THR HG2 H 1.19 0.025 1
658 . 57 THR CG2 C 20.6 0.4 1
659 . 57 THR C C 178.7 0.4 1
660 . 58 LYS N N 124.1 0.4 1
661 . 58 LYS H H 8.52 0.025 1
662 . 58 LYS CA C 58.9 0.4 1
663 . 58 LYS HA H 3.98 0.025 1
664 . 58 LYS CB C 32.0 0.4 1
665 . 58 LYS HB2 H 1.86 0.025 2
666 . 58 LYS HB3 H 1.70 0.025 2
667 . 58 LYS CG C 25.9 0.4 1
668 . 58 LYS HG2 H 1.46 0.025 2
669 . 58 LYS HG3 H 1.51 0.025 2
670 . 58 LYS CD C 28.6 0.4 1
671 . 58 LYS HD2 H 1.47 0.025 1
672 . 58 LYS HD3 H 1.47 0.025 1
673 . 58 LYS CE C 41.6 0.4 1
674 . 58 LYS HE2 H 2.79 0.025 2
675 . 58 LYS HE3 H 2.62 0.025 2
676 . 58 LYS C C 178.2 0.4 1
677 . 59 LEU N N 117.3 0.4 1
678 . 59 LEU H H 7.07 0.025 1
679 . 59 LEU CA C 54.1 0.4 1
680 . 59 LEU HA H 4.24 0.025 1
681 . 59 LEU CB C 42.3 0.4 1
682 . 59 LEU HB2 H 1.49 0.025 2
683 . 59 LEU HB3 H 1.47 0.025 2
684 . 59 LEU CG C 26.8 0.4 1
685 . 59 LEU HG H 1.51 0.025 1
686 . 59 LEU HD1 H 0.37 0.025 2
687 . 59 LEU HD2 H 0.90 0.025 2
688 . 59 LEU CD1 C 26.5 0.4 1
689 . 59 LEU CD2 C 22.4 0.4 1
690 . 59 LEU C C 175.4 0.4 1
691 . 60 ASN N N 115.4 0.4 1
692 . 60 ASN H H 8.10 0.025 1
693 . 60 ASN CA C 53.8 0.4 1
694 . 60 ASN HA H 4.58 0.025 1
695 . 60 ASN CB C 36.5 0.4 1
696 . 60 ASN HB2 H 2.71 0.025 2
697 . 60 ASN HB3 H 2.90 0.025 2
698 . 60 ASN ND2 N 112.5 0.4 1
699 . 60 ASN HD21 H 7.53 0.025 2
700 . 60 ASN HD22 H 6.74 0.025 2
701 . 60 ASN C C 175.1 0.4 1
702 . 61 MET N N 112.0 0.4 1
703 . 61 MET H H 8.27 0.025 1
704 . 61 MET CA C 56.6 0.4 1
705 . 61 MET HA H 4.25 0.025 1
706 . 61 MET CB C 34.8 0.4 1
707 . 61 MET HB2 H 1.86 0.025 2
708 . 61 MET HB3 H 2.25 0.025 2
709 . 61 MET CG C 33.1 0.4 1
710 . 61 MET HG2 H 2.16 0.025 2
711 . 61 MET HG3 H 2.39 0.025 2
712 . 61 MET HE H 1.64 0.025 1
713 . 61 MET CE C 16.4 0.4 1
714 . 61 MET C C 174.7 0.4 1
715 . 62 LEU N N 117.1 0.4 1
716 . 62 LEU H H 7.65 0.025 1
717 . 62 LEU CA C 52.7 0.4 1
718 . 62 LEU HA H 5.19 0.025 1
719 . 62 LEU CB C 43.5 0.4 1
720 . 62 LEU HB2 H 1.72 0.025 2
721 . 62 LEU HB3 H 1.23 0.025 2
722 . 62 LEU CG C 26.7 0.4 1
723 . 62 LEU HG H 1.22 0.025 1
724 . 62 LEU HD1 H 0.88 0.025 2
725 . 62 LEU HD2 H 0.67 0.025 2
726 . 62 LEU CD1 C 25.1 0.4 1
727 . 62 LEU CD2 C 21.5 0.4 1
728 . 62 LEU C C 177.1 0.4 1
729 . 63 ASP N N 126.4 0.4 1
730 . 63 ASP H H 9.77 0.025 1
731 . 63 ASP CA C 52.1 0.4 1
732 . 63 ASP HA H 4.72 0.025 1
733 . 63 ASP CB C 39.5 0.4 1
734 . 63 ASP HB2 H 2.50 0.025 2
735 . 63 ASP HB3 H 3.45 0.025 2
736 . 63 ASP C C 175.9 0.4 1
737 . 64 PRO CD C 51.1 0.4 1
738 . 64 PRO CA C 65.1 0.4 1
739 . 64 PRO HA H 4.31 0.025 1
740 . 64 PRO CB C 31.6 0.4 1
741 . 64 PRO HB2 H 1.82 0.025 2
742 . 64 PRO HB3 H 2.41 0.025 2
743 . 64 PRO CG C 27.7 0.4 1
744 . 64 PRO HG2 H 1.93 0.025 2
745 . 64 PRO HG3 H 2.10 0.025 2
746 . 64 PRO HD2 H 3.94 0.025 2
747 . 64 PRO HD3 H 3.66 0.025 2
748 . 64 PRO C C 177.47 0.4 1
749 . 65 GLU N N 114.6 0.4 1
750 . 65 GLU H H 7.91 0.025 1
751 . 65 GLU CA C 55.6 0.4 1
752 . 65 GLU HA H 4.24 0.025 1
753 . 65 GLU CB C 29.7 0.4 1
754 . 65 GLU HB2 H 2.09 0.025 2
755 . 65 GLU HB3 H 2.01 0.025 2
756 . 65 GLU CG C 36.6 0.4 1
757 . 65 GLU HG2 H 2.13 0.025 1
758 . 65 GLU HG3 H 2.13 0.025 1
759 . 65 GLU C C 176.4 0.4 1
760 . 66 GLY N N 108.4 0.4 1
761 . 66 GLY H H 8.34 0.025 1
762 . 66 GLY CA C 45.1 0.4 1
763 . 66 GLY HA2 H 3.48 0.025 2
764 . 66 GLY HA3 H 4.10 0.025 2
765 . 66 GLY C C 172.8 0.4 1
766 . 67 ASN N N 118.1 0.4 1
767 . 67 ASN H H 8.05 0.025 1
768 . 67 ASN CA C 51.3 0.4 1
769 . 67 ASN HA H 5.16 0.025 1
770 . 67 ASN CB C 40.0 0.4 1
771 . 67 ASN HB2 H 2.75 0.025 2
772 . 67 ASN HB3 H 2.96 0.025 2
773 . 67 ASN ND2 N 114.6 0.4 1
774 . 67 ASN HD21 H 8.03 0.025 2
775 . 67 ASN HD22 H 6.65 0.025 2
776 . 67 ASN C C 175.1 0.4 1
777 . 68 LEU N N 124.5 0.4 1
778 . 68 LEU H H 10.72 0.025 1
779 . 68 LEU CA C 56.0 0.4 1
780 . 68 LEU HA H 4.41 0.025 1
781 . 68 LEU CB C 42.0 0.4 1
782 . 68 LEU HB2 H 1.68 0.025 2
783 . 68 LEU HB3 H 1.63 0.025 2
784 . 68 LEU CG C 25.8 0.4 1
785 . 68 LEU HG H 1.47 0.025 1
786 . 68 LEU HD1 H 0.63 0.025 2
787 . 68 LEU HD2 H 0.96 0.025 2
788 . 68 LEU CD1 C 26.5 0.4 1
789 . 68 LEU CD2 C 23.6 0.4 1
790 . 68 LEU C C 177.2 0.4 1
791 . 69 HIS N N 131.6 0.4 1
792 . 69 HIS H H 9.33 0.025 1
793 . 69 HIS CA C 56.3 0.4 1
794 . 69 HIS HA H 4.42 0.025 1
795 . 69 HIS CB C 31.1 0.4 1
796 . 69 HIS HB2 H 2.46 0.025 2
797 . 69 HIS HB3 H 3.11 0.025 2
798 . 69 HIS ND1 N 250.0 0.4 1
799 . 69 HIS CD2 C 117.7 0.4 1
800 . 69 HIS CE1 C 139.7 0.4 1
801 . 69 HIS NE2 N 165.0 0.4 1
802 . 69 HIS HD2 H 6.90 0.025 1
803 . 69 HIS HE1 H 7.59 0.025 1
804 . 69 HIS C C 175.0 0.4 1
805 . 70 HIS N N 127.6 0.4 1
806 . 70 HIS H H 8.94 0.025 1
807 . 70 HIS CA C 60.2 0.4 1
808 . 70 HIS HA H 3.97 0.025 1
809 . 70 HIS CB C 30.0 0.4 1
810 . 70 HIS HB2 H 3.07 0.025 2
811 . 70 HIS HB3 H 3.15 0.025 2
812 . 70 HIS ND1 N 250.0 0.4 1
813 . 70 HIS CD2 C 118.8 0.4 1
814 . 70 HIS HD1 H 9.49 0.025 1
815 . 70 HIS CE1 C 138.1 0.4 1
816 . 70 HIS NE2 N 165.0 0.4 1
817 . 70 HIS HD2 H 7.02 0.025 1
818 . 70 HIS HE1 H 7.72 0.025 1
819 . 70 HIS C C 176.7 0.4 1
820 . 71 GLY N N 107.3 0.4 1
821 . 71 GLY H H 8.45 0.025 1
822 . 71 GLY CA C 47.3 0.4 1
823 . 71 GLY HA2 H 3.85 0.025 2
824 . 71 GLY HA3 H 4.09 0.025 2
825 . 71 GLY C C 177.1 0.4 1
826 . 72 ASN N N 124.8 0.4 1
827 . 72 ASN H H 11.06 0.025 1
828 . 72 ASN CA C 55.1 0.4 1
829 . 72 ASN HA H 4.61 0.025 1
830 . 72 ASN CB C 36.4 0.4 1
831 . 72 ASN HB2 H 2.63 0.025 2
832 . 72 ASN HB3 H 2.70 0.025 2
833 . 72 ASN ND2 N 109.6 0.4 1
834 . 72 ASN HD21 H 7.33 0.025 2
835 . 72 ASN HD22 H 6.53 0.025 2
836 . 72 ASN C C 179.6 0.4 1
837 . 73 ALA N N 125.7 0.4 1
838 . 73 ALA H H 8.88 0.025 1
839 . 73 ALA CA C 55.4 0.4 1
840 . 73 ALA HA H 4.40 0.025 1
841 . 73 ALA HB H 1.51 0.025 1
842 . 73 ALA CB C 18.5 0.4 1
843 . 73 ALA C C 178.7 0.4 1
844 . 74 MET N N 118.0 0.4 1
845 . 74 MET H H 8.53 0.025 1
846 . 74 MET CA C 58.2 0.4 1
847 . 74 MET HA H 4.04 0.025 1
848 . 74 MET CB C 31.2 0.4 1
849 . 74 MET HB2 H 2.20 0.025 2
850 . 74 MET HB3 H 2.15 0.025 2
851 . 74 MET CG C 31.8 0.4 1
852 . 74 MET HG2 H 2.40 0.025 2
853 . 74 MET HG3 H 2.50 0.025 2
854 . 74 MET HE H 2.02 0.025 1
855 . 74 MET CE C 16.3 0.4 1
856 . 74 MET C C 177.8 0.4 1
857 . 75 GLU N N 117.3 0.4 1
858 . 75 GLU H H 7.81 0.025 1
859 . 75 GLU CA C 59.0 0.4 1
860 . 75 GLU HA H 3.96 0.025 1
861 . 75 GLU CB C 29.1 0.4 1
862 . 75 GLU HB2 H 2.13 0.025 1
863 . 75 GLU HB3 H 2.13 0.025 1
864 . 75 GLU CG C 35.7 0.4 1
865 . 75 GLU HG2 H 2.39 0.025 2
866 . 75 GLU HG3 H 2.32 0.025 2
867 . 75 GLU C C 178.8 0.4 1
868 . 76 PHE N N 120.3 0.4 1
869 . 76 PHE H H 7.91 0.025 1
870 . 76 PHE CA C 61.3 0.4 1
871 . 76 PHE HA H 4.18 0.025 1
872 . 76 PHE CB C 39.2 0.4 1
873 . 76 PHE HB2 H 3.48 0.025 2
874 . 76 PHE HB3 H 3.29 0.025 2
875 . 76 PHE HD1 H 7.32 0.025 1
876 . 76 PHE HD2 H 7.32 0.025 1
877 . 76 PHE HE1 H 7.22 0.025 1
878 . 76 PHE HE2 H 7.22 0.025 1
879 . 76 PHE CD1 C 132.9 0.4 1
880 . 76 PHE CE1 C 132.2 0.4 1
881 . 76 PHE CZ C 129.2 0.4 1
882 . 76 PHE HZ H 7.07 0.025 1
883 . 76 PHE C C 176.1 0.4 1
884 . 77 ALA N N 119.6 0.4 1
885 . 77 ALA H H 8.54 0.025 1
886 . 77 ALA CA C 54.4 0.4 1
887 . 77 ALA HA H 3.87 0.025 1
888 . 77 ALA HB H 1.36 0.025 1
889 . 77 ALA CB C 16.5 0.4 1
890 . 77 ALA C C 179.6 0.4 1
891 . 78 LYS N N 116.1 0.4 1
892 . 78 LYS H H 8.33 0.025 1
893 . 78 LYS CA C 58.1 0.4 1
894 . 78 LYS HA H 4.55 0.025 1
895 . 78 LYS CB C 32.1 0.4 1
896 . 78 LYS HB2 H 1.70 0.025 2
897 . 78 LYS HB3 H 1.75 0.025 2
898 . 78 LYS CG C 24.8 0.4 1
899 . 78 LYS HG2 H 1.58 0.025 2
900 . 78 LYS HG3 H 1.27 0.025 2
901 . 78 LYS CD C 29.2 0.4 1
902 . 78 LYS HD2 H 1.62 0.025 2
903 . 78 LYS HD3 H 1.55 0.025 2
904 . 78 LYS CE C 41.3 0.4 1
905 . 78 LYS HE2 H 2.79 0.025 2
906 . 78 LYS HE3 H 2.81 0.025 2
907 . 78 LYS C C 180.5 0.4 1
908 . 79 LYS N N 120.5 0.4 1
909 . 79 LYS H H 7.93 0.025 1
910 . 79 LYS CA C 58.1 0.4 1
911 . 79 LYS HA H 3.78 0.025 1
912 . 79 LYS CB C 31.4 0.4 1
913 . 79 LYS HB2 H 1.64 0.025 2
914 . 79 LYS HB3 H 1.33 0.025 2
915 . 79 LYS CG C 24.0 0.4 1
916 . 79 LYS HG2 H 0.71 0.025 2
917 . 79 LYS HG3 H 0.93 0.025 2
918 . 79 LYS CD C 29.1 0.4 1
919 . 79 LYS HD2 H 1.42 0.025 2
920 . 79 LYS HD3 H 1.47 0.025 2
921 . 79 LYS CE C 41.6 0.4 1
922 . 79 LYS HE2 H 2.81 0.025 1
923 . 79 LYS HE3 H 2.81 0.025 1
924 . 79 LYS C C 177.2 0.4 1
925 . 80 HIS N N 113.4 0.4 1
926 . 80 HIS H H 6.72 0.025 1
927 . 80 HIS CA C 55.4 0.4 1
928 . 80 HIS HA H 4.65 0.025 1
929 . 80 HIS CB C 29.5 0.4 1
930 . 80 HIS HB2 H 2.30 0.025 2
931 . 80 HIS HB3 H 3.07 0.025 2
932 . 80 HIS CD2 C 122.3 0.4 1
933 . 80 HIS CE1 C 138.6 0.4 1
934 . 80 HIS HD2 H 5.69 0.025 1
935 . 80 HIS HE1 H 7.56 0.025 1
936 . 80 HIS C C 174.4 0.4 1
937 . 81 GLY N N 103.6 0.4 1
938 . 81 GLY H H 7.14 0.025 1
939 . 81 GLY CA C 45.2 0.4 1
940 . 81 GLY HA2 H 3.54 0.025 2
941 . 81 GLY HA3 H 4.33 0.025 2
942 . 81 GLY C C 174.2 0.4 1
943 . 82 ALA N N 123.4 0.4 1
944 . 82 ALA H H 8.16 0.025 1
945 . 82 ALA CA C 51.9 0.4 1
946 . 82 ALA HA H 4.30 0.025 1
947 . 82 ALA HB H 1.05 0.025 1
948 . 82 ALA CB C 19.2 0.4 1
949 . 82 ALA C C 176.8 0.4 1
950 . 83 ASP N N 119.9 0.4 1
951 . 83 ASP H H 7.81 0.025 1
952 . 83 ASP CA C 51.9 0.4 1
953 . 83 ASP HA H 4.62 0.025 1
954 . 83 ASP CB C 40.6 0.4 1
955 . 83 ASP HB2 H 2.72 0.025 2
956 . 83 ASP HB3 H 3.07 0.025 2
957 . 83 ASP C C 175.3 0.4 1
958 . 84 GLU N N 118.5 0.4 1
959 . 84 GLU H H 8.75 0.025 1
960 . 84 GLU CA C 60.4 0.4 1
961 . 84 GLU HA H 3.75 0.025 1
962 . 84 GLU CB C 29.4 0.4 1
963 . 84 GLU HB2 H 2.01 0.025 2
964 . 84 GLU HB3 H 2.05 0.025 2
965 . 84 GLU CG C 35.9 0.4 1
966 . 84 GLU HG2 H 2.31 0.025 1
967 . 84 GLU HG3 H 2.31 0.025 1
968 . 84 GLU C C 178.1 0.4 1
969 . 85 THR N N 114.4 0.4 1
970 . 85 THR H H 7.92 0.025 1
971 . 85 THR CA C 66.0 0.4 1
972 . 85 THR HA H 3.93 0.025 1
973 . 85 THR CB C 68.0 0.4 1
974 . 85 THR HB H 4.20 0.025 1
975 . 85 THR HG2 H 1.23 0.025 1
976 . 85 THR CG2 C 21.3 0.4 1
977 . 85 THR C C 176.6 0.4 1
978 . 86 MET N N 123.8 0.4 1
979 . 86 MET H H 8.46 0.025 1
980 . 86 MET CA C 59.0 0.4 1
981 . 86 MET HA H 4.24 0.025 1
982 . 86 MET CB C 31.9 0.4 1
983 . 86 MET HB2 H 2.11 0.025 2
984 . 86 MET HB3 H 1.72 0.025 2
985 . 86 MET CG C 32.4 0.4 1
986 . 86 MET HG2 H 2.33 0.025 2
987 . 86 MET HG3 H 2.04 0.025 2
988 . 86 MET C C 177.8 0.4 1
989 . 87 ALA N N 119.5 0.4 1
990 . 87 ALA H H 8.83 0.025 1
991 . 87 ALA CA C 55.6 0.4 1
992 . 87 ALA HA H 3.74 0.025 1
993 . 87 ALA HB H 1.41 0.025 1
994 . 87 ALA CB C 19.1 0.4 1
995 . 87 ALA C C 178.3 0.4 1
996 . 88 GLN N N 115.3 0.4 1
997 . 88 GLN H H 8.16 0.025 1
998 . 88 GLN CA C 57.9 0.4 1
999 . 88 GLN HA H 3.86 0.025 1
1000 . 88 GLN CB C 28.3 0.4 1
1001 . 88 GLN HB2 H 2.23 0.025 2
1002 . 88 GLN HB3 H 2.16 0.025 2
1003 . 88 GLN CG C 33.2 0.4 1
1004 . 88 GLN HG2 H 2.38 0.025 1
1005 . 88 GLN HG3 H 2.38 0.025 1
1006 . 88 GLN NE2 N 115.2 0.4 1
1007 . 88 GLN HE21 H 7.86 0.025 2
1008 . 88 GLN HE22 H 6.79 0.025 2
1009 . 88 GLN C C 177.5 0.4 1
1010 . 89 GLN N N 118.7 0.4 1
1011 . 89 GLN H H 7.96 0.025 1
1012 . 89 GLN CA C 59.0 0.4 1
1013 . 89 GLN HA H 4.20 0.025 1
1014 . 89 GLN CB C 28.5 0.4 1
1015 . 89 GLN HB2 H 2.24 0.025 2
1016 . 89 GLN HB3 H 2.50 0.025 2
1017 . 89 GLN CG C 34.1 0.4 1
1018 . 89 GLN HG2 H 2.31 0.025 2
1019 . 89 GLN HG3 H 2.52 0.025 2
1020 . 89 GLN NE2 N 109.9 0.4 1
1021 . 89 GLN HE21 H 6.68 0.025 2
1022 . 89 GLN HE22 H 7.22 0.025 2
1023 . 89 GLN C C 179.0 0.4 1
1024 . 90 LEU N N 117.8 0.4 1
1025 . 90 LEU H H 8.44 0.025 1
1026 . 90 LEU CA C 58.1 0.4 1
1027 . 90 LEU HA H 4.09 0.025 1
1028 . 90 LEU CB C 42.2 0.4 1
1029 . 90 LEU HB2 H 2.30 0.025 2
1030 . 90 LEU HB3 H 1.37 0.025 2
1031 . 90 LEU CG C 26.2 0.4 1
1032 . 90 LEU HG H 2.21 0.025 1
1033 . 90 LEU HD1 H 0.87 0.025 2
1034 . 90 LEU HD2 H 1.16 0.025 2
1035 . 90 LEU CD1 C 26.4 0.4 1
1036 . 90 LEU CD2 C 24.3 0.4 1
1037 . 90 LEU C C 178.3 0.4 1
1038 . 91 ILE N N 120.1 0.4 1
1039 . 91 ILE H H 7.96 0.025 1
1040 . 91 ILE CA C 64.9 0.4 1
1041 . 91 ILE HA H 3.19 0.025 1
1042 . 91 ILE CB C 37.2 0.4 1
1043 . 91 ILE HB H 1.82 0.025 1
1044 . 91 ILE HG2 H 0.44 0.025 1
1045 . 91 ILE CG2 C 17.2 0.4 1
1046 . 91 ILE CG1 C 30.3 0.4 1
1047 . 91 ILE HG12 H 0.89 0.025 2
1048 . 91 ILE HG13 H 1.52 0.025 2
1049 . 91 ILE HD1 H 0.68 0.025 1
1050 . 91 ILE CD1 C 13.6 0.4 1
1051 . 91 ILE C C 177.2 0.4 1
1052 . 92 ASP N N 120.5 0.4 1
1053 . 92 ASP H H 8.67 0.025 1
1054 . 92 ASP CA C 57.3 0.4 1
1055 . 92 ASP HA H 4.45 0.025 1
1056 . 92 ASP CB C 39.4 0.4 1
1057 . 92 ASP HB2 H 2.90 0.025 2
1058 . 92 ASP HB3 H 2.65 0.025 2
1059 . 92 ASP C C 180.6 0.4 1
1060 . 93 ILE N N 122.1 0.4 1
1061 . 93 ILE H H 8.38 0.025 1
1062 . 93 ILE CA C 64.9 0.4 1
1063 . 93 ILE HA H 3.79 0.025 1
1064 . 93 ILE CB C 37.8 0.4 1
1065 . 93 ILE HB H 2.12 0.025 1
1066 . 93 ILE HG2 H 0.95 0.025 1
1067 . 93 ILE CG2 C 19.4 0.4 1
1068 . 93 ILE CG1 C 29.1 0.4 1
1069 . 93 ILE HG12 H 0.93 0.025 2
1070 . 93 ILE HG13 H 2.00 0.025 2
1071 . 93 ILE HD1 H 0.60 0.025 1
1072 . 93 ILE CD1 C 14.1 0.4 1
1073 . 93 ILE C C 179.3 0.4 1
1074 . 94 VAL N N 121.0 0.4 1
1075 . 94 VAL H H 8.41 0.025 1
1076 . 94 VAL CA C 68.3 0.4 1
1077 . 94 VAL HA H 3.21 0.025 1
1078 . 94 VAL CB C 30.6 0.4 1
1079 . 94 VAL HB H 2.02 0.025 1
1080 . 94 VAL HG1 H 0.75 0.025 2
1081 . 94 VAL HG2 H 0.74 0.025 2
1082 . 94 VAL CG1 C 22.8 0.4 1
1083 . 94 VAL CG2 C 23.8 0.4 1
1084 . 94 VAL C C 177.8 0.4 1
1085 . 95 HIS N N 117.5 0.4 1
1086 . 95 HIS H H 9.08 0.025 1
1087 . 95 HIS CA C 57.7 0.4 1
1088 . 95 HIS HA H 4.80 0.025 1
1089 . 95 HIS CB C 28.9 0.4 1
1090 . 95 HIS HB2 H 3.23 0.025 2
1091 . 95 HIS HB3 H 3.34 0.025 2
1092 . 95 HIS CD2 C 121.5 0.4 1
1093 . 95 HIS CE1 C 137.7 0.4 1
1094 . 95 HIS HD2 H 7.60 0.025 1
1095 . 95 HIS HE1 H 8.37 0.025 1
1096 . 95 HIS C C 178.2 0.4 1
1097 . 96 GLY N N 106.5 0.4 1
1098 . 96 GLY H H 8.56 0.025 1
1099 . 96 GLY CA C 47.0 0.4 1
1100 . 96 GLY HA2 H 3.79 0.025 2
1101 . 96 GLY HA3 H 4.06 0.025 2
1102 . 96 GLY C C 177.4 0.4 1
1103 . 97 CYS N N 122.1 0.4 1
1104 . 97 CYS H H 8.34 0.025 1
1105 . 97 CYS CA C 56.4 0.4 1
1106 . 97 CYS HA H 4.78 0.025 1
1107 . 97 CYS CB C 38.4 0.4 1
1108 . 97 CYS HB2 H 3.25 0.025 2
1109 . 97 CYS HB3 H 2.92 0.025 2
1110 . 97 CYS C C 177.6 0.4 1
1111 . 98 GLU N N 124.8 0.4 1
1112 . 98 GLU H H 9.10 0.025 1
1113 . 98 GLU CA C 59.1 0.4 1
1114 . 98 GLU HA H 3.93 0.025 1
1115 . 98 GLU CB C 29.4 0.4 1
1116 . 98 GLU HB2 H 2.77 0.025 2
1117 . 98 GLU HB3 H 2.25 0.025 2
1118 . 98 GLU CG C 36.3 0.4 1
1119 . 98 GLU HG2 H 2.47 0.025 2
1120 . 98 GLU HG3 H 2.67 0.025 2
1121 . 98 GLU C C 178.4 0.4 1
1122 . 99 LYS N N 115.7 0.4 1
1123 . 99 LYS H H 7.56 0.025 1
1124 . 99 LYS CA C 57.4 0.4 1
1125 . 99 LYS HA H 4.27 0.025 1
1126 . 99 LYS CB C 32.2 0.4 1
1127 . 99 LYS HB2 H 1.90 0.025 1
1128 . 99 LYS HB3 H 1.90 0.025 1
1129 . 99 LYS CG C 24.4 0.4 1
1130 . 99 LYS HG2 H 1.45 0.025 1
1131 . 99 LYS HG3 H 1.45 0.025 1
1132 . 99 LYS CD C 28.4 0.4 1
1133 . 99 LYS HD2 H 1.59 0.025 1
1134 . 99 LYS HD3 H 1.59 0.025 1
1135 . 99 LYS CE C 41.5 0.4 1
1136 . 99 LYS HE2 H 2.79 0.025 1
1137 . 99 LYS HE3 H 2.79 0.025 1
1138 . 99 LYS C C 178.2 0.4 1
1139 . 100 SER N N 112.4 0.4 1
1140 . 100 SER H H 8.10 0.025 1
1141 . 100 SER CA C 58.8 0.4 1
1142 . 100 SER HA H 4.34 0.025 1
1143 . 100 SER CB C 63.2 0.4 1
1144 . 100 SER HB2 H 3.77 0.025 2
1145 . 100 SER HB3 H 4.02 0.025 2
1146 . 100 SER C C 174.7 0.4 1
1147 . 101 THR N N 123.2 0.4 1
1148 . 101 THR H H 7.36 0.025 1
1149 . 101 THR CA C 61.4 0.4 1
1150 . 101 THR HA H 4.38 0.025 1
1151 . 101 THR CB C 69.4 0.4 1
1152 . 101 THR HB H 3.68 0.025 1
1153 . 101 THR HG2 H 1.06 0.025 1
1154 . 101 THR CG2 C 20.0 0.4 1
1155 . 101 THR C C 171.9 0.4 1
1156 . 102 PRO CD C 51.1 0.4 1
1157 . 102 PRO CA C 62.7 0.4 1
1158 . 102 PRO HA H 4.33 0.025 1
1159 . 102 PRO CB C 31.8 0.4 1
1160 . 102 PRO HB2 H 1.91 0.025 2
1161 . 102 PRO HB3 H 2.34 0.025 2
1162 . 102 PRO CG C 27.4 0.4 1
1163 . 102 PRO HG2 H 2.11 0.025 2
1164 . 102 PRO HG3 H 1.98 0.025 2
1165 . 102 PRO HD2 H 3.67 0.025 2
1166 . 102 PRO HD3 H 4.08 0.025 2
1167 . 102 PRO C C 177.22 0.4 1
1168 . 103 ALA N N 124.5 0.4 1
1169 . 103 ALA H H 8.44 0.025 1
1170 . 103 ALA CA C 52.6 0.4 1
1171 . 103 ALA HA H 4.09 0.025 1
1172 . 103 ALA HB H 1.24 0.025 1
1173 . 103 ALA CB C 18.3 0.4 1
1174 . 103 ALA C C 177.2 0.4 1
1175 . 104 ASN N N 119.8 0.4 1
1176 . 104 ASN H H 8.13 0.025 1
1177 . 104 ASN CA C 52.8 0.4 1
1178 . 104 ASN HA H 4.59 0.025 1
1179 . 104 ASN CB C 42.5 0.4 1
1180 . 104 ASN HB2 H 2.70 0.025 2
1181 . 104 ASN HB3 H 2.75 0.025 2
1182 . 104 ASN ND2 N 114.1 0.4 1
1183 . 104 ASN HD21 H 8.04 0.025 2
1184 . 104 ASN HD22 H 7.12 0.025 2
1185 . 104 ASN C C 174.0 0.4 1
1186 . 105 ASP N N 125.5 0.4 1
1187 . 105 ASP H H 8.78 0.025 1
1188 . 105 ASP CA C 55.8 0.4 1
1189 . 105 ASP HA H 4.27 0.025 1
1190 . 105 ASP CB C 40.3 0.4 1
1191 . 105 ASP HB2 H 2.50 0.025 2
1192 . 105 ASP HB3 H 2.64 0.025 2
1193 . 105 ASP C C 176.1 0.4 1
1194 . 106 ASP N N 118.8 0.4 1
1195 . 106 ASP H H 9.08 0.025 1
1196 . 106 ASP CA C 52.1 0.4 1
1197 . 106 ASP HA H 4.70 0.025 1
1198 . 106 ASP CB C 39.8 0.4 1
1199 . 106 ASP HB2 H 2.45 0.025 2
1200 . 106 ASP HB3 H 3.03 0.025 2
1201 . 106 ASP C C 176.5 0.4 1
1202 . 107 LYS N N 125.1 0.4 1
1203 . 107 LYS H H 8.89 0.025 1
1204 . 107 LYS CA C 57.2 0.4 1
1205 . 107 LYS HA H 4.29 0.025 1
1206 . 107 LYS CB C 31.6 0.4 1
1207 . 107 LYS HB2 H 2.06 0.025 2
1208 . 107 LYS HB3 H 1.83 0.025 2
1209 . 107 LYS CG C 24.6 0.4 1
1210 . 107 LYS HG2 H 1.59 0.025 2
1211 . 107 LYS HG3 H 1.52 0.025 2
1212 . 107 LYS CD C 27.7 0.4 1
1213 . 107 LYS HD2 H 1.55 0.025 2
1214 . 107 LYS HD3 H 1.49 0.025 2
1215 . 107 LYS CE C 41.7 0.4 1
1216 . 107 LYS HE2 H 2.79 0.025 1
1217 . 107 LYS HE3 H 2.79 0.025 1
1218 . 107 LYS C C 180.8 0.4 1
1219 . 108 CYS N N 119.4 0.4 1
1220 . 108 CYS H H 8.62 0.025 1
1221 . 108 CYS CA C 61.6 0.4 1
1222 . 108 CYS HA H 4.17 0.025 1
1223 . 108 CYS CB C 44.6 0.4 1
1224 . 108 CYS HB2 H 3.88 0.025 2
1225 . 108 CYS HB3 H 3.06 0.025 2
1226 . 108 CYS C C 176.0 0.4 1
1227 . 109 ILE N N 121.1 0.4 1
1228 . 109 ILE H H 7.31 0.025 1
1229 . 109 ILE CA C 63.5 0.4 1
1230 . 109 ILE HA H 3.65 0.025 1
1231 . 109 ILE CB C 36.6 0.4 1
1232 . 109 ILE HB H 1.94 0.025 1
1233 . 109 ILE HG2 H 0.89 0.025 1
1234 . 109 ILE CG2 C 17.0 0.4 1
1235 . 109 ILE CG1 C 28.3 0.4 1
1236 . 109 ILE HG12 H 1.16 0.025 2
1237 . 109 ILE HG13 H 1.55 0.025 2
1238 . 109 ILE HD1 H 0.85 0.025 1
1239 . 109 ILE CD1 C 11.1 0.4 1
1240 . 109 ILE C C 179.0 0.4 1
1241 . 110 TRP N N 122.4 0.4 1
1242 . 110 TRP H H 8.38 0.025 1
1243 . 110 TRP CA C 62.2 0.4 1
1244 . 110 TRP HA H 4.21 0.025 1
1245 . 110 TRP CB C 29.1 0.4 1
1246 . 110 TRP HB2 H 3.25 0.025 2
1247 . 110 TRP HB3 H 3.34 0.025 2
1248 . 110 TRP CD1 C 129.0 0.4 1
1249 . 110 TRP CE3 C 120.4 0.4 1
1250 . 110 TRP NE1 N 129.8 0.4 1
1251 . 110 TRP HD1 H 7.59 0.025 1
1252 . 110 TRP HE3 H 7.53 0.025 1
1253 . 110 TRP CZ3 C 123.9 0.4 1
1254 . 110 TRP CZ2 C 115.0 0.4 1
1255 . 110 TRP HE1 H 10.01 0.025 1
1256 . 110 TRP HZ3 H 7.30 0.025 1
1257 . 110 TRP CH2 C 126.1 0.4 1
1258 . 110 TRP HZ2 H 7.53 0.025 1
1259 . 110 TRP HH2 H 7.39 0.025 1
1260 . 110 TRP C C 177.1 0.4 1
1261 . 111 THR N N 114.0 0.4 1
1262 . 111 THR H H 8.35 0.025 1
1263 . 111 THR CA C 67.5 0.4 1
1264 . 111 THR HA H 3.40 0.025 1
1265 . 111 THR CB C 68.0 0.4 1
1266 . 111 THR HB H 4.21 0.025 1
1267 . 111 THR HG2 H 1.22 0.025 1
1268 . 111 THR CG2 C 22.1 0.4 1
1269 . 111 THR C C 175.8 0.4 1
1270 . 112 LEU N N 121.1 0.4 1
1271 . 112 LEU H H 7.75 0.025 1
1272 . 112 LEU CA C 57.8 0.4 1
1273 . 112 LEU HA H 3.83 0.025 1
1274 . 112 LEU CB C 41.8 0.4 1
1275 . 112 LEU HB2 H 1.91 0.025 2
1276 . 112 LEU HB3 H 1.44 0.025 2
1277 . 112 LEU CG C 26.0 0.4 1
1278 . 112 LEU HG H 1.54 0.025 1
1279 . 112 LEU HD1 H 0.63 0.025 2
1280 . 112 LEU HD2 H 0.59 0.025 2
1281 . 112 LEU CD1 C 23.3 0.4 1
1282 . 112 LEU CD2 C 24.3 0.4 1
1283 . 112 LEU C C 178.6 0.4 1
1284 . 113 GLY N N 109.1 0.4 1
1285 . 113 GLY H H 7.90 0.025 1
1286 . 113 GLY CA C 46.9 0.4 1
1287 . 113 GLY HA2 H 3.69 0.025 1
1288 . 113 GLY HA3 H 3.69 0.025 1
1289 . 113 GLY C C 175.8 0.4 1
1290 . 114 VAL N N 125.0 0.4 1
1291 . 114 VAL H H 8.01 0.025 1
1292 . 114 VAL CA C 66.9 0.4 1
1293 . 114 VAL HA H 3.03 0.025 1
1294 . 114 VAL CB C 31.1 0.4 1
1295 . 114 VAL HB H 1.69 0.025 1
1296 . 114 VAL HG1 H 0.61 0.025 2
1297 . 114 VAL HG2 H -0.33 0.025 2
1298 . 114 VAL CG1 C 20.8 0.4 1
1299 . 114 VAL CG2 C 20.8 0.4 1
1300 . 114 VAL C C 178.0 0.4 1
1301 . 115 ALA N N 120.5 0.4 1
1302 . 115 ALA H H 8.70 0.025 1
1303 . 115 ALA CA C 55.0 0.4 1
1304 . 115 ALA HA H 3.96 0.025 1
1305 . 115 ALA HB H 1.41 0.025 1
1306 . 115 ALA CB C 18.4 0.4 1
1307 . 115 ALA C C 179.1 0.4 1
1308 . 116 THR N N 112.9 0.4 1
1309 . 116 THR H H 8.68 0.025 1
1310 . 116 THR CA C 66.1 0.4 1
1311 . 116 THR HA H 3.78 0.025 1
1312 . 116 THR CB C 68.2 0.4 1
1313 . 116 THR HB H 4.25 0.025 1
1314 . 116 THR HG2 H 1.21 0.025 1
1315 . 116 THR CG2 C 21.5 0.4 1
1316 . 116 THR C C 177.0 0.4 1
1317 . 117 CYS N N 126.0 0.4 1
1318 . 117 CYS H H 7.89 0.025 1
1319 . 117 CYS CA C 59.2 0.4 1
1320 . 117 CYS HA H 4.32 0.025 1
1321 . 117 CYS CB C 35.3 0.4 1
1322 . 117 CYS HB2 H 3.34 0.025 2
1323 . 117 CYS HB3 H 3.14 0.025 2
1324 . 117 CYS C C 175.1 0.4 1
1325 . 118 PHE N N 124.4 0.4 1
1326 . 118 PHE H H 8.83 0.025 1
1327 . 118 PHE CA C 60.7 0.4 1
1328 . 118 PHE HA H 3.89 0.025 1
1329 . 118 PHE CB C 39.2 0.4 1
1330 . 118 PHE HB2 H 2.86 0.025 2
1331 . 118 PHE HB3 H 3.42 0.025 2
1332 . 118 PHE HD1 H 7.05 0.025 1
1333 . 118 PHE HD2 H 7.05 0.025 1
1334 . 118 PHE HE1 H 7.28 0.025 1
1335 . 118 PHE HE2 H 7.28 0.025 1
1336 . 118 PHE CD1 C 133.1 0.4 1
1337 . 118 PHE CE1 C 131.4 0.4 1
1338 . 118 PHE CZ C 129.6 0.4 1
1339 . 118 PHE HZ H 7.05 0.025 1
1340 . 118 PHE C C 175.9 0.4 1
1341 . 119 LYS N N 119.2 0.4 1
1342 . 119 LYS H H 8.54 0.025 1
1343 . 119 LYS CA C 58.9 0.4 1
1344 . 119 LYS HA H 3.94 0.025 1
1345 . 119 LYS CB C 33.1 0.4 1
1346 . 119 LYS HB2 H 1.75 0.025 2
1347 . 119 LYS HB3 H 1.59 0.025 2
1348 . 119 LYS CG C 24.7 0.4 1
1349 . 119 LYS HG2 H 1.50 0.025 2
1350 . 119 LYS HG3 H 1.37 0.025 2
1351 . 119 LYS CD C 29.1 0.4 1
1352 . 119 LYS HD2 H 1.69 0.025 1
1353 . 119 LYS HD3 H 1.69 0.025 1
1354 . 119 LYS CE C 41.8 0.4 1
1355 . 119 LYS HE2 H 2.90 0.025 2
1356 . 119 LYS HE3 H 2.80 0.025 2
1357 . 119 LYS C C 177.3 0.4 1
1358 . 120 ALA N N 119.0 0.4 1
1359 . 120 ALA H H 7.58 0.025 1
1360 . 120 ALA CA C 55.0 0.4 1
1361 . 120 ALA HA H 4.18 0.025 1
1362 . 120 ALA HB H 1.53 0.025 1
1363 . 120 ALA CB C 17.5 0.4 1
1364 . 120 ALA C C 181.4 0.4 1
1365 . 121 GLU N N 117.8 0.4 1
1366 . 121 GLU H H 7.98 0.025 1
1367 . 121 GLU CA C 58.1 0.4 1
1368 . 121 GLU HA H 3.93 0.025 1
1369 . 121 GLU CB C 29.4 0.4 1
1370 . 121 GLU HB2 H 1.93 0.025 2
1371 . 121 GLU HB3 H 1.87 0.025 2
1372 . 121 GLU CG C 34.9 0.4 1
1373 . 121 GLU HG2 H 2.45 0.025 2
1374 . 121 GLU HG3 H 2.26 0.025 2
1375 . 121 GLU C C 179.0 0.4 1
1376 . 122 ILE N N 120.9 0.4 1
1377 . 122 ILE H H 8.19 0.025 1
1378 . 122 ILE CA C 61.3 0.4 1
1379 . 122 ILE HA H 3.50 0.025 1
1380 . 122 ILE CB C 34.3 0.4 1
1381 . 122 ILE HB H 2.16 0.025 1
1382 . 122 ILE HG2 H 0.49 0.025 1
1383 . 122 ILE CG2 C 19.0 0.4 1
1384 . 122 ILE CG1 C 26.1 0.4 1
1385 . 122 ILE HG12 H 1.13 0.025 2
1386 . 122 ILE HG13 H 0.56 0.025 2
1387 . 122 ILE HD1 H 0.38 0.025 1
1388 . 122 ILE CD1 C 9.6 0.4 1
1389 . 122 ILE C C 179.5 0.4 1
1390 . 123 HIS N N 118.8 0.4 1
1391 . 123 HIS H H 8.38 0.025 1
1392 . 123 HIS CA C 58.9 0.4 1
1393 . 123 HIS HA H 4.61 0.025 1
1394 . 123 HIS CB C 27.9 0.4 1
1395 . 123 HIS HB2 H 3.23 0.025 1
1396 . 123 HIS HB3 H 3.23 0.025 1
1397 . 123 HIS CD2 C 125.6 0.4 1
1398 . 123 HIS CE1 C 138.8 0.4 1
1399 . 123 HIS HD2 H 7.14 0.025 1
1400 . 123 HIS HE1 H 8.19 0.025 1
1401 . 123 HIS C C 179.5 0.4 1
1402 . 124 LYS N N 121.0 0.4 1
1403 . 124 LYS H H 7.70 0.025 1
1404 . 124 LYS CA C 59.1 0.4 1
1405 . 124 LYS HA H 3.90 0.025 1
1406 . 124 LYS CB C 32.1 0.4 1
1407 . 124 LYS HB2 H 1.83 0.025 1
1408 . 124 LYS HB3 H 1.83 0.025 1
1409 . 124 LYS CG C 25.0 0.4 1
1410 . 124 LYS HG2 H 1.33 0.025 2
1411 . 124 LYS HG3 H 1.56 0.025 2
1412 . 124 LYS CD C 29.3 0.4 1
1413 . 124 LYS HD2 H 1.60 0.025 1
1414 . 124 LYS HD3 H 1.60 0.025 1
1415 . 124 LYS CE C 41.5 0.4 1
1416 . 124 LYS HE2 H 2.76 0.025 1
1417 . 124 LYS HE3 H 2.76 0.025 1
1418 . 124 LYS C C 178.0 0.4 1
1419 . 125 LEU N N 117.4 0.4 1
1420 . 125 LEU H H 6.91 0.025 1
1421 . 125 LEU CA C 54.7 0.4 1
1422 . 125 LEU HA H 3.76 0.025 1
1423 . 125 LEU CB C 40.8 0.4 1
1424 . 125 LEU HB2 H 0.76 0.025 2
1425 . 125 LEU HB3 H -0.04 0.025 2
1426 . 125 LEU CG C 25.6 0.4 1
1427 . 125 LEU HG H 1.13 0.025 1
1428 . 125 LEU HD1 H -0.34 0.025 2
1429 . 125 LEU HD2 H 0.32 0.025 2
1430 . 125 LEU CD1 C 24.2 0.4 1
1431 . 125 LEU CD2 C 21.4 0.4 1
1432 . 125 LEU C C 175.9 0.4 1
1433 . 126 ASN N N 112.1 0.4 1
1434 . 126 ASN H H 7.95 0.025 1
1435 . 126 ASN CA C 54.0 0.4 1
1436 . 126 ASN HA H 4.46 0.025 1
1437 . 126 ASN CB C 36.7 0.4 1
1438 . 126 ASN HB2 H 2.81 0.025 2
1439 . 126 ASN HB3 H 3.19 0.025 2
1440 . 126 ASN ND2 N 111.6 0.4 1
1441 . 126 ASN HD21 H 7.49 0.025 2
1442 . 126 ASN HD22 H 6.78 0.025 2
1443 . 126 ASN C C 175.7 0.4 1
1444 . 127 TRP N N 116.9 0.4 1
1445 . 127 TRP H H 7.52 0.025 1
1446 . 127 TRP CA C 54.7 0.4 1
1447 . 127 TRP HA H 4.71 0.025 1
1448 . 127 TRP CB C 29.6 0.4 1
1449 . 127 TRP HB2 H 3.05 0.025 2
1450 . 127 TRP HB3 H 2.85 0.025 2
1451 . 127 TRP CD1 C 124.1 0.4 1
1452 . 127 TRP CE3 C 120.6 0.4 1
1453 . 127 TRP NE1 N 126.8 0.4 1
1454 . 127 TRP HD1 H 6.71 0.025 1
1455 . 127 TRP HE3 H 7.18 0.025 1
1456 . 127 TRP CZ3 C 121.7 0.4 1
1457 . 127 TRP CZ2 C 115.6 0.4 1
1458 . 127 TRP HE1 H 9.98 0.025 1
1459 . 127 TRP HZ3 H 6.66 0.025 1
1460 . 127 TRP CH2 C 125.5 0.4 1
1461 . 127 TRP HZ2 H 7.41 0.025 1
1462 . 127 TRP HH2 H 7.06 0.025 1
1463 . 127 TRP C C 173.3 0.4 1
1464 . 128 ALA N N 124.0 0.4 1
1465 . 128 ALA H H 7.58 0.025 1
1466 . 128 ALA CA C 52.9 0.4 1
1467 . 128 ALA HA H 3.72 0.025 1
1468 . 128 ALA HB H 0.71 0.025 1
1469 . 128 ALA CB C 20.7 0.4 1
1470 . 128 ALA C C 181.1 0.4 1
stop_
save_