data_17016
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
solution structure of the CARMIL CAH3a/b domain bound to capping protein (CP_
;
_BMRB_accession_number 17016
_BMRB_flat_file_name bmr17016.str
_Entry_type original
_Submission_date 2010-06-23
_Accession_date 2010-06-23
_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 Zwolak Adam . .
2 Nico Tjandra . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 3
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 474
"13C chemical shifts" 1504
"15N chemical shifts" 474
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2012-11-07 update BMRB 'switch the shifts of C and CB of residue 111 TYR'
2012-11-07 update BMRB 'switch the shifts of H and N of residue 26 SER, 127 ALA, 163 ARG'
2012-10-31 update BMRB 'switch the shifts of H and N of residue 238 GLU'
2010-09-15 update BMRB 'complete entry citation'
2010-08-12 original author 'original release'
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'Molecular basis for barbed end uncapping by CARMIL homology domain 3 of mouse CARMIL-1.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 20630878
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Zwolak Adam . .
2 Uruno Takehito . .
3 Piszczek Grzegorz . .
4 Hammer John A. 3rd
5 Tjandra Nico . .
stop_
_Journal_abbreviation 'J. Biol. Chem.'
_Journal_name_full 'The Journal of biological chemistry'
_Journal_volume 285
_Journal_issue 37
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 29014
_Page_last 29026
_Year 2010
_Details .
save_
##################################
# Molecular system description #
##################################
save_assembly
_Saveframe_category molecular_system
_Mol_system_name 'CARMIL CAH3a/b domain bound to capping protein'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
CPalpha_subunit $CPalpha_subunit
CPbeta_subunit $CPbeta_subunit
CARMIL_CAH3a_b_domain $CARMIL_CAH3a_b_domain
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state ?
_System_paramagnetic no
_System_thiol_state .
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_CPalpha_subunit
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common CPalpha_subunit
_Molecular_mass .
_Mol_thiol_state 'all free'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 286
_Mol_residue_sequence
;
MADFEDRVSDEEKVRIAAKF
ITHAPPGEFNEVFNDVRLLL
NNDNLLREGAAHAFAQYNMD
QFTPVKIEGYDDQVLITEHG
DLGNSRFLDPRNQISFKFDH
LRKEASDPQPEDVDGGLKSW
RESCDSALRAYVKDHYSNGF
CTVYAKTIDGQQTIIACIES
HQFQPKNFWNGRWRSEWKFT
ITPPSAQVVAVLKIQVHYYE
DGNVQLVSHKDVQDSVTVSN
EVQTAKEFIKIIESAENEYQ
TAISENYQTMSDTTFKALRR
QLPVTRTKIDWNKILSYKIG
KEMQNA
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 ALA 3 ASP 4 PHE 5 GLU
6 ASP 7 ARG 8 VAL 9 SER 10 ASP
11 GLU 12 GLU 13 LYS 14 VAL 15 ARG
16 ILE 17 ALA 18 ALA 19 LYS 20 PHE
21 ILE 22 THR 23 HIS 24 ALA 25 PRO
26 PRO 27 GLY 28 GLU 29 PHE 30 ASN
31 GLU 32 VAL 33 PHE 34 ASN 35 ASP
36 VAL 37 ARG 38 LEU 39 LEU 40 LEU
41 ASN 42 ASN 43 ASP 44 ASN 45 LEU
46 LEU 47 ARG 48 GLU 49 GLY 50 ALA
51 ALA 52 HIS 53 ALA 54 PHE 55 ALA
56 GLN 57 TYR 58 ASN 59 MET 60 ASP
61 GLN 62 PHE 63 THR 64 PRO 65 VAL
66 LYS 67 ILE 68 GLU 69 GLY 70 TYR
71 ASP 72 ASP 73 GLN 74 VAL 75 LEU
76 ILE 77 THR 78 GLU 79 HIS 80 GLY
81 ASP 82 LEU 83 GLY 84 ASN 85 SER
86 ARG 87 PHE 88 LEU 89 ASP 90 PRO
91 ARG 92 ASN 93 GLN 94 ILE 95 SER
96 PHE 97 LYS 98 PHE 99 ASP 100 HIS
101 LEU 102 ARG 103 LYS 104 GLU 105 ALA
106 SER 107 ASP 108 PRO 109 GLN 110 PRO
111 GLU 112 ASP 113 VAL 114 ASP 115 GLY
116 GLY 117 LEU 118 LYS 119 SER 120 TRP
121 ARG 122 GLU 123 SER 124 CYS 125 ASP
126 SER 127 ALA 128 LEU 129 ARG 130 ALA
131 TYR 132 VAL 133 LYS 134 ASP 135 HIS
136 TYR 137 SER 138 ASN 139 GLY 140 PHE
141 CYS 142 THR 143 VAL 144 TYR 145 ALA
146 LYS 147 THR 148 ILE 149 ASP 150 GLY
151 GLN 152 GLN 153 THR 154 ILE 155 ILE
156 ALA 157 CYS 158 ILE 159 GLU 160 SER
161 HIS 162 GLN 163 PHE 164 GLN 165 PRO
166 LYS 167 ASN 168 PHE 169 TRP 170 ASN
171 GLY 172 ARG 173 TRP 174 ARG 175 SER
176 GLU 177 TRP 178 LYS 179 PHE 180 THR
181 ILE 182 THR 183 PRO 184 PRO 185 SER
186 ALA 187 GLN 188 VAL 189 VAL 190 ALA
191 VAL 192 LEU 193 LYS 194 ILE 195 GLN
196 VAL 197 HIS 198 TYR 199 TYR 200 GLU
201 ASP 202 GLY 203 ASN 204 VAL 205 GLN
206 LEU 207 VAL 208 SER 209 HIS 210 LYS
211 ASP 212 VAL 213 GLN 214 ASP 215 SER
216 VAL 217 THR 218 VAL 219 SER 220 ASN
221 GLU 222 VAL 223 GLN 224 THR 225 ALA
226 LYS 227 GLU 228 PHE 229 ILE 230 LYS
231 ILE 232 ILE 233 GLU 234 SER 235 ALA
236 GLU 237 ASN 238 GLU 239 TYR 240 GLN
241 THR 242 ALA 243 ILE 244 SER 245 GLU
246 ASN 247 TYR 248 GLN 249 THR 250 MET
251 SER 252 ASP 253 THR 254 THR 255 PHE
256 LYS 257 ALA 258 LEU 259 ARG 260 ARG
261 GLN 262 LEU 263 PRO 264 VAL 265 THR
266 ARG 267 THR 268 LYS 269 ILE 270 ASP
271 TRP 272 ASN 273 LYS 274 ILE 275 LEU
276 SER 277 TYR 278 LYS 279 ILE 280 GLY
281 LYS 282 GLU 283 MET 284 GLN 285 ASN
286 ALA
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-07-08
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
DBJ BAE27053 "unnamed protein product [Mus musculus]" 93.71 290 98.13 98.88 0.00e+00
DBJ BAE27635 "unnamed protein product [Mus musculus]" 100.00 286 98.95 99.30 0.00e+00
DBJ BAE28985 "unnamed protein product [Mus musculus]" 100.00 286 98.95 99.30 0.00e+00
DBJ BAE30242 "unnamed protein product [Mus musculus]" 100.00 286 98.60 99.30 0.00e+00
DBJ BAE31154 "unnamed protein product [Mus musculus]" 100.00 286 98.95 99.30 0.00e+00
GB AAC00566 "capping protein alpha 1 subunit, partial [Mus musculus]" 99.30 284 98.94 99.30 0.00e+00
GB AAH16232 "Capping protein (actin filament) muscle Z-line, alpha 1 [Mus musculus]" 100.00 286 99.30 99.30 0.00e+00
GB AAH85506 "Capping protein (actin filament) muscle Z-line, alpha 1 [Mus musculus]" 100.00 286 98.95 99.30 0.00e+00
GB AAI66464 "Capping protein (actin filament) muscle Z-line, alpha 1 [Rattus norvegicus]" 100.00 286 98.60 99.65 0.00e+00
GB EDL07559 "capping protein (actin filament) muscle Z-line, alpha 1 [Mus musculus]" 100.00 286 98.95 99.30 0.00e+00
REF NP_001103095 "F-actin-capping protein subunit alpha-1 [Rattus norvegicus]" 100.00 286 98.60 99.65 0.00e+00
REF NP_033927 "F-actin-capping protein subunit alpha-1 [Mus musculus]" 100.00 286 98.95 99.30 0.00e+00
REF XP_002715812 "PREDICTED: F-actin-capping protein subunit alpha-1 [Oryctolagus cuniculus]" 100.00 286 97.20 99.65 0.00e+00
REF XP_002918295 "PREDICTED: F-actin-capping protein subunit alpha-1 [Ailuropoda melanoleuca]" 100.00 286 97.90 98.95 0.00e+00
REF XP_003990521 "PREDICTED: F-actin-capping protein subunit alpha-1 [Felis catus]" 100.00 286 98.25 99.30 0.00e+00
SP B2GUZ5 "RecName: Full=F-actin-capping protein subunit alpha-1; AltName: Full=CapZ alpha-1" 100.00 286 98.60 99.65 0.00e+00
SP P47753 "RecName: Full=F-actin-capping protein subunit alpha-1; AltName: Full=CapZ alpha-1" 100.00 286 99.30 99.30 0.00e+00
stop_
save_
save_CPbeta_subunit
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common CPbeta_subunit
_Molecular_mass .
_Mol_thiol_state 'all free'
_Details .
_Residue_count 277
_Mol_residue_sequence
;
MSDQQLDCALDLMRRLPPQQ
IEKNLSDLIDLVPSLCEDLL
SSVDQPLKIARDKVVGKDYL
LCDYNRDGDSYRSPWSNKYD
PPLEDGAMPSARLRKLEVEA
NNAFDQYRDLYFEGGVSSVY
LWDLDHGFAGVILIKKAGDG
SKKIKGCWDSIHVVEVQEKS
SGRTAHYKLTSTVMLWLQTN
KTGSGTMNLGGSLTRQMEKD
ETVSDSSPHIANIGRLVEDM
ENKIRSTLNEIYFGKTKDIV
NGLRSVQTFADKSKQEALKN
DLVEALKRKQQCIQPDN
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 SER 3 ASP 4 GLN 5 GLN
6 LEU 7 ASP 8 CYS 9 ALA 10 LEU
11 ASP 12 LEU 13 MET 14 ARG 15 ARG
16 LEU 17 PRO 18 PRO 19 GLN 20 GLN
21 ILE 22 GLU 23 LYS 24 ASN 25 LEU
26 SER 27 ASP 28 LEU 29 ILE 30 ASP
31 LEU 32 VAL 33 PRO 34 SER 35 LEU
36 CYS 37 GLU 38 ASP 39 LEU 40 LEU
41 SER 42 SER 43 VAL 44 ASP 45 GLN
46 PRO 47 LEU 48 LYS 49 ILE 50 ALA
51 ARG 52 ASP 53 LYS 54 VAL 55 VAL
56 GLY 57 LYS 58 ASP 59 TYR 60 LEU
61 LEU 62 CYS 63 ASP 64 TYR 65 ASN
66 ARG 67 ASP 68 GLY 69 ASP 70 SER
71 TYR 72 ARG 73 SER 74 PRO 75 TRP
76 SER 77 ASN 78 LYS 79 TYR 80 ASP
81 PRO 82 PRO 83 LEU 84 GLU 85 ASP
86 GLY 87 ALA 88 MET 89 PRO 90 SER
91 ALA 92 ARG 93 LEU 94 ARG 95 LYS
96 LEU 97 GLU 98 VAL 99 GLU 100 ALA
101 ASN 102 ASN 103 ALA 104 PHE 105 ASP
106 GLN 107 TYR 108 ARG 109 ASP 110 LEU
111 TYR 112 PHE 113 GLU 114 GLY 115 GLY
116 VAL 117 SER 118 SER 119 VAL 120 TYR
121 LEU 122 TRP 123 ASP 124 LEU 125 ASP
126 HIS 127 GLY 128 PHE 129 ALA 130 GLY
131 VAL 132 ILE 133 LEU 134 ILE 135 LYS
136 LYS 137 ALA 138 GLY 139 ASP 140 GLY
141 SER 142 LYS 143 LYS 144 ILE 145 LYS
146 GLY 147 CYS 148 TRP 149 ASP 150 SER
151 ILE 152 HIS 153 VAL 154 VAL 155 GLU
156 VAL 157 GLN 158 GLU 159 LYS 160 SER
161 SER 162 GLY 163 ARG 164 THR 165 ALA
166 HIS 167 TYR 168 LYS 169 LEU 170 THR
171 SER 172 THR 173 VAL 174 MET 175 LEU
176 TRP 177 LEU 178 GLN 179 THR 180 ASN
181 LYS 182 THR 183 GLY 184 SER 185 GLY
186 THR 187 MET 188 ASN 189 LEU 190 GLY
191 GLY 192 SER 193 LEU 194 THR 195 ARG
196 GLN 197 MET 198 GLU 199 LYS 200 ASP
201 GLU 202 THR 203 VAL 204 SER 205 ASP
206 SER 207 SER 208 PRO 209 HIS 210 ILE
211 ALA 212 ASN 213 ILE 214 GLY 215 ARG
216 LEU 217 VAL 218 GLU 219 ASP 220 MET
221 GLU 222 ASN 223 LYS 224 ILE 225 ARG
226 SER 227 THR 228 LEU 229 ASN 230 GLU
231 ILE 232 TYR 233 PHE 234 GLY 235 LYS
236 THR 237 LYS 238 ASP 239 ILE 240 VAL
241 ASN 242 GLY 243 LEU 244 ARG 245 SER
246 VAL 247 GLN 248 THR 249 PHE 250 ALA
251 ASP 252 LYS 253 SER 254 LYS 255 GLN
256 GLU 257 ALA 258 LEU 259 LYS 260 ASN
261 ASP 262 LEU 263 VAL 264 GLU 265 ALA
266 LEU 267 LYS 268 ARG 269 LYS 270 GLN
271 GLN 272 CYS 273 ILE 274 GLN 275 PRO
276 ASP 277 ASN
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-01-30
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 3AA0 "Crystal Structure Of Actin Capping Protein In Complex With The Cp- Binding Motif Derived From Carmil" 88.09 244 100.00 100.00 6.38e-179
PDB 3AA1 "Crystal Structure Of Actin Capping Protein In Complex With The Cp- Binding Motif Derived From Ckip-1" 88.09 244 100.00 100.00 6.38e-179
PDB 3AA6 "Crystal Structure Of Actin Capping Protein In Complex With The Cp- Binding Motif Derived From Cd2ap" 88.09 244 100.00 100.00 6.38e-179
PDB 3AA7 "Crystal Structure Of Actin Capping Protein" 88.09 244 100.00 100.00 6.38e-179
PDB 3LK2 "Crystal Structure Of Capz Bound To The Uncapping Motif From Carmil" 87.73 243 100.00 100.00 5.25e-178
DBJ BAE33851 "unnamed protein product [Mus musculus]" 98.19 272 99.26 99.63 0.00e+00
DBJ BAE35614 "unnamed protein product [Mus musculus]" 98.19 272 98.90 99.26 0.00e+00
DBJ BAE37051 "unnamed protein product [Mus musculus]" 93.86 260 98.85 99.23 0.00e+00
DBJ BAE40579 "unnamed protein product [Mus musculus]" 98.19 272 99.26 99.63 0.00e+00
DBJ BAG35935 "unnamed protein product [Homo sapiens]" 98.19 272 98.90 99.63 0.00e+00
EMBL CAA71401 "actin-binding protein CP3 [Bos taurus]" 97.83 301 99.26 99.63 0.00e+00
EMBL CAB06626 "capping protein, beta3 isoform [Bos taurus]" 97.83 301 99.26 99.63 0.00e+00
EMBL CAH93159 "hypothetical protein [Pongo abelii]" 98.56 380 98.90 99.63 0.00e+00
EMBL CAL69434 "F-actin capping protein subunit beta 2 [Sus scrofa]" 97.83 272 100.00 100.00 0.00e+00
GB AAA52222 "actin capping protein beta subunit, isoform 2 [Gallus gallus]" 97.83 272 100.00 100.00 0.00e+00
GB AAA52227 "capping protein beta subunit, isoform 2 [Mus musculus]" 98.19 272 99.26 99.63 0.00e+00
GB AAA87395 "F-actin capping protein beta subunit [Homo sapiens]" 98.19 272 99.26 99.63 0.00e+00
GB AAH02053 "Capping protein (actin filament) muscle Z-line, beta [Mus musculus]" 98.19 272 99.26 99.63 0.00e+00
GB AAH24601 "CAPZB protein, partial [Homo sapiens]" 68.23 189 98.94 99.47 4.07e-133
REF NP_001005903 "F-actin-capping protein subunit beta [Rattus norvegicus]" 98.19 272 99.26 99.63 0.00e+00
REF NP_001080116 "capping protein (actin filament) muscle Z-line, beta [Xenopus laevis]" 97.83 272 98.15 100.00 0.00e+00
REF NP_001090922 "F-actin capping protein subunit beta 2 [Sus scrofa]" 97.83 272 100.00 100.00 0.00e+00
REF NP_001106915 "F-actin-capping protein subunit beta [Sus scrofa]" 98.19 272 99.26 99.63 0.00e+00
REF NP_001127638 "F-actin-capping protein subunit beta [Pongo abelii]" 98.19 272 99.26 99.63 0.00e+00
SP P79136 "RecName: Full=F-actin-capping protein subunit beta; AltName: Full=CapZ beta [Bos taurus]" 97.83 301 99.26 99.63 0.00e+00
SP Q5R507 "RecName: Full=F-actin-capping protein subunit beta; AltName: Full=CapZ beta [Pongo abelii]" 98.19 272 99.26 99.63 0.00e+00
SP Q5XI32 "RecName: Full=F-actin-capping protein subunit beta; AltName: Full=CapZ beta [Rattus norvegicus]" 98.19 272 99.26 99.63 0.00e+00
TPG DAA32069 "TPA: F-actin-capping protein subunit beta [Bos taurus]" 97.83 301 99.26 99.63 0.00e+00
stop_
save_
save_CARMIL_CAH3a_b_domain
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common CARMIL_CAH3a_b_domain
_Molecular_mass .
_Mol_thiol_state 'all free'
_Details .
_Residue_count 81
_Mol_residue_sequence
;
GAMGSWSVRQEKRSSGLISE
LPSEEGRRLEHFTKLRPKRN
KKQQPTQAAVCTISILPQDG
EQNGLMGRVDEGVDEFFTKK
V
;
loop_
_Residue_seq_code
_Residue_label
1 GLY 2 ALA 3 MET 4 GLY 5 SER
6 TRP 7 SER 8 VAL 9 ARG 10 GLN
11 GLU 12 LYS 13 ARG 14 SER 15 SER
16 GLY 17 LEU 18 ILE 19 SER 20 GLU
21 LEU 22 PRO 23 SER 24 GLU 25 GLU
26 GLY 27 ARG 28 ARG 29 LEU 30 GLU
31 HIS 32 PHE 33 THR 34 LYS 35 LEU
36 ARG 37 PRO 38 LYS 39 ARG 40 ASN
41 LYS 42 LYS 43 GLN 44 GLN 45 PRO
46 THR 47 GLN 48 ALA 49 ALA 50 VAL
51 CYS 52 THR 53 ILE 54 SER 55 ILE
56 LEU 57 PRO 58 GLN 59 ASP 60 GLY
61 GLU 62 GLN 63 ASN 64 GLY 65 LEU
66 MET 67 GLY 68 ARG 69 VAL 70 ASP
71 GLU 72 GLY 73 VAL 74 ASP 75 GLU
76 PHE 77 PHE 78 THR 79 LYS 80 LYS
81 VAL
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-01-30
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 2KZ7 "Solution Structure Of The Carmil Cah3aB DOMAIN BOUND TO CAPPING Protein (Cp)" 101.23 85 97.56 97.56 1.33e-48
DBJ BAC31591 "unnamed protein product [Mus musculus]" 92.59 816 100.00 100.00 4.37e-42
GB AAH12229 "Lrrc16a protein [Mus musculus]" 92.59 589 100.00 100.00 1.94e-42
GB AAI67257 "Leucine rich repeat containing 16A [synthetic construct]" 92.59 1374 100.00 100.00 2.46e-41
GB AAR96060 "CARMIL [Mus musculus]" 92.59 1374 100.00 100.00 2.63e-41
REF NP_081101 "leucine-rich repeat-containing protein 16A [Mus musculus]" 92.59 1374 100.00 100.00 2.46e-41
REF XP_006516802 "PREDICTED: leucine-rich repeat-containing protein 16A isoform X1 [Mus musculus]" 92.59 1424 100.00 100.00 2.79e-41
REF XP_006516803 "PREDICTED: leucine-rich repeat-containing protein 16A isoform X2 [Mus musculus]" 92.59 1423 100.00 100.00 2.70e-41
REF XP_006516804 "PREDICTED: leucine-rich repeat-containing protein 16A isoform X3 [Mus musculus]" 92.59 1420 100.00 100.00 2.57e-41
REF XP_006516805 "PREDICTED: leucine-rich repeat-containing protein 16A isoform X4 [Mus musculus]" 92.59 1370 100.00 100.00 2.40e-41
SP Q6EDY6 "RecName: Full=Leucine-rich repeat-containing protein 16A; AltName: Full=CARMIL homolog [Mus musculus]" 92.59 1374 100.00 100.00 2.46e-41
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$CPalpha_subunit chicken 9031 Eukaryota Metazoa Gallus gallus
$CPbeta_subunit chicken 9031 Eukaryota Metazoa Gallus gallus
$CARMIL_CAH3a_b_domain 'house mouse' 10090 Eukaryota Metazoa Mus musculus
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Vector_name
$CPalpha_subunit 'recombinant technology' . Escherichia coli BL21 PET
$CPbeta_subunit 'recombinant technology' . Escherichia coli BL21 pET
$CARMIL_CAH3a_b_domain 'recombinant technology' . Escherichia coli BL21 pGEX4
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_CP_chemical_shift_perturpation
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$CPalpha_subunit 0.35 mM '[U-99% 15N; U-80% 2H]'
$CPbeta_subunit 0.35 mM '[U-99% 15N; U-80% 2H]'
$CARMIL_CAH3a_b_domain 0.39 mM [U-2H]
H2O 93 % 'natural abundance'
D2O 7 % 'natural abundance'
stop_
save_
save_CAH3a_b_chemical_shift_perturpation
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$CPalpha_subunit 0.35 mM '[U-99% 15N; U-80% 2H]'
$CPbeta_subunit 0.39 mM [U-2H]
$CARMIL_CAH3a_b_domain 0.39 mM [U-2H]
H2O 93 % 'natural abundance'
D2O 7 % 'natural abundance'
stop_
save_
save_intermolecular_PRE
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$CPalpha_subunit 0.35 mM '[U-99% 15N; U-80% 2H]'
$CPbeta_subunit 0.35 mM '[U-99% 15N; U-80% 2H]'
$CARMIL_CAH3a_b_domain 0.39 mM '[U-2H; spin labeled at 1 or 5 postions]'
H2O 93 % 'natural abundance'
D2O 7 % 'natural abundance'
stop_
save_
############################
# Computer software used #
############################
save_TOPSPIN
_Saveframe_category software
_Name TOPSPIN
_Version .
loop_
_Vendor
_Address
_Electronic_address
'Bruker Biospin' . .
stop_
loop_
_Task
collection
stop_
_Details .
save_
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version .
loop_
_Vendor
_Address
_Electronic_address
'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . .
stop_
loop_
_Task
processing
stop_
_Details .
save_
save_NMRDraw
_Saveframe_category software
_Name NMRDraw
_Version .
loop_
_Vendor
_Address
_Electronic_address
'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . .
stop_
loop_
_Task
processing
stop_
_Details .
save_
save_PIPP
_Saveframe_category software
_Name PIPP
_Version .
loop_
_Vendor
_Address
_Electronic_address
Garrett . .
stop_
loop_
_Task
'chemical shift assignment'
'chemical shift calculation'
'peak picking'
stop_
_Details .
save_
save_X-PLOR_NIH
_Saveframe_category software
_Name 'X-PLOR NIH'
_Version 2.23
loop_
_Vendor
_Address
_Electronic_address
'Schwieters, Kuszewski, Tjandra and Clore' . .
stop_
loop_
_Task
refinement
'structure solution'
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 800
_Details .
save_
save_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model Avance
_Field_strength 900
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_1H-15N_HSQC_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-15N HSQC'
_Sample_label $CP_chemical_shift_perturpation
save_
save_2D_1H-15N_HSQC_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-15N HSQC'
_Sample_label $CAH3a_b_chemical_shift_perturpation
save_
save_2D_1H-15N_HSQC_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-15N HSQC'
_Sample_label $intermolecular_PRE
save_
#######################
# Sample conditions #
#######################
save_sample_conditions_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
'ionic strength' 100 . mM
pH 6.5 . pH
pressure 1 . atm
temperature 305 . K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_reference_1
_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
acetate C 13 'methyl carbon' ppm 0 external direct . . . 1.000
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_shifts_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'2D 1H-15N HSQC'
stop_
loop_
_Sample_label
$CP_chemical_shift_perturpation
$CAH3a_b_chemical_shift_perturpation
stop_
_Sample_conditions_label $sample_conditions_1
_Chem_shift_reference_set_label $reference_1
_Mol_system_component_name CPalpha_subunit
_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 3 3 ASP H H 8.22 . 1
2 3 3 ASP C C 175.62 . 1
3 3 3 ASP CA C 54.26 . 1
4 3 3 ASP CB C 40.86 . 1
5 3 3 ASP N N 122.07 . 1
6 4 4 PHE H H 8.12 . 1
7 4 4 PHE C C 175.5 . 1
8 4 4 PHE CA C 57.34 . 1
9 4 4 PHE CB C 38.68 . 1
10 4 4 PHE N N 120.05 . 1
11 5 5 GLU H H 8.21 . 1
12 5 5 GLU C C 175.86 . 1
13 5 5 GLU CA C 55.99 . 1
14 5 5 GLU CB C 29.76 . 1
15 5 5 GLU N N 122.34 . 1
16 6 6 ASP H H 8.2 . 1
17 6 6 ASP C C 176.09 . 1
18 6 6 ASP CA C 54 . 1
19 6 6 ASP CB C 40.48 . 1
20 6 6 ASP N N 122.01 . 1
21 7 7 ARG H H 8.34 . 1
22 7 7 ARG C C 176.39 . 1
23 7 7 ARG CA C 56.22 . 1
24 7 7 ARG CB C 30.67 . 1
25 7 7 ARG N N 121.91 . 1
26 8 8 VAL H H 7.95 . 1
27 8 8 VAL C C 175.79 . 1
28 8 8 VAL CA C 60.81 . 1
29 8 8 VAL CB C 32.25 . 1
30 8 8 VAL N N 118.79 . 1
31 9 9 SER H H 8.47 . 1
32 9 9 SER C C 175.12 . 1
33 9 9 SER CA C 57.59 . 1
34 9 9 SER CB C 64.73 . 1
35 9 9 SER N N 121.03 . 1
36 10 10 ASP H H 8.87 . 1
37 10 10 ASP C C 177.86 . 1
38 10 10 ASP CA C 57.17 . 1
39 10 10 ASP CB C 38.88 . 1
40 10 10 ASP N N 122.93 . 1
41 11 11 GLU H H 8.32 . 1
42 11 11 GLU C C 179.22 . 1
43 11 11 GLU CA C 59.52 . 1
44 11 11 GLU CB C 28.22 . 1
45 11 11 GLU N N 118.69 . 1
46 12 12 GLU H H 7.63 . 1
47 12 12 GLU C C 178.81 . 1
48 12 12 GLU CA C 58.21 . 1
49 12 12 GLU CB C 28.9 . 1
50 12 12 GLU N N 121.69 . 1
51 13 13 LYS H H 8.27 . 1
52 13 13 LYS C C 178.61 . 1
53 13 13 LYS CA C 60.33 . 1
54 13 13 LYS CB C 31.89 . 1
55 13 13 LYS N N 119.72 . 1
56 14 14 VAL H H 7.91 . 1
57 14 14 VAL C C 176.77 . 1
58 14 14 VAL CA C 65.55 . 1
59 14 14 VAL CB C 30.45 . 1
60 14 14 VAL N N 117.3 . 1
61 15 15 ARG H H 7.39 . 1
62 15 15 ARG C C 179.85 . 1
63 15 15 ARG CA C 59.4 . 1
64 15 15 ARG CB C 28.46 . 1
65 15 15 ARG N N 122.19 . 1
66 16 16 ILE H H 7.79 . 1
67 16 16 ILE C C 176.73 . 1
68 16 16 ILE CA C 65 . 1
69 16 16 ILE CB C 37.18 . 1
70 16 16 ILE N N 121.88 . 1
71 17 17 ALA H H 8.09 . 1
72 17 17 ALA C C 178.9 . 1
73 17 17 ALA CA C 55.12 . 1
74 17 17 ALA CB C 73.54 . 1
75 17 17 ALA N N 120.54 . 1
76 18 18 ALA H H 8.44 . 1
77 18 18 ALA C C 179.14 . 1
78 18 18 ALA CA C 54.58 . 1
79 18 18 ALA CB C 73.62 . 1
80 18 18 ALA N N 117.47 . 1
81 19 19 LYS H H 7.57 . 1
82 19 19 LYS C C 179.54 . 1
83 19 19 LYS CA C 59.2 . 1
84 19 19 LYS CB C 30.64 . 1
85 19 19 LYS N N 120.7 . 1
86 20 20 PHE H H 7.97 . 1
87 20 20 PHE C C 177.76 . 1
88 20 20 PHE CA C 57.45 . 1
89 20 20 PHE CB C 37.2 . 1
90 20 20 PHE N N 119.18 . 1
91 21 21 ILE H H 7.95 . 1
92 21 21 ILE C C 177.4 . 1
93 21 21 ILE CA C 64.29 . 1
94 21 21 ILE CB C 36.51 . 1
95 21 21 ILE N N 116.96 . 1
96 22 22 THR H H 7.81 . 1
97 22 22 THR C C 175.43 . 1
98 22 22 THR CA C 64.77 . 1
99 22 22 THR N N 107.13 . 1
100 23 23 HIS H H 7.51 . 1
101 23 23 HIS C C 173.7 . 1
102 23 23 HIS CA C 56.06 . 1
103 23 23 HIS CB C 28.4 . 1
104 23 23 HIS N N 118.48 . 1
105 24 24 ALA H H 7.4 . 1
106 24 24 ALA C C 175.57 . 1
107 24 24 ALA CA C 50.87 . 1
108 24 24 ALA N N 124.4 . 1
109 26 26 PRO C C 179.37 . 1
110 26 26 PRO CA C 64.43 . 1
111 27 27 GLY H H 6.92 . 1
112 27 27 GLY C C 174.1 . 1
113 27 27 GLY CA C 46.14 . 1
114 27 27 GLY N N 108.18 . 1
115 28 28 GLU H H 6.99 . 1
116 28 28 GLU C C 179.23 . 1
117 28 28 GLU CA C 59.29 . 1
118 28 28 GLU CB C 29.4 . 1
119 28 28 GLU N N 118.65 . 1
120 29 29 PHE H H 6.86 . 1
121 29 29 PHE C C 178.56 . 1
122 29 29 PHE CA C 57.3 . 1
123 29 29 PHE CB C 41.2 . 1
124 29 29 PHE N N 119.19 . 1
125 30 30 ASN C C 177.12 . 1
126 30 30 ASN CA C 56.54 . 1
127 30 30 ASN CB C 36.8 . 1
128 31 31 GLU H H 8.7 . 1
129 31 31 GLU C C 178.7 . 1
130 31 31 GLU CA C 60.63 . 1
131 31 31 GLU CB C 27.4 . 1
132 31 31 GLU N N 121.49 . 1
133 32 32 VAL H H 7.39 . 1
134 32 32 VAL C C 177.05 . 1
135 32 32 VAL CA C 66.65 . 1
136 32 32 VAL CB C 30.66 . 1
137 32 32 VAL N N 119.14 . 1
138 33 33 PHE H H 8.73 . 1
139 33 33 PHE C C 176.19 . 1
140 33 33 PHE CA C 61.27 . 1
141 33 33 PHE CB C 38.96 . 1
142 33 33 PHE N N 120.23 . 1
143 34 34 ASN H H 8.25 . 1
144 34 34 ASN C C 177.27 . 1
145 34 34 ASN CA C 56.22 . 1
146 34 34 ASN CB C 38.09 . 1
147 34 34 ASN N N 117.15 . 1
148 35 35 ASP H H 7.76 . 1
149 35 35 ASP C C 176.81 . 1
150 35 35 ASP CA C 55.86 . 1
151 35 35 ASP CB C 37.49 . 1
152 35 35 ASP N N 118.26 . 1
153 36 36 VAL H H 8.24 . 1
154 36 36 VAL C C 176.98 . 1
155 36 36 VAL CA C 66.26 . 1
156 36 36 VAL CB C 30.45 . 1
157 36 36 VAL N N 117.58 . 1
158 37 37 ARG H H 8.65 . 1
159 37 37 ARG C C 180.07 . 1
160 37 37 ARG CA C 58.93 . 1
161 37 37 ARG CB C 28.83 . 1
162 37 37 ARG N N 120.82 . 1
163 38 38 LEU H H 7.48 . 1
164 38 38 LEU C C 179.36 . 1
165 38 38 LEU CA C 56.79 . 1
166 38 38 LEU CB C 40.63 . 1
167 38 38 LEU N N 120.95 . 1
168 39 39 LEU H H 7.57 . 1
169 39 39 LEU C C 177.69 . 1
170 39 39 LEU CA C 58.05 . 1
171 39 39 LEU CB C 40.63 . 1
172 39 39 LEU N N 119.01 . 1
173 40 40 LEU H H 8.29 . 1
174 40 40 LEU C C 176.96 . 1
175 40 40 LEU CA C 56.38 . 1
176 40 40 LEU CB C 41.82 . 1
177 40 40 LEU N N 118.81 . 1
178 41 41 ASN H H 7.66 . 1
179 41 41 ASN C C 174.67 . 1
180 41 41 ASN CA C 53.22 . 1
181 41 41 ASN CB C 37.14 . 1
182 41 41 ASN N N 113.94 . 1
183 42 42 ASN H H 9.23 . 1
184 42 42 ASN C C 173.95 . 1
185 42 42 ASN CA C 52.87 . 1
186 42 42 ASN CB C 36.06 . 1
187 42 42 ASN N N 116.09 . 1
188 43 43 ASP H H 8.86 . 1
189 43 43 ASP C C 178.39 . 1
190 43 43 ASP CA C 57.33 . 1
191 43 43 ASP CB C 39.4 . 1
192 43 43 ASP N N 125.91 . 1
193 44 44 ASN H H 8.47 . 1
194 44 44 ASN C C 177.12 . 1
195 44 44 ASN CA C 56.17 . 1
196 44 44 ASN CB C 37.56 . 1
197 44 44 ASN N N 118.29 . 1
198 45 45 LEU H H 7.12 . 1
199 45 45 LEU C C 178.8 . 1
200 45 45 LEU CA C 56.81 . 1
201 45 45 LEU CB C 41.16 . 1
202 45 45 LEU N N 121.39 . 1
203 46 46 LEU H H 7.73 . 1
204 46 46 LEU C C 177.64 . 1
205 46 46 LEU CA C 57.47 . 1
206 46 46 LEU CB C 41.16 . 1
207 46 46 LEU N N 118.4 . 1
208 47 47 ARG H H 8.13 . 1
209 47 47 ARG C C 177.83 . 1
210 47 47 ARG CA C 59.4 . 1
211 47 47 ARG CB C 29.49 . 1
212 47 47 ARG N N 115.41 . 1
213 48 48 GLU H H 7.78 . 1
214 48 48 GLU C C 179.35 . 1
215 48 48 GLU CA C 57.41 . 1
216 48 48 GLU CB C 29.39 . 1
217 48 48 GLU N N 115.3 . 1
218 49 49 GLY H H 8.41 . 1
219 49 49 GLY C C 175.02 . 1
220 49 49 GLY CA C 46.48 . 1
221 49 49 GLY N N 108.14 . 1
222 50 50 ALA H H 7.73 . 1
223 50 50 ALA C C 175.79 . 1
224 50 50 ALA CA C 50.42 . 1
225 50 50 ALA CB C 73.1 . 1
226 50 50 ALA N N 120.09 . 1
227 51 51 ALA H H 6.67 . 1
228 51 51 ALA C C 180.42 . 1
229 51 51 ALA CA C 55.11 . 1
230 51 51 ALA CB C 73.47 . 1
231 51 51 ALA N N 121.49 . 1
232 52 52 HIS C C 176.73 . 1
233 52 52 HIS CA C 58.16 . 1
234 52 52 HIS CB C 73.65 . 1
235 53 53 ALA H H 7.06 . 1
236 53 53 ALA C C 179.25 . 1
237 53 53 ALA CA C 53.6 . 1
238 53 53 ALA CB C 73.65 . 1
239 53 53 ALA N N 123.99 . 1
240 54 54 PHE H H 7.2 . 1
241 54 54 PHE C C 177.21 . 1
242 54 54 PHE CA C 57.81 . 1
243 54 54 PHE CB C 36.73 . 1
244 54 54 PHE N N 117.18 . 1
245 55 55 ALA H H 6.71 . 1
246 55 55 ALA C C 178.82 . 1
247 55 55 ALA CA C 53.5 . 1
248 55 55 ALA CB C 72.78 . 1
249 55 55 ALA N N 119.43 . 1
250 56 56 GLN H H 8.04 . 1
251 56 56 GLN C C 178.2 . 1
252 56 56 GLN CA C 58.32 . 1
253 56 56 GLN CB C 27.86 . 1
254 56 56 GLN N N 117.67 . 1
255 57 57 TYR H H 8.16 . 1
256 57 57 TYR C C 176.95 . 1
257 57 57 TYR CA C 61.54 . 1
258 57 57 TYR CB C 40.41 . 1
259 57 57 TYR N N 118.86 . 1
260 58 58 ASN H H 7.57 . 1
261 58 58 ASN C C 178.05 . 1
262 58 58 ASN CA C 55.86 . 1
263 58 58 ASN CB C 37.72 . 1
264 58 58 ASN N N 115.35 . 1
265 59 59 MET H H 7.98 . 1
266 59 59 MET C C 179.32 . 1
267 59 59 MET CA C 58.52 . 1
268 59 59 MET CB C 34 . 1
269 59 59 MET N N 116.2 . 1
270 60 60 ASP H H 8.76 . 1
271 60 60 ASP C C 179.04 . 1
272 60 60 ASP CA C 56.62 . 1
273 60 60 ASP CB C 40.74 . 1
274 60 60 ASP N N 122.34 . 1
275 61 61 GLN H H 7.79 . 1
276 61 61 GLN C C 173.29 . 1
277 61 61 GLN CA C 55.89 . 1
278 61 61 GLN CB C 27.12 . 1
279 61 61 GLN N N 115.82 . 1
280 62 62 PHE H H 7.54 . 1
281 62 62 PHE C C 174.41 . 1
282 62 62 PHE CA C 53.47 . 1
283 62 62 PHE N N 113.47 . 1
284 63 63 THR H H 7.16 . 1
285 63 63 THR C C 173.65 . 1
286 63 63 THR CA C 61.85 . 1
287 63 63 THR CB C 70.07 . 1
288 63 63 THR N N 111.23 . 1
289 64 64 PRO C C 177.09 . 1
290 64 64 PRO CA C 61.13 . 1
291 64 64 PRO CB C 30.7 . 1
292 65 65 VAL H H 8.94 . 1
293 65 65 VAL C C 172.31 . 1
294 65 65 VAL CA C 59.81 . 1
295 65 65 VAL CB C 34.84 . 1
296 65 65 VAL N N 121.63 . 1
297 66 66 LYS H H 7.86 . 1
298 66 66 LYS C C 174.95 . 1
299 66 66 LYS CA C 53.86 . 1
300 66 66 LYS CB C 33.41 . 1
301 66 66 LYS N N 125.21 . 1
302 67 67 ILE H H 9.33 . 1
303 67 67 ILE C C 176.06 . 1
304 67 67 ILE CA C 59.53 . 1
305 67 67 ILE CB C 37.17 . 1
306 67 67 ILE N N 130.03 . 1
307 68 68 GLU H H 8.48 . 1
308 68 68 GLU C C 176.61 . 1
309 68 68 GLU CA C 58.14 . 1
310 68 68 GLU CB C 28.49 . 1
311 68 68 GLU N N 129.04 . 1
312 69 69 GLY H H 8.44 . 1
313 69 69 GLY C C 173.7 . 1
314 69 69 GLY CA C 44.13 . 1
315 69 69 GLY N N 113.15 . 1
316 70 70 TYR H H 7.91 . 1
317 70 70 TYR C C 176.13 . 1
318 70 70 TYR CA C 57.13 . 1
319 70 70 TYR CB C 39.74 . 1
320 70 70 TYR N N 120.01 . 1
321 71 71 ASP H H 8.69 . 1
322 71 71 ASP C C 176.19 . 1
323 71 71 ASP CA C 55.59 . 1
324 71 71 ASP CB C 41.08 . 1
325 71 71 ASP N N 123.14 . 1
326 72 72 ASP H H 8.11 . 1
327 72 72 ASP C C 175.84 . 1
328 72 72 ASP CA C 53.93 . 1
329 72 72 ASP CB C 41.8 . 1
330 72 72 ASP N N 118.09 . 1
331 73 73 GLN H H 8.21 . 1
332 73 73 GLN C C 174.19 . 1
333 73 73 GLN CA C 56.6 . 1
334 73 73 GLN CB C 28.46 . 1
335 73 73 GLN N N 121.77 . 1
336 74 74 VAL H H 8.38 . 1
337 74 74 VAL C C 172.59 . 1
338 74 74 VAL CA C 58.66 . 1
339 74 74 VAL CB C 33.69 . 1
340 74 74 VAL N N 122.03 . 1
341 75 75 LEU H H 7.27 . 1
342 75 75 LEU C C 175.47 . 1
343 75 75 LEU CA C 53.75 . 1
344 75 75 LEU CB C 40.96 . 1
345 75 75 LEU N N 123.52 . 1
346 76 76 ILE H H 7.96 . 1
347 76 76 ILE C C 173.35 . 1
348 76 76 ILE CA C 57.84 . 1
349 76 76 ILE CB C 41.27 . 1
350 76 76 ILE N N 124.12 . 1
351 77 77 THR H H 6.29 . 1
352 77 77 THR C C 175.5 . 1
353 77 77 THR CA C 59.16 . 1
354 77 77 THR CB C 73.66 . 1
355 77 77 THR N N 109.48 . 1
356 78 78 GLU H H 9.62 . 1
357 78 78 GLU C C 177.53 . 1
358 78 78 GLU CA C 57.89 . 1
359 78 78 GLU CB C 28.4 . 1
360 78 78 GLU N N 120.65 . 1
361 79 79 HIS H H 6.69 . 1
362 79 79 HIS C C 176.41 . 1
363 79 79 HIS CA C 55.81 . 1
364 79 79 HIS CB C 28.48 . 1
365 79 79 HIS N N 118.94 . 1
366 80 80 GLY H H 7.27 . 1
367 80 80 GLY C C 172.22 . 1
368 80 80 GLY CA C 44.25 . 1
369 80 80 GLY N N 129.34 . 1
370 81 81 ASP H H 6.51 . 1
371 81 81 ASP C C 175.7 . 1
372 81 81 ASP CA C 55.78 . 1
373 81 81 ASP CB C 40.2 . 1
374 81 81 ASP N N 119.19 . 1
375 82 82 LEU H H 7.96 . 1
376 82 82 LEU C C 178.04 . 1
377 82 82 LEU CA C 53.72 . 1
378 82 82 LEU CB C 41.64 . 1
379 82 82 LEU N N 130.02 . 1
380 83 83 GLY H H 8.18 . 1
381 83 83 GLY C C 173.94 . 1
382 83 83 GLY CA C 67.77 . 1
383 83 83 GLY N N 110.2 . 1
384 84 84 ASN H H 8.71 . 1
385 84 84 ASN C C 174.62 . 1
386 84 84 ASN CA C 53.69 . 1
387 84 84 ASN CB C 36.78 . 1
388 84 84 ASN N N 116.68 . 1
389 85 85 SER H H 8.51 . 1
390 85 85 SER C C 173.55 . 1
391 85 85 SER CA C 59.78 . 1
392 85 85 SER CB C 63.93 . 1
393 85 85 SER N N 110.72 . 1
394 86 86 ARG H H 7.39 . 1
395 86 86 ARG C C 175.53 . 1
396 86 86 ARG CA C 54.3 . 1
397 86 86 ARG CB C 31.46 . 1
398 86 86 ARG N N 117.73 . 1
399 87 87 PHE H H 8.25 . 1
400 87 87 PHE C C 173.45 . 1
401 87 87 PHE CA C 55.14 . 1
402 87 87 PHE CB C 44.35 . 1
403 87 87 PHE N N 118.86 . 1
404 88 88 LEU H H 8.42 . 1
405 88 88 LEU C C 176.45 . 1
406 88 88 LEU CA C 53.54 . 1
407 88 88 LEU CB C 45.53 . 1
408 88 88 LEU N N 119.84 . 1
409 89 89 ASP H H 9.18 . 1
410 89 89 ASP C C 176.04 . 1
411 89 89 ASP CA C 49.53 . 1
412 89 89 ASP CB C 40.7 . 1
413 89 89 ASP N N 123.19 . 1
414 91 91 ARG C C 177.25 . 1
415 91 91 ARG CA C 58.12 . 1
416 91 91 ARG CB C 30.4 . 1
417 92 92 ASN H H 7.02 . 1
418 92 92 ASN C C 173.12 . 1
419 92 92 ASN CA C 52.94 . 1
420 92 92 ASN CB C 39.21 . 1
421 92 92 ASN N N 114.25 . 1
422 93 93 GLN H H 7.8 . 1
423 93 93 GLN C C 174.93 . 1
424 93 93 GLN CA C 56.57 . 1
425 93 93 GLN CB C 25.13 . 1
426 93 93 GLN N N 117.45 . 1
427 94 94 ILE H H 7.49 . 1
428 94 94 ILE C C 175.03 . 1
429 94 94 ILE CA C 58.24 . 1
430 94 94 ILE CB C 42.48 . 1
431 94 94 ILE N N 111.34 . 1
432 95 95 SER H H 9.62 . 1
433 95 95 SER C C 173.74 . 1
434 95 95 SER CA C 55.27 . 1
435 95 95 SER N N 116.06 . 1
436 96 96 PHE H H 8.55 . 1
437 96 96 PHE C C 173.17 . 1
438 96 96 PHE CA C 55.54 . 1
439 96 96 PHE CB C 38.79 . 1
440 96 96 PHE N N 115.32 . 1
441 97 97 LYS H H 8.92 . 1
442 97 97 LYS C C 175.46 . 1
443 97 97 LYS CA C 55.62 . 1
444 97 97 LYS CB C 32.32 . 1
445 97 97 LYS N N 123.61 . 1
446 98 98 PHE H H 8.97 . 1
447 98 98 PHE C C 172.85 . 1
448 98 98 PHE CA C 55.9 . 1
449 98 98 PHE CB C 43.44 . 1
450 98 98 PHE N N 127.27 . 1
451 99 99 ASP H H 7.32 . 1
452 99 99 ASP C C 176.36 . 1
453 99 99 ASP CA C 51.54 . 1
454 99 99 ASP CB C 41.72 . 1
455 99 99 ASP N N 126.87 . 1
456 100 100 HIS H H 8.41 . 1
457 100 100 HIS C C 176.35 . 1
458 100 100 HIS CA C 59.07 . 1
459 100 100 HIS CB C 31.38 . 1
460 100 100 HIS N N 123.5 . 1
461 101 101 LEU H H 7.84 . 1
462 101 101 LEU C C 178.08 . 1
463 101 101 LEU CA C 56.24 . 1
464 101 101 LEU CB C 40.66 . 1
465 101 101 LEU N N 118.86 . 1
466 102 102 ARG H H 7.67 . 1
467 102 102 ARG C C 175.84 . 1
468 102 102 ARG CA C 55.97 . 1
469 102 102 ARG CB C 29.75 . 1
470 102 102 ARG N N 117.39 . 1
471 103 103 LYS H H 7.63 . 1
472 103 103 LYS C C 174.18 . 1
473 103 103 LYS CA C 56.33 . 1
474 103 103 LYS CB C 27.14 . 1
475 103 103 LYS N N 116.86 . 1
476 104 104 GLU H H 6.06 . 1
477 104 104 GLU C C 174.86 . 1
478 104 104 GLU CA C 53.88 . 1
479 104 104 GLU CB C 33.37 . 1
480 104 104 GLU N N 115.64 . 1
481 105 105 ALA H H 9.16 . 1
482 105 105 ALA C C 176.8 . 1
483 105 105 ALA CA C 49.81 . 1
484 105 105 ALA CB C 22.6 . 1
485 105 105 ALA N N 130.63 . 1
486 106 106 SER H H 9.44 . 1
487 106 106 SER C C 172.43 . 1
488 106 106 SER CA C 57.08 . 1
489 106 106 SER CB C 66 . 1
490 106 106 SER N N 115.49 . 1
491 107 107 ASP H H 9.02 . 1
492 107 107 ASP C C 171.85 . 1
493 107 107 ASP CA C 54.58 . 1
494 107 107 ASP CB C 41 . 1
495 107 107 ASP N N 116.36 . 1
496 110 110 PRO C C 176.46 . 1
497 110 110 PRO CA C 63.02 . 1
498 110 110 PRO CB C 31.65 . 1
499 111 111 GLU H H 8.06 . 1
500 111 111 GLU C C 174.47 . 1
501 111 111 GLU CA C 54.14 . 1
502 111 111 GLU CB C 31.59 . 1
503 111 111 GLU N N 123.93 . 1
504 112 112 ASP H H 8.57 . 1
505 112 112 ASP C C 176.2 . 1
506 112 112 ASP CA C 53.48 . 1
507 112 112 ASP CB C 40.53 . 1
508 112 112 ASP N N 124.49 . 1
509 113 113 VAL H H 8.18 . 1
510 113 113 VAL C C 176.19 . 1
511 113 113 VAL CA C 60.21 . 1
512 113 113 VAL CB C 32.64 . 1
513 113 113 VAL N N 119.1 . 1
514 114 114 ASP H H 8.37 . 1
515 114 114 ASP C C 178.22 . 1
516 114 114 ASP CA C 55.47 . 1
517 114 114 ASP CB C 41.08 . 1
518 114 114 ASP N N 124.22 . 1
519 115 115 GLY H H 8.78 . 1
520 115 115 GLY C C 176.09 . 1
521 115 115 GLY CA C 46.34 . 1
522 115 115 GLY N N 112.28 . 1
523 116 116 GLY H H 8.65 . 1
524 116 116 GLY C C 176.12 . 1
525 116 116 GLY CA C 45.63 . 1
526 116 116 GLY N N 111 . 1
527 117 117 LEU H H 7.74 . 1
528 117 117 LEU C C 176.9 . 1
529 117 117 LEU CA C 54.12 . 1
530 117 117 LEU CB C 41.87 . 1
531 117 117 LEU N N 119.56 . 1
532 118 118 LYS H H 7.5 . 1
533 118 118 LYS C C 177.77 . 1
534 118 118 LYS CA C 60.47 . 1
535 118 118 LYS CB C 31.95 . 1
536 118 118 LYS N N 122.07 . 1
537 119 119 SER H H 8.6 . 1
538 119 119 SER C C 177.88 . 1
539 119 119 SER CA C 61.2 . 1
540 119 119 SER N N 113.95 . 1
541 120 120 TRP H H 7.27 . 1
542 120 120 TRP C C 177.86 . 1
543 120 120 TRP CA C 60.63 . 1
544 120 120 TRP CB C 33.2 . 1
545 120 120 TRP N N 125.14 . 1
546 121 121 ARG H H 8.49 . 1
547 121 121 ARG C C 178.69 . 1
548 121 121 ARG CA C 60.11 . 1
549 121 121 ARG CB C 28.4 . 1
550 121 121 ARG N N 120.52 . 1
551 122 122 GLU H H 8.86 . 1
552 122 122 GLU C C 179.83 . 1
553 122 122 GLU CA C 59.28 . 1
554 122 122 GLU CB C 28.48 . 1
555 122 122 GLU N N 117.66 . 1
556 123 123 SER H H 7.82 . 1
557 123 123 SER C C 179.22 . 1
558 123 123 SER CA C 57.29 . 1
559 123 123 SER N N 115.4 . 1
560 126 126 SER C C 177.7 . 1
561 126 126 SER CA C 61.69 . 1
562 126 126 SER CB C 59.0 . 1
563 127 127 ALA H H 7.58 . 1
564 127 127 ALA C C 180.78 . 1
565 127 127 ALA CA C 54.3 . 1
566 127 127 ALA CB C 22.5 . 1
567 127 127 ALA N N 123.45 . 1
568 128 128 LEU H H 9.22 . 1
569 128 128 LEU C C 178.73 . 1
570 128 128 LEU CA C 56.65 . 1
571 128 128 LEU CB C 40.86 . 1
572 128 128 LEU N N 122.78 . 1
573 129 129 ARG H H 8.62 . 1
574 129 129 ARG C C 179.59 . 1
575 129 129 ARG CA C 60.05 . 1
576 129 129 ARG CB C 29.83 . 1
577 129 129 ARG N N 119.07 . 1
578 130 130 ALA H H 7.06 . 1
579 130 130 ALA C C 178.96 . 1
580 130 130 ALA CA C 54.7 . 1
581 130 130 ALA CB C 73.7 . 1
582 130 130 ALA N N 121.56 . 1
583 131 131 TYR H H 7.56 . 1
584 131 131 TYR C C 177.63 . 1
585 131 131 TYR CA C 60.53 . 1
586 131 131 TYR CB C 37.89 . 1
587 131 131 TYR N N 120.75 . 1
588 132 132 VAL C C 178.25 . 1
589 132 132 VAL CA C 65.36 . 1
590 132 132 VAL CB C 30.8 . 1
591 133 133 LYS H H 7.68 . 1
592 133 133 LYS C C 178.07 . 1
593 133 133 LYS CA C 58.13 . 1
594 133 133 LYS CB C 31.26 . 1
595 133 133 LYS N N 119.85 . 1
596 134 134 ASP H H 7.32 . 1
597 134 134 ASP C C 177.09 . 1
598 134 134 ASP CA C 55.81 . 1
599 134 134 ASP CB C 41.14 . 1
600 134 134 ASP N N 116.97 . 1
601 135 135 HIS H H 7.03 . 1
602 135 135 HIS C C 172.38 . 1
603 135 135 HIS CA C 55.66 . 1
604 135 135 HIS CB C 30.22 . 1
605 135 135 HIS N N 110.79 . 1
606 136 136 TYR H H 8.76 . 1
607 136 136 TYR C C 176.19 . 1
608 136 136 TYR CA C 56.26 . 1
609 136 136 TYR N N 119.23 . 1
610 137 137 SER C C 174.83 . 1
611 137 137 SER CA C 60.51 . 1
612 137 137 SER CB C 62.7 . 1
613 138 138 ASN H H 8.19 . 1
614 138 138 ASN C C 173.33 . 1
615 138 138 ASN CA C 52 . 1
616 138 138 ASN CB C 38.54 . 1
617 138 138 ASN N N 121.19 . 1
618 139 139 GLY H H 7.31 . 1
619 139 139 GLY C C 172.26 . 1
620 139 139 GLY CA C 44.14 . 1
621 139 139 GLY N N 131.06 . 1
622 140 140 PHE H H 9.19 . 1
623 140 140 PHE C C 173.88 . 1
624 140 140 PHE CA C 56.24 . 1
625 140 140 PHE CB C 43.53 . 1
626 140 140 PHE N N 120.32 . 1
627 141 141 CYS H H 9 . 1
628 141 141 CYS C C 174.34 . 1
629 141 141 CYS CA C 54.91 . 1
630 141 141 CYS CB C 32.82 . 1
631 141 141 CYS N N 114.08 . 1
632 142 142 THR H H 8.78 . 1
633 142 142 THR C C 171.2 . 1
634 142 142 THR CA C 62.64 . 1
635 142 142 THR CB C 73.98 . 1
636 142 142 THR N N 120 . 1
637 143 143 VAL H H 8.55 . 1
638 143 143 VAL C C 173.73 . 1
639 143 143 VAL CA C 60.51 . 1
640 143 143 VAL CB C 33.08 . 1
641 143 143 VAL N N 126.98 . 1
642 144 144 TYR C C 174.81 . 1
643 144 144 TYR CA C 55.3 . 1
644 144 144 TYR CB C 40.47 . 1
645 145 145 ALA H H 8.85 . 1
646 145 145 ALA C C 175.85 . 1
647 145 145 ALA CA C 50.44 . 1
648 145 145 ALA CB C 21.31 . 1
649 145 145 ALA N N 123.43 . 1
650 146 146 LYS H H 8.94 . 1
651 146 146 LYS C C 174.34 . 1
652 146 146 LYS CA C 54.35 . 1
653 146 146 LYS CB C 35.52 . 1
654 146 146 LYS N N 122.45 . 1
655 147 147 THR H H 8.58 . 1
656 147 147 THR C C 174.13 . 1
657 147 147 THR CA C 62.57 . 1
658 147 147 THR CB C 67.76 . 1
659 147 147 THR N N 119.57 . 1
660 148 148 ILE H H 8.31 . 1
661 148 148 ILE C C 176.24 . 1
662 148 148 ILE CA C 59.76 . 1
663 148 148 ILE CB C 38.96 . 1
664 148 148 ILE N N 128.09 . 1
665 149 149 ASP H H 9.44 . 1
666 149 149 ASP C C 176.02 . 1
667 149 149 ASP CA C 55.08 . 1
668 149 149 ASP CB C 39.02 . 1
669 149 149 ASP N N 106.08 . 1
670 150 150 GLY H H 8.27 . 1
671 150 150 GLY C C 174.02 . 1
672 150 150 GLY CA C 44.82 . 1
673 150 150 GLY N N 128.15 . 1
674 151 151 GLN H H 7.8 . 1
675 151 151 GLN C C 176.55 . 1
676 151 151 GLN CA C 53.61 . 1
677 151 151 GLN CB C 29.48 . 1
678 151 151 GLN N N 118.79 . 1
679 152 152 GLN H H 9.15 . 1
680 152 152 GLN C C 174.76 . 1
681 152 152 GLN CA C 56.78 . 1
682 152 152 GLN CB C 27.84 . 1
683 152 152 GLN N N 129.39 . 1
684 153 153 THR H H 8.98 . 1
685 153 153 THR C C 171.49 . 1
686 153 153 THR CA C 62.07 . 1
687 153 153 THR CB C 71.3 . 1
688 153 153 THR N N 122.43 . 1
689 160 160 SER C C 174.13 . 1
690 160 160 SER CA C 56.92 . 1
691 160 160 SER CB C 65.76 . 1
692 161 161 HIS H H 8.47 . 1
693 161 161 HIS C C 173.25 . 1
694 161 161 HIS CA C 55.28 . 1
695 161 161 HIS CB C 31.94 . 1
696 161 161 HIS N N 122.07 . 1
697 162 162 GLN H H 8.41 . 1
698 162 162 GLN C C 173.44 . 1
699 162 162 GLN CA C 56.07 . 1
700 162 162 GLN CB C 31.46 . 1
701 162 162 GLN N N 19.34 . 1
702 163 163 PHE H H 9.16 . 1
703 163 163 PHE C C 175.13 . 1
704 163 163 PHE CA C 52.64 . 1
705 163 163 PHE CB C 38.42 . 1
706 163 163 PHE N N 127.98 . 1
707 164 164 GLN H H 8.33 . 1
708 164 164 GLN C C 174.17 . 1
709 164 164 GLN CA C 52.36 . 1
710 164 164 GLN CB C 29 . 1
711 164 164 GLN N N 125.17 . 1
712 165 165 PRO C C 177.16 . 1
713 165 165 PRO CA C 63.1 . 1
714 165 165 PRO CB C 31.29 . 1
715 166 166 LYS H H 8.52 . 1
716 166 166 LYS C C 176.35 . 1
717 166 166 LYS CA C 56.38 . 1
718 166 166 LYS CB C 29.45 . 1
719 166 166 LYS N N 120.8 . 1
720 167 167 ASN H H 8.28 . 1
721 167 167 ASN C C 176.48 . 1
722 167 167 ASN CA C 53.95 . 1
723 167 167 ASN CB C 41.39 . 1
724 167 167 ASN N N 122.12 . 1
725 168 168 PHE H H 7.41 . 1
726 168 168 PHE C C 174.54 . 1
727 168 168 PHE CA C 62.85 . 1
728 168 168 PHE CB C 41.6 . 1
729 168 168 PHE N N 118.43 . 1
730 169 169 TRP H H 8.41 . 1
731 169 169 TRP C C 179.5 . 1
732 169 169 TRP CA C 59.66 . 1
733 169 169 TRP CB C 28.1 . 1
734 169 169 TRP N N 117.64 . 1
735 171 171 GLY C C 171.67 . 1
736 171 171 GLY CA C 45.26 . 1
737 172 172 ARG H H 8.13 . 1
738 172 172 ARG C C 174.55 . 1
739 172 172 ARG CA C 58.84 . 1
740 172 172 ARG CB C 31.45 . 1
741 172 172 ARG N N 116.5 . 1
742 173 173 TRP H H 7.87 . 1
743 173 173 TRP C C 176.19 . 1
744 173 173 TRP CA C 55.89 . 1
745 173 173 TRP CB C 31.97 . 1
746 173 173 TRP N N 123 . 1
747 174 174 ARG H H 8.13 . 1
748 174 174 ARG C C 174.94 . 1
749 174 174 ARG CA C 55.27 . 1
750 174 174 ARG N N 122.53 . 1
751 180 180 THR C C 175.55 . 1
752 180 180 THR CA C 63.21 . 1
753 180 180 THR CB C 72.6 . 1
754 181 181 ILE H H 8.96 . 1
755 181 181 ILE C C 177.72 . 1
756 181 181 ILE CA C 58.08 . 1
757 181 181 ILE CB C 41.9 . 1
758 181 181 ILE N N 120.4 . 1
759 182 182 THR H H 8.14 . 1
760 182 182 THR CA C 61.66 . 1
761 182 182 THR CB C 74 . 1
762 182 182 THR N N 112.33 . 1
763 184 184 PRO C C 177.53 . 1
764 184 184 PRO CA C 57.8 . 1
765 185 185 SER H H 7.91 . 1
766 185 185 SER C C 171.51 . 1
767 185 185 SER CA C 57.23 . 1
768 185 185 SER CB C 65.04 . 1
769 185 185 SER N N 120.14 . 1
770 186 186 ALA H H 8.98 . 1
771 186 186 ALA C C 176.42 . 1
772 186 186 ALA CA C 50.17 . 1
773 186 186 ALA CB C 23.36 . 1
774 186 186 ALA N N 126.63 . 1
775 187 187 GLN H H 8.41 . 1
776 187 187 GLN C C 175.48 . 1
777 187 187 GLN CA C 55.6 . 1
778 187 187 GLN CB C 29.22 . 1
779 187 187 GLN N N 120.78 . 1
780 188 188 VAL H H 8.62 . 1
781 188 188 VAL C C 175.23 . 1
782 188 188 VAL CA C 60.35 . 1
783 188 188 VAL CB C 33.3 . 1
784 188 188 VAL N N 126.09 . 1
785 189 189 VAL H H 8.77 . 1
786 189 189 VAL C C 175.14 . 1
787 189 189 VAL CA C 60.17 . 1
788 189 189 VAL CB C 33.88 . 1
789 189 189 VAL N N 125.96 . 1
790 200 200 GLU C C 172.21 . 1
791 200 200 GLU CA C 51.36 . 1
792 200 200 GLU CB C 35.13 . 1
793 201 201 ASP H H 6.67 . 1
794 201 201 ASP C C 175.9 . 1
795 201 201 ASP CA C 53.89 . 1
796 201 201 ASP CB C 41 . 1
797 201 201 ASP N N 121.59 . 1
798 202 202 GLY H H 7.71 . 1
799 202 202 GLY C C 175.59 . 1
800 202 202 GLY CA C 44.73 . 1
801 202 202 GLY N N 107.55 . 1
802 203 203 ASN H H 7.9 . 1
803 203 203 ASN C C 176.15 . 1
804 203 203 ASN CA C 55.01 . 1
805 203 203 ASN CB C 37.4 . 1
806 203 203 ASN N N 122.2 . 1
807 206 206 LEU C C 175.54 . 1
808 206 206 LEU CA C 53.08 . 1
809 206 206 LEU CB C 44.42 . 1
810 207 207 VAL H H 9.13 . 1
811 207 207 VAL C C 175.17 . 1
812 207 207 VAL CA C 61.39 . 1
813 207 207 VAL CB C 34.13 . 1
814 207 207 VAL N N 125.9 . 1
815 208 208 SER H H 8.82 . 1
816 208 208 SER C C 172.69 . 1
817 208 208 SER CA C 55.01 . 1
818 208 208 SER CB C 66.2 . 1
819 208 208 SER N N 121.91 . 1
820 209 209 HIS H H 8.24 . 1
821 209 209 HIS C C 172.87 . 1
822 209 209 HIS CA C 54.89 . 1
823 209 209 HIS CB C 33.24 . 1
824 209 209 HIS N N 126.69 . 1
825 210 210 LYS H H 8.7 . 1
826 210 210 LYS C C 173.21 . 1
827 210 210 LYS CA C 55.43 . 1
828 210 210 LYS CB C 36.84 . 1
829 210 210 LYS N N 125.07 . 1
830 211 211 ASP H H 8.31 . 1
831 211 211 ASP C C 175.03 . 1
832 211 211 ASP CA C 53.31 . 1
833 211 211 ASP CB C 42.7 . 1
834 211 211 ASP N N 126.26 . 1
835 212 212 VAL H H 8.81 . 1
836 212 212 VAL C C 174.69 . 1
837 212 212 VAL CA C 60.65 . 1
838 212 212 VAL CB C 35.04 . 1
839 212 212 VAL N N 122.16 . 1
840 213 213 GLN H H 8.48 . 1
841 213 213 GLN C C 174.2 . 1
842 213 213 GLN CA C 54.53 . 1
843 213 213 GLN CB C 30.88 . 1
844 213 213 GLN N N 125.56 . 1
845 214 214 ASP H H 9.32 . 1
846 214 214 ASP C C 175.59 . 1
847 214 214 ASP CA C 52.84 . 1
848 214 214 ASP CB C 44.78 . 1
849 214 214 ASP N N 126.91 . 1
850 215 215 SER H H 10.45 . 1
851 215 215 SER C C 172 . 1
852 215 215 SER CA C 57.88 . 1
853 215 215 SER CB C 65.79 . 1
854 215 215 SER N N 119.77 . 1
855 216 216 VAL H H 8.85 . 1
856 216 216 VAL C C 173.83 . 1
857 216 216 VAL CA C 58.56 . 1
858 216 216 VAL CB C 36 . 1
859 216 216 VAL N N 119.79 . 1
860 217 217 THR H H 8.45 . 1
861 217 217 THR C C 174.25 . 1
862 217 217 THR CA C 63.07 . 1
863 217 217 THR CB C 74.07 . 1
864 217 217 THR N N 124.16 . 1
865 218 218 VAL H H 8.01 . 1
866 218 218 VAL C C 174.67 . 1
867 218 218 VAL CA C 61.46 . 1
868 218 218 VAL CB C 31.73 . 1
869 218 218 VAL N N 128.89 . 1
870 219 219 SER H H 8.31 . 1
871 219 219 SER C C 173.77 . 1
872 219 219 SER CA C 55.85 . 1
873 219 219 SER CB C 62.97 . 1
874 219 219 SER N N 124.14 . 1
875 220 220 ASN H H 8.53 . 1
876 220 220 ASN C C 175.94 . 1
877 220 220 ASN CA C 50.56 . 1
878 220 220 ASN CB C 40.02 . 1
879 220 220 ASN N N 120.48 . 1
880 221 221 GLU H H 10.24 . 1
881 221 221 GLU C C 178.62 . 1
882 221 221 GLU CA C 60.34 . 1
883 221 221 GLU N N 124.18 . 1
884 226 226 LYS C C 178.49 . 1
885 226 226 LYS CA C 61.25 . 1
886 226 226 LYS CB C 29.03 . 1
887 227 227 GLU H H 8.45 . 1
888 227 227 GLU C C 179.2 . 1
889 227 227 GLU CA C 55.64 . 1
890 227 227 GLU CB C 32.29 . 1
891 227 227 GLU N N 119.97 . 1
892 228 228 PHE H H 8.07 . 1
893 228 228 PHE C C 180.18 . 1
894 228 228 PHE CA C 59.1 . 1
895 228 228 PHE CB C 38.52 . 1
896 228 228 PHE N N 123.3 . 1
897 229 229 ILE H H 9.24 . 1
898 229 229 ILE C C 177.48 . 1
899 229 229 ILE CA C 65.73 . 1
900 229 229 ILE CB C 41 . 1
901 229 229 ILE N N 122.83 . 1
902 230 230 LYS H H 9.05 . 1
903 230 230 LYS C C 178.24 . 1
904 230 230 LYS CA C 60.64 . 1
905 230 230 LYS CB C 28.43 . 1
906 230 230 LYS N N 121.81 . 1
907 233 233 GLU C C 178.46 . 1
908 233 233 GLU CA C 58.67 . 1
909 233 233 GLU CB C 29.96 . 1
910 234 234 SER H H 7.88 . 1
911 234 234 SER C C 177.45 . 1
912 234 234 SER CA C 61.15 . 1
913 234 234 SER CB C 63.56 . 1
914 234 234 SER N N 112.22 . 1
915 235 235 ALA H H 8.54 . 1
916 235 235 ALA C C 182.15 . 1
917 235 235 ALA CA C 54.71 . 1
918 235 235 ALA CB C 19.24 . 1
919 235 235 ALA N N 124.26 . 1
920 237 237 ASN C C 178.38 . 1
921 237 237 ASN CA C 55.85 . 1
922 237 237 ASN CB C 36.74 . 1
923 238 238 GLU H H 8.52 . 1
924 238 238 GLU C C 178.64 . 1
925 238 238 GLU CA C 59.52 . 1
926 238 238 GLU CB C 28.46 . 1
927 238 238 GLU N N 123.45 . 1
928 239 239 TYR H H 8.08 . 1
929 239 239 TYR C C 176.17 . 1
930 239 239 TYR CA C 58.51 . 1
931 239 239 TYR N N 120.73 . 1
932 240 240 GLN H H 8.39 . 1
933 240 240 GLN C C 179.39 . 1
934 240 240 GLN CA C 60.35 . 1
935 240 240 GLN N N 118.56 . 1
936 241 241 THR H H 8.54 . 1
937 241 241 THR C C 176.04 . 1
938 241 241 THR CA C 66.32 . 1
939 241 241 THR N N 116.8 . 1
940 242 242 ALA H H 8.36 . 1
941 242 242 ALA C C 181.15 . 1
942 242 242 ALA CA C 54.69 . 1
943 242 242 ALA N N 126.4 . 1
944 243 243 ILE H H 8.28 . 1
945 243 243 ILE C C 178.16 . 1
946 243 243 ILE CA C 64.89 . 1
947 243 243 ILE N N 121.78 . 1
948 244 244 SER H H 8.13 . 1
949 244 244 SER C C 176.19 . 1
950 244 244 SER CA C 60.2 . 1
951 244 244 SER CB C 62.1 . 1
952 244 244 SER N N 113.09 . 1
953 245 245 GLU H H 7.97 . 1
954 245 245 GLU C C 176.52 . 1
955 245 245 GLU CA C 54.08 . 1
956 245 245 GLU N N 121.89 . 1
957 253 253 THR H H 7.6 . 1
958 253 253 THR C C 179.09 . 1
959 253 253 THR CA C 64.73 . 1
960 253 253 THR N N 121.05 . 1
961 254 254 THR H H 7.73 . 1
962 254 254 THR C C 177.82 . 1
963 254 254 THR CA C 67.72 . 1
964 254 254 THR CB C 72.6 . 1
965 254 254 THR N N 121.74 . 1
966 255 255 PHE H H 7.86 . 1
967 255 255 PHE C C 177.51 . 1
968 255 255 PHE CA C 59.71 . 1
969 255 255 PHE N N 114.12 . 1
970 256 256 LYS H H 6.64 . 1
971 256 256 LYS C C 175.94 . 1
972 256 256 LYS CA C 58.14 . 1
973 256 256 LYS CB C 31.55 . 1
974 256 256 LYS N N 115.82 . 1
975 257 257 ALA H H 7.04 . 1
976 257 257 ALA C C 177.93 . 1
977 257 257 ALA CA C 52.5 . 1
978 257 257 ALA N N 118.16 . 1
979 258 258 LEU H H 7.27 . 1
980 258 258 LEU C C 173.74 . 1
981 258 258 LEU CA C 56.14 . 1
982 258 258 LEU CB C 41.2 . 1
983 258 258 LEU N N 119.78 . 1
984 259 259 ARG H H 6.68 . 1
985 259 259 ARG C C 175.51 . 1
986 259 259 ARG CA C 54.39 . 1
987 259 259 ARG CB C 31.2 . 1
988 259 259 ARG N N 113.41 . 1
989 260 260 ARG H H 8.51 . 1
990 260 260 ARG C C 175.99 . 1
991 260 260 ARG CA C 56.4 . 1
992 260 260 ARG CB C 31.51 . 1
993 260 260 ARG N N 127.69 . 1
994 261 261 GLN H H 8.74 . 1
995 261 261 GLN C C 174.83 . 1
996 261 261 GLN CA C 58.1 . 1
997 261 261 GLN CB C 28.56 . 1
998 261 261 GLN N N 121.24 . 1
999 262 262 LEU H H 7.29 . 1
1000 262 262 LEU C C 173.17 . 1
1001 262 262 LEU CA C 51.7 . 1
1002 262 262 LEU CB C 45.38 . 1
1003 262 262 LEU N N 116.2 . 1
1004 263 263 PRO C C 177.88 . 1
1005 263 263 PRO CA C 61.51 . 1
1006 263 263 PRO CB C 31.9 . 1
1007 264 264 VAL H H 9.22 . 1
1008 264 264 VAL C C 176.04 . 1
1009 264 264 VAL CA C 64.72 . 1
1010 264 264 VAL CB C 31 . 1
1011 264 264 VAL N N 122.88 . 1
1012 265 265 THR H H 6.7 . 1
1013 265 265 THR C C 175.07 . 1
1014 265 265 THR CA C 62.07 . 1
1015 265 265 THR CB C 66.5 . 1
1016 265 265 THR N N 108.83 . 1
1017 266 266 ARG H H 8.28 . 1
1018 266 266 ARG C C 174.09 . 1
1019 266 266 ARG CA C 57.5 . 1
1020 266 266 ARG CB C 26.3 . 1
1021 266 266 ARG N N 114.5 . 1
1022 267 267 THR H H 7.36 . 1
1023 267 267 THR C C 172.84 . 1
1024 267 267 THR CA C 59.41 . 1
1025 267 267 THR CB C 71.29 . 1
1026 267 267 THR N N 111.19 . 1
1027 268 268 LYS H H 7.82 . 1
1028 268 268 LYS C C 177.29 . 1
1029 268 268 LYS CA C 56.33 . 1
1030 268 268 LYS CB C 31.5 . 1
1031 268 268 LYS N N 120.07 . 1
1032 269 269 ILE H H 9.44 . 1
1033 269 269 ILE C C 176.06 . 1
1034 269 269 ILE CA C 62.34 . 1
1035 269 269 ILE CB C 37.1 . 1
1036 269 269 ILE N N 124.09 . 1
1037 270 270 ASP H H 7.91 . 1
1038 270 270 ASP C C 176.7 . 1
1039 270 270 ASP CA C 51.49 . 1
1040 270 270 ASP CB C 38.94 . 1
1041 270 270 ASP N N 125.11 . 1
1042 271 271 TRP H H 8.28 . 1
1043 271 271 TRP C C 177.47 . 1
1044 271 271 TRP CA C 60.85 . 1
1045 271 271 TRP N N 126.78 . 1
1046 272 272 ASN H H 8.17 . 1
1047 272 272 ASN C C 177.75 . 1
1048 272 272 ASN CA C 55.9 . 1
1049 272 272 ASN CB C 37.21 . 1
1050 272 272 ASN N N 116.66 . 1
1051 273 273 LYS H H 7.38 . 1
1052 273 273 LYS C C 179.23 . 1
1053 273 273 LYS CA C 57.84 . 1
1054 273 273 LYS CB C 31.19 . 1
1055 273 273 LYS N N 120.62 . 1
1056 274 274 ILE H H 7.26 . 1
1057 274 274 ILE C C 177.4 . 1
1058 274 274 ILE CA C 63.12 . 1
1059 274 274 ILE CB C 36.29 . 1
1060 274 274 ILE N N 118.52 . 1
1061 275 275 LEU H H 7.48 . 1
1062 275 275 LEU C C 177.55 . 1
1063 275 275 LEU CA C 55.2 . 1
1064 275 275 LEU CB C 40.46 . 1
1065 275 275 LEU N N 119.03 . 1
1066 276 276 SER H H 7.65 . 1
1067 276 276 SER C C 174.31 . 1
1068 276 276 SER CA C 58.66 . 1
1069 276 276 SER CB C 63.64 . 1
1070 276 276 SER N N 114.76 . 1
1071 277 277 TYR H H 7.58 . 1
1072 277 277 TYR C C 175.45 . 1
1073 277 277 TYR CA C 57.74 . 1
1074 277 277 TYR CB C 37.71 . 1
1075 277 277 TYR N N 122.67 . 1
1076 278 278 LYS H H 7.95 . 1
1077 278 278 LYS C C 175.94 . 1
1078 278 278 LYS CA C 55.33 . 1
1079 278 278 LYS CB C 32.09 . 1
1080 278 278 LYS N N 123.74 . 1
1081 279 279 ILE H H 7.95 . 1
1082 279 279 ILE C C 176.76 . 1
1083 279 279 ILE CA C 60.96 . 1
1084 279 279 ILE CB C 37.6 . 1
1085 279 279 ILE N N 122.68 . 1
1086 280 280 GLY H H 8.33 . 1
1087 280 280 GLY C C 173.74 . 1
1088 280 280 GLY CA C 44.6 . 1
1089 280 280 GLY N N 113.44 . 1
1090 281 281 LYS H H 8.02 . 1
1091 281 281 LYS C C 175.67 . 1
1092 281 281 LYS CA C 55.64 . 1
1093 281 281 LYS CB C 32.1 . 1
1094 281 281 LYS N N 121.59 . 1
1095 282 282 GLU H H 8.48 . 1
1096 282 282 GLU C C 176.64 . 1
1097 282 282 GLU CA C 56.27 . 1
1098 282 282 GLU CB C 28.85 . 1
1099 282 282 GLU N N 122.02 . 1
1100 283 283 MET H H 8.03 . 1
1101 283 283 MET C C 176.1 . 1
1102 283 283 MET CA C 55.01 . 1
1103 283 283 MET CB C 31.91 . 1
1104 283 283 MET N N 121.14 . 1
1105 284 284 GLN H H 8.24 . 1
1106 284 284 GLN C C 175.54 . 1
1107 284 284 GLN CA C 55.48 . 1
1108 284 284 GLN CB C 28.54 . 1
1109 284 284 GLN N N 121.55 . 1
1110 285 285 ASN H H 8.32 . 1
1111 285 285 ASN C C 173.75 . 1
1112 285 285 ASN CA C 52.98 . 1
1113 285 285 ASN CB C 38.58 . 1
1114 285 285 ASN N N 120.64 . 1
1115 286 286 ALA H H 7.76 . 1
1116 286 286 ALA C C 182.36 . 1
1117 286 286 ALA CA C 53.44 . 1
1118 286 286 ALA CB C 19.26 . 1
1119 286 286 ALA N N 130.08 . 1
stop_
save_
save_chemical_shifts_2
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'2D 1H-15N HSQC'
stop_
loop_
_Sample_label
$CP_chemical_shift_perturpation
$CAH3a_b_chemical_shift_perturpation
stop_
_Sample_conditions_label $sample_conditions_1
_Chem_shift_reference_set_label $reference_1
_Mol_system_component_name CPbeta_subunit
_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 3 3 ASP C C 176.24 . 1
2 3 3 ASP CA C 54.63 . 1
3 3 3 ASP CB C 40.77 . 1
4 4 4 GLN H H 8.46 . 1
5 4 4 GLN C C 178.21 . 1
6 4 4 GLN CA C 57.87 . 1
7 4 4 GLN CB C 28.18 . 1
8 4 4 GLN N N 121.72 . 1
9 5 5 GLN H H 8.08 . 1
10 5 5 GLN C C 177.45 . 1
11 5 5 GLN CA C 59.56 . 1
12 5 5 GLN CB C 28.19 . 1
13 5 5 GLN N N 118.61 . 1
14 6 6 LEU H H 7.95 . 1
15 6 6 LEU C C 178.1 . 1
16 6 6 LEU CA C 57.78 . 1
17 6 6 LEU CB C 39.51 . 1
18 6 6 LEU N N 121.14 . 1
19 7 7 ASP H H 8 . 1
20 7 7 ASP C C 180.12 . 1
21 7 7 ASP CA C 57.32 . 1
22 7 7 ASP CB C 39.4 . 1
23 7 7 ASP N N 118.3 . 1
24 8 8 CYS H H 7.79 . 1
25 8 8 CYS C C 177.45 . 1
26 8 8 CYS CA C 57.79 . 1
27 8 8 CYS N N 120.43 . 1
28 9 9 ALA H H 8.2 . 1
29 9 9 ALA C C 177.65 . 1
30 9 9 ALA CA C 52.05 . 1
31 9 9 ALA CB C 18.4 . 1
32 9 9 ALA N N 129.24 . 1
33 10 10 LEU H H 8.23 . 1
34 10 10 LEU C C 175.95 . 1
35 10 10 LEU CA C 53.91 . 1
36 10 10 LEU CB C 40.7 . 1
37 10 10 LEU N N 119.67 . 1
38 11 11 ASP C C 175.99 . 1
39 11 11 ASP CA C 54 . 1
40 11 11 ASP CB C 41.26 . 1
41 12 12 LEU H H 7.88 . 1
42 12 12 LEU C C 179.69 . 1
43 12 12 LEU CA C 57.85 . 1
44 12 12 LEU CB C 40.41 . 1
45 12 12 LEU N N 120.08 . 1
46 13 13 MET H H 7.55 . 1
47 13 13 MET C C 178.29 . 1
48 13 13 MET CA C 55.34 . 1
49 13 13 MET CB C 29.4 . 1
50 13 13 MET N N 115.22 . 1
51 14 14 ARG H H 7.35 . 1
52 14 14 ARG C C 175.8 . 1
53 14 14 ARG CA C 56.93 . 1
54 14 14 ARG CB C 30 . 1
55 14 14 ARG N N 118.65 . 1
56 15 15 ARG H H 7.35 . 1
57 15 15 ARG C C 175.24 . 1
58 15 15 ARG CA C 55.87 . 1
59 15 15 ARG CB C 30.4 . 1
60 15 15 ARG N N 116.85 . 1
61 16 16 LEU H H 7.15 . 1
62 16 16 LEU C C 174.99 . 1
63 16 16 LEU CA C 53.14 . 1
64 16 16 LEU CB C 39.4 . 1
65 16 16 LEU N N 118.25 . 1
66 18 18 PRO C C 177.68 . 1
67 18 18 PRO CA C 64.18 . 1
68 19 19 GLN H H 8.89 . 1
69 19 19 GLN C C 176.5 . 1
70 19 19 GLN CA C 57.96 . 1
71 19 19 GLN CB C 26.67 . 1
72 19 19 GLN N N 118.05 . 1
73 20 20 GLN H H 7.21 . 1
74 20 20 GLN C C 175.04 . 1
75 20 20 GLN CA C 54.01 . 1
76 20 20 GLN CB C 28.09 . 1
77 20 20 GLN N N 117.12 . 1
78 21 21 ILE H H 7.01 . 1
79 21 21 ILE C C 175.94 . 1
80 21 21 ILE CA C 65.14 . 1
81 21 21 ILE CB C 37.52 . 1
82 21 21 ILE N N 120.56 . 1
83 22 22 GLU H H 8.6 . 1
84 22 22 GLU C C 179.23 . 1
85 22 22 GLU CA C 59.88 . 1
86 22 22 GLU CB C 28.43 . 1
87 22 22 GLU N N 119.6 . 1
88 23 23 LYS H H 7.63 . 1
89 23 23 LYS C C 178.24 . 1
90 23 23 LYS CA C 57.13 . 1
91 23 23 LYS CB C 30.99 . 1
92 23 23 LYS N N 120.55 . 1
93 24 24 ASN H H 8.43 . 1
94 24 24 ASN C C 176.94 . 1
95 24 24 ASN CA C 55.64 . 1
96 24 24 ASN CB C 36.61 . 1
97 24 24 ASN N N 118.28 . 1
98 25 25 LEU H H 8.5 . 1
99 25 25 LEU C C 177.8 . 1
100 25 25 LEU CA C 57.46 . 1
101 25 25 LEU CB C 41.2 . 1
102 25 25 LEU N N 120.49 . 1
103 26 26 SER H H 7.29 . 1
104 26 26 SER C C 177.18 . 1
105 26 26 SER CA C 61.56 . 1
106 26 26 SER CB C 62.97 . 1
107 26 26 SER N N 112.72 . 1
108 27 27 ASP H H 8.15 . 1
109 27 27 ASP C C 177.31 . 1
110 27 27 ASP CA C 56.84 . 1
111 27 27 ASP CB C 40.7 . 1
112 27 27 ASP N N 121.83 . 1
113 28 28 LEU H H 8.33 . 1
114 28 28 LEU C C 178.24 . 1
115 28 28 LEU CA C 57.9 . 1
116 28 28 LEU CB C 41.23 . 1
117 28 28 LEU N N 122.16 . 1
118 29 29 ILE H H 7.9 . 1
119 29 29 ILE C C 176.87 . 1
120 29 29 ILE CA C 64.61 . 1
121 29 29 ILE N N 119.13 . 1
122 30 30 ASP H H 7.25 . 1
123 30 30 ASP C C 177.66 . 1
124 30 30 ASP CA C 56.55 . 1
125 30 30 ASP CB C 39.9 . 1
126 30 30 ASP N N 118.25 . 1
127 31 31 LEU H H 7.61 . 1
128 31 31 LEU C C 177.33 . 1
129 31 31 LEU CA C 57.14 . 1
130 31 31 LEU CB C 41.86 . 1
131 31 31 LEU N N 118.91 . 1
132 32 32 VAL H H 7.85 . 1
133 32 32 VAL C C 172.74 . 1
134 32 32 VAL CA C 57.56 . 1
135 32 32 VAL CB C 31.22 . 1
136 32 32 VAL N N 115 . 1
137 34 34 SER H H 8.55 . 1
138 34 34 SER C C 175.05 . 1
139 34 34 SER CA C 57.77 . 1
140 34 34 SER CB C 64.43 . 1
141 34 34 SER N N 122.26 . 1
142 35 35 LEU H H 8.14 . 1
143 35 35 LEU C C 177.32 . 1
144 35 35 LEU CA C 55.65 . 1
145 35 35 LEU CB C 39.97 . 1
146 35 35 LEU N N 120.37 . 1
147 36 36 CYS H H 8.17 . 1
148 36 36 CYS C C 178.26 . 1
149 36 36 CYS CA C 57.8 . 1
150 36 36 CYS CB C 39.5 . 1
151 36 36 CYS N N 120.34 . 1
152 37 37 GLU H H 7.98 . 1
153 37 37 GLU C C 179.5 . 1
154 37 37 GLU CA C 59.58 . 1
155 37 37 GLU CB C 28.34 . 1
156 37 37 GLU N N 119.35 . 1
157 38 38 ASP H H 7.96 . 1
158 38 38 ASP C C 178.96 . 1
159 38 38 ASP CA C 56.77 . 1
160 38 38 ASP CB C 41.11 . 1
161 38 38 ASP N N 119.49 . 1
162 39 39 LEU H H 8.56 . 1
163 39 39 LEU C C 178.5 . 1
164 39 39 LEU CA C 57.6 . 1
165 39 39 LEU CB C 40.69 . 1
166 39 39 LEU N N 121.38 . 1
167 40 40 LEU H H 8.17 . 1
168 40 40 LEU C C 179.21 . 1
169 40 40 LEU CA C 57.19 . 1
170 40 40 LEU CB C 40.03 . 1
171 40 40 LEU N N 117.74 . 1
172 41 41 SER H H 7.3 . 1
173 41 41 SER C C 175.41 . 1
174 41 41 SER CA C 59.1 . 1
175 41 41 SER CB C 64.2 . 1
176 41 41 SER N N 109.6 . 1
177 42 42 SER H H 7.38 . 1
178 42 42 SER C C 173.43 . 1
179 42 42 SER CA C 59.92 . 1
180 42 42 SER CB C 65.3 . 1
181 42 42 SER N N 114.82 . 1
182 43 43 VAL H H 7.63 . 1
183 43 43 VAL C C 174.7 . 1
184 43 43 VAL CA C 61.28 . 1
185 43 43 VAL CB C 31.4 . 1
186 43 43 VAL N N 122.75 . 1
187 44 44 ASP H H 8.02 . 1
188 44 44 ASP C C 174.3 . 1
189 44 44 ASP CA C 54.82 . 1
190 44 44 ASP CB C 41.31 . 1
191 44 44 ASP N N 126.85 . 1
192 45 45 GLN H H 7.98 . 1
193 45 45 GLN C C 172.39 . 1
194 45 45 GLN CA C 52.7 . 1
195 45 45 GLN CB C 30.74 . 1
196 45 45 GLN N N 119.49 . 1
197 46 46 PRO C C 176.71 . 1
198 46 46 PRO CA C 62.49 . 1
199 46 46 PRO CB C 31.4 . 1
200 47 47 LEU H H 8.68 . 1
201 47 47 LEU C C 177.74 . 1
202 47 47 LEU CA C 54.7 . 1
203 47 47 LEU CB C 42.62 . 1
204 47 47 LEU N N 123.13 . 1
205 48 48 LYS H H 7.59 . 1
206 48 48 LYS C C 174.39 . 1
207 48 48 LYS CA C 54.41 . 1
208 48 48 LYS CB C 34.27 . 1
209 48 48 LYS N N 121.77 . 1
210 49 49 ILE H H 8.15 . 1
211 49 49 ILE C C 175.01 . 1
212 49 49 ILE CA C 60.37 . 1
213 49 49 ILE CB C 39.54 . 1
214 49 49 ILE N N 120.77 . 1
215 50 50 ALA H H 8.57 . 1
216 50 50 ALA C C 173.49 . 1
217 50 50 ALA CA C 49.8 . 1
218 50 50 ALA CB C 21.76 . 1
219 50 50 ALA N N 129.99 . 1
220 51 51 ARG H H 8.28 . 1
221 51 51 ARG C C 176.74 . 1
222 51 51 ARG CA C 54.28 . 1
223 51 51 ARG CB C 30.8 . 1
224 51 51 ARG N N 119.04 . 1
225 52 52 ASP H H 9.11 . 1
226 52 52 ASP C C 177.09 . 1
227 52 52 ASP CA C 53.38 . 1
228 52 52 ASP CB C 40.64 . 1
229 52 52 ASP N N 128.96 . 1
230 53 53 LYS H H 9.12 . 1
231 53 53 LYS C C 177.7 . 1
232 53 53 LYS CA C 57.6 . 1
233 53 53 LYS CB C 31.91 . 1
234 53 53 LYS N N 127.66 . 1
235 54 54 VAL H H 8.49 . 1
236 54 54 VAL C C 178 . 1
237 54 54 VAL CA C 64.95 . 1
238 54 54 VAL CB C 31.11 . 1
239 54 54 VAL N N 121.57 . 1
240 55 55 VAL H H 7.3 . 1
241 55 55 VAL C C 176.7 . 1
242 55 55 VAL CA C 60.99 . 1
243 55 55 VAL CB C 32.2 . 1
244 55 55 VAL N N 111.68 . 1
245 56 56 GLY H H 8.03 . 1
246 56 56 GLY C C 173.59 . 1
247 56 56 GLY CA C 46.31 . 1
248 56 56 GLY N N 111.54 . 1
249 57 57 LYS H H 6.94 . 1
250 57 57 LYS C C 175.6 . 1
251 57 57 LYS CA C 54.59 . 1
252 57 57 LYS CB C 35.8 . 1
253 57 57 LYS N N 116.98 . 1
254 58 58 ASP H H 8.73 . 1
255 58 58 ASP C C 176.72 . 1
256 58 58 ASP CA C 54.51 . 1
257 58 58 ASP CB C 42.11 . 1
258 58 58 ASP N N 125.44 . 1
259 59 59 TYR H H 9.76 . 1
260 59 59 TYR C C 172.09 . 1
261 59 59 TYR CA C 55.89 . 1
262 59 59 TYR CB C 40.6 . 1
263 59 59 TYR N N 119.58 . 1
264 60 60 LEU H H 7.94 . 1
265 60 60 LEU C C 176.54 . 1
266 60 60 LEU CA C 52.8 . 1
267 60 60 LEU CB C 44.18 . 1
268 60 60 LEU N N 118.84 . 1
269 61 61 LEU H H 8.45 . 1
270 61 61 LEU C C 176.43 . 1
271 61 61 LEU CA C 53.22 . 1
272 61 61 LEU CB C 40.63 . 1
273 61 61 LEU N N 121 . 1
274 62 62 CYS H H 8.93 . 1
275 62 62 CYS C C 173.06 . 1
276 62 62 CYS CA C 56.26 . 1
277 62 62 CYS CB C 30.6 . 1
278 62 62 CYS N N 116.74 . 1
279 63 63 ASP H H 8.72 . 1
280 63 63 ASP C C 177.8 . 1
281 63 63 ASP CA C 57.35 . 1
282 63 63 ASP CB C 41 . 1
283 63 63 ASP N N 116.43 . 1
284 64 64 TYR H H 7.48 . 1
285 64 64 TYR C C 175.77 . 1
286 64 64 TYR CA C 59.45 . 1
287 64 64 TYR CB C 35.1 . 1
288 64 64 TYR N N 114.08 . 1
289 65 65 ASN H H 7.74 . 1
290 65 65 ASN C C 172.26 . 1
291 65 65 ASN CA C 51.36 . 1
292 65 65 ASN CB C 35.1 . 1
293 65 65 ASN N N 116.81 . 1
294 66 66 ARG H H 6.74 . 1
295 66 66 ARG C C 175.97 . 1
296 66 66 ARG CA C 54.07 . 1
297 66 66 ARG CB C 31.98 . 1
298 66 66 ARG N N 121.78 . 1
299 67 67 ASP H H 8.51 . 1
300 67 67 ASP C C 175.94 . 1
301 67 67 ASP CA C 54.04 . 1
302 67 67 ASP CB C 41.27 . 1
303 67 67 ASP N N 128.78 . 1
304 68 68 GLY H H 8.3 . 1
305 68 68 GLY C C 174.28 . 1
306 68 68 GLY CA C 46.7 . 1
307 68 68 GLY N N 113.9 . 1
308 69 69 ASP H H 8.54 . 1
309 69 69 ASP C C 174.51 . 1
310 69 69 ASP CA C 53.28 . 1
311 69 69 ASP CB C 40.74 . 1
312 69 69 ASP N N 128.29 . 1
313 70 70 SER H H 7.78 . 1
314 70 70 SER C C 171.73 . 1
315 70 70 SER CA C 57.82 . 1
316 70 70 SER CB C 64.5 . 1
317 70 70 SER N N 115.64 . 1
318 71 71 TYR H H 7.9 . 1
319 71 71 TYR C C 175.17 . 1
320 71 71 TYR CA C 56.37 . 1
321 71 71 TYR CB C 41.2 . 1
322 71 71 TYR N N 118.46 . 1
323 72 72 ARG H H 8.62 . 1
324 72 72 ARG C C 174.73 . 1
325 72 72 ARG CA C 54.49 . 1
326 72 72 ARG CB C 31.02 . 1
327 72 72 ARG N N 125.33 . 1
328 73 73 SER H H 7.38 . 1
329 73 73 SER C C 176 . 1
330 73 73 SER CA C 52.28 . 1
331 73 73 SER CB C 64.26 . 1
332 73 73 SER N N 119.61 . 1
333 74 74 PRO C C 178.32 . 1
334 74 74 PRO CA C 62.05 . 1
335 74 74 PRO CB C 31.1 . 1
336 75 75 TRP H H 8.94 . 1
337 75 75 TRP C C 172.79 . 1
338 75 75 TRP CA C 52.25 . 1
339 75 75 TRP N N 122.53 . 1
340 76 76 SER H H 6.9 . 1
341 76 76 SER C C 175.34 . 1
342 76 76 SER CA C 57.9 . 1
343 76 76 SER CB C 63.6 . 1
344 76 76 SER N N 113.6 . 1
345 77 77 ASN H H 7.81 . 1
346 77 77 ASN C C 173.13 . 1
347 77 77 ASN CA C 53 . 1
348 77 77 ASN CB C 35.2 . 1
349 77 77 ASN N N 121.84 . 1
350 78 78 LYS H H 6.63 . 1
351 78 78 LYS C C 176.89 . 1
352 78 78 LYS CA C 53.4 . 1
353 78 78 LYS CB C 35.2 . 1
354 78 78 LYS N N 113.02 . 1
355 79 79 TYR H H 8.64 . 1
356 79 79 TYR C C 175.64 . 1
357 79 79 TYR CA C 58.96 . 1
358 79 79 TYR CB C 41 . 1
359 79 79 TYR N N 123.06 . 1
360 80 80 ASP H H 8.7 . 1
361 80 80 ASP C C 175.73 . 1
362 80 80 ASP CA C 51.69 . 1
363 80 80 ASP CB C 44.28 . 1
364 80 80 ASP N N 121.1 . 1
365 82 82 PRO C C 175.44 . 1
366 82 82 PRO CA C 64.15 . 1
367 82 82 PRO CB C 31.32 . 1
368 83 83 LEU H H 7.56 . 1
369 83 83 LEU C C 176.78 . 1
370 83 83 LEU CA C 53.27 . 1
371 83 83 LEU CB C 44.09 . 1
372 83 83 LEU N N 122.58 . 1
373 84 84 GLU H H 8.7 . 1
374 84 84 GLU C C 176.64 . 1
375 84 84 GLU CA C 57.52 . 1
376 84 84 GLU CB C 29.18 . 1
377 84 84 GLU N N 125.66 . 1
378 85 85 ASP H H 8.22 . 1
379 85 85 ASP C C 175.64 . 1
380 85 85 ASP CA C 53.06 . 1
381 85 85 ASP CB C 39.69 . 1
382 85 85 ASP N N 119.32 . 1
383 86 86 GLY H H 7.69 . 1
384 86 86 GLY C C 173.74 . 1
385 86 86 GLY CA C 44.49 . 1
386 86 86 GLY N N 107.81 . 1
387 87 87 ALA H H 8.54 . 1
388 87 87 ALA C C 178.59 . 1
389 87 87 ALA CA C 52.96 . 1
390 87 87 ALA CB C 73.781 . 1
391 87 87 ALA N N 126.15 . 1
392 88 88 MET H H 8.49 . 1
393 88 88 MET C C 174.04 . 1
394 88 88 MET CA C 52.07 . 1
395 88 88 MET CB C 33.86 . 1
396 88 88 MET N N 124.02 . 1
397 89 89 PRO C C 177.19 . 1
398 89 89 PRO CA C 61.92 . 1
399 89 89 PRO CB C 31.1 . 1
400 90 90 SER H H 8.94 . 1
401 90 90 SER C C 173.94 . 1
402 90 90 SER CA C 57.75 . 1
403 90 90 SER CB C 63.5 . 1
404 90 90 SER N N 118.69 . 1
405 91 91 ALA H H 8.71 . 1
406 91 91 ALA C C 181.31 . 1
407 91 91 ALA CA C 55.55 . 1
408 91 91 ALA CB C 73.4 . 1
409 91 91 ALA N N 123.94 . 1
410 92 92 ARG H H 8.43 . 1
411 92 92 ARG C C 178.72 . 1
412 92 92 ARG CA C 58.6 . 1
413 92 92 ARG CB C 29.2 . 1
414 92 92 ARG N N 117.69 . 1
415 93 93 LEU H H 7.52 . 1
416 93 93 LEU C C 178.85 . 1
417 93 93 LEU CA C 56.39 . 1
418 93 93 LEU CB C 40.45 . 1
419 93 93 LEU N N 122.41 . 1
420 94 94 ARG H H 9.28 . 1
421 94 94 ARG C C 177.46 . 1
422 94 94 ARG CA C 56.73 . 1
423 94 94 ARG CB C 27.58 . 1
424 94 94 ARG N N 121.47 . 1
425 95 95 LYS H H 7.27 . 1
426 95 95 LYS C C 179.52 . 1
427 95 95 LYS CA C 59.7 . 1
428 95 95 LYS CB C 31.29 . 1
429 95 95 LYS N N 118.68 . 1
430 96 96 LEU H H 6.82 . 1
431 96 96 LEU C C 177.93 . 1
432 96 96 LEU CA C 57.08 . 1
433 96 96 LEU CB C 40.84 . 1
434 96 96 LEU N N 120.4 . 1
435 97 97 GLU H H 8.85 . 1
436 97 97 GLU C C 180.12 . 1
437 97 97 GLU CA C 60.13 . 1
438 97 97 GLU CB C 31.47 . 1
439 97 97 GLU N N 123.68 . 1
440 98 98 VAL H H 8.68 . 1
441 98 98 VAL C C 179.08 . 1
442 98 98 VAL CA C 66.56 . 1
443 98 98 VAL CB C 31.2 . 1
444 98 98 VAL N N 125.75 . 1
445 99 99 GLU H H 7.53 . 1
446 99 99 GLU C C 180.12 . 1
447 99 99 GLU CA C 59.07 . 1
448 99 99 GLU CB C 28.6 . 1
449 99 99 GLU N N 120.83 . 1
450 104 104 PHE C C 177.4 . 1
451 104 104 PHE CA C 62.9 . 1
452 104 104 PHE CB C 40.5 . 1
453 105 105 ASP H H 7.92 . 1
454 105 105 ASP C C 178.54 . 1
455 105 105 ASP CA C 57.43 . 1
456 105 105 ASP CB C 41.2 . 1
457 105 105 ASP N N 123.1 . 1
458 106 106 GLN H H 7.1 . 1
459 106 106 GLN C C 178.05 . 1
460 106 106 GLN CA C 58.67 . 1
461 106 106 GLN CB C 27.97 . 1
462 106 106 GLN N N 117.96 . 1
463 107 107 TYR H H 7.98 . 1
464 107 107 TYR C C 175.87 . 1
465 107 107 TYR CA C 61.56 . 1
466 107 107 TYR CB C 38.5 . 1
467 107 107 TYR N N 120.47 . 1
468 108 108 ARG H H 8.82 . 1
469 108 108 ARG C C 178.83 . 1
470 108 108 ARG CA C 58.52 . 1
471 108 108 ARG CB C 26.8 . 1
472 108 108 ARG N N 119.9 . 1
473 109 109 ASP H H 8.11 . 1
474 109 109 ASP C C 178.76 . 1
475 109 109 ASP CA C 58.6 . 1
476 109 109 ASP CB C 40.6 . 1
477 109 109 ASP N N 121.91 . 1
478 110 110 LEU H H 7.89 . 1
479 110 110 LEU C C 179.13 . 1
480 110 110 LEU CA C 57.04 . 1
481 110 110 LEU CB C 40.95 . 1
482 110 110 LEU N N 117.6 . 1
483 111 111 TYR H H 7.9 . 1
484 111 111 TYR C C 175.36 . 1
485 111 111 TYR CA C 61.37 . 1
486 111 111 TYR CB C 42 . 1
487 111 111 TYR N N 113.13 . 1
488 112 112 PHE C C 176.1 . 1
489 112 112 PHE CA C 57.76 . 1
490 112 112 PHE CB C 41.1 . 1
491 113 113 GLU H H 7.8 . 1
492 113 113 GLU C C 175.56 . 1
493 113 113 GLU CA C 57.06 . 1
494 113 113 GLU CB C 26.7 . 1
495 113 113 GLU N N 115.83 . 1
496 114 114 GLY H H 6.95 . 1
497 114 114 GLY C C 173.79 . 1
498 114 114 GLY CA C 43.98 . 1
499 114 114 GLY N N 128.65 . 1
500 115 115 GLY H H 8.72 . 1
501 115 115 GLY C C 172.81 . 1
502 115 115 GLY CA C 44.65 . 1
503 115 115 GLY N N 109.14 . 1
504 116 116 VAL H H 8.87 . 1
505 116 116 VAL C C 173 . 1
506 116 116 VAL CA C 60.83 . 1
507 116 116 VAL CB C 35.45 . 1
508 116 116 VAL N N 119.52 . 1
509 117 117 SER H H 8.72 . 1
510 117 117 SER C C 177.9 . 1
511 117 117 SER CA C 56.44 . 1
512 117 117 SER CB C 67.95 . 1
513 117 117 SER N N 118.74 . 1
514 122 122 TRP C C 173.52 . 1
515 122 122 TRP CA C 57 . 1
516 122 122 TRP CB C 30 . 1
517 123 123 ASP H H 8.22 . 1
518 123 123 ASP C C 175.68 . 1
519 123 123 ASP CA C 55.6 . 1
520 123 123 ASP CB C 42.63 . 1
521 123 123 ASP N N 119.25 . 1
522 124 124 LEU H H 7.54 . 1
523 124 124 LEU C C 176.67 . 1
524 124 124 LEU CA C 52.88 . 1
525 124 124 LEU CB C 44.77 . 1
526 124 124 LEU N N 119.25 . 1
527 125 125 ASP H H 8.34 . 1
528 125 125 ASP C C 177.03 . 1
529 125 125 ASP CA C 56.6 . 1
530 125 125 ASP CB C 39.4 . 1
531 125 125 ASP N N 121.4 . 1
532 126 126 HIS H H 8.29 . 1
533 126 126 HIS C C 173.75 . 1
534 126 126 HIS CA C 55.06 . 1
535 126 126 HIS CB C 27.67 . 1
536 126 126 HIS N N 116.81 . 1
537 127 127 GLY H H 7.27 . 1
538 127 127 GLY C C 171.91 . 1
539 127 127 GLY CA C 45.39 . 1
540 127 127 GLY N N 106.79 . 1
541 128 128 PHE H H 8.24 . 1
542 128 128 PHE C C 181.55 . 1
543 128 128 PHE CA C 56.15 . 1
544 128 128 PHE CB C 37.37 . 1
545 128 128 PHE N N 120.2 . 1
546 135 135 LYS C C 175.1 . 1
547 135 135 LYS CA C 54.46 . 1
548 136 136 LYS H H 9.6 . 1
549 136 136 LYS C C 172.98 . 1
550 136 136 LYS CA C 55.42 . 1
551 136 136 LYS N N 128.71 . 1
552 137 137 ALA H H 8.87 . 1
553 137 137 ALA C C 178.07 . 1
554 137 137 ALA CA C 50.43 . 1
555 137 137 ALA CB C 19.92 . 1
556 137 137 ALA N N 130.89 . 1
557 138 138 GLY H H 8.36 . 1
558 138 138 GLY C C 174.01 . 1
559 138 138 GLY CA C 44.56 . 1
560 138 138 GLY N N 108.74 . 1
561 139 139 ASP H H 8.22 . 1
562 139 139 ASP C C 177.67 . 1
563 139 139 ASP CA C 53.83 . 1
564 139 139 ASP CB C 38.3 . 1
565 139 139 ASP N N 121.1 . 1
566 140 140 GLY H H 8.91 . 1
567 140 140 GLY C C 175.25 . 1
568 140 140 GLY CA C 45.6 . 1
569 140 140 GLY N N 112.13 . 1
570 143 143 LYS C C 176.26 . 1
571 143 143 LYS CA C 57.21 . 1
572 143 143 LYS CB C 30.17 . 1
573 144 144 ILE H H 7.3 . 1
574 144 144 ILE C C 175.05 . 1
575 144 144 ILE CA C 59.76 . 1
576 144 144 ILE CB C 38.07 . 1
577 144 144 ILE N N 120.32 . 1
578 145 145 LYS H H 8.76 . 1
579 145 145 LYS C C 175.19 . 1
580 145 145 LYS CA C 54.4 . 1
581 145 145 LYS CB C 34 . 1
582 145 145 LYS N N 127.65 . 1
583 146 146 GLY H H 8.08 . 1
584 146 146 GLY C C 172.61 . 1
585 146 146 GLY CA C 44.79 . 1
586 146 146 GLY N N 108.98 . 1
587 147 147 CYS H H 8.26 . 1
588 147 147 CYS C C 172.4 . 1
589 147 147 CYS CA C 55.72 . 1
590 147 147 CYS CB C 28.46 . 1
591 147 147 CYS N N 117.7 . 1
592 154 154 VAL C C 175.35 . 1
593 154 154 VAL CA C 60.57 . 1
594 154 154 VAL CB C 35.05 . 1
595 155 155 GLU H H 9.33 . 1
596 155 155 GLU C C 174.85 . 1
597 155 155 GLU CA C 54.83 . 1
598 155 155 GLU CB C 30.95 . 1
599 155 155 GLU N N 124.03 . 1
600 156 156 VAL H H 8.7 . 1
601 156 156 VAL C C 174.99 . 1
602 156 156 VAL CA C 60.56 . 1
603 156 156 VAL CB C 32.13 . 1
604 156 156 VAL N N 126.37 . 1
605 157 157 GLN H H 8.39 . 1
606 157 157 GLN C C 175.94 . 1
607 157 157 GLN CA C 53.65 . 1
608 157 157 GLN CB C 29.71 . 1
609 157 157 GLN N N 125.92 . 1
610 158 158 GLU H H 8.82 . 1
611 158 158 GLU C C 176.15 . 1
612 158 158 GLU CA C 56.29 . 1
613 158 158 GLU CB C 29.98 . 1
614 158 158 GLU N N 125.62 . 1
615 159 159 LYS H H 8.46 . 1
616 159 159 LYS C C 177.51 . 1
617 159 159 LYS CA C 54.86 . 1
618 159 159 LYS CB C 32.85 . 1
619 159 159 LYS N N 123.15 . 1
620 160 160 SER H H 7.81 . 1
621 160 160 SER C C 177.75 . 1
622 160 160 SER CA C 60.1 . 1
623 160 160 SER N N 122.08 . 1
624 161 161 SER C C 175.14 . 1
625 161 161 SER CA C 58.55 . 1
626 161 161 SER CB C 63.13 . 1
627 162 162 GLY H H 8.03 . 1
628 162 162 GLY C C 174.31 . 1
629 162 162 GLY CA C 45.09 . 1
630 162 162 GLY N N 109.19 . 1
631 163 163 ARG H H 8 . 1
632 163 163 ARG C C 176.36 . 1
633 163 163 ARG CA C 56.48 . 1
634 163 163 ARG CB C 29.96 . 1
635 163 163 ARG N N 118.18 . 1
636 164 164 THR H H 7.54 . 1
637 164 164 THR C C 172.63 . 1
638 164 164 THR CA C 59.99 . 1
639 164 164 THR CB C 71.17 . 1
640 164 164 THR N N 111.1 . 1
641 165 165 ALA H H 8.89 . 1
642 165 165 ALA C C 173.73 . 1
643 165 165 ALA CA C 50.51 . 1
644 165 165 ALA CB C 21.19 . 1
645 165 165 ALA N N 123.9 . 1
646 166 166 HIS H H 8.52 . 1
647 166 166 HIS C C 173 . 1
648 166 166 HIS CA C 54.64 . 1
649 166 166 HIS CB C 30.07 . 1
650 166 166 HIS N N 119.03 . 1
651 167 167 TYR H H 8.71 . 1
652 167 167 TYR C C 173.91 . 1
653 167 167 TYR CA C 56.49 . 1
654 167 167 TYR CB C 40.63 . 1
655 167 167 TYR N N 126.08 . 1
656 168 168 LYS H H 8.99 . 1
657 168 168 LYS C C 174.34 . 1
658 168 168 LYS CA C 55.01 . 1
659 168 168 LYS CB C 32.58 . 1
660 168 168 LYS N N 114.07 . 1
661 177 177 LEU C C 175.68 . 1
662 177 177 LEU CA C 54.19 . 1
663 177 177 LEU CB C 45.6 . 1
664 178 178 GLN H H 8.95 . 1
665 178 178 GLN C C 174.61 . 1
666 178 178 GLN CA C 54.37 . 1
667 178 178 GLN CB C 32.97 . 1
668 178 178 GLN N N 121.28 . 1
669 179 179 THR H H 8.7 . 1
670 179 179 THR C C 172.58 . 1
671 179 179 THR CA C 60.5 . 1
672 179 179 THR CB C 70 . 1
673 179 179 THR N N 116.24 . 1
674 180 180 ASN H H 8.42 . 1
675 180 180 ASN N N 123.8 . 1
676 183 183 GLY C C 175.1 . 1
677 184 184 SER H H 8.36 . 1
678 184 184 SER C C 174.36 . 1
679 184 184 SER CA C 57.34 . 1
680 184 184 SER CB C 64.65 . 1
681 184 184 SER N N 122.7 . 1
682 185 185 GLY H H 7.78 . 1
683 185 185 GLY C C 176.06 . 1
684 185 185 GLY CA C 45.74 . 1
685 185 185 GLY N N 109.1 . 1
686 186 186 THR H H 8.77 . 1
687 186 186 THR C C 174.94 . 1
688 186 186 THR CA C 62.04 . 1
689 186 186 THR CB C 69.7 . 1
690 186 186 THR N N 121.75 . 1
691 187 187 MET H H 8.91 . 1
692 187 187 MET C C 172.42 . 1
693 187 187 MET CA C 55.93 . 1
694 187 187 MET CB C 34.49 . 1
695 187 187 MET N N 127.98 . 1
696 188 188 ASN H H 8.89 . 1
697 188 188 ASN C C 173.13 . 1
698 188 188 ASN CA C 52.23 . 1
699 188 188 ASN CB C 41.07 . 1
700 188 188 ASN N N 125.86 . 1
701 189 189 LEU H H 9.05 . 1
702 189 189 LEU C C 175.87 . 1
703 189 189 LEU CA C 53.84 . 1
704 189 189 LEU CB C 46 . 1
705 189 189 LEU N N 128.22 . 1
706 190 190 GLY H H 9.47 . 1
707 190 190 GLY C C 171.1 . 1
708 190 190 GLY CA C 46.09 . 1
709 190 190 GLY N N 106.73 . 1
710 192 192 SER C C 175.18 . 1
711 192 192 SER CA C 56.17 . 1
712 192 192 SER CB C 61.8 . 1
713 193 193 LEU H H 8.66 . 1
714 193 193 LEU C C 174.83 . 1
715 193 193 LEU CA C 54.67 . 1
716 193 193 LEU CB C 46.05 . 1
717 193 193 LEU N N 125.33 . 1
718 194 194 THR H H 8.4 . 1
719 194 194 THR C C 174.88 . 1
720 194 194 THR CA C 60.58 . 1
721 194 194 THR CB C 71.71 . 1
722 194 194 THR N N 119.04 . 1
723 195 195 ARG H H 9.37 . 1
724 195 195 ARG C C 173.67 . 1
725 195 195 ARG CA C 53.49 . 1
726 195 195 ARG CB C 35.44 . 1
727 195 195 ARG N N 127.67 . 1
728 196 196 GLN H H 8.4 . 1
729 196 196 GLN C C 175.28 . 1
730 196 196 GLN CA C 54.04 . 1
731 196 196 GLN CB C 33.08 . 1
732 196 196 GLN N N 119.02 . 1
733 197 197 MET H H 9.05 . 1
734 197 197 MET C C 173.18 . 1
735 197 197 MET CA C 54.89 . 1
736 197 197 MET CB C 35.6 . 1
737 197 197 MET N N 121.32 . 1
738 198 198 GLU H H 8.33 . 1
739 198 198 GLU C C 174.94 . 1
740 198 198 GLU CA C 54.45 . 1
741 198 198 GLU CB C 33.19 . 1
742 198 198 GLU N N 119.36 . 1
743 199 199 LYS H H 8.57 . 1
744 199 199 LYS C C 173.98 . 1
745 199 199 LYS CA C 55.52 . 1
746 199 199 LYS CB C 36.05 . 1
747 199 199 LYS N N 119.56 . 1
748 200 200 ASP H H 8.47 . 1
749 200 200 ASP C C 175.84 . 1
750 200 200 ASP CA C 53.44 . 1
751 200 200 ASP CB C 42.27 . 1
752 200 200 ASP N N 124.03 . 1
753 201 201 GLU H H 8.88 . 1
754 201 201 GLU C C 175.31 . 1
755 201 201 GLU CA C 54.18 . 1
756 201 201 GLU CB C 33.75 . 1
757 201 201 GLU N N 120.52 . 1
758 202 202 THR H H 8.73 . 1
759 202 202 THR C C 173.5 . 1
760 202 202 THR CA C 63.32 . 1
761 202 202 THR CB C 69.62 . 1
762 202 202 THR N N 119.62 . 1
763 203 203 VAL H H 8.02 . 1
764 203 203 VAL C C 174.66 . 1
765 203 203 VAL CA C 60.63 . 1
766 203 203 VAL CB C 31.61 . 1
767 203 203 VAL N N 127.02 . 1
768 204 204 SER H H 7.75 . 1
769 204 204 SER C C 175.23 . 1
770 204 204 SER CA C 56.55 . 1
771 204 204 SER CB C 65.83 . 1
772 204 204 SER N N 121.31 . 1
773 209 209 HIS C C 176.28 . 1
774 209 209 HIS CA C 55.82 . 1
775 209 209 HIS CB C 28 . 1
776 210 210 ILE H H 8.12 . 1
777 210 210 ILE C C 176.42 . 1
778 210 210 ILE CA C 58.17 . 1
779 210 210 ILE CB C 38.41 . 1
780 210 210 ILE N N 123.39 . 1
781 211 211 ALA H H 8.17 . 1
782 211 211 ALA C C 177.38 . 1
783 211 211 ALA CA C 52.23 . 1
784 211 211 ALA CB C 18.54 . 1
785 211 211 ALA N N 124.79 . 1
786 212 212 ASN H H 8.03 . 1
787 212 212 ASN C C 176.04 . 1
788 212 212 ASN CA C 54.01 . 1
789 212 212 ASN CB C 40.46 . 1
790 212 212 ASN N N 119.86 . 1
791 218 218 GLU C C 178.77 . 1
792 218 218 GLU CA C 58.7 . 1
793 218 218 GLU CB C 28.8 . 1
794 219 219 ASP H H 8.37 . 1
795 219 219 ASP C C 173.65 . 1
796 219 219 ASP CA C 55.89 . 1
797 219 219 ASP CB C 39.5 . 1
798 219 219 ASP N N 121.3 . 1
799 220 220 MET H H 8.03 . 1
800 220 220 MET C C 176.95 . 1
801 220 220 MET CA C 61.62 . 1
802 220 220 MET CB C 33.59 . 1
803 220 220 MET N N 117.95 . 1
804 221 221 GLU H H 7.4 . 1
805 221 221 GLU C C 179.77 . 1
806 221 221 GLU CA C 59.05 . 1
807 221 221 GLU CB C 30.87 . 1
808 221 221 GLU N N 119.74 . 1
809 227 227 THR C C 176.6 . 1
810 227 227 THR CA C 66.7 . 1
811 228 228 LEU H H 9.28 . 1
812 228 228 LEU C C 178.12 . 1
813 228 228 LEU CA C 57.85 . 1
814 228 228 LEU CB C 40.78 . 1
815 228 228 LEU N N 122.48 . 1
816 229 229 ASN H H 7.84 . 1
817 229 229 ASN CA C 52.63 . 1
818 229 229 ASN N N 116.29 . 1
819 230 230 GLU C C 178.56 . 1
820 230 230 GLU CA C 60.35 . 1
821 230 230 GLU CB C 27.41 . 1
822 231 231 ILE H H 7.73 . 1
823 231 231 ILE C C 178.3 . 1
824 231 231 ILE CA C 63.95 . 1
825 231 231 ILE CB C 36.69 . 1
826 231 231 ILE N N 120.33 . 1
827 232 232 TYR H H 8.28 . 1
828 232 232 TYR C C 178.74 . 1
829 232 232 TYR CA C 58.33 . 1
830 232 232 TYR CB C 39.2 . 1
831 232 232 TYR N N 120.14 . 1
832 243 243 LEU C C 176.24 . 1
833 243 243 LEU CA C 56 . 1
834 243 243 LEU CB C 41.69 . 1
835 244 244 ARG H H 7.25 . 1
836 244 244 ARG C C 172.87 . 1
837 244 244 ARG CA C 54.5 . 1
838 244 244 ARG CB C 30.32 . 1
839 244 244 ARG N N 118.96 . 1
840 245 245 SER H H 8.69 . 1
841 245 245 SER C C 175.04 . 1
842 245 245 SER CA C 55.51 . 1
843 245 245 SER CB C 65.35 . 1
844 245 245 SER N N 119.83 . 1
845 246 246 VAL H H 8.59 . 1
846 246 246 VAL C C 176.79 . 1
847 246 246 VAL CA C 64.66 . 1
848 246 246 VAL CB C 31.12 . 1
849 246 246 VAL N N 128.98 . 1
850 247 247 GLN H H 7.57 . 1
851 247 247 GLN C C 176.16 . 1
852 247 247 GLN CA C 54.88 . 1
853 247 247 GLN CB C 28.32 . 1
854 247 247 GLN N N 118.61 . 1
855 248 248 THR H H 8.2 . 1
856 248 248 THR C C 175.44 . 1
857 248 248 THR CA C 60.47 . 1
858 248 248 THR CB C 69.09 . 1
859 248 248 THR N N 117.05 . 1
860 249 249 PHE H H 8.1 . 1
861 249 249 PHE C C 177.04 . 1
862 249 249 PHE CA C 58.94 . 1
863 249 249 PHE CB C 38.05 . 1
864 249 249 PHE N N 122.99 . 1
865 250 250 ALA H H 8.26 . 1
866 250 250 ALA C C 178.05 . 1
867 250 250 ALA CA C 52.76 . 1
868 250 250 ALA CB C 18.38 . 1
869 250 250 ALA N N 124.45 . 1
870 251 251 ASP H H 7.92 . 1
871 251 251 ASP C C 177.22 . 1
872 251 251 ASP CA C 54.5 . 1
873 251 251 ASP CB C 40.24 . 1
874 251 251 ASP N N 120.1 . 1
875 252 252 LYS H H 8.15 . 1
876 252 252 LYS C C 177.45 . 1
877 252 252 LYS CA C 56.96 . 1
878 252 252 LYS CB C 31.43 . 1
879 252 252 LYS N N 122.73 . 1
880 253 253 SER H H 8.13 . 1
881 253 253 SER C C 174.97 . 1
882 253 253 SER CA C 59.15 . 1
883 253 253 SER CB C 63.37 . 1
884 253 253 SER N N 116.24 . 1
885 254 254 LYS H H 7.78 . 1
886 254 254 LYS C C 177.66 . 1
887 254 254 LYS CA C 56.95 . 1
888 254 254 LYS CB C 31.91 . 1
889 254 254 LYS N N 123.19 . 1
890 255 255 GLN H H 8.13 . 1
891 255 255 GLN C C 176.67 . 1
892 255 255 GLN CA C 56.32 . 1
893 255 255 GLN CB C 27.97 . 1
894 255 255 GLN N N 121.46 . 1
895 256 256 GLU H H 8.11 . 1
896 256 256 GLU C C 177.21 . 1
897 256 256 GLU CA C 57.23 . 1
898 256 256 GLU CB C 29.01 . 1
899 256 256 GLU N N 121.06 . 1
900 257 257 ALA H H 7.91 . 1
901 257 257 ALA C C 178.59 . 1
902 257 257 ALA CA C 53.05 . 1
903 257 257 ALA CB C 73.88 . 1
904 257 257 ALA N N 123.69 . 1
905 258 258 LEU H H 7.82 . 1
906 258 258 LEU C C 178.21 . 1
907 258 258 LEU CA C 55.58 . 1
908 258 258 LEU CB C 41.05 . 1
909 258 258 LEU N N 120.26 . 1
910 259 259 LYS H H 7.87 . 1
911 259 259 LYS C C 177.15 . 1
912 259 259 LYS CA C 56.86 . 1
913 259 259 LYS CB C 31.64 . 1
914 259 259 LYS N N 121.22 . 1
915 260 260 ASN H H 8.17 . 1
916 260 260 ASN C C 175.69 . 1
917 260 260 ASN CA C 53.74 . 1
918 260 260 ASN CB C 38.27 . 1
919 260 260 ASN N N 119.53 . 1
920 261 261 ASP H H 8.22 . 1
921 261 261 ASP C C 177.19 . 1
922 261 261 ASP CA C 55.12 . 1
923 261 261 ASP CB C 40.33 . 1
924 261 261 ASP N N 121.41 . 1
925 262 262 LEU H H 7.94 . 1
926 262 262 LEU C C 178.39 . 1
927 262 262 LEU CA C 56.09 . 1
928 262 262 LEU CB C 40.87 . 1
929 262 262 LEU N N 122.61 . 1
930 263 263 VAL H H 7.76 . 1
931 263 263 VAL C C 177.87 . 1
932 263 263 VAL CA C 64.05 . 1
933 263 263 VAL CB C 31.23 . 1
934 263 263 VAL N N 120.39 . 1
935 264 264 GLU H H 8.12 . 1
936 264 264 GLU C C 178.04 . 1
937 264 264 GLU CA C 57.59 . 1
938 264 264 GLU CB C 28.75 . 1
939 264 264 GLU N N 122.18 . 1
940 265 265 ALA H H 8.01 . 1
941 265 265 ALA C C 179.53 . 1
942 265 265 ALA CA C 53.7 . 1
943 265 265 ALA CB C 73.78 . 1
944 265 265 ALA N N 123.2 . 1
945 266 266 LEU H H 7.82 . 1
946 266 266 LEU C C 178.58 . 1
947 266 266 LEU CA C 55.88 . 1
948 266 266 LEU CB C 40.92 . 1
949 266 266 LEU N N 119.62 . 1
950 267 267 LYS H H 7.78 . 1
951 267 267 LYS C C 177.6 . 1
952 267 267 LYS CA C 57.05 . 1
953 267 267 LYS CB C 31.75 . 1
954 267 267 LYS N N 120.63 . 1
955 268 268 ARG H H 7.82 . 1
956 268 268 ARG C C 176.8 . 1
957 268 268 ARG CA C 56.35 . 1
958 268 268 ARG CB C 29.62 . 1
959 268 268 ARG N N 120.2 . 1
960 269 269 LYS H H 7.93 . 1
961 269 269 LYS C C 176.69 . 1
962 269 269 LYS CA C 56.25 . 1
963 269 269 LYS CB C 31.59 . 1
964 269 269 LYS N N 121.82 . 1
965 270 270 GLN H H 7.97 . 1
966 270 270 GLN C C 177.71 . 1
967 270 270 GLN CA C 55.13 . 1
968 270 270 GLN N N 119.95 . 1
969 271 271 GLN H H 8.21 . 1
970 271 271 GLN C C 174.97 . 1
971 271 271 GLN CA C 55.49 . 1
972 271 271 GLN CB C 28.55 . 1
973 271 271 GLN N N 122.33 . 1
974 272 272 CYS H H 7.91 . 1
975 272 272 CYS C C 178.62 . 1
976 272 272 CYS CA C 58.86 . 1
977 272 272 CYS CB C 28 . 1
978 272 272 CYS N N 125.38 . 1
stop_
save_
save_chemical_shifts_3
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'2D 1H-15N HSQC'
stop_
loop_
_Sample_label
$CP_chemical_shift_perturpation
$CAH3a_b_chemical_shift_perturpation
stop_
_Sample_conditions_label $sample_conditions_1
_Chem_shift_reference_set_label $reference_1
_Mol_system_component_name CARMIL_CAH3a_b_domain
_Text_data_format .
_Text_data .
loop_
_Atom_shift_assign_ID
_Residue_author_seq_code
_Residue_seq_code
_Residue_label
_Atom_name
_Atom_type
_Chem_shift_value
_Chem_shift_value_error
_Chem_shift_ambiguity_code
1 4 4 GLY H H 8.19 . 1
2 4 4 GLY C C 173.4 . 1
3 4 4 GLY CA C 45.03 . 1
4 4 4 GLY N N 114.16 . 1
5 5 5 SER CA C 57.78 . 1
6 5 5 SER CB C 63.5 . 1
7 6 6 TRP H H 8.18 . 1
8 6 6 TRP C C 176.42 . 1
9 6 6 TRP CA C 55.68 . 1
10 6 6 TRP CB C 30.2 . 1
11 6 6 TRP N N 122.21 . 1
12 7 7 SER C C 174.26 . 1
13 7 7 SER CA C 58.04 . 1
14 8 8 VAL H H 7.79 . 1
15 8 8 VAL C C 176.13 . 1
16 8 8 VAL CA C 62.03 . 1
17 8 8 VAL CB C 31.47 . 1
18 8 8 VAL N N 121.33 . 1
19 9 9 ARG H H 8.1 . 1
20 9 9 ARG C C 176.21 . 1
21 9 9 ARG CA C 55.85 . 1
22 9 9 ARG CB C 29.55 . 1
23 9 9 ARG N N 123.87 . 1
24 10 10 GLN H H 8.18 . 1
25 10 10 GLN C C 175.91 . 1
26 10 10 GLN CA C 55.43 . 1
27 10 10 GLN CB C 30.05 . 1
28 10 10 GLN N N 121.7 . 1
29 11 11 GLU H H 8.29 . 1
30 11 11 GLU C C 176.37 . 1
31 11 11 GLU CA C 56.07 . 1
32 11 11 GLU CB C 29.4 . 1
33 11 11 GLU N N 122.66 . 1
34 12 12 LYS H H 8.25 . 1
35 12 12 LYS C C 176.49 . 1
36 12 12 LYS CA C 55.95 . 1
37 12 12 LYS CB C 31.91 . 1
38 12 12 LYS N N 122.65 . 1
39 13 13 ARG H H 8.21 . 1
40 13 13 ARG C C 176.04 . 1
41 13 13 ARG CA C 55.59 . 1
42 13 13 ARG CB C 29.39 . 1
43 13 13 ARG N N 122.58 . 1
44 15 15 SER C C 174.9 . 1
45 15 15 SER CA C 58.11 . 1
46 15 15 SER CB C 63.45 . 1
47 16 16 GLY H H 8.24 . 1
48 16 16 GLY C C 173.82 . 1
49 16 16 GLY CA C 44.8 . 1
50 16 16 GLY N N 110.56 . 1
51 17 17 LEU H H 7.91 . 1
52 17 17 LEU C C 177.4 . 1
53 17 17 LEU CA C 54.73 . 1
54 17 17 LEU CB C 41.39 . 1
55 17 17 LEU N N 121.73 . 1
56 18 18 ILE H H 8.04 . 1
57 18 18 ILE C C 176.18 . 1
58 18 18 ILE CA C 60.61 . 1
59 18 18 ILE CB C 37.62 . 1
60 18 18 ILE N N 121.96 . 1
61 19 19 SER H H 8.15 . 1
62 19 19 SER C C 174.17 . 1
63 19 19 SER CA C 57.88 . 1
64 19 19 SER CB C 63.81 . 1
65 19 19 SER N N 119.61 . 1
66 20 20 GLU H H 8.21 . 1
67 20 20 GLU C C 176.01 . 1
68 20 20 GLU CA C 55.7 . 1
69 20 20 GLU CB C 29.67 . 1
70 20 20 GLU N N 122.9 . 1
71 21 21 LEU H H 8.13 . 1
72 21 21 LEU C C 175.34 . 1
73 21 21 LEU CA C 52.59 . 1
74 21 21 LEU CB C 40.63 . 1
75 21 21 LEU N N 124.46 . 1
76 22 22 PRO C C 177.14 . 1
77 22 22 PRO CA C 62.78 . 1
78 22 22 PRO CB C 31.1 . 1
79 23 23 SER H H 8.22 . 1
80 23 23 SER C C 174.96 . 1
81 23 23 SER CA C 58 . 1
82 23 23 SER CB C 64.18 . 1
83 23 23 SER N N 115.97 . 1
84 24 24 GLU H H 8.41 . 1
85 24 24 GLU C C 176.97 . 1
86 24 24 GLU CA C 56.55 . 1
87 24 24 GLU CB C 29.27 . 1
88 24 24 GLU N N 122.94 . 1
89 25 25 GLU H H 8.28 . 1
90 25 25 GLU C C 177.47 . 1
91 25 25 GLU CA C 57.06 . 1
92 25 25 GLU CB C 29.12 . 1
93 25 25 GLU N N 121.52 . 1
94 26 26 GLY H H 8.28 . 1
95 26 26 GLY C C 174.63 . 1
96 26 26 GLY CA C 45.26 . 1
97 26 26 GLY N N 109.2 . 1
98 27 27 ARG H H 7.87 . 1
99 27 27 ARG C C 176.63 . 1
100 27 27 ARG CA C 56.03 . 1
101 27 27 ARG CB C 29.55 . 1
102 27 27 ARG N N 120.45 . 1
103 28 28 ARG H H 8.11 . 1
104 28 28 ARG C C 176.56 . 1
105 28 28 ARG CA C 56.07 . 1
106 28 28 ARG CB C 29.47 . 1
107 28 28 ARG N N 121.77 . 1
108 29 29 LEU H H 8.07 . 1
109 29 29 LEU C C 177.63 . 1
110 29 29 LEU CA C 55.09 . 1
111 29 29 LEU CB C 41.04 . 1
112 29 29 LEU N N 122.7 . 1
113 30 30 GLU H H 8.17 . 1
114 30 30 GLU C C 175.62 . 1
115 30 30 GLU CA C 55.11 . 1
116 30 30 GLU CB C 29.05 . 1
117 30 30 GLU N N 120.99 . 1
118 31 31 HIS H H 8.31 . 1
119 31 31 HIS C C 174.14 . 1
120 31 31 HIS CA C 53.03 . 1
121 31 31 HIS CB C 29.78 . 1
122 31 31 HIS N N 123.18 . 1
123 32 32 PHE H H 7.94 . 1
124 32 32 PHE C C 176.11 . 1
125 32 32 PHE CA C 57.87 . 1
126 32 32 PHE CB C 38.87 . 1
127 32 32 PHE N N 120.53 . 1
128 33 33 THR H H 7.92 . 1
129 33 33 THR C C 176.82 . 1
130 33 33 THR CA C 62.57 . 1
131 33 33 THR CB C 69.25 . 1
132 33 33 THR N N 115.58 . 1
133 34 34 LYS H H 8.28 . 1
134 34 34 LYS C C 176.34 . 1
135 34 34 LYS CA C 56.06 . 1
136 34 34 LYS CB C 32.07 . 1
137 34 34 LYS N N 121.92 . 1
138 35 35 LEU H H 7.91 . 1
139 35 35 LEU C C 176.92 . 1
140 35 35 LEU CA C 54.52 . 1
141 35 35 LEU CB C 41.37 . 1
142 35 35 LEU N N 122.45 . 1
143 36 36 ARG H H 8.09 . 1
144 36 36 ARG C C 174.01 . 1
145 36 36 ARG CA C 53.35 . 1
146 36 36 ARG CB C 29.18 . 1
147 36 36 ARG N N 123.14 . 1
148 37 37 PRO C C 176.82 . 1
149 37 37 PRO CA C 62.57 . 1
150 37 37 PRO CB C 31.51 . 1
151 38 38 LYS H H 8.28 . 1
152 38 38 LYS C C 176.65 . 1
153 38 38 LYS CA C 55.87 . 1
154 38 38 LYS CB C 31.83 . 1
155 38 38 LYS N N 121.91 . 1
156 39 39 ARG H H 8.22 . 1
157 39 39 ARG C C 175.05 . 1
158 39 39 ARG CA C 55.98 . 1
159 39 39 ARG CB C 28.85 . 1
160 39 39 ARG N N 122.37 . 1
161 40 40 ASN H H 7.87 . 1
162 40 40 ASN C C 175.54 . 1
163 40 40 ASN CA C 52.47 . 1
164 40 40 ASN CB C 42 . 1
165 40 40 ASN N N 122.03 . 1
166 42 42 LYS C C 176.37 . 1
167 42 42 LYS CA C 55.93 . 1
168 42 42 LYS CB C 32.1 . 1
169 43 43 GLN H H 8.23 . 1
170 43 43 GLN C C 175.74 . 1
171 43 43 GLN CA C 55.24 . 1
172 43 43 GLN CB C 28.94 . 1
173 43 43 GLN N N 122.03 . 1
174 44 44 GLN H H 8.3 . 1
175 44 44 GLN C C 174.14 . 1
176 44 44 GLN CA C 53.03 . 1
177 44 44 GLN CB C 28.11 . 1
178 44 44 GLN N N 123.1 . 1
179 45 45 PRO C C 177.02 . 1
180 45 45 PRO CA C 62.83 . 1
181 45 45 PRO CB C 31.27 . 1
182 46 46 THR H H 8.09 . 1
183 46 46 THR C C 174.46 . 1
184 46 46 THR CA C 61.39 . 1
185 46 46 THR CB C 69.28 . 1
186 46 46 THR N N 114.56 . 1
187 47 47 GLN H H 8.22 . 1
188 47 47 GLN C C 175.29 . 1
189 47 47 GLN CA C 54.97 . 1
190 47 47 GLN CB C 28.8 . 1
191 47 47 GLN N N 122.65 . 1
192 48 48 ALA H H 8.17 . 1
193 48 48 ALA C C 177.28 . 1
194 48 48 ALA CA C 51.91 . 1
195 48 48 ALA CB C 18.71 . 1
196 48 48 ALA N N 125.64 . 1
197 49 49 ALA H H 8.11 . 1
198 49 49 ALA C C 177.61 . 1
199 49 49 ALA CA C 51.85 . 1
200 49 49 ALA CB C 18.61 . 1
201 49 49 ALA N N 123.46 . 1
202 50 50 VAL H H 7.95 . 1
203 50 50 VAL C C 176.04 . 1
204 50 50 VAL CA C 61.71 . 1
205 50 50 VAL CB C 31.95 . 1
206 50 50 VAL N N 119.24 . 1
207 51 51 CYS H H 7.83 . 1
208 51 51 CYS C C 178.49 . 1
209 51 51 CYS CA C 58.98 . 1
210 51 51 CYS CB C 28.21 . 1
211 51 51 CYS N N 126.57 . 1
212 52 52 THR H H 8.17 . 1
213 52 52 THR C C 174.31 . 1
214 52 52 THR CA C 61.68 . 1
215 52 52 THR CB C 69.11 . 1
216 52 52 THR N N 117.8 . 1
217 53 53 ILE H H 7.99 . 1
218 53 53 ILE C C 175.91 . 1
219 53 53 ILE CA C 60.55 . 1
220 53 53 ILE CB C 38.03 . 1
221 53 53 ILE N N 123.15 . 1
222 54 54 SER H H 8.23 . 1
223 54 54 SER C C 174 . 1
224 54 54 SER CA C 57.66 . 1
225 54 54 SER CB C 63.35 . 1
226 54 54 SER N N 120.12 . 1
227 55 55 ILE H H 8 . 1
228 55 55 ILE C C 175.81 . 1
229 55 55 ILE CA C 60.41 . 1
230 55 55 ILE CB C 37.87 . 1
231 55 55 ILE N N 122.91 . 1
232 56 56 LEU H H 8.17 . 1
233 56 56 LEU C C 175.21 . 1
234 56 56 LEU CA C 52.34 . 1
235 56 56 LEU CB C 40.56 . 1
236 56 56 LEU N N 127.46 . 1
237 57 57 PRO C C 177.14 . 1
238 57 57 PRO CA C 62.75 . 1
239 57 57 PRO CB C 31.17 . 1
240 58 58 GLN H H 8.39 . 1
241 58 58 GLN C C 175.8 . 1
242 58 58 GLN CA C 55.27 . 1
243 58 58 GLN CB C 28.81 . 1
244 58 58 GLN N N 120.41 . 1
245 59 59 ASP H H 8.21 . 1
246 59 59 ASP C C 176.69 . 1
247 59 59 ASP CA C 54.17 . 1
248 59 59 ASP CB C 40.72 . 1
249 59 59 ASP N N 121.37 . 1
250 60 60 GLY H H 8.17 . 1
251 60 60 GLY C C 174.35 . 1
252 60 60 GLY CA C 44.98 . 1
253 60 60 GLY N N 109.18 . 1
254 61 61 GLU H H 8.15 . 1
255 61 61 GLU C C 176.85 . 1
256 61 61 GLU CA C 56.29 . 1
257 61 61 GLU CB C 29.36 . 1
258 61 61 GLU N N 120.69 . 1
259 62 62 GLN H H 8.35 . 1
260 62 62 GLN C C 175.91 . 1
261 62 62 GLN CA C 55.49 . 1
262 62 62 GLN CB C 28.4 . 1
263 62 62 GLN N N 120.81 . 1
264 63 63 ASN H H 8.3 . 1
265 63 63 ASN C C 175.74 . 1
266 63 63 ASN CA C 53.09 . 1
267 63 63 ASN CB C 38.5 . 1
268 63 63 ASN N N 119.5 . 1
269 64 64 GLY H H 8.25 . 1
270 64 64 GLY C C 174.25 . 1
271 64 64 GLY CA C 45.11 . 1
272 64 64 GLY N N 109.18 . 1
273 65 65 LEU H H 7.96 . 1
274 65 65 LEU C C 177.61 . 1
275 65 65 LEU CA C 54.91 . 1
276 65 65 LEU CB C 41 . 1
277 65 65 LEU N N 121.48 . 1
278 66 66 MET H H 8.18 . 1
279 66 66 MET C C 176.67 . 1
280 66 66 MET CA C 55.17 . 1
281 66 66 MET CB C 31.96 . 1
282 66 66 MET N N 120.15 . 1
283 67 67 GLY H H 8.19 . 1
284 67 67 GLY C C 173.72 . 1
285 67 67 GLY CA C 44.77 . 1
286 67 67 GLY N N 109.74 . 1
287 68 68 ARG H H 7.99 . 1
288 68 68 ARG C C 176.38 . 1
289 68 68 ARG CA C 55.44 . 1
290 68 68 ARG CB C 30.21 . 1
291 68 68 ARG N N 120.9 . 1
292 69 69 VAL H H 8.16 . 1
293 69 69 VAL C C 175.72 . 1
294 69 69 VAL CA C 61.71 . 1
295 69 69 VAL CB C 32.09 . 1
296 69 69 VAL N N 121.61 . 1
297 70 70 ASP H H 8.26 . 1
298 70 70 ASP C C 175.98 . 1
299 70 70 ASP CA C 53.76 . 1
300 70 70 ASP CB C 40.62 . 1
301 70 70 ASP N N 123.56 . 1
302 71 71 GLU H H 8.23 . 1
303 71 71 GLU C C 176.97 . 1
304 71 71 GLU CA C 56.34 . 1
305 71 71 GLU CB C 29.51 . 1
306 71 71 GLU N N 121.58 . 1
307 72 72 GLY H H 8.36 . 1
308 72 72 GLY C C 174.14 . 1
309 72 72 GLY CA C 44.97 . 1
310 72 72 GLY N N 109.83 . 1
311 73 73 VAL H H 7.74 . 1
312 73 73 VAL C C 175.81 . 1
313 73 73 VAL CA C 61.56 . 1
314 73 73 VAL CB C 32.16 . 1
315 73 73 VAL N N 118.61 . 1
316 74 74 ASP H H 8.22 . 1
317 74 74 ASP C C 176.38 . 1
318 74 74 ASP CA C 53.99 . 1
319 74 74 ASP CB C 40.82 . 1
320 74 74 ASP N N 123.63 . 1
321 75 75 GLU H H 8.23 . 1
322 75 75 GLU C C 176.22 . 1
323 75 75 GLU CA C 56.55 . 1
324 75 75 GLU CB C 29.25 . 1
325 75 75 GLU N N 121.53 . 1
326 76 76 PHE H H 8.1 . 1
327 76 76 PHE C C 175.72 . 1
328 76 76 PHE CA C 57.74 . 1
329 76 76 PHE CB C 38.76 . 1
330 76 76 PHE N N 120 . 1
331 77 77 PHE H H 7.87 . 1
332 77 77 PHE C C 175.7 . 1
333 77 77 PHE CA C 57.71 . 1
334 77 77 PHE CB C 38.92 . 1
335 77 77 PHE N N 120.3 . 1
336 78 78 THR H H 7.83 . 1
337 78 78 THR C C 173.9 . 1
338 78 78 THR CA C 61.47 . 1
339 78 78 THR CB C 69.19 . 1
340 78 78 THR N N 115.79 . 1
341 79 79 LYS H H 8 . 1
342 79 79 LYS C C 176.01 . 1
343 79 79 LYS CA C 55.68 . 1
344 79 79 LYS CB C 32.22 . 1
345 79 79 LYS N N 124.21 . 1
346 80 80 LYS H H 8.22 . 1
347 80 80 LYS C C 175.6 . 1
348 80 80 LYS CA C 55.93 . 1
349 80 80 LYS CB C 32.14 . 1
350 80 80 LYS N N 124.48 . 1
351 81 81 VAL H H 7.6 . 1
352 81 81 VAL C C 170.95 . 1
353 81 81 VAL CA C 63.09 . 1
354 81 81 VAL CB C 32.16 . 1
355 81 81 VAL N N 126.03 . 1
stop_
save_