data_5583
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
NMR structure of P41icf, a potent inhibitor of human cathepsin L
;
_BMRB_accession_number 5583
_BMRB_flat_file_name bmr5583.str
_Entry_type original
_Submission_date 2002-11-06
_Accession_date 2002-11-06
_Entry_origination author
_NMR_STAR_version 2.1.1
_Experimental_method NMR
_Details .
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Chiva C. . .
2 Barthe P. . .
3 Codina A. . .
4 Giralt E. . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
coupling_constants 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 339
"coupling constants" 42
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2003-05-14 original author .
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'Synthesis and NMR Structure of P41icf, a Potent Inhibitor of Human Cathepsin L'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 22456786
_PubMed_ID 12568610
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Chiva C. . .
2 Barthe P. . .
3 Codina A. . .
4 Gairi M. . .
5 Molina F. . .
6 Granier C. . .
7 Pugniere M. . .
8 Inui T. . .
9 Nishio H. . .
10 Nishiuchi Y. . .
11 Kimura T. . .
12 Sakakibara S. . .
13 Albericio F. . .
14 Giralt E. . .
stop_
_Journal_abbreviation 'J. Am. Chem. Soc.'
_Journal_volume 125
_Journal_issue 6
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 1508
_Page_last 1517
_Year 2003
_Details .
loop_
_Keyword
'ALPHA HELIX'
'BETA SHEET'
'DISULFIDE BONDS'
stop_
save_
##################################
# Molecular system description #
##################################
save_system_P41icf
_Saveframe_category molecular_system
_Mol_system_name 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT (P41icf)'
_Abbreviation_common 'p41 fragment, P41icf'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' $P41icf
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all disulfide bound'
loop_
_Biological_function
'Human cathepsin L inhibitor'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_P41icf
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT (P41icf)'
_Abbreviation_common 'P41 fragment'
_Molecular_mass 7246
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 65
_Mol_residue_sequence
;
LTKCQEEVSHIPAVHPGSFR
PKCDENGNYLPLQCYGSIGY
CWCVFPNGTEVPNTRSRGHH
NCSES
;
loop_
_Residue_seq_code
_Residue_label
1 LEU 2 THR 3 LYS 4 CYS 5 GLN
6 GLU 7 GLU 8 VAL 9 SER 10 HIS
11 ILE 12 PRO 13 ALA 14 VAL 15 HIS
16 PRO 17 GLY 18 SER 19 PHE 20 ARG
21 PRO 22 LYS 23 CYS 24 ASP 25 GLU
26 ASN 27 GLY 28 ASN 29 TYR 30 LEU
31 PRO 32 LEU 33 GLN 34 CYS 35 TYR
36 GLY 37 SER 38 ILE 39 GLY 40 TYR
41 CYS 42 TRP 43 CYS 44 VAL 45 PHE
46 PRO 47 ASN 48 GLY 49 THR 50 GLU
51 VAL 52 PRO 53 ASN 54 THR 55 ARG
56 SER 57 ARG 58 GLY 59 HIS 60 HIS
61 ASN 62 CYS 63 SER 64 GLU 65 SER
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-01-28
loop_
_Database_name
_Database_accession_code
_Database_entry_mol_name
_Sequence_query_to_submitted_percentage
_Sequence_subject_length
_Sequence_identity
_Sequence_positive
_Sequence_homology_expectation_value
PDB 1ICF "Crystal Structure Of Mhc Class Ii Associated P41 Ii Fragment In Complex With Cathepsin L" 100.00 65 100.00 100.00 4.05e-40
PDB 1L3H "Nmr Structure Of P41icf, A Potent Inhibitor Of Human Cathepsin L" 98.46 65 100.00 100.00 2.26e-39
DBJ BAG60210 "unnamed protein product [Homo sapiens]" 100.00 296 100.00 100.00 3.47e-40
GB AAA35996 "protein 41, partial [Homo sapiens]" 100.00 71 100.00 100.00 3.77e-40
GB EAW61731 "CD74 antigen (invariant polypeptide of major histocompatibility complex, class II antigen-associated), isoform CRA_c [Homo sapi" 100.00 296 100.00 100.00 3.47e-40
REF NP_001020330 "HLA class II histocompatibility antigen gamma chain isoform a [Homo sapiens]" 100.00 296 100.00 100.00 3.47e-40
REF XP_003266686 "PREDICTED: HLA class II histocompatibility antigen gamma chain isoform 2 [Nomascus leucogenys]" 100.00 296 100.00 100.00 3.23e-40
REF XP_003829068 "PREDICTED: HLA class II histocompatibility antigen gamma chain isoform X1 [Pan paniscus]" 100.00 296 100.00 100.00 3.47e-40
REF XP_004042860 "PREDICTED: HLA class II histocompatibility antigen gamma chain isoform 2 [Gorilla gorilla gorilla]" 100.00 296 98.46 98.46 1.97e-39
REF XP_008986092 "PREDICTED: HLA class II histocompatibility antigen gamma chain isoform X1 [Callithrix jacchus]" 100.00 280 98.46 98.46 7.69e-41
SP P04233 "RecName: Full=HLA class II histocompatibility antigen gamma chain; AltName: Full=HLA-DR antigens-associated invariant chain; Al" 100.00 296 100.00 100.00 3.47e-40
stop_
save_
########################################
# Molecular bond linkage definitions #
########################################
save_crosslink_bonds
_Saveframe_category crosslink_bonds
loop_
_Bond_order
_Bond_type
_Atom_one_mol_system_component_name
_Atom_one_residue_seq_code
_Atom_one_residue_label
_Atom_one_atom_name
_Atom_two_mol_system_component_name
_Atom_two_residue_seq_code
_Atom_two_residue_label
_Atom_two_atom_name
single disulfide 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' 4 CYS SG 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' 23 CYS SG
single disulfide 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' 34 CYS SG 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' 41 CYS SG
single disulfide 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' 43 CYS SG 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' 62 CYS SG
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$P41icf 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
$P41icf 'chemical synthesis' . . . . .
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
$P41icf 1 mM .
phosphate_buffer 20 mM .
NaN3 0.01 mM .
H20 85 % .
D2O 15 % .
stop_
save_
############################
# Computer software used #
############################
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version .
loop_
_Task
processing
stop_
_Details Delaglio
save_
save_NMRview
_Saveframe_category software
_Name NMRview
_Version .
loop_
_Task
'data analysis'
stop_
_Details Johnson
save_
save_DYANA
_Saveframe_category software
_Name DYANA
_Version 1.5
loop_
_Task
'structure solution'
stop_
_Details Guntert
save_
save_AMBER
_Saveframe_category software
_Name AMBER
_Version 5.0
loop_
_Task
refinement
stop_
_Details Case
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_DQF-COSY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name DQF-COSY
_Sample_label .
save_
save_2D_TOCSY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D TOCSY'
_Sample_label .
save_
save_2D_NOESY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_Sample_label .
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name DQF-COSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D TOCSY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 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 5.7 0.2 n/a
temperature 288 0.1 K
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
DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0
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 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT'
_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 LEU HA H 4.18 . 1
2 . 1 LEU HB2 H 1.76 . 1
3 . 1 LEU HD1 H 0.82 . 1
4 . 1 LEU HG H 1.67 . 1
5 . 2 THR H H 8.73 . 1
6 . 2 THR HA H 4.47 . 1
7 . 2 THR HB H 4.73 . 1
8 . 2 THR HG2 H 1.20 . 1
9 . 3 LYS H H 8.8 . 1
10 . 3 LYS HA H 4.02 . 1
11 . 3 LYS HB2 H 1.96 . 1
12 . 3 LYS HG2 H 1.67 . 1
13 . 3 LYS HG3 H 1.57 . 1
14 . 3 LYS HD2 H 1.81 . 1
15 . 3 LYS HE2 H 3.08 . 1
16 . 3 LYS HZ H 7.54 . 1
17 . 4 CYS H H 8.69 . 1
18 . 4 CYS HA H 3.49 . 1
19 . 4 CYS HB2 H 2.47 . 1
20 . 4 CYS HB3 H 1.16 . 1
21 . 5 GLN H H 7.41 . 1
22 . 5 GLN HA H 3.72 . 1
23 . 5 GLN HB2 H 2.22 . 1
24 . 5 GLN HG2 H 2.32 . 1
25 . 5 GLN HE21 H 7.59 . 1
26 . 5 GLN HE22 H 6.84 . 1
27 . 6 GLU H H 8.8 . 1
28 . 6 GLU HA H 3.92 . 1
29 . 6 GLU HB2 H 2.14 . 1
30 . 6 GLU HG2 H 2.44 . 1
31 . 6 GLU HG3 H 2.36 . 1
32 . 7 GLU H H 8.14 . 1
33 . 7 GLU HA H 4.05 . 1
34 . 7 GLU HB2 H 2.28 . 1
35 . 7 GLU HB3 H 2.07 . 1
36 . 7 GLU HG2 H 2.65 . 1
37 . 7 GLU HG3 H 2.39 . 1
38 . 8 VAL H H 7.95 . 1
39 . 8 VAL HA H 3.65 . 1
40 . 8 VAL HB H 2.05 . 1
41 . 8 VAL HG1 H 1.01 . 1
42 . 8 VAL HG2 H 0.86 . 1
43 . 9 SER H H 7.71 . 1
44 . 9 SER HA H 4.25 . 1
45 . 9 SER HB2 H 3.81 . 1
46 . 10 HIS H H 7.66 . 1
47 . 10 HIS HA H 4.75 . 1
48 . 10 HIS HB2 H 3.42 . 1
49 . 10 HIS HB3 H 3.17 . 1
50 . 10 HIS HD2 H 7.28 . 1
51 . 10 HIS HE1 H 8.56 . 1
52 . 11 ILE H H 7.8 . 1
53 . 11 ILE HA H 4.45 . 1
54 . 11 ILE HB H 1.75 . 1
55 . 11 ILE HG2 H 0.88 . 1
56 . 11 ILE HG12 H 1.15 . 1
57 . 11 ILE HD1 H 0.86 . 1
58 . 12 PRO HA H 4.35 . 1
59 . 12 PRO HB2 H 2.3 . 1
60 . 12 PRO HB3 H 1.98 . 1
61 . 12 PRO HG2 H 2.08 . 1
62 . 12 PRO HD2 H 3.86 . 1
63 . 13 ALA H H 8.26 . 1
64 . 13 ALA HA H 4.1 . 1
65 . 13 ALA HB H 1.37 . 1
66 . 14 VAL H H 7.81 . 1
67 . 14 VAL HA H 3.95 . 1
68 . 14 VAL HB H 1.98 . 1
69 . 14 VAL HG1 H 0.84 . 1
70 . 14 VAL HG2 H 0.77 . 1
71 . 15 HIS H H 8.43 . 1
72 . 15 HIS HA H 5.03 . 1
73 . 15 HIS HB2 H 3.21 . 1
74 . 15 HIS HB3 H 3.12 . 1
75 . 15 HIS HD2 H 7.36 . 1
76 . 15 HIS HE1 H 8.67 . 1
77 . 16 PRO HA H 4.37 . 1
78 . 16 PRO HB2 H 2.31 . 1
79 . 16 PRO HB3 H 1.97 . 1
80 . 16 PRO HG2 H 2.15 . 1
81 . 16 PRO HG3 H 2.04 . 1
82 . 16 PRO HD2 H 3.59 . 1
83 . 17 GLY H H 8.84 . 1
84 . 17 GLY HA2 H 4.1 . 1
85 . 17 GLY HA3 H 4.01 . 1
86 . 18 SER H H 7.99 . 1
87 . 18 SER HA H 4.66 . 1
88 . 18 SER HB2 H 3.88 . 1
89 . 19 PHE H H 8.55 . 1
90 . 19 PHE HA H 4.29 . 1
91 . 19 PHE HB2 H 2.54 . 1
92 . 19 PHE HB3 H 2.36 . 1
93 . 19 PHE HD1 H 7.11 . 1
94 . 19 PHE HE1 H 7.38 . 1
95 . 19 PHE HZ H 6.93 . 1
96 . 20 ARG H H 7.62 . 1
97 . 20 ARG HA H 4.35 . 1
98 . 20 ARG HB2 H 1.2 . 1
99 . 20 ARG HG2 H 1.57 . 1
100 . 20 ARG HG3 H 1.42 . 1
101 . 20 ARG HD2 H 3.14 . 1
102 . 20 ARG HD3 H 3.04 . 1
103 . 20 ARG HE H 7.15 . 1
104 . 21 PRO HA H 4.37 . 1
105 . 21 PRO HB2 H 2.31 . 1
106 . 21 PRO HB3 H 2.15 . 1
107 . 21 PRO HG2 H 1.95 . 1
108 . 21 PRO HD2 H 3.25 . 1
109 . 22 LYS H H 8.95 . 1
110 . 22 LYS HA H 4.54 . 1
111 . 22 LYS HB2 H 1.83 . 1
112 . 22 LYS HG2 H 1.56 . 1
113 . 22 LYS HG3 H 1.42 . 1
114 . 22 LYS HD2 H 1.70 . 1
115 . 22 LYS HE2 H 2.99 . 1
116 . 22 LYS HZ H 7.52 . 1
117 . 23 CYS H H 8.6 . 1
118 . 23 CYS HA H 5.26 . 1
119 . 23 CYS HB2 H 2.71 . 1
120 . 23 CYS HB3 H 2.49 . 1
121 . 24 ASP H H 9.08 . 1
122 . 24 ASP HA H 4.64 . 1
123 . 24 ASP HB2 H 3.33 . 1
124 . 24 ASP HB3 H 2.62 . 1
125 . 25 GLU H H 8.71 . 1
126 . 25 GLU HA H 4.09 . 1
127 . 25 GLU HB2 H 2.07 . 1
128 . 25 GLU HG2 H 2.44 . 1
129 . 26 ASN H H 8.04 . 1
130 . 26 ASN HA H 4.81 . 1
131 . 26 ASN HB2 H 2.91 . 1
132 . 26 ASN HB3 H 2.69 . 1
133 . 26 ASN HD21 H 7.82 . 1
134 . 26 ASN HD22 H 6.94 . 1
135 . 27 GLY H H 8.14 . 1
136 . 27 GLY HA2 H 4.2 . 1
137 . 27 GLY HA3 H 3.36 . 1
138 . 28 ASN H H 8.73 . 1
139 . 28 ASN HA H 4.85 . 1
140 . 28 ASN HB2 H 2.97 . 1
141 . 28 ASN HB3 H 2.75 . 1
142 . 28 ASN HD21 H 8.44 . 1
143 . 28 ASN HD22 H 7.27 . 1
144 . 29 TYR H H 8.79 . 1
145 . 29 TYR HA H 4.47 . 1
146 . 29 TYR HB2 H 2.8 . 1
147 . 29 TYR HB3 H 2.58 . 1
148 . 29 TYR HD1 H 7.15 . 1
149 . 29 TYR HE1 H 6.62 . 1
150 . 30 LEU H H 7.93 . 1
151 . 30 LEU HA H 4.46 . 1
152 . 30 LEU HB2 H 1.62 . 1
153 . 30 LEU HD1 H 0.92 . 1
154 . 30 LEU HD2 H 0.84 . 1
155 . 30 LEU HG H 1.47 . 1
156 . 31 PRO HA H 4.17 . 1
157 . 31 PRO HB2 H 2.32 . 1
158 . 31 PRO HB3 H 1.77 . 1
159 . 31 PRO HG2 H 2.01 . 1
160 . 31 PRO HD2 H 3.85 . 1
161 . 31 PRO HD3 H 3.69 . 1
162 . 32 LEU H H 6.81 . 1
163 . 32 LEU HA H 4.78 . 1
164 . 32 LEU HB2 H 1.63 . 1
165 . 32 LEU HD1 H 0.62 . 1
166 . 32 LEU HD2 H 0.27 . 1
167 . 32 LEU HG H 1.09 . 1
168 . 33 GLN H H 8.55 . 1
169 . 33 GLN HA H 4.17 . 1
170 . 33 GLN HB2 H 1.78 . 1
171 . 33 GLN HB3 H 0.33 . 1
172 . 33 GLN HG2 H 2.32 . 1
173 . 33 GLN HG3 H 2.16 . 1
174 . 33 GLN HE21 H 8.85 . 1
175 . 33 GLN HE22 H 8.18 . 1
176 . 34 CYS H H 8.47 . 1
177 . 34 CYS HA H 4.85 . 1
178 . 34 CYS HB2 H 2.92 . 1
179 . 34 CYS HB3 H 2.77 . 1
180 . 35 TYR H H 8.37 . 1
181 . 35 TYR HA H 5.15 . 1
182 . 35 TYR HB2 H 3.41 . 1
183 . 35 TYR HB3 H 3.27 . 1
184 . 35 TYR HD1 H 7.35 . 1
185 . 35 TYR HE1 H 6.90 . 1
186 . 36 GLY H H 8.64 . 1
187 . 36 GLY HA2 H 4.18 . 1
188 . 36 GLY HA3 H 3.71 . 1
189 . 37 SER H H 8.37 . 1
190 . 37 SER HA H 4.22 . 1
191 . 37 SER HB2 H 3.76 . 1
192 . 38 ILE H H 7.34 . 1
193 . 38 ILE HA H 4.36 . 1
194 . 38 ILE HB H 2.0 . 1
195 . 38 ILE HG2 H 0.87 . 1
196 . 38 ILE HG12 H 1.48 . 1
197 . 38 ILE HG13 H 1.09 . 1
198 . 38 ILE HD1 H 0.75 . 1
199 . 39 GLY H H 7.88 . 1
200 . 39 GLY HA2 H 4.08 . 1
201 . 39 GLY HA3 H 3.71 . 1
202 . 40 TYR H H 7.78 . 1
203 . 40 TYR HA H 4.83 . 1
204 . 40 TYR HB2 H 2.99 . 1
205 . 40 TYR HD1 H 6.96 . 1
206 . 40 TYR HD2 H 6.78 . 1
207 . 41 CYS H H 8.89 . 1
208 . 41 CYS HA H 5.49 . 1
209 . 41 CYS HB2 H 2.83 . 1
210 . 41 CYS HB3 H 2.58 . 1
211 . 42 TRP H H 9.39 . 1
212 . 42 TRP HA H 5.32 . 1
213 . 42 TRP HB2 H 3.12 . 1
214 . 42 TRP HB3 H 3.06 . 1
215 . 42 TRP HD1 H 6.76 . 1
216 . 42 TRP HE1 H 9.86 . 1
217 . 42 TRP HE3 H 6.36 . 1
218 . 42 TRP HZ2 H 6.93 . 1
219 . 42 TRP HZ3 H 6.21 . 1
220 . 42 TRP HH2 H 6.75 . 1
221 . 43 CYS H H 8.4 . 1
222 . 43 CYS HA H 6.06 . 1
223 . 43 CYS HB2 H 3.3 . 1
224 . 43 CYS HB3 H 2.57 . 1
225 . 44 VAL H H 9.29 . 1
226 . 44 VAL HA H 5.24 . 1
227 . 44 VAL HB H 1.87 . 1
228 . 44 VAL HG1 H 0.78 . 1
229 . 45 PHE H H 8.79 . 1
230 . 45 PHE HA H 4.77 . 1
231 . 45 PHE HB2 H 3.39 . 1
232 . 45 PHE HB3 H 2.78 . 1
233 . 45 PHE HD1 H 7.30 . 1
234 . 45 PHE HE1 H 7.37 . 1
235 . 45 PHE HZ H 7.10 . 1
236 . 46 PRO HA H 4.63 . 1
237 . 46 PRO HB2 H 2.49 . 1
238 . 46 PRO HB3 H 1.97 . 1
239 . 46 PRO HG2 H 2.23 . 1
240 . 46 PRO HG3 H 2.11 . 1
241 . 46 PRO HD2 H 4.11 . 1
242 . 46 PRO HD3 H 3.98 . 1
243 . 47 ASN H H 7.52 . 1
244 . 47 ASN HA H 4.72 . 1
245 . 47 ASN HB2 H 3.29 . 1
246 . 47 ASN HB3 H 2.86 . 1
247 . 47 ASN HD21 H 7.64 . 1
248 . 47 ASN HD22 H 6.8 . 1
249 . 48 GLY H H 8.69 . 1
250 . 48 GLY HA2 H 3.22 . 1
251 . 48 GLY HA3 H 2.16 . 1
252 . 49 THR H H 7.68 . 1
253 . 49 THR HA H 4.18 . 1
254 . 49 THR HB H 4.3 . 1
255 . 49 THR HG2 H 1.23 . 1
256 . 50 GLU H H 8.6 . 1
257 . 50 GLU HA H 4.37 . 1
258 . 50 GLU HB2 H 1.8 . 1
259 . 50 GLU HB3 H 1.71 . 1
260 . 50 GLU HG2 H 2.22 . 1
261 . 50 GLU HG3 H 2.03 . 1
262 . 51 VAL H H 8.89 . 1
263 . 51 VAL HA H 3.9 . 1
264 . 51 VAL HB H 1.54 . 1
265 . 51 VAL HG1 H 0.74 . 1
266 . 51 VAL HG2 H -0.37 . 1
267 . 52 PRO HA H 4.25 . 1
268 . 52 PRO HB2 H 2.3 . 1
269 . 52 PRO HB3 H 1.86 . 1
270 . 52 PRO HG2 H 2.16 . 1
271 . 52 PRO HG3 H 2.03 . 1
272 . 52 PRO HD2 H 4.31 . 1
273 . 52 PRO HD3 H 3.77 . 1
274 . 53 ASN H H 8.89 . 1
275 . 53 ASN HA H 4.51 . 1
276 . 53 ASN HB2 H 3.05 . 1
277 . 53 ASN HB3 H 2.92 . 1
278 . 53 ASN HD21 H 7.66 . 1
279 . 53 ASN HD22 H 6.98 . 1
280 . 54 THR H H 7.92 . 1
281 . 54 THR HA H 4.65 . 1
282 . 54 THR HB H 4.61 . 1
283 . 54 THR HG2 H 1.03 . 1
284 . 55 ARG H H 8.11 . 1
285 . 55 ARG HA H 5.46 . 1
286 . 55 ARG HB2 H 1.85 . 1
287 . 55 ARG HG2 H 1.48 . 1
288 . 55 ARG HD2 H 2.83 . 1
289 . 55 ARG HD3 H 2.74 . 1
290 . 55 ARG HE H 7.05 . 1
291 . 56 SER H H 9.41 . 1
292 . 56 SER HA H 4.77 . 1
293 . 56 SER HB2 H 3.92 . 1
294 . 56 SER HB3 H 3.84 . 1
295 . 57 ARG H H 8.81 . 1
296 . 57 ARG HA H 4.29 . 1
297 . 57 ARG HB2 H 1.73 . 1
298 . 57 ARG HB3 H 1.51 . 1
299 . 57 ARG HG2 H 1.25 . 1
300 . 57 ARG HG3 H 1.02 . 1
301 . 57 ARG HD2 H 2.96 . 1
302 . 57 ARG HE H 6.97 . 1
303 . 58 GLY H H 8.18 . 1
304 . 58 GLY HA2 H 4.03 . 1
305 . 58 GLY HA3 H 3.99 . 1
306 . 59 HIS H H 8.57 . 1
307 . 59 HIS HA H 4.22 . 1
308 . 59 HIS HB2 H 3.1 . 1
309 . 59 HIS HB3 H 3.07 . 1
310 . 59 HIS HD2 H 7.21 . 1
311 . 59 HIS HE1 H 8.53 . 1
312 . 60 HIS H H 7.35 . 1
313 . 60 HIS HA H 4.67 . 1
314 . 60 HIS HB2 H 3.35 . 1
315 . 60 HIS HB3 H 3.12 . 1
316 . 60 HIS HD2 H 7.27 . 1
317 . 60 HIS HE1 H 8.60 . 1
318 . 61 ASN H H 8.85 . 1
319 . 61 ASN HA H 4.75 . 1
320 . 61 ASN HB2 H 2.84 . 1
321 . 61 ASN HB3 H 2.73 . 1
322 . 61 ASN HD21 H 7.65 . 1
323 . 61 ASN HD22 H 7.01 . 1
324 . 62 CYS H H 8.71 . 1
325 . 62 CYS HA H 4.92 . 1
326 . 62 CYS HB2 H 3.25 . 1
327 . 62 CYS HB3 H 2.55 . 1
328 . 63 SER H H 8.55 . 1
329 . 63 SER HA H 4.45 . 1
330 . 63 SER HB2 H 3.87 . 1
331 . 64 GLU H H 8.47 . 1
332 . 64 GLU HA H 4.46 . 1
333 . 64 GLU HB2 H 2.2 . 1
334 . 64 GLU HB3 H 1.99 . 1
335 . 64 GLU HG2 H 2.46 . 1
336 . 65 SER H H 8.27 . 1
337 . 65 SER HA H 4.42 . 1
338 . 65 SER HB2 H 3.93 . 1
339 . 65 SER HB3 H 3.89 . 1
stop_
save_
########################
# Coupling constants #
########################
save_J_values_set_1
_Saveframe_category coupling_constants
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Spectrometer_frequency_1H 600
_Mol_system_component_name 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT'
_Text_data_format .
_Text_data .
loop_
_Coupling_constant_ID
_Coupling_constant_code
_Atom_one_residue_seq_code
_Atom_one_residue_label
_Atom_one_name
_Atom_two_residue_seq_code
_Atom_two_residue_label
_Atom_two_name
_Coupling_constant_value
_Coupling_constant_min_value
_Coupling_constant_max_value
_Coupling_constant_value_error
1 3JHNHA 2 THR H 2 THR HA 8.3 . . .
2 3JHNHA 4 CYS H 4 CYS HA 4.9 . . .
3 3JHNHA 5 GLN H 5 GLN HA 6.4 . . .
4 3JHNHA 6 GLU H 6 GLU HA 5.0 . . .
5 3JHNHA 7 GLU H 7 GLU HA 3.8 . . .
6 3JHNHA 8 VAL H 8 VAL HA 6.0 . . .
7 3JHNHA 9 SER H 9 SER HA 3.8 . . .
8 3JHNHA 11 ILE H 11 ILE HA 7.9 . . .
9 3JHNHA 13 ALA H 13 ALA HA 5.4 . . .
10 3JHNHA 14 VAL H 14 VAL HA 4.9 . . .
11 3JHNHA 15 HIS H 15 HIS HA 8.0 . . .
12 3JHNHA 19 PHE H 19 PHE HA 6.8 . . .
13 3JHNHA 20 ARG H 20 ARG HA 8.2 . . .
14 3JHNHA 22 LYS H 22 LYS HA 9.8 . . .
15 3JHNHA 23 CYS H 23 CYS HA 10.2 . . .
16 3JHNHA 24 ASP H 24 ASP HA 6.8 . . .
17 3JHNHA 25 GLU H 25 GLU HA 4.3 . . .
18 3JHNHA 26 ASN H 26 ASN HA 9.6 . . .
19 3JHNHA 28 ASN H 28 ASN HA 3.8 . . .
20 3JHNHA 30 LEU H 30 LEU HA 6.8 . . .
21 3JHNHA 33 GLN H 33 GLN HA 9.1 . . .
22 3JHNHA 34 CYS H 34 CYS HA 8.1 . . .
23 3JHNHA 35 TYR H 35 TYR HA 9.7 . . .
24 3JHNHA 37 SER H 37 SER HA 5.8 . . .
25 3JHNHA 38 ILE H 38 ILE HA 6.9 . . .
26 3JHNHA 40 TYR H 40 TYR HA 9.5 . . .
27 3JHNHA 41 CYS H 41 CYS HA 10.8 . . .
28 3JHNHA 42 TRP H 42 TRP HA 11.9 . . .
29 3JHNHA 43 CYS H 43 CYS HA 9.8 . . .
30 3JHNHA 44 VAL H 44 VAL HA 12.2 . . .
31 3JHNHA 45 PHE H 45 PHE HA 7.7 . . .
32 3JHNHA 49 THR H 49 THR HA 5.0 . . .
33 3JHNHA 50 GLU H 50 GLU HA 4.4 . . .
34 3JHNHA 51 VAL H 51 VAL HA 8.6 . . .
35 3JHNHA 53 ASN H 53 ASN HA 6.8 . . .
36 3JHNHA 55 ARG H 55 ARG HA 7.9 . . .
37 3JHNHA 57 ARG H 57 ARG HA 6.2 . . .
38 3JHNHA 60 HIS H 60 HIS HA 15.6 . . .
39 3JHNHA 62 CYS H 62 CYS HA 8.3 . . .
40 3JHNHA 63 SER H 63 SER HA 7.7 . . .
41 3JHNHA 64 GLU H 64 GLU HA 7.3 . . .
42 3JHNHA 65 SER H 65 SER HA 6.5 . . .
stop_
save_