data_9AV8
# 
_entry.id   9AV8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9AV8         pdb_00009av8 10.2210/pdb9av8/pdb 
WWPDB D_1000282056 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-27 
2 'Structure model' 1 1 2025-01-15 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9AV8 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9AV4 unspecified 
PDB . 9AV5 unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              shenping.liu@pfizer.com 
_pdbx_contact_author.name_first         Shenping 
_pdbx_contact_author.name_last          Liu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9400-3007 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Liu, S.'     1 0000-0001-9400-3007 
'Garnsey, M.' 2 0000-0003-1226-1868 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                297 
_citation.page_last                 297 
_citation.title                     
'Design and application of synthetic 17B-HSD13 substrates reveals preserved catalytic activity of protective human variants.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-54487-5 
_citation.pdbx_database_id_PubMed   39746932 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Garnsey, M.R.'         1  0000-0003-1226-1868 
primary 'Wang, Y.'              2  0000-0002-7584-6188 
primary 'Edmonds, D.J.'         3  0000-0001-9234-8618 
primary 'Sammons, M.F.'         4  0000-0001-6472-0646 
primary 'Reidich, B.'           5  ?                   
primary 'Ahn, Y.'               6  0000-0001-5988-7388 
primary 'Ashkenazi, Y.'         7  ?                   
primary 'Carlo, A.'             8  ?                   
primary 'Cerny, M.A.'           9  0000-0002-5976-3809 
primary 'Coffman, K.J.'         10 ?                   
primary 'Culver, J.A.'          11 ?                   
primary 'Dechert Schmitt, A.M.' 12 ?                   
primary 'Eng, H.'               13 0000-0002-2914-3967 
primary 'Fisher, E.L.'          14 0000-0002-8700-5108 
primary 'Gutierrez, J.A.'       15 0000-0002-5882-0955 
primary 'James, L.'             16 ?                   
primary 'Jordan, S.'            17 0009-0000-1537-0205 
primary 'Kohrt, J.T.'           18 0000-0001-5517-8357 
primary 'Kramer, M.'            19 ?                   
primary 'LaChapelle, E.A.'      20 ?                   
primary 'Lee, J.C.'             21 ?                   
primary 'Lee, J.'               22 0000-0003-1750-0063 
primary 'Li, D.'                23 ?                   
primary 'Li, Z.'                24 ?                   
primary 'Liu, S.'               25 0000-0001-9400-3007 
primary 'Liu, J.'               26 0000-0003-4000-9846 
primary 'Magee, T.V.'           27 ?                   
primary 'Miller, M.R.'          28 ?                   
primary 'Moran, M.'             29 0000-0003-1712-9444 
primary 'Nason, D.M.'           30 0009-0007-3042-7469 
primary 'Nedoma, N.L.'          31 0009-0000-3809-9120 
primary 
;O'Neil, S.V.
;
32 ?                   
primary 'Piotrowski, M.A.'      33 ?                   
primary 'Racich, J.'            34 ?                   
primary 'Sommese, R.F.'         35 0009-0005-1134-5711 
primary 'Stevens, L.M.'         36 ?                   
primary 'Wright, A.S.'          37 ?                   
primary 'Xiao, J.'              38 0009-0007-8649-8805 
primary 'Zhang, L.'             39 ?                   
primary 'Zhou, D.'              40 ?                   
primary 'Barrandon, O.'         41 ?                   
primary 'Clasquin, M.F.'        42 0000-0002-5361-6859 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hydroxysteroid 17-beta dehydrogenase 13'                                                        35229.992 2   ? 
? ? 'Dog HSD17B13 with 9 residues mutated to human ones' 
2 non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                                                663.425   2   ? 
? ? ?                                                    
3 non-polymer syn '7-[3-chloro-4-(cyclobutylmethoxy)benzene-1-sulfonamido]-2-methyl-2H-indazole-4-carboxylic acid' 449.908   1   ? 
? ? ?                                                    
4 water       nat water                                                                                            18.015    138 ? 
? ? ?                                                    
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGNIILDLLLLLLTIIYSYLEALVKVFFPRKRKSVAGEIVLITGAGHGIGRWTAYEFAKQKSRLVLWDINKHGVEETAAE
CRKLGATVHTFVVDCGNREDIYNSVKQVKKEVGDVTILVNNAGTVYPADLLSTKDEEITKTFEINILGHFWITKALLPSM
IKRNHGHIVTVASVCGHEGIPYLIPYCSSKFAAVGFHRGLTSELQALGITGIKTSCLCPVFVNTGFTKNPSTRLWPVLET
DTVARSLIDGILTNKKMIFVPSYINIFLILDKFLPERALAAINHLQNIQFEAVVGHKTRMKGSGHHHHHHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGNIILDLLLLLLTIIYSYLEALVKVFFPRKRKSVAGEIVLITGAGHGIGRWTAYEFAKQKSRLVLWDINKHGVEETAAE
CRKLGATVHTFVVDCGNREDIYNSVKQVKKEVGDVTILVNNAGTVYPADLLSTKDEEITKTFEINILGHFWITKALLPSM
IKRNHGHIVTVASVCGHEGIPYLIPYCSSKFAAVGFHRGLTSELQALGITGIKTSCLCPVFVNTGFTKNPSTRLWPVLET
DTVARSLIDGILTNKKMIFVPSYINIFLILDKFLPERALAAINHLQNIQFEAVVGHKTRMKGSGHHHHHHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                                                NAD   
3 '7-[3-chloro-4-(cyclobutylmethoxy)benzene-1-sulfonamido]-2-methyl-2H-indazole-4-carboxylic acid' A1AG6 
4 water                                                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   ASN n 
1 4   ILE n 
1 5   ILE n 
1 6   LEU n 
1 7   ASP n 
1 8   LEU n 
1 9   LEU n 
1 10  LEU n 
1 11  LEU n 
1 12  LEU n 
1 13  LEU n 
1 14  THR n 
1 15  ILE n 
1 16  ILE n 
1 17  TYR n 
1 18  SER n 
1 19  TYR n 
1 20  LEU n 
1 21  GLU n 
1 22  ALA n 
1 23  LEU n 
1 24  VAL n 
1 25  LYS n 
1 26  VAL n 
1 27  PHE n 
1 28  PHE n 
1 29  PRO n 
1 30  ARG n 
1 31  LYS n 
1 32  ARG n 
1 33  LYS n 
1 34  SER n 
1 35  VAL n 
1 36  ALA n 
1 37  GLY n 
1 38  GLU n 
1 39  ILE n 
1 40  VAL n 
1 41  LEU n 
1 42  ILE n 
1 43  THR n 
1 44  GLY n 
1 45  ALA n 
1 46  GLY n 
1 47  HIS n 
1 48  GLY n 
1 49  ILE n 
1 50  GLY n 
1 51  ARG n 
1 52  TRP n 
1 53  THR n 
1 54  ALA n 
1 55  TYR n 
1 56  GLU n 
1 57  PHE n 
1 58  ALA n 
1 59  LYS n 
1 60  GLN n 
1 61  LYS n 
1 62  SER n 
1 63  ARG n 
1 64  LEU n 
1 65  VAL n 
1 66  LEU n 
1 67  TRP n 
1 68  ASP n 
1 69  ILE n 
1 70  ASN n 
1 71  LYS n 
1 72  HIS n 
1 73  GLY n 
1 74  VAL n 
1 75  GLU n 
1 76  GLU n 
1 77  THR n 
1 78  ALA n 
1 79  ALA n 
1 80  GLU n 
1 81  CYS n 
1 82  ARG n 
1 83  LYS n 
1 84  LEU n 
1 85  GLY n 
1 86  ALA n 
1 87  THR n 
1 88  VAL n 
1 89  HIS n 
1 90  THR n 
1 91  PHE n 
1 92  VAL n 
1 93  VAL n 
1 94  ASP n 
1 95  CYS n 
1 96  GLY n 
1 97  ASN n 
1 98  ARG n 
1 99  GLU n 
1 100 ASP n 
1 101 ILE n 
1 102 TYR n 
1 103 ASN n 
1 104 SER n 
1 105 VAL n 
1 106 LYS n 
1 107 GLN n 
1 108 VAL n 
1 109 LYS n 
1 110 LYS n 
1 111 GLU n 
1 112 VAL n 
1 113 GLY n 
1 114 ASP n 
1 115 VAL n 
1 116 THR n 
1 117 ILE n 
1 118 LEU n 
1 119 VAL n 
1 120 ASN n 
1 121 ASN n 
1 122 ALA n 
1 123 GLY n 
1 124 THR n 
1 125 VAL n 
1 126 TYR n 
1 127 PRO n 
1 128 ALA n 
1 129 ASP n 
1 130 LEU n 
1 131 LEU n 
1 132 SER n 
1 133 THR n 
1 134 LYS n 
1 135 ASP n 
1 136 GLU n 
1 137 GLU n 
1 138 ILE n 
1 139 THR n 
1 140 LYS n 
1 141 THR n 
1 142 PHE n 
1 143 GLU n 
1 144 ILE n 
1 145 ASN n 
1 146 ILE n 
1 147 LEU n 
1 148 GLY n 
1 149 HIS n 
1 150 PHE n 
1 151 TRP n 
1 152 ILE n 
1 153 THR n 
1 154 LYS n 
1 155 ALA n 
1 156 LEU n 
1 157 LEU n 
1 158 PRO n 
1 159 SER n 
1 160 MET n 
1 161 ILE n 
1 162 LYS n 
1 163 ARG n 
1 164 ASN n 
1 165 HIS n 
1 166 GLY n 
1 167 HIS n 
1 168 ILE n 
1 169 VAL n 
1 170 THR n 
1 171 VAL n 
1 172 ALA n 
1 173 SER n 
1 174 VAL n 
1 175 CYS n 
1 176 GLY n 
1 177 HIS n 
1 178 GLU n 
1 179 GLY n 
1 180 ILE n 
1 181 PRO n 
1 182 TYR n 
1 183 LEU n 
1 184 ILE n 
1 185 PRO n 
1 186 TYR n 
1 187 CYS n 
1 188 SER n 
1 189 SER n 
1 190 LYS n 
1 191 PHE n 
1 192 ALA n 
1 193 ALA n 
1 194 VAL n 
1 195 GLY n 
1 196 PHE n 
1 197 HIS n 
1 198 ARG n 
1 199 GLY n 
1 200 LEU n 
1 201 THR n 
1 202 SER n 
1 203 GLU n 
1 204 LEU n 
1 205 GLN n 
1 206 ALA n 
1 207 LEU n 
1 208 GLY n 
1 209 ILE n 
1 210 THR n 
1 211 GLY n 
1 212 ILE n 
1 213 LYS n 
1 214 THR n 
1 215 SER n 
1 216 CYS n 
1 217 LEU n 
1 218 CYS n 
1 219 PRO n 
1 220 VAL n 
1 221 PHE n 
1 222 VAL n 
1 223 ASN n 
1 224 THR n 
1 225 GLY n 
1 226 PHE n 
1 227 THR n 
1 228 LYS n 
1 229 ASN n 
1 230 PRO n 
1 231 SER n 
1 232 THR n 
1 233 ARG n 
1 234 LEU n 
1 235 TRP n 
1 236 PRO n 
1 237 VAL n 
1 238 LEU n 
1 239 GLU n 
1 240 THR n 
1 241 ASP n 
1 242 THR n 
1 243 VAL n 
1 244 ALA n 
1 245 ARG n 
1 246 SER n 
1 247 LEU n 
1 248 ILE n 
1 249 ASP n 
1 250 GLY n 
1 251 ILE n 
1 252 LEU n 
1 253 THR n 
1 254 ASN n 
1 255 LYS n 
1 256 LYS n 
1 257 MET n 
1 258 ILE n 
1 259 PHE n 
1 260 VAL n 
1 261 PRO n 
1 262 SER n 
1 263 TYR n 
1 264 ILE n 
1 265 ASN n 
1 266 ILE n 
1 267 PHE n 
1 268 LEU n 
1 269 ILE n 
1 270 LEU n 
1 271 ASP n 
1 272 LYS n 
1 273 PHE n 
1 274 LEU n 
1 275 PRO n 
1 276 GLU n 
1 277 ARG n 
1 278 ALA n 
1 279 LEU n 
1 280 ALA n 
1 281 ALA n 
1 282 ILE n 
1 283 ASN n 
1 284 HIS n 
1 285 LEU n 
1 286 GLN n 
1 287 ASN n 
1 288 ILE n 
1 289 GLN n 
1 290 PHE n 
1 291 GLU n 
1 292 ALA n 
1 293 VAL n 
1 294 VAL n 
1 295 GLY n 
1 296 HIS n 
1 297 LYS n 
1 298 THR n 
1 299 ARG n 
1 300 MET n 
1 301 LYS n 
1 302 GLY n 
1 303 SER n 
1 304 GLY n 
1 305 HIS n 
1 306 HIS n 
1 307 HIS n 
1 308 HIS n 
1 309 HIS n 
1 310 HIS n 
1 311 HIS n 
1 312 HIS n 
1 313 HIS n 
1 314 HIS n 
1 315 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   315 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HSD17B13, HSD17B11' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Insect BA phytoplasma' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     1286942 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1AG6 non-polymer         . '7-[3-chloro-4-(cyclobutylmethoxy)benzene-1-sulfonamido]-2-methyl-2H-indazole-4-carboxylic acid' ? 
'C20 H20 Cl N3 O5 S' 449.908 
ALA   'L-peptide linking' y ALANINE                                                                                          ? 
'C3 H7 N O2'         89.093  
ARG   'L-peptide linking' y ARGININE                                                                                         ? 
'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                       ? 
'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                  ? 
'C4 H7 N O4'         133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                         ? 
'C3 H7 N O2 S'       121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                        ? 
'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                  ? 
'C5 H9 N O4'         147.129 
GLY   'peptide linking'   y GLYCINE                                                                                          ? 
'C2 H5 N O2'         75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                        ? 
'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer         . WATER                                                                                            ? 
'H2 O'               18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                       ? 
'C6 H13 N O2'        131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                          ? 
'C6 H13 N O2'        131.173 
LYS   'L-peptide linking' y LYSINE                                                                                           ? 
'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking' y METHIONINE                                                                                       ? 
'C5 H11 N O2 S'      149.211 
NAD   non-polymer         . NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                                                ? 
'C21 H27 N7 O14 P2'  663.425 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                    ? 
'C9 H11 N O2'        165.189 
PRO   'L-peptide linking' y PROLINE                                                                                          ? 
'C5 H9 N O2'         115.130 
SER   'L-peptide linking' y SERINE                                                                                           ? 
'C3 H7 N O3'         105.093 
THR   'L-peptide linking' y THREONINE                                                                                        ? 
'C4 H9 N O3'         119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                       ? 
'C11 H12 N2 O2'      204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                         ? 
'C9 H11 N O3'        181.189 
VAL   'L-peptide linking' y VALINE                                                                                           ? 
'C5 H11 N O2'        117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   GLY 2   1   1   GLY GLY A . n 
A 1 3   ASN 3   2   2   ASN ASN A . n 
A 1 4   ILE 4   3   3   ILE ILE A . n 
A 1 5   ILE 5   4   4   ILE ILE A . n 
A 1 6   LEU 6   5   5   LEU LEU A . n 
A 1 7   ASP 7   6   6   ASP ASP A . n 
A 1 8   LEU 8   7   7   LEU LEU A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  LEU 10  9   9   LEU LEU A . n 
A 1 11  LEU 11  10  10  LEU LEU A . n 
A 1 12  LEU 12  11  11  LEU LEU A . n 
A 1 13  LEU 13  12  12  LEU LEU A . n 
A 1 14  THR 14  13  13  THR THR A . n 
A 1 15  ILE 15  14  14  ILE ILE A . n 
A 1 16  ILE 16  15  15  ILE ILE A . n 
A 1 17  TYR 17  16  16  TYR TYR A . n 
A 1 18  SER 18  17  17  SER SER A . n 
A 1 19  TYR 19  18  18  TYR TYR A . n 
A 1 20  LEU 20  19  19  LEU LEU A . n 
A 1 21  GLU 21  20  20  GLU GLU A . n 
A 1 22  ALA 22  21  21  ALA ALA A . n 
A 1 23  LEU 23  22  22  LEU LEU A . n 
A 1 24  VAL 24  23  23  VAL VAL A . n 
A 1 25  LYS 25  24  24  LYS LYS A . n 
A 1 26  VAL 26  25  25  VAL VAL A . n 
A 1 27  PHE 27  26  26  PHE PHE A . n 
A 1 28  PHE 28  27  27  PHE PHE A . n 
A 1 29  PRO 29  28  28  PRO PRO A . n 
A 1 30  ARG 30  29  29  ARG ARG A . n 
A 1 31  LYS 31  30  30  LYS LYS A . n 
A 1 32  ARG 32  31  31  ARG ARG A . n 
A 1 33  LYS 33  32  32  LYS LYS A . n 
A 1 34  SER 34  33  33  SER SER A . n 
A 1 35  VAL 35  34  34  VAL VAL A . n 
A 1 36  ALA 36  35  35  ALA ALA A . n 
A 1 37  GLY 37  36  36  GLY GLY A . n 
A 1 38  GLU 38  37  37  GLU GLU A . n 
A 1 39  ILE 39  38  38  ILE ILE A . n 
A 1 40  VAL 40  39  39  VAL VAL A . n 
A 1 41  LEU 41  40  40  LEU LEU A . n 
A 1 42  ILE 42  41  41  ILE ILE A . n 
A 1 43  THR 43  42  42  THR THR A . n 
A 1 44  GLY 44  43  43  GLY GLY A . n 
A 1 45  ALA 45  44  44  ALA ALA A . n 
A 1 46  GLY 46  45  45  GLY GLY A . n 
A 1 47  HIS 47  46  46  HIS HIS A . n 
A 1 48  GLY 48  47  47  GLY GLY A . n 
A 1 49  ILE 49  48  48  ILE ILE A . n 
A 1 50  GLY 50  49  49  GLY GLY A . n 
A 1 51  ARG 51  50  50  ARG ARG A . n 
A 1 52  TRP 52  51  51  TRP TRP A . n 
A 1 53  THR 53  52  52  THR THR A . n 
A 1 54  ALA 54  53  53  ALA ALA A . n 
A 1 55  TYR 55  54  54  TYR TYR A . n 
A 1 56  GLU 56  55  55  GLU GLU A . n 
A 1 57  PHE 57  56  56  PHE PHE A . n 
A 1 58  ALA 58  57  57  ALA ALA A . n 
A 1 59  LYS 59  58  58  LYS LYS A . n 
A 1 60  GLN 60  59  59  GLN GLN A . n 
A 1 61  LYS 61  60  60  LYS LYS A . n 
A 1 62  SER 62  61  61  SER SER A . n 
A 1 63  ARG 63  62  62  ARG ARG A . n 
A 1 64  LEU 64  63  63  LEU LEU A . n 
A 1 65  VAL 65  64  64  VAL VAL A . n 
A 1 66  LEU 66  65  65  LEU LEU A . n 
A 1 67  TRP 67  66  66  TRP TRP A . n 
A 1 68  ASP 68  67  67  ASP ASP A . n 
A 1 69  ILE 69  68  68  ILE ILE A . n 
A 1 70  ASN 70  69  69  ASN ASN A . n 
A 1 71  LYS 71  70  70  LYS LYS A . n 
A 1 72  HIS 72  71  71  HIS HIS A . n 
A 1 73  GLY 73  72  72  GLY GLY A . n 
A 1 74  VAL 74  73  73  VAL VAL A . n 
A 1 75  GLU 75  74  74  GLU GLU A . n 
A 1 76  GLU 76  75  75  GLU GLU A . n 
A 1 77  THR 77  76  76  THR THR A . n 
A 1 78  ALA 78  77  77  ALA ALA A . n 
A 1 79  ALA 79  78  78  ALA ALA A . n 
A 1 80  GLU 80  79  79  GLU GLU A . n 
A 1 81  CYS 81  80  80  CYS CYS A . n 
A 1 82  ARG 82  81  81  ARG ARG A . n 
A 1 83  LYS 83  82  82  LYS LYS A . n 
A 1 84  LEU 84  83  83  LEU LEU A . n 
A 1 85  GLY 85  84  84  GLY GLY A . n 
A 1 86  ALA 86  85  85  ALA ALA A . n 
A 1 87  THR 87  86  86  THR THR A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  HIS 89  88  88  HIS HIS A . n 
A 1 90  THR 90  89  89  THR THR A . n 
A 1 91  PHE 91  90  90  PHE PHE A . n 
A 1 92  VAL 92  91  91  VAL VAL A . n 
A 1 93  VAL 93  92  92  VAL VAL A . n 
A 1 94  ASP 94  93  93  ASP ASP A . n 
A 1 95  CYS 95  94  94  CYS CYS A . n 
A 1 96  GLY 96  95  95  GLY GLY A . n 
A 1 97  ASN 97  96  96  ASN ASN A . n 
A 1 98  ARG 98  97  97  ARG ARG A . n 
A 1 99  GLU 99  98  98  GLU GLU A . n 
A 1 100 ASP 100 99  99  ASP ASP A . n 
A 1 101 ILE 101 100 100 ILE ILE A . n 
A 1 102 TYR 102 101 101 TYR TYR A . n 
A 1 103 ASN 103 102 102 ASN ASN A . n 
A 1 104 SER 104 103 103 SER SER A . n 
A 1 105 VAL 105 104 104 VAL VAL A . n 
A 1 106 LYS 106 105 105 LYS LYS A . n 
A 1 107 GLN 107 106 106 GLN GLN A . n 
A 1 108 VAL 108 107 107 VAL VAL A . n 
A 1 109 LYS 109 108 108 LYS LYS A . n 
A 1 110 LYS 110 109 109 LYS LYS A . n 
A 1 111 GLU 111 110 110 GLU GLU A . n 
A 1 112 VAL 112 111 111 VAL VAL A . n 
A 1 113 GLY 113 112 112 GLY GLY A . n 
A 1 114 ASP 114 113 113 ASP ASP A . n 
A 1 115 VAL 115 114 114 VAL VAL A . n 
A 1 116 THR 116 115 115 THR THR A . n 
A 1 117 ILE 117 116 116 ILE ILE A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 VAL 119 118 118 VAL VAL A . n 
A 1 120 ASN 120 119 119 ASN ASN A . n 
A 1 121 ASN 121 120 120 ASN ASN A . n 
A 1 122 ALA 122 121 121 ALA ALA A . n 
A 1 123 GLY 123 122 122 GLY GLY A . n 
A 1 124 THR 124 123 123 THR THR A . n 
A 1 125 VAL 125 124 124 VAL VAL A . n 
A 1 126 TYR 126 125 125 TYR TYR A . n 
A 1 127 PRO 127 126 126 PRO PRO A . n 
A 1 128 ALA 128 127 127 ALA ALA A . n 
A 1 129 ASP 129 128 128 ASP ASP A . n 
A 1 130 LEU 130 129 129 LEU LEU A . n 
A 1 131 LEU 131 130 130 LEU LEU A . n 
A 1 132 SER 132 131 131 SER SER A . n 
A 1 133 THR 133 132 132 THR THR A . n 
A 1 134 LYS 134 133 133 LYS LYS A . n 
A 1 135 ASP 135 134 134 ASP ASP A . n 
A 1 136 GLU 136 135 135 GLU GLU A . n 
A 1 137 GLU 137 136 136 GLU GLU A . n 
A 1 138 ILE 138 137 137 ILE ILE A . n 
A 1 139 THR 139 138 138 THR THR A . n 
A 1 140 LYS 140 139 139 LYS LYS A . n 
A 1 141 THR 141 140 140 THR THR A . n 
A 1 142 PHE 142 141 141 PHE PHE A . n 
A 1 143 GLU 143 142 142 GLU GLU A . n 
A 1 144 ILE 144 143 143 ILE ILE A . n 
A 1 145 ASN 145 144 144 ASN ASN A . n 
A 1 146 ILE 146 145 145 ILE ILE A . n 
A 1 147 LEU 147 146 146 LEU LEU A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 HIS 149 148 148 HIS HIS A . n 
A 1 150 PHE 150 149 149 PHE PHE A . n 
A 1 151 TRP 151 150 150 TRP TRP A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 THR 153 152 152 THR THR A . n 
A 1 154 LYS 154 153 153 LYS LYS A . n 
A 1 155 ALA 155 154 154 ALA ALA A . n 
A 1 156 LEU 156 155 155 LEU LEU A . n 
A 1 157 LEU 157 156 156 LEU LEU A . n 
A 1 158 PRO 158 157 157 PRO PRO A . n 
A 1 159 SER 159 158 158 SER SER A . n 
A 1 160 MET 160 159 159 MET MET A . n 
A 1 161 ILE 161 160 160 ILE ILE A . n 
A 1 162 LYS 162 161 161 LYS LYS A . n 
A 1 163 ARG 163 162 162 ARG ARG A . n 
A 1 164 ASN 164 163 163 ASN ASN A . n 
A 1 165 HIS 165 164 164 HIS HIS A . n 
A 1 166 GLY 166 165 165 GLY GLY A . n 
A 1 167 HIS 167 166 166 HIS HIS A . n 
A 1 168 ILE 168 167 167 ILE ILE A . n 
A 1 169 VAL 169 168 168 VAL VAL A . n 
A 1 170 THR 170 169 169 THR THR A . n 
A 1 171 VAL 171 170 170 VAL VAL A . n 
A 1 172 ALA 172 171 171 ALA ALA A . n 
A 1 173 SER 173 172 172 SER SER A . n 
A 1 174 VAL 174 173 173 VAL VAL A . n 
A 1 175 CYS 175 174 174 CYS CYS A . n 
A 1 176 GLY 176 175 175 GLY GLY A . n 
A 1 177 HIS 177 176 176 HIS HIS A . n 
A 1 178 GLU 178 177 177 GLU GLU A . n 
A 1 179 GLY 179 178 178 GLY GLY A . n 
A 1 180 ILE 180 179 179 ILE ILE A . n 
A 1 181 PRO 181 180 180 PRO PRO A . n 
A 1 182 TYR 182 181 181 TYR TYR A . n 
A 1 183 LEU 183 182 182 LEU LEU A . n 
A 1 184 ILE 184 183 183 ILE ILE A . n 
A 1 185 PRO 185 184 184 PRO PRO A . n 
A 1 186 TYR 186 185 185 TYR TYR A . n 
A 1 187 CYS 187 186 186 CYS CYS A . n 
A 1 188 SER 188 187 187 SER SER A . n 
A 1 189 SER 189 188 188 SER SER A . n 
A 1 190 LYS 190 189 189 LYS LYS A . n 
A 1 191 PHE 191 190 190 PHE PHE A . n 
A 1 192 ALA 192 191 191 ALA ALA A . n 
A 1 193 ALA 193 192 192 ALA ALA A . n 
A 1 194 VAL 194 193 193 VAL VAL A . n 
A 1 195 GLY 195 194 194 GLY GLY A . n 
A 1 196 PHE 196 195 195 PHE PHE A . n 
A 1 197 HIS 197 196 196 HIS HIS A . n 
A 1 198 ARG 198 197 197 ARG ARG A . n 
A 1 199 GLY 199 198 198 GLY GLY A . n 
A 1 200 LEU 200 199 199 LEU LEU A . n 
A 1 201 THR 201 200 200 THR THR A . n 
A 1 202 SER 202 201 201 SER SER A . n 
A 1 203 GLU 203 202 202 GLU GLU A . n 
A 1 204 LEU 204 203 203 LEU LEU A . n 
A 1 205 GLN 205 204 204 GLN GLN A . n 
A 1 206 ALA 206 205 205 ALA ALA A . n 
A 1 207 LEU 207 206 206 LEU LEU A . n 
A 1 208 GLY 208 207 207 GLY GLY A . n 
A 1 209 ILE 209 208 208 ILE ILE A . n 
A 1 210 THR 210 209 209 THR THR A . n 
A 1 211 GLY 211 210 210 GLY GLY A . n 
A 1 212 ILE 212 211 211 ILE ILE A . n 
A 1 213 LYS 213 212 212 LYS LYS A . n 
A 1 214 THR 214 213 213 THR THR A . n 
A 1 215 SER 215 214 214 SER SER A . n 
A 1 216 CYS 216 215 215 CYS CYS A . n 
A 1 217 LEU 217 216 216 LEU LEU A . n 
A 1 218 CYS 218 217 217 CYS CYS A . n 
A 1 219 PRO 219 218 218 PRO PRO A . n 
A 1 220 VAL 220 219 219 VAL VAL A . n 
A 1 221 PHE 221 220 220 PHE PHE A . n 
A 1 222 VAL 222 221 221 VAL VAL A . n 
A 1 223 ASN 223 222 222 ASN ASN A . n 
A 1 224 THR 224 223 223 THR THR A . n 
A 1 225 GLY 225 224 224 GLY GLY A . n 
A 1 226 PHE 226 225 225 PHE PHE A . n 
A 1 227 THR 227 226 226 THR THR A . n 
A 1 228 LYS 228 227 227 LYS LYS A . n 
A 1 229 ASN 229 228 228 ASN ASN A . n 
A 1 230 PRO 230 229 229 PRO PRO A . n 
A 1 231 SER 231 230 230 SER SER A . n 
A 1 232 THR 232 231 231 THR THR A . n 
A 1 233 ARG 233 232 232 ARG ARG A . n 
A 1 234 LEU 234 233 ?   ?   ?   A . n 
A 1 235 TRP 235 234 ?   ?   ?   A . n 
A 1 236 PRO 236 235 235 PRO PRO A . n 
A 1 237 VAL 237 236 236 VAL VAL A . n 
A 1 238 LEU 238 237 237 LEU LEU A . n 
A 1 239 GLU 239 238 238 GLU GLU A . n 
A 1 240 THR 240 239 239 THR THR A . n 
A 1 241 ASP 241 240 240 ASP ASP A . n 
A 1 242 THR 242 241 241 THR THR A . n 
A 1 243 VAL 243 242 242 VAL VAL A . n 
A 1 244 ALA 244 243 243 ALA ALA A . n 
A 1 245 ARG 245 244 244 ARG ARG A . n 
A 1 246 SER 246 245 245 SER SER A . n 
A 1 247 LEU 247 246 246 LEU LEU A . n 
A 1 248 ILE 248 247 247 ILE ILE A . n 
A 1 249 ASP 249 248 248 ASP ASP A . n 
A 1 250 GLY 250 249 249 GLY GLY A . n 
A 1 251 ILE 251 250 250 ILE ILE A . n 
A 1 252 LEU 252 251 251 LEU LEU A . n 
A 1 253 THR 253 252 252 THR THR A . n 
A 1 254 ASN 254 253 253 ASN ASN A . n 
A 1 255 LYS 255 254 254 LYS LYS A . n 
A 1 256 LYS 256 255 255 LYS LYS A . n 
A 1 257 MET 257 256 256 MET MET A . n 
A 1 258 ILE 258 257 257 ILE ILE A . n 
A 1 259 PHE 259 258 258 PHE PHE A . n 
A 1 260 VAL 260 259 259 VAL VAL A . n 
A 1 261 PRO 261 260 260 PRO PRO A . n 
A 1 262 SER 262 261 261 SER SER A . n 
A 1 263 TYR 263 262 262 TYR TYR A . n 
A 1 264 ILE 264 263 263 ILE ILE A . n 
A 1 265 ASN 265 264 264 ASN ASN A . n 
A 1 266 ILE 266 265 265 ILE ILE A . n 
A 1 267 PHE 267 266 266 PHE PHE A . n 
A 1 268 LEU 268 267 267 LEU LEU A . n 
A 1 269 ILE 269 268 268 ILE ILE A . n 
A 1 270 LEU 270 269 269 LEU LEU A . n 
A 1 271 ASP 271 270 270 ASP ASP A . n 
A 1 272 LYS 272 271 271 LYS LYS A . n 
A 1 273 PHE 273 272 272 PHE PHE A . n 
A 1 274 LEU 274 273 273 LEU LEU A . n 
A 1 275 PRO 275 274 ?   ?   ?   A . n 
A 1 276 GLU 276 275 ?   ?   ?   A . n 
A 1 277 ARG 277 276 ?   ?   ?   A . n 
A 1 278 ALA 278 277 ?   ?   ?   A . n 
A 1 279 LEU 279 278 ?   ?   ?   A . n 
A 1 280 ALA 280 279 ?   ?   ?   A . n 
A 1 281 ALA 281 280 ?   ?   ?   A . n 
A 1 282 ILE 282 281 ?   ?   ?   A . n 
A 1 283 ASN 283 282 ?   ?   ?   A . n 
A 1 284 HIS 284 283 ?   ?   ?   A . n 
A 1 285 LEU 285 284 ?   ?   ?   A . n 
A 1 286 GLN 286 285 ?   ?   ?   A . n 
A 1 287 ASN 287 286 ?   ?   ?   A . n 
A 1 288 ILE 288 287 ?   ?   ?   A . n 
A 1 289 GLN 289 288 ?   ?   ?   A . n 
A 1 290 PHE 290 289 ?   ?   ?   A . n 
A 1 291 GLU 291 290 ?   ?   ?   A . n 
A 1 292 ALA 292 291 ?   ?   ?   A . n 
A 1 293 VAL 293 292 ?   ?   ?   A . n 
A 1 294 VAL 294 293 ?   ?   ?   A . n 
A 1 295 GLY 295 294 ?   ?   ?   A . n 
A 1 296 HIS 296 295 ?   ?   ?   A . n 
A 1 297 LYS 297 296 ?   ?   ?   A . n 
A 1 298 THR 298 297 ?   ?   ?   A . n 
A 1 299 ARG 299 298 ?   ?   ?   A . n 
A 1 300 MET 300 299 ?   ?   ?   A . n 
A 1 301 LYS 301 300 ?   ?   ?   A . n 
A 1 302 GLY 302 301 ?   ?   ?   A . n 
A 1 303 SER 303 302 ?   ?   ?   A . n 
A 1 304 GLY 304 303 ?   ?   ?   A . n 
A 1 305 HIS 305 304 ?   ?   ?   A . n 
A 1 306 HIS 306 305 ?   ?   ?   A . n 
A 1 307 HIS 307 306 ?   ?   ?   A . n 
A 1 308 HIS 308 307 ?   ?   ?   A . n 
A 1 309 HIS 309 308 ?   ?   ?   A . n 
A 1 310 HIS 310 309 ?   ?   ?   A . n 
A 1 311 HIS 311 310 ?   ?   ?   A . n 
A 1 312 HIS 312 311 ?   ?   ?   A . n 
A 1 313 HIS 313 312 ?   ?   ?   A . n 
A 1 314 HIS 314 313 ?   ?   ?   A . n 
A 1 315 HIS 315 314 ?   ?   ?   A . n 
B 1 1   MET 1   0   ?   ?   ?   B . n 
B 1 2   GLY 2   1   ?   ?   ?   B . n 
B 1 3   ASN 3   2   ?   ?   ?   B . n 
B 1 4   ILE 4   3   ?   ?   ?   B . n 
B 1 5   ILE 5   4   ?   ?   ?   B . n 
B 1 6   LEU 6   5   ?   ?   ?   B . n 
B 1 7   ASP 7   6   ?   ?   ?   B . n 
B 1 8   LEU 8   7   ?   ?   ?   B . n 
B 1 9   LEU 9   8   ?   ?   ?   B . n 
B 1 10  LEU 10  9   ?   ?   ?   B . n 
B 1 11  LEU 11  10  ?   ?   ?   B . n 
B 1 12  LEU 12  11  ?   ?   ?   B . n 
B 1 13  LEU 13  12  ?   ?   ?   B . n 
B 1 14  THR 14  13  ?   ?   ?   B . n 
B 1 15  ILE 15  14  ?   ?   ?   B . n 
B 1 16  ILE 16  15  ?   ?   ?   B . n 
B 1 17  TYR 17  16  ?   ?   ?   B . n 
B 1 18  SER 18  17  ?   ?   ?   B . n 
B 1 19  TYR 19  18  ?   ?   ?   B . n 
B 1 20  LEU 20  19  ?   ?   ?   B . n 
B 1 21  GLU 21  20  ?   ?   ?   B . n 
B 1 22  ALA 22  21  ?   ?   ?   B . n 
B 1 23  LEU 23  22  ?   ?   ?   B . n 
B 1 24  VAL 24  23  ?   ?   ?   B . n 
B 1 25  LYS 25  24  ?   ?   ?   B . n 
B 1 26  VAL 26  25  25  VAL VAL B . n 
B 1 27  PHE 27  26  26  PHE PHE B . n 
B 1 28  PHE 28  27  27  PHE PHE B . n 
B 1 29  PRO 29  28  28  PRO PRO B . n 
B 1 30  ARG 30  29  29  ARG ARG B . n 
B 1 31  LYS 31  30  30  LYS LYS B . n 
B 1 32  ARG 32  31  31  ARG ARG B . n 
B 1 33  LYS 33  32  32  LYS LYS B . n 
B 1 34  SER 34  33  33  SER SER B . n 
B 1 35  VAL 35  34  34  VAL VAL B . n 
B 1 36  ALA 36  35  35  ALA ALA B . n 
B 1 37  GLY 37  36  36  GLY GLY B . n 
B 1 38  GLU 38  37  37  GLU GLU B . n 
B 1 39  ILE 39  38  38  ILE ILE B . n 
B 1 40  VAL 40  39  39  VAL VAL B . n 
B 1 41  LEU 41  40  40  LEU LEU B . n 
B 1 42  ILE 42  41  41  ILE ILE B . n 
B 1 43  THR 43  42  42  THR THR B . n 
B 1 44  GLY 44  43  43  GLY GLY B . n 
B 1 45  ALA 45  44  44  ALA ALA B . n 
B 1 46  GLY 46  45  45  GLY GLY B . n 
B 1 47  HIS 47  46  46  HIS HIS B . n 
B 1 48  GLY 48  47  47  GLY GLY B . n 
B 1 49  ILE 49  48  48  ILE ILE B . n 
B 1 50  GLY 50  49  49  GLY GLY B . n 
B 1 51  ARG 51  50  50  ARG ARG B . n 
B 1 52  TRP 52  51  51  TRP TRP B . n 
B 1 53  THR 53  52  52  THR THR B . n 
B 1 54  ALA 54  53  53  ALA ALA B . n 
B 1 55  TYR 55  54  54  TYR TYR B . n 
B 1 56  GLU 56  55  55  GLU GLU B . n 
B 1 57  PHE 57  56  56  PHE PHE B . n 
B 1 58  ALA 58  57  57  ALA ALA B . n 
B 1 59  LYS 59  58  58  LYS LYS B . n 
B 1 60  GLN 60  59  59  GLN GLN B . n 
B 1 61  LYS 61  60  60  LYS LYS B . n 
B 1 62  SER 62  61  61  SER SER B . n 
B 1 63  ARG 63  62  62  ARG ARG B . n 
B 1 64  LEU 64  63  63  LEU LEU B . n 
B 1 65  VAL 65  64  64  VAL VAL B . n 
B 1 66  LEU 66  65  65  LEU LEU B . n 
B 1 67  TRP 67  66  66  TRP TRP B . n 
B 1 68  ASP 68  67  67  ASP ASP B . n 
B 1 69  ILE 69  68  68  ILE ILE B . n 
B 1 70  ASN 70  69  69  ASN ASN B . n 
B 1 71  LYS 71  70  70  LYS LYS B . n 
B 1 72  HIS 72  71  71  HIS HIS B . n 
B 1 73  GLY 73  72  72  GLY GLY B . n 
B 1 74  VAL 74  73  73  VAL VAL B . n 
B 1 75  GLU 75  74  74  GLU GLU B . n 
B 1 76  GLU 76  75  75  GLU GLU B . n 
B 1 77  THR 77  76  76  THR THR B . n 
B 1 78  ALA 78  77  77  ALA ALA B . n 
B 1 79  ALA 79  78  78  ALA ALA B . n 
B 1 80  GLU 80  79  79  GLU GLU B . n 
B 1 81  CYS 81  80  80  CYS CYS B . n 
B 1 82  ARG 82  81  81  ARG ARG B . n 
B 1 83  LYS 83  82  82  LYS LYS B . n 
B 1 84  LEU 84  83  83  LEU LEU B . n 
B 1 85  GLY 85  84  84  GLY GLY B . n 
B 1 86  ALA 86  85  85  ALA ALA B . n 
B 1 87  THR 87  86  86  THR THR B . n 
B 1 88  VAL 88  87  87  VAL VAL B . n 
B 1 89  HIS 89  88  88  HIS HIS B . n 
B 1 90  THR 90  89  89  THR THR B . n 
B 1 91  PHE 91  90  90  PHE PHE B . n 
B 1 92  VAL 92  91  91  VAL VAL B . n 
B 1 93  VAL 93  92  92  VAL VAL B . n 
B 1 94  ASP 94  93  93  ASP ASP B . n 
B 1 95  CYS 95  94  94  CYS CYS B . n 
B 1 96  GLY 96  95  95  GLY GLY B . n 
B 1 97  ASN 97  96  96  ASN ASN B . n 
B 1 98  ARG 98  97  97  ARG ARG B . n 
B 1 99  GLU 99  98  98  GLU GLU B . n 
B 1 100 ASP 100 99  99  ASP ASP B . n 
B 1 101 ILE 101 100 100 ILE ILE B . n 
B 1 102 TYR 102 101 101 TYR TYR B . n 
B 1 103 ASN 103 102 102 ASN ASN B . n 
B 1 104 SER 104 103 103 SER SER B . n 
B 1 105 VAL 105 104 104 VAL VAL B . n 
B 1 106 LYS 106 105 105 LYS LYS B . n 
B 1 107 GLN 107 106 106 GLN GLN B . n 
B 1 108 VAL 108 107 107 VAL VAL B . n 
B 1 109 LYS 109 108 108 LYS LYS B . n 
B 1 110 LYS 110 109 109 LYS LYS B . n 
B 1 111 GLU 111 110 110 GLU GLU B . n 
B 1 112 VAL 112 111 111 VAL VAL B . n 
B 1 113 GLY 113 112 112 GLY GLY B . n 
B 1 114 ASP 114 113 113 ASP ASP B . n 
B 1 115 VAL 115 114 114 VAL VAL B . n 
B 1 116 THR 116 115 115 THR THR B . n 
B 1 117 ILE 117 116 116 ILE ILE B . n 
B 1 118 LEU 118 117 117 LEU LEU B . n 
B 1 119 VAL 119 118 118 VAL VAL B . n 
B 1 120 ASN 120 119 119 ASN ASN B . n 
B 1 121 ASN 121 120 120 ASN ASN B . n 
B 1 122 ALA 122 121 121 ALA ALA B . n 
B 1 123 GLY 123 122 122 GLY GLY B . n 
B 1 124 THR 124 123 123 THR THR B . n 
B 1 125 VAL 125 124 124 VAL VAL B . n 
B 1 126 TYR 126 125 125 TYR TYR B . n 
B 1 127 PRO 127 126 126 PRO PRO B . n 
B 1 128 ALA 128 127 127 ALA ALA B . n 
B 1 129 ASP 129 128 128 ASP ASP B . n 
B 1 130 LEU 130 129 129 LEU LEU B . n 
B 1 131 LEU 131 130 130 LEU LEU B . n 
B 1 132 SER 132 131 131 SER SER B . n 
B 1 133 THR 133 132 132 THR THR B . n 
B 1 134 LYS 134 133 133 LYS LYS B . n 
B 1 135 ASP 135 134 134 ASP ASP B . n 
B 1 136 GLU 136 135 135 GLU GLU B . n 
B 1 137 GLU 137 136 136 GLU GLU B . n 
B 1 138 ILE 138 137 137 ILE ILE B . n 
B 1 139 THR 139 138 138 THR THR B . n 
B 1 140 LYS 140 139 139 LYS LYS B . n 
B 1 141 THR 141 140 140 THR THR B . n 
B 1 142 PHE 142 141 141 PHE PHE B . n 
B 1 143 GLU 143 142 142 GLU GLU B . n 
B 1 144 ILE 144 143 143 ILE ILE B . n 
B 1 145 ASN 145 144 144 ASN ASN B . n 
B 1 146 ILE 146 145 145 ILE ILE B . n 
B 1 147 LEU 147 146 146 LEU LEU B . n 
B 1 148 GLY 148 147 147 GLY GLY B . n 
B 1 149 HIS 149 148 148 HIS HIS B . n 
B 1 150 PHE 150 149 149 PHE PHE B . n 
B 1 151 TRP 151 150 150 TRP TRP B . n 
B 1 152 ILE 152 151 151 ILE ILE B . n 
B 1 153 THR 153 152 152 THR THR B . n 
B 1 154 LYS 154 153 153 LYS LYS B . n 
B 1 155 ALA 155 154 154 ALA ALA B . n 
B 1 156 LEU 156 155 155 LEU LEU B . n 
B 1 157 LEU 157 156 156 LEU LEU B . n 
B 1 158 PRO 158 157 157 PRO PRO B . n 
B 1 159 SER 159 158 158 SER SER B . n 
B 1 160 MET 160 159 159 MET MET B . n 
B 1 161 ILE 161 160 160 ILE ILE B . n 
B 1 162 LYS 162 161 161 LYS LYS B . n 
B 1 163 ARG 163 162 162 ARG ARG B . n 
B 1 164 ASN 164 163 163 ASN ASN B . n 
B 1 165 HIS 165 164 164 HIS HIS B . n 
B 1 166 GLY 166 165 165 GLY GLY B . n 
B 1 167 HIS 167 166 166 HIS HIS B . n 
B 1 168 ILE 168 167 167 ILE ILE B . n 
B 1 169 VAL 169 168 168 VAL VAL B . n 
B 1 170 THR 170 169 169 THR THR B . n 
B 1 171 VAL 171 170 170 VAL VAL B . n 
B 1 172 ALA 172 171 171 ALA ALA B . n 
B 1 173 SER 173 172 172 SER SER B . n 
B 1 174 VAL 174 173 173 VAL VAL B . n 
B 1 175 CYS 175 174 174 CYS CYS B . n 
B 1 176 GLY 176 175 175 GLY GLY B . n 
B 1 177 HIS 177 176 176 HIS HIS B . n 
B 1 178 GLU 178 177 177 GLU GLU B . n 
B 1 179 GLY 179 178 178 GLY GLY B . n 
B 1 180 ILE 180 179 179 ILE ILE B . n 
B 1 181 PRO 181 180 180 PRO PRO B . n 
B 1 182 TYR 182 181 181 TYR TYR B . n 
B 1 183 LEU 183 182 182 LEU LEU B . n 
B 1 184 ILE 184 183 183 ILE ILE B . n 
B 1 185 PRO 185 184 184 PRO PRO B . n 
B 1 186 TYR 186 185 185 TYR TYR B . n 
B 1 187 CYS 187 186 186 CYS CYS B . n 
B 1 188 SER 188 187 187 SER SER B . n 
B 1 189 SER 189 188 188 SER SER B . n 
B 1 190 LYS 190 189 189 LYS LYS B . n 
B 1 191 PHE 191 190 190 PHE PHE B . n 
B 1 192 ALA 192 191 191 ALA ALA B . n 
B 1 193 ALA 193 192 192 ALA ALA B . n 
B 1 194 VAL 194 193 193 VAL VAL B . n 
B 1 195 GLY 195 194 194 GLY GLY B . n 
B 1 196 PHE 196 195 195 PHE PHE B . n 
B 1 197 HIS 197 196 196 HIS HIS B . n 
B 1 198 ARG 198 197 197 ARG ARG B . n 
B 1 199 GLY 199 198 198 GLY GLY B . n 
B 1 200 LEU 200 199 199 LEU LEU B . n 
B 1 201 THR 201 200 200 THR THR B . n 
B 1 202 SER 202 201 201 SER SER B . n 
B 1 203 GLU 203 202 202 GLU GLU B . n 
B 1 204 LEU 204 203 203 LEU LEU B . n 
B 1 205 GLN 205 204 204 GLN GLN B . n 
B 1 206 ALA 206 205 205 ALA ALA B . n 
B 1 207 LEU 207 206 206 LEU LEU B . n 
B 1 208 GLY 208 207 207 GLY GLY B . n 
B 1 209 ILE 209 208 208 ILE ILE B . n 
B 1 210 THR 210 209 209 THR THR B . n 
B 1 211 GLY 211 210 210 GLY GLY B . n 
B 1 212 ILE 212 211 211 ILE ILE B . n 
B 1 213 LYS 213 212 212 LYS LYS B . n 
B 1 214 THR 214 213 213 THR THR B . n 
B 1 215 SER 215 214 214 SER SER B . n 
B 1 216 CYS 216 215 215 CYS CYS B . n 
B 1 217 LEU 217 216 216 LEU LEU B . n 
B 1 218 CYS 218 217 217 CYS CYS B . n 
B 1 219 PRO 219 218 218 PRO PRO B . n 
B 1 220 VAL 220 219 219 VAL VAL B . n 
B 1 221 PHE 221 220 220 PHE PHE B . n 
B 1 222 VAL 222 221 221 VAL VAL B . n 
B 1 223 ASN 223 222 222 ASN ASN B . n 
B 1 224 THR 224 223 223 THR THR B . n 
B 1 225 GLY 225 224 224 GLY GLY B . n 
B 1 226 PHE 226 225 225 PHE PHE B . n 
B 1 227 THR 227 226 226 THR THR B . n 
B 1 228 LYS 228 227 227 LYS LYS B . n 
B 1 229 ASN 229 228 228 ASN ASN B . n 
B 1 230 PRO 230 229 229 PRO PRO B . n 
B 1 231 SER 231 230 230 SER SER B . n 
B 1 232 THR 232 231 ?   ?   ?   B . n 
B 1 233 ARG 233 232 ?   ?   ?   B . n 
B 1 234 LEU 234 233 ?   ?   ?   B . n 
B 1 235 TRP 235 234 ?   ?   ?   B . n 
B 1 236 PRO 236 235 235 PRO PRO B . n 
B 1 237 VAL 237 236 236 VAL VAL B . n 
B 1 238 LEU 238 237 237 LEU LEU B . n 
B 1 239 GLU 239 238 238 GLU GLU B . n 
B 1 240 THR 240 239 239 THR THR B . n 
B 1 241 ASP 241 240 240 ASP ASP B . n 
B 1 242 THR 242 241 241 THR THR B . n 
B 1 243 VAL 243 242 242 VAL VAL B . n 
B 1 244 ALA 244 243 243 ALA ALA B . n 
B 1 245 ARG 245 244 244 ARG ARG B . n 
B 1 246 SER 246 245 245 SER SER B . n 
B 1 247 LEU 247 246 246 LEU LEU B . n 
B 1 248 ILE 248 247 247 ILE ILE B . n 
B 1 249 ASP 249 248 248 ASP ASP B . n 
B 1 250 GLY 250 249 249 GLY GLY B . n 
B 1 251 ILE 251 250 250 ILE ILE B . n 
B 1 252 LEU 252 251 251 LEU LEU B . n 
B 1 253 THR 253 252 252 THR THR B . n 
B 1 254 ASN 254 253 253 ASN ASN B . n 
B 1 255 LYS 255 254 254 LYS LYS B . n 
B 1 256 LYS 256 255 255 LYS LYS B . n 
B 1 257 MET 257 256 256 MET MET B . n 
B 1 258 ILE 258 257 257 ILE ILE B . n 
B 1 259 PHE 259 258 258 PHE PHE B . n 
B 1 260 VAL 260 259 259 VAL VAL B . n 
B 1 261 PRO 261 260 260 PRO PRO B . n 
B 1 262 SER 262 261 261 SER SER B . n 
B 1 263 TYR 263 262 262 TYR TYR B . n 
B 1 264 ILE 264 263 263 ILE ILE B . n 
B 1 265 ASN 265 264 264 ASN ASN B . n 
B 1 266 ILE 266 265 265 ILE ILE B . n 
B 1 267 PHE 267 266 266 PHE PHE B . n 
B 1 268 LEU 268 267 267 LEU LEU B . n 
B 1 269 ILE 269 268 268 ILE ILE B . n 
B 1 270 LEU 270 269 269 LEU LEU B . n 
B 1 271 ASP 271 270 270 ASP ASP B . n 
B 1 272 LYS 272 271 271 LYS LYS B . n 
B 1 273 PHE 273 272 272 PHE PHE B . n 
B 1 274 LEU 274 273 ?   ?   ?   B . n 
B 1 275 PRO 275 274 ?   ?   ?   B . n 
B 1 276 GLU 276 275 ?   ?   ?   B . n 
B 1 277 ARG 277 276 ?   ?   ?   B . n 
B 1 278 ALA 278 277 ?   ?   ?   B . n 
B 1 279 LEU 279 278 ?   ?   ?   B . n 
B 1 280 ALA 280 279 ?   ?   ?   B . n 
B 1 281 ALA 281 280 ?   ?   ?   B . n 
B 1 282 ILE 282 281 ?   ?   ?   B . n 
B 1 283 ASN 283 282 ?   ?   ?   B . n 
B 1 284 HIS 284 283 ?   ?   ?   B . n 
B 1 285 LEU 285 284 ?   ?   ?   B . n 
B 1 286 GLN 286 285 ?   ?   ?   B . n 
B 1 287 ASN 287 286 ?   ?   ?   B . n 
B 1 288 ILE 288 287 ?   ?   ?   B . n 
B 1 289 GLN 289 288 ?   ?   ?   B . n 
B 1 290 PHE 290 289 ?   ?   ?   B . n 
B 1 291 GLU 291 290 ?   ?   ?   B . n 
B 1 292 ALA 292 291 ?   ?   ?   B . n 
B 1 293 VAL 293 292 ?   ?   ?   B . n 
B 1 294 VAL 294 293 ?   ?   ?   B . n 
B 1 295 GLY 295 294 ?   ?   ?   B . n 
B 1 296 HIS 296 295 ?   ?   ?   B . n 
B 1 297 LYS 297 296 ?   ?   ?   B . n 
B 1 298 THR 298 297 ?   ?   ?   B . n 
B 1 299 ARG 299 298 ?   ?   ?   B . n 
B 1 300 MET 300 299 ?   ?   ?   B . n 
B 1 301 LYS 301 300 ?   ?   ?   B . n 
B 1 302 GLY 302 301 ?   ?   ?   B . n 
B 1 303 SER 303 302 ?   ?   ?   B . n 
B 1 304 GLY 304 303 ?   ?   ?   B . n 
B 1 305 HIS 305 304 ?   ?   ?   B . n 
B 1 306 HIS 306 305 ?   ?   ?   B . n 
B 1 307 HIS 307 306 ?   ?   ?   B . n 
B 1 308 HIS 308 307 ?   ?   ?   B . n 
B 1 309 HIS 309 308 ?   ?   ?   B . n 
B 1 310 HIS 310 309 ?   ?   ?   B . n 
B 1 311 HIS 311 310 ?   ?   ?   B . n 
B 1 312 HIS 312 311 ?   ?   ?   B . n 
B 1 313 HIS 313 312 ?   ?   ?   B . n 
B 1 314 HIS 314 313 ?   ?   ?   B . n 
B 1 315 HIS 315 314 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 NAD   ? ? NAD   ? ? 'SUBJECT OF INVESTIGATION' ? 
2 A1AG6 ? ? A1AG6 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 NAD   1  401 296 NAD   NAD A . 
D 3 A1AG6 1  402 301 A1AG6 PFE A . 
E 2 NAD   1  401 296 NAD   NAD B . 
F 4 HOH   1  501 65  HOH   HOH A . 
F 4 HOH   2  502 159 HOH   HOH A . 
F 4 HOH   3  503 47  HOH   HOH A . 
F 4 HOH   4  504 39  HOH   HOH A . 
F 4 HOH   5  505 22  HOH   HOH A . 
F 4 HOH   6  506 5   HOH   HOH A . 
F 4 HOH   7  507 87  HOH   HOH A . 
F 4 HOH   8  508 83  HOH   HOH A . 
F 4 HOH   9  509 62  HOH   HOH A . 
F 4 HOH   10 510 97  HOH   HOH A . 
F 4 HOH   11 511 77  HOH   HOH A . 
F 4 HOH   12 512 73  HOH   HOH A . 
F 4 HOH   13 513 11  HOH   HOH A . 
F 4 HOH   14 514 49  HOH   HOH A . 
F 4 HOH   15 515 95  HOH   HOH A . 
F 4 HOH   16 516 70  HOH   HOH A . 
F 4 HOH   17 517 21  HOH   HOH A . 
F 4 HOH   18 518 131 HOH   HOH A . 
F 4 HOH   19 519 82  HOH   HOH A . 
F 4 HOH   20 520 141 HOH   HOH A . 
F 4 HOH   21 521 81  HOH   HOH A . 
F 4 HOH   22 522 121 HOH   HOH A . 
F 4 HOH   23 523 135 HOH   HOH A . 
F 4 HOH   24 524 10  HOH   HOH A . 
F 4 HOH   25 525 139 HOH   HOH A . 
F 4 HOH   26 526 2   HOH   HOH A . 
F 4 HOH   27 527 118 HOH   HOH A . 
F 4 HOH   28 528 23  HOH   HOH A . 
F 4 HOH   29 529 114 HOH   HOH A . 
F 4 HOH   30 530 4   HOH   HOH A . 
F 4 HOH   31 531 69  HOH   HOH A . 
F 4 HOH   32 532 58  HOH   HOH A . 
F 4 HOH   33 533 127 HOH   HOH A . 
F 4 HOH   34 534 55  HOH   HOH A . 
F 4 HOH   35 535 110 HOH   HOH A . 
F 4 HOH   36 536 68  HOH   HOH A . 
F 4 HOH   37 537 33  HOH   HOH A . 
F 4 HOH   38 538 147 HOH   HOH A . 
F 4 HOH   39 539 94  HOH   HOH A . 
F 4 HOH   40 540 63  HOH   HOH A . 
F 4 HOH   41 541 128 HOH   HOH A . 
F 4 HOH   42 542 91  HOH   HOH A . 
F 4 HOH   43 543 89  HOH   HOH A . 
F 4 HOH   44 544 101 HOH   HOH A . 
F 4 HOH   45 545 149 HOH   HOH A . 
F 4 HOH   46 546 53  HOH   HOH A . 
F 4 HOH   47 547 13  HOH   HOH A . 
F 4 HOH   48 548 126 HOH   HOH A . 
F 4 HOH   49 549 102 HOH   HOH A . 
F 4 HOH   50 550 20  HOH   HOH A . 
F 4 HOH   51 551 24  HOH   HOH A . 
F 4 HOH   52 552 122 HOH   HOH A . 
F 4 HOH   53 553 32  HOH   HOH A . 
F 4 HOH   54 554 30  HOH   HOH A . 
F 4 HOH   55 555 64  HOH   HOH A . 
F 4 HOH   56 556 78  HOH   HOH A . 
F 4 HOH   57 557 90  HOH   HOH A . 
F 4 HOH   58 558 154 HOH   HOH A . 
F 4 HOH   59 559 148 HOH   HOH A . 
F 4 HOH   60 560 9   HOH   HOH A . 
F 4 HOH   61 561 132 HOH   HOH A . 
F 4 HOH   62 562 160 HOH   HOH A . 
F 4 HOH   63 563 155 HOH   HOH A . 
F 4 HOH   64 564 117 HOH   HOH A . 
F 4 HOH   65 565 108 HOH   HOH A . 
F 4 HOH   66 566 74  HOH   HOH A . 
F 4 HOH   67 567 60  HOH   HOH A . 
F 4 HOH   68 568 92  HOH   HOH A . 
F 4 HOH   69 569 158 HOH   HOH A . 
F 4 HOH   70 570 138 HOH   HOH A . 
F 4 HOH   71 571 106 HOH   HOH A . 
F 4 HOH   72 572 28  HOH   HOH A . 
F 4 HOH   73 573 51  HOH   HOH A . 
F 4 HOH   74 574 151 HOH   HOH A . 
F 4 HOH   75 575 109 HOH   HOH A . 
G 4 HOH   1  501 123 HOH   HOH B . 
G 4 HOH   2  502 67  HOH   HOH B . 
G 4 HOH   3  503 96  HOH   HOH B . 
G 4 HOH   4  504 61  HOH   HOH B . 
G 4 HOH   5  505 88  HOH   HOH B . 
G 4 HOH   6  506 80  HOH   HOH B . 
G 4 HOH   7  507 133 HOH   HOH B . 
G 4 HOH   8  508 15  HOH   HOH B . 
G 4 HOH   9  509 46  HOH   HOH B . 
G 4 HOH   10 510 12  HOH   HOH B . 
G 4 HOH   11 511 66  HOH   HOH B . 
G 4 HOH   12 512 42  HOH   HOH B . 
G 4 HOH   13 513 120 HOH   HOH B . 
G 4 HOH   14 514 52  HOH   HOH B . 
G 4 HOH   15 515 27  HOH   HOH B . 
G 4 HOH   16 516 86  HOH   HOH B . 
G 4 HOH   17 517 76  HOH   HOH B . 
G 4 HOH   18 518 56  HOH   HOH B . 
G 4 HOH   19 519 6   HOH   HOH B . 
G 4 HOH   20 520 93  HOH   HOH B . 
G 4 HOH   21 521 116 HOH   HOH B . 
G 4 HOH   22 522 17  HOH   HOH B . 
G 4 HOH   23 523 105 HOH   HOH B . 
G 4 HOH   24 524 41  HOH   HOH B . 
G 4 HOH   25 525 38  HOH   HOH B . 
G 4 HOH   26 526 99  HOH   HOH B . 
G 4 HOH   27 527 104 HOH   HOH B . 
G 4 HOH   28 528 150 HOH   HOH B . 
G 4 HOH   29 529 35  HOH   HOH B . 
G 4 HOH   30 530 107 HOH   HOH B . 
G 4 HOH   31 531 16  HOH   HOH B . 
G 4 HOH   32 532 140 HOH   HOH B . 
G 4 HOH   33 533 36  HOH   HOH B . 
G 4 HOH   34 534 137 HOH   HOH B . 
G 4 HOH   35 535 7   HOH   HOH B . 
G 4 HOH   36 536 134 HOH   HOH B . 
G 4 HOH   37 537 45  HOH   HOH B . 
G 4 HOH   38 538 40  HOH   HOH B . 
G 4 HOH   39 539 43  HOH   HOH B . 
G 4 HOH   40 540 71  HOH   HOH B . 
G 4 HOH   41 541 84  HOH   HOH B . 
G 4 HOH   42 542 124 HOH   HOH B . 
G 4 HOH   43 543 85  HOH   HOH B . 
G 4 HOH   44 544 112 HOH   HOH B . 
G 4 HOH   45 545 29  HOH   HOH B . 
G 4 HOH   46 546 79  HOH   HOH B . 
G 4 HOH   47 547 111 HOH   HOH B . 
G 4 HOH   48 548 31  HOH   HOH B . 
G 4 HOH   49 549 129 HOH   HOH B . 
G 4 HOH   50 550 75  HOH   HOH B . 
G 4 HOH   51 551 144 HOH   HOH B . 
G 4 HOH   52 552 25  HOH   HOH B . 
G 4 HOH   53 553 146 HOH   HOH B . 
G 4 HOH   54 554 18  HOH   HOH B . 
G 4 HOH   55 555 152 HOH   HOH B . 
G 4 HOH   56 556 143 HOH   HOH B . 
G 4 HOH   57 557 50  HOH   HOH B . 
G 4 HOH   58 558 26  HOH   HOH B . 
G 4 HOH   59 559 136 HOH   HOH B . 
G 4 HOH   60 560 103 HOH   HOH B . 
G 4 HOH   61 561 125 HOH   HOH B . 
G 4 HOH   62 562 72  HOH   HOH B . 
G 4 HOH   63 563 119 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER   ? ? ? 2.11.8 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? BUSTER   ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9AV8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.68 
_cell.length_a_esd                 ? 
_cell.length_b                     185.24 
_cell.length_b_esd                 ? 
_cell.length_c                     64.45 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9AV8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9AV8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          62.62 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;protein was incubated at 12 mg/ml with 1 mM NAD+ and 1 mM compound 1 with the addition of 0.125% B-octyl-glucoside.  Sitting drop vapor diffusion crystallization was set up by mixing 300 nl protein complex with 300 nl of reservoir solution containing 30% PEG3350, 0.2 M ammonium chloride.  Crystals grew at room temperature over 2 weeks.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-12-03 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9AV8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.592 
_reflns.d_resolution_low                               185.240 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     12730 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           92.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.083 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.196 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.592 
_reflns_shell.d_res_low                                     2.952 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             637 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.3 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.410 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.546 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          66.6 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.957 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            9.159 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            9.0049 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -18.1639 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               70.15 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.814 
_refine.correlation_coeff_Fo_to_Fc_free          0.763 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9AV8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.592 
_refine.ls_d_res_low                             29.29 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     12677 
_refine.ls_number_reflns_R_free                  625 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    42.8 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2530 
_refine.ls_R_factor_R_free                       0.3065 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2503 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.608 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        9AV8 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.47 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.592 
_refine_hist.d_res_low                        29.29 
_refine_hist.number_atoms_solvent             138 
_refine_hist.number_atoms_total               4265 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4009 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         118 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 4221 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.89  ? 5740 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1459 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 717  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 4220 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 580  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 3301 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 2.54  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 20.94 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.592 
_refine_ls_shell.d_res_low                        2.87 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             19 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               5.28 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2684 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.348 
# 
_struct.entry_id                     9AV8 
_struct.title                        
;Design and application of synthetic 17B-HSD13 substrates to drug discovery, and to reveal preserved catalytic activity of protective human variants
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9AV8 
_struct_keywords.text            'Enzyme, substrate, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A8C0PP93_CANLF 
_struct_ref.pdbx_db_accession          A0A8C0PP93 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;NIILDLLLLLLTIIYSYLEALVKVFFPRKRKSVAGEIVLITGAGHGIGRWTAYEFAKQKSRLVLWDINKHGVEETAAECR
KLGATVHTFVVDCGNREDIYNSVKQVKKEVGDVTILVNNAGTVYPADLLSTKDEEITKTFEINILGHFWITKALLPSMIK
RNHGHIVTVASVCGHGVIPYLIPYCSSKFAAVGFHRALTLELQTLGITGIKTSCLCPVFVNTGFTKNPSTRLWPILETDT
VARSLIDGILTNKKMIFVPSYYNIYLILDKFLPERALAAINHLQNIQFEAVIGHKTRMK
;
_struct_ref.pdbx_align_begin           2 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9AV8 A 3 ? 301 ? A0A8C0PP93 2 ? 300 ? 2 300 
2 1 9AV8 B 3 ? 301 ? A0A8C0PP93 2 ? 300 ? 2 300 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9AV8 MET A 1   ? UNP A0A8C0PP93 ?   ?   'expression tag'      0   1  
1 9AV8 GLY A 2   ? UNP A0A8C0PP93 ?   ?   'expression tag'      1   2  
1 9AV8 GLU A 178 ? UNP A0A8C0PP93 GLY 177 'engineered mutation' 177 3  
1 9AV8 GLY A 179 ? UNP A0A8C0PP93 VAL 178 'engineered mutation' 178 4  
1 9AV8 GLY A 199 ? UNP A0A8C0PP93 ALA 198 'engineered mutation' 198 5  
1 9AV8 SER A 202 ? UNP A0A8C0PP93 LEU 201 'engineered mutation' 201 6  
1 9AV8 ALA A 206 ? UNP A0A8C0PP93 THR 205 'engineered mutation' 205 7  
1 9AV8 VAL A 237 ? UNP A0A8C0PP93 ILE 236 'engineered mutation' 236 8  
1 9AV8 ILE A 264 ? UNP A0A8C0PP93 TYR 263 'engineered mutation' 263 9  
1 9AV8 PHE A 267 ? UNP A0A8C0PP93 TYR 266 'engineered mutation' 266 10 
1 9AV8 VAL A 294 ? UNP A0A8C0PP93 ILE 293 'engineered mutation' 293 11 
1 9AV8 GLY A 302 ? UNP A0A8C0PP93 ?   ?   'expression tag'      301 12 
1 9AV8 SER A 303 ? UNP A0A8C0PP93 ?   ?   'expression tag'      302 13 
1 9AV8 GLY A 304 ? UNP A0A8C0PP93 ?   ?   'expression tag'      303 14 
1 9AV8 HIS A 305 ? UNP A0A8C0PP93 ?   ?   'expression tag'      304 15 
1 9AV8 HIS A 306 ? UNP A0A8C0PP93 ?   ?   'expression tag'      305 16 
1 9AV8 HIS A 307 ? UNP A0A8C0PP93 ?   ?   'expression tag'      306 17 
1 9AV8 HIS A 308 ? UNP A0A8C0PP93 ?   ?   'expression tag'      307 18 
1 9AV8 HIS A 309 ? UNP A0A8C0PP93 ?   ?   'expression tag'      308 19 
1 9AV8 HIS A 310 ? UNP A0A8C0PP93 ?   ?   'expression tag'      309 20 
1 9AV8 HIS A 311 ? UNP A0A8C0PP93 ?   ?   'expression tag'      310 21 
1 9AV8 HIS A 312 ? UNP A0A8C0PP93 ?   ?   'expression tag'      311 22 
1 9AV8 HIS A 313 ? UNP A0A8C0PP93 ?   ?   'expression tag'      312 23 
1 9AV8 HIS A 314 ? UNP A0A8C0PP93 ?   ?   'expression tag'      313 24 
1 9AV8 HIS A 315 ? UNP A0A8C0PP93 ?   ?   'expression tag'      314 25 
2 9AV8 MET B 1   ? UNP A0A8C0PP93 ?   ?   'expression tag'      0   26 
2 9AV8 GLY B 2   ? UNP A0A8C0PP93 ?   ?   'expression tag'      1   27 
2 9AV8 GLU B 178 ? UNP A0A8C0PP93 GLY 177 'engineered mutation' 177 28 
2 9AV8 GLY B 179 ? UNP A0A8C0PP93 VAL 178 'engineered mutation' 178 29 
2 9AV8 GLY B 199 ? UNP A0A8C0PP93 ALA 198 'engineered mutation' 198 30 
2 9AV8 SER B 202 ? UNP A0A8C0PP93 LEU 201 'engineered mutation' 201 31 
2 9AV8 ALA B 206 ? UNP A0A8C0PP93 THR 205 'engineered mutation' 205 32 
2 9AV8 VAL B 237 ? UNP A0A8C0PP93 ILE 236 'engineered mutation' 236 33 
2 9AV8 ILE B 264 ? UNP A0A8C0PP93 TYR 263 'engineered mutation' 263 34 
2 9AV8 PHE B 267 ? UNP A0A8C0PP93 TYR 266 'engineered mutation' 266 35 
2 9AV8 VAL B 294 ? UNP A0A8C0PP93 ILE 293 'engineered mutation' 293 36 
2 9AV8 GLY B 302 ? UNP A0A8C0PP93 ?   ?   'expression tag'      301 37 
2 9AV8 SER B 303 ? UNP A0A8C0PP93 ?   ?   'expression tag'      302 38 
2 9AV8 GLY B 304 ? UNP A0A8C0PP93 ?   ?   'expression tag'      303 39 
2 9AV8 HIS B 305 ? UNP A0A8C0PP93 ?   ?   'expression tag'      304 40 
2 9AV8 HIS B 306 ? UNP A0A8C0PP93 ?   ?   'expression tag'      305 41 
2 9AV8 HIS B 307 ? UNP A0A8C0PP93 ?   ?   'expression tag'      306 42 
2 9AV8 HIS B 308 ? UNP A0A8C0PP93 ?   ?   'expression tag'      307 43 
2 9AV8 HIS B 309 ? UNP A0A8C0PP93 ?   ?   'expression tag'      308 44 
2 9AV8 HIS B 310 ? UNP A0A8C0PP93 ?   ?   'expression tag'      309 45 
2 9AV8 HIS B 311 ? UNP A0A8C0PP93 ?   ?   'expression tag'      310 46 
2 9AV8 HIS B 312 ? UNP A0A8C0PP93 ?   ?   'expression tag'      311 47 
2 9AV8 HIS B 313 ? UNP A0A8C0PP93 ?   ?   'expression tag'      312 48 
2 9AV8 HIS B 314 ? UNP A0A8C0PP93 ?   ?   'expression tag'      313 49 
2 9AV8 HIS B 315 ? UNP A0A8C0PP93 ?   ?   'expression tag'      314 50 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6140  ? 
1 MORE         -48   ? 
1 'SSA (A^2)'  22440 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 3   ? PHE A 28  ? ASN A 2   PHE A 27  1 ? 26 
HELX_P HELX_P2  AA2 GLY A 48  ? GLN A 60  ? GLY A 47  GLN A 59  1 ? 13 
HELX_P HELX_P3  AA3 ASN A 70  ? LYS A 83  ? ASN A 69  LYS A 82  1 ? 14 
HELX_P HELX_P4  AA4 ASN A 97  ? LYS A 110 ? ASN A 96  LYS A 109 1 ? 14 
HELX_P HELX_P5  AA5 LYS A 134 ? ILE A 146 ? LYS A 133 ILE A 145 1 ? 13 
HELX_P HELX_P6  AA6 ILE A 146 ? ASN A 164 ? ILE A 145 ASN A 163 1 ? 19 
HELX_P HELX_P7  AA7 SER A 173 ? HIS A 177 ? SER A 172 HIS A 176 5 ? 5  
HELX_P HELX_P8  AA8 LEU A 183 ? LEU A 207 ? LEU A 182 LEU A 206 1 ? 25 
HELX_P HELX_P9  AA9 GLU A 239 ? ASN A 254 ? GLU A 238 ASN A 253 1 ? 16 
HELX_P HELX_P10 AB1 TYR A 263 ? LYS A 272 ? TYR A 262 LYS A 271 1 ? 10 
HELX_P HELX_P11 AB2 GLY B 48  ? GLN B 60  ? GLY B 47  GLN B 59  1 ? 13 
HELX_P HELX_P12 AB3 ASN B 70  ? LYS B 83  ? ASN B 69  LYS B 82  1 ? 14 
HELX_P HELX_P13 AB4 ASN B 97  ? LYS B 110 ? ASN B 96  LYS B 109 1 ? 14 
HELX_P HELX_P14 AB5 LYS B 134 ? ILE B 146 ? LYS B 133 ILE B 145 1 ? 13 
HELX_P HELX_P15 AB6 ILE B 146 ? ASN B 164 ? ILE B 145 ASN B 163 1 ? 19 
HELX_P HELX_P16 AB7 SER B 173 ? HIS B 177 ? SER B 172 HIS B 176 5 ? 5  
HELX_P HELX_P17 AB8 LEU B 183 ? LEU B 207 ? LEU B 182 LEU B 206 1 ? 25 
HELX_P HELX_P18 AB9 GLU B 239 ? ASN B 254 ? GLU B 238 ASN B 253 1 ? 16 
HELX_P HELX_P19 AC1 TYR B 263 ? LYS B 272 ? TYR B 262 LYS B 271 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 VAL 260 A . ? VAL 259 A PRO 261 A ? PRO 260 A 1 -5.74 
2 VAL 260 B . ? VAL 259 B PRO 261 B ? PRO 260 B 1 5.19  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 2 ? 
AA3 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? parallel 
AA2 1 2 ? parallel 
AA3 1 2 ? parallel 
AA3 2 3 ? parallel 
AA3 3 4 ? parallel 
AA3 4 5 ? parallel 
AA3 5 6 ? parallel 
AA3 6 7 ? parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 87  ? VAL A 92  ? THR A 86  VAL A 91  
AA1 2 ARG A 63  ? ASP A 68  ? ARG A 62  ASP A 67  
AA1 3 ILE A 39  ? THR A 43  ? ILE A 38  THR A 42  
AA1 4 ILE A 117 ? ASN A 120 ? ILE A 116 ASN A 119 
AA1 5 GLY A 166 ? VAL A 171 ? GLY A 165 VAL A 170 
AA1 6 ILE A 212 ? PRO A 219 ? ILE A 211 PRO A 218 
AA1 7 MET A 257 ? VAL A 260 ? MET A 256 VAL A 259 
AA2 1 PHE A 221 ? VAL A 222 ? PHE A 220 VAL A 221 
AA2 2 VAL A 237 ? LEU A 238 ? VAL A 236 LEU A 237 
AA3 1 THR B 87  ? VAL B 92  ? THR B 86  VAL B 91  
AA3 2 ARG B 63  ? ASP B 68  ? ARG B 62  ASP B 67  
AA3 3 ILE B 39  ? THR B 43  ? ILE B 38  THR B 42  
AA3 4 ILE B 117 ? ASN B 120 ? ILE B 116 ASN B 119 
AA3 5 GLY B 166 ? VAL B 171 ? GLY B 165 VAL B 170 
AA3 6 ILE B 212 ? PRO B 219 ? ILE B 211 PRO B 218 
AA3 7 MET B 257 ? VAL B 260 ? MET B 256 VAL B 259 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O PHE A 91  ? O PHE A 90  N LEU A 66  ? N LEU A 65  
AA1 2 3 O VAL A 65  ? O VAL A 64  N ILE A 42  ? N ILE A 41  
AA1 3 4 N LEU A 41  ? N LEU A 40  O ILE A 117 ? O ILE A 116 
AA1 4 5 N LEU A 118 ? N LEU A 117 O VAL A 169 ? O VAL A 168 
AA1 5 6 N THR A 170 ? N THR A 169 O SER A 215 ? O SER A 214 
AA1 6 7 N CYS A 216 ? N CYS A 215 O ILE A 258 ? O ILE A 257 
AA2 1 2 N PHE A 221 ? N PHE A 220 O LEU A 238 ? O LEU A 237 
AA3 1 2 O HIS B 89  ? O HIS B 88  N LEU B 66  ? N LEU B 65  
AA3 2 3 O VAL B 65  ? O VAL B 64  N VAL B 40  ? N VAL B 39  
AA3 3 4 N LEU B 41  ? N LEU B 40  O ILE B 117 ? O ILE B 116 
AA3 4 5 N ASN B 120 ? N ASN B 119 O VAL B 169 ? O VAL B 168 
AA3 5 6 N THR B 170 ? N THR B 169 O SER B 215 ? O SER B 214 
AA3 6 7 N CYS B 216 ? N CYS B 215 O ILE B 258 ? O ILE B 257 
# 
_pdbx_entry_details.entry_id                   9AV8 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 VAL A 25  ? ? -121.94 -52.58  
2  1 CYS A 94  ? ? -71.85  21.41   
3  1 GLU A 110 ? ? -133.11 -54.11  
4  1 ALA A 121 ? ? -27.33  138.47  
5  1 ILE A 145 ? ? -142.06 -41.43  
6  1 HIS A 166 ? ? -167.80 114.35  
7  1 ALA A 171 ? ? -121.15 -167.33 
8  1 CYS A 174 ? ? -68.90  8.46    
9  1 TYR A 181 ? ? 75.46   -20.80  
10 1 VAL A 219 ? ? -92.04  -142.37 
11 1 SER A 261 ? ? -19.88  -39.65  
12 1 LYS A 271 ? ? -89.04  41.93   
13 1 ARG B 29  ? ? -32.20  140.59  
14 1 CYS B 94  ? ? -71.98  21.46   
15 1 GLU B 110 ? ? -132.58 -53.27  
16 1 ALA B 121 ? ? -27.61  137.97  
17 1 ILE B 145 ? ? -142.84 -41.41  
18 1 HIS B 166 ? ? -167.74 113.93  
19 1 TYR B 181 ? ? 75.47   -20.28  
20 1 VAL B 219 ? ? -92.81  -143.98 
21 1 VAL B 236 ? ? 53.91   111.51  
22 1 LYS B 271 ? ? -89.08  42.49   
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? ? 37.0312 29.8163 60.2259 0.1077 ? 0.0999  ? -0.348  ? 0.2311 ? 0.0148 ? -0.378 ? 2.1645 ? -0.3617 ? 
-1.2874 ? 1.3163 ? 0.2531 ? 4.5829 ? 0.3338 ? -0.0499 ? 0.4427 ? -0.0499 ? -0.2635 ? 0.391   ? 0.4427 ? 0.391   ? -0.0704 ? 
2 'X-RAY DIFFRACTION' ? ? 19.1326 32.1811 84.7925 0.2105 ? -0.2832 ? -0.2415 ? 0.2155 ? 0.1793 ? -0.446 ? 3.249  ? -0.6337 ? 
-1.415  ? 2.2374 ? 0.2093 ? 2.9498 ? 0.3239 ? 0.3243  ? 0.3029 ? 0.3243  ? -0.2051 ? -0.2697 ? 0.3029 ? -0.2697 ? -0.1189 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 1   ? ? ? A 273 ? ? '{ A|* }' 
2 'X-RAY DIFFRACTION' 1 ? ? A 296 ? ? ? A 301 ? ? '{ A|* }' 
3 'X-RAY DIFFRACTION' 2 ? ? B 25  ? ? ? B 272 ? ? '{ B|* }' 
4 'X-RAY DIFFRACTION' 2 ? ? B 296 ? ? ? B 296 ? ? '{ B|* }' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1  1 O ? A HOH 554 ? 6.48  . 
2  1 O ? A HOH 555 ? 6.52  . 
3  1 O ? A HOH 556 ? 6.54  . 
4  1 O ? A HOH 557 ? 6.57  . 
5  1 O ? A HOH 558 ? 6.63  . 
6  1 O ? A HOH 559 ? 7.36  . 
7  1 O ? A HOH 560 ? 7.39  . 
8  1 O ? A HOH 561 ? 9.14  . 
9  1 O ? A HOH 562 ? 9.82  . 
10 1 O ? A HOH 563 ? 10.95 . 
11 1 O ? A HOH 564 ? 11.14 . 
12 1 O ? A HOH 565 ? 11.41 . 
13 1 O ? A HOH 566 ? 11.43 . 
14 1 O ? A HOH 567 ? 11.91 . 
15 1 O ? A HOH 568 ? 12.85 . 
16 1 O ? A HOH 569 ? 12.87 . 
17 1 O ? A HOH 570 ? 13.08 . 
18 1 O ? A HOH 571 ? 13.24 . 
19 1 O ? A HOH 572 ? 13.82 . 
20 1 O ? A HOH 573 ? 18.37 . 
21 1 O ? A HOH 574 ? 19.47 . 
22 1 O ? A HOH 575 ? 20.43 . 
23 1 O ? B HOH 554 ? 6.12  . 
24 1 O ? B HOH 555 ? 6.87  . 
25 1 O ? B HOH 556 ? 6.88  . 
26 1 O ? B HOH 557 ? 7.15  . 
27 1 O ? B HOH 558 ? 7.51  . 
28 1 O ? B HOH 559 ? 7.68  . 
29 1 O ? B HOH 560 ? 7.87  . 
30 1 O ? B HOH 561 ? 11.32 . 
31 1 O ? B HOH 562 ? 13.59 . 
32 1 O ? B HOH 563 ? 17.98 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 0   ? A MET 1   
2   1 Y 1 A LEU 233 ? A LEU 234 
3   1 Y 1 A TRP 234 ? A TRP 235 
4   1 Y 1 A PRO 274 ? A PRO 275 
5   1 Y 1 A GLU 275 ? A GLU 276 
6   1 Y 1 A ARG 276 ? A ARG 277 
7   1 Y 1 A ALA 277 ? A ALA 278 
8   1 Y 1 A LEU 278 ? A LEU 279 
9   1 Y 1 A ALA 279 ? A ALA 280 
10  1 Y 1 A ALA 280 ? A ALA 281 
11  1 Y 1 A ILE 281 ? A ILE 282 
12  1 Y 1 A ASN 282 ? A ASN 283 
13  1 Y 1 A HIS 283 ? A HIS 284 
14  1 Y 1 A LEU 284 ? A LEU 285 
15  1 Y 1 A GLN 285 ? A GLN 286 
16  1 Y 1 A ASN 286 ? A ASN 287 
17  1 Y 1 A ILE 287 ? A ILE 288 
18  1 Y 1 A GLN 288 ? A GLN 289 
19  1 Y 1 A PHE 289 ? A PHE 290 
20  1 Y 1 A GLU 290 ? A GLU 291 
21  1 Y 1 A ALA 291 ? A ALA 292 
22  1 Y 1 A VAL 292 ? A VAL 293 
23  1 Y 1 A VAL 293 ? A VAL 294 
24  1 Y 1 A GLY 294 ? A GLY 295 
25  1 Y 1 A HIS 295 ? A HIS 296 
26  1 Y 1 A LYS 296 ? A LYS 297 
27  1 Y 1 A THR 297 ? A THR 298 
28  1 Y 1 A ARG 298 ? A ARG 299 
29  1 Y 1 A MET 299 ? A MET 300 
30  1 Y 1 A LYS 300 ? A LYS 301 
31  1 Y 1 A GLY 301 ? A GLY 302 
32  1 Y 1 A SER 302 ? A SER 303 
33  1 Y 1 A GLY 303 ? A GLY 304 
34  1 Y 1 A HIS 304 ? A HIS 305 
35  1 Y 1 A HIS 305 ? A HIS 306 
36  1 Y 1 A HIS 306 ? A HIS 307 
37  1 Y 1 A HIS 307 ? A HIS 308 
38  1 Y 1 A HIS 308 ? A HIS 309 
39  1 Y 1 A HIS 309 ? A HIS 310 
40  1 Y 1 A HIS 310 ? A HIS 311 
41  1 Y 1 A HIS 311 ? A HIS 312 
42  1 Y 1 A HIS 312 ? A HIS 313 
43  1 Y 1 A HIS 313 ? A HIS 314 
44  1 Y 1 A HIS 314 ? A HIS 315 
45  1 Y 1 B MET 0   ? B MET 1   
46  1 Y 1 B GLY 1   ? B GLY 2   
47  1 Y 1 B ASN 2   ? B ASN 3   
48  1 Y 1 B ILE 3   ? B ILE 4   
49  1 Y 1 B ILE 4   ? B ILE 5   
50  1 Y 1 B LEU 5   ? B LEU 6   
51  1 Y 1 B ASP 6   ? B ASP 7   
52  1 Y 1 B LEU 7   ? B LEU 8   
53  1 Y 1 B LEU 8   ? B LEU 9   
54  1 Y 1 B LEU 9   ? B LEU 10  
55  1 Y 1 B LEU 10  ? B LEU 11  
56  1 Y 1 B LEU 11  ? B LEU 12  
57  1 Y 1 B LEU 12  ? B LEU 13  
58  1 Y 1 B THR 13  ? B THR 14  
59  1 Y 1 B ILE 14  ? B ILE 15  
60  1 Y 1 B ILE 15  ? B ILE 16  
61  1 Y 1 B TYR 16  ? B TYR 17  
62  1 Y 1 B SER 17  ? B SER 18  
63  1 Y 1 B TYR 18  ? B TYR 19  
64  1 Y 1 B LEU 19  ? B LEU 20  
65  1 Y 1 B GLU 20  ? B GLU 21  
66  1 Y 1 B ALA 21  ? B ALA 22  
67  1 Y 1 B LEU 22  ? B LEU 23  
68  1 Y 1 B VAL 23  ? B VAL 24  
69  1 Y 1 B LYS 24  ? B LYS 25  
70  1 Y 1 B THR 231 ? B THR 232 
71  1 Y 1 B ARG 232 ? B ARG 233 
72  1 Y 1 B LEU 233 ? B LEU 234 
73  1 Y 1 B TRP 234 ? B TRP 235 
74  1 Y 1 B LEU 273 ? B LEU 274 
75  1 Y 1 B PRO 274 ? B PRO 275 
76  1 Y 1 B GLU 275 ? B GLU 276 
77  1 Y 1 B ARG 276 ? B ARG 277 
78  1 Y 1 B ALA 277 ? B ALA 278 
79  1 Y 1 B LEU 278 ? B LEU 279 
80  1 Y 1 B ALA 279 ? B ALA 280 
81  1 Y 1 B ALA 280 ? B ALA 281 
82  1 Y 1 B ILE 281 ? B ILE 282 
83  1 Y 1 B ASN 282 ? B ASN 283 
84  1 Y 1 B HIS 283 ? B HIS 284 
85  1 Y 1 B LEU 284 ? B LEU 285 
86  1 Y 1 B GLN 285 ? B GLN 286 
87  1 Y 1 B ASN 286 ? B ASN 287 
88  1 Y 1 B ILE 287 ? B ILE 288 
89  1 Y 1 B GLN 288 ? B GLN 289 
90  1 Y 1 B PHE 289 ? B PHE 290 
91  1 Y 1 B GLU 290 ? B GLU 291 
92  1 Y 1 B ALA 291 ? B ALA 292 
93  1 Y 1 B VAL 292 ? B VAL 293 
94  1 Y 1 B VAL 293 ? B VAL 294 
95  1 Y 1 B GLY 294 ? B GLY 295 
96  1 Y 1 B HIS 295 ? B HIS 296 
97  1 Y 1 B LYS 296 ? B LYS 297 
98  1 Y 1 B THR 297 ? B THR 298 
99  1 Y 1 B ARG 298 ? B ARG 299 
100 1 Y 1 B MET 299 ? B MET 300 
101 1 Y 1 B LYS 300 ? B LYS 301 
102 1 Y 1 B GLY 301 ? B GLY 302 
103 1 Y 1 B SER 302 ? B SER 303 
104 1 Y 1 B GLY 303 ? B GLY 304 
105 1 Y 1 B HIS 304 ? B HIS 305 
106 1 Y 1 B HIS 305 ? B HIS 306 
107 1 Y 1 B HIS 306 ? B HIS 307 
108 1 Y 1 B HIS 307 ? B HIS 308 
109 1 Y 1 B HIS 308 ? B HIS 309 
110 1 Y 1 B HIS 309 ? B HIS 310 
111 1 Y 1 B HIS 310 ? B HIS 311 
112 1 Y 1 B HIS 311 ? B HIS 312 
113 1 Y 1 B HIS 312 ? B HIS 313 
114 1 Y 1 B HIS 313 ? B HIS 314 
115 1 Y 1 B HIS 314 ? B HIS 315 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AG6 C4   C  Y N 1   
A1AG6 N2   N  Y N 2   
A1AG6 C7   C  Y N 3   
A1AG6 C6   C  Y N 4   
A1AG6 C9   C  Y N 5   
A1AG6 C20  C  Y N 6   
A1AG6 C8   C  Y N 7   
A1AG6 C18  C  Y N 8   
A1AG6 C16  C  Y N 9   
A1AG6 C19  C  Y N 10  
A1AG6 C26  C  N N 11  
A1AG6 C1   C  N N 12  
A1AG6 C3   C  Y N 13  
A1AG6 C5   C  Y N 14  
A1AG6 N10  N  Y N 15  
A1AG6 N11  N  N N 16  
A1AG6 S12  S  N N 17  
A1AG6 O13  O  N N 18  
A1AG6 O14  O  N N 19  
A1AG6 C15  C  Y N 20  
A1AG6 C17  C  Y N 21  
A1AG6 CL21 CL N N 22  
A1AG6 C28  C  N N 23  
A1AG6 O29  O  N N 24  
A1AG6 O30  O  N N 25  
A1AG6 O22  O  N N 26  
A1AG6 C23  C  N N 27  
A1AG6 C24  C  N N 28  
A1AG6 C25  C  N N 29  
A1AG6 C27  C  N N 30  
A1AG6 H36  H  N N 31  
A1AG6 H35  H  N N 32  
A1AG6 H40  H  N N 33  
A1AG6 H38  H  N N 34  
A1AG6 H46  H  N N 35  
A1AG6 H47  H  N N 36  
A1AG6 H33  H  N N 37  
A1AG6 H32  H  N N 38  
A1AG6 H31  H  N N 39  
A1AG6 H34  H  N N 40  
A1AG6 H37  H  N N 41  
A1AG6 H39  H  N N 42  
A1AG6 H50  H  N N 43  
A1AG6 H42  H  N N 44  
A1AG6 H41  H  N N 45  
A1AG6 H43  H  N N 46  
A1AG6 H44  H  N N 47  
A1AG6 H45  H  N N 48  
A1AG6 H49  H  N N 49  
A1AG6 H48  H  N N 50  
ALA   N    N  N N 51  
ALA   CA   C  N S 52  
ALA   C    C  N N 53  
ALA   O    O  N N 54  
ALA   CB   C  N N 55  
ALA   OXT  O  N N 56  
ALA   H    H  N N 57  
ALA   H2   H  N N 58  
ALA   HA   H  N N 59  
ALA   HB1  H  N N 60  
ALA   HB2  H  N N 61  
ALA   HB3  H  N N 62  
ALA   HXT  H  N N 63  
ARG   N    N  N N 64  
ARG   CA   C  N S 65  
ARG   C    C  N N 66  
ARG   O    O  N N 67  
ARG   CB   C  N N 68  
ARG   CG   C  N N 69  
ARG   CD   C  N N 70  
ARG   NE   N  N N 71  
ARG   CZ   C  N N 72  
ARG   NH1  N  N N 73  
ARG   NH2  N  N N 74  
ARG   OXT  O  N N 75  
ARG   H    H  N N 76  
ARG   H2   H  N N 77  
ARG   HA   H  N N 78  
ARG   HB2  H  N N 79  
ARG   HB3  H  N N 80  
ARG   HG2  H  N N 81  
ARG   HG3  H  N N 82  
ARG   HD2  H  N N 83  
ARG   HD3  H  N N 84  
ARG   HE   H  N N 85  
ARG   HH11 H  N N 86  
ARG   HH12 H  N N 87  
ARG   HH21 H  N N 88  
ARG   HH22 H  N N 89  
ARG   HXT  H  N N 90  
ASN   N    N  N N 91  
ASN   CA   C  N S 92  
ASN   C    C  N N 93  
ASN   O    O  N N 94  
ASN   CB   C  N N 95  
ASN   CG   C  N N 96  
ASN   OD1  O  N N 97  
ASN   ND2  N  N N 98  
ASN   OXT  O  N N 99  
ASN   H    H  N N 100 
ASN   H2   H  N N 101 
ASN   HA   H  N N 102 
ASN   HB2  H  N N 103 
ASN   HB3  H  N N 104 
ASN   HD21 H  N N 105 
ASN   HD22 H  N N 106 
ASN   HXT  H  N N 107 
ASP   N    N  N N 108 
ASP   CA   C  N S 109 
ASP   C    C  N N 110 
ASP   O    O  N N 111 
ASP   CB   C  N N 112 
ASP   CG   C  N N 113 
ASP   OD1  O  N N 114 
ASP   OD2  O  N N 115 
ASP   OXT  O  N N 116 
ASP   H    H  N N 117 
ASP   H2   H  N N 118 
ASP   HA   H  N N 119 
ASP   HB2  H  N N 120 
ASP   HB3  H  N N 121 
ASP   HD2  H  N N 122 
ASP   HXT  H  N N 123 
CYS   N    N  N N 124 
CYS   CA   C  N R 125 
CYS   C    C  N N 126 
CYS   O    O  N N 127 
CYS   CB   C  N N 128 
CYS   SG   S  N N 129 
CYS   OXT  O  N N 130 
CYS   H    H  N N 131 
CYS   H2   H  N N 132 
CYS   HA   H  N N 133 
CYS   HB2  H  N N 134 
CYS   HB3  H  N N 135 
CYS   HG   H  N N 136 
CYS   HXT  H  N N 137 
GLN   N    N  N N 138 
GLN   CA   C  N S 139 
GLN   C    C  N N 140 
GLN   O    O  N N 141 
GLN   CB   C  N N 142 
GLN   CG   C  N N 143 
GLN   CD   C  N N 144 
GLN   OE1  O  N N 145 
GLN   NE2  N  N N 146 
GLN   OXT  O  N N 147 
GLN   H    H  N N 148 
GLN   H2   H  N N 149 
GLN   HA   H  N N 150 
GLN   HB2  H  N N 151 
GLN   HB3  H  N N 152 
GLN   HG2  H  N N 153 
GLN   HG3  H  N N 154 
GLN   HE21 H  N N 155 
GLN   HE22 H  N N 156 
GLN   HXT  H  N N 157 
GLU   N    N  N N 158 
GLU   CA   C  N S 159 
GLU   C    C  N N 160 
GLU   O    O  N N 161 
GLU   CB   C  N N 162 
GLU   CG   C  N N 163 
GLU   CD   C  N N 164 
GLU   OE1  O  N N 165 
GLU   OE2  O  N N 166 
GLU   OXT  O  N N 167 
GLU   H    H  N N 168 
GLU   H2   H  N N 169 
GLU   HA   H  N N 170 
GLU   HB2  H  N N 171 
GLU   HB3  H  N N 172 
GLU   HG2  H  N N 173 
GLU   HG3  H  N N 174 
GLU   HE2  H  N N 175 
GLU   HXT  H  N N 176 
GLY   N    N  N N 177 
GLY   CA   C  N N 178 
GLY   C    C  N N 179 
GLY   O    O  N N 180 
GLY   OXT  O  N N 181 
GLY   H    H  N N 182 
GLY   H2   H  N N 183 
GLY   HA2  H  N N 184 
GLY   HA3  H  N N 185 
GLY   HXT  H  N N 186 
HIS   N    N  N N 187 
HIS   CA   C  N S 188 
HIS   C    C  N N 189 
HIS   O    O  N N 190 
HIS   CB   C  N N 191 
HIS   CG   C  Y N 192 
HIS   ND1  N  Y N 193 
HIS   CD2  C  Y N 194 
HIS   CE1  C  Y N 195 
HIS   NE2  N  Y N 196 
HIS   OXT  O  N N 197 
HIS   H    H  N N 198 
HIS   H2   H  N N 199 
HIS   HA   H  N N 200 
HIS   HB2  H  N N 201 
HIS   HB3  H  N N 202 
HIS   HD1  H  N N 203 
HIS   HD2  H  N N 204 
HIS   HE1  H  N N 205 
HIS   HE2  H  N N 206 
HIS   HXT  H  N N 207 
HOH   O    O  N N 208 
HOH   H1   H  N N 209 
HOH   H2   H  N N 210 
ILE   N    N  N N 211 
ILE   CA   C  N S 212 
ILE   C    C  N N 213 
ILE   O    O  N N 214 
ILE   CB   C  N S 215 
ILE   CG1  C  N N 216 
ILE   CG2  C  N N 217 
ILE   CD1  C  N N 218 
ILE   OXT  O  N N 219 
ILE   H    H  N N 220 
ILE   H2   H  N N 221 
ILE   HA   H  N N 222 
ILE   HB   H  N N 223 
ILE   HG12 H  N N 224 
ILE   HG13 H  N N 225 
ILE   HG21 H  N N 226 
ILE   HG22 H  N N 227 
ILE   HG23 H  N N 228 
ILE   HD11 H  N N 229 
ILE   HD12 H  N N 230 
ILE   HD13 H  N N 231 
ILE   HXT  H  N N 232 
LEU   N    N  N N 233 
LEU   CA   C  N S 234 
LEU   C    C  N N 235 
LEU   O    O  N N 236 
LEU   CB   C  N N 237 
LEU   CG   C  N N 238 
LEU   CD1  C  N N 239 
LEU   CD2  C  N N 240 
LEU   OXT  O  N N 241 
LEU   H    H  N N 242 
LEU   H2   H  N N 243 
LEU   HA   H  N N 244 
LEU   HB2  H  N N 245 
LEU   HB3  H  N N 246 
LEU   HG   H  N N 247 
LEU   HD11 H  N N 248 
LEU   HD12 H  N N 249 
LEU   HD13 H  N N 250 
LEU   HD21 H  N N 251 
LEU   HD22 H  N N 252 
LEU   HD23 H  N N 253 
LEU   HXT  H  N N 254 
LYS   N    N  N N 255 
LYS   CA   C  N S 256 
LYS   C    C  N N 257 
LYS   O    O  N N 258 
LYS   CB   C  N N 259 
LYS   CG   C  N N 260 
LYS   CD   C  N N 261 
LYS   CE   C  N N 262 
LYS   NZ   N  N N 263 
LYS   OXT  O  N N 264 
LYS   H    H  N N 265 
LYS   H2   H  N N 266 
LYS   HA   H  N N 267 
LYS   HB2  H  N N 268 
LYS   HB3  H  N N 269 
LYS   HG2  H  N N 270 
LYS   HG3  H  N N 271 
LYS   HD2  H  N N 272 
LYS   HD3  H  N N 273 
LYS   HE2  H  N N 274 
LYS   HE3  H  N N 275 
LYS   HZ1  H  N N 276 
LYS   HZ2  H  N N 277 
LYS   HZ3  H  N N 278 
LYS   HXT  H  N N 279 
MET   N    N  N N 280 
MET   CA   C  N S 281 
MET   C    C  N N 282 
MET   O    O  N N 283 
MET   CB   C  N N 284 
MET   CG   C  N N 285 
MET   SD   S  N N 286 
MET   CE   C  N N 287 
MET   OXT  O  N N 288 
MET   H    H  N N 289 
MET   H2   H  N N 290 
MET   HA   H  N N 291 
MET   HB2  H  N N 292 
MET   HB3  H  N N 293 
MET   HG2  H  N N 294 
MET   HG3  H  N N 295 
MET   HE1  H  N N 296 
MET   HE2  H  N N 297 
MET   HE3  H  N N 298 
MET   HXT  H  N N 299 
NAD   PA   P  N S 300 
NAD   O1A  O  N N 301 
NAD   O2A  O  N N 302 
NAD   O5B  O  N N 303 
NAD   C5B  C  N N 304 
NAD   C4B  C  N R 305 
NAD   O4B  O  N N 306 
NAD   C3B  C  N S 307 
NAD   O3B  O  N N 308 
NAD   C2B  C  N R 309 
NAD   O2B  O  N N 310 
NAD   C1B  C  N R 311 
NAD   N9A  N  Y N 312 
NAD   C8A  C  Y N 313 
NAD   N7A  N  Y N 314 
NAD   C5A  C  Y N 315 
NAD   C6A  C  Y N 316 
NAD   N6A  N  N N 317 
NAD   N1A  N  Y N 318 
NAD   C2A  C  Y N 319 
NAD   N3A  N  Y N 320 
NAD   C4A  C  Y N 321 
NAD   O3   O  N N 322 
NAD   PN   P  N N 323 
NAD   O1N  O  N N 324 
NAD   O2N  O  N N 325 
NAD   O5D  O  N N 326 
NAD   C5D  C  N N 327 
NAD   C4D  C  N R 328 
NAD   O4D  O  N N 329 
NAD   C3D  C  N S 330 
NAD   O3D  O  N N 331 
NAD   C2D  C  N R 332 
NAD   O2D  O  N N 333 
NAD   C1D  C  N R 334 
NAD   N1N  N  Y N 335 
NAD   C2N  C  Y N 336 
NAD   C3N  C  Y N 337 
NAD   C7N  C  N N 338 
NAD   O7N  O  N N 339 
NAD   N7N  N  N N 340 
NAD   C4N  C  Y N 341 
NAD   C5N  C  Y N 342 
NAD   C6N  C  Y N 343 
NAD   HOA2 H  N N 344 
NAD   H51A H  N N 345 
NAD   H52A H  N N 346 
NAD   H4B  H  N N 347 
NAD   H3B  H  N N 348 
NAD   HO3A H  N N 349 
NAD   H2B  H  N N 350 
NAD   HO2A H  N N 351 
NAD   H1B  H  N N 352 
NAD   H8A  H  N N 353 
NAD   H61A H  N N 354 
NAD   H62A H  N N 355 
NAD   H2A  H  N N 356 
NAD   H51N H  N N 357 
NAD   H52N H  N N 358 
NAD   H4D  H  N N 359 
NAD   H3D  H  N N 360 
NAD   HO3N H  N N 361 
NAD   H2D  H  N N 362 
NAD   HO2N H  N N 363 
NAD   H1D  H  N N 364 
NAD   H2N  H  N N 365 
NAD   H71N H  N N 366 
NAD   H72N H  N N 367 
NAD   H4N  H  N N 368 
NAD   H5N  H  N N 369 
NAD   H6N  H  N N 370 
PHE   N    N  N N 371 
PHE   CA   C  N S 372 
PHE   C    C  N N 373 
PHE   O    O  N N 374 
PHE   CB   C  N N 375 
PHE   CG   C  Y N 376 
PHE   CD1  C  Y N 377 
PHE   CD2  C  Y N 378 
PHE   CE1  C  Y N 379 
PHE   CE2  C  Y N 380 
PHE   CZ   C  Y N 381 
PHE   OXT  O  N N 382 
PHE   H    H  N N 383 
PHE   H2   H  N N 384 
PHE   HA   H  N N 385 
PHE   HB2  H  N N 386 
PHE   HB3  H  N N 387 
PHE   HD1  H  N N 388 
PHE   HD2  H  N N 389 
PHE   HE1  H  N N 390 
PHE   HE2  H  N N 391 
PHE   HZ   H  N N 392 
PHE   HXT  H  N N 393 
PRO   N    N  N N 394 
PRO   CA   C  N S 395 
PRO   C    C  N N 396 
PRO   O    O  N N 397 
PRO   CB   C  N N 398 
PRO   CG   C  N N 399 
PRO   CD   C  N N 400 
PRO   OXT  O  N N 401 
PRO   H    H  N N 402 
PRO   HA   H  N N 403 
PRO   HB2  H  N N 404 
PRO   HB3  H  N N 405 
PRO   HG2  H  N N 406 
PRO   HG3  H  N N 407 
PRO   HD2  H  N N 408 
PRO   HD3  H  N N 409 
PRO   HXT  H  N N 410 
SER   N    N  N N 411 
SER   CA   C  N S 412 
SER   C    C  N N 413 
SER   O    O  N N 414 
SER   CB   C  N N 415 
SER   OG   O  N N 416 
SER   OXT  O  N N 417 
SER   H    H  N N 418 
SER   H2   H  N N 419 
SER   HA   H  N N 420 
SER   HB2  H  N N 421 
SER   HB3  H  N N 422 
SER   HG   H  N N 423 
SER   HXT  H  N N 424 
THR   N    N  N N 425 
THR   CA   C  N S 426 
THR   C    C  N N 427 
THR   O    O  N N 428 
THR   CB   C  N R 429 
THR   OG1  O  N N 430 
THR   CG2  C  N N 431 
THR   OXT  O  N N 432 
THR   H    H  N N 433 
THR   H2   H  N N 434 
THR   HA   H  N N 435 
THR   HB   H  N N 436 
THR   HG1  H  N N 437 
THR   HG21 H  N N 438 
THR   HG22 H  N N 439 
THR   HG23 H  N N 440 
THR   HXT  H  N N 441 
TRP   N    N  N N 442 
TRP   CA   C  N S 443 
TRP   C    C  N N 444 
TRP   O    O  N N 445 
TRP   CB   C  N N 446 
TRP   CG   C  Y N 447 
TRP   CD1  C  Y N 448 
TRP   CD2  C  Y N 449 
TRP   NE1  N  Y N 450 
TRP   CE2  C  Y N 451 
TRP   CE3  C  Y N 452 
TRP   CZ2  C  Y N 453 
TRP   CZ3  C  Y N 454 
TRP   CH2  C  Y N 455 
TRP   OXT  O  N N 456 
TRP   H    H  N N 457 
TRP   H2   H  N N 458 
TRP   HA   H  N N 459 
TRP   HB2  H  N N 460 
TRP   HB3  H  N N 461 
TRP   HD1  H  N N 462 
TRP   HE1  H  N N 463 
TRP   HE3  H  N N 464 
TRP   HZ2  H  N N 465 
TRP   HZ3  H  N N 466 
TRP   HH2  H  N N 467 
TRP   HXT  H  N N 468 
TYR   N    N  N N 469 
TYR   CA   C  N S 470 
TYR   C    C  N N 471 
TYR   O    O  N N 472 
TYR   CB   C  N N 473 
TYR   CG   C  Y N 474 
TYR   CD1  C  Y N 475 
TYR   CD2  C  Y N 476 
TYR   CE1  C  Y N 477 
TYR   CE2  C  Y N 478 
TYR   CZ   C  Y N 479 
TYR   OH   O  N N 480 
TYR   OXT  O  N N 481 
TYR   H    H  N N 482 
TYR   H2   H  N N 483 
TYR   HA   H  N N 484 
TYR   HB2  H  N N 485 
TYR   HB3  H  N N 486 
TYR   HD1  H  N N 487 
TYR   HD2  H  N N 488 
TYR   HE1  H  N N 489 
TYR   HE2  H  N N 490 
TYR   HH   H  N N 491 
TYR   HXT  H  N N 492 
VAL   N    N  N N 493 
VAL   CA   C  N S 494 
VAL   C    C  N N 495 
VAL   O    O  N N 496 
VAL   CB   C  N N 497 
VAL   CG1  C  N N 498 
VAL   CG2  C  N N 499 
VAL   OXT  O  N N 500 
VAL   H    H  N N 501 
VAL   H2   H  N N 502 
VAL   HA   H  N N 503 
VAL   HB   H  N N 504 
VAL   HG11 H  N N 505 
VAL   HG12 H  N N 506 
VAL   HG13 H  N N 507 
VAL   HG21 H  N N 508 
VAL   HG22 H  N N 509 
VAL   HG23 H  N N 510 
VAL   HXT  H  N N 511 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1AG6 C1  N2   sing N N 1   
A1AG6 N2  N10  sing Y N 2   
A1AG6 N2  C3   sing Y N 3   
A1AG6 C3  C4   doub Y N 4   
A1AG6 C4  C9   sing Y N 5   
A1AG6 C4  C5   sing Y N 6   
A1AG6 C5  C6   doub Y N 7   
A1AG6 C5  C28  sing N N 8   
A1AG6 C6  C7   sing Y N 9   
A1AG6 C7  C8   doub Y N 10  
A1AG6 C8  C9   sing Y N 11  
A1AG6 C8  N11  sing N N 12  
A1AG6 C9  N10  doub Y N 13  
A1AG6 N11 S12  sing N N 14  
A1AG6 S12 O13  doub N N 15  
A1AG6 S12 O14  doub N N 16  
A1AG6 S12 C15  sing N N 17  
A1AG6 C15 C20  doub Y N 18  
A1AG6 C15 C16  sing Y N 19  
A1AG6 C16 C17  doub Y N 20  
A1AG6 C17 C18  sing Y N 21  
A1AG6 C18 C19  doub Y N 22  
A1AG6 C18 O22  sing N N 23  
A1AG6 C19 C20  sing Y N 24  
A1AG6 C19 CL21 sing N N 25  
A1AG6 O22 C23  sing N N 26  
A1AG6 C23 C24  sing N N 27  
A1AG6 C24 C27  sing N N 28  
A1AG6 C24 C25  sing N N 29  
A1AG6 C25 C26  sing N N 30  
A1AG6 C26 C27  sing N N 31  
A1AG6 C28 O29  doub N N 32  
A1AG6 C28 O30  sing N N 33  
A1AG6 C7  H36  sing N N 34  
A1AG6 C6  H35  sing N N 35  
A1AG6 C20 H40  sing N N 36  
A1AG6 C16 H38  sing N N 37  
A1AG6 C26 H46  sing N N 38  
A1AG6 C26 H47  sing N N 39  
A1AG6 C1  H33  sing N N 40  
A1AG6 C1  H32  sing N N 41  
A1AG6 C1  H31  sing N N 42  
A1AG6 C3  H34  sing N N 43  
A1AG6 N11 H37  sing N N 44  
A1AG6 C17 H39  sing N N 45  
A1AG6 O30 H50  sing N N 46  
A1AG6 C23 H42  sing N N 47  
A1AG6 C23 H41  sing N N 48  
A1AG6 C24 H43  sing N N 49  
A1AG6 C25 H44  sing N N 50  
A1AG6 C25 H45  sing N N 51  
A1AG6 C27 H49  sing N N 52  
A1AG6 C27 H48  sing N N 53  
ALA   N   CA   sing N N 54  
ALA   N   H    sing N N 55  
ALA   N   H2   sing N N 56  
ALA   CA  C    sing N N 57  
ALA   CA  CB   sing N N 58  
ALA   CA  HA   sing N N 59  
ALA   C   O    doub N N 60  
ALA   C   OXT  sing N N 61  
ALA   CB  HB1  sing N N 62  
ALA   CB  HB2  sing N N 63  
ALA   CB  HB3  sing N N 64  
ALA   OXT HXT  sing N N 65  
ARG   N   CA   sing N N 66  
ARG   N   H    sing N N 67  
ARG   N   H2   sing N N 68  
ARG   CA  C    sing N N 69  
ARG   CA  CB   sing N N 70  
ARG   CA  HA   sing N N 71  
ARG   C   O    doub N N 72  
ARG   C   OXT  sing N N 73  
ARG   CB  CG   sing N N 74  
ARG   CB  HB2  sing N N 75  
ARG   CB  HB3  sing N N 76  
ARG   CG  CD   sing N N 77  
ARG   CG  HG2  sing N N 78  
ARG   CG  HG3  sing N N 79  
ARG   CD  NE   sing N N 80  
ARG   CD  HD2  sing N N 81  
ARG   CD  HD3  sing N N 82  
ARG   NE  CZ   sing N N 83  
ARG   NE  HE   sing N N 84  
ARG   CZ  NH1  sing N N 85  
ARG   CZ  NH2  doub N N 86  
ARG   NH1 HH11 sing N N 87  
ARG   NH1 HH12 sing N N 88  
ARG   NH2 HH21 sing N N 89  
ARG   NH2 HH22 sing N N 90  
ARG   OXT HXT  sing N N 91  
ASN   N   CA   sing N N 92  
ASN   N   H    sing N N 93  
ASN   N   H2   sing N N 94  
ASN   CA  C    sing N N 95  
ASN   CA  CB   sing N N 96  
ASN   CA  HA   sing N N 97  
ASN   C   O    doub N N 98  
ASN   C   OXT  sing N N 99  
ASN   CB  CG   sing N N 100 
ASN   CB  HB2  sing N N 101 
ASN   CB  HB3  sing N N 102 
ASN   CG  OD1  doub N N 103 
ASN   CG  ND2  sing N N 104 
ASN   ND2 HD21 sing N N 105 
ASN   ND2 HD22 sing N N 106 
ASN   OXT HXT  sing N N 107 
ASP   N   CA   sing N N 108 
ASP   N   H    sing N N 109 
ASP   N   H2   sing N N 110 
ASP   CA  C    sing N N 111 
ASP   CA  CB   sing N N 112 
ASP   CA  HA   sing N N 113 
ASP   C   O    doub N N 114 
ASP   C   OXT  sing N N 115 
ASP   CB  CG   sing N N 116 
ASP   CB  HB2  sing N N 117 
ASP   CB  HB3  sing N N 118 
ASP   CG  OD1  doub N N 119 
ASP   CG  OD2  sing N N 120 
ASP   OD2 HD2  sing N N 121 
ASP   OXT HXT  sing N N 122 
CYS   N   CA   sing N N 123 
CYS   N   H    sing N N 124 
CYS   N   H2   sing N N 125 
CYS   CA  C    sing N N 126 
CYS   CA  CB   sing N N 127 
CYS   CA  HA   sing N N 128 
CYS   C   O    doub N N 129 
CYS   C   OXT  sing N N 130 
CYS   CB  SG   sing N N 131 
CYS   CB  HB2  sing N N 132 
CYS   CB  HB3  sing N N 133 
CYS   SG  HG   sing N N 134 
CYS   OXT HXT  sing N N 135 
GLN   N   CA   sing N N 136 
GLN   N   H    sing N N 137 
GLN   N   H2   sing N N 138 
GLN   CA  C    sing N N 139 
GLN   CA  CB   sing N N 140 
GLN   CA  HA   sing N N 141 
GLN   C   O    doub N N 142 
GLN   C   OXT  sing N N 143 
GLN   CB  CG   sing N N 144 
GLN   CB  HB2  sing N N 145 
GLN   CB  HB3  sing N N 146 
GLN   CG  CD   sing N N 147 
GLN   CG  HG2  sing N N 148 
GLN   CG  HG3  sing N N 149 
GLN   CD  OE1  doub N N 150 
GLN   CD  NE2  sing N N 151 
GLN   NE2 HE21 sing N N 152 
GLN   NE2 HE22 sing N N 153 
GLN   OXT HXT  sing N N 154 
GLU   N   CA   sing N N 155 
GLU   N   H    sing N N 156 
GLU   N   H2   sing N N 157 
GLU   CA  C    sing N N 158 
GLU   CA  CB   sing N N 159 
GLU   CA  HA   sing N N 160 
GLU   C   O    doub N N 161 
GLU   C   OXT  sing N N 162 
GLU   CB  CG   sing N N 163 
GLU   CB  HB2  sing N N 164 
GLU   CB  HB3  sing N N 165 
GLU   CG  CD   sing N N 166 
GLU   CG  HG2  sing N N 167 
GLU   CG  HG3  sing N N 168 
GLU   CD  OE1  doub N N 169 
GLU   CD  OE2  sing N N 170 
GLU   OE2 HE2  sing N N 171 
GLU   OXT HXT  sing N N 172 
GLY   N   CA   sing N N 173 
GLY   N   H    sing N N 174 
GLY   N   H2   sing N N 175 
GLY   CA  C    sing N N 176 
GLY   CA  HA2  sing N N 177 
GLY   CA  HA3  sing N N 178 
GLY   C   O    doub N N 179 
GLY   C   OXT  sing N N 180 
GLY   OXT HXT  sing N N 181 
HIS   N   CA   sing N N 182 
HIS   N   H    sing N N 183 
HIS   N   H2   sing N N 184 
HIS   CA  C    sing N N 185 
HIS   CA  CB   sing N N 186 
HIS   CA  HA   sing N N 187 
HIS   C   O    doub N N 188 
HIS   C   OXT  sing N N 189 
HIS   CB  CG   sing N N 190 
HIS   CB  HB2  sing N N 191 
HIS   CB  HB3  sing N N 192 
HIS   CG  ND1  sing Y N 193 
HIS   CG  CD2  doub Y N 194 
HIS   ND1 CE1  doub Y N 195 
HIS   ND1 HD1  sing N N 196 
HIS   CD2 NE2  sing Y N 197 
HIS   CD2 HD2  sing N N 198 
HIS   CE1 NE2  sing Y N 199 
HIS   CE1 HE1  sing N N 200 
HIS   NE2 HE2  sing N N 201 
HIS   OXT HXT  sing N N 202 
HOH   O   H1   sing N N 203 
HOH   O   H2   sing N N 204 
ILE   N   CA   sing N N 205 
ILE   N   H    sing N N 206 
ILE   N   H2   sing N N 207 
ILE   CA  C    sing N N 208 
ILE   CA  CB   sing N N 209 
ILE   CA  HA   sing N N 210 
ILE   C   O    doub N N 211 
ILE   C   OXT  sing N N 212 
ILE   CB  CG1  sing N N 213 
ILE   CB  CG2  sing N N 214 
ILE   CB  HB   sing N N 215 
ILE   CG1 CD1  sing N N 216 
ILE   CG1 HG12 sing N N 217 
ILE   CG1 HG13 sing N N 218 
ILE   CG2 HG21 sing N N 219 
ILE   CG2 HG22 sing N N 220 
ILE   CG2 HG23 sing N N 221 
ILE   CD1 HD11 sing N N 222 
ILE   CD1 HD12 sing N N 223 
ILE   CD1 HD13 sing N N 224 
ILE   OXT HXT  sing N N 225 
LEU   N   CA   sing N N 226 
LEU   N   H    sing N N 227 
LEU   N   H2   sing N N 228 
LEU   CA  C    sing N N 229 
LEU   CA  CB   sing N N 230 
LEU   CA  HA   sing N N 231 
LEU   C   O    doub N N 232 
LEU   C   OXT  sing N N 233 
LEU   CB  CG   sing N N 234 
LEU   CB  HB2  sing N N 235 
LEU   CB  HB3  sing N N 236 
LEU   CG  CD1  sing N N 237 
LEU   CG  CD2  sing N N 238 
LEU   CG  HG   sing N N 239 
LEU   CD1 HD11 sing N N 240 
LEU   CD1 HD12 sing N N 241 
LEU   CD1 HD13 sing N N 242 
LEU   CD2 HD21 sing N N 243 
LEU   CD2 HD22 sing N N 244 
LEU   CD2 HD23 sing N N 245 
LEU   OXT HXT  sing N N 246 
LYS   N   CA   sing N N 247 
LYS   N   H    sing N N 248 
LYS   N   H2   sing N N 249 
LYS   CA  C    sing N N 250 
LYS   CA  CB   sing N N 251 
LYS   CA  HA   sing N N 252 
LYS   C   O    doub N N 253 
LYS   C   OXT  sing N N 254 
LYS   CB  CG   sing N N 255 
LYS   CB  HB2  sing N N 256 
LYS   CB  HB3  sing N N 257 
LYS   CG  CD   sing N N 258 
LYS   CG  HG2  sing N N 259 
LYS   CG  HG3  sing N N 260 
LYS   CD  CE   sing N N 261 
LYS   CD  HD2  sing N N 262 
LYS   CD  HD3  sing N N 263 
LYS   CE  NZ   sing N N 264 
LYS   CE  HE2  sing N N 265 
LYS   CE  HE3  sing N N 266 
LYS   NZ  HZ1  sing N N 267 
LYS   NZ  HZ2  sing N N 268 
LYS   NZ  HZ3  sing N N 269 
LYS   OXT HXT  sing N N 270 
MET   N   CA   sing N N 271 
MET   N   H    sing N N 272 
MET   N   H2   sing N N 273 
MET   CA  C    sing N N 274 
MET   CA  CB   sing N N 275 
MET   CA  HA   sing N N 276 
MET   C   O    doub N N 277 
MET   C   OXT  sing N N 278 
MET   CB  CG   sing N N 279 
MET   CB  HB2  sing N N 280 
MET   CB  HB3  sing N N 281 
MET   CG  SD   sing N N 282 
MET   CG  HG2  sing N N 283 
MET   CG  HG3  sing N N 284 
MET   SD  CE   sing N N 285 
MET   CE  HE1  sing N N 286 
MET   CE  HE2  sing N N 287 
MET   CE  HE3  sing N N 288 
MET   OXT HXT  sing N N 289 
NAD   PA  O1A  doub N N 290 
NAD   PA  O2A  sing N N 291 
NAD   PA  O5B  sing N N 292 
NAD   PA  O3   sing N N 293 
NAD   O2A HOA2 sing N N 294 
NAD   O5B C5B  sing N N 295 
NAD   C5B C4B  sing N N 296 
NAD   C5B H51A sing N N 297 
NAD   C5B H52A sing N N 298 
NAD   C4B O4B  sing N N 299 
NAD   C4B C3B  sing N N 300 
NAD   C4B H4B  sing N N 301 
NAD   O4B C1B  sing N N 302 
NAD   C3B O3B  sing N N 303 
NAD   C3B C2B  sing N N 304 
NAD   C3B H3B  sing N N 305 
NAD   O3B HO3A sing N N 306 
NAD   C2B O2B  sing N N 307 
NAD   C2B C1B  sing N N 308 
NAD   C2B H2B  sing N N 309 
NAD   O2B HO2A sing N N 310 
NAD   C1B N9A  sing N N 311 
NAD   C1B H1B  sing N N 312 
NAD   N9A C8A  sing Y N 313 
NAD   N9A C4A  sing Y N 314 
NAD   C8A N7A  doub Y N 315 
NAD   C8A H8A  sing N N 316 
NAD   N7A C5A  sing Y N 317 
NAD   C5A C6A  sing Y N 318 
NAD   C5A C4A  doub Y N 319 
NAD   C6A N6A  sing N N 320 
NAD   C6A N1A  doub Y N 321 
NAD   N6A H61A sing N N 322 
NAD   N6A H62A sing N N 323 
NAD   N1A C2A  sing Y N 324 
NAD   C2A N3A  doub Y N 325 
NAD   C2A H2A  sing N N 326 
NAD   N3A C4A  sing Y N 327 
NAD   O3  PN   sing N N 328 
NAD   PN  O1N  doub N N 329 
NAD   PN  O2N  sing N N 330 
NAD   PN  O5D  sing N N 331 
NAD   O5D C5D  sing N N 332 
NAD   C5D C4D  sing N N 333 
NAD   C5D H51N sing N N 334 
NAD   C5D H52N sing N N 335 
NAD   C4D O4D  sing N N 336 
NAD   C4D C3D  sing N N 337 
NAD   C4D H4D  sing N N 338 
NAD   O4D C1D  sing N N 339 
NAD   C3D O3D  sing N N 340 
NAD   C3D C2D  sing N N 341 
NAD   C3D H3D  sing N N 342 
NAD   O3D HO3N sing N N 343 
NAD   C2D O2D  sing N N 344 
NAD   C2D C1D  sing N N 345 
NAD   C2D H2D  sing N N 346 
NAD   O2D HO2N sing N N 347 
NAD   C1D N1N  sing N N 348 
NAD   C1D H1D  sing N N 349 
NAD   N1N C2N  sing Y N 350 
NAD   N1N C6N  doub Y N 351 
NAD   C2N C3N  doub Y N 352 
NAD   C2N H2N  sing N N 353 
NAD   C3N C7N  sing N N 354 
NAD   C3N C4N  sing Y N 355 
NAD   C7N O7N  doub N N 356 
NAD   C7N N7N  sing N N 357 
NAD   N7N H71N sing N N 358 
NAD   N7N H72N sing N N 359 
NAD   C4N C5N  doub Y N 360 
NAD   C4N H4N  sing N N 361 
NAD   C5N C6N  sing Y N 362 
NAD   C5N H5N  sing N N 363 
NAD   C6N H6N  sing N N 364 
PHE   N   CA   sing N N 365 
PHE   N   H    sing N N 366 
PHE   N   H2   sing N N 367 
PHE   CA  C    sing N N 368 
PHE   CA  CB   sing N N 369 
PHE   CA  HA   sing N N 370 
PHE   C   O    doub N N 371 
PHE   C   OXT  sing N N 372 
PHE   CB  CG   sing N N 373 
PHE   CB  HB2  sing N N 374 
PHE   CB  HB3  sing N N 375 
PHE   CG  CD1  doub Y N 376 
PHE   CG  CD2  sing Y N 377 
PHE   CD1 CE1  sing Y N 378 
PHE   CD1 HD1  sing N N 379 
PHE   CD2 CE2  doub Y N 380 
PHE   CD2 HD2  sing N N 381 
PHE   CE1 CZ   doub Y N 382 
PHE   CE1 HE1  sing N N 383 
PHE   CE2 CZ   sing Y N 384 
PHE   CE2 HE2  sing N N 385 
PHE   CZ  HZ   sing N N 386 
PHE   OXT HXT  sing N N 387 
PRO   N   CA   sing N N 388 
PRO   N   CD   sing N N 389 
PRO   N   H    sing N N 390 
PRO   CA  C    sing N N 391 
PRO   CA  CB   sing N N 392 
PRO   CA  HA   sing N N 393 
PRO   C   O    doub N N 394 
PRO   C   OXT  sing N N 395 
PRO   CB  CG   sing N N 396 
PRO   CB  HB2  sing N N 397 
PRO   CB  HB3  sing N N 398 
PRO   CG  CD   sing N N 399 
PRO   CG  HG2  sing N N 400 
PRO   CG  HG3  sing N N 401 
PRO   CD  HD2  sing N N 402 
PRO   CD  HD3  sing N N 403 
PRO   OXT HXT  sing N N 404 
SER   N   CA   sing N N 405 
SER   N   H    sing N N 406 
SER   N   H2   sing N N 407 
SER   CA  C    sing N N 408 
SER   CA  CB   sing N N 409 
SER   CA  HA   sing N N 410 
SER   C   O    doub N N 411 
SER   C   OXT  sing N N 412 
SER   CB  OG   sing N N 413 
SER   CB  HB2  sing N N 414 
SER   CB  HB3  sing N N 415 
SER   OG  HG   sing N N 416 
SER   OXT HXT  sing N N 417 
THR   N   CA   sing N N 418 
THR   N   H    sing N N 419 
THR   N   H2   sing N N 420 
THR   CA  C    sing N N 421 
THR   CA  CB   sing N N 422 
THR   CA  HA   sing N N 423 
THR   C   O    doub N N 424 
THR   C   OXT  sing N N 425 
THR   CB  OG1  sing N N 426 
THR   CB  CG2  sing N N 427 
THR   CB  HB   sing N N 428 
THR   OG1 HG1  sing N N 429 
THR   CG2 HG21 sing N N 430 
THR   CG2 HG22 sing N N 431 
THR   CG2 HG23 sing N N 432 
THR   OXT HXT  sing N N 433 
TRP   N   CA   sing N N 434 
TRP   N   H    sing N N 435 
TRP   N   H2   sing N N 436 
TRP   CA  C    sing N N 437 
TRP   CA  CB   sing N N 438 
TRP   CA  HA   sing N N 439 
TRP   C   O    doub N N 440 
TRP   C   OXT  sing N N 441 
TRP   CB  CG   sing N N 442 
TRP   CB  HB2  sing N N 443 
TRP   CB  HB3  sing N N 444 
TRP   CG  CD1  doub Y N 445 
TRP   CG  CD2  sing Y N 446 
TRP   CD1 NE1  sing Y N 447 
TRP   CD1 HD1  sing N N 448 
TRP   CD2 CE2  doub Y N 449 
TRP   CD2 CE3  sing Y N 450 
TRP   NE1 CE2  sing Y N 451 
TRP   NE1 HE1  sing N N 452 
TRP   CE2 CZ2  sing Y N 453 
TRP   CE3 CZ3  doub Y N 454 
TRP   CE3 HE3  sing N N 455 
TRP   CZ2 CH2  doub Y N 456 
TRP   CZ2 HZ2  sing N N 457 
TRP   CZ3 CH2  sing Y N 458 
TRP   CZ3 HZ3  sing N N 459 
TRP   CH2 HH2  sing N N 460 
TRP   OXT HXT  sing N N 461 
TYR   N   CA   sing N N 462 
TYR   N   H    sing N N 463 
TYR   N   H2   sing N N 464 
TYR   CA  C    sing N N 465 
TYR   CA  CB   sing N N 466 
TYR   CA  HA   sing N N 467 
TYR   C   O    doub N N 468 
TYR   C   OXT  sing N N 469 
TYR   CB  CG   sing N N 470 
TYR   CB  HB2  sing N N 471 
TYR   CB  HB3  sing N N 472 
TYR   CG  CD1  doub Y N 473 
TYR   CG  CD2  sing Y N 474 
TYR   CD1 CE1  sing Y N 475 
TYR   CD1 HD1  sing N N 476 
TYR   CD2 CE2  doub Y N 477 
TYR   CD2 HD2  sing N N 478 
TYR   CE1 CZ   doub Y N 479 
TYR   CE1 HE1  sing N N 480 
TYR   CE2 CZ   sing Y N 481 
TYR   CE2 HE2  sing N N 482 
TYR   CZ  OH   sing N N 483 
TYR   OH  HH   sing N N 484 
TYR   OXT HXT  sing N N 485 
VAL   N   CA   sing N N 486 
VAL   N   H    sing N N 487 
VAL   N   H2   sing N N 488 
VAL   CA  C    sing N N 489 
VAL   CA  CB   sing N N 490 
VAL   CA  HA   sing N N 491 
VAL   C   O    doub N N 492 
VAL   C   OXT  sing N N 493 
VAL   CB  CG1  sing N N 494 
VAL   CB  CG2  sing N N 495 
VAL   CB  HB   sing N N 496 
VAL   CG1 HG11 sing N N 497 
VAL   CG1 HG12 sing N N 498 
VAL   CG1 HG13 sing N N 499 
VAL   CG2 HG21 sing N N 500 
VAL   CG2 HG22 sing N N 501 
VAL   CG2 HG23 sing N N 502 
VAL   OXT HXT  sing N N 503 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9AV4 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9AV8 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.012873 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005398 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.015516 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
_atom_site.pdbx_tls_group_id 
ATOM   1    N  N    . GLY   A 1 2   ? 49.14  4.179  83.348  1 133.57 ? 1   GLY   A N    1 1 
ATOM   2    C  CA   . GLY   A 1 2   ? 47.956 3.353  83.54   1 134.06 ? 1   GLY   A CA   1 1 
ATOM   3    C  C    . GLY   A 1 2   ? 46.769 3.798  82.709  1 134.83 ? 1   GLY   A C    1 1 
ATOM   4    O  O    . GLY   A 1 2   ? 46.05  2.968  82.148  1 134.86 ? 1   GLY   A O    1 1 
ATOM   5    N  N    . ASN   A 1 3   ? 46.557 5.116  82.614  1 135.56 ? 2   ASN   A N    1 1 
ATOM   6    C  CA   . ASN   A 1 3   ? 45.45  5.679  81.838  1 136.62 ? 2   ASN   A CA   1 1 
ATOM   7    C  C    . ASN   A 1 3   ? 45.6   5.468  80.318  1 137.49 ? 2   ASN   A C    1 1 
ATOM   8    O  O    . ASN   A 1 3   ? 44.624 5.617  79.586  1 137.68 ? 2   ASN   A O    1 1 
ATOM   9    C  CB   . ASN   A 1 3   ? 45.276 7.166  82.162  1 137.62 ? 2   ASN   A CB   1 1 
ATOM   10   C  CG   . ASN   A 1 3   ? 44.093 7.809  81.483  1 140.3  ? 2   ASN   A CG   1 1 
ATOM   11   O  OD1  . ASN   A 1 3   ? 42.97  7.303  81.538  1 141.37 ? 2   ASN   A OD1  1 1 
ATOM   12   N  ND2  . ASN   A 1 3   ? 44.327 8.923  80.805  1 140.7  ? 2   ASN   A ND2  1 1 
ATOM   13   N  N    . ILE   A 1 4   ? 46.806 5.111  79.847  1 137.87 ? 3   ILE   A N    1 1 
ATOM   14   C  CA   . ILE   A 1 4   ? 47.08  4.879  78.425  1 138.74 ? 3   ILE   A CA   1 1 
ATOM   15   C  C    . ILE   A 1 4   ? 46.368 3.6    77.893  1 139.49 ? 3   ILE   A C    1 1 
ATOM   16   O  O    . ILE   A 1 4   ? 46.072 3.51   76.698  1 139.63 ? 3   ILE   A O    1 1 
ATOM   17   C  CB   . ILE   A 1 4   ? 48.615 4.886  78.134  1 139.2  ? 3   ILE   A CB   1 1 
ATOM   18   C  CG1  . ILE   A 1 4   ? 49.34  6.044  78.857  1 139.92 ? 3   ILE   A CG1  1 1 
ATOM   19   C  CG2  . ILE   A 1 4   ? 48.901 4.933  76.635  1 139.74 ? 3   ILE   A CG2  1 1 
ATOM   20   C  CD1  . ILE   A 1 4   ? 50.18  5.608  80.019  1 141.15 ? 3   ILE   A CD1  1 1 
ATOM   21   N  N    . ILE   A 1 5   ? 46.053 2.642  78.794  1 139.83 ? 4   ILE   A N    1 1 
ATOM   22   C  CA   . ILE   A 1 5   ? 45.362 1.387  78.474  1 140.52 ? 4   ILE   A CA   1 1 
ATOM   23   C  C    . ILE   A 1 5   ? 43.951 1.634  77.909  1 139.81 ? 4   ILE   A C    1 1 
ATOM   24   O  O    . ILE   A 1 5   ? 43.599 1.106  76.852  1 139.83 ? 4   ILE   A O    1 1 
ATOM   25   C  CB   . ILE   A 1 5   ? 45.323 0.485  79.736  1 141.4  ? 4   ILE   A CB   1 1 
ATOM   26   C  CG1  . ILE   A 1 5   ? 46.746 0.126  80.214  1 142.82 ? 4   ILE   A CG1  1 1 
ATOM   27   C  CG2  . ILE   A 1 5   ? 44.467 -0.756 79.501  1 142.23 ? 4   ILE   A CG2  1 1 
ATOM   28   C  CD1  . ILE   A 1 5   ? 46.809 -0.684 81.525  1 144.32 ? 4   ILE   A CD1  1 1 
ATOM   29   N  N    . LEU   A 1 6   ? 43.16  2.459  78.607  1 138.84 ? 5   LEU   A N    1 1 
ATOM   30   C  CA   . LEU   A 1 6   ? 41.796 2.818  78.214  1 138.17 ? 5   LEU   A CA   1 1 
ATOM   31   C  C    . LEU   A 1 6   ? 41.778 3.736  76.976  1 137.04 ? 5   LEU   A C    1 1 
ATOM   32   O  O    . LEU   A 1 6   ? 40.809 3.723  76.219  1 137.08 ? 5   LEU   A O    1 1 
ATOM   33   C  CB   . LEU   A 1 6   ? 41.065 3.512  79.387  1 138.41 ? 5   LEU   A CB   1 1 
ATOM   34   C  CG   . LEU   A 1 6   ? 41.171 2.853  80.767  1 139.84 ? 5   LEU   A CG   1 1 
ATOM   35   C  CD1  . LEU   A 1 6   ? 42.114 3.629  81.673  1 140.36 ? 5   LEU   A CD1  1 1 
ATOM   36   C  CD2  . LEU   A 1 6   ? 39.811 2.749  81.427  1 140.48 ? 5   LEU   A CD2  1 1 
ATOM   37   N  N    . ASP   A 1 7   ? 42.844 4.53   76.776  1 135.84 ? 6   ASP   A N    1 1 
ATOM   38   C  CA   . ASP   A 1 7   ? 42.962 5.47   75.666  1 135.14 ? 6   ASP   A CA   1 1 
ATOM   39   C  C    . ASP   A 1 7   ? 43.129 4.817  74.3    1 134.01 ? 6   ASP   A C    1 1 
ATOM   40   O  O    . ASP   A 1 7   ? 42.941 5.501  73.295  1 134.12 ? 6   ASP   A O    1 1 
ATOM   41   C  CB   . ASP   A 1 7   ? 44.091 6.478  75.919  1 136.89 ? 6   ASP   A CB   1 1 
ATOM   42   C  CG   . ASP   A 1 7   ? 43.669 7.65   76.778  1 141.57 ? 6   ASP   A CG   1 1 
ATOM   43   O  OD1  . ASP   A 1 7   ? 42.789 8.424  76.335  1 142.24 ? 6   ASP   A OD1  1 1 
ATOM   44   O  OD2  . ASP   A 1 7   ? 44.221 7.799  77.893  1 143.81 ? 6   ASP   A OD2  1 1 
ATOM   45   N  N    . LEU   A 1 8   ? 43.475 3.512  74.241  1 132.79 ? 7   LEU   A N    1 1 
ATOM   46   C  CA   . LEU   A 1 8   ? 43.621 2.841  72.941  1 132.01 ? 7   LEU   A CA   1 1 
ATOM   47   C  C    . LEU   A 1 8   ? 42.267 2.547  72.26   1 131.23 ? 7   LEU   A C    1 1 
ATOM   48   O  O    . LEU   A 1 8   ? 42.236 2.333  71.052  1 131.32 ? 7   LEU   A O    1 1 
ATOM   49   C  CB   . LEU   A 1 8   ? 44.498 1.583  73.007  1 131.88 ? 7   LEU   A CB   1 1 
ATOM   50   C  CG   . LEU   A 1 8   ? 45.301 1.313  71.734  1 132.86 ? 7   LEU   A CG   1 1 
ATOM   51   C  CD1  . LEU   A 1 8   ? 46.738 1.754  71.889  1 133.29 ? 7   LEU   A CD1  1 1 
ATOM   52   C  CD2  . LEU   A 1 8   ? 45.22  -0.141 71.333  1 133.44 ? 7   LEU   A CD2  1 1 
ATOM   53   N  N    . LEU   A 1 9   ? 41.152 2.587  73.021  1 130.21 ? 8   LEU   A N    1 1 
ATOM   54   C  CA   . LEU   A 1 9   ? 39.791 2.408  72.501  1 129.53 ? 8   LEU   A CA   1 1 
ATOM   55   C  C    . LEU   A 1 9   ? 39.431 3.611  71.601  1 128.36 ? 8   LEU   A C    1 1 
ATOM   56   O  O    . LEU   A 1 9   ? 38.799 3.438  70.559  1 128.39 ? 8   LEU   A O    1 1 
ATOM   57   C  CB   . LEU   A 1 9   ? 38.802 2.312  73.679  1 129.86 ? 8   LEU   A CB   1 1 
ATOM   58   C  CG   . LEU   A 1 9   ? 37.656 1.308  73.547  1 131.43 ? 8   LEU   A CG   1 1 
ATOM   59   C  CD1  . LEU   A 1 9   ? 37.179 0.838  74.921  1 132.04 ? 8   LEU   A CD1  1 1 
ATOM   60   C  CD2  . LEU   A 1 9   ? 36.504 1.889  72.753  1 132.06 ? 8   LEU   A CD2  1 1 
ATOM   61   N  N    . LEU   A 1 10  ? 39.843 4.824  72.011  1 127.2  ? 9   LEU   A N    1 1 
ATOM   62   C  CA   . LEU   A 1 10  ? 39.625 6.055  71.256  1 126.57 ? 9   LEU   A CA   1 1 
ATOM   63   C  C    . LEU   A 1 10  ? 40.51  6.069  70.011  1 125.56 ? 9   LEU   A C    1 1 
ATOM   64   O  O    . LEU   A 1 10  ? 40.072 6.522  68.958  1 125.67 ? 9   LEU   A O    1 1 
ATOM   65   C  CB   . LEU   A 1 10  ? 39.962 7.279  72.123  1 126.88 ? 9   LEU   A CB   1 1 
ATOM   66   C  CG   . LEU   A 1 10  ? 39.204 7.413  73.431  1 128.36 ? 9   LEU   A CG   1 1 
ATOM   67   C  CD1  . LEU   A 1 10  ? 39.839 8.467  74.318  1 128.89 ? 9   LEU   A CD1  1 1 
ATOM   68   C  CD2  . LEU   A 1 10  ? 37.746 7.729  73.181  1 129.02 ? 9   LEU   A CD2  1 1 
ATOM   69   N  N    . LEU   A 1 11  ? 41.757 5.585  70.138  1 124.43 ? 10  LEU   A N    1 1 
ATOM   70   C  CA   . LEU   A 1 11  ? 42.723 5.52   69.047  1 123.84 ? 10  LEU   A CA   1 1 
ATOM   71   C  C    . LEU   A 1 11  ? 42.255 4.57   67.945  1 122.98 ? 10  LEU   A C    1 1 
ATOM   72   O  O    . LEU   A 1 11  ? 42.501 4.84   66.772  1 123.15 ? 10  LEU   A O    1 1 
ATOM   73   C  CB   . LEU   A 1 11  ? 44.091 5.074  69.578  1 124.03 ? 10  LEU   A CB   1 1 
ATOM   74   C  CG   . LEU   A 1 11  ? 45.253 6.014  69.293  1 125.46 ? 10  LEU   A CG   1 1 
ATOM   75   C  CD1  . LEU   A 1 11  ? 46.463 5.633  70.116  1 126.06 ? 10  LEU   A CD1  1 1 
ATOM   76   C  CD2  . LEU   A 1 11  ? 45.597 6.038  67.812  1 126.01 ? 10  LEU   A CD2  1 1 
ATOM   77   N  N    . LEU   A 1 12  ? 41.576 3.472  68.309  1 121.92 ? 11  LEU   A N    1 1 
ATOM   78   C  CA   . LEU   A 1 12  ? 41.082 2.523  67.316  1 121.33 ? 11  LEU   A CA   1 1 
ATOM   79   C  C    . LEU   A 1 12  ? 39.88  3.088  66.556  1 120.69 ? 11  LEU   A C    1 1 
ATOM   80   O  O    . LEU   A 1 12  ? 39.746 2.835  65.361  1 120.78 ? 11  LEU   A O    1 1 
ATOM   81   C  CB   . LEU   A 1 12  ? 40.755 1.163  67.95   1 121.46 ? 11  LEU   A CB   1 1 
ATOM   82   C  CG   . LEU   A 1 12  ? 41.952 0.391  68.51   1 122.83 ? 11  LEU   A CG   1 1 
ATOM   83   C  CD1  . LEU   A 1 12  ? 41.506 -0.838 69.263  1 123.37 ? 11  LEU   A CD1  1 1 
ATOM   84   C  CD2  . LEU   A 1 12  ? 42.941 0.031  67.424  1 123.42 ? 11  LEU   A CD2  1 1 
ATOM   85   N  N    . LEU   A 1 13  ? 39.035 3.889  67.228  1 119.9  ? 12  LEU   A N    1 1 
ATOM   86   C  CA   . LEU   A 1 13  ? 37.865 4.499  66.587  1 119.62 ? 12  LEU   A CA   1 1 
ATOM   87   C  C    . LEU   A 1 13  ? 38.224 5.673  65.667  1 118.72 ? 12  LEU   A C    1 1 
ATOM   88   O  O    . LEU   A 1 13  ? 37.477 5.958  64.731  1 118.77 ? 12  LEU   A O    1 1 
ATOM   89   C  CB   . LEU   A 1 13  ? 36.809 4.915  67.621  1 120.04 ? 12  LEU   A CB   1 1 
ATOM   90   C  CG   . LEU   A 1 13  ? 35.486 4.157  67.541  1 121.62 ? 12  LEU   A CG   1 1 
ATOM   91   C  CD1  . LEU   A 1 13  ? 34.696 4.288  68.832  1 122.21 ? 12  LEU   A CD1  1 1 
ATOM   92   C  CD2  . LEU   A 1 13  ? 34.669 4.594  66.338  1 122.2  ? 12  LEU   A CD2  1 1 
ATOM   93   N  N    . THR   A 1 14  ? 39.37  6.333  65.905  1 117.74 ? 13  THR   A N    1 1 
ATOM   94   C  CA   . THR   A 1 14  ? 39.811 7.423  65.037  1 117.26 ? 13  THR   A CA   1 1 
ATOM   95   C  C    . THR   A 1 14  ? 40.358 6.865  63.723  1 116.48 ? 13  THR   A C    1 1 
ATOM   96   O  O    . THR   A 1 14  ? 40.137 7.466  62.677  1 116.59 ? 13  THR   A O    1 1 
ATOM   97   C  CB   . THR   A 1 14  ? 40.794 8.347  65.743  1 118.51 ? 13  THR   A CB   1 1 
ATOM   98   O  OG1  . THR   A 1 14  ? 41.854 7.573  66.295  1 119.64 ? 13  THR   A OG1  1 1 
ATOM   99   C  CG2  . THR   A 1 14  ? 40.137 9.168  66.821  1 118.76 ? 13  THR   A CG2  1 1 
ATOM   100  N  N    . ILE   A 1 15  ? 41.054 5.715  63.767  1 115.58 ? 14  ILE   A N    1 1 
ATOM   101  C  CA   . ILE   A 1 15  ? 41.527 5.06   62.544  1 115.29 ? 14  ILE   A CA   1 1 
ATOM   102  C  C    . ILE   A 1 15  ? 40.338 4.389  61.804  1 114.6  ? 14  ILE   A C    1 1 
ATOM   103  O  O    . ILE   A 1 15  ? 40.351 4.29   60.574  1 114.62 ? 14  ILE   A O    1 1 
ATOM   104  C  CB   . ILE   A 1 15  ? 42.697 4.082  62.815  1 115.99 ? 14  ILE   A CB   1 1 
ATOM   105  C  CG1  . ILE   A 1 15  ? 43.789 4.751  63.665  1 116.99 ? 14  ILE   A CG1  1 1 
ATOM   106  C  CG2  . ILE   A 1 15  ? 43.282 3.547  61.502  1 116.59 ? 14  ILE   A CG2  1 1 
ATOM   107  C  CD1  . ILE   A 1 15  ? 44.905 3.801  64.111  1 118.33 ? 14  ILE   A CD1  1 1 
ATOM   108  N  N    . ILE   A 1 16  ? 39.294 3.977  62.558  1 113.8  ? 15  ILE   A N    1 1 
ATOM   109  C  CA   . ILE   A 1 16  ? 38.051 3.416  62.038  1 113.52 ? 15  ILE   A CA   1 1 
ATOM   110  C  C    . ILE   A 1 16  ? 37.32  4.504  61.232  1 113.31 ? 15  ILE   A C    1 1 
ATOM   111  O  O    . ILE   A 1 16  ? 36.843 4.237  60.132  1 113.38 ? 15  ILE   A O    1 1 
ATOM   112  C  CB   . ILE   A 1 16  ? 37.217 2.809  63.21   1 113.77 ? 15  ILE   A CB   1 1 
ATOM   113  C  CG1  . ILE   A 1 16  ? 37.51  1.31   63.342  1 114.56 ? 15  ILE   A CG1  1 1 
ATOM   114  C  CG2  . ILE   A 1 16  ? 35.705 3.064  63.095  1 114.19 ? 15  ILE   A CG2  1 1 
ATOM   115  C  CD1  . ILE   A 1 16  ? 37.006 0.682  64.574  1 115.76 ? 15  ILE   A CD1  1 1 
ATOM   116  N  N    . TYR   A 1 17  ? 37.28  5.735  61.756  1 112.89 ? 16  TYR   A N    1 1 
ATOM   117  C  CA   . TYR   A 1 17  ? 36.659 6.856  61.061  1 112.88 ? 16  TYR   A CA   1 1 
ATOM   118  C  C    . TYR   A 1 17  ? 37.522 7.286  59.873  1 112.95 ? 16  TYR   A C    1 1 
ATOM   119  O  O    . TYR   A 1 17  ? 36.982 7.653  58.846  1 112.96 ? 16  TYR   A O    1 1 
ATOM   120  C  CB   . TYR   A 1 17  ? 36.452 8.035  62.022  1 112.71 ? 16  TYR   A CB   1 1 
ATOM   121  C  CG   . TYR   A 1 17  ? 35.522 9.105  61.494  1 113.21 ? 16  TYR   A CG   1 1 
ATOM   122  C  CD1  . TYR   A 1 17  ? 36.007 10.174 60.756  1 114.04 ? 16  TYR   A CD1  1 1 
ATOM   123  C  CD2  . TYR   A 1 17  ? 34.161 9.059  61.751  1 113.93 ? 16  TYR   A CD2  1 1 
ATOM   124  C  CE1  . TYR   A 1 17  ? 35.16  11.172 60.286  1 114.82 ? 16  TYR   A CE1  1 1 
ATOM   125  C  CE2  . TYR   A 1 17  ? 33.304 10.049 61.283  1 114.73 ? 16  TYR   A CE2  1 1 
ATOM   126  C  CZ   . TYR   A 1 17  ? 33.808 11.107 60.552  1 115.52 ? 16  TYR   A CZ   1 1 
ATOM   127  O  OH   . TYR   A 1 17  ? 32.973 12.094 60.087  1 116.74 ? 16  TYR   A OH   1 1 
ATOM   128  N  N    . SER   A 1 18  ? 38.851 7.233  60.009  1 112.93 ? 17  SER   A N    1 1 
ATOM   129  C  CA   . SER   A 1 18  ? 39.797 7.607  58.958  1 113.39 ? 17  SER   A CA   1 1 
ATOM   130  C  C    . SER   A 1 18  ? 39.539 6.904  57.619  1 113.27 ? 17  SER   A C    1 1 
ATOM   131  O  O    . SER   A 1 18  ? 39.442 7.581  56.598  1 113.31 ? 17  SER   A O    1 1 
ATOM   132  C  CB   . SER   A 1 18  ? 41.233 7.368  59.419  1 115.02 ? 17  SER   A CB   1 1 
ATOM   133  O  OG   . SER   A 1 18  ? 41.513 8.063  60.623  1 117.5  ? 17  SER   A OG   1 1 
ATOM   134  N  N    . TYR   A 1 19  ? 39.416 5.565  57.616  1 112.92 ? 18  TYR   A N    1 1 
ATOM   135  C  CA   . TYR   A 1 19  ? 39.157 4.835  56.378  1 113.14 ? 18  TYR   A CA   1 1 
ATOM   136  C  C    . TYR   A 1 19  ? 37.706 5.028  55.923  1 113.1  ? 18  TYR   A C    1 1 
ATOM   137  O  O    . TYR   A 1 19  ? 37.454 5.14   54.726  1 113.26 ? 18  TYR   A O    1 1 
ATOM   138  C  CB   . TYR   A 1 19  ? 39.487 3.344  56.534  1 113.28 ? 18  TYR   A CB   1 1 
ATOM   139  C  CG   . TYR   A 1 19  ? 40.154 2.737  55.317  1 114.3  ? 18  TYR   A CG   1 1 
ATOM   140  C  CD1  . TYR   A 1 19  ? 39.456 2.559  54.131  1 115.29 ? 18  TYR   A CD1  1 1 
ATOM   141  C  CD2  . TYR   A 1 19  ? 41.472 2.307  55.364  1 115.31 ? 18  TYR   A CD2  1 1 
ATOM   142  C  CE1  . TYR   A 1 19  ? 40.059 1.991  53.013  1 116.21 ? 18  TYR   A CE1  1 1 
ATOM   143  C  CE2  . TYR   A 1 19  ? 42.084 1.728  54.257  1 116.26 ? 18  TYR   A CE2  1 1 
ATOM   144  C  CZ   . TYR   A 1 19  ? 41.374 1.57   53.081  1 117.14 ? 18  TYR   A CZ   1 1 
ATOM   145  O  OH   . TYR   A 1 19  ? 41.981 1.003  51.984  1 118.58 ? 18  TYR   A OH   1 1 
ATOM   146  N  N    . LEU   A 1 20  ? 36.762 5.097  56.88   1 112.67 ? 19  LEU   A N    1 1 
ATOM   147  C  CA   . LEU   A 1 20  ? 35.327 5.286  56.639  1 112.69 ? 19  LEU   A CA   1 1 
ATOM   148  C  C    . LEU   A 1 20  ? 34.997 6.631  55.956  1 112.48 ? 19  LEU   A C    1 1 
ATOM   149  O  O    . LEU   A 1 20  ? 34.204 6.673  55.017  1 112.52 ? 19  LEU   A O    1 1 
ATOM   150  C  CB   . LEU   A 1 20  ? 34.58  5.173  57.978  1 112.95 ? 19  LEU   A CB   1 1 
ATOM   151  C  CG   . LEU   A 1 20  ? 33.078 5.369  57.94   1 114.48 ? 19  LEU   A CG   1 1 
ATOM   152  C  CD1  . LEU   A 1 20  ? 32.411 4.253  57.165  1 115.1  ? 19  LEU   A CD1  1 1 
ATOM   153  C  CD2  . LEU   A 1 20  ? 32.511 5.459  59.346  1 115.06 ? 19  LEU   A CD2  1 1 
ATOM   154  N  N    . GLU   A 1 21  ? 35.613 7.719  56.424  1 112.04 ? 20  GLU   A N    1 1 
ATOM   155  C  CA   . GLU   A 1 21  ? 35.423 9.069  55.904  1 112.08 ? 20  GLU   A CA   1 1 
ATOM   156  C  C    . GLU   A 1 21  ? 36.091 9.197  54.541  1 111.62 ? 20  GLU   A C    1 1 
ATOM   157  O  O    . GLU   A 1 21  ? 35.497 9.759  53.624  1 111.54 ? 20  GLU   A O    1 1 
ATOM   158  C  CB   . GLU   A 1 21  ? 35.976 10.089 56.919  1 114.52 ? 20  GLU   A CB   1 1 
ATOM   159  C  CG   . GLU   A 1 21  ? 36.299 11.475 56.387  1 119.55 ? 20  GLU   A CG   1 1 
ATOM   160  C  CD   . GLU   A 1 21  ? 37.708 11.929 56.715  1 125.8  ? 20  GLU   A CD   1 1 
ATOM   161  O  OE1  . GLU   A 1 21  ? 37.937 13.159 56.764  1 127.26 ? 20  GLU   A OE1  1 1 
ATOM   162  O  OE2  . GLU   A 1 21  ? 38.584 11.058 56.928  1 127.68 ? 20  GLU   A OE2  1 1 
ATOM   163  N  N    . ALA   A 1 22  ? 37.314 8.658  54.402  1 111.17 ? 21  ALA   A N    1 1 
ATOM   164  C  CA   . ALA   A 1 22  ? 38.038 8.684  53.127  1 111.25 ? 21  ALA   A CA   1 1 
ATOM   165  C  C    . ALA   A 1 22  ? 37.397 7.776  52.06   1 110.98 ? 21  ALA   A C    1 1 
ATOM   166  O  O    . ALA   A 1 22  ? 37.639 7.972  50.869  1 111    ? 21  ALA   A O    1 1 
ATOM   167  C  CB   . ALA   A 1 22  ? 39.494 8.306  53.333  1 111.46 ? 21  ALA   A CB   1 1 
ATOM   168  N  N    . LEU   A 1 23  ? 36.586 6.787  52.486  1 110.5  ? 22  LEU   A N    1 1 
ATOM   169  C  CA   . LEU   A 1 23  ? 35.864 5.907  51.574  1 110.44 ? 22  LEU   A CA   1 1 
ATOM   170  C  C    . LEU   A 1 23  ? 34.672 6.656  50.978  1 110.23 ? 22  LEU   A C    1 1 
ATOM   171  O  O    . LEU   A 1 23  ? 34.383 6.468  49.806  1 110.32 ? 22  LEU   A O    1 1 
ATOM   172  C  CB   . LEU   A 1 23  ? 35.386 4.637  52.288  1 110.64 ? 22  LEU   A CB   1 1 
ATOM   173  C  CG   . LEU   A 1 23  ? 36.13  3.363  51.917  1 112.16 ? 22  LEU   A CG   1 1 
ATOM   174  C  CD1  . LEU   A 1 23  ? 35.989 2.316  52.995  1 112.67 ? 22  LEU   A CD1  1 1 
ATOM   175  C  CD2  . LEU   A 1 23  ? 35.651 2.822  50.584  1 112.92 ? 22  LEU   A CD2  1 1 
ATOM   176  N  N    . VAL   A 1 24  ? 33.991 7.513  51.772  1 109.77 ? 23  VAL   A N    1 1 
ATOM   177  C  CA   . VAL   A 1 24  ? 32.856 8.318  51.304  1 109.69 ? 23  VAL   A CA   1 1 
ATOM   178  C  C    . VAL   A 1 24  ? 33.347 9.421  50.353  1 109.14 ? 23  VAL   A C    1 1 
ATOM   179  O  O    . VAL   A 1 24  ? 32.722 9.665  49.323  1 109.23 ? 23  VAL   A O    1 1 
ATOM   180  C  CB   . VAL   A 1 24  ? 32.033 8.892  52.484  1 110.58 ? 23  VAL   A CB   1 1 
ATOM   181  C  CG1  . VAL   A 1 24  ? 30.971 9.872  51.995  1 111.22 ? 23  VAL   A CG1  1 1 
ATOM   182  C  CG2  . VAL   A 1 24  ? 31.396 7.773  53.297  1 111.12 ? 23  VAL   A CG2  1 1 
ATOM   183  N  N    . LYS   A 1 25  ? 34.506 10.035 50.667  1 108.35 ? 24  LYS   A N    1 1 
ATOM   184  C  CA   . LYS   A 1 25  ? 35.14  11.069 49.834  1 107.94 ? 24  LYS   A CA   1 1 
ATOM   185  C  C    . LYS   A 1 25  ? 35.58  10.547 48.447  1 107.36 ? 24  LYS   A C    1 1 
ATOM   186  O  O    . LYS   A 1 25  ? 36.01  11.342 47.615  1 107.59 ? 24  LYS   A O    1 1 
ATOM   187  C  CB   . LYS   A 1 25  ? 36.379 11.647 50.544  1 109.4  ? 24  LYS   A CB   1 1 
ATOM   188  C  CG   . LYS   A 1 25  ? 36.088 12.517 51.756  1 112.55 ? 24  LYS   A CG   1 1 
ATOM   189  C  CD   . LYS   A 1 25  ? 37.388 12.953 52.423  1 115.71 ? 24  LYS   A CD   1 1 
ATOM   190  C  CE   . LYS   A 1 25  ? 37.159 13.96  53.518  1 118.58 ? 24  LYS   A CE   1 1 
ATOM   191  N  NZ   . LYS   A 1 25  ? 38.434 14.382 54.153  1 120.28 ? 24  LYS   A NZ   1 1 
ATOM   192  N  N    . VAL   A 1 26  ? 35.532 9.221  48.215  1 106.4  ? 25  VAL   A N    1 1 
ATOM   193  C  CA   . VAL   A 1 26  ? 35.952 8.625  46.953  1 105.94 ? 25  VAL   A CA   1 1 
ATOM   194  C  C    . VAL   A 1 26  ? 34.819 7.817  46.286  1 105.57 ? 25  VAL   A C    1 1 
ATOM   195  O  O    . VAL   A 1 26  ? 34.506 8.069  45.121  1 105.75 ? 25  VAL   A O    1 1 
ATOM   196  C  CB   . VAL   A 1 26  ? 37.254 7.804  47.129  1 106.38 ? 25  VAL   A CB   1 1 
ATOM   197  C  CG1  . VAL   A 1 26  ? 37.593 7.021  45.869  1 106.89 ? 25  VAL   A CG1  1 1 
ATOM   198  C  CG2  . VAL   A 1 26  ? 38.418 8.707  47.524  1 106.73 ? 25  VAL   A CG2  1 1 
ATOM   199  N  N    . PHE   A 1 27  ? 34.193 6.871  47.025  1 104.83 ? 26  PHE   A N    1 1 
ATOM   200  C  CA   . PHE   A 1 27  ? 33.09  6.014  46.544  1 104.49 ? 26  PHE   A CA   1 1 
ATOM   201  C  C    . PHE   A 1 27  ? 31.861 6.856  46.121  1 103.3  ? 26  PHE   A C    1 1 
ATOM   202  O  O    . PHE   A 1 27  ? 31.466 6.822  44.955  1 103.13 ? 26  PHE   A O    1 1 
ATOM   203  C  CB   . PHE   A 1 27  ? 32.729 4.952  47.612  1 104.82 ? 26  PHE   A CB   1 1 
ATOM   204  C  CG   . PHE   A 1 27  ? 32.124 3.66   47.115  1 105.95 ? 26  PHE   A CG   1 1 
ATOM   205  C  CD1  . PHE   A 1 27  ? 32.834 2.82   46.273  1 106.99 ? 26  PHE   A CD1  1 1 
ATOM   206  C  CD2  . PHE   A 1 27  ? 30.878 3.247  47.551  1 106.94 ? 26  PHE   A CD2  1 1 
ATOM   207  C  CE1  . PHE   A 1 27  ? 32.282 1.622  45.829  1 107.82 ? 26  PHE   A CE1  1 1 
ATOM   208  C  CE2  . PHE   A 1 27  ? 30.329 2.047  47.108  1 107.78 ? 26  PHE   A CE2  1 1 
ATOM   209  C  CZ   . PHE   A 1 27  ? 31.035 1.241  46.253  1 107.65 ? 26  PHE   A CZ   1 1 
ATOM   210  N  N    . PHE   A 1 28  ? 31.297 7.645  47.052  1 102.25 ? 27  PHE   A N    1 1 
ATOM   211  C  CA   . PHE   A 1 28  ? 30.184 8.547  46.77   1 101.62 ? 27  PHE   A CA   1 1 
ATOM   212  C  C    . PHE   A 1 28  ? 30.625 9.95   47.195  1 100.14 ? 27  PHE   A C    1 1 
ATOM   213  O  O    . PHE   A 1 28  ? 30.351 10.364 48.321  1 100.19 ? 27  PHE   A O    1 1 
ATOM   214  C  CB   . PHE   A 1 28  ? 28.915 8.105  47.523  1 101.84 ? 27  PHE   A CB   1 1 
ATOM   215  C  CG   . PHE   A 1 28  ? 28.253 6.877  46.935  1 102.96 ? 27  PHE   A CG   1 1 
ATOM   216  C  CD1  . PHE   A 1 28  ? 27.687 6.91   45.668  1 103.93 ? 27  PHE   A CD1  1 1 
ATOM   217  C  CD2  . PHE   A 1 28  ? 28.177 5.698  47.655  1 103.88 ? 27  PHE   A CD2  1 1 
ATOM   218  C  CE1  . PHE   A 1 28  ? 27.07  5.782  45.129  1 104.64 ? 27  PHE   A CE1  1 1 
ATOM   219  C  CE2  . PHE   A 1 28  ? 27.557 4.571  47.112  1 104.68 ? 27  PHE   A CE2  1 1 
ATOM   220  C  CZ   . PHE   A 1 28  ? 27.01  4.62   45.854  1 104.42 ? 27  PHE   A CZ   1 1 
ATOM   221  N  N    . PRO   A 1 29  ? 31.396 10.665 46.347  1 98.63  ? 28  PRO   A N    1 1 
ATOM   222  C  CA   . PRO   A 1 29  ? 31.909 11.977 46.761  1 97.34  ? 28  PRO   A CA   1 1 
ATOM   223  C  C    . PRO   A 1 29  ? 30.992 13.176 46.455  1 95.73  ? 28  PRO   A C    1 1 
ATOM   224  O  O    . PRO   A 1 29  ? 30.307 13.211 45.43   1 95.69  ? 28  PRO   A O    1 1 
ATOM   225  C  CB   . PRO   A 1 29  ? 33.24  12.085 46.014  1 98.25  ? 28  PRO   A CB   1 1 
ATOM   226  C  CG   . PRO   A 1 29  ? 33.094 11.172 44.805  1 99.02  ? 28  PRO   A CG   1 1 
ATOM   227  C  CD   . PRO   A 1 29  ? 31.868 10.301 44.995  1 97.86  ? 28  PRO   A CD   1 1 
ATOM   228  N  N    . ARG   A 1 30  ? 31.008 14.179 47.348  1 94.13  ? 29  ARG   A N    1 1 
ATOM   229  C  CA   . ARG   A 1 30  ? 30.217 15.411 47.219  1 92.95  ? 29  ARG   A CA   1 1 
ATOM   230  C  C    . ARG   A 1 30  ? 30.634 16.211 45.969  1 91.2   ? 29  ARG   A C    1 1 
ATOM   231  O  O    . ARG   A 1 30  ? 31.772 16.096 45.519  1 91.33  ? 29  ARG   A O    1 1 
ATOM   232  C  CB   . ARG   A 1 30  ? 30.392 16.253 48.497  1 94.18  ? 29  ARG   A CB   1 1 
ATOM   233  C  CG   . ARG   A 1 30  ? 29.253 17.233 48.794  1 96.74  ? 29  ARG   A CG   1 1 
ATOM   234  C  CD   . ARG   A 1 30  ? 29.158 17.583 50.271  1 99.01  ? 29  ARG   A CD   1 1 
ATOM   235  N  NE   . ARG   A 1 30  ? 28.131 18.598 50.522  1 100.71 ? 29  ARG   A NE   1 1 
ATOM   236  C  CZ   . ARG   A 1 30  ? 27.674 18.927 51.727  1 101.96 ? 29  ARG   A CZ   1 1 
ATOM   237  N  NH1  . ARG   A 1 30  ? 28.136 18.317 52.809  1 101.5  ? 29  ARG   A NH1  1 1 
ATOM   238  N  NH2  . ARG   A 1 30  ? 26.747 19.867 51.857  1 101.6  ? 29  ARG   A NH2  1 1 
ATOM   239  N  N    . LYS   A 1 31  ? 29.726 17.007 45.404  1 89.37  ? 30  LYS   A N    1 1 
ATOM   240  C  CA   . LYS   A 1 31  ? 30.02  17.803 44.213  1 88.07  ? 30  LYS   A CA   1 1 
ATOM   241  C  C    . LYS   A 1 31  ? 30.911 19.026 44.525  1 85.98  ? 30  LYS   A C    1 1 
ATOM   242  O  O    . LYS   A 1 31  ? 30.507 19.916 45.279  1 85.97  ? 30  LYS   A O    1 1 
ATOM   243  C  CB   . LYS   A 1 31  ? 28.705 18.252 43.531  1 90.15  ? 30  LYS   A CB   1 1 
ATOM   244  C  CG   . LYS   A 1 31  ? 28.753 18.275 41.998  1 94     ? 30  LYS   A CG   1 1 
ATOM   245  C  CD   . LYS   A 1 31  ? 27.397 18.652 41.393  1 98.5   ? 30  LYS   A CD   1 1 
ATOM   246  C  CE   . LYS   A 1 31  ? 27.182 18.062 40.003  1 102.44 ? 30  LYS   A CE   1 1 
ATOM   247  N  NZ   . LYS   A 1 31  ? 25.874 18.453 39.397  1 103.94 ? 30  LYS   A NZ   1 1 
ATOM   248  N  N    . ARG   A 1 32  ? 32.123 19.057 43.939  1 84.01  ? 31  ARG   A N    1 1 
ATOM   249  C  CA   . ARG   A 1 32  ? 33.074 20.155 44.103  1 82.73  ? 31  ARG   A CA   1 1 
ATOM   250  C  C    . ARG   A 1 32  ? 32.742 21.279 43.122  1 81.25  ? 31  ARG   A C    1 1 
ATOM   251  O  O    . ARG   A 1 32  ? 32.629 21.037 41.921  1 81.54  ? 31  ARG   A O    1 1 
ATOM   252  C  CB   . ARG   A 1 32  ? 34.506 19.668 43.848  1 83.98  ? 31  ARG   A CB   1 1 
ATOM   253  C  CG   . ARG   A 1 32  ? 35.201 19.091 45.068  1 87.75  ? 31  ARG   A CG   1 1 
ATOM   254  C  CD   . ARG   A 1 32  ? 36.308 19.994 45.591  1 92.12  ? 31  ARG   A CD   1 1 
ATOM   255  N  NE   . ARG   A 1 32  ? 37.315 20.293 44.57   1 95.9   ? 31  ARG   A NE   1 1 
ATOM   256  C  CZ   . ARG   A 1 32  ? 38.599 20.531 44.829  1 98.82  ? 31  ARG   A CZ   1 1 
ATOM   257  N  NH1  . ARG   A 1 32  ? 39.049 20.507 46.08   1 98.34  ? 31  ARG   A NH1  1 1 
ATOM   258  N  NH2  . ARG   A 1 32  ? 39.442 20.797 43.839  1 99.26  ? 31  ARG   A NH2  1 1 
ATOM   259  N  N    . LYS   A 1 33  ? 32.597 22.504 43.62   1 79.52  ? 32  LYS   A N    1 1 
ATOM   260  C  CA   . LYS   A 1 33  ? 32.291 23.654 42.771  1 78.24  ? 32  LYS   A CA   1 1 
ATOM   261  C  C    . LYS   A 1 33  ? 33.565 24.487 42.456  1 77.13  ? 32  LYS   A C    1 1 
ATOM   262  O  O    . LYS   A 1 33  ? 34.66  24.15  42.917  1 77.26  ? 32  LYS   A O    1 1 
ATOM   263  C  CB   . LYS   A 1 33  ? 31.195 24.516 43.435  1 79.46  ? 32  LYS   A CB   1 1 
ATOM   264  C  CG   . LYS   A 1 33  ? 31.695 25.356 44.616  1 82.45  ? 32  LYS   A CG   1 1 
ATOM   265  C  CD   . LYS   A 1 33  ? 30.609 26.258 45.182  1 85.2   ? 32  LYS   A CD   1 1 
ATOM   266  C  CE   . LYS   A 1 33  ? 31.137 27.143 46.278  1 87.59  ? 32  LYS   A CE   1 1 
ATOM   267  N  NZ   . LYS   A 1 33  ? 30.042 27.866 46.967  1 89.08  ? 32  LYS   A NZ   1 1 
ATOM   268  N  N    . SER   A 1 34  ? 33.427 25.557 41.654  1 75.88  ? 33  SER   A N    1 1 
ATOM   269  C  CA   . SER   A 1 34  ? 34.551 26.432 41.333  1 75.16  ? 33  SER   A CA   1 1 
ATOM   270  C  C    . SER   A 1 34  ? 34.376 27.791 42.012  1 74.02  ? 33  SER   A C    1 1 
ATOM   271  O  O    . SER   A 1 34  ? 33.281 28.349 42.015  1 74.33  ? 33  SER   A O    1 1 
ATOM   272  C  CB   . SER   A 1 34  ? 34.677 26.621 39.823  1 76.47  ? 33  SER   A CB   1 1 
ATOM   273  O  OG   . SER   A 1 34  ? 35.727 27.517 39.494  1 78.56  ? 33  SER   A OG   1 1 
ATOM   274  N  N    . VAL   A 1 35  ? 35.445 28.312 42.609  1 72.52  ? 34  VAL   A N    1 1 
ATOM   275  C  CA   . VAL   A 1 35  ? 35.41  29.638 43.233  1 71.27  ? 34  VAL   A CA   1 1 
ATOM   276  C  C    . VAL   A 1 35  ? 36.299 30.632 42.452  1 70.24  ? 34  VAL   A C    1 1 
ATOM   277  O  O    . VAL   A 1 35  ? 36.829 31.58  43.035  1 70.43  ? 34  VAL   A O    1 1 
ATOM   278  C  CB   . VAL   A 1 35  ? 35.782 29.578 44.726  1 71.34  ? 34  VAL   A CB   1 1 
ATOM   279  C  CG1  . VAL   A 1 35  ? 34.664 28.939 45.534  1 71.72  ? 34  VAL   A CG1  1 1 
ATOM   280  C  CG2  . VAL   A 1 35  ? 37.086 28.83  44.93   1 71.56  ? 34  VAL   A CG2  1 1 
ATOM   281  N  N    . ALA   A 1 36  ? 36.444 30.416 41.128  1 68.78  ? 35  ALA   A N    1 1 
ATOM   282  C  CA   . ALA   A 1 36  ? 37.267 31.245 40.266  1 67.78  ? 35  ALA   A CA   1 1 
ATOM   283  C  C    . ALA   A 1 36  ? 36.553 32.532 39.908  1 66.31  ? 35  ALA   A C    1 1 
ATOM   284  O  O    . ALA   A 1 36  ? 35.408 32.497 39.47   1 66.25  ? 35  ALA   A O    1 1 
ATOM   285  C  CB   . ALA   A 1 36  ? 37.634 30.474 39.006  1 67.94  ? 35  ALA   A CB   1 1 
ATOM   286  N  N    . GLY   A 1 37  ? 37.237 33.653 40.112  1 65.1   ? 36  GLY   A N    1 1 
ATOM   287  C  CA   . GLY   A 1 37  ? 36.716 34.983 39.825  1 64.65  ? 36  GLY   A CA   1 1 
ATOM   288  C  C    . GLY   A 1 37  ? 35.758 35.535 40.867  1 63.97  ? 36  GLY   A C    1 1 
ATOM   289  O  O    . GLY   A 1 37  ? 35.065 36.526 40.611  1 64.52  ? 36  GLY   A O    1 1 
ATOM   290  N  N    . GLU   A 1 38  ? 35.696 34.906 42.052  1 62.39  ? 37  GLU   A N    1 1 
ATOM   291  C  CA   . GLU   A 1 38  ? 34.8   35.359 43.113  1 61.18  ? 37  GLU   A CA   1 1 
ATOM   292  C  C    . GLU   A 1 38  ? 35.475 36.385 44.009  1 59.68  ? 37  GLU   A C    1 1 
ATOM   293  O  O    . GLU   A 1 38  ? 36.694 36.384 44.094  1 59.9   ? 37  GLU   A O    1 1 
ATOM   294  C  CB   . GLU   A 1 38  ? 34.329 34.164 43.95   1 63.19  ? 37  GLU   A CB   1 1 
ATOM   295  C  CG   . GLU   A 1 38  ? 33.415 33.211 43.203  1 67.71  ? 37  GLU   A CG   1 1 
ATOM   296  C  CD   . GLU   A 1 38  ? 31.944 33.403 43.503  1 72.64  ? 37  GLU   A CD   1 1 
ATOM   297  O  OE1  . GLU   A 1 38  ? 31.132 33.298 42.556  1 73.61  ? 37  GLU   A OE1  1 1 
ATOM   298  O  OE2  . GLU   A 1 38  ? 31.603 33.665 44.68   1 72.82  ? 37  GLU   A OE2  1 1 
ATOM   299  N  N    . ILE   A 1 39  ? 34.701 37.258 44.689  1 58.15  ? 38  ILE   A N    1 1 
ATOM   300  C  CA   . ILE   A 1 39  ? 35.293 38.238 45.602  1 57.37  ? 38  ILE   A CA   1 1 
ATOM   301  C  C    . ILE   A 1 39  ? 35.335 37.667 47.037  1 56.89  ? 38  ILE   A C    1 1 
ATOM   302  O  O    . ILE   A 1 39  ? 34.37  37.742 47.813  1 57.09  ? 38  ILE   A O    1 1 
ATOM   303  C  CB   . ILE   A 1 39  ? 34.692 39.66  45.519  1 57.62  ? 38  ILE   A CB   1 1 
ATOM   304  C  CG1  . ILE   A 1 39  ? 34.868 40.216 44.115  1 58.76  ? 38  ILE   A CG1  1 1 
ATOM   305  C  CG2  . ILE   A 1 39  ? 35.385 40.582 46.517  1 58.15  ? 38  ILE   A CG2  1 1 
ATOM   306  C  CD1  . ILE   A 1 39  ? 34.234 41.573 43.874  1 60.29  ? 38  ILE   A CD1  1 1 
ATOM   307  N  N    . VAL   A 1 40  ? 36.479 37.069 47.368  1 55.67  ? 39  VAL   A N    1 1 
ATOM   308  C  CA   . VAL   A 1 40  ? 36.688 36.433 48.655  1 54.4   ? 39  VAL   A CA   1 1 
ATOM   309  C  C    . VAL   A 1 40  ? 37.386 37.37  49.607  1 53.31  ? 39  VAL   A C    1 1 
ATOM   310  O  O    . VAL   A 1 40  ? 38.572 37.634 49.421  1 52.96  ? 39  VAL   A O    1 1 
ATOM   311  C  CB   . VAL   A 1 40  ? 37.506 35.13  48.505  1 54.7   ? 39  VAL   A CB   1 1 
ATOM   312  C  CG1  . VAL   A 1 40  ? 37.526 34.367 49.816  1 55.08  ? 39  VAL   A CG1  1 1 
ATOM   313  C  CG2  . VAL   A 1 40  ? 36.979 34.247 47.363  1 54.95  ? 39  VAL   A CG2  1 1 
ATOM   314  N  N    . LEU   A 1 41  ? 36.656 37.857 50.64   1 52.87  ? 40  LEU   A N    1 1 
ATOM   315  C  CA   . LEU   A 1 41  ? 37.183 38.698 51.728  1 52.39  ? 40  LEU   A CA   1 1 
ATOM   316  C  C    . LEU   A 1 41  ? 37.605 37.78  52.854  1 51.81  ? 40  LEU   A C    1 1 
ATOM   317  O  O    . LEU   A 1 41  ? 36.828 36.92  53.245  1 51.73  ? 40  LEU   A O    1 1 
ATOM   318  C  CB   . LEU   A 1 41  ? 36.118 39.666 52.268  1 52.35  ? 40  LEU   A CB   1 1 
ATOM   319  C  CG   . LEU   A 1 41  ? 36.64  40.809 53.125  1 53.53  ? 40  LEU   A CG   1 1 
ATOM   320  C  CD1  . LEU   A 1 41  ? 35.885 42.072 52.855  1 54.24  ? 40  LEU   A CD1  1 1 
ATOM   321  C  CD2  . LEU   A 1 41  ? 36.53  40.497 54.577  1 54.31  ? 40  LEU   A CD2  1 1 
ATOM   322  N  N    . ILE   A 1 42  ? 38.823 37.945 53.379  1 51.56  ? 41  ILE   A N    1 1 
ATOM   323  C  CA   . ILE   A 1 42  ? 39.3   37.113 54.491  1 51.7   ? 41  ILE   A CA   1 1 
ATOM   324  C  C    . ILE   A 1 42  ? 39.831 37.969 55.651  1 52.21  ? 41  ILE   A C    1 1 
ATOM   325  O  O    . ILE   A 1 42  ? 40.9   38.563 55.53   1 52.21  ? 41  ILE   A O    1 1 
ATOM   326  C  CB   . ILE   A 1 42  ? 40.348 36.071 54.016  1 51.54  ? 41  ILE   A CB   1 1 
ATOM   327  C  CG1  . ILE   A 1 42  ? 39.82  35.251 52.81   1 51.71  ? 41  ILE   A CG1  1 1 
ATOM   328  C  CG2  . ILE   A 1 42  ? 40.78  35.165 55.173  1 51.64  ? 41  ILE   A CG2  1 1 
ATOM   329  C  CD1  . ILE   A 1 42  ? 40.858 34.641 52.005  1 52.4   ? 41  ILE   A CD1  1 1 
ATOM   330  N  N    . THR   A 1 43  ? 39.081 38.05  56.765  1 52.49  ? 42  THR   A N    1 1 
ATOM   331  C  CA   . THR   A 1 43  ? 39.517 38.822 57.935  1 52.99  ? 42  THR   A CA   1 1 
ATOM   332  C  C    . THR   A 1 43  ? 40.515 38.011 58.751  1 52.69  ? 42  THR   A C    1 1 
ATOM   333  O  O    . THR   A 1 43  ? 40.337 36.81  58.904  1 52.55  ? 42  THR   A O    1 1 
ATOM   334  C  CB   . THR   A 1 43  ? 38.324 39.219 58.804  1 54.77  ? 42  THR   A CB   1 1 
ATOM   335  O  OG1  . THR   A 1 43  ? 37.711 38.044 59.346  1 55.93  ? 42  THR   A OG1  1 1 
ATOM   336  C  CG2  . THR   A 1 43  ? 37.314 40.056 58.051  1 55.27  ? 42  THR   A CG2  1 1 
ATOM   337  N  N    . GLY   A 1 44  ? 41.516 38.669 59.313  1 52.54  ? 43  GLY   A N    1 1 
ATOM   338  C  CA   . GLY   A 1 44  ? 42.546 37.982 60.077  1 53.06  ? 43  GLY   A CA   1 1 
ATOM   339  C  C    . GLY   A 1 44  ? 43.411 37.131 59.169  1 53.42  ? 43  GLY   A C    1 1 
ATOM   340  O  O    . GLY   A 1 44  ? 43.77  35.997 59.508  1 53.38  ? 43  GLY   A O    1 1 
ATOM   341  N  N    . ALA   A 1 45  ? 43.741 37.681 57.992  1 53.69  ? 44  ALA   A N    1 1 
ATOM   342  C  CA   . ALA   A 1 45  ? 44.529 36.982 56.978  1 54.52  ? 44  ALA   A CA   1 1 
ATOM   343  C  C    . ALA   A 1 45  ? 46.001 37.369 56.931  1 55.1   ? 44  ALA   A C    1 1 
ATOM   344  O  O    . ALA   A 1 45  ? 46.65  37.17  55.905  1 55.57  ? 44  ALA   A O    1 1 
ATOM   345  C  CB   . ALA   A 1 45  ? 43.902 37.15  55.599  1 54.55  ? 44  ALA   A CB   1 1 
ATOM   346  N  N    . GLY   A 1 46  ? 46.52  37.898 58.028  1 54.78  ? 45  GLY   A N    1 1 
ATOM   347  C  CA   . GLY   A 1 46  ? 47.927 38.26  58.105  1 55.08  ? 45  GLY   A CA   1 1 
ATOM   348  C  C    . GLY   A 1 46  ? 48.828 37.124 58.554  1 55.28  ? 45  GLY   A C    1 1 
ATOM   349  O  O    . GLY   A 1 46  ? 50.046 37.21  58.401  1 55.41  ? 45  GLY   A O    1 1 
ATOM   350  N  N    . HIS   A 1 47  ? 48.241 36.049 59.107  1 55.23  ? 46  HIS   A N    1 1 
ATOM   351  C  CA   . HIS   A 1 47  ? 48.994 34.91  59.596  1 56.04  ? 46  HIS   A CA   1 1 
ATOM   352  C  C    . HIS   A 1 47  ? 48.068 33.73  59.91   1 56.2   ? 46  HIS   A C    1 1 
ATOM   353  O  O    . HIS   A 1 47  ? 46.854 33.9   60.069  1 56.02  ? 46  HIS   A O    1 1 
ATOM   354  C  CB   . HIS   A 1 47  ? 49.766 35.34  60.862  1 57.78  ? 46  HIS   A CB   1 1 
ATOM   355  C  CG   . HIS   A 1 47  ? 50.633 34.285 61.478  1 61.45  ? 46  HIS   A CG   1 1 
ATOM   356  N  ND1  . HIS   A 1 47  ? 51.387 33.42  60.702  1 63.61  ? 46  HIS   A ND1  1 1 
ATOM   357  C  CD2  . HIS   A 1 47  ? 50.871 34.02  62.783  1 63.07  ? 46  HIS   A CD2  1 1 
ATOM   358  C  CE1  . HIS   A 1 47  ? 52.034 32.644 61.554  1 64.4   ? 46  HIS   A CE1  1 1 
ATOM   359  N  NE2  . HIS   A 1 47  ? 51.764 32.974 62.82   1 64.43  ? 46  HIS   A NE2  1 1 
ATOM   360  N  N    . GLY   A 1 48  ? 48.668 32.542 59.955  1 56.41  ? 47  GLY   A N    1 1 
ATOM   361  C  CA   . GLY   A 1 48  ? 48.037 31.286 60.331  1 57.08  ? 47  GLY   A CA   1 1 
ATOM   362  C  C    . GLY   A 1 48  ? 46.939 30.785 59.424  1 57.44  ? 47  GLY   A C    1 1 
ATOM   363  O  O    . GLY   A 1 48  ? 47.135 30.668 58.212  1 57.77  ? 47  GLY   A O    1 1 
ATOM   364  N  N    . ILE   A 1 49  ? 45.773 30.463 60.021  1 57.2   ? 48  ILE   A N    1 1 
ATOM   365  C  CA   . ILE   A 1 49  ? 44.609 29.949 59.295  1 57.18  ? 48  ILE   A CA   1 1 
ATOM   366  C  C    . ILE   A 1 49  ? 44.098 30.959 58.265  1 56.87  ? 48  ILE   A C    1 1 
ATOM   367  O  O    . ILE   A 1 49  ? 43.642 30.551 57.208  1 57.35  ? 48  ILE   A O    1 1 
ATOM   368  C  CB   . ILE   A 1 49  ? 43.482 29.434 60.237  1 57.58  ? 48  ILE   A CB   1 1 
ATOM   369  C  CG1  . ILE   A 1 49  ? 44.058 28.57  61.38   1 58.38  ? 48  ILE   A CG1  1 1 
ATOM   370  C  CG2  . ILE   A 1 49  ? 42.404 28.674 59.445  1 57.81  ? 48  ILE   A CG2  1 1 
ATOM   371  C  CD1  . ILE   A 1 49  ? 43.08  28.149 62.38   1 59.6   ? 48  ILE   A CD1  1 1 
ATOM   372  N  N    . GLY   A 1 50  ? 44.234 32.254 58.543  1 56.04  ? 49  GLY   A N    1 1 
ATOM   373  C  CA   . GLY   A 1 50  ? 43.803 33.282 57.603  1 55.6   ? 49  GLY   A CA   1 1 
ATOM   374  C  C    . GLY   A 1 50  ? 44.748 33.449 56.433  1 54.71  ? 49  GLY   A C    1 1 
ATOM   375  O  O    . GLY   A 1 50  ? 44.308 33.637 55.299  1 54.92  ? 49  GLY   A O    1 1 
ATOM   376  N  N    . ARG   A 1 51  ? 46.051 33.397 56.711  1 53.87  ? 50  ARG   A N    1 1 
ATOM   377  C  CA   . ARG   A 1 51  ? 47.112 33.548 55.727  1 53.89  ? 50  ARG   A CA   1 1 
ATOM   378  C  C    . ARG   A 1 51  ? 47.109 32.385 54.762  1 54.22  ? 50  ARG   A C    1 1 
ATOM   379  O  O    . ARG   A 1 51  ? 47.254 32.587 53.556  1 54.43  ? 50  ARG   A O    1 1 
ATOM   380  C  CB   . ARG   A 1 51  ? 48.48  33.673 56.436  1 54.86  ? 50  ARG   A CB   1 1 
ATOM   381  C  CG   . ARG   A 1 51  ? 49.708 33.356 55.59   1 57     ? 50  ARG   A CG   1 1 
ATOM   382  C  CD   . ARG   A 1 51  ? 50.987 33.727 56.288  1 58.95  ? 50  ARG   A CD   1 1 
ATOM   383  N  NE   . ARG   A 1 51  ? 51.32  35.127 56.046  1 61.19  ? 50  ARG   A NE   1 1 
ATOM   384  C  CZ   . ARG   A 1 51  ? 52.431 35.717 56.469  1 63.46  ? 50  ARG   A CZ   1 1 
ATOM   385  N  NH1  . ARG   A 1 51  ? 53.331 35.033 57.169  1 62.94  ? 50  ARG   A NH1  1 1 
ATOM   386  N  NH2  . ARG   A 1 51  ? 52.65  36.997 56.203  1 63.7   ? 50  ARG   A NH2  1 1 
ATOM   387  N  N    . TRP   A 1 52  ? 46.959 31.166 55.285  1 54.15  ? 51  TRP   A N    1 1 
ATOM   388  C  CA   . TRP   A 1 52  ? 46.978 29.976 54.437  1 54.57  ? 51  TRP   A CA   1 1 
ATOM   389  C  C    . TRP   A 1 52  ? 45.638 29.734 53.706  1 55.03  ? 51  TRP   A C    1 1 
ATOM   390  O  O    . TRP   A 1 52  ? 45.614 29.013 52.703  1 55.4   ? 51  TRP   A O    1 1 
ATOM   391  C  CB   . TRP   A 1 52  ? 47.479 28.758 55.215  1 54.25  ? 51  TRP   A CB   1 1 
ATOM   392  C  CG   . TRP   A 1 52  ? 48.944 28.893 55.502  1 54.36  ? 51  TRP   A CG   1 1 
ATOM   393  C  CD1  . TRP   A 1 52  ? 49.529 29.778 56.357  1 55.15  ? 51  TRP   A CD1  1 1 
ATOM   394  C  CD2  . TRP   A 1 52  ? 50.012 28.246 54.803  1 54.26  ? 51  TRP   A CD2  1 1 
ATOM   395  N  NE1  . TRP   A 1 52  ? 50.896 29.694 56.262  1 55.41  ? 51  TRP   A NE1  1 1 
ATOM   396  C  CE2  . TRP   A 1 52  ? 51.22  28.752 55.321  1 55.09  ? 51  TRP   A CE2  1 1 
ATOM   397  C  CE3  . TRP   A 1 52  ? 50.068 27.289 53.792  1 54.71  ? 51  TRP   A CE3  1 1 
ATOM   398  C  CZ2  . TRP   A 1 52  ? 52.464 28.299 54.889  1 55.69  ? 51  TRP   A CZ2  1 1 
ATOM   399  C  CZ3  . TRP   A 1 52  ? 51.303 26.84  53.368  1 55.56  ? 51  TRP   A CZ3  1 1 
ATOM   400  C  CH2  . TRP   A 1 52  ? 52.481 27.343 53.915  1 55.73  ? 51  TRP   A CH2  1 1 
ATOM   401  N  N    . THR   A 1 53  ? 44.56  30.414 54.129  1 54.75  ? 52  THR   A N    1 1 
ATOM   402  C  CA   . THR   A 1 53  ? 43.292 30.387 53.423  1 55.14  ? 52  THR   A CA   1 1 
ATOM   403  C  C    . THR   A 1 53  ? 43.43  31.283 52.178  1 56.53  ? 52  THR   A C    1 1 
ATOM   404  O  O    . THR   A 1 53  ? 43.051 30.869 51.08   1 56.77  ? 52  THR   A O    1 1 
ATOM   405  C  CB   . THR   A 1 53  ? 42.171 30.748 54.372  1 55.24  ? 52  THR   A CB   1 1 
ATOM   406  O  OG1  . THR   A 1 53  ? 41.824 29.556 55.073  1 55.5   ? 52  THR   A OG1  1 1 
ATOM   407  C  CG2  . THR   A 1 53  ? 40.96  31.313 53.671  1 55.66  ? 52  THR   A CG2  1 1 
ATOM   408  N  N    . ALA   A 1 54  ? 44.065 32.462 52.325  1 57.1   ? 53  ALA   A N    1 1 
ATOM   409  C  CA   . ALA   A 1 54  ? 44.344 33.345 51.192  1 57.83  ? 53  ALA   A CA   1 1 
ATOM   410  C  C    . ALA   A 1 54  ? 45.294 32.669 50.196  1 58.65  ? 53  ALA   A C    1 1 
ATOM   411  O  O    . ALA   A 1 54  ? 45.206 32.945 49.012  1 58.73  ? 53  ALA   A O    1 1 
ATOM   412  C  CB   . ALA   A 1 54  ? 44.933 34.654 51.678  1 57.96  ? 53  ALA   A CB   1 1 
ATOM   413  N  N    . TYR   A 1 55  ? 46.183 31.775 50.656  1 59.38  ? 54  TYR   A N    1 1 
ATOM   414  C  CA   . TYR   A 1 55  ? 47.069 31.038 49.753  1 60.44  ? 54  TYR   A CA   1 1 
ATOM   415  C  C    . TYR   A 1 55  ? 46.234 30.035 48.965  1 60.69  ? 54  TYR   A C    1 1 
ATOM   416  O  O    . TYR   A 1 55  ? 46.449 29.889 47.77   1 60.95  ? 54  TYR   A O    1 1 
ATOM   417  C  CB   . TYR   A 1 55  ? 48.169 30.266 50.51   1 60.97  ? 54  TYR   A CB   1 1 
ATOM   418  C  CG   . TYR   A 1 55  ? 49.227 31.091 51.213  1 62.35  ? 54  TYR   A CG   1 1 
ATOM   419  C  CD1  . TYR   A 1 55  ? 49.433 32.424 50.889  1 63.4   ? 54  TYR   A CD1  1 1 
ATOM   420  C  CD2  . TYR   A 1 55  ? 50.045 30.525 52.175  1 63.8   ? 54  TYR   A CD2  1 1 
ATOM   421  C  CE1  . TYR   A 1 55  ? 50.415 33.178 51.522  1 64.63  ? 54  TYR   A CE1  1 1 
ATOM   422  C  CE2  . TYR   A 1 55  ? 51.018 31.268 52.827  1 65.06  ? 54  TYR   A CE2  1 1 
ATOM   423  C  CZ   . TYR   A 1 55  ? 51.214 32.591 52.489  1 66.14  ? 54  TYR   A CZ   1 1 
ATOM   424  O  OH   . TYR   A 1 55  ? 52.194 33.295 53.157  1 68.04  ? 54  TYR   A OH   1 1 
ATOM   425  N  N    . GLU   A 1 56  ? 45.292 29.338 49.628  1 60.75  ? 55  GLU   A N    1 1 
ATOM   426  C  CA   . GLU   A 1 56  ? 44.439 28.341 48.981  1 61.53  ? 55  GLU   A CA   1 1 
ATOM   427  C  C    . GLU   A 1 56  ? 43.451 28.945 47.995  1 61.97  ? 55  GLU   A C    1 1 
ATOM   428  O  O    . GLU   A 1 56  ? 43.182 28.353 46.943  1 62.44  ? 55  GLU   A O    1 1 
ATOM   429  C  CB   . GLU   A 1 56  ? 43.715 27.472 50.009  1 64.2   ? 55  GLU   A CB   1 1 
ATOM   430  C  CG   . GLU   A 1 56  ? 44.586 26.368 50.574  1 69.77  ? 55  GLU   A CG   1 1 
ATOM   431  C  CD   . GLU   A 1 56  ? 45.002 25.296 49.583  1 76.83  ? 55  GLU   A CD   1 1 
ATOM   432  O  OE1  . GLU   A 1 56  ? 44.303 25.115 48.558  1 77.5   ? 55  GLU   A OE1  1 1 
ATOM   433  O  OE2  . GLU   A 1 56  ? 46.031 24.628 49.842  1 79.68  ? 55  GLU   A OE2  1 1 
ATOM   434  N  N    . PHE   A 1 57  ? 42.928 30.133 48.31   1 61.44  ? 56  PHE   A N    1 1 
ATOM   435  C  CA   . PHE   A 1 57  ? 42.021 30.822 47.398  1 61.19  ? 56  PHE   A CA   1 1 
ATOM   436  C  C    . PHE   A 1 57  ? 42.773 31.35  46.191  1 60.28  ? 56  PHE   A C    1 1 
ATOM   437  O  O    . PHE   A 1 57  ? 42.244 31.283 45.083  1 60.54  ? 56  PHE   A O    1 1 
ATOM   438  C  CB   . PHE   A 1 57  ? 41.265 31.936 48.108  1 61.5   ? 56  PHE   A CB   1 1 
ATOM   439  C  CG   . PHE   A 1 57  ? 40.039 31.426 48.813  1 62.68  ? 56  PHE   A CG   1 1 
ATOM   440  C  CD1  . PHE   A 1 57  ? 39.025 30.808 48.108  1 64.01  ? 56  PHE   A CD1  1 1 
ATOM   441  C  CD2  . PHE   A 1 57  ? 39.887 31.586 50.176  1 63.4   ? 56  PHE   A CD2  1 1 
ATOM   442  C  CE1  . PHE   A 1 57  ? 37.894 30.344 48.76   1 64.83  ? 56  PHE   A CE1  1 1 
ATOM   443  C  CE2  . PHE   A 1 57  ? 38.752 31.123 50.823  1 64.23  ? 56  PHE   A CE2  1 1 
ATOM   444  C  CZ   . PHE   A 1 57  ? 37.767 30.502 50.114  1 64.25  ? 56  PHE   A CZ   1 1 
ATOM   445  N  N    . ALA   A 1 58  ? 44.028 31.814 46.379  1 59.29  ? 57  ALA   A N    1 1 
ATOM   446  C  CA   . ALA   A 1 58  ? 44.879 32.261 45.272  1 58.98  ? 57  ALA   A CA   1 1 
ATOM   447  C  C    . ALA   A 1 58  ? 45.157 31.112 44.286  1 58.42  ? 57  ALA   A C    1 1 
ATOM   448  O  O    . ALA   A 1 58  ? 45.361 31.359 43.098  1 58.33  ? 57  ALA   A O    1 1 
ATOM   449  C  CB   . ALA   A 1 58  ? 46.19  32.825 45.798  1 59.01  ? 57  ALA   A CB   1 1 
ATOM   450  N  N    . LYS   A 1 59  ? 45.164 29.863 44.782  1 57.81  ? 58  LYS   A N    1 1 
ATOM   451  C  CA   . LYS   A 1 59  ? 45.348 28.677 43.963  1 57.98  ? 58  LYS   A CA   1 1 
ATOM   452  C  C    . LYS   A 1 59  ? 44.113 28.452 43.076  1 58.82  ? 58  LYS   A C    1 1 
ATOM   453  O  O    . LYS   A 1 59  ? 44.259 28.042 41.915  1 59.16  ? 58  LYS   A O    1 1 
ATOM   454  C  CB   . LYS   A 1 59  ? 45.63  27.447 44.846  1 58.49  ? 58  LYS   A CB   1 1 
ATOM   455  C  CG   . LYS   A 1 59  ? 47.028 27.452 45.472  1 60.31  ? 58  LYS   A CG   1 1 
ATOM   456  C  CD   . LYS   A 1 59  ? 47.364 26.143 46.177  1 62.29  ? 58  LYS   A CD   1 1 
ATOM   457  C  CE   . LYS   A 1 59  ? 48.844 26.012 46.43   1 64.75  ? 58  LYS   A CE   1 1 
ATOM   458  N  NZ   . LYS   A 1 59  ? 49.173 24.788 47.216  1 66.72  ? 58  LYS   A NZ   1 1 
ATOM   459  N  N    . GLN   A 1 60  ? 42.904 28.757 43.617  1 58.8   ? 59  GLN   A N    1 1 
ATOM   460  C  CA   . GLN   A 1 60  ? 41.602 28.62  42.944  1 59.14  ? 59  GLN   A CA   1 1 
ATOM   461  C  C    . GLN   A 1 60  ? 41.26  29.751 41.945  1 59.34  ? 59  GLN   A C    1 1 
ATOM   462  O  O    . GLN   A 1 60  ? 40.15  29.774 41.406  1 59     ? 59  GLN   A O    1 1 
ATOM   463  C  CB   . GLN   A 1 60  ? 40.489 28.514 43.989  1 60.32  ? 59  GLN   A CB   1 1 
ATOM   464  C  CG   . GLN   A 1 60  ? 40.69  27.38  44.977  1 63.24  ? 59  GLN   A CG   1 1 
ATOM   465  C  CD   . GLN   A 1 60  ? 40.403 26.027 44.364  1 66.41  ? 59  GLN   A CD   1 1 
ATOM   466  O  OE1  . GLN   A 1 60  ? 39.63  25.892 43.401  1 66.67  ? 59  GLN   A OE1  1 1 
ATOM   467  N  NE2  . GLN   A 1 60  ? 41.011 24.989 44.93   1 66.99  ? 59  GLN   A NE2  1 1 
ATOM   468  N  N    . LYS   A 1 61  ? 42.204 30.683 41.721  1 59.43  ? 60  LYS   A N    1 1 
ATOM   469  C  CA   . LYS   A 1 61  ? 42.063 31.828 40.828  1 59.81  ? 60  LYS   A CA   1 1 
ATOM   470  C  C    . LYS   A 1 61  ? 40.909 32.755 41.243  1 59.96  ? 60  LYS   A C    1 1 
ATOM   471  O  O    . LYS   A 1 61  ? 40.046 33.06  40.434  1 60.56  ? 60  LYS   A O    1 1 
ATOM   472  C  CB   . LYS   A 1 61  ? 41.966 31.378 39.362  1 61.98  ? 60  LYS   A CB   1 1 
ATOM   473  C  CG   . LYS   A 1 61  ? 43.16  30.529 38.927  1 66.96  ? 60  LYS   A CG   1 1 
ATOM   474  C  CD   . LYS   A 1 61  ? 43.161 30.249 37.435  1 72.84  ? 60  LYS   A CD   1 1 
ATOM   475  C  CE   . LYS   A 1 61  ? 44.48  29.685 36.935  1 77.23  ? 60  LYS   A CE   1 1 
ATOM   476  N  NZ   . LYS   A 1 61  ? 44.564 29.69  35.439  1 79.54  ? 60  LYS   A NZ   1 1 
ATOM   477  N  N    . SER   A 1 62  ? 40.907 33.208 42.504  1 59.54  ? 61  SER   A N    1 1 
ATOM   478  C  CA   . SER   A 1 62  ? 39.876 34.097 43.048  1 59.42  ? 61  SER   A CA   1 1 
ATOM   479  C  C    . SER   A 1 62  ? 40.358 35.552 43.164  1 59.45  ? 61  SER   A C    1 1 
ATOM   480  O  O    . SER   A 1 62  ? 41.555 35.815 43.066  1 59.83  ? 61  SER   A O    1 1 
ATOM   481  C  CB   . SER   A 1 62  ? 39.447 33.614 44.429  1 60.06  ? 61  SER   A CB   1 1 
ATOM   482  O  OG   . SER   A 1 62  ? 39.103 32.241 44.418  1 61.92  ? 61  SER   A OG   1 1 
ATOM   483  N  N    . ARG   A 1 63  ? 39.424 36.494 43.422  1 58.86  ? 62  ARG   A N    1 1 
ATOM   484  C  CA   . ARG   A 1 63  ? 39.699 37.926 43.618  1 58.54  ? 62  ARG   A CA   1 1 
ATOM   485  C  C    . ARG   A 1 63  ? 39.739 38.312 45.132  1 57.05  ? 62  ARG   A C    1 1 
ATOM   486  O  O    . ARG   A 1 63  ? 38.733 38.738 45.71   1 57.49  ? 62  ARG   A O    1 1 
ATOM   487  C  CB   . ARG   A 1 63  ? 38.707 38.798 42.811  1 60.44  ? 62  ARG   A CB   1 1 
ATOM   488  C  CG   . ARG   A 1 63  ? 39.307 39.279 41.489  1 64.78  ? 62  ARG   A CG   1 1 
ATOM   489  C  CD   . ARG   A 1 63  ? 38.293 39.897 40.553  1 68.74  ? 62  ARG   A CD   1 1 
ATOM   490  N  NE   . ARG   A 1 63  ? 37.727 41.124 41.109  1 72.28  ? 62  ARG   A NE   1 1 
ATOM   491  C  CZ   . ARG   A 1 63  ? 36.795 41.861 40.51   1 75.12  ? 62  ARG   A CZ   1 1 
ATOM   492  N  NH1  . ARG   A 1 63  ? 36.317 41.504 39.321  1 75.06  ? 62  ARG   A NH1  1 1 
ATOM   493  N  NH2  . ARG   A 1 63  ? 36.337 42.962 41.091  1 75.21  ? 62  ARG   A NH2  1 1 
ATOM   494  N  N    . LEU   A 1 64  ? 40.922 38.175 45.756  1 54.94  ? 63  LEU   A N    1 1 
ATOM   495  C  CA   . LEU   A 1 64  ? 41.114 38.411 47.186  1 52.99  ? 63  LEU   A CA   1 1 
ATOM   496  C  C    . LEU   A 1 64  ? 41.125 39.846 47.647  1 52.25  ? 63  LEU   A C    1 1 
ATOM   497  O  O    . LEU   A 1 64  ? 41.653 40.751 47.001  1 52.05  ? 63  LEU   A O    1 1 
ATOM   498  C  CB   . LEU   A 1 64  ? 42.387 37.731 47.679  1 51.97  ? 63  LEU   A CB   1 1 
ATOM   499  C  CG   . LEU   A 1 64  ? 42.375 36.24  47.53   1 51.98  ? 63  LEU   A CG   1 1 
ATOM   500  C  CD1  . LEU   A 1 64  ? 43.739 35.673 47.73   1 52.07  ? 63  LEU   A CD1  1 1 
ATOM   501  C  CD2  . LEU   A 1 64  ? 41.337 35.615 48.422  1 52.41  ? 63  LEU   A CD2  1 1 
ATOM   502  N  N    . VAL   A 1 65  ? 40.557 40.008 48.839  1 51.81  ? 64  VAL   A N    1 1 
ATOM   503  C  CA   . VAL   A 1 65  ? 40.427 41.216 49.637  1 51.57  ? 64  VAL   A CA   1 1 
ATOM   504  C  C    . VAL   A 1 65  ? 40.833 40.763 51.025  1 51.18  ? 64  VAL   A C    1 1 
ATOM   505  O  O    . VAL   A 1 65  ? 40.142 39.923 51.597  1 51.65  ? 64  VAL   A O    1 1 
ATOM   506  C  CB   . VAL   A 1 65  ? 38.959 41.686 49.658  1 52.48  ? 64  VAL   A CB   1 1 
ATOM   507  C  CG1  . VAL   A 1 65  ? 38.793 42.909 50.537  1 52.63  ? 64  VAL   A CG1  1 1 
ATOM   508  C  CG2  . VAL   A 1 65  ? 38.438 41.949 48.246  1 53.63  ? 64  VAL   A CG2  1 1 
ATOM   509  N  N    . LEU   A 1 66  ? 41.949 41.268 51.575  1 50     ? 65  LEU   A N    1 1 
ATOM   510  C  CA   . LEU   A 1 66  ? 42.411 40.813 52.892  1 48.85  ? 65  LEU   A CA   1 1 
ATOM   511  C  C    . LEU   A 1 66  ? 42.344 41.926 53.918  1 48.11  ? 65  LEU   A C    1 1 
ATOM   512  O  O    . LEU   A 1 66  ? 42.771 43.04  53.63   1 48.07  ? 65  LEU   A O    1 1 
ATOM   513  C  CB   . LEU   A 1 66  ? 43.836 40.248 52.816  1 48.76  ? 65  LEU   A CB   1 1 
ATOM   514  C  CG   . LEU   A 1 66  ? 44.249 39.478 51.552  1 50.04  ? 65  LEU   A CG   1 1 
ATOM   515  C  CD1  . LEU   A 1 66  ? 45.719 39.177 51.569  1 50.58  ? 65  LEU   A CD1  1 1 
ATOM   516  C  CD2  . LEU   A 1 66  ? 43.455 38.191 51.379  1 50.61  ? 65  LEU   A CD2  1 1 
ATOM   517  N  N    . TRP   A 1 67  ? 41.805 41.624 55.117  1 47.49  ? 66  TRP   A N    1 1 
ATOM   518  C  CA   . TRP   A 1 67  ? 41.634 42.554 56.238  1 47.31  ? 66  TRP   A CA   1 1 
ATOM   519  C  C    . TRP   A 1 67  ? 42.414 42.075 57.459  1 47.34  ? 66  TRP   A C    1 1 
ATOM   520  O  O    . TRP   A 1 67  ? 42.417 40.882 57.746  1 47.43  ? 66  TRP   A O    1 1 
ATOM   521  C  CB   . TRP   A 1 67  ? 40.145 42.677 56.591  1 47.2   ? 66  TRP   A CB   1 1 
ATOM   522  C  CG   . TRP   A 1 67  ? 39.341 43.565 55.679  1 47.97  ? 66  TRP   A CG   1 1 
ATOM   523  C  CD1  . TRP   A 1 67  ? 39.661 43.978 54.415  1 48.74  ? 66  TRP   A CD1  1 1 
ATOM   524  C  CD2  . TRP   A 1 67  ? 38.047 44.104 55.957  1 48.25  ? 66  TRP   A CD2  1 1 
ATOM   525  N  NE1  . TRP   A 1 67  ? 38.665 44.776 53.912  1 48.88  ? 66  TRP   A NE1  1 1 
ATOM   526  C  CE2  . TRP   A 1 67  ? 37.658 44.866 54.836  1 48.77  ? 66  TRP   A CE2  1 1 
ATOM   527  C  CE3  . TRP   A 1 67  ? 37.185 44.033 57.054  1 49.04  ? 66  TRP   A CE3  1 1 
ATOM   528  C  CZ2  . TRP   A 1 67  ? 36.451 45.557 54.79   1 49.53  ? 66  TRP   A CZ2  1 1 
ATOM   529  C  CZ3  . TRP   A 1 67  ? 35.983 44.709 56.998  1 49.72  ? 66  TRP   A CZ3  1 1 
ATOM   530  C  CH2  . TRP   A 1 67  ? 35.631 45.467 55.881  1 49.68  ? 66  TRP   A CH2  1 1 
ATOM   531  N  N    . ASP   A 1 68  ? 43.081 42.998 58.173  1 47.2   ? 67  ASP   A N    1 1 
ATOM   532  C  CA   . ASP   A 1 68  ? 43.873 42.671 59.363  1 47.63  ? 67  ASP   A CA   1 1 
ATOM   533  C  C    . ASP   A 1 68  ? 44.351 43.944 60.11   1 47.35  ? 67  ASP   A C    1 1 
ATOM   534  O  O    . ASP   A 1 68  ? 44.325 45.035 59.554  1 47.38  ? 67  ASP   A O    1 1 
ATOM   535  C  CB   . ASP   A 1 68  ? 45.093 41.819 58.952  1 49.63  ? 67  ASP   A CB   1 1 
ATOM   536  C  CG   . ASP   A 1 68  ? 45.625 40.936 60.065  1 54.17  ? 67  ASP   A CG   1 1 
ATOM   537  O  OD1  . ASP   A 1 68  ? 45.363 39.724 60.032  1 55.67  ? 67  ASP   A OD1  1 1 
ATOM   538  O  OD2  . ASP   A 1 68  ? 46.312 41.458 60.962  1 54.77  ? 67  ASP   A OD2  1 1 
ATOM   539  N  N    . ILE   A 1 69  ? 44.794 43.804 61.36   1 47.01  ? 68  ILE   A N    1 1 
ATOM   540  C  CA   . ILE   A 1 69  ? 45.36  44.924 62.121  1 47.38  ? 68  ILE   A CA   1 1 
ATOM   541  C  C    . ILE   A 1 69  ? 46.883 45.043 61.875  1 48.35  ? 68  ILE   A C    1 1 
ATOM   542  O  O    . ILE   A 1 69  ? 47.446 46.13  62.024  1 48.74  ? 68  ILE   A O    1 1 
ATOM   543  C  CB   . ILE   A 1 69  ? 45.023 44.834 63.627  1 47.21  ? 68  ILE   A CB   1 1 
ATOM   544  C  CG1  . ILE   A 1 69  ? 45.417 43.461 64.21   1 47.79  ? 68  ILE   A CG1  1 1 
ATOM   545  C  CG2  . ILE   A 1 69  ? 43.557 45.153 63.879  1 47.27  ? 68  ILE   A CG2  1 1 
ATOM   546  C  CD1  . ILE   A 1 69  ? 46.667 43.49  65.172  1 48.85  ? 68  ILE   A CD1  1 1 
ATOM   547  N  N    . ASN   A 1 70  ? 47.538 43.919 61.497  1 48.5   ? 69  ASN   A N    1 1 
ATOM   548  C  CA   . ASN   A 1 70  ? 48.961 43.801 61.209  1 49.06  ? 69  ASN   A CA   1 1 
ATOM   549  C  C    . ASN   A 1 70  ? 49.178 44.188 59.781  1 49.62  ? 69  ASN   A C    1 1 
ATOM   550  O  O    . ASN   A 1 70  ? 48.984 43.355 58.895  1 50.18  ? 69  ASN   A O    1 1 
ATOM   551  C  CB   . ASN   A 1 70  ? 49.406 42.354 61.409  1 50.08  ? 69  ASN   A CB   1 1 
ATOM   552  C  CG   . ASN   A 1 70  ? 50.889 42.168 61.47   1 53.55  ? 69  ASN   A CG   1 1 
ATOM   553  O  OD1  . ASN   A 1 70  ? 51.648 42.787 60.73   1 54.02  ? 69  ASN   A OD1  1 1 
ATOM   554  N  ND2  . ASN   A 1 70  ? 51.34  41.29  62.348  1 55.48  ? 69  ASN   A ND2  1 1 
ATOM   555  N  N    . LYS   A 1 71  ? 49.583 45.438 59.535  1 49.58  ? 70  LYS   A N    1 1 
ATOM   556  C  CA   . LYS   A 1 71  ? 49.799 45.901 58.16   1 50.09  ? 70  LYS   A CA   1 1 
ATOM   557  C  C    . LYS   A 1 71  ? 50.846 45.079 57.415  1 51.06  ? 70  LYS   A C    1 1 
ATOM   558  O  O    . LYS   A 1 71  ? 50.609 44.689 56.285  1 51.45  ? 70  LYS   A O    1 1 
ATOM   559  C  CB   . LYS   A 1 71  ? 50.154 47.395 58.129  1 51.01  ? 70  LYS   A CB   1 1 
ATOM   560  C  CG   . LYS   A 1 71  ? 50.356 47.958 56.737  1 52.97  ? 70  LYS   A CG   1 1 
ATOM   561  C  CD   . LYS   A 1 71  ? 50.229 49.461 56.738  1 56.87  ? 70  LYS   A CD   1 1 
ATOM   562  C  CE   . LYS   A 1 71  ? 50.192 50.045 55.351  1 61.71  ? 70  LYS   A CE   1 1 
ATOM   563  N  NZ   . LYS   A 1 71  ? 51.485 49.849 54.664  1 64.44  ? 70  LYS   A NZ   1 1 
ATOM   564  N  N    . HIS   A 1 72  ? 51.969 44.77  58.065  1 51.83  ? 71  HIS   A N    1 1 
ATOM   565  C  CA   . HIS   A 1 72  ? 53.079 44.003 57.5    1 53.2   ? 71  HIS   A CA   1 1 
ATOM   566  C  C    . HIS   A 1 72  ? 52.713 42.556 57.151  1 55.08  ? 71  HIS   A C    1 1 
ATOM   567  O  O    . HIS   A 1 72  ? 53.051 42.078 56.067  1 55.68  ? 71  HIS   A O    1 1 
ATOM   568  C  CB   . HIS   A 1 72  ? 54.282 44.062 58.454  1 53.78  ? 71  HIS   A CB   1 1 
ATOM   569  C  CG   . HIS   A 1 72  ? 55.461 43.254 58.023  1 55.83  ? 71  HIS   A CG   1 1 
ATOM   570  N  ND1  . HIS   A 1 72  ? 56.389 43.754 57.126  1 57.62  ? 71  HIS   A ND1  1 1 
ATOM   571  C  CD2  . HIS   A 1 72  ? 55.847 42.017 58.412  1 57.06  ? 71  HIS   A CD2  1 1 
ATOM   572  C  CE1  . HIS   A 1 72  ? 57.3   42.805 56.985  1 58.18  ? 71  HIS   A CE1  1 1 
ATOM   573  N  NE2  . HIS   A 1 72  ? 57.01  41.735 57.73   1 58.24  ? 71  HIS   A NE2  1 1 
ATOM   574  N  N    . GLY   A 1 73  ? 52.023 41.889 58.062  1 56.14  ? 72  GLY   A N    1 1 
ATOM   575  C  CA   . GLY   A 1 73  ? 51.61  40.501 57.924  1 57.82  ? 72  GLY   A CA   1 1 
ATOM   576  C  C    . GLY   A 1 73  ? 50.644 40.281 56.787  1 59.78  ? 72  GLY   A C    1 1 
ATOM   577  O  O    . GLY   A 1 73  ? 50.858 39.389 55.958  1 60.28  ? 72  GLY   A O    1 1 
ATOM   578  N  N    . VAL   A 1 74  ? 49.59  41.118 56.716  1 60.65  ? 73  VAL   A N    1 1 
ATOM   579  C  CA   . VAL   A 1 74  ? 48.587 41.027 55.649  1 61.69  ? 73  VAL   A CA   1 1 
ATOM   580  C  C    . VAL   A 1 74  ? 49.163 41.437 54.278  1 62.24  ? 73  VAL   A C    1 1 
ATOM   581  O  O    . VAL   A 1 74  ? 48.741 40.903 53.252  1 62.19  ? 73  VAL   A O    1 1 
ATOM   582  C  CB   . VAL   A 1 74  ? 47.289 41.788 56.006  1 62.54  ? 73  VAL   A CB   1 1 
ATOM   583  C  CG1  . VAL   A 1 74  ? 47.419 43.283 55.74   1 63.13  ? 73  VAL   A CG1  1 1 
ATOM   584  C  CG2  . VAL   A 1 74  ? 46.11  41.208 55.25   1 63.13  ? 73  VAL   A CG2  1 1 
ATOM   585  N  N    . GLU   A 1 75  ? 50.157 42.342 54.27   1 62.74  ? 74  GLU   A N    1 1 
ATOM   586  C  CA   . GLU   A 1 75  ? 50.812 42.761 53.037  1 63.91  ? 74  GLU   A CA   1 1 
ATOM   587  C  C    . GLU   A 1 75  ? 51.701 41.646 52.491  1 65.01  ? 74  GLU   A C    1 1 
ATOM   588  O  O    . GLU   A 1 75  ? 51.775 41.455 51.269  1 65     ? 74  GLU   A O    1 1 
ATOM   589  C  CB   . GLU   A 1 75  ? 51.619 44.045 53.254  1 65.64  ? 74  GLU   A CB   1 1 
ATOM   590  C  CG   . GLU   A 1 75  ? 50.759 45.287 53.108  1 69.83  ? 74  GLU   A CG   1 1 
ATOM   591  C  CD   . GLU   A 1 75  ? 51.489 46.604 53.273  1 75.86  ? 74  GLU   A CD   1 1 
ATOM   592  O  OE1  . GLU   A 1 75  ? 52.689 46.588 53.635  1 76.38  ? 74  GLU   A OE1  1 1 
ATOM   593  O  OE2  . GLU   A 1 75  ? 50.854 47.658 53.037  1 78.53  ? 74  GLU   A OE2  1 1 
ATOM   594  N  N    . GLU   A 1 76  ? 52.361 40.897 53.4    1 65.35  ? 75  GLU   A N    1 1 
ATOM   595  C  CA   . GLU   A 1 76  ? 53.206 39.772 53.01   1 65.94  ? 75  GLU   A CA   1 1 
ATOM   596  C  C    . GLU   A 1 76  ? 52.386 38.566 52.537  1 65.96  ? 75  GLU   A C    1 1 
ATOM   597  O  O    . GLU   A 1 76  ? 52.852 37.808 51.678  1 65.99  ? 75  GLU   A O    1 1 
ATOM   598  C  CB   . GLU   A 1 76  ? 54.173 39.396 54.124  1 68.06  ? 75  GLU   A CB   1 1 
ATOM   599  C  CG   . GLU   A 1 76  ? 55.387 40.297 54.139  1 73.51  ? 75  GLU   A CG   1 1 
ATOM   600  C  CD   . GLU   A 1 76  ? 56.579 39.699 54.854  1 81.88  ? 75  GLU   A CD   1 1 
ATOM   601  O  OE1  . GLU   A 1 76  ? 56.375 38.965 55.849  1 83.72  ? 75  GLU   A OE1  1 1 
ATOM   602  O  OE2  . GLU   A 1 76  ? 57.722 39.969 54.42   1 84.76  ? 75  GLU   A OE2  1 1 
ATOM   603  N  N    . THR   A 1 77  ? 51.151 38.406 53.058  1 65.53  ? 76  THR   A N    1 1 
ATOM   604  C  CA   . THR   A 1 77  ? 50.276 37.337 52.593  1 65.59  ? 76  THR   A CA   1 1 
ATOM   605  C  C    . THR   A 1 77  ? 49.851 37.672 51.169  1 66.17  ? 76  THR   A C    1 1 
ATOM   606  O  O    . THR   A 1 77  ? 49.961 36.819 50.292  1 66.26  ? 76  THR   A O    1 1 
ATOM   607  C  CB   . THR   A 1 77  ? 49.071 37.166 53.508  1 66.2   ? 76  THR   A CB   1 1 
ATOM   608  O  OG1  . THR   A 1 77  ? 49.528 36.833 54.815  1 66.84  ? 76  THR   A OG1  1 1 
ATOM   609  C  CG2  . THR   A 1 77  ? 48.129 36.091 53.007  1 66.61  ? 76  THR   A CG2  1 1 
ATOM   610  N  N    . ALA   A 1 78  ? 49.445 38.946 50.93   1 66.3   ? 77  ALA   A N    1 1 
ATOM   611  C  CA   . ALA   A 1 78  ? 49.065 39.472 49.616  1 66.53  ? 77  ALA   A CA   1 1 
ATOM   612  C  C    . ALA   A 1 78  ? 50.218 39.323 48.642  1 67.23  ? 77  ALA   A C    1 1 
ATOM   613  O  O    . ALA   A 1 78  ? 49.986 39.015 47.478  1 67.41  ? 77  ALA   A O    1 1 
ATOM   614  C  CB   . ALA   A 1 78  ? 48.688 40.938 49.728  1 66.4   ? 77  ALA   A CB   1 1 
ATOM   615  N  N    . ALA   A 1 79  ? 51.457 39.535 49.106  1 67.41  ? 78  ALA   A N    1 1 
ATOM   616  C  CA   . ALA   A 1 79  ? 52.635 39.382 48.268  1 68.09  ? 78  ALA   A CA   1 1 
ATOM   617  C  C    . ALA   A 1 79  ? 52.773 37.937 47.788  1 68.6   ? 78  ALA   A C    1 1 
ATOM   618  O  O    . ALA   A 1 79  ? 52.981 37.731 46.595  1 69     ? 78  ALA   A O    1 1 
ATOM   619  C  CB   . ALA   A 1 79  ? 53.883 39.817 49.021  1 68.22  ? 78  ALA   A CB   1 1 
ATOM   620  N  N    . GLU   A 1 80  ? 52.608 36.939 48.683  1 68.42  ? 79  GLU   A N    1 1 
ATOM   621  C  CA   . GLU   A 1 80  ? 52.703 35.535 48.262  1 68.79  ? 79  GLU   A CA   1 1 
ATOM   622  C  C    . GLU   A 1 80  ? 51.447 35.064 47.482  1 68.35  ? 79  GLU   A C    1 1 
ATOM   623  O  O    . GLU   A 1 80  ? 51.525 34.144 46.667  1 68.3   ? 79  GLU   A O    1 1 
ATOM   624  C  CB   . GLU   A 1 80  ? 53.058 34.599 49.435  1 71.74  ? 79  GLU   A CB   1 1 
ATOM   625  C  CG   . GLU   A 1 80  ? 53.545 33.211 49.016  1 78.5   ? 79  GLU   A CG   1 1 
ATOM   626  C  CD   . GLU   A 1 80  ? 54.466 33.093 47.806  1 87.25  ? 79  GLU   A CD   1 1 
ATOM   627  O  OE1  . GLU   A 1 80  ? 54.012 32.583 46.754  1 88.04  ? 79  GLU   A OE1  1 1 
ATOM   628  O  OE2  . GLU   A 1 80  ? 55.645 33.503 47.911  1 90.92  ? 79  GLU   A OE2  1 1 
ATOM   629  N  N    . CYS   A 1 81  ? 50.312 35.731 47.687  1 67.94  ? 80  CYS   A N    1 1 
ATOM   630  C  CA   . CYS   A 1 81  ? 49.093 35.444 46.935  1 68     ? 80  CYS   A CA   1 1 
ATOM   631  C  C    . CYS   A 1 81  ? 49.21  35.999 45.518  1 67.24  ? 80  CYS   A C    1 1 
ATOM   632  O  O    . CYS   A 1 81  ? 48.685 35.392 44.592  1 67.31  ? 80  CYS   A O    1 1 
ATOM   633  C  CB   . CYS   A 1 81  ? 47.869 35.999 47.654  1 69.41  ? 80  CYS   A CB   1 1 
ATOM   634  S  SG   . CYS   A 1 81  ? 47.538 35.227 49.257  1 73.67  ? 80  CYS   A SG   1 1 
ATOM   635  N  N    . ARG   A 1 82  ? 49.909 37.139 45.349  1 66.56  ? 81  ARG   A N    1 1 
ATOM   636  C  CA   . ARG   A 1 82  ? 50.192 37.75  44.055  1 66.5   ? 81  ARG   A CA   1 1 
ATOM   637  C  C    . ARG   A 1 82  ? 51.173 36.861 43.289  1 66.32  ? 81  ARG   A C    1 1 
ATOM   638  O  O    . ARG   A 1 82  ? 50.982 36.626 42.096  1 66.35  ? 81  ARG   A O    1 1 
ATOM   639  C  CB   . ARG   A 1 82  ? 50.784 39.151 44.233  1 67.75  ? 81  ARG   A CB   1 1 
ATOM   640  C  CG   . ARG   A 1 82  ? 49.741 40.201 44.539  1 71.06  ? 81  ARG   A CG   1 1 
ATOM   641  C  CD   . ARG   A 1 82  ? 50.396 41.522 44.851  1 74.5   ? 81  ARG   A CD   1 1 
ATOM   642  N  NE   . ARG   A 1 82  ? 49.429 42.499 45.342  1 77.55  ? 81  ARG   A NE   1 1 
ATOM   643  C  CZ   . ARG   A 1 82  ? 49.55  43.16  46.485  1 80.55  ? 81  ARG   A CZ   1 1 
ATOM   644  N  NH1  . ARG   A 1 82  ? 50.601 42.957 47.27   1 80.88  ? 81  ARG   A NH1  1 1 
ATOM   645  N  NH2  . ARG   A 1 82  ? 48.623 44.031 46.854  1 81.02  ? 81  ARG   A NH2  1 1 
ATOM   646  N  N    . LYS   A 1 83  ? 52.197 36.323 43.983  1 66.07  ? 82  LYS   A N    1 1 
ATOM   647  C  CA   . LYS   A 1 83  ? 53.161 35.4   43.375  1 66.29  ? 82  LYS   A CA   1 1 
ATOM   648  C  C    . LYS   A 1 83  ? 52.518 34.079 42.883  1 65.71  ? 82  LYS   A C    1 1 
ATOM   649  O  O    . LYS   A 1 83  ? 53.198 33.255 42.285  1 65.92  ? 82  LYS   A O    1 1 
ATOM   650  C  CB   . LYS   A 1 83  ? 54.352 35.129 44.316  1 68.88  ? 82  LYS   A CB   1 1 
ATOM   651  C  CG   . LYS   A 1 83  ? 55.187 36.373 44.624  1 74.48  ? 82  LYS   A CG   1 1 
ATOM   652  C  CD   . LYS   A 1 83  ? 56.643 36.045 44.993  1 80.57  ? 82  LYS   A CD   1 1 
ATOM   653  C  CE   . LYS   A 1 83  ? 57.545 35.969 43.764  1 85.03  ? 82  LYS   A CE   1 1 
ATOM   654  N  NZ   . LYS   A 1 83  ? 58.986 35.77  44.112  1 87.56  ? 82  LYS   A NZ   1 1 
ATOM   655  N  N    . LEU   A 1 84  ? 51.214 33.89  43.123  1 65.06  ? 83  LEU   A N    1 1 
ATOM   656  C  CA   . LEU   A 1 84  ? 50.442 32.744 42.661  1 65.2   ? 83  LEU   A CA   1 1 
ATOM   657  C  C    . LEU   A 1 84  ? 49.536 33.091 41.44   1 66.23  ? 83  LEU   A C    1 1 
ATOM   658  O  O    . LEU   A 1 84  ? 49.096 32.194 40.719  1 66.5   ? 83  LEU   A O    1 1 
ATOM   659  C  CB   . LEU   A 1 84  ? 49.601 32.164 43.804  1 64.67  ? 83  LEU   A CB   1 1 
ATOM   660  C  CG   . LEU   A 1 84  ? 50.361 31.533 44.953  1 64.95  ? 83  LEU   A CG   1 1 
ATOM   661  C  CD1  . LEU   A 1 84  ? 49.408 30.999 45.966  1 65.24  ? 83  LEU   A CD1  1 1 
ATOM   662  C  CD2  . LEU   A 1 84  ? 51.264 30.413 44.471  1 65.13  ? 83  LEU   A CD2  1 1 
ATOM   663  N  N    . GLY   A 1 85  ? 49.275 34.378 41.22   1 66.45  ? 84  GLY   A N    1 1 
ATOM   664  C  CA   . GLY   A 1 85  ? 48.468 34.832 40.099  1 67.05  ? 84  GLY   A CA   1 1 
ATOM   665  C  C    . GLY   A 1 85  ? 47.173 35.521 40.472  1 67.54  ? 84  GLY   A C    1 1 
ATOM   666  O  O    . GLY   A 1 85  ? 46.486 36.047 39.594  1 68.32  ? 84  GLY   A O    1 1 
ATOM   667  N  N    . ALA   A 1 86  ? 46.817 35.526 41.758  1 67.14  ? 85  ALA   A N    1 1 
ATOM   668  C  CA   . ALA   A 1 86  ? 45.577 36.146 42.214  1 67.34  ? 85  ALA   A CA   1 1 
ATOM   669  C  C    . ALA   A 1 86  ? 45.64  37.669 42.243  1 67.19  ? 85  ALA   A C    1 1 
ATOM   670  O  O    . ALA   A 1 86  ? 46.716 38.249 42.364  1 67.26  ? 85  ALA   A O    1 1 
ATOM   671  C  CB   . ALA   A 1 86  ? 45.207 35.617 43.593  1 67.57  ? 85  ALA   A CB   1 1 
ATOM   672  N  N    . THR   A 1 87  ? 44.481 38.305 42.083  1 66.91  ? 86  THR   A N    1 1 
ATOM   673  C  CA   . THR   A 1 87  ? 44.351 39.749 42.167  1 67.46  ? 86  THR   A CA   1 1 
ATOM   674  C  C    . THR   A 1 87  ? 44.11  39.98  43.641  1 67.74  ? 86  THR   A C    1 1 
ATOM   675  O  O    . THR   A 1 87  ? 43.116 39.473 44.159  1 68.08  ? 86  THR   A O    1 1 
ATOM   676  C  CB   . THR   A 1 87  ? 43.127 40.207 41.355  1 69.11  ? 86  THR   A CB   1 1 
ATOM   677  O  OG1  . THR   A 1 87  ? 43.412 40.127 39.948  1 70.27  ? 86  THR   A OG1  1 1 
ATOM   678  C  CG2  . THR   A 1 87  ? 42.663 41.622 41.73   1 69.49  ? 86  THR   A CG2  1 1 
ATOM   679  N  N    . VAL   A 1 88  ? 45.034 40.646 44.353  1 67.6   ? 87  VAL   A N    1 1 
ATOM   680  C  CA   . VAL   A 1 88  ? 44.86  40.838 45.8    1 67.94  ? 87  VAL   A CA   1 1 
ATOM   681  C  C    . VAL   A 1 88  ? 44.928 42.299 46.209  1 68.32  ? 87  VAL   A C    1 1 
ATOM   682  O  O    . VAL   A 1 88  ? 45.863 42.995 45.819  1 68.78  ? 87  VAL   A O    1 1 
ATOM   683  C  CB   . VAL   A 1 88  ? 45.85  39.993 46.629  1 68.5   ? 87  VAL   A CB   1 1 
ATOM   684  C  CG1  . VAL   A 1 88  ? 45.486 40.04  48.1    1 69.05  ? 87  VAL   A CG1  1 1 
ATOM   685  C  CG2  . VAL   A 1 88  ? 45.895 38.552 46.141  1 68.96  ? 87  VAL   A CG2  1 1 
ATOM   686  N  N    . HIS   A 1 89  ? 43.942 42.769 46.984  1 68.03  ? 88  HIS   A N    1 1 
ATOM   687  C  CA   . HIS   A 1 89  ? 43.917 44.149 47.459  1 68.44  ? 88  HIS   A CA   1 1 
ATOM   688  C  C    . HIS   A 1 89  ? 43.659 44.119 48.952  1 67.71  ? 88  HIS   A C    1 1 
ATOM   689  O  O    . HIS   A 1 89  ? 42.687 43.513 49.382  1 67.3   ? 88  HIS   A O    1 1 
ATOM   690  C  CB   . HIS   A 1 89  ? 42.851 44.965 46.713  1 70.41  ? 88  HIS   A CB   1 1 
ATOM   691  C  CG   . HIS   A 1 89  ? 42.997 44.919 45.216  1 74.78  ? 88  HIS   A CG   1 1 
ATOM   692  N  ND1  . HIS   A 1 89  ? 41.981 44.429 44.4    1 77.3   ? 88  HIS   A ND1  1 1 
ATOM   693  C  CD2  . HIS   A 1 89  ? 44.047 45.277 44.433  1 76.39  ? 88  HIS   A CD2  1 1 
ATOM   694  C  CE1  . HIS   A 1 89  ? 42.438 44.519 43.156  1 77.94  ? 88  HIS   A CE1  1 1 
ATOM   695  N  NE2  . HIS   A 1 89  ? 43.677 45.021 43.124  1 77.82  ? 88  HIS   A NE2  1 1 
ATOM   696  N  N    . THR   A 1 90  ? 44.555 44.717 49.745  1 67.48  ? 89  THR   A N    1 1 
ATOM   697  C  CA   . THR   A 1 90  ? 44.466 44.681 51.206  1 67.91  ? 89  THR   A CA   1 1 
ATOM   698  C  C    . THR   A 1 90  ? 44.046 45.992 51.863  1 67.9   ? 89  THR   A C    1 1 
ATOM   699  O  O    . THR   A 1 90  ? 44.239 47.055 51.268  1 67.99  ? 89  THR   A O    1 1 
ATOM   700  C  CB   . THR   A 1 90  ? 45.791 44.201 51.793  1 69.49  ? 89  THR   A CB   1 1 
ATOM   701  O  OG1  . THR   A 1 90  ? 46.814 45.141 51.467  1 70.45  ? 89  THR   A OG1  1 1 
ATOM   702  C  CG2  . THR   A 1 90  ? 46.168 42.83  51.304  1 70.09  ? 89  THR   A CG2  1 1 
ATOM   703  N  N    . PHE   A 1 91  ? 43.509 45.907 53.124  1 67.55  ? 90  PHE   A N    1 1 
ATOM   704  C  CA   . PHE   A 1 91  ? 43.026 47.034 53.932  1 67.6   ? 90  PHE   A CA   1 1 
ATOM   705  C  C    . PHE   A 1 91  ? 43.298 46.767 55.41   1 66.83  ? 90  PHE   A C    1 1 
ATOM   706  O  O    . PHE   A 1 91  ? 42.931 45.703 55.899  1 66.84  ? 90  PHE   A O    1 1 
ATOM   707  C  CB   . PHE   A 1 91  ? 41.505 47.203 53.753  1 68.08  ? 90  PHE   A CB   1 1 
ATOM   708  C  CG   . PHE   A 1 91  ? 41.018 47.275 52.325  1 69.59  ? 90  PHE   A CG   1 1 
ATOM   709  C  CD1  . PHE   A 1 91  ? 41.115 48.449 51.599  1 70.76  ? 90  PHE   A CD1  1 1 
ATOM   710  C  CD2  . PHE   A 1 91  ? 40.473 46.167 51.705  1 70.97  ? 90  PHE   A CD2  1 1 
ATOM   711  C  CE1  . PHE   A 1 91  ? 40.679 48.51  50.273  1 71.74  ? 90  PHE   A CE1  1 1 
ATOM   712  C  CE2  . PHE   A 1 91  ? 40.048 46.229 50.374  1 72.1   ? 90  PHE   A CE2  1 1 
ATOM   713  C  CZ   . PHE   A 1 91  ? 40.141 47.402 49.671  1 71.79  ? 90  PHE   A CZ   1 1 
ATOM   714  N  N    . VAL   A 1 92  ? 43.906 47.721 56.129  1 66.16  ? 91  VAL   A N    1 1 
ATOM   715  C  CA   . VAL   A 1 92  ? 44.136 47.555 57.571  1 66.3   ? 91  VAL   A CA   1 1 
ATOM   716  C  C    . VAL   A 1 92  ? 42.852 47.909 58.299  1 66.1   ? 91  VAL   A C    1 1 
ATOM   717  O  O    . VAL   A 1 92  ? 42.488 49.083 58.386  1 66.38  ? 91  VAL   A O    1 1 
ATOM   718  C  CB   . VAL   A 1 92  ? 45.325 48.378 58.102  1 66.95  ? 91  VAL   A CB   1 1 
ATOM   719  C  CG1  . VAL   A 1 92  ? 45.46  48.245 59.608  1 67.06  ? 91  VAL   A CG1  1 1 
ATOM   720  C  CG2  . VAL   A 1 92  ? 46.609 47.953 57.417  1 67.73  ? 91  VAL   A CG2  1 1 
ATOM   721  N  N    . VAL   A 1 93  ? 42.124 46.887 58.762  1 65.32  ? 92  VAL   A N    1 1 
ATOM   722  C  CA   . VAL   A 1 93  ? 40.822 47.082 59.4    1 64.65  ? 92  VAL   A CA   1 1 
ATOM   723  C  C    . VAL   A 1 93  ? 40.765 46.443 60.772  1 63.74  ? 92  VAL   A C    1 1 
ATOM   724  O  O    . VAL   A 1 93  ? 41.055 45.258 60.902  1 63.43  ? 92  VAL   A O    1 1 
ATOM   725  C  CB   . VAL   A 1 93  ? 39.676 46.509 58.514  1 65.06  ? 92  VAL   A CB   1 1 
ATOM   726  C  CG1  . VAL   A 1 93  ? 38.31  46.864 59.082  1 65.56  ? 92  VAL   A CG1  1 1 
ATOM   727  C  CG2  . VAL   A 1 93  ? 39.798 46.963 57.067  1 65.13  ? 92  VAL   A CG2  1 1 
ATOM   728  N  N    . ASP   A 1 94  ? 40.337 47.202 61.784  1 63.33  ? 93  ASP   A N    1 1 
ATOM   729  C  CA   . ASP   A 1 94  ? 40.148 46.654 63.126  1 63.58  ? 93  ASP   A CA   1 1 
ATOM   730  C  C    . ASP   A 1 94  ? 38.84  45.886 63.038  1 63.22  ? 93  ASP   A C    1 1 
ATOM   731  O  O    . ASP   A 1 94  ? 37.77  46.484 63.149  1 63.3   ? 93  ASP   A O    1 1 
ATOM   732  C  CB   . ASP   A 1 94  ? 40.02  47.793 64.148  1 65.55  ? 93  ASP   A CB   1 1 
ATOM   733  C  CG   . ASP   A 1 94  ? 39.924 47.361 65.599  1 69.63  ? 93  ASP   A CG   1 1 
ATOM   734  O  OD1  . ASP   A 1 94  ? 40.149 46.165 65.878  1 70.83  ? 93  ASP   A OD1  1 1 
ATOM   735  O  OD2  . ASP   A 1 94  ? 39.642 48.226 66.457  1 70.77  ? 93  ASP   A OD2  1 1 
ATOM   736  N  N    . CYS   A 1 95  ? 38.924 44.569 62.788  1 62.66  ? 94  CYS   A N    1 1 
ATOM   737  C  CA   . CYS   A 1 95  ? 37.758 43.706 62.575  1 62.51  ? 94  CYS   A CA   1 1 
ATOM   738  C  C    . CYS   A 1 95  ? 36.928 43.418 63.844  1 61.55  ? 94  CYS   A C    1 1 
ATOM   739  O  O    . CYS   A 1 95  ? 36.157 42.457 63.875  1 62.19  ? 94  CYS   A O    1 1 
ATOM   740  C  CB   . CYS   A 1 95  ? 38.158 42.416 61.864  1 63.66  ? 94  CYS   A CB   1 1 
ATOM   741  S  SG   . CYS   A 1 95  ? 39.061 42.675 60.308  1 67.61  ? 94  CYS   A SG   1 1 
ATOM   742  N  N    . GLY   A 1 96  ? 37.061 44.277 64.842  1 59.66  ? 95  GLY   A N    1 1 
ATOM   743  C  CA   . GLY   A 1 96  ? 36.276 44.238 66.066  1 58.51  ? 95  GLY   A CA   1 1 
ATOM   744  C  C    . GLY   A 1 96  ? 35.457 45.509 66.236  1 57.17  ? 95  GLY   A C    1 1 
ATOM   745  O  O    . GLY   A 1 96  ? 34.412 45.492 66.901  1 56.35  ? 95  GLY   A O    1 1 
ATOM   746  N  N    . ASN   A 1 97  ? 35.947 46.632 65.621  1 56.76  ? 96  ASN   A N    1 1 
ATOM   747  C  CA   . ASN   A 1 97  ? 35.352 47.968 65.626  1 56.71  ? 96  ASN   A CA   1 1 
ATOM   748  C  C    . ASN   A 1 97  ? 34.324 48.105 64.516  1 56.46  ? 96  ASN   A C    1 1 
ATOM   749  O  O    . ASN   A 1 97  ? 34.672 48.035 63.35   1 56.27  ? 96  ASN   A O    1 1 
ATOM   750  C  CB   . ASN   A 1 97  ? 36.421 49.048 65.479  1 57.49  ? 96  ASN   A CB   1 1 
ATOM   751  C  CG   . ASN   A 1 97  ? 35.878 50.443 65.661  1 60.36  ? 96  ASN   A CG   1 1 
ATOM   752  O  OD1  . ASN   A 1 97  ? 36.154 51.35  64.868  1 61.19  ? 96  ASN   A OD1  1 1 
ATOM   753  N  ND2  . ASN   A 1 97  ? 35.079 50.647 66.709  1 60.97  ? 96  ASN   A ND2  1 1 
ATOM   754  N  N    . ARG   A 1 98  ? 33.063 48.313 64.897  1 56.4   ? 97  ARG   A N    1 1 
ATOM   755  C  CA   . ARG   A 1 98  ? 31.897 48.425 64.037  1 56.78  ? 97  ARG   A CA   1 1 
ATOM   756  C  C    . ARG   A 1 98  ? 31.975 49.595 63.073  1 57.25  ? 97  ARG   A C    1 1 
ATOM   757  O  O    . ARG   A 1 98  ? 31.694 49.42  61.889  1 57.45  ? 97  ARG   A O    1 1 
ATOM   758  C  CB   . ARG   A 1 98  ? 30.643 48.525 64.911  1 58.21  ? 97  ARG   A CB   1 1 
ATOM   759  C  CG   . ARG   A 1 98  ? 29.338 48.415 64.152  1 61.32  ? 97  ARG   A CG   1 1 
ATOM   760  C  CD   . ARG   A 1 98  ? 28.13  48.647 65.049  1 64.15  ? 97  ARG   A CD   1 1 
ATOM   761  N  NE   . ARG   A 1 98  ? 28.197 49.952 65.703  1 67.27  ? 97  ARG   A NE   1 1 
ATOM   762  C  CZ   . ARG   A 1 98  ? 27.711 51.078 65.19   1 70.55  ? 97  ARG   A CZ   1 1 
ATOM   763  N  NH1  . ARG   A 1 98  ? 27.076 51.065 64.026  1 70.33  ? 97  ARG   A NH1  1 1 
ATOM   764  N  NH2  . ARG   A 1 98  ? 27.842 52.223 65.844  1 71.83  ? 97  ARG   A NH2  1 1 
ATOM   765  N  N    . GLU   A 1 99  ? 32.375 50.78  63.552  1 57.32  ? 98  GLU   A N    1 1 
ATOM   766  C  CA   . GLU   A 1 99  ? 32.479 51.951 62.677  1 57.82  ? 98  GLU   A CA   1 1 
ATOM   767  C  C    . GLU   A 1 99  ? 33.661 51.861 61.702  1 57.96  ? 98  GLU   A C    1 1 
ATOM   768  O  O    . GLU   A 1 99  ? 33.612 52.469 60.641  1 57.8   ? 98  GLU   A O    1 1 
ATOM   769  C  CB   . GLU   A 1 99  ? 32.494 53.257 63.483  1 60.16  ? 98  GLU   A CB   1 1 
ATOM   770  C  CG   . GLU   A 1 99  ? 31.197 53.506 64.243  1 65.02  ? 98  GLU   A CG   1 1 
ATOM   771  C  CD   . GLU   A 1 99  ? 31.213 54.712 65.171  1 70.74  ? 98  GLU   A CD   1 1 
ATOM   772  O  OE1  . GLU   A 1 99  ? 30.812 54.561 66.348  1 71.36  ? 98  GLU   A OE1  1 1 
ATOM   773  O  OE2  . GLU   A 1 99  ? 31.636 55.805 64.724  1 72.72  ? 98  GLU   A OE2  1 1 
ATOM   774  N  N    . ASP   A 1 100 ? 34.706 51.089 62.045  1 58.25  ? 99  ASP   A N    1 1 
ATOM   775  C  CA   . ASP   A 1 100 ? 35.856 50.894 61.156  1 58.98  ? 99  ASP   A CA   1 1 
ATOM   776  C  C    . ASP   A 1 100 ? 35.469 49.883 60.084  1 59.64  ? 99  ASP   A C    1 1 
ATOM   777  O  O    . ASP   A 1 100 ? 35.774 50.107 58.911  1 60.01  ? 99  ASP   A O    1 1 
ATOM   778  C  CB   . ASP   A 1 100 ? 37.1   50.395 61.928  1 60.58  ? 99  ASP   A CB   1 1 
ATOM   779  C  CG   . ASP   A 1 100 ? 38.43  50.544 61.199  1 64.36  ? 99  ASP   A CG   1 1 
ATOM   780  O  OD1  . ASP   A 1 100 ? 38.418 50.936 59.996  1 65.16  ? 99  ASP   A OD1  1 1 
ATOM   781  O  OD2  . ASP   A 1 100 ? 39.486 50.278 61.828  1 65.53  ? 99  ASP   A OD2  1 1 
ATOM   782  N  N    . ILE   A 1 101 ? 34.785 48.783 60.472  1 59.56  ? 100 ILE   A N    1 1 
ATOM   783  C  CA   . ILE   A 1 101 ? 34.337 47.76  59.534  1 60.11  ? 100 ILE   A CA   1 1 
ATOM   784  C  C    . ILE   A 1 101 ? 33.423 48.375 58.455  1 61.46  ? 100 ILE   A C    1 1 
ATOM   785  O  O    . ILE   A 1 101 ? 33.683 48.191 57.267  1 61.86  ? 100 ILE   A O    1 1 
ATOM   786  C  CB   . ILE   A 1 101 ? 33.67  46.58  60.272  1 60.2   ? 100 ILE   A CB   1 1 
ATOM   787  C  CG1  . ILE   A 1 101 ? 34.699 45.769 61.05   1 60.86  ? 100 ILE   A CG1  1 1 
ATOM   788  C  CG2  . ILE   A 1 101 ? 32.911 45.679 59.308  1 60.81  ? 100 ILE   A CG2  1 1 
ATOM   789  C  CD1  . ILE   A 1 101 ? 34.072 44.805 62.035  1 61.86  ? 100 ILE   A CD1  1 1 
ATOM   790  N  N    . TYR   A 1 102 ? 32.407 49.157 58.864  1 61.91  ? 101 TYR   A N    1 1 
ATOM   791  C  CA   . TYR   A 1 102 ? 31.467 49.816 57.946  1 62.65  ? 101 TYR   A CA   1 1 
ATOM   792  C  C    . TYR   A 1 102 ? 32.154 50.837 57.058  1 63.09  ? 101 TYR   A C    1 1 
ATOM   793  O  O    . TYR   A 1 102 ? 31.827 50.946 55.876  1 63.32  ? 101 TYR   A O    1 1 
ATOM   794  C  CB   . TYR   A 1 102 ? 30.3   50.467 58.718  1 62.91  ? 101 TYR   A CB   1 1 
ATOM   795  C  CG   . TYR   A 1 102 ? 29.37  49.481 59.403  1 63.63  ? 101 TYR   A CG   1 1 
ATOM   796  C  CD1  . TYR   A 1 102 ? 29.233 48.18  58.936  1 64.63  ? 101 TYR   A CD1  1 1 
ATOM   797  C  CD2  . TYR   A 1 102 ? 28.585 49.867 60.478  1 64.09  ? 101 TYR   A CD2  1 1 
ATOM   798  C  CE1  . TYR   A 1 102 ? 28.379 47.278 59.549  1 65.28  ? 101 TYR   A CE1  1 1 
ATOM   799  C  CE2  . TYR   A 1 102 ? 27.711 48.977 61.085  1 64.92  ? 101 TYR   A CE2  1 1 
ATOM   800  C  CZ   . TYR   A 1 102 ? 27.624 47.676 60.627  1 65.89  ? 101 TYR   A CZ   1 1 
ATOM   801  O  OH   . TYR   A 1 102 ? 26.776 46.773 61.21   1 67.47  ? 101 TYR   A OH   1 1 
ATOM   802  N  N    . ASN   A 1 103 ? 33.127 51.555 57.616  1 63.15  ? 102 ASN   A N    1 1 
ATOM   803  C  CA   . ASN   A 1 103 ? 33.904 52.534 56.876  1 64     ? 102 ASN   A CA   1 1 
ATOM   804  C  C    . ASN   A 1 103 ? 34.716 51.847 55.779  1 64.32  ? 102 ASN   A C    1 1 
ATOM   805  O  O    . ASN   A 1 103 ? 34.798 52.366 54.669  1 64.66  ? 102 ASN   A O    1 1 
ATOM   806  C  CB   . ASN   A 1 103 ? 34.839 53.267 57.821  1 65.5   ? 102 ASN   A CB   1 1 
ATOM   807  C  CG   . ASN   A 1 103 ? 34.866 54.755 57.618  1 69.1   ? 102 ASN   A CG   1 1 
ATOM   808  O  OD1  . ASN   A 1 103 ? 35.195 55.262 56.53   1 69.96  ? 102 ASN   A OD1  1 1 
ATOM   809  N  ND2  . ASN   A 1 103 ? 34.54  55.486 58.676  1 70.07  ? 102 ASN   A ND2  1 1 
ATOM   810  N  N    . SER   A 1 104 ? 35.293 50.675 56.078  1 64.18  ? 103 SER   A N    1 1 
ATOM   811  C  CA   . SER   A 1 104 ? 36.102 49.923 55.123  1 64.75  ? 103 SER   A CA   1 1 
ATOM   812  C  C    . SER   A 1 104 ? 35.281 49.12  54.118  1 65.06  ? 103 SER   A C    1 1 
ATOM   813  O  O    . SER   A 1 104 ? 35.787 48.807 53.04   1 64.64  ? 103 SER   A O    1 1 
ATOM   814  C  CB   . SER   A 1 104 ? 37.085 49.019 55.85   1 66.28  ? 103 SER   A CB   1 1 
ATOM   815  O  OG   . SER   A 1 104 ? 37.972 49.774 56.659  1 68.79  ? 103 SER   A OG   1 1 
ATOM   816  N  N    . VAL   A 1 105 ? 34.016 48.798 54.453  1 65.5   ? 104 VAL   A N    1 1 
ATOM   817  C  CA   . VAL   A 1 105 ? 33.121 48.101 53.52   1 66.23  ? 104 VAL   A CA   1 1 
ATOM   818  C  C    . VAL   A 1 105 ? 32.828 49.049 52.338  1 65.86  ? 104 VAL   A C    1 1 
ATOM   819  O  O    . VAL   A 1 105 ? 32.91  48.636 51.185  1 65.8   ? 104 VAL   A O    1 1 
ATOM   820  C  CB   . VAL   A 1 105 ? 31.821 47.593 54.215  1 67.44  ? 104 VAL   A CB   1 1 
ATOM   821  C  CG1  . VAL   A 1 105 ? 30.72  47.282 53.192  1 68.33  ? 104 VAL   A CG1  1 1 
ATOM   822  C  CG2  . VAL   A 1 105 ? 32.109 46.368 55.074  1 67.8   ? 104 VAL   A CG2  1 1 
ATOM   823  N  N    . LYS   A 1 106 ? 32.58  50.334 52.63   1 65.43  ? 105 LYS   A N    1 1 
ATOM   824  C  CA   . LYS   A 1 106 ? 32.35  51.334 51.605  1 65.53  ? 105 LYS   A CA   1 1 
ATOM   825  C  C    . LYS   A 1 106 ? 33.601 51.554 50.738  1 65.23  ? 105 LYS   A C    1 1 
ATOM   826  O  O    . LYS   A 1 106 ? 33.463 51.855 49.561  1 65.48  ? 105 LYS   A O    1 1 
ATOM   827  C  CB   . LYS   A 1 106 ? 31.807 52.64  52.212  1 67.62  ? 105 LYS   A CB   1 1 
ATOM   828  C  CG   . LYS   A 1 106 ? 30.383 52.503 52.761  1 71.8   ? 105 LYS   A CG   1 1 
ATOM   829  C  CD   . LYS   A 1 106 ? 29.763 53.842 53.216  1 75.83  ? 105 LYS   A CD   1 1 
ATOM   830  C  CE   . LYS   A 1 106 ? 28.658 53.671 54.248  1 77.96  ? 105 LYS   A CE   1 1 
ATOM   831  N  NZ   . LYS   A 1 106 ? 27.877 54.922 54.45   1 78.8   ? 105 LYS   A NZ   1 1 
ATOM   832  N  N    . GLN   A 1 107 ? 34.802 51.367 51.292  1 64.86  ? 106 GLN   A N    1 1 
ATOM   833  C  CA   . GLN   A 1 107 ? 36.043 51.456 50.519  1 65.48  ? 106 GLN   A CA   1 1 
ATOM   834  C  C    . GLN   A 1 107 ? 36.233 50.187 49.654  1 64.97  ? 106 GLN   A C    1 1 
ATOM   835  O  O    . GLN   A 1 107 ? 36.811 50.25  48.569  1 64.46  ? 106 GLN   A O    1 1 
ATOM   836  C  CB   . GLN   A 1 107 ? 37.254 51.643 51.443  1 68.35  ? 106 GLN   A CB   1 1 
ATOM   837  C  CG   . GLN   A 1 107 ? 38.557 51.895 50.664  1 73.53  ? 106 GLN   A CG   1 1 
ATOM   838  C  CD   . GLN   A 1 107 ? 39.842 51.756 51.467  1 79.2   ? 106 GLN   A CD   1 1 
ATOM   839  O  OE1  . GLN   A 1 107 ? 40.941 51.749 50.897  1 81.42  ? 106 GLN   A OE1  1 1 
ATOM   840  N  NE2  . GLN   A 1 107 ? 39.752 51.658 52.795  1 79.68  ? 106 GLN   A NE2  1 1 
ATOM   841  N  N    . VAL   A 1 108 ? 35.749 49.037 50.144  1 64.81  ? 107 VAL   A N    1 1 
ATOM   842  C  CA   . VAL   A 1 108 ? 35.779 47.774 49.418  1 64.82  ? 107 VAL   A CA   1 1 
ATOM   843  C  C    . VAL   A 1 108 ? 34.866 47.912 48.196  1 64.28  ? 107 VAL   A C    1 1 
ATOM   844  O  O    . VAL   A 1 108 ? 35.249 47.487 47.126  1 64.86  ? 107 VAL   A O    1 1 
ATOM   845  C  CB   . VAL   A 1 108 ? 35.391 46.583 50.35   1 65.83  ? 107 VAL   A CB   1 1 
ATOM   846  C  CG1  . VAL   A 1 108 ? 34.782 45.413 49.578  1 66.59  ? 107 VAL   A CG1  1 1 
ATOM   847  C  CG2  . VAL   A 1 108 ? 36.585 46.118 51.17   1 66.13  ? 107 VAL   A CG2  1 1 
ATOM   848  N  N    . LYS   A 1 109 ? 33.691 48.543 48.335  1 63.44  ? 108 LYS   A N    1 1 
ATOM   849  C  CA   . LYS   A 1 109 ? 32.772 48.745 47.216  1 63.21  ? 108 LYS   A CA   1 1 
ATOM   850  C  C    . LYS   A 1 109 ? 33.239 49.86  46.266  1 63.53  ? 108 LYS   A C    1 1 
ATOM   851  O  O    . LYS   A 1 109 ? 32.963 49.796 45.064  1 63.83  ? 108 LYS   A O    1 1 
ATOM   852  C  CB   . LYS   A 1 109 ? 31.34  48.948 47.711  1 64.52  ? 108 LYS   A CB   1 1 
ATOM   853  C  CG   . LYS   A 1 109 ? 30.886 47.758 48.559  1 68.57  ? 108 LYS   A CG   1 1 
ATOM   854  C  CD   . LYS   A 1 109 ? 29.409 47.783 48.931  1 72.72  ? 108 LYS   A CD   1 1 
ATOM   855  C  CE   . LYS   A 1 109 ? 29.006 46.502 49.625  1 76.09  ? 108 LYS   A CE   1 1 
ATOM   856  N  NZ   . LYS   A 1 109 ? 27.543 46.448 49.898  1 77.85  ? 108 LYS   A NZ   1 1 
ATOM   857  N  N    . LYS   A 1 110 ? 34.007 50.836 46.779  1 63.31  ? 109 LYS   A N    1 1 
ATOM   858  C  CA   . LYS   A 1 110 ? 34.589 51.905 45.96   1 63.82  ? 109 LYS   A CA   1 1 
ATOM   859  C  C    . LYS   A 1 110 ? 35.944 51.482 45.314  1 64.05  ? 109 LYS   A C    1 1 
ATOM   860  O  O    . LYS   A 1 110 ? 36.552 52.287 44.607  1 64.84  ? 109 LYS   A O    1 1 
ATOM   861  C  CB   . LYS   A 1 110 ? 34.753 53.197 46.775  1 64.53  ? 109 LYS   A CB   1 1 
ATOM   862  C  CG   . LYS   A 1 110 ? 34.405 54.469 46.015  1 67.25  ? 109 LYS   A CG   1 1 
ATOM   863  C  CD   . LYS   A 1 110 ? 35.651 55.296 45.702  1 71.37  ? 109 LYS   A CD   1 1 
ATOM   864  C  CE   . LYS   A 1 110 ? 35.493 56.181 44.472  1 76.19  ? 109 LYS   A CE   1 1 
ATOM   865  N  NZ   . LYS   A 1 110 ? 35.689 55.46  43.159  1 78.35  ? 109 LYS   A NZ   1 1 
ATOM   866  N  N    . GLU   A 1 111 ? 36.413 50.231 45.531  1 63.16  ? 110 GLU   A N    1 1 
ATOM   867  C  CA   . GLU   A 1 111 ? 37.669 49.78  44.931  1 62.65  ? 110 GLU   A CA   1 1 
ATOM   868  C  C    . GLU   A 1 111 ? 37.576 48.405 44.277  1 61.89  ? 110 GLU   A C    1 1 
ATOM   869  O  O    . GLU   A 1 111 ? 37.92  48.266 43.106  1 62.04  ? 110 GLU   A O    1 1 
ATOM   870  C  CB   . GLU   A 1 111 ? 38.829 49.839 45.931  1 64.69  ? 110 GLU   A CB   1 1 
ATOM   871  C  CG   . GLU   A 1 111 ? 39.674 51.085 45.769  1 69.04  ? 110 GLU   A CG   1 1 
ATOM   872  C  CD   . GLU   A 1 111 ? 41.139 50.879 46.091  1 75.14  ? 110 GLU   A CD   1 1 
ATOM   873  O  OE1  . GLU   A 1 111 ? 41.993 51.266 45.26   1 76.47  ? 110 GLU   A OE1  1 1 
ATOM   874  O  OE2  . GLU   A 1 111 ? 41.435 50.315 47.169  1 77.24  ? 110 GLU   A OE2  1 1 
ATOM   875  N  N    . VAL   A 1 112 ? 37.12  47.397 45.017  1 60.93  ? 111 VAL   A N    1 1 
ATOM   876  C  CA   . VAL   A 1 112 ? 37.002 46.042 44.505  1 60.85  ? 111 VAL   A CA   1 1 
ATOM   877  C  C    . VAL   A 1 112 ? 35.601 45.765 43.925  1 61.07  ? 111 VAL   A C    1 1 
ATOM   878  O  O    . VAL   A 1 112 ? 35.468 45.312 42.785  1 60.93  ? 111 VAL   A O    1 1 
ATOM   879  C  CB   . VAL   A 1 112 ? 37.423 45.026 45.593  1 61.01  ? 111 VAL   A CB   1 1 
ATOM   880  C  CG1  . VAL   A 1 112 ? 37.142 43.594 45.165  1 61.5   ? 111 VAL   A CG1  1 1 
ATOM   881  C  CG2  . VAL   A 1 112 ? 38.89  45.199 45.951  1 61.38  ? 111 VAL   A CG2  1 1 
ATOM   882  N  N    . GLY   A 1 113 ? 34.576 46.083 44.701  1 61.11  ? 112 GLY   A N    1 1 
ATOM   883  C  CA   . GLY   A 1 113 ? 33.188 45.868 44.313  1 61.87  ? 112 GLY   A CA   1 1 
ATOM   884  C  C    . GLY   A 1 113 ? 32.367 45.272 45.445  1 62.53  ? 112 GLY   A C    1 1 
ATOM   885  O  O    . GLY   A 1 113 ? 32.582 45.608 46.611  1 62.81  ? 112 GLY   A O    1 1 
ATOM   886  N  N    . ASP   A 1 114 ? 31.436 44.366 45.128  1 62.62  ? 113 ASP   A N    1 1 
ATOM   887  C  CA   . ASP   A 1 114 ? 30.606 43.727 46.152  1 63.05  ? 113 ASP   A CA   1 1 
ATOM   888  C  C    . ASP   A 1 114 ? 31.179 42.34  46.518  1 62.8   ? 113 ASP   A C    1 1 
ATOM   889  O  O    . ASP   A 1 114 ? 31.303 41.483 45.648  1 63.08  ? 113 ASP   A O    1 1 
ATOM   890  C  CB   . ASP   A 1 114 ? 29.157 43.596 45.652  1 65     ? 113 ASP   A CB   1 1 
ATOM   891  C  CG   . ASP   A 1 114 ? 28.541 44.886 45.148  1 69.29  ? 113 ASP   A CG   1 1 
ATOM   892  O  OD1  . ASP   A 1 114 ? 28.854 45.953 45.716  1 70.33  ? 113 ASP   A OD1  1 1 
ATOM   893  O  OD2  . ASP   A 1 114 ? 27.724 44.823 44.208  1 71.02  ? 113 ASP   A OD2  1 1 
ATOM   894  N  N    . VAL   A 1 115 ? 31.532 42.12  47.788  1 62.2   ? 114 VAL   A N    1 1 
ATOM   895  C  CA   . VAL   A 1 115 ? 32.097 40.835 48.219  1 62.12  ? 114 VAL   A CA   1 1 
ATOM   896  C  C    . VAL   A 1 115 ? 31.12  39.674 47.982  1 61.85  ? 114 VAL   A C    1 1 
ATOM   897  O  O    . VAL   A 1 115 ? 29.925 39.847 48.208  1 62.02  ? 114 VAL   A O    1 1 
ATOM   898  C  CB   . VAL   A 1 115 ? 32.565 40.914 49.692  1 62.71  ? 114 VAL   A CB   1 1 
ATOM   899  C  CG1  . VAL   A 1 115 ? 32.99  39.556 50.223  1 62.95  ? 114 VAL   A CG1  1 1 
ATOM   900  C  CG2  . VAL   A 1 115 ? 33.683 41.928 49.848  1 63.22  ? 114 VAL   A CG2  1 1 
ATOM   901  N  N    . THR   A 1 116 ? 31.606 38.522 47.467  1 61.28  ? 115 THR   A N    1 1 
ATOM   902  C  CA   . THR   A 1 116 ? 30.746 37.357 47.192  1 61.1   ? 115 THR   A CA   1 1 
ATOM   903  C  C    . THR   A 1 116 ? 31.013 36.15  48.099  1 60.4   ? 115 THR   A C    1 1 
ATOM   904  O  O    . THR   A 1 116 ? 30.218 35.215 48.087  1 60.53  ? 115 THR   A O    1 1 
ATOM   905  C  CB   . THR   A 1 116 ? 30.792 36.932 45.714  1 62.44  ? 115 THR   A CB   1 1 
ATOM   906  O  OG1  . THR   A 1 116 ? 32.011 36.245 45.436  1 63.34  ? 115 THR   A OG1  1 1 
ATOM   907  C  CG2  . THR   A 1 116 ? 30.624 38.097 44.767  1 62.99  ? 115 THR   A CG2  1 1 
ATOM   908  N  N    . ILE   A 1 117 ? 32.15  36.135 48.82   1 59.45  ? 116 ILE   A N    1 1 
ATOM   909  C  CA   . ILE   A 1 117 ? 32.515 35.065 49.756  1 59.16  ? 116 ILE   A CA   1 1 
ATOM   910  C  C    . ILE   A 1 117 ? 33.156 35.741 50.959  1 58.78  ? 116 ILE   A C    1 1 
ATOM   911  O  O    . ILE   A 1 117 ? 34.103 36.5   50.779  1 59.01  ? 116 ILE   A O    1 1 
ATOM   912  C  CB   . ILE   A 1 117 ? 33.501 34.023 49.142  1 59.54  ? 116 ILE   A CB   1 1 
ATOM   913  C  CG1  . ILE   A 1 117 ? 32.858 33.198 48.017  1 60.38  ? 116 ILE   A CG1  1 1 
ATOM   914  C  CG2  . ILE   A 1 117 ? 34.066 33.092 50.221  1 59.95  ? 116 ILE   A CG2  1 1 
ATOM   915  C  CD1  . ILE   A 1 117 ? 33.821 32.3   47.253  1 61.53  ? 116 ILE   A CD1  1 1 
ATOM   916  N  N    . LEU   A 1 118 ? 32.662 35.471 52.177  1 58.01  ? 117 LEU   A N    1 1 
ATOM   917  C  CA   . LEU   A 1 118 ? 33.234 36.06  53.39   1 57.38  ? 117 LEU   A CA   1 1 
ATOM   918  C  C    . LEU   A 1 118 ? 33.89  34.985 54.262  1 56.51  ? 117 LEU   A C    1 1 
ATOM   919  O  O    . LEU   A 1 118 ? 33.327 33.913 54.444  1 56.64  ? 117 LEU   A O    1 1 
ATOM   920  C  CB   . LEU   A 1 118 ? 32.154 36.812 54.185  1 57.35  ? 117 LEU   A CB   1 1 
ATOM   921  C  CG   . LEU   A 1 118 ? 32.594 37.429 55.519  1 58.63  ? 117 LEU   A CG   1 1 
ATOM   922  C  CD1  . LEU   A 1 118 ? 33.713 38.427 55.328  1 58.79  ? 117 LEU   A CD1  1 1 
ATOM   923  C  CD2  . LEU   A 1 118 ? 31.434 38.103 56.21   1 59.46  ? 117 LEU   A CD2  1 1 
ATOM   924  N  N    . VAL   A 1 119 ? 35.094 35.259 54.768  1 55.39  ? 118 VAL   A N    1 1 
ATOM   925  C  CA   . VAL   A 1 119 ? 35.819 34.342 55.636  1 54.84  ? 118 VAL   A CA   1 1 
ATOM   926  C  C    . VAL   A 1 119 ? 36.094 35.067 56.951  1 54.29  ? 118 VAL   A C    1 1 
ATOM   927  O  O    . VAL   A 1 119 ? 37.084 35.792 57.056  1 54.73  ? 118 VAL   A O    1 1 
ATOM   928  C  CB   . VAL   A 1 119 ? 37.122 33.833 54.973  1 55.5   ? 118 VAL   A CB   1 1 
ATOM   929  C  CG1  . VAL   A 1 119 ? 37.903 32.923 55.919  1 55.95  ? 118 VAL   A CG1  1 1 
ATOM   930  C  CG2  . VAL   A 1 119 ? 36.823 33.115 53.654  1 56.01  ? 118 VAL   A CG2  1 1 
ATOM   931  N  N    . ASN   A 1 120 ? 35.194 34.928 57.942  1 53.02  ? 119 ASN   A N    1 1 
ATOM   932  C  CA   . ASN   A 1 120 ? 35.347 35.588 59.237  1 52.07  ? 119 ASN   A CA   1 1 
ATOM   933  C  C    . ASN   A 1 120 ? 36.339 34.803 60.087  1 52.93  ? 119 ASN   A C    1 1 
ATOM   934  O  O    . ASN   A 1 120 ? 35.965 34.152 61.054  1 53.25  ? 119 ASN   A O    1 1 
ATOM   935  C  CB   . ASN   A 1 120 ? 34.001 35.706 59.937  1 50.67  ? 119 ASN   A CB   1 1 
ATOM   936  C  CG   . ASN   A 1 120 ? 33.075 36.715 59.331  1 49.25  ? 119 ASN   A CG   1 1 
ATOM   937  O  OD1  . ASN   A 1 120 ? 31.889 36.459 59.111  1 48.89  ? 119 ASN   A OD1  1 1 
ATOM   938  N  ND2  . ASN   A 1 120 ? 33.593 37.887 59.075  1 48.46  ? 119 ASN   A ND2  1 1 
ATOM   939  N  N    . ASN   A 1 121 ? 37.605 34.854 59.712  1 53.32  ? 120 ASN   A N    1 1 
ATOM   940  C  CA   . ASN   A 1 121 ? 38.674 34.118 60.361  1 54.2   ? 120 ASN   A CA   1 1 
ATOM   941  C  C    . ASN   A 1 121 ? 39.118 34.762 61.668  1 55.34  ? 120 ASN   A C    1 1 
ATOM   942  O  O    . ASN   A 1 121 ? 39.091 34.093 62.705  1 55.98  ? 120 ASN   A O    1 1 
ATOM   943  C  CB   . ASN   A 1 121 ? 39.841 33.924 59.386  1 54.98  ? 120 ASN   A CB   1 1 
ATOM   944  C  CG   . ASN   A 1 121 ? 41.014 33.152 59.929  1 56.98  ? 120 ASN   A CG   1 1 
ATOM   945  O  OD1  . ASN   A 1 121 ? 41.053 31.922 59.854  1 58.12  ? 120 ASN   A OD1  1 1 
ATOM   946  N  ND2  . ASN   A 1 121 ? 42.023 33.85  60.44   1 56.76  ? 120 ASN   A ND2  1 1 
ATOM   947  N  N    . ALA   A 1 122 ? 39.468 36.075 61.645  1 55.27  ? 121 ALA   A N    1 1 
ATOM   948  C  CA   . ALA   A 1 122 ? 39.955 36.872 62.793  1 55.26  ? 121 ALA   A CA   1 1 
ATOM   949  C  C    . ALA   A 1 122 ? 39.479 36.401 64.161  1 55.19  ? 121 ALA   A C    1 1 
ATOM   950  O  O    . ALA   A 1 122 ? 38.326 35.993 64.308  1 55.46  ? 121 ALA   A O    1 1 
ATOM   951  C  CB   . ALA   A 1 122 ? 39.62  38.346 62.607  1 55.3   ? 121 ALA   A CB   1 1 
ATOM   952  N  N    . GLY   A 1 123 ? 40.392 36.415 65.126  1 54.69  ? 122 GLY   A N    1 1 
ATOM   953  C  CA   . GLY   A 1 123 ? 40.124 36.005 66.491  1 54.53  ? 122 GLY   A CA   1 1 
ATOM   954  C  C    . GLY   A 1 123 ? 41.185 36.484 67.462  1 54.71  ? 122 GLY   A C    1 1 
ATOM   955  O  O    . GLY   A 1 123 ? 42.295 36.836 67.057  1 54.63  ? 122 GLY   A O    1 1 
ATOM   956  N  N    . THR   A 1 124 ? 40.843 36.502 68.762  1 54.68  ? 123 THR   A N    1 1 
ATOM   957  C  CA   . THR   A 1 124 ? 41.755 36.881 69.84   1 55.13  ? 123 THR   A CA   1 1 
ATOM   958  C  C    . THR   A 1 124 ? 41.534 35.95  71.047  1 55.78  ? 123 THR   A C    1 1 
ATOM   959  O  O    . THR   A 1 124 ? 40.413 35.493 71.286  1 55.76  ? 123 THR   A O    1 1 
ATOM   960  C  CB   . THR   A 1 124 ? 41.686 38.399 70.143  1 55.94  ? 123 THR   A CB   1 1 
ATOM   961  O  OG1  . THR   A 1 124 ? 42.937 38.851 70.663  1 56.45  ? 123 THR   A OG1  1 1 
ATOM   962  C  CG2  . THR   A 1 124 ? 40.575 38.768 71.09   1 56.48  ? 123 THR   A CG2  1 1 
ATOM   963  N  N    . VAL   A 1 125 ? 42.615 35.604 71.753  1 56.29  ? 124 VAL   A N    1 1 
ATOM   964  C  CA   . VAL   A 1 125 ? 42.528 34.709 72.898  1 57.62  ? 124 VAL   A CA   1 1 
ATOM   965  C  C    . VAL   A 1 125 ? 43.352 35.247 74.065  1 60.09  ? 124 VAL   A C    1 1 
ATOM   966  O  O    . VAL   A 1 125 ? 44.445 35.776 73.873  1 59.83  ? 124 VAL   A O    1 1 
ATOM   967  C  CB   . VAL   A 1 125 ? 42.917 33.251 72.545  1 57.61  ? 124 VAL   A CB   1 1 
ATOM   968  C  CG1  . VAL   A 1 125 ? 44.428 33.078 72.471  1 58     ? 124 VAL   A CG1  1 1 
ATOM   969  C  CG2  . VAL   A 1 125 ? 42.327 32.269 73.538  1 57.83  ? 124 VAL   A CG2  1 1 
ATOM   970  N  N    . TYR   A 1 126 ? 42.816 35.119 75.281  1 62.21  ? 125 TYR   A N    1 1 
ATOM   971  C  CA   . TYR   A 1 126 ? 43.491 35.556 76.493  1 64.37  ? 125 TYR   A CA   1 1 
ATOM   972  C  C    . TYR   A 1 126 ? 43.381 34.429 77.501  1 66.74  ? 125 TYR   A C    1 1 
ATOM   973  O  O    . TYR   A 1 126 ? 42.53  34.473 78.391  1 67.28  ? 125 TYR   A O    1 1 
ATOM   974  C  CB   . TYR   A 1 126 ? 42.857 36.846 77.012  1 64.46  ? 125 TYR   A CB   1 1 
ATOM   975  C  CG   . TYR   A 1 126 ? 43.028 37.986 76.034  1 65.53  ? 125 TYR   A CG   1 1 
ATOM   976  C  CD1  . TYR   A 1 126 ? 44.284 38.5   75.749  1 66.44  ? 125 TYR   A CD1  1 1 
ATOM   977  C  CD2  . TYR   A 1 126 ? 41.946 38.491 75.33   1 66.6   ? 125 TYR   A CD2  1 1 
ATOM   978  C  CE1  . TYR   A 1 126 ? 44.454 39.525 74.832  1 67.34  ? 125 TYR   A CE1  1 1 
ATOM   979  C  CE2  . TYR   A 1 126 ? 42.099 39.534 74.43   1 67.66  ? 125 TYR   A CE2  1 1 
ATOM   980  C  CZ   . TYR   A 1 126 ? 43.357 40.048 74.183  1 68.7   ? 125 TYR   A CZ   1 1 
ATOM   981  O  OH   . TYR   A 1 126 ? 43.534 41.071 73.286  1 71.1   ? 125 TYR   A OH   1 1 
ATOM   982  N  N    . PRO   A 1 127 ? 44.203 33.37  77.329  1 67.97  ? 126 PRO   A N    1 1 
ATOM   983  C  CA   . PRO   A 1 127 ? 44.11  32.208 78.227  1 68.95  ? 126 PRO   A CA   1 1 
ATOM   984  C  C    . PRO   A 1 127 ? 44.325 32.474 79.717  1 70.19  ? 126 PRO   A C    1 1 
ATOM   985  O  O    . PRO   A 1 127 ? 45.452 32.737 80.12   1 70.6   ? 126 PRO   A O    1 1 
ATOM   986  C  CB   . PRO   A 1 127 ? 45.175 31.244 77.677  1 69.4   ? 126 PRO   A CB   1 1 
ATOM   987  C  CG   . PRO   A 1 127 ? 45.44  31.693 76.283  1 69.5   ? 126 PRO   A CG   1 1 
ATOM   988  C  CD   . PRO   A 1 127 ? 45.244 33.171 76.298  1 67.68  ? 126 PRO   A CD   1 1 
ATOM   989  N  N    . ALA   A 1 128 ? 43.251 32.367 80.535  1 70.66  ? 127 ALA   A N    1 1 
ATOM   990  C  CA   . ALA   A 1 128 ? 43.292 32.541 81.997  1 71.51  ? 127 ALA   A CA   1 1 
ATOM   991  C  C    . ALA   A 1 128 ? 42.021 32.004 82.684  1 72.06  ? 127 ALA   A C    1 1 
ATOM   992  O  O    . ALA   A 1 128 ? 40.982 31.875 82.033  1 72.1   ? 127 ALA   A O    1 1 
ATOM   993  C  CB   . ALA   A 1 128 ? 43.483 34.016 82.352  1 71.78  ? 127 ALA   A CB   1 1 
ATOM   994  N  N    . ASP   A 1 129 ? 42.092 31.703 84      1 72.37  ? 128 ASP   A N    1 1 
ATOM   995  C  CA   . ASP   A 1 129 ? 40.904 31.262 84.745  1 72.92  ? 128 ASP   A CA   1 1 
ATOM   996  C  C    . ASP   A 1 129 ? 39.938 32.435 84.905  1 72.41  ? 128 ASP   A C    1 1 
ATOM   997  O  O    . ASP   A 1 129 ? 40.361 33.592 84.845  1 72.64  ? 128 ASP   A O    1 1 
ATOM   998  C  CB   . ASP   A 1 129 ? 41.252 30.647 86.107  1 75.45  ? 128 ASP   A CB   1 1 
ATOM   999  C  CG   . ASP   A 1 129 ? 42.016 31.581 87.017  1 82.44  ? 128 ASP   A CG   1 1 
ATOM   1000 O  OD1  . ASP   A 1 129 ? 43.04  32.135 86.564  1 84.13  ? 128 ASP   A OD1  1 1 
ATOM   1001 O  OD2  . ASP   A 1 129 ? 41.602 31.739 88.201  1 84.87  ? 128 ASP   A OD2  1 1 
ATOM   1002 N  N    . LEU   A 1 130 ? 38.642 32.154 85.102  1 71.5   ? 129 LEU   A N    1 1 
ATOM   1003 C  CA   . LEU   A 1 130 ? 37.633 33.209 85.175  1 71.07  ? 129 LEU   A CA   1 1 
ATOM   1004 C  C    . LEU   A 1 130 ? 37.938 34.313 86.17   1 71.01  ? 129 LEU   A C    1 1 
ATOM   1005 O  O    . LEU   A 1 130 ? 37.493 35.439 85.976  1 71.08  ? 129 LEU   A O    1 1 
ATOM   1006 C  CB   . LEU   A 1 130 ? 36.239 32.647 85.434  1 70.82  ? 129 LEU   A CB   1 1 
ATOM   1007 C  CG   . LEU   A 1 130 ? 35.125 33.493 84.852  1 71.6   ? 129 LEU   A CG   1 1 
ATOM   1008 C  CD1  . LEU   A 1 130 ? 34.629 32.91  83.57   1 71.79  ? 129 LEU   A CD1  1 1 
ATOM   1009 C  CD2  . LEU   A 1 130 ? 34.001 33.665 85.835  1 72.2   ? 129 LEU   A CD2  1 1 
ATOM   1010 N  N    . LEU   A 1 131 ? 38.734 34.017 87.198  1 70.83  ? 130 LEU   A N    1 1 
ATOM   1011 C  CA   . LEU   A 1 131 ? 39.061 35.005 88.223  1 71.03  ? 130 LEU   A CA   1 1 
ATOM   1012 C  C    . LEU   A 1 131 ? 40.344 35.804 87.937  1 70.96  ? 130 LEU   A C    1 1 
ATOM   1013 O  O    . LEU   A 1 131 ? 40.541 36.862 88.534  1 71.02  ? 130 LEU   A O    1 1 
ATOM   1014 C  CB   . LEU   A 1 131 ? 39.095 34.339 89.596  1 71.31  ? 130 LEU   A CB   1 1 
ATOM   1015 C  CG   . LEU   A 1 131 ? 37.771 33.651 89.961  1 72.7   ? 130 LEU   A CG   1 1 
ATOM   1016 C  CD1  . LEU   A 1 131 ? 37.917 32.767 91.179  1 73.56  ? 130 LEU   A CD1  1 1 
ATOM   1017 C  CD2  . LEU   A 1 131 ? 36.635 34.665 90.107  1 73.05  ? 130 LEU   A CD2  1 1 
ATOM   1018 N  N    . SER   A 1 132 ? 41.189 35.333 87.001  1 70.59  ? 131 SER   A N    1 1 
ATOM   1019 C  CA   . SER   A 1 132 ? 42.406 36.052 86.597  1 70.44  ? 131 SER   A CA   1 1 
ATOM   1020 C  C    . SER   A 1 132 ? 42.269 36.767 85.241  1 69.02  ? 131 SER   A C    1 1 
ATOM   1021 O  O    . SER   A 1 132 ? 43.157 37.531 84.869  1 69.13  ? 131 SER   A O    1 1 
ATOM   1022 C  CB   . SER   A 1 132 ? 43.628 35.139 86.598  1 72.52  ? 131 SER   A CB   1 1 
ATOM   1023 O  OG   . SER   A 1 132 ? 43.947 34.698 87.909  1 75.15  ? 131 SER   A OG   1 1 
ATOM   1024 N  N    . THR   A 1 133 ? 41.169 36.525 84.509  1 67.58  ? 132 THR   A N    1 1 
ATOM   1025 C  CA   . THR   A 1 133 ? 40.898 37.175 83.233  1 66.76  ? 132 THR   A CA   1 1 
ATOM   1026 C  C    . THR   A 1 133 ? 40.543 38.626 83.471  1 65.46  ? 132 THR   A C    1 1 
ATOM   1027 O  O    . THR   A 1 133 ? 39.806 38.928 84.401  1 65.08  ? 132 THR   A O    1 1 
ATOM   1028 C  CB   . THR   A 1 133 ? 39.686 36.54  82.545  1 68.29  ? 132 THR   A CB   1 1 
ATOM   1029 O  OG1  . THR   A 1 133 ? 38.637 36.341 83.497  1 69.1   ? 132 THR   A OG1  1 1 
ATOM   1030 C  CG2  . THR   A 1 133 ? 40.025 35.254 81.808  1 68.99  ? 132 THR   A CG2  1 1 
ATOM   1031 N  N    . LYS   A 1 134 ? 41.03  39.518 82.611  1 64.6   ? 133 LYS   A N    1 1 
ATOM   1032 C  CA   . LYS   A 1 134 ? 40.728 40.942 82.713  1 64.25  ? 133 LYS   A CA   1 1 
ATOM   1033 C  C    . LYS   A 1 134 ? 39.414 41.253 81.97   1 64.06  ? 133 LYS   A C    1 1 
ATOM   1034 O  O    . LYS   A 1 134 ? 39.122 40.631 80.952  1 63.81  ? 133 LYS   A O    1 1 
ATOM   1035 C  CB   . LYS   A 1 134 ? 41.881 41.761 82.127  1 65.47  ? 133 LYS   A CB   1 1 
ATOM   1036 C  CG   . LYS   A 1 134 ? 43.258 41.333 82.608  1 68.85  ? 133 LYS   A CG   1 1 
ATOM   1037 C  CD   . LYS   A 1 134 ? 44.35  41.954 81.757  1 73.18  ? 133 LYS   A CD   1 1 
ATOM   1038 C  CE   . LYS   A 1 134 ? 45.593 41.109 81.714  1 76.82  ? 133 LYS   A CE   1 1 
ATOM   1039 N  NZ   . LYS   A 1 134 ? 46.092 40.969 80.32   1 78.58  ? 133 LYS   A NZ   1 1 
ATOM   1040 N  N    . ASP   A 1 135 ? 38.621 42.205 82.475  1 63.97  ? 134 ASP   A N    1 1 
ATOM   1041 C  CA   . ASP   A 1 135 ? 37.34  42.556 81.852  1 64.16  ? 134 ASP   A CA   1 1 
ATOM   1042 C  C    . ASP   A 1 135 ? 37.491 43.032 80.429  1 64.08  ? 134 ASP   A C    1 1 
ATOM   1043 O  O    . ASP   A 1 135 ? 36.632 42.754 79.591  1 64.57  ? 134 ASP   A O    1 1 
ATOM   1044 C  CB   . ASP   A 1 135 ? 36.611 43.635 82.659  1 65.83  ? 134 ASP   A CB   1 1 
ATOM   1045 C  CG   . ASP   A 1 135 ? 36.047 43.146 83.96   1 69.95  ? 134 ASP   A CG   1 1 
ATOM   1046 O  OD1  . ASP   A 1 135 ? 35.771 41.935 84.068  1 70.34  ? 134 ASP   A OD1  1 1 
ATOM   1047 O  OD2  . ASP   A 1 135 ? 35.896 43.97  84.878  1 72.61  ? 134 ASP   A OD2  1 1 
ATOM   1048 N  N    . GLU   A 1 136 ? 38.578 43.761 80.159  1 63.35  ? 135 GLU   A N    1 1 
ATOM   1049 C  CA   . GLU   A 1 136 ? 38.907 44.305 78.84   1 62.94  ? 135 GLU   A CA   1 1 
ATOM   1050 C  C    . GLU   A 1 136 ? 39.164 43.164 77.849  1 60.96  ? 135 GLU   A C    1 1 
ATOM   1051 O  O    . GLU   A 1 136 ? 38.767 43.263 76.7    1 60.39  ? 135 GLU   A O    1 1 
ATOM   1052 C  CB   . GLU   A 1 136 ? 40.137 45.237 78.942  1 66.44  ? 135 GLU   A CB   1 1 
ATOM   1053 C  CG   . GLU   A 1 136 ? 40.08  46.26  80.076  1 72.72  ? 135 GLU   A CG   1 1 
ATOM   1054 C  CD   . GLU   A 1 136 ? 40.522 45.739 81.433  1 81.78  ? 135 GLU   A CD   1 1 
ATOM   1055 O  OE1  . GLU   A 1 136 ? 41.277 44.742 81.451  1 83.44  ? 135 GLU   A OE1  1 1 
ATOM   1056 O  OE2  . GLU   A 1 136 ? 40.113 46.31  82.474  1 84.97  ? 135 GLU   A OE2  1 1 
ATOM   1057 N  N    . GLU   A 1 137 ? 39.815 42.081 78.318  1 59.91  ? 136 GLU   A N    1 1 
ATOM   1058 C  CA   . GLU   A 1 137 ? 40.114 40.877 77.555  1 59.16  ? 136 GLU   A CA   1 1 
ATOM   1059 C  C    . GLU   A 1 137 ? 38.813 40.198 77.15   1 57.88  ? 136 GLU   A C    1 1 
ATOM   1060 O  O    . GLU   A 1 137 ? 38.693 39.762 76.015  1 57.92  ? 136 GLU   A O    1 1 
ATOM   1061 C  CB   . GLU   A 1 137 ? 40.976 39.902 78.383  1 61.41  ? 136 GLU   A CB   1 1 
ATOM   1062 C  CG   . GLU   A 1 137 ? 42.405 40.361 78.6    1 67.31  ? 136 GLU   A CG   1 1 
ATOM   1063 C  CD   . GLU   A 1 137 ? 43.277 39.367 79.344  1 77.3   ? 136 GLU   A CD   1 1 
ATOM   1064 O  OE1  . GLU   A 1 137 ? 42.768 38.696 80.272  1 80.44  ? 136 GLU   A OE1  1 1 
ATOM   1065 O  OE2  . GLU   A 1 137 ? 44.476 39.254 78.999  1 80.1   ? 136 GLU   A OE2  1 1 
ATOM   1066 N  N    . ILE   A 1 138 ? 37.842 40.107 78.071  1 56.65  ? 137 ILE   A N    1 1 
ATOM   1067 C  CA   . ILE   A 1 138 ? 36.545 39.487 77.808  1 55.99  ? 137 ILE   A CA   1 1 
ATOM   1068 C  C    . ILE   A 1 138 ? 35.793 40.276 76.752  1 55.66  ? 137 ILE   A C    1 1 
ATOM   1069 O  O    . ILE   A 1 138 ? 35.262 39.7   75.791  1 56.33  ? 137 ILE   A O    1 1 
ATOM   1070 C  CB   . ILE   A 1 138 ? 35.731 39.394 79.108  1 56.26  ? 137 ILE   A CB   1 1 
ATOM   1071 C  CG1  . ILE   A 1 138 ? 36.478 38.553 80.156  1 57.17  ? 137 ILE   A CG1  1 1 
ATOM   1072 C  CG2  . ILE   A 1 138 ? 34.337 38.856 78.827  1 56.57  ? 137 ILE   A CG2  1 1 
ATOM   1073 C  CD1  . ILE   A 1 138 ? 36.114 38.862 81.561  1 58.05  ? 137 ILE   A CD1  1 1 
ATOM   1074 N  N    . THR   A 1 139 ? 35.8   41.611 76.899  1 54.14  ? 138 THR   A N    1 1 
ATOM   1075 C  CA   . THR   A 1 139 ? 35.154 42.53  75.974  1 52.71  ? 138 THR   A CA   1 1 
ATOM   1076 C  C    . THR   A 1 139 ? 35.781 42.374 74.573  1 51.6   ? 138 THR   A C    1 1 
ATOM   1077 O  O    . THR   A 1 139 ? 35.051 42.081 73.636  1 51.35  ? 138 THR   A O    1 1 
ATOM   1078 C  CB   . THR   A 1 139 ? 35.17  43.933 76.597  1 52.78  ? 138 THR   A CB   1 1 
ATOM   1079 O  OG1  . THR   A 1 139 ? 34.068 44.037 77.488  1 52.41  ? 138 THR   A OG1  1 1 
ATOM   1080 C  CG2  . THR   A 1 139 ? 35.059 45.019 75.589  1 53.37  ? 138 THR   A CG2  1 1 
ATOM   1081 N  N    . LYS   A 1 140 ? 37.132 42.438 74.463  1 50.99  ? 139 LYS   A N    1 1 
ATOM   1082 C  CA   . LYS   A 1 140 ? 37.874 42.277 73.203  1 50.89  ? 139 LYS   A CA   1 1 
ATOM   1083 C  C    . LYS   A 1 140 ? 37.66  40.914 72.58   1 50.53  ? 139 LYS   A C    1 1 
ATOM   1084 O  O    . LYS   A 1 140 ? 37.614 40.801 71.356  1 51.28  ? 139 LYS   A O    1 1 
ATOM   1085 C  CB   . LYS   A 1 140 ? 39.377 42.519 73.389  1 53.25  ? 139 LYS   A CB   1 1 
ATOM   1086 C  CG   . LYS   A 1 140 ? 39.836 43.898 72.952  1 59.73  ? 139 LYS   A CG   1 1 
ATOM   1087 C  CD   . LYS   A 1 140 ? 41.33  43.913 72.605  1 67.19  ? 139 LYS   A CD   1 1 
ATOM   1088 C  CE   . LYS   A 1 140 ? 41.802 45.259 72.076  1 73.17  ? 139 LYS   A CE   1 1 
ATOM   1089 N  NZ   . LYS   A 1 140 ? 43.09  45.174 71.325  1 76.2   ? 139 LYS   A NZ   1 1 
ATOM   1090 N  N    . THR   A 1 141 ? 37.49  39.873 73.409  1 49.53  ? 140 THR   A N    1 1 
ATOM   1091 C  CA   . THR   A 1 141 ? 37.225 38.508 72.944  1 49.16  ? 140 THR   A CA   1 1 
ATOM   1092 C  C    . THR   A 1 141 ? 35.916 38.516 72.139  1 48.71  ? 140 THR   A C    1 1 
ATOM   1093 O  O    . THR   A 1 141 ? 35.929 38.229 70.942  1 49.03  ? 140 THR   A O    1 1 
ATOM   1094 C  CB   . THR   A 1 141 ? 37.198 37.51  74.133  1 50.2   ? 140 THR   A CB   1 1 
ATOM   1095 O  OG1  . THR   A 1 141 ? 38.529 37.241 74.577  1 51.5   ? 140 THR   A OG1  1 1 
ATOM   1096 C  CG2  . THR   A 1 141 ? 36.525 36.205 73.784  1 50.11  ? 140 THR   A CG2  1 1 
ATOM   1097 N  N    . PHE   A 1 142 ? 34.834 39.006 72.753  1 47.56  ? 141 PHE   A N    1 1 
ATOM   1098 C  CA   . PHE   A 1 142 ? 33.537 39.047 72.104  1 46.58  ? 141 PHE   A CA   1 1 
ATOM   1099 C  C    . PHE   A 1 142 ? 33.468 40.015 70.946  1 45.67  ? 141 PHE   A C    1 1 
ATOM   1100 O  O    . PHE   A 1 142 ? 32.81  39.725 69.954  1 45.59  ? 141 PHE   A O    1 1 
ATOM   1101 C  CB   . PHE   A 1 142 ? 32.44  39.322 73.131  1 46.08  ? 141 PHE   A CB   1 1 
ATOM   1102 C  CG   . PHE   A 1 142 ? 31.945 38.038 73.732  1 46.15  ? 141 PHE   A CG   1 1 
ATOM   1103 C  CD1  . PHE   A 1 142 ? 32.718 37.34  74.639  1 46.91  ? 141 PHE   A CD1  1 1 
ATOM   1104 C  CD2  . PHE   A 1 142 ? 30.729 37.504 73.355  1 46.57  ? 141 PHE   A CD2  1 1 
ATOM   1105 C  CE1  . PHE   A 1 142 ? 32.268 36.15  75.181  1 47.66  ? 141 PHE   A CE1  1 1 
ATOM   1106 C  CE2  . PHE   A 1 142 ? 30.287 36.306 73.884  1 47.26  ? 141 PHE   A CE2  1 1 
ATOM   1107 C  CZ   . PHE   A 1 142 ? 31.054 35.642 74.803  1 47.34  ? 141 PHE   A CZ   1 1 
ATOM   1108 N  N    . GLU   A 1 143 ? 34.171 41.141 71.057  1 44.82  ? 142 GLU   A N    1 1 
ATOM   1109 C  CA   . GLU   A 1 143 ? 34.183 42.174 70.028  1 44.52  ? 142 GLU   A CA   1 1 
ATOM   1110 C  C    . GLU   A 1 143 ? 34.732 41.682 68.7    1 43.7   ? 142 GLU   A C    1 1 
ATOM   1111 O  O    . GLU   A 1 143 ? 34.281 42.138 67.649  1 42.97  ? 142 GLU   A O    1 1 
ATOM   1112 C  CB   . GLU   A 1 143 ? 34.961 43.417 70.513  1 46.47  ? 142 GLU   A CB   1 1 
ATOM   1113 C  CG   . GLU   A 1 143 ? 34.094 44.398 71.283  1 50.8   ? 142 GLU   A CG   1 1 
ATOM   1114 C  CD   . GLU   A 1 143 ? 34.819 45.456 72.093  1 56.72  ? 142 GLU   A CD   1 1 
ATOM   1115 O  OE1  . GLU   A 1 143 ? 36.07  45.435 72.135  1 57.69  ? 142 GLU   A OE1  1 1 
ATOM   1116 O  OE2  . GLU   A 1 143 ? 34.13  46.299 72.711  1 58.95  ? 142 GLU   A OE2  1 1 
ATOM   1117 N  N    . ILE   A 1 144 ? 35.699 40.751 68.752  1 43.57  ? 143 ILE   A N    1 1 
ATOM   1118 C  CA   . ILE   A 1 144 ? 36.37  40.212 67.568  1 43.92  ? 143 ILE   A CA   1 1 
ATOM   1119 C  C    . ILE   A 1 144 ? 35.787 38.869 67.098  1 43.31  ? 143 ILE   A C    1 1 
ATOM   1120 O  O    . ILE   A 1 144 ? 35.51  38.685 65.901  1 42.89  ? 143 ILE   A O    1 1 
ATOM   1121 C  CB   . ILE   A 1 144 ? 37.898 40.11  67.875  1 44.73  ? 143 ILE   A CB   1 1 
ATOM   1122 C  CG1  . ILE   A 1 144 ? 38.524 41.505 68.024  1 45.9   ? 143 ILE   A CG1  1 1 
ATOM   1123 C  CG2  . ILE   A 1 144 ? 38.647 39.279 66.834  1 44.95  ? 143 ILE   A CG2  1 1 
ATOM   1124 C  CD1  . ILE   A 1 144 ? 39.844 41.488 68.663  1 47.44  ? 143 ILE   A CD1  1 1 
ATOM   1125 N  N    . ASN   A 1 145 ? 35.611 37.94  68.052  1 42.84  ? 144 ASN   A N    1 1 
ATOM   1126 C  CA   . ASN   A 1 145 ? 35.147 36.582 67.799  1 42.83  ? 144 ASN   A CA   1 1 
ATOM   1127 C  C    . ASN   A 1 145 ? 33.687 36.435 67.383  1 42.2   ? 144 ASN   A C    1 1 
ATOM   1128 O  O    . ASN   A 1 145 ? 33.372 35.435 66.725  1 42.25  ? 144 ASN   A O    1 1 
ATOM   1129 C  CB   . ASN   A 1 145 ? 35.415 35.687 69.004  1 44.4   ? 144 ASN   A CB   1 1 
ATOM   1130 C  CG   . ASN   A 1 145 ? 36.864 35.541 69.374  1 48.05  ? 144 ASN   A CG   1 1 
ATOM   1131 O  OD1  . ASN   A 1 145 ? 37.758 35.97  68.646  1 50.1   ? 144 ASN   A OD1  1 1 
ATOM   1132 N  ND2  . ASN   A 1 145 ? 37.12  34.938 70.524  1 48.45  ? 144 ASN   A ND2  1 1 
ATOM   1133 N  N    . ILE   A 1 146 ? 32.785 37.362 67.793  1 41.44  ? 145 ILE   A N    1 1 
ATOM   1134 C  CA   . ILE   A 1 146 ? 31.374 37.222 67.408  1 41.26  ? 145 ILE   A CA   1 1 
ATOM   1135 C  C    . ILE   A 1 146 ? 30.668 38.575 67.074  1 41.17  ? 145 ILE   A C    1 1 
ATOM   1136 O  O    . ILE   A 1 146 ? 29.942 38.631 66.087  1 40.72  ? 145 ILE   A O    1 1 
ATOM   1137 C  CB   . ILE   A 1 146 ? 30.578 36.378 68.427  1 41.52  ? 145 ILE   A CB   1 1 
ATOM   1138 C  CG1  . ILE   A 1 146 ? 29.112 36.202 67.981  1 42.41  ? 145 ILE   A CG1  1 1 
ATOM   1139 C  CG2  . ILE   A 1 146 ? 30.713 36.911 69.845  1 41.87  ? 145 ILE   A CG2  1 1 
ATOM   1140 C  CD1  . ILE   A 1 146 ? 28.946 35.522 66.592  1 43.38  ? 145 ILE   A CD1  1 1 
ATOM   1141 N  N    . LEU   A 1 147 ? 30.901 39.654 67.838  1 41.37  ? 146 LEU   A N    1 1 
ATOM   1142 C  CA   . LEU   A 1 147 ? 30.288 40.952 67.537  1 41.6   ? 146 LEU   A CA   1 1 
ATOM   1143 C  C    . LEU   A 1 147 ? 30.722 41.449 66.168  1 41.42  ? 146 LEU   A C    1 1 
ATOM   1144 O  O    . LEU   A 1 147 ? 29.893 41.918 65.395  1 41.24  ? 146 LEU   A O    1 1 
ATOM   1145 C  CB   . LEU   A 1 147 ? 30.633 41.99  68.618  1 42.04  ? 146 LEU   A CB   1 1 
ATOM   1146 C  CG   . LEU   A 1 147 ? 29.882 41.84  69.933  1 44.11  ? 146 LEU   A CG   1 1 
ATOM   1147 C  CD1  . LEU   A 1 147 ? 30.342 42.874 70.937  1 44.62  ? 146 LEU   A CD1  1 1 
ATOM   1148 C  CD2  . LEU   A 1 147 ? 28.383 41.954 69.729  1 45.49  ? 146 LEU   A CD2  1 1 
ATOM   1149 N  N    . GLY   A 1 148 ? 32.011 41.292 65.876  1 41.56  ? 147 GLY   A N    1 1 
ATOM   1150 C  CA   . GLY   A 1 148 ? 32.616 41.675 64.608  1 41.84  ? 147 GLY   A CA   1 1 
ATOM   1151 C  C    . GLY   A 1 148 ? 32.073 40.859 63.465  1 41.86  ? 147 GLY   A C    1 1 
ATOM   1152 O  O    . GLY   A 1 148 ? 31.883 41.401 62.383  1 42.49  ? 147 GLY   A O    1 1 
ATOM   1153 N  N    . HIS   A 1 149 ? 31.785 39.563 63.695  1 41.2   ? 148 HIS   A N    1 1 
ATOM   1154 C  CA   . HIS   A 1 149 ? 31.195 38.678 62.684  1 41.33  ? 148 HIS   A CA   1 1 
ATOM   1155 C  C    . HIS   A 1 149 ? 29.83  39.212 62.192  1 41.85  ? 148 HIS   A C    1 1 
ATOM   1156 O  O    . HIS   A 1 149 ? 29.479 39.051 61.017  1 41.45  ? 148 HIS   A O    1 1 
ATOM   1157 C  CB   . HIS   A 1 149 ? 30.977 37.271 63.253  1 41.45  ? 148 HIS   A CB   1 1 
ATOM   1158 C  CG   . HIS   A 1 149 ? 32.205 36.434 63.349  1 43.33  ? 148 HIS   A CG   1 1 
ATOM   1159 N  ND1  . HIS   A 1 149 ? 32.178 35.092 63.033  1 45.02  ? 148 HIS   A ND1  1 1 
ATOM   1160 C  CD2  . HIS   A 1 149 ? 33.448 36.759 63.778  1 44.92  ? 148 HIS   A CD2  1 1 
ATOM   1161 C  CE1  . HIS   A 1 149 ? 33.401 34.641 63.27   1 45.96  ? 148 HIS   A CE1  1 1 
ATOM   1162 N  NE2  . HIS   A 1 149 ? 34.201 35.605 63.726  1 46.15  ? 148 HIS   A NE2  1 1 
ATOM   1163 N  N    . PHE   A 1 150 ? 29.07  39.842 63.1    1 42.27  ? 149 PHE   A N    1 1 
ATOM   1164 C  CA   . PHE   A 1 150 ? 27.758 40.349 62.757  1 43.27  ? 149 PHE   A CA   1 1 
ATOM   1165 C  C    . PHE   A 1 150 ? 27.889 41.523 61.809  1 44.89  ? 149 PHE   A C    1 1 
ATOM   1166 O  O    . PHE   A 1 150 ? 27.201 41.552 60.801  1 44.76  ? 149 PHE   A O    1 1 
ATOM   1167 C  CB   . PHE   A 1 150 ? 26.978 40.757 64.013  1 42.94  ? 149 PHE   A CB   1 1 
ATOM   1168 C  CG   . PHE   A 1 150 ? 26.232 39.629 64.681  1 43.41  ? 149 PHE   A CG   1 1 
ATOM   1169 C  CD1  . PHE   A 1 150 ? 26.833 38.868 65.665  1 44.19  ? 149 PHE   A CD1  1 1 
ATOM   1170 C  CD2  . PHE   A 1 150 ? 24.92  39.351 64.343  1 43.97  ? 149 PHE   A CD2  1 1 
ATOM   1171 C  CE1  . PHE   A 1 150 ? 26.148 37.832 66.276  1 44.94  ? 149 PHE   A CE1  1 1 
ATOM   1172 C  CE2  . PHE   A 1 150 ? 24.228 38.327 64.971  1 44.59  ? 149 PHE   A CE2  1 1 
ATOM   1173 C  CZ   . PHE   A 1 150 ? 24.845 37.575 65.932  1 44.59  ? 149 PHE   A CZ   1 1 
ATOM   1174 N  N    . TRP   A 1 151 ? 28.78  42.484 62.109  1 45.95  ? 150 TRP   A N    1 1 
ATOM   1175 C  CA   . TRP   A 1 151 ? 28.921 43.676 61.27   1 46.91  ? 150 TRP   A CA   1 1 
ATOM   1176 C  C    . TRP   A 1 151 ? 29.471 43.385 59.906  1 46.99  ? 150 TRP   A C    1 1 
ATOM   1177 O  O    . TRP   A 1 151 ? 29.028 44.021 58.947  1 48.27  ? 150 TRP   A O    1 1 
ATOM   1178 C  CB   . TRP   A 1 151 ? 29.731 44.813 61.932  1 47.5   ? 150 TRP   A CB   1 1 
ATOM   1179 C  CG   . TRP   A 1 151 ? 29.764 44.851 63.435  1 48.61  ? 150 TRP   A CG   1 1 
ATOM   1180 C  CD1  . TRP   A 1 151 ? 30.877 44.929 64.216  1 49.71  ? 150 TRP   A CD1  1 1 
ATOM   1181 C  CD2  . TRP   A 1 151 ? 28.638 44.889 64.332  1 49.03  ? 150 TRP   A CD2  1 1 
ATOM   1182 N  NE1  . TRP   A 1 151 ? 30.518 45     65.544  1 50.16  ? 150 TRP   A NE1  1 1 
ATOM   1183 C  CE2  . TRP   A 1 151 ? 29.15  44.977 65.641  1 49.94  ? 150 TRP   A CE2  1 1 
ATOM   1184 C  CE3  . TRP   A 1 151 ? 27.249 44.859 64.156  1 49.63  ? 150 TRP   A CE3  1 1 
ATOM   1185 C  CZ2  . TRP   A 1 151 ? 28.324 45.032 66.763  1 50.88  ? 150 TRP   A CZ2  1 1 
ATOM   1186 C  CZ3  . TRP   A 1 151 ? 26.437 44.882 65.268  1 50.67  ? 150 TRP   A CZ3  1 1 
ATOM   1187 C  CH2  . TRP   A 1 151 ? 26.974 44.981 66.553  1 51.05  ? 150 TRP   A CH2  1 1 
ATOM   1188 N  N    . ILE   A 1 152 ? 30.403 42.416 59.776  1 45.65  ? 151 ILE   A N    1 1 
ATOM   1189 C  CA   . ILE   A 1 152 ? 30.944 42.108 58.445  1 44.84  ? 151 ILE   A CA   1 1 
ATOM   1190 C  C    . ILE   A 1 152 ? 29.851 41.457 57.627  1 43.97  ? 151 ILE   A C    1 1 
ATOM   1191 O  O    . ILE   A 1 152 ? 29.45  42.029 56.63   1 44.3   ? 151 ILE   A O    1 1 
ATOM   1192 C  CB   . ILE   A 1 152 ? 32.251 41.296 58.466  1 45.31  ? 151 ILE   A CB   1 1 
ATOM   1193 C  CG1  . ILE   A 1 152 ? 33.215 41.83  59.537  1 46.38  ? 151 ILE   A CG1  1 1 
ATOM   1194 C  CG2  . ILE   A 1 152 ? 32.898 41.353 57.099  1 45.52  ? 151 ILE   A CG2  1 1 
ATOM   1195 C  CD1  . ILE   A 1 152 ? 34.274 40.886 59.992  1 47.74  ? 151 ILE   A CD1  1 1 
ATOM   1196 N  N    . THR   A 1 153 ? 29.248 40.38  58.156  1 43.28  ? 152 THR   A N    1 1 
ATOM   1197 C  CA   . THR   A 1 153 ? 28.127 39.632 57.575  1 43.28  ? 152 THR   A CA   1 1 
ATOM   1198 C  C    . THR   A 1 153 ? 26.954 40.54  57.173  1 44.47  ? 152 THR   A C    1 1 
ATOM   1199 O  O    . THR   A 1 153 ? 26.363 40.351 56.109  1 44.67  ? 152 THR   A O    1 1 
ATOM   1200 C  CB   . THR   A 1 153 ? 27.627 38.585 58.584  1 43.2   ? 152 THR   A CB   1 1 
ATOM   1201 O  OG1  . THR   A 1 153 ? 28.729 37.855 59.139  1 43.89  ? 152 THR   A OG1  1 1 
ATOM   1202 C  CG2  . THR   A 1 153 ? 26.582 37.654 58.008  1 42.92  ? 152 THR   A CG2  1 1 
ATOM   1203 N  N    . LYS   A 1 154 ? 26.642 41.535 58.018  1 45.07  ? 153 LYS   A N    1 1 
ATOM   1204 C  CA   . LYS   A 1 154 ? 25.553 42.5   57.855  1 46.32  ? 153 LYS   A CA   1 1 
ATOM   1205 C  C    . LYS   A 1 154 ? 25.797 43.499 56.73   1 47.38  ? 153 LYS   A C    1 1 
ATOM   1206 O  O    . LYS   A 1 154 ? 24.84  43.986 56.128  1 47.55  ? 153 LYS   A O    1 1 
ATOM   1207 C  CB   . LYS   A 1 154 ? 25.36  43.281 59.157  1 48.46  ? 153 LYS   A CB   1 1 
ATOM   1208 C  CG   . LYS   A 1 154 ? 24.089 42.964 59.908  1 53.46  ? 153 LYS   A CG   1 1 
ATOM   1209 C  CD   . LYS   A 1 154 ? 23.334 44.255 60.137  1 59.16  ? 153 LYS   A CD   1 1 
ATOM   1210 C  CE   . LYS   A 1 154 ? 22.698 44.318 61.492  1 63.97  ? 153 LYS   A CE   1 1 
ATOM   1211 N  NZ   . LYS   A 1 154 ? 22.395 45.721 61.865  1 67.22  ? 153 LYS   A NZ   1 1 
ATOM   1212 N  N    . ALA   A 1 155 ? 27.062 43.849 56.48   1 47.87  ? 154 ALA   A N    1 1 
ATOM   1213 C  CA   . ALA   A 1 155 ? 27.397 44.811 55.44   1 49.01  ? 154 ALA   A CA   1 1 
ATOM   1214 C  C    . ALA   A 1 155 ? 27.545 44.181 54.032  1 50.62  ? 154 ALA   A C    1 1 
ATOM   1215 O  O    . ALA   A 1 155 ? 27.471 44.892 53.023  1 50.59  ? 154 ALA   A O    1 1 
ATOM   1216 C  CB   . ALA   A 1 155 ? 28.658 45.559 55.824  1 48.85  ? 154 ALA   A CB   1 1 
ATOM   1217 N  N    . LEU   A 1 156 ? 27.741 42.855 53.96   1 51.69  ? 155 LEU   A N    1 1 
ATOM   1218 C  CA   . LEU   A 1 156 ? 27.932 42.173 52.678  1 53.17  ? 155 LEU   A CA   1 1 
ATOM   1219 C  C    . LEU   A 1 156 ? 26.714 41.369 52.218  1 54.91  ? 155 LEU   A C    1 1 
ATOM   1220 O  O    . LEU   A 1 156 ? 26.507 41.219 51.01   1 55.66  ? 155 LEU   A O    1 1 
ATOM   1221 C  CB   . LEU   A 1 156 ? 29.194 41.304 52.717  1 53.35  ? 155 LEU   A CB   1 1 
ATOM   1222 C  CG   . LEU   A 1 156 ? 30.455 42.042 53.159  1 55.05  ? 155 LEU   A CG   1 1 
ATOM   1223 C  CD1  . LEU   A 1 156 ? 31.607 41.099 53.338  1 55.7   ? 155 LEU   A CD1  1 1 
ATOM   1224 C  CD2  . LEU   A 1 156 ? 30.811 43.153 52.19   1 55.78  ? 155 LEU   A CD2  1 1 
ATOM   1225 N  N    . LEU   A 1 157 ? 25.884 40.912 53.177  1 55.58  ? 156 LEU   A N    1 1 
ATOM   1226 C  CA   . LEU   A 1 157 ? 24.638 40.174 52.95   1 56.95  ? 156 LEU   A CA   1 1 
ATOM   1227 C  C    . LEU   A 1 157 ? 23.624 40.932 52.098  1 59.05  ? 156 LEU   A C    1 1 
ATOM   1228 O  O    . LEU   A 1 157 ? 22.972 40.281 51.286  1 59.73  ? 156 LEU   A O    1 1 
ATOM   1229 C  CB   . LEU   A 1 157 ? 23.986 39.784 54.275  1 57.18  ? 156 LEU   A CB   1 1 
ATOM   1230 C  CG   . LEU   A 1 157 ? 23.599 38.332 54.463  1 58.39  ? 156 LEU   A CG   1 1 
ATOM   1231 C  CD1  . LEU   A 1 157 ? 24.821 37.458 54.566  1 58.87  ? 156 LEU   A CD1  1 1 
ATOM   1232 C  CD2  . LEU   A 1 157 ? 22.788 38.169 55.729  1 58.71  ? 156 LEU   A CD2  1 1 
ATOM   1233 N  N    . PRO   A 1 158 ? 23.464 42.279 52.191  1 60.04  ? 157 PRO   A N    1 1 
ATOM   1234 C  CA   . PRO   A 1 158 ? 22.493 42.954 51.31   1 61.08  ? 157 PRO   A CA   1 1 
ATOM   1235 C  C    . PRO   A 1 158 ? 22.777 42.717 49.84   1 63.01  ? 157 PRO   A C    1 1 
ATOM   1236 O  O    . PRO   A 1 158 ? 21.827 42.564 49.065  1 64.16  ? 157 PRO   A O    1 1 
ATOM   1237 C  CB   . PRO   A 1 158 ? 22.661 44.437 51.649  1 61.39  ? 157 PRO   A CB   1 1 
ATOM   1238 C  CG   . PRO   A 1 158 ? 23.269 44.455 52.989  1 61.58  ? 157 PRO   A CG   1 1 
ATOM   1239 C  CD   . PRO   A 1 158 ? 24.136 43.248 53.077  1 59.64  ? 157 PRO   A CD   1 1 
ATOM   1240 N  N    . SER   A 1 159 ? 24.073 42.675 49.445  1 63.28  ? 158 SER   A N    1 1 
ATOM   1241 C  CA   . SER   A 1 159 ? 24.399 42.468 48.032  1 63.98  ? 158 SER   A CA   1 1 
ATOM   1242 C  C    . SER   A 1 159 ? 24.276 41.011 47.619  1 64.19  ? 158 SER   A C    1 1 
ATOM   1243 O  O    . SER   A 1 159 ? 23.749 40.73  46.547  1 64.34  ? 158 SER   A O    1 1 
ATOM   1244 C  CB   . SER   A 1 159 ? 25.778 43.014 47.693  1 65.55  ? 158 SER   A CB   1 1 
ATOM   1245 O  OG   . SER   A 1 159 ? 25.936 43.061 46.285  1 68.03  ? 158 SER   A OG   1 1 
ATOM   1246 N  N    . MET   A 1 160 ? 24.709 40.083 48.487  1 64.22  ? 159 MET   A N    1 1 
ATOM   1247 C  CA   . MET   A 1 160 ? 24.577 38.649 48.226  1 64.61  ? 159 MET   A CA   1 1 
ATOM   1248 C  C    . MET   A 1 160 ? 23.112 38.233 48.133  1 65.74  ? 159 MET   A C    1 1 
ATOM   1249 O  O    . MET   A 1 160 ? 22.813 37.269 47.444  1 65.92  ? 159 MET   A O    1 1 
ATOM   1250 C  CB   . MET   A 1 160 ? 25.268 37.825 49.313  1 64.51  ? 159 MET   A CB   1 1 
ATOM   1251 C  CG   . MET   A 1 160 ? 26.71  38.206 49.535  1 64.99  ? 159 MET   A CG   1 1 
ATOM   1252 S  SD   . MET   A 1 160 ? 27.576 37.004 50.561  1 61.93  ? 159 MET   A SD   1 1 
ATOM   1253 C  CE   . MET   A 1 160 ? 29.119 37.782 50.708  1 59.79  ? 159 MET   A CE   1 1 
ATOM   1254 N  N    . ILE   A 1 161 ? 22.205 38.951 48.825  1 66.49  ? 160 ILE   A N    1 1 
ATOM   1255 C  CA   . ILE   A 1 161 ? 20.764 38.721 48.789  1 67.68  ? 160 ILE   A CA   1 1 
ATOM   1256 C  C    . ILE   A 1 161 ? 20.176 39.116 47.407  1 68.91  ? 160 ILE   A C    1 1 
ATOM   1257 O  O    . ILE   A 1 161 ? 19.302 38.411 46.897  1 68.98  ? 160 ILE   A O    1 1 
ATOM   1258 C  CB   . ILE   A 1 161 ? 20.079 39.414 50.006  1 68.14  ? 160 ILE   A CB   1 1 
ATOM   1259 C  CG1  . ILE   A 1 161 ? 19.579 38.377 51.018  1 69.43  ? 160 ILE   A CG1  1 1 
ATOM   1260 C  CG2  . ILE   A 1 161 ? 18.965 40.382 49.627  1 68.47  ? 160 ILE   A CG2  1 1 
ATOM   1261 C  CD1  . ILE   A 1 161 ? 20.578 37.969 52.074  1 70.91  ? 160 ILE   A CD1  1 1 
ATOM   1262 N  N    . LYS   A 1 162 ? 20.666 40.232 46.807  1 69.66  ? 161 LYS   A N    1 1 
ATOM   1263 C  CA   . LYS   A 1 162 ? 20.212 40.695 45.491  1 70.79  ? 161 LYS   A CA   1 1 
ATOM   1264 C  C    . LYS   A 1 162 ? 20.585 39.662 44.443  1 71.59  ? 161 LYS   A C    1 1 
ATOM   1265 O  O    . LYS   A 1 162 ? 19.757 39.288 43.613  1 73.09  ? 161 LYS   A O    1 1 
ATOM   1266 C  CB   . LYS   A 1 162 ? 20.866 42.039 45.09   1 73.06  ? 161 LYS   A CB   1 1 
ATOM   1267 C  CG   . LYS   A 1 162 ? 20.557 43.234 45.957  1 78.02  ? 161 LYS   A CG   1 1 
ATOM   1268 C  CD   . LYS   A 1 162 ? 21.449 44.429 45.56   1 82.19  ? 161 LYS   A CD   1 1 
ATOM   1269 C  CE   . LYS   A 1 162 ? 22.423 44.811 46.663  1 84.29  ? 161 LYS   A CE   1 1 
ATOM   1270 N  NZ   . LYS   A 1 162 ? 21.709 45.107 47.927  1 84.63  ? 161 LYS   A NZ   1 1 
ATOM   1271 N  N    . ARG   A 1 163 ? 21.837 39.205 44.474  1 70.81  ? 162 ARG   A N    1 1 
ATOM   1272 C  CA   . ARG   A 1 163 ? 22.326 38.258 43.493  1 70.77  ? 162 ARG   A CA   1 1 
ATOM   1273 C  C    . ARG   A 1 163 ? 21.976 36.813 43.81   1 69.99  ? 162 ARG   A C    1 1 
ATOM   1274 O  O    . ARG   A 1 163 ? 22.203 35.969 42.951  1 70.11  ? 162 ARG   A O    1 1 
ATOM   1275 C  CB   . ARG   A 1 163 ? 23.847 38.417 43.316  1 72.67  ? 162 ARG   A CB   1 1 
ATOM   1276 C  CG   . ARG   A 1 163 ? 24.265 39.825 42.915  1 76.42  ? 162 ARG   A CG   1 1 
ATOM   1277 C  CD   . ARG   A 1 163 ? 25.719 40.139 43.249  1 79.76  ? 162 ARG   A CD   1 1 
ATOM   1278 N  NE   . ARG   A 1 163 ? 25.986 41.576 43.146  1 82.26  ? 162 ARG   A NE   1 1 
ATOM   1279 C  CZ   . ARG   A 1 163 ? 26.392 42.182 42.036  1 83.57  ? 162 ARG   A CZ   1 1 
ATOM   1280 N  NH1  . ARG   A 1 163 ? 26.633 41.479 40.938  1 83.46  ? 162 ARG   A NH1  1 1 
ATOM   1281 N  NH2  . ARG   A 1 163 ? 26.595 43.494 42.026  1 82.93  ? 162 ARG   A NH2  1 1 
ATOM   1282 N  N    . ASN   A 1 164 ? 21.456 36.514 45.033  1 69.1   ? 163 ASN   A N    1 1 
ATOM   1283 C  CA   . ASN   A 1 164 ? 21.143 35.163 45.533  1 68.86  ? 163 ASN   A CA   1 1 
ATOM   1284 C  C    . ASN   A 1 164 ? 22.37  34.258 45.348  1 68.06  ? 163 ASN   A C    1 1 
ATOM   1285 O  O    . ASN   A 1 164 ? 22.259 33.152 44.833  1 68.67  ? 163 ASN   A O    1 1 
ATOM   1286 C  CB   . ASN   A 1 164 ? 19.9   34.586 44.84   1 70.37  ? 163 ASN   A CB   1 1 
ATOM   1287 C  CG   . ASN   A 1 164 ? 19.34  33.327 45.473  1 73.02  ? 163 ASN   A CG   1 1 
ATOM   1288 O  OD1  . ASN   A 1 164 ? 18.927 33.307 46.638  1 73.77  ? 163 ASN   A OD1  1 1 
ATOM   1289 N  ND2  . ASN   A 1 164 ? 19.322 32.242 44.708  1 73.42  ? 163 ASN   A ND2  1 1 
ATOM   1290 N  N    . HIS   A 1 165 ? 23.555 34.791 45.657  1 66.67  ? 164 HIS   A N    1 1 
ATOM   1291 C  CA   . HIS   A 1 165 ? 24.804 34.078 45.459  1 66.16  ? 164 HIS   A CA   1 1 
ATOM   1292 C  C    . HIS   A 1 165 ? 25.831 34.602 46.425  1 65.63  ? 164 HIS   A C    1 1 
ATOM   1293 O  O    . HIS   A 1 165 ? 26.125 35.795 46.43   1 66.05  ? 164 HIS   A O    1 1 
ATOM   1294 C  CB   . HIS   A 1 165 ? 25.303 34.296 44.03   1 67.13  ? 164 HIS   A CB   1 1 
ATOM   1295 C  CG   . HIS   A 1 165 ? 26.595 33.627 43.72   1 69.37  ? 164 HIS   A CG   1 1 
ATOM   1296 N  ND1  . HIS   A 1 165 ? 26.803 32.297 44.015  1 71.43  ? 164 HIS   A ND1  1 1 
ATOM   1297 C  CD2  . HIS   A 1 165 ? 27.69  34.118 43.095  1 70.44  ? 164 HIS   A CD2  1 1 
ATOM   1298 C  CE1  . HIS   A 1 165 ? 28.025 32.025 43.589  1 71.98  ? 164 HIS   A CE1  1 1 
ATOM   1299 N  NE2  . HIS   A 1 165 ? 28.597 33.091 43.028  1 71.69  ? 164 HIS   A NE2  1 1 
ATOM   1300 N  N    . GLY   A 1 166 ? 26.373 33.699 47.228  1 64.35  ? 165 GLY   A N    1 1 
ATOM   1301 C  CA   . GLY   A 1 166 ? 27.392 34.006 48.214  1 63.42  ? 165 GLY   A CA   1 1 
ATOM   1302 C  C    . GLY   A 1 166 ? 27.783 32.797 49.035  1 62.33  ? 165 GLY   A C    1 1 
ATOM   1303 O  O    . GLY   A 1 166 ? 27.406 31.669 48.704  1 62.59  ? 165 GLY   A O    1 1 
ATOM   1304 N  N    . HIS   A 1 167 ? 28.54  33.026 50.122  1 60.88  ? 166 HIS   A N    1 1 
ATOM   1305 C  CA   . HIS   A 1 167 ? 28.985 31.979 51.032  1 59.89  ? 166 HIS   A CA   1 1 
ATOM   1306 C  C    . HIS   A 1 167 ? 29.551 32.607 52.29   1 58.54  ? 166 HIS   A C    1 1 
ATOM   1307 O  O    . HIS   A 1 167 ? 30.585 33.267 52.224  1 58.75  ? 166 HIS   A O    1 1 
ATOM   1308 C  CB   . HIS   A 1 167 ? 30.044 31.085 50.385  1 61.01  ? 166 HIS   A CB   1 1 
ATOM   1309 C  CG   . HIS   A 1 167 ? 30.093 29.704 50.959  1 64.11  ? 166 HIS   A CG   1 1 
ATOM   1310 N  ND1  . HIS   A 1 167 ? 29.998 28.581 50.152  1 66.26  ? 166 HIS   A ND1  1 1 
ATOM   1311 C  CD2  . HIS   A 1 167 ? 30.211 29.308 52.247  1 65.62  ? 166 HIS   A CD2  1 1 
ATOM   1312 C  CE1  . HIS   A 1 167 ? 30.08  27.544 50.97   1 66.96  ? 166 HIS   A CE1  1 1 
ATOM   1313 N  NE2  . HIS   A 1 167 ? 30.197 27.932 52.241  1 66.97  ? 166 HIS   A NE2  1 1 
ATOM   1314 N  N    . ILE   A 1 168 ? 28.894 32.394 53.433  1 57.06  ? 167 ILE   A N    1 1 
ATOM   1315 C  CA   . ILE   A 1 168 ? 29.379 32.954 54.683  1 56.52  ? 167 ILE   A CA   1 1 
ATOM   1316 C  C    . ILE   A 1 168 ? 30.148 31.921 55.514  1 56.07  ? 167 ILE   A C    1 1 
ATOM   1317 O  O    . ILE   A 1 168 ? 29.561 31.006 56.097  1 56.32  ? 167 ILE   A O    1 1 
ATOM   1318 C  CB   . ILE   A 1 168 ? 28.253 33.642 55.473  1 56.72  ? 167 ILE   A CB   1 1 
ATOM   1319 C  CG1  . ILE   A 1 168 ? 27.62  34.769 54.643  1 57.16  ? 167 ILE   A CG1  1 1 
ATOM   1320 C  CG2  . ILE   A 1 168 ? 28.775 34.164 56.802  1 57.15  ? 167 ILE   A CG2  1 1 
ATOM   1321 C  CD1  . ILE   A 1 168 ? 28.589 35.88  54.247  1 57.93  ? 167 ILE   A CD1  1 1 
ATOM   1322 N  N    . VAL   A 1 169 ? 31.475 32.073 55.552  1 55.11  ? 168 VAL   A N    1 1 
ATOM   1323 C  CA   . VAL   A 1 169 ? 32.361 31.181 56.289  1 54.54  ? 168 VAL   A CA   1 1 
ATOM   1324 C  C    . VAL   A 1 169 ? 32.674 31.692 57.698  1 53.88  ? 168 VAL   A C    1 1 
ATOM   1325 O  O    . VAL   A 1 169 ? 33.394 32.673 57.868  1 53.85  ? 168 VAL   A O    1 1 
ATOM   1326 C  CB   . VAL   A 1 169 ? 33.643 30.864 55.494  1 55.08  ? 168 VAL   A CB   1 1 
ATOM   1327 C  CG1  . VAL   A 1 169 ? 34.564 29.943 56.285  1 55.53  ? 168 VAL   A CG1  1 1 
ATOM   1328 C  CG2  . VAL   A 1 169 ? 33.298 30.26  54.14   1 55.58  ? 168 VAL   A CG2  1 1 
ATOM   1329 N  N    . THR   A 1 170 ? 32.128 31.019 58.71   1 53.21  ? 169 THR   A N    1 1 
ATOM   1330 C  CA   . THR   A 1 170 ? 32.351 31.376 60.104  1 52.95  ? 169 THR   A CA   1 1 
ATOM   1331 C  C    . THR   A 1 170 ? 33.456 30.497 60.697  1 53.05  ? 169 THR   A C    1 1 
ATOM   1332 O  O    . THR   A 1 170 ? 33.241 29.306 60.894  1 53.12  ? 169 THR   A O    1 1 
ATOM   1333 C  CB   . THR   A 1 170 ? 31.052 31.204 60.893  1 53.69  ? 169 THR   A CB   1 1 
ATOM   1334 O  OG1  . THR   A 1 170 ? 30.01  31.978 60.296  1 54.25  ? 169 THR   A OG1  1 1 
ATOM   1335 C  CG2  . THR   A 1 170 ? 31.212 31.564 62.357  1 54.11  ? 169 THR   A CG2  1 1 
ATOM   1336 N  N    . VAL   A 1 171 ? 34.635 31.068 60.976  1 52.97  ? 170 VAL   A N    1 1 
ATOM   1337 C  CA   . VAL   A 1 171 ? 35.732 30.3   61.563  1 53.38  ? 170 VAL   A CA   1 1 
ATOM   1338 C  C    . VAL   A 1 171 ? 35.65  30.271 63.086  1 54.03  ? 170 VAL   A C    1 1 
ATOM   1339 O  O    . VAL   A 1 171 ? 35.888 31.281 63.757  1 54.44  ? 170 VAL   A O    1 1 
ATOM   1340 C  CB   . VAL   A 1 171 ? 37.118 30.756 61.073  1 53.96  ? 170 VAL   A CB   1 1 
ATOM   1341 C  CG1  . VAL   A 1 171 ? 38.219 29.906 61.701  1 54.43  ? 170 VAL   A CG1  1 1 
ATOM   1342 C  CG2  . VAL   A 1 171 ? 37.195 30.708 59.554  1 54.47  ? 170 VAL   A CG2  1 1 
ATOM   1343 N  N    . ALA   A 1 172 ? 35.286 29.11  63.629  1 54.08  ? 171 ALA   A N    1 1 
ATOM   1344 C  CA   . ALA   A 1 172 ? 35.163 28.884 65.078  1 54.42  ? 171 ALA   A CA   1 1 
ATOM   1345 C  C    . ALA   A 1 172 ? 36.135 27.711 65.499  1 54.6   ? 171 ALA   A C    1 1 
ATOM   1346 O  O    . ALA   A 1 172 ? 36.997 27.367 64.699  1 55.09  ? 171 ALA   A O    1 1 
ATOM   1347 C  CB   . ALA   A 1 172 ? 33.691 28.597 65.417  1 54.6   ? 171 ALA   A CB   1 1 
ATOM   1348 N  N    . SER   A 1 173 ? 36.051 27.127 66.701  1 54.42  ? 172 SER   A N    1 1 
ATOM   1349 C  CA   . SER   A 1 173 ? 36.922 26.029 67.119  1 55.15  ? 172 SER   A CA   1 1 
ATOM   1350 C  C    . SER   A 1 173 ? 36.064 24.922 67.748  1 55.22  ? 172 SER   A C    1 1 
ATOM   1351 O  O    . SER   A 1 173 ? 34.849 25.09  67.877  1 55.25  ? 172 SER   A O    1 1 
ATOM   1352 C  CB   . SER   A 1 173 ? 37.926 26.563 68.148  1 57.15  ? 172 SER   A CB   1 1 
ATOM   1353 O  OG   . SER   A 1 173 ? 38.617 25.582 68.91   1 59.37  ? 172 SER   A OG   1 1 
ATOM   1354 N  N    . VAL   A 1 174 ? 36.686 23.799 68.166  1 55.12  ? 173 VAL   A N    1 1 
ATOM   1355 C  CA   . VAL   A 1 174 ? 35.992 22.763 68.944  1 55.55  ? 173 VAL   A CA   1 1 
ATOM   1356 C  C    . VAL   A 1 174 ? 35.39  23.359 70.246  1 56.12  ? 173 VAL   A C    1 1 
ATOM   1357 O  O    . VAL   A 1 174 ? 34.429 22.806 70.79   1 55.87  ? 173 VAL   A O    1 1 
ATOM   1358 C  CB   . VAL   A 1 174 ? 36.859 21.517 69.232  1 56.02  ? 173 VAL   A CB   1 1 
ATOM   1359 C  CG1  . VAL   A 1 174 ? 36.787 20.537 68.08   1 56.42  ? 173 VAL   A CG1  1 1 
ATOM   1360 C  CG2  . VAL   A 1 174 ? 38.306 21.89  69.547  1 56.48  ? 173 VAL   A CG2  1 1 
ATOM   1361 N  N    . CYS   A 1 175 ? 35.934 24.532 70.691  1 56.74  ? 174 CYS   A N    1 1 
ATOM   1362 C  CA   . CYS   A 1 175 ? 35.506 25.383 71.81   1 57.71  ? 174 CYS   A CA   1 1 
ATOM   1363 C  C    . CYS   A 1 175 ? 34.144 26.088 71.542  1 58.79  ? 174 CYS   A C    1 1 
ATOM   1364 O  O    . CYS   A 1 175 ? 33.783 27.008 72.27   1 59.02  ? 174 CYS   A O    1 1 
ATOM   1365 C  CB   . CYS   A 1 175 ? 36.595 26.403 72.136  1 57.87  ? 174 CYS   A CB   1 1 
ATOM   1366 S  SG   . CYS   A 1 175 ? 38.2   25.674 72.555  1 58.64  ? 174 CYS   A SG   1 1 
ATOM   1367 N  N    . GLY   A 1 176 ? 33.477 25.705 70.451  1 59.17  ? 175 GLY   A N    1 1 
ATOM   1368 C  CA   . GLY   A 1 176 ? 32.142 26.12  70.036  1 59.75  ? 175 GLY   A CA   1 1 
ATOM   1369 C  C    . GLY   A 1 176 ? 31.139 24.985 70.189  1 60.05  ? 175 GLY   A C    1 1 
ATOM   1370 O  O    . GLY   A 1 176 ? 29.931 25.203 70.104  1 60.16  ? 175 GLY   A O    1 1 
ATOM   1371 N  N    . HIS   A 1 177 ? 31.642 23.754 70.414  1 60.04  ? 176 HIS   A N    1 1 
ATOM   1372 C  CA   . HIS   A 1 177 ? 30.879 22.542 70.633  1 60.61  ? 176 HIS   A CA   1 1 
ATOM   1373 C  C    . HIS   A 1 177 ? 31.044 22.032 72.066  1 61.61  ? 176 HIS   A C    1 1 
ATOM   1374 O  O    . HIS   A 1 177 ? 30.139 21.36  72.559  1 62.01  ? 176 HIS   A O    1 1 
ATOM   1375 C  CB   . HIS   A 1 177 ? 31.271 21.466 69.619  1 60.96  ? 176 HIS   A CB   1 1 
ATOM   1376 C  CG   . HIS   A 1 177 ? 30.828 21.789 68.225  1 62.65  ? 176 HIS   A CG   1 1 
ATOM   1377 N  ND1  . HIS   A 1 177 ? 29.66  21.266 67.699  1 64.32  ? 176 HIS   A ND1  1 1 
ATOM   1378 C  CD2  . HIS   A 1 177 ? 31.394 22.602 67.301  1 63.62  ? 176 HIS   A CD2  1 1 
ATOM   1379 C  CE1  . HIS   A 1 177 ? 29.561 21.761 66.475  1 64.72  ? 176 HIS   A CE1  1 1 
ATOM   1380 N  NE2  . HIS   A 1 177 ? 30.583 22.569 66.19   1 64.56  ? 176 HIS   A NE2  1 1 
ATOM   1381 N  N    . GLU   A 1 178 ? 32.165 22.371 72.753  1 61.84  ? 177 GLU   A N    1 1 
ATOM   1382 C  CA   . GLU   A 1 178 ? 32.408 21.971 74.145  1 62.5   ? 177 GLU   A CA   1 1 
ATOM   1383 C  C    . GLU   A 1 178 ? 33.528 22.814 74.806  1 62.59  ? 177 GLU   A C    1 1 
ATOM   1384 O  O    . GLU   A 1 178 ? 34.603 22.972 74.229  1 62.73  ? 177 GLU   A O    1 1 
ATOM   1385 C  CB   . GLU   A 1 178 ? 32.655 20.455 74.239  1 65.2   ? 177 GLU   A CB   1 1 
ATOM   1386 C  CG   . GLU   A 1 178 ? 33.234 19.968 75.551  1 70.47  ? 177 GLU   A CG   1 1 
ATOM   1387 C  CD   . GLU   A 1 178 ? 34.691 19.571 75.438  1 77.68  ? 177 GLU   A CD   1 1 
ATOM   1388 O  OE1  . GLU   A 1 178 ? 35.364 19.999 74.469  1 76.85  ? 177 GLU   A OE1  1 1 
ATOM   1389 O  OE2  . GLU   A 1 178 ? 35.157 18.813 76.321  1 81.96  ? 177 GLU   A OE2  1 1 
ATOM   1390 N  N    . GLY   A 1 179 ? 33.252 23.34  76.002  1 62.24  ? 178 GLY   A N    1 1 
ATOM   1391 C  CA   . GLY   A 1 179 ? 34.152 24.223 76.736  1 62.4   ? 178 GLY   A CA   1 1 
ATOM   1392 C  C    . GLY   A 1 179 ? 35.374 23.608 77.386  1 62.59  ? 178 GLY   A C    1 1 
ATOM   1393 O  O    . GLY   A 1 179 ? 35.32  22.506 77.935  1 62.8   ? 178 GLY   A O    1 1 
ATOM   1394 N  N    . ILE   A 1 180 ? 36.477 24.366 77.395  1 62.41  ? 179 ILE   A N    1 1 
ATOM   1395 C  CA   . ILE   A 1 180 ? 37.746 23.926 77.968  1 62.7   ? 179 ILE   A CA   1 1 
ATOM   1396 C  C    . ILE   A 1 180 ? 38.226 24.854 79.129  1 63.56  ? 179 ILE   A C    1 1 
ATOM   1397 O  O    . ILE   A 1 180 ? 37.875 26.03  79.136  1 63.54  ? 179 ILE   A O    1 1 
ATOM   1398 C  CB   . ILE   A 1 180 ? 38.813 23.76  76.831  1 62.68  ? 179 ILE   A CB   1 1 
ATOM   1399 C  CG1  . ILE   A 1 180 ? 39.409 25.093 76.379  1 63.21  ? 179 ILE   A CG1  1 1 
ATOM   1400 C  CG2  . ILE   A 1 180 ? 38.341 22.93  75.647  1 62.99  ? 179 ILE   A CG2  1 1 
ATOM   1401 C  CD1  . ILE   A 1 180 ? 40.809 25.1   76.63   1 64.17  ? 179 ILE   A CD1  1 1 
ATOM   1402 N  N    . PRO   A 1 181 ? 39.011 24.362 80.122  1 64.29  ? 180 PRO   A N    1 1 
ATOM   1403 C  CA   . PRO   A 1 181 ? 39.478 25.254 81.207  1 64.69  ? 180 PRO   A CA   1 1 
ATOM   1404 C  C    . PRO   A 1 181 ? 40.476 26.307 80.715  1 64.9   ? 180 PRO   A C    1 1 
ATOM   1405 O  O    . PRO   A 1 181 ? 41.172 26.075 79.731  1 65.19  ? 180 PRO   A O    1 1 
ATOM   1406 C  CB   . PRO   A 1 181 ? 40.135 24.289 82.215  1 65.75  ? 180 PRO   A CB   1 1 
ATOM   1407 C  CG   . PRO   A 1 181 ? 39.713 22.919 81.804  1 66.04  ? 180 PRO   A CG   1 1 
ATOM   1408 C  CD   . PRO   A 1 181 ? 39.504 22.986 80.323  1 64.23  ? 180 PRO   A CD   1 1 
ATOM   1409 N  N    . TYR   A 1 182 ? 40.52  27.474 81.39   1 64.82  ? 181 TYR   A N    1 1 
ATOM   1410 C  CA   . TYR   A 1 182 ? 41.352 28.653 81.084  1 65.38  ? 181 TYR   A CA   1 1 
ATOM   1411 C  C    . TYR   A 1 182 ? 40.828 29.457 79.885  1 64.47  ? 181 TYR   A C    1 1 
ATOM   1412 O  O    . TYR   A 1 182 ? 41.143 30.637 79.758  1 64.35  ? 181 TYR   A O    1 1 
ATOM   1413 C  CB   . TYR   A 1 182 ? 42.846 28.327 80.924  1 66.71  ? 181 TYR   A CB   1 1 
ATOM   1414 C  CG   . TYR   A 1 182 ? 43.376 27.374 81.967  1 69.72  ? 181 TYR   A CG   1 1 
ATOM   1415 C  CD1  . TYR   A 1 182 ? 43.253 27.655 83.324  1 71.56  ? 181 TYR   A CD1  1 1 
ATOM   1416 C  CD2  . TYR   A 1 182 ? 43.981 26.181 81.602  1 71.59  ? 181 TYR   A CD2  1 1 
ATOM   1417 C  CE1  . TYR   A 1 182 ? 43.734 26.778 84.287  1 73.05  ? 181 TYR   A CE1  1 1 
ATOM   1418 C  CE2  . TYR   A 1 182 ? 44.463 25.295 82.559  1 73     ? 181 TYR   A CE2  1 1 
ATOM   1419 C  CZ   . TYR   A 1 182 ? 44.346 25.601 83.899  1 74.2   ? 181 TYR   A CZ   1 1 
ATOM   1420 O  OH   . TYR   A 1 182 ? 44.827 24.714 84.827  1 76.83  ? 181 TYR   A OH   1 1 
ATOM   1421 N  N    . LEU   A 1 183 ? 40.012 28.837 79.02   1 63.51  ? 182 LEU   A N    1 1 
ATOM   1422 C  CA   . LEU   A 1 183 ? 39.447 29.515 77.861  1 62.61  ? 182 LEU   A CA   1 1 
ATOM   1423 C  C    . LEU   A 1 183 ? 37.925 29.701 77.972  1 60.99  ? 182 LEU   A C    1 1 
ATOM   1424 O  O    . LEU   A 1 183 ? 37.232 29.486 77      1 60.62  ? 182 LEU   A O    1 1 
ATOM   1425 C  CB   . LEU   A 1 183 ? 39.833 28.772 76.567  1 63.02  ? 182 LEU   A CB   1 1 
ATOM   1426 C  CG   . LEU   A 1 183 ? 41.323 28.662 76.305  1 64.8   ? 182 LEU   A CG   1 1 
ATOM   1427 C  CD1  . LEU   A 1 183 ? 41.597 27.874 75.052  1 65.17  ? 182 LEU   A CD1  1 1 
ATOM   1428 C  CD2  . LEU   A 1 183 ? 41.957 30.022 76.184  1 65.68  ? 182 LEU   A CD2  1 1 
ATOM   1429 N  N    . ILE   A 1 184 ? 37.403 30.085 79.154  1 59.98  ? 183 ILE   A N    1 1 
ATOM   1430 C  CA   . ILE   A 1 184 ? 35.965 30.313 79.317  1 59.23  ? 183 ILE   A CA   1 1 
ATOM   1431 C  C    . ILE   A 1 184 ? 35.495 31.531 78.529  1 58.88  ? 183 ILE   A C    1 1 
ATOM   1432 O  O    . ILE   A 1 184 ? 34.492 31.395 77.836  1 59.79  ? 183 ILE   A O    1 1 
ATOM   1433 C  CB   . ILE   A 1 184 ? 35.466 30.35  80.774  1 59.38  ? 183 ILE   A CB   1 1 
ATOM   1434 C  CG1  . ILE   A 1 184 ? 36.14  29.263 81.629  1 60.54  ? 183 ILE   A CG1  1 1 
ATOM   1435 C  CG2  . ILE   A 1 184 ? 33.939 30.262 80.82   1 59.42  ? 183 ILE   A CG2  1 1 
ATOM   1436 C  CD1  . ILE   A 1 184 ? 35.719 29.262 83.11   1 61.66  ? 183 ILE   A CD1  1 1 
ATOM   1437 N  N    . PRO   A 1 185 ? 36.173 32.706 78.55   1 57.67  ? 184 PRO   A N    1 1 
ATOM   1438 C  CA   . PRO   A 1 185 ? 35.693 33.826 77.721  1 56.94  ? 184 PRO   A CA   1 1 
ATOM   1439 C  C    . PRO   A 1 185 ? 35.792 33.508 76.228  1 55.82  ? 184 PRO   A C    1 1 
ATOM   1440 O  O    . PRO   A 1 185 ? 34.885 33.839 75.464  1 55.88  ? 184 PRO   A O    1 1 
ATOM   1441 C  CB   . PRO   A 1 185 ? 36.601 34.984 78.125  1 57.92  ? 184 PRO   A CB   1 1 
ATOM   1442 C  CG   . PRO   A 1 185 ? 37.837 34.342 78.642  1 58.55  ? 184 PRO   A CG   1 1 
ATOM   1443 C  CD   . PRO   A 1 185 ? 37.394 33.074 79.294  1 57.09  ? 184 PRO   A CD   1 1 
ATOM   1444 N  N    . TYR   A 1 186 ? 36.865 32.805 75.831  1 54.69  ? 185 TYR   A N    1 1 
ATOM   1445 C  CA   . TYR   A 1 186 ? 37.108 32.403 74.452  1 54.06  ? 185 TYR   A CA   1 1 
ATOM   1446 C  C    . TYR   A 1 186 ? 36.101 31.353 73.98   1 53.42  ? 185 TYR   A C    1 1 
ATOM   1447 O  O    . TYR   A 1 186 ? 35.592 31.463 72.875  1 53.88  ? 185 TYR   A O    1 1 
ATOM   1448 C  CB   . TYR   A 1 186 ? 38.545 31.896 74.313  1 53.87  ? 185 TYR   A CB   1 1 
ATOM   1449 C  CG   . TYR   A 1 186 ? 38.857 31.27  72.975  1 54.4   ? 185 TYR   A CG   1 1 
ATOM   1450 C  CD1  . TYR   A 1 186 ? 39.185 32.052 71.88   1 55.28  ? 185 TYR   A CD1  1 1 
ATOM   1451 C  CD2  . TYR   A 1 186 ? 38.876 29.892 72.818  1 55.3   ? 185 TYR   A CD2  1 1 
ATOM   1452 C  CE1  . TYR   A 1 186 ? 39.519 31.478 70.658  1 56.35  ? 185 TYR   A CE1  1 1 
ATOM   1453 C  CE2  . TYR   A 1 186 ? 39.193 29.306 71.598  1 56.11  ? 185 TYR   A CE2  1 1 
ATOM   1454 C  CZ   . TYR   A 1 186 ? 39.525 30.103 70.523  1 57.11  ? 185 TYR   A CZ   1 1 
ATOM   1455 O  OH   . TYR   A 1 186 ? 39.849 29.519 69.326  1 58.63  ? 185 TYR   A OH   1 1 
ATOM   1456 N  N    . CYS   A 1 187 ? 35.836 30.329 74.794  1 52.35  ? 186 CYS   A N    1 1 
ATOM   1457 C  CA   . CYS   A 1 187 ? 34.873 29.282 74.457  1 51.85  ? 186 CYS   A CA   1 1 
ATOM   1458 C  C    . CYS   A 1 187 ? 33.48  29.853 74.374  1 51.19  ? 186 CYS   A C    1 1 
ATOM   1459 O  O    . CYS   A 1 187 ? 32.708 29.426 73.52   1 51.81  ? 186 CYS   A O    1 1 
ATOM   1460 C  CB   . CYS   A 1 187 ? 34.93  28.118 75.44   1 52.48  ? 186 CYS   A CB   1 1 
ATOM   1461 S  SG   . CYS   A 1 187 ? 36.52  27.263 75.482  1 56.31  ? 186 CYS   A SG   1 1 
ATOM   1462 N  N    . SER   A 1 188 ? 33.152 30.827 75.229  1 49.83  ? 187 SER   A N    1 1 
ATOM   1463 C  CA   . SER   A 1 188 ? 31.85  31.453 75.204  1 49.64  ? 187 SER   A CA   1 1 
ATOM   1464 C  C    . SER   A 1 188 ? 31.635 32.181 73.885  1 49.53  ? 187 SER   A C    1 1 
ATOM   1465 O  O    . SER   A 1 188 ? 30.548 32.095 73.322  1 50.07  ? 187 SER   A O    1 1 
ATOM   1466 C  CB   . SER   A 1 188 ? 31.718 32.428 76.358  1 50.96  ? 187 SER   A CB   1 1 
ATOM   1467 O  OG   . SER   A 1 188 ? 30.352 32.721 76.58   1 53.55  ? 187 SER   A OG   1 1 
ATOM   1468 N  N    . SER   A 1 189 ? 32.681 32.841 73.352  1 48.63  ? 188 SER   A N    1 1 
ATOM   1469 C  CA   . SER   A 1 189 ? 32.583 33.545 72.067  1 48.08  ? 188 SER   A CA   1 1 
ATOM   1470 C  C    . SER   A 1 189 ? 32.598 32.578 70.881  1 46.35  ? 188 SER   A C    1 1 
ATOM   1471 O  O    . SER   A 1 189 ? 31.861 32.79  69.928  1 45.88  ? 188 SER   A O    1 1 
ATOM   1472 C  CB   . SER   A 1 189 ? 33.696 34.572 71.927  1 49.9   ? 188 SER   A CB   1 1 
ATOM   1473 O  OG   . SER   A 1 189 ? 34.942 33.939 71.695  1 52.83  ? 188 SER   A OG   1 1 
ATOM   1474 N  N    . LYS   A 1 190 ? 33.401 31.503 70.953  1 45.3   ? 189 LYS   A N    1 1 
ATOM   1475 C  CA   . LYS   A 1 190 ? 33.431 30.505 69.896  1 44.93  ? 189 LYS   A CA   1 1 
ATOM   1476 C  C    . LYS   A 1 190 ? 32.093 29.764 69.809  1 45.6   ? 189 LYS   A C    1 1 
ATOM   1477 O  O    . LYS   A 1 190 ? 31.627 29.497 68.706  1 46.29  ? 189 LYS   A O    1 1 
ATOM   1478 C  CB   . LYS   A 1 190 ? 34.618 29.547 70.046  1 45.25  ? 189 LYS   A CB   1 1 
ATOM   1479 C  CG   . LYS   A 1 190 ? 35.955 30.197 69.726  1 47.94  ? 189 LYS   A CG   1 1 
ATOM   1480 C  CD   . LYS   A 1 190 ? 36.094 30.559 68.263  1 52.92  ? 189 LYS   A CD   1 1 
ATOM   1481 C  CE   . LYS   A 1 190 ? 36.386 32.026 68.024  1 57.25  ? 189 LYS   A CE   1 1 
ATOM   1482 N  NZ   . LYS   A 1 190 ? 36.24  32.405 66.576  1 59.82  ? 189 LYS   A NZ   1 1 
ATOM   1483 N  N    . PHE   A 1 191 ? 31.432 29.501 70.947  1 45.36  ? 190 PHE   A N    1 1 
ATOM   1484 C  CA   . PHE   A 1 191 ? 30.105 28.866 70.956  1 45.73  ? 190 PHE   A CA   1 1 
ATOM   1485 C  C    . PHE   A 1 191 ? 29.085 29.782 70.264  1 45.75  ? 190 PHE   A C    1 1 
ATOM   1486 O  O    . PHE   A 1 191 ? 28.214 29.304 69.544  1 46.01  ? 190 PHE   A O    1 1 
ATOM   1487 C  CB   . PHE   A 1 191 ? 29.637 28.631 72.392  1 46     ? 190 PHE   A CB   1 1 
ATOM   1488 C  CG   . PHE   A 1 191 ? 29.68  27.21  72.895  1 47.04  ? 190 PHE   A CG   1 1 
ATOM   1489 C  CD1  . PHE   A 1 191 ? 30.848 26.675 73.406  1 47.86  ? 190 PHE   A CD1  1 1 
ATOM   1490 C  CD2  . PHE   A 1 191 ? 28.529 26.448 72.962  1 48.14  ? 190 PHE   A CD2  1 1 
ATOM   1491 C  CE1  . PHE   A 1 191 ? 30.876 25.39  73.93   1 48.5   ? 190 PHE   A CE1  1 1 
ATOM   1492 C  CE2  . PHE   A 1 191 ? 28.558 25.163 73.495  1 48.87  ? 190 PHE   A CE2  1 1 
ATOM   1493 C  CZ   . PHE   A 1 191 ? 29.729 24.647 73.982  1 48.44  ? 190 PHE   A CZ   1 1 
ATOM   1494 N  N    . ALA   A 1 192 ? 29.204 31.1   70.489  1 45.45  ? 191 ALA   A N    1 1 
ATOM   1495 C  CA   . ALA   A 1 192 ? 28.361 32.128 69.895  1 45.66  ? 191 ALA   A CA   1 1 
ATOM   1496 C  C    . ALA   A 1 192 ? 28.549 32.16  68.378  1 45.93  ? 191 ALA   A C    1 1 
ATOM   1497 O  O    . ALA   A 1 192 ? 27.576 32.338 67.642  1 46.33  ? 191 ALA   A O    1 1 
ATOM   1498 C  CB   . ALA   A 1 192 ? 28.706 33.482 70.491  1 45.63  ? 191 ALA   A CB   1 1 
ATOM   1499 N  N    . ALA   A 1 193 ? 29.793 31.979 67.909  1 45.23  ? 192 ALA   A N    1 1 
ATOM   1500 C  CA   . ALA   A 1 193 ? 30.107 31.953 66.491  1 44.92  ? 192 ALA   A CA   1 1 
ATOM   1501 C  C    . ALA   A 1 193 ? 29.439 30.739 65.815  1 44.82  ? 192 ALA   A C    1 1 
ATOM   1502 O  O    . ALA   A 1 193 ? 28.862 30.88  64.738  1 44.78  ? 192 ALA   A O    1 1 
ATOM   1503 C  CB   . ALA   A 1 193 ? 31.617 31.929 66.296  1 44.83  ? 192 ALA   A CB   1 1 
ATOM   1504 N  N    . VAL   A 1 194 ? 29.457 29.567 66.478  1 44.51  ? 193 VAL   A N    1 1 
ATOM   1505 C  CA   . VAL   A 1 194 ? 28.814 28.339 65.977  1 44.64  ? 193 VAL   A CA   1 1 
ATOM   1506 C  C    . VAL   A 1 194 ? 27.27  28.476 65.927  1 44.75  ? 193 VAL   A C    1 1 
ATOM   1507 O  O    . VAL   A 1 194 ? 26.605 27.926 65.049  1 44.59  ? 193 VAL   A O    1 1 
ATOM   1508 C  CB   . VAL   A 1 194 ? 29.267 27.114 66.807  1 45.13  ? 193 VAL   A CB   1 1 
ATOM   1509 C  CG1  . VAL   A 1 194 ? 28.449 25.874 66.465  1 45.53  ? 193 VAL   A CG1  1 1 
ATOM   1510 C  CG2  . VAL   A 1 194 ? 30.756 26.85  66.613  1 45.55  ? 193 VAL   A CG2  1 1 
ATOM   1511 N  N    . GLY   A 1 195 ? 26.726 29.244 66.857  1 44.85  ? 194 GLY   A N    1 1 
ATOM   1512 C  CA   . GLY   A 1 195 ? 25.301 29.516 66.904  1 45.5   ? 194 GLY   A CA   1 1 
ATOM   1513 C  C    . GLY   A 1 195 ? 24.867 30.563 65.902  1 45.91  ? 194 GLY   A C    1 1 
ATOM   1514 O  O    . GLY   A 1 195 ? 23.753 30.506 65.381  1 46.09  ? 194 GLY   A O    1 1 
ATOM   1515 N  N    . PHE   A 1 196 ? 25.75  31.518 65.599  1 45.79  ? 195 PHE   A N    1 1 
ATOM   1516 C  CA   . PHE   A 1 196 ? 25.467 32.538 64.601  1 46.05  ? 195 PHE   A CA   1 1 
ATOM   1517 C  C    . PHE   A 1 196 ? 25.379 31.865 63.234  1 46.55  ? 195 PHE   A C    1 1 
ATOM   1518 O  O    . PHE   A 1 196 ? 24.492 32.198 62.468  1 47.19  ? 195 PHE   A O    1 1 
ATOM   1519 C  CB   . PHE   A 1 196 ? 26.551 33.618 64.624  1 46.04  ? 195 PHE   A CB   1 1 
ATOM   1520 C  CG   . PHE   A 1 196 ? 26.563 34.542 63.437  1 46.77  ? 195 PHE   A CG   1 1 
ATOM   1521 C  CD1  . PHE   A 1 196 ? 25.636 35.551 63.319  1 47.59  ? 195 PHE   A CD1  1 1 
ATOM   1522 C  CD2  . PHE   A 1 196 ? 27.506 34.395 62.432  1 47.73  ? 195 PHE   A CD2  1 1 
ATOM   1523 C  CE1  . PHE   A 1 196 ? 25.661 36.41  62.228  1 48.48  ? 195 PHE   A CE1  1 1 
ATOM   1524 C  CE2  . PHE   A 1 196 ? 27.523 35.25  61.342  1 48.33  ? 195 PHE   A CE2  1 1 
ATOM   1525 C  CZ   . PHE   A 1 196 ? 26.604 36.251 61.248  1 48.22  ? 195 PHE   A CZ   1 1 
ATOM   1526 N  N    . HIS   A 1 197 ? 26.27  30.911 62.926  1 46.28  ? 196 HIS   A N    1 1 
ATOM   1527 C  CA   . HIS   A 1 197 ? 26.216 30.184 61.656  1 46.32  ? 196 HIS   A CA   1 1 
ATOM   1528 C  C    . HIS   A 1 197 ? 24.984 29.276 61.649  1 47.28  ? 196 HIS   A C    1 1 
ATOM   1529 O  O    . HIS   A 1 197 ? 24.342 29.153 60.613  1 47.52  ? 196 HIS   A O    1 1 
ATOM   1530 C  CB   . HIS   A 1 197 ? 27.523 29.391 61.412  1 46.39  ? 196 HIS   A CB   1 1 
ATOM   1531 C  CG   . HIS   A 1 197 ? 27.413 28.22  60.471  1 47.71  ? 196 HIS   A CG   1 1 
ATOM   1532 N  ND1  . HIS   A 1 197 ? 27.853 28.301 59.162  1 49.35  ? 196 HIS   A ND1  1 1 
ATOM   1533 C  CD2  . HIS   A 1 197 ? 26.937 26.969 60.693  1 48.38  ? 196 HIS   A CD2  1 1 
ATOM   1534 C  CE1  . HIS   A 1 197 ? 27.617 27.109 58.633  1 49.56  ? 196 HIS   A CE1  1 1 
ATOM   1535 N  NE2  . HIS   A 1 197 ? 27.06  26.278 59.513  1 49.13  ? 196 HIS   A NE2  1 1 
ATOM   1536 N  N    . ARG   A 1 198 ? 24.639 28.654 62.79   1 47.99  ? 197 ARG   A N    1 1 
ATOM   1537 C  CA   . ARG   A 1 198 ? 23.46  27.787 62.842  1 49.25  ? 197 ARG   A CA   1 1 
ATOM   1538 C  C    . ARG   A 1 198 ? 22.149 28.56  62.63   1 49.52  ? 197 ARG   A C    1 1 
ATOM   1539 O  O    . ARG   A 1 198 ? 21.226 28.04  62.008  1 49.54  ? 197 ARG   A O    1 1 
ATOM   1540 C  CB   . ARG   A 1 198 ? 23.429 26.925 64.114  1 51.54  ? 197 ARG   A CB   1 1 
ATOM   1541 C  CG   . ARG   A 1 198 ? 23.622 25.451 63.783  1 55.99  ? 197 ARG   A CG   1 1 
ATOM   1542 C  CD   . ARG   A 1 198 ? 23.064 24.517 64.834  1 60.06  ? 197 ARG   A CD   1 1 
ATOM   1543 N  NE   . ARG   A 1 198 ? 24.071 24.171 65.837  1 64.04  ? 197 ARG   A NE   1 1 
ATOM   1544 C  CZ   . ARG   A 1 198 ? 24.945 23.172 65.718  1 66.77  ? 197 ARG   A CZ   1 1 
ATOM   1545 N  NH1  . ARG   A 1 198 ? 24.958 22.415 64.624  1 66.18  ? 197 ARG   A NH1  1 1 
ATOM   1546 N  NH2  . ARG   A 1 198 ? 25.814 22.923 66.692  1 66.79  ? 197 ARG   A NH2  1 1 
ATOM   1547 N  N    . GLY   A 1 199 ? 22.096 29.8   63.094  1 49.58  ? 198 GLY   A N    1 1 
ATOM   1548 C  CA   . GLY   A 1 199 ? 20.937 30.661 62.9    1 50.13  ? 198 GLY   A CA   1 1 
ATOM   1549 C  C    . GLY   A 1 199 ? 20.924 31.252 61.502  1 50.66  ? 198 GLY   A C    1 1 
ATOM   1550 O  O    . GLY   A 1 199 ? 19.862 31.415 60.904  1 51.07  ? 198 GLY   A O    1 1 
ATOM   1551 N  N    . LEU   A 1 200 ? 22.107 31.568 60.958  1 50.4   ? 199 LEU   A N    1 1 
ATOM   1552 C  CA   . LEU   A 1 200 ? 22.214 32.078 59.599  1 50.88  ? 199 LEU   A CA   1 1 
ATOM   1553 C  C    . LEU   A 1 200 ? 21.783 31.007 58.616  1 52.87  ? 199 LEU   A C    1 1 
ATOM   1554 O  O    . LEU   A 1 200 ? 21.09  31.311 57.662  1 53.94  ? 199 LEU   A O    1 1 
ATOM   1555 C  CB   . LEU   A 1 200 ? 23.644 32.509 59.281  1 49.98  ? 199 LEU   A CB   1 1 
ATOM   1556 C  CG   . LEU   A 1 200 ? 23.841 33.187 57.945  1 49.79  ? 199 LEU   A CG   1 1 
ATOM   1557 C  CD1  . LEU   A 1 200 ? 23.044 34.46  57.865  1 50.12  ? 199 LEU   A CD1  1 1 
ATOM   1558 C  CD2  . LEU   A 1 200 ? 25.274 33.509 57.729  1 49.86  ? 199 LEU   A CD2  1 1 
ATOM   1559 N  N    . THR   A 1 201 ? 22.136 29.751 58.873  1 53.39  ? 200 THR   A N    1 1 
ATOM   1560 C  CA   . THR   A 1 201 ? 21.747 28.64  58.025  1 54.28  ? 200 THR   A CA   1 1 
ATOM   1561 C  C    . THR   A 1 201 ? 20.232 28.372 58.112  1 55.8   ? 200 THR   A C    1 1 
ATOM   1562 O  O    . THR   A 1 201 ? 19.617 28.119 57.084  1 56.05  ? 200 THR   A O    1 1 
ATOM   1563 C  CB   . THR   A 1 201 ? 22.618 27.436 58.347  1 54.92  ? 200 THR   A CB   1 1 
ATOM   1564 O  OG1  . THR   A 1 201 ? 23.985 27.81  58.185  1 55.54  ? 200 THR   A OG1  1 1 
ATOM   1565 C  CG2  . THR   A 1 201 ? 22.308 26.248 57.478  1 55.11  ? 200 THR   A CG2  1 1 
ATOM   1566 N  N    . SER   A 1 202 ? 19.62  28.467 59.313  1 56.89  ? 201 SER   A N    1 1 
ATOM   1567 C  CA   . SER   A 1 202 ? 18.167 28.254 59.435  1 58.31  ? 201 SER   A CA   1 1 
ATOM   1568 C  C    . SER   A 1 202 ? 17.37  29.42  58.848  1 59.91  ? 201 SER   A C    1 1 
ATOM   1569 O  O    . SER   A 1 202 ? 16.359 29.187 58.198  1 59.8   ? 201 SER   A O    1 1 
ATOM   1570 C  CB   . SER   A 1 202 ? 17.749 27.983 60.882  1 59.03  ? 201 SER   A CB   1 1 
ATOM   1571 O  OG   . SER   A 1 202 ? 16.37  27.665 61.002  1 60.38  ? 201 SER   A OG   1 1 
ATOM   1572 N  N    . GLU   A 1 203 ? 17.823 30.661 59.061  1 61.24  ? 202 GLU   A N    1 1 
ATOM   1573 C  CA   . GLU   A 1 203 ? 17.142 31.845 58.531  1 62.76  ? 202 GLU   A CA   1 1 
ATOM   1574 C  C    . GLU   A 1 203 ? 17.318 31.977 57.031  1 63.48  ? 202 GLU   A C    1 1 
ATOM   1575 O  O    . GLU   A 1 203 ? 16.348 32.319 56.356  1 64.48  ? 202 GLU   A O    1 1 
ATOM   1576 C  CB   . GLU   A 1 203 ? 17.559 33.131 59.262  1 66.05  ? 202 GLU   A CB   1 1 
ATOM   1577 C  CG   . GLU   A 1 203 ? 16.644 34.309 58.979  1 71.19  ? 202 GLU   A CG   1 1 
ATOM   1578 C  CD   . GLU   A 1 203 ? 17.125 35.61  59.587  1 76.44  ? 202 GLU   A CD   1 1 
ATOM   1579 O  OE1  . GLU   A 1 203 ? 17.781 36.401 58.87   1 78.51  ? 202 GLU   A OE1  1 1 
ATOM   1580 O  OE2  . GLU   A 1 203 ? 16.874 35.824 60.794  1 76.91  ? 202 GLU   A OE2  1 1 
ATOM   1581 N  N    . LEU   A 1 204 ? 18.506 31.644 56.463  1 62.87  ? 203 LEU   A N    1 1 
ATOM   1582 C  CA   . LEU   A 1 204 ? 18.68  31.677 54.997  1 62.51  ? 203 LEU   A CA   1 1 
ATOM   1583 C  C    . LEU   A 1 204 ? 17.697 30.706 54.348  1 63.18  ? 203 LEU   A C    1 1 
ATOM   1584 O  O    . LEU   A 1 204 ? 16.98  31.088 53.429  1 63.49  ? 203 LEU   A O    1 1 
ATOM   1585 C  CB   . LEU   A 1 204 ? 20.108 31.31  54.581  1 62.04  ? 203 LEU   A CB   1 1 
ATOM   1586 C  CG   . LEU   A 1 204 ? 21.154 32.39  54.763  1 63     ? 203 LEU   A CG   1 1 
ATOM   1587 C  CD1  . LEU   A 1 204 ? 22.548 31.855 54.502  1 63.53  ? 203 LEU   A CD1  1 1 
ATOM   1588 C  CD2  . LEU   A 1 204 ? 20.853 33.6   53.927  1 63.39  ? 203 LEU   A CD2  1 1 
ATOM   1589 N  N    . GLN   A 1 205 ? 17.579 29.5   54.922  1 63.69  ? 204 GLN   A N    1 1 
ATOM   1590 C  CA   . GLN   A 1 205 ? 16.657 28.472 54.459  1 65.06  ? 204 GLN   A CA   1 1 
ATOM   1591 C  C    . GLN   A 1 205 ? 15.191 28.907 54.602  1 65.67  ? 204 GLN   A C    1 1 
ATOM   1592 O  O    . GLN   A 1 205 ? 14.41  28.738 53.667  1 65.99  ? 204 GLN   A O    1 1 
ATOM   1593 C  CB   . GLN   A 1 205 ? 16.917 27.153 55.209  1 67.6   ? 204 GLN   A CB   1 1 
ATOM   1594 C  CG   . GLN   A 1 205 ? 16.088 25.97  54.711  1 72.96  ? 204 GLN   A CG   1 1 
ATOM   1595 C  CD   . GLN   A 1 205 ? 14.883 25.666 55.576  1 78.98  ? 204 GLN   A CD   1 1 
ATOM   1596 O  OE1  . GLN   A 1 205 ? 13.784 25.377 55.069  1 80.64  ? 204 GLN   A OE1  1 1 
ATOM   1597 N  NE2  . GLN   A 1 205 ? 15.063 25.716 56.902  1 80.01  ? 204 GLN   A NE2  1 1 
ATOM   1598 N  N    . ALA   A 1 206 ? 14.826 29.488 55.747  1 65.78  ? 205 ALA   A N    1 1 
ATOM   1599 C  CA   . ALA   A 1 206 ? 13.461 29.941 56.003  1 66.73  ? 205 ALA   A CA   1 1 
ATOM   1600 C  C    . ALA   A 1 206 ? 13.026 31.093 55.115  1 67.53  ? 205 ALA   A C    1 1 
ATOM   1601 O  O    . ALA   A 1 206 ? 11.829 31.242 54.872  1 67.93  ? 205 ALA   A O    1 1 
ATOM   1602 C  CB   . ALA   A 1 206 ? 13.303 30.337 57.455  1 67.16  ? 205 ALA   A CB   1 1 
ATOM   1603 N  N    . LEU   A 1 207 ? 13.975 31.909 54.631  1 67.5   ? 206 LEU   A N    1 1 
ATOM   1604 C  CA   . LEU   A 1 207 ? 13.627 33.026 53.759  1 67.94  ? 206 LEU   A CA   1 1 
ATOM   1605 C  C    . LEU   A 1 207 ? 13.616 32.69  52.253  1 69.58  ? 206 LEU   A C    1 1 
ATOM   1606 O  O    . LEU   A 1 207 ? 13.387 33.577 51.428  1 70.19  ? 206 LEU   A O    1 1 
ATOM   1607 C  CB   . LEU   A 1 207 ? 14.531 34.23  54.038  1 67.22  ? 206 LEU   A CB   1 1 
ATOM   1608 C  CG   . LEU   A 1 207 ? 14.514 34.787 55.454  1 67.25  ? 206 LEU   A CG   1 1 
ATOM   1609 C  CD1  . LEU   A 1 207 ? 15.369 36.012 55.544  1 67.52  ? 206 LEU   A CD1  1 1 
ATOM   1610 C  CD2  . LEU   A 1 207 ? 13.115 35.116 55.92   1 67.51  ? 206 LEU   A CD2  1 1 
ATOM   1611 N  N    . GLY   A 1 208 ? 13.828 31.426 51.904  1 70.15  ? 207 GLY   A N    1 1 
ATOM   1612 C  CA   . GLY   A 1 208 ? 13.842 30.99  50.511  1 70.99  ? 207 GLY   A CA   1 1 
ATOM   1613 C  C    . GLY   A 1 208 ? 15.172 31.169 49.805  1 70.31  ? 207 GLY   A C    1 1 
ATOM   1614 O  O    . GLY   A 1 208 ? 15.281 30.86  48.625  1 71.62  ? 207 GLY   A O    1 1 
ATOM   1615 N  N    . ILE   A 1 209 ? 16.206 31.636 50.52   1 68.78  ? 208 ILE   A N    1 1 
ATOM   1616 C  CA   . ILE   A 1 209 ? 17.536 31.883 49.968  1 67.52  ? 208 ILE   A CA   1 1 
ATOM   1617 C  C    . ILE   A 1 209 ? 18.326 30.609 49.739  1 67.41  ? 208 ILE   A C    1 1 
ATOM   1618 O  O    . ILE   A 1 209 ? 18.742 29.942 50.679  1 66.98  ? 208 ILE   A O    1 1 
ATOM   1619 C  CB   . ILE   A 1 209 ? 18.327 32.894 50.818  1 66.83  ? 208 ILE   A CB   1 1 
ATOM   1620 C  CG1  . ILE   A 1 209 ? 17.477 34.145 51.136  1 67.05  ? 208 ILE   A CG1  1 1 
ATOM   1621 C  CG2  . ILE   A 1 209 ? 19.635 33.242 50.128  1 66.85  ? 208 ILE   A CG2  1 1 
ATOM   1622 C  CD1  . ILE   A 1 209 ? 18.061 35.096 52.06   1 67.7   ? 208 ILE   A CD1  1 1 
ATOM   1623 N  N    . THR   A 1 210 ? 18.549 30.283 48.476  1 67.78  ? 209 THR   A N    1 1 
ATOM   1624 C  CA   . THR   A 1 210 ? 19.269 29.071 48.113  1 68.23  ? 209 THR   A CA   1 1 
ATOM   1625 C  C    . THR   A 1 210 ? 20.727 29.348 47.814  1 67.85  ? 209 THR   A C    1 1 
ATOM   1626 O  O    . THR   A 1 210 ? 21.595 28.709 48.405  1 68.32  ? 209 THR   A O    1 1 
ATOM   1627 C  CB   . THR   A 1 210 ? 18.558 28.306 46.981  1 70.09  ? 209 THR   A CB   1 1 
ATOM   1628 O  OG1  . THR   A 1 210 ? 17.957 29.216 46.049  1 71.78  ? 209 THR   A OG1  1 1 
ATOM   1629 C  CG2  . THR   A 1 210 ? 17.52  27.332 47.502  1 70.56  ? 209 THR   A CG2  1 1 
ATOM   1630 N  N    . GLY   A 1 211 ? 20.975 30.325 46.948  1 66.9   ? 210 GLY   A N    1 1 
ATOM   1631 C  CA   . GLY   A 1 211 ? 22.302 30.704 46.485  1 67.01  ? 210 GLY   A CA   1 1 
ATOM   1632 C  C    . GLY   A 1 211 ? 23.353 31.051 47.517  1 67.37  ? 210 GLY   A C    1 1 
ATOM   1633 O  O    . GLY   A 1 211 ? 24.547 30.986 47.206  1 68.09  ? 210 GLY   A O    1 1 
ATOM   1634 N  N    . ILE   A 1 212 ? 22.94  31.427 48.747  1 66.45  ? 211 ILE   A N    1 1 
ATOM   1635 C  CA   . ILE   A 1 212 ? 23.9   31.754 49.791  1 66.08  ? 211 ILE   A CA   1 1 
ATOM   1636 C  C    . ILE   A 1 212 ? 24.151 30.554 50.675  1 66.03  ? 211 ILE   A C    1 1 
ATOM   1637 O  O    . ILE   A 1 212 ? 23.295 30.182 51.477  1 66.31  ? 211 ILE   A O    1 1 
ATOM   1638 C  CB   . ILE   A 1 212 ? 23.489 32.981 50.624  1 66.25  ? 211 ILE   A CB   1 1 
ATOM   1639 C  CG1  . ILE   A 1 212 ? 23.256 34.195 49.725  1 67.16  ? 211 ILE   A CG1  1 1 
ATOM   1640 C  CG2  . ILE   A 1 212 ? 24.551 33.28  51.666  1 66.54  ? 211 ILE   A CG2  1 1 
ATOM   1641 C  CD1  . ILE   A 1 212 ? 22.665 35.377 50.422  1 68.38  ? 211 ILE   A CD1  1 1 
ATOM   1642 N  N    . LYS   A 1 213 ? 25.325 29.942 50.531  1 65.34  ? 212 LYS   A N    1 1 
ATOM   1643 C  CA   . LYS   A 1 213 ? 25.691 28.783 51.341  1 64.88  ? 212 LYS   A CA   1 1 
ATOM   1644 C  C    . LYS   A 1 213 ? 26.435 29.222 52.619  1 64.07  ? 212 LYS   A C    1 1 
ATOM   1645 O  O    . LYS   A 1 213 ? 26.827 30.382 52.74   1 64.27  ? 212 LYS   A O    1 1 
ATOM   1646 C  CB   . LYS   A 1 213 ? 26.55  27.804 50.521  1 66.7   ? 212 LYS   A CB   1 1 
ATOM   1647 C  CG   . LYS   A 1 213 ? 26.041 27.529 49.119  1 70.81  ? 212 LYS   A CG   1 1 
ATOM   1648 C  CD   . LYS   A 1 213 ? 24.694 26.828 49.084  1 76.73  ? 212 LYS   A CD   1 1 
ATOM   1649 C  CE   . LYS   A 1 213 ? 24.348 26.517 47.635  1 83.11  ? 212 LYS   A CE   1 1 
ATOM   1650 N  NZ   . LYS   A 1 213 ? 22.983 25.947 47.442  1 86.53  ? 212 LYS   A NZ   1 1 
ATOM   1651 N  N    . THR   A 1 214 ? 26.607 28.308 53.591  1 62.96  ? 213 THR   A N    1 1 
ATOM   1652 C  CA   . THR   A 1 214 ? 27.331 28.62  54.828  1 61.87  ? 213 THR   A CA   1 1 
ATOM   1653 C  C    . THR   A 1 214 ? 28.255 27.475 55.225  1 60.28  ? 213 THR   A C    1 1 
ATOM   1654 O  O    . THR   A 1 214 ? 27.86  26.311 55.181  1 60.28  ? 213 THR   A O    1 1 
ATOM   1655 C  CB   . THR   A 1 214 ? 26.374 28.937 55.988  1 63.32  ? 213 THR   A CB   1 1 
ATOM   1656 O  OG1  . THR   A 1 214 ? 25.33  27.968 56.033  1 64.27  ? 213 THR   A OG1  1 1 
ATOM   1657 C  CG2  . THR   A 1 214 ? 25.781 30.33  55.91   1 64.04  ? 213 THR   A CG2  1 1 
ATOM   1658 N  N    . SER   A 1 215 ? 29.48  27.804 55.622  1 58.95  ? 214 SER   A N    1 1 
ATOM   1659 C  CA   . SER   A 1 215 ? 30.443 26.819 56.107  1 58.1   ? 214 SER   A CA   1 1 
ATOM   1660 C  C    . SER   A 1 215 ? 31.017 27.304 57.433  1 56.86  ? 214 SER   A C    1 1 
ATOM   1661 O  O    . SER   A 1 215 ? 31.185 28.505 57.626  1 57.22  ? 214 SER   A O    1 1 
ATOM   1662 C  CB   . SER   A 1 215 ? 31.568 26.61  55.105  1 59.37  ? 214 SER   A CB   1 1 
ATOM   1663 O  OG   . SER   A 1 215 ? 31.282 25.503 54.268  1 61.49  ? 214 SER   A OG   1 1 
ATOM   1664 N  N    . CYS   A 1 216 ? 31.295 26.381 58.358  1 55     ? 215 CYS   A N    1 1 
ATOM   1665 C  CA   . CYS   A 1 216 ? 31.843 26.738 59.654  1 53.37  ? 215 CYS   A CA   1 1 
ATOM   1666 C  C    . CYS   A 1 216 ? 33.048 25.878 59.928  1 52.15  ? 215 CYS   A C    1 1 
ATOM   1667 O  O    . CYS   A 1 216 ? 32.893 24.672 60.038  1 52.11  ? 215 CYS   A O    1 1 
ATOM   1668 C  CB   . CYS   A 1 216 ? 30.784 26.577 60.739  1 53.59  ? 215 CYS   A CB   1 1 
ATOM   1669 S  SG   . CYS   A 1 216 ? 31.398 26.845 62.424  1 56.12  ? 215 CYS   A SG   1 1 
ATOM   1670 N  N    . LEU   A 1 217 ? 34.24  26.469 60.04   1 51.38  ? 216 LEU   A N    1 1 
ATOM   1671 C  CA   . LEU   A 1 217 ? 35.444 25.687 60.326  1 51.58  ? 216 LEU   A CA   1 1 
ATOM   1672 C  C    . LEU   A 1 217 ? 35.641 25.479 61.854  1 52.27  ? 216 LEU   A C    1 1 
ATOM   1673 O  O    . LEU   A 1 217 ? 35.771 26.445 62.597  1 52.16  ? 216 LEU   A O    1 1 
ATOM   1674 C  CB   . LEU   A 1 217 ? 36.673 26.338 59.684  1 51.29  ? 216 LEU   A CB   1 1 
ATOM   1675 C  CG   . LEU   A 1 217 ? 37.963 25.546 59.798  1 52.27  ? 216 LEU   A CG   1 1 
ATOM   1676 C  CD1  . LEU   A 1 217 ? 37.994 24.418 58.811  1 52.52  ? 216 LEU   A CD1  1 1 
ATOM   1677 C  CD2  . LEU   A 1 217 ? 39.158 26.437 59.583  1 52.88  ? 216 LEU   A CD2  1 1 
ATOM   1678 N  N    . CYS   A 1 218 ? 35.638 24.222 62.311  1 52.69  ? 217 CYS   A N    1 1 
ATOM   1679 C  CA   . CYS   A 1 218 ? 35.793 23.866 63.72   1 53.96  ? 217 CYS   A CA   1 1 
ATOM   1680 C  C    . CYS   A 1 218 ? 36.999 22.936 63.961  1 55.85  ? 217 CYS   A C    1 1 
ATOM   1681 O  O    . CYS   A 1 218 ? 36.804 21.737 64.192  1 56.29  ? 217 CYS   A O    1 1 
ATOM   1682 C  CB   . CYS   A 1 218 ? 34.508 23.239 64.255  1 54.03  ? 217 CYS   A CB   1 1 
ATOM   1683 S  SG   . CYS   A 1 218 ? 33.174 24.418 64.566  1 55.81  ? 217 CYS   A SG   1 1 
ATOM   1684 N  N    . PRO   A 1 219 ? 38.246 23.45  63.955  1 56.62  ? 218 PRO   A N    1 1 
ATOM   1685 C  CA   . PRO   A 1 219 ? 39.399 22.566 64.179  1 57.25  ? 218 PRO   A CA   1 1 
ATOM   1686 C  C    . PRO   A 1 219 ? 39.817 22.447 65.648  1 58.46  ? 218 PRO   A C    1 1 
ATOM   1687 O  O    . PRO   A 1 219 ? 39.284 23.151 66.5    1 58.68  ? 218 PRO   A O    1 1 
ATOM   1688 C  CB   . PRO   A 1 219 ? 40.494 23.214 63.324  1 57.67  ? 218 PRO   A CB   1 1 
ATOM   1689 C  CG   . PRO   A 1 219 ? 40.076 24.658 63.158  1 57.88  ? 218 PRO   A CG   1 1 
ATOM   1690 C  CD   . PRO   A 1 219 ? 38.684 24.832 63.692  1 56.24  ? 218 PRO   A CD   1 1 
ATOM   1691 N  N    . VAL   A 1 220 ? 40.768 21.542 65.951  1 59.18  ? 219 VAL   A N    1 1 
ATOM   1692 C  CA   . VAL   A 1 220 ? 41.307 21.371 67.307  1 60.4   ? 219 VAL   A CA   1 1 
ATOM   1693 C  C    . VAL   A 1 220 ? 42.578 22.286 67.458  1 61.18  ? 219 VAL   A C    1 1 
ATOM   1694 O  O    . VAL   A 1 220 ? 42.516 23.39  66.92   1 61.43  ? 219 VAL   A O    1 1 
ATOM   1695 C  CB   . VAL   A 1 220 ? 41.484 19.87  67.68   1 61.5   ? 219 VAL   A CB   1 1 
ATOM   1696 C  CG1  . VAL   A 1 220 ? 40.138 19.172 67.731  1 62.33  ? 219 VAL   A CG1  1 1 
ATOM   1697 C  CG2  . VAL   A 1 220 ? 42.42  19.161 66.708  1 62     ? 219 VAL   A CG2  1 1 
ATOM   1698 N  N    . PHE   A 1 221 ? 43.686 21.901 68.158  1 61.4   ? 220 PHE   A N    1 1 
ATOM   1699 C  CA   . PHE   A 1 221 ? 44.839 22.791 68.249  1 62.21  ? 220 PHE   A CA   1 1 
ATOM   1700 C  C    . PHE   A 1 221 ? 45.544 22.897 66.922  1 62.29  ? 220 PHE   A C    1 1 
ATOM   1701 O  O    . PHE   A 1 221 ? 45.92  21.886 66.336  1 62.62  ? 220 PHE   A O    1 1 
ATOM   1702 C  CB   . PHE   A 1 221 ? 45.846 22.389 69.328  1 62.59  ? 220 PHE   A CB   1 1 
ATOM   1703 C  CG   . PHE   A 1 221 ? 46.756 23.552 69.668  1 63.87  ? 220 PHE   A CG   1 1 
ATOM   1704 C  CD1  . PHE   A 1 221 ? 48.014 23.66  69.1    1 64.83  ? 220 PHE   A CD1  1 1 
ATOM   1705 C  CD2  . PHE   A 1 221 ? 46.322 24.576 70.493  1 64.94  ? 220 PHE   A CD2  1 1 
ATOM   1706 C  CE1  . PHE   A 1 221 ? 48.829 24.749 69.382  1 65.66  ? 220 PHE   A CE1  1 1 
ATOM   1707 C  CE2  . PHE   A 1 221 ? 47.147 25.655 70.785  1 65.67  ? 220 PHE   A CE2  1 1 
ATOM   1708 C  CZ   . PHE   A 1 221 ? 48.39  25.74  70.219  1 65.48  ? 220 PHE   A CZ   1 1 
ATOM   1709 N  N    . VAL   A 1 222 ? 45.732 24.125 66.451  1 61.75  ? 221 VAL   A N    1 1 
ATOM   1710 C  CA   . VAL   A 1 222 ? 46.473 24.366 65.23   1 61.7   ? 221 VAL   A CA   1 1 
ATOM   1711 C  C    . VAL   A 1 222 ? 47.771 25.052 65.636  1 62.28  ? 221 VAL   A C    1 1 
ATOM   1712 O  O    . VAL   A 1 222 ? 47.755 25.995 66.436  1 62.2   ? 221 VAL   A O    1 1 
ATOM   1713 C  CB   . VAL   A 1 222 ? 45.684 25.195 64.205  1 61.7   ? 221 VAL   A CB   1 1 
ATOM   1714 C  CG1  . VAL   A 1 222 ? 46.432 25.261 62.89   1 61.95  ? 221 VAL   A CG1  1 1 
ATOM   1715 C  CG2  . VAL   A 1 222 ? 44.296 24.617 64.002  1 62.05  ? 221 VAL   A CG2  1 1 
ATOM   1716 N  N    . ASN   A 1 223 ? 48.901 24.541 65.126  1 62.58  ? 222 ASN   A N    1 1 
ATOM   1717 C  CA   . ASN   A 1 223 ? 50.221 25.083 65.416  1 63.32  ? 222 ASN   A CA   1 1 
ATOM   1718 C  C    . ASN   A 1 223 ? 50.402 26.44  64.716  1 63.87  ? 222 ASN   A C    1 1 
ATOM   1719 O  O    . ASN   A 1 223 ? 50.986 26.498 63.634  1 64.41  ? 222 ASN   A O    1 1 
ATOM   1720 C  CB   . ASN   A 1 223 ? 51.29  24.101 64.938  1 64.64  ? 222 ASN   A CB   1 1 
ATOM   1721 C  CG   . ASN   A 1 223 ? 52.702 24.532 65.251  1 68.63  ? 222 ASN   A CG   1 1 
ATOM   1722 O  OD1  . ASN   A 1 223 ? 52.96  25.293 66.196  1 70.44  ? 222 ASN   A OD1  1 1 
ATOM   1723 N  ND2  . ASN   A 1 223 ? 53.65  24.051 64.459  1 69.35  ? 222 ASN   A ND2  1 1 
ATOM   1724 N  N    . THR   A 1 224 ? 49.885 27.531 65.307  1 63.4   ? 223 THR   A N    1 1 
ATOM   1725 C  CA   . THR   A 1 224 ? 50.014 28.868 64.703  1 63.28  ? 223 THR   A CA   1 1 
ATOM   1726 C  C    . THR   A 1 224 ? 50.661 29.896 65.626  1 63.07  ? 223 THR   A C    1 1 
ATOM   1727 O  O    . THR   A 1 224 ? 51.087 30.95  65.158  1 63.44  ? 223 THR   A O    1 1 
ATOM   1728 C  CB   . THR   A 1 224 ? 48.647 29.422 64.275  1 64.2   ? 223 THR   A CB   1 1 
ATOM   1729 O  OG1  . THR   A 1 224 ? 47.811 29.56  65.428  1 64.91  ? 223 THR   A OG1  1 1 
ATOM   1730 C  CG2  . THR   A 1 224 ? 47.971 28.579 63.209  1 64.44  ? 223 THR   A CG2  1 1 
ATOM   1731 N  N    . GLY   A 1 225 ? 50.697 29.612 66.917  1 62.32  ? 224 GLY   A N    1 1 
ATOM   1732 C  CA   . GLY   A 1 225 ? 51.213 30.561 67.885  1 62.23  ? 224 GLY   A CA   1 1 
ATOM   1733 C  C    . GLY   A 1 225 ? 50.124 31.396 68.523  1 61.99  ? 224 GLY   A C    1 1 
ATOM   1734 O  O    . GLY   A 1 225 ? 50.432 32.296 69.304  1 61.94  ? 224 GLY   A O    1 1 
ATOM   1735 N  N    . PHE   A 1 226 ? 48.838 31.095 68.206  1 61.84  ? 225 PHE   A N    1 1 
ATOM   1736 C  CA   . PHE   A 1 226 ? 47.63  31.729 68.74   1 62.39  ? 225 PHE   A CA   1 1 
ATOM   1737 C  C    . PHE   A 1 226 ? 47.69  31.595 70.286  1 65.21  ? 225 PHE   A C    1 1 
ATOM   1738 O  O    . PHE   A 1 226 ? 47.61  32.584 71.016  1 65.18  ? 225 PHE   A O    1 1 
ATOM   1739 C  CB   . PHE   A 1 226 ? 46.405 31.035 68.12   1 60.6   ? 225 PHE   A CB   1 1 
ATOM   1740 C  CG   . PHE   A 1 226 ? 45.05  31.64  68.382  1 59.17  ? 225 PHE   A CG   1 1 
ATOM   1741 C  CD1  . PHE   A 1 226 ? 44.78  32.95  68.038  1 59.09  ? 225 PHE   A CD1  1 1 
ATOM   1742 C  CD2  . PHE   A 1 226 ? 44.019 30.87  68.882  1 58.86  ? 225 PHE   A CD2  1 1 
ATOM   1743 C  CE1  . PHE   A 1 226 ? 43.522 33.493 68.252  1 59.19  ? 225 PHE   A CE1  1 1 
ATOM   1744 C  CE2  . PHE   A 1 226 ? 42.763 31.416 69.088  1 58.9   ? 225 PHE   A CE2  1 1 
ATOM   1745 C  CZ   . PHE   A 1 226 ? 42.525 32.724 68.781  1 58.6   ? 225 PHE   A CZ   1 1 
ATOM   1746 N  N    . THR   A 1 227 ? 47.969 30.383 70.761  1 67.28  ? 226 THR   A N    1 1 
ATOM   1747 C  CA   . THR   A 1 227 ? 48.27  30.123 72.166  1 69.8   ? 226 THR   A CA   1 1 
ATOM   1748 C  C    . THR   A 1 227 ? 49.666 29.394 72.175  1 72.08  ? 226 THR   A C    1 1 
ATOM   1749 O  O    . THR   A 1 227 ? 50.3   29.269 71.114  1 72.32  ? 226 THR   A O    1 1 
ATOM   1750 C  CB   . THR   A 1 227 ? 47.09  29.436 72.958  1 71.41  ? 226 THR   A CB   1 1 
ATOM   1751 O  OG1  . THR   A 1 227 ? 47.36  28.051 73.182  1 72.83  ? 226 THR   A OG1  1 1 
ATOM   1752 C  CG2  . THR   A 1 227 ? 45.703 29.626 72.332  1 71.54  ? 226 THR   A CG2  1 1 
ATOM   1753 N  N    . LYS   A 1 228 ? 50.15  28.933 73.34   1 73.53  ? 227 LYS   A N    1 1 
ATOM   1754 C  CA   . LYS   A 1 228 ? 51.423 28.207 73.372  1 75.49  ? 227 LYS   A CA   1 1 
ATOM   1755 C  C    . LYS   A 1 228 ? 51.238 26.7   73.121  1 77.02  ? 227 LYS   A C    1 1 
ATOM   1756 O  O    . LYS   A 1 228 ? 51.716 26.189 72.109  1 76.82  ? 227 LYS   A O    1 1 
ATOM   1757 C  CB   . LYS   A 1 228 ? 52.249 28.496 74.647  1 78.02  ? 227 LYS   A CB   1 1 
ATOM   1758 C  CG   . LYS   A 1 228 ? 53.391 29.498 74.43   1 82.65  ? 227 LYS   A CG   1 1 
ATOM   1759 C  CD   . LYS   A 1 228 ? 54.454 28.989 73.43   1 87.03  ? 227 LYS   A CD   1 1 
ATOM   1760 C  CE   . LYS   A 1 228 ? 54.436 29.648 72.061  1 89.6   ? 227 LYS   A CE   1 1 
ATOM   1761 N  NZ   . LYS   A 1 228 ? 55.165 28.824 71.064  1 90.87  ? 227 LYS   A NZ   1 1 
ATOM   1762 N  N    . ASN   A 1 229 ? 50.547 25.996 74.024  1 78.38  ? 228 ASN   A N    1 1 
ATOM   1763 C  CA   . ASN   A 1 229 ? 50.358 24.553 73.915  1 80.28  ? 228 ASN   A CA   1 1 
ATOM   1764 C  C    . ASN   A 1 229 ? 48.856 24.177 73.947  1 81.46  ? 228 ASN   A C    1 1 
ATOM   1765 O  O    . ASN   A 1 229 ? 48.04  24.929 74.49   1 81.44  ? 228 ASN   A O    1 1 
ATOM   1766 C  CB   . ASN   A 1 229 ? 51.12  23.84  75.067  1 82.24  ? 228 ASN   A CB   1 1 
ATOM   1767 C  CG   . ASN   A 1 229 ? 52.589 24.177 75.174  1 86.19  ? 228 ASN   A CG   1 1 
ATOM   1768 O  OD1  . ASN   A 1 229 ? 53.33  24.182 74.182  1 87.88  ? 228 ASN   A OD1  1 1 
ATOM   1769 N  ND2  . ASN   A 1 229 ? 53.045 24.459 76.387  1 86.51  ? 228 ASN   A ND2  1 1 
ATOM   1770 N  N    . PRO   A 1 230 ? 48.479 22.999 73.399  1 82.24  ? 229 PRO   A N    1 1 
ATOM   1771 C  CA   . PRO   A 1 230 ? 47.059 22.587 73.439  1 83.04  ? 229 PRO   A CA   1 1 
ATOM   1772 C  C    . PRO   A 1 230 ? 46.531 22.27  74.836  1 84.48  ? 229 PRO   A C    1 1 
ATOM   1773 O  O    . PRO   A 1 230 ? 47.311 22.03  75.757  1 84.85  ? 229 PRO   A O    1 1 
ATOM   1774 C  CB   . PRO   A 1 230 ? 47.032 21.333 72.561  1 83.39  ? 229 PRO   A CB   1 1 
ATOM   1775 C  CG   . PRO   A 1 230 ? 48.42  20.802 72.604  1 83.54  ? 229 PRO   A CG   1 1 
ATOM   1776 C  CD   . PRO   A 1 230 ? 49.316 22     72.703  1 81.81  ? 229 PRO   A CD   1 1 
ATOM   1777 N  N    . SER   A 1 231 ? 45.206 22.232 74.99   1 85.19  ? 230 SER   A N    1 1 
ATOM   1778 C  CA   . SER   A 1 231 ? 44.592 21.942 76.287  1 86.45  ? 230 SER   A CA   1 1 
ATOM   1779 C  C    . SER   A 1 231 ? 44.565 20.448 76.674  1 87.19  ? 230 SER   A C    1 1 
ATOM   1780 O  O    . SER   A 1 231 ? 44.615 20.142 77.866  1 87.38  ? 230 SER   A O    1 1 
ATOM   1781 C  CB   . SER   A 1 231 ? 43.187 22.526 76.357  1 88.18  ? 230 SER   A CB   1 1 
ATOM   1782 O  OG   . SER   A 1 231 ? 42.347 21.939 75.377  1 90.67  ? 230 SER   A OG   1 1 
ATOM   1783 N  N    . THR   A 1 232 ? 44.45  19.521 75.698  1 87.52  ? 231 THR   A N    1 1 
ATOM   1784 C  CA   . THR   A 1 232 ? 44.349 18.087 76.027  1 88.33  ? 231 THR   A CA   1 1 
ATOM   1785 C  C    . THR   A 1 232 ? 45.224 17.155 75.15   1 88.9   ? 231 THR   A C    1 1 
ATOM   1786 O  O    . THR   A 1 232 ? 45.581 17.496 74.024  1 88.63  ? 231 THR   A O    1 1 
ATOM   1787 C  CB   . THR   A 1 232 ? 42.87  17.58  76.034  1 89.64  ? 231 THR   A CB   1 1 
ATOM   1788 O  OG1  . THR   A 1 232 ? 41.913 18.651 75.967  1 90.56  ? 231 THR   A OG1  1 1 
ATOM   1789 C  CG2  . THR   A 1 232 ? 42.567 16.677 77.238  1 89.98  ? 231 THR   A CG2  1 1 
ATOM   1790 N  N    . ARG   A 1 233 ? 45.551 15.962 75.69   1 89.5   ? 232 ARG   A N    1 1 
ATOM   1791 C  CA   . ARG   A 1 233 ? 46.349 14.937 75.018  1 90.42  ? 232 ARG   A CA   1 1 
ATOM   1792 C  C    . ARG   A 1 233 ? 45.46  13.955 74.23   1 90.76  ? 232 ARG   A C    1 1 
ATOM   1793 O  O    . ARG   A 1 233 ? 45.488 12.745 74.466  1 90.82  ? 232 ARG   A O    1 1 
ATOM   1794 C  CB   . ARG   A 1 233 ? 47.232 14.184 76.036  1 91.99  ? 232 ARG   A CB   1 1 
ATOM   1795 C  CG   . ARG   A 1 233 ? 48.58  14.85  76.297  1 95.57  ? 232 ARG   A CG   1 1 
ATOM   1796 C  CD   . ARG   A 1 233 ? 49.415 14.046 77.282  1 99.72  ? 232 ARG   A CD   1 1 
ATOM   1797 N  NE   . ARG   A 1 233 ? 50.788 14.548 77.401  1 103.38 ? 232 ARG   A NE   1 1 
ATOM   1798 C  CZ   . ARG   A 1 233 ? 51.664 14.138 78.317  1 106.02 ? 232 ARG   A CZ   1 1 
ATOM   1799 N  NH1  . ARG   A 1 233 ? 51.319 13.217 79.212  1 105.52 ? 232 ARG   A NH1  1 1 
ATOM   1800 N  NH2  . ARG   A 1 233 ? 52.889 14.647 78.348  1 106.35 ? 232 ARG   A NH2  1 1 
ATOM   1801 N  N    . PRO   A 1 236 ? 45.595 15.804 68.722  1 80.1   ? 235 PRO   A N    1 1 
ATOM   1802 C  CA   . PRO   A 1 236 ? 46.527 16.132 67.63   1 79.88  ? 235 PRO   A CA   1 1 
ATOM   1803 C  C    . PRO   A 1 236 ? 46.763 17.634 67.459  1 79.25  ? 235 PRO   A C    1 1 
ATOM   1804 O  O    . PRO   A 1 236 ? 45.877 18.453 67.737  1 79.63  ? 235 PRO   A O    1 1 
ATOM   1805 C  CB   . PRO   A 1 236 ? 45.827 15.557 66.394  1 80.71  ? 235 PRO   A CB   1 1 
ATOM   1806 C  CG   . PRO   A 1 236 ? 44.372 15.712 66.704  1 81.28  ? 235 PRO   A CG   1 1 
ATOM   1807 C  CD   . PRO   A 1 236 ? 44.252 15.468 68.207  1 79.83  ? 235 PRO   A CD   1 1 
ATOM   1808 N  N    . VAL   A 1 237 ? 47.965 17.998 66.993  1 77.97  ? 236 VAL   A N    1 1 
ATOM   1809 C  CA   . VAL   A 1 237 ? 48.263 19.391 66.725  1 77.06  ? 236 VAL   A CA   1 1 
ATOM   1810 C  C    . VAL   A 1 237 ? 48.416 19.557 65.232  1 76.1   ? 236 VAL   A C    1 1 
ATOM   1811 O  O    . VAL   A 1 237 ? 49.425 19.19  64.624  1 76.02  ? 236 VAL   A O    1 1 
ATOM   1812 C  CB   . VAL   A 1 237 ? 49.393 20.003 67.57   1 77.5   ? 236 VAL   A CB   1 1 
ATOM   1813 C  CG1  . VAL   A 1 237 ? 49.81  21.359 67.025  1 78.05  ? 236 VAL   A CG1  1 1 
ATOM   1814 C  CG2  . VAL   A 1 237 ? 48.939 20.145 69.009  1 77.88  ? 236 VAL   A CG2  1 1 
ATOM   1815 N  N    . LEU   A 1 238 ? 47.319 20.015 64.645  1 75.24  ? 237 LEU   A N    1 1 
ATOM   1816 C  CA   . LEU   A 1 238 ? 47.155 20.28  63.23   1 74.98  ? 237 LEU   A CA   1 1 
ATOM   1817 C  C    . LEU   A 1 238 ? 48.134 21.334 62.78   1 74.66  ? 237 LEU   A C    1 1 
ATOM   1818 O  O    . LEU   A 1 238 ? 48.454 22.248 63.542  1 74.92  ? 237 LEU   A O    1 1 
ATOM   1819 C  CB   . LEU   A 1 238 ? 45.754 20.829 62.973  1 74.95  ? 237 LEU   A CB   1 1 
ATOM   1820 C  CG   . LEU   A 1 238 ? 44.602 20.041 63.518  1 76.07  ? 237 LEU   A CG   1 1 
ATOM   1821 C  CD1  . LEU   A 1 238 ? 43.409 20.921 63.661  1 76.53  ? 237 LEU   A CD1  1 1 
ATOM   1822 C  CD2  . LEU   A 1 238 ? 44.309 18.842 62.647  1 76.64  ? 237 LEU   A CD2  1 1 
ATOM   1823 N  N    . GLU   A 1 239 ? 48.567 21.243 61.523  1 73.75  ? 238 GLU   A N    1 1 
ATOM   1824 C  CA   . GLU   A 1 239 ? 49.471 22.24  60.984  1 73.31  ? 238 GLU   A CA   1 1 
ATOM   1825 C  C    . GLU   A 1 239 ? 48.702 23.424 60.384  1 72.84  ? 238 GLU   A C    1 1 
ATOM   1826 O  O    . GLU   A 1 239 ? 47.497 23.315 60.149  1 72.83  ? 238 GLU   A O    1 1 
ATOM   1827 C  CB   . GLU   A 1 239 ? 50.462 21.603 59.999  1 75.26  ? 238 GLU   A CB   1 1 
ATOM   1828 C  CG   . GLU   A 1 239 ? 51.584 20.851 60.685  1 79.91  ? 238 GLU   A CG   1 1 
ATOM   1829 C  CD   . GLU   A 1 239 ? 52.378 21.702 61.658  1 86.51  ? 238 GLU   A CD   1 1 
ATOM   1830 O  OE1  . GLU   A 1 239 ? 52.593 22.899 61.357  1 86.85  ? 238 GLU   A OE1  1 1 
ATOM   1831 O  OE2  . GLU   A 1 239 ? 52.763 21.181 62.73   1 89.44  ? 238 GLU   A OE2  1 1 
ATOM   1832 N  N    . THR   A 1 240 ? 49.383 24.563 60.149  1 72.3   ? 239 THR   A N    1 1 
ATOM   1833 C  CA   . THR   A 1 240 ? 48.756 25.755 59.564  1 72.09  ? 239 THR   A CA   1 1 
ATOM   1834 C  C    . THR   A 1 240 ? 48.16  25.463 58.185  1 71.55  ? 239 THR   A C    1 1 
ATOM   1835 O  O    . THR   A 1 240 ? 47.06  25.912 57.888  1 71.72  ? 239 THR   A O    1 1 
ATOM   1836 C  CB   . THR   A 1 240 ? 49.777 26.896 59.421  1 73.41  ? 239 THR   A CB   1 1 
ATOM   1837 O  OG1  . THR   A 1 240 ? 50.835 26.462 58.565  1 74.41  ? 239 THR   A OG1  1 1 
ATOM   1838 C  CG2  . THR   A 1 240 ? 50.346 27.348 60.74   1 73.74  ? 239 THR   A CG2  1 1 
ATOM   1839 N  N    . ASP   A 1 241 ? 48.888 24.722 57.342  1 70.9   ? 240 ASP   A N    1 1 
ATOM   1840 C  CA   . ASP   A 1 241 ? 48.458 24.412 55.981  1 70.72  ? 240 ASP   A CA   1 1 
ATOM   1841 C  C    . ASP   A 1 241 ? 47.421 23.309 55.879  1 70.4   ? 240 ASP   A C    1 1 
ATOM   1842 O  O    . ASP   A 1 241 ? 46.603 23.339 54.969  1 70.63  ? 240 ASP   A O    1 1 
ATOM   1843 C  CB   . ASP   A 1 241 ? 49.665 24.086 55.09   1 72.14  ? 240 ASP   A CB   1 1 
ATOM   1844 C  CG   . ASP   A 1 241 ? 50.453 22.866 55.507  1 76.47  ? 240 ASP   A CG   1 1 
ATOM   1845 O  OD1  . ASP   A 1 241 ? 50.722 22.716 56.723  1 77.14  ? 240 ASP   A OD1  1 1 
ATOM   1846 O  OD2  . ASP   A 1 241 ? 50.817 22.068 54.619  1 78.48  ? 240 ASP   A OD2  1 1 
ATOM   1847 N  N    . THR   A 1 242 ? 47.465 22.328 56.778  1 69.85  ? 241 THR   A N    1 1 
ATOM   1848 C  CA   . THR   A 1 242 ? 46.532 21.206 56.768  1 69.91  ? 241 THR   A CA   1 1 
ATOM   1849 C  C    . THR   A 1 242 ? 45.102 21.675 56.998  1 69.74  ? 241 THR   A C    1 1 
ATOM   1850 O  O    . THR   A 1 242 ? 44.182 21.218 56.321  1 69.73  ? 241 THR   A O    1 1 
ATOM   1851 C  CB   . THR   A 1 242 ? 46.986 20.159 57.783  1 71.34  ? 241 THR   A CB   1 1 
ATOM   1852 O  OG1  . THR   A 1 242 ? 48.233 19.606 57.347  1 72.29  ? 241 THR   A OG1  1 1 
ATOM   1853 C  CG2  . THR   A 1 242 ? 45.964 19.053 57.979  1 71.85  ? 241 THR   A CG2  1 1 
ATOM   1854 N  N    . VAL   A 1 243 ? 44.931 22.624 57.92   1 69.66  ? 242 VAL   A N    1 1 
ATOM   1855 C  CA   . VAL   A 1 243 ? 43.64  23.218 58.261  1 70.15  ? 242 VAL   A CA   1 1 
ATOM   1856 C  C    . VAL   A 1 243 ? 43.083 24.044 57.097  1 70.42  ? 242 VAL   A C    1 1 
ATOM   1857 O  O    . VAL   A 1 243 ? 41.88  24.009 56.835  1 70.56  ? 242 VAL   A O    1 1 
ATOM   1858 C  CB   . VAL   A 1 243 ? 43.782 24.048 59.555  1 70.89  ? 242 VAL   A CB   1 1 
ATOM   1859 C  CG1  . VAL   A 1 243 ? 42.535 24.879 59.839  1 71.38  ? 242 VAL   A CG1  1 1 
ATOM   1860 C  CG2  . VAL   A 1 243 ? 44.099 23.138 60.726  1 71.49  ? 242 VAL   A CG2  1 1 
ATOM   1861 N  N    . ALA   A 1 244 ? 43.967 24.744 56.37   1 70.25  ? 243 ALA   A N    1 1 
ATOM   1862 C  CA   . ALA   A 1 244 ? 43.601 25.561 55.216  1 70.56  ? 243 ALA   A CA   1 1 
ATOM   1863 C  C    . ALA   A 1 244 ? 43.081 24.687 54.076  1 71.15  ? 243 ALA   A C    1 1 
ATOM   1864 O  O    . ALA   A 1 244 ? 42.14  25.08  53.388  1 71.27  ? 243 ALA   A O    1 1 
ATOM   1865 C  CB   . ALA   A 1 244 ? 44.803 26.359 54.753  1 70.54  ? 243 ALA   A CB   1 1 
ATOM   1866 N  N    . ARG   A 1 245 ? 43.68  23.495 53.886  1 71.29  ? 244 ARG   A N    1 1 
ATOM   1867 C  CA   . ARG   A 1 245 ? 43.239 22.539 52.871  1 71.74  ? 244 ARG   A CA   1 1 
ATOM   1868 C  C    . ARG   A 1 245 ? 41.85  22     53.23   1 71.52  ? 244 ARG   A C    1 1 
ATOM   1869 O  O    . ARG   A 1 245 ? 41.029 21.799 52.346  1 71.71  ? 244 ARG   A O    1 1 
ATOM   1870 C  CB   . ARG   A 1 245 ? 44.236 21.385 52.738  1 73.59  ? 244 ARG   A CB   1 1 
ATOM   1871 C  CG   . ARG   A 1 245 ? 45.581 21.786 52.152  1 77.48  ? 244 ARG   A CG   1 1 
ATOM   1872 C  CD   . ARG   A 1 245 ? 46.298 20.57  51.586  1 81.32  ? 244 ARG   A CD   1 1 
ATOM   1873 N  NE   . ARG   A 1 245 ? 47.537 20.242 52.296  1 84.32  ? 244 ARG   A NE   1 1 
ATOM   1874 C  CZ   . ARG   A 1 245 ? 47.607 19.472 53.381  1 86.04  ? 244 ARG   A CZ   1 1 
ATOM   1875 N  NH1  . ARG   A 1 245 ? 46.504 18.956 53.91   1 85.35  ? 244 ARG   A NH1  1 1 
ATOM   1876 N  NH2  . ARG   A 1 245 ? 48.778 19.223 53.949  1 85.7   ? 244 ARG   A NH2  1 1 
ATOM   1877 N  N    . SER   A 1 246 ? 41.583 21.776 54.526  1 70.98  ? 245 SER   A N    1 1 
ATOM   1878 C  CA   . SER   A 1 246 ? 40.279 21.314 54.995  1 70.81  ? 245 SER   A CA   1 1 
ATOM   1879 C  C    . SER   A 1 246 ? 39.214 22.393 54.767  1 70.43  ? 245 SER   A C    1 1 
ATOM   1880 O  O    . SER   A 1 246 ? 38.089 22.067 54.397  1 70.87  ? 245 SER   A O    1 1 
ATOM   1881 C  CB   . SER   A 1 246 ? 40.338 20.937 56.473  1 71.64  ? 245 SER   A CB   1 1 
ATOM   1882 O  OG   . SER   A 1 246 ? 41.046 19.722 56.654  1 73.4   ? 245 SER   A OG   1 1 
ATOM   1883 N  N    . LEU   A 1 247 ? 39.571 23.673 54.961  1 69.28  ? 246 LEU   A N    1 1 
ATOM   1884 C  CA   . LEU   A 1 247 ? 38.636 24.768 54.746  1 68.45  ? 246 LEU   A CA   1 1 
ATOM   1885 C  C    . LEU   A 1 247 ? 38.4   24.975 53.267  1 68.35  ? 246 LEU   A C    1 1 
ATOM   1886 O  O    . LEU   A 1 247 ? 37.247 25.133 52.872  1 68.96  ? 246 LEU   A O    1 1 
ATOM   1887 C  CB   . LEU   A 1 247 ? 39.117 26.066 55.407  1 68.02  ? 246 LEU   A CB   1 1 
ATOM   1888 C  CG   . LEU   A 1 247 ? 38.163 27.26  55.34   1 68.43  ? 246 LEU   A CG   1 1 
ATOM   1889 C  CD1  . LEU   A 1 247 ? 36.813 26.929 55.917  1 68.63  ? 246 LEU   A CD1  1 1 
ATOM   1890 C  CD2  . LEU   A 1 247 ? 38.727 28.448 56.07   1 68.75  ? 246 LEU   A CD2  1 1 
ATOM   1891 N  N    . ILE   A 1 248 ? 39.456 24.92  52.43   1 67.5   ? 247 ILE   A N    1 1 
ATOM   1892 C  CA   . ILE   A 1 248 ? 39.258 25.091 50.985  1 67.23  ? 247 ILE   A CA   1 1 
ATOM   1893 C  C    . ILE   A 1 248 ? 38.418 23.95  50.414  1 66.92  ? 247 ILE   A C    1 1 
ATOM   1894 O  O    . ILE   A 1 248 ? 37.642 24.189 49.499  1 67.26  ? 247 ILE   A O    1 1 
ATOM   1895 C  CB   . ILE   A 1 248 ? 40.557 25.344 50.163  1 67.61  ? 247 ILE   A CB   1 1 
ATOM   1896 C  CG1  . ILE   A 1 248 ? 40.249 26.027 48.815  1 68.01  ? 247 ILE   A CG1  1 1 
ATOM   1897 C  CG2  . ILE   A 1 248 ? 41.355 24.073 49.934  1 68.29  ? 247 ILE   A CG2  1 1 
ATOM   1898 C  CD1  . ILE   A 1 248 ? 40.081 27.452 48.905  1 68.87  ? 247 ILE   A CD1  1 1 
ATOM   1899 N  N    . ASP   A 1 249 ? 38.518 22.733 50.977  1 66.13  ? 248 ASP   A N    1 1 
ATOM   1900 C  CA   . ASP   A 1 249 ? 37.739 21.6   50.481  1 65.86  ? 248 ASP   A CA   1 1 
ATOM   1901 C  C    . ASP   A 1 249 ? 36.287 21.586 51      1 64.93  ? 248 ASP   A C    1 1 
ATOM   1902 O  O    . ASP   A 1 249 ? 35.407 21.024 50.344  1 65.08  ? 248 ASP   A O    1 1 
ATOM   1903 C  CB   . ASP   A 1 249 ? 38.457 20.267 50.752  1 67.63  ? 248 ASP   A CB   1 1 
ATOM   1904 C  CG   . ASP   A 1 249 ? 39.735 20.093 49.942  1 71.97  ? 248 ASP   A CG   1 1 
ATOM   1905 O  OD1  . ASP   A 1 249 ? 39.709 20.373 48.716  1 72.05  ? 248 ASP   A OD1  1 1 
ATOM   1906 O  OD2  . ASP   A 1 249 ? 40.764 19.685 50.536  1 74.39  ? 248 ASP   A OD2  1 1 
ATOM   1907 N  N    . GLY   A 1 250 ? 36.046 22.219 52.143  1 63.72  ? 249 GLY   A N    1 1 
ATOM   1908 C  CA   . GLY   A 1 250 ? 34.713 22.303 52.728  1 63.03  ? 249 GLY   A CA   1 1 
ATOM   1909 C  C    . GLY   A 1 250 ? 33.865 23.383 52.091  1 61.99  ? 249 GLY   A C    1 1 
ATOM   1910 O  O    . GLY   A 1 250 ? 32.644 23.242 51.992  1 62     ? 249 GLY   A O    1 1 
ATOM   1911 N  N    . ILE   A 1 251 ? 34.504 24.479 51.668  1 61.03  ? 250 ILE   A N    1 1 
ATOM   1912 C  CA   . ILE   A 1 251 ? 33.812 25.57  50.99   1 60.69  ? 250 ILE   A CA   1 1 
ATOM   1913 C  C    . ILE   A 1 251 ? 33.386 25.123 49.591  1 60.35  ? 250 ILE   A C    1 1 
ATOM   1914 O  O    . ILE   A 1 251 ? 32.269 25.421 49.173  1 60.18  ? 250 ILE   A O    1 1 
ATOM   1915 C  CB   . ILE   A 1 251 ? 34.704 26.827 50.953  1 60.85  ? 250 ILE   A CB   1 1 
ATOM   1916 C  CG1  . ILE   A 1 251 ? 34.925 27.366 52.369  1 61.39  ? 250 ILE   A CG1  1 1 
ATOM   1917 C  CG2  . ILE   A 1 251 ? 34.108 27.901 50.046  1 61.2   ? 250 ILE   A CG2  1 1 
ATOM   1918 C  CD1  . ILE   A 1 251 ? 35.975 28.397 52.45   1 62.56  ? 250 ILE   A CD1  1 1 
ATOM   1919 N  N    . LEU   A 1 252 ? 34.253 24.354 48.9    1 60.29  ? 251 LEU   A N    1 1 
ATOM   1920 C  CA   . LEU   A 1 252 ? 34.004 23.82  47.562  1 60.89  ? 251 LEU   A CA   1 1 
ATOM   1921 C  C    . LEU   A 1 252 ? 32.906 22.761 47.509  1 61.28  ? 251 LEU   A C    1 1 
ATOM   1922 O  O    . LEU   A 1 252 ? 32.228 22.648 46.491  1 61.48  ? 251 LEU   A O    1 1 
ATOM   1923 C  CB   . LEU   A 1 252 ? 35.295 23.301 46.927  1 61.14  ? 251 LEU   A CB   1 1 
ATOM   1924 C  CG   . LEU   A 1 252 ? 36.353 24.356 46.638  1 62.84  ? 251 LEU   A CG   1 1 
ATOM   1925 C  CD1  . LEU   A 1 252 ? 37.579 23.736 46.024  1 63.41  ? 251 LEU   A CD1  1 1 
ATOM   1926 C  CD2  . LEU   A 1 252 ? 35.819 25.464 45.747  1 63.56  ? 251 LEU   A CD2  1 1 
ATOM   1927 N  N    . THR   A 1 253 ? 32.713 21.999 48.592  1 61.37  ? 252 THR   A N    1 1 
ATOM   1928 C  CA   . THR   A 1 253 ? 31.615 21.03  48.634  1 61.85  ? 252 THR   A CA   1 1 
ATOM   1929 C  C    . THR   A 1 253 ? 30.373 21.591 49.396  1 62.52  ? 252 THR   A C    1 1 
ATOM   1930 O  O    . THR   A 1 253 ? 29.352 20.912 49.449  1 62.9   ? 252 THR   A O    1 1 
ATOM   1931 C  CB   . THR   A 1 253 ? 32.088 19.671 49.147  1 62.71  ? 252 THR   A CB   1 1 
ATOM   1932 O  OG1  . THR   A 1 253 ? 32.476 19.776 50.516  1 63.43  ? 252 THR   A OG1  1 1 
ATOM   1933 C  CG2  . THR   A 1 253 ? 33.228 19.115 48.318  1 62.95  ? 252 THR   A CG2  1 1 
ATOM   1934 N  N    . ASN   A 1 254 ? 30.456 22.838 49.938  1 62.36  ? 253 ASN   A N    1 1 
ATOM   1935 C  CA   . ASN   A 1 254 ? 29.401 23.548 50.665  1 62.61  ? 253 ASN   A CA   1 1 
ATOM   1936 C  C    . ASN   A 1 254 ? 28.977 22.826 51.932  1 62.41  ? 253 ASN   A C    1 1 
ATOM   1937 O  O    . ASN   A 1 254 ? 27.78  22.747 52.227  1 62.38  ? 253 ASN   A O    1 1 
ATOM   1938 C  CB   . ASN   A 1 254 ? 28.194 23.861 49.766  1 64.28  ? 253 ASN   A CB   1 1 
ATOM   1939 C  CG   . ASN   A 1 254 ? 28.464 24.833 48.645  1 67.6   ? 253 ASN   A CG   1 1 
ATOM   1940 O  OD1  . ASN   A 1 254 ? 27.956 24.678 47.532  1 68.69  ? 253 ASN   A OD1  1 1 
ATOM   1941 N  ND2  . ASN   A 1 254 ? 29.258 25.86  48.911  1 68.38  ? 253 ASN   A ND2  1 1 
ATOM   1942 N  N    . LYS   A 1 255 ? 29.957 22.3   52.691  1 62.22  ? 254 LYS   A N    1 1 
ATOM   1943 C  CA   . LYS   A 1 255 ? 29.654 21.597 53.936  1 62.48  ? 254 LYS   A CA   1 1 
ATOM   1944 C  C    . LYS   A 1 255 ? 29.408 22.582 55.079  1 62.63  ? 254 LYS   A C    1 1 
ATOM   1945 O  O    . LYS   A 1 255 ? 30.152 23.547 55.251  1 62.69  ? 254 LYS   A O    1 1 
ATOM   1946 C  CB   . LYS   A 1 255 ? 30.74  20.574 54.296  1 63.99  ? 254 LYS   A CB   1 1 
ATOM   1947 C  CG   . LYS   A 1 255 ? 30.264 19.561 55.326  1 67.8   ? 254 LYS   A CG   1 1 
ATOM   1948 C  CD   . LYS   A 1 255 ? 30.869 18.185 55.115  1 72.26  ? 254 LYS   A CD   1 1 
ATOM   1949 C  CE   . LYS   A 1 255 ? 30.163 17.127 55.929  1 76.5   ? 254 LYS   A CE   1 1 
ATOM   1950 N  NZ   . LYS   A 1 255 ? 30.29  17.377 57.397  1 79.64  ? 254 LYS   A NZ   1 1 
ATOM   1951 N  N    . LYS   A 1 256 ? 28.342 22.35  55.837  1 62.46  ? 255 LYS   A N    1 1 
ATOM   1952 C  CA   . LYS   A 1 256 ? 27.945 23.216 56.938  1 62.82  ? 255 LYS   A CA   1 1 
ATOM   1953 C  C    . LYS   A 1 256 ? 28.911 23.186 58.108  1 62.98  ? 255 LYS   A C    1 1 
ATOM   1954 O  O    . LYS   A 1 256 ? 29.138 24.227 58.724  1 63.25  ? 255 LYS   A O    1 1 
ATOM   1955 C  CB   . LYS   A 1 256 ? 26.559 22.816 57.439  1 64.79  ? 255 LYS   A CB   1 1 
ATOM   1956 C  CG   . LYS   A 1 256 ? 25.518 22.721 56.343  1 68.58  ? 255 LYS   A CG   1 1 
ATOM   1957 C  CD   . LYS   A 1 256 ? 25.093 24.088 55.89   1 73.01  ? 255 LYS   A CD   1 1 
ATOM   1958 C  CE   . LYS   A 1 256 ? 23.843 23.951 55.1    1 77.42  ? 255 LYS   A CE   1 1 
ATOM   1959 N  NZ   . LYS   A 1 256 ? 22.771 23.333 55.943  1 79.7   ? 255 LYS   A NZ   1 1 
ATOM   1960 N  N    . MET   A 1 257 ? 29.438 21.998 58.462  1 62.67  ? 256 MET   A N    1 1 
ATOM   1961 C  CA   . MET   A 1 257 ? 30.345 21.87  59.606  1 62.56  ? 256 MET   A CA   1 1 
ATOM   1962 C  C    . MET   A 1 257 ? 31.655 21.216 59.229  1 63.33  ? 256 MET   A C    1 1 
ATOM   1963 O  O    . MET   A 1 257 ? 31.71  20.006 59.026  1 63.7   ? 256 MET   A O    1 1 
ATOM   1964 C  CB   . MET   A 1 257 ? 29.689 21.093 60.75   1 61.84  ? 256 MET   A CB   1 1 
ATOM   1965 C  CG   . MET   A 1 257 ? 30.322 21.376 62.068  1 61.79  ? 256 MET   A CG   1 1 
ATOM   1966 S  SD   . MET   A 1 257 ? 29.973 23.059 62.626  1 59.75  ? 256 MET   A SD   1 1 
ATOM   1967 C  CE   . MET   A 1 257 ? 28.309 22.855 63.212  1 56.33  ? 256 MET   A CE   1 1 
ATOM   1968 N  N    . ILE   A 1 258 ? 32.716 22.009 59.163  1 63.46  ? 257 ILE   A N    1 1 
ATOM   1969 C  CA   . ILE   A 1 258 ? 34.038 21.519 58.807  1 64.23  ? 257 ILE   A CA   1 1 
ATOM   1970 C  C    . ILE   A 1 258 ? 34.865 21.198 60.065  1 64.87  ? 257 ILE   A C    1 1 
ATOM   1971 O  O    . ILE   A 1 258 ? 35.627 22.034 60.541  1 64.72  ? 257 ILE   A O    1 1 
ATOM   1972 C  CB   . ILE   A 1 258 ? 34.783 22.491 57.845  1 64.82  ? 257 ILE   A CB   1 1 
ATOM   1973 C  CG1  . ILE   A 1 258 ? 33.86  23.034 56.736  1 65.75  ? 257 ILE   A CG1  1 1 
ATOM   1974 C  CG2  . ILE   A 1 258 ? 36.017 21.822 57.233  1 65.34  ? 257 ILE   A CG2  1 1 
ATOM   1975 C  CD1  . ILE   A 1 258 ? 34.463 24.153 55.94   1 66.91  ? 257 ILE   A CD1  1 1 
ATOM   1976 N  N    . PHE   A 1 259 ? 34.722 19.98  60.591  1 65.33  ? 258 PHE   A N    1 1 
ATOM   1977 C  CA   . PHE   A 1 259 ? 35.473 19.536 61.76   1 66.3   ? 258 PHE   A CA   1 1 
ATOM   1978 C  C    . PHE   A 1 259 ? 36.881 19.153 61.348  1 67.01  ? 258 PHE   A C    1 1 
ATOM   1979 O  O    . PHE   A 1 259 ? 37.04  18.402 60.389  1 66.98  ? 258 PHE   A O    1 1 
ATOM   1980 C  CB   . PHE   A 1 259 ? 34.804 18.312 62.378  1 66.48  ? 258 PHE   A CB   1 1 
ATOM   1981 C  CG   . PHE   A 1 259 ? 33.627 18.653 63.245  1 67.55  ? 258 PHE   A CG   1 1 
ATOM   1982 C  CD1  . PHE   A 1 259 ? 33.725 19.627 64.22   1 68.46  ? 258 PHE   A CD1  1 1 
ATOM   1983 C  CD2  . PHE   A 1 259 ? 32.424 17.985 63.097  1 68.71  ? 258 PHE   A CD2  1 1 
ATOM   1984 C  CE1  . PHE   A 1 259 ? 32.639 19.934 65.025  1 69.46  ? 258 PHE   A CE1  1 1 
ATOM   1985 C  CE2  . PHE   A 1 259 ? 31.338 18.289 63.907  1 69.63  ? 258 PHE   A CE2  1 1 
ATOM   1986 C  CZ   . PHE   A 1 259 ? 31.452 19.261 64.865  1 69.47  ? 258 PHE   A CZ   1 1 
ATOM   1987 N  N    . VAL   A 1 260 ? 37.903 19.637 62.066  1 67.58  ? 259 VAL   A N    1 1 
ATOM   1988 C  CA   . VAL   A 1 260 ? 39.285 19.298 61.732  1 68.76  ? 259 VAL   A CA   1 1 
ATOM   1989 C  C    . VAL   A 1 260 ? 40.019 18.701 62.936  1 70.36  ? 259 VAL   A C    1 1 
ATOM   1990 O  O    . VAL   A 1 260 ? 40.286 19.445 63.876  1 70.6   ? 259 VAL   A O    1 1 
ATOM   1991 C  CB   . VAL   A 1 260 ? 40.056 20.521 61.181  1 69.36  ? 259 VAL   A CB   1 1 
ATOM   1992 C  CG1  . VAL   A 1 260 ? 41.416 20.099 60.647  1 69.97  ? 259 VAL   A CG1  1 1 
ATOM   1993 C  CG2  . VAL   A 1 260 ? 39.266 21.251 60.1    1 69.67  ? 259 VAL   A CG2  1 1 
ATOM   1994 N  N    . PRO   A 1 261 ? 40.469 17.419 62.917  1 71.4   ? 260 PRO   A N    1 1 
ATOM   1995 C  CA   . PRO   A 1 261 ? 40.266 16.384 61.895  1 72.29  ? 260 PRO   A CA   1 1 
ATOM   1996 C  C    . PRO   A 1 261 ? 38.938 15.695 62.142  1 73.74  ? 260 PRO   A C    1 1 
ATOM   1997 O  O    . PRO   A 1 261 ? 38.686 15.242 63.258  1 73.48  ? 260 PRO   A O    1 1 
ATOM   1998 C  CB   . PRO   A 1 261 ? 41.447 15.422 62.121  1 72.68  ? 260 PRO   A CB   1 1 
ATOM   1999 C  CG   . PRO   A 1 261 ? 42.124 15.857 63.416  1 72.96  ? 260 PRO   A CG   1 1 
ATOM   2000 C  CD   . PRO   A 1 261 ? 41.212 16.864 64.06   1 71.22  ? 260 PRO   A CD   1 1 
ATOM   2001 N  N    . SER   A 1 262 ? 38.104 15.641 61.079  1 75.02  ? 261 SER   A N    1 1 
ATOM   2002 C  CA   . SER   A 1 262 ? 36.722 15.164 60.954  1 76.54  ? 261 SER   A CA   1 1 
ATOM   2003 C  C    . SER   A 1 262 ? 36.209 14.216 62.036  1 78.32  ? 261 SER   A C    1 1 
ATOM   2004 O  O    . SER   A 1 262 ? 35.05  14.36  62.428  1 78.53  ? 261 SER   A O    1 1 
ATOM   2005 C  CB   . SER   A 1 262 ? 36.499 14.53  59.589  1 77.43  ? 261 SER   A CB   1 1 
ATOM   2006 O  OG   . SER   A 1 262 ? 36.826 15.469 58.58   1 79.52  ? 261 SER   A OG   1 1 
ATOM   2007 N  N    . TYR   A 1 263 ? 37.035 13.258 62.519  1 79.35  ? 262 TYR   A N    1 1 
ATOM   2008 C  CA   . TYR   A 1 263 ? 36.599 12.303 63.53   1 80.78  ? 262 TYR   A CA   1 1 
ATOM   2009 C  C    . TYR   A 1 263 ? 36.088 12.934 64.811  1 81.52  ? 262 TYR   A C    1 1 
ATOM   2010 O  O    . TYR   A 1 263 ? 35.379 12.264 65.558  1 81.69  ? 262 TYR   A O    1 1 
ATOM   2011 C  CB   . TYR   A 1 263 ? 37.677 11.259 63.838  1 81.38  ? 262 TYR   A CB   1 1 
ATOM   2012 C  CG   . TYR   A 1 263 ? 39.027 11.812 64.239  1 82.89  ? 262 TYR   A CG   1 1 
ATOM   2013 C  CD1  . TYR   A 1 263 ? 39.218 12.402 65.481  1 84.12  ? 262 TYR   A CD1  1 1 
ATOM   2014 C  CD2  . TYR   A 1 263 ? 40.141 11.616 63.439  1 84.12  ? 262 TYR   A CD2  1 1 
ATOM   2015 C  CE1  . TYR   A 1 263 ? 40.461 12.879 65.871  1 85.22  ? 262 TYR   A CE1  1 1 
ATOM   2016 C  CE2  . TYR   A 1 263 ? 41.398 12.061 63.831  1 85.25  ? 262 TYR   A CE2  1 1 
ATOM   2017 C  CZ   . TYR   A 1 263 ? 41.557 12.682 65.056  1 86.27  ? 262 TYR   A CZ   1 1 
ATOM   2018 O  OH   . TYR   A 1 263 ? 42.796 13.116 65.462  1 87.86  ? 262 TYR   A OH   1 1 
ATOM   2019 N  N    . ILE   A 1 264 ? 36.435 14.201 65.078  1 81.85  ? 263 ILE   A N    1 1 
ATOM   2020 C  CA   . ILE   A 1 264 ? 35.977 14.89  66.286  1 82.64  ? 263 ILE   A CA   1 1 
ATOM   2021 C  C    . ILE   A 1 264 ? 34.42  15.013 66.35   1 83.35  ? 263 ILE   A C    1 1 
ATOM   2022 O  O    . ILE   A 1 264 ? 33.885 15.472 67.35   1 83.36  ? 263 ILE   A O    1 1 
ATOM   2023 C  CB   . ILE   A 1 264 ? 36.705 16.25  66.47   1 83.19  ? 263 ILE   A CB   1 1 
ATOM   2024 C  CG1  . ILE   A 1 264 ? 36.72  17.064 65.172  1 84.18  ? 263 ILE   A CG1  1 1 
ATOM   2025 C  CG2  . ILE   A 1 264 ? 38.14  16.082 67.012  1 83.69  ? 263 ILE   A CG2  1 1 
ATOM   2026 C  CD1  . ILE   A 1 264 ? 37.062 18.417 65.329  1 85.43  ? 263 ILE   A CD1  1 1 
ATOM   2027 N  N    . ASN   A 1 265 ? 33.713 14.589 65.293  1 83.92  ? 264 ASN   A N    1 1 
ATOM   2028 C  CA   . ASN   A 1 265 ? 32.264 14.57  65.236  1 85.15  ? 264 ASN   A CA   1 1 
ATOM   2029 C  C    . ASN   A 1 265 ? 31.768 13.39  66.062  1 86.21  ? 264 ASN   A C    1 1 
ATOM   2030 O  O    . ASN   A 1 265 ? 30.804 13.546 66.805  1 86.55  ? 264 ASN   A O    1 1 
ATOM   2031 C  CB   . ASN   A 1 265 ? 31.8   14.429 63.788  1 86.65  ? 264 ASN   A CB   1 1 
ATOM   2032 C  CG   . ASN   A 1 265 ? 30.305 14.316 63.624  1 90.29  ? 264 ASN   A CG   1 1 
ATOM   2033 O  OD1  . ASN   A 1 265 ? 29.523 14.76  64.478  1 91.61  ? 264 ASN   A OD1  1 1 
ATOM   2034 N  ND2  . ASN   A 1 265 ? 29.878 13.718 62.517  1 91.04  ? 264 ASN   A ND2  1 1 
ATOM   2035 N  N    . ILE   A 1 266 ? 32.405 12.209 65.932  1 86.67  ? 265 ILE   A N    1 1 
ATOM   2036 C  CA   . ILE   A 1 266 ? 31.991 11.04  66.706  1 87.61  ? 265 ILE   A CA   1 1 
ATOM   2037 C  C    . ILE   A 1 266 ? 32.27  11.222 68.195  1 88.71  ? 265 ILE   A C    1 1 
ATOM   2038 O  O    . ILE   A 1 266 ? 31.523 10.688 69.005  1 89.01  ? 265 ILE   A O    1 1 
ATOM   2039 C  CB   . ILE   A 1 266 ? 32.544 9.705  66.162  1 88     ? 265 ILE   A CB   1 1 
ATOM   2040 C  CG1  . ILE   A 1 266 ? 34.032 9.496  66.501  1 88.84  ? 265 ILE   A CG1  1 1 
ATOM   2041 C  CG2  . ILE   A 1 266 ? 32.271 9.584  64.678  1 88.44  ? 265 ILE   A CG2  1 1 
ATOM   2042 C  CD1  . ILE   A 1 266 ? 34.298 8.388  67.477  1 90.09  ? 265 ILE   A CD1  1 1 
ATOM   2043 N  N    . PHE   A 1 267 ? 33.302 12.002 68.56   1 89.12  ? 266 PHE   A N    1 1 
ATOM   2044 C  CA   . PHE   A 1 267 ? 33.61  12.279 69.959  1 89.89  ? 266 PHE   A CA   1 1 
ATOM   2045 C  C    . PHE   A 1 267 ? 32.521 13.118 70.604  1 90.66  ? 266 PHE   A C    1 1 
ATOM   2046 O  O    . PHE   A 1 267 ? 32.2   12.904 71.766  1 90.81  ? 266 PHE   A O    1 1 
ATOM   2047 C  CB   . PHE   A 1 267 ? 34.965 12.97  70.091  1 89.86  ? 266 PHE   A CB   1 1 
ATOM   2048 C  CG   . PHE   A 1 267 ? 36.115 12.021 69.904  1 90.77  ? 266 PHE   A CG   1 1 
ATOM   2049 C  CD1  . PHE   A 1 267 ? 36.09  10.758 70.47   1 91.68  ? 266 PHE   A CD1  1 1 
ATOM   2050 C  CD2  . PHE   A 1 267 ? 37.227 12.392 69.174  1 91.79  ? 266 PHE   A CD2  1 1 
ATOM   2051 C  CE1  . PHE   A 1 267 ? 37.15  9.882  70.3    1 92.52  ? 266 PHE   A CE1  1 1 
ATOM   2052 C  CE2  . PHE   A 1 267 ? 38.286 11.512 69.005  1 92.64  ? 266 PHE   A CE2  1 1 
ATOM   2053 C  CZ   . PHE   A 1 267 ? 38.245 10.267 69.58   1 92.44  ? 266 PHE   A CZ   1 1 
ATOM   2054 N  N    . LEU   A 1 268 ? 31.938 14.055 69.851  1 91.2   ? 267 LEU   A N    1 1 
ATOM   2055 C  CA   . LEU   A 1 268 ? 30.846 14.881 70.349  1 92.51  ? 267 LEU   A CA   1 1 
ATOM   2056 C  C    . LEU   A 1 268 ? 29.549 14.086 70.513  1 93.91  ? 267 LEU   A C    1 1 
ATOM   2057 O  O    . LEU   A 1 268 ? 28.725 14.432 71.357  1 93.95  ? 267 LEU   A O    1 1 
ATOM   2058 C  CB   . LEU   A 1 268 ? 30.629 16.071 69.427  1 92.85  ? 267 LEU   A CB   1 1 
ATOM   2059 C  CG   . LEU   A 1 268 ? 31.771 17.064 69.421  1 94.58  ? 267 LEU   A CG   1 1 
ATOM   2060 C  CD1  . LEU   A 1 268 ? 31.622 18.039 68.29   1 95.27  ? 267 LEU   A CD1  1 1 
ATOM   2061 C  CD2  . LEU   A 1 268 ? 31.893 17.778 70.763  1 95.2   ? 267 LEU   A CD2  1 1 
ATOM   2062 N  N    . ILE   A 1 269 ? 29.371 13.023 69.718  1 95.07  ? 268 ILE   A N    1 1 
ATOM   2063 C  CA   . ILE   A 1 269 ? 28.218 12.137 69.795  1 96.91  ? 268 ILE   A CA   1 1 
ATOM   2064 C  C    . ILE   A 1 269 ? 28.261 11.4   71.137  1 99.07  ? 268 ILE   A C    1 1 
ATOM   2065 O  O    . ILE   A 1 269 ? 27.279 11.414 71.876  1 99.27  ? 268 ILE   A O    1 1 
ATOM   2066 C  CB   . ILE   A 1 269 ? 28.234 11.168 68.587  1 97.32  ? 268 ILE   A CB   1 1 
ATOM   2067 C  CG1  . ILE   A 1 269 ? 27.91  11.92  67.285  1 98.2   ? 268 ILE   A CG1  1 1 
ATOM   2068 C  CG2  . ILE   A 1 269 ? 27.288 9.988  68.798  1 97.78  ? 268 ILE   A CG2  1 1 
ATOM   2069 C  CD1  . ILE   A 1 269 ? 28.182 11.145 66.033  1 99.38  ? 268 ILE   A CD1  1 1 
ATOM   2070 N  N    . LEU   A 1 270 ? 29.431 10.838 71.486  1 100.48 ? 269 LEU   A N    1 1 
ATOM   2071 C  CA   . LEU   A 1 270 ? 29.654 10.109 72.74   1 102.34 ? 269 LEU   A CA   1 1 
ATOM   2072 C  C    . LEU   A 1 270 ? 29.491 10.987 73.991  1 104.33 ? 269 LEU   A C    1 1 
ATOM   2073 O  O    . LEU   A 1 270 ? 29.251 10.463 75.074  1 104.35 ? 269 LEU   A O    1 1 
ATOM   2074 C  CB   . LEU   A 1 270 ? 31.038 9.438  72.75   1 102.59 ? 269 LEU   A CB   1 1 
ATOM   2075 C  CG   . LEU   A 1 270 ? 31.446 8.681  71.488  1 104.12 ? 269 LEU   A CG   1 1 
ATOM   2076 C  CD1  . LEU   A 1 270 ? 32.861 8.159  71.602  1 104.82 ? 269 LEU   A CD1  1 1 
ATOM   2077 C  CD2  . LEU   A 1 270 ? 30.464 7.571  71.152  1 104.72 ? 269 LEU   A CD2  1 1 
ATOM   2078 N  N    . ASP   A 1 271 ? 29.632 12.312 73.845  1 105.92 ? 270 ASP   A N    1 1 
ATOM   2079 C  CA   . ASP   A 1 271 ? 29.448 13.263 74.943  1 107.96 ? 270 ASP   A CA   1 1 
ATOM   2080 C  C    . ASP   A 1 271 ? 27.982 13.292 75.396  1 109.36 ? 270 ASP   A C    1 1 
ATOM   2081 O  O    . ASP   A 1 271 ? 27.717 13.504 76.58   1 109.44 ? 270 ASP   A O    1 1 
ATOM   2082 C  CB   . ASP   A 1 271 ? 29.899 14.681 74.532  1 110.31 ? 270 ASP   A CB   1 1 
ATOM   2083 C  CG   . ASP   A 1 271 ? 31.392 14.941 74.673  1 115.55 ? 270 ASP   A CG   1 1 
ATOM   2084 O  OD1  . ASP   A 1 271 ? 32.079 14.128 75.339  1 116.6  ? 270 ASP   A OD1  1 1 
ATOM   2085 O  OD2  . ASP   A 1 271 ? 31.872 15.965 74.124  1 117.61 ? 270 ASP   A OD2  1 1 
ATOM   2086 N  N    . LYS   A 1 272 ? 27.03  13.059 74.469  1 110.25 ? 271 LYS   A N    1 1 
ATOM   2087 C  CA   . LYS   A 1 272 ? 25.613 13.038 74.82   1 111.56 ? 271 LYS   A CA   1 1 
ATOM   2088 C  C    . LYS   A 1 272 ? 25.136 11.64  75.246  1 112.63 ? 271 LYS   A C    1 1 
ATOM   2089 O  O    . LYS   A 1 272 ? 24.037 11.228 74.877  1 112.73 ? 271 LYS   A O    1 1 
ATOM   2090 C  CB   . LYS   A 1 272 ? 24.743 13.615 73.697  1 113.44 ? 271 LYS   A CB   1 1 
ATOM   2091 C  CG   . LYS   A 1 272 ? 24.642 15.132 73.746  1 117.58 ? 271 LYS   A CG   1 1 
ATOM   2092 C  CD   . LYS   A 1 272 ? 23.495 15.629 72.878  1 122    ? 271 LYS   A CD   1 1 
ATOM   2093 C  CE   . LYS   A 1 272 ? 23.285 17.121 72.993  1 125.64 ? 271 LYS   A CE   1 1 
ATOM   2094 N  NZ   . LYS   A 1 272 ? 22.759 17.499 74.329  1 127.77 ? 271 LYS   A NZ   1 1 
ATOM   2095 N  N    . PHE   A 1 273 ? 25.964 10.933 76.051  1 113.16 ? 272 PHE   A N    1 1 
ATOM   2096 C  CA   . PHE   A 1 273 ? 25.709 9.601  76.62   1 114.03 ? 272 PHE   A CA   1 1 
ATOM   2097 C  C    . PHE   A 1 273 ? 26.416 9.499  77.992  1 114.44 ? 272 PHE   A C    1 1 
ATOM   2098 O  O    . PHE   A 1 273 ? 27.571 9.075  78.041  1 114.62 ? 272 PHE   A O    1 1 
ATOM   2099 C  CB   . PHE   A 1 273 ? 26.26  8.491  75.7    1 114.2  ? 272 PHE   A CB   1 1 
ATOM   2100 C  CG   . PHE   A 1 273 ? 25.514 8.261  74.411  1 115.15 ? 272 PHE   A CG   1 1 
ATOM   2101 C  CD1  . PHE   A 1 273 ? 24.401 7.443  74.373  1 116.14 ? 272 PHE   A CD1  1 1 
ATOM   2102 C  CD2  . PHE   A 1 273 ? 25.934 8.853  73.234  1 116.03 ? 272 PHE   A CD2  1 1 
ATOM   2103 C  CE1  . PHE   A 1 273 ? 23.718 7.229  73.18   1 116.96 ? 272 PHE   A CE1  1 1 
ATOM   2104 C  CE2  . PHE   A 1 273 ? 25.248 8.644  72.045  1 116.83 ? 272 PHE   A CE2  1 1 
ATOM   2105 C  CZ   . PHE   A 1 273 ? 24.147 7.831  72.023  1 116.71 ? 272 PHE   A CZ   1 1 
ATOM   2106 N  N    . LEU   A 1 274 ? 25.752 9.89   79.098  1 114.43 ? 273 LEU   A N    1 1 
ATOM   2107 C  CA   . LEU   A 1 274 ? 26.392 9.834  80.421  1 114.91 ? 273 LEU   A CA   1 1 
ATOM   2108 C  C    . LEU   A 1 274 ? 25.74  8.843  81.393  1 115.02 ? 273 LEU   A C    1 1 
ATOM   2109 O  O    . LEU   A 1 274 ? 26.44  8.148  82.134  1 114.93 ? 273 LEU   A O    1 1 
ATOM   2110 C  CB   . LEU   A 1 274 ? 26.482 11.232 81.048  1 115.32 ? 273 LEU   A CB   1 1 
ATOM   2111 C  CG   . LEU   A 1 274 ? 27.88  11.854 81.08   1 117.05 ? 273 LEU   A CG   1 1 
ATOM   2112 C  CD1  . LEU   A 1 274 ? 28.414 12.092 79.678  1 117.53 ? 273 LEU   A CD1  1 1 
ATOM   2113 C  CD2  . LEU   A 1 274 ? 27.887 13.149 81.878  1 117.85 ? 273 LEU   A CD2  1 1 
ATOM   2114 N  N    . VAL   B 1 26  ? 14.357 6.507  87.56   1 126.19 ? 25  VAL   B N    1 2 
ATOM   2115 C  CA   . VAL   B 1 26  ? 13.057 6.132  88.102  1 126.88 ? 25  VAL   B CA   1 2 
ATOM   2116 C  C    . VAL   B 1 26  ? 13.18  5.123  89.265  1 127.69 ? 25  VAL   B C    1 2 
ATOM   2117 O  O    . VAL   B 1 26  ? 12.635 5.374  90.343  1 128.04 ? 25  VAL   B O    1 2 
ATOM   2118 C  CB   . VAL   B 1 26  ? 12.104 5.648  86.987  1 127.44 ? 25  VAL   B CB   1 2 
ATOM   2119 C  CG1  . VAL   B 1 26  ? 10.807 5.097  87.561  1 128.01 ? 25  VAL   B CG1  1 2 
ATOM   2120 C  CG2  . VAL   B 1 26  ? 11.828 6.758  85.981  1 127.82 ? 25  VAL   B CG2  1 2 
ATOM   2121 N  N    . PHE   B 1 27  ? 13.916 4.004  89.059  1 127.77 ? 26  PHE   B N    1 2 
ATOM   2122 C  CA   . PHE   B 1 27  ? 14.138 2.944  90.064  1 128.18 ? 26  PHE   B CA   1 2 
ATOM   2123 C  C    . PHE   B 1 27  ? 14.859 3.494  91.327  1 128.39 ? 26  PHE   B C    1 2 
ATOM   2124 O  O    . PHE   B 1 27  ? 14.304 3.447  92.423  1 128.51 ? 26  PHE   B O    1 2 
ATOM   2125 C  CB   . PHE   B 1 27  ? 14.904 1.756  89.428  1 128.09 ? 26  PHE   B CB   1 2 
ATOM   2126 C  CG   . PHE   B 1 27  ? 14.682 0.393  90.046  1 128.72 ? 26  PHE   B CG   1 2 
ATOM   2127 C  CD1  . PHE   B 1 27  ? 13.43  -0.196 90.031  1 129.5  ? 26  PHE   B CD1  1 2 
ATOM   2128 C  CD2  . PHE   B 1 27  ? 15.741 -0.334 90.559  1 129.5  ? 26  PHE   B CD2  1 2 
ATOM   2129 C  CE1  . PHE   B 1 27  ? 13.234 -1.462 90.571  1 130.17 ? 26  PHE   B CE1  1 2 
ATOM   2130 C  CE2  . PHE   B 1 27  ? 15.54  -1.599 91.102  1 130.2  ? 26  PHE   B CE2  1 2 
ATOM   2131 C  CZ   . PHE   B 1 27  ? 14.29  -2.156 91.102  1 129.98 ? 26  PHE   B CZ   1 2 
ATOM   2132 N  N    . PHE   B 1 28  ? 16.066 4.056  91.159  1 128.19 ? 27  PHE   B N    1 2 
ATOM   2133 C  CA   . PHE   B 1 28  ? 16.824 4.688  92.24   1 128.33 ? 27  PHE   B CA   1 2 
ATOM   2134 C  C    . PHE   B 1 28  ? 17.151 6.111  91.752  1 127.86 ? 27  PHE   B C    1 2 
ATOM   2135 O  O    . PHE   B 1 28  ? 18.213 6.34   91.166  1 128.02 ? 27  PHE   B O    1 2 
ATOM   2136 C  CB   . PHE   B 1 28  ? 18.109 3.896  92.544  1 128.57 ? 27  PHE   B CB   1 2 
ATOM   2137 C  CG   . PHE   B 1 28  ? 17.876 2.588  93.266  1 129.57 ? 27  PHE   B CG   1 2 
ATOM   2138 C  CD1  . PHE   B 1 28  ? 17.385 2.57   94.559  1 130.5  ? 27  PHE   B CD1  1 2 
ATOM   2139 C  CD2  . PHE   B 1 28  ? 18.177 1.379  92.663  1 130.53 ? 27  PHE   B CD2  1 2 
ATOM   2140 C  CE1  . PHE   B 1 28  ? 17.182 1.363  95.228  1 131.24 ? 27  PHE   B CE1  1 2 
ATOM   2141 C  CE2  . PHE   B 1 28  ? 17.977 0.175  93.337  1 131.3  ? 27  PHE   B CE2  1 2 
ATOM   2142 C  CZ   . PHE   B 1 28  ? 17.478 0.175  94.614  1 131.04 ? 27  PHE   B CZ   1 2 
ATOM   2143 N  N    . PRO   B 1 29  ? 16.201 7.059  91.91   1 127.08 ? 28  PRO   B N    1 2 
ATOM   2144 C  CA   . PRO   B 1 29  ? 16.399 8.405  91.345  1 126.6  ? 28  PRO   B CA   1 2 
ATOM   2145 C  C    . PRO   B 1 29  ? 17.169 9.401  92.187  1 125.7  ? 28  PRO   B C    1 2 
ATOM   2146 O  O    . PRO   B 1 29  ? 17.128 9.349  93.411  1 125.82 ? 28  PRO   B O    1 2 
ATOM   2147 C  CB   . PRO   B 1 29  ? 14.971 8.893  91.075  1 127.48 ? 28  PRO   B CB   1 2 
ATOM   2148 C  CG   . PRO   B 1 29  ? 14.091 8.067  91.946  1 127.98 ? 28  PRO   B CG   1 2 
ATOM   2149 C  CD   . PRO   B 1 29  ? 14.869 6.924  92.527  1 126.46 ? 28  PRO   B CD   1 2 
ATOM   2150 N  N    . ARG   B 1 30  ? 17.812 10.357 91.484  1 124.6  ? 29  ARG   B N    1 2 
ATOM   2151 C  CA   . ARG   B 1 30  ? 18.691 11.424 91.953  1 124.05 ? 29  ARG   B CA   1 2 
ATOM   2152 C  C    . ARG   B 1 30  ? 18.37  11.987 93.34   1 123.4  ? 29  ARG   B C    1 2 
ATOM   2153 O  O    . ARG   B 1 30  ? 17.206 12.146 93.72   1 123.63 ? 29  ARG   B O    1 2 
ATOM   2154 C  CB   . ARG   B 1 30  ? 18.782 12.567 90.928  1 125.06 ? 29  ARG   B CB   1 2 
ATOM   2155 C  CG   . ARG   B 1 30  ? 20.179 13.163 90.845  1 127.52 ? 29  ARG   B CG   1 2 
ATOM   2156 C  CD   . ARG   B 1 30  ? 20.462 13.812 89.496  1 130.14 ? 29  ARG   B CD   1 2 
ATOM   2157 N  NE   . ARG   B 1 30  ? 21.789 14.429 89.468  1 132.53 ? 29  ARG   B NE   1 2 
ATOM   2158 C  CZ   . ARG   B 1 30  ? 22.394 14.87  88.369  1 134.43 ? 29  ARG   B CZ   1 2 
ATOM   2159 N  NH1  . ARG   B 1 30  ? 21.802 14.759 87.187  1 134.07 ? 29  ARG   B NH1  1 2 
ATOM   2160 N  NH2  . ARG   B 1 30  ? 23.597 15.422 88.445  1 134.31 ? 29  ARG   B NH2  1 2 
ATOM   2161 N  N    . LYS   B 1 31  ? 19.443 12.267 94.102  1 122.3  ? 30  LYS   B N    1 2 
ATOM   2162 C  CA   . LYS   B 1 31  ? 19.366 12.785 95.464  1 121.36 ? 30  LYS   B CA   1 2 
ATOM   2163 C  C    . LYS   B 1 31  ? 18.972 14.27  95.488  1 120.06 ? 30  LYS   B C    1 2 
ATOM   2164 O  O    . LYS   B 1 31  ? 19.704 15.121 94.972  1 120.06 ? 30  LYS   B O    1 2 
ATOM   2165 C  CB   . LYS   B 1 31  ? 20.697 12.544 96.206  1 122.81 ? 30  LYS   B CB   1 2 
ATOM   2166 C  CG   . LYS   B 1 31  ? 20.534 12.19  97.679  1 126.03 ? 30  LYS   B CG   1 2 
ATOM   2167 C  CD   . LYS   B 1 31  ? 21.882 12.018 98.394  1 129.3  ? 30  LYS   B CD   1 2 
ATOM   2168 C  CE   . LYS   B 1 31  ? 21.715 11.89  99.892  1 131.69 ? 30  LYS   B CE   1 2 
ATOM   2169 N  NZ   . LYS   B 1 31  ? 23.025 11.776 100.586 1 132.98 ? 30  LYS   B NZ   1 2 
ATOM   2170 N  N    . ARG   B 1 32  ? 17.809 14.573 96.091  1 118.63 ? 31  ARG   B N    1 2 
ATOM   2171 C  CA   . ARG   B 1 32  ? 17.309 15.938 96.243  1 117.55 ? 31  ARG   B CA   1 2 
ATOM   2172 C  C    . ARG   B 1 32  ? 17.941 16.584 97.478  1 115.78 ? 31  ARG   B C    1 2 
ATOM   2173 O  O    . ARG   B 1 32  ? 17.882 16.019 98.573  1 115.98 ? 31  ARG   B O    1 2 
ATOM   2174 C  CB   . ARG   B 1 32  ? 15.782 15.937 96.401  1 119.07 ? 31  ARG   B CB   1 2 
ATOM   2175 C  CG   . ARG   B 1 32  ? 15.01  15.984 95.09   1 122.04 ? 31  ARG   B CG   1 2 
ATOM   2176 C  CD   . ARG   B 1 32  ? 14.317 17.326 94.875  1 124.79 ? 31  ARG   B CD   1 2 
ATOM   2177 N  NE   . ARG   B 1 32  ? 13.416 17.686 95.976  1 127.02 ? 31  ARG   B NE   1 2 
ATOM   2178 C  CZ   . ARG   B 1 32  ? 12.312 18.417 95.838  1 128.47 ? 31  ARG   B CZ   1 2 
ATOM   2179 N  NH1  . ARG   B 1 32  ? 11.953 18.869 94.645  1 127.87 ? 31  ARG   B NH1  1 2 
ATOM   2180 N  NH2  . ARG   B 1 32  ? 11.562 18.701 96.893  1 128.2  ? 31  ARG   B NH2  1 2 
ATOM   2181 N  N    . LYS   B 1 33  ? 18.539 17.763 97.308  1 113.89 ? 32  LYS   B N    1 2 
ATOM   2182 C  CA   . LYS   B 1 33  ? 19.177 18.472 98.413  1 112.6  ? 32  LYS   B CA   1 2 
ATOM   2183 C  C    . LYS   B 1 33  ? 18.261 19.581 98.985  1 110.78 ? 32  LYS   B C    1 2 
ATOM   2184 O  O    . LYS   B 1 33  ? 17.149 19.777 98.497  1 110.68 ? 32  LYS   B O    1 2 
ATOM   2185 C  CB   . LYS   B 1 33  ? 20.547 19.03  97.956  1 114.28 ? 32  LYS   B CB   1 2 
ATOM   2186 C  CG   . LYS   B 1 33  ? 20.453 20.263 97.068  1 117.75 ? 32  LYS   B CG   1 2 
ATOM   2187 C  CD   . LYS   B 1 33  ? 21.822 20.827 96.726  1 122.09 ? 32  LYS   B CD   1 2 
ATOM   2188 C  CE   . LYS   B 1 33  ? 21.713 22.095 95.913  1 126.14 ? 32  LYS   B CE   1 2 
ATOM   2189 N  NZ   . LYS   B 1 33  ? 23.037 22.527 95.387  1 128.59 ? 32  LYS   B NZ   1 2 
ATOM   2190 N  N    . SER   B 1 34  ? 18.711 20.281 100.038 1 109.13 ? 33  SER   B N    1 2 
ATOM   2191 C  CA   . SER   B 1 34  ? 17.944 21.374 100.621 1 107.9  ? 33  SER   B CA   1 2 
ATOM   2192 C  C    . SER   B 1 34  ? 18.633 22.709 100.324 1 106.66 ? 33  SER   B C    1 2 
ATOM   2193 O  O    . SER   B 1 34  ? 19.855 22.819 100.432 1 106.88 ? 33  SER   B O    1 2 
ATOM   2194 C  CB   . SER   B 1 34  ? 17.797 21.19  102.129 1 108.48 ? 33  SER   B CB   1 2 
ATOM   2195 O  OG   . SER   B 1 34  ? 17.107 22.281 102.72  1 109.77 ? 33  SER   B OG   1 2 
ATOM   2196 N  N    . VAL   B 1 35  ? 17.856 23.715 99.931  1 105.09 ? 34  VAL   B N    1 2 
ATOM   2197 C  CA   . VAL   B 1 35  ? 18.393 25.052 99.69   1 104.02 ? 34  VAL   B CA   1 2 
ATOM   2198 C  C    . VAL   B 1 35  ? 17.859 26.05  100.742 1 102.28 ? 34  VAL   B C    1 2 
ATOM   2199 O  O    . VAL   B 1 35  ? 17.734 27.239 100.46  1 102.26 ? 34  VAL   B O    1 2 
ATOM   2200 C  CB   . VAL   B 1 35  ? 18.119 25.521 98.246  1 105.17 ? 34  VAL   B CB   1 2 
ATOM   2201 C  CG1  . VAL   B 1 35  ? 18.996 24.765 97.252  1 105.91 ? 34  VAL   B CG1  1 2 
ATOM   2202 C  CG2  . VAL   B 1 35  ? 16.646 25.369 97.892  1 105.78 ? 34  VAL   B CG2  1 2 
ATOM   2203 N  N    . ALA   B 1 36  ? 17.562 25.558 101.962 1 100.67 ? 35  ALA   B N    1 2 
ATOM   2204 C  CA   . ALA   B 1 36  ? 17.031 26.363 103.048 1 99.51  ? 35  ALA   B CA   1 2 
ATOM   2205 C  C    . ALA   B 1 36  ? 18.13  27.17  103.722 1 98.27  ? 35  ALA   B C    1 2 
ATOM   2206 O  O    . ALA   B 1 36  ? 19.165 26.619 104.099 1 98.18  ? 35  ALA   B O    1 2 
ATOM   2207 C  CB   . ALA   B 1 36  ? 16.339 25.469 104.058 1 99.47  ? 35  ALA   B CB   1 2 
ATOM   2208 N  N    . GLY   B 1 37  ? 17.898 28.473 103.848 1 97.09  ? 36  GLY   B N    1 2 
ATOM   2209 C  CA   . GLY   B 1 37  ? 18.84  29.401 104.46  1 96.31  ? 36  GLY   B CA   1 2 
ATOM   2210 C  C    . GLY   B 1 37  ? 19.985 29.836 103.558 1 95.1   ? 36  GLY   B C    1 2 
ATOM   2211 O  O    . GLY   B 1 37  ? 20.953 30.427 104.041 1 95.73  ? 36  GLY   B O    1 2 
ATOM   2212 N  N    . GLU   B 1 38  ? 19.905 29.551 102.249 1 93     ? 37  GLU   B N    1 2 
ATOM   2213 C  CA   . GLU   B 1 38  ? 20.971 29.921 101.316 1 91.65  ? 37  GLU   B CA   1 2 
ATOM   2214 C  C    . GLU   B 1 38  ? 20.735 31.308 100.74  1 90.04  ? 37  GLU   B C    1 2 
ATOM   2215 O  O    . GLU   B 1 38  ? 19.588 31.75  100.674 1 90.22  ? 37  GLU   B O    1 2 
ATOM   2216 C  CB   . GLU   B 1 38  ? 21.043 28.903 100.17  1 93.68  ? 37  GLU   B CB   1 2 
ATOM   2217 C  CG   . GLU   B 1 38  ? 21.529 27.533 100.602 1 97.83  ? 37  GLU   B CG   1 2 
ATOM   2218 C  CD   . GLU   B 1 38  ? 22.993 27.282 100.297 1 103.61 ? 37  GLU   B CD   1 2 
ATOM   2219 O  OE1  . GLU   B 1 38  ? 23.691 26.691 101.153 1 104.17 ? 37  GLU   B OE1  1 2 
ATOM   2220 O  OE2  . GLU   B 1 38  ? 23.447 27.691 99.203  1 106.4  ? 37  GLU   B OE2  1 2 
ATOM   2221 N  N    . ILE   B 1 39  ? 21.804 31.992 100.294 1 88.25  ? 38  ILE   B N    1 2 
ATOM   2222 C  CA   . ILE   B 1 39  ? 21.647 33.309 99.676  1 86.72  ? 38  ILE   B CA   1 2 
ATOM   2223 C  C    . ILE   B 1 39  ? 21.472 33.138 98.191  1 84.63  ? 38  ILE   B C    1 2 
ATOM   2224 O  O    . ILE   B 1 39  ? 22.439 32.855 97.492  1 84.72  ? 38  ILE   B O    1 2 
ATOM   2225 C  CB   . ILE   B 1 39  ? 22.779 34.301 100.02  1 87.26  ? 38  ILE   B CB   1 2 
ATOM   2226 C  CG1  . ILE   B 1 39  ? 22.883 34.467 101.553 1 88.44  ? 38  ILE   B CG1  1 2 
ATOM   2227 C  CG2  . ILE   B 1 39  ? 22.522 35.641 99.324  1 87.58  ? 38  ILE   B CG2  1 2 
ATOM   2228 C  CD1  . ILE   B 1 39  ? 23.902 35.474 102.044 1 89.99  ? 38  ILE   B CD1  1 2 
ATOM   2229 N  N    . VAL   B 1 40  ? 20.233 33.266 97.709  1 82.78  ? 39  VAL   B N    1 2 
ATOM   2230 C  CA   . VAL   B 1 40  ? 19.938 33.084 96.294  1 81.51  ? 39  VAL   B CA   1 2 
ATOM   2231 C  C    . VAL   B 1 40  ? 19.704 34.402 95.594  1 79.81  ? 39  VAL   B C    1 2 
ATOM   2232 O  O    . VAL   B 1 40  ? 18.714 35.076 95.867  1 80.06  ? 39  VAL   B O    1 2 
ATOM   2233 C  CB   . VAL   B 1 40  ? 18.741 32.136 96.06   1 82.23  ? 39  VAL   B CB   1 2 
ATOM   2234 C  CG1  . VAL   B 1 40  ? 18.565 31.837 94.574  1 82.68  ? 39  VAL   B CG1  1 2 
ATOM   2235 C  CG2  . VAL   B 1 40  ? 18.895 30.848 96.86   1 82.82  ? 39  VAL   B CG2  1 2 
ATOM   2236 N  N    . LEU   B 1 41  ? 20.597 34.76  94.673  1 77.92  ? 40  LEU   B N    1 2 
ATOM   2237 C  CA   . LEU   B 1 41  ? 20.451 35.977 93.882  1 76.51  ? 40  LEU   B CA   1 2 
ATOM   2238 C  C    . LEU   B 1 41  ? 19.789 35.596 92.576  1 75.31  ? 40  LEU   B C    1 2 
ATOM   2239 O  O    . LEU   B 1 41  ? 20.228 34.645 91.946  1 75.22  ? 40  LEU   B O    1 2 
ATOM   2240 C  CB   . LEU   B 1 41  ? 21.815 36.61  93.589  1 76.25  ? 40  LEU   B CB   1 2 
ATOM   2241 C  CG   . LEU   B 1 41  ? 21.772 38.047 93.085  1 77.2   ? 40  LEU   B CG   1 2 
ATOM   2242 C  CD1  . LEU   B 1 41  ? 22.902 38.849 93.652  1 77.33  ? 40  LEU   B CD1  1 2 
ATOM   2243 C  CD2  . LEU   B 1 41  ? 21.844 38.108 91.578  1 77.91  ? 40  LEU   B CD2  1 2 
ATOM   2244 N  N    . ILE   B 1 42  ? 18.734 36.314 92.164  1 74.3   ? 41  ILE   B N    1 2 
ATOM   2245 C  CA   . ILE   B 1 42  ? 18.051 36.021 90.901  1 73.92  ? 41  ILE   B CA   1 2 
ATOM   2246 C  C    . ILE   B 1 42  ? 17.918 37.276 90.024  1 73.06  ? 41  ILE   B C    1 2 
ATOM   2247 O  O    . ILE   B 1 42  ? 17.12  38.154 90.335  1 73.09  ? 41  ILE   B O    1 2 
ATOM   2248 C  CB   . ILE   B 1 42  ? 16.679 35.335 91.13   1 74.52  ? 41  ILE   B CB   1 2 
ATOM   2249 C  CG1  . ILE   B 1 42  ? 16.814 34.102 92.036  1 75.47  ? 41  ILE   B CG1  1 2 
ATOM   2250 C  CG2  . ILE   B 1 42  ? 16.024 34.971 89.795  1 75.09  ? 41  ILE   B CG2  1 2 
ATOM   2251 C  CD1  . ILE   B 1 42  ? 15.575 33.724 92.711  1 76.9   ? 41  ILE   B CD1  1 2 
ATOM   2252 N  N    . THR   B 1 43  ? 18.708 37.371 88.944  1 72.15  ? 42  THR   B N    1 2 
ATOM   2253 C  CA   . THR   B 1 43  ? 18.639 38.525 88.049  1 72.21  ? 42  THR   B CA   1 2 
ATOM   2254 C  C    . THR   B 1 43  ? 17.464 38.362 87.094  1 72.19  ? 42  THR   B C    1 2 
ATOM   2255 O  O    . THR   B 1 43  ? 17.214 37.259 86.624  1 72.6   ? 42  THR   B O    1 2 
ATOM   2256 C  CB   . THR   B 1 43  ? 19.946 38.689 87.266  1 73.59  ? 42  THR   B CB   1 2 
ATOM   2257 O  OG1  . THR   B 1 43  ? 20.151 37.557 86.424  1 75     ? 42  THR   B OG1  1 2 
ATOM   2258 C  CG2  . THR   B 1 43  ? 21.137 38.883 88.157  1 73.86  ? 42  THR   B CG2  1 2 
ATOM   2259 N  N    . GLY   B 1 44  ? 16.787 39.452 86.766  1 71.47  ? 43  GLY   B N    1 2 
ATOM   2260 C  CA   . GLY   B 1 44  ? 15.627 39.396 85.886  1 71.21  ? 43  GLY   B CA   1 2 
ATOM   2261 C  C    . GLY   B 1 44  ? 14.465 38.706 86.572  1 70.66  ? 43  GLY   B C    1 2 
ATOM   2262 O  O    . GLY   B 1 44  ? 13.756 37.9   85.962  1 70.45  ? 43  GLY   B O    1 2 
ATOM   2263 N  N    . ALA   B 1 45  ? 14.281 39.013 87.866  1 70.43  ? 44  ALA   B N    1 2 
ATOM   2264 C  CA   . ALA   B 1 45  ? 13.24  38.402 88.686  1 70.45  ? 44  ALA   B CA   1 2 
ATOM   2265 C  C    . ALA   B 1 45  ? 11.991 39.262 88.887  1 69.96  ? 44  ALA   B C    1 2 
ATOM   2266 O  O    . ALA   B 1 45  ? 11.25  39.053 89.84   1 70.27  ? 44  ALA   B O    1 2 
ATOM   2267 C  CB   . ALA   B 1 45  ? 13.811 37.978 90.032  1 70.85  ? 44  ALA   B CB   1 2 
ATOM   2268 N  N    . GLY   B 1 46  ? 11.756 40.203 87.992  1 69.14  ? 45  GLY   B N    1 2 
ATOM   2269 C  CA   . GLY   B 1 46  ? 10.569 41.048 88.064  1 68.82  ? 45  GLY   B CA   1 2 
ATOM   2270 C  C    . GLY   B 1 46  ? 9.353  40.457 87.366  1 67.98  ? 45  GLY   B C    1 2 
ATOM   2271 O  O    . GLY   B 1 46  ? 8.232  40.93  87.577  1 68.31  ? 45  GLY   B O    1 2 
ATOM   2272 N  N    . HIS   B 1 47  ? 9.559  39.419 86.527  1 66.47  ? 46  HIS   B N    1 2 
ATOM   2273 C  CA   . HIS   B 1 47  ? 8.486  38.781 85.786  1 65.43  ? 46  HIS   B CA   1 2 
ATOM   2274 C  C    . HIS   B 1 47  ? 8.965  37.479 85.147  1 64.45  ? 46  HIS   B C    1 2 
ATOM   2275 O  O    . HIS   B 1 47  ? 10.167 37.247 84.989  1 63.68  ? 46  HIS   B O    1 2 
ATOM   2276 C  CB   . HIS   B 1 47  ? 7.986  39.765 84.707  1 66.28  ? 46  HIS   B CB   1 2 
ATOM   2277 C  CG   . HIS   B 1 47  ? 6.842  39.278 83.868  1 68.28  ? 46  HIS   B CG   1 2 
ATOM   2278 N  ND1  . HIS   B 1 47  ? 5.79   38.565 84.419  1 70.16  ? 46  HIS   B ND1  1 2 
ATOM   2279 C  CD2  . HIS   B 1 47  ? 6.606  39.456 82.546  1 69.03  ? 46  HIS   B CD2  1 2 
ATOM   2280 C  CE1  . HIS   B 1 47  ? 4.967  38.314 83.415  1 70.49  ? 46  HIS   B CE1  1 2 
ATOM   2281 N  NE2  . HIS   B 1 47  ? 5.413  38.835 82.27   1 70.11  ? 46  HIS   B NE2  1 2 
ATOM   2282 N  N    . GLY   B 1 48  ? 7.998  36.633 84.82   1 64.59  ? 47  GLY   B N    1 2 
ATOM   2283 C  CA   . GLY   B 1 48  ? 8.181  35.38  84.105  1 65.16  ? 47  GLY   B CA   1 2 
ATOM   2284 C  C    . GLY   B 1 48  ? 8.977  34.307 84.809  1 65.42  ? 47  GLY   B C    1 2 
ATOM   2285 O  O    . GLY   B 1 48  ? 8.679  33.958 85.955  1 65.7   ? 47  GLY   B O    1 2 
ATOM   2286 N  N    . ILE   B 1 49  ? 9.99   33.762 84.105  1 65     ? 48  ILE   B N    1 2 
ATOM   2287 C  CA   . ILE   B 1 49  ? 10.856 32.702 84.627  1 64.96  ? 48  ILE   B CA   1 2 
ATOM   2288 C  C    . ILE   B 1 49  ? 11.627 33.163 85.869  1 65.1   ? 48  ILE   B C    1 2 
ATOM   2289 O  O    . ILE   B 1 49  ? 11.854 32.362 86.769  1 65.47  ? 48  ILE   B O    1 2 
ATOM   2290 C  CB   . ILE   B 1 49  ? 11.788 32.087 83.538  1 65.1   ? 48  ILE   B CB   1 2 
ATOM   2291 C  CG1  . ILE   B 1 49  ? 11.013 31.795 82.247  1 65.58  ? 48  ILE   B CG1  1 2 
ATOM   2292 C  CG2  . ILE   B 1 49  ? 12.484 30.823 84.059  1 65.64  ? 48  ILE   B CG2  1 2 
ATOM   2293 C  CD1  . ILE   B 1 49  ? 11.839 31.33  81.14   1 66.8   ? 48  ILE   B CD1  1 2 
ATOM   2294 N  N    . GLY   B 1 50  ? 11.968 34.447 85.944  1 64.51  ? 49  GLY   B N    1 2 
ATOM   2295 C  CA   . GLY   B 1 50  ? 12.674 34.979 87.103  1 64.04  ? 49  GLY   B CA   1 2 
ATOM   2296 C  C    . GLY   B 1 50  ? 11.775 35.163 88.302  1 63.07  ? 49  GLY   B C    1 2 
ATOM   2297 O  O    . GLY   B 1 50  ? 12.183 34.883 89.421  1 63.01  ? 49  GLY   B O    1 2 
ATOM   2298 N  N    . ARG   B 1 51  ? 10.552 35.65  88.069  1 62.59  ? 50  ARG   B N    1 2 
ATOM   2299 C  CA   . ARG   B 1 51  ? 9.548  35.907 89.098  1 62.78  ? 50  ARG   B CA   1 2 
ATOM   2300 C  C    . ARG   B 1 51  ? 9.089  34.612 89.724  1 63.38  ? 50  ARG   B C    1 2 
ATOM   2301 O  O    . ARG   B 1 51  ? 8.954  34.539 90.942  1 63.55  ? 50  ARG   B O    1 2 
ATOM   2302 C  CB   . ARG   B 1 51  ? 8.351  36.681 88.497  1 63.41  ? 50  ARG   B CB   1 2 
ATOM   2303 C  CG   . ARG   B 1 51  ? 7.04   36.612 89.278  1 64.41  ? 50  ARG   B CG   1 2 
ATOM   2304 C  CD   . ARG   B 1 51  ? 6.01   37.579 88.752  1 65.82  ? 50  ARG   B CD   1 2 
ATOM   2305 N  NE   . ARG   B 1 51  ? 6.17   38.899 89.361  1 66.85  ? 50  ARG   B NE   1 2 
ATOM   2306 C  CZ   . ARG   B 1 51  ? 5.361  39.933 89.143  1 68.33  ? 50  ARG   B CZ   1 2 
ATOM   2307 N  NH1  . ARG   B 1 51  ? 4.327  39.814 88.321  1 68.75  ? 50  ARG   B NH1  1 2 
ATOM   2308 N  NH2  . ARG   B 1 51  ? 5.588  41.098 89.737  1 67.31  ? 50  ARG   B NH2  1 2 
ATOM   2309 N  N    . TRP   B 1 52  ? 8.838  33.596 88.9    1 63.72  ? 51  TRP   B N    1 2 
ATOM   2310 C  CA   . TRP   B 1 52  ? 8.354  32.314 89.407  1 64.53  ? 51  TRP   B CA   1 2 
ATOM   2311 C  C    . TRP   B 1 52  ? 9.479  31.44  90.001  1 65.04  ? 51  TRP   B C    1 2 
ATOM   2312 O  O    . TRP   B 1 52  ? 9.19   30.526 90.774  1 65.05  ? 51  TRP   B O    1 2 
ATOM   2313 C  CB   . TRP   B 1 52  ? 7.505  31.592 88.353  1 64.52  ? 51  TRP   B CB   1 2 
ATOM   2314 C  CG   . TRP   B 1 52  ? 6.199  32.3   88.164  1 64.91  ? 51  TRP   B CG   1 2 
ATOM   2315 C  CD1  . TRP   B 1 52  ? 6.009  33.526 87.598  1 65.79  ? 51  TRP   B CD1  1 2 
ATOM   2316 C  CD2  . TRP   B 1 52  ? 4.935  31.908 88.702  1 64.96  ? 51  TRP   B CD2  1 2 
ATOM   2317 N  NE1  . TRP   B 1 52  ? 4.694  33.903 87.718  1 66.02  ? 51  TRP   B NE1  1 2 
ATOM   2318 C  CE2  . TRP   B 1 52  ? 4.01   32.921 88.383  1 65.66  ? 51  TRP   B CE2  1 2 
ATOM   2319 C  CE3  . TRP   B 1 52  ? 4.495  30.8   89.426  1 65.55  ? 51  TRP   B CE3  1 2 
ATOM   2320 C  CZ2  . TRP   B 1 52  ? 2.666  32.836 88.725  1 66.26  ? 51  TRP   B CZ2  1 2 
ATOM   2321 C  CZ3  . TRP   B 1 52  ? 3.16   30.714 89.754  1 66.44  ? 51  TRP   B CZ3  1 2 
ATOM   2322 C  CH2  . TRP   B 1 52  ? 2.262  31.722 89.403  1 66.45  ? 51  TRP   B CH2  1 2 
ATOM   2323 N  N    . THR   B 1 53  ? 10.748 31.779 89.733  1 65.34  ? 52  THR   B N    1 2 
ATOM   2324 C  CA   . THR   B 1 53  ? 11.884 31.121 90.363  1 66.1   ? 52  THR   B CA   1 2 
ATOM   2325 C  C    . THR   B 1 53  ? 12.001 31.662 91.796  1 66.86  ? 52  THR   B C    1 2 
ATOM   2326 O  O    . THR   B 1 53  ? 12.148 30.88  92.734  1 67.1   ? 52  THR   B O    1 2 
ATOM   2327 C  CB   . THR   B 1 53  ? 13.122 31.285 89.496  1 67.45  ? 52  THR   B CB   1 2 
ATOM   2328 O  OG1  . THR   B 1 53  ? 13.074 30.279 88.484  1 68.53  ? 52  THR   B OG1  1 2 
ATOM   2329 C  CG2  . THR   B 1 53  ? 14.415 31.177 90.277  1 67.61  ? 52  THR   B CG2  1 2 
ATOM   2330 N  N    . ALA   B 1 54  ? 11.825 32.982 91.982  1 67.09  ? 53  ALA   B N    1 2 
ATOM   2331 C  CA   . ALA   B 1 54  ? 11.806 33.586 93.308  1 67.83  ? 53  ALA   B CA   1 2 
ATOM   2332 C  C    . ALA   B 1 54  ? 10.615 33.058 94.131  1 68.85  ? 53  ALA   B C    1 2 
ATOM   2333 O  O    . ALA   B 1 54  ? 10.724 32.97  95.35   1 69.57  ? 53  ALA   B O    1 2 
ATOM   2334 C  CB   . ALA   B 1 54  ? 11.745 35.099 93.195  1 67.84  ? 53  ALA   B CB   1 2 
ATOM   2335 N  N    . TYR   B 1 55  ? 9.496  32.689 93.485  1 69.07  ? 54  TYR   B N    1 2 
ATOM   2336 C  CA   . TYR   B 1 55  ? 8.36   32.111 94.198  1 70.06  ? 54  TYR   B CA   1 2 
ATOM   2337 C  C    . TYR   B 1 55  ? 8.743  30.705 94.669  1 70.85  ? 54  TYR   B C    1 2 
ATOM   2338 O  O    . TYR   B 1 55  ? 8.417  30.34  95.79   1 70.75  ? 54  TYR   B O    1 2 
ATOM   2339 C  CB   . TYR   B 1 55  ? 7.111  31.996 93.309  1 70.39  ? 54  TYR   B CB   1 2 
ATOM   2340 C  CG   . TYR   B 1 55  ? 6.443  33.288 92.886  1 71.58  ? 54  TYR   B CG   1 2 
ATOM   2341 C  CD1  . TYR   B 1 55  ? 6.696  34.48  93.553  1 72.49  ? 54  TYR   B CD1  1 2 
ATOM   2342 C  CD2  . TYR   B 1 55  ? 5.529  33.308 91.842  1 72.82  ? 54  TYR   B CD2  1 2 
ATOM   2343 C  CE1  . TYR   B 1 55  ? 6.073  35.666 93.172  1 73.53  ? 54  TYR   B CE1  1 2 
ATOM   2344 C  CE2  . TYR   B 1 55  ? 4.913  34.486 91.442  1 73.79  ? 54  TYR   B CE2  1 2 
ATOM   2345 C  CZ   . TYR   B 1 55  ? 5.175  35.662 92.117  1 74.74  ? 54  TYR   B CZ   1 2 
ATOM   2346 O  OH   . TYR   B 1 55  ? 4.548  36.813 91.699  1 76.43  ? 54  TYR   B OH   1 2 
ATOM   2347 N  N    . GLU   B 1 56  ? 9.42   29.916 93.815  1 71.6   ? 55  GLU   B N    1 2 
ATOM   2348 C  CA   . GLU   B 1 56  ? 9.827  28.553 94.145  1 73.14  ? 55  GLU   B CA   1 2 
ATOM   2349 C  C    . GLU   B 1 56  ? 10.899 28.498 95.215  1 74.9   ? 55  GLU   B C    1 2 
ATOM   2350 O  O    . GLU   B 1 56  ? 10.874 27.601 96.061  1 75.16  ? 55  GLU   B O    1 2 
ATOM   2351 C  CB   . GLU   B 1 56  ? 10.262 27.78  92.896  1 75.28  ? 55  GLU   B CB   1 2 
ATOM   2352 C  CG   . GLU   B 1 56  ? 9.098  27.237 92.088  1 80.09  ? 55  GLU   B CG   1 2 
ATOM   2353 C  CD   . GLU   B 1 56  ? 8.275  26.165 92.778  1 86.86  ? 55  GLU   B CD   1 2 
ATOM   2354 O  OE1  . GLU   B 1 56  ? 8.804  25.494 93.694  1 88.52  ? 55  GLU   B OE1  1 2 
ATOM   2355 O  OE2  . GLU   B 1 56  ? 7.096  25.988 92.393  1 89.02  ? 55  GLU   B OE2  1 2 
ATOM   2356 N  N    . PHE   B 1 57  ? 11.825 29.462 95.205  1 75.88  ? 56  PHE   B N    1 2 
ATOM   2357 C  CA   . PHE   B 1 57  ? 12.861 29.527 96.235  1 77.17  ? 56  PHE   B CA   1 2 
ATOM   2358 C  C    . PHE   B 1 57  ? 12.271 29.961 97.568  1 77.84  ? 56  PHE   B C    1 2 
ATOM   2359 O  O    . PHE   B 1 57  ? 12.676 29.43  98.599  1 77.98  ? 56  PHE   B O    1 2 
ATOM   2360 C  CB   . PHE   B 1 57  ? 14.007 30.44  95.818  1 77.46  ? 56  PHE   B CB   1 2 
ATOM   2361 C  CG   . PHE   B 1 57  ? 15.022 29.73  94.961  1 78.29  ? 56  PHE   B CG   1 2 
ATOM   2362 C  CD1  . PHE   B 1 57  ? 15.71  28.632 95.441  1 79.13  ? 56  PHE   B CD1  1 2 
ATOM   2363 C  CD2  . PHE   B 1 57  ? 15.313 30.18  93.689  1 79.09  ? 56  PHE   B CD2  1 2 
ATOM   2364 C  CE1  . PHE   B 1 57  ? 16.651 27.983 94.653  1 79.83  ? 56  PHE   B CE1  1 2 
ATOM   2365 C  CE2  . PHE   B 1 57  ? 16.257 29.532 92.907  1 79.86  ? 56  PHE   B CE2  1 2 
ATOM   2366 C  CZ   . PHE   B 1 57  ? 16.921 28.439 93.394  1 79.63  ? 56  PHE   B CZ   1 2 
ATOM   2367 N  N    . ALA   B 1 58  ? 11.269 30.863 97.552  1 78.1   ? 57  ALA   B N    1 2 
ATOM   2368 C  CA   . ALA   B 1 58  ? 10.559 31.277 98.769  1 78.79  ? 57  ALA   B CA   1 2 
ATOM   2369 C  C    . ALA   B 1 58  ? 9.831  30.089 99.427  1 79.39  ? 57  ALA   B C    1 2 
ATOM   2370 O  O    . ALA   B 1 58  ? 9.648  30.076 100.642 1 79.83  ? 57  ALA   B O    1 2 
ATOM   2371 C  CB   . ALA   B 1 58  ? 9.565  32.386 98.455  1 78.99  ? 57  ALA   B CB   1 2 
ATOM   2372 N  N    . LYS   B 1 59  ? 9.419  29.098 98.625  1 79.6   ? 58  LYS   B N    1 2 
ATOM   2373 C  CA   . LYS   B 1 59  ? 8.782  27.881 99.108  1 80.3   ? 58  LYS   B CA   1 2 
ATOM   2374 C  C    . LYS   B 1 59  ? 9.817  27.005 99.848  1 81.07  ? 58  LYS   B C    1 2 
ATOM   2375 O  O    . LYS   B 1 59  ? 9.484  26.385 100.865 1 81.28  ? 58  LYS   B O    1 2 
ATOM   2376 C  CB   . LYS   B 1 59  ? 8.141  27.104 97.94   1 81.89  ? 58  LYS   B CB   1 2 
ATOM   2377 C  CG   . LYS   B 1 59  ? 6.876  27.767 97.392  1 85.28  ? 58  LYS   B CG   1 2 
ATOM   2378 C  CD   . LYS   B 1 59  ? 6.142  26.901 96.362  1 88.47  ? 58  LYS   B CD   1 2 
ATOM   2379 C  CE   . LYS   B 1 59  ? 4.738  27.41  96.107  1 91.12  ? 58  LYS   B CE   1 2 
ATOM   2380 N  NZ   . LYS   B 1 59  ? 4.052  26.674 95.014  1 92.59  ? 58  LYS   B NZ   1 2 
ATOM   2381 N  N    . GLN   B 1 60  ? 11.083 26.997 99.359  1 81.15  ? 59  GLN   B N    1 2 
ATOM   2382 C  CA   . GLN   B 1 60  ? 12.216 26.244 99.917  1 81.68  ? 59  GLN   B CA   1 2 
ATOM   2383 C  C    . GLN   B 1 60  ? 12.872 26.88  101.153 1 81.89  ? 59  GLN   B C    1 2 
ATOM   2384 O  O    . GLN   B 1 60  ? 13.893 26.374 101.617 1 82.12  ? 59  GLN   B O    1 2 
ATOM   2385 C  CB   . GLN   B 1 60  ? 13.285 26.034 98.836  1 83.32  ? 59  GLN   B CB   1 2 
ATOM   2386 C  CG   . GLN   B 1 60  ? 12.763 25.351 97.577  1 86.81  ? 59  GLN   B CG   1 2 
ATOM   2387 C  CD   . GLN   B 1 60  ? 12.528 23.879 97.78   1 91.97  ? 59  GLN   B CD   1 2 
ATOM   2388 O  OE1  . GLN   B 1 60  ? 13.151 23.235 98.632  1 94.5   ? 59  GLN   B OE1  1 2 
ATOM   2389 N  NE2  . GLN   B 1 60  ? 11.628 23.306 96.995  1 92.15  ? 59  GLN   B NE2  1 2 
ATOM   2390 N  N    . LYS   B 1 61  ? 12.297 27.982 101.665 1 81.82  ? 60  LYS   B N    1 2 
ATOM   2391 C  CA   . LYS   B 1 61  ? 12.777 28.723 102.828 1 82.35  ? 60  LYS   B CA   1 2 
ATOM   2392 C  C    . LYS   B 1 61  ? 14.208 29.261 102.639 1 82.33  ? 60  LYS   B C    1 2 
ATOM   2393 O  O    . LYS   B 1 61  ? 15.078 29.025 103.484 1 83     ? 60  LYS   B O    1 2 
ATOM   2394 C  CB   . LYS   B 1 61  ? 12.629 27.899 104.126 1 84.31  ? 60  LYS   B CB   1 2 
ATOM   2395 C  CG   . LYS   B 1 61  ? 11.207 27.403 104.379 1 88.32  ? 60  LYS   B CG   1 2 
ATOM   2396 C  CD   . LYS   B 1 61  ? 11.123 26.671 105.716 1 92.95  ? 60  LYS   B CD   1 2 
ATOM   2397 C  CE   . LYS   B 1 61  ? 9.735  26.221 106.096 1 96.67  ? 60  LYS   B CE   1 2 
ATOM   2398 N  NZ   . LYS   B 1 61  ? 9.707  25.652 107.48  1 98.47  ? 60  LYS   B NZ   1 2 
ATOM   2399 N  N    . SER   B 1 62  ? 14.443 29.994 101.543 1 81.2   ? 61  SER   B N    1 2 
ATOM   2400 C  CA   . SER   B 1 62  ? 15.756 30.566 101.238 1 80.84  ? 61  SER   B CA   1 2 
ATOM   2401 C  C    . SER   B 1 62  ? 15.823 32.066 101.575 1 80.11  ? 61  SER   B C    1 2 
ATOM   2402 O  O    . SER   B 1 62  ? 14.783 32.71  101.715 1 80.57  ? 61  SER   B O    1 2 
ATOM   2403 C  CB   . SER   B 1 62  ? 16.078 30.361 99.76   1 82.1   ? 61  SER   B CB   1 2 
ATOM   2404 O  OG   . SER   B 1 62  ? 15.915 29.004 99.383  1 84.69  ? 61  SER   B OG   1 2 
ATOM   2405 N  N    . ARG   B 1 63  ? 17.039 32.612 101.748 1 78.68  ? 62  ARG   B N    1 2 
ATOM   2406 C  CA   . ARG   B 1 63  ? 17.234 34.048 101.964 1 77.44  ? 62  ARG   B CA   1 2 
ATOM   2407 C  C    . ARG   B 1 63  ? 17.391 34.592 100.529 1 75.41  ? 62  ARG   B C    1 2 
ATOM   2408 O  O    . ARG   B 1 63  ? 18.323 34.19  99.839  1 75.44  ? 62  ARG   B O    1 2 
ATOM   2409 C  CB   . ARG   B 1 63  ? 18.501 34.307 102.804 1 79     ? 62  ARG   B CB   1 2 
ATOM   2410 C  CG   . ARG   B 1 63  ? 18.267 34.352 104.314 1 82.49  ? 62  ARG   B CG   1 2 
ATOM   2411 C  CD   . ARG   B 1 63  ? 19.378 33.672 105.109 1 85.58  ? 62  ARG   B CD   1 2 
ATOM   2412 N  NE   . ARG   B 1 63  ? 20.687 34.309 104.916 1 88.54  ? 62  ARG   B NE   1 2 
ATOM   2413 C  CZ   . ARG   B 1 63  ? 21.842 33.792 105.334 1 90.82  ? 62  ARG   B CZ   1 2 
ATOM   2414 N  NH1  . ARG   B 1 63  ? 21.864 32.634 105.986 1 90.93  ? 62  ARG   B NH1  1 2 
ATOM   2415 N  NH2  . ARG   B 1 63  ? 22.981 34.445 105.131 1 90.24  ? 62  ARG   B NH2  1 2 
ATOM   2416 N  N    . LEU   B 1 64  ? 16.448 35.416 100.045 1 73.59  ? 63  LEU   B N    1 2 
ATOM   2417 C  CA   . LEU   B 1 64  ? 16.46  35.857 98.644  1 72.47  ? 63  LEU   B CA   1 2 
ATOM   2418 C  C    . LEU   B 1 64  ? 16.947 37.295 98.38   1 71.02  ? 63  LEU   B C    1 2 
ATOM   2419 O  O    . LEU   B 1 64  ? 16.719 38.188 99.189  1 71.5   ? 63  LEU   B O    1 2 
ATOM   2420 C  CB   . LEU   B 1 64  ? 15.061 35.661 98.037  1 72.5   ? 63  LEU   B CB   1 2 
ATOM   2421 C  CG   . LEU   B 1 64  ? 14.68  34.219 97.7    1 73.55  ? 63  LEU   B CG   1 2 
ATOM   2422 C  CD1  . LEU   B 1 64  ? 13.169 34.034 97.659  1 73.83  ? 63  LEU   B CD1  1 2 
ATOM   2423 C  CD2  . LEU   B 1 64  ? 15.316 33.787 96.402  1 74.07  ? 63  LEU   B CD2  1 2 
ATOM   2424 N  N    . VAL   B 1 65  ? 17.608 37.499 97.218  1 69.15  ? 64  VAL   B N    1 2 
ATOM   2425 C  CA   . VAL   B 1 65  ? 18.156 38.769 96.724  1 67.79  ? 64  VAL   B CA   1 2 
ATOM   2426 C  C    . VAL   B 1 65  ? 17.697 38.91  95.279  1 65.83  ? 64  VAL   B C    1 2 
ATOM   2427 O  O    . VAL   B 1 65  ? 18.086 38.085 94.46   1 65.68  ? 64  VAL   B O    1 2 
ATOM   2428 C  CB   . VAL   B 1 65  ? 19.701 38.716 96.749  1 68.72  ? 64  VAL   B CB   1 2 
ATOM   2429 C  CG1  . VAL   B 1 65  ? 20.319 40.003 96.212  1 69.45  ? 64  VAL   B CG1  1 2 
ATOM   2430 C  CG2  . VAL   B 1 65  ? 20.223 38.391 98.142  1 69.22  ? 64  VAL   B CG2  1 2 
ATOM   2431 N  N    . LEU   B 1 66  ? 16.875 39.918 94.961  1 64.28  ? 65  LEU   B N    1 2 
ATOM   2432 C  CA   . LEU   B 1 66  ? 16.405 40.083 93.587  1 63.36  ? 65  LEU   B CA   1 2 
ATOM   2433 C  C    . LEU   B 1 66  ? 16.967 41.311 92.882  1 62.09  ? 65  LEU   B C    1 2 
ATOM   2434 O  O    . LEU   B 1 66  ? 17.045 42.396 93.46   1 61.47  ? 65  LEU   B O    1 2 
ATOM   2435 C  CB   . LEU   B 1 66  ? 14.877 40.065 93.5    1 63.69  ? 65  LEU   B CB   1 2 
ATOM   2436 C  CG   . LEU   B 1 66  ? 14.155 38.901 94.17   1 65.43  ? 65  LEU   B CG   1 2 
ATOM   2437 C  CD1  . LEU   B 1 66  ? 12.653 39.012 93.967  1 65.99  ? 65  LEU   B CD1  1 2 
ATOM   2438 C  CD2  . LEU   B 1 66  ? 14.654 37.56  93.661  1 66.27  ? 65  LEU   B CD2  1 2 
ATOM   2439 N  N    . TRP   B 1 67  ? 17.332 41.129 91.596  1 61.63  ? 66  TRP   B N    1 2 
ATOM   2440 C  CA   . TRP   B 1 67  ? 17.884 42.185 90.733  1 60.94  ? 66  TRP   B CA   1 2 
ATOM   2441 C  C    . TRP   B 1 67  ? 17.038 42.348 89.478  1 60.44  ? 66  TRP   B C    1 2 
ATOM   2442 O  O    . TRP   B 1 67  ? 16.626 41.349 88.894  1 60.48  ? 66  TRP   B O    1 2 
ATOM   2443 C  CB   . TRP   B 1 67  ? 19.344 41.863 90.355  1 60.53  ? 66  TRP   B CB   1 2 
ATOM   2444 C  CG   . TRP   B 1 67  ? 20.356 42.14  91.428  1 61.03  ? 66  TRP   B CG   1 2 
ATOM   2445 C  CD1  . TRP   B 1 67  ? 20.13  42.285 92.775  1 62.22  ? 66  TRP   B CD1  1 2 
ATOM   2446 C  CD2  . TRP   B 1 67  ? 21.768 42.246 91.245  1 60.96  ? 66  TRP   B CD2  1 2 
ATOM   2447 N  NE1  . TRP   B 1 67  ? 21.316 42.518 93.429  1 62.42  ? 66  TRP   B NE1  1 2 
ATOM   2448 C  CE2  . TRP   B 1 67  ? 22.339 42.504 92.511  1 62.11  ? 66  TRP   B CE2  1 2 
ATOM   2449 C  CE3  . TRP   B 1 67  ? 22.607 42.158 90.135  1 61.18  ? 66  TRP   B CE3  1 2 
ATOM   2450 C  CZ2  . TRP   B 1 67  ? 23.709 42.689 92.682  1 62.59  ? 66  TRP   B CZ2  1 2 
ATOM   2451 C  CZ3  . TRP   B 1 67  ? 23.962 42.341 90.308  1 62.07  ? 66  TRP   B CZ3  1 2 
ATOM   2452 C  CH2  . TRP   B 1 67  ? 24.5   42.61  91.565  1 62.34  ? 66  TRP   B CH2  1 2 
ATOM   2453 N  N    . ASP   B 1 68  ? 16.779 43.598 89.062  1 59.87  ? 67  ASP   B N    1 2 
ATOM   2454 C  CA   . ASP   B 1 68  ? 15.981 43.895 87.862  1 59.65  ? 67  ASP   B CA   1 2 
ATOM   2455 C  C    . ASP   B 1 68  ? 16.025 45.398 87.505  1 59.5   ? 67  ASP   B C    1 2 
ATOM   2456 O  O    . ASP   B 1 68  ? 16.399 46.219 88.337  1 59.85  ? 67  ASP   B O    1 2 
ATOM   2457 C  CB   . ASP   B 1 68  ? 14.517 43.462 88.079  1 60.81  ? 67  ASP   B CB   1 2 
ATOM   2458 C  CG   . ASP   B 1 68  ? 13.776 43.146 86.803  1 64.78  ? 67  ASP   B CG   1 2 
ATOM   2459 O  OD1  . ASP   B 1 68  ? 13.593 41.956 86.507  1 65.31  ? 67  ASP   B OD1  1 2 
ATOM   2460 O  OD2  . ASP   B 1 68  ? 13.368 44.092 86.105  1 66.99  ? 67  ASP   B OD2  1 2 
ATOM   2461 N  N    . ILE   B 1 69  ? 15.642 45.759 86.276  1 58.92  ? 68  ILE   B N    1 2 
ATOM   2462 C  CA   . ILE   B 1 69  ? 15.56  47.166 85.871  1 58.65  ? 68  ILE   B CA   1 2 
ATOM   2463 C  C    . ILE   B 1 69  ? 14.171 47.759 86.212  1 58.58  ? 68  ILE   B C    1 2 
ATOM   2464 O  O    . ILE   B 1 69  ? 14.048 48.968 86.402  1 58.29  ? 68  ILE   B O    1 2 
ATOM   2465 C  CB   . ILE   B 1 69  ? 15.926 47.347 84.377  1 58.8   ? 68  ILE   B CB   1 2 
ATOM   2466 C  CG1  . ILE   B 1 69  ? 15.109 46.411 83.472  1 59.62  ? 68  ILE   B CG1  1 2 
ATOM   2467 C  CG2  . ILE   B 1 69  ? 17.417 47.173 84.153  1 59.05  ? 68  ILE   B CG2  1 2 
ATOM   2468 C  CD1  . ILE   B 1 69  ? 14.032 47.133 82.615  1 60.86  ? 68  ILE   B CD1  1 2 
ATOM   2469 N  N    . ASN   B 1 70  ? 13.137 46.894 86.287  1 58.71  ? 69  ASN   B N    1 2 
ATOM   2470 C  CA   . ASN   B 1 70  ? 11.751 47.229 86.577  1 59.25  ? 69  ASN   B CA   1 2 
ATOM   2471 C  C    . ASN   B 1 70  ? 11.586 47.271 88.061  1 59.46  ? 69  ASN   B C    1 2 
ATOM   2472 O  O    . ASN   B 1 70  ? 11.412 46.219 88.675  1 59.19  ? 69  ASN   B O    1 2 
ATOM   2473 C  CB   . ASN   B 1 70  ? 10.826 46.15  85.995  1 60.61  ? 69  ASN   B CB   1 2 
ATOM   2474 C  CG   . ASN   B 1 70  ? 9.382  46.569 85.922  1 63.63  ? 69  ASN   B CG   1 2 
ATOM   2475 O  OD1  . ASN   B 1 70  ? 8.839  47.182 86.844  1 64.81  ? 69  ASN   B OD1  1 2 
ATOM   2476 N  ND2  . ASN   B 1 70  ? 8.725  46.256 84.821  1 63.75  ? 69  ASN   B ND2  1 2 
ATOM   2477 N  N    . LYS   B 1 71  ? 11.628 48.471 88.646  1 59.86  ? 70  LYS   B N    1 2 
ATOM   2478 C  CA   . LYS   B 1 71  ? 11.492 48.607 90.094  1 60.82  ? 70  LYS   B CA   1 2 
ATOM   2479 C  C    . LYS   B 1 71  ? 10.171 48.042 90.625  1 61.57  ? 70  LYS   B C    1 2 
ATOM   2480 O  O    . LYS   B 1 71  ? 10.177 47.329 91.623  1 61.75  ? 70  LYS   B O    1 2 
ATOM   2481 C  CB   . LYS   B 1 71  ? 11.68  50.067 90.531  1 62.36  ? 70  LYS   B CB   1 2 
ATOM   2482 C  CG   . LYS   B 1 71  ? 11.59  50.281 92.049  1 64.99  ? 70  LYS   B CG   1 2 
ATOM   2483 C  CD   . LYS   B 1 71  ? 12.137 51.639 92.444  1 67.92  ? 70  LYS   B CD   1 2 
ATOM   2484 C  CE   . LYS   B 1 71  ? 11.586 52.137 93.766  1 70.81  ? 70  LYS   B CE   1 2 
ATOM   2485 N  NZ   . LYS   B 1 71  ? 10.103 52.356 93.768  1 72.09  ? 70  LYS   B NZ   1 2 
ATOM   2486 N  N    . HIS   B 1 72  ? 9.056  48.341 89.946  1 61.67  ? 71  HIS   B N    1 2 
ATOM   2487 C  CA   . HIS   B 1 72  ? 7.714  47.905 90.324  1 62.26  ? 71  HIS   B CA   1 2 
ATOM   2488 C  C    . HIS   B 1 72  ? 7.537  46.38  90.266  1 62.91  ? 71  HIS   B C    1 2 
ATOM   2489 O  O    . HIS   B 1 72  ? 6.986  45.79  91.197  1 63.06  ? 71  HIS   B O    1 2 
ATOM   2490 C  CB   . HIS   B 1 72  ? 6.677  48.625 89.436  1 62.94  ? 71  HIS   B CB   1 2 
ATOM   2491 C  CG   . HIS   B 1 72  ? 5.256  48.203 89.66   1 65.01  ? 71  HIS   B CG   1 2 
ATOM   2492 N  ND1  . HIS   B 1 72  ? 4.482  48.775 90.653  1 66.6   ? 71  HIS   B ND1  1 2 
ATOM   2493 C  CD2  . HIS   B 1 72  ? 4.5    47.308 88.98   1 66.11  ? 71  HIS   B CD2  1 2 
ATOM   2494 C  CE1  . HIS   B 1 72  ? 3.296  48.192 90.57   1 66.94  ? 71  HIS   B CE1  1 2 
ATOM   2495 N  NE2  . HIS   B 1 72  ? 3.26   47.298 89.583  1 67.01  ? 71  HIS   B NE2  1 2 
ATOM   2496 N  N    . GLY   B 1 73  ? 8.008  45.771 89.182  1 63.14  ? 72  GLY   B N    1 2 
ATOM   2497 C  CA   . GLY   B 1 73  ? 7.909  44.338 88.935  1 63.85  ? 72  GLY   B CA   1 2 
ATOM   2498 C  C    . GLY   B 1 73  ? 8.66   43.502 89.945  1 64.25  ? 72  GLY   B C    1 2 
ATOM   2499 O  O    . GLY   B 1 73  ? 8.098  42.562 90.515  1 64.21  ? 72  GLY   B O    1 2 
ATOM   2500 N  N    . VAL   B 1 74  ? 9.93   43.86  90.197  1 64.5   ? 73  VAL   B N    1 2 
ATOM   2501 C  CA   . VAL   B 1 74  ? 10.769 43.151 91.168  1 65.24  ? 73  VAL   B CA   1 2 
ATOM   2502 C  C    . VAL   B 1 74  ? 10.29  43.375 92.616  1 66.14  ? 73  VAL   B C    1 2 
ATOM   2503 O  O    . VAL   B 1 74  ? 10.439 42.486 93.455  1 66.31  ? 73  VAL   B O    1 2 
ATOM   2504 C  CB   . VAL   B 1 74  ? 12.275 43.46  90.988  1 65.76  ? 73  VAL   B CB   1 2 
ATOM   2505 C  CG1  . VAL   B 1 74  ? 12.659 44.782 91.646  1 66.24  ? 73  VAL   B CG1  1 2 
ATOM   2506 C  CG2  . VAL   B 1 74  ? 13.132 42.324 91.525  1 66.06  ? 73  VAL   B CG2  1 2 
ATOM   2507 N  N    . GLU   B 1 75  ? 9.679  44.538 92.901  1 66.39  ? 74  GLU   B N    1 2 
ATOM   2508 C  CA   . GLU   B 1 75  ? 9.14   44.818 94.226  1 66.99  ? 74  GLU   B CA   1 2 
ATOM   2509 C  C    . GLU   B 1 75  ? 7.889  43.993 94.475  1 67.85  ? 74  GLU   B C    1 2 
ATOM   2510 O  O    . GLU   B 1 75  ? 7.68   43.535 95.592  1 68.18  ? 74  GLU   B O    1 2 
ATOM   2511 C  CB   . GLU   B 1 75  ? 8.843  46.309 94.399  1 68.83  ? 74  GLU   B CB   1 2 
ATOM   2512 C  CG   . GLU   B 1 75  ? 10.057 47.107 94.847  1 72.32  ? 74  GLU   B CG   1 2 
ATOM   2513 C  CD   . GLU   B 1 75  ? 9.817  48.589 95.064  1 76.55  ? 74  GLU   B CD   1 2 
ATOM   2514 O  OE1  . GLU   B 1 75  ? 8.705  49.072 94.745  1 78.48  ? 74  GLU   B OE1  1 2 
ATOM   2515 O  OE2  . GLU   B 1 75  ? 10.747 49.272 95.553  1 76.46  ? 74  GLU   B OE2  1 2 
ATOM   2516 N  N    . GLU   B 1 76  ? 7.065  43.791 93.442  1 68.47  ? 75  GLU   B N    1 2 
ATOM   2517 C  CA   . GLU   B 1 76  ? 5.862  42.983 93.557  1 69.81  ? 75  GLU   B CA   1 2 
ATOM   2518 C  C    . GLU   B 1 76  ? 6.176  41.487 93.665  1 70.45  ? 75  GLU   B C    1 2 
ATOM   2519 O  O    . GLU   B 1 76  ? 5.424  40.753 94.311  1 70.14  ? 75  GLU   B O    1 2 
ATOM   2520 C  CB   . GLU   B 1 76  ? 4.891  43.282 92.413  1 73.03  ? 75  GLU   B CB   1 2 
ATOM   2521 C  CG   . GLU   B 1 76  ? 4.074  44.533 92.663  1 79.02  ? 75  GLU   B CG   1 2 
ATOM   2522 C  CD   . GLU   B 1 76  ? 2.797  44.597 91.852  1 86.68  ? 75  GLU   B CD   1 2 
ATOM   2523 O  OE1  . GLU   B 1 76  ? 2.793  44.11  90.695  1 88     ? 75  GLU   B OE1  1 2 
ATOM   2524 O  OE2  . GLU   B 1 76  ? 1.798  45.14  92.38   1 88.85  ? 75  GLU   B OE2  1 2 
ATOM   2525 N  N    . THR   B 1 77  ? 7.299  41.037 93.071  1 71.23  ? 76  THR   B N    1 2 
ATOM   2526 C  CA   . THR   B 1 77  ? 7.715  39.641 93.204  1 72.6   ? 76  THR   B CA   1 2 
ATOM   2527 C  C    . THR   B 1 77  ? 8.161  39.426 94.64   1 74.29  ? 76  THR   B C    1 2 
ATOM   2528 O  O    . THR   B 1 77  ? 7.714  38.474 95.275  1 74.88  ? 76  THR   B O    1 2 
ATOM   2529 C  CB   . THR   B 1 77  ? 8.835  39.289 92.237  1 73.67  ? 76  THR   B CB   1 2 
ATOM   2530 O  OG1  . THR   B 1 77  ? 8.368  39.491 90.906  1 75.04  ? 76  THR   B OG1  1 2 
ATOM   2531 C  CG2  . THR   B 1 77  ? 9.317  37.854 92.417  1 73.67  ? 76  THR   B CG2  1 2 
ATOM   2532 N  N    . ALA   B 1 78  ? 8.981  40.361 95.177  1 74.76  ? 77  ALA   B N    1 2 
ATOM   2533 C  CA   . ALA   B 1 78  ? 9.452  40.346 96.555  1 75.44  ? 77  ALA   B CA   1 2 
ATOM   2534 C  C    . ALA   B 1 78  ? 8.276  40.39  97.513  1 76.22  ? 77  ALA   B C    1 2 
ATOM   2535 O  O    . ALA   B 1 78  ? 8.324  39.733 98.541  1 76.47  ? 77  ALA   B O    1 2 
ATOM   2536 C  CB   . ALA   B 1 78  ? 10.343 41.54  96.804  1 75.57  ? 77  ALA   B CB   1 2 
ATOM   2537 N  N    . ALA   B 1 79  ? 7.221  41.149 97.183  1 76.56  ? 78  ALA   B N    1 2 
ATOM   2538 C  CA   . ALA   B 1 79  ? 6.027  41.224 98.006  1 77.56  ? 78  ALA   B CA   1 2 
ATOM   2539 C  C    . ALA   B 1 79  ? 5.352  39.856 98.094  1 78.59  ? 78  ALA   B C    1 2 
ATOM   2540 O  O    . ALA   B 1 79  ? 5.015  39.445 99.196  1 79     ? 78  ALA   B O    1 2 
ATOM   2541 C  CB   . ALA   B 1 79  ? 5.063  42.256 97.45   1 77.72  ? 78  ALA   B CB   1 2 
ATOM   2542 N  N    . GLU   B 1 80  ? 5.196  39.125 96.967  1 79.04  ? 79  GLU   B N    1 2 
ATOM   2543 C  CA   . GLU   B 1 80  ? 4.582  37.791 97.014  1 79.97  ? 79  GLU   B CA   1 2 
ATOM   2544 C  C    . GLU   B 1 80  ? 5.539  36.725 97.595  1 80.52  ? 79  GLU   B C    1 2 
ATOM   2545 O  O    . GLU   B 1 80  ? 5.087  35.725 98.154  1 80.55  ? 79  GLU   B O    1 2 
ATOM   2546 C  CB   . GLU   B 1 80  ? 3.988  37.374 95.653  1 82.56  ? 79  GLU   B CB   1 2 
ATOM   2547 C  CG   . GLU   B 1 80  ? 3.014  36.197 95.723  1 88.97  ? 79  GLU   B CG   1 2 
ATOM   2548 C  CD   . GLU   B 1 80  ? 2.04   36.129 96.898  1 97.86  ? 79  GLU   B CD   1 2 
ATOM   2549 O  OE1  . GLU   B 1 80  ? 2.218  35.246 97.772  1 98.84  ? 79  GLU   B OE1  1 2 
ATOM   2550 O  OE2  . GLU   B 1 80  ? 1.097  36.953 96.944  1 101.38 ? 79  GLU   B OE2  1 2 
ATOM   2551 N  N    . CYS   B 1 81  ? 6.851  36.963 97.521  1 80.9   ? 80  CYS   B N    1 2 
ATOM   2552 C  CA   . CYS   B 1 81  ? 7.842  36.079 98.128  1 81.86  ? 80  CYS   B CA   1 2 
ATOM   2553 C  C    . CYS   B 1 81  ? 7.85   36.26  99.646  1 82.48  ? 80  CYS   B C    1 2 
ATOM   2554 O  O    . CYS   B 1 81  ? 8.071  35.291 100.364 1 82.74  ? 80  CYS   B O    1 2 
ATOM   2555 C  CB   . CYS   B 1 81  ? 9.221  36.317 97.531  1 82.76  ? 80  CYS   B CB   1 2 
ATOM   2556 S  SG   . CYS   B 1 81  ? 9.335  35.915 95.776  1 87.25  ? 80  CYS   B SG   1 2 
ATOM   2557 N  N    . ARG   B 1 82  ? 7.597  37.494 100.131 1 82.49  ? 81  ARG   B N    1 2 
ATOM   2558 C  CA   . ARG   B 1 82  ? 7.483  37.819 101.546 1 82.99  ? 81  ARG   B CA   1 2 
ATOM   2559 C  C    . ARG   B 1 82  ? 6.204  37.181 102.096 1 83.83  ? 81  ARG   B C    1 2 
ATOM   2560 O  O    . ARG   B 1 82  ? 6.231  36.596 103.185 1 84.22  ? 81  ARG   B O    1 2 
ATOM   2561 C  CB   . ARG   B 1 82  ? 7.451  39.337 101.75  1 83.9   ? 81  ARG   B CB   1 2 
ATOM   2562 C  CG   . ARG   B 1 82  ? 8.822  39.974 101.677 1 86.75  ? 81  ARG   B CG   1 2 
ATOM   2563 C  CD   . ARG   B 1 82  ? 8.741  41.482 101.723 1 90.24  ? 81  ARG   B CD   1 2 
ATOM   2564 N  NE   . ARG   B 1 82  ? 10.04  42.098 101.443 1 93.56  ? 81  ARG   B NE   1 2 
ATOM   2565 C  CZ   . ARG   B 1 82  ? 10.254 43.001 100.488 1 95.87  ? 81  ARG   B CZ   1 2 
ATOM   2566 N  NH1  . ARG   B 1 82  ? 9.251  43.425 99.727  1 95.33  ? 81  ARG   B NH1  1 2 
ATOM   2567 N  NH2  . ARG   B 1 82  ? 11.471 43.498 100.296 1 96     ? 81  ARG   B NH2  1 2 
ATOM   2568 N  N    . LYS   B 1 83  ? 5.094  37.24  101.326 1 83.88  ? 82  LYS   B N    1 2 
ATOM   2569 C  CA   . LYS   B 1 83  ? 3.828  36.606 101.712 1 84.58  ? 82  LYS   B CA   1 2 
ATOM   2570 C  C    . LYS   B 1 83  ? 3.92   35.062 101.82  1 84.78  ? 82  LYS   B C    1 2 
ATOM   2571 O  O    . LYS   B 1 83  ? 2.952  34.419 102.219 1 84.87  ? 82  LYS   B O    1 2 
ATOM   2572 C  CB   . LYS   B 1 83  ? 2.676  37.039 100.786 1 86.83  ? 82  LYS   B CB   1 2 
ATOM   2573 C  CG   . LYS   B 1 83  ? 2.371  38.536 100.847 1 91.53  ? 82  LYS   B CG   1 2 
ATOM   2574 C  CD   . LYS   B 1 83  ? 0.927  38.88  100.454 1 96.8   ? 82  LYS   B CD   1 2 
ATOM   2575 C  CE   . LYS   B 1 83  ? -0.005 38.85  101.65  1 101.26 ? 82  LYS   B CE   1 2 
ATOM   2576 N  NZ   . LYS   B 1 83  ? -1.298 39.537 101.379 1 103.64 ? 82  LYS   B NZ   1 2 
ATOM   2577 N  N    . LEU   B 1 84  ? 5.083  34.481 101.484 1 84.72  ? 83  LEU   B N    1 2 
ATOM   2578 C  CA   . LEU   B 1 84  ? 5.371  33.055 101.604 1 85.09  ? 83  LEU   B CA   1 2 
ATOM   2579 C  C    . LEU   B 1 84  ? 6.262  32.73  102.828 1 85.52  ? 83  LEU   B C    1 2 
ATOM   2580 O  O    . LEU   B 1 84  ? 6.303  31.58  103.261 1 85.8   ? 83  LEU   B O    1 2 
ATOM   2581 C  CB   . LEU   B 1 84  ? 6.022  32.521 100.319 1 85.11  ? 83  LEU   B CB   1 2 
ATOM   2582 C  CG   . LEU   B 1 84  ? 5.162  32.524 99.068  1 86.06  ? 83  LEU   B CG   1 2 
ATOM   2583 C  CD1  . LEU   B 1 84  ? 5.927  31.948 97.921  1 86.51  ? 83  LEU   B CD1  1 2 
ATOM   2584 C  CD2  . LEU   B 1 84  ? 3.883  31.728 99.267  1 86.65  ? 83  LEU   B CD2  1 2 
ATOM   2585 N  N    . GLY   B 1 85  ? 6.959  33.732 103.364 1 85.42  ? 84  GLY   B N    1 2 
ATOM   2586 C  CA   . GLY   B 1 85  ? 7.81   33.565 104.533 1 85.99  ? 84  GLY   B CA   1 2 
ATOM   2587 C  C    . GLY   B 1 85  ? 9.289  33.805 104.302 1 86.19  ? 84  GLY   B C    1 2 
ATOM   2588 O  O    . GLY   B 1 85  ? 10.072 33.788 105.255 1 86.74  ? 84  GLY   B O    1 2 
ATOM   2589 N  N    . ALA   B 1 86  ? 9.695  34.016 103.052 1 85.67  ? 85  ALA   B N    1 2 
ATOM   2590 C  CA   . ALA   B 1 86  ? 11.105 34.241 102.724 1 85.88  ? 85  ALA   B CA   1 2 
ATOM   2591 C  C    . ALA   B 1 86  ? 11.587 35.66  103.064 1 85.73  ? 85  ALA   B C    1 2 
ATOM   2592 O  O    . ALA   B 1 86  ? 10.769 36.572 103.177 1 86.47  ? 85  ALA   B O    1 2 
ATOM   2593 C  CB   . ALA   B 1 86  ? 11.335 33.972 101.245 1 86.12  ? 85  ALA   B CB   1 2 
ATOM   2594 N  N    . THR   B 1 87  ? 12.915 35.864 103.193 1 84.32  ? 86  THR   B N    1 2 
ATOM   2595 C  CA   . THR   B 1 87  ? 13.456 37.198 103.433 1 82.84  ? 86  THR   B CA   1 2 
ATOM   2596 C  C    . THR   B 1 87  ? 14.049 37.727 102.125 1 81.07  ? 86  THR   B C    1 2 
ATOM   2597 O  O    . THR   B 1 87  ? 15.135 37.329 101.701 1 80.98  ? 86  THR   B O    1 2 
ATOM   2598 C  CB   . THR   B 1 87  ? 14.365 37.217 104.643 1 83.3   ? 86  THR   B CB   1 2 
ATOM   2599 O  OG1  . THR   B 1 87  ? 13.544 36.916 105.768 1 83.88  ? 86  THR   B OG1  1 2 
ATOM   2600 C  CG2  . THR   B 1 87  ? 15.026 38.569 104.843 1 83.58  ? 86  THR   B CG2  1 2 
ATOM   2601 N  N    . VAL   B 1 88  ? 13.288 38.585 101.464 1 79.5   ? 87  VAL   B N    1 2 
ATOM   2602 C  CA   . VAL   B 1 88  ? 13.684 39.099 100.171 1 78.92  ? 87  VAL   B CA   1 2 
ATOM   2603 C  C    . VAL   B 1 88  ? 14.146 40.541 100.236 1 77.42  ? 87  VAL   B C    1 2 
ATOM   2604 O  O    . VAL   B 1 88  ? 13.5   41.381 100.857 1 77.35  ? 87  VAL   B O    1 2 
ATOM   2605 C  CB   . VAL   B 1 88  ? 12.571 38.884 99.119  1 80.18  ? 87  VAL   B CB   1 2 
ATOM   2606 C  CG1  . VAL   B 1 88  ? 13.054 39.265 97.723  1 80.77  ? 87  VAL   B CG1  1 2 
ATOM   2607 C  CG2  . VAL   B 1 88  ? 12.068 37.44  99.141  1 80.87  ? 87  VAL   B CG2  1 2 
ATOM   2608 N  N    . HIS   B 1 89  ? 15.289 40.814 99.594  1 75.96  ? 88  HIS   B N    1 2 
ATOM   2609 C  CA   . HIS   B 1 89  ? 15.88  42.139 99.495  1 74.85  ? 88  HIS   B CA   1 2 
ATOM   2610 C  C    . HIS   B 1 89  ? 16.061 42.439 98.011  1 73.49  ? 88  HIS   B C    1 2 
ATOM   2611 O  O    . HIS   B 1 89  ? 16.643 41.639 97.28   1 73.33  ? 88  HIS   B O    1 2 
ATOM   2612 C  CB   . HIS   B 1 89  ? 17.214 42.208 100.259 1 75.35  ? 88  HIS   B CB   1 2 
ATOM   2613 C  CG   . HIS   B 1 89  ? 17.072 41.898 101.713 1 77.02  ? 88  HIS   B CG   1 2 
ATOM   2614 N  ND1  . HIS   B 1 89  ? 17.239 40.612 102.195 1 78.82  ? 88  HIS   B ND1  1 2 
ATOM   2615 C  CD2  . HIS   B 1 89  ? 16.739 42.71  102.743 1 77.93  ? 88  HIS   B CD2  1 2 
ATOM   2616 C  CE1  . HIS   B 1 89  ? 17.03  40.685 103.501 1 79.11  ? 88  HIS   B CE1  1 2 
ATOM   2617 N  NE2  . HIS   B 1 89  ? 16.726 41.927 103.876 1 78.92  ? 88  HIS   B NE2  1 2 
ATOM   2618 N  N    . THR   B 1 90  ? 15.504 43.561 97.557  1 72.27  ? 89  THR   B N    1 2 
ATOM   2619 C  CA   . THR   B 1 90  ? 15.55  43.938 96.152  1 71.33  ? 89  THR   B CA   1 2 
ATOM   2620 C  C    . THR   B 1 90  ? 16.521 45.072 95.871  1 70.72  ? 89  THR   B C    1 2 
ATOM   2621 O  O    . THR   B 1 90  ? 16.733 45.937 96.724  1 71     ? 89  THR   B O    1 2 
ATOM   2622 C  CB   . THR   B 1 90  ? 14.149 44.286 95.642  1 71.83  ? 89  THR   B CB   1 2 
ATOM   2623 O  OG1  . THR   B 1 90  ? 13.711 45.531 96.191  1 72.32  ? 89  THR   B OG1  1 2 
ATOM   2624 C  CG2  . THR   B 1 90  ? 13.15  43.206 95.932  1 72.13  ? 89  THR   B CG2  1 2 
ATOM   2625 N  N    . PHE   B 1 91  ? 17.111 45.059 94.662  1 69.52  ? 90  PHE   B N    1 2 
ATOM   2626 C  CA   . PHE   B 1 91  ? 18.025 46.09  94.196  1 68.72  ? 90  PHE   B CA   1 2 
ATOM   2627 C  C    . PHE   B 1 91  ? 17.749 46.32  92.727  1 68.03  ? 90  PHE   B C    1 2 
ATOM   2628 O  O    . PHE   B 1 91  ? 17.745 45.363 91.958  1 68.31  ? 90  PHE   B O    1 2 
ATOM   2629 C  CB   . PHE   B 1 91  ? 19.491 45.649 94.353  1 68.69  ? 90  PHE   B CB   1 2 
ATOM   2630 C  CG   . PHE   B 1 91  ? 19.888 45.169 95.729  1 69.54  ? 90  PHE   B CG   1 2 
ATOM   2631 C  CD1  . PHE   B 1 91  ? 20.169 46.067 96.738  1 70.41  ? 90  PHE   B CD1  1 2 
ATOM   2632 C  CD2  . PHE   B 1 91  ? 19.97  43.817 96.012  1 70.16  ? 90  PHE   B CD2  1 2 
ATOM   2633 C  CE1  . PHE   B 1 91  ? 20.531 45.625 97.992  1 71.24  ? 90  PHE   B CE1  1 2 
ATOM   2634 C  CE2  . PHE   B 1 91  ? 20.324 43.382 97.267  1 70.67  ? 90  PHE   B CE2  1 2 
ATOM   2635 C  CZ   . PHE   B 1 91  ? 20.616 44.288 98.247  1 70.98  ? 90  PHE   B CZ   1 2 
ATOM   2636 N  N    . VAL   B 1 92  ? 17.541 47.577 92.314  1 66.96  ? 91  VAL   B N    1 2 
ATOM   2637 C  CA   . VAL   B 1 92  ? 17.342 47.889 90.899  1 65.98  ? 91  VAL   B CA   1 2 
ATOM   2638 C  C    . VAL   B 1 92  ? 18.717 47.949 90.239  1 64.79  ? 91  VAL   B C    1 2 
ATOM   2639 O  O    . VAL   B 1 92  ? 19.48  48.892 90.463  1 64.83  ? 91  VAL   B O    1 2 
ATOM   2640 C  CB   . VAL   B 1 92  ? 16.541 49.186 90.683  1 66.63  ? 91  VAL   B CB   1 2 
ATOM   2641 C  CG1  . VAL   B 1 92  ? 16.461 49.521 89.198  1 67.23  ? 91  VAL   B CG1  1 2 
ATOM   2642 C  CG2  . VAL   B 1 92  ? 15.149 49.074 91.296  1 67.01  ? 91  VAL   B CG2  1 2 
ATOM   2643 N  N    . VAL   B 1 93  ? 19.067 46.899 89.484  1 63.58  ? 92  VAL   B N    1 2 
ATOM   2644 C  CA   . VAL   B 1 93  ? 20.387 46.793 88.86   1 62.76  ? 92  VAL   B CA   1 2 
ATOM   2645 C  C    . VAL   B 1 93  ? 20.295 46.559 87.365  1 61.67  ? 92  VAL   B C    1 2 
ATOM   2646 O  O    . VAL   B 1 93  ? 19.621 45.626 86.939  1 61.79  ? 92  VAL   B O    1 2 
ATOM   2647 C  CB   . VAL   B 1 93  ? 21.214 45.647 89.504  1 63.38  ? 92  VAL   B CB   1 2 
ATOM   2648 C  CG1  . VAL   B 1 93  ? 22.653 45.641 88.987  1 63.85  ? 92  VAL   B CG1  1 2 
ATOM   2649 C  CG2  . VAL   B 1 93  ? 21.184 45.716 91.026  1 63.83  ? 92  VAL   B CG2  1 2 
ATOM   2650 N  N    . ASP   B 1 94  ? 21.011 47.36  86.568  1 60.44  ? 93  ASP   B N    1 2 
ATOM   2651 C  CA   . ASP   B 1 94  ? 21.079 47.145 85.126  1 59.71  ? 93  ASP   B CA   1 2 
ATOM   2652 C  C    . ASP   B 1 94  ? 22.037 45.968 84.957  1 58.3   ? 93  ASP   B C    1 2 
ATOM   2653 O  O    . ASP   B 1 94  ? 23.254 46.158 84.962  1 58.55  ? 93  ASP   B O    1 2 
ATOM   2654 C  CB   . ASP   B 1 94  ? 21.65  48.393 84.433  1 61.64  ? 93  ASP   B CB   1 2 
ATOM   2655 C  CG   . ASP   B 1 94  ? 21.666 48.343 82.92   1 65.69  ? 93  ASP   B CG   1 2 
ATOM   2656 O  OD1  . ASP   B 1 94  ? 21.051 47.416 82.35   1 66.47  ? 93  ASP   B OD1  1 2 
ATOM   2657 O  OD2  . ASP   B 1 94  ? 22.287 49.243 82.303  1 67.52  ? 93  ASP   B OD2  1 2 
ATOM   2658 N  N    . CYS   B 1 95  ? 21.487 44.748 84.854  1 56.67  ? 94  CYS   B N    1 2 
ATOM   2659 C  CA   . CYS   B 1 95  ? 22.27  43.51  84.779  1 55.34  ? 94  CYS   B CA   1 2 
ATOM   2660 C  C    . CYS   B 1 95  ? 23.014 43.291 83.439  1 54.8   ? 94  CYS   B C    1 2 
ATOM   2661 O  O    . CYS   B 1 95  ? 23.404 42.166 83.121  1 54.45  ? 94  CYS   B O    1 2 
ATOM   2662 C  CB   . CYS   B 1 95  ? 21.41  42.303 85.143  1 54.39  ? 94  CYS   B CB   1 2 
ATOM   2663 S  SG   . CYS   B 1 95  ? 20.549 42.451 86.731  1 51     ? 94  CYS   B SG   1 2 
ATOM   2664 N  N    . GLY   B 1 96  ? 23.238 44.371 82.709  1 54.61  ? 95  GLY   B N    1 2 
ATOM   2665 C  CA   . GLY   B 1 96  ? 24.009 44.39  81.474  1 55.28  ? 95  GLY   B CA   1 2 
ATOM   2666 C  C    . GLY   B 1 96  ? 25.224 45.296 81.598  1 55.78  ? 95  GLY   B C    1 2 
ATOM   2667 O  O    . GLY   B 1 96  ? 26.223 45.097 80.895  1 55.73  ? 95  GLY   B O    1 2 
ATOM   2668 N  N    . ASN   B 1 97  ? 25.136 46.313 82.512  1 55.97  ? 96  ASN   B N    1 2 
ATOM   2669 C  CA   . ASN   B 1 97  ? 26.167 47.31  82.823  1 56.53  ? 96  ASN   B CA   1 2 
ATOM   2670 C  C    . ASN   B 1 97  ? 27.12  46.788 83.883  1 57.03  ? 96  ASN   B C    1 2 
ATOM   2671 O  O    . ASN   B 1 97  ? 26.709 46.538 85.011  1 57.08  ? 96  ASN   B O    1 2 
ATOM   2672 C  CB   . ASN   B 1 97  ? 25.538 48.618 83.298  1 57.42  ? 96  ASN   B CB   1 2 
ATOM   2673 C  CG   . ASN   B 1 97  ? 26.544 49.727 83.475  1 60.11  ? 96  ASN   B CG   1 2 
ATOM   2674 O  OD1  . ASN   B 1 97  ? 26.56  50.428 84.489  1 61.31  ? 96  ASN   B OD1  1 2 
ATOM   2675 N  ND2  . ASN   B 1 97  ? 27.416 49.909 82.496  1 60.43  ? 96  ASN   B ND2  1 2 
ATOM   2676 N  N    . ARG   B 1 98  ? 28.393 46.644 83.508  1 57.35  ? 97  ARG   B N    1 2 
ATOM   2677 C  CA   . ARG   B 1 98  ? 29.481 46.11  84.317  1 58.26  ? 97  ARG   B CA   1 2 
ATOM   2678 C  C    . ARG   B 1 98  ? 29.766 46.927 85.567  1 58.64  ? 97  ARG   B C    1 2 
ATOM   2679 O  O    . ARG   B 1 98  ? 29.901 46.351 86.65   1 58.94  ? 97  ARG   B O    1 2 
ATOM   2680 C  CB   . ARG   B 1 98  ? 30.737 45.993 83.452  1 60.45  ? 97  ARG   B CB   1 2 
ATOM   2681 C  CG   . ARG   B 1 98  ? 31.879 45.238 84.103  1 64.93  ? 97  ARG   B CG   1 2 
ATOM   2682 C  CD   . ARG   B 1 98  ? 33.14  45.264 83.251  1 69.81  ? 97  ARG   B CD   1 2 
ATOM   2683 N  NE   . ARG   B 1 98  ? 33.576 46.632 82.963  1 74.04  ? 97  ARG   B NE   1 2 
ATOM   2684 C  CZ   . ARG   B 1 98  ? 34.403 47.335 83.73   1 77.21  ? 97  ARG   B CZ   1 2 
ATOM   2685 N  NH1  . ARG   B 1 98  ? 34.916 46.8   84.834  1 76.82  ? 97  ARG   B NH1  1 2 
ATOM   2686 N  NH2  . ARG   B 1 98  ? 34.73  48.576 83.396  1 77.65  ? 97  ARG   B NH2  1 2 
ATOM   2687 N  N    . GLU   B 1 99  ? 29.835 48.26  85.438  1 58.42  ? 98  GLU   B N    1 2 
ATOM   2688 C  CA   . GLU   B 1 99  ? 30.094 49.107 86.6    1 58.69  ? 98  GLU   B CA   1 2 
ATOM   2689 C  C    . GLU   B 1 99  ? 28.901 49.179 87.56   1 57.91  ? 98  GLU   B C    1 2 
ATOM   2690 O  O    . GLU   B 1 99  ? 29.107 49.423 88.743  1 58.3   ? 98  GLU   B O    1 2 
ATOM   2691 C  CB   . GLU   B 1 99  ? 30.584 50.498 86.183  1 62.04  ? 98  GLU   B CB   1 2 
ATOM   2692 C  CG   . GLU   B 1 99  ? 31.936 50.451 85.493  1 68.76  ? 98  GLU   B CG   1 2 
ATOM   2693 C  CD   . GLU   B 1 99  ? 32.484 51.786 85.029  1 76.91  ? 98  GLU   B CD   1 2 
ATOM   2694 O  OE1  . GLU   B 1 99  ? 32.839 51.894 83.83   1 78.23  ? 98  GLU   B OE1  1 2 
ATOM   2695 O  OE2  . GLU   B 1 99  ? 32.56  52.718 85.866  1 79.26  ? 98  GLU   B OE2  1 2 
ATOM   2696 N  N    . ASP   B 1 100 ? 27.668 48.946 87.071  1 56.79  ? 99  ASP   B N    1 2 
ATOM   2697 C  CA   . ASP   B 1 100 ? 26.479 48.939 87.928  1 56.25  ? 99  ASP   B CA   1 2 
ATOM   2698 C  C    . ASP   B 1 100 ? 26.436 47.613 88.678  1 55.69  ? 99  ASP   B C    1 2 
ATOM   2699 O  O    . ASP   B 1 100 ? 26.166 47.613 89.884  1 55.95  ? 99  ASP   B O    1 2 
ATOM   2700 C  CB   . ASP   B 1 100 ? 25.181 49.127 87.11   1 57.4   ? 99  ASP   B CB   1 2 
ATOM   2701 C  CG   . ASP   B 1 100 ? 23.954 49.54  87.919  1 60.18  ? 99  ASP   B CG   1 2 
ATOM   2702 O  OD1  . ASP   B 1 100 ? 24.046 49.57  89.17   1 60.96  ? 99  ASP   B OD1  1 2 
ATOM   2703 O  OD2  . ASP   B 1 100 ? 22.9   49.841 87.298  1 60.86  ? 99  ASP   B OD2  1 2 
ATOM   2704 N  N    . ILE   B 1 101 ? 26.716 46.486 87.978  1 54.6   ? 100 ILE   B N    1 2 
ATOM   2705 C  CA   . ILE   B 1 101 ? 26.733 45.161 88.595  1 54.14  ? 100 ILE   B CA   1 2 
ATOM   2706 C  C    . ILE   B 1 101 ? 27.736 45.106 89.758  1 53.84  ? 100 ILE   B C    1 2 
ATOM   2707 O  O    . ILE   B 1 101 ? 27.356 44.723 90.856  1 53.83  ? 100 ILE   B O    1 2 
ATOM   2708 C  CB   . ILE   B 1 101 ? 26.986 44.061 87.542  1 54.17  ? 100 ILE   B CB   1 2 
ATOM   2709 C  CG1  . ILE   B 1 101 ? 25.778 43.902 86.624  1 54.63  ? 100 ILE   B CG1  1 2 
ATOM   2710 C  CG2  . ILE   B 1 101 ? 27.332 42.729 88.202  1 54.73  ? 100 ILE   B CG2  1 2 
ATOM   2711 C  CD1  . ILE   B 1 101 ? 26.08  43.08  85.402  1 55.76  ? 100 ILE   B CD1  1 2 
ATOM   2712 N  N    . TYR   B 1 102 ? 28.982 45.554 89.528  1 53.56  ? 101 TYR   B N    1 2 
ATOM   2713 C  CA   . TYR   B 1 102 ? 30.038 45.576 90.546  1 53.74  ? 101 TYR   B CA   1 2 
ATOM   2714 C  C    . TYR   B 1 102 ? 29.705 46.505 91.708  1 53.61  ? 101 TYR   B C    1 2 
ATOM   2715 O  O    . TYR   B 1 102 ? 29.983 46.184 92.86   1 52.94  ? 101 TYR   B O    1 2 
ATOM   2716 C  CB   . TYR   B 1 102 ? 31.398 45.955 89.927  1 53.78  ? 101 TYR   B CB   1 2 
ATOM   2717 C  CG   . TYR   B 1 102 ? 31.967 44.931 88.966  1 54.3   ? 101 TYR   B CG   1 2 
ATOM   2718 C  CD1  . TYR   B 1 102 ? 31.626 43.59  89.065  1 54.96  ? 101 TYR   B CD1  1 2 
ATOM   2719 C  CD2  . TYR   B 1 102 ? 32.888 45.295 87.995  1 55.25  ? 101 TYR   B CD2  1 2 
ATOM   2720 C  CE1  . TYR   B 1 102 ? 32.156 42.645 88.195  1 55.87  ? 101 TYR   B CE1  1 2 
ATOM   2721 C  CE2  . TYR   B 1 102 ? 33.433 44.356 87.126  1 56.03  ? 101 TYR   B CE2  1 2 
ATOM   2722 C  CZ   . TYR   B 1 102 ? 33.051 43.032 87.215  1 56.52  ? 101 TYR   B CZ   1 2 
ATOM   2723 O  OH   . TYR   B 1 102 ? 33.58  42.094 86.354  1 57.02  ? 101 TYR   B OH   1 2 
ATOM   2724 N  N    . ASN   B 1 103 ? 29.082 47.635 91.402  1 54.14  ? 102 ASN   B N    1 2 
ATOM   2725 C  CA   . ASN   B 1 103 ? 28.662 48.594 92.404  1 55.35  ? 102 ASN   B CA   1 2 
ATOM   2726 C  C    . ASN   B 1 103 ? 27.598 47.98  93.315  1 56.54  ? 102 ASN   B C    1 2 
ATOM   2727 O  O    . ASN   B 1 103 ? 27.632 48.186 94.519  1 56.61  ? 102 ASN   B O    1 2 
ATOM   2728 C  CB   . ASN   B 1 103 ? 28.104 49.834 91.717  1 56.74  ? 102 ASN   B CB   1 2 
ATOM   2729 C  CG   . ASN   B 1 103 ? 28.624 51.129 92.273  1 60.31  ? 102 ASN   B CG   1 2 
ATOM   2730 O  OD1  . ASN   B 1 103 ? 28.438 51.445 93.451  1 62     ? 102 ASN   B OD1  1 2 
ATOM   2731 N  ND2  . ASN   B 1 103 ? 29.27  51.92  91.427  1 60.68  ? 102 ASN   B ND2  1 2 
ATOM   2732 N  N    . SER   B 1 104 ? 26.67  47.215 92.746  1 57.75  ? 103 SER   B N    1 2 
ATOM   2733 C  CA   . SER   B 1 104 ? 25.594 46.575 93.5    1 59.66  ? 103 SER   B CA   1 2 
ATOM   2734 C  C    . SER   B 1 104 ? 26.024 45.297 94.219  1 61.26  ? 103 SER   B C    1 2 
ATOM   2735 O  O    . SER   B 1 104 ? 25.377 44.91  95.194  1 61.19  ? 103 SER   B O    1 2 
ATOM   2736 C  CB   . SER   B 1 104 ? 24.394 46.299 92.602  1 61.44  ? 103 SER   B CB   1 2 
ATOM   2737 O  OG   . SER   B 1 104 ? 23.869 47.505 92.073  1 64.2   ? 103 SER   B OG   1 2 
ATOM   2738 N  N    . VAL   B 1 105 ? 27.111 44.646 93.759  1 62.47  ? 104 VAL   B N    1 2 
ATOM   2739 C  CA   . VAL   B 1 105 ? 27.647 43.456 94.43   1 64.22  ? 104 VAL   B CA   1 2 
ATOM   2740 C  C    . VAL   B 1 105 ? 28.183 43.895 95.811  1 66.5   ? 104 VAL   B C    1 2 
ATOM   2741 O  O    . VAL   B 1 105 ? 27.895 43.247 96.823  1 66.79  ? 104 VAL   B O    1 2 
ATOM   2742 C  CB   . VAL   B 1 105 ? 28.722 42.728 93.574  1 64.65  ? 104 VAL   B CB   1 2 
ATOM   2743 C  CG1  . VAL   B 1 105 ? 29.581 41.794 94.419  1 65.09  ? 104 VAL   B CG1  1 2 
ATOM   2744 C  CG2  . VAL   B 1 105 ? 28.079 41.952 92.435  1 65.14  ? 104 VAL   B CG2  1 2 
ATOM   2745 N  N    . LYS   B 1 106 ? 28.885 45.042 95.861  1 67.75  ? 105 LYS   B N    1 2 
ATOM   2746 C  CA   . LYS   B 1 106 ? 29.39  45.589 97.112  1 69.34  ? 105 LYS   B CA   1 2 
ATOM   2747 C  C    . LYS   B 1 106 ? 28.25  45.989 98.06   1 70.2   ? 105 LYS   B C    1 2 
ATOM   2748 O  O    . LYS   B 1 106 ? 28.417 45.888 99.264  1 70.37  ? 105 LYS   B O    1 2 
ATOM   2749 C  CB   . LYS   B 1 106 ? 30.378 46.742 96.857  1 72.01  ? 105 LYS   B CB   1 2 
ATOM   2750 C  CG   . LYS   B 1 106 ? 31.696 46.278 96.222  1 76.99  ? 105 LYS   B CG   1 2 
ATOM   2751 C  CD   . LYS   B 1 106 ? 32.747 47.406 96.088  1 81.77  ? 105 LYS   B CD   1 2 
ATOM   2752 C  CE   . LYS   B 1 106 ? 33.786 47.112 95.016  1 84.97  ? 105 LYS   B CE   1 2 
ATOM   2753 N  NZ   . LYS   B 1 106 ? 34.795 48.2   94.883  1 86.56  ? 105 LYS   B NZ   1 2 
ATOM   2754 N  N    . GLN   B 1 107 ? 27.09  46.394 97.527  1 70.79  ? 106 GLN   B N    1 2 
ATOM   2755 C  CA   . GLN   B 1 107 ? 25.911 46.705 98.34   1 72     ? 106 GLN   B CA   1 2 
ATOM   2756 C  C    . GLN   B 1 107 ? 25.245 45.407 98.838  1 72.96  ? 106 GLN   B C    1 2 
ATOM   2757 O  O    . GLN   B 1 107 ? 24.671 45.38  99.93   1 73.33  ? 106 GLN   B O    1 2 
ATOM   2758 C  CB   . GLN   B 1 107 ? 24.896 47.539 97.546  1 74.14  ? 106 GLN   B CB   1 2 
ATOM   2759 C  CG   . GLN   B 1 107 ? 23.731 48.026 98.412  1 78.41  ? 106 GLN   B CG   1 2 
ATOM   2760 C  CD   . GLN   B 1 107 ? 22.525 48.567 97.666  1 83.65  ? 106 GLN   B CD   1 2 
ATOM   2761 O  OE1  . GLN   B 1 107 ? 21.466 48.808 98.268  1 86.22  ? 106 GLN   B OE1  1 2 
ATOM   2762 N  NE2  . GLN   B 1 107 ? 22.649 48.793 96.359  1 83.23  ? 106 GLN   B NE2  1 2 
ATOM   2763 N  N    . VAL   B 1 108 ? 25.319 44.334 98.038  1 73.31  ? 107 VAL   B N    1 2 
ATOM   2764 C  CA   . VAL   B 1 108 ? 24.811 43.018 98.402  1 74.07  ? 107 VAL   B CA   1 2 
ATOM   2765 C  C    . VAL   B 1 108 ? 25.636 42.494 99.587  1 75.01  ? 107 VAL   B C    1 2 
ATOM   2766 O  O    . VAL   B 1 108 ? 25.065 41.962 100.524 1 74.8   ? 107 VAL   B O    1 2 
ATOM   2767 C  CB   . VAL   B 1 108 ? 24.807 42.058 97.175  1 74.29  ? 107 VAL   B CB   1 2 
ATOM   2768 C  CG1  . VAL   B 1 108 ? 24.923 40.59  97.58   1 74.66  ? 107 VAL   B CG1  1 2 
ATOM   2769 C  CG2  . VAL   B 1 108 ? 23.568 42.277 96.325  1 74.51  ? 107 VAL   B CG2  1 2 
ATOM   2770 N  N    . LYS   B 1 109 ? 26.962 42.686 99.566  1 75.87  ? 108 LYS   B N    1 2 
ATOM   2771 C  CA   . LYS   B 1 109 ? 27.821 42.242 100.661 1 77.33  ? 108 LYS   B CA   1 2 
ATOM   2772 C  C    . LYS   B 1 109 ? 27.723 43.152 101.907 1 78.23  ? 108 LYS   B C    1 2 
ATOM   2773 O  O    . LYS   B 1 109 ? 27.9   42.684 103.036 1 78.03  ? 108 LYS   B O    1 2 
ATOM   2774 C  CB   . LYS   B 1 109 ? 29.262 42.056 100.17  1 79.84  ? 108 LYS   B CB   1 2 
ATOM   2775 C  CG   . LYS   B 1 109 ? 29.318 41.055 99.015  1 85.19  ? 108 LYS   B CG   1 2 
ATOM   2776 C  CD   . LYS   B 1 109 ? 30.726 40.661 98.599  1 90.54  ? 108 LYS   B CD   1 2 
ATOM   2777 C  CE   . LYS   B 1 109 ? 30.684 39.545 97.577  1 94.7   ? 108 LYS   B CE   1 2 
ATOM   2778 N  NZ   . LYS   B 1 109 ? 32.042 39.038 97.245  1 97.36  ? 108 LYS   B NZ   1 2 
ATOM   2779 N  N    . LYS   B 1 110 ? 27.383 44.433 101.702 1 78.74  ? 109 LYS   B N    1 2 
ATOM   2780 C  CA   . LYS   B 1 110 ? 27.176 45.379 102.792 1 79.49  ? 109 LYS   B CA   1 2 
ATOM   2781 C  C    . LYS   B 1 110 ? 25.729 45.311 103.36  1 80.72  ? 109 LYS   B C    1 2 
ATOM   2782 O  O    . LYS   B 1 110 ? 25.414 46.05  104.299 1 81.03  ? 109 LYS   B O    1 2 
ATOM   2783 C  CB   . LYS   B 1 110 ? 27.528 46.814 102.345 1 80.73  ? 109 LYS   B CB   1 2 
ATOM   2784 C  CG   . LYS   B 1 110 ? 28.305 47.614 103.38  1 84.63  ? 109 LYS   B CG   1 2 
ATOM   2785 C  CD   . LYS   B 1 110 ? 27.451 48.701 104.013 1 89.02  ? 109 LYS   B CD   1 2 
ATOM   2786 C  CE   . LYS   B 1 110 ? 27.874 49.054 105.427 1 92.02  ? 109 LYS   B CE   1 2 
ATOM   2787 N  NZ   . LYS   B 1 110 ? 27.219 48.19  106.449 1 93.49  ? 109 LYS   B NZ   1 2 
ATOM   2788 N  N    . GLU   B 1 111 ? 24.855 44.423 102.827 1 81.19  ? 110 GLU   B N    1 2 
ATOM   2789 C  CA   . GLU   B 1 111 ? 23.487 44.308 103.336 1 82.09  ? 110 GLU   B CA   1 2 
ATOM   2790 C  C    . GLU   B 1 111 ? 23.033 42.871 103.596 1 81.87  ? 110 GLU   B C    1 2 
ATOM   2791 O  O    . GLU   B 1 111 ? 22.573 42.567 104.693 1 82.28  ? 110 GLU   B O    1 2 
ATOM   2792 C  CB   . GLU   B 1 111 ? 22.488 45.04  102.433 1 85.58  ? 110 GLU   B CB   1 2 
ATOM   2793 C  CG   . GLU   B 1 111 ? 22.146 46.421 102.954 1 93.14  ? 110 GLU   B CG   1 2 
ATOM   2794 C  CD   . GLU   B 1 111 ? 20.729 46.865 102.661 1 101.84 ? 110 GLU   B CD   1 2 
ATOM   2795 O  OE1  . GLU   B 1 111 ? 20.062 47.359 103.602 1 103.71 ? 110 GLU   B OE1  1 2 
ATOM   2796 O  OE2  . GLU   B 1 111 ? 20.289 46.72  101.494 1 104.15 ? 110 GLU   B OE2  1 2 
ATOM   2797 N  N    . VAL   B 1 112 ? 23.152 41.997 102.605 1 81.18  ? 111 VAL   B N    1 2 
ATOM   2798 C  CA   . VAL   B 1 112 ? 22.739 40.607 102.732 1 81.17  ? 111 VAL   B CA   1 2 
ATOM   2799 C  C    . VAL   B 1 112 ? 23.912 39.703 103.147 1 81.33  ? 111 VAL   B C    1 2 
ATOM   2800 O  O    . VAL   B 1 112 ? 23.782 38.919 104.092 1 81.74  ? 111 VAL   B O    1 2 
ATOM   2801 C  CB   . VAL   B 1 112 ? 22.068 40.136 101.424 1 81.84  ? 111 VAL   B CB   1 2 
ATOM   2802 C  CG1  . VAL   B 1 112 ? 21.801 38.637 101.452 1 82.46  ? 111 VAL   B CG1  1 2 
ATOM   2803 C  CG2  . VAL   B 1 112 ? 20.783 40.916 101.166 1 82.15  ? 111 VAL   B CG2  1 2 
ATOM   2804 N  N    . GLY   B 1 113 ? 25.044 39.831 102.455 1 80.95  ? 112 GLY   B N    1 2 
ATOM   2805 C  CA   . GLY   B 1 113 ? 26.245 39.046 102.727 1 80.87  ? 112 GLY   B CA   1 2 
ATOM   2806 C  C    . GLY   B 1 113 ? 26.885 38.523 101.457 1 80.42  ? 112 GLY   B C    1 2 
ATOM   2807 O  O    . GLY   B 1 113 ? 26.861 39.203 100.434 1 80.6   ? 112 GLY   B O    1 2 
ATOM   2808 N  N    . ASP   B 1 114 ? 27.45  37.306 101.497 1 79.74  ? 113 ASP   B N    1 2 
ATOM   2809 C  CA   . ASP   B 1 114 ? 28.093 36.708 100.317 1 79.51  ? 113 ASP   B CA   1 2 
ATOM   2810 C  C    . ASP   B 1 114 ? 27.129 35.756 99.598  1 78.22  ? 113 ASP   B C    1 2 
ATOM   2811 O  O    . ASP   B 1 114 ? 26.7   34.787 100.205 1 78.38  ? 113 ASP   B O    1 2 
ATOM   2812 C  CB   . ASP   B 1 114 ? 29.378 35.971 100.736 1 82.01  ? 113 ASP   B CB   1 2 
ATOM   2813 C  CG   . ASP   B 1 114 ? 30.351 36.832 101.536 1 87.76  ? 113 ASP   B CG   1 2 
ATOM   2814 O  OD1  . ASP   B 1 114 ? 30.458 38.04  101.239 1 88.63  ? 113 ASP   B OD1  1 2 
ATOM   2815 O  OD2  . ASP   B 1 114 ? 31.009 36.291 102.459 1 90.22  ? 113 ASP   B OD2  1 2 
ATOM   2816 N  N    . VAL   B 1 115 ? 26.773 36.026 98.33   1 76.78  ? 114 VAL   B N    1 2 
ATOM   2817 C  CA   . VAL   B 1 115 ? 25.812 35.185 97.606  1 76.02  ? 114 VAL   B CA   1 2 
ATOM   2818 C  C    . VAL   B 1 115 ? 26.284 33.732 97.483  1 75.38  ? 114 VAL   B C    1 2 
ATOM   2819 O  O    . VAL   B 1 115 ? 27.467 33.512 97.247  1 75.76  ? 114 VAL   B O    1 2 
ATOM   2820 C  CB   . VAL   B 1 115 ? 25.441 35.806 96.247  1 76.22  ? 114 VAL   B CB   1 2 
ATOM   2821 C  CG1  . VAL   B 1 115 ? 24.574 34.869 95.422  1 76.71  ? 114 VAL   B CG1  1 2 
ATOM   2822 C  CG2  . VAL   B 1 115 ? 24.74  37.14  96.444  1 76.5   ? 114 VAL   B CG2  1 2 
ATOM   2823 N  N    . THR   B 1 116 ? 25.379 32.743 97.716  1 74.18  ? 115 THR   B N    1 2 
ATOM   2824 C  CA   . THR   B 1 116 ? 25.728 31.316 97.659  1 73.4   ? 115 THR   B CA   1 2 
ATOM   2825 C  C    . THR   B 1 116 ? 25.112 30.556 96.487  1 71.83  ? 115 THR   B C    1 2 
ATOM   2826 O  O    . THR   B 1 116 ? 25.519 29.426 96.237  1 71.9   ? 115 THR   B O    1 2 
ATOM   2827 C  CB   . THR   B 1 116 ? 25.409 30.603 98.973  1 75.21  ? 115 THR   B CB   1 2 
ATOM   2828 O  OG1  . THR   B 1 116 ? 23.999 30.385 99.099  1 76.43  ? 115 THR   B OG1  1 2 
ATOM   2829 C  CG2  . THR   B 1 116 ? 25.945 31.34  100.178 1 76.03  ? 115 THR   B CG2  1 2 
ATOM   2830 N  N    . ILE   B 1 117 ? 24.1   31.135 95.813  1 70.21  ? 116 ILE   B N    1 2 
ATOM   2831 C  CA   . ILE   B 1 117 ? 23.427 30.545 94.648  1 68.62  ? 116 ILE   B CA   1 2 
ATOM   2832 C  C    . ILE   B 1 117 ? 23.131 31.695 93.695  1 66.97  ? 116 ILE   B C    1 2 
ATOM   2833 O  O    . ILE   B 1 117 ? 22.504 32.666 94.103  1 67.04  ? 116 ILE   B O    1 2 
ATOM   2834 C  CB   . ILE   B 1 117 ? 22.105 29.796 95.014  1 69.07  ? 116 ILE   B CB   1 2 
ATOM   2835 C  CG1  . ILE   B 1 117 ? 22.351 28.536 95.87   1 70.09  ? 116 ILE   B CG1  1 2 
ATOM   2836 C  CG2  . ILE   B 1 117 ? 21.299 29.445 93.762  1 69.49  ? 116 ILE   B CG2  1 2 
ATOM   2837 C  CD1  . ILE   B 1 117 ? 21.072 27.903 96.444  1 71.22  ? 116 ILE   B CD1  1 2 
ATOM   2838 N  N    . LEU   B 1 118 ? 23.564 31.596 92.434  1 65.31  ? 117 LEU   B N    1 2 
ATOM   2839 C  CA   . LEU   B 1 118 ? 23.299 32.639 91.445  1 64.17  ? 117 LEU   B CA   1 2 
ATOM   2840 C  C    . LEU   B 1 118 ? 22.359 32.13  90.353  1 62.59  ? 117 LEU   B C    1 2 
ATOM   2841 O  O    . LEU   B 1 118 ? 22.522 31.022 89.869  1 62.47  ? 117 LEU   B O    1 2 
ATOM   2842 C  CB   . LEU   B 1 118 ? 24.617 33.143 90.828  1 64.41  ? 117 LEU   B CB   1 2 
ATOM   2843 C  CG   . LEU   B 1 118 ? 24.511 34.194 89.722  1 65.57  ? 117 LEU   B CG   1 2 
ATOM   2844 C  CD1  . LEU   B 1 118 ? 23.811 35.44  90.215  1 66.05  ? 117 LEU   B CD1  1 2 
ATOM   2845 C  CD2  . LEU   B 1 118 ? 25.876 34.567 89.215  1 66.16  ? 117 LEU   B CD2  1 2 
ATOM   2846 N  N    . VAL   B 1 119 ? 21.358 32.926 89.992  1 61.27  ? 118 VAL   B N    1 2 
ATOM   2847 C  CA   . VAL   B 1 119 ? 20.408 32.592 88.942  1 60.54  ? 118 VAL   B CA   1 2 
ATOM   2848 C  C    . VAL   B 1 119 ? 20.485 33.684 87.864  1 59.21  ? 118 VAL   B C    1 2 
ATOM   2849 O  O    . VAL   B 1 119 ? 19.831 34.723 87.986  1 58.91  ? 118 VAL   B O    1 2 
ATOM   2850 C  CB   . VAL   B 1 119 ? 18.97  32.421 89.499  1 61.26  ? 118 VAL   B CB   1 2 
ATOM   2851 C  CG1  . VAL   B 1 119 ? 17.973 32.125 88.381  1 61.88  ? 118 VAL   B CG1  1 2 
ATOM   2852 C  CG2  . VAL   B 1 119 ? 18.922 31.334 90.565  1 61.52  ? 118 VAL   B CG2  1 2 
ATOM   2853 N  N    . ASN   B 1 120 ? 21.339 33.461 86.844  1 58.27  ? 119 ASN   B N    1 2 
ATOM   2854 C  CA   . ASN   B 1 120 ? 21.535 34.358 85.702  1 57.95  ? 119 ASN   B CA   1 2 
ATOM   2855 C  C    . ASN   B 1 120 ? 20.325 34.206 84.776  1 57     ? 119 ASN   B C    1 2 
ATOM   2856 O  O    . ASN   B 1 120 ? 20.417 33.57  83.729  1 56.72  ? 119 ASN   B O    1 2 
ATOM   2857 C  CB   . ASN   B 1 120 ? 22.824 33.994 84.95   1 59.33  ? 119 ASN   B CB   1 2 
ATOM   2858 C  CG   . ASN   B 1 120 ? 24.097 34.337 85.671  1 62.92  ? 119 ASN   B CG   1 2 
ATOM   2859 O  OD1  . ASN   B 1 120 ? 24.815 33.458 86.143  1 64.45  ? 119 ASN   B OD1  1 2 
ATOM   2860 N  ND2  . ASN   B 1 120 ? 24.417 35.62  85.757  1 63.44  ? 119 ASN   B ND2  1 2 
ATOM   2861 N  N    . ASN   B 1 121 ? 19.174 34.742 85.195  1 56.5   ? 120 ASN   B N    1 2 
ATOM   2862 C  CA   . ASN   B 1 121 ? 17.932 34.626 84.441  1 56.45  ? 120 ASN   B CA   1 2 
ATOM   2863 C  C    . ASN   B 1 121 ? 17.813 35.704 83.368  1 55.75  ? 120 ASN   B C    1 2 
ATOM   2864 O  O    . ASN   B 1 121 ? 17.668 35.357 82.202  1 55.4   ? 120 ASN   B O    1 2 
ATOM   2865 C  CB   . ASN   B 1 121 ? 16.713 34.612 85.386  1 57.76  ? 120 ASN   B CB   1 2 
ATOM   2866 C  CG   . ASN   B 1 121 ? 15.376 34.475 84.71   1 61.32  ? 120 ASN   B CG   1 2 
ATOM   2867 O  OD1  . ASN   B 1 121 ? 14.906 33.365 84.462  1 62.79  ? 120 ASN   B OD1  1 2 
ATOM   2868 N  ND2  . ASN   B 1 121 ? 14.704 35.594 84.438  1 61.92  ? 120 ASN   B ND2  1 2 
ATOM   2869 N  N    . ALA   B 1 122 ? 17.943 37.004 83.746  1 55.24  ? 121 ALA   B N    1 2 
ATOM   2870 C  CA   . ALA   B 1 122 ? 17.831 38.185 82.878  1 55.17  ? 121 ALA   B CA   1 2 
ATOM   2871 C  C    . ALA   B 1 122 ? 18.195 37.947 81.418  1 55.85  ? 121 ALA   B C    1 2 
ATOM   2872 O  O    . ALA   B 1 122 ? 19.142 37.209 81.118  1 56.12  ? 121 ALA   B O    1 2 
ATOM   2873 C  CB   . ALA   B 1 122 ? 18.644 39.344 83.433  1 54.88  ? 121 ALA   B CB   1 2 
ATOM   2874 N  N    . GLY   B 1 123 ? 17.39  38.525 80.53   1 55.66  ? 122 GLY   B N    1 2 
ATOM   2875 C  CA   . GLY   B 1 123 ? 17.568 38.409 79.094  1 55.33  ? 122 GLY   B CA   1 2 
ATOM   2876 C  C    . GLY   B 1 123 ? 16.791 39.457 78.332  1 54.96  ? 122 GLY   B C    1 2 
ATOM   2877 O  O    . GLY   B 1 123 ? 15.852 40.059 78.866  1 54.72  ? 122 GLY   B O    1 2 
ATOM   2878 N  N    . THR   B 1 124 ? 17.187 39.681 77.067  1 54.73  ? 123 THR   B N    1 2 
ATOM   2879 C  CA   . THR   B 1 124 ? 16.519 40.612 76.161  1 54.72  ? 123 THR   B CA   1 2 
ATOM   2880 C  C    . THR   B 1 124 ? 16.48  39.997 74.75   1 55.17  ? 123 THR   B C    1 2 
ATOM   2881 O  O    . THR   B 1 124 ? 17.385 39.252 74.366  1 54.97  ? 123 THR   B O    1 2 
ATOM   2882 C  CB   . THR   B 1 124 ? 17.11  42.031 76.26   1 55.13  ? 123 THR   B CB   1 2 
ATOM   2883 O  OG1  . THR   B 1 124 ? 16.106 42.995 75.938  1 55.57  ? 123 THR   B OG1  1 2 
ATOM   2884 C  CG2  . THR   B 1 124 ? 18.333 42.226 75.391  1 55.31  ? 123 THR   B CG2  1 2 
ATOM   2885 N  N    . VAL   B 1 125 ? 15.387 40.235 74.012  1 55.69  ? 124 VAL   B N    1 2 
ATOM   2886 C  CA   . VAL   B 1 125 ? 15.229 39.69  72.66   1 56.57  ? 124 VAL   B CA   1 2 
ATOM   2887 C  C    . VAL   B 1 125 ? 14.705 40.747 71.71   1 57.97  ? 124 VAL   B C    1 2 
ATOM   2888 O  O    . VAL   B 1 125 ? 13.858 41.543 72.093  1 58.44  ? 124 VAL   B O    1 2 
ATOM   2889 C  CB   . VAL   B 1 125 ? 14.336 38.43  72.643  1 56.88  ? 124 VAL   B CB   1 2 
ATOM   2890 C  CG1  . VAL   B 1 125 ? 12.859 38.786 72.745  1 57.49  ? 124 VAL   B CG1  1 2 
ATOM   2891 C  CG2  . VAL   B 1 125 ? 14.593 37.598 71.408  1 57.06  ? 124 VAL   B CG2  1 2 
ATOM   2892 N  N    . TYR   B 1 126 ? 15.203 40.77  70.479  1 58.55  ? 125 TYR   B N    1 2 
ATOM   2893 C  CA   . TYR   B 1 126 ? 14.747 41.721 69.472  1 59.66  ? 125 TYR   B CA   1 2 
ATOM   2894 C  C    . TYR   B 1 126 ? 14.491 40.94  68.199  1 60.5   ? 125 TYR   B C    1 2 
ATOM   2895 O  O    . TYR   B 1 126 ? 15.347 40.9   67.316  1 61.15  ? 125 TYR   B O    1 2 
ATOM   2896 C  CB   . TYR   B 1 126 ? 15.805 42.81  69.279  1 59.99  ? 125 TYR   B CB   1 2 
ATOM   2897 C  CG   . TYR   B 1 126 ? 15.995 43.645 70.533  1 61.15  ? 125 TYR   B CG   1 2 
ATOM   2898 C  CD1  . TYR   B 1 126 ? 14.983 44.467 71.002  1 62.33  ? 125 TYR   B CD1  1 2 
ATOM   2899 C  CD2  . TYR   B 1 126 ? 17.152 43.542 71.296  1 61.84  ? 125 TYR   B CD2  1 2 
ATOM   2900 C  CE1  . TYR   B 1 126 ? 15.13  45.196 72.175  1 63.11  ? 125 TYR   B CE1  1 2 
ATOM   2901 C  CE2  . TYR   B 1 126 ? 17.325 44.298 72.449  1 62.6   ? 125 TYR   B CE2  1 2 
ATOM   2902 C  CZ   . TYR   B 1 126 ? 16.308 45.121 72.888  1 63.73  ? 125 TYR   B CZ   1 2 
ATOM   2903 O  OH   . TYR   B 1 126 ? 16.448 45.859 74.037  1 65.4   ? 125 TYR   B OH   1 2 
ATOM   2904 N  N    . PRO   B 1 127 ? 13.342 40.24  68.127  1 60.33  ? 126 PRO   B N    1 2 
ATOM   2905 C  CA   . PRO   B 1 127 ? 13.083 39.371 66.967  1 60.43  ? 126 PRO   B CA   1 2 
ATOM   2906 C  C    . PRO   B 1 127 ? 13.05  40.052 65.601  1 61.19  ? 126 PRO   B C    1 2 
ATOM   2907 O  O    . PRO   B 1 127 ? 12.098 40.769 65.31   1 62.21  ? 126 PRO   B O    1 2 
ATOM   2908 C  CB   . PRO   B 1 127 ? 11.73  38.724 67.304  1 60.86  ? 126 PRO   B CB   1 2 
ATOM   2909 C  CG   . PRO   B 1 127 ? 11.559 38.884 68.778  1 61.16  ? 126 PRO   B CG   1 2 
ATOM   2910 C  CD   . PRO   B 1 127 ? 12.254 40.158 69.125  1 59.64  ? 126 PRO   B CD   1 2 
ATOM   2911 N  N    . ALA   B 1 128 ? 14.063 39.796 64.739  1 60.42  ? 127 ALA   B N    1 2 
ATOM   2912 C  CA   . ALA   B 1 128 ? 14.158 40.342 63.374  1 59.88  ? 127 ALA   B CA   1 2 
ATOM   2913 C  C    . ALA   B 1 128 ? 15.207 39.597 62.526  1 59.79  ? 127 ALA   B C    1 2 
ATOM   2914 O  O    . ALA   B 1 128 ? 16.104 38.962 63.078  1 59.78  ? 127 ALA   B O    1 2 
ATOM   2915 C  CB   . ALA   B 1 128 ? 14.504 41.828 63.421  1 59.75  ? 127 ALA   B CB   1 2 
ATOM   2916 N  N    . ASP   B 1 129 ? 15.11  39.687 61.181  1 59.67  ? 128 ASP   B N    1 2 
ATOM   2917 C  CA   . ASP   B 1 129 ? 16.116 39.074 60.308  1 59.81  ? 128 ASP   B CA   1 2 
ATOM   2918 C  C    . ASP   B 1 129 ? 17.433 39.839 60.414  1 58.95  ? 128 ASP   B C    1 2 
ATOM   2919 O  O    . ASP   B 1 129 ? 17.427 41.011 60.787  1 59.25  ? 128 ASP   B O    1 2 
ATOM   2920 C  CB   . ASP   B 1 129 ? 15.651 38.992 58.85   1 62.71  ? 128 ASP   B CB   1 2 
ATOM   2921 C  CG   . ASP   B 1 129 ? 15.301 40.328 58.244  1 68.64  ? 128 ASP   B CG   1 2 
ATOM   2922 O  OD1  . ASP   B 1 129 ? 14.508 41.071 58.873  1 69.92  ? 128 ASP   B OD1  1 2 
ATOM   2923 O  OD2  . ASP   B 1 129 ? 15.806 40.628 57.123  1 70.27  ? 128 ASP   B OD2  1 2 
ATOM   2924 N  N    . LEU   B 1 130 ? 18.564 39.194 60.093  1 57.71  ? 129 LEU   B N    1 2 
ATOM   2925 C  CA   . LEU   B 1 130 ? 19.879 39.82  60.248  1 56.8   ? 129 LEU   B CA   1 2 
ATOM   2926 C  C    . LEU   B 1 130 ? 20.021 41.17  59.588  1 56.34  ? 129 LEU   B C    1 2 
ATOM   2927 O  O    . LEU   B 1 130 ? 20.817 41.983 60.05   1 56.6   ? 129 LEU   B O    1 2 
ATOM   2928 C  CB   . LEU   B 1 130 ? 21.01  38.906 59.789  1 56.4   ? 129 LEU   B CB   1 2 
ATOM   2929 C  CG   . LEU   B 1 130 ? 22.313 39.141 60.522  1 57.09  ? 129 LEU   B CG   1 2 
ATOM   2930 C  CD1  . LEU   B 1 130 ? 22.512 38.105 61.587  1 57.51  ? 129 LEU   B CD1  1 2 
ATOM   2931 C  CD2  . LEU   B 1 130 ? 23.472 39.164 59.568  1 57.55  ? 129 LEU   B CD2  1 2 
ATOM   2932 N  N    . LEU   B 1 131 ? 19.224 41.44  58.552  1 55.53  ? 130 LEU   B N    1 2 
ATOM   2933 C  CA   . LEU   B 1 131 ? 19.309 42.71  57.838  1 55.16  ? 130 LEU   B CA   1 2 
ATOM   2934 C  C    . LEU   B 1 131 ? 18.367 43.802 58.386  1 54.65  ? 130 LEU   B C    1 2 
ATOM   2935 O  O    . LEU   B 1 131 ? 18.576 44.981 58.1    1 54.64  ? 130 LEU   B O    1 2 
ATOM   2936 C  CB   . LEU   B 1 131 ? 19.111 42.481 56.335  1 55.08  ? 130 LEU   B CB   1 2 
ATOM   2937 C  CG   . LEU   B 1 131 ? 20.106 41.503 55.725  1 56.04  ? 130 LEU   B CG   1 2 
ATOM   2938 C  CD1  . LEU   B 1 131 ? 19.732 41.173 54.313  1 56.83  ? 130 LEU   B CD1  1 2 
ATOM   2939 C  CD2  . LEU   B 1 131 ? 21.526 42.037 55.802  1 56.33  ? 130 LEU   B CD2  1 2 
ATOM   2940 N  N    . SER   B 1 132 ? 17.364 43.421 59.196  1 54.03  ? 131 SER   B N    1 2 
ATOM   2941 C  CA   . SER   B 1 132 ? 16.451 44.381 59.822  1 53.99  ? 131 SER   B CA   1 2 
ATOM   2942 C  C    . SER   B 1 132 ? 16.753 44.633 61.305  1 52.97  ? 131 SER   B C    1 2 
ATOM   2943 O  O    . SER   B 1 132 ? 16.162 45.536 61.889  1 53.36  ? 131 SER   B O    1 2 
ATOM   2944 C  CB   . SER   B 1 132 ? 14.992 43.976 59.631  1 56.28  ? 131 SER   B CB   1 2 
ATOM   2945 O  OG   . SER   B 1 132 ? 14.627 44.037 58.256  1 60.21  ? 131 SER   B OG   1 2 
ATOM   2946 N  N    . THR   B 1 133 ? 17.66  43.845 61.911  1 51.48  ? 132 THR   B N    1 2 
ATOM   2947 C  CA   . THR   B 1 133 ? 18.072 44.008 63.301  1 50.55  ? 132 THR   B CA   1 2 
ATOM   2948 C  C    . THR   B 1 133 ? 18.906 45.256 63.436  1 49.16  ? 132 THR   B C    1 2 
ATOM   2949 O  O    . THR   B 1 133 ? 19.752 45.512 62.591  1 49.44  ? 132 THR   B O    1 2 
ATOM   2950 C  CB   . THR   B 1 133 ? 18.955 42.845 63.748  1 51.94  ? 132 THR   B CB   1 2 
ATOM   2951 O  OG1  . THR   B 1 133 ? 19.921 42.552 62.735  1 52.84  ? 132 THR   B OG1  1 2 
ATOM   2952 C  CG2  . THR   B 1 133 ? 18.157 41.612 64.134  1 52.56  ? 132 THR   B CG2  1 2 
ATOM   2953 N  N    . LYS   B 1 134 ? 18.706 46.012 64.509  1 47.62  ? 133 LYS   B N    1 2 
ATOM   2954 C  CA   . LYS   B 1 134 ? 19.47  47.23  64.759  1 46.73  ? 133 LYS   B CA   1 2 
ATOM   2955 C  C    . LYS   B 1 134 ? 20.768 46.886 65.503  1 45.27  ? 133 LYS   B C    1 2 
ATOM   2956 O  O    . LYS   B 1 134 ? 20.781 45.971 66.32   1 45.34  ? 133 LYS   B O    1 2 
ATOM   2957 C  CB   . LYS   B 1 134 ? 18.634 48.212 65.583  1 48.96  ? 133 LYS   B CB   1 2 
ATOM   2958 C  CG   . LYS   B 1 134 ? 17.222 48.423 65.05   1 53.41  ? 133 LYS   B CG   1 2 
ATOM   2959 C  CD   . LYS   B 1 134 ? 16.34  49.129 66.081  1 57.12  ? 133 LYS   B CD   1 2 
ATOM   2960 C  CE   . LYS   B 1 134 ? 14.883 48.765 65.901  1 60.26  ? 133 LYS   B CE   1 2 
ATOM   2961 N  NZ   . LYS   B 1 134 ? 14.265 49.398 64.693  1 61.96  ? 133 LYS   B NZ   1 2 
ATOM   2962 N  N    . ASP   B 1 135 ? 21.86  47.606 65.227  1 43.8   ? 134 ASP   B N    1 2 
ATOM   2963 C  CA   . ASP   B 1 135 ? 23.151 47.334 65.866  1 42.61  ? 134 ASP   B CA   1 2 
ATOM   2964 C  C    . ASP   B 1 135 ? 23.097 47.447 67.364  1 41.95  ? 134 ASP   B C    1 2 
ATOM   2965 O  O    . ASP   B 1 135 ? 23.772 46.69  68.058  1 41.87  ? 134 ASP   B O    1 2 
ATOM   2966 C  CB   . ASP   B 1 135 ? 24.245 48.262 65.326  1 42.75  ? 134 ASP   B CB   1 2 
ATOM   2967 C  CG   . ASP   B 1 135 ? 24.659 47.945 63.917  1 44.05  ? 134 ASP   B CG   1 2 
ATOM   2968 O  OD1  . ASP   B 1 135 ? 24.53  46.775 63.511  1 43.16  ? 134 ASP   B OD1  1 2 
ATOM   2969 O  OD2  . ASP   B 1 135 ? 25.092 48.867 63.214  1 46.07  ? 134 ASP   B OD2  1 2 
ATOM   2970 N  N    . GLU   B 1 136 ? 22.307 48.401 67.86   1 41.6   ? 135 GLU   B N    1 2 
ATOM   2971 C  CA   . GLU   B 1 136 ? 22.113 48.668 69.284  1 41.79  ? 135 GLU   B CA   1 2 
ATOM   2972 C  C    . GLU   B 1 136 ? 21.443 47.469 69.958  1 41.16  ? 135 GLU   B C    1 2 
ATOM   2973 O  O    . GLU   B 1 136 ? 21.795 47.123 71.085  1 41.54  ? 135 GLU   B O    1 2 
ATOM   2974 C  CB   . GLU   B 1 136 ? 21.278 49.95  69.483  1 45.12  ? 135 GLU   B CB   1 2 
ATOM   2975 C  CG   . GLU   B 1 136 ? 21.739 51.149 68.658  1 53     ? 135 GLU   B CG   1 2 
ATOM   2976 C  CD   . GLU   B 1 136 ? 21.226 51.181 67.228  1 63.22  ? 135 GLU   B CD   1 2 
ATOM   2977 O  OE1  . GLU   B 1 136 ? 20.179 50.543 66.974  1 66.05  ? 135 GLU   B OE1  1 2 
ATOM   2978 O  OE2  . GLU   B 1 136 ? 21.869 51.824 66.362  1 65.66  ? 135 GLU   B OE2  1 2 
ATOM   2979 N  N    . GLU   B 1 137 ? 20.494 46.833 69.252  1 40.23  ? 136 GLU   B N    1 2 
ATOM   2980 C  CA   . GLU   B 1 137 ? 19.773 45.652 69.697  1 40.2   ? 136 GLU   B CA   1 2 
ATOM   2981 C  C    . GLU   B 1 137 ? 20.744 44.493 69.856  1 39.84  ? 136 GLU   B C    1 2 
ATOM   2982 O  O    . GLU   B 1 137 ? 20.658 43.771 70.841  1 39.79  ? 136 GLU   B O    1 2 
ATOM   2983 C  CB   . GLU   B 1 137 ? 18.673 45.275 68.684  1 42.96  ? 136 GLU   B CB   1 2 
ATOM   2984 C  CG   . GLU   B 1 137 ? 17.488 46.227 68.644  1 48.55  ? 136 GLU   B CG   1 2 
ATOM   2985 C  CD   . GLU   B 1 137 ? 16.365 45.818 67.702  1 54.74  ? 136 GLU   B CD   1 2 
ATOM   2986 O  OE1  . GLU   B 1 137 ? 16.662 45.28  66.609  1 54.56  ? 136 GLU   B OE1  1 2 
ATOM   2987 O  OE2  . GLU   B 1 137 ? 15.184 46.027 68.063  1 57.17  ? 136 GLU   B OE2  1 2 
ATOM   2988 N  N    . ILE   B 1 138 ? 21.665 44.313 68.893  1 39.54  ? 137 ILE   B N    1 2 
ATOM   2989 C  CA   . ILE   B 1 138 ? 22.667 43.246 68.927  1 39.6   ? 137 ILE   B CA   1 2 
ATOM   2990 C  C    . ILE   B 1 138 ? 23.593 43.428 70.121  1 39.79  ? 137 ILE   B C    1 2 
ATOM   2991 O  O    . ILE   B 1 138 ? 23.859 42.478 70.857  1 39.9   ? 137 ILE   B O    1 2 
ATOM   2992 C  CB   . ILE   B 1 138 ? 23.457 43.219 67.61   1 39.75  ? 137 ILE   B CB   1 2 
ATOM   2993 C  CG1  . ILE   B 1 138 ? 22.525 42.96  66.44   1 40.62  ? 137 ILE   B CG1  1 2 
ATOM   2994 C  CG2  . ILE   B 1 138 ? 24.571 42.194 67.673  1 40.11  ? 137 ILE   B CG2  1 2 
ATOM   2995 C  CD1  . ILE   B 1 138 ? 23.04  43.484 65.145  1 42.06  ? 137 ILE   B CD1  1 2 
ATOM   2996 N  N    . THR   B 1 139 ? 24.038 44.669 70.338  1 39.65  ? 138 THR   B N    1 2 
ATOM   2997 C  CA   . THR   B 1 139 ? 24.912 45.048 71.433  1 39.72  ? 138 THR   B CA   1 2 
ATOM   2998 C  C    . THR   B 1 139 ? 24.21  44.756 72.764  1 39.63  ? 138 THR   B C    1 2 
ATOM   2999 O  O    . THR   B 1 139 ? 24.749 43.991 73.561  1 39.8   ? 138 THR   B O    1 2 
ATOM   3000 C  CB   . THR   B 1 139 ? 25.395 46.491 71.201  1 41.57  ? 138 THR   B CB   1 2 
ATOM   3001 O  OG1  . THR   B 1 139 ? 26.503 46.457 70.298  1 43.71  ? 138 THR   B OG1  1 2 
ATOM   3002 C  CG2  . THR   B 1 139 ? 25.813 47.189 72.448  1 41.89  ? 138 THR   B CG2  1 2 
ATOM   3003 N  N    . LYS   B 1 140 ? 22.961 45.248 72.95   1 39.08  ? 139 LYS   B N    1 2 
ATOM   3004 C  CA   . LYS   B 1 140 ? 22.16  45.02  74.165  1 38.75  ? 139 LYS   B CA   1 2 
ATOM   3005 C  C    . LYS   B 1 140 ? 21.864 43.548 74.395  1 38.84  ? 139 LYS   B C    1 2 
ATOM   3006 O  O    . LYS   B 1 140 ? 21.807 43.114 75.534  1 38.88  ? 139 LYS   B O    1 2 
ATOM   3007 C  CB   . LYS   B 1 140 ? 20.842 45.805 74.129  1 39.68  ? 139 LYS   B CB   1 2 
ATOM   3008 C  CG   . LYS   B 1 140 ? 20.868 47.087 74.946  1 41.82  ? 139 LYS   B CG   1 2 
ATOM   3009 C  CD   . LYS   B 1 140 ? 19.455 47.519 75.351  1 45.48  ? 139 LYS   B CD   1 2 
ATOM   3010 C  CE   . LYS   B 1 140 ? 19.436 48.785 76.185  1 49.41  ? 139 LYS   B CE   1 2 
ATOM   3011 N  NZ   . LYS   B 1 140 ? 18.155 48.97  76.939  1 51.42  ? 139 LYS   B NZ   1 2 
ATOM   3012 N  N    . THR   B 1 141 ? 21.701 42.766 73.319  1 39.01  ? 140 THR   B N    1 2 
ATOM   3013 C  CA   . THR   B 1 141 ? 21.464 41.321 73.389  1 39.33  ? 140 THR   B CA   1 2 
ATOM   3014 C  C    . THR   B 1 141 ? 22.657 40.673 74.099  1 39.63  ? 140 THR   B C    1 2 
ATOM   3015 O  O    . THR   B 1 141 ? 22.49  40.105 75.169  1 39.9   ? 140 THR   B O    1 2 
ATOM   3016 C  CB   . THR   B 1 141 ? 21.213 40.723 71.96   1 40.29  ? 140 THR   B CB   1 2 
ATOM   3017 O  OG1  . THR   B 1 141 ? 19.902 41.051 71.514  1 40.67  ? 140 THR   B OG1  1 2 
ATOM   3018 C  CG2  . THR   B 1 141 ? 21.382 39.223 71.917  1 40.82  ? 140 THR   B CG2  1 2 
ATOM   3019 N  N    . PHE   B 1 142 ? 23.867 40.903 73.589  1 39.59  ? 141 PHE   B N    1 2 
ATOM   3020 C  CA   . PHE   B 1 142 ? 25.065 40.323 74.161  1 40.04  ? 141 PHE   B CA   1 2 
ATOM   3021 C  C    . PHE   B 1 142 ? 25.41  40.871 75.519  1 38.75  ? 141 PHE   B C    1 2 
ATOM   3022 O  O    . PHE   B 1 142 ? 25.877 40.124 76.364  1 38.63  ? 141 PHE   B O    1 2 
ATOM   3023 C  CB   . PHE   B 1 142 ? 26.233 40.457 73.191  1 41.24  ? 141 PHE   B CB   1 2 
ATOM   3024 C  CG   . PHE   B 1 142 ? 26.289 39.285 72.248  1 43.35  ? 141 PHE   B CG   1 2 
ATOM   3025 C  CD1  . PHE   B 1 142 ? 25.372 39.161 71.216  1 45.01  ? 141 PHE   B CD1  1 2 
ATOM   3026 C  CD2  . PHE   B 1 142 ? 27.222 38.281 72.425  1 44.83  ? 141 PHE   B CD2  1 2 
ATOM   3027 C  CE1  . PHE   B 1 142 ? 25.413 38.072 70.356  1 46.11  ? 141 PHE   B CE1  1 2 
ATOM   3028 C  CE2  . PHE   B 1 142 ? 27.252 37.186 71.579  1 46.07  ? 141 PHE   B CE2  1 2 
ATOM   3029 C  CZ   . PHE   B 1 142 ? 26.354 37.093 70.543  1 46.15  ? 141 PHE   B CZ   1 2 
ATOM   3030 N  N    . GLU   B 1 143 ? 25.147 42.156 75.744  1 37.8   ? 142 GLU   B N    1 2 
ATOM   3031 C  CA   . GLU   B 1 143 ? 25.443 42.824 77.004  1 37.37  ? 142 GLU   B CA   1 2 
ATOM   3032 C  C    . GLU   B 1 143 ? 24.692 42.231 78.18   1 38.93  ? 142 GLU   B C    1 2 
ATOM   3033 O  O    . GLU   B 1 143 ? 25.222 42.216 79.297  1 39.33  ? 142 GLU   B O    1 2 
ATOM   3034 C  CB   . GLU   B 1 143 ? 25.171 44.335 76.901  1 36.56  ? 142 GLU   B CB   1 2 
ATOM   3035 C  CG   . GLU   B 1 143 ? 26.36  45.116 76.368  1 35.61  ? 142 GLU   B CG   1 2 
ATOM   3036 C  CD   . GLU   B 1 143 ? 26.089 46.536 75.914  1 34.49  ? 142 GLU   B CD   1 2 
ATOM   3037 O  OE1  . GLU   B 1 143 ? 24.915 46.969 75.94   1 32.99  ? 142 GLU   B OE1  1 2 
ATOM   3038 O  OE2  . GLU   B 1 143 ? 27.061 47.209 75.506  1 35.22  ? 142 GLU   B OE2  1 2 
ATOM   3039 N  N    . ILE   B 1 144 ? 23.464 41.738 77.935  1 39.48  ? 143 ILE   B N    1 2 
ATOM   3040 C  CA   . ILE   B 1 144 ? 22.588 41.174 78.97   1 40.3   ? 143 ILE   B CA   1 2 
ATOM   3041 C  C    . ILE   B 1 144 ? 22.65  39.645 79.038  1 40.75  ? 143 ILE   B C    1 2 
ATOM   3042 O  O    . ILE   B 1 144 ? 22.796 39.079 80.126  1 40.93  ? 143 ILE   B O    1 2 
ATOM   3043 C  CB   . ILE   B 1 144 ? 21.139 41.688 78.724  1 40.76  ? 143 ILE   B CB   1 2 
ATOM   3044 C  CG1  . ILE   B 1 144 ? 21.044 43.196 78.984  1 41.97  ? 143 ILE   B CG1  1 2 
ATOM   3045 C  CG2  . ILE   B 1 144 ? 20.107 40.933 79.542  1 40.95  ? 143 ILE   B CG2  1 2 
ATOM   3046 C  CD1  . ILE   B 1 144 ? 19.831 43.812 78.426  1 43.41  ? 143 ILE   B CD1  1 2 
ATOM   3047 N  N    . ASN   B 1 145 ? 22.535 38.989 77.874  1 40.78  ? 144 ASN   B N    1 2 
ATOM   3048 C  CA   . ASN   B 1 145 ? 22.496 37.538 77.748  1 41.4   ? 144 ASN   B CA   1 2 
ATOM   3049 C  C    . ASN   B 1 145 ? 23.795 36.798 78.042  1 41.7   ? 144 ASN   B C    1 2 
ATOM   3050 O  O    . ASN   B 1 145 ? 23.716 35.619 78.403  1 41.73  ? 144 ASN   B O    1 2 
ATOM   3051 C  CB   . ASN   B 1 145 ? 22     37.129 76.376  1 42.91  ? 144 ASN   B CB   1 2 
ATOM   3052 C  CG   . ASN   B 1 145 ? 20.61  37.595 76.045  1 46.69  ? 144 ASN   B CG   1 2 
ATOM   3053 O  OD1  . ASN   B 1 145 ? 19.883 38.102 76.906  1 47.71  ? 144 ASN   B OD1  1 2 
ATOM   3054 N  ND2  . ASN   B 1 145 ? 20.218 37.443 74.773  1 47.43  ? 144 ASN   B ND2  1 2 
ATOM   3055 N  N    . ILE   B 1 146 ? 24.98  37.432 77.852  1 41.71  ? 145 ILE   B N    1 2 
ATOM   3056 C  CA   . ILE   B 1 146 ? 26.236 36.723 78.117  1 41.95  ? 145 ILE   B CA   1 2 
ATOM   3057 C  C    . ILE   B 1 146 ? 27.344 37.614 78.744  1 42.09  ? 145 ILE   B C    1 2 
ATOM   3058 O  O    . ILE   B 1 146 ? 27.988 37.153 79.676  1 42.29  ? 145 ILE   B O    1 2 
ATOM   3059 C  CB   . ILE   B 1 146 ? 26.735 35.946 76.875  1 42.27  ? 145 ILE   B CB   1 2 
ATOM   3060 C  CG1  . ILE   B 1 146 ? 28.028 35.161 77.196  1 43.46  ? 145 ILE   B CG1  1 2 
ATOM   3061 C  CG2  . ILE   B 1 146 ? 26.86  36.835 75.646  1 42.2   ? 145 ILE   B CG2  1 2 
ATOM   3062 C  CD1  . ILE   B 1 146 ? 27.87  34.128 78.375  1 44.78  ? 145 ILE   B CD1  1 2 
ATOM   3063 N  N    . LEU   B 1 147 ? 27.539 38.861 78.303  1 42.07  ? 146 LEU   B N    1 2 
ATOM   3064 C  CA   . LEU   B 1 147 ? 28.548 39.741 78.901  1 42.91  ? 146 LEU   B CA   1 2 
ATOM   3065 C  C    . LEU   B 1 147 ? 28.238 39.994 80.377  1 43.87  ? 146 LEU   B C    1 2 
ATOM   3066 O  O    . LEU   B 1 147 ? 29.13  39.928 81.218  1 44.48  ? 146 LEU   B O    1 2 
ATOM   3067 C  CB   . LEU   B 1 147 ? 28.645 41.072 78.153  1 43.23  ? 146 LEU   B CB   1 2 
ATOM   3068 C  CG   . LEU   B 1 147 ? 29.371 41.017 76.824  1 45.18  ? 146 LEU   B CG   1 2 
ATOM   3069 C  CD1  . LEU   B 1 147 ? 29.325 42.362 76.114  1 46.03  ? 146 LEU   B CD1  1 2 
ATOM   3070 C  CD2  . LEU   B 1 147 ? 30.815 40.562 77.007  1 45.73  ? 146 LEU   B CD2  1 2 
ATOM   3071 N  N    . GLY   B 1 148 ? 26.965 40.226 80.677  1 43.72  ? 147 GLY   B N    1 2 
ATOM   3072 C  CA   . GLY   B 1 148 ? 26.486 40.446 82.033  1 43.84  ? 147 GLY   B CA   1 2 
ATOM   3073 C  C    . GLY   B 1 148 ? 26.663 39.216 82.888  1 44.31  ? 147 GLY   B C    1 2 
ATOM   3074 O  O    . GLY   B 1 148 ? 26.979 39.336 84.064  1 44.92  ? 147 GLY   B O    1 2 
ATOM   3075 N  N    . HIS   B 1 149 ? 26.514 38.024 82.293  1 44.34  ? 148 HIS   B N    1 2 
ATOM   3076 C  CA   . HIS   B 1 149 ? 26.704 36.726 82.952  1 44.94  ? 148 HIS   B CA   1 2 
ATOM   3077 C  C    . HIS   B 1 149 ? 28.136 36.49  83.394  1 44.55  ? 148 HIS   B C    1 2 
ATOM   3078 O  O    . HIS   B 1 149 ? 28.36  35.607 84.201  1 45.08  ? 148 HIS   B O    1 2 
ATOM   3079 C  CB   . HIS   B 1 149 ? 26.315 35.571 82.018  1 46.86  ? 148 HIS   B CB   1 2 
ATOM   3080 C  CG   . HIS   B 1 149 ? 24.847 35.339 81.869  1 50.66  ? 148 HIS   B CG   1 2 
ATOM   3081 N  ND1  . HIS   B 1 149 ? 24.365 34.2   81.251  1 52.93  ? 148 HIS   B ND1  1 2 
ATOM   3082 C  CD2  . HIS   B 1 149 ? 23.8   36.111 82.244  1 52.27  ? 148 HIS   B CD2  1 2 
ATOM   3083 C  CE1  . HIS   B 1 149 ? 23.046 34.309 81.273  1 53.75  ? 148 HIS   B CE1  1 2 
ATOM   3084 N  NE2  . HIS   B 1 149 ? 22.659 35.446 81.855  1 53.68  ? 148 HIS   B NE2  1 2 
ATOM   3085 N  N    . PHE   B 1 150 ? 29.105 37.187 82.818  1 43.99  ? 149 PHE   B N    1 2 
ATOM   3086 C  CA   . PHE   B 1 150 ? 30.491 37.07  83.205  1 44.51  ? 149 PHE   B CA   1 2 
ATOM   3087 C  C    . PHE   B 1 150 ? 30.742 37.926 84.429  1 45.32  ? 149 PHE   B C    1 2 
ATOM   3088 O  O    . PHE   B 1 150 ? 31.358 37.448 85.37   1 45.21  ? 149 PHE   B O    1 2 
ATOM   3089 C  CB   . PHE   B 1 150 ? 31.418 37.5   82.063  1 44.61  ? 149 PHE   B CB   1 2 
ATOM   3090 C  CG   . PHE   B 1 150 ? 31.753 36.398 81.09   1 45.51  ? 149 PHE   B CG   1 2 
ATOM   3091 C  CD1  . PHE   B 1 150 ? 30.963 36.166 79.983  1 46.42  ? 149 PHE   B CD1  1 2 
ATOM   3092 C  CD2  . PHE   B 1 150 ? 32.87  35.608 81.271  1 46.55  ? 149 PHE   B CD2  1 2 
ATOM   3093 C  CE1  . PHE   B 1 150 ? 31.273 35.151 79.085  1 47.2   ? 149 PHE   B CE1  1 2 
ATOM   3094 C  CE2  . PHE   B 1 150 ? 33.184 34.6   80.364  1 47.32  ? 149 PHE   B CE2  1 2 
ATOM   3095 C  CZ   . PHE   B 1 150 ? 32.386 34.382 79.277  1 47.03  ? 149 PHE   B CZ   1 2 
ATOM   3096 N  N    . TRP   B 1 151 ? 30.249 39.175 84.446  1 45.97  ? 150 TRP   B N    1 2 
ATOM   3097 C  CA   . TRP   B 1 151 ? 30.491 40.074 85.583  1 46.92  ? 150 TRP   B CA   1 2 
ATOM   3098 C  C    . TRP   B 1 151 ? 29.816 39.649 86.853  1 48.34  ? 150 TRP   B C    1 2 
ATOM   3099 O  O    . TRP   B 1 151 ? 30.422 39.793 87.913  1 49.24  ? 150 TRP   B O    1 2 
ATOM   3100 C  CB   . TRP   B 1 151 ? 30.152 41.55  85.292  1 46.71  ? 150 TRP   B CB   1 2 
ATOM   3101 C  CG   . TRP   B 1 151 ? 30.206 42     83.854  1 46.97  ? 150 TRP   B CG   1 2 
ATOM   3102 C  CD1  . TRP   B 1 151 ? 29.226 42.662 83.177  1 47.82  ? 150 TRP   B CD1  1 2 
ATOM   3103 C  CD2  . TRP   B 1 151 ? 31.315 41.887 82.942  1 46.77  ? 150 TRP   B CD2  1 2 
ATOM   3104 N  NE1  . TRP   B 1 151 ? 29.646 42.955 81.902  1 48     ? 150 TRP   B NE1  1 2 
ATOM   3105 C  CE2  . TRP   B 1 151 ? 30.925 42.492 81.733  1 47.46  ? 150 TRP   B CE2  1 2 
ATOM   3106 C  CE3  . TRP   B 1 151 ? 32.596 41.331 83.025  1 47.14  ? 150 TRP   B CE3  1 2 
ATOM   3107 C  CZ2  . TRP   B 1 151 ? 31.769 42.556 80.626  1 47.7   ? 150 TRP   B CZ2  1 2 
ATOM   3108 C  CZ3  . TRP   B 1 151 ? 33.41  41.36  81.91   1 47.69  ? 150 TRP   B CZ3  1 2 
ATOM   3109 C  CH2  . TRP   B 1 151 ? 33.006 41.99  80.741  1 47.57  ? 150 TRP   B CH2  1 2 
ATOM   3110 N  N    . ILE   B 1 152 ? 28.568 39.167 86.791  1 48.84  ? 151 ILE   B N    1 2 
ATOM   3111 C  CA   . ILE   B 1 152 ? 27.897 38.745 88.019  1 50.23  ? 151 ILE   B CA   1 2 
ATOM   3112 C  C    . ILE   B 1 152 ? 28.586 37.499 88.571  1 51.91  ? 151 ILE   B C    1 2 
ATOM   3113 O  O    . ILE   B 1 152 ? 28.912 37.46  89.75   1 52     ? 151 ILE   B O    1 2 
ATOM   3114 C  CB   . ILE   B 1 152 ? 26.378 38.59  87.882  1 50.71  ? 151 ILE   B CB   1 2 
ATOM   3115 C  CG1  . ILE   B 1 152 ? 25.783 39.794 87.186  1 52.02  ? 151 ILE   B CG1  1 2 
ATOM   3116 C  CG2  . ILE   B 1 152 ? 25.74  38.418 89.253  1 51.09  ? 151 ILE   B CG2  1 2 
ATOM   3117 C  CD1  . ILE   B 1 152 ? 24.468 39.547 86.662  1 53.87  ? 151 ILE   B CD1  1 2 
ATOM   3118 N  N    . THR   B 1 153 ? 28.92  36.539 87.699  1 52.93  ? 152 THR   B N    1 2 
ATOM   3119 C  CA   . THR   B 1 153 ? 29.589 35.31  88.142  1 54.13  ? 152 THR   B CA   1 2 
ATOM   3120 C  C    . THR   B 1 153 ? 30.992 35.572 88.666  1 55.12  ? 152 THR   B C    1 2 
ATOM   3121 O  O    . THR   B 1 153 ? 31.402 34.96  89.633  1 54.93  ? 152 THR   B O    1 2 
ATOM   3122 C  CB   . THR   B 1 153 ? 29.599 34.257 87.036  1 55.43  ? 152 THR   B CB   1 2 
ATOM   3123 O  OG1  . THR   B 1 153 ? 28.327 34.228 86.378  1 56.15  ? 152 THR   B OG1  1 2 
ATOM   3124 C  CG2  . THR   B 1 153 ? 29.948 32.873 87.574  1 56.02  ? 152 THR   B CG2  1 2 
ATOM   3125 N  N    . LYS   B 1 154 ? 31.717 36.485 88.021  1 56.23  ? 153 LYS   B N    1 2 
ATOM   3126 C  CA   . LYS   B 1 154 ? 33.084 36.902 88.356  1 57.55  ? 153 LYS   B CA   1 2 
ATOM   3127 C  C    . LYS   B 1 154 ? 33.156 37.569 89.708  1 58.57  ? 153 LYS   B C    1 2 
ATOM   3128 O  O    . LYS   B 1 154 ? 34.177 37.459 90.387  1 58.89  ? 153 LYS   B O    1 2 
ATOM   3129 C  CB   . LYS   B 1 154 ? 33.6   37.905 87.309  1 59.55  ? 153 LYS   B CB   1 2 
ATOM   3130 C  CG   . LYS   B 1 154 ? 34.713 37.396 86.424  1 62.69  ? 153 LYS   B CG   1 2 
ATOM   3131 C  CD   . LYS   B 1 154 ? 35.856 38.369 86.498  1 66.72  ? 153 LYS   B CD   1 2 
ATOM   3132 C  CE   . LYS   B 1 154 ? 36.542 38.545 85.179  1 70.4   ? 153 LYS   B CE   1 2 
ATOM   3133 N  NZ   . LYS   B 1 154 ? 37.335 39.795 85.156  1 72.91  ? 153 LYS   B NZ   1 2 
ATOM   3134 N  N    . ALA   B 1 155 ? 32.102 38.305 90.082  1 59.14  ? 154 ALA   B N    1 2 
ATOM   3135 C  CA   . ALA   B 1 155 ? 32.06  38.988 91.372  1 60.28  ? 154 ALA   B CA   1 2 
ATOM   3136 C  C    . ALA   B 1 155 ? 31.505 38.1   92.506  1 60.72  ? 154 ALA   B C    1 2 
ATOM   3137 O  O    . ALA   B 1 155 ? 31.862 38.316 93.668  1 61.4   ? 154 ALA   B O    1 2 
ATOM   3138 C  CB   . ALA   B 1 155 ? 31.253 40.276 91.261  1 60.72  ? 154 ALA   B CB   1 2 
ATOM   3139 N  N    . LEU   B 1 156 ? 30.644 37.113 92.185  1 60.2   ? 155 LEU   B N    1 2 
ATOM   3140 C  CA   . LEU   B 1 156 ? 30.087 36.245 93.22   1 60.44  ? 155 LEU   B CA   1 2 
ATOM   3141 C  C    . LEU   B 1 156 ? 30.915 34.961 93.448  1 62.38  ? 155 LEU   B C    1 2 
ATOM   3142 O  O    . LEU   B 1 156 ? 30.845 34.373 94.528  1 62.74  ? 155 LEU   B O    1 2 
ATOM   3143 C  CB   . LEU   B 1 156 ? 28.603 35.939 92.965  1 59.33  ? 155 LEU   B CB   1 2 
ATOM   3144 C  CG   . LEU   B 1 156 ? 27.684 37.142 92.705  1 59.22  ? 155 LEU   B CG   1 2 
ATOM   3145 C  CD1  . LEU   B 1 156 ? 26.26  36.722 92.651  1 59.36  ? 155 LEU   B CD1  1 2 
ATOM   3146 C  CD2  . LEU   B 1 156 ? 27.822 38.213 93.755  1 59.57  ? 155 LEU   B CD2  1 2 
ATOM   3147 N  N    . LEU   B 1 157 ? 31.754 34.583 92.474  1 63.53  ? 156 LEU   B N    1 2 
ATOM   3148 C  CA   . LEU   B 1 157 ? 32.617 33.401 92.518  1 65.48  ? 156 LEU   B CA   1 2 
ATOM   3149 C  C    . LEU   B 1 157 ? 33.718 33.382 93.622  1 68.01  ? 156 LEU   B C    1 2 
ATOM   3150 O  O    . LEU   B 1 157 ? 33.921 32.311 94.188  1 68.16  ? 156 LEU   B O    1 2 
ATOM   3151 C  CB   . LEU   B 1 157 ? 33.265 33.183 91.132  1 65.49  ? 156 LEU   B CB   1 2 
ATOM   3152 C  CG   . LEU   B 1 157 ? 33.985 31.865 90.853  1 66.66  ? 156 LEU   B CG   1 2 
ATOM   3153 C  CD1  . LEU   B 1 157 ? 33.093 30.674 91.135  1 67.14  ? 156 LEU   B CD1  1 2 
ATOM   3154 C  CD2  . LEU   B 1 157 ? 34.476 31.813 89.417  1 67.12  ? 156 LEU   B CD2  1 2 
ATOM   3155 N  N    . PRO   B 1 158 ? 34.464 34.474 93.938  1 69.73  ? 157 PRO   B N    1 2 
ATOM   3156 C  CA   . PRO   B 1 158 ? 35.566 34.344 94.917  1 71.03  ? 157 PRO   B CA   1 2 
ATOM   3157 C  C    . PRO   B 1 158 ? 35.175 33.792 96.286  1 72.68  ? 157 PRO   B C    1 2 
ATOM   3158 O  O    . PRO   B 1 158 ? 35.855 32.898 96.784  1 72.85  ? 157 PRO   B O    1 2 
ATOM   3159 C  CB   . PRO   B 1 158 ? 36.151 35.76  95.007  1 71.66  ? 157 PRO   B CB   1 2 
ATOM   3160 C  CG   . PRO   B 1 158 ? 35.739 36.43  93.751  1 71.82  ? 157 PRO   B CG   1 2 
ATOM   3161 C  CD   . PRO   B 1 158 ? 34.416 35.835 93.365  1 69.76  ? 157 PRO   B CD   1 2 
ATOM   3162 N  N    . SER   B 1 159 ? 34.082 34.294 96.881  1 73.58  ? 158 SER   B N    1 2 
ATOM   3163 C  CA   . SER   B 1 159 ? 33.611 33.809 98.173  1 74.84  ? 158 SER   B CA   1 2 
ATOM   3164 C  C    . SER   B 1 159 ? 33.149 32.359 98.064  1 76.1   ? 158 SER   B C    1 2 
ATOM   3165 O  O    . SER   B 1 159 ? 33.389 31.577 98.978  1 77.02  ? 158 SER   B O    1 2 
ATOM   3166 C  CB   . SER   B 1 159 ? 32.482 34.688 98.695  1 76.19  ? 158 SER   B CB   1 2 
ATOM   3167 O  OG   . SER   B 1 159 ? 31.851 34.115 99.827  1 78.23  ? 158 SER   B OG   1 2 
ATOM   3168 N  N    . MET   B 1 160 ? 32.507 31.993 96.944  1 76.21  ? 159 MET   B N    1 2 
ATOM   3169 C  CA   . MET   B 1 160 ? 32.073 30.616 96.716  1 76.69  ? 159 MET   B CA   1 2 
ATOM   3170 C  C    . MET   B 1 160 ? 33.287 29.693 96.641  1 78.01  ? 159 MET   B C    1 2 
ATOM   3171 O  O    . MET   B 1 160 ? 33.28  28.629 97.247  1 78.28  ? 159 MET   B O    1 2 
ATOM   3172 C  CB   . MET   B 1 160 ? 31.259 30.511 95.427  1 76.02  ? 159 MET   B CB   1 2 
ATOM   3173 C  CG   . MET   B 1 160 ? 29.959 31.236 95.491  1 75.53  ? 159 MET   B CG   1 2 
ATOM   3174 S  SD   . MET   B 1 160 ? 29.367 31.497 93.822  1 70.02  ? 159 MET   B SD   1 2 
ATOM   3175 C  CE   . MET   B 1 160 ? 27.704 31.985 94.144  1 67.16  ? 159 MET   B CE   1 2 
ATOM   3176 N  N    . ILE   B 1 161 ? 34.34  30.126 95.93   1 78.47  ? 160 ILE   B N    1 2 
ATOM   3177 C  CA   . ILE   B 1 161 ? 35.602 29.414 95.783  1 79.33  ? 160 ILE   B CA   1 2 
ATOM   3178 C  C    . ILE   B 1 161 ? 36.218 29.166 97.166  1 80.41  ? 160 ILE   B C    1 2 
ATOM   3179 O  O    . ILE   B 1 161 ? 36.643 28.051 97.463  1 80.19  ? 160 ILE   B O    1 2 
ATOM   3180 C  CB   . ILE   B 1 161 ? 36.527 30.247 94.855  1 79.57  ? 160 ILE   B CB   1 2 
ATOM   3181 C  CG1  . ILE   B 1 161 ? 36.09  30.111 93.399  1 80.56  ? 160 ILE   B CG1  1 2 
ATOM   3182 C  CG2  . ILE   B 1 161 ? 37.996 29.881 95.009  1 80.01  ? 160 ILE   B CG2  1 2 
ATOM   3183 C  CD1  . ILE   B 1 161 ? 36.134 28.697 92.85   1 81.95  ? 160 ILE   B CD1  1 2 
ATOM   3184 N  N    . LYS   B 1 162 ? 36.203 30.193 98.019  1 81.54  ? 161 LYS   B N    1 2 
ATOM   3185 C  CA   . LYS   B 1 162 ? 36.746 30.143 99.369  1 83.35  ? 161 LYS   B CA   1 2 
ATOM   3186 C  C    . LYS   B 1 162 ? 36.009 29.116 100.214 1 85.67  ? 161 LYS   B C    1 2 
ATOM   3187 O  O    . LYS   B 1 162 ? 36.629 28.273 100.865 1 87.86  ? 161 LYS   B O    1 2 
ATOM   3188 C  CB   . LYS   B 1 162 ? 36.636 31.533 100.021 1 84.55  ? 161 LYS   B CB   1 2 
ATOM   3189 C  CG   . LYS   B 1 162 ? 37.659 32.526 99.506  1 88.06  ? 161 LYS   B CG   1 2 
ATOM   3190 C  CD   . LYS   B 1 162 ? 37.439 33.904 100.095 1 92.35  ? 161 LYS   B CD   1 2 
ATOM   3191 C  CE   . LYS   B 1 162 ? 37.128 34.936 99.033  1 96.53  ? 161 LYS   B CE   1 2 
ATOM   3192 N  NZ   . LYS   B 1 162 ? 38.131 34.96  97.93   1 98.31  ? 161 LYS   B NZ   1 2 
ATOM   3193 N  N    . ARG   B 1 163 ? 34.683 29.173 100.183 1 85.49  ? 162 ARG   B N    1 2 
ATOM   3194 C  CA   . ARG   B 1 163 ? 33.848 28.272 100.962 1 85.81  ? 162 ARG   B CA   1 2 
ATOM   3195 C  C    . ARG   B 1 163 ? 33.638 26.9   100.341 1 85.33  ? 162 ARG   B C    1 2 
ATOM   3196 O  O    . ARG   B 1 163 ? 33.077 26.027 101.002 1 86.4   ? 162 ARG   B O    1 2 
ATOM   3197 C  CB   . ARG   B 1 163 ? 32.497 28.942 101.246 1 87.99  ? 162 ARG   B CB   1 2 
ATOM   3198 C  CG   . ARG   B 1 163 ? 32.671 30.253 102.008 1 92.49  ? 162 ARG   B CG   1 2 
ATOM   3199 C  CD   . ARG   B 1 163 ? 31.432 31.122 102.024 1 96.27  ? 162 ARG   B CD   1 2 
ATOM   3200 N  NE   . ARG   B 1 163 ? 31.734 32.504 102.416 1 99.03  ? 162 ARG   B NE   1 2 
ATOM   3201 C  CZ   . ARG   B 1 163 ? 31.807 32.935 103.672 1 100.82 ? 162 ARG   B CZ   1 2 
ATOM   3202 N  NH1  . ARG   B 1 163 ? 31.635 32.091 104.682 1 100.48 ? 162 ARG   B NH1  1 2 
ATOM   3203 N  NH2  . ARG   B 1 163 ? 32.078 34.208 103.928 1 100.65 ? 162 ARG   B NH2  1 2 
ATOM   3204 N  N    . ASN   B 1 164 ? 34.053 26.709 99.066  1 83.74  ? 163 ASN   B N    1 2 
ATOM   3205 C  CA   . ASN   B 1 164 ? 33.863 25.49  98.272  1 82.55  ? 163 ASN   B CA   1 2 
ATOM   3206 C  C    . ASN   B 1 164 ? 32.382 25.084 98.295  1 81.07  ? 163 ASN   B C    1 2 
ATOM   3207 O  O    . ASN   B 1 164 ? 32.056 23.922 98.507  1 81.23  ? 163 ASN   B O    1 2 
ATOM   3208 C  CB   . ASN   B 1 164 ? 34.777 24.353 98.755  1 83.45  ? 163 ASN   B CB   1 2 
ATOM   3209 C  CG   . ASN   B 1 164 ? 34.899 23.192 97.801  1 85.89  ? 163 ASN   B CG   1 2 
ATOM   3210 O  OD1  . ASN   B 1 164 ? 35.358 23.328 96.662  1 86.55  ? 163 ASN   B OD1  1 2 
ATOM   3211 N  ND2  . ASN   B 1 164 ? 34.481 22.014 98.248  1 86.42  ? 163 ASN   B ND2  1 2 
ATOM   3212 N  N    . HIS   B 1 165 ? 31.494 26.073 98.183  1 79.53  ? 164 HIS   B N    1 2 
ATOM   3213 C  CA   . HIS   B 1 165 ? 30.066 25.844 98.244  1 78.8   ? 164 HIS   B CA   1 2 
ATOM   3214 C  C    . HIS   B 1 165 ? 29.348 26.936 97.479  1 77.8   ? 164 HIS   B C    1 2 
ATOM   3215 O  O    . HIS   B 1 165 ? 29.487 28.115 97.82   1 78.45  ? 164 HIS   B O    1 2 
ATOM   3216 C  CB   . HIS   B 1 165 ? 29.595 25.855 99.696  1 79.68  ? 164 HIS   B CB   1 2 
ATOM   3217 C  CG   . HIS   B 1 165 ? 28.116 25.648 99.858  1 81.28  ? 164 HIS   B CG   1 2 
ATOM   3218 N  ND1  . HIS   B 1 165 ? 27.456 24.611 99.22   1 82.7   ? 164 HIS   B ND1  1 2 
ATOM   3219 C  CD2  . HIS   B 1 165 ? 27.226 26.325 100.626 1 82.38  ? 164 HIS   B CD2  1 2 
ATOM   3220 C  CE1  . HIS   B 1 165 ? 26.19  24.705 99.598  1 83.26  ? 164 HIS   B CE1  1 2 
ATOM   3221 N  NE2  . HIS   B 1 165 ? 26.004 25.72  100.445 1 83.35  ? 164 HIS   B NE2  1 2 
ATOM   3222 N  N    . GLY   B 1 166 ? 28.574 26.528 96.477  1 75.68  ? 165 GLY   B N    1 2 
ATOM   3223 C  CA   . GLY   B 1 166 ? 27.785 27.422 95.65   1 74.26  ? 165 GLY   B CA   1 2 
ATOM   3224 C  C    . GLY   B 1 166 ? 27.035 26.683 94.559  1 72.8   ? 165 GLY   B C    1 2 
ATOM   3225 O  O    . GLY   B 1 166 ? 26.968 25.451 94.573  1 73.44  ? 165 GLY   B O    1 2 
ATOM   3226 N  N    . HIS   B 1 167 ? 26.466 27.434 93.606  1 70.52  ? 166 HIS   B N    1 2 
ATOM   3227 C  CA   . HIS   B 1 167 ? 25.728 26.88  92.477  1 68.94  ? 166 HIS   B CA   1 2 
ATOM   3228 C  C    . HIS   B 1 167 ? 25.483 27.969 91.443  1 66.58  ? 166 HIS   B C    1 2 
ATOM   3229 O  O    . HIS   B 1 167 ? 24.743 28.91  91.716  1 66.51  ? 166 HIS   B O    1 2 
ATOM   3230 C  CB   . HIS   B 1 167 ? 24.384 26.279 92.917  1 69.89  ? 166 HIS   B CB   1 2 
ATOM   3231 C  CG   . HIS   B 1 167 ? 23.878 25.206 91.999  1 71.86  ? 166 HIS   B CG   1 2 
ATOM   3232 N  ND1  . HIS   B 1 167 ? 23.523 23.957 92.48   1 73.63  ? 166 HIS   B ND1  1 2 
ATOM   3233 C  CD2  . HIS   B 1 167 ? 23.7   25.222 90.657  1 72.55  ? 166 HIS   B CD2  1 2 
ATOM   3234 C  CE1  . HIS   B 1 167 ? 23.124 23.266 91.424  1 73.8   ? 166 HIS   B CE1  1 2 
ATOM   3235 N  NE2  . HIS   B 1 167 ? 23.227 23.979 90.306  1 73.48  ? 166 HIS   B NE2  1 2 
ATOM   3236 N  N    . ILE   B 1 168 ? 26.087 27.841 90.26   1 64.54  ? 167 ILE   B N    1 2 
ATOM   3237 C  CA   . ILE   B 1 168 ? 25.904 28.839 89.213  1 63.22  ? 167 ILE   B CA   1 2 
ATOM   3238 C  C    . ILE   B 1 168 ? 24.867 28.396 88.182  1 61.82  ? 167 ILE   B C    1 2 
ATOM   3239 O  O    . ILE   B 1 168 ? 25.124 27.516 87.362  1 61.88  ? 167 ILE   B O    1 2 
ATOM   3240 C  CB   . ILE   B 1 168 ? 27.242 29.263 88.58   1 63.23  ? 167 ILE   B CB   1 2 
ATOM   3241 C  CG1  . ILE   B 1 168 ? 28.185 29.834 89.65   1 63.98  ? 167 ILE   B CG1  1 2 
ATOM   3242 C  CG2  . ILE   B 1 168 ? 27.013 30.274 87.469  1 63.42  ? 167 ILE   B CG2  1 2 
ATOM   3243 C  CD1  . ILE   B 1 168 ? 27.647 31.071 90.373  1 65.03  ? 167 ILE   B CD1  1 2 
ATOM   3244 N  N    . VAL   B 1 169 ? 23.683 29.009 88.243  1 60.44  ? 168 VAL   B N    1 2 
ATOM   3245 C  CA   . VAL   B 1 169 ? 22.581 28.71  87.34   1 59.65  ? 168 VAL   B CA   1 2 
ATOM   3246 C  C    . VAL   B 1 169 ? 22.548 29.645 86.128  1 58.42  ? 168 VAL   B C    1 2 
ATOM   3247 O  O    . VAL   B 1 169 ? 22.228 30.824 86.252  1 58.13  ? 168 VAL   B O    1 2 
ATOM   3248 C  CB   . VAL   B 1 169 ? 21.224 28.668 88.077  1 60.29  ? 168 VAL   B CB   1 2 
ATOM   3249 C  CG1  . VAL   B 1 169 ? 20.082 28.373 87.106  1 61.17  ? 168 VAL   B CG1  1 2 
ATOM   3250 C  CG2  . VAL   B 1 169 ? 21.257 27.65  89.204  1 60.19  ? 168 VAL   B CG2  1 2 
ATOM   3251 N  N    . THR   B 1 170 ? 22.884 29.11  84.956  1 57.61  ? 169 THR   B N    1 2 
ATOM   3252 C  CA   . THR   B 1 170 ? 22.884 29.874 83.715  1 57.27  ? 169 THR   B CA   1 2 
ATOM   3253 C  C    . THR   B 1 170 ? 21.576 29.624 82.956  1 56.46  ? 169 THR   B C    1 2 
ATOM   3254 O  O    . THR   B 1 170 ? 21.369 28.524 82.451  1 56.41  ? 169 THR   B O    1 2 
ATOM   3255 C  CB   . THR   B 1 170 ? 24.097 29.48  82.863  1 58.54  ? 169 THR   B CB   1 2 
ATOM   3256 O  OG1  . THR   B 1 170 ? 25.296 29.714 83.604  1 59.35  ? 169 THR   B OG1  1 2 
ATOM   3257 C  CG2  . THR   B 1 170 ? 24.15  30.239 81.558  1 59.03  ? 169 THR   B CG2  1 2 
ATOM   3258 N  N    . VAL   B 1 171 ? 20.692 30.63  82.884  1 55.66  ? 170 VAL   B N    1 2 
ATOM   3259 C  CA   . VAL   B 1 171 ? 19.427 30.474 82.168  1 55.41  ? 170 VAL   B CA   1 2 
ATOM   3260 C  C    . VAL   B 1 171 ? 19.578 30.802 80.681  1 54.89  ? 170 VAL   B C    1 2 
ATOM   3261 O  O    . VAL   B 1 171 ? 19.743 31.964 80.302  1 55.1   ? 170 VAL   B O    1 2 
ATOM   3262 C  CB   . VAL   B 1 171 ? 18.256 31.242 82.821  1 56.01  ? 170 VAL   B CB   1 2 
ATOM   3263 C  CG1  . VAL   B 1 171 ? 16.963 31.028 82.039  1 56.55  ? 170 VAL   B CG1  1 2 
ATOM   3264 C  CG2  . VAL   B 1 171 ? 18.081 30.828 84.277  1 56.3   ? 170 VAL   B CG2  1 2 
ATOM   3265 N  N    . ALA   B 1 172 ? 19.541 29.766 79.849  1 53.96  ? 171 ALA   B N    1 2 
ATOM   3266 C  CA   . ALA   B 1 172 ? 19.658 29.888 78.404  1 53.88  ? 171 ALA   B CA   1 2 
ATOM   3267 C  C    . ALA   B 1 172 ? 18.354 29.295 77.726  1 53.57  ? 171 ALA   B C    1 2 
ATOM   3268 O  O    . ALA   B 1 172 ? 17.379 29.078 78.44   1 54.28  ? 171 ALA   B O    1 2 
ATOM   3269 C  CB   . ALA   B 1 172 ? 20.953 29.193 77.942  1 54.04  ? 171 ALA   B CB   1 2 
ATOM   3270 N  N    . SER   B 1 173 ? 18.285 29.132 76.391  1 52.22  ? 172 SER   B N    1 2 
ATOM   3271 C  CA   . SER   B 1 173 ? 17.116 28.594 75.709  1 51.53  ? 172 SER   B CA   1 2 
ATOM   3272 C  C    . SER   B 1 173 ? 17.57  27.406 74.806  1 51.11  ? 172 SER   B C    1 2 
ATOM   3273 O  O    . SER   B 1 173 ? 18.774 27.134 74.705  1 50.93  ? 172 SER   B O    1 2 
ATOM   3274 C  CB   . SER   B 1 173 ? 16.499 29.717 74.867  1 52.19  ? 172 SER   B CB   1 2 
ATOM   3275 O  OG   . SER   B 1 173 ? 15.303 29.384 74.182  1 53.38  ? 172 SER   B OG   1 2 
ATOM   3276 N  N    . VAL   B 1 174 ? 16.623 26.699 74.141  1 50.79  ? 173 VAL   B N    1 2 
ATOM   3277 C  CA   . VAL   B 1 174 ? 17.009 25.674 73.145  1 50.87  ? 173 VAL   B CA   1 2 
ATOM   3278 C  C    . VAL   B 1 174 ? 17.757 26.31  71.934  1 51.08  ? 173 VAL   B C    1 2 
ATOM   3279 O  O    . VAL   B 1 174 ? 18.342 25.589 71.122  1 50.63  ? 173 VAL   B O    1 2 
ATOM   3280 C  CB   . VAL   B 1 174 ? 15.856 24.754 72.701  1 51.05  ? 173 VAL   B CB   1 2 
ATOM   3281 C  CG1  . VAL   B 1 174 ? 15.376 23.906 73.873  1 51.75  ? 173 VAL   B CG1  1 2 
ATOM   3282 C  CG2  . VAL   B 1 174 ? 14.714 25.563 72.118  1 51.01  ? 173 VAL   B CG2  1 2 
ATOM   3283 N  N    . CYS   B 1 175 ? 17.751 27.678 71.864  1 51.56  ? 174 CYS   B N    1 2 
ATOM   3284 C  CA   . CYS   B 1 175 ? 18.495 28.588 70.985  1 52.4   ? 174 CYS   B CA   1 2 
ATOM   3285 C  C    . CYS   B 1 175 ? 20.005 28.684 71.381  1 53.75  ? 174 CYS   B C    1 2 
ATOM   3286 O  O    . CYS   B 1 175 ? 20.701 29.576 70.909  1 53.46  ? 174 CYS   B O    1 2 
ATOM   3287 C  CB   . CYS   B 1 175 ? 17.846 29.969 70.995  1 52.22  ? 174 CYS   B CB   1 2 
ATOM   3288 S  SG   . CYS   B 1 175 ? 16.107 29.983 70.492  1 52.63  ? 174 CYS   B SG   1 2 
ATOM   3289 N  N    . GLY   B 1 176 ? 20.437 27.829 72.308  1 54.97  ? 175 GLY   B N    1 2 
ATOM   3290 C  CA   . GLY   B 1 176 ? 21.806 27.629 72.764  1 56.35  ? 175 GLY   B CA   1 2 
ATOM   3291 C  C    . GLY   B 1 176 ? 22.363 26.292 72.282  1 57.5   ? 175 GLY   B C    1 2 
ATOM   3292 O  O    . GLY   B 1 176 ? 23.567 26.04  72.375  1 57.44  ? 175 GLY   B O    1 2 
ATOM   3293 N  N    . HIS   B 1 177 ? 21.476 25.421 71.759  1 58.29  ? 176 HIS   B N    1 2 
ATOM   3294 C  CA   . HIS   B 1 177 ? 21.776 24.116 71.202  1 59.45  ? 176 HIS   B CA   1 2 
ATOM   3295 C  C    . HIS   B 1 177 ? 21.53  24.084 69.693  1 60.1   ? 176 HIS   B C    1 2 
ATOM   3296 O  O    . HIS   B 1 177 ? 22.167 23.284 69.013  1 60.04  ? 176 HIS   B O    1 2 
ATOM   3297 C  CB   . HIS   B 1 177 ? 20.956 23.038 71.913  1 60.74  ? 176 HIS   B CB   1 2 
ATOM   3298 C  CG   . HIS   B 1 177 ? 21.396 22.807 73.323  1 63.69  ? 176 HIS   B CG   1 2 
ATOM   3299 N  ND1  . HIS   B 1 177 ? 22.265 21.778 73.647  1 65.76  ? 176 HIS   B ND1  1 2 
ATOM   3300 C  CD2  . HIS   B 1 177 ? 21.105 23.506 74.447  1 65.01  ? 176 HIS   B CD2  1 2 
ATOM   3301 C  CE1  . HIS   B 1 177 ? 22.469 21.879 74.954  1 66.23  ? 176 HIS   B CE1  1 2 
ATOM   3302 N  NE2  . HIS   B 1 177 ? 21.784 22.898 75.48   1 66.05  ? 176 HIS   B NE2  1 2 
ATOM   3303 N  N    . GLU   B 1 178 ? 20.641 24.958 69.161  1 60.73  ? 177 GLU   B N    1 2 
ATOM   3304 C  CA   . GLU   B 1 178 ? 20.353 25.042 67.716  1 62.01  ? 177 GLU   B CA   1 2 
ATOM   3305 C  C    . GLU   B 1 178 ? 19.641 26.367 67.347  1 62.24  ? 177 GLU   B C    1 2 
ATOM   3306 O  O    . GLU   B 1 178 ? 18.667 26.74  67.995  1 62.6   ? 177 GLU   B O    1 2 
ATOM   3307 C  CB   . GLU   B 1 178 ? 19.595 23.787 67.232  1 64.96  ? 177 GLU   B CB   1 2 
ATOM   3308 C  CG   . GLU   B 1 178 ? 18.927 23.909 65.883  1 71.41  ? 177 GLU   B CG   1 2 
ATOM   3309 C  CD   . GLU   B 1 178 ? 17.416 24.043 65.967  1 81.17  ? 177 GLU   B CD   1 2 
ATOM   3310 O  OE1  . GLU   B 1 178 ? 16.9   24.41  67.052  1 82.15  ? 177 GLU   B OE1  1 2 
ATOM   3311 O  OE2  . GLU   B 1 178 ? 16.746 23.786 64.937  1 85.17  ? 177 GLU   B OE2  1 2 
ATOM   3312 N  N    . GLY   B 1 179 ? 20.145 27.055 66.326  1 61.88  ? 178 GLY   B N    1 2 
ATOM   3313 C  CA   . GLY   B 1 179 ? 19.638 28.357 65.898  1 62.28  ? 178 GLY   B CA   1 2 
ATOM   3314 C  C    . GLY   B 1 179 ? 18.309 28.395 65.167  1 62.68  ? 178 GLY   B C    1 2 
ATOM   3315 O  O    . GLY   B 1 179 ? 18.023 27.53  64.338  1 63.1   ? 178 GLY   B O    1 2 
ATOM   3316 N  N    . ILE   B 1 180 ? 17.513 29.448 65.419  1 62.45  ? 179 ILE   B N    1 2 
ATOM   3317 C  CA   . ILE   B 1 180 ? 16.188 29.623 64.823  1 62.74  ? 179 ILE   B CA   1 2 
ATOM   3318 C  C    . ILE   B 1 180 ? 16.108 30.927 63.975  1 63.21  ? 179 ILE   B C    1 2 
ATOM   3319 O  O    . ILE   B 1 180 ? 16.855 31.874 64.243  1 63.09  ? 179 ILE   B O    1 2 
ATOM   3320 C  CB   . ILE   B 1 180 ? 15.187 29.595 66.004  1 63.04  ? 179 ILE   B CB   1 2 
ATOM   3321 C  CG1  . ILE   B 1 180 ? 13.879 28.928 65.647  1 63.96  ? 179 ILE   B CG1  1 2 
ATOM   3322 C  CG2  . ILE   B 1 180 ? 14.977 30.955 66.647  1 63.42  ? 179 ILE   B CG2  1 2 
ATOM   3323 C  CD1  . ILE   B 1 180 ? 13.654 27.775 66.493  1 65.25  ? 179 ILE   B CD1  1 2 
ATOM   3324 N  N    . PRO   B 1 181 ? 15.258 30.998 62.918  1 63.57  ? 180 PRO   B N    1 2 
ATOM   3325 C  CA   . PRO   B 1 181 ? 15.185 32.237 62.121  1 63.78  ? 180 PRO   B CA   1 2 
ATOM   3326 C  C    . PRO   B 1 181 ? 14.587 33.412 62.903  1 64.34  ? 180 PRO   B C    1 2 
ATOM   3327 O  O    . PRO   B 1 181 ? 13.806 33.195 63.829  1 64.49  ? 180 PRO   B O    1 2 
ATOM   3328 C  CB   . PRO   B 1 181 ? 14.317 31.843 60.921  1 64.13  ? 180 PRO   B CB   1 2 
ATOM   3329 C  CG   . PRO   B 1 181 ? 14.245 30.348 60.958  1 64.46  ? 180 PRO   B CG   1 2 
ATOM   3330 C  CD   . PRO   B 1 181 ? 14.331 29.98  62.393  1 63.01  ? 180 PRO   B CD   1 2 
ATOM   3331 N  N    . TYR   B 1 182 ? 14.985 34.653 62.546  1 64.44  ? 181 TYR   B N    1 2 
ATOM   3332 C  CA   . TYR   B 1 182 ? 14.591 35.927 63.176  1 65.07  ? 181 TYR   B CA   1 2 
ATOM   3333 C  C    . TYR   B 1 182 ? 15.299 36.167 64.525  1 64.76  ? 181 TYR   B C    1 2 
ATOM   3334 O  O    . TYR   B 1 182 ? 15.399 37.309 64.975  1 65.08  ? 181 TYR   B O    1 2 
ATOM   3335 C  CB   . TYR   B 1 182 ? 13.065 36.107 63.298  1 65.77  ? 181 TYR   B CB   1 2 
ATOM   3336 C  CG   . TYR   B 1 182 ? 12.31  35.698 62.054  1 67.57  ? 181 TYR   B CG   1 2 
ATOM   3337 C  CD1  . TYR   B 1 182 ? 12.612 36.253 60.818  1 69.02  ? 181 TYR   B CD1  1 2 
ATOM   3338 C  CD2  . TYR   B 1 182 ? 11.317 34.729 62.105  1 68.95  ? 181 TYR   B CD2  1 2 
ATOM   3339 C  CE1  . TYR   B 1 182 ? 11.937 35.863 59.663  1 70.25  ? 181 TYR   B CE1  1 2 
ATOM   3340 C  CE2  . TYR   B 1 182 ? 10.629 34.334 60.959  1 70.15  ? 181 TYR   B CE2  1 2 
ATOM   3341 C  CZ   . TYR   B 1 182 ? 10.946 34.901 59.736  1 71.26  ? 181 TYR   B CZ   1 2 
ATOM   3342 O  OH   . TYR   B 1 182 ? 10.285 34.515 58.587  1 72.82  ? 181 TYR   B OH   1 2 
ATOM   3343 N  N    . LEU   B 1 183 ? 15.814 35.108 65.159  1 63.79  ? 182 LEU   B N    1 2 
ATOM   3344 C  CA   . LEU   B 1 183 ? 16.521 35.238 66.424  1 63.09  ? 182 LEU   B CA   1 2 
ATOM   3345 C  C    . LEU   B 1 183 ? 18.017 34.907 66.295  1 62.82  ? 182 LEU   B C    1 2 
ATOM   3346 O  O    . LEU   B 1 183 ? 18.55  34.223 67.151  1 62.98  ? 182 LEU   B O    1 2 
ATOM   3347 C  CB   . LEU   B 1 183 ? 15.844 34.374 67.498  1 62.81  ? 182 LEU   B CB   1 2 
ATOM   3348 C  CG   . LEU   B 1 183 ? 14.393 34.712 67.787  1 63.72  ? 182 LEU   B CG   1 2 
ATOM   3349 C  CD1  . LEU   B 1 183 ? 13.803 33.756 68.789  1 64.11  ? 182 LEU   B CD1  1 2 
ATOM   3350 C  CD2  . LEU   B 1 183 ? 14.256 36.124 68.277  1 64.23  ? 182 LEU   B CD2  1 2 
ATOM   3351 N  N    . ILE   B 1 184 ? 18.697 35.38  65.225  1 62.11  ? 183 ILE   B N    1 2 
ATOM   3352 C  CA   . ILE   B 1 184 ? 20.135 35.121 65.063  1 61.44  ? 183 ILE   B CA   1 2 
ATOM   3353 C  C    . ILE   B 1 184 ? 20.974 35.848 66.121  1 60.08  ? 183 ILE   B C    1 2 
ATOM   3354 O  O    . ILE   B 1 184 ? 21.836 35.199 66.705  1 60.02  ? 183 ILE   B O    1 2 
ATOM   3355 C  CB   . ILE   B 1 184 ? 20.681 35.363 63.638  1 62.22  ? 183 ILE   B CB   1 2 
ATOM   3356 C  CG1  . ILE   B 1 184 ? 19.719 34.83  62.568  1 63.12  ? 183 ILE   B CG1  1 2 
ATOM   3357 C  CG2  . ILE   B 1 184 ? 22.089 34.762 63.507  1 62.9   ? 183 ILE   B CG2  1 2 
ATOM   3358 C  CD1  . ILE   B 1 184 ? 20.2   35.055 61.139  1 64.44  ? 183 ILE   B CD1  1 2 
ATOM   3359 N  N    . PRO   B 1 185 ? 20.742 37.147 66.432  1 58.93  ? 184 PRO   B N    1 2 
ATOM   3360 C  CA   . PRO   B 1 185 ? 21.538 37.78  67.491  1 58.26  ? 184 PRO   B CA   1 2 
ATOM   3361 C  C    . PRO   B 1 185 ? 21.26  37.14  68.856  1 57.84  ? 184 PRO   B C    1 2 
ATOM   3362 O  O    . PRO   B 1 185 ? 22.182 36.939 69.648  1 58.15  ? 184 PRO   B O    1 2 
ATOM   3363 C  CB   . PRO   B 1 185 ? 21.104 39.25  67.432  1 58.94  ? 184 PRO   B CB   1 2 
ATOM   3364 C  CG   . PRO   B 1 185 ? 19.744 39.225 66.85   1 59.59  ? 184 PRO   B CG   1 2 
ATOM   3365 C  CD   . PRO   B 1 185 ? 19.753 38.093 65.87   1 58.3   ? 184 PRO   B CD   1 2 
ATOM   3366 N  N    . TYR   B 1 186 ? 19.997 36.769 69.105  1 56.74  ? 185 TYR   B N    1 2 
ATOM   3367 C  CA   . TYR   B 1 186 ? 19.565 36.14  70.347  1 55.93  ? 185 TYR   B CA   1 2 
ATOM   3368 C  C    . TYR   B 1 186 ? 20.118 34.725 70.489  1 54.27  ? 185 TYR   B C    1 2 
ATOM   3369 O  O    . TYR   B 1 186 ? 20.575 34.362 71.564  1 54.12  ? 185 TYR   B O    1 2 
ATOM   3370 C  CB   . TYR   B 1 186 ? 18.033 36.142 70.416  1 56.21  ? 185 TYR   B CB   1 2 
ATOM   3371 C  CG   . TYR   B 1 186 ? 17.457 35.344 71.559  1 57     ? 185 TYR   B CG   1 2 
ATOM   3372 C  CD1  . TYR   B 1 186 ? 17.376 35.88  72.835  1 57.8   ? 185 TYR   B CD1  1 2 
ATOM   3373 C  CD2  . TYR   B 1 186 ? 16.948 34.073 71.354  1 58.07  ? 185 TYR   B CD2  1 2 
ATOM   3374 C  CE1  . TYR   B 1 186 ? 16.798 35.172 73.876  1 58.93  ? 185 TYR   B CE1  1 2 
ATOM   3375 C  CE2  . TYR   B 1 186 ? 16.387 33.346 72.391  1 59.19  ? 185 TYR   B CE2  1 2 
ATOM   3376 C  CZ   . TYR   B 1 186 ? 16.303 33.902 73.65   1 60.19  ? 185 TYR   B CZ   1 2 
ATOM   3377 O  OH   . TYR   B 1 186 ? 15.73  33.174 74.664  1 62.24  ? 185 TYR   B OH   1 2 
ATOM   3378 N  N    . CYS   B 1 187 ? 20.056 33.925 69.425  1 52.89  ? 186 CYS   B N    1 2 
ATOM   3379 C  CA   . CYS   B 1 187 ? 20.578 32.559 69.439  1 52.01  ? 186 CYS   B CA   1 2 
ATOM   3380 C  C    . CYS   B 1 187 ? 22.081 32.563 69.606  1 50.05  ? 186 CYS   B C    1 2 
ATOM   3381 O  O    . CYS   B 1 187 ? 22.612 31.69  70.278  1 50.02  ? 186 CYS   B O    1 2 
ATOM   3382 C  CB   . CYS   B 1 187 ? 20.17  31.789 68.187  1 53.12  ? 186 CYS   B CB   1 2 
ATOM   3383 S  SG   . CYS   B 1 187 ? 18.381 31.582 67.989  1 56.93  ? 186 CYS   B SG   1 2 
ATOM   3384 N  N    . SER   B 1 188 ? 22.769 33.543 69.014  1 48.25  ? 187 SER   B N    1 2 
ATOM   3385 C  CA   . SER   B 1 188 ? 24.205 33.654 69.144  1 47.24  ? 187 SER   B CA   1 2 
ATOM   3386 C  C    . SER   B 1 188 ? 24.589 33.906 70.6    1 46.61  ? 187 SER   B C    1 2 
ATOM   3387 O  O    . SER   B 1 188 ? 25.548 33.313 71.079  1 47.3   ? 187 SER   B O    1 2 
ATOM   3388 C  CB   . SER   B 1 188 ? 24.714 34.791 68.28   1 48.22  ? 187 SER   B CB   1 2 
ATOM   3389 O  OG   . SER   B 1 188 ? 26.108 34.651 68.097  1 50.41  ? 187 SER   B OG   1 2 
ATOM   3390 N  N    . SER   B 1 189 ? 23.805 34.727 71.33   1 44.91  ? 188 SER   B N    1 2 
ATOM   3391 C  CA   . SER   B 1 189 ? 24.073 35.003 72.735  1 43.27  ? 188 SER   B CA   1 2 
ATOM   3392 C  C    . SER   B 1 189 ? 23.663 33.828 73.625  1 42.73  ? 188 SER   B C    1 2 
ATOM   3393 O  O    . SER   B 1 189 ? 24.374 33.517 74.572  1 43.2   ? 188 SER   B O    1 2 
ATOM   3394 C  CB   . SER   B 1 189 ? 23.373 36.282 73.17   1 43.45  ? 188 SER   B CB   1 2 
ATOM   3395 O  OG   . SER   B 1 189 ? 21.976 36.082 73.284  1 44.8   ? 188 SER   B OG   1 2 
ATOM   3396 N  N    . LYS   B 1 190 ? 22.547 33.158 73.324  1 42.1   ? 189 LYS   B N    1 2 
ATOM   3397 C  CA   . LYS   B 1 190 ? 22.117 31.996 74.101  1 42.37  ? 189 LYS   B CA   1 2 
ATOM   3398 C  C    . LYS   B 1 190 ? 23.104 30.843 73.94   1 43.54  ? 189 LYS   B C    1 2 
ATOM   3399 O  O    . LYS   B 1 190 ? 23.385 30.162 74.917  1 43.68  ? 189 LYS   B O    1 2 
ATOM   3400 C  CB   . LYS   B 1 190 ? 20.684 31.572 73.765  1 43.11  ? 189 LYS   B CB   1 2 
ATOM   3401 C  CG   . LYS   B 1 190 ? 19.64  32.539 74.297  1 44.93  ? 189 LYS   B CG   1 2 
ATOM   3402 C  CD   . LYS   B 1 190 ? 19.562 32.543 75.81   1 46.9   ? 189 LYS   B CD   1 2 
ATOM   3403 C  CE   . LYS   B 1 190 ? 19.783 33.908 76.426  1 49.65  ? 189 LYS   B CE   1 2 
ATOM   3404 N  NZ   . LYS   B 1 190 ? 19.964 33.835 77.908  1 51.64  ? 189 LYS   B NZ   1 2 
ATOM   3405 N  N    . PHE   B 1 191 ? 23.692 30.666 72.745  1 44.37  ? 190 PHE   B N    1 2 
ATOM   3406 C  CA   . PHE   B 1 191 ? 24.715 29.631 72.513  1 45.56  ? 190 PHE   B CA   1 2 
ATOM   3407 C  C    . PHE   B 1 191 ? 25.944 29.924 73.382  1 46.22  ? 190 PHE   B C    1 2 
ATOM   3408 O  O    . PHE   B 1 191 ? 26.55  29.007 73.919  1 46.19  ? 190 PHE   B O    1 2 
ATOM   3409 C  CB   . PHE   B 1 191 ? 25.152 29.626 71.042  1 45.82  ? 190 PHE   B CB   1 2 
ATOM   3410 C  CG   . PHE   B 1 191 ? 24.649 28.49  70.193  1 46.87  ? 190 PHE   B CG   1 2 
ATOM   3411 C  CD1  . PHE   B 1 191 ? 23.397 28.541 69.615  1 47.82  ? 190 PHE   B CD1  1 2 
ATOM   3412 C  CD2  . PHE   B 1 191 ? 25.469 27.419 69.884  1 47.97  ? 190 PHE   B CD2  1 2 
ATOM   3413 C  CE1  . PHE   B 1 191 ? 22.957 27.525 68.778  1 48.68  ? 190 PHE   B CE1  1 2 
ATOM   3414 C  CE2  . PHE   B 1 191 ? 25.028 26.404 69.042  1 48.76  ? 190 PHE   B CE2  1 2 
ATOM   3415 C  CZ   . PHE   B 1 191 ? 23.78  26.468 68.488  1 48.55  ? 190 PHE   B CZ   1 2 
ATOM   3416 N  N    . ALA   B 1 192 ? 26.309 31.21  73.504  1 46.58  ? 191 ALA   B N    1 2 
ATOM   3417 C  CA   . ALA   B 1 192 ? 27.424 31.694 74.306  1 47.15  ? 191 ALA   B CA   1 2 
ATOM   3418 C  C    . ALA   B 1 192 ? 27.179 31.412 75.772  1 47.41  ? 191 ALA   B C    1 2 
ATOM   3419 O  O    . ALA   B 1 192 ? 28.113 31.05  76.477  1 47.53  ? 191 ALA   B O    1 2 
ATOM   3420 C  CB   . ALA   B 1 192 ? 27.604 33.189 74.086  1 47.57  ? 191 ALA   B CB   1 2 
ATOM   3421 N  N    . ALA   B 1 193 ? 25.927 31.563 76.235  1 47.6   ? 192 ALA   B N    1 2 
ATOM   3422 C  CA   . ALA   B 1 193 ? 25.547 31.287 77.619  1 48.24  ? 192 ALA   B CA   1 2 
ATOM   3423 C  C    . ALA   B 1 193 ? 25.71  29.785 77.933  1 48.79  ? 192 ALA   B C    1 2 
ATOM   3424 O  O    . ALA   B 1 193 ? 26.25  29.436 78.981  1 48.94  ? 192 ALA   B O    1 2 
ATOM   3425 C  CB   . ALA   B 1 193 ? 24.116 31.739 77.871  1 48.34  ? 192 ALA   B CB   1 2 
ATOM   3426 N  N    . VAL   B 1 194 ? 25.303 28.899 76.997  1 48.88  ? 193 VAL   B N    1 2 
ATOM   3427 C  CA   . VAL   B 1 194 ? 25.447 27.439 77.133  1 48.86  ? 193 VAL   B CA   1 2 
ATOM   3428 C  C    . VAL   B 1 194 ? 26.933 27.009 77.154  1 49.2   ? 193 VAL   B C    1 2 
ATOM   3429 O  O    . VAL   B 1 194 ? 27.307 26.057 77.84   1 49.13  ? 193 VAL   B O    1 2 
ATOM   3430 C  CB   . VAL   B 1 194 ? 24.639 26.706 76.035  1 48.91  ? 193 VAL   B CB   1 2 
ATOM   3431 C  CG1  . VAL   B 1 194 ? 24.947 25.215 76.016  1 49.51  ? 193 VAL   B CG1  1 2 
ATOM   3432 C  CG2  . VAL   B 1 194 ? 23.146 26.941 76.212  1 48.94  ? 193 VAL   B CG2  1 2 
ATOM   3433 N  N    . GLY   B 1 195 ? 27.762 27.739 76.423  1 49.4   ? 194 GLY   B N    1 2 
ATOM   3434 C  CA   . GLY   B 1 195 ? 29.193 27.498 76.368  1 49.92  ? 194 GLY   B CA   1 2 
ATOM   3435 C  C    . GLY   B 1 195 ? 29.924 28.045 77.571  1 50.01  ? 194 GLY   B C    1 2 
ATOM   3436 O  O    . GLY   B 1 195 ? 30.917 27.465 78.006  1 50.05  ? 194 GLY   B O    1 2 
ATOM   3437 N  N    . PHE   B 1 196 ? 29.434 29.154 78.134  1 49.89  ? 195 PHE   B N    1 2 
ATOM   3438 C  CA   . PHE   B 1 196 ? 30.003 29.721 79.35   1 50.49  ? 195 PHE   B CA   1 2 
ATOM   3439 C  C    . PHE   B 1 196 ? 29.763 28.734 80.493  1 51.35  ? 195 PHE   B C    1 2 
ATOM   3440 O  O    . PHE   B 1 196 ? 30.66  28.503 81.289  1 51.72  ? 195 PHE   B O    1 2 
ATOM   3441 C  CB   . PHE   B 1 196 ? 29.357 31.074 79.665  1 50.28  ? 195 PHE   B CB   1 2 
ATOM   3442 C  CG   . PHE   B 1 196 ? 29.625 31.601 81.058  1 50.78  ? 195 PHE   B CG   1 2 
ATOM   3443 C  CD1  . PHE   B 1 196 ? 30.85  32.153 81.382  1 51.26  ? 195 PHE   B CD1  1 2 
ATOM   3444 C  CD2  . PHE   B 1 196 ? 28.654 31.528 82.046  1 51.47  ? 195 PHE   B CD2  1 2 
ATOM   3445 C  CE1  . PHE   B 1 196 ? 31.091 32.656 82.651  1 51.72  ? 195 PHE   B CE1  1 2 
ATOM   3446 C  CE2  . PHE   B 1 196 ? 28.911 32.003 83.329  1 51.91  ? 195 PHE   B CE2  1 2 
ATOM   3447 C  CZ   . PHE   B 1 196 ? 30.125 32.573 83.618  1 51.47  ? 195 PHE   B CZ   1 2 
ATOM   3448 N  N    . HIS   B 1 197 ? 28.56  28.144 80.535  1 51.63  ? 196 HIS   B N    1 2 
ATOM   3449 C  CA   . HIS   B 1 197 ? 28.182 27.141 81.496  1 52.77  ? 196 HIS   B CA   1 2 
ATOM   3450 C  C    . HIS   B 1 197 ? 29.067 25.902 81.325  1 53.88  ? 196 HIS   B C    1 2 
ATOM   3451 O  O    . HIS   B 1 197 ? 29.536 25.356 82.315  1 54.4   ? 196 HIS   B O    1 2 
ATOM   3452 C  CB   . HIS   B 1 197 ? 26.699 26.786 81.307  1 53.52  ? 196 HIS   B CB   1 2 
ATOM   3453 C  CG   . HIS   B 1 197 ? 26.263 25.599 82.106  1 55.38  ? 196 HIS   B CG   1 2 
ATOM   3454 N  ND1  . HIS   B 1 197 ? 26.098 25.674 83.48   1 56.89  ? 196 HIS   B ND1  1 2 
ATOM   3455 C  CD2  . HIS   B 1 197 ? 26.015 24.33  81.701  1 56.31  ? 196 HIS   B CD2  1 2 
ATOM   3456 C  CE1  . HIS   B 1 197 ? 25.726 24.462 83.857  1 57.47  ? 196 HIS   B CE1  1 2 
ATOM   3457 N  NE2  . HIS   B 1 197 ? 25.66  23.62  82.818  1 57.42  ? 196 HIS   B NE2  1 2 
ATOM   3458 N  N    . ARG   B 1 198 ? 29.3   25.466 80.087  1 54.25  ? 197 ARG   B N    1 2 
ATOM   3459 C  CA   . ARG   B 1 198 ? 30.107 24.285 79.79   1 55.27  ? 197 ARG   B CA   1 2 
ATOM   3460 C  C    . ARG   B 1 198 ? 31.601 24.474 80.082  1 55.53  ? 197 ARG   B C    1 2 
ATOM   3461 O  O    . ARG   B 1 198 ? 32.269 23.527 80.493  1 55.69  ? 197 ARG   B O    1 2 
ATOM   3462 C  CB   . ARG   B 1 198 ? 29.873 23.8   78.349  1 57.29  ? 197 ARG   B CB   1 2 
ATOM   3463 C  CG   . ARG   B 1 198 ? 29.143 22.465 78.311  1 61.64  ? 197 ARG   B CG   1 2 
ATOM   3464 C  CD   . ARG   B 1 198 ? 29.399 21.687 77.04   1 66.16  ? 197 ARG   B CD   1 2 
ATOM   3465 N  NE   . ARG   B 1 198 ? 28.411 21.987 76      1 70.33  ? 197 ARG   B NE   1 2 
ATOM   3466 C  CZ   . ARG   B 1 198 ? 27.24  21.367 75.878  1 73.26  ? 197 ARG   B CZ   1 2 
ATOM   3467 N  NH1  . ARG   B 1 198 ? 26.887 20.419 76.743  1 73.35  ? 197 ARG   B NH1  1 2 
ATOM   3468 N  NH2  . ARG   B 1 198 ? 26.41  21.691 74.891  1 72.9   ? 197 ARG   B NH2  1 2 
ATOM   3469 N  N    . GLY   B 1 199 ? 32.1   25.684 79.857  1 55.45  ? 198 GLY   B N    1 2 
ATOM   3470 C  CA   . GLY   B 1 199 ? 33.487 26.034 80.13   1 56.09  ? 198 GLY   B CA   1 2 
ATOM   3471 C  C    . GLY   B 1 199 ? 33.683 26.148 81.627  1 56.88  ? 198 GLY   B C    1 2 
ATOM   3472 O  O    . GLY   B 1 199 ? 34.627 25.589 82.194  1 57.17  ? 198 GLY   B O    1 2 
ATOM   3473 N  N    . LEU   B 1 200 ? 32.729 26.807 82.304  1 56.84  ? 199 LEU   B N    1 2 
ATOM   3474 C  CA   . LEU   B 1 200 ? 32.733 26.949 83.75   1 57.17  ? 199 LEU   B CA   1 2 
ATOM   3475 C  C    . LEU   B 1 200 ? 32.691 25.575 84.396  1 57.99  ? 199 LEU   B C    1 2 
ATOM   3476 O  O    . LEU   B 1 200 ? 33.45  25.338 85.319  1 58.7   ? 199 LEU   B O    1 2 
ATOM   3477 C  CB   . LEU   B 1 200 ? 31.538 27.793 84.209  1 57.28  ? 199 LEU   B CB   1 2 
ATOM   3478 C  CG   . LEU   B 1 200 ? 31.294 27.89  85.715  1 58.91  ? 199 LEU   B CG   1 2 
ATOM   3479 C  CD1  . LEU   B 1 200 ? 32.473 28.546 86.44   1 59.27  ? 199 LEU   B CD1  1 2 
ATOM   3480 C  CD2  . LEU   B 1 200 ? 30.02  28.643 85.997  1 59.79  ? 199 LEU   B CD2  1 2 
ATOM   3481 N  N    . THR   B 1 201 ? 31.887 24.651 83.857  1 57.87  ? 200 THR   B N    1 2 
ATOM   3482 C  CA   . THR   B 1 201 ? 31.794 23.297 84.379  1 58.54  ? 200 THR   B CA   1 2 
ATOM   3483 C  C    . THR   B 1 201 ? 33.155 22.583 84.272  1 60.45  ? 200 THR   B C    1 2 
ATOM   3484 O  O    . THR   B 1 201 ? 33.669 22.099 85.292  1 60.91  ? 200 THR   B O    1 2 
ATOM   3485 C  CB   . THR   B 1 201 ? 30.607 22.565 83.736  1 58.39  ? 200 THR   B CB   1 2 
ATOM   3486 O  OG1  . THR   B 1 201 ? 29.439 22.893 84.479  1 58.52  ? 200 THR   B OG1  1 2 
ATOM   3487 C  CG2  . THR   B 1 201 ? 30.763 21.059 83.719  1 58.55  ? 200 THR   B CG2  1 2 
ATOM   3488 N  N    . SER   B 1 202 ? 33.772 22.59  83.08   1 61.36  ? 201 SER   B N    1 2 
ATOM   3489 C  CA   . SER   B 1 202 ? 35.063 21.931 82.875  1 63.13  ? 201 SER   B CA   1 2 
ATOM   3490 C  C    . SER   B 1 202 ? 36.193 22.535 83.711  1 64.46  ? 201 SER   B C    1 2 
ATOM   3491 O  O    . SER   B 1 202 ? 37.015 21.795 84.252  1 64.61  ? 201 SER   B O    1 2 
ATOM   3492 C  CB   . SER   B 1 202 ? 35.443 21.865 81.396  1 65.35  ? 201 SER   B CB   1 2 
ATOM   3493 O  OG   . SER   B 1 202 ? 34.814 22.825 80.561  1 68.62  ? 201 SER   B OG   1 2 
ATOM   3494 N  N    . GLU   B 1 203 ? 36.207 23.869 83.86   1 65     ? 202 GLU   B N    1 2 
ATOM   3495 C  CA   . GLU   B 1 203 ? 37.225 24.548 84.659  1 65.69  ? 202 GLU   B CA   1 2 
ATOM   3496 C  C    . GLU   B 1 203 ? 37.003 24.314 86.147  1 66.33  ? 202 GLU   B C    1 2 
ATOM   3497 O  O    . GLU   B 1 203 ? 37.974 24.12  86.882  1 66.59  ? 202 GLU   B O    1 2 
ATOM   3498 C  CB   . GLU   B 1 203 ? 37.291 26.051 84.346  1 67.43  ? 202 GLU   B CB   1 2 
ATOM   3499 C  CG   . GLU   B 1 203 ? 38.551 26.703 84.887  1 70.95  ? 202 GLU   B CG   1 2 
ATOM   3500 C  CD   . GLU   B 1 203 ? 38.64  28.195 84.66   1 76.05  ? 202 GLU   B CD   1 2 
ATOM   3501 O  OE1  . GLU   B 1 203 ? 38.289 28.963 85.584  1 76.17  ? 202 GLU   B OE1  1 2 
ATOM   3502 O  OE2  . GLU   B 1 203 ? 39.049 28.597 83.549  1 78.87  ? 202 GLU   B OE2  1 2 
ATOM   3503 N  N    . LEU   B 1 204 ? 35.73  24.239 86.584  1 66.65  ? 203 LEU   B N    1 2 
ATOM   3504 C  CA   . LEU   B 1 204 ? 35.389 23.956 87.983  1 67.82  ? 203 LEU   B CA   1 2 
ATOM   3505 C  C    . LEU   B 1 204 ? 35.947 22.585 88.379  1 69.1   ? 203 LEU   B C    1 2 
ATOM   3506 O  O    . LEU   B 1 204 ? 36.536 22.438 89.441  1 68.85  ? 203 LEU   B O    1 2 
ATOM   3507 C  CB   . LEU   B 1 204 ? 33.862 23.975 88.205  1 67.83  ? 203 LEU   B CB   1 2 
ATOM   3508 C  CG   . LEU   B 1 204 ? 33.203 25.335 88.446  1 68.94  ? 203 LEU   B CG   1 2 
ATOM   3509 C  CD1  . LEU   B 1 204 ? 31.716 25.182 88.617  1 69.42  ? 203 LEU   B CD1  1 2 
ATOM   3510 C  CD2  . LEU   B 1 204 ? 33.799 26.05  89.639  1 69.4   ? 203 LEU   B CD2  1 2 
ATOM   3511 N  N    . GLN   B 1 205 ? 35.804 21.605 87.483  1 70.26  ? 204 GLN   B N    1 2 
ATOM   3512 C  CA   . GLN   B 1 205 ? 36.293 20.245 87.65   1 71.68  ? 204 GLN   B CA   1 2 
ATOM   3513 C  C    . GLN   B 1 205 ? 37.829 20.184 87.586  1 72.72  ? 204 GLN   B C    1 2 
ATOM   3514 O  O    . GLN   B 1 205 ? 38.456 19.516 88.411  1 73.01  ? 204 GLN   B O    1 2 
ATOM   3515 C  CB   . GLN   B 1 205 ? 35.663 19.342 86.575  1 73.4   ? 204 GLN   B CB   1 2 
ATOM   3516 C  CG   . GLN   B 1 205 ? 36.016 17.861 86.716  1 77.08  ? 204 GLN   B CG   1 2 
ATOM   3517 C  CD   . GLN   B 1 205 ? 37.097 17.411 85.756  1 82.1   ? 204 GLN   B CD   1 2 
ATOM   3518 O  OE1  . GLN   B 1 205 ? 37.999 16.644 86.121  1 83.3   ? 204 GLN   B OE1  1 2 
ATOM   3519 N  NE2  . GLN   B 1 205 ? 37.03  17.874 84.502  1 83.2   ? 204 GLN   B NE2  1 2 
ATOM   3520 N  N    . ALA   B 1 206 ? 38.432 20.892 86.619  1 73.09  ? 205 ALA   B N    1 2 
ATOM   3521 C  CA   . ALA   B 1 206 ? 39.884 20.91  86.439  1 73.8   ? 205 ALA   B CA   1 2 
ATOM   3522 C  C    . ALA   B 1 206 ? 40.63  21.553 87.591  1 73.98  ? 205 ALA   B C    1 2 
ATOM   3523 O  O    . ALA   B 1 206 ? 41.787 21.21  87.815  1 74.18  ? 205 ALA   B O    1 2 
ATOM   3524 C  CB   . ALA   B 1 206 ? 40.248 21.606 85.137  1 74.19  ? 205 ALA   B CB   1 2 
ATOM   3525 N  N    . LEU   B 1 207 ? 39.99  22.479 88.316  1 73.87  ? 206 LEU   B N    1 2 
ATOM   3526 C  CA   . LEU   B 1 207 ? 40.649 23.129 89.448  1 74.32  ? 206 LEU   B CA   1 2 
ATOM   3527 C  C    . LEU   B 1 207 ? 40.457 22.421 90.808  1 74.99  ? 206 LEU   B C    1 2 
ATOM   3528 O  O    . LEU   B 1 207 ? 40.915 22.93  91.83   1 74.97  ? 206 LEU   B O    1 2 
ATOM   3529 C  CB   . LEU   B 1 207 ? 40.228 24.598 89.545  1 74.2   ? 206 LEU   B CB   1 2 
ATOM   3530 C  CG   . LEU   B 1 207 ? 40.499 25.469 88.332  1 74.99  ? 206 LEU   B CG   1 2 
ATOM   3531 C  CD1  . LEU   B 1 207 ? 40.1   26.893 88.612  1 75.3   ? 206 LEU   B CD1  1 2 
ATOM   3532 C  CD2  . LEU   B 1 207 ? 41.955 25.415 87.923  1 75.59  ? 206 LEU   B CD2  1 2 
ATOM   3533 N  N    . GLY   B 1 208 ? 39.796 21.266 90.812  1 75.46  ? 207 GLY   B N    1 2 
ATOM   3534 C  CA   . GLY   B 1 208 ? 39.547 20.509 92.034  1 76.38  ? 207 GLY   B CA   1 2 
ATOM   3535 C  C    . GLY   B 1 208 ? 38.342 20.962 92.841  1 77.37  ? 207 GLY   B C    1 2 
ATOM   3536 O  O    . GLY   B 1 208 ? 38.064 20.391 93.896  1 78.15  ? 207 GLY   B O    1 2 
ATOM   3537 N  N    . ILE   B 1 209 ? 37.62  21.997 92.377  1 77.4   ? 208 ILE   B N    1 2 
ATOM   3538 C  CA   . ILE   B 1 209 ? 36.447 22.513 93.089  1 77.89  ? 208 ILE   B CA   1 2 
ATOM   3539 C  C    . ILE   B 1 209 ? 35.263 21.555 92.939  1 78.68  ? 208 ILE   B C    1 2 
ATOM   3540 O  O    . ILE   B 1 209 ? 34.822 21.26  91.832  1 78.85  ? 208 ILE   B O    1 2 
ATOM   3541 C  CB   . ILE   B 1 209 ? 36.101 23.993 92.725  1 78.06  ? 208 ILE   B CB   1 2 
ATOM   3542 C  CG1  . ILE   B 1 209 ? 37.055 24.979 93.429  1 79.08  ? 208 ILE   B CG1  1 2 
ATOM   3543 C  CG2  . ILE   B 1 209 ? 34.662 24.348 93.094  1 78.25  ? 208 ILE   B CG2  1 2 
ATOM   3544 C  CD1  . ILE   B 1 209 ? 38.424 25.115 92.854  1 80.4   ? 208 ILE   B CD1  1 2 
ATOM   3545 N  N    . THR   B 1 210 ? 34.773 21.053 94.062  1 79.18  ? 209 THR   B N    1 2 
ATOM   3546 C  CA   . THR   B 1 210 ? 33.658 20.118 94.075  1 80.12  ? 209 THR   B CA   1 2 
ATOM   3547 C  C    . THR   B 1 210 ? 32.355 20.778 94.512  1 80.02  ? 209 THR   B C    1 2 
ATOM   3548 O  O    . THR   B 1 210 ? 31.345 20.655 93.816  1 80.36  ? 209 THR   B O    1 2 
ATOM   3549 C  CB   . THR   B 1 210 ? 33.989 18.859 94.903  1 82.33  ? 209 THR   B CB   1 2 
ATOM   3550 O  OG1  . THR   B 1 210 ? 34.788 19.181 96.061  1 83.52  ? 209 THR   B OG1  1 2 
ATOM   3551 C  CG2  . THR   B 1 210 ? 34.663 17.782 94.062  1 83.09  ? 209 THR   B CG2  1 2 
ATOM   3552 N  N    . GLY   B 1 211 ? 32.405 21.496 95.633  1 79.28  ? 210 GLY   B N    1 2 
ATOM   3553 C  CA   . GLY   B 1 211 ? 31.264 22.175 96.243  1 79.09  ? 210 GLY   B CA   1 2 
ATOM   3554 C  C    . GLY   B 1 211 ? 30.46  23.138 95.386  1 78.6   ? 210 GLY   B C    1 2 
ATOM   3555 O  O    . GLY   B 1 211 ? 29.304 23.427 95.712  1 78.54  ? 210 GLY   B O    1 2 
ATOM   3556 N  N    . ILE   B 1 212 ? 31.051 23.65  94.289  1 77.99  ? 211 ILE   B N    1 2 
ATOM   3557 C  CA   . ILE   B 1 212 ? 30.329 24.558 93.397  1 77.7   ? 211 ILE   B CA   1 2 
ATOM   3558 C  C    . ILE   B 1 212 ? 29.717 23.799 92.242  1 76.72  ? 211 ILE   B C    1 2 
ATOM   3559 O  O    . ILE   B 1 212 ? 30.429 23.364 91.34   1 76.66  ? 211 ILE   B O    1 2 
ATOM   3560 C  CB   . ILE   B 1 212 ? 31.19  25.734 92.9    1 78.43  ? 211 ILE   B CB   1 2 
ATOM   3561 C  CG1  . ILE   B 1 212 ? 31.797 26.498 94.088  1 79.92  ? 211 ILE   B CG1  1 2 
ATOM   3562 C  CG2  . ILE   B 1 212 ? 30.36  26.651 92.01   1 78.66  ? 211 ILE   B CG2  1 2 
ATOM   3563 C  CD1  . ILE   B 1 212 ? 32.795 27.532 93.694  1 81.52  ? 211 ILE   B CD1  1 2 
ATOM   3564 N  N    . LYS   B 1 213 ? 28.397 23.626 92.275  1 75.89  ? 212 LYS   B N    1 2 
ATOM   3565 C  CA   . LYS   B 1 213 ? 27.685 22.92  91.213  1 75.68  ? 212 LYS   B CA   1 2 
ATOM   3566 C  C    . LYS   B 1 213 ? 27.216 23.907 90.117  1 74.79  ? 212 LYS   B C    1 2 
ATOM   3567 O  O    . LYS   B 1 213 ? 27.27  25.121 90.314  1 75.13  ? 212 LYS   B O    1 2 
ATOM   3568 C  CB   . LYS   B 1 213 ? 26.489 22.138 91.793  1 77.54  ? 212 LYS   B CB   1 2 
ATOM   3569 C  CG   . LYS   B 1 213 ? 26.794 21.342 93.046  1 81.62  ? 212 LYS   B CG   1 2 
ATOM   3570 C  CD   . LYS   B 1 213 ? 27.803 20.227 92.826  1 86.8   ? 212 LYS   B CD   1 2 
ATOM   3571 C  CE   . LYS   B 1 213 ? 27.96  19.436 94.107  1 92.08  ? 212 LYS   B CE   1 2 
ATOM   3572 N  NZ   . LYS   B 1 213 ? 29.037 18.409 94.027  1 95.17  ? 212 LYS   B NZ   1 2 
ATOM   3573 N  N    . THR   B 1 214 ? 26.784 23.394 88.955  1 73.41  ? 213 THR   B N    1 2 
ATOM   3574 C  CA   . THR   B 1 214 ? 26.295 24.247 87.871  1 72.59  ? 213 THR   B CA   1 2 
ATOM   3575 C  C    . THR   B 1 214 ? 25.049 23.653 87.225  1 71.5   ? 213 THR   B C    1 2 
ATOM   3576 O  O    . THR   B 1 214 ? 25.005 22.457 86.95   1 71.83  ? 213 THR   B O    1 2 
ATOM   3577 C  CB   . THR   B 1 214 ? 27.372 24.489 86.796  1 73.58  ? 213 THR   B CB   1 2 
ATOM   3578 O  OG1  . THR   B 1 214 ? 28.011 23.257 86.465  1 74.48  ? 213 THR   B OG1  1 2 
ATOM   3579 C  CG2  . THR   B 1 214 ? 28.405 25.524 87.202  1 73.83  ? 213 THR   B CG2  1 2 
ATOM   3580 N  N    . SER   B 1 215 ? 24.041 24.485 86.972  1 70.01  ? 214 SER   B N    1 2 
ATOM   3581 C  CA   . SER   B 1 215 ? 22.821 24.064 86.292  1 69.09  ? 214 SER   B CA   1 2 
ATOM   3582 C  C    . SER   B 1 215 ? 22.532 25.041 85.173  1 68.32  ? 214 SER   B C    1 2 
ATOM   3583 O  O    . SER   B 1 215 ? 22.805 26.231 85.306  1 68.36  ? 214 SER   B O    1 2 
ATOM   3584 C  CB   . SER   B 1 215 ? 21.639 24.02  87.252  1 70.2   ? 214 SER   B CB   1 2 
ATOM   3585 O  OG   . SER   B 1 215 ? 21.461 22.709 87.761  1 72.44  ? 214 SER   B OG   1 2 
ATOM   3586 N  N    . CYS   B 1 216 ? 22.001 24.549 84.057  1 67.61  ? 215 CYS   B N    1 2 
ATOM   3587 C  CA   . CYS   B 1 216 ? 21.689 25.4   82.914  1 67.09  ? 215 CYS   B CA   1 2 
ATOM   3588 C  C    . CYS   B 1 216 ? 20.28  25.12  82.47   1 66.39  ? 215 CYS   B C    1 2 
ATOM   3589 O  O    . CYS   B 1 216 ? 20.007 24.008 82.041  1 66.38  ? 215 CYS   B O    1 2 
ATOM   3590 C  CB   . CYS   B 1 216 ? 22.685 25.163 81.784  1 67.63  ? 215 CYS   B CB   1 2 
ATOM   3591 S  SG   . CYS   B 1 216 ? 22.313 26.058 80.256  1 71.29  ? 215 CYS   B SG   1 2 
ATOM   3592 N  N    . LEU   B 1 217 ? 19.381 26.104 82.566  1 65.86  ? 216 LEU   B N    1 2 
ATOM   3593 C  CA   . LEU   B 1 217 ? 17.998 25.9   82.139  1 66.03  ? 216 LEU   B CA   1 2 
ATOM   3594 C  C    . LEU   B 1 217 ? 17.823 26.176 80.63   1 65.51  ? 216 LEU   B C    1 2 
ATOM   3595 O  O    . LEU   B 1 217 ? 18.077 27.287 80.176  1 65.18  ? 216 LEU   B O    1 2 
ATOM   3596 C  CB   . LEU   B 1 217 ? 17.044 26.755 82.979  1 66.64  ? 216 LEU   B CB   1 2 
ATOM   3597 C  CG   . LEU   B 1 217 ? 15.562 26.525 82.712  1 68.74  ? 216 LEU   B CG   1 2 
ATOM   3598 C  CD1  . LEU   B 1 217 ? 15.079 25.263 83.376  1 69.37  ? 216 LEU   B CD1  1 2 
ATOM   3599 C  CD2  . LEU   B 1 217 ? 14.74  27.691 83.197  1 69.73  ? 216 LEU   B CD2  1 2 
ATOM   3600 N  N    . CYS   B 1 218 ? 17.414 25.155 79.858  1 65.28  ? 217 CYS   B N    1 2 
ATOM   3601 C  CA   . CYS   B 1 218 ? 17.217 25.248 78.408  1 65.59  ? 217 CYS   B CA   1 2 
ATOM   3602 C  C    . CYS   B 1 218 ? 15.779 24.895 77.99   1 65.99  ? 217 CYS   B C    1 2 
ATOM   3603 O  O    . CYS   B 1 218 ? 15.554 23.806 77.462  1 66.06  ? 217 CYS   B O    1 2 
ATOM   3604 C  CB   . CYS   B 1 218 ? 18.231 24.376 77.671  1 65.79  ? 217 CYS   B CB   1 2 
ATOM   3605 S  SG   . CYS   B 1 218 ? 19.906 25.057 77.619  1 68.13  ? 217 CYS   B SG   1 2 
ATOM   3606 N  N    . PRO   B 1 219 ? 14.796 25.795 78.173  1 66.17  ? 218 PRO   B N    1 2 
ATOM   3607 C  CA   . PRO   B 1 219 ? 13.42  25.465 77.776  1 66.33  ? 218 PRO   B CA   1 2 
ATOM   3608 C  C    . PRO   B 1 219 ? 13.06  25.889 76.348  1 66.43  ? 218 PRO   B C    1 2 
ATOM   3609 O  O    . PRO   B 1 219 ? 13.849 26.555 75.687  1 66.59  ? 218 PRO   B O    1 2 
ATOM   3610 C  CB   . PRO   B 1 219 ? 12.577 26.21  78.817  1 67.14  ? 218 PRO   B CB   1 2 
ATOM   3611 C  CG   . PRO   B 1 219 ? 13.465 27.323 79.332  1 67.58  ? 218 PRO   B CG   1 2 
ATOM   3612 C  CD   . PRO   B 1 219 ? 14.859 27.128 78.798  1 65.9   ? 218 PRO   B CD   1 2 
ATOM   3613 N  N    . VAL   B 1 220 ? 11.867 25.493 75.864  1 66.28  ? 219 VAL   B N    1 2 
ATOM   3614 C  CA   . VAL   B 1 220 ? 11.38  25.883 74.534  1 66.79  ? 219 VAL   B CA   1 2 
ATOM   3615 C  C    . VAL   B 1 220 ? 10.512 27.189 74.688  1 66.91  ? 219 VAL   B C    1 2 
ATOM   3616 O  O    . VAL   B 1 220 ? 10.897 28.006 75.519  1 67.06  ? 219 VAL   B O    1 2 
ATOM   3617 C  CB   . VAL   B 1 220 ? 10.715 24.682 73.79   1 67.77  ? 219 VAL   B CB   1 2 
ATOM   3618 C  CG1  . VAL   B 1 220 ? 11.735 23.586 73.508  1 68.44  ? 219 VAL   B CG1  1 2 
ATOM   3619 C  CG2  . VAL   B 1 220 ? 9.536  24.126 74.579  1 68.4   ? 219 VAL   B CG2  1 2 
ATOM   3620 N  N    . PHE   B 1 221 ? 9.405  27.423 73.938  1 66.93  ? 220 PHE   B N    1 2 
ATOM   3621 C  CA   . PHE   B 1 221 ? 8.614  28.642 74.122  1 67.83  ? 220 PHE   B CA   1 2 
ATOM   3622 C  C    . PHE   B 1 221 ? 7.838  28.62  75.426  1 68     ? 220 PHE   B C    1 2 
ATOM   3623 O  O    . PHE   B 1 221 ? 6.976  27.775 75.638  1 67.89  ? 220 PHE   B O    1 2 
ATOM   3624 C  CB   . PHE   B 1 221 ? 7.679  28.943 72.93   1 68.36  ? 220 PHE   B CB   1 2 
ATOM   3625 C  CG   . PHE   B 1 221 ? 6.92   30.255 73.034  1 69.33  ? 220 PHE   B CG   1 2 
ATOM   3626 C  CD1  . PHE   B 1 221 ? 5.595  30.279 73.434  1 70.16  ? 220 PHE   B CD1  1 2 
ATOM   3627 C  CD2  . PHE   B 1 221 ? 7.525  31.455 72.704  1 70.2   ? 220 PHE   B CD2  1 2 
ATOM   3628 C  CE1  . PHE   B 1 221 ? 4.902  31.479 73.527  1 70.83  ? 220 PHE   B CE1  1 2 
ATOM   3629 C  CE2  . PHE   B 1 221 ? 6.82   32.65  72.782  1 70.89  ? 220 PHE   B CE2  1 2 
ATOM   3630 C  CZ   . PHE   B 1 221 ? 5.52   32.656 73.203  1 70.66  ? 220 PHE   B CZ   1 2 
ATOM   3631 N  N    . VAL   B 1 222 ? 8.157  29.562 76.295  1 68.15  ? 221 VAL   B N    1 2 
ATOM   3632 C  CA   . VAL   B 1 222 ? 7.492  29.74  77.575  1 68.74  ? 221 VAL   B CA   1 2 
ATOM   3633 C  C    . VAL   B 1 222 ? 6.548  30.939 77.395  1 69.22  ? 221 VAL   B C    1 2 
ATOM   3634 O  O    . VAL   B 1 222 ? 6.957  31.978 76.876  1 69.47  ? 221 VAL   B O    1 2 
ATOM   3635 C  CB   . VAL   B 1 222 ? 8.524  29.999 78.708  1 69.64  ? 221 VAL   B CB   1 2 
ATOM   3636 C  CG1  . VAL   B 1 222 ? 7.852  30.012 80.077  1 70.24  ? 221 VAL   B CG1  1 2 
ATOM   3637 C  CG2  . VAL   B 1 222 ? 9.667  28.986 78.673  1 70.13  ? 221 VAL   B CG2  1 2 
ATOM   3638 N  N    . ASN   B 1 223 ? 5.288  30.785 77.781  1 69.31  ? 222 ASN   B N    1 2 
ATOM   3639 C  CA   . ASN   B 1 223 ? 4.271  31.827 77.669  1 70.16  ? 222 ASN   B CA   1 2 
ATOM   3640 C  C    . ASN   B 1 223 ? 4.506  32.943 78.704  1 70.69  ? 222 ASN   B C    1 2 
ATOM   3641 O  O    . ASN   B 1 223 ? 3.894  32.923 79.771  1 71.09  ? 222 ASN   B O    1 2 
ATOM   3642 C  CB   . ASN   B 1 223 ? 2.895  31.195 77.872  1 71.53  ? 222 ASN   B CB   1 2 
ATOM   3643 C  CG   . ASN   B 1 223 ? 1.746  32.145 77.717  1 75.38  ? 222 ASN   B CG   1 2 
ATOM   3644 O  OD1  . ASN   B 1 223 ? 1.83   33.156 77.01   1 76.63  ? 222 ASN   B OD1  1 2 
ATOM   3645 N  ND2  . ASN   B 1 223 ? 0.645  31.835 78.383  1 76.51  ? 222 ASN   B ND2  1 2 
ATOM   3646 N  N    . THR   B 1 224 ? 5.409  33.896 78.411  1 70.56  ? 223 THR   B N    1 2 
ATOM   3647 C  CA   . THR   B 1 224 ? 5.713  35.002 79.335  1 70.82  ? 223 THR   B CA   1 2 
ATOM   3648 C  C    . THR   B 1 224 ? 5.52   36.394 78.727  1 71.08  ? 223 THR   B C    1 2 
ATOM   3649 O  O    . THR   B 1 224 ? 5.468  37.386 79.453  1 70.68  ? 223 THR   B O    1 2 
ATOM   3650 C  CB   . THR   B 1 224 ? 7.163  34.916 79.846  1 71.7   ? 223 THR   B CB   1 2 
ATOM   3651 O  OG1  . THR   B 1 224 ? 8.058  35.039 78.741  1 72.79  ? 223 THR   B OG1  1 2 
ATOM   3652 C  CG2  . THR   B 1 224 ? 7.444  33.649 80.632  1 71.69  ? 223 THR   B CG2  1 2 
ATOM   3653 N  N    . GLY   B 1 225 ? 5.461  36.462 77.409  1 71.7   ? 224 GLY   B N    1 2 
ATOM   3654 C  CA   . GLY   B 1 225 ? 5.363  37.727 76.698  1 72.78  ? 224 GLY   B CA   1 2 
ATOM   3655 C  C    . GLY   B 1 225 ? 6.72   38.268 76.271  1 73.4   ? 224 GLY   B C    1 2 
ATOM   3656 O  O    . GLY   B 1 225 ? 6.805  39.391 75.759  1 73.57  ? 224 GLY   B O    1 2 
ATOM   3657 N  N    . PHE   B 1 226 ? 7.8    37.467 76.478  1 73.31  ? 225 PHE   B N    1 2 
ATOM   3658 C  CA   . PHE   B 1 226 ? 9.18   37.762 76.091  1 73.54  ? 225 PHE   B CA   1 2 
ATOM   3659 C  C    . PHE   B 1 226 ? 9.183  37.979 74.561  1 74.69  ? 225 PHE   B C    1 2 
ATOM   3660 O  O    . PHE   B 1 226 ? 9.615  39.03  74.073  1 74.86  ? 225 PHE   B O    1 2 
ATOM   3661 C  CB   . PHE   B 1 226 ? 10.054 36.555 76.49   1 72.6   ? 225 PHE   B CB   1 2 
ATOM   3662 C  CG   . PHE   B 1 226 ? 11.543 36.691 76.334  1 72.36  ? 225 PHE   B CG   1 2 
ATOM   3663 C  CD1  . PHE   B 1 226 ? 12.233 37.688 76.989  1 72.79  ? 225 PHE   B CD1  1 2 
ATOM   3664 C  CD2  . PHE   B 1 226 ? 12.267 35.76  75.611  1 72.8   ? 225 PHE   B CD2  1 2 
ATOM   3665 C  CE1  . PHE   B 1 226 ? 13.611 37.786 76.879  1 73.34  ? 225 PHE   B CE1  1 2 
ATOM   3666 C  CE2  . PHE   B 1 226 ? 13.645 35.86  75.503  1 73.34  ? 225 PHE   B CE2  1 2 
ATOM   3667 C  CZ   . PHE   B 1 226 ? 14.308 36.876 76.13   1 73.06  ? 225 PHE   B CZ   1 2 
ATOM   3668 N  N    . THR   B 1 227 ? 8.602  36.991 73.838  1 75.17  ? 226 THR   B N    1 2 
ATOM   3669 C  CA   . THR   B 1 227 ? 8.408  36.911 72.39   1 76.1   ? 226 THR   B CA   1 2 
ATOM   3670 C  C    . THR   B 1 227 ? 6.915  36.68  72.115  1 76.61  ? 226 THR   B C    1 2 
ATOM   3671 O  O    . THR   B 1 227 ? 6.24   36.01  72.904  1 76.67  ? 226 THR   B O    1 2 
ATOM   3672 C  CB   . THR   B 1 227 ? 9.303  35.828 71.75   1 77.73  ? 226 THR   B CB   1 2 
ATOM   3673 O  OG1  . THR   B 1 227 ? 9.395  34.679 72.597  1 78.94  ? 226 THR   B OG1  1 2 
ATOM   3674 C  CG2  . THR   B 1 227 ? 10.695 36.336 71.426  1 78.03  ? 226 THR   B CG2  1 2 
ATOM   3675 N  N    . LYS   B 1 228 ? 6.397  37.25  71.011  1 76.75  ? 227 LYS   B N    1 2 
ATOM   3676 C  CA   . LYS   B 1 228 ? 4.977  37.206 70.706  1 77.49  ? 227 LYS   B CA   1 2 
ATOM   3677 C  C    . LYS   B 1 228 ? 4.438  35.79  70.443  1 78.22  ? 227 LYS   B C    1 2 
ATOM   3678 O  O    . LYS   B 1 228 ? 3.538  35.337 71.15   1 78.36  ? 227 LYS   B O    1 2 
ATOM   3679 C  CB   . LYS   B 1 228 ? 4.625  38.181 69.555  1 79.05  ? 227 LYS   B CB   1 2 
ATOM   3680 C  CG   . LYS   B 1 228 ? 3.985  39.505 70.012  1 82.41  ? 227 LYS   B CG   1 2 
ATOM   3681 C  CD   . LYS   B 1 228 ? 2.628  39.299 70.72   1 86.43  ? 227 LYS   B CD   1 2 
ATOM   3682 C  CE   . LYS   B 1 228 ? 2.691  39.553 72.227  1 89.55  ? 227 LYS   B CE   1 2 
ATOM   3683 N  NZ   . LYS   B 1 228 ? 1.593  38.894 73.006  1 90.85  ? 227 LYS   B NZ   1 2 
ATOM   3684 N  N    . ASN   B 1 229 ? 4.982  35.091 69.447  1 78.55  ? 228 ASN   B N    1 2 
ATOM   3685 C  CA   . ASN   B 1 229 ? 4.506  33.756 69.087  1 79.38  ? 228 ASN   B CA   1 2 
ATOM   3686 C  C    . ASN   B 1 229 ? 5.626  32.702 69.192  1 79.8   ? 228 ASN   B C    1 2 
ATOM   3687 O  O    . ASN   B 1 229 ? 6.811  33.052 69.142  1 79.71  ? 228 ASN   B O    1 2 
ATOM   3688 C  CB   . ASN   B 1 229 ? 3.894  33.787 67.67   1 80.83  ? 228 ASN   B CB   1 2 
ATOM   3689 C  CG   . ASN   B 1 229 ? 2.809  34.835 67.481  1 83.86  ? 228 ASN   B CG   1 2 
ATOM   3690 O  OD1  . ASN   B 1 229 ? 1.879  34.971 68.294  1 85.11  ? 228 ASN   B OD1  1 2 
ATOM   3691 N  ND2  . ASN   B 1 229 ? 2.9    35.59  66.39   1 84.04  ? 228 ASN   B ND2  1 2 
ATOM   3692 N  N    . PRO   B 1 230 ? 5.276  31.405 69.341  1 80.11  ? 229 PRO   B N    1 2 
ATOM   3693 C  CA   . PRO   B 1 230 ? 6.32   30.384 69.484  1 80.42  ? 229 PRO   B CA   1 2 
ATOM   3694 C  C    . PRO   B 1 230 ? 7.173  30.16  68.242  1 80.72  ? 229 PRO   B C    1 2 
ATOM   3695 O  O    . PRO   B 1 230 ? 6.773  30.513 67.138  1 80.91  ? 229 PRO   B O    1 2 
ATOM   3696 C  CB   . PRO   B 1 230 ? 5.54   29.124 69.876  1 81.04  ? 229 PRO   B CB   1 2 
ATOM   3697 C  CG   . PRO   B 1 230 ? 4.189  29.339 69.331  1 81.4   ? 229 PRO   B CG   1 2 
ATOM   3698 C  CD   . PRO   B 1 230 ? 3.929  30.811 69.457  1 79.73  ? 229 PRO   B CD   1 2 
ATOM   3699 N  N    . SER   B 1 231 ? 8.356  29.558 68.437  1 80.6   ? 230 SER   B N    1 2 
ATOM   3700 C  CA   . SER   B 1 231 ? 9.301  29.268 67.364  1 80.58  ? 230 SER   B CA   1 2 
ATOM   3701 C  C    . SER   B 1 231 ? 8.888  28.045 66.531  1 80.14  ? 230 SER   B C    1 2 
ATOM   3702 O  O    . SER   B 1 231 ? 9.22   27.95  65.357  1 79.65  ? 230 SER   B O    1 2 
ATOM   3703 C  CB   . SER   B 1 231 ? 10.703 29.071 67.946  1 81.77  ? 230 SER   B CB   1 2 
ATOM   3704 O  OG   . SER   B 1 231 ? 10.785 28.085 68.969  1 83.11  ? 230 SER   B OG   1 2 
ATOM   3705 N  N    . PRO   B 1 236 ? 4.439  22.412 71.794  1 84.74  ? 235 PRO   B N    1 2 
ATOM   3706 C  CA   . PRO   B 1 236 ? 3.875  22.123 73.131  1 84.46  ? 235 PRO   B CA   1 2 
ATOM   3707 C  C    . PRO   B 1 236 ? 3.598  23.385 73.95   1 83.83  ? 235 PRO   B C    1 2 
ATOM   3708 O  O    . PRO   B 1 236 ? 2.551  23.475 74.596  1 83.81  ? 235 PRO   B O    1 2 
ATOM   3709 C  CB   . PRO   B 1 236 ? 4.925  21.214 73.79   1 85.26  ? 235 PRO   B CB   1 2 
ATOM   3710 C  CG   . PRO   B 1 236 ? 6.178  21.417 73      1 85.88  ? 235 PRO   B CG   1 2 
ATOM   3711 C  CD   . PRO   B 1 236 ? 5.769  21.804 71.6    1 84.35  ? 235 PRO   B CD   1 2 
ATOM   3712 N  N    . VAL   B 1 237 ? 4.534  24.363 73.902  1 83.09  ? 236 VAL   B N    1 2 
ATOM   3713 C  CA   . VAL   B 1 237 ? 4.477  25.653 74.593  1 82.87  ? 236 VAL   B CA   1 2 
ATOM   3714 C  C    . VAL   B 1 237 ? 4.242  25.482 76.103  1 82.58  ? 236 VAL   B C    1 2 
ATOM   3715 O  O    . VAL   B 1 237 ? 3.176  25.043 76.546  1 82.75  ? 236 VAL   B O    1 2 
ATOM   3716 C  CB   . VAL   B 1 237 ? 3.492  26.64  73.929  1 83.54  ? 236 VAL   B CB   1 2 
ATOM   3717 C  CG1  . VAL   B 1 237 ? 3.282  27.879 74.789  1 84.13  ? 236 VAL   B CG1  1 2 
ATOM   3718 C  CG2  . VAL   B 1 237 ? 3.988  27.03  72.544  1 84.04  ? 236 VAL   B CG2  1 2 
ATOM   3719 N  N    . LEU   B 1 238 ? 5.273  25.817 76.885  1 81.91  ? 237 LEU   B N    1 2 
ATOM   3720 C  CA   . LEU   B 1 238 ? 5.29   25.685 78.34   1 81.59  ? 237 LEU   B CA   1 2 
ATOM   3721 C  C    . LEU   B 1 238 ? 4.68   26.9   79.028  1 81.71  ? 237 LEU   B C    1 2 
ATOM   3722 O  O    . LEU   B 1 238 ? 4.668  27.996 78.464  1 81.85  ? 237 LEU   B O    1 2 
ATOM   3723 C  CB   . LEU   B 1 238 ? 6.739  25.518 78.851  1 81.29  ? 237 LEU   B CB   1 2 
ATOM   3724 C  CG   . LEU   B 1 238 ? 7.715  24.727 78      1 82.07  ? 237 LEU   B CG   1 2 
ATOM   3725 C  CD1  . LEU   B 1 238 ? 9.101  25.288 78.108  1 82.38  ? 237 LEU   B CD1  1 2 
ATOM   3726 C  CD2  . LEU   B 1 238 ? 7.656  23.258 78.319  1 82.5   ? 237 LEU   B CD2  1 2 
ATOM   3727 N  N    . GLU   B 1 239 ? 4.224  26.717 80.274  1 81.45  ? 238 GLU   B N    1 2 
ATOM   3728 C  CA   . GLU   B 1 239 ? 3.683  27.805 81.067  1 81.68  ? 238 GLU   B CA   1 2 
ATOM   3729 C  C    . GLU   B 1 239 ? 4.764  28.464 81.933  1 81.89  ? 238 GLU   B C    1 2 
ATOM   3730 O  O    . GLU   B 1 239 ? 5.855  27.917 82.115  1 82.21  ? 238 GLU   B O    1 2 
ATOM   3731 C  CB   . GLU   B 1 239 ? 2.476  27.338 81.9    1 83.46  ? 238 GLU   B CB   1 2 
ATOM   3732 C  CG   . GLU   B 1 239 ? 1.207  27.225 81.078  1 87.14  ? 238 GLU   B CG   1 2 
ATOM   3733 C  CD   . GLU   B 1 239 ? 0.809  28.5   80.359  1 92.52  ? 238 GLU   B CD   1 2 
ATOM   3734 O  OE1  . GLU   B 1 239 ? 0.454  28.417 79.161  1 94.01  ? 238 GLU   B OE1  1 2 
ATOM   3735 O  OE2  . GLU   B 1 239 ? 0.86   29.582 80.986  1 94.08  ? 238 GLU   B OE2  1 2 
ATOM   3736 N  N    . THR   B 1 240 ? 4.465  29.657 82.447  1 81.43  ? 239 THR   B N    1 2 
ATOM   3737 C  CA   . THR   B 1 240 ? 5.379  30.425 83.282  1 81.35  ? 239 THR   B CA   1 2 
ATOM   3738 C  C    . THR   B 1 240 ? 5.855  29.596 84.488  1 81.07  ? 239 THR   B C    1 2 
ATOM   3739 O  O    . THR   B 1 240 ? 7.054  29.398 84.663  1 80.92  ? 239 THR   B O    1 2 
ATOM   3740 C  CB   . THR   B 1 240 ? 4.698  31.747 83.702  1 82.59  ? 239 THR   B CB   1 2 
ATOM   3741 O  OG1  . THR   B 1 240 ? 4.041  32.352 82.58   1 83.51  ? 239 THR   B OG1  1 2 
ATOM   3742 C  CG2  . THR   B 1 240 ? 5.667  32.724 84.33   1 82.92  ? 239 THR   B CG2  1 2 
ATOM   3743 N  N    . ASP   B 1 241 ? 4.893  29.016 85.23   1 80.94  ? 240 ASP   B N    1 2 
ATOM   3744 C  CA   . ASP   B 1 241 ? 5.107  28.234 86.451  1 81.1   ? 240 ASP   B CA   1 2 
ATOM   3745 C  C    . ASP   B 1 241 ? 5.684  26.842 86.241  1 81.21  ? 240 ASP   B C    1 2 
ATOM   3746 O  O    . ASP   B 1 241 ? 6.407  26.353 87.107  1 81.43  ? 240 ASP   B O    1 2 
ATOM   3747 C  CB   . ASP   B 1 241 ? 3.808  28.138 87.266  1 82.12  ? 240 ASP   B CB   1 2 
ATOM   3748 C  CG   . ASP   B 1 241 ? 2.672  27.419 86.575  1 85.34  ? 240 ASP   B CG   1 2 
ATOM   3749 O  OD1  . ASP   B 1 241 ? 2.448  27.68  85.372  1 85.74  ? 240 ASP   B OD1  1 2 
ATOM   3750 O  OD2  . ASP   B 1 241 ? 1.998  26.607 87.237  1 87.14  ? 240 ASP   B OD2  1 2 
ATOM   3751 N  N    . THR   B 1 242 ? 5.353  26.194 85.12   1 80.88  ? 241 THR   B N    1 2 
ATOM   3752 C  CA   . THR   B 1 242 ? 5.838  24.85  84.817  1 80.96  ? 241 THR   B CA   1 2 
ATOM   3753 C  C    . THR   B 1 242 ? 7.355  24.839 84.669  1 80.9   ? 241 THR   B C    1 2 
ATOM   3754 O  O    . THR   B 1 242 ? 8.019  23.934 85.178  1 81.06  ? 241 THR   B O    1 2 
ATOM   3755 C  CB   . THR   B 1 242 ? 5.113  24.31  83.582  1 82.09  ? 241 THR   B CB   1 2 
ATOM   3756 O  OG1  . THR   B 1 242 ? 3.733  24.138 83.9    1 83.03  ? 241 THR   B OG1  1 2 
ATOM   3757 C  CG2  . THR   B 1 242 ? 5.693  23.001 83.082  1 82.42  ? 241 THR   B CG2  1 2 
ATOM   3758 N  N    . VAL   B 1 243 ? 7.899  25.875 84.015  1 80.38  ? 242 VAL   B N    1 2 
ATOM   3759 C  CA   . VAL   B 1 243 ? 9.332  26.046 83.797  1 80.41  ? 242 VAL   B CA   1 2 
ATOM   3760 C  C    . VAL   B 1 243 ? 10.072 26.299 85.115  1 80.07  ? 242 VAL   B C    1 2 
ATOM   3761 O  O    . VAL   B 1 243 ? 11.17  25.775 85.313  1 79.9   ? 242 VAL   B O    1 2 
ATOM   3762 C  CB   . VAL   B 1 243 ? 9.562  27.17  82.767  1 81.2   ? 242 VAL   B CB   1 2 
ATOM   3763 C  CG1  . VAL   B 1 243 ? 11.036 27.546 82.662  1 81.94  ? 242 VAL   B CG1  1 2 
ATOM   3764 C  CG2  . VAL   B 1 243 ? 9.019  26.757 81.414  1 81.61  ? 242 VAL   B CG2  1 2 
ATOM   3765 N  N    . ALA   B 1 244 ? 9.444  27.053 86.03   1 79.95  ? 243 ALA   B N    1 2 
ATOM   3766 C  CA   . ALA   B 1 244 ? 9.999  27.361 87.349  1 80.47  ? 243 ALA   B CA   1 2 
ATOM   3767 C  C    . ALA   B 1 244 ? 10.116 26.098 88.208  1 80.76  ? 243 ALA   B C    1 2 
ATOM   3768 O  O    . ALA   B 1 244 ? 11.092 25.943 88.944  1 80.78  ? 243 ALA   B O    1 2 
ATOM   3769 C  CB   . ALA   B 1 244 ? 9.126  28.382 88.05   1 80.65  ? 243 ALA   B CB   1 2 
ATOM   3770 N  N    . ARG   B 1 245 ? 9.132  25.191 88.098  1 80.67  ? 244 ARG   B N    1 2 
ATOM   3771 C  CA   . ARG   B 1 245 ? 9.156  23.918 88.811  1 81.05  ? 244 ARG   B CA   1 2 
ATOM   3772 C  C    . ARG   B 1 245 ? 10.29  23.035 88.268  1 81.22  ? 244 ARG   B C    1 2 
ATOM   3773 O  O    . ARG   B 1 245 ? 10.94  22.337 89.036  1 81.18  ? 244 ARG   B O    1 2 
ATOM   3774 C  CB   . ARG   B 1 245 ? 7.813  23.193 88.677  1 82.48  ? 244 ARG   B CB   1 2 
ATOM   3775 C  CG   . ARG   B 1 245 ? 6.662  23.877 89.396  1 85.76  ? 244 ARG   B CG   1 2 
ATOM   3776 C  CD   . ARG   B 1 245 ? 5.534  22.893 89.656  1 89.45  ? 244 ARG   B CD   1 2 
ATOM   3777 N  NE   . ARG   B 1 245 ? 4.301  23.224 88.933  1 92.87  ? 244 ARG   B NE   1 2 
ATOM   3778 C  CZ   . ARG   B 1 245 ? 4.025  22.828 87.693  1 95.11  ? 244 ARG   B CZ   1 2 
ATOM   3779 N  NH1  . ARG   B 1 245 ? 4.902  22.101 87.009  1 95.13  ? 244 ARG   B NH1  1 2 
ATOM   3780 N  NH2  . ARG   B 1 245 ? 2.873  23.161 87.125  1 94.65  ? 244 ARG   B NH2  1 2 
ATOM   3781 N  N    . SER   B 1 246 ? 10.537 23.075 86.948  1 81.17  ? 245 SER   B N    1 2 
ATOM   3782 C  CA   . SER   B 1 246 ? 11.623 22.32  86.327  1 81.48  ? 245 SER   B CA   1 2 
ATOM   3783 C  C    . SER   B 1 246 ? 12.982 22.853 86.787  1 81.64  ? 245 SER   B C    1 2 
ATOM   3784 O  O    . SER   B 1 246 ? 13.899 22.068 87.012  1 81.75  ? 245 SER   B O    1 2 
ATOM   3785 C  CB   . SER   B 1 246 ? 11.521 22.383 84.807  1 82.66  ? 245 SER   B CB   1 2 
ATOM   3786 O  OG   . SER   B 1 246 ? 10.445 21.586 84.341  1 84.75  ? 245 SER   B OG   1 2 
ATOM   3787 N  N    . LEU   B 1 247 ? 13.106 24.177 86.946  1 81.55  ? 246 LEU   B N    1 2 
ATOM   3788 C  CA   . LEU   B 1 247 ? 14.351 24.776 87.402  1 81.97  ? 246 LEU   B CA   1 2 
ATOM   3789 C  C    . LEU   B 1 247 ? 14.563 24.502 88.877  1 82.98  ? 246 LEU   B C    1 2 
ATOM   3790 O  O    . LEU   B 1 247 ? 15.676 24.141 89.257  1 83.47  ? 246 LEU   B O    1 2 
ATOM   3791 C  CB   . LEU   B 1 247 ? 14.393 26.284 87.118  1 81.79  ? 246 LEU   B CB   1 2 
ATOM   3792 C  CG   . LEU   B 1 247 ? 15.701 27.003 87.458  1 82.76  ? 246 LEU   B CG   1 2 
ATOM   3793 C  CD1  . LEU   B 1 247 ? 16.887 26.373 86.762  1 83.21  ? 246 LEU   B CD1  1 2 
ATOM   3794 C  CD2  . LEU   B 1 247 ? 15.631 28.457 87.087  1 83.23  ? 246 LEU   B CD2  1 2 
ATOM   3795 N  N    . ILE   B 1 248 ? 13.507 24.61  89.709  1 83.16  ? 247 ILE   B N    1 2 
ATOM   3796 C  CA   . ILE   B 1 248 ? 13.665 24.321 91.14   1 83.8   ? 247 ILE   B CA   1 2 
ATOM   3797 C  C    . ILE   B 1 248 ? 14.022 22.849 91.36   1 83.91  ? 247 ILE   B C    1 2 
ATOM   3798 O  O    . ILE   B 1 248 ? 14.78  22.556 92.271  1 84.18  ? 247 ILE   B O    1 2 
ATOM   3799 C  CB   . ILE   B 1 248 ? 12.486 24.795 92.049  1 84.54  ? 247 ILE   B CB   1 2 
ATOM   3800 C  CG1  . ILE   B 1 248 ? 12.934 24.958 93.51   1 85.33  ? 247 ILE   B CG1  1 2 
ATOM   3801 C  CG2  . ILE   B 1 248 ? 11.286 23.868 91.974  1 85.2   ? 247 ILE   B CG2  1 2 
ATOM   3802 C  CD1  . ILE   B 1 248 ? 13.599 26.209 93.797  1 86.57  ? 247 ILE   B CD1  1 2 
ATOM   3803 N  N    . ASP   B 1 249 ? 13.539 21.936 90.503  1 83.61  ? 248 ASP   B N    1 2 
ATOM   3804 C  CA   . ASP   B 1 249 ? 13.844 20.516 90.654  1 83.91  ? 248 ASP   B CA   1 2 
ATOM   3805 C  C    . ASP   B 1 249 ? 15.227 20.128 90.103  1 83.56  ? 248 ASP   B C    1 2 
ATOM   3806 O  O    . ASP   B 1 249 ? 15.816 19.149 90.555  1 83.68  ? 248 ASP   B O    1 2 
ATOM   3807 C  CB   . ASP   B 1 249 ? 12.723 19.641 90.064  1 86.14  ? 248 ASP   B CB   1 2 
ATOM   3808 C  CG   . ASP   B 1 249 ? 11.412 19.72  90.839  1 91.31  ? 248 ASP   B CG   1 2 
ATOM   3809 O  OD1  . ASP   B 1 249 ? 11.453 19.654 92.094  1 91.92  ? 248 ASP   B OD1  1 2 
ATOM   3810 O  OD2  . ASP   B 1 249 ? 10.344 19.856 90.191  1 93.51  ? 248 ASP   B OD2  1 2 
ATOM   3811 N  N    . GLY   B 1 250 ? 15.739 20.903 89.158  1 83.15  ? 249 GLY   B N    1 2 
ATOM   3812 C  CA   . GLY   B 1 250 ? 17.049 20.656 88.566  1 83.29  ? 249 GLY   B CA   1 2 
ATOM   3813 C  C    . GLY   B 1 250 ? 18.186 21.163 89.431  1 83.03  ? 249 GLY   B C    1 2 
ATOM   3814 O  O    . GLY   B 1 250 ? 19.272 20.579 89.446  1 83.1   ? 249 GLY   B O    1 2 
ATOM   3815 N  N    . ILE   B 1 251 ? 17.946 22.265 90.147  1 82.57  ? 250 ILE   B N    1 2 
ATOM   3816 C  CA   . ILE   B 1 251 ? 18.94  22.83  91.049  1 82.87  ? 250 ILE   B CA   1 2 
ATOM   3817 C  C    . ILE   B 1 251 ? 19.103 21.916 92.266  1 83.67  ? 250 ILE   B C    1 2 
ATOM   3818 O  O    . ILE   B 1 251 ? 20.229 21.681 92.71   1 84.09  ? 250 ILE   B O    1 2 
ATOM   3819 C  CB   . ILE   B 1 251 ? 18.544 24.269 91.451  1 83.07  ? 250 ILE   B CB   1 2 
ATOM   3820 C  CG1  . ILE   B 1 251 ? 18.595 25.198 90.236  1 83.97  ? 250 ILE   B CG1  1 2 
ATOM   3821 C  CG2  . ILE   B 1 251 ? 19.433 24.794 92.576  1 83.39  ? 250 ILE   B CG2  1 2 
ATOM   3822 C  CD1  . ILE   B 1 251 ? 17.969 26.518 90.468  1 85.09  ? 250 ILE   B CD1  1 2 
ATOM   3823 N  N    . LEU   B 1 252 ? 17.979 21.354 92.769  1 83.55  ? 251 LEU   B N    1 2 
ATOM   3824 C  CA   . LEU   B 1 252 ? 17.943 20.447 93.91   1 83.52  ? 251 LEU   B CA   1 2 
ATOM   3825 C  C    . LEU   B 1 252 ? 18.597 19.094 93.641  1 84.05  ? 251 LEU   B C    1 2 
ATOM   3826 O  O    . LEU   B 1 252 ? 19.13  18.491 94.57   1 84.56  ? 251 LEU   B O    1 2 
ATOM   3827 C  CB   . LEU   B 1 252 ? 16.514 20.275 94.433  1 83.33  ? 251 LEU   B CB   1 2 
ATOM   3828 C  CG   . LEU   B 1 252 ? 15.876 21.526 95.023  1 84.6   ? 251 LEU   B CG   1 2 
ATOM   3829 C  CD1  . LEU   B 1 252 ? 14.48  21.241 95.502  1 85.18  ? 251 LEU   B CD1  1 2 
ATOM   3830 C  CD2  . LEU   B 1 252 ? 16.709 22.115 96.143  1 85.34  ? 251 LEU   B CD2  1 2 
ATOM   3831 N  N    . THR   B 1 253 ? 18.575 18.615 92.389  1 83.84  ? 252 THR   B N    1 2 
ATOM   3832 C  CA   . THR   B 1 253 ? 19.266 17.363 92.058  1 84.04  ? 252 THR   B CA   1 2 
ATOM   3833 C  C    . THR   B 1 253 ? 20.67  17.622 91.429  1 83.99  ? 252 THR   B C    1 2 
ATOM   3834 O  O    . THR   B 1 253 ? 21.394 16.662 91.169  1 84.4   ? 252 THR   B O    1 2 
ATOM   3835 C  CB   . THR   B 1 253 ? 18.383 16.432 91.227  1 85.21  ? 252 THR   B CB   1 2 
ATOM   3836 O  OG1  . THR   B 1 253 ? 18.132 17.02  89.955  1 86.2   ? 252 THR   B OG1  1 2 
ATOM   3837 C  CG2  . THR   B 1 253 ? 17.076 16.109 91.92   1 85.55  ? 252 THR   B CG2  1 2 
ATOM   3838 N  N    . ASN   B 1 254 ? 21.059 18.91  91.233  1 83.24  ? 253 ASN   B N    1 2 
ATOM   3839 C  CA   . ASN   B 1 254 ? 22.336 19.36  90.673  1 82.82  ? 253 ASN   B CA   1 2 
ATOM   3840 C  C    . ASN   B 1 254 ? 22.547 18.889 89.237  1 82.07  ? 253 ASN   B C    1 2 
ATOM   3841 O  O    . ASN   B 1 254 ? 23.649 18.468 88.883  1 82.26  ? 253 ASN   B O    1 2 
ATOM   3842 C  CB   . ASN   B 1 254 ? 23.524 18.978 91.576  1 83.75  ? 253 ASN   B CB   1 2 
ATOM   3843 C  CG   . ASN   B 1 254 ? 23.547 19.664 92.918  1 86.65  ? 253 ASN   B CG   1 2 
ATOM   3844 O  OD1  . ASN   B 1 254 ? 23.905 19.066 93.933  1 87.88  ? 253 ASN   B OD1  1 2 
ATOM   3845 N  ND2  . ASN   B 1 254 ? 23.183 20.936 92.959  1 87.24  ? 253 ASN   B ND2  1 2 
ATOM   3846 N  N    . LYS   B 1 255 ? 21.496 18.96  88.407  1 81.03  ? 254 LYS   B N    1 2 
ATOM   3847 C  CA   . LYS   B 1 255 ? 21.606 18.537 87.016  1 80.57  ? 254 LYS   B CA   1 2 
ATOM   3848 C  C    . LYS   B 1 255 ? 22.249 19.624 86.164  1 79.9   ? 254 LYS   B C    1 2 
ATOM   3849 O  O    . LYS   B 1 255 ? 21.902 20.798 86.276  1 79.95  ? 254 LYS   B O    1 2 
ATOM   3850 C  CB   . LYS   B 1 255 ? 20.252 18.097 86.446  1 82.44  ? 254 LYS   B CB   1 2 
ATOM   3851 C  CG   . LYS   B 1 255 ? 20.394 17.28  85.166  1 86.61  ? 254 LYS   B CG   1 2 
ATOM   3852 C  CD   . LYS   B 1 255 ? 19.318 16.215 85.04   1 91.02  ? 254 LYS   B CD   1 2 
ATOM   3853 C  CE   . LYS   B 1 255 ? 19.631 15.224 83.945  1 94.69  ? 254 LYS   B CE   1 2 
ATOM   3854 N  NZ   . LYS   B 1 255 ? 19.679 15.871 82.605  1 96.84  ? 254 LYS   B NZ   1 2 
ATOM   3855 N  N    . LYS   B 1 256 ? 23.206 19.232 85.33   1 79.19  ? 255 LYS   B N    1 2 
ATOM   3856 C  CA   . LYS   B 1 256 ? 23.948 20.149 84.471  1 79     ? 255 LYS   B CA   1 2 
ATOM   3857 C  C    . LYS   B 1 256 ? 23.101 20.767 83.362  1 78.59  ? 255 LYS   B C    1 2 
ATOM   3858 O  O    . LYS   B 1 256 ? 23.285 21.941 83.048  1 78.64  ? 255 LYS   B O    1 2 
ATOM   3859 C  CB   . LYS   B 1 256 ? 25.137 19.417 83.843  1 80.64  ? 255 LYS   B CB   1 2 
ATOM   3860 C  CG   . LYS   B 1 256 ? 26.003 18.687 84.837  1 83.88  ? 255 LYS   B CG   1 2 
ATOM   3861 C  CD   . LYS   B 1 256 ? 26.88  19.648 85.581  1 87.82  ? 255 LYS   B CD   1 2 
ATOM   3862 C  CE   . LYS   B 1 256 ? 27.813 18.865 86.462  1 91.36  ? 255 LYS   B CE   1 2 
ATOM   3863 N  NZ   . LYS   B 1 256 ? 27.017 18.113 87.466  1 93.35  ? 255 LYS   B NZ   1 2 
ATOM   3864 N  N    . MET   B 1 257 ? 22.213 19.976 82.735  1 77.98  ? 256 MET   B N    1 2 
ATOM   3865 C  CA   . MET   B 1 257 ? 21.386 20.476 81.638  1 77.89  ? 256 MET   B CA   1 2 
ATOM   3866 C  C    . MET   B 1 257 ? 19.912 20.253 81.88   1 78.49  ? 256 MET   B C    1 2 
ATOM   3867 O  O    . MET   B 1 257 ? 19.427 19.132 81.755  1 78.53  ? 256 MET   B O    1 2 
ATOM   3868 C  CB   . MET   B 1 257 ? 21.789 19.839 80.305  1 77.48  ? 256 MET   B CB   1 2 
ATOM   3869 C  CG   . MET   B 1 257 ? 21.37  20.664 79.126  1 77.47  ? 256 MET   B CG   1 2 
ATOM   3870 S  SD   . MET   B 1 257 ? 22.296 22.21  78.998  1 74.89  ? 256 MET   B SD   1 2 
ATOM   3871 C  CE   . MET   B 1 257 ? 23.829 21.592 78.327  1 71.4   ? 256 MET   B CE   1 2 
ATOM   3872 N  N    . ILE   B 1 258 ? 19.192 21.323 82.195  1 78.9   ? 257 ILE   B N    1 2 
ATOM   3873 C  CA   . ILE   B 1 258 ? 17.762 21.258 82.465  1 79.88  ? 257 ILE   B CA   1 2 
ATOM   3874 C  C    . ILE   B 1 258 ? 16.95  21.577 81.206  1 80.73  ? 257 ILE   B C    1 2 
ATOM   3875 O  O    . ILE   B 1 258 ? 16.557 22.721 80.994  1 80.86  ? 257 ILE   B O    1 2 
ATOM   3876 C  CB   . ILE   B 1 258 ? 17.35  22.153 83.675  1 80.39  ? 257 ILE   B CB   1 2 
ATOM   3877 C  CG1  . ILE   B 1 258 ? 18.337 22.032 84.85   1 81.26  ? 257 ILE   B CG1  1 2 
ATOM   3878 C  CG2  . ILE   B 1 258 ? 15.927 21.833 84.135  1 80.98  ? 257 ILE   B CG2  1 2 
ATOM   3879 C  CD1  . ILE   B 1 258 ? 18.117 23.047 85.93   1 82.56  ? 257 ILE   B CD1  1 2 
ATOM   3880 N  N    . PHE   B 1 259 ? 16.692 20.562 80.374  1 81.23  ? 258 PHE   B N    1 2 
ATOM   3881 C  CA   . PHE   B 1 259 ? 15.902 20.73  79.154  1 82.21  ? 258 PHE   B CA   1 2 
ATOM   3882 C  C    . PHE   B 1 259 ? 14.425 20.776 79.502  1 83.53  ? 258 PHE   B C    1 2 
ATOM   3883 O  O    . PHE   B 1 259 ? 13.96  19.911 80.245  1 84.07  ? 258 PHE   B O    1 2 
ATOM   3884 C  CB   . PHE   B 1 259 ? 16.143 19.55  78.213  1 81.76  ? 258 PHE   B CB   1 2 
ATOM   3885 C  CG   . PHE   B 1 259 ? 17.407 19.674 77.412  1 81.83  ? 258 PHE   B CG   1 2 
ATOM   3886 C  CD1  . PHE   B 1 259 ? 17.696 20.836 76.724  1 82.37  ? 258 PHE   B CD1  1 2 
ATOM   3887 C  CD2  . PHE   B 1 259 ? 18.297 18.62  77.327  1 82.33  ? 258 PHE   B CD2  1 2 
ATOM   3888 C  CE1  . PHE   B 1 259 ? 18.859 20.947 75.981  1 82.95  ? 258 PHE   B CE1  1 2 
ATOM   3889 C  CE2  . PHE   B 1 259 ? 19.456 18.733 76.577  1 82.91  ? 258 PHE   B CE2  1 2 
ATOM   3890 C  CZ   . PHE   B 1 259 ? 19.729 19.894 75.909  1 82.7   ? 258 PHE   B CZ   1 2 
ATOM   3891 N  N    . VAL   B 1 260 ? 13.681 21.766 78.98   1 83.8   ? 259 VAL   B N    1 2 
ATOM   3892 C  CA   . VAL   B 1 260 ? 12.255 21.867 79.279  1 84.76  ? 259 VAL   B CA   1 2 
ATOM   3893 C  C    . VAL   B 1 260 ? 11.446 21.886 77.992  1 85.77  ? 259 VAL   B C    1 2 
ATOM   3894 O  O    . VAL   B 1 260 ? 11.468 22.891 77.288  1 85.92  ? 259 VAL   B O    1 2 
ATOM   3895 C  CB   . VAL   B 1 260 ? 11.925 23.098 80.155  1 85.54  ? 259 VAL   B CB   1 2 
ATOM   3896 C  CG1  . VAL   B 1 260 ? 10.478 23.058 80.614  1 86.13  ? 259 VAL   B CG1  1 2 
ATOM   3897 C  CG2  . VAL   B 1 260 ? 12.855 23.194 81.358  1 86.17  ? 259 VAL   B CG2  1 2 
ATOM   3898 N  N    . PRO   B 1 261 ? 10.805 20.769 77.602  1 86.31  ? 260 PRO   B N    1 2 
ATOM   3899 C  CA   . PRO   B 1 261 ? 10.678 19.487 78.318  1 86.77  ? 260 PRO   B CA   1 2 
ATOM   3900 C  C    . PRO   B 1 261 ? 11.876 18.546 78.134  1 87.51  ? 260 PRO   B C    1 2 
ATOM   3901 O  O    . PRO   B 1 261 ? 12.635 18.697 77.185  1 87.53  ? 260 PRO   B O    1 2 
ATOM   3902 C  CB   . PRO   B 1 261 ? 9.365  18.903 77.752  1 87.35  ? 260 PRO   B CB   1 2 
ATOM   3903 C  CG   . PRO   B 1 261 ? 8.806  19.952 76.778  1 87.61  ? 260 PRO   B CG   1 2 
ATOM   3904 C  CD   . PRO   B 1 261 ? 9.997  20.756 76.373  1 85.94  ? 260 PRO   B CD   1 2 
ATOM   3905 N  N    . SER   B 1 262 ? 12.051 17.591 79.064  1 88.06  ? 261 SER   B N    1 2 
ATOM   3906 C  CA   . SER   B 1 262 ? 13.16  16.626 79.114  1 89.15  ? 261 SER   B CA   1 2 
ATOM   3907 C  C    . SER   B 1 262 ? 13.454 15.856 77.825  1 90.31  ? 261 SER   B C    1 2 
ATOM   3908 O  O    . SER   B 1 262 ? 14.586 15.432 77.612  1 90.45  ? 261 SER   B O    1 2 
ATOM   3909 C  CB   . SER   B 1 262 ? 12.93  15.626 80.24   1 90.25  ? 261 SER   B CB   1 2 
ATOM   3910 O  OG   . SER   B 1 262 ? 11.882 14.725 79.917  1 92.23  ? 261 SER   B OG   1 2 
ATOM   3911 N  N    . TYR   B 1 263 ? 12.438 15.63  76.998  1 91.06  ? 262 TYR   B N    1 2 
ATOM   3912 C  CA   . TYR   B 1 263 ? 12.591 14.878 75.759  1 92.25  ? 262 TYR   B CA   1 2 
ATOM   3913 C  C    . TYR   B 1 263 ? 13.298 15.634 74.649  1 93.61  ? 262 TYR   B C    1 2 
ATOM   3914 O  O    . TYR   B 1 263 ? 13.759 15.003 73.703  1 93.95  ? 262 TYR   B O    1 2 
ATOM   3915 C  CB   . TYR   B 1 263 ? 11.243 14.33  75.26   1 92.24  ? 262 TYR   B CB   1 2 
ATOM   3916 C  CG   . TYR   B 1 263 ? 10.138 15.357 75.121  1 92.99  ? 262 TYR   B CG   1 2 
ATOM   3917 C  CD1  . TYR   B 1 263 ? 10.153 16.289 74.093  1 93.96  ? 262 TYR   B CD1  1 2 
ATOM   3918 C  CD2  . TYR   B 1 263 ? 9.02   15.319 75.941  1 93.93  ? 262 TYR   B CD2  1 2 
ATOM   3919 C  CE1  . TYR   B 1 263 ? 9.128  17.214 73.943  1 94.95  ? 262 TYR   B CE1  1 2 
ATOM   3920 C  CE2  . TYR   B 1 263 ? 7.979  16.226 75.788  1 94.87  ? 262 TYR   B CE2  1 2 
ATOM   3921 C  CZ   . TYR   B 1 263 ? 8.036  17.175 74.788  1 95.86  ? 262 TYR   B CZ   1 2 
ATOM   3922 O  OH   . TYR   B 1 263 ? 7.012  18.082 74.652  1 97.42  ? 262 TYR   B OH   1 2 
ATOM   3923 N  N    . ILE   B 1 264 ? 13.375 16.968 74.732  1 94.34  ? 263 ILE   B N    1 2 
ATOM   3924 C  CA   . ILE   B 1 264 ? 14.043 17.754 73.695  1 95.66  ? 263 ILE   B CA   1 2 
ATOM   3925 C  C    . ILE   B 1 264 ? 15.565 17.406 73.556  1 96.84  ? 263 ILE   B C    1 2 
ATOM   3926 O  O    . ILE   B 1 264 ? 16.248 17.911 72.669  1 96.69  ? 263 ILE   B O    1 2 
ATOM   3927 C  CB   . ILE   B 1 264 ? 13.769 19.259 73.908  1 96.45  ? 263 ILE   B CB   1 2 
ATOM   3928 C  CG1  . ILE   B 1 264 ? 13.615 19.999 72.577  1 97.95  ? 263 ILE   B CG1  1 2 
ATOM   3929 C  CG2  . ILE   B 1 264 ? 14.792 19.881 74.801  1 96.91  ? 263 ILE   B CG2  1 2 
ATOM   3930 C  CD1  . ILE   B 1 264 ? 12.131 19.974 71.946  1 99.51  ? 263 ILE   B CD1  1 2 
ATOM   3931 N  N    . ASN   B 1 265 ? 16.077 16.516 74.418  1 98.01  ? 264 ASN   B N    1 2 
ATOM   3932 C  CA   . ASN   B 1 265 ? 17.442 16.026 74.372  1 99.75  ? 264 ASN   B CA   1 2 
ATOM   3933 C  C    . ASN   B 1 265 ? 17.55  15.013 73.235  1 100.91 ? 264 ASN   B C    1 2 
ATOM   3934 O  O    . ASN   B 1 265 ? 18.526 15.05  72.491  1 100.88 ? 264 ASN   B O    1 2 
ATOM   3935 C  CB   . ASN   B 1 265 ? 17.805 15.366 75.706  1 101.66 ? 264 ASN   B CB   1 2 
ATOM   3936 C  CG   . ASN   B 1 265 ? 19.179 14.741 75.737  1 105.94 ? 264 ASN   B CG   1 2 
ATOM   3937 O  OD1  . ASN   B 1 265 ? 20.084 15.124 74.981  1 107.38 ? 264 ASN   B OD1  1 2 
ATOM   3938 N  ND2  . ASN   B 1 265 ? 19.366 13.763 76.619  1 106.93 ? 264 ASN   B ND2  1 2 
ATOM   3939 N  N    . ILE   B 1 266 ? 16.566 14.103 73.104  1 101.81 ? 265 ILE   B N    1 2 
ATOM   3940 C  CA   . ILE   B 1 266 ? 16.596 13.11  72.031  1 103.13 ? 265 ILE   B CA   1 2 
ATOM   3941 C  C    . ILE   B 1 266 ? 16.413 13.755 70.665  1 104.51 ? 265 ILE   B C    1 2 
ATOM   3942 O  O    . ILE   B 1 266 ? 16.962 13.247 69.696  1 104.72 ? 265 ILE   B O    1 2 
ATOM   3943 C  CB   . ILE   B 1 266 ? 15.633 11.921 72.256  1 103.66 ? 265 ILE   B CB   1 2 
ATOM   3944 C  CG1  . ILE   B 1 266 ? 14.165 12.286 71.983  1 104.53 ? 265 ILE   B CG1  1 2 
ATOM   3945 C  CG2  . ILE   B 1 266 ? 15.819 11.337 73.647  1 104.26 ? 265 ILE   B CG2  1 2 
ATOM   3946 C  CD1  . ILE   B 1 266 ? 13.578 11.612 70.784  1 105.81 ? 265 ILE   B CD1  1 2 
ATOM   3947 N  N    . PHE   B 1 267 ? 15.69  14.884 70.585  1 105.4  ? 266 PHE   B N    1 2 
ATOM   3948 C  CA   . PHE   B 1 267 ? 15.507 15.602 69.328  1 106.83 ? 266 PHE   B CA   1 2 
ATOM   3949 C  C    . PHE   B 1 267 ? 16.821 16.2   68.843  1 107.82 ? 266 PHE   B C    1 2 
ATOM   3950 O  O    . PHE   B 1 267 ? 17.074 16.21  67.643  1 107.91 ? 266 PHE   B O    1 2 
ATOM   3951 C  CB   . PHE   B 1 267 ? 14.444 16.692 69.474  1 107.07 ? 266 PHE   B CB   1 2 
ATOM   3952 C  CG   . PHE   B 1 267 ? 13.046 16.131 69.498  1 108    ? 266 PHE   B CG   1 2 
ATOM   3953 C  CD1  . PHE   B 1 267 ? 12.671 15.129 68.621  1 108.84 ? 266 PHE   B CD1  1 2 
ATOM   3954 C  CD2  . PHE   B 1 267 ? 12.102 16.618 70.385  1 108.89 ? 266 PHE   B CD2  1 2 
ATOM   3955 C  CE1  . PHE   B 1 267 ? 11.384 14.615 68.641  1 109.62 ? 266 PHE   B CE1  1 2 
ATOM   3956 C  CE2  . PHE   B 1 267 ? 10.814 16.103 70.404  1 109.72 ? 266 PHE   B CE2  1 2 
ATOM   3957 C  CZ   . PHE   B 1 267 ? 10.462 15.106 69.53   1 109.53 ? 266 PHE   B CZ   1 2 
ATOM   3958 N  N    . LEU   B 1 268 ? 17.666 16.674 69.769  1 108.39 ? 267 LEU   B N    1 2 
ATOM   3959 C  CA   . LEU   B 1 268 ? 18.976 17.217 69.423  1 109.38 ? 267 LEU   B CA   1 2 
ATOM   3960 C  C    . LEU   B 1 268 ? 19.952 16.126 68.966  1 110.25 ? 267 LEU   B C    1 2 
ATOM   3961 O  O    . LEU   B 1 268 ? 20.856 16.406 68.18   1 110.41 ? 267 LEU   B O    1 2 
ATOM   3962 C  CB   . LEU   B 1 268 ? 19.554 17.977 70.607  1 109.65 ? 267 LEU   B CB   1 2 
ATOM   3963 C  CG   . LEU   B 1 268 ? 18.816 19.244 70.955  1 111.25 ? 267 LEU   B CG   1 2 
ATOM   3964 C  CD1  . LEU   B 1 268 ? 19.275 19.772 72.292  1 111.98 ? 267 LEU   B CD1  1 2 
ATOM   3965 C  CD2  . LEU   B 1 268 ? 19.006 20.284 69.877  1 111.87 ? 267 LEU   B CD2  1 2 
ATOM   3966 N  N    . ILE   B 1 269 ? 19.766 14.892 69.449  1 110.65 ? 268 ILE   B N    1 2 
ATOM   3967 C  CA   . ILE   B 1 269 ? 20.575 13.749 69.064  1 111.6  ? 268 ILE   B CA   1 2 
ATOM   3968 C  C    . ILE   B 1 269 ? 20.318 13.447 67.586  1 112.46 ? 268 ILE   B C    1 2 
ATOM   3969 O  O    . ILE   B 1 269 ? 21.265 13.355 66.809  1 112.49 ? 268 ILE   B O    1 2 
ATOM   3970 C  CB   . ILE   B 1 269 ? 20.229 12.553 69.984  1 112.24 ? 268 ILE   B CB   1 2 
ATOM   3971 C  CG1  . ILE   B 1 269 ? 20.759 12.794 71.414  1 113.17 ? 268 ILE   B CG1  1 2 
ATOM   3972 C  CG2  . ILE   B 1 269 ? 20.745 11.234 69.409  1 112.82 ? 268 ILE   B CG2  1 2 
ATOM   3973 C  CD1  . ILE   B 1 269 ? 20.232 11.843 72.446  1 114.39 ? 268 ILE   B CD1  1 2 
ATOM   3974 N  N    . LEU   B 1 270 ? 19.033 13.39  67.188  1 113.03 ? 269 LEU   B N    1 2 
ATOM   3975 C  CA   . LEU   B 1 270 ? 18.603 13.128 65.806  1 114.07 ? 269 LEU   B CA   1 2 
ATOM   3976 C  C    . LEU   B 1 270 ? 19.058 14.205 64.81   1 114.98 ? 269 LEU   B C    1 2 
ATOM   3977 O  O    . LEU   B 1 270 ? 19.131 13.937 63.61   1 114.99 ? 269 LEU   B O    1 2 
ATOM   3978 C  CB   . LEU   B 1 270 ? 17.076 12.953 65.724  1 114.36 ? 269 LEU   B CB   1 2 
ATOM   3979 C  CG   . LEU   B 1 270 ? 16.429 12.054 66.778  1 115.99 ? 269 LEU   B CG   1 2 
ATOM   3980 C  CD1  . LEU   B 1 270 ? 14.923 12.045 66.64   1 116.55 ? 269 LEU   B CD1  1 2 
ATOM   3981 C  CD2  . LEU   B 1 270 ? 16.999 10.646 66.748  1 116.73 ? 269 LEU   B CD2  1 2 
ATOM   3982 N  N    . ASP   B 1 271 ? 19.348 15.422 65.302  1 115.56 ? 270 ASP   B N    1 2 
ATOM   3983 C  CA   . ASP   B 1 271 ? 19.841 16.525 64.475  1 116.48 ? 270 ASP   B CA   1 2 
ATOM   3984 C  C    . ASP   B 1 271 ? 21.244 16.217 63.941  1 116.96 ? 270 ASP   B C    1 2 
ATOM   3985 O  O    . ASP   B 1 271 ? 21.578 16.641 62.836  1 117.13 ? 270 ASP   B O    1 2 
ATOM   3986 C  CB   . ASP   B 1 271 ? 19.855 17.848 65.262  1 118.3  ? 270 ASP   B CB   1 2 
ATOM   3987 C  CG   . ASP   B 1 271 ? 18.525 18.577 65.303  1 122.75 ? 270 ASP   B CG   1 2 
ATOM   3988 O  OD1  . ASP   B 1 271 ? 17.633 18.24  64.489  1 123.12 ? 270 ASP   B OD1  1 2 
ATOM   3989 O  OD2  . ASP   B 1 271 ? 18.38  19.49  66.14   1 125.17 ? 270 ASP   B OD2  1 2 
ATOM   3990 N  N    . LYS   B 1 272 ? 22.06  15.467 64.708  1 117.01 ? 271 LYS   B N    1 2 
ATOM   3991 C  CA   . LYS   B 1 272 ? 23.394 15.1   64.259  1 117.62 ? 271 LYS   B CA   1 2 
ATOM   3992 C  C    . LYS   B 1 272 ? 23.41  13.79  63.466  1 118.4  ? 271 LYS   B C    1 2 
ATOM   3993 O  O    . LYS   B 1 272 ? 24.315 12.975 63.642  1 118.47 ? 271 LYS   B O    1 2 
ATOM   3994 C  CB   . LYS   B 1 272 ? 24.402 15.085 65.421  1 118.95 ? 271 LYS   B CB   1 2 
ATOM   3995 C  CG   . LYS   B 1 272 ? 24.969 16.476 65.73   1 121.93 ? 271 LYS   B CG   1 2 
ATOM   3996 C  CD   . LYS   B 1 272 ? 26.409 16.444 66.25   1 124.92 ? 271 LYS   B CD   1 2 
ATOM   3997 C  CE   . LYS   B 1 272 ? 27.012 17.823 66.404  1 127.47 ? 271 LYS   B CE   1 2 
ATOM   3998 N  NZ   . LYS   B 1 272 ? 27.22  18.506 65.097  1 128.84 ? 271 LYS   B NZ   1 2 
ATOM   3999 N  N    . PHE   B 1 273 ? 22.417 13.617 62.568  1 118.82 ? 272 PHE   B N    1 2 
ATOM   4000 C  CA   . PHE   B 1 273 ? 22.247 12.47  61.668  1 119.67 ? 272 PHE   B CA   1 2 
ATOM   4001 C  C    . PHE   B 1 273 ? 21.601 12.945 60.361  1 119.8  ? 272 PHE   B C    1 2 
ATOM   4002 O  O    . PHE   B 1 273 ? 20.375 12.956 60.254  1 119.8  ? 272 PHE   B O    1 2 
ATOM   4003 C  CB   . PHE   B 1 273 ? 21.354 11.384 62.303  1 119.93 ? 272 PHE   B CB   1 2 
ATOM   4004 C  CG   . PHE   B 1 273 ? 21.97  10.599 63.438  1 120.74 ? 272 PHE   B CG   1 2 
ATOM   4005 C  CD1  . PHE   B 1 273 ? 22.766 9.497  63.189  1 121.62 ? 272 PHE   B CD1  1 2 
ATOM   4006 C  CD2  . PHE   B 1 273 ? 21.742 10.959 64.752  1 121.47 ? 272 PHE   B CD2  1 2 
ATOM   4007 C  CE1  . PHE   B 1 273 ? 23.327 8.777  64.233  1 122.34 ? 272 PHE   B CE1  1 2 
ATOM   4008 C  CE2  . PHE   B 1 273 ? 22.307 10.241 65.794  1 122.22 ? 272 PHE   B CE2  1 2 
ATOM   4009 C  CZ   . PHE   B 1 273 ? 23.092 9.152  65.529  1 122.1  ? 272 PHE   B CZ   1 2 
HETATM 4010 P  PA   . NAD   C 2 .   ? 46.874 33.667 64.395  1 59.75  ? 401 NAD   A PA   1 1 
HETATM 4011 O  O1A  . NAD   C 2 .   ? 47.94  32.906 63.712  1 59.84  ? 401 NAD   A O1A  1 1 
HETATM 4012 O  O2A  . NAD   C 2 .   ? 47.159 34.281 65.714  1 59.71  ? 401 NAD   A O2A  1 1 
HETATM 4013 O  O5B  . NAD   C 2 .   ? 46.367 34.776 63.366  1 59.4   ? 401 NAD   A O5B  1 1 
HETATM 4014 C  C5B  . NAD   C 2 .   ? 45.102 35.437 63.572  1 59.39  ? 401 NAD   A C5B  1 1 
HETATM 4015 C  C4B  . NAD   C 2 .   ? 45.118 36.748 62.828  1 59.75  ? 401 NAD   A C4B  1 1 
HETATM 4016 O  O4B  . NAD   C 2 .   ? 43.991 37.552 63.24   1 59.99  ? 401 NAD   A O4B  1 1 
HETATM 4017 C  C3B  . NAD   C 2 .   ? 46.375 37.606 63.035  1 59.92  ? 401 NAD   A C3B  1 1 
HETATM 4018 O  O3B  . NAD   C 2 .   ? 47.095 37.797 61.821  1 60.05  ? 401 NAD   A O3B  1 1 
HETATM 4019 C  C2B  . NAD   C 2 .   ? 45.841 38.916 63.638  1 59.92  ? 401 NAD   A C2B  1 1 
HETATM 4020 O  O2B  . NAD   C 2 .   ? 46.519 40.077 63.171  1 59.72  ? 401 NAD   A O2B  1 1 
HETATM 4021 C  C1B  . NAD   C 2 .   ? 44.382 38.908 63.201  1 60.24  ? 401 NAD   A C1B  1 1 
HETATM 4022 N  N9A  . NAD   C 2 .   ? 43.497 39.686 64.067  1 60.79  ? 401 NAD   A N9A  1 1 
HETATM 4023 C  C8A  . NAD   C 2 .   ? 43.378 39.597 65.43   1 61.09  ? 401 NAD   A C8A  1 1 
HETATM 4024 N  N7A  . NAD   C 2 .   ? 42.595 40.506 65.96   1 61.21  ? 401 NAD   A N7A  1 1 
HETATM 4025 C  C5A  . NAD   C 2 .   ? 42.166 41.246 64.868  1 61.39  ? 401 NAD   A C5A  1 1 
HETATM 4026 C  C6A  . NAD   C 2 .   ? 41.34  42.38  64.756  1 61.75  ? 401 NAD   A C6A  1 1 
HETATM 4027 N  N6A  . NAD   C 2 .   ? 40.803 43.018 65.803  1 62.07  ? 401 NAD   A N6A  1 1 
HETATM 4028 N  N1A  . NAD   C 2 .   ? 41.127 42.882 63.521  1 61.61  ? 401 NAD   A N1A  1 1 
HETATM 4029 C  C2A  . NAD   C 2 .   ? 41.714 42.289 62.477  1 61.7   ? 401 NAD   A C2A  1 1 
HETATM 4030 N  N3A  . NAD   C 2 .   ? 42.515 41.222 62.461  1 61.6   ? 401 NAD   A N3A  1 1 
HETATM 4031 C  C4A  . NAD   C 2 .   ? 42.71  40.748 63.695  1 61.23  ? 401 NAD   A C4A  1 1 
HETATM 4032 O  O3   . NAD   C 2 .   ? 45.574 32.745 64.519  1 60.44  ? 401 NAD   A O3   1 1 
HETATM 4033 P  PN   . NAD   C 2 .   ? 45.04  31.445 63.751  1 61.28  ? 401 NAD   A PN   1 1 
HETATM 4034 O  O1N  . NAD   C 2 .   ? 44.96  31.719 62.298  1 61.38  ? 401 NAD   A O1N  1 1 
HETATM 4035 O  O2N  . NAD   C 2 .   ? 45.794 30.263 64.232  1 61.12  ? 401 NAD   A O2N  1 1 
HETATM 4036 O  O5D  . NAD   C 2 .   ? 43.529 31.373 64.268  1 61.65  ? 401 NAD   A O5D  1 1 
HETATM 4037 C  C5D  . NAD   C 2 .   ? 42.679 32.534 64.133  1 61.69  ? 401 NAD   A C5D  1 1 
HETATM 4038 C  C4D  . NAD   C 2 .   ? 41.238 32.096 64.123  1 61.54  ? 401 NAD   A C4D  1 1 
HETATM 4039 O  O4D  . NAD   C 2 .   ? 41.169 30.656 64.013  1 61.66  ? 401 NAD   A O4D  1 1 
HETATM 4040 C  C3D  . NAD   C 2 .   ? 40.434 32.475 65.368  1 61.54  ? 401 NAD   A C3D  1 1 
HETATM 4041 O  O3D  . NAD   C 2 .   ? 39.112 32.88  65.03   1 61.33  ? 401 NAD   A O3D  1 1 
HETATM 4042 C  C2D  . NAD   C 2 .   ? 40.466 31.19  66.2    1 61.88  ? 401 NAD   A C2D  1 1 
HETATM 4043 O  O2D  . NAD   C 2 .   ? 39.37  31.084 67.105  1 61.95  ? 401 NAD   A O2D  1 1 
HETATM 4044 C  C1D  . NAD   C 2 .   ? 40.459 30.125 65.099  1 62.06  ? 401 NAD   A C1D  1 1 
HETATM 4045 N  N1N  . NAD   C 2 .   ? 41.119 28.842 65.544  1 62.44  ? 401 NAD   A N1N  1 1 
HETATM 4046 C  C2N  . NAD   C 2 .   ? 42.429 28.848 65.849  1 62.72  ? 401 NAD   A C2N  1 1 
HETATM 4047 C  C3N  . NAD   C 2 .   ? 43.036 27.711 66.348  1 62.9   ? 401 NAD   A C3N  1 1 
HETATM 4048 C  C7N  . NAD   C 2 .   ? 44.51  27.694 66.665  1 63.1   ? 401 NAD   A C7N  1 1 
HETATM 4049 O  O7N  . NAD   C 2 .   ? 44.931 26.98  67.596  1 62.87  ? 401 NAD   A O7N  1 1 
HETATM 4050 N  N7N  . NAD   C 2 .   ? 45.312 28.455 65.924  1 63.27  ? 401 NAD   A N7N  1 1 
HETATM 4051 C  C4N  . NAD   C 2 .   ? 42.264 26.569 66.519  1 62.65  ? 401 NAD   A C4N  1 1 
HETATM 4052 C  C5N  . NAD   C 2 .   ? 40.924 26.579 66.171  1 62.44  ? 401 NAD   A C5N  1 1 
HETATM 4053 C  C6N  . NAD   C 2 .   ? 40.364 27.734 65.678  1 62.42  ? 401 NAD   A C6N  1 1 
HETATM 4054 C  C4   . A1AG6 D 3 .   ? 43.07  25.66  72.023  1 97.19  ? 402 A1AG6 A C4   1 1 
HETATM 4055 N  N2   . A1AG6 D 3 .   ? 44.37  25.807 73.81   1 97.24  ? 402 A1AG6 A N2   1 1 
HETATM 4056 C  C7   . A1AG6 D 3 .   ? 41.834 23.389 70.93   1 97.44  ? 402 A1AG6 A C7   1 1 
HETATM 4057 C  C6   . A1AG6 D 3 .   ? 41.573 24.643 70.409  1 97.11  ? 402 A1AG6 A C6   1 1 
HETATM 4058 C  C9   . A1AG6 D 3 .   ? 43.33  24.387 72.569  1 97.43  ? 402 A1AG6 A C9   1 1 
HETATM 4059 C  C20  . A1AG6 D 3 .   ? 40.331 20.585 72.479  1 98.99  ? 402 A1AG6 A C20  1 1 
HETATM 4060 C  C8   . A1AG6 D 3 .   ? 42.7   23.254 72.013  1 97.77  ? 402 A1AG6 A C8   1 1 
HETATM 4061 C  C18  . A1AG6 D 3 .   ? 38.833 18.747 71.989  1 99.1   ? 402 A1AG6 A C18  1 1 
HETATM 4062 C  C16  . A1AG6 D 3 .   ? 41.176 18.556 71.479  1 99.28  ? 402 A1AG6 A C16  1 1 
HETATM 4063 C  C19  . A1AG6 D 3 .   ? 39.062 20.035 72.48   1 98.85  ? 402 A1AG6 A C19  1 1 
HETATM 4064 C  C26  . A1AG6 D 3 .   ? 35.135 16.482 73.758  1 98.86  ? 402 A1AG6 A C26  1 1 
HETATM 4065 C  C1   . A1AG6 D 3 .   ? 45.091 26.301 74.983  1 97.23  ? 402 A1AG6 A C1   1 1 
HETATM 4066 C  C3   . A1AG6 D 3 .   ? 43.792 26.566 72.869  1 97.2   ? 402 A1AG6 A C3   1 1 
HETATM 4067 C  C5   . A1AG6 D 3 .   ? 42.178 25.784 70.935  1 96.87  ? 402 A1AG6 A C5   1 1 
HETATM 4068 N  N10  . A1AG6 D 3 .   ? 44.138 24.468 73.658  1 97.26  ? 402 A1AG6 A N10  1 1 
HETATM 4069 N  N11  . A1AG6 D 3 .   ? 42.9   21.999 72.656  1 98.39  ? 402 A1AG6 A N11  1 1 
HETATM 4070 S  S12  . A1AG6 D 3 .   ? 43.011 20.513 71.987  1 98.98  ? 402 A1AG6 A S12  1 1 
HETATM 4071 O  O13  . A1AG6 D 3 .   ? 43.437 20.658 70.629  1 99.12  ? 402 A1AG6 A O13  1 1 
HETATM 4072 O  O14  . A1AG6 D 3 .   ? 43.807 19.743 72.892  1 99.07  ? 402 A1AG6 A O14  1 1 
HETATM 4073 C  C15  . A1AG6 D 3 .   ? 41.383 19.833 71.977  1 99.16  ? 402 A1AG6 A C15  1 1 
HETATM 4074 C  C17  . A1AG6 D 3 .   ? 39.902 18.017 71.487  1 99.27  ? 402 A1AG6 A C17  1 1 
HETATM 4075 CL CL21 . A1AG6 D 3 .   ? 37.735 20.975 73.092  1 98.39  ? 402 A1AG6 A CL21 1 1 
HETATM 4076 C  C28  . A1AG6 D 3 .   ? 41.874 27.076 70.254  1 96.31  ? 402 A1AG6 A C28  1 1 
HETATM 4077 O  O29  . A1AG6 D 3 .   ? 40.92  27.164 69.502  1 96.04  ? 402 A1AG6 A O29  1 1 
HETATM 4078 O  O30  . A1AG6 D 3 .   ? 42.601 28.102 70.58   1 96.18  ? 402 A1AG6 A O30  1 1 
HETATM 4079 O  O22  . A1AG6 D 3 .   ? 37.539 18.287 72.047  1 99.13  ? 402 A1AG6 A O22  1 1 
HETATM 4080 C  C23  . A1AG6 D 3 .   ? 37.288 16.934 71.631  1 99.03  ? 402 A1AG6 A C23  1 1 
HETATM 4081 C  C24  . A1AG6 D 3 .   ? 35.806 16.662 71.733  1 98.94  ? 402 A1AG6 A C24  1 1 
HETATM 4082 C  C25  . A1AG6 D 3 .   ? 34.988 17.556 72.673  1 98.84  ? 402 A1AG6 A C25  1 1 
HETATM 4083 C  C27  . A1AG6 D 3 .   ? 35.487 15.476 72.655  1 98.89  ? 402 A1AG6 A C27  1 1 
HETATM 4084 H  H37  . A1AG6 D 3 .   ? 42.949 22.12  73.663  0 116.88 ? 402 A1AG6 A H37  1 1 
HETATM 4085 P  PA   . NAD   E 2 .   ? 10.314 38.16  80.761  1 58.49  ? 401 NAD   B PA   1 2 
HETATM 4086 O  O1A  . NAD   E 2 .   ? 9.009  37.675 81.258  1 58.3   ? 401 NAD   B O1A  1 2 
HETATM 4087 O  O2A  . NAD   E 2 .   ? 10.34  39.152 79.657  1 58.33  ? 401 NAD   B O2A  1 2 
HETATM 4088 O  O5B  . NAD   E 2 .   ? 11.118 38.722 82.022  1 59.29  ? 401 NAD   B O5B  1 2 
HETATM 4089 C  C5B  . NAD   E 2 .   ? 12.547 38.917 81.961  1 59.73  ? 401 NAD   B C5B  1 2 
HETATM 4090 C  C4B  . NAD   E 2 .   ? 12.942 39.914 83.022  1 60.02  ? 401 NAD   B C4B  1 2 
HETATM 4091 O  O4B  . NAD   E 2 .   ? 14.304 40.339 82.8    1 60.5   ? 401 NAD   B O4B  1 2 
HETATM 4092 C  C3B  . NAD   E 2 .   ? 12.08  41.184 83.087  1 59.97  ? 401 NAD   B C3B  1 2 
HETATM 4093 O  O3B  . NAD   E 2 .   ? 11.398 41.303 84.329  1 59.84  ? 401 NAD   B O3B  1 2 
HETATM 4094 C  C2B  . NAD   E 2 .   ? 13.075 42.328 82.835  1 60.41  ? 401 NAD   B C2B  1 2 
HETATM 4095 O  O2B  . NAD   E 2 .   ? 12.811 43.495 83.609  1 60.38  ? 401 NAD   B O2B  1 2 
HETATM 4096 C  C1B  . NAD   E 2 .   ? 14.412 41.687 83.203  1 61     ? 401 NAD   B C1B  1 2 
HETATM 4097 N  N9A  . NAD   E 2 .   ? 15.567 42.288 82.537  1 62.04  ? 401 NAD   B N9A  1 2 
HETATM 4098 C  C8A  . NAD   E 2 .   ? 15.72  42.518 81.193  1 62.3   ? 401 NAD   B C8A  1 2 
HETATM 4099 N  N7A  . NAD   E 2 .   ? 16.801 43.194 80.886  1 62.44  ? 401 NAD   B N7A  1 2 
HETATM 4100 C  C5A  . NAD   E 2 .   ? 17.405 43.425 82.115  1 62.54  ? 401 NAD   B C5A  1 2 
HETATM 4101 C  C6A  . NAD   E 2 .   ? 18.564 44.133 82.484  1 62.65  ? 401 NAD   B C6A  1 2 
HETATM 4102 N  N6A  . NAD   E 2 .   ? 19.343 44.793 81.623  1 62.84  ? 401 NAD   B N6A  1 2 
HETATM 4103 N  N1A  . NAD   E 2 .   ? 18.863 44.202 83.797  1 62.52  ? 401 NAD   B N1A  1 2 
HETATM 4104 C  C2A  . NAD   E 2 .   ? 18.049 43.607 84.673  1 62.53  ? 401 NAD   B C2A  1 2 
HETATM 4105 N  N3A  . NAD   E 2 .   ? 16.93  42.918 84.443  1 62.32  ? 401 NAD   B N3A  1 2 
HETATM 4106 C  C4A  . NAD   E 2 .   ? 16.657 42.868 83.14   1 62.3   ? 401 NAD   B C4A  1 2 
HETATM 4107 O  O3   . NAD   E 2 .   ? 11.225 36.901 80.369  1 58.31  ? 401 NAD   B O3   1 2 
HETATM 4108 P  PN   . NAD   E 2 .   ? 11.234 35.342 80.746  1 57.89  ? 401 NAD   B PN   1 2 
HETATM 4109 O  O1N  . NAD   E 2 .   ? 11.314 35.193 82.215  1 58.3   ? 401 NAD   B O1N  1 2 
HETATM 4110 O  O2N  . NAD   E 2 .   ? 10.135 34.667 80.012  1 58.1   ? 401 NAD   B O2N  1 2 
HETATM 4111 O  O5D  . NAD   E 2 .   ? 12.65  34.88  80.167  1 56.68  ? 401 NAD   B O5D  1 2 
HETATM 4112 C  C5D  . NAD   E 2 .   ? 13.838 35.595 80.555  1 55.89  ? 401 NAD   B C5D  1 2 
HETATM 4113 C  C4D  . NAD   E 2 .   ? 15.03  34.687 80.39   1 55.45  ? 401 NAD   B C4D  1 2 
HETATM 4114 O  O4D  . NAD   E 2 .   ? 14.583 33.338 80.126  1 55.41  ? 401 NAD   B O4D  1 2 
HETATM 4115 C  C3D  . NAD   E 2 .   ? 15.989 35.054 79.259  1 55.2   ? 401 NAD   B C3D  1 2 
HETATM 4116 O  O3D  . NAD   E 2 .   ? 17.351 34.865 79.631  1 55.04  ? 401 NAD   B O3D  1 2 
HETATM 4117 C  C2D  . NAD   E 2 .   ? 15.557 34.117 78.131  1 55.45  ? 401 NAD   B C2D  1 2 
HETATM 4118 O  O2D  . NAD   E 2 .   ? 16.598 33.859 77.195  1 55.33  ? 401 NAD   B O2D  1 2 
HETATM 4119 C  C1D  . NAD   E 2 .   ? 15.129 32.877 78.922  1 55.81  ? 401 NAD   B C1D  1 2 
HETATM 4120 N  N1N  . NAD   E 2 .   ? 14.087 32.07  78.194  1 56.67  ? 401 NAD   B N1N  1 2 
HETATM 4121 C  C2N  . NAD   E 2 .   ? 12.881 32.616 77.954  1 56.93  ? 401 NAD   B C2N  1 2 
HETATM 4122 C  C3N  . NAD   E 2 .   ? 11.941 31.935 77.202  1 56.98  ? 401 NAD   B C3N  1 2 
HETATM 4123 C  C7N  . NAD   E 2 .   ? 10.577 32.518 76.948  1 56.83  ? 401 NAD   B C7N  1 2 
HETATM 4124 O  O7N  . NAD   E 2 .   ? 9.993  32.262 75.888  1 56.84  ? 401 NAD   B O7N  1 2 
HETATM 4125 N  N7N  . NAD   E 2 .   ? 10.054 33.299 77.884  1 56.77  ? 401 NAD   B N7N  1 2 
HETATM 4126 C  C4N  . NAD   E 2 .   ? 12.27  30.68  76.708  1 57.16  ? 401 NAD   B C4N  1 2 
HETATM 4127 C  C5N  . NAD   E 2 .   ? 13.508 30.126 76.992  1 57.18  ? 401 NAD   B C5N  1 2 
HETATM 4128 C  C6N  . NAD   E 2 .   ? 14.41  30.839 77.75   1 56.99  ? 401 NAD   B C6N  1 2 
HETATM 4129 O  O    . HOH   F 4 .   ? 32.1   49.715 42.978  1 22.39  ? 501 HOH   A O    1 ? 
HETATM 4130 O  O    . HOH   F 4 .   ? 33.135 47.248 68.182  1 3      ? 502 HOH   A O    1 ? 
HETATM 4131 O  O    . HOH   F 4 .   ? 50.718 20.684 52.455  1 22.89  ? 503 HOH   A O    1 ? 
HETATM 4132 O  O    . HOH   F 4 .   ? 24.354 17.504 76.397  1 20.35  ? 504 HOH   A O    1 ? 
HETATM 4133 O  O    . HOH   F 4 .   ? 44.465 48.341 48.96   1 3      ? 505 HOH   A O    1 ? 
HETATM 4134 O  O    . HOH   F 4 .   ? 52.801 24.973 57.573  1 3      ? 506 HOH   A O    1 ? 
HETATM 4135 O  O    . HOH   F 4 .   ? 55.487 25.49  73.321  1 24.54  ? 507 HOH   A O    1 ? 
HETATM 4136 O  O    . HOH   F 4 .   ? 45.963 37.757 80.72   1 6.37   ? 508 HOH   A O    1 ? 
HETATM 4137 O  O    . HOH   F 4 .   ? 50.487 17.573 55.398  1 8.94   ? 509 HOH   A O    1 ? 
HETATM 4138 O  O    . HOH   F 4 .   ? 12.477 23.035 54.258  1 17.25  ? 510 HOH   A O    1 ? 
HETATM 4139 O  O    . HOH   F 4 .   ? 46.722 34.935 78.821  1 3      ? 511 HOH   A O    1 ? 
HETATM 4140 O  O    . HOH   F 4 .   ? 49.698 45.302 49.185  1 3      ? 512 HOH   A O    1 ? 
HETATM 4141 O  O    . HOH   F 4 .   ? 20.449 25.151 62.286  1 21.29  ? 513 HOH   A O    1 ? 
HETATM 4142 O  O    . HOH   F 4 .   ? 45.244 38.604 86.841  1 3      ? 514 HOH   A O    1 ? 
HETATM 4143 O  O    . HOH   F 4 .   ? 56.189 37.257 58.406  1 12.69  ? 515 HOH   A O    1 ? 
HETATM 4144 O  O    . HOH   F 4 .   ? 27.147 22.082 45.979  1 31.5   ? 516 HOH   A O    1 ? 
HETATM 4145 O  O    . HOH   F 4 .   ? 19.057 37.47  56.175  1 3      ? 517 HOH   A O    1 ? 
HETATM 4146 O  O    . HOH   F 4 .   ? 39.072 43.951 85.227  1 14.95  ? 518 HOH   A O    1 ? 
HETATM 4147 O  O    . HOH   F 4 .   ? 51.344 27.188 68.902  1 9.72   ? 519 HOH   A O    1 ? 
HETATM 4148 O  O    . HOH   F 4 .   ? 55.095 29.575 46.327  1 34.6   ? 520 HOH   A O    1 ? 
HETATM 4149 O  O    . HOH   F 4 .   ? 28.779 43.004 49.234  1 5.48   ? 521 HOH   A O    1 ? 
HETATM 4150 O  O    . HOH   F 4 .   ? 46.545 29.99  81.457  1 3      ? 522 HOH   A O    1 ? 
HETATM 4151 O  O    . HOH   F 4 .   ? 27.461 56.645 51.691  1 28.05  ? 523 HOH   A O    1 ? 
HETATM 4152 O  O    . HOH   F 4 .   ? 47.79  33.782 74.08   1 3      ? 524 HOH   A O    1 ? 
HETATM 4153 O  O    . HOH   F 4 .   ? 30.542 31.097 46.545  1 26.64  ? 525 HOH   A O    1 ? 
HETATM 4154 O  O    . HOH   F 4 .   ? 31.312 51.315 67.084  1 3      ? 526 HOH   A O    1 ? 
HETATM 4155 O  O    . HOH   F 4 .   ? 48.488 40.221 40.238  1 18.47  ? 527 HOH   A O    1 ? 
HETATM 4156 O  O    . HOH   F 4 .   ? 27.478 19.375 57.467  1 13.42  ? 528 HOH   A O    1 ? 
HETATM 4157 O  O    . HOH   F 4 .   ? 53.13  44.061 49.49   1 3      ? 529 HOH   A O    1 ? 
HETATM 4158 O  O    . HOH   F 4 .   ? 19.133 37.942 40.485  1 3      ? 530 HOH   A O    1 ? 
HETATM 4159 O  O    . HOH   F 4 .   ? 52.344 32.382 72.259  1 17.02  ? 531 HOH   A O    1 ? 
HETATM 4160 O  O    . HOH   F 4 .   ? 42.952 40.261 87.185  1 3.63   ? 532 HOH   A O    1 ? 
HETATM 4161 O  O    . HOH   F 4 .   ? 25.747 53.242 52.094  1 10.41  ? 533 HOH   A O    1 ? 
HETATM 4162 O  O    . HOH   F 4 .   ? 32.709 58.268 57.247  1 3      ? 534 HOH   A O    1 ? 
HETATM 4163 O  O    . HOH   F 4 .   ? 48.216 8.058  83.941  1 19.39  ? 535 HOH   A O    1 ? 
HETATM 4164 O  O    . HOH   F 4 .   ? 45.414 41.769 68.202  1 3      ? 536 HOH   A O    1 ? 
HETATM 4165 O  O    . HOH   F 4 .   ? 43.626 11.193 68.742  1 22.27  ? 537 HOH   A O    1 ? 
HETATM 4166 O  O    . HOH   F 4 .   ? 35.949 55.07  50.575  1 3      ? 538 HOH   A O    1 ? 
HETATM 4167 O  O    . HOH   F 4 .   ? 44.495 18.789 49.248  1 23.66  ? 539 HOH   A O    1 ? 
HETATM 4168 O  O    . HOH   F 4 .   ? 18.196 43.06  51.142  1 3      ? 540 HOH   A O    1 ? 
HETATM 4169 O  O    . HOH   F 4 .   ? 27.717 49.821 55.638  1 3      ? 541 HOH   A O    1 ? 
HETATM 4170 O  O    . HOH   F 4 .   ? 34.247 48.955 40.664  1 28.61  ? 542 HOH   A O    1 ? 
HETATM 4171 O  O    . HOH   F 4 .   ? 31.938 43.161 40.902  1 23.48  ? 543 HOH   A O    1 ? 
HETATM 4172 O  O    . HOH   F 4 .   ? 47.698 26.066 81.668  1 3      ? 544 HOH   A O    1 ? 
HETATM 4173 O  O    . HOH   F 4 .   ? 25.324 48.731 57.433  1 8.42   ? 545 HOH   A O    1 ? 
HETATM 4174 O  O    . HOH   F 4 .   ? 52.225 19.698 74.489  1 26.99  ? 546 HOH   A O    1 ? 
HETATM 4175 O  O    . HOH   F 4 .   ? 53.61  28.732 49.75   1 24.86  ? 547 HOH   A O    1 ? 
HETATM 4176 O  O    . HOH   F 4 .   ? 19.879 49.685 46.963  1 43.65  ? 548 HOH   A O    1 ? 
HETATM 4177 O  O    . HOH   F 4 .   ? 11.08  20.972 55.718  1 17.01  ? 549 HOH   A O    1 ? 
HETATM 4178 O  O    . HOH   F 4 .   ? 25.54  52.54  58.497  1 26.27  ? 550 HOH   A O    1 ? 
HETATM 4179 O  O    . HOH   F 4 .   ? 56.065 34.338 65.5    1 3      ? 551 HOH   A O    1 ? 
HETATM 4180 O  O    . HOH   F 4 .   ? 52.123 35.241 73.761  1 34.41  ? 552 HOH   A O    1 ? 
HETATM 4181 O  O    . HOH   F 4 .   ? 46.848 1.214  48.839  1 8.55   ? 553 HOH   A O    1 ? 
HETATM 4182 O  O    . HOH   F 4 .   ? 34.14  61.79  57.214  1 14.26  ? 554 HOH   A O    1 ? 
HETATM 4183 O  O    . HOH   F 4 .   ? 45.455 43.291 86.882  1 14.98  ? 555 HOH   A O    1 ? 
HETATM 4184 O  O    . HOH   F 4 .   ? 56.916 34.533 73.735  1 22.3   ? 556 HOH   A O    1 ? 
HETATM 4185 O  O    . HOH   F 4 .   ? 55.554 32.344 76.602  1 34.52  ? 557 HOH   A O    1 ? 
HETATM 4186 O  O    . HOH   F 4 .   ? 21.029 5.493  76.277  1 44.95  ? 558 HOH   A O    1 ? 
HETATM 4187 O  O    . HOH   F 4 .   ? 50.684 8.712  88.94   1 31.41  ? 559 HOH   A O    1 ? 
HETATM 4188 O  O    . HOH   F 4 .   ? 54.101 19.282 47.057  1 17.84  ? 560 HOH   A O    1 ? 
HETATM 4189 O  O    . HOH   F 4 .   ? 28.893 -0.574 53.359  1 29.89  ? 561 HOH   A O    1 ? 
HETATM 4190 O  O    . HOH   F 4 .   ? 52.582 28.434 89.56   1 31.92  ? 562 HOH   A O    1 ? 
HETATM 4191 O  O    . HOH   F 4 .   ? 61.965 25.244 43.627  1 12.42  ? 563 HOH   A O    1 ? 
HETATM 4192 O  O    . HOH   F 4 .   ? 26.154 -2.005 49.19   1 34.03  ? 564 HOH   A O    1 ? 
HETATM 4193 O  O    . HOH   F 4 .   ? 53.088 4.521  62.528  1 5.58   ? 565 HOH   A O    1 ? 
HETATM 4194 O  O    . HOH   F 4 .   ? 58.433 33.137 81.522  1 18.72  ? 566 HOH   A O    1 ? 
HETATM 4195 O  O    . HOH   F 4 .   ? 64.172 26.072 51.635  1 18.16  ? 567 HOH   A O    1 ? 
HETATM 4196 O  O    . HOH   F 4 .   ? 63     22.766 84.338  1 10.92  ? 568 HOH   A O    1 ? 
HETATM 4197 O  O    . HOH   F 4 .   ? 0.081  25.983 54.985  1 19.28  ? 569 HOH   A O    1 ? 
HETATM 4198 O  O    . HOH   F 4 .   ? 29.314 67.536 51.301  1 11.17  ? 570 HOH   A O    1 ? 
HETATM 4199 O  O    . HOH   F 4 .   ? 60.971 22.346 41.731  1 15.62  ? 571 HOH   A O    1 ? 
HETATM 4200 O  O    . HOH   F 4 .   ? 61.59  32.706 83.453  1 9.8    ? 572 HOH   A O    1 ? 
HETATM 4201 O  O    . HOH   F 4 .   ? 62.439 12.993 42.488  1 42.51  ? 573 HOH   A O    1 ? 
HETATM 4202 O  O    . HOH   F 4 .   ? 61.294 34.149 96.742  1 25.07  ? 574 HOH   A O    1 ? 
HETATM 4203 O  O    . HOH   F 4 .   ? 63.416 30.892 92.789  1 19.8   ? 575 HOH   A O    1 ? 
HETATM 4204 O  O    . HOH   G 4 .   ? 14.526 24.994 64.588  1 6.11   ? 501 HOH   B O    1 ? 
HETATM 4205 O  O    . HOH   G 4 .   ? 2.843  35.287 75.82   1 16.86  ? 502 HOH   B O    1 ? 
HETATM 4206 O  O    . HOH   G 4 .   ? 31.998 44.491 93.42   1 36.36  ? 503 HOH   B O    1 ? 
HETATM 4207 O  O    . HOH   G 4 .   ? 22.405 51.11  63.821  1 23.41  ? 504 HOH   B O    1 ? 
HETATM 4208 O  O    . HOH   G 4 .   ? 25.219 52.288 85.928  1 7.01   ? 505 HOH   B O    1 ? 
HETATM 4209 O  O    . HOH   G 4 .   ? 25.857 20.109 89.131  1 41.03  ? 506 HOH   B O    1 ? 
HETATM 4210 O  O    . HOH   G 4 .   ? 11.367 35.86  107.178 1 3      ? 507 HOH   B O    1 ? 
HETATM 4211 O  O    . HOH   G 4 .   ? 14.964 41.065 54.442  1 6.89   ? 508 HOH   B O    1 ? 
HETATM 4212 O  O    . HOH   G 4 .   ? 17.751 39.596 69.844  1 58.66  ? 509 HOH   B O    1 ? 
HETATM 4213 O  O    . HOH   G 4 .   ? 2.968  38.111 86.422  1 3      ? 510 HOH   B O    1 ? 
HETATM 4214 O  O    . HOH   G 4 .   ? 5.81   41.505 73.948  1 9.48   ? 511 HOH   B O    1 ? 
HETATM 4215 O  O    . HOH   G 4 .   ? 34.025 36.324 102.217 1 3      ? 512 HOH   B O    1 ? 
HETATM 4216 O  O    . HOH   G 4 .   ? 15.841 44.889 78.323  1 9.52   ? 513 HOH   B O    1 ? 
HETATM 4217 O  O    . HOH   G 4 .   ? 32.805 23.496 102.701 1 10.44  ? 514 HOH   B O    1 ? 
HETATM 4218 O  O    . HOH   G 4 .   ? 7.986  50.060 86.238  1 14.36  ? 515 HOH   B O    1 ? 
HETATM 4219 O  O    . HOH   G 4 .   ? 30.044 36.133 96.914  1 11.97  ? 516 HOH   B O    1 ? 
HETATM 4220 O  O    . HOH   G 4 .   ? 16.987 49.057 96.587  1 3.24   ? 517 HOH   B O    1 ? 
HETATM 4221 O  O    . HOH   G 4 .   ? 20.518 8.256  92.13   1 23.36  ? 518 HOH   B O    1 ? 
HETATM 4222 O  O    . HOH   G 4 .   ? 23.194 19.376 62.702  1 5.98   ? 519 HOH   B O    1 ? 
HETATM 4223 O  O    . HOH   G 4 .   ? 29.076 48.987 108.920 1 3      ? 520 HOH   B O    1 ? 
HETATM 4224 O  O    . HOH   G 4 .   ? 32.423 46.15  79.993  1 25.03  ? 521 HOH   B O    1 ? 
HETATM 4225 O  O    . HOH   G 4 .   ? 30.557 40.88  103.328 1 10.55  ? 522 HOH   B O    1 ? 
HETATM 4226 O  O    . HOH   G 4 .   ? 35.939 41.614 88.602  1 3.4    ? 523 HOH   B O    1 ? 
HETATM 4227 O  O    . HOH   G 4 .   ? 35.041 49.326 98.004  1 3      ? 524 HOH   B O    1 ? 
HETATM 4228 O  O    . HOH   G 4 .   ? 25.119 50.217 75.221  1 18.07  ? 525 HOH   B O    1 ? 
HETATM 4229 O  O    . HOH   G 4 .   ? 13.152 42.019 78.848  1 3.13   ? 526 HOH   B O    1 ? 
HETATM 4230 O  O    . HOH   G 4 .   ? 22.654 16.094 81.097  1 15.1   ? 527 HOH   B O    1 ? 
HETATM 4231 O  O    . HOH   G 4 .   ? 23.959 52.099 82.862  1 34.92  ? 528 HOH   B O    1 ? 
HETATM 4232 O  O    . HOH   G 4 .   ? 4.398  43.451 87.613  1 33.32  ? 529 HOH   B O    1 ? 
HETATM 4233 O  O    . HOH   G 4 .   ? 32.152 49.317 90.348  1 33.37  ? 530 HOH   B O    1 ? 
HETATM 4234 O  O    . HOH   G 4 .   ? 7.741  27.865 103.451 1 41.37  ? 531 HOH   B O    1 ? 
HETATM 4235 O  O    . HOH   G 4 .   ? 13.265 46.516 99.505  1 7.79   ? 532 HOH   B O    1 ? 
HETATM 4236 O  O    . HOH   G 4 .   ? 28.981 46.908 79.686  1 17.21  ? 533 HOH   B O    1 ? 
HETATM 4237 O  O    . HOH   G 4 .   ? 1.22   23.914 71.297  1 14.1   ? 534 HOH   B O    1 ? 
HETATM 4238 O  O    . HOH   G 4 .   ? 17.589 16.047 79.67   1 7.66   ? 535 HOH   B O    1 ? 
HETATM 4239 O  O    . HOH   G 4 .   ? 41.819 26.035 93.495  1 6      ? 536 HOH   B O    1 ? 
HETATM 4240 O  O    . HOH   G 4 .   ? 14.147 21.229 64.715  1 3      ? 537 HOH   B O    1 ? 
HETATM 4241 O  O    . HOH   G 4 .   ? 8.416  21.555 93.029  1 15.32  ? 538 HOH   B O    1 ? 
HETATM 4242 O  O    . HOH   G 4 .   ? 35.285 54.966 83.937  1 3      ? 539 HOH   B O    1 ? 
HETATM 4243 O  O    . HOH   G 4 .   ? 36.51  46.21  97.811  1 4.29   ? 540 HOH   B O    1 ? 
HETATM 4244 O  O    . HOH   G 4 .   ? 25.823 32.059 103.597 1 31.24  ? 541 HOH   B O    1 ? 
HETATM 4245 O  O    . HOH   G 4 .   ? 13.422 3.925  84.585  1 19.62  ? 542 HOH   B O    1 ? 
HETATM 4246 O  O    . HOH   G 4 .   ? 13.563 45.327 79.713  1 3      ? 543 HOH   B O    1 ? 
HETATM 4247 O  O    . HOH   G 4 .   ? 6.478  23.194 107.862 1 3      ? 544 HOH   B O    1 ? 
HETATM 4248 O  O    . HOH   G 4 .   ? 7.275  23.956 103.431 1 19.19  ? 545 HOH   B O    1 ? 
HETATM 4249 O  O    . HOH   G 4 .   ? 2.093  40.582 103.789 1 24.52  ? 546 HOH   B O    1 ? 
HETATM 4250 O  O    . HOH   G 4 .   ? 28.02  56.234 91.361  1 14.19  ? 547 HOH   B O    1 ? 
HETATM 4251 O  O    . HOH   G 4 .   ? 29.207 24.558 103.469 1 11.8   ? 548 HOH   B O    1 ? 
HETATM 4252 O  O    . HOH   G 4 .   ? 36.149 56.436 86.125  1 31.89  ? 549 HOH   B O    1 ? 
HETATM 4253 O  O    . HOH   G 4 .   ? 1.078  22.364 93.894  1 33.15  ? 550 HOH   B O    1 ? 
HETATM 4254 O  O    . HOH   G 4 .   ? 21.470 57.010 64.999  1 35.8   ? 551 HOH   B O    1 ? 
HETATM 4255 O  O    . HOH   G 4 .   ? 34.914 42.811 92.294  1 4.91   ? 552 HOH   B O    1 ? 
HETATM 4256 O  O    . HOH   G 4 .   ? 22.588 15.454 55.667  1 43.91  ? 553 HOH   B O    1 ? 
HETATM 4257 O  O    . HOH   G 4 .   ? 22.232 57.854 67.346  1 10.51  ? 554 HOH   B O    1 ? 
HETATM 4258 O  O    . HOH   G 4 .   ? 30.562 12.073 91.851  1 20.04  ? 555 HOH   B O    1 ? 
HETATM 4259 O  O    . HOH   G 4 .   ? 35.646 55.742 78.868  1 27.48  ? 556 HOH   B O    1 ? 
HETATM 4260 O  O    . HOH   G 4 .   ? 11.769 45.596 107.486 1 22.57  ? 557 HOH   B O    1 ? 
HETATM 4261 O  O    . HOH   G 4 .   ? 38.57  53.286 78.987  1 22.19  ? 558 HOH   B O    1 ? 
HETATM 4262 O  O    . HOH   G 4 .   ? 11.34  17.158 104.416 1 35.22  ? 559 HOH   B O    1 ? 
HETATM 4263 O  O    . HOH   G 4 .   ? 27.411 58.199 83.544  1 17.55  ? 560 HOH   B O    1 ? 
HETATM 4264 O  O    . HOH   G 4 .   ? 16.438 12.817 109.734 1 31.93  ? 561 HOH   B O    1 ? 
HETATM 4265 O  O    . HOH   G 4 .   ? 4.915  9.432  64.353  1 30.61  ? 562 HOH   B O    1 ? 
HETATM 4266 O  O    . HOH   G 4 .   ? -0.38  5.843  63.756  1 61.45  ? 563 HOH   B O    1 ? 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N    . GLY   A 2   ? 2.2481 1.5655 1.2613 0.8736  -0.4056 0.7008  1   GLY   A N    
2    C  CA   . GLY   A 2   ? 2.3195 1.4878 1.2863 0.8461  -0.3818 0.7083  1   GLY   A CA   
3    C  C    . GLY   A 2   ? 2.3341 1.4644 1.3246 0.7728  -0.3728 0.667   1   GLY   A C    
4    O  O    . GLY   A 2   ? 2.3843 1.3907 1.349  0.7588  -0.3503 0.6569  1   GLY   A O    
5    N  N    . ASN   A 3   ? 2.2917 1.5286 1.3302 0.7256  -0.3897 0.6422  2   ASN   A N    
6    C  CA   . ASN   A 3   ? 2.3034 1.5203 1.3674 0.6581  -0.3834 0.6034  2   ASN   A CA   
7    C  C    . ASN   A 3   ? 2.3138 1.5094 1.401  0.6635  -0.3761 0.5674  2   ASN   A C    
8    O  O    . ASN   A 3   ? 2.3263 1.4802 1.4247 0.6143  -0.3669 0.5366  2   ASN   A O    
9    C  CB   . ASN   A 3   ? 2.2633 1.598  1.3674 0.6116  -0.4023 0.5895  2   ASN   A CB   
10   C  CG   . ASN   A 3   ? 2.294  1.6145 1.4223 0.5445  -0.3964 0.553   2   ASN   A CG   
11   O  OD1  . ASN   A 3   ? 2.3447 1.577  1.4496 0.5086  -0.381  0.5525  2   ASN   A OD1  
12   N  ND2  . ASN   A 3   ? 2.2544 1.6621 1.4293 0.5273  -0.4076 0.5221  2   ASN   A ND2  
13   N  N    . ILE   A 4   ? 2.3063 1.5324 1.3997 0.7239  -0.38   0.5711  3   ILE   A N    
14   C  CA   . ILE   A 4   ? 2.3159 1.5265 1.4291 0.7359  -0.3731 0.5385  3   ILE   A CA   
15   C  C    . ILE   A 4   ? 2.3921 1.4451 1.4627 0.7376  -0.3466 0.5325  3   ILE   A C    
16   O  O    . ILE   A 4   ? 2.3995 1.4218 1.4839 0.7228  -0.3383 0.4976  3   ILE   A O    
17   C  CB   . ILE   A 4   ? 2.2848 1.585  1.419  0.8008  -0.3849 0.5447  3   ILE   A CB   
18   C  CG1  . ILE   A 4   ? 2.2317 1.6832 1.4015 0.798   -0.41   0.5542  3   ILE   A CG1  
19   C  CG2  . ILE   A 4   ? 2.2793 1.588  1.4424 0.8053  -0.3801 0.5069  3   ILE   A CG2  
20   C  CD1  . ILE   A 4   ? 2.2456 1.7274 1.39   0.8505  -0.4187 0.5978  3   ILE   A CD1  
21   N  N    . ILE   A 5   ? 2.4476 1.4003 1.465  0.7519  -0.3328 0.5655  4   ILE   A N    
22   C  CA   . ILE   A 5   ? 2.5249 1.3193 1.4949 0.7501  -0.3055 0.5635  4   ILE   A CA   
23   C  C    . ILE   A 5   ? 2.5279 1.2753 1.5087 0.6723  -0.2959 0.528   4   ILE   A C    
24   O  O    . ILE   A 5   ? 2.5548 1.2284 1.5298 0.6617  -0.2811 0.4987  4   ILE   A O    
25   C  CB   . ILE   A 5   ? 2.5842 1.2937 1.4948 0.7777  -0.2937 0.6109  4   ILE   A CB   
26   C  CG1  . ILE   A 5   ? 2.5913 1.3467 1.4883 0.8614  -0.3027 0.6469  4   ILE   A CG1  
27   C  CG2  . ILE   A 5   ? 2.6693 1.2073 1.5275 0.765   -0.2627 0.6086  4   ILE   A CG2  
28   C  CD1  . ILE   A 5   ? 2.6547 1.3378 1.491  0.8957  -0.293  0.6983  4   ILE   A CD1  
29   N  N    . LEU   A 6   ? 2.4941 1.2904 1.491  0.6192  -0.305  0.5299  5   LEU   A N    
30   C  CA   . LEU   A 6   ? 2.4894 1.2604 1.4999 0.5453  -0.2984 0.4997  5   LEU   A CA   
31   C  C    . LEU   A 6   ? 2.431  1.2815 1.4943 0.5205  -0.3095 0.4554  5   LEU   A C    
32   O  O    . LEU   A 6   ? 2.4425 1.2531 1.513  0.4739  -0.3003 0.4236  5   LEU   A O    
33   C  CB   . LEU   A 6   ? 2.4782 1.2899 1.4906 0.5033  -0.3056 0.5179  5   LEU   A CB   
34   C  CG   . LEU   A 6   ? 2.5305 1.2889 1.4937 0.5281  -0.2986 0.5656  5   LEU   A CG   
35   C  CD1  . LEU   A 6   ? 2.4943 1.3677 1.4711 0.5615  -0.3215 0.5928  5   LEU   A CD1  
36   C  CD2  . LEU   A 6   ? 2.5649 1.2647 1.5079 0.4691  -0.2854 0.5706  5   LEU   A CD2  
37   N  N    . ASP   A 7   ? 2.3658 1.3305 1.4648 0.5513  -0.3287 0.4538  6   ASP   A N    
38   C  CA   . ASP   A 7   ? 2.3134 1.3605 1.4607 0.5325  -0.3392 0.4162  6   ASP   A CA   
39   C  C    . ASP   A 7   ? 2.3176 1.3108 1.4635 0.5492  -0.3276 0.3868  6   ASP   A C    
40   O  O    . ASP   A 7   ? 2.2926 1.3313 1.4719 0.5225  -0.332  0.352   6   ASP   A O    
41   C  CB   . ASP   A 7   ? 2.2784 1.4612 1.4614 0.5587  -0.3611 0.4246  6   ASP   A CB   
42   C  CG   . ASP   A 7   ? 2.305  1.5672 1.5069 0.5181  -0.375  0.4322  6   ASP   A CG   
43   O  OD1  . ASP   A 7   ? 2.2959 1.5857 1.5229 0.4666  -0.3769 0.4054  6   ASP   A OD1  
44   O  OD2  . ASP   A 7   ? 2.3256 1.6231 1.5154 0.5394  -0.3838 0.4648  6   ASP   A OD2  
45   N  N    . LEU   A 8   ? 2.3484 1.2434 1.4536 0.594   -0.3119 0.4     7   LEU   A N    
46   C  CA   . LEU   A 8   ? 2.3598 1.1967 1.4593 0.6107  -0.2992 0.3704  7   LEU   A CA   
47   C  C    . LEU   A 8   ? 2.3819 1.1334 1.4709 0.5522  -0.2842 0.3376  7   LEU   A C    
48   O  O    . LEU   A 8   ? 2.3896 1.1163 1.4836 0.5517  -0.2774 0.3042  7   LEU   A O    
49   C  CB   . LEU   A 8   ? 2.3975 1.1573 1.456  0.6805  -0.2861 0.3923  7   LEU   A CB   
50   C  CG   . LEU   A 8   ? 2.4032 1.1717 1.4733 0.7198  -0.2829 0.3668  7   LEU   A CG   
51   C  CD1  . LEU   A 8   ? 2.3712 1.2343 1.4588 0.7859  -0.2963 0.3889  7   LEU   A CD1  
52   C  CD2  . LEU   A 8   ? 2.4769 1.0959 1.4973 0.7363  -0.2569 0.3574  7   LEU   A CD2  
53   N  N    . LEU   A 9   ? 2.385  1.1008 1.4616 0.5017  -0.2796 0.3456  8   LEU   A N    
54   C  CA   . LEU   A 9   ? 2.3993 1.0515 1.4708 0.4397  -0.2672 0.3153  8   LEU   A CA   
55   C  C    . LEU   A 9   ? 2.3341 1.0861 1.4569 0.4021  -0.2818 0.2783  8   LEU   A C    
56   O  O    . LEU   A 9   ? 2.344  1.0636 1.4704 0.3735  -0.2743 0.2419  8   LEU   A O    
57   C  CB   . LEU   A 9   ? 2.4236 1.0362 1.4744 0.3985  -0.2608 0.3379  8   LEU   A CB   
58   C  CG   . LEU   A 9   ? 2.4966 0.9846 1.5127 0.3551  -0.2372 0.3243  8   LEU   A CG   
59   C  CD1  . LEU   A 9   ? 2.5378 0.9629 1.5164 0.3434  -0.2259 0.3622  8   LEU   A CD1  
60   C  CD2  . LEU   A 9   ? 2.4818 1.0056 1.5304 0.2898  -0.2401 0.2836  8   LEU   A CD2  
61   N  N    . LEU   A 10  ? 2.2673 1.139  1.4267 0.4025  -0.3018 0.2879  9   LEU   A N    
62   C  CA   . LEU   A 10  ? 2.2114 1.1811 1.4166 0.3726  -0.3153 0.2584  9   LEU   A CA   
63   C  C    . LEU   A 10  ? 2.1832 1.1824 1.405  0.4071  -0.3177 0.2347  9   LEU   A C    
64   O  O    . LEU   A 10  ? 2.1691 1.1936 1.4122 0.3806  -0.319  0.2002  9   LEU   A O    
65   C  CB   . LEU   A 10  ? 2.1694 1.249  1.4023 0.3685  -0.3336 0.2782  9   LEU   A CB   
66   C  CG   . LEU   A 10  ? 2.1979 1.2634 1.4157 0.339   -0.3329 0.3041  9   LEU   A CG   
67   C  CD1  . LEU   A 10  ? 2.1642 1.3315 1.4015 0.3501  -0.3505 0.3271  9   LEU   A CD1  
68   C  CD2  . LEU   A 10  ? 2.2082 1.2599 1.4341 0.2759  -0.3277 0.2811  9   LEU   A CD2  
69   N  N    . LEU   A 11  ? 2.1721 1.172  1.3837 0.4675  -0.3181 0.2537  10  LEU   A N    
70   C  CA   . LEU   A 11  ? 2.1502 1.1795 1.3759 0.5067  -0.3189 0.2347  10  LEU   A CA   
71   C  C    . LEU   A 11  ? 2.1803 1.1105 1.3821 0.5018  -0.3015 0.2039  10  LEU   A C    
72   O  O    . LEU   A 11  ? 2.1652 1.1276 1.3862 0.5035  -0.3028 0.173   10  LEU   A O    
73   C  CB   . LEU   A 11  ? 2.1491 1.1975 1.3659 0.5746  -0.3218 0.2654  10  LEU   A CB   
74   C  CG   . LEU   A 11  ? 2.1107 1.2872 1.3691 0.6018  -0.3376 0.2633  10  LEU   A CG   
75   C  CD1  . LEU   A 11  ? 2.11   1.3188 1.3611 0.6616  -0.3431 0.2994  10  LEU   A CD1  
76   C  CD2  . LEU   A 11  ? 2.11   1.2952 1.3826 0.6143  -0.3327 0.2283  10  LEU   A CD2  
77   N  N    . LEU   A 12  ? 2.2215 1.0309 1.3799 0.4939  -0.2845 0.2115  11  LEU   A N    
78   C  CA   . LEU   A 12  ? 2.2573 0.9643 1.3885 0.4842  -0.2663 0.1806  11  LEU   A CA   
79   C  C    . LEU   A 12  ? 2.2371 0.9602 1.3884 0.4185  -0.2681 0.1425  11  LEU   A C    
80   O  O    . LEU   A 12  ? 2.2481 0.9442 1.3969 0.4123  -0.2615 0.1067  11  LEU   A O    
81   C  CB   . LEU   A 12  ? 2.3238 0.8918 1.3995 0.4928  -0.2454 0.2001  11  LEU   A CB   
82   C  CG   . LEU   A 12  ? 2.3617 0.8962 1.409  0.5661  -0.24   0.2351  11  LEU   A CG   
83   C  CD1  . LEU   A 12  ? 2.4315 0.8333 1.4227 0.5689  -0.2197 0.2609  11  LEU   A CD1  
84   C  CD2  . LEU   A 12  ? 2.3729 0.899  1.4177 0.616   -0.2346 0.2154  11  LEU   A CD2  
85   N  N    . LEU   A 13  ? 2.2037 0.9771 1.3749 0.3719  -0.2775 0.1497  12  LEU   A N    
86   C  CA   . LEU   A 13  ? 2.1839 0.9849 1.3763 0.3118  -0.2805 0.1168  12  LEU   A CA   
87   C  C    . LEU   A 13  ? 2.1211 1.0338 1.3561 0.3131  -0.2958 0.094   12  LEU   A C    
88   O  O    . LEU   A 13  ? 2.1141 1.0379 1.3606 0.2793  -0.2958 0.0593  12  LEU   A O    
89   C  CB   . LEU   A 13  ? 2.1841 0.9963 1.3804 0.2644  -0.283  0.1333  12  LEU   A CB   
90   C  CG   . LEU   A 13  ? 2.2408 0.966  1.4142 0.2123  -0.2674 0.1161  12  LEU   A CG   
91   C  CD1  . LEU   A 13  ? 2.2527 0.9711 1.4196 0.1798  -0.2658 0.1436  12  LEU   A CD1  
92   C  CD2  . LEU   A 13  ? 2.2283 0.9897 1.4252 0.1713  -0.2708 0.0716  12  LEU   A CD2  
93   N  N    . THR   A 14  ? 2.0738 1.069  1.3307 0.3519  -0.3082 0.1129  13  THR   A N    
94   C  CA   . THR   A 14  ? 2.0215 1.118  1.3157 0.3552  -0.3203 0.0934  13  THR   A CA   
95   C  C    . THR   A 14  ? 2.0218 1.0943 1.3096 0.3852  -0.3131 0.0661  13  THR   A C    
96   O  O    . THR   A 14  ? 2.0007 1.1205 1.3085 0.3701  -0.317  0.0367  13  THR   A O    
97   C  CB   . THR   A 14  ? 1.9963 1.1904 1.3162 0.3789  -0.3346 0.1203  13  THR   A CB   
98   O  OG1  . THR   A 14  ? 2.0249 1.1938 1.3272 0.4317  -0.3318 0.1474  13  THR   A OG1  
99   C  CG2  . THR   A 14  ? 1.983  1.2159 1.3135 0.3414  -0.3428 0.1383  13  THR   A CG2  
100  N  N    . ILE   A 15  ? 2.0456 1.0428 1.303  0.429   -0.3017 0.076   14  ILE   A N    
101  C  CA   . ILE   A 15  ? 2.0582 1.0188 1.3034 0.4585  -0.292  0.0491  14  ILE   A CA   
102  C  C    . ILE   A 15  ? 2.0857 0.9609 1.3077 0.4163  -0.2798 0.0135  14  ILE   A C    
103  O  O    . ILE   A 15  ? 2.086  0.9604 1.3086 0.4183  -0.2763 -0.0205 14  ILE   A O    
104  C  CB   . ILE   A 15  ? 2.0928 1.0027 1.3117 0.5235  -0.2829 0.0718  14  ILE   A CB   
105  C  CG1  . ILE   A 15  ? 2.0656 1.0701 1.3095 0.5601  -0.2967 0.1069  14  ILE   A CG1  
106  C  CG2  . ILE   A 15  ? 2.1134 0.9951 1.3215 0.5577  -0.2728 0.0432  14  ILE   A CG2  
107  C  CD1  . ILE   A 15  ? 2.1055 1.0673 1.3233 0.6258  -0.2891 0.1353  14  ILE   A CD1  
108  N  N    . ILE   A 16  ? 2.1036 0.9139 1.3064 0.3755  -0.2735 0.0206  15  ILE   A N    
109  C  CA   . ILE   A 16  ? 2.1301 0.869  1.3142 0.3257  -0.2628 -0.0112 15  ILE   A CA   
110  C  C    . ILE   A 16  ? 2.0859 0.9136 1.3056 0.2838  -0.2754 -0.0416 15  ILE   A C    
111  O  O    . ILE   A 16  ? 2.0966 0.9015 1.3098 0.2636  -0.2705 -0.0796 15  ILE   A O    
112  C  CB   . ILE   A 16  ? 2.1684 0.8281 1.3263 0.2946  -0.2529 0.0106  15  ILE   A CB   
113  C  CG1  . ILE   A 16  ? 2.2418 0.7633 1.3476 0.3182  -0.2307 0.0137  15  ILE   A CG1  
114  C  CG2  . ILE   A 16  ? 2.1672 0.8356 1.3359 0.2238  -0.2541 -0.0104 15  ILE   A CG2  
115  C  CD1  . ILE   A 16  ? 2.2938 0.7355 1.3691 0.3035  -0.2192 0.044   15  ILE   A CD1  
116  N  N    . TYR   A 17  ? 2.0351 0.9642 1.29   0.2736  -0.2913 -0.025  16  TYR   A N    
117  C  CA   . TYR   A 17  ? 1.995  1.0118 1.2821 0.2407  -0.3028 -0.0485 16  TYR   A CA   
118  C  C    . TYR   A 17  ? 1.9725 1.0448 1.2743 0.2736  -0.3073 -0.068  16  TYR   A C    
119  O  O    . TYR   A 17  ? 1.9597 1.0615 1.2708 0.2518  -0.3098 -0.1    16  TYR   A O    
120  C  CB   . TYR   A 17  ? 1.9561 1.0553 1.2712 0.2239  -0.3158 -0.0226 16  TYR   A CB   
121  C  CG   . TYR   A 17  ? 1.9285 1.1026 1.2703 0.1841  -0.325  -0.0437 16  TYR   A CG   
122  C  CD1  . TYR   A 17  ? 1.9009 1.1636 1.2687 0.1983  -0.3347 -0.0526 16  TYR   A CD1  
123  C  CD2  . TYR   A 17  ? 1.9433 1.1016 1.2837 0.1336  -0.3231 -0.0533 16  TYR   A CD2  
124  C  CE1  . TYR   A 17  ? 1.8819 1.2103 1.2704 0.1661  -0.342  -0.0693 16  TYR   A CE1  
125  C  CE2  . TYR   A 17  ? 1.9213 1.1523 1.2856 0.1017  -0.3315 -0.0709 16  TYR   A CE2  
126  C  CZ   . TYR   A 17  ? 1.8963 1.21   1.2831 0.1196  -0.3409 -0.0782 16  TYR   A CZ   
127  O  OH   . TYR   A 17  ? 1.8824 1.2644 1.2889 0.0923  -0.348  -0.0935 16  TYR   A OH   
128  N  N    . SER   A 18  ? 1.9657 1.0557 1.2695 0.326   -0.308  -0.0485 17  SER   A N    
129  C  CA   . SER   A 18  ? 1.9484 1.0934 1.2663 0.3611  -0.3106 -0.0631 17  SER   A CA   
130  C  C    . SER   A 18  ? 1.9695 1.0658 1.2684 0.3607  -0.301  -0.1036 17  SER   A C    
131  O  O    . SER   A 18  ? 1.9442 1.1013 1.26   0.3541  -0.3062 -0.1278 17  SER   A O    
132  C  CB   . SER   A 18  ? 1.9656 1.1216 1.2831 0.4188  -0.3098 -0.0349 17  SER   A CB   
133  O  OG   . SER   A 18  ? 1.9725 1.1836 1.3083 0.4184  -0.3201 0       17  SER   A OG   
134  N  N    . TYR   A 19  ? 2.0146 1.0001 1.2759 0.3671  -0.2863 -0.1114 18  TYR   A N    
135  C  CA   . TYR   A 19  ? 2.0426 0.9746 1.2815 0.3642  -0.2762 -0.1523 18  TYR   A CA   
136  C  C    . TYR   A 19  ? 2.0414 0.9736 1.2824 0.3021  -0.2789 -0.183  18  TYR   A C    
137  O  O    . TYR   A 19  ? 2.0364 0.989  1.2782 0.2929  -0.2796 -0.2186 18  TYR   A O    
138  C  CB   . TYR   A 19  ? 2.101  0.9079 1.2952 0.3909  -0.2575 -0.1514 18  TYR   A CB   
139  C  CG   . TYR   A 19  ? 2.1304 0.9068 1.3057 0.4267  -0.2474 -0.1805 18  TYR   A CG   
140  C  CD1  . TYR   A 19  ? 2.1498 0.9143 1.3163 0.3974  -0.2447 -0.2257 18  TYR   A CD1  
141  C  CD2  . TYR   A 19  ? 2.1525 0.9119 1.3168 0.4908  -0.2401 -0.1632 18  TYR   A CD2  
142  C  CE1  . TYR   A 19  ? 2.178  0.9129 1.3244 0.4301  -0.2347 -0.2537 18  TYR   A CE1  
143  C  CE2  . TYR   A 19  ? 2.181  0.9104 1.3261 0.5255  -0.2293 -0.1901 18  TYR   A CE2  
144  C  CZ   . TYR   A 19  ? 2.2002 0.9153 1.3355 0.4945  -0.2264 -0.2358 18  TYR   A CZ   
145  O  OH   . TYR   A 19  ? 2.2353 0.9207 1.3494 0.5291  -0.2152 -0.2634 18  TYR   A OH   
146  N  N    . LEU   A 20  ? 2.0408 0.9569 1.2833 0.2608  -0.2806 -0.1688 19  LEU   A N    
147  C  CA   . LEU   A 20  ? 2.0372 0.9601 1.2845 0.2001  -0.2834 -0.1935 19  LEU   A CA   
148  C  C    . LEU   A 20  ? 1.9838 1.0231 1.2667 0.1844  -0.299  -0.2074 19  LEU   A C    
149  O  O    . LEU   A 20  ? 1.9801 1.0325 1.2627 0.1549  -0.3005 -0.2428 19  LEU   A O    
150  C  CB   . LEU   A 20  ? 2.0511 0.9443 1.2962 0.1677  -0.2818 -0.1667 19  LEU   A CB   
151  C  CG   . LEU   A 20  ? 2.0615 0.9721 1.316  0.1048  -0.2848 -0.1857 19  LEU   A CG   
152  C  CD1  . LEU   A 20  ? 2.1047 0.9374 1.3312 0.075   -0.2725 -0.2259 19  LEU   A CD1  
153  C  CD2  . LEU   A 20  ? 2.073  0.9696 1.3293 0.0802  -0.2837 -0.1533 19  LEU   A CD2  
154  N  N    . GLU   A 21  ? 1.9412 1.0633 1.2523 0.2044  -0.3099 -0.1796 20  GLU   A N    
155  C  CA   . GLU   A 21  ? 1.8962 1.1243 1.2381 0.1948  -0.3227 -0.186  20  GLU   A CA   
156  C  C    . GLU   A 21  ? 1.8803 1.1386 1.2222 0.223   -0.3224 -0.2113 20  GLU   A C    
157  O  O    . GLU   A 21  ? 1.8613 1.1659 1.2109 0.2032  -0.3275 -0.2374 20  GLU   A O    
158  C  CB   . GLU   A 21  ? 1.8974 1.1903 1.2636 0.208   -0.3313 -0.1474 20  GLU   A CB   
159  C  CG   . GLU   A 21  ? 1.9174 1.3134 1.3114 0.2143  -0.3412 -0.1481 20  GLU   A CG   
160  C  CD   . GLU   A 21  ? 1.9772 1.4175 1.385  0.2549  -0.3439 -0.121  20  GLU   A CD   
161  O  OE1  . GLU   A 21  ? 1.9614 1.4821 1.3919 0.2528  -0.3512 -0.1121 20  GLU   A OE1  
162  O  OE2  . GLU   A 21  ? 2.0203 1.4155 1.4153 0.2889  -0.338  -0.1088 20  GLU   A OE2  
163  N  N    . ALA   A 22  ? 1.886  1.1197 1.2182 0.2708  -0.316  -0.2033 21  ALA   A N    
164  C  CA   . ALA   A 22  ? 1.8796 1.1377 1.2096 0.3015  -0.3134 -0.2264 21  ALA   A CA   
165  C  C    . ALA   A 22  ? 1.9063 1.1021 1.2082 0.2863  -0.3053 -0.269  21  ALA   A C    
166  O  O    . ALA   A 22  ? 1.8969 1.1236 1.1971 0.2995  -0.3051 -0.2948 21  ALA   A O    
167  C  CB   . ALA   A 22  ? 1.8861 1.1353 1.2134 0.3571  -0.3077 -0.206  21  ALA   A CB   
168  N  N    . LEU   A 23  ? 1.9374 1.0456 1.2156 0.2574  -0.2979 -0.2769 22  LEU   A N    
169  C  CA   . LEU   A 23  ? 1.9669 1.0123 1.217  0.2339  -0.2899 -0.3191 22  LEU   A CA   
170  C  C    . LEU   A 23  ? 1.9367 1.0489 1.2029 0.1882  -0.3009 -0.3445 22  LEU   A C    
171  O  O    . LEU   A 23  ? 1.9398 1.0571 1.1947 0.1822  -0.3002 -0.3817 22  LEU   A O    
172  C  CB   . LEU   A 23  ? 2.0182 0.9482 1.2375 0.2133  -0.2768 -0.3176 22  LEU   A CB   
173  C  CG   . LEU   A 23  ? 2.0854 0.9115 1.2649 0.2464  -0.2592 -0.3306 22  LEU   A CG   
174  C  CD1  . LEU   A 23  ? 2.1375 0.8546 1.2889 0.241   -0.2455 -0.31   22  LEU   A CD1  
175  C  CD2  . LEU   A 23  ? 2.1123 0.909  1.2693 0.226   -0.2538 -0.3821 22  LEU   A CD2  
176  N  N    . VAL   A 24  ? 1.9045 1.0705 1.1959 0.1584  -0.311  -0.3244 23  VAL   A N    
177  C  CA   . VAL   A 24  ? 1.8736 1.1118 1.1823 0.1193  -0.3219 -0.3438 23  VAL   A CA   
178  C  C    . VAL   A 24  ? 1.83   1.161  1.1559 0.145   -0.3304 -0.3485 23  VAL   A C    
179  O  O    . VAL   A 24  ? 1.819  1.1882 1.1432 0.1301  -0.3351 -0.3797 23  VAL   A O    
180  C  CB   . VAL   A 24  ? 1.8685 1.1355 1.1976 0.0852  -0.3283 -0.3187 23  VAL   A CB   
181  C  CG1  . VAL   A 24  ? 1.8419 1.1936 1.1904 0.0528  -0.3397 -0.3358 23  VAL   A CG1  
182  C  CG2  . VAL   A 24  ? 1.9126 1.0873 1.2222 0.0552  -0.3182 -0.3166 23  VAL   A CG2  
183  N  N    . LYS   A 25  ? 1.8036 1.1694 1.1439 0.1844  -0.3315 -0.3182 24  LYS   A N    
184  C  CA   . LYS   A 25  ? 1.766  1.214  1.1211 0.2112  -0.3365 -0.3182 24  LYS   A CA   
185  C  C    . LYS   A 25  ? 1.7691 1.2056 1.1046 0.2331  -0.3308 -0.3524 24  LYS   A C    
186  O  O    . LYS   A 25  ? 1.7467 1.2506 1.0906 0.2501  -0.3339 -0.358  24  LYS   A O    
187  C  CB   . LYS   A 25  ? 1.77   1.2452 1.1416 0.2476  -0.3361 -0.2805 24  LYS   A CB   
188  C  CG   . LYS   A 25  ? 1.7886 1.3049 1.183  0.2301  -0.3436 -0.2474 24  LYS   A CG   
189  C  CD   . LYS   A 25  ? 1.8138 1.3596 1.223  0.2652  -0.3433 -0.2143 24  LYS   A CD   
190  C  CE   . LYS   A 25  ? 1.8272 1.4209 1.2574 0.2474  -0.3507 -0.1848 24  LYS   A CE   
191  N  NZ   . LYS   A 25  ? 1.8324 1.4604 1.2771 0.2781  -0.3511 -0.1553 24  LYS   A NZ   
192  N  N    . VAL   A 26  ? 1.7958 1.1443 1.1028 0.2344  -0.321  -0.3741 25  VAL   A N    
193  C  CA   . VAL   A 26  ? 1.8045 1.1323 1.0885 0.2554  -0.314  -0.4081 25  VAL   A CA   
194  C  C    . VAL   A 26  ? 1.8232 1.1052 1.0829 0.2162  -0.3124 -0.451  25  VAL   A C    
195  O  O    . VAL   A 26  ? 1.8133 1.1374 1.0674 0.2105  -0.3165 -0.4818 25  VAL   A O    
196  C  CB   . VAL   A 26  ? 1.8351 1.103  1.1038 0.3036  -0.3013 -0.3972 25  VAL   A CB   
197  C  CG1  . VAL   A 26  ? 1.8628 1.096  1.1025 0.3239  -0.2919 -0.4353 25  VAL   A CG1  
198  C  CG2  . VAL   A 26  ? 1.8084 1.1427 1.104  0.3418  -0.3041 -0.3608 25  VAL   A CG2  
199  N  N    . PHE   A 27  ? 1.8467 1.0454 1.0911 0.1877  -0.3062 -0.453  26  PHE   A N    
200  C  CA   . PHE   A 27  ? 1.8674 1.0143 1.0882 0.1436  -0.3029 -0.4935 26  PHE   A CA   
201  C  C    . PHE   A 27  ? 1.8173 1.0504 1.0571 0.1015  -0.3175 -0.5111 26  PHE   A C    
202  O  O    . PHE   A 27  ? 1.8101 1.0698 1.0386 0.0923  -0.3208 -0.5488 26  PHE   A O    
203  C  CB   . PHE   A 27  ? 1.9118 0.9555 1.1154 0.1205  -0.2919 -0.4834 26  PHE   A CB   
204  C  CG   . PHE   A 27  ? 1.9705 0.9188 1.1361 0.0915  -0.2795 -0.5243 26  PHE   A CG   
205  C  CD1  . PHE   A 27  ? 2.0155 0.9019 1.1479 0.1216  -0.2673 -0.5497 26  PHE   A CD1  
206  C  CD2  . PHE   A 27  ? 1.9954 0.911  1.1567 0.0338  -0.2781 -0.5368 26  PHE   A CD2  
207  C  CE1  . PHE   A 27  ? 2.0705 0.8621 1.1641 0.0929  -0.2542 -0.5892 26  PHE   A CE1  
208  C  CE2  . PHE   A 27  ? 2.0488 0.873  1.1734 0.0029  -0.2651 -0.5761 26  PHE   A CE2  
209  C  CZ   . PHE   A 27  ? 2.0802 0.8401 1.1699 0.0322  -0.2531 -0.6024 26  PHE   A CZ   
210  N  N    . PHE   A 28  ? 1.7788 1.0598 1.0465 0.0796  -0.3263 -0.4832 27  PHE   A N    
211  C  CA   . PHE   A 28  ? 1.7347 1.1038 1.0226 0.0463  -0.3399 -0.4937 27  PHE   A CA   
212  C  C    . PHE   A 28  ? 1.678  1.1311 0.9958 0.0698  -0.3486 -0.4559 27  PHE   A C    
213  O  O    . PHE   A 28  ? 1.6693 1.132  1.0054 0.0568  -0.3511 -0.4256 27  PHE   A O    
214  C  CB   . PHE   A 28  ? 1.7454 1.0882 1.036  -0.0083 -0.3401 -0.4989 27  PHE   A CB   
215  C  CG   . PHE   A 28  ? 1.7917 1.0667 1.0537 -0.0425 -0.3325 -0.5431 27  PHE   A CG   
216  C  CD1  . PHE   A 28  ? 1.7919 1.1109 1.046  -0.0582 -0.3391 -0.5862 27  PHE   A CD1  
217  C  CD2  . PHE   A 28  ? 1.8465 1.0133 1.0872 -0.0606 -0.3182 -0.5421 27  PHE   A CD2  
218  C  CE1  . PHE   A 28  ? 1.8306 1.0881 1.0572 -0.0936 -0.332  -0.6298 27  PHE   A CE1  
219  C  CE2  . PHE   A 28  ? 1.889  0.988  1.1006 -0.096  -0.3092 -0.5846 27  PHE   A CE2  
220  C  CZ   . PHE   A 28  ? 1.8721 1.0179 1.0775 -0.1137 -0.3165 -0.6294 27  PHE   A CZ   
221  N  N    . PRO   A 29  ? 1.6394 1.1478 0.9602 0.1058  -0.3513 -0.4562 28  PRO   A N    
222  C  CA   . PRO   A 29  ? 1.5909 1.1706 0.937  0.1275  -0.3567 -0.4204 28  PRO   A CA   
223  C  C    . PRO   A 29  ? 1.5348 1.2049 0.8975 0.1084  -0.368  -0.421  28  PRO   A C    
224  O  O    . PRO   A 29  ? 1.5263 1.2292 0.8803 0.0949  -0.3731 -0.4526 28  PRO   A O    
225  C  CB   . PRO   A 29  ? 1.6016 1.1908 0.9406 0.1748  -0.3511 -0.4201 28  PRO   A CB   
226  C  CG   . PRO   A 29  ? 1.6316 1.188  0.9427 0.174   -0.3472 -0.4643 28  PRO   A CG   
227  C  CD   . PRO   A 29  ? 1.6378 1.1434 0.9371 0.1279  -0.3478 -0.4888 28  PRO   A CD   
228  N  N    . ARG   A 30  ? 1.4935 1.2048 0.8783 0.1094  -0.3717 -0.3858 29  ARG   A N    
229  C  CA   . ARG   A 30  ? 1.4465 1.2394 0.8458 0.0968  -0.3803 -0.38   29  ARG   A CA   
230  C  C    . ARG   A 30  ? 1.4061 1.2596 0.7995 0.1241  -0.3818 -0.39   29  ARG   A C    
231  O  O    . ARG   A 30  ? 1.4144 1.2555 0.8002 0.1565  -0.3754 -0.3885 29  ARG   A O    
232  C  CB   . ARG   A 30  ? 1.4495 1.26   0.8691 0.0971  -0.3809 -0.3388 29  ARG   A CB   
233  C  CG   . ARG   A 30  ? 1.457  1.3286 0.8901 0.0735  -0.3881 -0.3316 29  ARG   A CG   
234  C  CD   . ARG   A 30  ? 1.4834 1.3465 0.932  0.0614  -0.3875 -0.2979 29  ARG   A CD   
235  N  NE   . ARG   A 30  ? 1.4809 1.4045 0.941  0.0439  -0.3929 -0.2904 29  ARG   A NE   
236  C  CZ   . ARG   A 30  ? 1.4922 1.4172 0.9646 0.0263  -0.3931 -0.267  29  ARG   A CZ   
237  N  NH1  . ARG   A 30  ? 1.5042 1.3741 0.9784 0.0226  -0.3889 -0.248  29  ARG   A NH1  
238  N  NH2  . ARG   A 30  ? 1.4658 1.4477 0.9468 0.0144  -0.397  -0.262  29  ARG   A NH2  
239  N  N    . LYS   A 31  ? 1.3602 1.28   0.7557 0.1128  -0.3893 -0.3994 30  LYS   A N    
240  C  CA   . LYS   A 31  ? 1.3276 1.3051 0.7137 0.1381  -0.39   -0.4075 30  LYS   A CA   
241  C  C    . LYS   A 31  ? 1.2869 1.2973 0.6826 0.1659  -0.3848 -0.3719 30  LYS   A C    
242  O  O    . LYS   A 31  ? 1.2728 1.3117 0.6821 0.1571  -0.3868 -0.3471 30  LYS   A O    
243  C  CB   . LYS   A 31  ? 1.3341 1.3739 0.7174 0.119   -0.3998 -0.4271 30  LYS   A CB   
244  C  CG   . LYS   A 31  ? 1.376  1.4568 0.7389 0.1382  -0.4016 -0.4534 30  LYS   A CG   
245  C  CD   . LYS   A 31  ? 1.412  1.5582 0.7723 0.1191  -0.4128 -0.473  30  LYS   A CD   
246  C  CE   . LYS   A 31  ? 1.4602 1.6354 0.7965 0.1302  -0.4163 -0.5084 30  LYS   A CE   
247  N  NZ   . LYS   A 31  ? 1.4584 1.6985 0.7923 0.1091  -0.4289 -0.5317 30  LYS   A NZ   
248  N  N    . ARG   A 32  ? 1.2661 1.2722 0.6537 0.198   -0.3772 -0.3708 31  ARG   A N    
249  C  CA   . ARG   A 32  ? 1.2369 1.2744 0.632  0.2227  -0.3704 -0.3411 31  ARG   A CA   
250  C  C    . ARG   A 32  ? 1.2002 1.3024 0.5845 0.2332  -0.3704 -0.3436 31  ARG   A C    
251  O  O    . ARG   A 32  ? 1.2048 1.3225 0.571  0.2433  -0.371  -0.3697 31  ARG   A O    
252  C  CB   . ARG   A 32  ? 1.2629 1.2728 0.655  0.2523  -0.3611 -0.3398 31  ARG   A CB   
253  C  CG   . ARG   A 32  ? 1.3219 1.284  0.7283 0.2534  -0.3584 -0.319  31  ARG   A CG   
254  C  CD   . ARG   A 32  ? 1.3629 1.353  0.7841 0.2719  -0.3521 -0.2866 31  ARG   A CD   
255  N  NE   . ARG   A 32  ? 1.4036 1.4223 0.818  0.3022  -0.3433 -0.2914 31  ARG   A NE   
256  C  CZ   . ARG   A 32  ? 1.4332 1.4628 0.8587 0.3242  -0.3355 -0.2725 31  ARG   A CZ   
257  N  NH1  . ARG   A 32  ? 1.426  1.4413 0.8692 0.3206  -0.3365 -0.2476 31  ARG   A NH1  
258  N  NH2  . ARG   A 32  ? 1.4312 1.4901 0.8502 0.3496  -0.3265 -0.2786 31  ARG   A NH2  
259  N  N    . LYS   A 33  ? 1.1639 1.3014 0.5562 0.2322  -0.3688 -0.3165 32  LYS   A N    
260  C  CA   . LYS   A 33  ? 1.1335 1.3271 0.5123 0.2448  -0.3666 -0.3139 32  LYS   A CA   
261  C  C    . LYS   A 33  ? 1.1159 1.3241 0.4907 0.2717  -0.3533 -0.2942 32  LYS   A C    
262  O  O    . LYS   A 33  ? 1.1227 1.3042 0.5087 0.2796  -0.3474 -0.2835 32  LYS   A O    
263  C  CB   . LYS   A 33  ? 1.1374 1.3592 0.5224 0.227   -0.3716 -0.2982 32  LYS   A CB   
264  C  CG   . LYS   A 33  ? 1.173  1.3876 0.5721 0.2248  -0.3649 -0.2627 32  LYS   A CG   
265  C  CD   . LYS   A 33  ? 1.198  1.4397 0.5996 0.2106  -0.368  -0.2485 32  LYS   A CD   
266  C  CE   . LYS   A 33  ? 1.2277 1.4628 0.6376 0.21    -0.3596 -0.2154 32  LYS   A CE   
267  N  NZ   . LYS   A 33  ? 1.2398 1.4922 0.6526 0.195   -0.3623 -0.2026 32  LYS   A NZ   
268  N  N    . SER   A 34  ? 1.0912 1.3431 0.449  0.2861  -0.3479 -0.2894 33  SER   A N    
269  C  CA   . SER   A 34  ? 1.0789 1.346  0.4309 0.3075  -0.3331 -0.2706 33  SER   A CA   
270  C  C    . SER   A 34  ? 1.0582 1.3422 0.4119 0.3018  -0.3267 -0.2399 33  SER   A C    
271  O  O    . SER   A 34  ? 1.0583 1.3617 0.4042 0.2942  -0.3315 -0.2375 33  SER   A O    
272  C  CB   . SER   A 34  ? 1.0942 1.3913 0.4199 0.3303  -0.3278 -0.287  33  SER   A CB   
273  O  OG   . SER   A 34  ? 1.1178 1.4305 0.4365 0.3488  -0.3114 -0.2681 33  SER   A OG   
274  N  N    . VAL   A 35  ? 1.0383 1.3155 0.4017 0.3051  -0.3154 -0.2171 34  VAL   A N    
275  C  CA   . VAL   A 35  ? 1.0197 1.3073 0.381  0.2988  -0.3065 -0.1892 34  VAL   A CA   
276  C  C    . VAL   A 35  ? 1.0056 1.3139 0.3494 0.3167  -0.2882 -0.1776 34  VAL   A C    
277  O  O    . VAL   A 35  ? 1.0076 1.3153 0.3531 0.3109  -0.2765 -0.1545 34  VAL   A O    
278  C  CB   . VAL   A 35  ? 1.0203 1.2839 0.4062 0.2801  -0.3084 -0.1709 34  VAL   A CB   
279  C  CG1  . VAL   A 35  ? 1.0272 1.2735 0.4242 0.2599  -0.3233 -0.1767 34  VAL   A CG1  
280  C  CG2  . VAL   A 35  ? 1.0222 1.2716 0.4253 0.2868  -0.3061 -0.1717 34  VAL   A CG2  
281  N  N    . ALA   A 36  ? 0.9875 1.3134 0.3123 0.3369  -0.2848 -0.1945 35  ALA   A N    
282  C  CA   . ALA   A 36  ? 0.9749 1.3201 0.2803 0.3545  -0.2664 -0.1855 35  ALA   A CA   
283  C  C    . ALA   A 36  ? 0.9606 1.3214 0.2375 0.3592  -0.2579 -0.1711 35  ALA   A C    
284  O  O    . ALA   A 36  ? 0.9604 1.334  0.2227 0.3632  -0.2678 -0.1815 35  ALA   A O    
285  C  CB   . ALA   A 36  ? 0.9768 1.3339 0.2707 0.3752  -0.2661 -0.2096 35  ALA   A CB   
286  N  N    . GLY   A 37  ? 0.9486 1.3081 0.2168 0.3584  -0.239  -0.1473 36  GLY   A N    
287  C  CA   . GLY   A 37  ? 0.9517 1.3165 0.1882 0.3648  -0.226  -0.1294 36  GLY   A CA   
288  C  C    . GLY   A 37  ? 0.9467 1.298  0.1858 0.3496  -0.2314 -0.1156 36  GLY   A C    
289  O  O    . GLY   A 37  ? 0.962  1.3169 0.1725 0.3587  -0.2233 -0.1031 36  GLY   A O    
290  N  N    . GLU   A 38  ? 0.9214 1.2567 0.1925 0.3283  -0.2441 -0.1167 37  GLU   A N    
291  C  CA   . GLU   A 38  ? 0.9087 1.2318 0.184  0.3128  -0.2492 -0.1044 37  GLU   A CA   
292  C  C    . GLU   A 38  ? 0.8967 1.1997 0.1711 0.299   -0.2328 -0.0799 37  GLU   A C    
293  O  O    . GLU   A 38  ? 0.8969 1.1964 0.1825 0.2937  -0.2241 -0.0761 37  GLU   A O    
294  C  CB   . GLU   A 38  ? 0.9265 1.2409 0.2336 0.2956  -0.2702 -0.1176 37  GLU   A CB   
295  C  CG   . GLU   A 38  ? 0.9783 1.3098 0.2847 0.3023  -0.2868 -0.1431 37  GLU   A CG   
296  C  CD   . GLU   A 38  ? 1.0379 1.3822 0.34   0.2966  -0.2965 -0.1433 37  GLU   A CD   
297  O  OE1  . GLU   A 38  ? 1.046  1.4194 0.3316 0.3102  -0.3024 -0.1574 37  GLU   A OE1  
298  O  OE2  . GLU   A 38  ? 1.0408 1.3703 0.3557 0.2792  -0.298  -0.1296 37  GLU   A OE2  
299  N  N    . ILE   A 39  ? 0.8857 1.1771 0.1466 0.2926  -0.2281 -0.0642 38  ILE   A N    
300  C  CA   . ILE   A 39  ? 0.8848 1.1528 0.1421 0.2763  -0.2121 -0.0432 38  ILE   A CA   
301  C  C    . ILE   A 39  ? 0.872  1.1273 0.1623 0.2515  -0.2252 -0.0419 38  ILE   A C    
302  O  O    . ILE   A 39  ? 0.8759 1.1239 0.1693 0.243   -0.2336 -0.0385 38  ILE   A O    
303  C  CB   . ILE   A 39  ? 0.9055 1.1593 0.1243 0.2841  -0.1942 -0.0249 38  ILE   A CB   
304  C  CG1  . ILE   A 39  ? 0.9284 1.1916 0.1125 0.3093  -0.1787 -0.0234 38  ILE   A CG1  
305  C  CG2  . ILE   A 39  ? 0.923  1.1478 0.1386 0.2624  -0.1776 -0.0068 38  ILE   A CG2  
306  C  CD1  . ILE   A 39  ? 0.9681 1.2146 0.1079 0.3239  -0.1599 -0.0048 38  ILE   A CD1  
307  N  N    . VAL   A 40  ? 0.8481 1.1043 0.163  0.2416  -0.2268 -0.0445 39  VAL   A N    
308  C  CA   . VAL   A 40  ? 0.825  1.0717 0.1703 0.2214  -0.2393 -0.0429 39  VAL   A CA   
309  C  C    . VAL   A 40  ? 0.8154 1.0503 0.1599 0.2017  -0.2263 -0.0253 39  VAL   A C    
310  O  O    . VAL   A 40  ? 0.8068 1.0507 0.1549 0.1988  -0.215  -0.0221 39  VAL   A O    
311  C  CB   . VAL   A 40  ? 0.8164 1.0726 0.1894 0.2258  -0.251  -0.057  39  VAL   A CB   
312  C  CG1  . VAL   A 40  ? 0.8162 1.0598 0.2167 0.2088  -0.2654 -0.0546 39  VAL   A CG1  
313  C  CG2  . VAL   A 40  ? 0.8178 1.0837 0.1866 0.2449  -0.2607 -0.0777 39  VAL   A CG2  
314  N  N    . LEU   A 41  ? 0.8171 1.0344 0.1575 0.1868  -0.2279 -0.0151 40  LEU   A N    
315  C  CA   . LEU   A 41  ? 0.8163 1.0194 0.155  0.1644  -0.2177 -0.0004 40  LEU   A CA   
316  C  C    . LEU   A 41  ? 0.7966 1.0032 0.1687 0.149   -0.234  -0.0015 40  LEU   A C    
317  O  O    . LEU   A 41  ? 0.7923 0.9951 0.1779 0.1496  -0.2509 -0.0071 40  LEU   A O    
318  C  CB   . LEU   A 41  ? 0.8317 1.0121 0.1453 0.1591  -0.2103 0.0105  40  LEU   A CB   
319  C  CG   . LEU   A 41  ? 0.8584 1.0182 0.1574 0.1377  -0.1932 0.0244  40  LEU   A CG   
320  C  CD1  . LEU   A 41  ? 0.8896 1.0241 0.1473 0.1452  -0.1739 0.0344  40  LEU   A CD1  
321  C  CD2  . LEU   A 41  ? 0.8641 1.0174 0.1819 0.1165  -0.2051 0.0281  40  LEU   A CD2  
322  N  N    . ILE   A 42  ? 0.7863 1.0018 0.1708 0.1351  -0.2288 0.0039  41  ILE   A N    
323  C  CA   . ILE   A 42  ? 0.7762 0.998  0.1901 0.1232  -0.2441 0.0052  41  ILE   A CA   
324  C  C    . ILE   A 42  ? 0.7842 1.0035 0.1958 0.0975  -0.2363 0.0174  41  ILE   A C    
325  O  O    . ILE   A 42  ? 0.7795 1.0143 0.1899 0.0887  -0.2233 0.02    41  ILE   A O    
326  C  CB   . ILE   A 42  ? 0.7575 1.004  0.1968 0.1364  -0.2514 -0.0035 41  ILE   A CB   
327  C  CG1  . ILE   A 42  ? 0.7605 1.0061 0.198  0.1606  -0.2578 -0.0183 41  ILE   A CG1  
328  C  CG2  . ILE   A 42  ? 0.7482 0.9993 0.2146 0.1288  -0.2673 0       41  ILE   A CG2  
329  C  CD1  . ILE   A 42  ? 0.7578 1.0258 0.2072 0.1768  -0.2559 -0.0269 41  ILE   A CD1  
330  N  N    . THR   A 43  ? 0.7944 0.9958 0.2041 0.084   -0.2436 0.0238  42  THR   A N    
331  C  CA   . THR   A 43  ? 0.8035 1.0013 0.2086 0.0586  -0.2374 0.0336  42  THR   A CA   
332  C  C    . THR   A 43  ? 0.7812 1.0046 0.2164 0.051   -0.2508 0.0349  42  THR   A C    
333  O  O    . THR   A 43  ? 0.7716 0.998  0.227  0.0626  -0.2682 0.0321  42  THR   A O    
334  C  CB   . THR   A 43  ? 0.8407 1.0106 0.2298 0.049   -0.2388 0.0399  42  THR   A CB   
335  O  OG1  . THR   A 43  ? 0.8486 1.0182 0.2581 0.0528  -0.2593 0.0386  42  THR   A OG1  
336  C  CG2  . THR   A 43  ? 0.8643 1.0128 0.2229 0.0606  -0.2257 0.0402  42  THR   A CG2  
337  N  N    . GLY   A 44  ? 0.773  1.0139 0.2093 0.0313  -0.2426 0.0391  43  GLY   A N    
338  C  CA   . GLY   A 44  ? 0.7589 1.0335 0.2234 0.0258  -0.2551 0.0411  43  GLY   A CA   
339  C  C    . GLY   A 44  ? 0.7457 1.051  0.233  0.0478  -0.2593 0.0343  43  GLY   A C    
340  O  O    . GLY   A 44  ? 0.7322 1.0526 0.2433 0.0608  -0.2756 0.0345  43  GLY   A O    
341  N  N    . ALA   A 45  ? 0.7503 1.0621 0.2276 0.0539  -0.2431 0.0287  44  ALA   A N    
342  C  CA   . ALA   A 45  ? 0.7453 1.0858 0.2404 0.0763  -0.2439 0.021   44  ALA   A CA   
343  C  C    . ALA   A 45  ? 0.7312 1.1203 0.242  0.0666  -0.2346 0.021   44  ALA   A C    
344  O  O    . ALA   A 45  ? 0.7261 1.1397 0.2456 0.083   -0.2285 0.0146  44  ALA   A O    
345  C  CB   . ALA   A 45  ? 0.7587 1.08   0.2338 0.0938  -0.2336 0.0137  44  ALA   A CB   
346  N  N    . GLY   A 46  ? 0.7202 1.1265 0.2349 0.0398  -0.2337 0.0271  45  GLY   A N    
347  C  CA   . GLY   A 46  ? 0.6997 1.1607 0.2322 0.0262  -0.226  0.0261  45  GLY   A CA   
348  C  C    . GLY   A 46  ? 0.6741 1.1835 0.2428 0.0423  -0.2444 0.0269  45  GLY   A C    
349  O  O    . GLY   A 46  ? 0.6503 1.2159 0.2392 0.0391  -0.2394 0.0247  45  GLY   A O    
350  N  N    . HIS   A 47  ? 0.6777 1.1666 0.2541 0.0603  -0.2646 0.0306  46  HIS   A N    
351  C  CA   . HIS   A 47  ? 0.666  1.1914 0.2717 0.0799  -0.2818 0.034   46  HIS   A CA   
352  C  C    . HIS   A 47  ? 0.6832 1.1645 0.2876 0.1019  -0.2992 0.0371  46  HIS   A C    
353  O  O    . HIS   A 47  ? 0.7046 1.1354 0.2885 0.0941  -0.3001 0.0378  46  HIS   A O    
354  C  CB   . HIS   A 47  ? 0.6701 1.2386 0.2868 0.0549  -0.2868 0.0412  46  HIS   A CB   
355  C  CG   . HIS   A 47  ? 0.6915 1.3063 0.337  0.0753  -0.3043 0.0472  46  HIS   A CG   
356  N  ND1  . HIS   A 47  ? 0.7012 1.3473 0.3682 0.1086  -0.3065 0.0437  46  HIS   A ND1  
357  C  CD2  . HIS   A 47  ? 0.7023 1.3384 0.3556 0.0681  -0.3189 0.0569  46  HIS   A CD2  
358  C  CE1  . HIS   A 47  ? 0.6923 1.3753 0.3792 0.1227  -0.3223 0.0524  46  HIS   A CE1  
359  N  NE2  . HIS   A 47  ? 0.696  1.3763 0.3756 0.099   -0.3307 0.0608  46  HIS   A NE2  
360  N  N    . GLY   A 48  ? 0.6721 1.1735 0.2978 0.1299  -0.3114 0.0386  47  GLY   A N    
361  C  CA   . GLY   A 48  ? 0.6935 1.1557 0.3196 0.1514  -0.327  0.0424  47  GLY   A CA   
362  C  C    . GLY   A 48  ? 0.7216 1.1284 0.3324 0.1648  -0.3257 0.0326  47  GLY   A C    
363  O  O    . GLY   A 48  ? 0.7243 1.1354 0.3352 0.1807  -0.3175 0.0213  47  GLY   A O    
364  N  N    . ILE   A 49  ? 0.7393 1.0972 0.337  0.1574  -0.334  0.0364  48  ILE   A N    
365  C  CA   . ILE   A 49  ? 0.7601 1.0682 0.3441 0.1658  -0.3346 0.0263  48  ILE   A CA   
366  C  C    . ILE   A 49  ? 0.7627 1.0677 0.3304 0.1564  -0.3206 0.0164  48  ILE   A C    
367  O  O    . ILE   A 49  ? 0.7773 1.0637 0.3382 0.1711  -0.3187 0.0039  48  ILE   A O    
368  C  CB   . ILE   A 49  ? 0.7832 1.0461 0.3584 0.1562  -0.3454 0.033   48  ILE   A CB   
369  C  CG1  . ILE   A 49  ? 0.7882 1.0546 0.3752 0.165   -0.3577 0.0467  48  ILE   A CG1  
370  C  CG2  . ILE   A 49  ? 0.8042 1.0225 0.3697 0.166   -0.3474 0.02    48  ILE   A CG2  
371  C  CD1  . ILE   A 49  ? 0.8201 1.0471 0.3975 0.1527  -0.366  0.0558  48  ILE   A CD1  
372  N  N    . GLY   A 50  ? 0.749  1.0717 0.3084 0.1333  -0.3102 0.0216  49  GLY   A N    
373  C  CA   . GLY   A 50  ? 0.7521 1.0686 0.2918 0.1265  -0.2947 0.0152  49  GLY   A CA   
374  C  C    . GLY   A 50  ? 0.7288 1.0766 0.2732 0.1401  -0.2829 0.0073  49  GLY   A C    
375  O  O    . GLY   A 50  ? 0.7403 1.0765 0.2698 0.1498  -0.2743 -0.0017 49  GLY   A O    
376  N  N    . ARG   A 51  ? 0.6967 1.0885 0.2615 0.1411  -0.2822 0.0107  50  ARG   A N    
377  C  CA   . ARG   A 51  ? 0.6809 1.1123 0.2545 0.1524  -0.2701 0.0044  50  ARG   A CA   
378  C  C    . ARG   A 51  ? 0.6856 1.1095 0.2651 0.186   -0.2753 -0.0068 50  ARG   A C    
379  O  O    . ARG   A 51  ? 0.6886 1.1195 0.2599 0.1971  -0.2634 -0.016  50  ARG   A O    
380  C  CB   . ARG   A 51  ? 0.6661 1.1544 0.2641 0.1443  -0.2706 0.011   50  ARG   A CB   
381  C  CG   . ARG   A 51  ? 0.6698 1.2088 0.2871 0.1637  -0.2632 0.0048  50  ARG   A CG   
382  C  CD   . ARG   A 51  ? 0.6652 1.2691 0.3057 0.1494  -0.2616 0.0108  50  ARG   A CD   
383  N  NE   . ARG   A 51  ? 0.691  1.3135 0.3205 0.1179  -0.2413 0.0099  50  ARG   A NE   
384  C  CZ   . ARG   A 51  ? 0.6943 1.3762 0.3406 0.0967  -0.2347 0.012   50  ARG   A CZ   
385  N  NH1  . ARG   A 51  ? 0.6598 1.3954 0.3364 0.1064  -0.2486 0.0158  50  ARG   A NH1  
386  N  NH2  . ARG   A 51  ? 0.7002 1.3884 0.3316 0.0653  -0.2136 0.0102  50  ARG   A NH2  
387  N  N    . TRP   A 52  ? 0.6864 1.0937 0.2775 0.2022  -0.2917 -0.0061 51  TRP   A N    
388  C  CA   . TRP   A 52  ? 0.6953 1.0885 0.2896 0.2339  -0.2961 -0.0181 51  TRP   A CA   
389  C  C    . TRP   A 52  ? 0.7248 1.0689 0.297  0.2365  -0.2975 -0.03   51  TRP   A C    
390  O  O    . TRP   A 52  ? 0.734  1.0682 0.3026 0.259   -0.2968 -0.0442 51  TRP   A O    
391  C  CB   . TRP   A 52  ? 0.6854 1.0781 0.2979 0.2529  -0.31   -0.0124 51  TRP   A CB   
392  C  CG   . TRP   A 52  ? 0.6581 1.1133 0.2939 0.2598  -0.3073 -0.0051 51  TRP   A CG   
393  C  CD1  . TRP   A 52  ? 0.6509 1.1478 0.2966 0.2362  -0.3057 0.0064  51  TRP   A CD1  
394  C  CD2  . TRP   A 52  ? 0.6399 1.1301 0.2915 0.2909  -0.3036 -0.0111 51  TRP   A CD2  
395  N  NE1  . TRP   A 52  ? 0.6254 1.1856 0.2944 0.2493  -0.3024 0.008   51  TRP   A NE1  
396  C  CE2  . TRP   A 52  ? 0.6206 1.1785 0.2942 0.2847  -0.3009 -0.0018 51  TRP   A CE2  
397  C  CE3  . TRP   A 52  ? 0.6527 1.1249 0.3011 0.3233  -0.3017 -0.0245 51  TRP   A CE3  
398  C  CZ2  . TRP   A 52  ? 0.603  1.2148 0.2981 0.3118  -0.2971 -0.004  51  TRP   A CZ2  
399  C  CZ3  . TRP   A 52  ? 0.6415 1.1609 0.3086 0.3514  -0.2971 -0.0266 51  TRP   A CZ3  
400  C  CH2  . TRP   A 52  ? 0.6119 1.2024 0.3031 0.3464  -0.2949 -0.0158 51  TRP   A CH2  
401  N  N    . THR   A 53  ? 0.735  1.0538 0.2915 0.2137  -0.2982 -0.0255 52  THR   A N    
402  C  CA   . THR   A 53  ? 0.7579 1.0431 0.2942 0.2139  -0.2986 -0.0363 52  THR   A CA   
403  C  C    . THR   A 53  ? 0.7745 1.0784 0.295  0.218   -0.2825 -0.043  52  THR   A C    
404  O  O    . THR   A 53  ? 0.784  1.0791 0.2939 0.2344  -0.2816 -0.0576 52  THR   A O    
405  C  CB   . THR   A 53  ? 0.7708 1.0296 0.2984 0.1913  -0.3046 -0.0278 52  THR   A CB   
406  O  OG1  . THR   A 53  ? 0.7802 1.0114 0.3171 0.1948  -0.3193 -0.0278 52  THR   A OG1  
407  C  CG2  . THR   A 53  ? 0.7891 1.0317 0.2941 0.1863  -0.2998 -0.0346 52  THR   A CG2  
408  N  N    . ALA   A 54  ? 0.7739 1.1039 0.2918 0.2035  -0.2689 -0.0329 53  ALA   A N    
409  C  CA   . ALA   A 54  ? 0.7832 1.1296 0.2845 0.2069  -0.2506 -0.0364 53  ALA   A CA   
410  C  C    . ALA   A 54  ? 0.7812 1.1539 0.2933 0.232   -0.247  -0.0475 53  ALA   A C    
411  O  O    . ALA   A 54  ? 0.787  1.1624 0.282  0.244   -0.2367 -0.056  53  ALA   A O    
412  C  CB   . ALA   A 54  ? 0.7799 1.1451 0.2772 0.183   -0.2357 -0.0235 53  ALA   A CB   
413  N  N    . TYR   A 55  ? 0.7752 1.1674 0.3136 0.2427  -0.2551 -0.0472 54  TYR   A N    
414  C  CA   . TYR   A 55  ? 0.7772 1.1934 0.326  0.2703  -0.2517 -0.0581 54  TYR   A CA   
415  C  C    . TYR   A 55  ? 0.7965 1.1766 0.3327 0.2911  -0.26   -0.0751 54  TYR   A C    
416  O  O    . TYR   A 55  ? 0.7997 1.1894 0.3268 0.3098  -0.2519 -0.0877 54  TYR   A O    
417  C  CB   . TYR   A 55  ? 0.7645 1.2087 0.3434 0.2812  -0.2595 -0.0527 54  TYR   A CB   
418  C  CG   . TYR   A 55  ? 0.7593 1.2538 0.3558 0.2631  -0.2523 -0.0395 54  TYR   A CG   
419  C  CD1  . TYR   A 55  ? 0.7695 1.2843 0.355  0.2409  -0.2345 -0.0357 54  TYR   A CD1  
420  C  CD2  . TYR   A 55  ? 0.7596 1.2822 0.3823 0.2683  -0.2624 -0.0313 54  TYR   A CD2  
421  C  CE1  . TYR   A 55  ? 0.7642 1.3259 0.3654 0.2198  -0.2269 -0.0262 54  TYR   A CE1  
422  C  CE2  . TYR   A 55  ? 0.752  1.328  0.3919 0.2496  -0.2569 -0.0212 54  TYR   A CE2  
423  C  CZ   . TYR   A 55  ? 0.7623 1.3584 0.3922 0.2235  -0.239  -0.0199 54  TYR   A CZ   
424  O  OH   . TYR   A 55  ? 0.7627 1.4126 0.4099 0.2011  -0.2333 -0.0123 54  TYR   A OH   
425  N  N    . GLU   A 56  ? 0.8112 1.151  0.3461 0.2865  -0.2755 -0.0763 55  GLU   A N    
426  C  CA   . GLU   A 56  ? 0.837  1.1405 0.3602 0.3004  -0.2839 -0.0942 55  GLU   A CA   
427  C  C    . GLU   A 56  ? 0.8535 1.1501 0.3508 0.2969  -0.2786 -0.1043 55  GLU   A C    
428  O  O    . GLU   A 56  ? 0.8659 1.1551 0.3513 0.3141  -0.2787 -0.123  55  GLU   A O    
429  C  CB   . GLU   A 56  ? 0.8825 1.1457 0.4112 0.2922  -0.2998 -0.0919 55  GLU   A CB   
430  C  CG   . GLU   A 56  ? 0.9485 1.2067 0.4958 0.3093  -0.3063 -0.0886 55  GLU   A CG   
431  C  CD   . GLU   A 56  ? 1.042  1.2905 0.5867 0.3397  -0.3045 -0.107  55  GLU   A CD   
432  O  OE1  . GLU   A 56  ? 1.0629 1.2925 0.5894 0.3436  -0.3034 -0.1261 55  GLU   A OE1  
433  O  OE2  . GLU   A 56  ? 1.0688 1.33   0.6286 0.3607  -0.3042 -0.1027 55  GLU   A OE2  
434  N  N    . PHE   A 57  ? 0.8494 1.1494 0.3356 0.2764  -0.2732 -0.0922 56  PHE   A N    
435  C  CA   . PHE   A 57  ? 0.856  1.1535 0.3154 0.2765  -0.267  -0.0983 56  PHE   A CA   
436  C  C    . PHE   A 57  ? 0.8392 1.165  0.2863 0.2915  -0.2502 -0.102  56  PHE   A C    
437  O  O    . PHE   A 57  ? 0.8494 1.1747 0.276  0.3048  -0.2481 -0.1151 56  PHE   A O    
438  C  CB   . PHE   A 57  ? 0.8663 1.1557 0.3146 0.2541  -0.2642 -0.083  56  PHE   A CB   
439  C  CG   . PHE   A 57  ? 0.8898 1.1513 0.3406 0.2429  -0.28   -0.085  56  PHE   A CG   
440  C  CD1  . PHE   A 57  ? 0.9137 1.1628 0.3557 0.2509  -0.2894 -0.1028 56  PHE   A CD1  
441  C  CD2  . PHE   A 57  ? 0.8992 1.1497 0.36   0.2227  -0.2847 -0.07   56  PHE   A CD2  
442  C  CE1  . PHE   A 57  ? 0.9302 1.1573 0.3757 0.2374  -0.3026 -0.1052 56  PHE   A CE1  
443  C  CE2  . PHE   A 57  ? 0.917  1.1437 0.3796 0.2116  -0.2975 -0.0713 56  PHE   A CE2  
444  C  CZ   . PHE   A 57  ? 0.9231 1.1388 0.3791 0.2183  -0.306  -0.0887 56  PHE   A CZ   
445  N  N    . ALA   A 58  ? 0.813  1.1669 0.273  0.2895  -0.2383 -0.0916 57  ALA   A N    
446  C  CA   . ALA   A 58  ? 0.802  1.186  0.253  0.3026  -0.2204 -0.0944 57  ALA   A CA   
447  C  C    . ALA   A 58  ? 0.793  1.1814 0.2455 0.3311  -0.2241 -0.1147 57  ALA   A C    
448  O  O    . ALA   A 58  ? 0.7928 1.1962 0.2271 0.3456  -0.212  -0.1224 57  ALA   A O    
449  C  CB   . ALA   A 58  ? 0.7847 1.2026 0.2547 0.2915  -0.2085 -0.0809 57  ALA   A CB   
450  N  N    . LYS   A 59  ? 0.7846 1.1564 0.2556 0.3396  -0.2396 -0.1229 58  LYS   A N    
451  C  CA   . LYS   A 59  ? 0.7893 1.1544 0.2591 0.3661  -0.2435 -0.1437 58  LYS   A CA   
452  C  C    . LYS   A 59  ? 0.817  1.1584 0.2596 0.3701  -0.2491 -0.1618 58  LYS   A C    
453  O  O    . LYS   A 59  ? 0.8237 1.1721 0.2521 0.3906  -0.2442 -0.1793 58  LYS   A O    
454  C  CB   . LYS   A 59  ? 0.7954 1.1393 0.2877 0.3729  -0.2572 -0.1454 58  LYS   A CB   
455  C  CG   . LYS   A 59  ? 0.7977 1.1767 0.3171 0.3788  -0.252  -0.1316 58  LYS   A CG   
456  C  CD   . LYS   A 59  ? 0.8242 1.1817 0.3609 0.3945  -0.264  -0.1333 58  LYS   A CD   
457  C  CE   . LYS   A 59  ? 0.8318 1.235  0.3934 0.4111  -0.2576 -0.1242 58  LYS   A CE   
458  N  NZ   . LYS   A 59  ? 0.8595 1.2404 0.4353 0.4297  -0.2689 -0.1222 58  LYS   A NZ   
459  N  N    . GLN   A 60  ? 0.8268 1.1454 0.2619 0.3504  -0.259  -0.1578 59  GLN   A N    
460  C  CA   . GLN   A 60  ? 0.8437 1.1473 0.256  0.3499  -0.2665 -0.1735 59  GLN   A CA   
461  C  C    . GLN   A 60  ? 0.8479 1.1748 0.2319 0.3544  -0.2542 -0.1712 59  GLN   A C    
462  O  O    . GLN   A 60  ? 0.8515 1.1747 0.2157 0.3554  -0.2607 -0.1827 59  GLN   A O    
463  C  CB   . GLN   A 60  ? 0.8654 1.143  0.2836 0.3274  -0.2806 -0.168  59  GLN   A CB   
464  C  CG   . GLN   A 60  ? 0.9049 1.1526 0.3451 0.323   -0.2926 -0.1701 59  GLN   A CG   
465  C  CD   . GLN   A 60  ? 0.9558 1.1777 0.3897 0.3343  -0.3011 -0.1969 59  GLN   A CD   
466  O  OE1  . GLN   A 60  ? 0.9647 1.1898 0.3788 0.3375  -0.3032 -0.2158 59  GLN   A OE1  
467  N  NE2  . GLN   A 60  ? 0.9673 1.162  0.4159 0.3406  -0.3059 -0.1994 59  GLN   A NE2  
468  N  N    . LYS   A 61  ? 0.8418 1.1932 0.2231 0.3565  -0.2362 -0.1559 60  LYS   A N    
469  C  CA   . LYS   A 61  ? 0.8506 1.2195 0.2023 0.3615  -0.2203 -0.1491 60  LYS   A CA   
470  C  C    . LYS   A 61  ? 0.8623 1.2189 0.197  0.347   -0.2219 -0.1364 60  LYS   A C    
471  O  O    . LYS   A 61  ? 0.8777 1.2384 0.185  0.357   -0.2217 -0.1422 60  LYS   A O    
472  C  CB   . LYS   A 61  ? 0.8815 1.2627 0.2108 0.3861  -0.218  -0.17   60  LYS   A CB   
473  C  CG   . LYS   A 61  ? 0.9356 1.3294 0.2792 0.4034  -0.2135 -0.1821 60  LYS   A CG   
474  C  CD   . LYS   A 61  ? 1.0146 1.4205 0.3326 0.4276  -0.2098 -0.2035 60  LYS   A CD   
475  C  CE   . LYS   A 61  ? 1.0606 1.4855 0.3884 0.4472  -0.1988 -0.2114 60  LYS   A CE   
476  N  NZ   . LYS   A 61  ? 1.0942 1.5368 0.3911 0.4702  -0.1897 -0.2279 60  LYS   A NZ   
477  N  N    . SER   A 62  ? 0.8563 1.2002 0.206  0.3252  -0.2232 -0.1191 61  SER   A N    
478  C  CA   . SER   A 62  ? 0.8643 1.1944 0.199  0.3118  -0.2235 -0.1059 61  SER   A CA   
479  C  C    . SER   A 62  ? 0.8701 1.2013 0.1874 0.3032  -0.2011 -0.0839 61  SER   A C    
480  O  O    . SER   A 62  ? 0.8682 1.2125 0.1927 0.3007  -0.1872 -0.0781 61  SER   A O    
481  C  CB   . SER   A 62  ? 0.8707 1.1812 0.2299 0.2921  -0.2393 -0.1022 61  SER   A CB   
482  O  OG   . SER   A 62  ? 0.8919 1.1942 0.2665 0.2967  -0.2576 -0.1215 61  SER   A OG   
483  N  N    . ARG   A 63  ? 0.8752 1.1918 0.1696 0.2977  -0.1968 -0.0719 62  ARG   A N    
484  C  CA   . ARG   A 63  ? 0.8826 1.1878 0.1539 0.288   -0.1743 -0.0508 62  ARG   A CA   
485  C  C    . ARG   A 63  ? 0.8645 1.151  0.1521 0.2605  -0.1759 -0.0375 62  ARG   A C    
486  O  O    . ARG   A 63  ? 0.88   1.1478 0.1566 0.2545  -0.1795 -0.0302 62  ARG   A O    
487  C  CB   . ARG   A 63  ? 0.9231 1.2212 0.1523 0.3047  -0.1653 -0.0448 62  ARG   A CB   
488  C  CG   . ARG   A 63  ? 0.9828 1.2946 0.1841 0.3251  -0.1476 -0.0455 62  ARG   A CG   
489  C  CD   . ARG   A 63  ? 1.0473 1.3579 0.2066 0.3481  -0.1423 -0.0415 62  ARG   A CD   
490  N  NE   . ARG   A 63  ? 1.1108 1.3921 0.2435 0.3415  -0.1274 -0.0197 62  ARG   A NE   
491  C  CZ   . ARG   A 63  ? 1.1627 1.4373 0.2543 0.3624  -0.1188 -0.0099 62  ARG   A CZ   
492  N  NH1  . ARG   A 63  ? 1.1594 1.4599 0.2325 0.3902  -0.1249 -0.0204 62  ARG   A NH1  
493  N  NH2  . ARG   A 63  ? 1.1829 1.4251 0.2496 0.3572  -0.1036 0.0102  62  ARG   A NH2  
494  N  N    . LEU   A 64  ? 0.8262 1.122  0.1392 0.2448  -0.1729 -0.0346 63  LEU   A N    
495  C  CA   . LEU   A 64  ? 0.7991 1.0841 0.13   0.2186  -0.1762 -0.0243 63  LEU   A CA   
496  C  C    . LEU   A 64  ? 0.8053 1.069  0.1111 0.2001  -0.156  -0.0073 63  LEU   A C    
497  O  O    . LEU   A 64  ? 0.8114 1.0731 0.0932 0.1997  -0.133  -0.0004 63  LEU   A O    
498  C  CB   . LEU   A 64  ? 0.7662 1.0759 0.1324 0.2104  -0.1807 -0.0275 63  LEU   A CB   
499  C  CG   . LEU   A 64  ? 0.7542 1.0745 0.1464 0.2264  -0.2015 -0.0428 63  LEU   A CG   
500  C  CD1  . LEU   A 64  ? 0.7358 1.0852 0.1574 0.2266  -0.2017 -0.0448 63  LEU   A CD1  
501  C  CD2  . LEU   A 64  ? 0.7636 1.0619 0.1657 0.22    -0.2217 -0.0443 63  LEU   A CD2  
502  N  N    . VAL   A 65  ? 0.8042 1.0491 0.1153 0.1832  -0.1643 -0.0009 64  VAL   A N    
503  C  CA   . VAL   A 65  ? 0.8169 1.0351 0.1076 0.162   -0.1493 0.0135  64  VAL   A CA   
504  C  C    . VAL   A 65  ? 0.7991 1.0239 0.1216 0.1389  -0.1629 0.0143  64  VAL   A C    
505  O  O    . VAL   A 65  ? 0.7993 1.0231 0.1401 0.1417  -0.1839 0.0099  64  VAL   A O    
506  C  CB   . VAL   A 65  ? 0.8469 1.0375 0.1097 0.172   -0.15   0.0186  64  VAL   A CB   
507  C  CG1  . VAL   A 65  ? 0.8681 1.0252 0.1065 0.1519  -0.1331 0.0329  64  VAL   A CG1  
508  C  CG2  . VAL   A 65  ? 0.8709 1.0628 0.1038 0.2008  -0.1416 0.0168  64  VAL   A CG2  
509  N  N    . LEU   A 66  ? 0.7787 1.0129 0.1082 0.1156  -0.1514 0.0194  65  LEU   A N    
510  C  CA   . LEU   A 66  ? 0.7497 0.9973 0.1092 0.0952  -0.1653 0.0203  65  LEU   A CA   
511  C  C    . LEU   A 66  ? 0.7547 0.9776 0.0956 0.0665  -0.1533 0.0302  65  LEU   A C    
512  O  O    . LEU   A 66  ? 0.7672 0.977  0.0824 0.0536  -0.1292 0.035   65  LEU   A O    
513  C  CB   . LEU   A 66  ? 0.7235 1.0154 0.1139 0.0919  -0.1667 0.0154  65  LEU   A CB   
514  C  CG   . LEU   A 66  ? 0.7278 1.0447 0.1287 0.1191  -0.1683 0.0055  65  LEU   A CG   
515  C  CD1  . LEU   A 66  ? 0.7095 1.073  0.1394 0.114   -0.1662 0.0028  65  LEU   A CD1  
516  C  CD2  . LEU   A 66  ? 0.7325 1.0438 0.1467 0.1429  -0.1912 -0.0036 65  LEU   A CD2  
517  N  N    . TRP   A 67  ? 0.7465 0.9599 0.0978 0.0558  -0.1688 0.0328  66  TRP   A N    
518  C  CA   . TRP   A 67  ? 0.7584 0.9472 0.0921 0.029   -0.1601 0.0405  66  TRP   A CA   
519  C  C    . TRP   A 67  ? 0.7397 0.9558 0.1032 0.0077  -0.174  0.0403  66  TRP   A C    
520  O  O    . TRP   A 67  ? 0.7241 0.9608 0.1173 0.0189  -0.1961 0.0375  66  TRP   A O    
521  C  CB   . TRP   A 67  ? 0.7752 0.9287 0.0895 0.0376  -0.1651 0.0446  66  TRP   A CB   
522  C  CG   . TRP   A 67  ? 0.8086 0.9308 0.0832 0.0534  -0.1464 0.0486  66  TRP   A CG   
523  C  CD1  . TRP   A 67  ? 0.8241 0.9467 0.081  0.0676  -0.1303 0.048   66  TRP   A CD1  
524  C  CD2  . TRP   A 67  ? 0.8327 0.921  0.0796 0.0603  -0.1423 0.0548  66  TRP   A CD2  
525  N  NE1  . TRP   A 67  ? 0.8501 0.9393 0.0678 0.0833  -0.1162 0.0546  66  TRP   A NE1  
526  C  CE2  . TRP   A 67  ? 0.8574 0.9266 0.0692 0.0801  -0.1234 0.0586  66  TRP   A CE2  
527  C  CE3  . TRP   A 67  ? 0.8473 0.9214 0.0946 0.0528  -0.1518 0.0581  66  TRP   A CE3  
528  C  CZ2  . TRP   A 67  ? 0.8887 0.9268 0.0666 0.0945  -0.1143 0.066   66  TRP   A CZ2  
529  C  CZ3  . TRP   A 67  ? 0.8763 0.921  0.0919 0.0657  -0.1424 0.0643  66  TRP   A CZ3  
530  C  CH2  . TRP   A 67  ? 0.8929 0.9205 0.0743 0.0872  -0.124  0.0684  66  TRP   A CH2  
531  N  N    . ASP   A 68  ? 0.7414 0.9571 0.095  -0.0229 -0.1605 0.0431  67  ASP   A N    
532  C  CA   . ASP   A 68  ? 0.7275 0.9755 0.1066 -0.0447 -0.173  0.0428  67  ASP   A CA   
533  C  C    . ASP   A 68  ? 0.7351 0.972  0.092  -0.0824 -0.1544 0.0439  67  ASP   A C    
534  O  O    . ASP   A 68  ? 0.7562 0.9631 0.0808 -0.0918 -0.1293 0.0445  67  ASP   A O    
535  C  CB   . ASP   A 68  ? 0.7216 1.0263 0.1379 -0.0362 -0.182  0.0377  67  ASP   A CB   
536  C  CG   . ASP   A 68  ? 0.7557 1.0976 0.2048 -0.0405 -0.2047 0.0389  67  ASP   A CG   
537  O  OD1  . ASP   A 68  ? 0.7657 1.1139 0.2355 -0.0157 -0.2242 0.0389  67  ASP   A OD1  
538  O  OD2  . ASP   A 68  ? 0.755  1.1188 0.2071 -0.0688 -0.2022 0.0395  67  ASP   A OD2  
539  N  N    . ILE   A 69  ? 0.7181 0.978  0.0902 -0.1043 -0.1661 0.0439  68  ILE   A N    
540  C  CA   . ILE   A 69  ? 0.7301 0.9863 0.0837 -0.1438 -0.1503 0.0416  68  ILE   A CA   
541  C  C    . ILE   A 69  ? 0.7158 1.0295 0.0918 -0.1628 -0.144  0.0351  68  ILE   A C    
542  O  O    . ILE   A 69  ? 0.729  1.0374 0.0855 -0.1968 -0.1229 0.0307  68  ILE   A O    
543  C  CB   . ILE   A 69  ? 0.7291 0.982  0.0826 -0.1603 -0.1647 0.0439  68  ILE   A CB   
544  C  CG1  . ILE   A 69  ? 0.7052 1.0096 0.1012 -0.1464 -0.1947 0.0459  68  ILE   A CG1  
545  C  CG2  . ILE   A 69  ? 0.7607 0.9525 0.0827 -0.1506 -0.1614 0.0495  68  ILE   A CG2  
546  C  CD1  . ILE   A 69  ? 0.6922 1.0549 0.1089 -0.1742 -0.2022 0.0422  68  ILE   A CD1  
547  N  N    . ASN   A 70  ? 0.6861 1.0544 0.1024 -0.1411 -0.1613 0.0338  69  ASN   A N    
548  C  CA   . ASN   A 70  ? 0.6616 1.0961 0.1064 -0.1512 -0.1585 0.0281  69  ASN   A CA   
549  C  C    . ASN   A 70  ? 0.6754 1.101  0.1088 -0.1417 -0.1368 0.0258  69  ASN   A C    
550  O  O    . ASN   A 70  ? 0.6766 1.1071 0.123  -0.1065 -0.1446 0.0264  69  ASN   A O    
551  C  CB   . ASN   A 70  ? 0.6419 1.1306 0.1304 -0.1236 -0.1862 0.0295  69  ASN   A CB   
552  C  CG   . ASN   A 70  ? 0.6478 1.2168 0.17   -0.1344 -0.1882 0.0246  69  ASN   A CG   
553  O  OD1  . ASN   A 70  ? 0.6457 1.2384 0.1685 -0.1469 -0.1687 0.019   69  ASN   A OD1  
554  N  ND2  . ASN   A 70  ? 0.647  1.2628 0.1981 -0.1287 -0.2115 0.0273  69  ASN   A ND2  
555  N  N    . LYS   A 71  ? 0.689  1.0988 0.0958 -0.173  -0.1086 0.0228  70  LYS   A N    
556  C  CA   . LYS   A 71  ? 0.7049 1.1024 0.0957 -0.165  -0.0847 0.0223  70  LYS   A CA   
557  C  C    . LYS   A 71  ? 0.6807 1.1481 0.1114 -0.1478 -0.0908 0.018   70  LYS   A C    
558  O  O    . LYS   A 71  ? 0.6891 1.1485 0.1174 -0.1171 -0.0875 0.019   70  LYS   A O    
559  C  CB   . LYS   A 71  ? 0.7392 1.1057 0.093  -0.2059 -0.0511 0.0203  70  LYS   A CB   
560  C  CG   . LYS   A 71  ? 0.7771 1.1264 0.1092 -0.1993 -0.0234 0.0219  70  LYS   A CG   
561  C  CD   . LYS   A 71  ? 0.8626 1.1533 0.145  -0.2347 0.0115  0.023   70  LYS   A CD   
562  C  CE   . LYS   A 71  ? 0.947  1.2014 0.1963 -0.2213 0.04    0.0287  70  LYS   A CE   
563  N  NZ   . LYS   A 71  ? 0.9503 1.2699 0.2281 -0.2288 0.0486  0.0233  70  LYS   A NZ   
564  N  N    . HIS   A 72  ? 0.6545 1.1932 0.1216 -0.1648 -0.101  0.013   71  HIS   A N    
565  C  CA   . HIS   A 72  ? 0.6329 1.2477 0.1409 -0.1492 -0.1068 0.0088  71  HIS   A CA   
566  C  C    . HIS   A 72  ? 0.6455 1.2698 0.1778 -0.0995 -0.1317 0.0112  71  HIS   A C    
567  O  O    . HIS   A 72  ? 0.6429 1.2867 0.1858 -0.0736 -0.1273 0.0087  71  HIS   A O    
568  C  CB   . HIS   A 72  ? 0.604  1.2958 0.1436 -0.1802 -0.1132 0.0034  71  HIS   A CB   
569  C  CG   . HIS   A 72  ? 0.5856 1.3651 0.1706 -0.1624 -0.1211 -0.0003 71  HIS   A CG   
570  N  ND1  . HIS   A 72  ? 0.5929 1.4122 0.1844 -0.1749 -0.0979 -0.0058 71  HIS   A ND1  
571  C  CD2  . HIS   A 72  ? 0.5705 1.4035 0.1942 -0.1326 -0.1482 0.0015  71  HIS   A CD2  
572  C  CE1  . HIS   A 72  ? 0.5585 1.458  0.1942 -0.1513 -0.1122 -0.0079 71  HIS   A CE1  
573  N  NE2  . HIS   A 72  ? 0.5498 1.4579 0.205  -0.1238 -0.1424 -0.0032 71  HIS   A NE2  
574  N  N    . GLY   A 73  ? 0.6625 1.2698 0.2007 -0.0878 -0.1558 0.0155  72  GLY   A N    
575  C  CA   . GLY   A 73  ? 0.6772 1.2846 0.2351 -0.0455 -0.1796 0.0176  72  GLY   A CA   
576  C  C    . GLY   A 73  ? 0.7266 1.2815 0.2632 -0.0168 -0.1746 0.017   72  GLY   A C    
577  O  O    . GLY   A 73  ? 0.7215 1.2945 0.2743 0.0152  -0.1802 0.0132  72  GLY   A O    
578  N  N    . VAL   A 74  ? 0.7716 1.2631 0.2699 -0.0274 -0.1632 0.02    73  VAL   A N    
579  C  CA   . VAL   A 74  ? 0.8083 1.253  0.2827 -0.0013 -0.1581 0.0196  73  VAL   A CA   
580  C  C    . VAL   A 74  ? 0.8136 1.2719 0.2792 0.0059  -0.1362 0.0158  73  VAL   A C    
581  O  O    . VAL   A 74  ? 0.8183 1.2655 0.279  0.0364  -0.1379 0.0125  73  VAL   A O    
582  C  CB   . VAL   A 74  ? 0.8533 1.2332 0.2899 -0.0111 -0.1524 0.0252  73  VAL   A CB   
583  C  CG1  . VAL   A 74  ? 0.8813 1.2353 0.2823 -0.0379 -0.1222 0.0278  73  VAL   A CG1  
584  C  CG2  . VAL   A 74  ? 0.8767 1.2213 0.3006 0.0214  -0.16   0.0243  73  VAL   A CG2  
585  N  N    . GLU   A 75  ? 0.8116 1.2966 0.2755 -0.0234 -0.1156 0.0153  74  GLU   A N    
586  C  CA   . GLU   A 75  ? 0.8234 1.3254 0.2796 -0.0206 -0.0924 0.0127  74  GLU   A CA   
587  C  C    . GLU   A 75  ? 0.8033 1.3681 0.2988 0.0054  -0.1033 0.0061  74  GLU   A C    
588  O  O    . GLU   A 75  ? 0.8045 1.3718 0.2934 0.0285  -0.0937 0.0029  74  GLU   A O    
589  C  CB   . GLU   A 75  ? 0.8467 1.3577 0.2895 -0.0643 -0.0658 0.0135  74  GLU   A CB   
590  C  CG   . GLU   A 75  ? 0.9425 1.3785 0.3321 -0.0797 -0.0426 0.02    74  GLU   A CG   
591  C  CD   . GLU   A 75  ? 1.0274 1.4586 0.3964 -0.1253 -0.0126 0.0201  74  GLU   A CD   
592  O  OE1  . GLU   A 75  ? 1.0027 1.4969 0.4027 -0.1507 -0.0116 0.0138  74  GLU   A OE1  
593  O  OE2  . GLU   A 75  ? 1.0997 1.464  0.4202 -0.1354 0.0107  0.0263  74  GLU   A OE2  
594  N  N    . GLU   A 76  ? 0.778  1.3929 0.3122 0.0042  -0.1233 0.0045  75  GLU   A N    
595  C  CA   . GLU   A 76  ? 0.7534 1.4272 0.325  0.0331  -0.1347 -0.0007 75  GLU   A CA   
596  C  C    . GLU   A 76  ? 0.7637 1.4067 0.3357 0.076   -0.153  -0.0035 75  GLU   A C    
597  O  O    . GLU   A 76  ? 0.7504 1.4203 0.3368 0.1053  -0.1536 -0.0097 75  GLU   A O    
598  C  CB   . GLU   A 76  ? 0.7463 1.484  0.3558 0.0215  -0.1495 0       75  GLU   A CB   
599  C  CG   . GLU   A 76  ? 0.7922 1.5883 0.4125 -0.0141 -0.1299 -0.0025 75  GLU   A CG   
600  C  CD   . GLU   A 76  ? 0.8537 1.7379 0.5195 -0.0134 -0.1441 -0.004  75  GLU   A CD   
601  O  OE1  . GLU   A 76  ? 0.8705 1.7592 0.5512 -0.0031 -0.1689 0.0002  75  GLU   A OE1  
602  O  OE2  . GLU   A 76  ? 0.861  1.8124 0.5472 -0.0225 -0.13   -0.0088 75  GLU   A OE2  
603  N  N    . THR   A 77  ? 0.783  1.3692 0.3376 0.0785  -0.1664 0       76  THR   A N    
604  C  CA   . THR   A 77  ? 0.7959 1.3487 0.3476 0.1132  -0.182  -0.0044 76  THR   A CA   
605  C  C    . THR   A 77  ? 0.8201 1.3495 0.3444 0.1276  -0.1656 -0.0096 76  THR   A C    
606  O  O    . THR   A 77  ? 0.8159 1.3544 0.3472 0.1579  -0.1697 -0.0181 76  THR   A O    
607  C  CB   . THR   A 77  ? 0.824  1.3274 0.364  0.1077  -0.1979 0.0005  76  THR   A CB   
608  O  OG1  . THR   A 77  ? 0.8163 1.344  0.3794 0.0948  -0.2121 0.0063  76  THR   A OG1  
609  C  CG2  . THR   A 77  ? 0.8412 1.3114 0.3783 0.1386  -0.213  -0.0057 76  THR   A CG2  
610  N  N    . ALA   A 78  ? 0.8425 1.343  0.3338 0.1064  -0.1454 -0.0044 77  ALA   A N    
611  C  CA   . ALA   A 78  ? 0.8636 1.3417 0.3227 0.1183  -0.1267 -0.0062 77  ALA   A CA   
612  C  C    . ALA   A 78  ? 0.8522 1.3781 0.3242 0.1291  -0.1131 -0.0118 77  ALA   A C    
613  O  O    . ALA   A 78  ? 0.8611 1.3809 0.3192 0.1549  -0.1084 -0.0178 77  ALA   A O    
614  C  CB   . ALA   A 78  ? 0.8863 1.328  0.3085 0.091   -0.1046 0.0032  77  ALA   A CB   
615  N  N    . ALA   A 79  ? 0.8286 1.4062 0.3267 0.1094  -0.1067 -0.0107 78  ALA   A N    
616  C  CA   . ALA   A 79  ? 0.8132 1.4459 0.3282 0.1184  -0.0933 -0.016  78  ALA   A CA   
617  C  C    . ALA   A 79  ? 0.8047 1.4587 0.3432 0.1596  -0.1112 -0.0258 78  ALA   A C    
618  O  O    . ALA   A 79  ? 0.8092 1.4731 0.3396 0.1818  -0.1006 -0.0323 78  ALA   A O    
619  C  CB   . ALA   A 79  ? 0.7859 1.4774 0.329  0.0875  -0.0862 -0.0137 78  ALA   A CB   
620  N  N    . GLU   A 80  ? 0.7938 1.4492 0.3568 0.171   -0.1371 -0.0268 79  GLU   A N    
621  C  CA   . GLU   A 80  ? 0.7895 1.4543 0.3701 0.2106  -0.1527 -0.0363 79  GLU   A CA   
622  C  C    . GLU   A 80  ? 0.8126 1.4194 0.3649 0.2333  -0.1593 -0.044  79  GLU   A C    
623  O  O    . GLU   A 80  ? 0.8101 1.4201 0.3649 0.2648  -0.1631 -0.0553 79  GLU   A O    
624  C  CB   . GLU   A 80  ? 0.8086 1.4944 0.4226 0.2174  -0.1753 -0.0336 79  GLU   A CB   
625  C  CG   . GLU   A 80  ? 0.8809 1.5863 0.5155 0.2586  -0.186  -0.0424 79  GLU   A CG   
626  C  CD   . GLU   A 80  ? 0.9758 1.7236 0.6157 0.2798  -0.1694 -0.0512 79  GLU   A CD   
627  O  OE1  . GLU   A 80  ? 1.0018 1.72   0.6231 0.3049  -0.1675 -0.0621 79  GLU   A OE1  
628  O  OE2  . GLU   A 80  ? 0.9927 1.8066 0.6554 0.2706  -0.1581 -0.0481 79  GLU   A OE2  
629  N  N    . CYS   A 81  ? 0.8332 1.3907 0.3576 0.2172  -0.1594 -0.0389 80  CYS   A N    
630  C  CA   . CYS   A 81  ? 0.8585 1.3699 0.3554 0.235   -0.1646 -0.0461 80  CYS   A CA   
631  C  C    . CYS   A 81  ? 0.8559 1.3723 0.3264 0.2456  -0.1434 -0.0502 80  CYS   A C    
632  O  O    . CYS   A 81  ? 0.8664 1.3683 0.3228 0.2709  -0.1479 -0.0615 80  CYS   A O    
633  C  CB   . CYS   A 81  ? 0.8983 1.3634 0.3755 0.2162  -0.1709 -0.0383 80  CYS   A CB   
634  S  SG   . CYS   A 81  ? 0.9476 1.4008 0.4507 0.2061  -0.1964 -0.0337 80  CYS   A SG   
635  N  N    . ARG   A 82  ? 0.8435 1.38   0.3054 0.2253  -0.1198 -0.0414 81  ARG   A N    
636  C  CA   . ARG   A 82  ? 0.8487 1.3931 0.285  0.233   -0.096  -0.0423 81  ARG   A CA   
637  C  C    . ARG   A 82  ? 0.8236 1.4143 0.2818 0.2587  -0.0949 -0.054  81  ARG   A C    
638  O  O    . ARG   A 82  ? 0.8319 1.4189 0.2703 0.283   -0.0889 -0.0626 81  ARG   A O    
639  C  CB   . ARG   A 82  ? 0.8662 1.4181 0.2898 0.1998  -0.0697 -0.0295 81  ARG   A CB   
640  C  CG   . ARG   A 82  ? 0.9394 1.4358 0.3247 0.1826  -0.062  -0.0185 81  ARG   A CG   
641  C  CD   . ARG   A 82  ? 0.9859 1.484  0.361  0.1453  -0.0369 -0.0072 81  ARG   A CD   
642  N  NE   . ARG   A 82  ? 1.0557 1.4959 0.3948 0.1291  -0.0302 0.0036  81  ARG   A NE   
643  C  CZ   . ARG   A 82  ? 1.0978 1.525  0.4378 0.0948  -0.0262 0.0105  81  ARG   A CZ   
644  N  NH1  . ARG   A 82  ? 1.0747 1.5474 0.4511 0.0715  -0.0294 0.0078  81  ARG   A NH1  
645  N  NH2  . ARG   A 82  ? 1.1347 1.5053 0.4383 0.0847  -0.0187 0.0198  81  ARG   A NH2  
646  N  N    . LYS   A 83  ? 0.7921 1.4279 0.2904 0.2559  -0.1015 -0.0547 82  LYS   A N    
647  C  CA   . LYS   A 83  ? 0.7715 1.4537 0.2935 0.2839  -0.1013 -0.0655 82  LYS   A CA   
648  C  C    . LYS   A 83  ? 0.7741 1.4294 0.2934 0.3206  -0.1203 -0.0804 82  LYS   A C    
649  O  O    . LYS   A 83  ? 0.7626 1.4466 0.2954 0.3483  -0.1197 -0.0911 82  LYS   A O    
650  C  CB   . LYS   A 83  ? 0.7704 1.5107 0.3359 0.2747  -0.1052 -0.0614 82  LYS   A CB   
651  C  CG   . LYS   A 83  ? 0.8273 1.6056 0.397  0.2373  -0.0831 -0.0512 82  LYS   A CG   
652  C  CD   . LYS   A 83  ? 0.8627 1.7218 0.4767 0.2357  -0.0817 -0.0515 82  LYS   A CD   
653  C  CE   . LYS   A 83  ? 0.9007 1.8109 0.5193 0.2508  -0.0599 -0.0577 82  LYS   A CE   
654  N  NZ   . LYS   A 83  ? 0.8886 1.8876 0.5507 0.2443  -0.055  -0.0571 82  LYS   A NZ   
655  N  N    . LEU   A 84  ? 0.7901 1.3908 0.291  0.3199  -0.1359 -0.082  83  LEU   A N    
656  C  CA   . LEU   A 84  ? 0.8054 1.3736 0.2983 0.3473  -0.1527 -0.0976 83  LEU   A CA   
657  C  C    . LEU   A 84  ? 0.8408 1.3825 0.2931 0.357   -0.1455 -0.1056 83  LEU   A C    
658  O  O    . LEU   A 84  ? 0.8533 1.3774 0.2959 0.3804  -0.1555 -0.1224 83  LEU   A O    
659  C  CB   . LEU   A 84  ? 0.8079 1.3386 0.3106 0.3389  -0.1762 -0.0955 83  LEU   A CB   
660  C  CG   . LEU   A 84  ? 0.7925 1.3437 0.3315 0.3386  -0.1878 -0.0899 83  LEU   A CG   
661  C  CD1  . LEU   A 84  ? 0.8098 1.3178 0.3513 0.3303  -0.2087 -0.0871 83  LEU   A CD1  
662  C  CD2  . LEU   A 84  ? 0.7812 1.3561 0.3374 0.3724  -0.1895 -0.1019 83  LEU   A CD2  
663  N  N    . GLY   A 85  ? 0.8529 1.3917 0.2802 0.3397  -0.1278 -0.0937 84  GLY   A N    
664  C  CA   . GLY   A 85  ? 0.8808 1.3996 0.2673 0.3505  -0.1194 -0.0976 84  GLY   A CA   
665  C  C    . GLY   A 85  ? 0.9088 1.3871 0.2703 0.3361  -0.1244 -0.0887 84  GLY   A C    
666  O  O    . GLY   A 85  ? 0.9353 1.4003 0.2603 0.3448  -0.1156 -0.088  84  GLY   A O    
667  N  N    . ALA   A 86  ? 0.9039 1.3643 0.283  0.3164  -0.1382 -0.0813 85  ALA   A N    
668  C  CA   . ALA   A 86  ? 0.9256 1.3497 0.2835 0.3037  -0.1433 -0.073  85  ALA   A CA   
669  C  C    . ALA   A 86  ? 0.9356 1.3503 0.2671 0.2849  -0.1199 -0.0544 85  ALA   A C    
670  O  O    . ALA   A 86  ? 0.927  1.3621 0.2663 0.2699  -0.1024 -0.0462 85  ALA   A O    
671  C  CB   . ALA   A 86  ? 0.9249 1.3332 0.3092 0.2889  -0.1641 -0.071  85  ALA   A CB   
672  N  N    . THR   A 87  ? 0.9532 1.3372 0.2517 0.2867  -0.1185 -0.0486 86  THR   A N    
673  C  CA   . THR   A 87  ? 0.9783 1.3401 0.2447 0.2717  -0.096  -0.0302 86  THR   A CA   
674  C  C    . THR   A 87  ? 0.9825 1.3259 0.2655 0.2452  -0.1046 -0.0217 86  THR   A C    
675  O  O    . THR   A 87  ? 0.9897 1.3178 0.2791 0.2481  -0.1251 -0.0258 86  THR   A O    
676  C  CB   . THR   A 87  ? 1.0209 1.3599 0.2449 0.2917  -0.0937 -0.028  86  THR   A CB   
677  O  OG1  . THR   A 87  ? 1.0364 1.3938 0.2398 0.3162  -0.0834 -0.0348 86  THR   A OG1  
678  C  CG2  . THR   A 87  ? 1.0495 1.3525 0.2382 0.2784  -0.0743 -0.0077 86  THR   A CG2  
679  N  N    . VAL   A 88  ? 0.9758 1.3244 0.2682 0.218   -0.0903 -0.0118 87  VAL   A N    
680  C  CA   . VAL   A 88  ? 0.9798 1.3138 0.2878 0.1917  -0.0992 -0.005  87  VAL   A CA   
681  C  C    . VAL   A 88  ? 1.0046 1.3087 0.2825 0.1666  -0.0751 0.0104  87  VAL   A C    
682  O  O    . VAL   A 88  ? 1.0112 1.3239 0.2783 0.1542  -0.051  0.0153  87  VAL   A O    
683  C  CB   . VAL   A 88  ? 0.9593 1.3297 0.3139 0.1797  -0.1122 -0.0104 87  VAL   A CB   
684  C  CG1  . VAL   A 88  ? 0.9668 1.3214 0.3355 0.1585  -0.1265 -0.0049 87  VAL   A CG1  
685  C  CG2  . VAL   A 88  ? 0.9483 1.3436 0.3282 0.2072  -0.1308 -0.0255 87  VAL   A CG2  
686  N  N    . HIS   A 89  ? 1.0183 1.2857 0.281  0.1583  -0.08   0.0175  88  HIS   A N    
687  C  CA   . HIS   A 89  ? 1.0468 1.2766 0.2768 0.1351  -0.0568 0.0313  88  HIS   A CA   
688  C  C    . HIS   A 89  ? 1.0355 1.2542 0.2828 0.1114  -0.0702 0.0333  88  HIS   A C    
689  O  O    . HIS   A 89  ? 1.0306 1.2407 0.2858 0.1223  -0.0912 0.0308  88  HIS   A O    
690  C  CB   . HIS   A 89  ? 1.102  1.2911 0.282  0.1561  -0.0434 0.0402  88  HIS   A CB   
691  C  CG   . HIS   A 89  ? 1.1602 1.3613 0.3197 0.1826  -0.0317 0.0386  88  HIS   A CG   
692  N  ND1  . HIS   A 89  ? 1.195  1.3996 0.3424 0.2168  -0.0448 0.0334  88  HIS   A ND1  
693  C  CD2  . HIS   A 89  ? 1.18   1.3931 0.3292 0.1783  -0.0084 0.041   88  HIS   A CD2  
694  C  CE1  . HIS   A 89  ? 1.2054 1.4224 0.3337 0.2336  -0.0296 0.0331  88  HIS   A CE1  
695  N  NE2  . HIS   A 89  ? 1.2022 1.4238 0.3309 0.2118  -0.0068 0.0381  88  HIS   A NE2  
696  N  N    . THR   A 90  ? 1.0286 1.252  0.2833 0.0778  -0.0587 0.0366  89  THR   A N    
697  C  CA   . THR   A 90  ? 1.0299 1.2488 0.3015 0.0532  -0.0713 0.0376  89  THR   A CA   
698  C  C    . THR   A 90  ? 1.0594 1.2277 0.2927 0.0299  -0.0515 0.0474  89  THR   A C    
699  O  O    . THR   A 90  ? 1.0821 1.2225 0.2786 0.0231  -0.0227 0.0538  89  THR   A O    
700  C  CB   . THR   A 90  ? 1.0192 1.289  0.332  0.0321  -0.0781 0.0317  89  THR   A CB   
701  O  OG1  . THR   A 90  ? 1.0336 1.31   0.3332 0.0076  -0.0504 0.034   89  THR   A OG1  
702  C  CG2  . THR   A 90  ? 0.9992 1.3147 0.3493 0.0574  -0.0978 0.0224  89  THR   A CG2  
703  N  N    . PHE   A 91  ? 1.0572 1.2118 0.2977 0.0168  -0.0658 0.0486  90  PHE   A N    
704  C  CA   . PHE   A 91  ? 1.0858 1.1911 0.2917 -0.0047 -0.0503 0.0561  90  PHE   A CA   
705  C  C    . PHE   A 91  ? 1.0626 1.1827 0.294  -0.0323 -0.0659 0.053   90  PHE   A C    
706  O  O    . PHE   A 91  ? 1.0446 1.1878 0.3072 -0.0209 -0.0932 0.0497  90  PHE   A O    
707  C  CB   . PHE   A 91  ? 1.1155 1.1796 0.2916 0.022   -0.0521 0.0626  90  PHE   A CB   
708  C  CG   . PHE   A 91  ? 1.1452 1.2013 0.2975 0.0558  -0.0429 0.0656  90  PHE   A CG   
709  C  CD1  . PHE   A 91  ? 1.1877 1.2068 0.2939 0.0563  -0.011  0.0744  90  PHE   A CD1  
710  C  CD2  . PHE   A 91  ? 1.146  1.2309 0.3196 0.0863  -0.0655 0.0592  90  PHE   A CD2  
711  C  CE1  . PHE   A 91  ? 1.2096 1.2244 0.2917 0.0895  -0.0027 0.0783  90  PHE   A CE1  
712  C  CE2  . PHE   A 91  ? 1.1685 1.2516 0.3193 0.117   -0.0579 0.0606  90  PHE   A CE2  
713  C  CZ   . PHE   A 91  ? 1.1911 1.2407 0.2961 0.1199  -0.0272 0.071   90  PHE   A CZ   
714  N  N    . VAL   A 92  ? 1.0644 1.1693 0.2801 -0.0688 -0.0481 0.0537  91  VAL   A N    
715  C  CA   . VAL   A 92  ? 1.0552 1.174  0.2899 -0.0957 -0.0623 0.0505  91  VAL   A CA   
716  C  C    . VAL   A 92  ? 1.0784 1.1472 0.2859 -0.0908 -0.0642 0.0562  91  VAL   A C    
717  O  O    . VAL   A 92  ? 1.1149 1.1299 0.2774 -0.1006 -0.0397 0.0609  91  VAL   A O    
718  C  CB   . VAL   A 92  ? 1.0615 1.1907 0.2918 -0.1399 -0.0444 0.0459  91  VAL   A CB   
719  C  CG1  . VAL   A 92  ? 1.0539 1.1959 0.2981 -0.1663 -0.0594 0.0425  91  VAL   A CG1  
720  C  CG2  . VAL   A 92  ? 1.0401 1.2303 0.3033 -0.144  -0.0441 0.04    91  VAL   A CG2  
721  N  N    . VAL   A 93  ? 1.0551 1.1392 0.2876 -0.0733 -0.0918 0.0562  92  VAL   A N    
722  C  CA   . VAL   A 93  ? 1.0667 1.1117 0.2781 -0.0654 -0.0954 0.0615  92  VAL   A CA   
723  C  C    . VAL   A 93  ? 1.0403 1.1044 0.2769 -0.0802 -0.1176 0.06    92  VAL   A C    
724  O  O    . VAL   A 93  ? 1.0091 1.1153 0.2855 -0.072  -0.1415 0.0571  92  VAL   A O    
725  C  CB   . VAL   A 93  ? 1.0743 1.1133 0.2842 -0.0257 -0.1047 0.0642  92  VAL   A CB   
726  C  CG1  . VAL   A 93  ? 1.1024 1.1025 0.2858 -0.0172 -0.1029 0.0703  92  VAL   A CG1  
727  C  CG2  . VAL   A 93  ? 1.0844 1.116  0.2742 -0.0065 -0.0869 0.0655  92  VAL   A CG2  
728  N  N    . ASP   A 94  ? 1.0552 1.0852 0.2658 -0.0994 -0.1092 0.0625  93  ASP   A N    
729  C  CA   . ASP   A 94  ? 1.0476 1.0919 0.2763 -0.112  -0.1291 0.0624  93  ASP   A CA   
730  C  C    . ASP   A 94  ? 1.0428 1.0804 0.2789 -0.0824 -0.1452 0.0668  93  ASP   A C    
731  O  O    . ASP   A 94  ? 1.0666 1.0656 0.2728 -0.0743 -0.1352 0.0713  93  ASP   A O    
732  C  CB   . ASP   A 94  ? 1.0974 1.1031 0.2902 -0.1409 -0.1122 0.0624  93  ASP   A CB   
733  C  CG   . ASP   A 94  ? 1.1395 1.1604 0.3459 -0.1573 -0.1305 0.062   93  ASP   A CG   
734  O  OD1  . ASP   A 94  ? 1.1266 1.1918 0.3727 -0.1498 -0.1561 0.0625  93  ASP   A OD1  
735  O  OD2  . ASP   A 94  ? 1.176  1.1622 0.3508 -0.177  -0.1181 0.0615  93  ASP   A OD2  
736  N  N    . CYS   A 95  ? 1.0103 1.0855 0.2851 -0.0659 -0.1687 0.065   94  CYS   A N    
737  C  CA   . CYS   A 95  ? 1.0052 1.079  0.2909 -0.0403 -0.1844 0.0667  94  CYS   A CA   
738  C  C    . CYS   A 95  ? 0.996  1.0602 0.2827 -0.0479 -0.196  0.0711  94  CYS   A C    
739  O  O    . CYS   A 95  ? 0.9962 1.0671 0.2995 -0.0327 -0.2119 0.0717  94  CYS   A O    
740  C  CB   . CYS   A 95  ? 0.9956 1.1052 0.3179 -0.0225 -0.2029 0.0618  94  CYS   A CB   
741  S  SG   . CYS   A 95  ? 1.0414 1.1652 0.3623 -0.0099 -0.1893 0.0563  94  CYS   A SG   
742  N  N    . GLY   A 96  ? 0.9844 1.0315 0.2508 -0.0722 -0.1861 0.0733  95  GLY   A N    
743  C  CA   . GLY   A 96  ? 0.9766 1.0104 0.2362 -0.0805 -0.1924 0.0778  95  GLY   A CA   
744  C  C    . GLY   A 96  ? 0.9893 0.9779 0.205  -0.0819 -0.1698 0.0805  95  GLY   A C    
745  O  O    . GLY   A 96  ? 0.9864 0.9613 0.1932 -0.0777 -0.1724 0.0846  95  GLY   A O    
746  N  N    . ASN   A 97  ? 1.0023 0.9659 0.1884 -0.0871 -0.1457 0.0787  96  ASN   A N    
747  C  CA   . ASN   A 97  ? 1.0353 0.947  0.1725 -0.0867 -0.1188 0.0816  96  ASN   A CA   
748  C  C    . ASN   A 97  ? 1.042  0.9388 0.1646 -0.0512 -0.1113 0.0864  96  ASN   A C    
749  O  O    . ASN   A 97  ? 1.0356 0.941  0.1616 -0.0372 -0.1075 0.0855  96  ASN   A O    
750  C  CB   . ASN   A 97  ? 1.0611 0.9505 0.1725 -0.1112 -0.0955 0.0775  96  ASN   A CB   
751  C  CG   . ASN   A 97  ? 1.1371 0.9633 0.193  -0.1152 -0.0657 0.0801  96  ASN   A CG   
752  O  OD1  . ASN   A 97  ? 1.1698 0.9616 0.1937 -0.1136 -0.0407 0.0811  96  ASN   A OD1  
753  N  ND2  . ASN   A 97  ? 1.1566 0.9628 0.197  -0.1193 -0.0662 0.0818  96  ASN   A ND2  
754  N  N    . ARG   A 98  ? 1.0531 0.9312 0.1586 -0.0363 -0.1089 0.0914  97  ARG   A N    
755  C  CA   . ARG   A 98  ? 1.0644 0.9364 0.1565 -0.001  -0.1041 0.0964  97  ARG   A CA   
756  C  C    . ARG   A 98  ? 1.0981 0.9306 0.1467 0.0131  -0.0758 0.1007  97  ARG   A C    
757  O  O    . ARG   A 98  ? 1.0961 0.9411 0.1456 0.0402  -0.076  0.1024  97  ARG   A O    
758  C  CB   . ARG   A 98  ? 1.0893 0.9518 0.1707 0.0064  -0.105  0.1009  97  ARG   A CB   
759  C  CG   . ARG   A 98  ? 1.1257 1.0001 0.204  0.0429  -0.1064 0.105   97  ARG   A CG   
760  C  CD   . ARG   A 98  ? 1.1676 1.0354 0.2342 0.0498  -0.1043 0.1096  97  ARG   A CD   
761  N  NE   . ARG   A 98  ? 1.2415 1.0545 0.2599 0.0423  -0.0777 0.1138  97  ARG   A NE   
762  C  CZ   . ARG   A 98  ? 1.311  1.0856 0.284  0.0671  -0.0527 0.1206  97  ARG   A CZ   
763  N  NH1  . ARG   A 98  ? 1.3031 1.0949 0.2741 0.1026  -0.0523 0.1249  97  ARG   A NH1  
764  N  NH2  . ARG   A 98  ? 1.3614 1.0792 0.2885 0.0575  -0.0274 0.123   97  ARG   A NH2  
765  N  N    . GLU   A 99  ? 1.1289 0.912  0.137  -0.0056 -0.0506 0.1021  98  GLU   A N    
766  C  CA   . GLU   A 99  ? 1.1671 0.9023 0.1276 0.0062  -0.0199 0.1076  98  GLU   A CA   
767  C  C    . GLU   A 99  ? 1.1609 0.9095 0.1318 -0.0029 -0.0162 0.1041  98  GLU   A C    
768  O  O    . GLU   A 99  ? 1.1777 0.9006 0.118  0.016   0.0038  0.11    98  GLU   A O    
769  C  CB   . GLU   A 99  ? 1.2359 0.9055 0.1447 -0.0115 0.0087  0.1094  98  GLU   A CB   
770  C  CG   . GLU   A 99  ? 1.3093 0.9614 0.1999 0.0066  0.0102  0.1146  98  GLU   A CG   
771  C  CD   . GLU   A 99  ? 1.4193 1.0075 0.2609 -0.0129 0.036   0.1139  98  GLU   A CD   
772  O  OE1  . GLU   A 99  ? 1.4219 1.0173 0.2719 -0.0267 0.0261  0.1103  98  GLU   A OE1  
773  O  OE2  . GLU   A 99  ? 1.4808 1.009  0.2733 -0.0152 0.0674  0.1166  98  GLU   A OE2  
774  N  N    . ASP   A 100 ? 1.1362 0.9273 0.1495 -0.0291 -0.0349 0.0954  99  ASP   A N    
775  C  CA   . ASP   A 100 ? 1.1327 0.9465 0.1617 -0.0366 -0.0332 0.0914  99  ASP   A CA   
776  C  C    . ASP   A 100 ? 1.1175 0.9726 0.1757 -0.0034 -0.052  0.0916  99  ASP   A C    
777  O  O    . ASP   A 100 ? 1.1265 0.98   0.1736 0.0107  -0.0405 0.0933  99  ASP   A O    
778  C  CB   . ASP   A 100 ? 1.1291 0.9794 0.1934 -0.0737 -0.0466 0.0821  99  ASP   A CB   
779  C  CG   . ASP   A 100 ? 1.1691 1.0358 0.2403 -0.0898 -0.0361 0.0776  99  ASP   A CG   
780  O  OD1  . ASP   A 100 ? 1.1908 1.0425 0.2425 -0.0705 -0.0202 0.0818  99  ASP   A OD1  
781  O  OD2  . ASP   A 100 ? 1.1654 1.0632 0.261  -0.1211 -0.0436 0.0701  99  ASP   A OD2  
782  N  N    . ILE   A 101 ? 1.0932 0.9834 0.1862 0.0078  -0.0796 0.0893  100 ILE   A N    
783  C  CA   . ILE   A 101 ? 1.0786 1.0067 0.1987 0.0362  -0.0983 0.0868  100 ILE   A CA   
784  C  C    . ILE   A 101 ? 1.114  1.0222 0.1991 0.0707  -0.0832 0.0935  100 ILE   A C    
785  O  O    . ILE   A 101 ? 1.1144 1.0365 0.1996 0.0879  -0.0812 0.0922  100 ILE   A O    
786  C  CB   . ILE   A 101 ? 1.0564 1.0166 0.2142 0.0376  -0.1269 0.0831  100 ILE   A CB   
787  C  CG1  . ILE   A 101 ? 1.0438 1.0304 0.2381 0.0109  -0.1437 0.0776  100 ILE   A CG1  
788  C  CG2  . ILE   A 101 ? 1.0472 1.0385 0.2246 0.0667  -0.1429 0.0791  100 ILE   A CG2  
789  C  CD1  . ILE   A 101 ? 1.0413 1.0459 0.2631 0.0074  -0.1667 0.0769  100 ILE   A CD1  
790  N  N    . TYR   A 102 ? 1.1415 1.0172 0.1937 0.082   -0.0711 0.1012  101 TYR   A N    
791  C  CA   . TYR   A 102 ? 1.1691 1.0268 0.1844 0.1186  -0.0562 0.1098  101 TYR   A CA   
792  C  C    . TYR   A 102 ? 1.2014 1.0205 0.1753 0.1229  -0.0272 0.1163  101 TYR   A C    
793  O  O    . TYR   A 102 ? 1.208  1.0324 0.1654 0.154   -0.0216 0.1209  101 TYR   A O    
794  C  CB   . TYR   A 102 ? 1.1907 1.0209 0.1785 0.1296  -0.0474 0.1174  101 TYR   A CB   
795  C  CG   . TYR   A 102 ? 1.1737 1.0454 0.1985 0.1322  -0.0739 0.1127  101 TYR   A CG   
796  C  CD1  . TYR   A 102 ? 1.1533 1.0796 0.2229 0.1383  -0.1011 0.104   101 TYR   A CD1  
797  C  CD2  . TYR   A 102 ? 1.1896 1.0436 0.2017 0.1291  -0.0698 0.1168  101 TYR   A CD2  
798  C  CE1  . TYR   A 102 ? 1.1395 1.1    0.241  0.1376  -0.1231 0.0996  101 TYR   A CE1  
799  C  CE2  . TYR   A 102 ? 1.1762 1.069  0.2213 0.1303  -0.0921 0.1133  101 TYR   A CE2  
800  C  CZ   . TYR   A 102 ? 1.1561 1.1013 0.2462 0.1329  -0.1185 0.1047  101 TYR   A CZ   
801  O  OH   . TYR   A 102 ? 1.1538 1.1344 0.2755 0.1306  -0.1387 0.1008  101 TYR   A OH   
802  N  N    . ASN   A 103 ? 1.2198 1.0027 0.1769 0.0904  -0.0087 0.1161  102 ASN   A N    
803  C  CA   . ASN   A 103 ? 1.2573 0.9997 0.1747 0.0869  0.0215  0.1217  102 ASN   A CA   
804  C  C    . ASN   A 103 ? 1.2385 1.0227 0.1828 0.0909  0.0128  0.1165  102 ASN   A C    
805  O  O    . ASN   A 103 ? 1.2583 1.0261 0.1723 0.1121  0.0306  0.1236  102 ASN   A O    
806  C  CB   . ASN   A 103 ? 1.2945 0.9982 0.1959 0.0433  0.0398  0.1185  102 ASN   A CB   
807  C  CG   . ASN   A 103 ? 1.388  1.0146 0.2229 0.0434  0.0799  0.1284  102 ASN   A CG   
808  O  OD1  . ASN   A 103 ? 1.4154 1.0209 0.2218 0.0564  0.1004  0.1353  102 ASN   A OD1  
809  N  ND2  . ASN   A 103 ? 1.4258 1.0051 0.2316 0.0282  0.0931  0.1292  102 ASN   A ND2  
810  N  N    . SER   A 104 ? 1.2009 1.0379 0.1996 0.0735  -0.0139 0.1049  103 SER   A N    
811  C  CA   . SER   A 104 ? 1.1843 1.0639 0.2119 0.0775  -0.0235 0.0984  103 SER   A CA   
812  C  C    . SER   A 104 ? 1.1729 1.0863 0.2128 0.1161  -0.0408 0.0967  103 SER   A C    
813  O  O    . SER   A 104 ? 1.1585 1.0938 0.204  0.1281  -0.0403 0.0937  103 SER   A O    
814  C  CB   . SER   A 104 ? 1.1731 1.0942 0.2508 0.0479  -0.0441 0.0873  103 SER   A CB   
815  O  OG   . SER   A 104 ? 1.2158 1.1148 0.283  0.0102  -0.0284 0.0869  103 SER   A OG   
816  N  N    . VAL   A 105 ? 1.1751 1.0951 0.2186 0.1344  -0.0553 0.0977  104 VAL   A N    
817  C  CA   . VAL   A 105 ? 1.1698 1.1241 0.2225 0.1691  -0.0714 0.0946  104 VAL   A CA   
818  C  C    . VAL   A 105 ? 1.1895 1.1199 0.1929 0.1996  -0.0476 0.1053  104 VAL   A C    
819  O  O    . VAL   A 105 ? 1.1786 1.1364 0.1851 0.2201  -0.0523 0.1016  104 VAL   A O    
820  C  CB   . VAL   A 105 ? 1.1754 1.1445 0.2424 0.1777  -0.09   0.0932  104 VAL   A CB   
821  C  CG1  . VAL   A 105 ? 1.1795 1.177  0.2399 0.2156  -0.0984 0.0925  104 VAL   A CG1  
822  C  CG2  . VAL   A 105 ? 1.1521 1.1532 0.2708 0.1542  -0.1171 0.0819  104 VAL   A CG2  
823  N  N    . LYS   A 106 ? 1.2185 1.0942 0.1735 0.2018  -0.0202 0.1189  105 LYS   A N    
824  C  CA   . LYS   A 106 ? 1.2486 1.0913 0.1499 0.231   0.0063  0.1323  105 LYS   A CA   
825  C  C    . LYS   A 106 ? 1.2504 1.0858 0.1422 0.221   0.0228  0.1325  105 LYS   A C    
826  O  O    . LYS   A 106 ? 1.264  1.0974 0.1266 0.2502  0.0344  0.1396  105 LYS   A O    
827  C  CB   . LYS   A 106 ? 1.3142 1.0919 0.1632 0.2356  0.0336  0.1469  105 LYS   A CB   
828  C  CG   . LYS   A 106 ? 1.3615 1.1533 0.2131 0.2584  0.02    0.1491  105 LYS   A CG   
829  C  CD   . LYS   A 106 ? 1.4536 1.1802 0.2476 0.2725  0.0492  0.1647  105 LYS   A CD   
830  C  CE   . LYS   A 106 ? 1.4715 1.2117 0.2791 0.2778  0.0355  0.1635  105 LYS   A CE   
831  N  NZ   . LYS   A 106 ? 1.52   1.205  0.269  0.3054  0.0629  0.1795  105 LYS   A NZ   
832  N  N    . GLN   A 107 ? 1.2365 1.074  0.1537 0.1813  0.0231  0.1246  106 GLN   A N    
833  C  CA   . GLN   A 107 ? 1.2429 1.0852 0.1596 0.1687  0.0367  0.1228  106 GLN   A CA   
834  C  C    . GLN   A 107 ? 1.2016 1.108  0.1592 0.185   0.0114  0.111   106 GLN   A C    
835  O  O    . GLN   A 107 ? 1.1962 1.1107 0.1423 0.1953  0.0227  0.1121  106 GLN   A O    
836  C  CB   . GLN   A 107 ? 1.2759 1.1104 0.2106 0.1205  0.0435  0.1167  106 GLN   A CB   
837  C  CG   . GLN   A 107 ? 1.3397 1.1814 0.2728 0.1048  0.0612  0.1153  106 GLN   A CG   
838  C  CD   . GLN   A 107 ? 1.3965 1.2534 0.3594 0.0578  0.0619  0.106   106 GLN   A CD   
839  O  OE1  . GLN   A 107 ? 1.4146 1.2922 0.387  0.0431  0.0722  0.1025  106 GLN   A OE1  
840  N  NE2  . GLN   A 107 ? 1.3996 1.2507 0.3772 0.0333  0.0517  0.1018  106 GLN   A NE2  
841  N  N    . VAL   A 108 ? 1.1703 1.119  0.1733 0.1866  -0.0215 0.0994  107 VAL   A N    
842  C  CA   . VAL   A 108 ? 1.1399 1.1431 0.1798 0.2019  -0.0465 0.0861  107 VAL   A CA   
843  C  C    . VAL   A 108 ? 1.1406 1.1509 0.1507 0.2433  -0.0443 0.0902  107 VAL   A C    
844  O  O    . VAL   A 108 ? 1.1383 1.1748 0.1515 0.2579  -0.0464 0.0843  107 VAL   A O    
845  C  CB   . VAL   A 108 ? 1.1255 1.1609 0.215  0.191   -0.0791 0.074   107 VAL   A CB   
846  C  CG1  . VAL   A 108 ? 1.1123 1.1918 0.2261 0.2152  -0.1039 0.0613  107 VAL   A CG1  
847  C  CG2  . VAL   A 108 ? 1.1135 1.1604 0.2389 0.1567  -0.0852 0.0676  107 VAL   A CG2  
848  N  N    . LYS   A 109 ? 1.1473 1.1364 0.1267 0.2635  -0.0391 0.1003  108 LYS   A N    
849  C  CA   . LYS   A 109 ? 1.1508 1.1514 0.0994 0.3054  -0.037  0.1056  108 LYS   A CA   
850  C  C    . LYS   A 109 ? 1.1855 1.1485 0.0797 0.3207  -0.0037 0.1211  108 LYS   A C    
851  O  O    . LYS   A 109 ? 1.1889 1.1725 0.0638 0.3524  -0.0029 0.1225  108 LYS   A O    
852  C  CB   . LYS   A 109 ? 1.1708 1.1715 0.1093 0.3243  -0.0446 0.1109  108 LYS   A CB   
853  C  CG   . LYS   A 109 ? 1.1908 1.231  0.1836 0.3077  -0.077  0.0951  108 LYS   A CG   
854  C  CD   . LYS   A 109 ? 1.2391 1.2951 0.229  0.3272  -0.0876 0.0974  108 LYS   A CD   
855  C  CE   . LYS   A 109 ? 1.25   1.3473 0.2937 0.3095  -0.119  0.0806  108 LYS   A CE   
856  N  NZ   . LYS   A 109 ? 1.2632 1.387  0.3079 0.3278  -0.1301 0.0809  108 LYS   A NZ   
857  N  N    . LYS   A 110 ? 1.2091 1.1181 0.0784 0.296   0.0242  0.1317  109 LYS   A N    
858  C  CA   . LYS   A 110 ? 1.2475 1.113  0.0644 0.3032  0.0595  0.1466  109 LYS   A CA   
859  C  C    . LYS   A 110 ? 1.2358 1.1249 0.073  0.2849  0.0631  0.1381  109 LYS   A C    
860  O  O    . LYS   A 110 ? 1.2695 1.1274 0.0669 0.2872  0.0928  0.1494  109 LYS   A O    
861  C  CB   . LYS   A 110 ? 1.2949 1.0862 0.0707 0.2831  0.091   0.1608  109 LYS   A CB   
862  C  CG   . LYS   A 110 ? 1.3717 1.1041 0.0794 0.3119  0.1265  0.1818  109 LYS   A CG   
863  C  CD   . LYS   A 110 ? 1.4514 1.1364 0.1238 0.2841  0.1621  0.1895  109 LYS   A CD   
864  C  CE   . LYS   A 110 ? 1.548  1.1927 0.1541 0.3186  0.1935  0.2096  109 LYS   A CE   
865  N  NZ   . LYS   A 110 ? 1.5527 1.2536 0.1705 0.3437  0.1819  0.2056  109 LYS   A NZ   
866  N  N    . GLU   A 111 ? 1.1866 1.1297 0.0834 0.2683  0.0347  0.1192  110 GLU   A N    
867  C  CA   . GLU   A 111 ? 1.1639 1.1348 0.0819 0.2548  0.0375  0.1107  110 GLU   A CA   
868  C  C    . GLU   A 111 ? 1.1202 1.1533 0.0779 0.2727  0.0076  0.0933  110 GLU   A C    
869  O  O    . GLU   A 111 ? 1.1198 1.1714 0.0662 0.2903  0.0141  0.0916  110 GLU   A O    
870  C  CB   . GLU   A 111 ? 1.1819 1.1479 0.1281 0.2085  0.0428  0.106   110 GLU   A CB   
871  C  CG   . GLU   A 111 ? 1.2663 1.1852 0.1715 0.188   0.082   0.1186  110 GLU   A CG   
872  C  CD   . GLU   A 111 ? 1.3243 1.2675 0.2633 0.1483  0.0865  0.1096  110 GLU   A CD   
873  O  OE1  . GLU   A 111 ? 1.346  1.29   0.2693 0.1437  0.1093  0.1129  110 GLU   A OE1  
874  O  OE2  . GLU   A 111 ? 1.3294 1.2946 0.3108 0.1227  0.0673  0.0995  110 GLU   A OE2  
875  N  N    . VAL   A 112 ? 1.0838 1.146  0.0851 0.2675  -0.0235 0.0801  111 VAL   A N    
876  C  CA   . VAL   A 112 ? 1.0534 1.167  0.0914 0.2812  -0.0516 0.0617  111 VAL   A CA   
877  C  C    . VAL   A 112 ? 1.0553 1.1858 0.0795 0.3151  -0.0668 0.0588  111 VAL   A C    
878  O  O    . VAL   A 112 ? 1.0457 1.2054 0.0638 0.3396  -0.0727 0.0506  111 VAL   A O    
879  C  CB   . VAL   A 112 ? 1.03   1.1647 0.1233 0.2541  -0.0749 0.0485  111 VAL   A CB   
880  C  CG1  . VAL   A 112 ? 1.0108 1.1877 0.1382 0.2684  -0.1043 0.0292  111 VAL   A CG1  
881  C  CG2  . VAL   A 112 ? 1.0288 1.1651 0.1385 0.2264  -0.062  0.0486  111 VAL   A CG2  
882  N  N    . GLY   A 113 ? 1.0632 1.1778 0.0809 0.3162  -0.0717 0.0652  112 GLY   A N    
883  C  CA   . GLY   A 113 ? 1.0686 1.2055 0.0766 0.3455  -0.0864 0.0627  112 GLY   A CA   
884  C  C    . GLY   A 113 ? 1.0619 1.21   0.1038 0.3318  -0.1095 0.0553  112 GLY   A C    
885  O  O    . GLY   A 113 ? 1.0721 1.1919 0.1225 0.3068  -0.1047 0.0618  112 GLY   A O    
886  N  N    . ASP   A 114 ? 1.0424 1.2328 0.1039 0.3457  -0.1343 0.0407  113 ASP   A N    
887  C  CA   . ASP   A 114 ? 1.0326 1.2366 0.1266 0.3319  -0.1558 0.033   113 ASP   A CA   
888  C  C    . ASP   A 114 ? 1.0066 1.2293 0.1503 0.3082  -0.1778 0.0138  113 ASP   A C    
889  O  O    . ASP   A 114 ? 0.9963 1.2483 0.1521 0.3174  -0.1902 -0.0025 113 ASP   A O    
890  C  CB   . ASP   A 114 ? 1.0479 1.2889 0.133  0.3589  -0.1685 0.0285  113 ASP   A CB   
891  C  CG   . ASP   A 114 ? 1.124  1.3516 0.1572 0.3907  -0.1477 0.048   113 ASP   A CG   
892  O  OD1  . ASP   A 114 ? 1.1623 1.3412 0.1689 0.3858  -0.1243 0.0668  113 ASP   A OD1  
893  O  OD2  . ASP   A 114 ? 1.1383 1.4041 0.1562 0.421   -0.1547 0.0441  113 ASP   A OD2  
894  N  N    . VAL   A 115 ? 0.9965 1.2009 0.166  0.2794  -0.1821 0.0158  114 VAL   A N    
895  C  CA   . VAL   A 115 ? 0.9767 1.1937 0.1899 0.2596  -0.2014 0.0008  114 VAL   A CA   
896  C  C    . VAL   A 115 ? 0.9553 1.2042 0.1905 0.265   -0.226  -0.0175 114 VAL   A C    
897  O  O    . VAL   A 115 ? 0.9558 1.2152 0.1855 0.2705  -0.2313 -0.0159 114 VAL   A O    
898  C  CB   . VAL   A 115 ? 0.986  1.1785 0.218  0.2299  -0.2009 0.0089  114 VAL   A CB   
899  C  CG1  . VAL   A 115 ? 0.9709 1.1752 0.2455 0.2135  -0.2221 -0.0044 114 VAL   A CG1  
900  C  CG2  . VAL   A 115 ? 1.0068 1.1737 0.2215 0.2194  -0.1779 0.0217  114 VAL   A CG2  
901  N  N    . THR   A 116 ? 0.9351 1.2004 0.1928 0.2644  -0.2393 -0.0357 115 THR   A N    
902  C  CA   . THR   A 116 ? 0.9178 1.209  0.1947 0.2656  -0.2613 -0.0563 115 THR   A CA   
903  C  C    . THR   A 116 ? 0.8999 1.1805 0.2144 0.2418  -0.2772 -0.0659 115 THR   A C    
904  O  O    . THR   A 116 ? 0.8919 1.1861 0.222  0.2365  -0.2937 -0.0816 115 THR   A O    
905  C  CB   . THR   A 116 ? 0.9299 1.2472 0.1955 0.2872  -0.2645 -0.0731 115 THR   A CB   
906  O  OG1  . THR   A 116 ? 0.9391 1.2483 0.219  0.2837  -0.2644 -0.0817 115 THR   A OG1  
907  C  CG2  . THR   A 116 ? 0.9475 1.2734 0.1726 0.3133  -0.2476 -0.0617 115 THR   A CG2  
908  N  N    . ILE   A 117 ? 0.8912 1.1491 0.2187 0.2281  -0.2717 -0.0571 116 ILE   A N    
909  C  CA   . ILE   A 117 ? 0.8813 1.126  0.2406 0.2089  -0.2848 -0.0619 116 ILE   A CA   
910  C  C    . ILE   A 117 ? 0.882  1.1065 0.2447 0.1922  -0.2758 -0.0425 116 ILE   A C    
911  O  O    . ILE   A 117 ? 0.8897 1.1107 0.2417 0.1944  -0.2609 -0.0333 116 ILE   A O    
912  C  CB   . ILE   A 117 ? 0.8806 1.1269 0.2548 0.2152  -0.2903 -0.0768 116 ILE   A CB   
913  C  CG1  . ILE   A 117 ? 0.8866 1.1498 0.2577 0.228   -0.3008 -0.1    116 ILE   A CG1  
914  C  CG2  . ILE   A 117 ? 0.8827 1.1101 0.2852 0.1988  -0.2999 -0.0757 116 ILE   A CG2  
915  C  CD1  . ILE   A 117 ? 0.8989 1.1623 0.2768 0.2392  -0.3025 -0.1154 116 ILE   A CD1  
916  N  N    . LEU   A 118 ? 0.8716 1.0843 0.2484 0.1739  -0.2841 -0.037  117 LEU   A N    
917  C  CA   . LEU   A 118 ? 0.8684 1.064  0.2478 0.1565  -0.2772 -0.0202 117 LEU   A CA   
918  C  C    . LEU   A 118 ? 0.8506 1.038  0.2586 0.143   -0.2897 -0.0215 117 LEU   A C    
919  O  O    . LEU   A 118 ? 0.8482 1.0323 0.2716 0.1397  -0.304  -0.0308 117 LEU   A O    
920  C  CB   . LEU   A 118 ? 0.8748 1.0625 0.2415 0.1482  -0.2738 -0.0096 117 LEU   A CB   
921  C  CG   . LEU   A 118 ? 0.8978 1.0663 0.2638 0.1283  -0.2672 0.006   117 LEU   A CG   
922  C  CD1  . LEU   A 118 ? 0.9075 1.0688 0.2574 0.1272  -0.2492 0.0145  117 LEU   A CD1  
923  C  CD2  . LEU   A 118 ? 0.9154 1.0764 0.2672 0.1237  -0.2635 0.0143  117 LEU   A CD2  
924  N  N    . VAL   A 119 ? 0.8351 1.0202 0.2492 0.1355  -0.2837 -0.0125 118 VAL   A N    
925  C  CA   . VAL   A 119 ? 0.8213 1.0024 0.2601 0.1265  -0.2946 -0.0106 118 VAL   A CA   
926  C  C    . VAL   A 119 ? 0.8171 0.9915 0.2544 0.1064  -0.2902 0.0055  118 VAL   A C    
927  O  O    . VAL   A 119 ? 0.8208 1.004  0.2547 0.1011  -0.2797 0.012   118 VAL   A O    
928  C  CB   . VAL   A 119 ? 0.8208 1.0161 0.2718 0.1393  -0.2938 -0.0169 118 VAL   A CB   
929  C  CG1  . VAL   A 119 ? 0.8193 1.0126 0.2939 0.1341  -0.3044 -0.0124 118 VAL   A CG1  
930  C  CG2  . VAL   A 119 ? 0.8264 1.026  0.2756 0.1591  -0.2977 -0.0348 118 VAL   A CG2  
931  N  N    . ASN   A 120 ? 0.8053 0.9658 0.2434 0.0936  -0.2971 0.011   119 ASN   A N    
932  C  CA   . ASN   A 120 ? 0.7972 0.9501 0.231  0.0741  -0.2935 0.025   119 ASN   A CA   
933  C  C    . ASN   A 120 ? 0.7996 0.9571 0.2546 0.0671  -0.3036 0.03    119 ASN   A C    
934  O  O    . ASN   A 120 ? 0.8045 0.9512 0.2675 0.0577  -0.3137 0.0357  119 ASN   A O    
935  C  CB   . ASN   A 120 ? 0.7866 0.9261 0.2126 0.0654  -0.2963 0.0289  119 ASN   A CB   
936  C  CG   . ASN   A 120 ? 0.7772 0.9154 0.1787 0.0725  -0.2839 0.0286  119 ASN   A CG   
937  O  OD1  . ASN   A 120 ? 0.7726 0.913  0.1722 0.0773  -0.2883 0.0241  119 ASN   A OD1  
938  N  ND2  . ASN   A 120 ? 0.775  0.91   0.1561 0.073   -0.2675 0.034   119 ASN   A ND2  
939  N  N    . ASN   A 121 ? 0.7955 0.9715 0.2589 0.0731  -0.3004 0.0286  120 ASN   A N    
940  C  CA   . ASN   A 121 ? 0.7953 0.9846 0.2794 0.0725  -0.3096 0.0331  120 ASN   A CA   
941  C  C    . ASN   A 121 ? 0.8082 1.0043 0.29   0.0513  -0.3082 0.0458  120 ASN   A C    
942  O  O    . ASN   A 121 ? 0.8153 1.0058 0.306  0.0458  -0.3199 0.0532  120 ASN   A O    
943  C  CB   . ASN   A 121 ? 0.7932 1.0077 0.288  0.0884  -0.3056 0.0261  120 ASN   A CB   
944  C  CG   . ASN   A 121 ? 0.8038 1.0404 0.3208 0.093   -0.3142 0.0308  120 ASN   A CG   
945  O  OD1  . ASN   A 121 ? 0.8163 1.0454 0.3467 0.1089  -0.3255 0.028   120 ASN   A OD1  
946  N  ND2  . ASN   A 121 ? 0.7902 1.0559 0.3106 0.0802  -0.3081 0.0375  120 ASN   A ND2  
947  N  N    . ALA   A 122 ? 0.8095 1.0142 0.2761 0.038   -0.293  0.048   121 ALA   A N    
948  C  CA   . ALA   A 122 ? 0.809  1.0215 0.2692 0.0141  -0.2888 0.0566  121 ALA   A CA   
949  C  C    . ALA   A 122 ? 0.8107 1.0125 0.2735 0.0036  -0.3013 0.0655  121 ALA   A C    
950  O  O    . ALA   A 122 ? 0.824  1.0009 0.2823 0.0073  -0.3065 0.0662  121 ALA   A O    
951  C  CB   . ALA   A 122 ? 0.8245 1.0214 0.2554 0.0003  -0.2686 0.0567  121 ALA   A CB   
952  N  N    . GLY   A 123 ? 0.7942 1.019  0.2649 -0.0094 -0.3062 0.0718  122 GLY   A N    
953  C  CA   . GLY   A 123 ? 0.7938 1.0131 0.265  -0.0196 -0.3177 0.0817  122 GLY   A CA   
954  C  C    . GLY   A 123 ? 0.7849 1.0362 0.2578 -0.0382 -0.3188 0.0866  122 GLY   A C    
955  O  O    . GLY   A 123 ? 0.7697 1.0546 0.2513 -0.0409 -0.3137 0.0821  122 GLY   A O    
956  N  N    . THR   A 124 ? 0.7898 1.0341 0.2538 -0.0524 -0.3252 0.0952  123 THR   A N    
957  C  CA   . THR   A 124 ? 0.7846 1.0617 0.2484 -0.0714 -0.3289 0.0996  123 THR   A CA   
958  C  C    . THR   A 124 ? 0.7919 1.068  0.2597 -0.0679 -0.3459 0.1123  123 THR   A C    
959  O  O    . THR   A 124 ? 0.8062 1.046  0.2664 -0.0632 -0.3486 0.1172  123 THR   A O    
960  C  CB   . THR   A 124 ? 0.8066 1.0754 0.2436 -0.1006 -0.3116 0.0942  123 THR   A CB   
961  O  OG1  . THR   A 124 ? 0.7963 1.1099 0.2385 -0.1196 -0.3123 0.092   123 THR   A OG1  
962  C  CG2  . THR   A 124 ? 0.8335 1.0664 0.2459 -0.113  -0.3091 0.099   123 THR   A CG2  
963  N  N    . VAL   A 125 ? 0.7796 1.0986 0.2604 -0.0682 -0.3572 0.1181  124 VAL   A N    
964  C  CA   . VAL   A 125 ? 0.7955 1.1161 0.2775 -0.0622 -0.373  0.1324  124 VAL   A CA   
965  C  C    . VAL   A 125 ? 0.814  1.1783 0.2908 -0.0824 -0.378  0.1357  124 VAL   A C    
966  O  O    . VAL   A 125 ? 0.7922 1.2026 0.2785 -0.0916 -0.3753 0.1282  124 VAL   A O    
967  C  CB   . VAL   A 125 ? 0.7866 1.1117 0.2906 -0.0294 -0.3862 0.1397  124 VAL   A CB   
968  C  CG1  . VAL   A 125 ? 0.7642 1.1501 0.2894 -0.0189 -0.3928 0.1396  124 VAL   A CG1  
969  C  CG2  . VAL   A 125 ? 0.8    1.1002 0.2972 -0.0215 -0.3979 0.1556  124 VAL   A CG2  
970  N  N    . TYR   A 126 ? 0.8504 1.2022 0.3111 -0.0913 -0.3847 0.1462  125 TYR   A N    
971  C  CA   . TYR   A 126 ? 0.8671 1.2594 0.3193 -0.1105 -0.3911 0.1494  125 TYR   A CA   
972  C  C    . TYR   A 126 ? 0.8972 1.2896 0.3489 -0.0942 -0.4079 0.1682  125 TYR   A C    
973  O  O    . TYR   A 126 ? 0.9209 1.2844 0.3511 -0.1046 -0.4078 0.1754  125 TYR   A O    
974  C  CB   . TYR   A 126 ? 0.886  1.2551 0.3081 -0.1433 -0.3771 0.1412  125 TYR   A CB   
975  C  CG   . TYR   A 126 ? 0.9028 1.2666 0.3205 -0.1588 -0.3583 0.1244  125 TYR   A CG   
976  C  CD1  . TYR   A 126 ? 0.8937 1.3076 0.323  -0.1713 -0.3559 0.1148  125 TYR   A CD1  
977  C  CD2  . TYR   A 126 ? 0.9391 1.2499 0.3416 -0.1589 -0.3426 0.1191  125 TYR   A CD2  
978  C  CE1  . TYR   A 126 ? 0.9105 1.315  0.333  -0.1862 -0.3365 0.1007  125 TYR   A CE1  
979  C  CE2  . TYR   A 126 ? 0.9585 1.2599 0.3525 -0.1704 -0.324  0.106   125 TYR   A CE2  
980  C  CZ   . TYR   A 126 ? 0.9541 1.2991 0.357  -0.1849 -0.3202 0.0971  125 TYR   A CZ   
981  O  OH   . TYR   A 126 ? 0.9925 1.3246 0.3845 -0.1976 -0.2998 0.0853  125 TYR   A OH   
982  N  N    . PRO   A 127 ? 0.8961 1.3169 0.3697 -0.0656 -0.421  0.1772  126 PRO   A N    
983  C  CA   . PRO   A 127 ? 0.9122 1.3255 0.3822 -0.0454 -0.4354 0.1976  126 PRO   A CA   
984  C  C    . PRO   A 127 ? 0.9241 1.3669 0.376  -0.0608 -0.4442 0.2073  126 PRO   A C    
985  O  O    . PRO   A 127 ? 0.9051 1.4127 0.3648 -0.065  -0.4522 0.2056  126 PRO   A O    
986  C  CB   . PRO   A 127 ? 0.8983 1.3445 0.394  -0.0111 -0.4453 0.203   126 PRO   A CB   
987  C  CG   . PRO   A 127 ? 0.8917 1.3441 0.4049 -0.0109 -0.4344 0.1852  126 PRO   A CG   
988  C  CD   . PRO   A 127 ? 0.8707 1.3296 0.3713 -0.0484 -0.4217 0.17    126 PRO   A CD   
989  N  N    . ALA   A 128 ? 0.9525 1.3516 0.3805 -0.0689 -0.4431 0.2172  127 ALA   A N    
990  C  CA   . ALA   A 128 ? 0.9642 1.3829 0.37   -0.0822 -0.4509 0.2279  127 ALA   A CA   
991  C  C    . ALA   A 128 ? 0.9979 1.358  0.3818 -0.0814 -0.4485 0.2423  127 ALA   A C    
992  O  O    . ALA   A 128 ? 1.0161 1.3231 0.4001 -0.0814 -0.4377 0.2383  127 ALA   A O    
993  C  CB   . ALA   A 128 ? 0.9635 1.4088 0.355  -0.1194 -0.4429 0.2107  127 ALA   A CB   
994  N  N    . ASP   A 129 ? 1.0041 1.3772 0.3686 -0.0816 -0.4582 0.2588  128 ASP   A N    
995  C  CA   . ASP   A 129 ? 1.0361 1.357  0.3776 -0.0843 -0.4542 0.2729  128 ASP   A CA   
996  C  C    . ASP   A 129 ? 1.0435 1.3416 0.3663 -0.1166 -0.4393 0.2586  128 ASP   A C    
997  O  O    . ASP   A 129 ? 1.0378 1.365  0.3571 -0.138  -0.4346 0.2415  128 ASP   A O    
998  C  CB   . ASP   A 129 ? 1.0679 1.4085 0.3906 -0.0742 -0.4676 0.2958  128 ASP   A CB   
999  C  CG   . ASP   A 129 ? 1.1402 1.5426 0.4495 -0.0939 -0.4747 0.2902  128 ASP   A CG   
1000 O  OD1  . ASP   A 129 ? 1.1383 1.5933 0.4649 -0.0989 -0.4785 0.2756  128 ASP   A OD1  
1001 O  OD2  . ASP   A 129 ? 1.1814 1.5813 0.462  -0.1055 -0.4763 0.3001  128 ASP   A OD2  
1002 N  N    . LEU   A 130 ? 1.0538 1.2994 0.3635 -0.1203 -0.4304 0.2651  129 LEU   A N    
1003 C  CA   . LEU   A 130 ? 1.062  1.2841 0.3544 -0.1456 -0.4148 0.2524  129 LEU   A CA   
1004 C  C    . LEU   A 130 ? 1.06   1.3113 0.3269 -0.17   -0.4135 0.246   129 LEU   A C    
1005 O  O    . LEU   A 130 ? 1.0687 1.3087 0.3234 -0.1902 -0.3995 0.2296  129 LEU   A O    
1006 C  CB   . LEU   A 130 ? 1.0787 1.251  0.3611 -0.1454 -0.4069 0.2628  129 LEU   A CB   
1007 C  CG   . LEU   A 130 ? 1.0992 1.244  0.3773 -0.1602 -0.3895 0.2473  129 LEU   A CG   
1008 C  CD1  . LEU   A 130 ? 1.1028 1.2202 0.4046 -0.1469 -0.3853 0.2422  129 LEU   A CD1  
1009 C  CD2  . LEU   A 130 ? 1.1223 1.2467 0.3744 -0.1745 -0.3809 0.2544  129 LEU   A CD2  
1010 N  N    . LEU   A 131 ? 1.0482 1.3376 0.3055 -0.1674 -0.4277 0.2579  130 LEU   A N    
1011 C  CA   . LEU   A 131 ? 1.049  1.3701 0.2798 -0.192  -0.4282 0.2509  130 LEU   A CA   
1012 C  C    . LEU   A 131 ? 1.0265 1.4024 0.2672 -0.2048 -0.4325 0.233   130 LEU   A C    
1013 O  O    . LEU   A 131 ? 1.0286 1.4226 0.2473 -0.2324 -0.4277 0.2191  130 LEU   A O    
1014 C  CB   . LEU   A 131 ? 1.0548 1.3899 0.2649 -0.1851 -0.4405 0.2729  130 LEU   A CB   
1015 C  CG   . LEU   A 131 ? 1.0951 1.3748 0.2924 -0.1779 -0.4332 0.2901  130 LEU   A CG   
1016 C  CD1  . LEU   A 131 ? 1.1087 1.3993 0.2871 -0.1651 -0.4455 0.316   130 LEU   A CD1  
1017 C  CD2  . LEU   A 131 ? 1.1175 1.3638 0.294  -0.2021 -0.4143 0.2773  130 LEU   A CD2  
1018 N  N    . SER   A 132 ? 1.0029 1.4035 0.2757 -0.1866 -0.4398 0.2317  131 SER   A N    
1019 C  CA   . SER   A 132 ? 0.978  1.4337 0.2648 -0.1991 -0.4423 0.2143  131 SER   A CA   
1020 C  C    . SER   A 132 ? 0.963  1.3953 0.2643 -0.2069 -0.4259 0.195   131 SER   A C    
1021 O  O    . SER   A 132 ? 0.9488 1.4194 0.2585 -0.2228 -0.4234 0.1787  131 SER   A O    
1022 C  CB   . SER   A 132 ? 0.9764 1.4914 0.2874 -0.1739 -0.462  0.226   131 SER   A CB   
1023 O  OG   . SER   A 132 ? 1.0051 1.5516 0.2986 -0.1686 -0.4771 0.2426  131 SER   A OG   
1024 N  N    . THR   A 133 ? 0.9639 1.3363 0.2674 -0.1965 -0.4146 0.1968  132 THR   A N    
1025 C  CA   . THR   A 133 ? 0.9593 1.3053 0.2719 -0.2007 -0.3986 0.1806  132 THR   A CA   
1026 C  C    . THR   A 133 ? 0.9583 1.2868 0.242  -0.2325 -0.381  0.1639  132 THR   A C    
1027 O  O    . THR   A 133 ? 0.97   1.2769 0.2259 -0.2444 -0.3768 0.167   132 THR   A O    
1028 C  CB   . THR   A 133 ? 0.9952 1.2857 0.314  -0.1821 -0.3921 0.1872  132 THR   A CB   
1029 O  OG1  . THR   A 133 ? 1.0229 1.2831 0.3197 -0.1857 -0.3908 0.1986  132 THR   A OG1  
1030 C  CG2  . THR   A 133 ? 0.9927 1.2868 0.3417 -0.1514 -0.4029 0.1964  132 THR   A CG2  
1031 N  N    . LYS   A 134 ? 0.9448 1.2774 0.2323 -0.2451 -0.3689 0.1466  133 LYS   A N    
1032 C  CA   . LYS   A 134 ? 0.9592 1.266  0.2159 -0.2743 -0.3487 0.1299  133 LYS   A CA   
1033 C  C    . LYS   A 134 ? 0.9813 1.225  0.2278 -0.2648 -0.3308 0.1285  133 LYS   A C    
1034 O  O    . LYS   A 134 ? 0.9745 1.206  0.2441 -0.2416 -0.3319 0.1328  133 LYS   A O    
1035 C  CB   . LYS   A 134 ? 0.9617 1.3008 0.225  -0.2937 -0.342  0.1126  133 LYS   A CB   
1036 C  CG   . LYS   A 134 ? 0.9729 1.3873 0.2559 -0.2982 -0.3611 0.1135  133 LYS   A CG   
1037 C  CD   . LYS   A 134 ? 1.0109 1.4594 0.3102 -0.3122 -0.3538 0.0978  133 LYS   A CD   
1038 C  CE   . LYS   A 134 ? 1.0196 1.5442 0.3551 -0.298  -0.3742 0.1035  133 LYS   A CE   
1039 N  NZ   . LYS   A 134 ? 1.0287 1.5648 0.3921 -0.2872 -0.3675 0.0974  133 LYS   A NZ   
1040 N  N    . ASP   A 135 ? 1.0045 1.2103 0.2156 -0.2815 -0.3143 0.122   134 ASP   A N    
1041 C  CA   . ASP   A 135 ? 1.0289 1.1809 0.2281 -0.2706 -0.2971 0.1213  134 ASP   A CA   
1042 C  C    . ASP   A 135 ? 1.0299 1.1671 0.2378 -0.2642 -0.284  0.1117  134 ASP   A C    
1043 O  O    . ASP   A 135 ? 1.0422 1.1529 0.2581 -0.2433 -0.2786 0.1153  134 ASP   A O    
1044 C  CB   . ASP   A 135 ? 1.0761 1.1928 0.2322 -0.2891 -0.2797 0.1148  134 ASP   A CB   
1045 C  CG   . ASP   A 135 ? 1.1309 1.252  0.2747 -0.2909 -0.2891 0.1259  134 ASP   A CG   
1046 O  OD1  . ASP   A 135 ? 1.1238 1.258  0.2909 -0.2723 -0.3049 0.1416  134 ASP   A OD1  
1047 O  OD2  . ASP   A 135 ? 1.1803 1.2896 0.289  -0.3116 -0.2797 0.1188  134 ASP   A OD2  
1048 N  N    . GLU   A 136 ? 1.0152 1.1714 0.2204 -0.2833 -0.2781 0.0991  135 GLU   A N    
1049 C  CA   . GLU   A 136 ? 1.0119 1.157  0.2223 -0.2809 -0.2639 0.0898  135 GLU   A CA   
1050 C  C    . GLU   A 136 ? 0.965  1.1344 0.2167 -0.2529 -0.2782 0.0973  135 GLU   A C    
1051 O  O    . GLU   A 136 ? 0.964  1.1104 0.2203 -0.237  -0.2685 0.0956  135 GLU   A O    
1052 C  CB   . GLU   A 136 ? 1.0517 1.2206 0.2523 -0.3127 -0.2561 0.0749  135 GLU   A CB   
1053 C  CG   . GLU   A 136 ? 1.15   1.3027 0.3102 -0.3453 -0.2452 0.065   135 GLU   A CG   
1054 C  CD   . GLU   A 136 ? 1.2499 1.4449 0.4126 -0.3556 -0.2658 0.0697  135 GLU   A CD   
1055 O  OE1  . GLU   A 136 ? 1.2424 1.4877 0.4402 -0.3403 -0.2887 0.08    135 GLU   A OE1  
1056 O  OE2  . GLU   A 136 ? 1.308  1.4849 0.4355 -0.3767 -0.2587 0.0638  135 GLU   A OE2  
1057 N  N    . GLU   A 137 ? 0.9276 1.1424 0.2063 -0.2454 -0.3008 0.1058  136 GLU   A N    
1058 C  CA   . GLU   A 137 ? 0.8986 1.1352 0.214  -0.2178 -0.3155 0.1135  136 GLU   A CA   
1059 C  C    . GLU   A 137 ? 0.8941 1.0918 0.2131 -0.1943 -0.3159 0.1218  136 GLU   A C    
1060 O  O    . GLU   A 137 ? 0.8909 1.082  0.2278 -0.175  -0.3151 0.1205  136 GLU   A O    
1061 C  CB   . GLU   A 137 ? 0.9038 1.1906 0.2391 -0.2131 -0.3383 0.1232  136 GLU   A CB   
1062 C  CG   . GLU   A 137 ? 0.9577 1.3    0.2998 -0.2323 -0.3413 0.1144  136 GLU   A CG   
1063 C  CD   . GLU   A 137 ? 1.0586 1.4573 0.4212 -0.222  -0.3646 0.1253  136 GLU   A CD   
1064 O  OE1  . GLU   A 137 ? 1.1036 1.4942 0.4586 -0.2136 -0.376  0.1391  136 GLU   A OE1  
1065 O  OE2  . GLU   A 137 ? 1.0685 1.5211 0.454  -0.2208 -0.3709 0.121   136 GLU   A OE2  
1066 N  N    . ILE   A 138 ? 0.8919 1.0668 0.1936 -0.1973 -0.3167 0.1294  137 ILE   A N    
1067 C  CA   . ILE   A 138 ? 0.8932 1.0361 0.198  -0.1797 -0.3163 0.1365  137 ILE   A CA   
1068 C  C    . ILE   A 138 ? 0.9027 1.0149 0.1971 -0.1745 -0.2978 0.1272  137 ILE   A C    
1069 O  O    . ILE   A 138 ? 0.9085 1.012  0.2197 -0.1548 -0.2992 0.1274  137 ILE   A O    
1070 C  CB   . ILE   A 138 ? 0.9077 1.0369 0.1929 -0.1883 -0.3178 0.1456  137 ILE   A CB   
1071 C  CG1  . ILE   A 138 ? 0.9062 1.0663 0.1995 -0.1899 -0.3367 0.1573  137 ILE   A CG1  
1072 C  CG2  . ILE   A 138 ? 0.9202 1.0204 0.2087 -0.1742 -0.3148 0.151   137 ILE   A CG2  
1073 C  CD1  . ILE   A 138 ? 0.9276 1.0841 0.1941 -0.2059 -0.3363 0.1632  137 ILE   A CD1  
1074 N  N    . THR   A 139 ? 0.8989 0.9947 0.1635 -0.1918 -0.28   0.1184  138 THR   A N    
1075 C  CA   . THR   A 139 ? 0.8976 0.9609 0.1441 -0.1865 -0.2594 0.1108  138 THR   A CA   
1076 C  C    . THR   A 139 ? 0.8709 0.9452 0.1443 -0.1725 -0.2575 0.1054  138 THR   A C    
1077 O  O    . THR   A 139 ? 0.869  0.9321 0.1501 -0.1515 -0.2568 0.1063  138 THR   A O    
1078 C  CB   . THR   A 139 ? 0.9192 0.96   0.1262 -0.2102 -0.2404 0.103   138 THR   A CB   
1079 O  OG1  . THR   A 139 ? 0.9277 0.9478 0.1157 -0.2132 -0.2361 0.1076  138 THR   A OG1  
1080 C  CG2  . THR   A 139 ? 0.9446 0.9531 0.13   -0.207  -0.2173 0.0949  138 THR   A CG2  
1081 N  N    . LYS   A 140 ? 0.8469 0.9494 0.141  -0.1837 -0.2573 0.1     139 LYS   A N    
1082 C  CA   . LYS   A 140 ? 0.8349 0.9549 0.1436 -0.1722 -0.2587 0.0953  139 LYS   A CA   
1083 C  C    . LYS   A 140 ? 0.8146 0.9463 0.1589 -0.1455 -0.2735 0.1005  139 LYS   A C    
1084 O  O    . LYS   A 140 ? 0.8266 0.9551 0.1665 -0.1283 -0.2741 0.0972  139 LYS   A O    
1085 C  CB   . LYS   A 140 ? 0.8512 1.0121 0.1602 -0.1906 -0.2649 0.0903  139 LYS   A CB   
1086 C  CG   . LYS   A 140 ? 0.9468 1.0928 0.2299 -0.2123 -0.2416 0.0793  139 LYS   A CG   
1087 C  CD   . LYS   A 140 ? 1.0186 1.2112 0.3232 -0.2221 -0.2436 0.0726  139 LYS   A CD   
1088 C  CE   . LYS   A 140 ? 1.1088 1.2842 0.3873 -0.2468 -0.218  0.0613  139 LYS   A CE   
1089 N  NZ   . LYS   A 140 ? 1.126  1.3412 0.428  -0.2481 -0.216  0.0557  139 LYS   A NZ   
1090 N  N    . THR   A 141 ? 0.7875 0.9278 0.1667 -0.1421 -0.2822 0.1081  140 THR   A N    
1091 C  CA   . THR   A 141 ? 0.7723 0.9147 0.1808 -0.1193 -0.2943 0.1126  140 THR   A CA   
1092 C  C    . THR   A 141 ? 0.7784 0.8905 0.182  -0.106  -0.287  0.1096  140 THR   A C    
1093 O  O    . THR   A 141 ? 0.7807 0.8952 0.187  -0.0893 -0.2905 0.1046  140 THR   A O    
1094 C  CB   . THR   A 141 ? 0.7819 0.9334 0.1922 -0.1198 -0.3132 0.1251  140 THR   A CB   
1095 O  OG1  . THR   A 141 ? 0.7841 0.9758 0.197  -0.1225 -0.3281 0.1288  140 THR   A OG1  
1096 C  CG2  . THR   A 141 ? 0.7806 0.9179 0.2054 -0.1001 -0.3243 0.1304  140 THR   A CG2  
1097 N  N    . PHE   A 142 ? 0.7733 0.8606 0.1733 -0.1142 -0.2729 0.1106  141 PHE   A N    
1098 C  CA   . PHE   A 142 ? 0.7662 0.8323 0.1714 -0.102  -0.2627 0.107   141 PHE   A CA   
1099 C  C    . PHE   A 142 ? 0.76   0.8167 0.1587 -0.0938 -0.2456 0.0981  141 PHE   A C    
1100 O  O    . PHE   A 142 ? 0.7578 0.8125 0.1617 -0.0763 -0.2459 0.0942  141 PHE   A O    
1101 C  CB   . PHE   A 142 ? 0.7673 0.8164 0.1673 -0.1115 -0.2542 0.1113  141 PHE   A CB   
1102 C  CG   . PHE   A 142 ? 0.7609 0.8119 0.1806 -0.1099 -0.2663 0.1183  141 PHE   A CG   
1103 C  CD1  . PHE   A 142 ? 0.7656 0.8273 0.1894 -0.1173 -0.2798 0.1269  141 PHE   A CD1  
1104 C  CD2  . PHE   A 142 ? 0.7682 0.8136 0.1875 -0.1001 -0.2702 0.1182  141 PHE   A CD2  
1105 C  CE1  . PHE   A 142 ? 0.7752 0.8336 0.2021 -0.1148 -0.2942 0.1363  141 PHE   A CE1  
1106 C  CE2  . PHE   A 142 ? 0.7754 0.8203 0.1999 -0.1012 -0.2848 0.1257  141 PHE   A CE2  
1107 C  CZ   . PHE   A 142 ? 0.7734 0.82   0.2053 -0.1086 -0.2936 0.1347  141 PHE   A CZ   
1108 N  N    . GLU   A 143 ? 0.754  0.8053 0.1438 -0.107  -0.2299 0.0944  142 GLU   A N    
1109 C  CA   . GLU   A 143 ? 0.7616 0.7986 0.1313 -0.1006 -0.2141 0.0885  142 GLU   A CA   
1110 C  C    . GLU   A 143 ? 0.7377 0.7903 0.1325 -0.0846 -0.2149 0.083   142 GLU   A C    
1111 O  O    . GLU   A 143 ? 0.7336 0.7743 0.1248 -0.0699 -0.2023 0.0786  142 GLU   A O    
1112 C  CB   . GLU   A 143 ? 0.8077 0.8347 0.1231 -0.1227 -0.2078 0.0883  142 GLU   A CB   
1113 C  CG   . GLU   A 143 ? 0.9033 0.8998 0.127  -0.1292 -0.2084 0.0945  142 GLU   A CG   
1114 C  CD   . GLU   A 143 ? 0.9934 0.9744 0.1874 -0.1574 -0.1946 0.0901  142 GLU   A CD   
1115 O  OE1  . GLU   A 143 ? 0.9945 0.9984 0.199  -0.1746 -0.198  0.0854  142 GLU   A OE1  
1116 O  OE2  . GLU   A 143 ? 1.0438 0.9918 0.2044 -0.1629 -0.18   0.0906  142 GLU   A OE2  
1117 N  N    . ILE   A 144 ? 0.7178 0.7971 0.1404 -0.0854 -0.2277 0.0832  143 ILE   A N    
1118 C  CA   . ILE   A 144 ? 0.7124 0.8108 0.1456 -0.0698 -0.2338 0.0786  143 ILE   A CA   
1119 C  C    . ILE   A 144 ? 0.6946 0.7953 0.1558 -0.0501 -0.2449 0.0769  143 ILE   A C    
1120 O  O    . ILE   A 144 ? 0.6876 0.787  0.1549 -0.0326 -0.2412 0.0702  143 ILE   A O    
1121 C  CB   . ILE   A 144 ? 0.711  0.8417 0.1469 -0.0817 -0.2422 0.0794  143 ILE   A CB   
1122 C  CG1  . ILE   A 144 ? 0.7407 0.8701 0.1331 -0.1028 -0.2326 0.0776  143 ILE   A CG1  
1123 C  CG2  . ILE   A 144 ? 0.6986 0.8545 0.1548 -0.0632 -0.2511 0.0753  143 ILE   A CG2  
1124 C  CD1  . ILE   A 144 ? 0.7508 0.9177 0.1341 -0.1215 -0.2455 0.0783  143 ILE   A CD1  
1125 N  N    . ASN   A 145 ? 0.682  0.7832 0.1627 -0.0543 -0.2548 0.0822  144 ASN   A N    
1126 C  CA   . ASN   A 145 ? 0.6772 0.7758 0.1744 -0.0404 -0.2681 0.0815  144 ASN   A CA   
1127 C  C    . ASN   A 145 ? 0.6741 0.7551 0.1741 -0.0335 -0.2627 0.0771  144 ASN   A C    
1128 O  O    . ASN   A 145 ? 0.6716 0.7516 0.1821 -0.0212 -0.2718 0.072   144 ASN   A O    
1129 C  CB   . ASN   A 145 ? 0.6977 0.8021 0.1873 -0.0467 -0.2902 0.0928  144 ASN   A CB   
1130 C  CG   . ASN   A 145 ? 0.7423 0.8818 0.2015 -0.0473 -0.318  0.1013  144 ASN   A CG   
1131 O  OD1  . ASN   A 145 ? 0.766  0.9296 0.2078 -0.0434 -0.324  0.0975  144 ASN   A OD1  
1132 N  ND2  . ASN   A 145 ? 0.7446 0.8887 0.2078 -0.0525 -0.3291 0.1118  144 ASN   A ND2  
1133 N  N    . ILE   A 146 ? 0.6711 0.7394 0.1642 -0.0413 -0.2478 0.0782  145 ILE   A N    
1134 C  CA   . ILE   A 146 ? 0.6706 0.7329 0.1644 -0.0333 -0.2454 0.0745  145 ILE   A CA   
1135 C  C    . ILE   A 146 ? 0.678  0.7341 0.1524 -0.0287 -0.2289 0.073   145 ILE   A C    
1136 O  O    . ILE   A 146 ? 0.669  0.7297 0.1485 -0.0133 -0.2235 0.0663  145 ILE   A O    
1137 C  CB   . ILE   A 146 ? 0.6742 0.7312 0.1722 -0.0432 -0.2557 0.0808  145 ILE   A CB   
1138 C  CG1  . ILE   A 146 ? 0.6873 0.7491 0.1752 -0.0366 -0.2597 0.0774  145 ILE   A CG1  
1139 C  CG2  . ILE   A 146 ? 0.6853 0.7366 0.1689 -0.0607 -0.2545 0.0912  145 ILE   A CG2  
1140 C  CD1  . ILE   A 146 ? 0.6961 0.7702 0.182  -0.0203 -0.2718 0.0669  145 ILE   A CD1  
1141 N  N    . LEU   A 147 ? 0.691  0.7359 0.1449 -0.0406 -0.2193 0.0782  146 LEU   A N    
1142 C  CA   . LEU   A 147 ? 0.7075 0.7393 0.1338 -0.0336 -0.2038 0.0778  146 LEU   A CA   
1143 C  C    . LEU   A 147 ? 0.7076 0.74   0.1263 -0.0178 -0.1958 0.0723  146 LEU   A C    
1144 O  O    . LEU   A 147 ? 0.7085 0.738  0.1205 0       -0.1859 0.0697  146 LEU   A O    
1145 C  CB   . LEU   A 147 ? 0.7282 0.7415 0.1277 -0.0517 -0.195  0.0831  146 LEU   A CB   
1146 C  CG   . LEU   A 147 ? 0.7642 0.7759 0.1357 -0.0629 -0.2066 0.0918  146 LEU   A CG   
1147 C  CD1  . LEU   A 147 ? 0.787  0.781  0.1275 -0.0824 -0.1989 0.0952  146 LEU   A CD1  
1148 C  CD2  . LEU   A 147 ? 0.7893 0.8018 0.1373 -0.0476 -0.2066 0.0943  146 LEU   A CD2  
1149 N  N    . GLY   A 148 ? 0.7063 0.746  0.1268 -0.0231 -0.2003 0.0711  147 GLY   A N    
1150 C  CA   . GLY   A 148 ? 0.7127 0.756  0.1209 -0.0103 -0.1949 0.0669  147 GLY   A CA   
1151 C  C    . GLY   A 148 ? 0.7029 0.7617 0.1258 0.0119  -0.2022 0.0603  147 GLY   A C    
1152 O  O    . GLY   A 148 ? 0.7177 0.7756 0.121  0.0291  -0.1947 0.058   147 GLY   A O    
1153 N  N    . HIS   A 149 ? 0.6801 0.7508 0.1346 0.0114  -0.2158 0.0571  148 HIS   A N    
1154 C  CA   . HIS   A 149 ? 0.6732 0.7576 0.1397 0.0286  -0.2244 0.0485  148 HIS   A CA   
1155 C  C    . HIS   A 149 ? 0.6831 0.7707 0.1363 0.0427  -0.2177 0.0468  148 HIS   A C    
1156 O  O    . HIS   A 149 ? 0.6707 0.7708 0.1333 0.0607  -0.2144 0.0382  148 HIS   A O    
1157 C  CB   . HIS   A 149 ? 0.6676 0.7562 0.1513 0.0212  -0.2433 0.0477  148 HIS   A CB   
1158 C  CG   . HIS   A 149 ? 0.6926 0.7888 0.165  0.0191  -0.2659 0.0496  148 HIS   A CG   
1159 N  ND1  . HIS   A 149 ? 0.7125 0.8152 0.1827 0.0254  -0.2906 0.045   148 HIS   A ND1  
1160 C  CD2  . HIS   A 149 ? 0.7173 0.82   0.1696 0.0122  -0.2734 0.0566  148 HIS   A CD2  
1161 C  CE1  . HIS   A 149 ? 0.723  0.831  0.1921 0.0251  -0.3024 0.0486  148 HIS   A CE1  
1162 N  NE2  . HIS   A 149 ? 0.7273 0.8406 0.1854 0.017   -0.2942 0.0558  148 HIS   A NE2  
1163 N  N    . PHE   A 150 ? 0.6968 0.7754 0.134  0.0357  -0.2132 0.0543  149 PHE   A N    
1164 C  CA   . PHE   A 150 ? 0.7131 0.8004 0.1307 0.0514  -0.2096 0.0547  149 PHE   A CA   
1165 C  C    . PHE   A 150 ? 0.7506 0.8311 0.1239 0.0713  -0.1995 0.0577  149 PHE   A C    
1166 O  O    . PHE   A 150 ? 0.7415 0.8392 0.1198 0.0927  -0.1959 0.0522  149 PHE   A O    
1167 C  CB   . PHE   A 150 ? 0.7128 0.7911 0.1275 0.0403  -0.2037 0.0618  149 PHE   A CB   
1168 C  CG   . PHE   A 150 ? 0.7081 0.8027 0.1385 0.029   -0.2201 0.0615  149 PHE   A CG   
1169 C  CD1  . PHE   A 150 ? 0.7208 0.8076 0.1507 0.0082  -0.235  0.0668  149 PHE   A CD1  
1170 C  CD2  . PHE   A 150 ? 0.7054 0.8261 0.1392 0.0392  -0.2243 0.0574  149 PHE   A CD2  
1171 C  CE1  . PHE   A 150 ? 0.7241 0.8214 0.162  -0.0026 -0.2504 0.068   149 PHE   A CE1  
1172 C  CE2  . PHE   A 150 ? 0.7046 0.8398 0.1497 0.0251  -0.2391 0.0571  149 PHE   A CE2  
1173 C  CZ   . PHE   A 150 ? 0.7079 0.8269 0.1595 0.0038  -0.249  0.0622  149 PHE   A CZ   
1174 N  N    . TRP   A 151 ? 0.7859 0.8405 0.1196 0.0636  -0.1914 0.0659  150 TRP   A N    
1175 C  CA   . TRP   A 151 ? 0.8186 0.8557 0.1082 0.0807  -0.1751 0.0704  150 TRP   A CA   
1176 C  C    . TRP   A 151 ? 0.815  0.8669 0.1036 0.0959  -0.1781 0.0649  150 TRP   A C    
1177 O  O    . TRP   A 151 ? 0.8447 0.8958 0.0934 0.1203  -0.1712 0.0684  150 TRP   A O    
1178 C  CB   . TRP   A 151 ? 0.8513 0.8507 0.1027 0.0642  -0.1593 0.0785  150 TRP   A CB   
1179 C  CG   . TRP   A 151 ? 0.8745 0.8625 0.1101 0.0396  -0.1658 0.0841  150 TRP   A CG   
1180 C  CD1  . TRP   A 151 ? 0.8975 0.8771 0.1142 0.0132  -0.1707 0.0867  150 TRP   A CD1  
1181 C  CD2  . TRP   A 151 ? 0.8817 0.8684 0.1128 0.0398  -0.1676 0.0881  150 TRP   A CD2  
1182 N  NE1  . TRP   A 151 ? 0.9087 0.8799 0.1172 -0.003  -0.1741 0.0909  150 TRP   A NE1  
1183 C  CE2  . TRP   A 151 ? 0.9033 0.8771 0.1171 0.0129  -0.1723 0.0925  150 TRP   A CE2  
1184 C  CE3  . TRP   A 151 ? 0.8858 0.8866 0.1134 0.0605  -0.1685 0.0896  150 TRP   A CE3  
1185 C  CZ2  . TRP   A 151 ? 0.9216 0.8914 0.1203 0.0063  -0.1752 0.098   150 TRP   A CZ2  
1186 C  CZ3  . TRP   A 151 ? 0.9039 0.9042 0.1171 0.0534  -0.1723 0.0953  150 TRP   A CZ3  
1187 C  CH2  . TRP   A 151 ? 0.919  0.9013 0.1195 0.0268  -0.1742 0.0994  150 TRP   A CH2  
1188 N  N    . ILE   A 152 ? 0.7791 0.8452 0.1103 0.0846  -0.1873 0.0566  151 ILE   A N    
1189 C  CA   . ILE   A 152 ? 0.7577 0.8378 0.1082 0.0995  -0.1839 0.048   151 ILE   A CA   
1190 C  C    . ILE   A 152 ? 0.7287 0.8331 0.1088 0.1199  -0.1871 0.0378  151 ILE   A C    
1191 O  O    . ILE   A 152 ? 0.7364 0.8451 0.1015 0.1424  -0.1768 0.0375  151 ILE   A O    
1192 C  CB   . ILE   A 152 ? 0.7562 0.8473 0.1182 0.0865  -0.1974 0.0444  151 ILE   A CB   
1193 C  CG1  . ILE   A 152 ? 0.7835 0.8599 0.1189 0.0621  -0.197  0.0537  151 ILE   A CG1  
1194 C  CG2  . ILE   A 152 ? 0.7567 0.8591 0.1138 0.1029  -0.1928 0.0388  151 ILE   A CG2  
1195 C  CD1  . ILE   A 152 ? 0.793  0.8884 0.1325 0.0485  -0.2192 0.0531  151 ILE   A CD1  
1196 N  N    . THR   A 153 ? 0.704  0.8227 0.1176 0.1111  -0.2004 0.0315  152 THR   A N    
1197 C  CA   . THR   A 153 ? 0.6889 0.8344 0.121  0.1231  -0.2084 0.0213  152 THR   A CA   
1198 C  C    . THR   A 153 ? 0.7089 0.8666 0.1142 0.1443  -0.2011 0.0254  152 THR   A C    
1199 O  O    . THR   A 153 ? 0.7008 0.8853 0.1111 0.1639  -0.2023 0.0168  152 THR   A O    
1200 C  CB   . THR   A 153 ? 0.679  0.8285 0.1338 0.1034  -0.223  0.0192  152 THR   A CB   
1201 O  OG1  . THR   A 153 ? 0.6911 0.8281 0.1485 0.087   -0.2358 0.0205  152 THR   A OG1  
1202 C  CG2  . THR   A 153 ? 0.659  0.8362 0.1357 0.1091  -0.2316 0.0063  152 THR   A CG2  
1203 N  N    . LYS   A 154 ? 0.7319 0.8699 0.1104 0.1417  -0.1917 0.038   153 LYS   A N    
1204 C  CA   . LYS   A 154 ? 0.7562 0.8999 0.1038 0.1638  -0.1825 0.0451  153 LYS   A CA   
1205 C  C    . LYS   A 154 ? 0.7854 0.9196 0.0952 0.1908  -0.1686 0.0502  153 LYS   A C    
1206 O  O    . LYS   A 154 ? 0.7831 0.9341 0.0894 0.2177  -0.1595 0.0509  153 LYS   A O    
1207 C  CB   . LYS   A 154 ? 0.8095 0.9262 0.1055 0.1529  -0.1824 0.0609  153 LYS   A CB   
1208 C  CG   . LYS   A 154 ? 0.8833 1.028  0.1201 0.1519  -0.2116 0.0699  153 LYS   A CG   
1209 C  CD   . LYS   A 154 ? 0.9718 1.1042 0.1719 0.173   -0.1919 0.0816  153 LYS   A CD   
1210 C  CE   . LYS   A 154 ? 1.0351 1.1588 0.2367 0.1577  -0.1896 0.0875  153 LYS   A CE   
1211 N  NZ   . LYS   A 154 ? 1.1016 1.1935 0.2588 0.176   -0.165  0.1     153 LYS   A NZ   
1212 N  N    . ALA   A 155 ? 0.8085 0.9164 0.094  0.184   -0.1641 0.0542  154 ALA   A N    
1213 C  CA   . ALA   A 155 ? 0.8422 0.9346 0.0853 0.2067  -0.1485 0.0611  154 ALA   A CA   
1214 C  C    . ALA   A 155 ? 0.8539 0.979  0.0905 0.2252  -0.1604 0.0528  154 ALA   A C    
1215 O  O    . ALA   A 155 ? 0.8602 0.9813 0.0809 0.2505  -0.1441 0.0562  154 ALA   A O    
1216 C  CB   . ALA   A 155 ? 0.8633 0.9123 0.0806 0.1881  -0.1341 0.0694  154 ALA   A CB   
1217 N  N    . LEU   A 156 ? 0.8524 1.0072 0.1044 0.2135  -0.1874 0.041   155 LEU   A N    
1218 C  CA   . LEU   A 156 ? 0.8641 1.0489 0.107  0.2288  -0.2012 0.0303  155 LEU   A CA   
1219 C  C    . LEU   A 156 ? 0.8699 1.1014 0.1149 0.2415  -0.2233 0.0186  155 LEU   A C    
1220 O  O    . LEU   A 156 ? 0.8726 1.1303 0.112  0.2637  -0.2244 0.0108  155 LEU   A O    
1221 C  CB   . LEU   A 156 ? 0.8638 1.0462 0.1172 0.2097  -0.215  0.0228  155 LEU   A CB   
1222 C  CG   . LEU   A 156 ? 0.9044 1.0534 0.1337 0.1947  -0.2024 0.0346  155 LEU   A CG   
1223 C  CD1  . LEU   A 156 ? 0.8998 1.0549 0.1615 0.1776  -0.2137 0.0256  155 LEU   A CD1  
1224 C  CD2  . LEU   A 156 ? 0.9321 1.0652 0.1219 0.2131  -0.1791 0.0435  155 LEU   A CD2  
1225 N  N    . LEU   A 157 ? 0.8714 1.1156 0.125  0.2266  -0.2398 0.0173  156 LEU   A N    
1226 C  CA   . LEU   A 157 ? 0.8684 1.159  0.1366 0.2312  -0.2579 0.0048  156 LEU   A CA   
1227 C  C    . LEU   A 157 ? 0.8935 1.2157 0.1344 0.2647  -0.2516 0.0085  156 LEU   A C    
1228 O  O    . LEU   A 157 ? 0.8834 1.2515 0.1346 0.2744  -0.2656 -0.0069 156 LEU   A O    
1229 C  CB   . LEU   A 157 ? 0.8637 1.1547 0.1541 0.2084  -0.2653 0.0066  156 LEU   A CB   
1230 C  CG   . LEU   A 157 ? 0.8589 1.172  0.1875 0.1864  -0.2867 -0.0111 156 LEU   A CG   
1231 C  CD1  . LEU   A 157 ? 0.8688 1.1532 0.2148 0.1684  -0.2927 -0.0168 156 LEU   A CD1  
1232 C  CD2  . LEU   A 157 ? 0.857  1.1732 0.2006 0.1677  -0.29   -0.0061 156 LEU   A CD2  
1233 N  N    . PRO   A 158 ? 0.926  1.2257 0.1295 0.2846  -0.2305 0.0278  157 PRO   A N    
1234 C  CA   . PRO   A 158 ? 0.9378 1.2699 0.113  0.3223  -0.2247 0.0326  157 PRO   A CA   
1235 C  C    . PRO   A 158 ? 0.9573 1.3143 0.1225 0.3428  -0.2289 0.023   157 PRO   A C    
1236 O  O    . PRO   A 158 ? 0.9547 1.3652 0.1178 0.3649  -0.2386 0.0151  157 PRO   A O    
1237 C  CB   . PRO   A 158 ? 0.973  1.2556 0.1039 0.3382  -0.197  0.0562  157 PRO   A CB   
1238 C  CG   . PRO   A 158 ? 0.9854 1.225  0.1294 0.3048  -0.1929 0.0609  157 PRO   A CG   
1239 C  CD   . PRO   A 158 ? 0.9467 1.1901 0.1294 0.2748  -0.2105 0.0455  157 PRO   A CD   
1240 N  N    . SER   A 159 ? 0.9736 1.2972 0.1334 0.3352  -0.2222 0.0225  158 SER   A N    
1241 C  CA   . SER   A 159 ? 0.9792 1.3245 0.1271 0.3549  -0.2245 0.0134  158 SER   A CA   
1242 C  C    . SER   A 159 ? 0.9559 1.3417 0.1415 0.3407  -0.25   -0.0131 158 SER   A C    
1243 O  O    . SER   A 159 ? 0.945  1.3752 0.1246 0.3604  -0.2592 -0.0252 158 SER   A O    
1244 C  CB   . SER   A 159 ? 1.0218 1.3206 0.148  0.3538  -0.2056 0.023   158 SER   A CB   
1245 O  OG   . SER   A 159 ? 1.0542 1.3735 0.157  0.3811  -0.2024 0.0196  158 SER   A OG   
1246 N  N    . MET   A 160 ? 0.9493 1.3194 0.1712 0.3069  -0.2613 -0.0223 159 MET   A N    
1247 C  CA   . MET   A 160 ? 0.9337 1.3315 0.1896 0.2906  -0.2836 -0.0475 159 MET   A CA   
1248 C  C    . MET   A 160 ? 0.926  1.3781 0.1939 0.2933  -0.299  -0.0601 159 MET   A C    
1249 O  O    . MET   A 160 ? 0.9121 1.3976 0.1949 0.2896  -0.315  -0.0831 159 MET   A O    
1250 C  CB   . MET   A 160 ? 0.9328 1.2975 0.2208 0.2565  -0.2902 -0.0504 159 MET   A CB   
1251 C  CG   . MET   A 160 ? 0.9561 1.2761 0.2371 0.2508  -0.2763 -0.0384 159 MET   A CG   
1252 S  SD   . MET   A 160 ? 0.9133 1.2068 0.2329 0.2176  -0.2882 -0.0458 159 MET   A SD   
1253 C  CE   . MET   A 160 ? 0.9026 1.1603 0.2088 0.2168  -0.2698 -0.0303 159 MET   A CE   
1254 N  N    . ILE   A 161 ? 0.9341 1.3965 0.1957 0.2989  -0.2936 -0.0464 160 ILE   A N    
1255 C  CA   . ILE   A 161 ? 0.9257 1.4473 0.1984 0.3034  -0.3058 -0.0557 160 ILE   A CA   
1256 C  C    . ILE   A 161 ? 0.9328 1.5058 0.1798 0.3402  -0.307  -0.0603 160 ILE   A C    
1257 O  O    . ILE   A 161 ? 0.9086 1.5409 0.1715 0.3388  -0.3243 -0.0811 160 ILE   A O    
1258 C  CB   . ILE   A 161 ? 0.9341 1.4483 0.2067 0.3     -0.2972 -0.0377 160 ILE   A CB   
1259 C  CG1  . ILE   A 161 ? 0.9343 1.4565 0.2473 0.2628  -0.3115 -0.0492 160 ILE   A CG1  
1260 C  CG2  . ILE   A 161 ? 0.9313 1.4902 0.1799 0.3351  -0.2911 -0.0278 160 ILE   A CG2  
1261 C  CD1  . ILE   A 161 ? 0.9687 1.4301 0.2955 0.2331  -0.3081 -0.0424 160 ILE   A CD1  
1262 N  N    . LYS   A 162 ? 0.9636 1.5136 0.1695 0.3717  -0.2881 -0.0414 161 LYS   A N    
1263 C  CA   . LYS   A 162 ? 0.974  1.5668 0.1489 0.4107  -0.2868 -0.0416 161 LYS   A CA   
1264 C  C    . LYS   A 162 ? 0.9717 1.5907 0.1578 0.4051  -0.3024 -0.0676 161 LYS   A C    
1265 O  O    . LYS   A 162 ? 0.969  1.6525 0.1557 0.4185  -0.3166 -0.084  161 LYS   A O    
1266 C  CB   . LYS   A 162 ? 1.0344 1.5811 0.1603 0.4411  -0.2603 -0.0152 161 LYS   A CB   
1267 C  CG   . LYS   A 162 ? 1.1154 1.6313 0.2176 0.4545  -0.2407 0.0111  161 LYS   A CG   
1268 C  CD   . LYS   A 162 ? 1.205  1.6594 0.2583 0.4755  -0.2121 0.0349  161 LYS   A CD   
1269 C  CE   . LYS   A 162 ? 1.2554 1.6373 0.31   0.4475  -0.196  0.0476  161 LYS   A CE   
1270 N  NZ   . LYS   A 162 ? 1.2569 1.6365 0.3223 0.4389  -0.1957 0.0547  161 LYS   A NZ   
1271 N  N    . ARG   A 163 ? 0.9749 1.5464 0.1693 0.3857  -0.2997 -0.0723 162 ARG   A N    
1272 C  CA   . ARG   A 163 ? 0.9668 1.5538 0.1683 0.382   -0.3115 -0.0964 162 ARG   A CA   
1273 C  C    . ARG   A 163 ? 0.9366 1.5428 0.1798 0.3481  -0.3336 -0.1247 162 ARG   A C    
1274 O  O    . ARG   A 163 ? 0.931  1.5541 0.1786 0.3455  -0.3445 -0.1482 162 ARG   A O    
1275 C  CB   . ARG   A 163 ? 1.0132 1.5446 0.2033 0.3803  -0.2969 -0.0885 162 ARG   A CB   
1276 C  CG   . ARG   A 163 ? 1.0839 1.5902 0.2295 0.4101  -0.2721 -0.0613 162 ARG   A CG   
1277 C  CD   . ARG   A 163 ? 1.148  1.5934 0.2893 0.3977  -0.2546 -0.0487 162 ARG   A CD   
1278 N  NE   . ARG   A 163 ? 1.2046 1.6176 0.3032 0.4193  -0.2282 -0.0211 162 ARG   A NE   
1279 C  CZ   . ARG   A 163 ? 1.2341 1.6462 0.2948 0.4468  -0.2138 -0.0136 162 ARG   A CZ   
1280 N  NH1  . ARG   A 163 ? 1.2218 1.6665 0.283  0.4564  -0.2241 -0.0322 162 ARG   A NH1  
1281 N  NH2  . ARG   A 163 ? 1.2523 1.6268 0.2718 0.464   -0.1876 0.0125  162 ARG   A NH2  
1282 N  N    . ASN   A 164 ? 0.9184 1.5176 0.1897 0.3217  -0.3389 -0.1227 163 ASN   A N    
1283 C  CA   . ASN   A 164 ? 0.9005 1.5059 0.2101 0.2854  -0.3565 -0.1462 163 ASN   A CA   
1284 C  C    . ASN   A 164 ? 0.9021 1.4626 0.2214 0.2698  -0.3583 -0.1586 163 ASN   A C    
1285 O  O    . ASN   A 164 ? 0.9006 1.4753 0.2333 0.2564  -0.372  -0.1859 163 ASN   A O    
1286 C  CB   . ASN   A 164 ? 0.8923 1.5705 0.2108 0.2851  -0.3739 -0.1714 163 ASN   A CB   
1287 C  CG   . ASN   A 164 ? 0.911  1.5969 0.2665 0.2446  -0.3895 -0.1939 163 ASN   A CG   
1288 O  OD1  . ASN   A 164 ? 0.9174 1.5933 0.2922 0.2243  -0.3886 -0.1844 163 ASN   A OD1  
1289 N  ND2  . ASN   A 164 ? 0.9085 1.6091 0.2721 0.2314  -0.4026 -0.2246 163 ASN   A ND2  
1290 N  N    . HIS   A 165 ? 0.9051 1.4141 0.2141 0.2743  -0.3433 -0.1393 164 HIS   A N    
1291 C  CA   . HIS   A 165 ? 0.9087 1.3798 0.2252 0.2656  -0.3428 -0.1478 164 HIS   A CA   
1292 C  C    . HIS   A 165 ? 0.9186 1.3383 0.2366 0.2584  -0.3288 -0.1243 164 HIS   A C    
1293 O  O    . HIS   A 165 ? 0.9355 1.3447 0.2294 0.2752  -0.3124 -0.1031 164 HIS   A O    
1294 C  CB   . HIS   A 165 ? 0.9244 1.4114 0.2149 0.2926  -0.3385 -0.1556 164 HIS   A CB   
1295 C  CG   . HIS   A 165 ? 0.9618 1.4159 0.2581 0.2883  -0.3364 -0.1646 164 HIS   A CG   
1296 N  ND1  . HIS   A 165 ? 0.985  1.4216 0.3076 0.2653  -0.3488 -0.1848 164 HIS   A ND1  
1297 C  CD2  . HIS   A 165 ? 0.9871 1.425  0.2644 0.306   -0.3224 -0.156  164 HIS   A CD2  
1298 C  CE1  . HIS   A 165 ? 1.0012 1.4129 0.3208 0.2721  -0.3424 -0.1875 164 HIS   A CE1  
1299 N  NE2  . HIS   A 165 ? 1.005  1.4196 0.2993 0.2953  -0.3268 -0.1709 164 HIS   A NE2  
1300 N  N    . GLY   A 166 ? 0.9043 1.2921 0.2487 0.2332  -0.3347 -0.1286 165 GLY   A N    
1301 C  CA   . GLY   A 166 ? 0.9049 1.2496 0.2553 0.2229  -0.3247 -0.1094 165 GLY   A CA   
1302 C  C    . GLY   A 166 ? 0.8906 1.2075 0.2702 0.198   -0.3349 -0.1172 165 GLY   A C    
1303 O  O    . GLY   A 166 ? 0.8874 1.2109 0.2801 0.189   -0.3479 -0.1391 165 GLY   A O    
1304 N  N    . HIS   A 167 ? 0.8803 1.1648 0.268  0.1865  -0.3285 -0.0995 166 HIS   A N    
1305 C  CA   . HIS   A 167 ? 0.8694 1.1248 0.2815 0.166   -0.3366 -0.1017 166 HIS   A CA   
1306 C  C    . HIS   A 167 ? 0.8588 1.0911 0.2741 0.1552  -0.3288 -0.0783 166 HIS   A C    
1307 O  O    . HIS   A 167 ? 0.8669 1.0914 0.2738 0.1629  -0.3178 -0.0672 166 HIS   A O    
1308 C  CB   . HIS   A 167 ? 0.886  1.1279 0.3043 0.1732  -0.3392 -0.1151 166 HIS   A CB   
1309 C  CG   . HIS   A 167 ? 0.9271 1.1424 0.3662 0.1567  -0.3504 -0.1254 166 HIS   A CG   
1310 N  ND1  . HIS   A 167 ? 0.9549 1.1662 0.3966 0.1589  -0.3584 -0.1501 166 HIS   A ND1  
1311 C  CD2  . HIS   A 167 ? 0.9503 1.1388 0.4043 0.1387  -0.3534 -0.1137 166 HIS   A CD2  
1312 C  CE1  . HIS   A 167 ? 0.9697 1.1474 0.427  0.1425  -0.3647 -0.1518 166 HIS   A CE1  
1313 N  NE2  . HIS   A 167 ? 0.9716 1.1361 0.4368 0.1307  -0.3623 -0.1295 166 HIS   A NE2  
1314 N  N    . ILE   A 168 ? 0.8393 1.0624 0.2662 0.1358  -0.3339 -0.0717 167 ILE   A N    
1315 C  CA   . ILE   A 168 ? 0.8388 1.0415 0.2672 0.1242  -0.3274 -0.0508 167 ILE   A CA   
1316 C  C    . ILE   A 168 ? 0.8353 1.0112 0.2838 0.1105  -0.335  -0.0492 167 ILE   A C    
1317 O  O    . ILE   A 168 ? 0.8377 1.0026 0.2996 0.0955  -0.3445 -0.0535 167 ILE   A O    
1318 C  CB   . ILE   A 168 ? 0.8409 1.051  0.2632 0.1153  -0.3246 -0.0403 167 ILE   A CB   
1319 C  CG1  . ILE   A 168 ? 0.8464 1.0809 0.2445 0.1351  -0.3149 -0.0387 167 ILE   A CG1  
1320 C  CG2  . ILE   A 168 ? 0.8541 1.0412 0.276  0.1016  -0.3182 -0.0208 167 ILE   A CG2  
1321 C  CD1  . ILE   A 168 ? 0.867  1.0911 0.2428 0.1491  -0.2987 -0.027  167 ILE   A CD1  
1322 N  N    . VAL   A 169 ? 0.8258 0.9928 0.2754 0.1164  -0.33   -0.0423 168 VAL   A N    
1323 C  CA   . VAL   A 169 ? 0.8198 0.9663 0.2862 0.1097  -0.3362 -0.0383 168 VAL   A CA   
1324 C  C    . VAL   A 169 ? 0.8139 0.9511 0.2821 0.0946  -0.3335 -0.0182 168 VAL   A C    
1325 O  O    . VAL   A 169 ? 0.814  0.9584 0.2738 0.0952  -0.3236 -0.0076 168 VAL   A O    
1326 C  CB   . VAL   A 169 ? 0.8242 0.9742 0.2944 0.1264  -0.3339 -0.0441 168 VAL   A CB   
1327 C  CG1  . VAL   A 169 ? 0.8302 0.9628 0.3169 0.1238  -0.34   -0.0376 168 VAL   A CG1  
1328 C  CG2  . VAL   A 169 ? 0.8295 0.9854 0.2967 0.1405  -0.3375 -0.066  168 VAL   A CG2  
1329 N  N    . THR   A 170 ? 0.8079 0.9284 0.2853 0.0794  -0.3416 -0.0138 169 THR   A N    
1330 C  CA   . THR   A 170 ? 0.8074 0.9191 0.2853 0.0646  -0.3406 0.0043  169 THR   A CA   
1331 C  C    . THR   A 170 ? 0.8086 0.9071 0.2999 0.0658  -0.3472 0.0105  169 THR   A C    
1332 O  O    . THR   A 170 ? 0.8134 0.8913 0.3137 0.0644  -0.3558 0.0065  169 THR   A O    
1333 C  CB   . THR   A 170 ? 0.8193 0.9234 0.2971 0.0482  -0.344  0.0072  169 THR   A CB   
1334 O  OG1  . THR   A 170 ? 0.8241 0.9466 0.2904 0.0512  -0.3383 0.0016  169 THR   A OG1  
1335 C  CG2  . THR   A 170 ? 0.8285 0.9232 0.3042 0.0329  -0.3428 0.0255  169 THR   A CG2  
1336 N  N    . VAL   A 171 ? 0.8035 0.9142 0.295  0.0685  -0.3427 0.0201  170 VAL   A N    
1337 C  CA   . VAL   A 171 ? 0.8055 0.9128 0.31   0.0731  -0.3494 0.0274  170 VAL   A CA   
1338 C  C    . VAL   A 171 ? 0.8167 0.9148 0.3213 0.0572  -0.3539 0.044   170 VAL   A C    
1339 O  O    . VAL   A 171 ? 0.82   0.9316 0.3171 0.0456  -0.3486 0.0539  170 VAL   A O    
1340 C  CB   . VAL   A 171 ? 0.8026 0.9362 0.3115 0.0849  -0.3439 0.0275  170 VAL   A CB   
1341 C  CG1  . VAL   A 171 ? 0.8025 0.9394 0.3263 0.0931  -0.352  0.0356  170 VAL   A CG1  
1342 C  CG2  . VAL   A 171 ? 0.8071 0.9485 0.3142 0.1021  -0.3391 0.0113  170 VAL   A CG2  
1343 N  N    . ALA   A 172 ? 0.8242 0.8964 0.3343 0.0557  -0.3627 0.0465  171 ALA   A N    
1344 C  CA   . ALA   A 172 ? 0.8332 0.8929 0.3416 0.0425  -0.3674 0.0632  171 ALA   A CA   
1345 C  C    . ALA   A 172 ? 0.8365 0.8842 0.354  0.057   -0.3758 0.0711  171 ALA   A C    
1346 O  O    . ALA   A 172 ? 0.8373 0.8932 0.3627 0.0763  -0.3763 0.0636  171 ALA   A O    
1347 C  CB   . ALA   A 172 ? 0.8448 0.8818 0.3479 0.0269  -0.368  0.0616  171 ALA   A CB   
1348 N  N    . SER   A 173 ? 0.841  0.8708 0.3557 0.0507  -0.3814 0.0866  172 SER   A N    
1349 C  CA   . SER   A 173 ? 0.8534 0.8694 0.3727 0.0681  -0.3884 0.0965  172 SER   A CA   
1350 C  C    . SER   A 173 ? 0.873  0.8402 0.3848 0.0613  -0.3911 0.1028  172 SER   A C    
1351 O  O    . SER   A 173 ? 0.88   0.833  0.3862 0.0409  -0.3879 0.0987  172 SER   A O    
1352 C  CB   . SER   A 173 ? 0.8675 0.9164 0.3876 0.068   -0.392  0.1137  172 SER   A CB   
1353 O  OG   . SER   A 173 ? 0.8989 0.9374 0.4196 0.0838  -0.3997 0.129   172 SER   A OG   
1354 N  N    . VAL   A 174 ? 0.8807 0.8224 0.3911 0.0784  -0.3959 0.1136  173 VAL   A N    
1355 C  CA   . VAL   A 174 ? 0.907  0.7978 0.406  0.0712  -0.3966 0.124   173 VAL   A CA   
1356 C  C    . VAL   A 174 ? 0.9147 0.8129 0.4048 0.0476  -0.3967 0.1402  173 VAL   A C    
1357 O  O    . VAL   A 174 ? 0.9268 0.7885 0.4075 0.0315  -0.3942 0.145   173 VAL   A O    
1358 C  CB   . VAL   A 174 ? 0.925  0.7842 0.4192 0.098   -0.4001 0.1363  173 VAL   A CB   
1359 C  CG1  . VAL   A 174 ? 0.9434 0.7628 0.4376 0.1121  -0.3966 0.1182  173 VAL   A CG1  
1360 C  CG2  . VAL   A 174 ? 0.9126 0.8187 0.4146 0.1208  -0.406  0.1482  173 VAL   A CG2  
1361 N  N    . CYS   A 175 ? 0.9059 0.8519 0.398  0.0435  -0.3982 0.1466  174 CYS   A N    
1362 C  CA   . CYS   A 175 ? 0.9159 0.8783 0.3985 0.022   -0.3974 0.1583  174 CYS   A CA   
1363 C  C    . CYS   A 175 ? 0.9311 0.8918 0.4109 -0.0015 -0.3896 0.1466  174 CYS   A C    
1364 O  O    . CYS   A 175 ? 0.9311 0.9089 0.4025 -0.0179 -0.3866 0.1526  174 CYS   A O    
1365 C  CB   . CYS   A 175 ? 0.9001 0.9131 0.3855 0.0249  -0.4    0.1632  174 CYS   A CB   
1366 S  SG   . CYS   A 175 ? 0.9015 0.9334 0.393  0.054   -0.4101 0.1773  174 CYS   A SG   
1367 N  N    . GLY   A 176 ? 0.9391 0.8838 0.4253 -0.0008 -0.3864 0.129   175 GLY   A N    
1368 C  CA   . GLY   A 176 ? 0.9466 0.8914 0.4322 -0.0184 -0.3803 0.1165  175 GLY   A CA   
1369 C  C    . GLY   A 176 ? 0.9644 0.8691 0.4483 -0.0302 -0.3795 0.115   175 GLY   A C    
1370 O  O    . GLY   A 176 ? 0.9647 0.8723 0.4488 -0.0483 -0.3749 0.1076  175 GLY   A O    
1371 N  N    . HIS   A 177 ? 0.9777 0.8447 0.4591 -0.0198 -0.383  0.1221  176 HIS   A N    
1372 C  CA   . HIS   A 177 ? 1.003  0.8211 0.4788 -0.0311 -0.3805 0.1226  176 HIS   A CA   
1373 C  C    . HIS   A 177 ? 1.0293 0.8208 0.491  -0.0345 -0.3809 0.1486  176 HIS   A C    
1374 O  O    . HIS   A 177 ? 1.0486 0.8047 0.5026 -0.0529 -0.3759 0.1527  176 HIS   A O    
1375 C  CB   . HIS   A 177 ? 1.0176 0.8023 0.4961 -0.0151 -0.3812 0.1083  176 HIS   A CB   
1376 C  CG   . HIS   A 177 ? 1.029  0.8334 0.518  -0.0172 -0.38   0.0812  176 HIS   A CG   
1377 N  ND1  . HIS   A 177 ? 1.0562 0.8413 0.5463 -0.037  -0.3764 0.0638  176 HIS   A ND1  
1378 C  CD2  . HIS   A 177 ? 1.0253 0.8696 0.5226 -0.0028 -0.3815 0.0695  176 HIS   A CD2  
1379 C  CE1  . HIS   A 177 ? 1.0482 0.864  0.5469 -0.0318 -0.3772 0.0423  176 HIS   A CE1  
1380 N  NE2  . HIS   A 177 ? 1.0338 0.8831 0.536  -0.0107 -0.3796 0.0457  176 HIS   A NE2  
1381 N  N    . GLU   A 178 ? 1.0268 0.8385 0.4843 -0.0185 -0.3863 0.166   177 GLU   A N    
1382 C  CA   . GLU   A 178 ? 1.0463 0.8403 0.488  -0.0186 -0.3879 0.1922  177 GLU   A CA   
1383 C  C    . GLU   A 178 ? 1.0325 0.8726 0.473  -0.0065 -0.395  0.2057  177 GLU   A C    
1384 O  O    . GLU   A 178 ? 1.023  0.8875 0.4729 0.015   -0.4002 0.2016  177 GLU   A O    
1385 C  CB   . GLU   A 178 ? 1.104  0.8383 0.535  -0.0043 -0.3871 0.2013  177 GLU   A CB   
1386 C  CG   . GLU   A 178 ? 1.1829 0.8995 0.5951 0.0054  -0.3896 0.2309  177 GLU   A CG   
1387 C  CD   . GLU   A 178 ? 1.2715 0.9965 0.6834 0.0422  -0.3975 0.2413  177 GLU   A CD   
1388 O  OE1  . GLU   A 178 ? 1.2447 1.0018 0.6733 0.0578  -0.4013 0.226   177 GLU   A OE1  
1389 O  OE2  . GLU   A 178 ? 1.3397 1.0408 0.7337 0.0567  -0.3993 0.2658  177 GLU   A OE2  
1390 N  N    . GLY   A 179 ? 1.0276 0.881  0.4562 -0.022  -0.3945 0.2205  178 GLY   A N    
1391 C  CA   . GLY   A 179 ? 1.016  0.9145 0.4406 -0.0178 -0.4005 0.231   178 GLY   A CA   
1392 C  C    . GLY   A 179 ? 1.0193 0.9215 0.4374 0.0064  -0.4095 0.2504  178 GLY   A C    
1393 O  O    . GLY   A 179 ? 1.0401 0.901  0.4449 0.015   -0.4097 0.2671  178 GLY   A O    
1394 N  N    . ILE   A 180 ? 0.9972 0.9512 0.4229 0.0167  -0.4163 0.2494  179 ILE   A N    
1395 C  CA   . ILE   A 180 ? 0.9949 0.9695 0.4178 0.0419  -0.4264 0.2664  179 ILE   A CA   
1396 C  C    . ILE   A 180 ? 0.9917 1.0179 0.4055 0.0312  -0.4326 0.2766  179 ILE   A C    
1397 O  O    . ILE   A 180 ? 0.983  1.034  0.3972 0.0074  -0.4282 0.2647  179 ILE   A O    
1398 C  CB   . ILE   A 180 ? 0.9812 0.9761 0.4244 0.0684  -0.4299 0.2548  179 ILE   A CB   
1399 C  CG1  . ILE   A 180 ? 0.9619 1.0194 0.4203 0.0606  -0.4309 0.2397  179 ILE   A CG1  
1400 C  CG2  . ILE   A 180 ? 0.9988 0.9455 0.449  0.0762  -0.4233 0.2405  179 ILE   A CG2  
1401 C  CD1  . ILE   A 180 ? 0.9553 1.0617 0.4213 0.0819  -0.4405 0.2481  179 ILE   A CD1  
1402 N  N    . PRO   A 181 ? 0.9991 1.0416 0.4021 0.0486  -0.4422 0.2981  180 PRO   A N    
1403 C  CA   . PRO   A 181 ? 0.9898 1.0851 0.383  0.0362  -0.4488 0.3052  180 PRO   A CA   
1404 C  C    . PRO   A 181 ? 0.9644 1.1256 0.3759 0.0328  -0.4525 0.2887  180 PRO   A C    
1405 O  O    . PRO   A 181 ? 0.9568 1.1317 0.3885 0.0515  -0.4539 0.2795  180 PRO   A O    
1406 C  CB   . PRO   A 181 ? 1.0081 1.1044 0.3858 0.0617  -0.4589 0.3326  180 PRO   A CB   
1407 C  CG   . PRO   A 181 ? 1.0362 1.0635 0.4094 0.0819  -0.4539 0.3417  180 PRO   A CG   
1408 C  CD   . PRO   A 181 ? 1.0105 1.0233 0.4065 0.0813  -0.4471 0.3173  180 PRO   A CD   
1409 N  N    . TYR   A 182 ? 0.9536 1.1531 0.3562 0.0074  -0.4526 0.2841  181 TYR   A N    
1410 C  CA   . TYR   A 182 ? 0.9371 1.1956 0.3514 -0.0057 -0.4532 0.2673  181 TYR   A CA   
1411 C  C    . TYR   A 182 ? 0.9268 1.1705 0.3521 -0.0206 -0.44   0.2441  181 TYR   A C    
1412 O  O    . TYR   A 182 ? 0.9137 1.1908 0.3404 -0.0399 -0.4354 0.2298  181 TYR   A O    
1413 C  CB   . TYR   A 182 ? 0.9288 1.2452 0.3608 0.0185  -0.4651 0.2707  181 TYR   A CB   
1414 C  CG   . TYR   A 182 ? 0.9666 1.2945 0.3879 0.043   -0.4784 0.2959  181 TYR   A CG   
1415 C  CD1  . TYR   A 182 ? 0.993  1.3356 0.3904 0.0295  -0.4839 0.3088  181 TYR   A CD1  
1416 C  CD2  . TYR   A 182 ? 0.9893 1.3099 0.4208 0.0819  -0.4844 0.3078  181 TYR   A CD2  
1417 C  CE1  . TYR   A 182 ? 1.0128 1.3657 0.397  0.0544  -0.4958 0.334   181 TYR   A CE1  
1418 C  CE2  . TYR   A 182 ? 1.0096 1.3368 0.4275 0.1086  -0.4954 0.3334  181 TYR   A CE2  
1419 C  CZ   . TYR   A 182 ? 1.0267 1.3714 0.421  0.095   -0.5014 0.3471  181 TYR   A CZ   
1420 O  OH   . TYR   A 182 ? 1.0634 1.4143 0.4414 0.1241  -0.512  0.3741  181 TYR   A OH   
1421 N  N    . LEU   A 183 ? 0.9297 1.1228 0.3606 -0.0125 -0.4333 0.2401  182 LEU   A N    
1422 C  CA   . LEU   A 183 ? 0.92   1.0994 0.3595 -0.0228 -0.4216 0.2198  182 LEU   A CA   
1423 C  C    . LEU   A 183 ? 0.9189 1.054  0.3443 -0.0409 -0.4116 0.2174  182 LEU   A C    
1424 O  O    . LEU   A 183 ? 0.9207 1.0287 0.354  -0.0384 -0.4049 0.2067  182 LEU   A O    
1425 C  CB   . LEU   A 183 ? 0.9217 1.091  0.3818 0.0022  -0.4223 0.2125  182 LEU   A CB   
1426 C  CG   . LEU   A 183 ? 0.9222 1.1408 0.3991 0.0222  -0.4303 0.213   182 LEU   A CG   
1427 C  CD1  . LEU   A 183 ? 0.9265 1.1293 0.4205 0.0479  -0.4293 0.2055  182 LEU   A CD1  
1428 C  CD2  . LEU   A 183 ? 0.9148 1.1844 0.3962 0.0033  -0.4262 0.2001  182 LEU   A CD2  
1429 N  N    . ILE   A 184 ? 0.9141 1.0458 0.319  -0.0585 -0.4106 0.227   183 ILE   A N    
1430 C  CA   . ILE   A 184 ? 0.9203 1.0173 0.3128 -0.0753 -0.4002 0.225   183 ILE   A CA   
1431 C  C    . ILE   A 184 ? 0.9143 1.016  0.3069 -0.0885 -0.3879 0.2058  183 ILE   A C    
1432 O  O    . ILE   A 184 ? 0.933  1.009  0.3299 -0.0888 -0.3807 0.1985  183 ILE   A O    
1433 C  CB   . ILE   A 184 ? 0.9321 1.0229 0.3011 -0.0893 -0.4005 0.2402  183 ILE   A CB   
1434 C  CG1  . ILE   A 184 ? 0.9483 1.0388 0.313  -0.0733 -0.4128 0.2616  183 ILE   A CG1  
1435 C  CG2  . ILE   A 184 ? 0.9472 1.002  0.3085 -0.1022 -0.3896 0.2392  183 ILE   A CG2  
1436 C  CD1  . ILE   A 184 ? 0.9723 1.0596 0.311  -0.0854 -0.4136 0.2786  183 ILE   A CD1  
1437 N  N    . PRO   A 185 ? 0.8905 1.0231 0.2776 -0.099  -0.3844 0.197   184 PRO   A N    
1438 C  CA   . PRO   A 185 ? 0.8843 1.0118 0.2674 -0.1083 -0.3702 0.1804  184 PRO   A CA   
1439 C  C    . PRO   A 185 ? 0.8649 0.9876 0.2685 -0.0919 -0.3686 0.1694  184 PRO   A C    
1440 O  O    . PRO   A 185 ? 0.8723 0.9764 0.2746 -0.092  -0.359  0.1603  184 PRO   A O    
1441 C  CB   . PRO   A 185 ? 0.8903 1.0486 0.2619 -0.1237 -0.3671 0.1746  184 PRO   A CB   
1442 C  CG   . PRO   A 185 ? 0.8832 1.076  0.2656 -0.1157 -0.3823 0.1837  184 PRO   A CG   
1443 C  CD   . PRO   A 185 ? 0.871  1.0443 0.2539 -0.1036 -0.3922 0.201   184 PRO   A CD   
1444 N  N    . TYR   A 186 ? 0.8383 0.9797 0.2602 -0.0755 -0.3783 0.1708  185 TYR   A N    
1445 C  CA   . TYR   A 186 ? 0.8247 0.9641 0.2653 -0.0579 -0.3777 0.1604  185 TYR   A CA   
1446 C  C    . TYR   A 186 ? 0.8268 0.9292 0.2736 -0.0478 -0.3788 0.1603  185 TYR   A C    
1447 O  O    . TYR   A 186 ? 0.8344 0.9266 0.2863 -0.0436 -0.3724 0.1476  185 TYR   A O    
1448 C  CB   . TYR   A 186 ? 0.8059 0.9778 0.2631 -0.0418 -0.3875 0.1633  185 TYR   A CB   
1449 C  CG   . TYR   A 186 ? 0.8075 0.9759 0.2836 -0.02   -0.3879 0.1541  185 TYR   A CG   
1450 C  CD1  . TYR   A 186 ? 0.8113 0.9961 0.2931 -0.0198 -0.379  0.1395  185 TYR   A CD1  
1451 C  CD2  . TYR   A 186 ? 0.823  0.9696 0.3085 0.0009  -0.396  0.1601  185 TYR   A CD2  
1452 C  CE1  . TYR   A 186 ? 0.8197 1.0039 0.3172 0.001   -0.3791 0.1307  185 TYR   A CE1  
1453 C  CE2  . TYR   A 186 ? 0.8299 0.9718 0.3302 0.0214  -0.3958 0.1501  185 TYR   A CE2  
1454 C  CZ   . TYR   A 186 ? 0.8331 0.9966 0.3401 0.0216  -0.3879 0.1352  185 TYR   A CZ   
1455 O  OH   . TYR   A 186 ? 0.8492 1.0093 0.3691 0.0425  -0.3874 0.125   185 TYR   A OH   
1456 N  N    . CYS   A 187 ? 0.8205 0.9033 0.2653 -0.0446 -0.3864 0.1741  186 CYS   A N    
1457 C  CA   . CYS   A 187 ? 0.8256 0.8701 0.2742 -0.0402 -0.3864 0.1739  186 CYS   A CA   
1458 C  C    . CYS   A 187 ? 0.8242 0.856  0.2647 -0.0572 -0.3766 0.1669  186 CYS   A C    
1459 O  O    . CYS   A 187 ? 0.8352 0.85   0.2835 -0.0548 -0.3737 0.1566  186 CYS   A O    
1460 C  CB   . CYS   A 187 ? 0.843  0.8648 0.286  -0.0354 -0.394  0.1924  186 CYS   A CB   
1461 S  SG   . CYS   A 187 ? 0.8837 0.9201 0.3357 -0.0076 -0.4058 0.2027  186 CYS   A SG   
1462 N  N    . SER   A 188 ? 0.8059 0.8457 0.2417 -0.0746 -0.3645 0.169   187 SER   A N    
1463 C  CA   . SER   A 188 ? 0.8094 0.842  0.2347 -0.0873 -0.3552 0.1639  187 SER   A CA   
1464 C  C    . SER   A 188 ? 0.8039 0.8457 0.2323 -0.0808 -0.3488 0.1473  187 SER   A C    
1465 O  O    . SER   A 188 ? 0.8142 0.8501 0.2382 -0.081  -0.3482 0.141   187 SER   A O    
1466 C  CB   . SER   A 188 ? 0.8317 0.8747 0.23   -0.1025 -0.3531 0.1723  187 SER   A CB   
1467 O  OG   . SER   A 188 ? 0.872  0.9049 0.2578 -0.1127 -0.3463 0.1726  187 SER   A OG   
1468 N  N    . SER   A 189 ? 0.7824 0.8392 0.2261 -0.0752 -0.3397 0.139   188 SER   A N    
1469 C  CA   . SER   A 189 ? 0.7722 0.8352 0.2194 -0.0675 -0.3304 0.1246  188 SER   A CA   
1470 C  C    . SER   A 189 ? 0.743  0.7974 0.2208 -0.0522 -0.3283 0.1135  188 SER   A C    
1471 O  O    . SER   A 189 ? 0.7367 0.7895 0.2171 -0.0471 -0.3222 0.1026  188 SER   A O    
1472 C  CB   . SER   A 189 ? 0.7951 0.8812 0.2195 -0.0679 -0.3342 0.1241  188 SER   A CB   
1473 O  OG   . SER   A 189 ? 0.8235 0.927  0.2568 -0.0577 -0.3478 0.1265  188 SER   A OG   
1474 N  N    . LYS   A 190 ? 0.7246 0.7725 0.2241 -0.0438 -0.3323 0.1158  189 LYS   A N    
1475 C  CA   . LYS   A 190 ? 0.72   0.7574 0.2295 -0.0283 -0.3387 0.1069  189 LYS   A CA   
1476 C  C    . LYS   A 190 ? 0.7397 0.7581 0.2349 -0.0335 -0.3494 0.1059  189 LYS   A C    
1477 O  O    . LYS   A 190 ? 0.7499 0.7701 0.2389 -0.0261 -0.3566 0.0936  189 LYS   A O    
1478 C  CB   . LYS   A 190 ? 0.7221 0.7585 0.2388 -0.0142 -0.3493 0.1133  189 LYS   A CB   
1479 C  CG   . LYS   A 190 ? 0.7477 0.8233 0.2504 -0.0037 -0.3618 0.116   189 LYS   A CG   
1480 C  CD   . LYS   A 190 ? 0.8089 0.9011 0.3006 0.0088  -0.3676 0.103   189 LYS   A CD   
1481 C  CE   . LYS   A 190 ? 0.8585 0.9755 0.3412 -0.0002 -0.3571 0.0994  189 LYS   A CE   
1482 N  NZ   . LYS   A 190 ? 0.8889 1.0114 0.3728 0.0103  -0.3491 0.0847  189 LYS   A NZ   
1483 N  N    . PHE   A 191 ? 0.7431 0.7474 0.2331 -0.0482 -0.3493 0.1174  190 PHE   A N    
1484 C  CA   . PHE   A 191 ? 0.7566 0.747  0.234  -0.0581 -0.3571 0.1164  190 PHE   A CA   
1485 C  C    . PHE   A 191 ? 0.7511 0.762  0.2252 -0.0618 -0.3502 0.1042  190 PHE   A C    
1486 O  O    . PHE   A 191 ? 0.7542 0.7662 0.2277 -0.0628 -0.3557 0.0928  190 PHE   A O    
1487 C  CB   . PHE   A 191 ? 0.7681 0.7459 0.234  -0.074  -0.3581 0.1335  190 PHE   A CB   
1488 C  CG   . PHE   A 191 ? 0.7944 0.7399 0.2532 -0.0745 -0.3688 0.1445  190 PHE   A CG   
1489 C  CD1  . PHE   A 191 ? 0.8089 0.7443 0.2651 -0.0617 -0.3758 0.1575  190 PHE   A CD1  
1490 C  CD2  . PHE   A 191 ? 0.8148 0.7387 0.2754 -0.0894 -0.3657 0.142   190 PHE   A CD2  
1491 C  CE1  . PHE   A 191 ? 0.831  0.7286 0.2833 -0.0602 -0.3789 0.169   190 PHE   A CE1  
1492 C  CE2  . PHE   A 191 ? 0.8386 0.7226 0.2956 -0.0924 -0.3679 0.1523  190 PHE   A CE2  
1493 C  CZ   . PHE   A 191 ? 0.8405 0.7083 0.2916 -0.0763 -0.374  0.1667  190 PHE   A CZ   
1494 N  N    . ALA   A 192 ? 0.7425 0.7692 0.2152 -0.0635 -0.3365 0.1058  191 ALA   A N    
1495 C  CA   . ALA   A 192 ? 0.7414 0.7856 0.2077 -0.0619 -0.327  0.0973  191 ALA   A CA   
1496 C  C    . ALA   A 192 ? 0.7396 0.7946 0.2107 -0.0454 -0.3283 0.0821  191 ALA   A C    
1497 O  O    . ALA   A 192 ? 0.741  0.8096 0.2096 -0.0419 -0.3273 0.0723  191 ALA   A O    
1498 C  CB   . ALA   A 192 ? 0.7428 0.7928 0.1981 -0.0653 -0.3139 0.1034  191 ALA   A CB   
1499 N  N    . ALA   A 193 ? 0.7276 0.7788 0.212  -0.0349 -0.3266 0.0792  192 ALA   A N    
1500 C  CA   . ALA   A 193 ? 0.7183 0.7778 0.2108 -0.0187 -0.3245 0.065   192 ALA   A CA   
1501 C  C    . ALA   A 193 ? 0.7165 0.7685 0.218  -0.0166 -0.3338 0.0532  192 ALA   A C    
1502 O  O    . ALA   A 193 ? 0.7105 0.7753 0.2158 -0.009  -0.3299 0.0394  192 ALA   A O    
1503 C  CB   . ALA   A 193 ? 0.7147 0.7766 0.2119 -0.0089 -0.3258 0.0665  192 ALA   A CB   
1504 N  N    . VAL   A 194 ? 0.7187 0.7482 0.2241 -0.0247 -0.3433 0.0583  193 VAL   A N    
1505 C  CA   . VAL   A 194 ? 0.7247 0.7411 0.2301 -0.0277 -0.3551 0.047   193 VAL   A CA   
1506 C  C    . VAL   A 194 ? 0.7208 0.751  0.2283 -0.0422 -0.3512 0.0398  193 VAL   A C    
1507 O  O    . VAL   A 194 ? 0.7148 0.7502 0.2293 -0.0433 -0.3534 0.0229  193 VAL   A O    
1508 C  CB   . VAL   A 194 ? 0.7443 0.7282 0.2422 -0.0323 -0.3682 0.0579  193 VAL   A CB   
1509 C  CG1  . VAL   A 194 ? 0.7558 0.7145 0.2596 -0.0426 -0.3705 0.0456  193 VAL   A CG1  
1510 C  CG2  . VAL   A 194 ? 0.7512 0.7284 0.2512 -0.0127 -0.372  0.062   193 VAL   A CG2  
1511 N  N    . GLY   A 195 ? 0.7203 0.7594 0.2243 -0.0528 -0.3433 0.0518  194 GLY   A N    
1512 C  CA   . GLY   A 195 ? 0.7219 0.7839 0.2232 -0.0639 -0.342  0.0472  194 GLY   A CA   
1513 C  C    . GLY   A 195 ? 0.7157 0.81   0.2186 -0.0493 -0.3326 0.0371  194 GLY   A C    
1514 O  O    . GLY   A 195 ? 0.7077 0.8271 0.2166 -0.052  -0.3321 0.0259  194 GLY   A O    
1515 N  N    . PHE   A 196 ? 0.7153 0.8097 0.2147 -0.0338 -0.323  0.0408  195 PHE   A N    
1516 C  CA   . PHE   A 196 ? 0.7116 0.8299 0.208  -0.0168 -0.3126 0.0332  195 PHE   A CA   
1517 C  C    . PHE   A 196 ? 0.7124 0.8434 0.2131 -0.0064 -0.3219 0.015   195 PHE   A C    
1518 O  O    . PHE   A 196 ? 0.7113 0.8715 0.21   0.0016  -0.3206 0.0052  195 PHE   A O    
1519 C  CB   . PHE   A 196 ? 0.7177 0.8276 0.2039 -0.0065 -0.3018 0.0413  195 PHE   A CB   
1520 C  CG   . PHE   A 196 ? 0.7253 0.8518 0.1999 0.0137  -0.2939 0.0344  195 PHE   A CG   
1521 C  CD1  . PHE   A 196 ? 0.7355 0.8789 0.1937 0.0219  -0.2853 0.0365  195 PHE   A CD1  
1522 C  CD2  . PHE   A 196 ? 0.7399 0.8678 0.2059 0.0268  -0.3012 0.0276  195 PHE   A CD2  
1523 C  CE1  . PHE   A 196 ? 0.7492 0.9048 0.188  0.0431  -0.2792 0.0328  195 PHE   A CE1  
1524 C  CE2  . PHE   A 196 ? 0.748  0.8896 0.1988 0.0457  -0.2933 0.023   195 PHE   A CE2  
1525 C  CZ   . PHE   A 196 ? 0.7459 0.8984 0.1878 0.0537  -0.2795 0.0259  195 PHE   A CZ   
1526 N  N    . HIS   A 197 ? 0.7139 0.8246 0.22   -0.0051 -0.3309 0.0097  196 HIS   A N    
1527 C  CA   . HIS   A 197 ? 0.71   0.8271 0.2227 0.0037  -0.3369 -0.0096 196 HIS   A CA   
1528 C  C    . HIS   A 197 ? 0.7187 0.8461 0.2317 -0.0136 -0.3504 -0.0222 196 HIS   A C    
1529 O  O    . HIS   A 197 ? 0.7116 0.8637 0.2302 -0.0086 -0.3508 -0.0396 196 HIS   A O    
1530 C  CB   . HIS   A 197 ? 0.7201 0.8128 0.2295 0.0113  -0.3467 -0.0115 196 HIS   A CB   
1531 C  CG   . HIS   A 197 ? 0.7403 0.8303 0.242  0.0134  -0.3649 -0.0323 196 HIS   A CG   
1532 N  ND1  . HIS   A 197 ? 0.7577 0.8618 0.2557 0.0322  -0.3649 -0.0468 196 HIS   A ND1  
1533 C  CD2  . HIS   A 197 ? 0.7542 0.8195 0.2646 -0.0018 -0.3708 -0.0407 196 HIS   A CD2  
1534 C  CE1  . HIS   A 197 ? 0.7631 0.8521 0.2677 0.0279  -0.3713 -0.0648 196 HIS   A CE1  
1535 N  NE2  . HIS   A 197 ? 0.7639 0.8272 0.2756 0.0068  -0.3745 -0.0621 196 HIS   A NE2  
1536 N  N    . ARG   A 198 ? 0.7349 0.8466 0.242  -0.035  -0.3606 -0.014  197 ARG   A N    
1537 C  CA   . ARG   A 198 ? 0.7451 0.8627 0.2634 -0.0563 -0.3641 -0.026  197 ARG   A CA   
1538 C  C    . ARG   A 198 ? 0.7312 0.8995 0.2508 -0.0582 -0.3609 -0.0311 197 ARG   A C    
1539 O  O    . ARG   A 198 ? 0.7193 0.912  0.251  -0.0678 -0.3633 -0.0494 197 ARG   A O    
1540 C  CB   . ARG   A 198 ? 0.7854 0.8655 0.3076 -0.0786 -0.3641 -0.0137 197 ARG   A CB   
1541 C  CG   . ARG   A 198 ? 0.8513 0.896  0.3801 -0.0904 -0.3691 -0.0277 197 ARG   A CG   
1542 C  CD   . ARG   A 198 ? 0.9125 0.9258 0.4438 -0.1173 -0.367  -0.0191 197 ARG   A CD   
1543 N  NE   . ARG   A 198 ? 0.9811 0.9483 0.504  -0.1121 -0.3666 0.0017  197 ARG   A NE   
1544 C  CZ   . ARG   A 198 ? 1.0325 0.9527 0.552  -0.1063 -0.3691 0       197 ARG   A CZ   
1545 N  NH1  . ARG   A 198 ? 1.028  0.936  0.5505 -0.1066 -0.3715 -0.0232 197 ARG   A NH1  
1546 N  NH2  . ARG   A 198 ? 1.0469 0.9328 0.5583 -0.0988 -0.369  0.0212  197 ARG   A NH2  
1547 N  N    . GLY   A 199 ? 0.7304 0.9147 0.2388 -0.0477 -0.3532 -0.0158 198 GLY   A N    
1548 C  CA   . GLY   A 199 ? 0.7222 0.9536 0.229  -0.0422 -0.3478 -0.0175 198 GLY   A CA   
1549 C  C    . GLY   A 199 ? 0.7199 0.9808 0.224  -0.017  -0.3449 -0.0295 198 GLY   A C    
1550 O  O    . GLY   A 199 ? 0.7069 1.0115 0.2222 -0.0132 -0.3417 -0.0406 198 GLY   A O    
1551 N  N    . LEU   A 200 ? 0.7275 0.9667 0.2209 0.0008  -0.343  -0.0272 199 LEU   A N    
1552 C  CA   . LEU   A 200 ? 0.728  0.9909 0.2142 0.0252  -0.3406 -0.0376 199 LEU   A CA   
1553 C  C    . LEU   A 200 ? 0.7446 1.0293 0.235  0.0194  -0.3579 -0.0626 199 LEU   A C    
1554 O  O    . LEU   A 200 ? 0.745  1.0726 0.232  0.0322  -0.3597 -0.0747 199 LEU   A O    
1555 C  CB   . LEU   A 200 ? 0.7291 0.9612 0.2089 0.0407  -0.332  -0.0307 199 LEU   A CB   
1556 C  CG   . LEU   A 200 ? 0.7218 0.9717 0.1985 0.0673  -0.3205 -0.0371 199 LEU   A CG   
1557 C  CD1  . LEU   A 200 ? 0.7221 0.995  0.1871 0.0827  -0.3064 -0.0274 199 LEU   A CD1  
1558 C  CD2  . LEU   A 200 ? 0.7361 0.96   0.1983 0.0772  -0.3192 -0.0315 199 LEU   A CD2  
1559 N  N    . THR   A 201 ? 0.7574 1.0099 0.2612 0       -0.3649 -0.0704 200 THR   A N    
1560 C  CA   . THR   A 201 ? 0.7624 1.0231 0.2768 -0.01   -0.3741 -0.0958 200 THR   A CA   
1561 C  C    . THR   A 201 ? 0.7631 1.0666 0.2903 -0.0296 -0.3776 -0.1075 200 THR   A C    
1562 O  O    . THR   A 201 ? 0.7525 1.0942 0.2831 -0.0282 -0.3839 -0.1294 200 THR   A O    
1563 C  CB   . THR   A 201 ? 0.7871 0.9922 0.3073 -0.0225 -0.3776 -0.0986 200 THR   A CB   
1564 O  OG1  . THR   A 201 ? 0.8068 0.9864 0.317  -0.0015 -0.3742 -0.0876 200 THR   A OG1  
1565 C  CG2  . THR   A 201 ? 0.7882 0.9908 0.3148 -0.033  -0.3853 -0.1266 200 THR   A CG2  
1566 N  N    . SER   A 202 ? 0.7748 1.0779 0.309  -0.0477 -0.3735 -0.0935 201 SER   A N    
1567 C  CA   . SER   A 202 ? 0.7719 1.123  0.3205 -0.0672 -0.3756 -0.104  201 SER   A CA   
1568 C  C    . SER   A 202 ? 0.7721 1.1893 0.3148 -0.0436 -0.3736 -0.1044 201 SER   A C    
1569 O  O    . SER   A 202 ? 0.7489 1.2208 0.3023 -0.0495 -0.3796 -0.1234 201 SER   A O    
1570 C  CB   . SER   A 202 ? 0.7843 1.1175 0.3412 -0.0926 -0.3703 -0.0887 201 SER   A CB   
1571 O  OG   . SER   A 202 ? 0.7805 1.1594 0.3544 -0.1165 -0.3719 -0.101  201 SER   A OG   
1572 N  N    . GLU   A 203 ? 0.7967 1.2092 0.3209 -0.0167 -0.3648 -0.084  202 GLU   A N    
1573 C  CA   . GLU   A 203 ? 0.8021 1.2681 0.3145 0.011   -0.3602 -0.0807 202 GLU   A CA   
1574 C  C    . GLU   A 203 ? 0.8058 1.2978 0.3085 0.0347  -0.3655 -0.0961 202 GLU   A C    
1575 O  O    . GLU   A 203 ? 0.7977 1.3517 0.3004 0.0479  -0.3683 -0.1051 202 GLU   A O    
1576 C  CB   . GLU   A 203 ? 0.8583 1.3019 0.3494 0.0301  -0.3463 -0.0543 202 GLU   A CB   
1577 C  CG   . GLU   A 203 ? 0.9109 1.4051 0.3887 0.0568  -0.3387 -0.0477 202 GLU   A CG   
1578 C  CD   . GLU   A 203 ? 0.9976 1.4589 0.4479 0.0768  -0.3228 -0.0237 202 GLU   A CD   
1579 O  OE1  . GLU   A 203 ? 1.0367 1.4833 0.4632 0.103   -0.3164 -0.0186 202 GLU   A OE1  
1580 O  OE2  . GLU   A 203 ? 1.008  1.4551 0.459  0.0645  -0.3159 -0.0106 202 GLU   A OE2  
1581 N  N    . LEU   A 204 ? 0.8142 1.2649 0.3095 0.0404  -0.3677 -0.1006 203 LEU   A N    
1582 C  CA   . LEU   A 204 ? 0.8049 1.2802 0.2901 0.0616  -0.3727 -0.1169 203 LEU   A CA   
1583 C  C    . LEU   A 204 ? 0.7918 1.3139 0.2949 0.0439  -0.3856 -0.1454 203 LEU   A C    
1584 O  O    . LEU   A 204 ? 0.7775 1.3592 0.2754 0.0612  -0.3897 -0.1561 203 LEU   A O    
1585 C  CB   . LEU   A 204 ? 0.8187 1.2421 0.2966 0.0665  -0.3726 -0.1187 203 LEU   A CB   
1586 C  CG   . LEU   A 204 ? 0.8485 1.2399 0.3052 0.0887  -0.3602 -0.0963 203 LEU   A CG   
1587 C  CD1  . LEU   A 204 ? 0.8708 1.2161 0.3271 0.0883  -0.3609 -0.0987 203 LEU   A CD1  
1588 C  CD2  . LEU   A 204 ? 0.8497 1.276  0.2827 0.1215  -0.3532 -0.0914 203 LEU   A CD2  
1589 N  N    . GLN   A 205 ? 0.7999 1.297  0.323  0.0085  -0.3911 -0.1563 204 GLN   A N    
1590 C  CA   . GLN   A 205 ? 0.7994 1.3327 0.3399 -0.0171 -0.4017 -0.185  204 GLN   A CA   
1591 C  C    . GLN   A 205 ? 0.7776 1.3875 0.3299 -0.0212 -0.4031 -0.1872 204 GLN   A C    
1592 O  O    . GLN   A 205 ? 0.759  1.4319 0.3163 -0.0204 -0.4119 -0.2096 204 GLN   A O    
1593 C  CB   . GLN   A 205 ? 0.8459 1.3221 0.4006 -0.0548 -0.4031 -0.1916 204 GLN   A CB   
1594 C  CG   . GLN   A 205 ? 0.9004 1.4013 0.4705 -0.0872 -0.4121 -0.224  204 GLN   A CG   
1595 C  CD   . GLN   A 205 ? 0.96   1.4905 0.5505 -0.1203 -0.4108 -0.2244 204 GLN   A CD   
1596 O  OE1  . GLN   A 205 ? 0.9549 1.5501 0.559  -0.1371 -0.4173 -0.2468 204 GLN   A OE1  
1597 N  NE2  . GLN   A 205 ? 0.9862 1.4741 0.5796 -0.1312 -0.4023 -0.2    204 GLN   A NE2  
1598 N  N    . ALA   A 206 ? 0.7782 1.3872 0.3339 -0.0237 -0.3945 -0.1646 205 ALA   A N    
1599 C  CA   . ALA   A 206 ? 0.762  1.444  0.3295 -0.0252 -0.3939 -0.164  205 ALA   A CA   
1600 C  C    . ALA   A 206 ? 0.7565 1.5012 0.3082 0.0164  -0.3935 -0.1611 205 ALA   A C    
1601 O  O    . ALA   A 206 ? 0.7312 1.5554 0.2947 0.0174  -0.3981 -0.1713 205 ALA   A O    
1602 C  CB   . ALA   A 206 ? 0.7744 1.4328 0.3447 -0.0339 -0.3828 -0.1389 205 ALA   A CB   
1603 N  N    . LEU   A 207 ? 0.7761 1.488  0.3005 0.051   -0.3873 -0.1469 206 LEU   A N    
1604 C  CA   . LEU   A 207 ? 0.772  1.5341 0.2753 0.0936  -0.3846 -0.1413 206 LEU   A CA   
1605 C  C    . LEU   A 207 ? 0.7817 1.5829 0.2792 0.1065  -0.3962 -0.1652 206 LEU   A C    
1606 O  O    . LEU   A 207 ? 0.7826 1.6252 0.2592 0.1444  -0.3944 -0.1603 206 LEU   A O    
1607 C  CB   . LEU   A 207 ? 0.7906 1.5003 0.2633 0.1245  -0.3689 -0.1126 206 LEU   A CB   
1608 C  CG   . LEU   A 207 ? 0.8023 1.4793 0.2735 0.1184  -0.3561 -0.0885 206 LEU   A CG   
1609 C  CD1  . LEU   A 207 ? 0.8326 1.4627 0.27   0.1486  -0.3403 -0.0646 206 LEU   A CD1  
1610 C  CD2  . LEU   A 207 ? 0.78   1.5226 0.2626 0.1203  -0.3547 -0.0863 206 LEU   A CD2  
1611 N  N    . GLY   A 208 ? 0.7881 1.576  0.3013 0.0761  -0.4073 -0.1906 207 GLY   A N    
1612 C  CA   . GLY   A 208 ? 0.7894 1.6109 0.297  0.0841  -0.4182 -0.2165 207 GLY   A CA   
1613 C  C    . GLY   A 208 ? 0.8071 1.5754 0.2891 0.1073  -0.4146 -0.2122 207 GLY   A C    
1614 O  O    . GLY   A 208 ? 0.8183 1.6112 0.2918 0.1181  -0.4217 -0.232  207 GLY   A O    
1615 N  N    . ILE   A 209 ? 0.815  1.512  0.2864 0.1135  -0.4022 -0.1875 208 ILE   A N    
1616 C  CA   . ILE   A 209 ? 0.8231 1.4698 0.2725 0.134   -0.396  -0.1806 208 ILE   A CA   
1617 C  C    . ILE   A 209 ? 0.8334 1.4352 0.2927 0.1112  -0.4028 -0.2005 208 ILE   A C    
1618 O  O    . ILE   A 209 ? 0.8411 1.3898 0.3142 0.0865  -0.401  -0.1957 208 ILE   A O    
1619 C  CB   . ILE   A 209 ? 0.8366 1.4318 0.2709 0.1481  -0.3797 -0.1479 208 ILE   A CB   
1620 C  CG1  . ILE   A 209 ? 0.8312 1.4632 0.2531 0.1703  -0.3707 -0.1282 208 ILE   A CG1  
1621 C  CG2  . ILE   A 209 ? 0.8572 1.4142 0.2685 0.1703  -0.3723 -0.1419 208 ILE   A CG2  
1622 C  CD1  . ILE   A 209 ? 0.8609 1.4441 0.2674 0.1791  -0.3545 -0.0996 208 ILE   A CD1  
1623 N  N    . THR   A 210 ? 0.8346 1.4566 0.284  0.1221  -0.4097 -0.2222 209 THR   A N    
1624 C  CA   . THR   A 210 ? 0.8523 1.433  0.3072 0.1044  -0.4154 -0.2439 209 THR   A CA   
1625 C  C    . THR   A 210 ? 0.8705 1.3996 0.3079 0.126   -0.4063 -0.2319 209 THR   A C    
1626 O  O    . THR   A 210 ? 0.8934 1.3633 0.3391 0.1119  -0.4037 -0.2288 209 THR   A O    
1627 C  CB   . THR   A 210 ? 0.8586 1.4895 0.3149 0.0965  -0.429  -0.28   209 THR   A CB   
1628 O  OG1  . THR   A 210 ? 0.8622 1.5635 0.3014 0.1275  -0.4312 -0.2801 209 THR   A OG1  
1629 C  CG2  . THR   A 210 ? 0.8499 1.4991 0.332  0.0551  -0.438  -0.3002 209 THR   A CG2  
1630 N  N    . GLY   A 211 ? 0.8586 1.4119 0.2715 0.1606  -0.4005 -0.2234 210 GLY   A N    
1631 C  CA   . GLY   A 211 ? 0.8786 1.3946 0.2728 0.1827  -0.3904 -0.2129 210 GLY   A CA   
1632 C  C    . GLY   A 211 ? 0.9016 1.3591 0.2991 0.179   -0.3786 -0.1873 210 GLY   A C    
1633 O  O    . GLY   A 211 ? 0.9243 1.3485 0.3145 0.1885  -0.3724 -0.1845 210 GLY   A O    
1634 N  N    . ILE   A 212 ? 0.8894 1.3376 0.2979 0.1653  -0.3752 -0.169  211 ILE   A N    
1635 C  CA   . ILE   A 212 ? 0.9007 1.2978 0.312  0.1595  -0.3652 -0.1459 211 ILE   A CA   
1636 C  C    . ILE   A 212 ? 0.9048 1.2638 0.3402 0.13    -0.3722 -0.1521 211 ILE   A C    
1637 O  O    . ILE   A 212 ? 0.9013 1.2658 0.3522 0.1078  -0.3774 -0.1534 211 ILE   A O    
1638 C  CB   . ILE   A 212 ? 0.9046 1.3058 0.3068 0.1654  -0.3545 -0.1201 211 ILE   A CB   
1639 C  CG1  . ILE   A 212 ? 0.9162 1.3467 0.2888 0.1985  -0.3449 -0.1116 211 ILE   A CG1  
1640 C  CG2  . ILE   A 212 ? 0.9245 1.275  0.3288 0.1566  -0.3451 -0.0995 211 ILE   A CG2  
1641 C  CD1  . ILE   A 212 ? 0.9344 1.37   0.2937 0.2075  -0.3337 -0.089  211 ILE   A CD1  
1642 N  N    . LYS   A 213 ? 0.9083 1.2288 0.3456 0.131   -0.3712 -0.1551 212 LYS   A N    
1643 C  CA   . LYS   A 213 ? 0.9106 1.1883 0.3663 0.1084  -0.3762 -0.1587 212 LYS   A CA   
1644 C  C    . LYS   A 213 ? 0.91   1.1541 0.3701 0.1035  -0.3687 -0.1316 212 LYS   A C    
1645 O  O    . LYS   A 213 ? 0.9145 1.1649 0.3625 0.117   -0.3589 -0.1133 212 LYS   A O    
1646 C  CB   . LYS   A 213 ? 0.9416 1.1966 0.3962 0.1151  -0.3793 -0.1778 212 LYS   A CB   
1647 C  CG   . LYS   A 213 ? 0.9857 1.2752 0.4297 0.1251  -0.385  -0.2045 212 LYS   A CG   
1648 C  CD   . LYS   A 213 ? 1.0494 1.3633 0.5027 0.1022  -0.3957 -0.226  212 LYS   A CD   
1649 C  CE   . LYS   A 213 ? 1.122  1.4729 0.5628 0.1132  -0.402  -0.2542 212 LYS   A CE   
1650 N  NZ   . LYS   A 213 ? 1.1509 1.5364 0.6004 0.0896  -0.4131 -0.279  212 LYS   A NZ   
1651 N  N    . THR   A 214 ? 0.9032 1.1106 0.3782 0.0835  -0.3727 -0.129  213 THR   A N    
1652 C  CA   . THR   A 214 ? 0.8977 1.0764 0.3766 0.0784  -0.3674 -0.1047 213 THR   A CA   
1653 C  C    . THR   A 214 ? 0.8889 1.0243 0.3774 0.0736  -0.371  -0.1059 213 THR   A C    
1654 O  O    . THR   A 214 ? 0.8932 1.009  0.3884 0.0608  -0.3774 -0.1213 213 THR   A O    
1655 C  CB   . THR   A 214 ? 0.9127 1.0962 0.3969 0.0592  -0.367  -0.0915 213 THR   A CB   
1656 O  OG1  . THR   A 214 ? 0.9199 1.1071 0.4151 0.039   -0.3749 -0.1075 213 THR   A OG1  
1657 C  CG2  . THR   A 214 ? 0.915  1.1323 0.3862 0.0697  -0.3593 -0.0807 213 THR   A CG2  
1658 N  N    . SER   A 215 ? 0.8771 0.9977 0.3651 0.0838  -0.366  -0.0899 214 SER   A N    
1659 C  CA   . SER   A 215 ? 0.876  0.9595 0.3722 0.0845  -0.3687 -0.0867 214 SER   A CA   
1660 C  C    . SER   A 215 ? 0.8622 0.9364 0.3619 0.0786  -0.3658 -0.0611 214 SER   A C    
1661 O  O    . SER   A 215 ? 0.8617 0.9572 0.3552 0.082   -0.3591 -0.0486 214 SER   A O    
1662 C  CB   . SER   A 215 ? 0.8928 0.9769 0.386  0.1077  -0.3663 -0.0959 214 SER   A CB   
1663 O  OG   . SER   A 215 ? 0.9239 0.9969 0.4154 0.11    -0.3711 -0.1209 214 SER   A OG   
1664 N  N    . CYS   A 216 ? 0.8473 0.8881 0.3543 0.0694  -0.3701 -0.0534 215 CYS   A N    
1665 C  CA   . CYS   A 216 ? 0.8282 0.8624 0.3374 0.0638  -0.3689 -0.0298 215 CYS   A CA   
1666 C  C    . CYS   A 216 ? 0.8188 0.8293 0.3335 0.0766  -0.3717 -0.024  215 CYS   A C    
1667 O  O    . CYS   A 216 ? 0.8295 0.8047 0.3457 0.0747  -0.3758 -0.0294 215 CYS   A O    
1668 C  CB   . CYS   A 216 ? 0.8349 0.8565 0.3448 0.0402  -0.3709 -0.0212 215 CYS   A CB   
1669 S  SG   . CYS   A 216 ? 0.8706 0.8813 0.3805 0.0322  -0.3707 0.0071  215 CYS   A SG   
1670 N  N    . LEU   A 217 ? 0.8018 0.8315 0.3187 0.0898  -0.3687 -0.0132 216 LEU   A N    
1671 C  CA   . LEU   A 217 ? 0.8066 0.823  0.3302 0.1057  -0.3716 -0.0063 216 LEU   A CA   
1672 C  C    . LEU   A 217 ? 0.8193 0.822  0.3446 0.0961  -0.3756 0.0158  216 LEU   A C    
1673 O  O    . LEU   A 217 ? 0.8107 0.8363 0.3348 0.086   -0.3737 0.0294  216 LEU   A O    
1674 C  CB   . LEU   A 217 ? 0.7902 0.841  0.3177 0.124   -0.3666 -0.0065 216 LEU   A CB   
1675 C  CG   . LEU   A 217 ? 0.8007 0.8482 0.3372 0.1456  -0.3692 -0.0016 216 LEU   A CG   
1676 C  CD1  . LEU   A 217 ? 0.8133 0.8339 0.3482 0.1631  -0.37   -0.0198 216 LEU   A CD1  
1677 C  CD2  . LEU   A 217 ? 0.7912 0.8837 0.3343 0.1556  -0.3637 0.0036  216 LEU   A CD2  
1678 N  N    . CYS   A 218 ? 0.8382 0.8007 0.363  0.0991  -0.3801 0.019   217 CYS   A N    
1679 C  CA   . CYS   A 218 ? 0.8609 0.8057 0.3838 0.0929  -0.3839 0.0405  217 CYS   A CA   
1680 C  C    . CYS   A 218 ? 0.8891 0.8185 0.4144 0.1184  -0.3872 0.0497  217 CYS   A C    
1681 O  O    . CYS   A 218 ? 0.9131 0.794  0.4316 0.1229  -0.3884 0.0509  217 CYS   A O    
1682 C  CB   . CYS   A 218 ? 0.8769 0.7834 0.3926 0.0709  -0.3844 0.0404  217 CYS   A CB   
1683 S  SG   . CYS   A 218 ? 0.8915 0.8242 0.4047 0.042   -0.3812 0.041   217 CYS   A SG   
1684 N  N    . PRO   A 219 ? 0.8825 0.8523 0.4164 0.1352  -0.3879 0.057   218 PRO   A N    
1685 C  CA   . PRO   A 219 ? 0.8916 0.8546 0.4289 0.1634  -0.3912 0.0664  218 PRO   A CA   
1686 C  C    . PRO   A 219 ? 0.9063 0.8733 0.4415 0.1634  -0.3971 0.092   218 PRO   A C    
1687 O  O    . PRO   A 219 ? 0.9063 0.8853 0.4378 0.1399  -0.3983 0.1018  218 PRO   A O    
1688 C  CB   . PRO   A 219 ? 0.8758 0.8898 0.4255 0.1806  -0.3883 0.0586  218 PRO   A CB   
1689 C  CG   . PRO   A 219 ? 0.8656 0.917  0.4164 0.157   -0.3841 0.0551  218 PRO   A CG   
1690 C  CD   . PRO   A 219 ? 0.8577 0.8814 0.3978 0.13    -0.3843 0.0561  218 PRO   A CD   
1691 N  N    . VAL   A 220 ? 0.9185 0.876  0.4541 0.192   -0.4006 0.1032  219 VAL   A N    
1692 C  CA   . VAL   A 220 ? 0.9316 0.8992 0.4641 0.1982  -0.4072 0.1286  219 VAL   A CA   
1693 C  C    . VAL   A 220 ? 0.9101 0.9553 0.4592 0.2072  -0.4107 0.1341  219 VAL   A C    
1694 O  O    . VAL   A 220 ? 0.8984 0.9802 0.4556 0.1908  -0.4066 0.1216  219 VAL   A O    
1695 C  CB   . VAL   A 220 ? 0.969  0.8793 0.4883 0.224   -0.4082 0.1404  219 VAL   A CB   
1696 C  CG1  . VAL   A 220 ? 1.0093 0.8473 0.5116 0.2041  -0.4034 0.135   219 VAL   A CG1  
1697 C  CG2  . VAL   A 220 ? 0.9737 0.883  0.4989 0.2612  -0.4059 0.1311  219 VAL   A CG2  
1698 N  N    . PHE   A 221 ? 0.9024 0.9752 0.4556 0.231   -0.4175 0.152   220 PHE   A N    
1699 C  CA   . PHE   A 221 ? 0.8801 1.0327 0.451  0.2346  -0.4205 0.1543  220 PHE   A CA   
1700 C  C    . PHE   A 221 ? 0.8664 1.0473 0.453  0.2521  -0.4146 0.1366  220 PHE   A C    
1701 O  O    . PHE   A 221 ? 0.8791 1.0345 0.4657 0.2832  -0.4129 0.1328  220 PHE   A O    
1702 C  CB   . PHE   A 221 ? 0.8731 1.0589 0.4462 0.2571  -0.4303 0.1768  220 PHE   A CB   
1703 C  CG   . PHE   A 221 ? 0.855  1.1273 0.4445 0.245   -0.4341 0.1782  220 PHE   A CG   
1704 C  CD1  . PHE   A 221 ? 0.8392 1.1741 0.4499 0.2673  -0.4344 0.1739  220 PHE   A CD1  
1705 C  CD2  . PHE   A 221 ? 0.8645 1.1554 0.4477 0.209   -0.4356 0.1816  220 PHE   A CD2  
1706 C  CE1  . PHE   A 221 ? 0.8176 1.2334 0.4437 0.2509  -0.4365 0.1729  220 PHE   A CE1  
1707 C  CE2  . PHE   A 221 ? 0.8443 1.2106 0.4401 0.1939  -0.4376 0.1802  220 PHE   A CE2  
1708 C  CZ   . PHE   A 221 ? 0.8139 1.2426 0.4316 0.2131  -0.438  0.1754  220 PHE   A CZ   
1709 N  N    . VAL   A 222 ? 0.8394 1.0701 0.4367 0.2323  -0.4098 0.126   221 VAL   A N    
1710 C  CA   . VAL   A 222 ? 0.8222 1.088  0.4343 0.2464  -0.4028 0.1105  221 VAL   A CA   
1711 C  C    . VAL   A 222 ? 0.7957 1.1441 0.4264 0.2481  -0.4054 0.1175  221 VAL   A C    
1712 O  O    . VAL   A 222 ? 0.7849 1.1638 0.4148 0.2204  -0.4076 0.1239  221 VAL   A O    
1713 C  CB   . VAL   A 222 ? 0.828  1.0812 0.435  0.2237  -0.3926 0.0914  221 VAL   A CB   
1714 C  CG1  . VAL   A 222 ? 0.8173 1.1003 0.4362 0.2421  -0.3845 0.0762  221 VAL   A CG1  
1715 C  CG2  . VAL   A 222 ? 0.8622 1.0434 0.4519 0.2164  -0.3919 0.0848  221 VAL   A CG2  
1716 N  N    . ASN   A 223 ? 0.7816 1.1675 0.4286 0.2807  -0.4048 0.1156  222 ASN   A N    
1717 C  CA   . ASN   A 223 ? 0.7545 1.228  0.4231 0.2847  -0.4071 0.1205  222 ASN   A CA   
1718 C  C    . ASN   A 223 ? 0.7445 1.2611 0.4213 0.2543  -0.3958 0.1059  222 ASN   A C    
1719 O  O    . ASN   A 223 ? 0.7375 1.2829 0.4269 0.2674  -0.3871 0.0941  222 ASN   A O    
1720 C  CB   . ASN   A 223 ? 0.7581 1.2565 0.4413 0.3316  -0.4079 0.1217  222 ASN   A CB   
1721 C  CG   . ASN   A 223 ? 0.7674 1.3642 0.4759 0.3409  -0.4119 0.1283  222 ASN   A CG   
1722 O  OD1  . ASN   A 223 ? 0.7729 1.4174 0.4862 0.315   -0.4179 0.136   222 ASN   A OD1  
1723 N  ND2  . ASN   A 223 ? 0.7593 1.3913 0.4843 0.3779  -0.4085 0.1243  222 ASN   A ND2  
1724 N  N    . THR   A 224 ? 0.7418 1.2585 0.4086 0.2144  -0.3943 0.1066  223 THR   A N    
1725 C  CA   . THR   A 224 ? 0.7295 1.2768 0.3982 0.1842  -0.3812 0.0941  223 THR   A CA   
1726 C  C    . THR   A 224 ? 0.7051 1.3119 0.3795 0.1542  -0.3827 0.0992  223 THR   A C    
1727 O  O    . THR   A 224 ? 0.6975 1.338  0.3751 0.1305  -0.3705 0.0894  223 THR   A O    
1728 C  CB   . THR   A 224 ? 0.7698 1.2541 0.4155 0.1616  -0.3726 0.0856  223 THR   A CB   
1729 O  OG1  . THR   A 224 ? 0.7949 1.2465 0.4248 0.1419  -0.3797 0.0958  223 THR   A OG1  
1730 C  CG2  . THR   A 224 ? 0.7923 1.2243 0.4318 0.1849  -0.3697 0.0759  223 THR   A CG2  
1731 N  N    . GLY   A 225 ? 0.6929 1.3095 0.3656 0.1537  -0.3963 0.1137  224 GLY   A N    
1732 C  CA   . GLY   A 225 ? 0.6732 1.3436 0.3477 0.1227  -0.399  0.117   224 GLY   A CA   
1733 C  C    . GLY   A 225 ? 0.694  1.3188 0.3426 0.0856  -0.395  0.1165  224 GLY   A C    
1734 O  O    . GLY   A 225 ? 0.6827 1.343  0.3276 0.0547  -0.3946 0.1161  224 GLY   A O    
1735 N  N    . PHE   A 226 ? 0.724  1.2715 0.354  0.0883  -0.3918 0.1156  225 PHE   A N    
1736 C  CA   . PHE   A 226 ? 0.7562 1.2535 0.3609 0.0599  -0.3877 0.116   225 PHE   A CA   
1737 C  C    . PHE   A 226 ? 0.7899 1.3004 0.3875 0.0503  -0.4007 0.1306  225 PHE   A C    
1738 O  O    . PHE   A 226 ? 0.79   1.3115 0.3748 0.0182  -0.3974 0.1293  225 PHE   A O    
1739 C  CB   . PHE   A 226 ? 0.7611 1.1868 0.3546 0.0742  -0.3858 0.1139  225 PHE   A CB   
1740 C  CG   . PHE   A 226 ? 0.768  1.1425 0.3378 0.0504  -0.38   0.1126  225 PHE   A CG   
1741 C  CD1  . PHE   A 226 ? 0.7714 1.1453 0.3285 0.0243  -0.3658 0.1033  225 PHE   A CD1  
1742 C  CD2  . PHE   A 226 ? 0.7841 1.1089 0.3435 0.0559  -0.3868 0.1204  225 PHE   A CD2  
1743 C  CE1  . PHE   A 226 ? 0.7952 1.1238 0.33   0.0072  -0.3596 0.1027  225 PHE   A CE1  
1744 C  CE2  . PHE   A 226 ? 0.8045 1.089  0.3444 0.0357  -0.3808 0.1188  225 PHE   A CE2  
1745 C  CZ   . PHE   A 226 ? 0.8034 1.0916 0.3314 0.0131  -0.3678 0.1102  225 PHE   A CZ   
1746 N  N    . THR   A 227 ? 0.8127 1.3261 0.4177 0.0797  -0.4148 0.1443  226 THR   A N    
1747 C  CA   . THR   A 227 ? 0.838  1.3757 0.4382 0.0787  -0.4286 0.1603  226 THR   A CA   
1748 C  C    . THR   A 227 ? 0.8367 1.4409 0.4612 0.1111  -0.439  0.1675  226 THR   A C    
1749 O  O    . THR   A 227 ? 0.825  1.4542 0.4685 0.1273  -0.4334 0.1579  226 THR   A O    
1750 C  CB   . THR   A 227 ? 0.8883 1.3583 0.4666 0.082   -0.4341 0.174   226 THR   A CB   
1751 O  OG1  . THR   A 227 ? 0.9092 1.3662 0.4918 0.1198  -0.4443 0.1885  226 THR   A OG1  
1752 C  CG2  . THR   A 227 ? 0.9182 1.3184 0.4816 0.0682  -0.4227 0.1647  226 THR   A CG2  
1753 N  N    . LYS   A 228 ? 0.8449 1.4808 0.4681 0.1222  -0.4537 0.1843  227 LYS   A N    
1754 C  CA   . LYS   A 228 ? 0.841  1.5414 0.486  0.158   -0.4639 0.1928  227 LYS   A CA   
1755 C  C    . LYS   A 228 ? 0.8785 1.5275 0.5202 0.2053  -0.4683 0.206   227 LYS   A C    
1756 O  O    . LYS   A 228 ? 0.869  1.5233 0.5266 0.2335  -0.4638 0.1999  227 LYS   A O    
1757 C  CB   . LYS   A 228 ? 0.8463 1.624  0.494  0.1502  -0.4778 0.2032  227 LYS   A CB   
1758 C  CG   . LYS   A 228 ? 0.8651 1.739  0.5364 0.1288  -0.4755 0.1886  227 LYS   A CG   
1759 C  CD   . LYS   A 228 ? 0.8932 1.8182 0.5953 0.1632  -0.4738 0.1845  227 LYS   A CD   
1760 C  CE   . LYS   A 228 ? 0.923  1.8446 0.6366 0.1456  -0.4556 0.1631  227 LYS   A CE   
1761 N  NZ   . LYS   A 228 ? 0.9234 1.8689 0.6605 0.1875  -0.4531 0.1616  227 LYS   A NZ   
1762 N  N    . ASN   A 229 ? 0.9208 1.5172 0.54   0.2131  -0.4752 0.2236  228 ASN   A N    
1763 C  CA   . ASN   A 229 ? 0.9664 1.5067 0.5773 0.2557  -0.4777 0.2375  228 ASN   A CA   
1764 C  C    . ASN   A 229 ? 1.0237 1.4622 0.6092 0.2432  -0.4712 0.2388  228 ASN   A C    
1765 O  O    . ASN   A 229 ? 1.0341 1.4546 0.6057 0.2069  -0.4692 0.2371  228 ASN   A O    
1766 C  CB   . ASN   A 229 ? 0.98   1.5582 0.5864 0.286   -0.4926 0.2625  228 ASN   A CB   
1767 C  CG   . ASN   A 229 ? 0.9843 1.6738 0.6166 0.2979  -0.5011 0.2624  228 ASN   A CG   
1768 O  OD1  . ASN   A 229 ? 0.9844 1.7135 0.641  0.3147  -0.4966 0.2508  228 ASN   A OD1  
1769 N  ND2  . ASN   A 229 ? 0.9709 1.7174 0.5987 0.2891  -0.5137 0.2748  228 ASN   A ND2  
1770 N  N    . PRO   A 230 ? 1.0581 1.43   0.6365 0.2727  -0.4671 0.2414  229 PRO   A N    
1771 C  CA   . PRO   A 230 ? 1.1066 1.3862 0.6622 0.2586  -0.4608 0.2419  229 PRO   A CA   
1772 C  C    . PRO   A 230 ? 1.1417 1.3946 0.6735 0.2535  -0.4673 0.265   229 PRO   A C    
1773 O  O    . PRO   A 230 ? 1.1348 1.4252 0.664  0.2758  -0.4775 0.2844  229 PRO   A O    
1774 C  CB   . PRO   A 230 ? 1.1304 1.3541 0.6839 0.2944  -0.4554 0.2393  229 PRO   A CB   
1775 C  CG   . PRO   A 230 ? 1.1099 1.3879 0.6765 0.3366  -0.4622 0.2497  229 PRO   A CG   
1776 C  CD   . PRO   A 230 ? 1.0471 1.4246 0.6368 0.3194  -0.467  0.2429  229 PRO   A CD   
1777 N  N    . SER   A 231 ? 1.1775 1.3681 0.6914 0.226   -0.4613 0.2636  230 SER   A N    
1778 C  CA   . SER   A 231 ? 1.2112 1.373  0.7006 0.2181  -0.4653 0.2853  230 SER   A CA   
1779 C  C    . SER   A 231 ? 1.249  1.3454 0.7183 0.2507  -0.4651 0.3057  230 SER   A C    
1780 O  O    . SER   A 231 ? 1.2612 1.3489 0.7101 0.2542  -0.4702 0.3289  230 SER   A O    
1781 C  CB   . SER   A 231 ? 1.2485 1.3751 0.7268 0.1758  -0.4579 0.2767  230 SER   A CB   
1782 O  OG   . SER   A 231 ? 1.2996 1.3666 0.7789 0.1712  -0.4476 0.2611  230 SER   A OG   
1783 N  N    . THR   A 232 ? 1.2698 1.3148 0.7407 0.2732  -0.4578 0.2975  231 THR   A N    
1784 C  CA   . THR   A 232 ? 1.3133 1.2829 0.7599 0.3021  -0.4544 0.316   231 THR   A CA   
1785 C  C    . THR   A 232 ? 1.3233 1.279  0.7754 0.3483  -0.452  0.3136  231 THR   A C    
1786 O  O    . THR   A 232 ? 1.303  1.287  0.7774 0.3518  -0.4495 0.2916  231 THR   A O    
1787 C  CB   . THR   A 232 ? 1.3666 1.2461 0.7934 0.2742  -0.4431 0.3119  231 THR   A CB   
1788 O  OG1  . THR   A 232 ? 1.3696 1.2662 0.805  0.2286  -0.4406 0.2953  231 THR   A OG1  
1789 C  CG2  . THR   A 232 ? 1.4003 1.2241 0.7946 0.2817  -0.4419 0.3412  231 THR   A CG2  
1790 N  N    . ARG   A 233 ? 1.3545 1.2628 0.7831 0.3852  -0.4513 0.3373  232 ARG   A N    
1791 C  CA   . ARG   A 233 ? 1.3753 1.2586 0.8017 0.4346  -0.4474 0.339   232 ARG   A CA   
1792 C  C    . ARG   A 233 ? 1.4225 1.1962 0.8297 0.4325  -0.4322 0.3268  232 ARG   A C    
1793 O  O    . ARG   A 233 ? 1.4574 1.157  0.8362 0.4625  -0.4253 0.3433  232 ARG   A O    
1794 C  CB   . ARG   A 233 ? 1.3977 1.2915 0.8062 0.4809  -0.4544 0.3728  232 ARG   A CB   
1795 C  CG   . ARG   A 233 ? 1.3944 1.4077 0.829  0.5019  -0.4689 0.3783  232 ARG   A CG   
1796 C  CD   . ARG   A 233 ? 1.4494 1.475  0.8646 0.5508  -0.4764 0.4127  232 ARG   A CD   
1797 N  NE   . ARG   A 233 ? 1.4467 1.5916 0.8896 0.5769  -0.49   0.4159  232 ARG   A NE   
1798 C  CZ   . ARG   A 233 ? 1.4681 1.6586 0.9015 0.6182  -0.5006 0.4444  232 ARG   A CZ   
1799 N  NH1  . ARG   A 233 ? 1.4981 1.6192 0.8919 0.6401  -0.4986 0.474   232 ARG   A NH1  
1800 N  NH2  . ARG   A 233 ? 1.4232 1.7314 0.8862 0.6378  -0.5131 0.4436  232 ARG   A NH2  
1801 N  N    . PRO   A 236 ? 1.2254 1.0949 0.723  0.4003  -0.4157 0.2027  235 PRO   A N    
1802 C  CA   . PRO   A 236 ? 1.1968 1.1215 0.7168 0.4225  -0.4142 0.1862  235 PRO   A CA   
1803 C  C    . PRO   A 236 ? 1.151  1.163  0.6973 0.3941  -0.4182 0.1755  235 PRO   A C    
1804 O  O    . PRO   A 236 ? 1.1566 1.167  0.7021 0.3524  -0.4183 0.1693  235 PRO   A O    
1805 C  CB   . PRO   A 236 ? 1.2339 1.0893 0.7434 0.4221  -0.4031 0.1609  235 PRO   A CB   
1806 C  CG   . PRO   A 236 ? 1.2638 1.0655 0.759  0.378   -0.4009 0.1556  235 PRO   A CG   
1807 C  CD   . PRO   A 236 ? 1.2544 1.0428 0.7358 0.3737  -0.4066 0.1855  235 PRO   A CD   
1808 N  N    . VAL   A 237 ? 1.102  1.1897 0.6706 0.4169  -0.4202 0.1734  236 VAL   A N    
1809 C  CA   . VAL   A 237 ? 1.0567 1.223  0.6482 0.3901  -0.4211 0.1623  236 VAL   A CA   
1810 C  C    . VAL   A 237 ? 1.0395 1.2108 0.641  0.3954  -0.4114 0.1368  236 VAL   A C    
1811 O  O    . VAL   A 237 ? 1.0252 1.2254 0.6379 0.4304  -0.4086 0.1329  236 VAL   A O    
1812 C  CB   . VAL   A 237 ? 1.0252 1.2842 0.6354 0.3967  -0.4301 0.1777  236 VAL   A CB   
1813 C  CG1  . VAL   A 237 ? 1.0001 1.3329 0.6324 0.3698  -0.427  0.1623  236 VAL   A CG1  
1814 C  CG2  . VAL   A 237 ? 1.0364 1.2895 0.6333 0.3794  -0.4393 0.1992  236 VAL   A CG2  
1815 N  N    . LEU   A 238 ? 1.0424 1.1798 0.6367 0.3626  -0.406  0.1199  237 LEU   A N    
1816 C  CA   . LEU   A 238 ? 1.0383 1.1738 0.6366 0.3606  -0.3969 0.0948  237 LEU   A CA   
1817 C  C    . LEU   A 238 ? 0.9981 1.2195 0.6193 0.359   -0.3943 0.0895  237 LEU   A C    
1818 O  O    . LEU   A 238 ? 0.9812 1.2538 0.6116 0.3367  -0.3982 0.099   237 LEU   A O    
1819 C  CB   . LEU   A 238 ? 1.0541 1.1525 0.641  0.3212  -0.3939 0.0821  237 LEU   A CB   
1820 C  CG   . LEU   A 238 ? 1.1007 1.1227 0.6669 0.3089  -0.3958 0.0866  237 LEU   A CG   
1821 C  CD1  . LEU   A 238 ? 1.1099 1.1266 0.6714 0.2674  -0.3951 0.0808  237 LEU   A CD1  
1822 C  CD2  . LEU   A 238 ? 1.1345 1.0905 0.687  0.3288  -0.3902 0.0719  237 LEU   A CD2  
1823 N  N    . GLU   A 239 ? 0.9794 1.2149 0.6077 0.3795  -0.3863 0.073   238 GLU   A N    
1824 C  CA   . GLU   A 239 ? 0.9404 1.2556 0.5895 0.3759  -0.381  0.0669  238 GLU   A CA   
1825 C  C    . GLU   A 239 ? 0.9352 1.2526 0.5796 0.3376  -0.374  0.0532  238 GLU   A C    
1826 O  O    . GLU   A 239 ? 0.9604 1.2197 0.5872 0.3212  -0.3732 0.0453  238 GLU   A O    
1827 C  CB   . GLU   A 239 ? 0.9547 1.2914 0.6136 0.4161  -0.3743 0.057   238 GLU   A CB   
1828 C  CG   . GLU   A 239 ? 0.9938 1.3749 0.6674 0.4532  -0.3798 0.0733  238 GLU   A CG   
1829 C  CD   . GLU   A 239 ? 1.046  1.5033 0.7378 0.437   -0.3877 0.0902  238 GLU   A CD   
1830 O  OE1  . GLU   A 239 ? 1.0274 1.5405 0.732  0.4072  -0.3832 0.0838  238 GLU   A OE1  
1831 O  OE2  . GLU   A 239 ? 1.0838 1.541  0.7736 0.4526  -0.398  0.1098  238 GLU   A OE2  
1832 N  N    . THR   A 240 ? 0.9011 1.2858 0.56   0.3236  -0.3679 0.0507  239 THR   A N    
1833 C  CA   . THR   A 240 ? 0.9004 1.287  0.5517 0.2909  -0.3588 0.0398  239 THR   A CA   
1834 C  C    . THR   A 240 ? 0.9105 1.2589 0.5494 0.3003  -0.3507 0.0201  239 THR   A C    
1835 O  O    . THR   A 240 ? 0.9297 1.2429 0.5525 0.2789  -0.3483 0.0129  239 THR   A O    
1836 C  CB   . THR   A 240 ? 0.8863 1.3491 0.5537 0.2778  -0.3506 0.04    239 THR   A CB   
1837 O  OG1  . THR   A 240 ? 0.8812 1.3823 0.5638 0.3084  -0.3448 0.0329  239 THR   A OG1  
1838 C  CG2  . THR   A 240 ? 0.8717 1.3796 0.5504 0.2624  -0.3583 0.0561  239 THR   A CG2  
1839 N  N    . ASP   A 241 ? 0.8965 1.2552 0.5421 0.3334  -0.3465 0.011   240 ASP   A N    
1840 C  CA   . ASP   A 241 ? 0.9083 1.2374 0.5415 0.3449  -0.3386 -0.0095 240 ASP   A CA   
1841 C  C    . ASP   A 241 ? 0.9359 1.1882 0.5506 0.3516  -0.3442 -0.0178 240 ASP   A C    
1842 O  O    . ASP   A 241 ? 0.9535 1.1768 0.5535 0.3451  -0.3401 -0.0349 240 ASP   A O    
1843 C  CB   . ASP   A 241 ? 0.9082 1.2787 0.5543 0.3779  -0.3306 -0.0171 240 ASP   A CB   
1844 C  CG   . ASP   A 241 ? 0.961  1.3284 0.616  0.4153  -0.3365 -0.0097 240 ASP   A CG   
1845 O  OD1  . ASP   A 241 ? 0.9626 1.342  0.6262 0.4143  -0.3459 0.009   240 ASP   A OD1  
1846 O  OD2  . ASP   A 241 ? 0.9922 1.3459 0.6437 0.4475  -0.3311 -0.0222 240 ASP   A OD2  
1847 N  N    . THR   A 242 ? 0.9399 1.1601 0.5539 0.3647  -0.3529 -0.0062 241 THR   A N    
1848 C  CA   . THR   A 242 ? 0.973  1.1153 0.5681 0.3691  -0.3566 -0.0132 241 THR   A CA   
1849 C  C    . THR   A 242 ? 0.9863 1.0952 0.5684 0.3317  -0.3594 -0.0166 241 THR   A C    
1850 O  O    . THR   A 242 ? 1.0063 1.0698 0.5734 0.3265  -0.358  -0.0342 241 THR   A O    
1851 C  CB   . THR   A 242 ? 0.9993 1.1169 0.5945 0.3912  -0.3633 0.0045  241 THR   A CB   
1852 O  OG1  . THR   A 242 ? 0.9991 1.1437 0.604  0.4321  -0.3593 0.004   241 THR   A OG1  
1853 C  CG2  . THR   A 242 ? 1.0421 1.0726 0.6152 0.3885  -0.3657 0.0005  241 THR   A CG2  
1854 N  N    . VAL   A 243 ? 0.9742 1.1103 0.5621 0.3057  -0.363  -0.0013 242 VAL   A N    
1855 C  CA   . VAL   A 243 ? 0.9914 1.1054 0.5686 0.2715  -0.3649 -0.0016 242 VAL   A CA   
1856 C  C    . VAL   A 243 ? 0.9928 1.1195 0.5633 0.2598  -0.3574 -0.0195 242 VAL   A C    
1857 O  O    . VAL   A 243 ? 1.0094 1.104  0.5675 0.2439  -0.3584 -0.0297 242 VAL   A O    
1858 C  CB   . VAL   A 243 ? 0.9888 1.1321 0.5725 0.2505  -0.3692 0.0194  242 VAL   A CB   
1859 C  CG1  . VAL   A 243 ? 1.0036 1.1321 0.5764 0.2169  -0.3689 0.019   242 VAL   A CG1  
1860 C  CG2  . VAL   A 243 ? 1.0019 1.1269 0.5874 0.2625  -0.3777 0.0375  242 VAL   A CG2  
1861 N  N    . ALA   A 244 ? 0.9719 1.1473 0.5501 0.269   -0.3493 -0.0233 243 ALA   A N    
1862 C  CA   . ALA   A 244 ? 0.9736 1.1643 0.543  0.2625  -0.3404 -0.0377 243 ALA   A CA   
1863 C  C    . ALA   A 244 ? 0.9963 1.1533 0.5537 0.2778  -0.3397 -0.06   243 ALA   A C    
1864 O  O    . ALA   A 244 ? 1.0051 1.1538 0.5491 0.2665  -0.3376 -0.0724 243 ALA   A O    
1865 C  CB   . ALA   A 244 ? 0.9509 1.1986 0.5307 0.2702  -0.3304 -0.0352 243 ALA   A CB   
1866 N  N    . ARG   A 245 ? 1.0035 1.1412 0.5641 0.3045  -0.3414 -0.0655 244 ARG   A N    
1867 C  CA   . ARG   A 245 ? 1.0266 1.1258 0.5734 0.3187  -0.3404 -0.0886 244 ARG   A CA   
1868 C  C    . ARG   A 245 ? 1.046  1.0913 0.5801 0.2974  -0.3477 -0.095  244 ARG   A C    
1869 O  O    . ARG   A 245 ? 1.0588 1.0864 0.5794 0.292   -0.3471 -0.1159 244 ARG   A O    
1870 C  CB   . ARG   A 245 ? 1.0535 1.1382 0.6042 0.3532  -0.3391 -0.0909 244 ARG   A CB   
1871 C  CG   . ARG   A 245 ? 1.0793 1.2215 0.6432 0.377   -0.3306 -0.0894 244 ARG   A CG   
1872 C  CD   . ARG   A 245 ? 1.136  1.257  0.6969 0.4149  -0.327  -0.1005 244 ARG   A CD   
1873 N  NE   . ARG   A 245 ? 1.1589 1.3075 0.7375 0.4399  -0.3276 -0.0824 244 ARG   A NE   
1874 C  CZ   . ARG   A 245 ? 1.1912 1.3074 0.7706 0.4477  -0.3349 -0.067  244 ARG   A CZ   
1875 N  NH1  . ARG   A 245 ? 1.2091 1.2609 0.7729 0.4293  -0.3412 -0.0675 244 ARG   A NH1  
1876 N  NH2  . ARG   A 245 ? 1.1698 1.3209 0.7653 0.4741  -0.3357 -0.0505 244 ARG   A NH2  
1877 N  N    . SER   A 246 ? 1.0453 1.0683 0.5833 0.2844  -0.3544 -0.0773 245 SER   A N    
1878 C  CA   . SER   A 246 ? 1.0623 1.038  0.59   0.2609  -0.3601 -0.0808 245 SER   A CA   
1879 C  C    . SER   A 246 ? 1.0511 1.0498 0.5751 0.2338  -0.3602 -0.0853 245 SER   A C    
1880 O  O    . SER   A 246 ? 1.068  1.0425 0.582  0.2193  -0.3624 -0.1014 245 SER   A O    
1881 C  CB   . SER   A 246 ? 1.0791 1.0319 0.611  0.2544  -0.3656 -0.0576 245 SER   A CB   
1882 O  OG   . SER   A 246 ? 1.114  1.0314 0.6434 0.2809  -0.3654 -0.0548 245 SER   A OG   
1883 N  N    . LEU   A 247 ? 1.0186 1.0643 0.5494 0.2273  -0.357  -0.0719 246 LEU   A N    
1884 C  CA   . LEU   A 247 ? 1.0035 1.0698 0.5277 0.2066  -0.355  -0.0737 246 LEU   A CA   
1885 C  C    . LEU   A 247 ? 1.0008 1.0818 0.5145 0.2161  -0.3501 -0.095  246 LEU   A C    
1886 O  O    . LEU   A 247 ? 1.0132 1.0898 0.5172 0.2031  -0.3522 -0.1063 246 LEU   A O    
1887 C  CB   . LEU   A 247 ? 0.9836 1.0877 0.5132 0.1974  -0.3505 -0.0538 246 LEU   A CB   
1888 C  CG   . LEU   A 247 ? 0.9869 1.1068 0.5061 0.1786  -0.3463 -0.0524 246 LEU   A CG   
1889 C  CD1  . LEU   A 247 ? 0.9998 1.0932 0.5146 0.159   -0.3532 -0.0531 246 LEU   A CD1  
1890 C  CD2  . LEU   A 247 ? 0.9811 1.1288 0.5025 0.1688  -0.3401 -0.034  246 LEU   A CD2  
1891 N  N    . ILE   A 248 ? 0.9829 1.0835 0.4981 0.2395  -0.3437 -0.1013 247 ILE   A N    
1892 C  CA   . ILE   A 248 ? 0.979  1.0941 0.4813 0.2502  -0.3385 -0.1216 247 ILE   A CA   
1893 C  C    . ILE   A 248 ? 0.9906 1.069  0.4829 0.2503  -0.3448 -0.1455 247 ILE   A C    
1894 O  O    . ILE   A 248 ? 0.996  1.0844 0.4754 0.2461  -0.3449 -0.1617 247 ILE   A O    
1895 C  CB   . ILE   A 248 ? 0.9722 1.1198 0.4769 0.2744  -0.3284 -0.1234 247 ILE   A CB   
1896 C  CG1  . ILE   A 248 ? 0.975  1.1463 0.4626 0.2804  -0.3211 -0.1379 247 ILE   A CG1  
1897 C  CG2  . ILE   A 248 ? 0.9855 1.1134 0.4958 0.2986  -0.3293 -0.1322 247 ILE   A CG2  
1898 C  CD1  . ILE   A 248 ? 0.977  1.1799 0.4597 0.2704  -0.3126 -0.1237 247 ILE   A CD1  
1899 N  N    . ASP   A 249 ? 0.9939 1.0289 0.4898 0.2536  -0.3496 -0.1476 248 ASP   A N    
1900 C  CA   . ASP   A 249 ? 1.0086 1.0012 0.4927 0.2497  -0.3538 -0.1719 248 ASP   A CA   
1901 C  C    . ASP   A 249 ? 1.0028 0.9801 0.4843 0.218   -0.3609 -0.1744 248 ASP   A C    
1902 O  O    . ASP   A 249 ? 1.0132 0.9755 0.4842 0.2082  -0.364  -0.1983 248 ASP   A O    
1903 C  CB   . ASP   A 249 ? 1.0471 0.9916 0.531  0.2673  -0.3532 -0.1742 248 ASP   A CB   
1904 C  CG   . ASP   A 249 ? 1.0965 1.0576 0.5805 0.3015  -0.3457 -0.1797 248 ASP   A CG   
1905 O  OD1  . ASP   A 249 ? 1.0934 1.0769 0.5675 0.3101  -0.3416 -0.1989 248 ASP   A OD1  
1906 O  OD2  . ASP   A 249 ? 1.1258 1.0813 0.6195 0.3208  -0.3437 -0.1642 248 ASP   A OD2  
1907 N  N    . GLY   A 250 ? 0.9814 0.9671 0.4725 0.2017  -0.3631 -0.1511 249 GLY   A N    
1908 C  CA   . GLY   A 250 ? 0.9753 0.9536 0.466  0.1725  -0.3684 -0.1504 249 GLY   A CA   
1909 C  C    . GLY   A 250 ? 0.9489 0.9721 0.4344 0.1644  -0.3681 -0.1565 249 GLY   A C    
1910 O  O    . GLY   A 250 ? 0.9498 0.9739 0.432  0.1452  -0.3728 -0.1683 249 GLY   A O    
1911 N  N    . ILE   A 251 ? 0.9245 0.9861 0.4082 0.1791  -0.3616 -0.1476 250 ILE   A N    
1912 C  CA   . ILE   A 251 ? 0.9103 1.0117 0.3841 0.1775  -0.359  -0.1507 250 ILE   A CA   
1913 C  C    . ILE   A 251 ? 0.9071 1.0178 0.3683 0.1865  -0.3609 -0.1791 250 ILE   A C    
1914 O  O    . ILE   A 251 ? 0.9001 1.0324 0.354  0.1774  -0.3645 -0.1893 250 ILE   A O    
1915 C  CB   . ILE   A 251 ? 0.903  1.0342 0.3748 0.1895  -0.3488 -0.1322 250 ILE   A CB   
1916 C  CG1  . ILE   A 251 ? 0.9081 1.0344 0.3899 0.1757  -0.3478 -0.1066 250 ILE   A CG1  
1917 C  CG2  . ILE   A 251 ? 0.9013 1.0673 0.3566 0.1943  -0.3435 -0.1358 250 ILE   A CG2  
1918 C  CD1  . ILE   A 251 ? 0.9154 1.0648 0.3968 0.1837  -0.3375 -0.0907 250 ILE   A CD1  
1919 N  N    . LEU   A 252 ? 0.9122 1.0081 0.3706 0.2049  -0.3587 -0.1926 251 LEU   A N    
1920 C  CA   . LEU   A 252 ? 0.9228 1.0238 0.367  0.2152  -0.3599 -0.2217 251 LEU   A CA   
1921 C  C    . LEU   A 252 ? 0.9372 1.0128 0.3784 0.1951  -0.3691 -0.2455 251 LEU   A C    
1922 O  O    . LEU   A 252 ? 0.9374 1.0322 0.3661 0.195   -0.3724 -0.2697 251 LEU   A O    
1923 C  CB   . LEU   A 252 ? 0.9304 1.0207 0.3719 0.2414  -0.3534 -0.2285 251 LEU   A CB   
1924 C  CG   . LEU   A 252 ? 0.9398 1.0655 0.3822 0.2604  -0.3427 -0.211  251 LEU   A CG   
1925 C  CD1  . LEU   A 252 ? 0.9494 1.0681 0.3918 0.286   -0.3363 -0.2186 251 LEU   A CD1  
1926 C  CD2  . LEU   A 252 ? 0.9402 1.1082 0.3666 0.2639  -0.3386 -0.2134 251 LEU   A CD2  
1927 N  N    . THR   A 253 ? 0.9487 0.9831 0.4001 0.1769  -0.3728 -0.2392 252 THR   A N    
1928 C  CA   . THR   A 253 ? 0.9641 0.973  0.4129 0.1518  -0.3796 -0.2608 252 THR   A CA   
1929 C  C    . THR   A 253 ? 0.962  0.9937 0.4198 0.1244  -0.3846 -0.2504 252 THR   A C    
1930 O  O    . THR   A 253 ? 0.9704 0.9908 0.4286 0.0994  -0.3899 -0.2674 252 THR   A O    
1931 C  CB   . THR   A 253 ? 0.9977 0.939  0.4459 0.1495  -0.3782 -0.2657 252 THR   A CB   
1932 O  OG1  . THR   A 253 ? 1.01   0.9293 0.4706 0.1447  -0.3769 -0.2361 252 THR   A OG1  
1933 C  CG2  . THR   A 253 ? 1.0101 0.9331 0.4486 0.1798  -0.3724 -0.2768 252 THR   A CG2  
1934 N  N    . ASN   A 254 ? 0.947  1.0117 0.4108 0.1288  -0.3819 -0.224  253 ASN   A N    
1935 C  CA   . ASN   A 254 ? 0.9395 1.0294 0.41   0.1093  -0.3843 -0.2109 253 ASN   A CA   
1936 C  C    . ASN   A 254 ? 0.9461 0.9976 0.4275 0.0837  -0.3869 -0.2025 253 ASN   A C    
1937 O  O    . ASN   A 254 ? 0.9401 1.0043 0.426  0.0599  -0.391  -0.2083 253 ASN   A O    
1938 C  CB   . ASN   A 254 ? 0.9472 1.0842 0.411  0.1035  -0.3893 -0.2304 253 ASN   A CB   
1939 C  CG   . ASN   A 254 ? 0.98   1.159  0.4295 0.1299  -0.3856 -0.2331 253 ASN   A CG   
1940 O  OD1  . ASN   A 254 ? 0.989  1.1931 0.4279 0.1349  -0.3897 -0.2575 253 ASN   A OD1  
1941 N  ND2  . ASN   A 254 ? 0.9878 1.1753 0.4349 0.1463  -0.3771 -0.2084 253 ASN   A ND2  
1942 N  N    . LYS   A 255 ? 0.9572 0.9646 0.4424 0.0893  -0.384  -0.1879 254 LYS   A N    
1943 C  CA   . LYS   A 255 ? 0.972  0.9379 0.4639 0.0679  -0.385  -0.1767 254 LYS   A CA   
1944 C  C    . LYS   A 255 ? 0.9644 0.9514 0.4641 0.0584  -0.384  -0.1492 254 LYS   A C    
1945 O  O    . LYS   A 255 ? 0.9574 0.967  0.4577 0.0741  -0.3804 -0.1313 254 LYS   A O    
1946 C  CB   . LYS   A 255 ? 1.0106 0.9206 0.5002 0.0807  -0.3824 -0.1712 254 LYS   A CB   
1947 C  CG   . LYS   A 255 ? 1.0767 0.9332 0.5664 0.0578  -0.3825 -0.1666 254 LYS   A CG   
1948 C  CD   . LYS   A 255 ? 1.1579 0.9507 0.6369 0.0683  -0.3794 -0.1773 254 LYS   A CD   
1949 C  CE   . LYS   A 255 ? 1.2328 0.9677 0.7062 0.0407  -0.3775 -0.1796 254 LYS   A CE   
1950 N  NZ   . LYS   A 255 ? 1.2738 0.9988 0.7533 0.0317  -0.3769 -0.1475 254 LYS   A NZ   
1951 N  N    . LYS   A 256 ? 0.9628 0.9429 0.4674 0.0312  -0.386  -0.1472 255 LYS   A N    
1952 C  CA   . LYS   A 256 ? 0.9593 0.9581 0.4694 0.0202  -0.3844 -0.1237 255 LYS   A CA   
1953 C  C    . LYS   A 256 ? 0.9708 0.9398 0.4824 0.0254  -0.382  -0.0971 255 LYS   A C    
1954 O  O    . LYS   A 256 ? 0.9662 0.9582 0.4788 0.0287  -0.3794 -0.0773 255 LYS   A O    
1955 C  CB   . LYS   A 256 ? 0.9823 0.9819 0.4977 -0.0112 -0.3865 -0.1302 255 LYS   A CB   
1956 C  CG   . LYS   A 256 ? 1.0181 1.054  0.5338 -0.0198 -0.3904 -0.1584 255 LYS   A CG   
1957 C  CD   . LYS   A 256 ? 1.0539 1.1518 0.5682 -0.0065 -0.39   -0.1545 255 LYS   A CD   
1958 C  CE   . LYS   A 256 ? 1.0948 1.2355 0.6113 -0.018  -0.3952 -0.1796 255 LYS   A CE   
1959 N  NZ   . LYS   A 256 ? 1.1207 1.259  0.6485 -0.0523 -0.3965 -0.1828 255 LYS   A NZ   
1960 N  N    . MET   A 257 ? 0.9847 0.9018 0.4947 0.026   -0.3824 -0.0964 256 MET   A N    
1961 C  CA   . MET   A 257 ? 0.9917 0.8831 0.5022 0.0329  -0.3812 -0.0704 256 MET   A CA   
1962 C  C    . MET   A 257 ? 1.0112 0.8764 0.5187 0.0597  -0.3806 -0.071  256 MET   A C    
1963 O  O    . MET   A 257 ? 1.0339 0.8512 0.5351 0.0608  -0.38   -0.0813 256 MET   A O    
1964 C  CB   . MET   A 257 ? 0.9964 0.848  0.5054 0.0089  -0.3808 -0.0605 256 MET   A CB   
1965 C  CG   . MET   A 257 ? 0.9985 0.842  0.5071 0.0125  -0.3804 -0.0307 256 MET   A CG   
1966 S  SD   . MET   A 257 ? 0.9522 0.853  0.4652 0.005   -0.3794 -0.0154 256 MET   A SD   
1967 C  CE   . MET   A 257 ? 0.9097 0.8067 0.4238 -0.0294 -0.378  -0.018  256 MET   A CE   
1968 N  N    . ILE   A 258 ? 1.0015 0.8971 0.5126 0.0809  -0.3796 -0.0599 257 ILE   A N    
1969 C  CA   . ILE   A 258 ? 1.0153 0.8988 0.5265 0.1092  -0.3786 -0.0591 257 ILE   A CA   
1970 C  C    . ILE   A 258 ? 1.029  0.8935 0.5421 0.1168  -0.3799 -0.0331 257 ILE   A C    
1971 O  O    . ILE   A 258 ? 1.0133 0.9129 0.5329 0.124   -0.3801 -0.0164 257 ILE   A O    
1972 C  CB   . ILE   A 258 ? 1.0055 0.9373 0.52   0.1285  -0.3757 -0.0644 257 ILE   A CB   
1973 C  CG1  . ILE   A 258 ? 1.0099 0.9686 0.5198 0.121   -0.3746 -0.0851 257 ILE   A CG1  
1974 C  CG2  . ILE   A 258 ? 1.0157 0.9366 0.5305 0.1582  -0.3737 -0.0701 257 ILE   A CG2  
1975 C  CD1  . ILE   A 258 ? 1.0095 1.0139 0.5189 0.1366  -0.3696 -0.0856 257 ILE   A CD1  
1976 N  N    . PHE   A 259 ? 1.056  0.8648 0.5616 0.1152  -0.3801 -0.0301 258 PHE   A N    
1977 C  CA   . PHE   A 259 ? 1.0758 0.8635 0.5797 0.1263  -0.3815 -0.0047 258 PHE   A CA   
1978 C  C    . PHE   A 259 ? 1.0831 0.8738 0.5892 0.1627  -0.3809 -0.0029 258 PHE   A C    
1979 O  O    . PHE   A 259 ? 1.0935 0.8578 0.5938 0.1774  -0.3777 -0.0217 258 PHE   A O    
1980 C  CB   . PHE   A 259 ? 1.105  0.8253 0.5957 0.1134  -0.3796 -0.0016 258 PHE   A CB   
1981 C  CG   . PHE   A 259 ? 1.1189 0.8391 0.6087 0.0792  -0.3799 0.0065  258 PHE   A CG   
1982 C  CD1  . PHE   A 259 ? 1.1162 0.8735 0.6116 0.0725  -0.3827 0.0282  258 PHE   A CD1  
1983 C  CD2  . PHE   A 259 ? 1.1475 0.8321 0.6308 0.0528  -0.3767 -0.0086 258 PHE   A CD2  
1984 C  CE1  . PHE   A 259 ? 1.1293 0.8871 0.6229 0.0428  -0.3818 0.0355  258 PHE   A CE1  
1985 C  CE2  . PHE   A 259 ? 1.1573 0.8469 0.6415 0.0216  -0.3761 -0.0009 258 PHE   A CE2  
1986 C  CZ   . PHE   A 259 ? 1.1416 0.8672 0.6306 0.0183  -0.3784 0.0216  258 PHE   A CZ   
1987 N  N    . VAL   A 260 ? 1.0764 0.901  0.5905 0.1774  -0.3836 0.0187  259 VAL   A N    
1988 C  CA   . VAL   A 260 ? 1.0853 0.9228 0.6044 0.2134  -0.3832 0.0219  259 VAL   A CA   
1989 C  C    . VAL   A 260 ? 1.1119 0.9338 0.6277 0.2298  -0.3867 0.0483  259 VAL   A C    
1990 O  O    . VAL   A 260 ? 1.1    0.9599 0.6225 0.2215  -0.3912 0.0671  259 VAL   A O    
1991 C  CB   . VAL   A 260 ? 1.0637 0.9733 0.5982 0.2205  -0.3825 0.0194  259 VAL   A CB   
1992 C  CG1  . VAL   A 260 ? 1.0638 0.9898 0.605  0.2577  -0.3806 0.018   259 VAL   A CG1  
1993 C  CG2  . VAL   A 260 ? 1.0617 0.9894 0.5959 0.2036  -0.3788 -0.0021 259 VAL   A CG2  
1994 N  N    . PRO   A 261 ? 1.1462 0.9163 0.6503 0.2563  -0.3843 0.0508  260 PRO   A N    
1995 C  CA   . PRO   A 261 ? 1.18   0.8951 0.6716 0.2688  -0.3777 0.0287  260 PRO   A CA   
1996 C  C    . PRO   A 261 ? 1.2269 0.8738 0.701  0.2396  -0.3745 0.0218  260 PRO   A C    
1997 O  O    . PRO   A 261 ? 1.2397 0.8495 0.7028 0.2332  -0.3748 0.042   260 PRO   A O    
1998 C  CB   . PRO   A 261 ? 1.1945 0.8872 0.6796 0.3124  -0.376  0.0421  260 PRO   A CB   
1999 C  CG   . PRO   A 261 ? 1.1823 0.9145 0.6752 0.3191  -0.3832 0.0737  260 PRO   A CG   
2000 C  CD   . PRO   A 261 ? 1.1499 0.9079 0.6484 0.2772  -0.3876 0.0784  260 PRO   A CD   
2001 N  N    . SER   A 262 ? 1.248  0.883  0.7194 0.2214  -0.3713 -0.0071 261 SER   A N    
2002 C  CA   . SER   A 262 ? 1.2867 0.8748 0.7465 0.1871  -0.3683 -0.0234 261 SER   A CA   
2003 C  C    . SER   A 262 ? 1.3384 0.8569 0.7806 0.174   -0.3646 -0.008  261 SER   A C    
2004 O  O    . SER   A 262 ? 1.3437 0.8548 0.7851 0.1374  -0.3644 -0.0097 261 SER   A O    
2005 C  CB   . SER   A 262 ? 1.3103 0.8705 0.761  0.191   -0.3633 -0.0567 261 SER   A CB   
2006 O  OG   . SER   A 262 ? 1.3102 0.936  0.7751 0.1999  -0.3659 -0.0706 261 SER   A OG   
2007 N  N    . TYR   A 263 ? 1.3733 0.8414 0.8003 0.2041  -0.3605 0.0077  262 TYR   A N    
2008 C  CA   . TYR   A 263 ? 1.4233 0.8175 0.8286 0.1944  -0.3548 0.0246  262 TYR   A CA   
2009 C  C    . TYR   A 263 ? 1.4226 0.8416 0.8333 0.1702  -0.3595 0.0497  262 TYR   A C    
2010 O  O    . TYR   A 263 ? 1.4497 0.8111 0.843  0.1503  -0.3537 0.0596  262 TYR   A O    
2011 C  CB   . TYR   A 263 ? 1.4552 0.7959 0.8412 0.2381  -0.3494 0.041   262 TYR   A CB   
2012 C  CG   . TYR   A 263 ? 1.4487 0.8515 0.8492 0.2769  -0.357  0.0639  262 TYR   A CG   
2013 C  CD1  . TYR   A 263 ? 1.4491 0.8905 0.8565 0.2735  -0.3644 0.0938  262 TYR   A CD1  
2014 C  CD2  . TYR   A 263 ? 1.4574 0.8766 0.862  0.3182  -0.3559 0.0563  262 TYR   A CD2  
2015 C  CE1  . TYR   A 263 ? 1.438  0.9409 0.8589 0.3065  -0.3719 0.1132  262 TYR   A CE1  
2016 C  CE2  . TYR   A 263 ? 1.4465 0.9271 0.8656 0.353   -0.3625 0.0771  262 TYR   A CE2  
2017 C  CZ   . TYR   A 263 ? 1.4425 0.9655 0.87   0.3463  -0.3709 0.1052  262 TYR   A CZ   
2018 O  OH   . TYR   A 263 ? 1.4355 1.025  0.878  0.3778  -0.3781 0.1241  262 TYR   A OH   
2019 N  N    . ILE   A 264 ? 1.3923 0.893  0.8246 0.1706  -0.3686 0.0598  263 ILE   A N    
2020 C  CA   . ILE   A 264 ? 1.392  0.9198 0.8282 0.1481  -0.3728 0.082   263 ILE   A CA   
2021 C  C    . ILE   A 264 ? 1.406  0.9201 0.841  0.1019  -0.3694 0.0699  263 ILE   A C    
2022 O  O    . ILE   A 264 ? 1.4013 0.9296 0.8366 0.0809  -0.3708 0.0867  263 ILE   A O    
2023 C  CB   . ILE   A 264 ? 1.3629 0.9781 0.8199 0.157   -0.3816 0.0916  263 ILE   A CB   
2024 C  CG1  . ILE   A 264 ? 1.3532 1.0182 0.8271 0.1555  -0.3827 0.0658  263 ILE   A CG1  
2025 C  CG2  . ILE   A 264 ? 1.3637 0.9957 0.8207 0.1962  -0.3859 0.1141  263 ILE   A CG2  
2026 C  CD1  . ILE   A 264 ? 1.3389 1.0777 0.8291 0.1533  -0.3879 0.072   263 ILE   A CD1  
2027 N  N    . ASN   A 265 ? 1.4217 0.9118 0.8551 0.0868  -0.3648 0.0402  264 ASN   A N    
2028 C  CA   . ASN   A 265 ? 1.4404 0.9209 0.874  0.0445  -0.3613 0.0254  264 ASN   A CA   
2029 C  C    . ASN   A 265 ? 1.4883 0.8879 0.8994 0.0289  -0.3521 0.0365  264 ASN   A C    
2030 O  O    . ASN   A 265 ? 1.4924 0.8925 0.9034 -0.0035 -0.3498 0.044   264 ASN   A O    
2031 C  CB   . ASN   A 265 ? 1.4564 0.9416 0.8944 0.0365  -0.3603 -0.0112 264 ASN   A CB   
2032 C  CG   . ASN   A 265 ? 1.503  0.985  0.9427 -0.007  -0.3573 -0.0299 264 ASN   A CG   
2033 O  OD1  . ASN   A 265 ? 1.5113 1.0131 0.9564 -0.0325 -0.3575 -0.0171 264 ASN   A OD1  
2034 N  ND2  . ASN   A 265 ? 1.5211 0.9816 0.9563 -0.0166 -0.3544 -0.0618 264 ASN   A ND2  
2035 N  N    . ILE   A 266 ? 1.5249 0.8531 0.9151 0.0521  -0.3453 0.0378  265 ILE   A N    
2036 C  CA   . ILE   A 266 ? 1.575  0.8156 0.9383 0.0391  -0.3339 0.05    265 ILE   A CA   
2037 C  C    . ILE   A 266 ? 1.5907 0.833  0.947  0.0452  -0.3352 0.0891  265 ILE   A C    
2038 O  O    . ILE   A 266 ? 1.6154 0.8108 0.9558 0.019   -0.3268 0.1006  265 ILE   A O    
2039 C  CB   . ILE   A 266 ? 1.6173 0.7715 0.9547 0.0633  -0.3237 0.0409  265 ILE   A CB   
2040 C  CG1  . ILE   A 266 ? 1.6333 0.7802 0.9619 0.1175  -0.326  0.0663  265 ILE   A CG1  
2041 C  CG2  . ILE   A 266 ? 1.619  0.7784 0.9627 0.0573  -0.3233 0.0005  265 ILE   A CG2  
2042 C  CD1  . ILE   A 266 ? 1.6898 0.7483 0.9848 0.1317  -0.3151 0.0933  265 ILE   A CD1  
2043 N  N    . PHE   A 267 ? 1.5727 0.8728 0.9406 0.0765  -0.3455 0.1084  266 PHE   A N    
2044 C  CA   . PHE   A 267 ? 1.58   0.8936 0.9418 0.0828  -0.3489 0.1437  266 PHE   A CA   
2045 C  C    . PHE   A 267 ? 1.5735 0.9257 0.9456 0.0418  -0.3503 0.1467  266 PHE   A C    
2046 O  O    . PHE   A 267 ? 1.5887 0.9159 0.9457 0.0298  -0.3463 0.1703  266 PHE   A O    
2047 C  CB   . PHE   A 267 ? 1.5538 0.9317 0.9289 0.1213  -0.3603 0.1578  266 PHE   A CB   
2048 C  CG   . PHE   A 267 ? 1.5837 0.9213 0.9438 0.1676  -0.3581 0.1669  266 PHE   A CG   
2049 C  CD1  . PHE   A 267 ? 1.6351 0.8851 0.9633 0.1787  -0.3479 0.1842  266 PHE   A CD1  
2050 C  CD2  . PHE   A 267 ? 1.5747 0.9616 0.9512 0.2013  -0.3648 0.1592  266 PHE   A CD2  
2051 C  CE1  . PHE   A 267 ? 1.6641 0.8753 0.976  0.226   -0.3448 0.1939  266 PHE   A CE1  
2052 C  CE2  . PHE   A 267 ? 1.6009 0.955  0.9642 0.2471  -0.3621 0.1679  266 PHE   A CE2  
2053 C  CZ   . PHE   A 267 ? 1.6384 0.9048 0.9691 0.2609  -0.3524 0.1857  266 PHE   A CZ   
2054 N  N    . LEU   A 268 ? 1.5526 0.9644 0.9482 0.0219  -0.355  0.1235  267 LEU   A N    
2055 C  CA   . LEU   A 268 ? 1.5527 1.0038 0.9584 -0.0145 -0.3553 0.1237  267 LEU   A CA   
2056 C  C    . LEU   A 268 ? 1.5913 0.9904 0.9864 -0.0527 -0.3441 0.1154  267 LEU   A C    
2057 O  O    . LEU   A 268 ? 1.5871 0.9999 0.9826 -0.08   -0.3413 0.1262  267 LEU   A O    
2058 C  CB   . LEU   A 268 ? 1.5239 1.0495 0.9544 -0.0197 -0.3621 0.1019  267 LEU   A CB   
2059 C  CG   . LEU   A 268 ? 1.5229 1.1062 0.9643 0.0094  -0.3712 0.1112  267 LEU   A CG   
2060 C  CD1  . LEU   A 268 ? 1.5063 1.1468 0.9667 0.0078  -0.3749 0.0874  267 LEU   A CD1  
2061 C  CD2  . LEU   A 268 ? 1.522  1.1346 0.9606 0.0058  -0.3745 0.1386  267 LEU   A CD2  
2062 N  N    . ILE   A 269 ? 1.6291 0.9688 1.0141 -0.056  -0.3368 0.0955  268 ILE   A N    
2063 C  CA   . ILE   A 269 ? 1.6753 0.9586 1.0483 -0.0944 -0.3245 0.0848  268 ILE   A CA   
2064 C  C    . ILE   A 269 ? 1.7331 0.952  1.079  -0.0959 -0.315  0.1174  268 ILE   A C    
2065 O  O    . ILE   A 269 ? 1.7384 0.9521 1.0813 -0.1308 -0.308  0.1249  268 ILE   A O    
2066 C  CB   . ILE   A 269 ? 1.7004 0.9321 1.0652 -0.0933 -0.319  0.0543  268 ILE   A CB   
2067 C  CG1  . ILE   A 269 ? 1.6802 0.9802 1.0706 -0.1    -0.3275 0.0207  268 ILE   A CG1  
2068 C  CG2  . ILE   A 269 ? 1.7403 0.891  1.084  -0.1299 -0.3032 0.0468  268 ILE   A CG2  
2069 C  CD1  . ILE   A 269 ? 1.7101 0.973  1.093  -0.0894 -0.325  -0.0089 268 ILE   A CD1  
2070 N  N    . LEU   A 270 ? 1.7714 0.9487 1.0979 -0.0556 -0.315  0.1387  269 LEU   A N    
2071 C  CA   . LEU   A 270 ? 1.8258 0.9407 1.122  -0.0476 -0.3064 0.1732  269 LEU   A CA   
2072 C  C    . LEU   A 270 ? 1.832  0.9993 1.1328 -0.0548 -0.3121 0.2011  269 LEU   A C    
2073 O  O    . LEU   A 270 ? 1.8557 0.9769 1.1321 -0.0619 -0.3032 0.2272  269 LEU   A O    
2074 C  CB   . LEU   A 270 ? 1.8502 0.9213 1.1264 0.0045  -0.307  0.1893  269 LEU   A CB   
2075 C  CG   . LEU   A 270 ? 1.8871 0.9114 1.1576 0.0211  -0.3022 0.1624  269 LEU   A CG   
2076 C  CD1  . LEU   A 270 ? 1.9115 0.9064 1.1648 0.0778  -0.3035 0.1815  269 LEU   A CD1  
2077 C  CD2  . LEU   A 270 ? 1.9313 0.8671 1.1805 -0.0151 -0.2846 0.1442  269 LEU   A CD2  
2078 N  N    . ASP   A 271 ? 1.8122 1.0715 1.1408 -0.0526 -0.3254 0.1957  270 ASP   A N    
2079 C  CA   . ASP   A 271 ? 1.8185 1.1317 1.1517 -0.0614 -0.3306 0.2171  270 ASP   A CA   
2080 C  C    . ASP   A 271 ? 1.8377 1.1464 1.1711 -0.1089 -0.3206 0.2137  270 ASP   A C    
2081 O  O    . ASP   A 271 ? 1.8408 1.1544 1.163  -0.1187 -0.3179 0.2381  270 ASP   A O    
2082 C  CB   . ASP   A 271 ? 1.8082 1.2139 1.169  -0.0502 -0.3446 0.2075  270 ASP   A CB   
2083 C  CG   . ASP   A 271 ? 1.866  1.2982 1.2262 -0.0073 -0.3553 0.2234  270 ASP   A CG   
2084 O  OD1  . ASP   A 271 ? 1.9016 1.2894 1.2392 0.0165  -0.3536 0.2476  270 ASP   A OD1  
2085 O  OD2  . ASP   A 271 ? 1.8627 1.3617 1.2443 0.0026  -0.3649 0.2122  270 ASP   A OD2  
2086 N  N    . LYS   A 272 ? 1.8467 1.1498 1.1925 -0.1385 -0.315  0.1833  271 LYS   A N    
2087 C  CA   . LYS   A 272 ? 1.8613 1.167  1.2105 -0.1847 -0.305  0.1775  271 LYS   A CA   
2088 C  C    . LYS   A 272 ? 1.9153 1.1275 1.2366 -0.2064 -0.2877 0.1855  271 LYS   A C    
2089 O  O    . LYS   A 272 ? 1.9197 1.1175 1.2459 -0.246  -0.2778 0.165   271 LYS   A O    
2090 C  CB   . LYS   A 272 ? 1.8571 1.2178 1.2352 -0.2081 -0.3083 0.1416  271 LYS   A CB   
2091 C  CG   . LYS   A 272 ? 1.871  1.3244 1.2721 -0.2045 -0.3188 0.1409  271 LYS   A CG   
2092 C  CD   . LYS   A 272 ? 1.9018 1.4069 1.3267 -0.2343 -0.3182 0.1115  271 LYS   A CD   
2093 C  CE   . LYS   A 272 ? 1.9142 1.5029 1.3567 -0.2292 -0.3257 0.1126  271 LYS   A CE   
2094 N  NZ   . LYS   A 272 ? 1.94   1.5403 1.3746 -0.2418 -0.3205 0.1379  271 LYS   A NZ   
2095 N  N    . PHE   A 273 ? 1.9527 1.1034 1.2433 -0.1805 -0.2834 0.216   272 PHE   A N    
2096 C  CA   . PHE   A 273 ? 2.0088 1.0597 1.2642 -0.1935 -0.265  0.2315  272 PHE   A CA   
2097 C  C    . PHE   A 273 ? 2.0299 1.0605 1.2578 -0.1665 -0.2647 0.2752  272 PHE   A C    
2098 O  O    . PHE   A 273 ? 2.0487 1.0471 1.2591 -0.1228 -0.2688 0.2909  272 PHE   A O    
2099 C  CB   . PHE   A 273 ? 2.0433 1.0143 1.2815 -0.1758 -0.2587 0.217   272 PHE   A CB   
2100 C  CG   . PHE   A 273 ? 2.0508 1.0189 1.3056 -0.2063 -0.2551 0.1743  272 PHE   A CG   
2101 C  CD1  . PHE   A 273 ? 2.086  0.9976 1.329  -0.2535 -0.2374 0.1611  272 PHE   A CD1  
2102 C  CD2  . PHE   A 273 ? 2.0348 1.0581 1.3156 -0.1888 -0.2691 0.147   272 PHE   A CD2  
2103 C  CE1  . PHE   A 273 ? 2.0902 1.0053 1.3485 -0.283  -0.2352 0.1197  272 PHE   A CE1  
2104 C  CE2  . PHE   A 273 ? 2.04   1.0648 1.3341 -0.2159 -0.2667 0.1074  272 PHE   A CE2  
2105 C  CZ   . PHE   A 273 ? 2.0596 1.0321 1.3427 -0.2629 -0.2506 0.0932  272 PHE   A CZ   
2106 N  N    . LEU   A 274 ? 2.0236 1.077  1.2472 -0.1899 -0.2603 0.2948  273 LEU   A N    
2107 C  CA   . LEU   A 274 ? 2.0433 1.0834 1.2391 -0.1647 -0.2609 0.3359  273 LEU   A CA   
2108 C  C    . LEU   A 274 ? 2.0837 1.0437 1.2429 -0.1884 -0.2398 0.3603  273 LEU   A C    
2109 O  O    . LEU   A 274 ? 2.1137 1.0166 1.2367 -0.1596 -0.2351 0.3925  273 LEU   A O    
2110 C  CB   . LEU   A 274 ? 2.0095 1.1475 1.2248 -0.1608 -0.2755 0.3441  273 LEU   A CB   
2111 C  CG   . LEU   A 274 ? 2.0147 1.1982 1.2343 -0.1126 -0.2941 0.3549  273 LEU   A CG   
2112 C  CD1  . LEU   A 274 ? 2.0042 1.2116 1.2498 -0.0949 -0.3041 0.3251  273 LEU   A CD1  
2113 C  CD2  . LEU   A 274 ? 1.9932 1.2608 1.224  -0.115  -0.3049 0.3647  273 LEU   A CD2  
2114 N  N    . VAL   B 26  ? 2.0171 1.239  1.5387 -0.5342 -0.0926 0.5233  25  VAL   B N    
2115 C  CA   . VAL   B 26  ? 2.0177 1.2439 1.5592 -0.5727 -0.0688 0.5308  25  VAL   B CA   
2116 C  C    . VAL   B 26  ? 2.0512 1.2249 1.5757 -0.5727 -0.041  0.5865  25  VAL   B C    
2117 O  O    . VAL   B 26  ? 2.0495 1.2558 1.5596 -0.5818 -0.0277 0.6135  25  VAL   B O    
2118 C  CB   . VAL   B 26  ? 2.0149 1.2234 1.6039 -0.6088 -0.0642 0.4869  25  VAL   B CB   
2119 C  CG1  . VAL   B 26  ? 2.0136 1.2211 1.6291 -0.6508 -0.0364 0.4964  25  VAL   B CG1  
2120 C  CG2  . VAL   B 26  ? 1.9943 1.2664 1.596  -0.6078 -0.0908 0.4363  25  VAL   B CG2  
2121 N  N    . PHE   B 27  ? 2.0795 1.172  1.6031 -0.5601 -0.0315 0.6049  26  PHE   B N    
2122 C  CA   . PHE   B 27  ? 2.1107 1.1422 1.6174 -0.5552 -0.0039 0.6604  26  PHE   B CA   
2123 C  C    . PHE   B 27  ? 2.1171 1.1871 1.5742 -0.5223 -0.0096 0.7067  26  PHE   B C    
2124 O  O    . PHE   B 27  ? 2.1185 1.2039 1.5605 -0.5339 0.0094  0.7395  26  PHE   B O    
2125 C  CB   . PHE   B 27  ? 2.1374 1.0766 1.6529 -0.5413 0.0036  0.6658  26  PHE   B CB   
2126 C  CG   . PHE   B 27  ? 2.1717 1.0276 1.6916 -0.5539 0.0404  0.7073  26  PHE   B CG   
2127 C  CD1  . PHE   B 27  ? 2.1775 1.011  1.7321 -0.6011 0.0671  0.6977  26  PHE   B CD1  
2128 C  CD2  . PHE   B 27  ? 2.21   1.0075 1.703  -0.5182 0.0492  0.7545  26  PHE   B CD2  
2129 C  CE1  . PHE   B 27  ? 2.2114 0.9627 1.7718 -0.6138 0.104   0.7362  26  PHE   B CE1  
2130 C  CE2  . PHE   B 27  ? 2.245  0.9603 1.7416 -0.5279 0.0855  0.7947  26  PHE   B CE2  
2131 C  CZ   . PHE   B 27  ? 2.2395 0.9296 1.7694 -0.5764 0.1137  0.7853  26  PHE   B CZ   
2132 N  N    . PHE   B 28  ? 2.1158 1.2064 1.5484 -0.4827 -0.0358 0.7065  27  PHE   B N    
2133 C  CA   . PHE   B 28  ? 2.1174 1.2539 1.5047 -0.4512 -0.0467 0.7419  27  PHE   B CA   
2134 C  C    . PHE   B 28  ? 2.0874 1.3003 1.4704 -0.4395 -0.0787 0.7026  27  PHE   B C    
2135 O  O    . PHE   B 28  ? 2.091  1.3033 1.4698 -0.4108 -0.0996 0.6909  27  PHE   B O    
2136 C  CB   . PHE   B 28  ? 2.1452 1.2303 1.5094 -0.4119 -0.0466 0.7831  27  PHE   B CB   
2137 C  CG   . PHE   B 28  ? 2.1837 1.1966 1.5426 -0.4169 -0.0132 0.8324  27  PHE   B CG   
2138 C  CD1  . PHE   B 28  ? 2.1985 1.2302 1.5296 -0.423  0.0046  0.8742  27  PHE   B CD1  
2139 C  CD2  . PHE   B 28  ? 2.2187 1.1426 1.5984 -0.414  0.002   0.8379  27  PHE   B CD2  
2140 C  CE1  . PHE   B 28  ? 2.2333 1.1956 1.5578 -0.4263 0.0379  0.9229  27  PHE   B CE1  
2141 C  CE2  . PHE   B 28  ? 2.2541 1.106  1.6287 -0.4176 0.0355  0.8854  27  PHE   B CE2  
2142 C  CZ   . PHE   B 28  ? 2.2535 1.1249 1.6006 -0.4237 0.0535  0.9288  27  PHE   B CZ   
2143 N  N    . PRO   B 29  ? 2.0548 1.3312 1.4427 -0.4626 -0.0807 0.6798  28  PRO   B N    
2144 C  CA   . PRO   B 29  ? 2.0266 1.3692 1.4143 -0.4538 -0.1077 0.6399  28  PRO   B CA   
2145 C  C    . PRO   B 29  ? 2.0093 1.4094 1.3573 -0.4265 -0.1241 0.6553  28  PRO   B C    
2146 O  O    . PRO   B 29  ? 2.0167 1.4295 1.3345 -0.4224 -0.1138 0.6931  28  PRO   B O    
2147 C  CB   . PRO   B 29  ? 2.0163 1.3964 1.4309 -0.4907 -0.1001 0.6085  28  PRO   B CB   
2148 C  CG   . PRO   B 29  ? 2.0301 1.3858 1.4467 -0.5157 -0.0697 0.641   28  PRO   B CG   
2149 C  CD   . PRO   B 29  ? 2.0397 1.3278 1.4375 -0.4982 -0.0563 0.6878  28  PRO   B CD   
2150 N  N    . ARG   B 30  ? 1.9828 1.4197 1.3318 -0.4097 -0.1492 0.6229  29  ARG   B N    
2151 C  CA   . ARG   B 30  ? 1.9674 1.4592 1.2868 -0.3839 -0.1692 0.6244  29  ARG   B CA   
2152 C  C    . ARG   B 30  ? 1.9541 1.4948 1.2399 -0.3868 -0.1631 0.6484  29  ARG   B C    
2153 O  O    . ARG   B 30  ? 1.9493 1.5084 1.2396 -0.4132 -0.1474 0.6455  29  ARG   B O    
2154 C  CB   . ARG   B 30  ? 1.9618 1.4932 1.2966 -0.3812 -0.189  0.5764  29  ARG   B CB   
2155 C  CG   . ARG   B 30  ? 1.9914 1.544  1.3095 -0.3481 -0.2108 0.5754  29  ARG   B CG   
2156 C  CD   . ARG   B 30  ? 2.0146 1.5754 1.3547 -0.342  -0.2263 0.5322  29  ARG   B CD   
2157 N  NE   . ARG   B 30  ? 2.0414 1.6256 1.3683 -0.3125 -0.2449 0.5318  29  ARG   B NE   
2158 C  CZ   . ARG   B 30  ? 2.06   1.6458 1.4019 -0.2996 -0.2578 0.5027  29  ARG   B CZ   
2159 N  NH1  . ARG   B 30  ? 2.054  1.619  1.4209 -0.3118 -0.2557 0.4716  29  ARG   B NH1  
2160 N  NH2  . ARG   B 30  ? 2.0537 1.6638 1.3857 -0.2746 -0.2727 0.5044  29  ARG   B NH2  
2161 N  N    . LYS   B 31  ? 1.9438 1.5073 1.1956 -0.3587 -0.1758 0.6721  30  LYS   B N    
2162 C  CA   . LYS   B 31  ? 1.9293 1.5401 1.1416 -0.356  -0.173  0.696   30  LYS   B CA   
2163 C  C    . LYS   B 31  ? 1.8916 1.5703 1.0997 -0.365  -0.1825 0.66    30  LYS   B C    
2164 O  O    . LYS   B 31  ? 1.8813 1.5881 1.0922 -0.3507 -0.2032 0.633   30  LYS   B O    
2165 C  CB   . LYS   B 31  ? 1.9574 1.5726 1.1364 -0.3218 -0.186  0.7309  30  LYS   B CB   
2166 C  CG   . LYS   B 31  ? 2.0065 1.6396 1.1423 -0.3187 -0.1742 0.7746  30  LYS   B CG   
2167 C  CD   . LYS   B 31  ? 2.0549 1.7007 1.1574 -0.2824 -0.1903 0.8082  30  LYS   B CD   
2168 C  CE   . LYS   B 31  ? 2.093  1.7633 1.1473 -0.2782 -0.1799 0.8503  30  LYS   B CE   
2169 N  NZ   . LYS   B 31  ? 2.1138 1.8034 1.1355 -0.2415 -0.1979 0.8826  30  LYS   B NZ   
2170 N  N    . ARG   B 32  ? 1.8672 1.5706 1.0696 -0.3887 -0.1652 0.6603  31  ARG   B N    
2171 C  CA   . ARG   B 32  ? 1.8348 1.5999 1.0316 -0.3975 -0.1692 0.6297  31  ARG   B CA   
2172 C  C    . ARG   B 32  ? 1.8129 1.6245 0.9618 -0.3815 -0.1766 0.6469  31  ARG   B C    
2173 O  O    . ARG   B 32  ? 1.8267 1.6353 0.9447 -0.3801 -0.1643 0.6854  31  ARG   B O    
2174 C  CB   . ARG   B 32  ? 1.8459 1.6191 1.0591 -0.4288 -0.1458 0.6234  31  ARG   B CB   
2175 C  CG   . ARG   B 32  ? 1.8713 1.6327 1.1329 -0.4467 -0.1454 0.5859  31  ARG   B CG   
2176 C  CD   . ARG   B 32  ? 1.8846 1.7025 1.1543 -0.4547 -0.1485 0.5486  31  ARG   B CD   
2177 N  NE   . ARG   B 32  ? 1.9063 1.7617 1.1582 -0.4692 -0.1296 0.5599  31  ARG   B NE   
2178 C  CZ   . ARG   B 32  ? 1.9058 1.7991 1.1761 -0.4857 -0.1206 0.5348  31  ARG   B CZ   
2179 N  NH1  . ARG   B 32  ? 1.884  1.784  1.1903 -0.4895 -0.1296 0.498   31  ARG   B NH1  
2180 N  NH2  . ARG   B 32  ? 1.8976 1.8238 1.1496 -0.4969 -0.1018 0.5471  31  ARG   B NH2  
2181 N  N    . LYS   B 33  ? 1.777  1.6315 0.9191 -0.37   -0.1957 0.618   32  LYS   B N    
2182 C  CA   . LYS   B 33  ? 1.7587 1.6619 0.8575 -0.3565 -0.2051 0.6264  32  LYS   B CA   
2183 C  C    . LYS   B 33  ? 1.7237 1.6763 0.809  -0.3731 -0.1949 0.6046  32  LYS   B C    
2184 O  O    . LYS   B 33  ? 1.7143 1.6644 0.8266 -0.393  -0.1812 0.5845  32  LYS   B O    
2185 C  CB   . LYS   B 33  ? 1.7745 1.6935 0.8744 -0.3332 -0.232  0.6095  32  LYS   B CB   
2186 C  CG   . LYS   B 33  ? 1.8025 1.7453 0.9261 -0.3382 -0.2405 0.5608  32  LYS   B CG   
2187 C  CD   . LYS   B 33  ? 1.8514 1.8111 0.9764 -0.317  -0.2641 0.5461  32  LYS   B CD   
2188 C  CE   . LYS   B 33  ? 1.8884 1.8724 1.0319 -0.3221 -0.2689 0.5006  32  LYS   B CE   
2189 N  NZ   . LYS   B 33  ? 1.9134 1.9053 1.0673 -0.3035 -0.289  0.4856  32  LYS   B NZ   
2190 N  N    . SER   B 34  ? 1.7015 1.7002 0.7449 -0.3646 -0.2009 0.6084  33  SER   B N    
2191 C  CA   . SER   B 34  ? 1.676  1.7206 0.7033 -0.3778 -0.1907 0.5863  33  SER   B CA   
2192 C  C    . SER   B 34  ? 1.6481 1.7293 0.6751 -0.3692 -0.2092 0.5467  33  SER   B C    
2193 O  O    . SER   B 34  ? 1.6517 1.7426 0.6668 -0.3513 -0.23   0.5482  33  SER   B O    
2194 C  CB   . SER   B 34  ? 1.6919 1.7619 0.668  -0.3773 -0.1798 0.6178  33  SER   B CB   
2195 O  OG   . SER   B 34  ? 1.6992 1.814  0.6574 -0.3887 -0.1693 0.5944  33  SER   B OG   
2196 N  N    . VAL   B 35  ? 1.6164 1.7174 0.6591 -0.3817 -0.2008 0.5114  34  VAL   B N    
2197 C  CA   . VAL   B 35  ? 1.5926 1.7248 0.6349 -0.3756 -0.2134 0.4732  34  VAL   B CA   
2198 C  C    . VAL   B 35  ? 1.5665 1.744  0.5755 -0.3836 -0.2016 0.4593  34  VAL   B C    
2199 O  O    . VAL   B 35  ? 1.557  1.7548 0.5737 -0.3858 -0.2008 0.4231  34  VAL   B O    
2200 C  CB   . VAL   B 35  ? 1.5978 1.7119 0.6864 -0.3779 -0.2153 0.4407  34  VAL   B CB   
2201 C  CG1  . VAL   B 35  ? 1.6114 1.6877 0.7252 -0.3654 -0.2314 0.4479  34  VAL   B CG1  
2202 C  CG2  . VAL   B 35  ? 1.6003 1.7053 0.7134 -0.3954 -0.1946 0.4363  34  VAL   B CG2  
2203 N  N    . ALA   B 36  ? 1.5545 1.7459 0.5246 -0.3867 -0.1911 0.4889  35  ALA   B N    
2204 C  CA   . ALA   B 36  ? 1.5383 1.7713 0.4715 -0.3938 -0.1779 0.4791  35  ALA   B CA   
2205 C  C    . ALA   B 36  ? 1.522  1.7922 0.4196 -0.3826 -0.1966 0.4642  35  ALA   B C    
2206 O  O    . ALA   B 36  ? 1.5265 1.7991 0.4048 -0.3691 -0.2148 0.4862  35  ALA   B O    
2207 C  CB   . ALA   B 36  ? 1.5477 1.7801 0.4517 -0.4007 -0.1587 0.5184  35  ALA   B CB   
2208 N  N    . GLY   B 37  ? 1.4994 1.7988 0.3909 -0.3881 -0.1917 0.426   36  GLY   B N    
2209 C  CA   . GLY   B 37  ? 1.4871 1.8239 0.3482 -0.382  -0.2071 0.403   36  GLY   B CA   
2210 C  C    . GLY   B 37  ? 1.4642 1.7947 0.3544 -0.373  -0.2299 0.3799  36  GLY   B C    
2211 O  O    . GLY   B 37  ? 1.4688 1.8304 0.3381 -0.3679 -0.2462 0.3644  36  GLY   B O    
2212 N  N    . GLU   B 38  ? 1.4342 1.7268 0.3726 -0.3712 -0.2312 0.3765  37  GLU   B N    
2213 C  CA   . GLU   B 38  ? 1.4103 1.6943 0.3779 -0.3621 -0.2501 0.3564  37  GLU   B CA   
2214 C  C    . GLU   B 38  ? 1.3818 1.6713 0.3682 -0.3679 -0.2421 0.3117  37  GLU   B C    
2215 O  O    . GLU   B 38  ? 1.3833 1.6694 0.3754 -0.3769 -0.2215 0.3004  37  GLU   B O    
2216 C  CB   . GLU   B 38  ? 1.438  1.6767 0.4448 -0.3557 -0.2547 0.3749  37  GLU   B CB   
2217 C  CG   . GLU   B 38  ? 1.4994 1.725  0.4926 -0.3459 -0.2644 0.4184  37  GLU   B CG   
2218 C  CD   . GLU   B 38  ? 1.5692 1.797  0.5706 -0.329  -0.2892 0.4218  37  GLU   B CD   
2219 O  OE1  . GLU   B 38  ? 1.5797 1.8261 0.5521 -0.3185 -0.3014 0.4483  37  GLU   B OE1  
2220 O  OE2  . GLU   B 38  ? 1.5976 1.8109 0.6342 -0.3252 -0.2961 0.3985  37  GLU   B OE2  
2221 N  N    . ILE   B 39  ? 1.3523 1.6495 0.3512 -0.3623 -0.2569 0.2871  38  ILE   B N    
2222 C  CA   . ILE   B 39  ? 1.3269 1.6228 0.3453 -0.3666 -0.2473 0.2464  38  ILE   B CA   
2223 C  C    . ILE   B 39  ? 1.2984 1.5554 0.362  -0.3609 -0.2456 0.2435  38  ILE   B C    
2224 O  O    . ILE   B 39  ? 1.2969 1.5406 0.3813 -0.3516 -0.2613 0.2464  38  ILE   B O    
2225 C  CB   . ILE   B 39  ? 1.3274 1.6515 0.3367 -0.367  -0.259  0.2167  38  ILE   B CB   
2226 C  CG1  . ILE   B 39  ? 1.3445 1.7118 0.304  -0.3736 -0.2606 0.2163  38  ILE   B CG1  
2227 C  CG2  . ILE   B 39  ? 1.3275 1.6403 0.3599 -0.3711 -0.2445 0.1774  38  ILE   B CG2  
2228 C  CD1  . ILE   B 39  ? 1.3567 1.7579 0.3046 -0.3778 -0.2717 0.1832  38  ILE   B CD1  
2229 N  N    . VAL   B 40  ? 1.275  1.5165 0.3539 -0.3656 -0.2269 0.2387  39  VAL   B N    
2230 C  CA   . VAL   B 40  ? 1.2566 1.4648 0.3756 -0.3599 -0.2254 0.2356  39  VAL   B CA   
2231 C  C    . VAL   B 40  ? 1.2303 1.4356 0.3667 -0.3581 -0.2137 0.2014  39  VAL   B C    
2232 O  O    . VAL   B 40  ? 1.2317 1.4472 0.3629 -0.3635 -0.1952 0.189   39  VAL   B O    
2233 C  CB   . VAL   B 40  ? 1.2674 1.4589 0.3982 -0.3649 -0.2158 0.258   39  VAL   B CB   
2234 C  CG1  . VAL   B 40  ? 1.2705 1.43   0.441  -0.3585 -0.2185 0.254   39  VAL   B CG1  
2235 C  CG2  . VAL   B 40  ? 1.2818 1.4721 0.3927 -0.3672 -0.2226 0.2944  39  VAL   B CG2  
2236 N  N    . LEU   B 41  ? 1.2042 1.3942 0.3622 -0.3492 -0.2227 0.1878  40  LEU   B N    
2237 C  CA   . LEU   B 41  ? 1.1834 1.364  0.3596 -0.3449 -0.2106 0.1585  40  LEU   B CA   
2238 C  C    . LEU   B 41  ? 1.1673 1.3206 0.3737 -0.337  -0.2074 0.1637  40  LEU   B C    
2239 O  O    . LEU   B 41  ? 1.1676 1.3026 0.388  -0.3316 -0.221  0.1798  40  LEU   B O    
2240 C  CB   . LEU   B 41  ? 1.1781 1.3577 0.3615 -0.3404 -0.22   0.1407  40  LEU   B CB   
2241 C  CG   . LEU   B 41  ? 1.1889 1.3609 0.3835 -0.3383 -0.2036 0.109   40  LEU   B CG   
2242 C  CD1  . LEU   B 41  ? 1.188  1.3771 0.3733 -0.3444 -0.2073 0.0873  40  LEU   B CD1  
2243 C  CD2  . LEU   B 41  ? 1.1977 1.3386 0.4238 -0.3252 -0.2024 0.1068  40  LEU   B CD2  
2244 N  N    . ILE   B 42  ? 1.1516 1.3035 0.3681 -0.3352 -0.1899 0.1499  41  ILE   B N    
2245 C  CA   . ILE   B 42  ? 1.1439 1.2762 0.3884 -0.3267 -0.1881 0.1525  41  ILE   B CA   
2246 C  C    . ILE   B 42  ? 1.1314 1.2544 0.39   -0.3148 -0.1755 0.1287  41  ILE   B C    
2247 O  O    . ILE   B 42  ? 1.1293 1.2645 0.3833 -0.315  -0.1577 0.1155  41  ILE   B O    
2248 C  CB   . ILE   B 42  ? 1.1468 1.2893 0.3953 -0.3346 -0.1807 0.1667  41  ILE   B CB   
2249 C  CG1  . ILE   B 42  ? 1.1626 1.3095 0.3955 -0.3461 -0.1898 0.1931  41  ILE   B CG1  
2250 C  CG2  . ILE   B 42  ? 1.1491 1.2763 0.4277 -0.3269 -0.1821 0.167   41  ILE   B CG2  
2251 C  CD1  . ILE   B 42  ? 1.1765 1.3415 0.4038 -0.3578 -0.1768 0.2039  41  ILE   B CD1  
2252 N  N    . THR   B 43  ? 1.122  1.2225 0.3968 -0.3032 -0.1828 0.1241  42  THR   B N    
2253 C  CA   . THR   B 43  ? 1.123  1.2107 0.4098 -0.2899 -0.1696 0.105   42  THR   B CA   
2254 C  C    . THR   B 43  ? 1.1182 1.2026 0.4221 -0.2801 -0.1644 0.1082  42  THR   B C    
2255 O  O    . THR   B 43  ? 1.1214 1.2014 0.4357 -0.2809 -0.1769 0.1224  42  THR   B O    
2256 C  CB   . THR   B 43  ? 1.1444 1.2108 0.4408 -0.2812 -0.1774 0.0999  42  THR   B CB   
2257 O  OG1  . THR   B 43  ? 1.1629 1.2141 0.4725 -0.2751 -0.1927 0.1151  42  THR   B OG1  
2258 C  CG2  . THR   B 43  ? 1.1487 1.2247 0.4328 -0.2911 -0.1845 0.0952  42  THR   B CG2  
2259 N  N    . GLY   B 44  ? 1.107  1.1934 0.4151 -0.2699 -0.1463 0.0943  43  GLY   B N    
2260 C  CA   . GLY   B 44  ? 1.0965 1.1876 0.4214 -0.2584 -0.1418 0.0964  43  GLY   B CA   
2261 C  C    . GLY   B 44  ? 1.0801 1.1982 0.4065 -0.2711 -0.1414 0.1066  43  GLY   B C    
2262 O  O    . GLY   B 44  ? 1.0699 1.1939 0.4128 -0.271  -0.1495 0.1154  43  GLY   B O    
2263 N  N    . ALA   B 45  ? 1.0773 1.2126 0.3862 -0.2833 -0.1312 0.1044  44  ALA   B N    
2264 C  CA   . ALA   B 45  ? 1.0691 1.2309 0.3767 -0.297  -0.1274 0.1152  44  ALA   B CA   
2265 C  C    . ALA   B 45  ? 1.0528 1.2383 0.3669 -0.2911 -0.1061 0.106   44  ALA   B C    
2266 O  O    . ALA   B 45  ? 1.0503 1.2604 0.3591 -0.303  -0.0977 0.1119  44  ALA   B O    
2267 C  CB   . ALA   B 45  ? 1.0806 1.2495 0.3618 -0.3141 -0.1307 0.123   44  ALA   B CB   
2268 N  N    . GLY   B 46  ? 1.0408 1.2194 0.3666 -0.2714 -0.0964 0.0933  45  GLY   B N    
2269 C  CA   . GLY   B 46  ? 1.0263 1.2272 0.3612 -0.2609 -0.0758 0.0855  45  GLY   B CA   
2270 C  C    . GLY   B 46  ? 0.9978 1.2237 0.3612 -0.2564 -0.0802 0.0939  45  GLY   B C    
2271 O  O    . GLY   B 46  ? 0.9889 1.2431 0.3635 -0.2504 -0.0644 0.0906  45  GLY   B O    
2272 N  N    . HIS   B 47  ? 0.9769 1.1947 0.3538 -0.2593 -0.1013 0.1033  46  HIS   B N    
2273 C  CA   . HIS   B 47  ? 0.946  1.1884 0.3516 -0.2575 -0.1085 0.1081  46  HIS   B CA   
2274 C  C    . HIS   B 47  ? 0.9366 1.1625 0.3498 -0.2679 -0.1319 0.1172  46  HIS   B C    
2275 O  O    . HIS   B 47  ? 0.9427 1.1358 0.3412 -0.2684 -0.1424 0.1192  46  HIS   B O    
2276 C  CB   . HIS   B 47  ? 0.9501 1.1987 0.3693 -0.229  -0.1017 0.0982  46  HIS   B CB   
2277 C  CG   . HIS   B 47  ? 0.9543 1.2361 0.404  -0.2233 -0.1098 0.0999  46  HIS   B CG   
2278 N  ND1  . HIS   B 47  ? 0.9591 1.2784 0.4284 -0.2414 -0.1091 0.1052  46  HIS   B ND1  
2279 C  CD2  . HIS   B 47  ? 0.958  1.2437 0.4211 -0.2015 -0.1179 0.0959  46  HIS   B CD2  
2280 C  CE1  . HIS   B 47  ? 0.9451 1.2914 0.4418 -0.2318 -0.1185 0.1025  46  HIS   B CE1  
2281 N  NE2  . HIS   B 47  ? 0.9477 1.2761 0.4399 -0.2068 -0.1248 0.097   46  HIS   B NE2  
2282 N  N    . GLY   B 48  ? 0.9219 1.1722 0.36   -0.2767 -0.1387 0.1217  47  GLY   B N    
2283 C  CA   . GLY   B 48  ? 0.929  1.1667 0.3799 -0.2867 -0.1589 0.1272  47  GLY   B CA   
2284 C  C    . GLY   B 48  ? 0.9456 1.1573 0.3828 -0.3076 -0.167  0.1409  47  GLY   B C    
2285 O  O    . GLY   B 48  ? 0.9475 1.1705 0.3784 -0.3255 -0.1585 0.1512  47  GLY   B O    
2286 N  N    . ILE   B 49  ? 0.9537 1.1307 0.3855 -0.3039 -0.1829 0.1423  48  ILE   B N    
2287 C  CA   . ILE   B 49  ? 0.9665 1.1153 0.3864 -0.3192 -0.1921 0.1568  48  ILE   B CA   
2288 C  C    . ILE   B 49  ? 0.9796 1.1229 0.371  -0.3225 -0.1843 0.1636  48  ILE   B C    
2289 O  O    . ILE   B 49  ? 0.9897 1.127  0.3707 -0.3382 -0.1859 0.1795  48  ILE   B O    
2290 C  CB   . ILE   B 49  ? 0.9793 1.093  0.4011 -0.311  -0.2094 0.1553  48  ILE   B CB   
2291 C  CG1  . ILE   B 49  ? 0.9741 1.0973 0.4204 -0.3057 -0.2174 0.144   48  ILE   B CG1  
2292 C  CG2  . ILE   B 49  ? 0.9976 1.084  0.4126 -0.3266 -0.2179 0.1724  48  ILE   B CG2  
2293 C  CD1  . ILE   B 49  ? 1.0005 1.0922 0.4455 -0.2947 -0.2316 0.1393  48  ILE   B CD1  
2294 N  N    . GLY   B 50  ? 0.9752 1.122  0.3541 -0.308  -0.1751 0.1516  49  GLY   B N    
2295 C  CA   . GLY   B 50  ? 0.9785 1.1242 0.3306 -0.3121 -0.168  0.1531  49  GLY   B CA   
2296 C  C    . GLY   B 50  ? 0.959  1.1343 0.3031 -0.3246 -0.1523 0.1567  49  GLY   B C    
2297 O  O    . GLY   B 50  ? 0.9652 1.1422 0.2869 -0.3363 -0.1511 0.1664  49  GLY   B O    
2298 N  N    . ARG   B 51  ? 0.9384 1.1396 0.3001 -0.3206 -0.14   0.1491  50  ARG   B N    
2299 C  CA   . ARG   B 51  ? 0.9312 1.1644 0.2897 -0.3301 -0.1218 0.1508  50  ARG   B CA   
2300 C  C    . ARG   B 51  ? 0.9347 1.1763 0.2972 -0.3522 -0.1242 0.1703  50  ARG   B C    
2301 O  O    . ARG   B 51  ? 0.9394 1.1934 0.2818 -0.3641 -0.1135 0.179   50  ARG   B O    
2302 C  CB   . ARG   B 51  ? 0.9218 1.1825 0.3048 -0.3168 -0.1094 0.1384  50  ARG   B CB   
2303 C  CG   . ARG   B 51  ? 0.9179 1.218  0.3113 -0.3276 -0.0922 0.1424  50  ARG   B CG   
2304 C  CD   . ARG   B 51  ? 0.919  1.2477 0.3344 -0.3095 -0.0788 0.1292  50  ARG   B CD   
2305 N  NE   . ARG   B 51  ? 0.9395 1.2674 0.3332 -0.297  -0.0592 0.117   50  ARG   B NE   
2306 C  CZ   . ARG   B 51  ? 0.9471 1.2956 0.3534 -0.2783 -0.0421 0.1059  50  ARG   B CZ   
2307 N  NH1  . ARG   B 51  ? 0.9314 1.3087 0.3722 -0.2685 -0.0442 0.106   50  ARG   B NH1  
2308 N  NH2  . ARG   B 51  ? 0.944  1.2846 0.3288 -0.2684 -0.0229 0.0936  50  ARG   B NH2  
2309 N  N    . TRP   B 52  ? 0.9333 1.1671 0.3205 -0.358  -0.137  0.1769  51  TRP   B N    
2310 C  CA   . TRP   B 52  ? 0.94   1.1766 0.3354 -0.3805 -0.137  0.1957  51  TRP   B CA   
2311 C  C    . TRP   B 52  ? 0.9656 1.1698 0.3359 -0.3888 -0.147  0.2144  51  TRP   B C    
2312 O  O    . TRP   B 52  ? 0.9668 1.1713 0.3333 -0.4064 -0.142  0.2339  51  TRP   B O    
2313 C  CB   . TRP   B 52  ? 0.9242 1.1684 0.3588 -0.3862 -0.1442 0.1924  51  TRP   B CB   
2314 C  CG   . TRP   B 52  ? 0.9062 1.1947 0.3655 -0.3819 -0.1315 0.1799  51  TRP   B CG   
2315 C  CD1  . TRP   B 52  ? 0.9111 1.2148 0.3739 -0.359  -0.1277 0.1626  51  TRP   B CD1  
2316 C  CD2  . TRP   B 52  ? 0.887  1.212  0.369  -0.3995 -0.1176 0.1856  51  TRP   B CD2  
2317 N  NE1  . TRP   B 52  ? 0.8909 1.2398 0.3779 -0.3595 -0.1138 0.1574  51  TRP   B NE1  
2318 C  CE2  . TRP   B 52  ? 0.8764 1.2412 0.3772 -0.385  -0.1076 0.1703  51  TRP   B CE2  
2319 C  CE3  . TRP   B 52  ? 0.8912 1.2188 0.3804 -0.4257 -0.1108 0.2032  51  TRP   B CE3  
2320 C  CZ2  . TRP   B 52  ? 0.8589 1.2702 0.3886 -0.396  -0.0929 0.1708  51  TRP   B CZ2  
2321 C  CZ3  . TRP   B 52  ? 0.8785 1.2497 0.3963 -0.4387 -0.0951 0.2035  51  TRP   B CZ3  
2322 C  CH2  . TRP   B 52  ? 0.8571 1.2718 0.396  -0.424  -0.0869 0.1868  51  TRP   B CH2  
2323 N  N    . THR   B 53  ? 0.9836 1.1627 0.3362 -0.3753 -0.159  0.2099  52  THR   B N    
2324 C  CA   . THR   B 53  ? 1.0094 1.1647 0.3374 -0.379  -0.1686 0.2268  52  THR   B CA   
2325 C  C    . THR   B 53  ? 1.0234 1.1988 0.3181 -0.3835 -0.157  0.2316  52  THR   B C    
2326 O  O    . THR   B 53  ? 1.0333 1.2067 0.3094 -0.3945 -0.1563 0.2534  52  THR   B O    
2327 C  CB   . THR   B 53  ? 1.036  1.1636 0.3631 -0.3632 -0.1848 0.2185  52  THR   B CB   
2328 O  OG1  . THR   B 53  ? 1.0498 1.1539 0.3999 -0.3645 -0.1961 0.2229  52  THR   B OG1  
2329 C  CG2  . THR   B 53  ? 1.0514 1.1678 0.3497 -0.3609 -0.1927 0.2285  52  THR   B CG2  
2330 N  N    . ALA   B 54  ? 1.0225 1.2177 0.3091 -0.3751 -0.146  0.2117  53  ALA   B N    
2331 C  CA   . ALA   B 54  ? 1.0352 1.2521 0.2902 -0.3798 -0.1329 0.2109  53  ALA   B CA   
2332 C  C    . ALA   B 54  ? 1.0402 1.2805 0.2954 -0.3954 -0.1168 0.2261  53  ALA   B C    
2333 O  O    . ALA   B 54  ? 1.0559 1.3076 0.2798 -0.4034 -0.11   0.2378  53  ALA   B O    
2334 C  CB   . ALA   B 54  ? 1.0323 1.2608 0.2843 -0.3676 -0.1214 0.1839  53  ALA   B CB   
2335 N  N    . TYR   B 55  ? 1.0281 1.278  0.3182 -0.4002 -0.1107 0.2263  54  TYR   B N    
2336 C  CA   . TYR   B 55  ? 1.0308 1.3037 0.3276 -0.4171 -0.0944 0.2413  54  TYR   B CA   
2337 C  C    . TYR   B 55  ? 1.0514 1.3026 0.3381 -0.4314 -0.1011 0.2705  54  TYR   B C    
2338 O  O    . TYR   B 55  ? 1.0526 1.3162 0.3192 -0.4433 -0.0876 0.2885  54  TYR   B O    
2339 C  CB   . TYR   B 55  ? 1.0135 1.3047 0.3562 -0.4202 -0.089  0.2334  54  TYR   B CB   
2340 C  CG   . TYR   B 55  ? 1.0147 1.333  0.3719 -0.4051 -0.0783 0.2094  54  TYR   B CG   
2341 C  CD1  . TYR   B 55  ? 1.0325 1.3602 0.3616 -0.3943 -0.0662 0.1966  54  TYR   B CD1  
2342 C  CD2  . TYR   B 55  ? 1.0107 1.3464 0.4096 -0.4012 -0.0796 0.1992  54  TYR   B CD2  
2343 C  CE1  . TYR   B 55  ? 1.0344 1.3825 0.377  -0.3785 -0.0538 0.176   54  TYR   B CE1  
2344 C  CE2  . TYR   B 55  ? 1.0103 1.3712 0.4223 -0.3838 -0.0695 0.18    54  TYR   B CE2  
2345 C  CZ   . TYR   B 55  ? 1.0303 1.3952 0.4144 -0.372  -0.0553 0.1695  54  TYR   B CZ   
2346 O  OH   . TYR   B 55  ? 1.04   1.4257 0.4383 -0.3528 -0.0431 0.1519  54  TYR   B OH   
2347 N  N    . GLU   B 56  ? 1.0677 1.2853 0.3675 -0.4292 -0.1201 0.2761  55  GLU   B N    
2348 C  CA   . GLU   B 56  ? 1.0987 1.2888 0.3916 -0.4399 -0.1259 0.3043  55  GLU   B CA   
2349 C  C    . GLU   B 56  ? 1.1382 1.3218 0.386  -0.4353 -0.1303 0.3208  55  GLU   B C    
2350 O  O    . GLU   B 56  ? 1.1491 1.3267 0.3797 -0.4455 -0.124  0.3487  55  GLU   B O    
2351 C  CB   . GLU   B 56  ? 1.1287 1.2835 0.4481 -0.4367 -0.1439 0.3027  55  GLU   B CB   
2352 C  CG   . GLU   B 56  ? 1.1737 1.3331 0.5364 -0.4494 -0.1394 0.2964  55  GLU   B CG   
2353 C  CD   . GLU   B 56  ? 1.2561 1.4165 0.6278 -0.4729 -0.1241 0.3193  55  GLU   B CD   
2354 O  OE1  . GLU   B 56  ? 1.2927 1.4329 0.6379 -0.4778 -0.1212 0.3462  55  GLU   B OE1  
2355 O  OE2  . GLU   B 56  ? 1.2644 1.447  0.6711 -0.4863 -0.1144 0.3111  55  GLU   B OE2  
2356 N  N    . PHE   B 57  ? 1.156  1.3428 0.3845 -0.4201 -0.1402 0.304   56  PHE   B N    
2357 C  CA   . PHE   B 57  ? 1.1854 1.375  0.3716 -0.4155 -0.1465 0.3153  56  PHE   B CA   
2358 C  C    . PHE   B 57  ? 1.1934 1.4161 0.3482 -0.4232 -0.1279 0.3193  56  PHE   B C    
2359 O  O    . PHE   B 57  ? 1.2055 1.4314 0.326  -0.4258 -0.1283 0.3421  56  PHE   B O    
2360 C  CB   . PHE   B 57  ? 1.1925 1.3788 0.3718 -0.4    -0.1616 0.2932  56  PHE   B CB   
2361 C  CG   . PHE   B 57  ? 1.2089 1.3621 0.4036 -0.3912 -0.1818 0.2999  56  PHE   B CG   
2362 C  CD1  . PHE   B 57  ? 1.2298 1.3648 0.4119 -0.3917 -0.1911 0.3293  56  PHE   B CD1  
2363 C  CD2  . PHE   B 57  ? 1.2152 1.3549 0.4348 -0.3804 -0.1901 0.2779  56  PHE   B CD2  
2364 C  CE1  . PHE   B 57  ? 1.2441 1.348  0.4411 -0.3819 -0.2081 0.335   56  PHE   B CE1  
2365 C  CE2  . PHE   B 57  ? 1.2307 1.3405 0.4631 -0.3715 -0.207  0.2834  56  PHE   B CE2  
2366 C  CZ   . PHE   B 57  ? 1.2371 1.3294 0.4591 -0.3723 -0.2159 0.3111  56  PHE   B CZ   
2367 N  N    . ALA   B 58  ? 1.1847 1.4324 0.3504 -0.4256 -0.1105 0.2989  57  ALA   B N    
2368 C  CA   . ALA   B 58  ? 1.1918 1.4718 0.3301 -0.433  -0.0891 0.3009  57  ALA   B CA   
2369 C  C    . ALA   B 58  ? 1.1999 1.481  0.3355 -0.4486 -0.076  0.3339  57  ALA   B C    
2370 O  O    . ALA   B 58  ? 1.2113 1.5115 0.3103 -0.4538 -0.0629 0.3472  57  ALA   B O    
2371 C  CB   . ALA   B 58  ? 1.1797 1.4833 0.3382 -0.4304 -0.0721 0.2736  57  ALA   B CB   
2372 N  N    . LYS   B 59  ? 1.197  1.4568 0.3705 -0.4567 -0.0785 0.3463  58  LYS   B N    
2373 C  CA   . LYS   B 59  ? 1.2069 1.4597 0.3845 -0.4735 -0.0654 0.3779  58  LYS   B CA   
2374 C  C    . LYS   B 59  ? 1.2372 1.4666 0.3767 -0.4706 -0.0751 0.4095  58  LYS   B C    
2375 O  O    . LYS   B 59  ? 1.2463 1.4808 0.3614 -0.4797 -0.0596 0.4375  58  LYS   B O    
2376 C  CB   . LYS   B 59  ? 1.2155 1.4492 0.4467 -0.4836 -0.0676 0.3772  58  LYS   B CB   
2377 C  CG   . LYS   B 59  ? 1.2349 1.5007 0.5047 -0.4886 -0.0547 0.3531  58  LYS   B CG   
2378 C  CD   . LYS   B 59  ? 1.2616 1.5162 0.5838 -0.5022 -0.0562 0.3528  58  LYS   B CD   
2379 C  CE   . LYS   B 59  ? 1.2686 1.5659 0.6278 -0.5096 -0.04   0.3352  58  LYS   B CE   
2380 N  NZ   . LYS   B 59  ? 1.2708 1.5642 0.6831 -0.5222 -0.0452 0.3285  58  LYS   B NZ   
2381 N  N    . GLN   B 60  ? 1.2478 1.4541 0.3814 -0.4561 -0.0998 0.4057  59  GLN   B N    
2382 C  CA   . GLN   B 60  ? 1.2718 1.4582 0.3733 -0.448  -0.1134 0.4333  59  GLN   B CA   
2383 C  C    . GLN   B 60  ? 1.2828 1.4987 0.3299 -0.4396 -0.1155 0.4357  59  GLN   B C    
2384 O  O    . GLN   B 60  ? 1.2981 1.5052 0.317  -0.4301 -0.1291 0.4576  59  GLN   B O    
2385 C  CB   . GLN   B 60  ? 1.2963 1.4521 0.4175 -0.4348 -0.1384 0.4249  59  GLN   B CB   
2386 C  CG   . GLN   B 60  ? 1.3349 1.4586 0.5049 -0.442  -0.1393 0.4225  59  GLN   B CG   
2387 C  CD   . GLN   B 60  ? 1.4103 1.5005 0.5837 -0.4515 -0.1326 0.4585  59  GLN   B CD   
2388 O  OE1  . GLN   B 60  ? 1.4565 1.5378 0.5962 -0.4458 -0.1342 0.4888  59  GLN   B OE1  
2389 N  NE2  . GLN   B 60  ? 1.4052 1.4763 0.6199 -0.466  -0.1248 0.4561  59  GLN   B NE2  
2390 N  N    . LYS   B 61  ? 1.2746 1.5265 0.3077 -0.4421 -0.1024 0.4122  60  LYS   B N    
2391 C  CA   . LYS   B 61  ? 1.2876 1.5718 0.2695 -0.4367 -0.1022 0.4066  60  LYS   B CA   
2392 C  C    . LYS   B 61  ? 1.2917 1.5764 0.2602 -0.4221 -0.1286 0.39    60  LYS   B C    
2393 O  O    . LYS   B 61  ? 1.3097 1.606  0.2381 -0.4154 -0.1399 0.4055  60  LYS   B O    
2394 C  CB   . LYS   B 61  ? 1.3238 1.6166 0.2628 -0.4412 -0.0906 0.4449  60  LYS   B CB   
2395 C  CG   . LYS   B 61  ? 1.3692 1.664  0.3224 -0.4576 -0.0613 0.4614  60  LYS   B CG   
2396 C  CD   . LYS   B 61  ? 1.4414 1.7424 0.3479 -0.4605 -0.0482 0.5016  60  LYS   B CD   
2397 C  CE   . LYS   B 61  ? 1.483  1.7893 0.4008 -0.4781 -0.0158 0.5194  60  LYS   B CE   
2398 N  NZ   . LYS   B 61  ? 1.5207 1.8362 0.3843 -0.4785 -0.0013 0.5581  60  LYS   B NZ   
2399 N  N    . SER   B 62  ? 1.2693 1.5447 0.2714 -0.4168 -0.1377 0.3587  61  SER   B N    
2400 C  CA   . SER   B 62  ? 1.2662 1.5418 0.2635 -0.4049 -0.1602 0.3402  61  SER   B CA   
2401 C  C    . SER   B 62  ? 1.2528 1.5566 0.2342 -0.4046 -0.1546 0.3022  61  SER   B C    
2402 O  O    . SER   B 62  ? 1.2536 1.5697 0.2381 -0.4107 -0.1334 0.2867  61  SER   B O    
2403 C  CB   . SER   B 62  ? 1.2777 1.5203 0.3213 -0.3986 -0.1728 0.332   61  SER   B CB   
2404 O  OG   . SER   B 62  ? 1.3147 1.5275 0.3755 -0.4003 -0.1755 0.3629  61  SER   B OG   
2405 N  N    . ARG   B 63  ? 1.2366 1.5514 0.2015 -0.3977 -0.1724 0.287   62  ARG   B N    
2406 C  CA   . ARG   B 63  ? 1.2177 1.5529 0.1719 -0.3986 -0.1675 0.2473  62  ARG   B CA   
2407 C  C    . ARG   B 63  ? 1.1853 1.4937 0.1861 -0.3927 -0.1705 0.2248  62  ARG   B C    
2408 O  O    . ARG   B 63  ? 1.1852 1.4767 0.2044 -0.3854 -0.1897 0.2301  62  ARG   B O    
2409 C  CB   . ARG   B 63  ? 1.2405 1.602  0.1592 -0.396  -0.1863 0.2407  62  ARG   B CB   
2410 C  CG   . ARG   B 63  ? 1.291  1.6882 0.1549 -0.4015 -0.1795 0.2491  62  ARG   B CG   
2411 C  CD   . ARG   B 63  ? 1.3339 1.7528 0.1648 -0.3952 -0.2037 0.2699  62  ARG   B CD   
2412 N  NE   . ARG   B 63  ? 1.365  1.7989 0.2003 -0.3921 -0.2244 0.2414  62  ARG   B NE   
2413 C  CZ   . ARG   B 63  ? 1.392  1.8464 0.2122 -0.3844 -0.2501 0.2546  62  ARG   B CZ   
2414 N  NH1  . ARG   B 63  ? 1.3999 1.8592 0.1959 -0.3767 -0.2579 0.2977  62  ARG   B NH1  
2415 N  NH2  . ARG   B 63  ? 1.3757 1.8475 0.2054 -0.384  -0.2671 0.2251  62  ARG   B NH2  
2416 N  N    . LEU   B 64  ? 1.1571 1.4612 0.1777 -0.3941 -0.1509 0.2034  63  LEU   B N    
2417 C  CA   . LEU   B 64  ? 1.1374 1.4158 0.2004 -0.3863 -0.1519 0.1869  63  LEU   B CA   
2418 C  C    . LEU   B 64  ? 1.1178 1.3962 0.1842 -0.3822 -0.1471 0.1492  63  LEU   B C    
2419 O  O    . LEU   B 64  ? 1.1255 1.4227 0.1683 -0.3869 -0.133  0.1288  63  LEU   B O    
2420 C  CB   . LEU   B 64  ? 1.131  1.402  0.2217 -0.3875 -0.1352 0.1927  63  LEU   B CB   
2421 C  CG   . LEU   B 64  ? 1.1436 1.3996 0.2514 -0.3909 -0.1421 0.2252  63  LEU   B CG   
2422 C  CD1  . LEU   B 64  ? 1.1386 1.4034 0.2634 -0.3981 -0.1222 0.2317  63  LEU   B CD1  
2423 C  CD2  . LEU   B 64  ? 1.1496 1.3756 0.289  -0.382  -0.1594 0.2259  63  LEU   B CD2  
2424 N  N    . VAL   B 65  ? 1.0923 1.3467 0.1885 -0.3735 -0.1572 0.14    64  VAL   B N    
2425 C  CA   . VAL   B 65  ? 1.0744 1.3201 0.1811 -0.3688 -0.1521 0.1074  64  VAL   B CA   
2426 C  C    . VAL   B 65  ? 1.0461 1.2642 0.1911 -0.3573 -0.1464 0.1049  64  VAL   B C    
2427 O  O    . VAL   B 65  ? 1.0433 1.2442 0.2081 -0.3518 -0.1614 0.1211  64  VAL   B O    
2428 C  CB   . VAL   B 65  ? 1.0868 1.3337 0.1907 -0.3686 -0.1732 0.103   64  VAL   B CB   
2429 C  CG1  . VAL   B 65  ? 1.0952 1.331  0.2127 -0.3663 -0.166  0.0694  64  VAL   B CG1  
2430 C  CG2  . VAL   B 65  ? 1.0952 1.3744 0.1606 -0.3776 -0.1842 0.1102  64  VAL   B CG2  
2431 N  N    . LEU   B 66  ? 1.0247 1.2388 0.1788 -0.3523 -0.125  0.0855  65  LEU   B N    
2432 C  CA   . LEU   B 66  ? 1.0091 1.2012 0.1968 -0.3388 -0.1202 0.0842  65  LEU   B CA   
2433 C  C    . LEU   B 66  ? 0.996  1.1679 0.1951 -0.3289 -0.1113 0.059   65  LEU   B C    
2434 O  O    . LEU   B 66  ? 0.9916 1.167  0.1769 -0.3317 -0.0955 0.0362  65  LEU   B O    
2435 C  CB   . LEU   B 66  ? 1.0062 1.2096 0.204  -0.3363 -0.1036 0.0893  65  LEU   B CB   
2436 C  CG   . LEU   B 66  ? 1.0242 1.2465 0.2153 -0.3476 -0.1072 0.1143  65  LEU   B CG   
2437 C  CD1  . LEU   B 66  ? 1.0204 1.2576 0.2292 -0.345  -0.0894 0.1156  65  LEU   B CD1  
2438 C  CD2  . LEU   B 66  ? 1.0357 1.2436 0.2388 -0.3495 -0.1295 0.1377  65  LEU   B CD2  
2439 N  N    . TRP   B 67  ? 0.9897 1.138  0.2139 -0.3171 -0.1195 0.0632  66  TRP   B N    
2440 C  CA   . TRP   B 67  ? 0.9845 1.1088 0.2222 -0.3058 -0.1102 0.0441  66  TRP   B CA   
2441 C  C    . TRP   B 67  ? 0.9754 1.0845 0.2364 -0.2876 -0.1016 0.0477  66  TRP   B C    
2442 O  O    . TRP   B 67  ? 0.9714 1.0816 0.245  -0.2841 -0.1143 0.0658  66  TRP   B O    
2443 C  CB   . TRP   B 67  ? 0.9815 1.0934 0.2251 -0.3072 -0.1283 0.0453  66  TRP   B CB   
2444 C  CG   . TRP   B 67  ? 0.9889 1.1165 0.2136 -0.3218 -0.1339 0.0329  66  TRP   B CG   
2445 C  CD1  . TRP   B 67  ? 1.0043 1.158  0.2016 -0.3353 -0.1308 0.0269  66  TRP   B CD1  
2446 C  CD2  . TRP   B 67  ? 0.9871 1.1099 0.2191 -0.3245 -0.1452 0.0249  66  TRP   B CD2  
2447 N  NE1  . TRP   B 67  ? 1.0063 1.173  0.1924 -0.3462 -0.1405 0.0139  66  TRP   B NE1  
2448 C  CE2  . TRP   B 67  ? 1.0004 1.1496 0.2099 -0.3403 -0.1495 0.0123  66  TRP   B CE2  
2449 C  CE3  . TRP   B 67  ? 0.9893 1.0905 0.2449 -0.315  -0.1514 0.0265  66  TRP   B CE3  
2450 C  CZ2  . TRP   B 67  ? 1.0023 1.1599 0.216  -0.3475 -0.161  0.0004  66  TRP   B CZ2  
2451 C  CZ3  . TRP   B 67  ? 0.9968 1.1041 0.2574 -0.3219 -0.1606 0.016   66  TRP   B CZ3  
2452 C  CH2  . TRP   B 67  ? 0.9968 1.1335 0.2384 -0.3384 -0.1659 0.0025  66  TRP   B CH2  
2453 N  N    . ASP   B 68  ? 0.9711 1.0662 0.2374 -0.2756 -0.0799 0.0303  67  ASP   B N    
2454 C  CA   . ASP   B 68  ? 0.9656 1.0492 0.2516 -0.2544 -0.0708 0.0338  67  ASP   B CA   
2455 C  C    . ASP   B 68  ? 0.9706 1.0315 0.2588 -0.2404 -0.045  0.0147  67  ASP   B C    
2456 O  O    . ASP   B 68  ? 0.9808 1.038  0.2554 -0.2497 -0.0312 -0.0036 67  ASP   B O    
2457 C  CB   . ASP   B 68  ? 0.9697 1.0803 0.2603 -0.2531 -0.0671 0.0442  67  ASP   B CB   
2458 C  CG   . ASP   B 68  ? 1.0126 1.1228 0.326  -0.2354 -0.0714 0.0547  67  ASP   B CG   
2459 O  OD1  . ASP   B 68  ? 1.0134 1.1326 0.3354 -0.2413 -0.0905 0.0698  67  ASP   B OD1  
2460 O  OD2  . ASP   B 68  ? 1.0408 1.1417 0.3627 -0.2152 -0.0554 0.0475  67  ASP   B OD2  
2461 N  N    . ILE   B 69  ? 0.9632 1.0082 0.2673 -0.2177 -0.0378 0.0188  68  ILE   B N    
2462 C  CA   . ILE   B 69  ? 0.9673 0.9873 0.2737 -0.2007 -0.0104 0.005   68  ILE   B CA   
2463 C  C    . ILE   B 69  ? 0.9608 0.9973 0.2675 -0.1895 0.01    0.0023  68  ILE   B C    
2464 O  O    . ILE   B 69  ? 0.9646 0.983  0.2673 -0.1808 0.0366  -0.0125 68  ILE   B O    
2465 C  CB   . ILE   B 69  ? 0.9737 0.9668 0.2936 -0.1787 -0.0105 0.0124  68  ILE   B CB   
2466 C  CG1  . ILE   B 69  ? 0.974  0.9855 0.3057 -0.1655 -0.0276 0.0313  68  ILE   B CG1  
2467 C  CG2  . ILE   B 69  ? 0.9838 0.9558 0.3039 -0.1888 -0.0207 0.0091  68  ILE   B CG2  
2468 C  CD1  . ILE   B 69  ? 0.9865 0.9986 0.3272 -0.136  -0.011  0.0351  68  ILE   B CD1  
2469 N  N    . ASN   B 70  ? 0.949  1.0191 0.2624 -0.1899 -0.0013 0.0163  69  ASN   B N    
2470 C  CA   . ASN   B 70  ? 0.9456 1.0411 0.2646 -0.1798 0.0146  0.0168  69  ASN   B CA   
2471 C  C    . ASN   B 70  ? 0.9485 1.0614 0.2495 -0.2007 0.0225  0.0071  69  ASN   B C    
2472 O  O    . ASN   B 70  ? 0.9379 1.0766 0.2346 -0.219  0.0062  0.0172  69  ASN   B O    
2473 C  CB   . ASN   B 70  ? 0.9459 1.0734 0.2834 -0.1759 -0.0036 0.0351  69  ASN   B CB   
2474 C  CG   . ASN   B 70  ? 0.9697 1.1259 0.3219 -0.1586 0.012   0.037   69  ASN   B CG   
2475 O  OD1  . ASN   B 70  ? 0.9827 1.1513 0.3283 -0.1611 0.032   0.0283  69  ASN   B OD1  
2476 N  ND2  . ASN   B 70  ? 0.9599 1.1298 0.3324 -0.1398 0.0032  0.0474  69  ASN   B ND2  
2477 N  N    . LYS   B 71  ? 0.9625 1.0602 0.2515 -0.1981 0.0486  -0.0124 70  LYS   B N    
2478 C  CA   . LYS   B 71  ? 0.9765 1.091  0.2436 -0.2175 0.0579  -0.0249 70  LYS   B CA   
2479 C  C    . LYS   B 71  ? 0.9706 1.127  0.2419 -0.2191 0.06    -0.0136 70  LYS   B C    
2480 O  O    . LYS   B 71  ? 0.9706 1.1499 0.2258 -0.2403 0.0513  -0.0101 70  LYS   B O    
2481 C  CB   . LYS   B 71  ? 1.0088 1.0966 0.2638 -0.2127 0.0885  -0.0509 70  LYS   B CB   
2482 C  CG   . LYS   B 71  ? 1.0452 1.1504 0.2736 -0.2322 0.0996  -0.0678 70  LYS   B CG   
2483 C  CD   . LYS   B 71  ? 1.0977 1.1699 0.3132 -0.2322 0.1268  -0.098  70  LYS   B CD   
2484 C  CE   . LYS   B 71  ? 1.1364 1.2253 0.3288 -0.2407 0.148   -0.1163 70  LYS   B CE   
2485 N  NZ   . LYS   B 71  ? 1.1427 1.2493 0.3473 -0.2195 0.1689  -0.1083 70  LYS   B NZ   
2486 N  N    . HIS   B 72  ? 0.9604 1.129  0.254  -0.1962 0.0714  -0.0067 71  HIS   B N    
2487 C  CA   . HIS   B 72  ? 0.9493 1.1613 0.2548 -0.1954 0.0762  0.0032  71  HIS   B CA   
2488 C  C    . HIS   B 72  ? 0.9451 1.185  0.2602 -0.2126 0.0486  0.0237  71  HIS   B C    
2489 O  O    . HIS   B 72  ? 0.9392 1.2087 0.2481 -0.2293 0.0497  0.0293  71  HIS   B O    
2490 C  CB   . HIS   B 72  ? 0.9469 1.1664 0.278  -0.1634 0.0927  0.0055  71  HIS   B CB   
2491 C  CG   . HIS   B 72  ? 0.9495 1.2192 0.3013 -0.16   0.0967  0.0158  71  HIS   B CG   
2492 N  ND1  . HIS   B 72  ? 0.9648 1.2549 0.3108 -0.1596 0.1225  0.0069  71  HIS   B ND1  
2493 C  CD2  . HIS   B 72  ? 0.9426 1.2464 0.3227 -0.1571 0.0792  0.0324  71  HIS   B CD2  
2494 C  CE1  . HIS   B 72  ? 0.9444 1.282  0.3169 -0.1569 0.12    0.0198  71  HIS   B CE1  
2495 N  NE2  . HIS   B 72  ? 0.9345 1.2827 0.329  -0.1564 0.0937  0.0346  71  HIS   B NE2  
2496 N  N    . GLY   B 73  ? 0.9474 1.1751 0.2766 -0.2083 0.0262  0.0345  72  GLY   B N    
2497 C  CA   . GLY   B 73  ? 0.9465 1.1921 0.2875 -0.2228 0.0005  0.0524  72  GLY   B CA   
2498 C  C    . GLY   B 73  ? 0.9599 1.2033 0.2779 -0.2502 -0.0121 0.0576  72  GLY   B C    
2499 O  O    . GLY   B 73  ? 0.9499 1.2195 0.2703 -0.2663 -0.0174 0.0703  72  GLY   B O    
2500 N  N    . VAL   B 74  ? 0.9803 1.1941 0.2765 -0.2554 -0.0158 0.0483  73  VAL   B N    
2501 C  CA   . VAL   B 74  ? 0.9978 1.2114 0.2697 -0.2783 -0.029  0.053   73  VAL   B CA   
2502 C  C    . VAL   B 74  ? 1.0092 1.2466 0.2574 -0.2913 -0.0127 0.0478  73  VAL   B C    
2503 O  O    . VAL   B 74  ? 1.012  1.2636 0.2439 -0.3092 -0.0227 0.0603  73  VAL   B O    
2504 C  CB   . VAL   B 74  ? 1.019  1.2012 0.2784 -0.2797 -0.0387 0.0432  73  VAL   B CB   
2505 C  CG1  . VAL   B 74  ? 1.035  1.2063 0.2756 -0.279  -0.0177 0.0183  73  VAL   B CG1  
2506 C  CG2  . VAL   B 74  ? 1.0268 1.2115 0.2718 -0.2982 -0.0617 0.0566  73  VAL   B CG2  
2507 N  N    . GLU   B 75  ? 1.012  1.2533 0.2573 -0.2807 0.0136  0.0306  74  GLU   B N    
2508 C  CA   . GLU   B 75  ? 1.0195 1.2839 0.2419 -0.2906 0.0322  0.0234  74  GLU   B CA   
2509 C  C    . GLU   B 75  ? 1.0134 1.3143 0.2503 -0.2954 0.0352  0.0421  74  GLU   B C    
2510 O  O    . GLU   B 75  ? 1.0178 1.3396 0.2331 -0.3116 0.039   0.0483  74  GLU   B O    
2511 C  CB   . GLU   B 75  ? 1.0481 1.3019 0.2653 -0.2762 0.0616  -0.0017 74  GLU   B CB   
2512 C  CG   . GLU   B 75  ? 1.1104 1.3367 0.3007 -0.2834 0.0645  -0.0249 74  GLU   B CG   
2513 C  CD   . GLU   B 75  ? 1.1719 1.3804 0.3562 -0.2712 0.0958  -0.0521 74  GLU   B CD   
2514 O  OE1  . GLU   B 75  ? 1.1879 1.4033 0.3908 -0.2521 0.1161  -0.0513 74  GLU   B OE1  
2515 O  OE2  . GLU   B 75  ? 1.1849 1.3729 0.3474 -0.2805 0.1005  -0.075  74  GLU   B OE2  
2516 N  N    . GLU   B 76  ? 1.0058 1.3165 0.2791 -0.282  0.0334  0.051   75  GLU   B N    
2517 C  CA   . GLU   B 76  ? 1.0031 1.3514 0.2981 -0.2882 0.0355  0.0673  75  GLU   B CA   
2518 C  C    . GLU   B 76  ? 1.0105 1.3612 0.3051 -0.3095 0.0123  0.0892  75  GLU   B C    
2519 O  O    . GLU   B 76  ? 0.9963 1.3747 0.2939 -0.324  0.0175  0.1029  75  GLU   B O    
2520 C  CB   . GLU   B 76  ? 1.0254 1.3886 0.3608 -0.267  0.0392  0.0676  75  GLU   B CB   
2521 C  CG   . GLU   B 76  ? 1.0959 1.4716 0.4351 -0.2473 0.0688  0.0526  75  GLU   B CG   
2522 C  CD   . GLU   B 76  ? 1.1673 1.5779 0.5483 -0.2295 0.0741  0.058   75  GLU   B CD   
2523 O  OE1  . GLU   B 76  ? 1.1759 1.5861 0.5815 -0.2221 0.0543  0.0657  75  GLU   B OE1  
2524 O  OE2  . GLU   B 76  ? 1.1819 1.623  0.571  -0.2223 0.0982  0.0537  75  GLU   B OE2  
2525 N  N    . THR   B 77  ? 1.0319 1.3522 0.3225 -0.3113 -0.0109 0.0932  76  THR   B N    
2526 C  CA   . THR   B 77  ? 1.0517 1.3675 0.3394 -0.3294 -0.0317 0.114   76  THR   B CA   
2527 C  C    . THR   B 77  ? 1.0843 1.4052 0.3331 -0.3457 -0.0275 0.119   76  THR   B C    
2528 O  O    . THR   B 77  ? 1.0877 1.4247 0.333  -0.3613 -0.0274 0.1381  76  THR   B O    
2529 C  CB   . THR   B 77  ? 1.0749 1.3572 0.3671 -0.3244 -0.0553 0.1155  76  THR   B CB   
2530 O  OG1  . THR   B 77  ? 1.0825 1.3622 0.4065 -0.3076 -0.0582 0.1105  76  THR   B OG1  
2531 C  CG2  . THR   B 77  ? 1.0787 1.3525 0.3677 -0.341  -0.075  0.1374  76  THR   B CG2  
2532 N  N    . ALA   B 78  ? 1.1041 1.4133 0.3233 -0.3423 -0.0221 0.1011  77  ALA   B N    
2533 C  CA   . ALA   B 78  ? 1.1236 1.4417 0.3012 -0.3555 -0.0184 0.1008  77  ALA   B CA   
2534 C  C    . ALA   B 78  ? 1.1255 1.4762 0.2942 -0.362  0.0049  0.1044  77  ALA   B C    
2535 O  O    . ALA   B 78  ? 1.1334 1.4977 0.2745 -0.3762 0.0049  0.1187  77  ALA   B O    
2536 C  CB   . ALA   B 78  ? 1.1377 1.4408 0.293  -0.3499 -0.0135 0.0737  77  ALA   B CB   
2537 N  N    . ALA   B 79  ? 1.1176 1.4821 0.3093 -0.3502 0.0257  0.0928  78  ALA   B N    
2538 C  CA   . ALA   B 79  ? 1.1197 1.5182 0.3089 -0.3545 0.0502  0.0957  78  ALA   B CA   
2539 C  C    . ALA   B 79  ? 1.1207 1.5386 0.3269 -0.3696 0.0447  0.1246  78  ALA   B C    
2540 O  O    . ALA   B 79  ? 1.1271 1.5647 0.3099 -0.3828 0.0562  0.1361  78  ALA   B O    
2541 C  CB   . ALA   B 79  ? 1.1087 1.5182 0.3262 -0.3354 0.0714  0.0793  78  ALA   B CB   
2542 N  N    . GLU   B 80  ? 1.1158 1.5268 0.3606 -0.3687 0.0279  0.1361  79  GLU   B N    
2543 C  CA   . GLU   B 80  ? 1.1165 1.5416 0.3804 -0.3858 0.0235  0.1617  79  GLU   B CA   
2544 C  C    . GLU   B 80  ? 1.1403 1.5445 0.3743 -0.4013 0.0069  0.1828  79  GLU   B C    
2545 O  O    . GLU   B 80  ? 1.1376 1.5526 0.3705 -0.4176 0.0115  0.2055  79  GLU   B O    
2546 C  CB   . GLU   B 80  ? 1.1308 1.5596 0.4464 -0.3811 0.0127  0.1637  79  GLU   B CB   
2547 C  CG   . GLU   B 80  ? 1.1946 1.6466 0.5391 -0.4002 0.0157  0.184   79  GLU   B CG   
2548 C  CD   . GLU   B 80  ? 1.2981 1.785  0.635  -0.4128 0.0425  0.1931  79  GLU   B CD   
2549 O  OE1  . GLU   B 80  ? 1.3202 1.8015 0.6338 -0.4309 0.0443  0.2142  79  GLU   B OE1  
2550 O  OE2  . GLU   B 80  ? 1.3259 1.846  0.6801 -0.4032 0.0628  0.1806  79  GLU   B OE2  
2551 N  N    . CYS   B 81  ? 1.1629 1.5387 0.3724 -0.3955 -0.0104 0.1759  80  CYS   B N    
2552 C  CA   . CYS   B 81  ? 1.1907 1.5502 0.3694 -0.4058 -0.0265 0.195   80  CYS   B CA   
2553 C  C    . CYS   B 81  ? 1.2076 1.5869 0.3394 -0.4136 -0.012  0.1987  80  CYS   B C    
2554 O  O    . CYS   B 81  ? 1.2184 1.5975 0.3278 -0.4247 -0.0164 0.2239  80  CYS   B O    
2555 C  CB   . CYS   B 81  ? 1.2143 1.5438 0.3864 -0.3962 -0.0492 0.1849  80  CYS   B CB   
2556 S  SG   . CYS   B 81  ? 1.2637 1.5678 0.4836 -0.3868 -0.0674 0.1836  80  CYS   B SG   
2557 N  N    . ARG   B 82  ? 1.2078 1.603  0.3233 -0.4067 0.0064  0.174   81  ARG   B N    
2558 C  CA   . ARG   B 82  ? 1.222  1.6393 0.2921 -0.4128 0.0233  0.1719  81  ARG   B CA   
2559 C  C    . ARG   B 82  ? 1.2211 1.6652 0.299  -0.4234 0.0446  0.1927  81  ARG   B C    
2560 O  O    . ARG   B 82  ? 1.2341 1.6896 0.2763 -0.4341 0.05    0.2122  81  ARG   B O    
2561 C  CB   . ARG   B 82  ? 1.2359 1.6586 0.2934 -0.4021 0.0399  0.1364  81  ARG   B CB   
2562 C  CG   . ARG   B 82  ? 1.2866 1.6885 0.3209 -0.3977 0.0233  0.1159  81  ARG   B CG   
2563 C  CD   . ARG   B 82  ? 1.3327 1.7311 0.3651 -0.3871 0.0415  0.0794  81  ARG   B CD   
2564 N  NE   . ARG   B 82  ? 1.3861 1.7614 0.4074 -0.3843 0.0258  0.0585  81  ARG   B NE   
2565 C  CZ   . ARG   B 82  ? 1.4153 1.7669 0.4606 -0.3722 0.0288  0.0361  81  ARG   B CZ   
2566 N  NH1  . ARG   B 82  ? 1.3979 1.7471 0.4772 -0.359  0.0459  0.0319  81  ARG   B NH1  
2567 N  NH2  . ARG   B 82  ? 1.4264 1.7584 0.4627 -0.3726 0.0155  0.0183  81  ARG   B NH2  
2568 N  N    . LYS   B 83  ? 1.2018 1.6578 0.3275 -0.4205 0.0563  0.1902  82  LYS   B N    
2569 C  CA   . LYS   B 83  ? 1.1951 1.6797 0.3388 -0.4322 0.0769  0.209   82  LYS   B CA   
2570 C  C    . LYS   B 83  ? 1.1997 1.6737 0.3479 -0.4495 0.066   0.2441  82  LYS   B C    
2571 O  O    . LYS   B 83  ? 1.1894 1.6842 0.3509 -0.4628 0.0839  0.2627  82  LYS   B O    
2572 C  CB   . LYS   B 83  ? 1.1986 1.7035 0.3969 -0.4242 0.0889  0.1964  82  LYS   B CB   
2573 C  CG   . LYS   B 83  ? 1.256  1.7733 0.4484 -0.4063 0.1076  0.1661  82  LYS   B CG   
2574 C  CD   . LYS   B 83  ? 1.2954 1.847  0.5357 -0.3984 0.1278  0.1596  82  LYS   B CD   
2575 C  CE   . LYS   B 83  ? 1.3435 1.9325 0.5714 -0.4047 0.1602  0.1631  82  LYS   B CE   
2576 N  NZ   . LYS   B 83  ? 1.3489 1.9715 0.6176 -0.3897 0.1821  0.1488  82  LYS   B NZ   
2577 N  N    . LEU   B 84  ? 1.2136 1.6544 0.351  -0.4492 0.039   0.2534  83  LEU   B N    
2578 C  CA   . LEU   B 84  ? 1.225  1.647  0.3609 -0.4624 0.0279  0.2865  83  LEU   B CA   
2579 C  C    . LEU   B 84  ? 1.2522 1.6691 0.328  -0.4646 0.0239  0.3045  83  LEU   B C    
2580 O  O    . LEU   B 84  ? 1.2628 1.6676 0.3295 -0.4747 0.0218  0.3368  83  LEU   B O    
2581 C  CB   . LEU   B 84  ? 1.2258 1.6141 0.3938 -0.4583 0.0008  0.2865  83  LEU   B CB   
2582 C  CG   . LEU   B 84  ? 1.2167 1.6098 0.4433 -0.4583 0.001   0.2756  83  LEU   B CG   
2583 C  CD1  . LEU   B 84  ? 1.227  1.5852 0.475  -0.4539 -0.0258 0.2759  83  LEU   B CD1  
2584 C  CD2  . LEU   B 84  ? 1.2079 1.6214 0.463  -0.4769 0.0194  0.2941  83  LEU   B CD2  
2585 N  N    . GLY   B 85  ? 1.2612 1.6873 0.2971 -0.455  0.023   0.2836  84  GLY   B N    
2586 C  CA   . GLY   B 85  ? 1.2868 1.7167 0.2637 -0.4556 0.0175  0.2959  84  GLY   B CA   
2587 C  C    . GLY   B 85  ? 1.3015 1.7132 0.2602 -0.4458 -0.0113 0.2849  84  GLY   B C    
2588 O  O    . GLY   B 85  ? 1.3216 1.7431 0.2309 -0.4444 -0.0185 0.2894  84  GLY   B O    
2589 N  N    . ALA   B 86  ? 1.2897 1.678  0.2874 -0.4387 -0.0282 0.2707  85  ALA   B N    
2590 C  CA   . ALA   B 86  ? 1.3013 1.6728 0.2888 -0.4298 -0.0545 0.2599  85  ALA   B CA   
2591 C  C    . ALA   B 86  ? 1.3026 1.6874 0.2673 -0.4236 -0.0521 0.2226  85  ALA   B C    
2592 O  O    . ALA   B 86  ? 1.306  1.7045 0.275  -0.4228 -0.0303 0.2007  85  ALA   B O    
2593 C  CB   . ALA   B 86  ? 1.2981 1.6396 0.3343 -0.4241 -0.0703 0.2571  85  ALA   B CB   
2594 N  N    . THR   B 87  ? 1.2932 1.6739 0.2368 -0.4192 -0.0737 0.214   86  THR   B N    
2595 C  CA   . THR   B 87  ? 1.277  1.6669 0.2037 -0.4161 -0.0721 0.1757  86  THR   B CA   
2596 C  C    . THR   B 87  ? 1.2503 1.6133 0.2167 -0.4077 -0.084  0.1557  86  THR   B C    
2597 O  O    . THR   B 87  ? 1.2512 1.6007 0.2251 -0.4043 -0.1076 0.1629  86  THR   B O    
2598 C  CB   . THR   B 87  ? 1.2925 1.7062 0.1662 -0.4195 -0.0832 0.175   86  THR   B CB   
2599 O  OG1  . THR   B 87  ? 1.3035 1.7416 0.1417 -0.4257 -0.0642 0.1897  86  THR   B OG1  
2600 C  CG2  . THR   B 87  ? 1.2981 1.7193 0.1582 -0.4191 -0.0839 0.1321  86  THR   B CG2  
2601 N  N    . VAL   B 88  ? 1.2241 1.5796 0.2171 -0.4028 -0.0662 0.1334  87  VAL   B N    
2602 C  CA   . VAL   B 88  ? 1.2132 1.5421 0.2433 -0.393  -0.0734 0.1172  87  VAL   B CA   
2603 C  C    . VAL   B 88  ? 1.1979 1.5235 0.22   -0.3897 -0.0647 0.079   87  VAL   B C    
2604 O  O    . VAL   B 88  ? 1.198  1.5356 0.2055 -0.3906 -0.0418 0.0599  87  VAL   B O    
2605 C  CB   . VAL   B 88  ? 1.2184 1.5365 0.2917 -0.3868 -0.0636 0.1251  87  VAL   B CB   
2606 C  CG1  . VAL   B 88  ? 1.2235 1.5137 0.3315 -0.3748 -0.0731 0.1126  87  VAL   B CG1  
2607 C  CG2  . VAL   B 88  ? 1.2233 1.5438 0.3057 -0.394  -0.0702 0.1605  87  VAL   B CG2  
2608 N  N    . HIS   B 89  ? 1.1818 1.4898 0.2147 -0.3864 -0.0816 0.0678  88  HIS   B N    
2609 C  CA   . HIS   B 89  ? 1.1712 1.4696 0.2032 -0.3848 -0.0743 0.0316  88  HIS   B CA   
2610 C  C    . HIS   B 89  ? 1.1506 1.4167 0.2249 -0.3724 -0.0759 0.0273  88  HIS   B C    
2611 O  O    . HIS   B 89  ? 1.1463 1.4003 0.2396 -0.3689 -0.0959 0.0457  88  HIS   B O    
2612 C  CB   . HIS   B 89  ? 1.1818 1.4948 0.1862 -0.3944 -0.0927 0.0208  88  HIS   B CB   
2613 C  CG   . HIS   B 89  ? 1.2071 1.5544 0.165  -0.4046 -0.0921 0.0257  88  HIS   B CG   
2614 N  ND1  . HIS   B 89  ? 1.23   1.5938 0.1708 -0.4069 -0.1091 0.0605  88  HIS   B ND1  
2615 C  CD2  . HIS   B 89  ? 1.2236 1.5894 0.1481 -0.4116 -0.0745 0.0009  88  HIS   B CD2  
2616 C  CE1  . HIS   B 89  ? 1.2386 1.6324 0.1347 -0.4147 -0.1022 0.0572  88  HIS   B CE1  
2617 N  NE2  . HIS   B 89  ? 1.2391 1.6362 0.1233 -0.4182 -0.0819 0.0205  88  HIS   B NE2  
2618 N  N    . THR   B 90  ? 1.1355 1.3868 0.2235 -0.364  -0.0531 0.0049  89  THR   B N    
2619 C  CA   . THR   B 90  ? 1.1214 1.3428 0.246  -0.3494 -0.051  0.002   89  THR   B CA   
2620 C  C    . THR   B 90  ? 1.1199 1.319  0.2481 -0.3481 -0.0451 -0.0271 89  THR   B C    
2621 O  O    . THR   B 90  ? 1.129  1.3333 0.2355 -0.3563 -0.0316 -0.0531 89  THR   B O    
2622 C  CB   . THR   B 90  ? 1.1218 1.3419 0.2656 -0.3365 -0.0299 0.0047  89  THR   B CB   
2623 O  OG1  . THR   B 90  ? 1.1321 1.3527 0.2631 -0.3343 -0.0025 -0.0212 89  THR   B OG1  
2624 C  CG2  . THR   B 90  ? 1.1172 1.3611 0.2623 -0.3407 -0.0336 0.0314  89  THR   B CG2  
2625 N  N    . PHE   B 91  ? 1.104  1.2778 0.2598 -0.3385 -0.054  -0.0235 90  PHE   B N    
2626 C  CA   . PHE   B 91  ? 1.0989 1.2475 0.2645 -0.3367 -0.0465 -0.0479 90  PHE   B CA   
2627 C  C    . PHE   B 91  ? 1.0898 1.2082 0.2868 -0.3168 -0.0394 -0.0411 90  PHE   B C    
2628 O  O    . PHE   B 91  ? 1.0887 1.2054 0.3013 -0.3098 -0.0565 -0.0179 90  PHE   B O    
2629 C  CB   . PHE   B 91  ? 1.0973 1.2519 0.2605 -0.3484 -0.0707 -0.0488 90  PHE   B CB   
2630 C  CG   . PHE   B 91  ? 1.1069 1.2972 0.2379 -0.3657 -0.0847 -0.0493 90  PHE   B CG   
2631 C  CD1  . PHE   B 91  ? 1.1218 1.3245 0.2288 -0.3787 -0.0735 -0.0792 90  PHE   B CD1  
2632 C  CD2  . PHE   B 91  ? 1.1107 1.3212 0.2338 -0.368  -0.1083 -0.0197 90  PHE   B CD2  
2633 C  CE1  . PHE   B 91  ? 1.1314 1.3705 0.205  -0.3929 -0.0875 -0.0793 90  PHE   B CE1  
2634 C  CE2  . PHE   B 91  ? 1.117  1.3607 0.2075 -0.3809 -0.1204 -0.0171 90  PHE   B CE2  
2635 C  CZ   . PHE   B 91  ? 1.1239 1.384  0.1888 -0.3929 -0.1111 -0.0469 90  PHE   B CZ   
2636 N  N    . VAL   B 92  ? 1.082  1.1751 0.287  -0.3068 -0.0137 -0.0612 91  VAL   B N    
2637 C  CA   . VAL   B 92  ? 1.0706 1.1343 0.3019 -0.2852 -0.0056 -0.0542 91  VAL   B CA   
2638 C  C    . VAL   B 92  ? 1.0585 1.1011 0.3021 -0.2878 -0.0162 -0.0582 91  VAL   B C    
2639 O  O    . VAL   B 92  ? 1.0647 1.0922 0.3064 -0.2962 -0.0041 -0.0821 91  VAL   B O    
2640 C  CB   . VAL   B 92  ? 1.0846 1.1274 0.3197 -0.2697 0.028   -0.0698 91  VAL   B CB   
2641 C  CG1  . VAL   B 92  ? 1.0945 1.1067 0.3534 -0.2457 0.0355  -0.061  91  VAL   B CG1  
2642 C  CG2  . VAL   B 92  ? 1.0836 1.1518 0.3108 -0.2652 0.0387  -0.0641 91  VAL   B CG2  
2643 N  N    . VAL   B 93  ? 1.0385 1.082  0.2953 -0.2825 -0.0389 -0.0361 92  VAL   B N    
2644 C  CA   . VAL   B 93  ? 1.0289 1.0567 0.2989 -0.2843 -0.0502 -0.0373 92  VAL   B CA   
2645 C  C    . VAL   B 93  ? 1.0161 1.0205 0.3067 -0.2629 -0.0513 -0.0216 92  VAL   B C    
2646 O  O    . VAL   B 93  ? 1.0131 1.0272 0.3074 -0.2546 -0.0642 -0.0013 92  VAL   B O    
2647 C  CB   . VAL   B 93  ? 1.0304 1.0843 0.2933 -0.3002 -0.0798 -0.0269 92  VAL   B CB   
2648 C  CG1  . VAL   B 93  ? 1.035  1.078  0.3131 -0.3034 -0.0889 -0.0325 92  VAL   B CG1  
2649 C  CG2  . VAL   B 93  ? 1.0349 1.1189 0.2714 -0.3192 -0.082  -0.0373 92  VAL   B CG2  
2650 N  N    . ASP   B 94  ? 1.0061 0.9805 0.3097 -0.255  -0.0378 -0.0313 93  ASP   B N    
2651 C  CA   . ASP   B 94  ? 0.999  0.9512 0.3184 -0.2341 -0.039  -0.0167 93  ASP   B CA   
2652 C  C    . ASP   B 94  ? 0.9756 0.9381 0.3013 -0.2415 -0.067  -0.0043 93  ASP   B C    
2653 O  O    . ASP   B 94  ? 0.9783 0.9344 0.3121 -0.2498 -0.0691 -0.0129 93  ASP   B O    
2654 C  CB   . ASP   B 94  ? 1.0323 0.9479 0.3619 -0.2248 -0.0131 -0.0301 93  ASP   B CB   
2655 C  CG   . ASP   B 94  ? 1.0878 0.9789 0.4291 -0.2001 -0.0096 -0.015  93  ASP   B CG   
2656 O  OD1  . ASP   B 94  ? 1.0936 0.9969 0.435  -0.1882 -0.026  0.0036  93  ASP   B OD1  
2657 O  OD2  . ASP   B 94  ? 1.1185 0.9783 0.4685 -0.1932 0.0105  -0.0224 93  ASP   B OD2  
2658 N  N    . CYS   B 95  ? 0.9501 0.9293 0.2737 -0.2391 -0.0875 0.0153  94  CYS   B N    
2659 C  CA   . CYS   B 95  ? 0.929  0.9169 0.257  -0.2449 -0.1137 0.0293  94  CYS   B CA   
2660 C  C    . CYS   B 95  ? 0.9247 0.8889 0.2688 -0.2301 -0.117  0.0358  94  CYS   B C    
2661 O  O    . CYS   B 95  ? 0.9176 0.8848 0.2665 -0.2296 -0.1373 0.0495  94  CYS   B O    
2662 C  CB   . CYS   B 95  ? 0.9124 0.9205 0.2336 -0.2485 -0.1308 0.0472  94  CYS   B CB   
2663 S  SG   . CYS   B 95  ? 0.8664 0.9046 0.1668 -0.2659 -0.1261 0.0427  94  CYS   B SG   
2664 N  N    . GLY   B 96  ? 0.9282 0.8675 0.2792 -0.218  -0.0956 0.0261  95  GLY   B N    
2665 C  CA   . GLY   B 96  ? 0.9404 0.8559 0.3043 -0.2038 -0.0932 0.0304  95  GLY   B CA   
2666 C  C    . GLY   B 96  ? 0.9471 0.8507 0.3216 -0.2126 -0.0794 0.0144  95  GLY   B C    
2667 O  O    . GLY   B 96  ? 0.9457 0.8384 0.3335 -0.2082 -0.0821 0.0175  95  GLY   B O    
2668 N  N    . ASN   B 97  ? 0.9502 0.8566 0.3197 -0.2263 -0.0633 -0.0046 96  ASN   B N    
2669 C  CA   . ASN   B 97  ? 0.9568 0.8541 0.3369 -0.2399 -0.0473 -0.0258 96  ASN   B CA   
2670 C  C    . ASN   B 97  ? 0.9512 0.8815 0.334  -0.2636 -0.0684 -0.0337 96  ASN   B C    
2671 O  O    . ASN   B 97  ? 0.9484 0.905  0.3152 -0.2769 -0.0787 -0.0377 96  ASN   B O    
2672 C  CB   . ASN   B 97  ? 0.9756 0.8585 0.3477 -0.2428 -0.0192 -0.0443 96  ASN   B CB   
2673 C  CG   . ASN   B 97  ? 1.011  0.8763 0.3965 -0.2565 0.0021  -0.0681 96  ASN   B CG   
2674 O  OD1  . ASN   B 97  ? 1.0259 0.8979 0.4056 -0.2749 0.0118  -0.0908 96  ASN   B OD1  
2675 N  ND2  . ASN   B 97  ? 1.0164 0.8591 0.4207 -0.249  0.011   -0.0646 96  ASN   B ND2  
2676 N  N    . ARG   B 98  ? 0.9485 0.8794 0.3513 -0.2676 -0.0737 -0.0355 97  ARG   B N    
2677 C  CA   . ARG   B 98  ? 0.9458 0.9113 0.3567 -0.2861 -0.0953 -0.0409 97  ARG   B CA   
2678 C  C    . ARG   B 98  ? 0.9454 0.9313 0.3514 -0.3105 -0.0898 -0.0681 97  ARG   B C    
2679 O  O    . ARG   B 98  ? 0.9407 0.964  0.3346 -0.3238 -0.1113 -0.0689 97  ARG   B O    
2680 C  CB   . ARG   B 98  ? 0.9666 0.9251 0.4052 -0.282  -0.0955 -0.0388 97  ARG   B CB   
2681 C  CG   . ARG   B 98  ? 1.0059 1.0042 0.4569 -0.2948 -0.1216 -0.0383 97  ARG   B CG   
2682 C  CD   . ARG   B 98  ? 1.0588 1.0522 0.5415 -0.2908 -0.118  -0.0383 97  ARG   B CD   
2683 N  NE   . ARG   B 98  ? 1.1131 1.0863 0.6137 -0.3    -0.0883 -0.0611 97  ARG   B NE   
2684 C  CZ   . ARG   B 98  ? 1.1396 1.1364 0.6575 -0.3239 -0.0855 -0.0863 97  ARG   B CZ   
2685 N  NH1  . ARG   B 98  ? 1.1184 1.1644 0.6363 -0.339  -0.1127 -0.0911 97  ARG   B NH1  
2686 N  NH2  . ARG   B 98  ? 1.1478 1.1195 0.6832 -0.3328 -0.0552 -0.1068 97  ARG   B NH2  
2687 N  N    . GLU   B 99  ? 0.9486 0.9091 0.3619 -0.3159 -0.0602 -0.0905 98  GLU   B N    
2688 C  CA   . GLU   B 99  ? 0.9483 0.9249 0.3566 -0.3406 -0.0527 -0.1211 98  GLU   B CA   
2689 C  C    . GLU   B 99  ? 0.946  0.9317 0.3226 -0.3433 -0.0514 -0.1246 98  GLU   B C    
2690 O  O    . GLU   B 99  ? 0.946  0.9586 0.3106 -0.364  -0.0559 -0.1458 98  GLU   B O    
2691 C  CB   . GLU   B 99  ? 0.9953 0.9383 0.4237 -0.348  -0.0194 -0.1457 98  GLU   B CB   
2692 C  CG   . GLU   B 99  ? 1.0684 1.0135 0.5306 -0.3522 -0.0216 -0.1467 98  GLU   B CG   
2693 C  CD   . GLU   B 99  ? 1.1761 1.0841 0.6621 -0.3595 0.014   -0.1678 98  GLU   B CD   
2694 O  OE1  . GLU   B 99  ? 1.1974 1.0747 0.7003 -0.3428 0.0283  -0.1531 98  GLU   B OE1  
2695 O  OE2  . GLU   B 99  ? 1.2054 1.1139 0.6923 -0.3822 0.0287  -0.1994 98  GLU   B OE2  
2696 N  N    . ASP   B 100 ? 0.9421 0.91   0.3054 -0.3228 -0.0462 -0.1047 99  ASP   B N    
2697 C  CA   . ASP   B 100 ? 0.9404 0.9202 0.2766 -0.3239 -0.0445 -0.1053 99  ASP   B CA   
2698 C  C    . ASP   B 100 ? 0.9247 0.9456 0.2458 -0.3299 -0.0772 -0.0879 99  ASP   B C    
2699 O  O    . ASP   B 100 ? 0.9263 0.9739 0.2255 -0.3439 -0.0822 -0.0976 99  ASP   B O    
2700 C  CB   . ASP   B 100 ? 0.9658 0.9171 0.2978 -0.2995 -0.0273 -0.0903 99  ASP   B CB   
2701 C  CG   . ASP   B 100 ? 1.0064 0.9635 0.3165 -0.3002 -0.0141 -0.0978 99  ASP   B CG   
2702 O  OD1  . ASP   B 100 ? 1.0129 0.9974 0.306  -0.3197 -0.0206 -0.1125 99  ASP   B OD1  
2703 O  OD2  . ASP   B 100 ? 1.0221 0.9587 0.3318 -0.28   0.0029  -0.089  99  ASP   B OD2  
2704 N  N    . ILE   B 101 ? 0.9063 0.9305 0.2378 -0.3187 -0.098  -0.0622 100 ILE   B N    
2705 C  CA   . ILE   B 101 ? 0.8936 0.9506 0.2127 -0.3224 -0.1273 -0.0423 100 ILE   B CA   
2706 C  C    . ILE   B 101 ? 0.8792 0.974  0.1924 -0.3429 -0.1432 -0.0561 100 ILE   B C    
2707 O  O    . ILE   B 101 ? 0.878  1.0011 0.1663 -0.3522 -0.1534 -0.0542 100 ILE   B O    
2708 C  CB   . ILE   B 101 ? 0.8923 0.9394 0.2264 -0.3065 -0.1434 -0.0156 100 ILE   B CB   
2709 C  CG1  . ILE   B 101 ? 0.9072 0.9281 0.2405 -0.2877 -0.1331 -0.0015 100 ILE   B CG1  
2710 C  CG2  . ILE   B 101 ? 0.8923 0.9698 0.2172 -0.3112 -0.1725 0.0039  100 ILE   B CG2  
2711 C  CD1  . ILE   B 101 ? 0.9217 0.9262 0.2705 -0.2716 -0.1438 0.0177  100 ILE   B CD1  
2712 N  N    . TYR   B 102 ? 0.8673 0.9647 0.2032 -0.3501 -0.1436 -0.071  101 TYR   B N    
2713 C  CA   . TYR   B 102 ? 0.8558 0.9948 0.1911 -0.3696 -0.1599 -0.087  101 TYR   B CA   
2714 C  C    . TYR   B 102 ? 0.8568 1.0107 0.1696 -0.3885 -0.1485 -0.1165 101 TYR   B C    
2715 O  O    . TYR   B 102 ? 0.8406 1.0366 0.1342 -0.4014 -0.1668 -0.1215 101 TYR   B O    
2716 C  CB   . TYR   B 102 ? 0.8446 0.9832 0.2156 -0.374  -0.1589 -0.0996 101 TYR   B CB   
2717 C  CG   . TYR   B 102 ? 0.8456 0.9799 0.2377 -0.3571 -0.1743 -0.0723 101 TYR   B CG   
2718 C  CD1  . TYR   B 102 ? 0.8547 1.0005 0.2331 -0.3452 -0.197  -0.0417 101 TYR   B CD1  
2719 C  CD2  . TYR   B 102 ? 0.8518 0.9698 0.2777 -0.3536 -0.1645 -0.0779 101 TYR   B CD2  
2720 C  CE1  . TYR   B 102 ? 0.8622 1.0011 0.2594 -0.3295 -0.2097 -0.0188 101 TYR   B CE1  
2721 C  CE2  . TYR   B 102 ? 0.8568 0.9712 0.3009 -0.3374 -0.1774 -0.0544 101 TYR   B CE2  
2722 C  CZ   . TYR   B 102 ? 0.8648 0.9884 0.2941 -0.3248 -0.1999 -0.0256 101 TYR   B CZ   
2723 O  OH   . TYR   B 102 ? 0.8679 0.9842 0.3144 -0.3082 -0.211  -0.004  101 TYR   B OH   
2724 N  N    . ASN   B 103 ? 0.875  0.9938 0.1882 -0.3883 -0.1178 -0.1351 102 ASN   B N    
2725 C  CA   . ASN   B 103 ? 0.8954 1.0204 0.1871 -0.4045 -0.1021 -0.1652 102 ASN   B CA   
2726 C  C    . ASN   B 103 ? 0.9155 1.0621 0.1705 -0.4024 -0.1107 -0.1515 102 ASN   B C    
2727 O  O    . ASN   B 103 ? 0.914  1.0926 0.1442 -0.4186 -0.1164 -0.1688 102 ASN   B O    
2728 C  CB   . ASN   B 103 ? 0.9264 1.0016 0.228  -0.3991 -0.0645 -0.1823 102 ASN   B CB   
2729 C  CG   . ASN   B 103 ? 0.9716 1.0425 0.2774 -0.4213 -0.0451 -0.2246 102 ASN   B CG   
2730 O  OD1  . ASN   B 103 ? 0.993  1.0886 0.2741 -0.438  -0.0462 -0.2469 102 ASN   B OD1  
2731 N  ND2  . ASN   B 103 ? 0.9771 1.0147 0.3136 -0.4224 -0.0251 -0.2372 102 ASN   B ND2  
2732 N  N    . SER   B 104 ? 0.937  1.0683 0.1888 -0.3834 -0.1116 -0.1211 103 SER   B N    
2733 C  CA   . SER   B 104 ? 0.9652 1.1146 0.1869 -0.381  -0.1171 -0.1049 103 SER   B CA   
2734 C  C    . SER   B 104 ? 0.9771 1.1666 0.1837 -0.3854 -0.1491 -0.083  103 SER   B C    
2735 O  O    . SER   B 104 ? 0.9786 1.1915 0.1549 -0.3899 -0.1534 -0.0759 103 SER   B O    
2736 C  CB   . SER   B 104 ? 0.9951 1.1161 0.2232 -0.3608 -0.1057 -0.0824 103 SER   B CB   
2737 O  OG   . SER   B 104 ? 1.0384 1.125  0.2759 -0.3536 -0.0751 -0.1001 103 SER   B OG   
2738 N  N    . VAL   B 105 ? 0.9831 1.1802 0.2103 -0.3828 -0.1698 -0.0713 104 VAL   B N    
2739 C  CA   . VAL   B 105 ? 0.997  1.2309 0.2123 -0.3842 -0.1999 -0.0495 104 VAL   B CA   
2740 C  C    . VAL   B 105 ? 1.0195 1.2972 0.21   -0.4032 -0.2079 -0.073  104 VAL   B C    
2741 O  O    . VAL   B 105 ? 1.0237 1.3317 0.1822 -0.4058 -0.221  -0.0593 104 VAL   B O    
2742 C  CB   . VAL   B 105 ? 0.9928 1.224  0.2395 -0.375  -0.2174 -0.0342 104 VAL   B CB   
2743 C  CG1  . VAL   B 105 ? 0.9866 1.2625 0.224  -0.3783 -0.2472 -0.0208 104 VAL   B CG1  
2744 C  CG2  . VAL   B 105 ? 1.0062 1.2025 0.2664 -0.3559 -0.2159 -0.0057 104 VAL   B CG2  
2745 N  N    . LYS   B 106 ? 1.0303 1.31   0.2338 -0.4171 -0.1977 -0.1096 105 LYS   B N    
2746 C  CA   . LYS   B 106 ? 1.0441 1.3653 0.2253 -0.4373 -0.2041 -0.1388 105 LYS   B CA   
2747 C  C    . LYS   B 106 ? 1.0675 1.3917 0.2081 -0.443  -0.1887 -0.149  105 LYS   B C    
2748 O  O    . LYS   B 106 ? 1.0664 1.4329 0.1746 -0.4542 -0.2014 -0.1575 105 LYS   B O    
2749 C  CB   . LYS   B 106 ? 1.0694 1.3878 0.2791 -0.453  -0.194  -0.1781 105 LYS   B CB   
2750 C  CG   . LYS   B 106 ? 1.115  1.4482 0.362  -0.4506 -0.2136 -0.17   105 LYS   B CG   
2751 C  CD   . LYS   B 106 ? 1.1638 1.5017 0.4412 -0.4705 -0.2038 -0.211  105 LYS   B CD   
2752 C  CE   . LYS   B 106 ? 1.1911 1.5226 0.5149 -0.4635 -0.2099 -0.2008 105 LYS   B CE   
2753 N  NZ   . LYS   B 106 ? 1.199  1.5336 0.556  -0.4846 -0.1972 -0.2402 105 LYS   B NZ   
2754 N  N    . GLN   B 107 ? 1.0885 1.3715 0.2299 -0.4338 -0.1622 -0.1465 106 GLN   B N    
2755 C  CA   . GLN   B 107 ? 1.1149 1.3997 0.2213 -0.4361 -0.1453 -0.1526 106 GLN   B CA   
2756 C  C    . GLN   B 107 ? 1.1283 1.4349 0.209  -0.4276 -0.1613 -0.1142 106 GLN   B C    
2757 O  O    . GLN   B 107 ? 1.1375 1.4683 0.1805 -0.4339 -0.1585 -0.1169 106 GLN   B O    
2758 C  CB   . GLN   B 107 ? 1.1533 1.3898 0.274  -0.4258 -0.112  -0.1597 106 GLN   B CB   
2759 C  CG   . GLN   B 107 ? 1.2173 1.4569 0.3052 -0.4277 -0.0912 -0.1697 106 GLN   B CG   
2760 C  CD   . GLN   B 107 ? 1.2928 1.4913 0.3942 -0.4126 -0.0606 -0.1688 106 GLN   B CD   
2761 O  OE1  . GLN   B 107 ? 1.3316 1.5332 0.4111 -0.4105 -0.0431 -0.1719 106 GLN   B OE1  
2762 N  NE2  . GLN   B 107 ? 1.288  1.4495 0.4248 -0.4004 -0.0524 -0.1646 106 GLN   B NE2  
2763 N  N    . VAL   B 108 ? 1.1295 1.4257 0.2302 -0.4135 -0.1762 -0.0788 107 VAL   B N    
2764 C  CA   . VAL   B 108 ? 1.1404 1.4513 0.2226 -0.4061 -0.1911 -0.0403 107 VAL   B CA   
2765 C  C    . VAL   B 108 ? 1.1459 1.5052 0.1992 -0.4145 -0.216  -0.0361 107 VAL   B C    
2766 O  O    . VAL   B 108 ? 1.1476 1.5287 0.1656 -0.4157 -0.2188 -0.0201 107 VAL   B O    
2767 C  CB   . VAL   B 108 ? 1.142  1.4252 0.2557 -0.3901 -0.1998 -0.0085 107 VAL   B CB   
2768 C  CG1  . VAL   B 108 ? 1.145  1.4465 0.2452 -0.3849 -0.2226 0.0296  107 VAL   B CG1  
2769 C  CG2  . VAL   B 108 ? 1.152  1.3993 0.2799 -0.3803 -0.1772 -0.0041 107 VAL   B CG2  
2770 N  N    . LYS   B 109 ? 1.1453 1.5241 0.2134 -0.42   -0.2331 -0.0506 108 LYS   B N    
2771 C  CA   . LYS   B 109 ? 1.1547 1.586  0.1974 -0.4262 -0.259  -0.0481 108 LYS   B CA   
2772 C  C    . LYS   B 109 ? 1.1681 1.6318 0.1727 -0.4437 -0.2521 -0.0831 108 LYS   B C    
2773 O  O    . LYS   B 109 ? 1.1636 1.6711 0.1302 -0.4465 -0.2685 -0.0746 108 LYS   B O    
2774 C  CB   . LYS   B 109 ? 1.1703 1.6168 0.2464 -0.4248 -0.2808 -0.0501 108 LYS   B CB   
2775 C  CG   . LYS   B 109 ? 1.2382 1.6529 0.3459 -0.4062 -0.2872 -0.0145 108 LYS   B CG   
2776 C  CD   . LYS   B 109 ? 1.2892 1.7234 0.4276 -0.4013 -0.3101 -0.0098 108 LYS   B CD   
2777 C  CE   . LYS   B 109 ? 1.3446 1.7473 0.5064 -0.3815 -0.3162 0.0277  108 LYS   B CE   
2778 N  NZ   . LYS   B 109 ? 1.3617 1.7863 0.5514 -0.3738 -0.3388 0.0364  108 LYS   B NZ   
2779 N  N    . LYS   B 110 ? 1.1798 1.6197 0.1923 -0.4539 -0.226  -0.121  109 LYS   B N    
2780 C  CA   . LYS   B 110 ? 1.1936 1.6555 0.1711 -0.4705 -0.2144 -0.1581 109 LYS   B CA   
2781 C  C    . LYS   B 110 ? 1.2243 1.6773 0.1653 -0.4662 -0.1939 -0.1472 109 LYS   B C    
2782 O  O    . LYS   B 110 ? 1.2339 1.7042 0.1406 -0.4781 -0.1819 -0.176  109 LYS   B O    
2783 C  CB   . LYS   B 110 ? 1.2089 1.646  0.2124 -0.4841 -0.1931 -0.2055 109 LYS   B CB   
2784 C  CG   . LYS   B 110 ? 1.252  1.7295 0.2341 -0.5068 -0.1987 -0.2503 109 LYS   B CG   
2785 C  CD   . LYS   B 110 ? 1.3222 1.7833 0.2768 -0.5171 -0.1675 -0.2855 109 LYS   B CD   
2786 C  CE   . LYS   B 110 ? 1.3576 1.8703 0.2685 -0.5364 -0.1773 -0.3193 109 LYS   B CE   
2787 N  NZ   . LYS   B 110 ? 1.3822 1.9302 0.2399 -0.5287 -0.1882 -0.2919 109 LYS   B NZ   
2788 N  N    . GLU   B 111 ? 1.2358 1.6646 0.1844 -0.4503 -0.1895 -0.1075 110 GLU   B N    
2789 C  CA   . GLU   B 111 ? 1.2583 1.6827 0.178  -0.4469 -0.1695 -0.096  110 GLU   B CA   
2790 C  C    . GLU   B 111 ? 1.2569 1.6934 0.1605 -0.4368 -0.1827 -0.0473 110 GLU   B C    
2791 O  O    . GLU   B 111 ? 1.2672 1.7309 0.128  -0.44   -0.1808 -0.0386 110 GLU   B O    
2792 C  CB   . GLU   B 111 ? 1.309  1.6872 0.2554 -0.4403 -0.1384 -0.1057 110 GLU   B CB   
2793 C  CG   . GLU   B 111 ? 1.4118 1.7849 0.3424 -0.4505 -0.1118 -0.1498 110 GLU   B CG   
2794 C  CD   . GLU   B 111 ? 1.53   1.874  0.4654 -0.441  -0.0794 -0.1492 110 GLU   B CD   
2795 O  OE1  . GLU   B 111 ? 1.5605 1.9178 0.4622 -0.4461 -0.0613 -0.1651 110 GLU   B OE1  
2796 O  OE2  . GLU   B 111 ? 1.558  1.8687 0.5306 -0.4274 -0.0724 -0.1331 110 GLU   B OE2  
2797 N  N    . VAL   B 112 ? 1.2444 1.6591 0.1809 -0.4251 -0.1941 -0.0161 111 VAL   B N    
2798 C  CA   . VAL   B 112 ? 1.2464 1.6645 0.1732 -0.4162 -0.2046 0.03    111 VAL   B CA   
2799 C  C    . VAL   B 112 ? 1.2421 1.6893 0.1586 -0.413  -0.2365 0.051   111 VAL   B C    
2800 O  O    . VAL   B 112 ? 1.2508 1.724  0.131  -0.4114 -0.2452 0.0767  111 VAL   B O    
2801 C  CB   . VAL   B 112 ? 1.2557 1.6309 0.2228 -0.4053 -0.1958 0.0509  111 VAL   B CB   
2802 C  CG1  . VAL   B 112 ? 1.265  1.6384 0.2296 -0.3977 -0.2088 0.0971  111 VAL   B CG1  
2803 C  CG2  . VAL   B 112 ? 1.2646 1.6212 0.2356 -0.4058 -0.1652 0.0371  111 VAL   B CG2  
2804 N  N    . GLY   B 113 ? 1.2277 1.672  0.1761 -0.4109 -0.2523 0.0408  112 GLY   B N    
2805 C  CA   . GLY   B 113 ? 1.2174 1.6912 0.1641 -0.4055 -0.2827 0.0587  112 GLY   B CA   
2806 C  C    . GLY   B 113 ? 1.2054 1.6509 0.1993 -0.394  -0.2932 0.0737  112 GLY   B C    
2807 O  O    . GLY   B 113 ? 1.2065 1.6206 0.2355 -0.3947 -0.2806 0.0538  112 GLY   B O    
2808 N  N    . ASP   B 114 ? 1.1937 1.6481 0.1878 -0.3816 -0.3147 0.1102  113 ASP   B N    
2809 C  CA   . ASP   B 114 ? 1.1854 1.6132 0.2225 -0.369  -0.3247 0.1258  113 ASP   B CA   
2810 C  C    . ASP   B 114 ? 1.1804 1.5632 0.2283 -0.3594 -0.3145 0.1582  113 ASP   B C    
2811 O  O    . ASP   B 114 ? 1.1895 1.576  0.2128 -0.3548 -0.3181 0.191   113 ASP   B O    
2812 C  CB   . ASP   B 114 ? 1.2054 1.6696 0.2408 -0.3595 -0.3542 0.1443  113 ASP   B CB   
2813 C  CG   . ASP   B 114 ? 1.2638 1.7821 0.2886 -0.3703 -0.368  0.112   113 ASP   B CG   
2814 O  OD1  . ASP   B 114 ? 1.2707 1.786  0.3108 -0.3843 -0.3557 0.071   113 ASP   B OD1  
2815 O  OD2  . ASP   B 114 ? 1.2875 1.8514 0.2891 -0.3647 -0.3908 0.1279  113 ASP   B OD2  
2816 N  N    . VAL   B 115 ? 1.1641 1.5057 0.2477 -0.3566 -0.3013 0.1492  114 VAL   B N    
2817 C  CA   . VAL   B 115 ? 1.1634 1.4657 0.2592 -0.3496 -0.2921 0.1749  114 VAL   B CA   
2818 C  C    . VAL   B 115 ? 1.1566 1.4506 0.257  -0.3369 -0.3097 0.2133  114 VAL   B C    
2819 O  O    . VAL   B 115 ? 1.1532 1.4563 0.2691 -0.3285 -0.327  0.2152  114 VAL   B O    
2820 C  CB   . VAL   B 115 ? 1.1664 1.4317 0.2979 -0.3472 -0.2771 0.1561  114 VAL   B CB   
2821 C  CG1  . VAL   B 115 ? 1.1793 1.4084 0.3271 -0.3397 -0.2725 0.1807  114 VAL   B CG1  
2822 C  CG2  . VAL   B 115 ? 1.1718 1.4398 0.295  -0.3573 -0.2553 0.1248  114 VAL   B CG2  
2823 N  N    . THR   B 116 ? 1.1511 1.4295 0.2379 -0.3358 -0.3043 0.2441  115 THR   B N    
2824 C  CA   . THR   B 116 ? 1.1454 1.409  0.2345 -0.3239 -0.3171 0.2826  115 THR   B CA   
2825 C  C    . THR   B 116 ? 1.1319 1.3465 0.251  -0.3194 -0.3094 0.2957  115 THR   B C    
2826 O  O    . THR   B 116 ? 1.1365 1.3313 0.2641 -0.3087 -0.3191 0.3229  115 THR   B O    
2827 C  CB   . THR   B 116 ? 1.1751 1.4594 0.2229 -0.3252 -0.3187 0.3124  115 THR   B CB   
2828 O  OG1  . THR   B 116 ? 1.1996 1.4659 0.2387 -0.3351 -0.2979 0.3213  115 THR   B OG1  
2829 C  CG2  . THR   B 116 ? 1.1797 1.5164 0.1928 -0.3299 -0.3271 0.2979  115 THR   B CG2  
2830 N  N    . ILE   B 117 ? 1.1125 1.3086 0.2464 -0.3271 -0.2919 0.277   116 ILE   B N    
2831 C  CA   . ILE   B 117 ? 1.0965 1.2516 0.2591 -0.3246 -0.2849 0.2833  116 ILE   B CA   
2832 C  C    . ILE   B 117 ? 1.0707 1.2186 0.2553 -0.3255 -0.2745 0.2499  116 ILE   B C    
2833 O  O    . ILE   B 117 ? 1.0696 1.2343 0.2431 -0.334  -0.2611 0.231   116 ILE   B O    
2834 C  CB   . ILE   B 117 ? 1.109  1.2529 0.2626 -0.3341 -0.2717 0.3043  116 ILE   B CB   
2835 C  CG1  . ILE   B 117 ? 1.1295 1.2714 0.2623 -0.3315 -0.279  0.3427  116 ILE   B CG1  
2836 C  CG2  . ILE   B 117 ? 1.115  1.2242 0.301  -0.3348 -0.2638 0.3008  116 ILE   B CG2  
2837 C  CD1  . ILE   B 117 ? 1.15   1.2867 0.2695 -0.3437 -0.2626 0.3634  116 ILE   B CD1  
2838 N  N    . LEU   B 118 ? 1.0487 1.1704 0.2626 -0.3155 -0.2789 0.2434  117 LEU   B N    
2839 C  CA   . LEU   B 118 ? 1.031  1.1426 0.2645 -0.3133 -0.2682 0.2155  117 LEU   B CA   
2840 C  C    . LEU   B 118 ? 1.0141 1.0957 0.2682 -0.3105 -0.2619 0.2194  117 LEU   B C    
2841 O  O    . LEU   B 118 ? 1.0167 1.0755 0.2814 -0.3056 -0.2704 0.2371  117 LEU   B O    
2842 C  CB   . LEU   B 118 ? 1.0293 1.139  0.279  -0.3037 -0.2767 0.2011  117 LEU   B CB   
2843 C  CG   . LEU   B 118 ? 1.0423 1.1368 0.312  -0.2986 -0.2647 0.1754  117 LEU   B CG   
2844 C  CD1  . LEU   B 118 ? 1.0472 1.1572 0.305  -0.3073 -0.2478 0.1536  117 LEU   B CD1  
2845 C  CD2  . LEU   B 118 ? 1.0448 1.1385 0.3307 -0.2906 -0.2719 0.1649  117 LEU   B CD2  
2846 N  N    . VAL   B 119 ? 0.9951 1.0782 0.2548 -0.3133 -0.2468 0.2025  118 VAL   B N    
2847 C  CA   . VAL   B 119 ? 0.9856 1.049  0.2655 -0.3106 -0.2416 0.2021  118 VAL   B CA   
2848 C  C    . VAL   B 119 ? 0.9665 1.0217 0.2615 -0.2993 -0.2344 0.1782  118 VAL   B C    
2849 O  O    . VAL   B 119 ? 0.9594 1.0274 0.2517 -0.3003 -0.22   0.1625  118 VAL   B O    
2850 C  CB   . VAL   B 119 ? 0.9919 1.0691 0.2667 -0.3229 -0.2296 0.2081  118 VAL   B CB   
2851 C  CG1  . VAL   B 119 ? 0.9959 1.0601 0.2952 -0.3208 -0.2258 0.2043  118 VAL   B CG1  
2852 C  CG2  . VAL   B 119 ? 0.9992 1.0807 0.2575 -0.3335 -0.2341 0.2347  118 VAL   B CG2  
2853 N  N    . ASN   B 120 ? 0.9569 0.9902 0.2667 -0.2873 -0.243  0.1765  119 ASN   B N    
2854 C  CA   . ASN   B 120 ? 0.9527 0.9734 0.2758 -0.2741 -0.2362 0.158   119 ASN   B CA   
2855 C  C    . ASN   B 120 ? 0.9395 0.9518 0.2746 -0.2694 -0.231  0.1555  119 ASN   B C    
2856 O  O    . ASN   B 120 ? 0.9385 0.9305 0.286  -0.2605 -0.2379 0.1575  119 ASN   B O    
2857 C  CB   . ASN   B 120 ? 0.9729 0.9746 0.3067 -0.263  -0.2469 0.1599  119 ASN   B CB   
2858 C  CG   . ASN   B 120 ? 1.0154 1.031  0.3443 -0.2651 -0.2511 0.1563  119 ASN   B CG   
2859 O  OD1  . ASN   B 120 ? 1.0343 1.0525 0.3619 -0.2654 -0.2649 0.1706  119 ASN   B OD1  
2860 N  ND2  . ASN   B 120 ? 1.0193 1.0445 0.3465 -0.2661 -0.2391 0.1366  119 ASN   B ND2  
2861 N  N    . ASN   B 121 ? 0.928  0.9591 0.2594 -0.2756 -0.2191 0.1506  120 ASN   B N    
2862 C  CA   . ASN   B 121 ? 0.9222 0.9558 0.2668 -0.2721 -0.2148 0.1478  120 ASN   B CA   
2863 C  C    . ASN   B 121 ? 0.9128 0.9405 0.2648 -0.254  -0.2055 0.1316  120 ASN   B C    
2864 O  O    . ASN   B 121 ? 0.909  0.9236 0.2723 -0.2431 -0.2114 0.1303  120 ASN   B O    
2865 C  CB   . ASN   B 121 ? 0.9313 0.9914 0.2719 -0.2858 -0.2056 0.1518  120 ASN   B CB   
2866 C  CG   . ASN   B 121 ? 0.9666 1.0386 0.3247 -0.2837 -0.2011 0.148   120 ASN   B CG   
2867 O  OD1  . ASN   B 121 ? 0.9818 1.0517 0.3522 -0.2918 -0.2093 0.1568  120 ASN   B OD1  
2868 N  ND2  . ASN   B 121 ? 0.9683 1.0549 0.3294 -0.2731 -0.1873 0.1345  120 ASN   B ND2  
2869 N  N    . ALA   B 122 ? 0.9065 0.9416 0.2507 -0.2499 -0.1902 0.1192  121 ALA   B N    
2870 C  CA   . ALA   B 122 ? 0.9068 0.9341 0.2555 -0.2317 -0.1764 0.1056  121 ALA   B CA   
2871 C  C    . ALA   B 122 ? 0.9193 0.925  0.2776 -0.2146 -0.183  0.1056  121 ALA   B C    
2872 O  O    . ALA   B 122 ? 0.9276 0.9171 0.2876 -0.2155 -0.1958 0.1114  121 ALA   B O    
2873 C  CB   . ALA   B 122 ? 0.9079 0.9305 0.2468 -0.2321 -0.1631 0.0934  121 ALA   B CB   
2874 N  N    . GLY   B 123 ? 0.9143 0.9223 0.2782 -0.1978 -0.1742 0.1     122 GLY   B N    
2875 C  CA   . GLY   B 123 ? 0.9141 0.9054 0.2829 -0.1788 -0.1786 0.0992  122 GLY   B CA   
2876 C  C    . GLY   B 123 ? 0.9074 0.9038 0.2772 -0.1572 -0.1639 0.0931  122 GLY   B C    
2877 O  O    . GLY   B 123 ? 0.8972 0.914  0.2681 -0.1574 -0.1525 0.0903  122 GLY   B O    
2878 N  N    . THR   B 124 ? 0.9111 0.889  0.2794 -0.1365 -0.1631 0.0921  123 THR   B N    
2879 C  CA   . THR   B 124 ? 0.9106 0.8912 0.2772 -0.1108 -0.1501 0.0897  123 THR   B CA   
2880 C  C    . THR   B 124 ? 0.9182 0.894  0.2839 -0.0941 -0.1631 0.0918  123 THR   B C    
2881 O  O    . THR   B 124 ? 0.9229 0.8792 0.2866 -0.0978 -0.174  0.0931  123 THR   B O    
2882 C  CB   . THR   B 124 ? 0.9252 0.8843 0.285  -0.0996 -0.1252 0.0854  123 THR   B CB   
2883 O  OG1  . THR   B 124 ? 0.9277 0.8969 0.2867 -0.0788 -0.1092 0.0849  123 THR   B OG1  
2884 C  CG2  . THR   B 124 ? 0.9399 0.8666 0.2951 -0.0886 -0.1212 0.0861  123 THR   B CG2  
2885 N  N    . VAL   B 125 ? 0.9171 0.9143 0.2844 -0.0762 -0.1632 0.0914  124 VAL   B N    
2886 C  CA   . VAL   B 125 ? 0.929  0.9278 0.2926 -0.0594 -0.1764 0.0909  124 VAL   B CA   
2887 C  C    . VAL   B 125 ? 0.9474 0.9526 0.3027 -0.0265 -0.1632 0.0928  124 VAL   B C    
2888 O  O    . VAL   B 125 ? 0.9453 0.9698 0.3053 -0.0194 -0.1506 0.0939  124 VAL   B O    
2889 C  CB   . VAL   B 125 ? 0.9193 0.9466 0.2953 -0.0748 -0.1991 0.0875  124 VAL   B CB   
2890 C  CG1  . VAL   B 125 ? 0.9087 0.9793 0.2965 -0.07   -0.1977 0.0858  124 VAL   B CG1  
2891 C  CG2  . VAL   B 125 ? 0.9263 0.9455 0.2963 -0.0652 -0.2152 0.0835  124 VAL   B CG2  
2892 N  N    . TYR   B 126 ? 0.9648 0.9534 0.3066 -0.0048 -0.1644 0.0944  125 TYR   B N    
2893 C  CA   . TYR   B 126 ? 0.9813 0.9745 0.3109 0.0303  -0.1521 0.0993  125 TYR   B CA   
2894 C  C    . TYR   B 126 ? 0.9906 0.9968 0.3111 0.0442  -0.1719 0.0965  125 TYR   B C    
2895 O  O    . TYR   B 126 ? 1.0136 0.9925 0.3175 0.0581  -0.1695 0.0985  125 TYR   B O    
2896 C  CB   . TYR   B 126 ? 1.0038 0.9548 0.3209 0.0449  -0.126  0.1055  125 TYR   B CB   
2897 C  CG   . TYR   B 126 ? 1.0194 0.9589 0.3451 0.0304  -0.106  0.1044  125 TYR   B CG   
2898 C  CD1  . TYR   B 126 ? 1.0263 0.9849 0.357  0.039   -0.0927 0.1055  125 TYR   B CD1  
2899 C  CD2  . TYR   B 126 ? 1.0354 0.9491 0.3651 0.0071  -0.1019 0.1006  125 TYR   B CD2  
2900 C  CE1  . TYR   B 126 ? 1.0377 0.9856 0.3744 0.0246  -0.0743 0.1015  125 TYR   B CE1  
2901 C  CE2  . TYR   B 126 ? 1.0455 0.9517 0.3812 -0.0073 -0.0849 0.0964  125 TYR   B CE2  
2902 C  CZ   . TYR   B 126 ? 1.0539 0.9755 0.392  0.001   -0.0707 0.0961  125 TYR   B CZ   
2903 O  OH   . TYR   B 126 ? 1.0765 0.99   0.4184 -0.0136 -0.0533 0.0893  125 TYR   B OH   
2904 N  N    . PRO   B 127 ? 0.9704 1.0192 0.3027 0.0379  -0.1921 0.0899  126 PRO   B N    
2905 C  CA   . PRO   B 127 ? 0.9693 1.033  0.2938 0.0462  -0.2138 0.0825  126 PRO   B CA   
2906 C  C    . PRO   B 127 ? 0.9867 1.0515 0.2868 0.0861  -0.2081 0.0877  126 PRO   B C    
2907 O  O    . PRO   B 127 ? 0.9893 1.0853 0.2891 0.1088  -0.2033 0.0926  126 PRO   B O    
2908 C  CB   . PRO   B 127 ? 0.9502 1.0649 0.2973 0.0303  -0.2324 0.0737  126 PRO   B CB   
2909 C  CG   . PRO   B 127 ? 0.9467 1.0639 0.3131 0.0057  -0.2227 0.077   126 PRO   B CG   
2910 C  CD   . PRO   B 127 ? 0.9418 1.0278 0.2964 0.0203  -0.1956 0.0873  126 PRO   B CD   
2911 N  N    . ALA   B 128 ? 0.9947 1.0274 0.2738 0.0962  -0.2084 0.0874  127 ALA   B N    
2912 C  CA   . ALA   B 128 ? 0.9983 1.028  0.2487 0.1345  -0.2027 0.0934  127 ALA   B CA   
2913 C  C    . ALA   B 128 ? 1.0137 1.0127 0.2454 0.1355  -0.2091 0.088   127 ALA   B C    
2914 O  O    . ALA   B 128 ? 1.0201 0.9899 0.2614 0.1106  -0.21   0.0841  127 ALA   B O    
2915 C  CB   . ALA   B 128 ? 1.0086 1.0132 0.2484 0.1591  -0.1706 0.1106  127 ALA   B CB   
2916 N  N    . ASP   B 129 ? 1.019  1.0256 0.2227 0.1663  -0.2127 0.0884  128 ASP   B N    
2917 C  CA   . ASP   B 129 ? 1.0379 1.0144 0.2203 0.1711  -0.2153 0.0835  128 ASP   B CA   
2918 C  C    . ASP   B 129 ? 1.0462 0.9725 0.221  0.1785  -0.1858 0.0979  128 ASP   B C    
2919 O  O    . ASP   B 129 ? 1.0524 0.9695 0.2292 0.1898  -0.1625 0.1121  128 ASP   B O    
2920 C  CB   . ASP   B 129 ? 1.0771 1.0776 0.2279 0.2026  -0.2267 0.0792  128 ASP   B CB   
2921 C  CG   . ASP   B 129 ? 1.1569 1.1661 0.2851 0.2436  -0.2078 0.0981  128 ASP   B CG   
2922 O  OD1  . ASP   B 129 ? 1.1607 1.191  0.3048 0.2471  -0.2007 0.1068  128 ASP   B OD1  
2923 O  OD2  . ASP   B 129 ? 1.1941 1.1884 0.2876 0.2738  -0.1989 0.105   128 ASP   B OD2  
2924 N  N    . LEU   B 130 ? 1.0436 0.9374 0.2116 0.1719  -0.1852 0.0935  129 LEU   B N    
2925 C  CA   . LEU   B 130 ? 1.047  0.897  0.2142 0.1745  -0.158  0.1051  129 LEU   B CA   
2926 C  C    . LEU   B 130 ? 1.0531 0.8893 0.1985 0.2088  -0.1296 0.1227  129 LEU   B C    
2927 O  O    . LEU   B 130 ? 1.0636 0.8692 0.2176 0.2065  -0.1034 0.133   129 LEU   B O    
2928 C  CB   . LEU   B 130 ? 1.0527 0.8758 0.2144 0.1684  -0.1618 0.098   129 LEU   B CB   
2929 C  CG   . LEU   B 130 ? 1.067  0.8552 0.2471 0.1533  -0.1426 0.1045  129 LEU   B CG   
2930 C  CD1  . LEU   B 130 ? 1.0628 0.8516 0.2707 0.1183  -0.1604 0.0948  129 LEU   B CD1  
2931 C  CD2  . LEU   B 130 ? 1.0886 0.8474 0.2505 0.1721  -0.1261 0.1092  129 LEU   B CD2  
2932 N  N    . LEU   B 131 ? 1.044  0.9037 0.1621 0.2402  -0.1341 0.1264  130 LEU   B N    
2933 C  CA   . LEU   B 131 ? 1.0524 0.8978 0.1455 0.2774  -0.1061 0.1464  130 LEU   B CA   
2934 C  C    . LEU   B 131 ? 1.0376 0.8986 0.1401 0.2879  -0.094  0.1581  130 LEU   B C    
2935 O  O    . LEU   B 131 ? 1.0498 0.887  0.1394 0.3131  -0.0636 0.1768  130 LEU   B O    
2936 C  CB   . LEU   B 131 ? 1.0601 0.9199 0.1126 0.3111  -0.1146 0.1472  130 LEU   B CB   
2937 C  CG   . LEU   B 131 ? 1.0831 0.9231 0.1232 0.3043  -0.122  0.1356  130 LEU   B CG   
2938 C  CD1  . LEU   B 131 ? 1.0997 0.9613 0.0982 0.3353  -0.1348 0.1318  130 LEU   B CD1  
2939 C  CD2  . LEU   B 131 ? 1.1028 0.8922 0.1455 0.3034  -0.09   0.1474  130 LEU   B CD2  
2940 N  N    . SER   B 132 ? 1.0095 0.9077 0.1356 0.2684  -0.115  0.1476  131 SER   B N    
2941 C  CA   . SER   B 132 ? 0.999  0.9144 0.1379 0.2762  -0.1039 0.1566  131 SER   B CA   
2942 C  C    . SER   B 132 ? 0.981  0.8791 0.1526 0.2425  -0.0931 0.1529  131 SER   B C    
2943 O  O    . SER   B 132 ? 0.9806 0.8846 0.1623 0.2483  -0.0786 0.1598  131 SER   B O    
2944 C  CB   . SER   B 132 ? 1.007  0.9829 0.1483 0.2844  -0.131  0.1496  131 SER   B CB   
2945 O  OG   . SER   B 132 ? 1.0617 1.057  0.1691 0.3215  -0.1379 0.155   131 SER   B OG   
2946 N  N    . THR   B 133 ? 0.9638 0.8418 0.1505 0.2092  -0.1    0.1421  132 THR   B N    
2947 C  CA   . THR   B 133 ? 0.9479 0.8108 0.1619 0.177   -0.0917 0.1378  132 THR   B CA   
2948 C  C    . THR   B 133 ? 0.9451 0.7657 0.157  0.1859  -0.0555 0.149   132 THR   B C    
2949 O  O    . THR   B 133 ? 0.9639 0.7556 0.1592 0.2027  -0.0403 0.1567  132 THR   B O    
2950 C  CB   . THR   B 133 ? 0.9648 0.8168 0.1919 0.1448  -0.1081 0.1261  132 THR   B CB   
2951 O  OG1  . THR   B 133 ? 0.9902 0.8183 0.1993 0.1579  -0.1051 0.128   132 THR   B OG1  
2952 C  CG2  . THR   B 133 ? 0.9563 0.8438 0.1969 0.1223  -0.1403 0.1132  132 THR   B CG2  
2953 N  N    . LYS   B 134 ? 0.9214 0.737  0.1509 0.173   -0.0404 0.1485  133 LYS   B N    
2954 C  CA   . LYS   B 134 ? 0.9234 0.6973 0.155  0.1764  -0.0045 0.1554  133 LYS   B CA   
2955 C  C    . LYS   B 134 ? 0.9062 0.6577 0.1562 0.1426  -0.003  0.1454  133 LYS   B C    
2956 O  O    . LYS   B 134 ? 0.8954 0.6665 0.1608 0.1138  -0.0264 0.134   133 LYS   B O    
2957 C  CB   . LYS   B 134 ? 0.9467 0.7257 0.1879 0.1784  0.0117  0.1568  133 LYS   B CB   
2958 C  CG   . LYS   B 134 ? 0.9954 0.8086 0.2254 0.209   0.0053  0.1653  133 LYS   B CG   
2959 C  CD   . LYS   B 134 ? 1.0327 0.8589 0.2786 0.2038  0.0157  0.1626  133 LYS   B CD   
2960 C  CE   . LYS   B 134 ? 1.0538 0.9344 0.3013 0.2178  -0.0059 0.1636  133 LYS   B CE   
2961 N  NZ   . LYS   B 134 ? 1.0796 0.9701 0.3046 0.2639  -0.0004 0.1802  133 LYS   B NZ   
2962 N  N    . ASP   B 135 ? 0.9009 0.6131 0.1504 0.1464  0.0248  0.1504  134 ASP   B N    
2963 C  CA   . ASP   B 135 ? 0.8846 0.5802 0.1541 0.1164  0.0269  0.1409  134 ASP   B CA   
2964 C  C    . ASP   B 135 ? 0.8656 0.5709 0.1576 0.0843  0.0239  0.1282  134 ASP   B C    
2965 O  O    . ASP   B 135 ? 0.8566 0.5699 0.1645 0.0566  0.0081  0.1185  134 ASP   B O    
2966 C  CB   . ASP   B 135 ? 0.9005 0.5545 0.1692 0.1264  0.0618  0.1482  134 ASP   B CB   
2967 C  CG   . ASP   B 135 ? 0.9279 0.5712 0.1746 0.1533  0.0642  0.1598  134 ASP   B CG   
2968 O  OD1  . ASP   B 135 ? 0.9119 0.5775 0.1506 0.1539  0.0354  0.1564  134 ASP   B OD1  
2969 O  OD2  . ASP   B 135 ? 0.9676 0.579  0.2038 0.1742  0.0962  0.1721  134 ASP   B OD2  
2970 N  N    . GLU   B 136 ? 0.8615 0.5658 0.1535 0.0897  0.0401  0.1286  135 GLU   B N    
2971 C  CA   . GLU   B 136 ? 0.8553 0.5686 0.1639 0.0625  0.0409  0.1157  135 GLU   B CA   
2972 C  C    . GLU   B 136 ? 0.8319 0.5863 0.1456 0.044   0.0057  0.1094  135 GLU   B C    
2973 O  O    . GLU   B 136 ? 0.8289 0.5931 0.1563 0.014   -0.004  0.0986  135 GLU   B O    
2974 C  CB   . GLU   B 136 ? 0.9026 0.605  0.2068 0.0792  0.0677  0.1189  135 GLU   B CB   
2975 C  CG   . GLU   B 136 ? 1.0199 0.6783 0.3154 0.1044  0.1053  0.1299  135 GLU   B CG   
2976 C  CD   . GLU   B 136 ? 1.1577 0.8147 0.4298 0.1444  0.1066  0.1494  135 GLU   B CD   
2977 O  OE1  . GLU   B 136 ? 1.1839 0.8787 0.4471 0.1548  0.0789  0.1525  135 GLU   B OE1  
2978 O  OE2  . GLU   B 136 ? 1.2041 0.8239 0.4667 0.1644  0.1352  0.1611  135 GLU   B OE2  
2979 N  N    . GLU   B 137 ? 0.8156 0.5948 0.1181 0.0618  -0.0129 0.1161  136 GLU   B N    
2980 C  CA   . GLU   B 137 ? 0.801  0.6176 0.1089 0.0461  -0.0447 0.1112  136 GLU   B CA   
2981 C  C    . GLU   B 137 ? 0.7947 0.6093 0.1097 0.0241  -0.0649 0.1064  136 GLU   B C    
2982 O  O    . GLU   B 137 ? 0.7844 0.6166 0.1106 -0.002  -0.0817 0.1003  136 GLU   B O    
2983 C  CB   . GLU   B 137 ? 0.8316 0.6736 0.1271 0.0715  -0.0587 0.1177  136 GLU   B CB   
2984 C  CG   . GLU   B 137 ? 0.8988 0.7551 0.1909 0.0935  -0.0444 0.1232  136 GLU   B CG   
2985 C  CD   . GLU   B 137 ? 0.9686 0.86   0.2514 0.1178  -0.0615 0.1283  136 GLU   B CD   
2986 O  OE1  . GLU   B 137 ? 0.9718 0.8609 0.2403 0.1318  -0.0724 0.1312  136 GLU   B OE1  
2987 O  OE2  . GLU   B 137 ? 0.9859 0.9099 0.2763 0.1225  -0.0642 0.1281  136 GLU   B OE2  
2988 N  N    . ILE   B 138 ? 0.8004 0.5935 0.1083 0.0359  -0.062  0.1105  137 ILE   B N    
2989 C  CA   . ILE   B 138 ? 0.8002 0.5889 0.1156 0.0196  -0.0784 0.1072  137 ILE   B CA   
2990 C  C    . ILE   B 138 ? 0.7985 0.5812 0.1322 -0.0078 -0.073  0.1007  137 ILE   B C    
2991 O  O    . ILE   B 138 ? 0.7919 0.5884 0.1356 -0.0299 -0.0932 0.097   137 ILE   B O    
2992 C  CB   . ILE   B 138 ? 0.8138 0.5793 0.1173 0.0412  -0.07   0.113   137 ILE   B CB   
2993 C  CG1  . ILE   B 138 ? 0.8281 0.6051 0.1101 0.068   -0.0791 0.1176  137 ILE   B CG1  
2994 C  CG2  . ILE   B 138 ? 0.8168 0.5763 0.1308 0.026   -0.0834 0.1096  137 ILE   B CG2  
2995 C  CD1  . ILE   B 138 ? 0.8605 0.6139 0.1236 0.0971  -0.0608 0.1263  137 ILE   B CD1  
2996 N  N    . THR   B 139 ? 0.8019 0.565  0.1395 -0.0064 -0.0454 0.099   138 THR   B N    
2997 C  CA   . THR   B 139 ? 0.7986 0.5576 0.1532 -0.0316 -0.037  0.0896  138 THR   B CA   
2998 C  C    . THR   B 139 ? 0.7868 0.5733 0.1458 -0.0543 -0.0527 0.0828  138 THR   B C    
2999 O  O    . THR   B 139 ? 0.7811 0.5818 0.1494 -0.0757 -0.0711 0.0795  138 THR   B O    
3000 C  CB   . THR   B 139 ? 0.8314 0.5608 0.1875 -0.0227 -0.0009 0.0881  138 THR   B CB   
3001 O  OG1  . THR   B 139 ? 0.8655 0.5719 0.2235 -0.0112 0.0112  0.0936  138 THR   B OG1  
3002 C  CG2  . THR   B 139 ? 0.8305 0.5592 0.202  -0.0487 0.0103  0.0741  138 THR   B CG2  
3003 N  N    . LYS   B 140 ? 0.7791 0.5755 0.1302 -0.0468 -0.0468 0.0831  139 LYS   B N    
3004 C  CA   . LYS   B 140 ? 0.7652 0.5886 0.1186 -0.0656 -0.0579 0.0776  139 LYS   B CA   
3005 C  C    . LYS   B 140 ? 0.7577 0.6053 0.1126 -0.0777 -0.0892 0.0815  139 LYS   B C    
3006 O  O    . LYS   B 140 ? 0.751  0.6157 0.1106 -0.1007 -0.1004 0.0779  139 LYS   B O    
3007 C  CB   . LYS   B 140 ? 0.7768 0.6078 0.123  -0.0497 -0.0449 0.0791  139 LYS   B CB   
3008 C  CG   . LYS   B 140 ? 0.808  0.6248 0.1561 -0.0543 -0.0173 0.0697  139 LYS   B CG   
3009 C  CD   . LYS   B 140 ? 0.8486 0.6861 0.1932 -0.0486 -0.0124 0.069   139 LYS   B CD   
3010 C  CE   . LYS   B 140 ? 0.9039 0.7246 0.249  -0.0526 0.0168  0.0577  139 LYS   B CE   
3011 N  NZ   . LYS   B 140 ? 0.9208 0.7682 0.2648 -0.0558 0.0178  0.0539  139 LYS   B NZ   
3012 N  N    . THR   B 141 ? 0.7615 0.6091 0.1114 -0.0626 -0.1024 0.0886  140 THR   B N    
3013 C  CA   . THR   B 141 ? 0.7594 0.6233 0.1117 -0.0735 -0.13   0.0914  140 THR   B CA   
3014 C  C    . THR   B 141 ? 0.762  0.6207 0.1232 -0.0938 -0.1399 0.0908  140 THR   B C    
3015 O  O    . THR   B 141 ? 0.7585 0.6339 0.1238 -0.1144 -0.1521 0.0909  140 THR   B O    
3016 C  CB   . THR   B 141 ? 0.7757 0.6354 0.1196 -0.0521 -0.1394 0.0955  140 THR   B CB   
3017 O  OG1  . THR   B 141 ? 0.7765 0.6545 0.1142 -0.0369 -0.1382 0.0963  140 THR   B OG1  
3018 C  CG2  . THR   B 141 ? 0.7797 0.6438 0.1274 -0.0641 -0.1644 0.0962  140 THR   B CG2  
3019 N  N    . PHE   B 142 ? 0.7672 0.605  0.132  -0.0876 -0.1315 0.0905  141 PHE   B N    
3020 C  CA   . PHE   B 142 ? 0.7694 0.6064 0.1455 -0.1033 -0.1407 0.0904  141 PHE   B CA   
3021 C  C    . PHE   B 142 ? 0.7466 0.5961 0.1296 -0.1247 -0.1361 0.0838  141 PHE   B C    
3022 O  O    . PHE   B 142 ? 0.7387 0.6021 0.1272 -0.1413 -0.1521 0.0858  141 PHE   B O    
3023 C  CB   . PHE   B 142 ? 0.7904 0.6055 0.1712 -0.0899 -0.1314 0.0915  141 PHE   B CB   
3024 C  CG   . PHE   B 142 ? 0.8206 0.6293 0.1972 -0.0789 -0.1476 0.0973  141 PHE   B CG   
3025 C  CD1  . PHE   B 142 ? 0.8478 0.6526 0.2096 -0.0603 -0.1492 0.0989  141 PHE   B CD1  
3026 C  CD2  . PHE   B 142 ? 0.8359 0.6444 0.223  -0.0871 -0.162  0.1004  141 PHE   B CD2  
3027 C  CE1  . PHE   B 142 ? 0.8657 0.664  0.2223 -0.052  -0.1641 0.1007  141 PHE   B CE1  
3028 C  CE2  . PHE   B 142 ? 0.8562 0.6551 0.239  -0.0774 -0.1753 0.104   141 PHE   B CE2  
3029 C  CZ   . PHE   B 142 ? 0.8645 0.6573 0.2315 -0.0609 -0.176  0.1028  141 PHE   B CZ   
3030 N  N    . GLU   B 143 ? 0.7367 0.5816 0.1178 -0.1234 -0.1143 0.076   142 GLU   B N    
3031 C  CA   . GLU   B 143 ? 0.7263 0.5819 0.1117 -0.1437 -0.1071 0.0653  142 GLU   B CA   
3032 C  C    . GLU   B 143 ? 0.7394 0.6218 0.1182 -0.1606 -0.1225 0.0662  142 GLU   B C    
3033 O  O    . GLU   B 143 ? 0.7386 0.6364 0.1194 -0.1802 -0.1273 0.0602  142 GLU   B O    
3034 C  CB   . GLU   B 143 ? 0.7224 0.561  0.1059 -0.1366 -0.0772 0.0559  142 GLU   B CB   
3035 C  CG   . GLU   B 143 ? 0.714  0.5293 0.1096 -0.1336 -0.0582 0.0503  142 GLU   B CG   
3036 C  CD   . GLU   B 143 ? 0.7098 0.4976 0.103  -0.1209 -0.0251 0.0452  142 GLU   B CD   
3037 O  OE1  . GLU   B 143 ? 0.6951 0.4821 0.0764 -0.1106 -0.0166 0.0465  142 GLU   B OE1  
3038 O  OE2  . GLU   B 143 ? 0.7223 0.4888 0.1271 -0.1203 -0.0064 0.0408  142 GLU   B OE2  
3039 N  N    . ILE   B 144 ? 0.7462 0.6367 0.1172 -0.1534 -0.1302 0.0736  143 ILE   B N    
3040 C  CA   . ILE   B 144 ? 0.7502 0.6657 0.1155 -0.1686 -0.1417 0.0761  143 ILE   B CA   
3041 C  C    . ILE   B 144 ? 0.7525 0.6761 0.1196 -0.1761 -0.1666 0.0881  143 ILE   B C    
3042 O  O    . ILE   B 144 ? 0.7504 0.6896 0.1152 -0.1938 -0.1775 0.0917  143 ILE   B O    
3043 C  CB   . ILE   B 144 ? 0.7553 0.678  0.1154 -0.1574 -0.1309 0.0753  143 ILE   B CB   
3044 C  CG1  . ILE   B 144 ? 0.7743 0.6887 0.1316 -0.1534 -0.1044 0.0637  143 ILE   B CG1  
3045 C  CG2  . ILE   B 144 ? 0.7496 0.699  0.1072 -0.1706 -0.1432 0.0805  143 ILE   B CG2  
3046 C  CD1  . ILE   B 144 ? 0.7932 0.7085 0.1478 -0.1337 -0.0909 0.0649  143 ILE   B CD1  
3047 N  N    . ASN   B 145 ? 0.7561 0.6677 0.1257 -0.162  -0.1745 0.0941  144 ASN   B N    
3048 C  CA   . ASN   B 145 ? 0.7628 0.6751 0.1349 -0.1671 -0.1954 0.1039  144 ASN   B CA   
3049 C  C    . ASN   B 145 ? 0.7673 0.6722 0.1448 -0.1737 -0.2069 0.1097  144 ASN   B C    
3050 O  O    . ASN   B 145 ? 0.7666 0.6738 0.145  -0.1824 -0.2226 0.1195  144 ASN   B O    
3051 C  CB   . ASN   B 145 ? 0.7857 0.6871 0.1576 -0.1499 -0.1995 0.1045  144 ASN   B CB   
3052 C  CG   . ASN   B 145 ? 0.8299 0.7456 0.1986 -0.1417 -0.1932 0.1009  144 ASN   B CG   
3053 O  OD1  . ASN   B 145 ? 0.8371 0.7709 0.2049 -0.15   -0.1856 0.0989  144 ASN   B OD1  
3054 N  ND2  . ASN   B 145 ? 0.8419 0.752  0.2083 -0.1237 -0.196  0.0994  144 ASN   B ND2  
3055 N  N    . ILE   B 146 ? 0.7685 0.6645 0.1518 -0.1689 -0.1986 0.1047  145 ILE   B N    
3056 C  CA   . ILE   B 146 ? 0.769  0.6637 0.1611 -0.1733 -0.2102 0.1106  145 ILE   B CA   
3057 C  C    . ILE   B 146 ? 0.7648 0.6691 0.1651 -0.1805 -0.2017 0.1023  145 ILE   B C    
3058 O  O    . ILE   B 146 ? 0.7607 0.6817 0.1645 -0.1921 -0.2136 0.1067  145 ILE   B O    
3059 C  CB   . ILE   B 146 ? 0.7786 0.6513 0.1761 -0.1572 -0.2159 0.1155  145 ILE   B CB   
3060 C  CG1  . ILE   B 146 ? 0.7897 0.6627 0.1987 -0.1594 -0.2273 0.123   145 ILE   B CG1  
3061 C  CG2  . ILE   B 146 ? 0.7838 0.6393 0.1805 -0.1386 -0.1989 0.1077  145 ILE   B CG2  
3062 C  CD1  . ILE   B 146 ? 0.8026 0.69   0.2089 -0.1743 -0.2447 0.1355  145 ILE   B CD1  
3063 N  N    . LEU   B 147 ? 0.7666 0.662  0.1699 -0.1747 -0.1813 0.0904  146 LEU   B N    
3064 C  CA   . LEU   B 147 ? 0.7706 0.6753 0.1846 -0.1852 -0.1718 0.079   146 LEU   B CA   
3065 C  C    . LEU   B 147 ? 0.7768 0.7076 0.1826 -0.2055 -0.176  0.0731  146 LEU   B C    
3066 O  O    . LEU   B 147 ? 0.7753 0.7266 0.188  -0.2185 -0.1839 0.0693  146 LEU   B O    
3067 C  CB   . LEU   B 147 ? 0.78   0.6645 0.1979 -0.1759 -0.1452 0.0677  146 LEU   B CB   
3068 C  CG   . LEU   B 147 ? 0.8093 0.6711 0.2364 -0.1576 -0.1378 0.0719  146 LEU   B CG   
3069 C  CD1  . LEU   B 147 ? 0.8282 0.6664 0.2544 -0.1462 -0.1089 0.0646  146 LEU   B CD1  
3070 C  CD2  . LEU   B 147 ? 0.8059 0.678  0.2535 -0.1638 -0.1455 0.0719  146 LEU   B CD2  
3071 N  N    . GLY   B 148 ? 0.7792 0.7121 0.17   -0.2073 -0.1714 0.0725  147 GLY   B N    
3072 C  CA   . GLY   B 148 ? 0.7768 0.7333 0.1555 -0.2248 -0.1732 0.0674  147 GLY   B CA   
3073 C  C    . GLY   B 148 ? 0.7775 0.7549 0.1511 -0.2349 -0.1966 0.0814  147 GLY   B C    
3074 O  O    . GLY   B 148 ? 0.7795 0.7809 0.1464 -0.2499 -0.202  0.0771  147 GLY   B O    
3075 N  N    . HIS   B 149 ? 0.7805 0.7476 0.1564 -0.2262 -0.2101 0.098   148 HIS   B N    
3076 C  CA   . HIS   B 149 ? 0.7857 0.764  0.1579 -0.2322 -0.2307 0.1153  148 HIS   B CA   
3077 C  C    . HIS   B 149 ? 0.7729 0.7653 0.1544 -0.235  -0.2417 0.1172  148 HIS   B C    
3078 O  O    . HIS   B 149 ? 0.7766 0.7842 0.1519 -0.2406 -0.2572 0.1313  148 HIS   B O    
3079 C  CB   . HIS   B 149 ? 0.8159 0.7722 0.1922 -0.221  -0.2393 0.129   148 HIS   B CB   
3080 C  CG   . HIS   B 149 ? 0.8677 0.8211 0.2359 -0.2227 -0.2365 0.1319  148 HIS   B CG   
3081 N  ND1  . HIS   B 149 ? 0.9005 0.8389 0.2716 -0.2186 -0.2461 0.1429  148 HIS   B ND1  
3082 C  CD2  . HIS   B 149 ? 0.887  0.8521 0.2469 -0.2281 -0.2248 0.124   148 HIS   B CD2  
3083 C  CE1  . HIS   B 149 ? 0.9102 0.8553 0.2766 -0.223  -0.241  0.141   148 HIS   B CE1  
3084 N  NE2  . HIS   B 149 ? 0.9059 0.8678 0.2658 -0.2275 -0.228  0.1307  148 HIS   B NE2  
3085 N  N    . PHE   B 150 ? 0.7619 0.75   0.1595 -0.2299 -0.2336 0.1052  149 PHE   B N    
3086 C  CA   . PHE   B 150 ? 0.7572 0.7651 0.1689 -0.233  -0.2432 0.1045  149 PHE   B CA   
3087 C  C    . PHE   B 150 ? 0.7589 0.7985 0.1645 -0.251  -0.2416 0.0893  149 PHE   B C    
3088 O  O    . PHE   B 150 ? 0.7483 0.8177 0.1516 -0.2581 -0.2581 0.0953  149 PHE   B O    
3089 C  CB   . PHE   B 150 ? 0.7561 0.748  0.1908 -0.2215 -0.233  0.0968  149 PHE   B CB   
3090 C  CG   . PHE   B 150 ? 0.7711 0.743  0.2149 -0.2042 -0.2414 0.1124  149 PHE   B CG   
3091 C  CD1  . PHE   B 150 ? 0.7952 0.7354 0.2331 -0.1909 -0.2341 0.1157  149 PHE   B CD1  
3092 C  CD2  . PHE   B 150 ? 0.7747 0.7609 0.233  -0.2002 -0.2563 0.1228  149 PHE   B CD2  
3093 C  CE1  . PHE   B 150 ? 0.8096 0.73   0.2537 -0.1757 -0.2412 0.1269  149 PHE   B CE1  
3094 C  CE2  . PHE   B 150 ? 0.789  0.7534 0.2554 -0.1833 -0.2618 0.1357  149 PHE   B CE2  
3095 C  CZ   . PHE   B 150 ? 0.7994 0.7297 0.2579 -0.1719 -0.2538 0.1366  149 PHE   B CZ   
3096 N  N    . TRP   B 151 ? 0.7706 0.8041 0.1718 -0.2577 -0.2217 0.0696  150 TRP   B N    
3097 C  CA   . TRP   B 151 ? 0.7757 0.8366 0.1706 -0.2762 -0.2179 0.0502  150 TRP   B CA   
3098 C  C    . TRP   B 151 ? 0.7943 0.8797 0.1629 -0.287  -0.229  0.0568  150 TRP   B C    
3099 O  O    . TRP   B 151 ? 0.7963 0.9156 0.1591 -0.3002 -0.2387 0.0489  150 TRP   B O    
3100 C  CB   . TRP   B 151 ? 0.7782 0.821  0.1755 -0.2802 -0.1906 0.0265  150 TRP   B CB   
3101 C  CG   . TRP   B 151 ? 0.7884 0.7945 0.2018 -0.2643 -0.1726 0.0257  150 TRP   B CG   
3102 C  CD1  . TRP   B 151 ? 0.8112 0.7884 0.2176 -0.2541 -0.1522 0.0231  150 TRP   B CD1  
3103 C  CD2  . TRP   B 151 ? 0.7807 0.7775 0.2188 -0.2555 -0.1719 0.0279  150 TRP   B CD2  
3104 N  NE1  . TRP   B 151 ? 0.8174 0.767  0.2393 -0.2389 -0.1394 0.0245  150 TRP   B NE1  
3105 C  CE2  . TRP   B 151 ? 0.8006 0.7607 0.2421 -0.2403 -0.1502 0.027   150 TRP   B CE2  
3106 C  CE3  . TRP   B 151 ? 0.7718 0.7897 0.2297 -0.2575 -0.187  0.0314  150 TRP   B CE3  
3107 C  CZ2  . TRP   B 151 ? 0.8029 0.7452 0.2643 -0.2282 -0.1419 0.0293  150 TRP   B CZ2  
3108 C  CZ3  . TRP   B 151 ? 0.7767 0.7777 0.2576 -0.2454 -0.1789 0.0333  150 TRP   B CZ3  
3109 C  CH2  . TRP   B 151 ? 0.7876 0.7506 0.2693 -0.2319 -0.1558 0.0318  150 TRP   B CH2  
3110 N  N    . ILE   B 152 ? 0.8104 0.8824 0.1629 -0.2824 -0.2273 0.07    151 ILE   B N    
3111 C  CA   . ILE   B 152 ? 0.8289 0.924  0.1558 -0.293  -0.2354 0.0782  151 ILE   B CA   
3112 C  C    . ILE   B 152 ? 0.8445 0.9592 0.1685 -0.292  -0.2597 0.1002  151 ILE   B C    
3113 O  O    . ILE   B 152 ? 0.8399 0.9875 0.1482 -0.3023 -0.2697 0.0998  151 ILE   B O    
3114 C  CB   . ILE   B 152 ? 0.8441 0.9244 0.1582 -0.2903 -0.226  0.0864  151 ILE   B CB   
3115 C  CG1  . ILE   B 152 ? 0.8656 0.9251 0.186  -0.2852 -0.2026 0.0681  151 ILE   B CG1  
3116 C  CG2  . ILE   B 152 ? 0.8491 0.9558 0.1364 -0.3034 -0.2286 0.0903  151 ILE   B CG2  
3117 C  CD1  . ILE   B 152 ? 0.8947 0.9398 0.2124 -0.2771 -0.1962 0.0778  151 ILE   B CD1  
3118 N  N    . THR   B 153 ? 0.8589 0.9538 0.1983 -0.2782 -0.2686 0.118   152 THR   B N    
3119 C  CA   . THR   B 153 ? 0.8702 0.9779 0.2087 -0.2735 -0.2897 0.1413  152 THR   B CA   
3120 C  C    . THR   B 153 ? 0.868  1.0099 0.2162 -0.2763 -0.3014 0.1339  152 THR   B C    
3121 O  O    . THR   B 153 ? 0.8601 1.0309 0.196  -0.2781 -0.3179 0.1479  152 THR   B O    
3122 C  CB   . THR   B 153 ? 0.8927 0.9671 0.2463 -0.2577 -0.2937 0.1587  152 THR   B CB   
3123 O  OG1  . THR   B 153 ? 0.9126 0.9593 0.2614 -0.2564 -0.2821 0.159   152 THR   B OG1  
3124 C  CG2  . THR   B 153 ? 0.9    0.9796 0.2487 -0.252  -0.312  0.1866  152 THR   B CG2  
3125 N  N    . LYS   B 154 ? 0.875  1.0154 0.2461 -0.2765 -0.2922 0.1124  153 LYS   B N    
3126 C  CA   . LYS   B 154 ? 0.8743 1.0489 0.2634 -0.2814 -0.3004 0.0994  153 LYS   B CA   
3127 C  C    . LYS   B 154 ? 0.8799 1.0954 0.2502 -0.2998 -0.3044 0.0831  153 LYS   B C    
3128 O  O    . LYS   B 154 ? 0.8681 1.1252 0.2444 -0.3038 -0.3209 0.0809  153 LYS   B O    
3129 C  CB   . LYS   B 154 ? 0.8964 1.0527 0.3135 -0.2807 -0.2822 0.0773  153 LYS   B CB   
3130 C  CG   . LYS   B 154 ? 0.9278 1.0785 0.3756 -0.2661 -0.2874 0.0859  153 LYS   B CG   
3131 C  CD   . LYS   B 154 ? 0.9604 1.1398 0.4349 -0.2765 -0.284  0.0628  153 LYS   B CD   
3132 C  CE   . LYS   B 154 ? 1.005  1.1594 0.5104 -0.2659 -0.2693 0.0582  153 LYS   B CE   
3133 N  NZ   . LYS   B 154 ? 1.0219 1.1957 0.5526 -0.2814 -0.257  0.0302  153 LYS   B NZ   
3134 N  N    . ALA   B 155 ? 0.8973 1.1038 0.2459 -0.3106 -0.2891 0.0696  154 ALA   B N    
3135 C  CA   . ALA   B 155 ? 0.9072 1.1496 0.2337 -0.3286 -0.2903 0.0509  154 ALA   B CA   
3136 C  C    . ALA   B 155 ? 0.9173 1.1814 0.2085 -0.3295 -0.3045 0.0729  154 ALA   B C    
3137 O  O    . ALA   B 155 ? 0.9187 1.224  0.19   -0.341  -0.3141 0.0636  154 ALA   B O    
3138 C  CB   . ALA   B 155 ? 0.9216 1.143  0.2426 -0.3388 -0.2639 0.0236  154 ALA   B CB   
3139 N  N    . LEU   B 156 ? 0.9224 1.1597 0.2052 -0.3182 -0.3052 0.1014  155 LEU   B N    
3140 C  CA   . LEU   B 156 ? 0.9309 1.184  0.1814 -0.3192 -0.3152 0.1252  155 LEU   B CA   
3141 C  C    . LEU   B 156 ? 0.9502 1.2173 0.2024 -0.3066 -0.3384 0.1562  155 LEU   B C    
3142 O  O    . LEU   B 156 ? 0.9562 1.2473 0.1803 -0.3074 -0.3494 0.1751  155 LEU   B O    
3143 C  CB   . LEU   B 156 ? 0.9317 1.1525 0.1699 -0.3185 -0.3002 0.1367  155 LEU   B CB   
3144 C  CG   . LEU   B 156 ? 0.9357 1.142  0.1725 -0.3266 -0.2762 0.1103  155 LEU   B CG   
3145 C  CD1  . LEU   B 156 ? 0.9477 1.136  0.1717 -0.3262 -0.2653 0.1243  155 LEU   B CD1  
3146 C  CD2  . LEU   B 156 ? 0.9359 1.1737 0.1539 -0.3417 -0.271  0.0832  155 LEU   B CD2  
3147 N  N    . LEU   B 157 ? 0.9586 1.2126 0.2428 -0.294  -0.3448 0.1611  156 LEU   B N    
3148 C  CA   . LEU   B 157 ? 0.9777 1.2408 0.2694 -0.2785 -0.3646 0.1895  156 LEU   B CA   
3149 C  C    . LEU   B 157 ? 0.9926 1.3142 0.2772 -0.2794 -0.3857 0.1905  156 LEU   B C    
3150 O  O    . LEU   B 157 ? 0.995  1.3284 0.2664 -0.2676 -0.401  0.2213  156 LEU   B O    
3151 C  CB   . LEU   B 157 ? 0.9751 1.2087 0.3047 -0.2645 -0.3623 0.1897  156 LEU   B CB   
3152 C  CG   . LEU   B 157 ? 0.9875 1.2153 0.3297 -0.2447 -0.3776 0.2198  156 LEU   B CG   
3153 C  CD1  . LEU   B 157 ? 1.01   1.2124 0.3286 -0.2391 -0.3793 0.2518  156 LEU   B CD1  
3154 C  CD2  . LEU   B 157 ? 0.9927 1.1881 0.3695 -0.2324 -0.3706 0.2146  156 LEU   B CD2  
3155 N  N    . PRO   B 158 ? 0.9987 1.3581 0.2925 -0.292  -0.3875 0.1587  157 PRO   B N    
3156 C  CA   . PRO   B 158 ? 0.9958 1.4169 0.286  -0.2916 -0.411  0.1597  157 PRO   B CA   
3157 C  C    . PRO   B 158 ? 1.0215 1.4736 0.2664 -0.292  -0.4237 0.1799  157 PRO   B C    
3158 O  O    . PRO   B 158 ? 1.0149 1.498  0.2551 -0.2778 -0.4448 0.2052  157 PRO   B O    
3159 C  CB   . PRO   B 158 ? 0.9888 1.4387 0.2954 -0.3111 -0.4055 0.1156  157 PRO   B CB   
3160 C  CG   . PRO   B 158 ? 1.0002 1.3981 0.3306 -0.3142 -0.3804 0.0983  157 PRO   B CG   
3161 C  CD   . PRO   B 158 ? 0.9972 1.3452 0.3081 -0.3064 -0.3684 0.1208  157 PRO   B CD   
3162 N  N    . SER   B 159 ? 1.0468 1.491  0.258  -0.3062 -0.41   0.1706  158 SER   B N    
3163 C  CA   . SER   B 159 ? 1.0693 1.5406 0.2337 -0.3068 -0.4184 0.1903  158 SER   B CA   
3164 C  C    . SER   B 159 ? 1.099  1.539  0.2533 -0.2886 -0.4211 0.2374  158 SER   B C    
3165 O  O    . SER   B 159 ? 1.1102 1.5784 0.2378 -0.279  -0.4365 0.2654  158 SER   B O    
3166 C  CB   . SER   B 159 ? 1.0985 1.5641 0.2325 -0.3256 -0.3991 0.1684  158 SER   B CB   
3167 O  OG   . SER   B 159 ? 1.1344 1.6157 0.2224 -0.3245 -0.4023 0.1927  158 SER   B OG   
3168 N  N    . MET   B 160 ? 1.1128 1.4948 0.2882 -0.2838 -0.4059 0.246   159 MET   B N    
3169 C  CA   . MET   B 160 ? 1.1323 1.4779 0.3037 -0.2689 -0.4061 0.2869  159 MET   B CA   
3170 C  C    . MET   B 160 ? 1.1388 1.4986 0.3265 -0.2476 -0.4267 0.3115  159 MET   B C    
3171 O  O    . MET   B 160 ? 1.1488 1.5094 0.3161 -0.2348 -0.435  0.3481  159 MET   B O    
3172 C  CB   . MET   B 160 ? 1.1356 1.4214 0.3314 -0.2692 -0.3876 0.2837  159 MET   B CB   
3173 C  CG   . MET   B 160 ? 1.1394 1.41   0.3203 -0.2859 -0.3671 0.2668  159 MET   B CG   
3174 S  SD   . MET   B 160 ? 1.0755 1.2924 0.2926 -0.285  -0.3498 0.2505  159 MET   B SD   
3175 C  CE   . MET   B 160 ? 1.0504 1.2555 0.2459 -0.3005 -0.3284 0.243   159 MET   B CE   
3176 N  N    . ILE   B 161 ? 1.1282 1.5006 0.3528 -0.2432 -0.4337 0.2919  160 ILE   B N    
3177 C  CA   . ILE   B 161 ? 1.1249 1.5174 0.372  -0.2224 -0.4527 0.3101  160 ILE   B CA   
3178 C  C    . ILE   B 161 ? 1.1272 1.5821 0.346  -0.2167 -0.4746 0.3256  160 ILE   B C    
3179 O  O    . ILE   B 161 ? 1.125  1.5836 0.3381 -0.1952 -0.4872 0.3628  160 ILE   B O    
3180 C  CB   . ILE   B 161 ? 1.1097 1.5121 0.4015 -0.2246 -0.4522 0.2781  160 ILE   B CB   
3181 C  CG1  . ILE   B 161 ? 1.1347 1.4734 0.453  -0.2208 -0.4337 0.2745  160 ILE   B CG1  
3182 C  CG2  . ILE   B 161 ? 1.0919 1.5404 0.4077 -0.2076 -0.4743 0.2875  160 ILE   B CG2  
3183 C  CD1  . ILE   B 161 ? 1.1633 1.4615 0.489  -0.1986 -0.4358 0.3104  160 ILE   B CD1  
3184 N  N    . LYS   B 162 ? 1.1329 1.6343 0.3312 -0.2353 -0.4778 0.2977  161 LYS   B N    
3185 C  CA   . LYS   B 162 ? 1.144  1.7119 0.3109 -0.2328 -0.4991 0.3053  161 LYS   B CA   
3186 C  C    . LYS   B 162 ? 1.1926 1.7489 0.3136 -0.2224 -0.4991 0.3477  161 LYS   B C    
3187 O  O    . LYS   B 162 ? 1.2149 1.802  0.3213 -0.2023 -0.5178 0.3802  161 LYS   B O    
3188 C  CB   . LYS   B 162 ? 1.1507 1.7596 0.302  -0.2591 -0.497  0.2607  161 LYS   B CB   
3189 C  CG   . LYS   B 162 ? 1.1709 1.8093 0.3655 -0.2693 -0.5019 0.2205  161 LYS   B CG   
3190 C  CD   . LYS   B 162 ? 1.2207 1.8877 0.4004 -0.2974 -0.4951 0.1743  161 LYS   B CD   
3191 C  CE   . LYS   B 162 ? 1.2764 1.9013 0.4902 -0.3133 -0.471  0.1387  161 LYS   B CE   
3192 N  NZ   . LYS   B 162 ? 1.2822 1.902  0.5512 -0.3049 -0.474  0.1341  161 LYS   B NZ   
3193 N  N    . ARG   B 163 ? 1.2123 1.724  0.3121 -0.2349 -0.4769 0.3491  162 ARG   B N    
3194 C  CA   . ARG   B 163 ? 1.2356 1.732  0.2929 -0.2288 -0.4717 0.3878  162 ARG   B CA   
3195 C  C    . ARG   B 163 ? 1.2439 1.6837 0.3144 -0.2098 -0.4661 0.4298  162 ARG   B C    
3196 O  O    . ARG   B 163 ? 1.273  1.699  0.311  -0.2028 -0.4619 0.4667  162 ARG   B O    
3197 C  CB   . ARG   B 163 ? 1.2779 1.7563 0.3088 -0.2517 -0.4491 0.3701  162 ARG   B CB   
3198 C  CG   . ARG   B 163 ? 1.3233 1.8542 0.3368 -0.2704 -0.4524 0.3281  162 ARG   B CG   
3199 C  CD   . ARG   B 163 ? 1.3837 1.8938 0.3804 -0.2921 -0.4274 0.3038  162 ARG   B CD   
3200 N  NE   . ARG   B 163 ? 1.407  1.9565 0.3992 -0.3102 -0.4281 0.2562  162 ARG   B NE   
3201 C  CZ   . ARG   B 163 ? 1.4256 2.0287 0.3764 -0.3176 -0.4369 0.245   162 ARG   B CZ   
3202 N  NH1  . ARG   B 163 ? 1.4278 2.0545 0.3356 -0.3065 -0.4465 0.2808  162 ARG   B NH1  
3203 N  NH2  . ARG   B 163 ? 1.4135 2.0462 0.3646 -0.3358 -0.4354 0.1978  162 ARG   B NH2  
3204 N  N    . ASN   B 164 ? 1.2202 1.6246 0.3371 -0.2022 -0.4639 0.4236  163 ASN   B N    
3205 C  CA   . ASN   B 164 ? 1.2192 1.5629 0.3543 -0.1863 -0.4564 0.4551  163 ASN   B CA   
3206 C  C    . ASN   B 164 ? 1.2238 1.5176 0.3386 -0.199  -0.4339 0.468   163 ASN   B C    
3207 O  O    . ASN   B 164 ? 1.2409 1.5027 0.3429 -0.1882 -0.4292 0.5068  163 ASN   B O    
3208 C  CB   . ASN   B 164 ? 1.2276 1.5861 0.357  -0.1578 -0.4736 0.4974  163 ASN   B CB   
3209 C  CG   . ASN   B 164 ? 1.2698 1.5673 0.4262 -0.1391 -0.4672 0.5238  163 ASN   B CG   
3210 O  OD1  . ASN   B 164 ? 1.2714 1.5485 0.4685 -0.1348 -0.466  0.506   163 ASN   B OD1  
3211 N  ND2  . ASN   B 164 ? 1.2952 1.56   0.4285 -0.1278 -0.461  0.5667  163 ASN   B ND2  
3212 N  N    . HIS   B 165 ? 1.2066 1.4979 0.3174 -0.2221 -0.4193 0.4359  164 HIS   B N    
3213 C  CA   . HIS   B 165 ? 1.2149 1.4694 0.3098 -0.2362 -0.398  0.4434  164 HIS   B CA   
3214 C  C    . HIS   B 165 ? 1.2005 1.4424 0.3133 -0.2552 -0.3829 0.4028  164 HIS   B C    
3215 O  O    . HIS   B 165 ? 1.1991 1.4781 0.3036 -0.2665 -0.3838 0.3719  164 HIS   B O    
3216 C  CB   . HIS   B 165 ? 1.2314 1.5192 0.2767 -0.2421 -0.3968 0.46    164 HIS   B CB   
3217 C  CG   . HIS   B 165 ? 1.2676 1.5238 0.2971 -0.2575 -0.3733 0.4685  164 HIS   B CG   
3218 N  ND1  . HIS   B 165 ? 1.2989 1.4982 0.345  -0.2559 -0.3604 0.4921  164 HIS   B ND1  
3219 C  CD2  . HIS   B 165 ? 1.2844 1.5614 0.2844 -0.2747 -0.3605 0.4563  164 HIS   B CD2  
3220 C  CE1  . HIS   B 165 ? 1.3147 1.5048 0.3441 -0.273  -0.3409 0.4931  164 HIS   B CE1  
3221 N  NE2  . HIS   B 165 ? 1.31   1.5457 0.311  -0.2836 -0.3397 0.473   164 HIS   B NE2  
3222 N  N    . GLY   B 166 ? 1.1832 1.3732 0.3192 -0.258  -0.3689 0.4034  165 GLY   B N    
3223 C  CA   . GLY   B 166 ? 1.1647 1.3382 0.3186 -0.2722 -0.3538 0.3703  165 GLY   B CA   
3224 C  C    . GLY   B 166 ? 1.1564 1.2753 0.3344 -0.272  -0.3425 0.3776  165 GLY   B C    
3225 O  O    . GLY   B 166 ? 1.1741 1.2642 0.3521 -0.2643 -0.3433 0.4085  165 GLY   B O    
3226 N  N    . HIS   B 167 ? 1.1257 1.2299 0.3239 -0.2801 -0.3314 0.3487  166 HIS   B N    
3227 C  CA   . HIS   B 167 ? 1.113  1.1716 0.3349 -0.2809 -0.322  0.3491  166 HIS   B CA   
3228 C  C    . HIS   B 167 ? 1.0773 1.1323 0.3201 -0.2838 -0.3147 0.3141  166 HIS   B C    
3229 O  O    . HIS   B 167 ? 1.0734 1.146  0.3076 -0.2951 -0.3039 0.2957  166 HIS   B O    
3230 C  CB   . HIS   B 167 ? 1.1338 1.1783 0.3433 -0.2944 -0.3082 0.3656  166 HIS   B CB   
3231 C  CG   . HIS   B 167 ? 1.1673 1.1643 0.3988 -0.294  -0.3034 0.3768  166 HIS   B CG   
3232 N  ND1  . HIS   B 167 ? 1.2002 1.1739 0.4234 -0.2968 -0.2992 0.4092  166 HIS   B ND1  
3233 C  CD2  . HIS   B 167 ? 1.1758 1.1451 0.4357 -0.2915 -0.3016 0.3588  166 HIS   B CD2  
3234 C  CE1  . HIS   B 167 ? 1.2077 1.14   0.4565 -0.2979 -0.295  0.4071  166 HIS   B CE1  
3235 N  NE2  . HIS   B 167 ? 1.1973 1.1273 0.4672 -0.2942 -0.2975 0.377   166 HIS   B NE2  
3236 N  N    . ILE   B 168 ? 1.0508 1.082  0.3196 -0.2721 -0.319  0.3059  167 ILE   B N    
3237 C  CA   . ILE   B 168 ? 1.03   1.0552 0.3169 -0.2718 -0.3112 0.2759  167 ILE   B CA   
3238 C  C    . ILE   B 168 ? 1.0188 1.0096 0.3204 -0.2737 -0.3026 0.2732  167 ILE   B C    
3239 O  O    . ILE   B 168 ? 1.0249 0.9845 0.3416 -0.2647 -0.3071 0.2809  167 ILE   B O    
3240 C  CB   . ILE   B 168 ? 1.023  1.0517 0.3275 -0.2586 -0.3192 0.2636  167 ILE   B CB   
3241 C  CG1  . ILE   B 168 ? 1.0224 1.0938 0.3146 -0.2604 -0.3281 0.2611  167 ILE   B CG1  
3242 C  CG2  . ILE   B 168 ? 1.0236 1.0418 0.3444 -0.2571 -0.3082 0.2358  167 ILE   B CG2  
3243 C  CD1  . ILE   B 168 ? 1.0318 1.1319 0.3072 -0.2751 -0.3186 0.2398  167 ILE   B CD1  
3244 N  N    . VAL   B 169 ? 1      0.9991 0.2974 -0.2851 -0.2903 0.2612  168 VAL   B N    
3245 C  CA   . VAL   B 169 ? 0.9923 0.9698 0.3043 -0.2886 -0.2827 0.2556  168 VAL   B CA   
3246 C  C    . VAL   B 169 ? 0.9734 0.9456 0.3007 -0.2795 -0.2781 0.2299  168 VAL   B C    
3247 O  O    . VAL   B 169 ? 0.9646 0.9564 0.2877 -0.2813 -0.269  0.2127  168 VAL   B O    
3248 C  CB   . VAL   B 169 ? 0.9988 0.9906 0.3014 -0.305  -0.2717 0.2603  168 VAL   B CB   
3249 C  CG1  . VAL   B 169 ? 1.0083 0.9855 0.3305 -0.309  -0.2653 0.2513  168 VAL   B CG1  
3250 C  CG2  . VAL   B 169 ? 1.0031 0.9941 0.2898 -0.3128 -0.2741 0.2896  168 VAL   B CG2  
3251 N  N    . THR   B 170 ? 0.9672 0.9111 0.3106 -0.2687 -0.2831 0.2279  169 THR   B N    
3252 C  CA   . THR   B 170 ? 0.9615 0.8976 0.3168 -0.2575 -0.2786 0.2068  169 THR   B CA   
3253 C  C    . THR   B 170 ? 0.9511 0.8792 0.315  -0.2613 -0.274  0.1999  169 THR   B C    
3254 O  O    . THR   B 170 ? 0.9553 0.8607 0.3274 -0.2626 -0.2796 0.2068  169 THR   B O    
3255 C  CB   . THR   B 170 ? 0.9817 0.895  0.3475 -0.2418 -0.2864 0.2074  169 THR   B CB   
3256 O  OG1  . THR   B 170 ? 0.9884 0.9167 0.3501 -0.2389 -0.2917 0.2132  169 THR   B OG1  
3257 C  CG2  . THR   B 170 ? 0.9881 0.8917 0.3631 -0.2288 -0.2803 0.188   169 THR   B CG2  
3258 N  N    . VAL   B 171 ? 0.9346 0.8824 0.2978 -0.2629 -0.2635 0.1857  170 VAL   B N    
3259 C  CA   . VAL   B 171 ? 0.9275 0.8768 0.3012 -0.2654 -0.2604 0.1782  170 VAL   B CA   
3260 C  C    . VAL   B 171 ? 0.9227 0.8579 0.3048 -0.2479 -0.2614 0.1632  170 VAL   B C    
3261 O  O    . VAL   B 171 ? 0.9239 0.8664 0.3034 -0.2359 -0.2533 0.1512  170 VAL   B O    
3262 C  CB   . VAL   B 171 ? 0.9258 0.906  0.2965 -0.2745 -0.2486 0.1731  170 VAL   B CB   
3263 C  CG1  . VAL   B 171 ? 0.9249 0.9127 0.3111 -0.2762 -0.2474 0.1653  170 VAL   B CG1  
3264 C  CG2  . VAL   B 171 ? 0.9288 0.9224 0.2881 -0.2917 -0.2467 0.1891  170 VAL   B CG2  
3265 N  N    . ALA   B 172 ? 0.9154 0.8285 0.3062 -0.2463 -0.2703 0.1643  171 ALA   B N    
3266 C  CA   . ALA   B 172 ? 0.9176 0.8167 0.3131 -0.2298 -0.2726 0.1507  171 ALA   B CA   
3267 C  C    . ALA   B 172 ? 0.908  0.8132 0.3143 -0.2366 -0.2766 0.1425  171 ALA   B C    
3268 O  O    . ALA   B 172 ? 0.9089 0.8326 0.3209 -0.2537 -0.2746 0.1469  171 ALA   B O    
3269 C  CB   . ALA   B 172 ? 0.93   0.7976 0.3255 -0.2203 -0.2799 0.1557  171 ALA   B CB   
3270 N  N    . SER   B 173 ? 0.8934 0.7886 0.3023 -0.2236 -0.2814 0.1293  172 SER   B N    
3271 C  CA   . SER   B 173 ? 0.8774 0.7833 0.2974 -0.2301 -0.2874 0.1181  172 SER   B CA   
3272 C  C    . SER   B 173 ? 0.8826 0.7542 0.3051 -0.229  -0.2977 0.113   172 SER   B C    
3273 O  O    . SER   B 173 ? 0.8925 0.7345 0.3083 -0.2205 -0.2986 0.1196  172 SER   B O    
3274 C  CB   . SER   B 173 ? 0.8782 0.8093 0.2953 -0.2121 -0.2836 0.1043  172 SER   B CB   
3275 O  OG   . SER   B 173 ? 0.8819 0.8357 0.3105 -0.2161 -0.2903 0.0918  172 SER   B OG   
3276 N  N    . VAL   B 174 ? 0.8732 0.75   0.3067 -0.2377 -0.3052 0.0997  173 VAL   B N    
3277 C  CA   . VAL   B 174 ? 0.8852 0.729  0.3188 -0.235  -0.3139 0.0894  173 VAL   B CA   
3278 C  C    . VAL   B 174 ? 0.8959 0.7312 0.3135 -0.2063 -0.3145 0.0786  173 VAL   B C    
3279 O  O    . VAL   B 174 ? 0.9019 0.7069 0.315  -0.1994 -0.3195 0.0707  173 VAL   B O    
3280 C  CB   . VAL   B 174 ? 0.8796 0.7302 0.3298 -0.2541 -0.322  0.0745  173 VAL   B CB   
3281 C  CG1  . VAL   B 174 ? 0.8852 0.7302 0.351  -0.2827 -0.3184 0.0886  173 VAL   B CG1  
3282 C  CG2  . VAL   B 174 ? 0.8616 0.7598 0.3168 -0.2494 -0.3251 0.0587  173 VAL   B CG2  
3283 N  N    . CYS   B 175 ? 0.8969 0.7568 0.3054 -0.1896 -0.3071 0.0792  174 CYS   B N    
3284 C  CA   . CYS   B 175 ? 0.9147 0.769  0.3071 -0.162  -0.3015 0.0752  174 CYS   B CA   
3285 C  C    . CYS   B 175 ? 0.9431 0.769  0.3302 -0.1548 -0.2947 0.088   174 CYS   B C    
3286 O  O    . CYS   B 175 ? 0.9439 0.7665 0.3209 -0.1351 -0.2861 0.0878  174 CYS   B O    
3287 C  CB   . CYS   B 175 ? 0.9025 0.7911 0.2908 -0.1505 -0.293  0.0742  174 CYS   B CB   
3288 S  SG   . CYS   B 175 ? 0.8899 0.822  0.288  -0.1553 -0.3014 0.0603  174 CYS   B SG   
3289 N  N    . GLY   B 176 ? 0.9612 0.771  0.3565 -0.171  -0.2975 0.1001  175 GLY   B N    
3290 C  CA   . GLY   B 176 ? 0.9865 0.7734 0.3811 -0.1666 -0.2949 0.1129  175 GLY   B CA   
3291 C  C    . GLY   B 176 ? 1.0123 0.7629 0.4097 -0.1659 -0.3018 0.1123  175 GLY   B C    
3292 O  O    . GLY   B 176 ? 1.0181 0.7483 0.416  -0.1566 -0.3001 0.1209  175 GLY   B O    
3293 N  N    . HIS   B 177 ? 1.0234 0.7668 0.4247 -0.1759 -0.3091 0.1009  176 HIS   B N    
3294 C  CA   . HIS   B 177 ? 1.0496 0.7558 0.4535 -0.1774 -0.3145 0.0954  176 HIS   B CA   
3295 C  C    . HIS   B 177 ? 1.0625 0.7641 0.4567 -0.1638 -0.3182 0.0718  176 HIS   B C    
3296 O  O    . HIS   B 177 ? 1.0742 0.7418 0.4652 -0.1563 -0.3197 0.065   176 HIS   B O    
3297 C  CB   . HIS   B 177 ? 1.0641 0.7624 0.4814 -0.204  -0.3185 0.1001  176 HIS   B CB   
3298 C  CG   . HIS   B 177 ? 1.1016 0.7943 0.5239 -0.2137 -0.3149 0.1258  176 HIS   B CG   
3299 N  ND1  . HIS   B 177 ? 1.1397 0.7939 0.5651 -0.2125 -0.3148 0.1393  176 HIS   B ND1  
3300 C  CD2  . HIS   B 177 ? 1.1086 0.8306 0.5307 -0.2221 -0.3112 0.14    176 HIS   B CD2  
3301 C  CE1  . HIS   B 177 ? 1.1421 0.806  0.5684 -0.2197 -0.3122 0.1624  176 HIS   B CE1  
3302 N  NE2  . HIS   B 177 ? 1.1272 0.8317 0.5508 -0.2267 -0.3101 0.1625  176 HIS   B NE2  
3303 N  N    . GLU   B 178 ? 1.0614 0.7971 0.4492 -0.1583 -0.3191 0.0597  177 GLU   B N    
3304 C  CA   . GLU   B 178 ? 1.0812 0.8197 0.4553 -0.1425 -0.3235 0.0381  177 GLU   B CA   
3305 C  C    . GLU   B 178 ? 1.0734 0.8531 0.4383 -0.1291 -0.321  0.0339  177 GLU   B C    
3306 O  O    . GLU   B 178 ? 1.0638 0.8757 0.439  -0.1418 -0.3224 0.0362  177 GLU   B O    
3307 C  CB   . GLU   B 178 ? 1.1199 0.8475 0.501  -0.1593 -0.3348 0.0193  177 GLU   B CB   
3308 C  CG   . GLU   B 178 ? 1.2009 0.9443 0.5679 -0.1471 -0.3427 -0.006  177 GLU   B CG   
3309 C  CD   . GLU   B 178 ? 1.3057 1.0949 0.6835 -0.1615 -0.3521 -0.0181 177 GLU   B CD   
3310 O  OE1  . GLU   B 178 ? 1.305  1.1172 0.6991 -0.1769 -0.3492 -0.0047 177 GLU   B OE1  
3311 O  OE2  . GLU   B 178 ? 1.3538 1.1587 0.7234 -0.1566 -0.3624 -0.0416 177 GLU   B OE2  
3312 N  N    . GLY   B 179 ? 1.0761 0.8533 0.4217 -0.1023 -0.3155 0.0293  178 GLY   B N    
3313 C  CA   . GLY   B 179 ? 1.0745 0.8836 0.4083 -0.0841 -0.3098 0.0288  178 GLY   B CA   
3314 C  C    . GLY   B 179 ? 1.0696 0.9128 0.3991 -0.082  -0.3211 0.0119  178 GLY   B C    
3315 O  O    . GLY   B 179 ? 1.0787 0.9162 0.4026 -0.0831 -0.3326 -0.0063 178 GLY   B O    
3316 N  N    . ILE   B 180 ? 1.0534 0.9341 0.3852 -0.077  -0.3174 0.0168  179 ILE   B N    
3317 C  CA   . ILE   B 180 ? 1.0429 0.9664 0.3745 -0.0733 -0.3284 0.0031  179 ILE   B CA   
3318 C  C    . ILE   B 180 ? 1.0495 0.9933 0.359  -0.039  -0.3198 0.0069  179 ILE   B C    
3319 O  O    . ILE   B 180 ? 1.0556 0.9839 0.3574 -0.0252 -0.3022 0.0226  179 ILE   B O    
3320 C  CB   . ILE   B 180 ? 1.0281 0.9802 0.3871 -0.0996 -0.331  0.0076  179 ILE   B CB   
3321 C  CG1  . ILE   B 180 ? 1.0238 1.0088 0.3975 -0.1155 -0.3484 -0.0116 179 ILE   B CG1  
3322 C  CG2  . ILE   B 180 ? 1.0242 1.0008 0.3848 -0.0894 -0.3173 0.0223  179 ILE   B CG2  
3323 C  CD1  . ILE   B 180 ? 1.035  1.0096 0.4347 -0.1514 -0.3517 -0.0104 179 ILE   B CD1  
3324 N  N    . PRO   B 181 ? 1.0466 1.0241 0.3448 -0.024  -0.3311 -0.0069 180 PRO   B N    
3325 C  CA   . PRO   B 181 ? 1.0514 1.046  0.3261 0.0118  -0.3214 0.0005  180 PRO   B CA   
3326 C  C    . PRO   B 181 ? 1.046  1.0664 0.3324 0.0166  -0.309  0.0161  180 PRO   B C    
3327 O  O    . PRO   B 181 ? 1.0314 1.075  0.344  -0.0067 -0.314  0.0154  180 PRO   B O    
3328 C  CB   . PRO   B 181 ? 1.0483 1.0785 0.31   0.0234  -0.3407 -0.0195 180 PRO   B CB   
3329 C  CG   . PRO   B 181 ? 1.0519 1.0702 0.327  -0.0061 -0.3579 -0.0399 180 PRO   B CG   
3330 C  CD   . PRO   B 181 ? 1.0286 1.0311 0.3343 -0.038  -0.3529 -0.0302 180 PRO   B CD   
3331 N  N    . TYR   B 182 ? 1.0561 1.0692 0.323  0.0467  -0.2903 0.0303  181 TYR   B N    
3332 C  CA   . TYR   B 182 ? 1.0572 1.0846 0.3304 0.057   -0.2729 0.0458  181 TYR   B CA   
3333 C  C    . TYR   B 182 ? 1.057  1.0564 0.3472 0.0351  -0.2581 0.0564  181 TYR   B C    
3334 O  O    . TYR   B 182 ? 1.0621 1.0582 0.3525 0.0449  -0.2385 0.0685  181 TYR   B O    
3335 C  CB   . TYR   B 182 ? 1.0422 1.1264 0.3304 0.058   -0.2835 0.0415  181 TYR   B CB   
3336 C  CG   . TYR   B 182 ? 1.0568 1.1777 0.3328 0.0735  -0.3041 0.0269  181 TYR   B CG   
3337 C  CD1  . TYR   B 182 ? 1.0877 1.2048 0.3299 0.11    -0.2999 0.0304  181 TYR   B CD1  
3338 C  CD2  . TYR   B 182 ? 1.054  1.2138 0.352  0.0505  -0.3274 0.0088  181 TYR   B CD2  
3339 C  CE1  . TYR   B 182 ? 1.0958 1.25   0.3234 0.1248  -0.3206 0.0155  181 TYR   B CE1  
3340 C  CE2  . TYR   B 182 ? 1.06   1.2576 0.3478 0.0625  -0.3482 -0.0082 181 TYR   B CE2  
3341 C  CZ   . TYR   B 182 ? 1.0868 1.2829 0.3378 0.1004  -0.3458 -0.0053 181 TYR   B CZ   
3342 O  OH   . TYR   B 182 ? 1.0975 1.3345 0.3349 0.1133  -0.3678 -0.0234 181 TYR   B OH   
3343 N  N    . LEU   B 183 ? 1.0473 1.026  0.3504 0.0067  -0.2667 0.0516  182 LEU   B N    
3344 C  CA   . LEU   B 183 ? 1.0413 0.9978 0.3581 -0.0136 -0.2558 0.0611  182 LEU   B CA   
3345 C  C    . LEU   B 183 ? 1.0551 0.9677 0.3642 -0.0136 -0.2499 0.0644  182 LEU   B C    
3346 O  O    . LEU   B 183 ? 1.0579 0.955  0.3802 -0.0362 -0.2531 0.0668  182 LEU   B O    
3347 C  CB   . LEU   B 183 ? 1.024  0.9974 0.3648 -0.0466 -0.2688 0.0573  182 LEU   B CB   
3348 C  CG   . LEU   B 183 ? 1.0154 1.0358 0.3698 -0.0497 -0.2728 0.0544  182 LEU   B CG   
3349 C  CD1  . LEU   B 183 ? 1.0081 1.0416 0.3863 -0.0838 -0.2837 0.0512  182 LEU   B CD1  
3350 C  CD2  . LEU   B 183 ? 1.0193 1.0487 0.3722 -0.0361 -0.2527 0.0652  182 LEU   B CD2  
3351 N  N    . ILE   B 184 ? 1.0591 0.9537 0.3471 0.0129  -0.2406 0.0658  183 ILE   B N    
3352 C  CA   . ILE   B 184 ? 1.0648 0.9213 0.3484 0.0145  -0.2328 0.0691  183 ILE   B CA   
3353 C  C    . ILE   B 184 ? 1.0484 0.8901 0.3443 0.0049  -0.2156 0.0802  183 ILE   B C    
3354 O  O    . ILE   B 184 ? 1.0495 0.874  0.357  -0.0113 -0.2189 0.0816  183 ILE   B O    
3355 C  CB   . ILE   B 184 ? 1.0885 0.9292 0.3462 0.0443  -0.2253 0.068   183 ILE   B CB   
3356 C  CG1  . ILE   B 184 ? 1.0978 0.9606 0.3399 0.0554  -0.2431 0.0548  183 ILE   B CG1  
3357 C  CG2  . ILE   B 184 ? 1.1086 0.9139 0.3673 0.0419  -0.2206 0.0689  183 ILE   B CG2  
3358 C  CD1  . ILE   B 184 ? 1.1288 0.9797 0.34   0.0867  -0.2362 0.0535  183 ILE   B CD1  
3359 N  N    . PRO   B 185 ? 1.0317 0.8806 0.3267 0.0137  -0.1978 0.0871  184 PRO   B N    
3360 C  CA   . PRO   B 185 ? 1.0232 0.8593 0.3311 0.0007  -0.1827 0.0932  184 PRO   B CA   
3361 C  C    . PRO   B 185 ? 1.0073 0.8568 0.3335 -0.0298 -0.1953 0.0922  184 PRO   B C    
3362 O  O    . PRO   B 185 ? 1.0117 0.8493 0.3483 -0.0452 -0.1942 0.0949  184 PRO   B O    
3363 C  CB   . PRO   B 185 ? 1.0325 0.8729 0.3339 0.0174  -0.1612 0.0983  184 PRO   B CB   
3364 C  CG   . PRO   B 185 ? 1.0343 0.9029 0.3269 0.0311  -0.1709 0.096   184 PRO   B CG   
3365 C  CD   . PRO   B 185 ? 1.0211 0.8899 0.304  0.0362  -0.19   0.0892  184 PRO   B CD   
3366 N  N    . TYR   B 186 ? 0.983  0.8596 0.3132 -0.038  -0.2077 0.0888  185 TYR   B N    
3367 C  CA   . TYR   B 186 ? 0.9628 0.854  0.3083 -0.0659 -0.2181 0.0893  185 TYR   B CA   
3368 C  C    . TYR   B 186 ? 0.9446 0.821  0.2964 -0.0819 -0.2344 0.089   185 TYR   B C    
3369 O  O    . TYR   B 186 ? 0.9412 0.8131 0.302  -0.1007 -0.2363 0.0947  185 TYR   B O    
3370 C  CB   . TYR   B 186 ? 0.9532 0.8791 0.3034 -0.0684 -0.2249 0.0855  185 TYR   B CB   
3371 C  CG   . TYR   B 186 ? 0.9527 0.8947 0.3184 -0.0972 -0.2356 0.0864  185 TYR   B CG   
3372 C  CD1  . TYR   B 186 ? 0.9577 0.9092 0.3293 -0.111  -0.2259 0.0915  185 TYR   B CD1  
3373 C  CD2  . TYR   B 186 ? 0.9619 0.9094 0.3353 -0.1105 -0.2537 0.0815  185 TYR   B CD2  
3374 C  CE1  . TYR   B 186 ? 0.9629 0.9303 0.3459 -0.1359 -0.2336 0.0941  185 TYR   B CE1  
3375 C  CE2  . TYR   B 186 ? 0.967  0.9272 0.3548 -0.1369 -0.2606 0.0843  185 TYR   B CE2  
3376 C  CZ   . TYR   B 186 ? 0.9748 0.9458 0.3664 -0.1488 -0.2503 0.0918  185 TYR   B CZ   
3377 O  OH   . TYR   B 186 ? 0.9925 0.9763 0.3959 -0.1739 -0.2554 0.0963  185 TYR   B OH   
3378 N  N    . CYS   B 187 ? 0.9317 0.8004 0.2774 -0.0738 -0.2458 0.0823  186 CYS   B N    
3379 C  CA   . CYS   B 187 ? 0.9254 0.7742 0.2764 -0.0861 -0.2591 0.081   186 CYS   B CA   
3380 C  C    . CYS   B 187 ? 0.9094 0.7313 0.261  -0.0826 -0.2518 0.0881  186 CYS   B C    
3381 O  O    . CYS   B 187 ? 0.9098 0.7198 0.2711 -0.0973 -0.259  0.0935  186 CYS   B O    
3382 C  CB   . CYS   B 187 ? 0.9437 0.7888 0.286  -0.0765 -0.2709 0.0686  186 CYS   B CB   
3383 S  SG   . CYS   B 187 ? 0.9769 0.8616 0.3245 -0.0838 -0.2836 0.0574  186 CYS   B SG   
3384 N  N    . SER   B 188 ? 0.8923 0.7058 0.2352 -0.0629 -0.2366 0.0891  187 SER   B N    
3385 C  CA   . SER   B 188 ? 0.8845 0.6779 0.2323 -0.0597 -0.228  0.0947  187 SER   B CA   
3386 C  C    . SER   B 188 ? 0.8688 0.6714 0.2308 -0.0794 -0.2261 0.1021  187 SER   B C    
3387 O  O    . SER   B 188 ? 0.8773 0.6706 0.2492 -0.0866 -0.2304 0.1074  187 SER   B O    
3388 C  CB   . SER   B 188 ? 0.9032 0.6882 0.2406 -0.0369 -0.2086 0.0945  187 SER   B CB   
3389 O  OG   . SER   B 188 ? 0.9358 0.7008 0.2787 -0.0313 -0.2021 0.0974  187 SER   B OG   
3390 N  N    . SER   B 189 ? 0.8403 0.6633 0.2028 -0.0876 -0.2204 0.1022  188 SER   B N    
3391 C  CA   . SER   B 189 ? 0.8126 0.6472 0.1844 -0.1065 -0.2188 0.107   188 SER   B CA   
3392 C  C    . SER   B 189 ? 0.8013 0.6434 0.1787 -0.1267 -0.2358 0.1127  188 SER   B C    
3393 O  O    . SER   B 189 ? 0.8048 0.6479 0.1887 -0.1387 -0.2399 0.1198  188 SER   B O    
3394 C  CB   . SER   B 189 ? 0.8106 0.6614 0.1791 -0.1069 -0.2046 0.1037  188 SER   B CB   
3395 O  OG   . SER   B 189 ? 0.8223 0.6917 0.1881 -0.1106 -0.211  0.1021  188 SER   B OG   
3396 N  N    . LYS   B 190 ? 0.792  0.64   0.1677 -0.1302 -0.2454 0.1102  189 LYS   B N    
3397 C  CA   . LYS   B 190 ? 0.7924 0.643  0.1745 -0.1501 -0.2587 0.1165  189 LYS   B CA   
3398 C  C    . LYS   B 190 ? 0.8146 0.6392 0.2007 -0.1498 -0.2677 0.1223  189 LYS   B C    
3399 O  O    . LYS   B 190 ? 0.8151 0.6382 0.2063 -0.1636 -0.2737 0.1334  189 LYS   B O    
3400 C  CB   . LYS   B 190 ? 0.7967 0.661  0.1804 -0.1556 -0.2655 0.1101  189 LYS   B CB   
3401 C  CG   . LYS   B 190 ? 0.8094 0.7043 0.1932 -0.159  -0.2572 0.1078  189 LYS   B CG   
3402 C  CD   . LYS   B 190 ? 0.8287 0.7372 0.2159 -0.179  -0.2547 0.117   189 LYS   B CD   
3403 C  CE   . LYS   B 190 ? 0.8613 0.7821 0.243  -0.1747 -0.2395 0.1156  189 LYS   B CE   
3404 N  NZ   . LYS   B 190 ? 0.8828 0.8156 0.2635 -0.1938 -0.2381 0.1234  189 LYS   B NZ   
3405 N  N    . PHE   B 191 ? 0.8329 0.6373 0.2156 -0.1322 -0.2673 0.116   190 PHE   B N    
3406 C  CA   . PHE   B 191 ? 0.8553 0.6333 0.2425 -0.1283 -0.2734 0.1207  190 PHE   B CA   
3407 C  C    . PHE   B 191 ? 0.8602 0.641  0.2551 -0.1296 -0.2698 0.1318  190 PHE   B C    
3408 O  O    . PHE   B 191 ? 0.8607 0.6317 0.2627 -0.1349 -0.2775 0.1426  190 PHE   B O    
3409 C  CB   . PHE   B 191 ? 0.8674 0.6265 0.247  -0.1066 -0.2698 0.1104  190 PHE   B CB   
3410 C  CG   . PHE   B 191 ? 0.8881 0.629  0.2636 -0.1056 -0.2797 0.1012  190 PHE   B CG   
3411 C  CD1  . PHE   B 191 ? 0.8979 0.6522 0.2666 -0.1076 -0.2843 0.0892  190 PHE   B CD1  
3412 C  CD2  . PHE   B 191 ? 0.9108 0.6222 0.2895 -0.1009 -0.2837 0.1026  190 PHE   B CD2  
3413 C  CE1  . PHE   B 191 ? 0.915  0.6545 0.2801 -0.108  -0.2939 0.0765  190 PHE   B CE1  
3414 C  CE2  . PHE   B 191 ? 0.9292 0.6204 0.303  -0.1002 -0.2912 0.0904  190 PHE   B CE2  
3415 C  CZ   . PHE   B 191 ? 0.924  0.6299 0.2908 -0.1049 -0.2967 0.0762  190 PHE   B CZ   
3416 N  N    . ALA   B 192 ? 0.8601 0.6553 0.2545 -0.1245 -0.2578 0.1288  191 ALA   B N    
3417 C  CA   . ALA   B 192 ? 0.8609 0.6661 0.2644 -0.1276 -0.2537 0.1346  191 ALA   B CA   
3418 C  C    . ALA   B 192 ? 0.8576 0.6813 0.2626 -0.1472 -0.2619 0.1443  191 ALA   B C    
3419 O  O    . ALA   B 192 ? 0.8549 0.6834 0.2676 -0.1504 -0.2677 0.1537  191 ALA   B O    
3420 C  CB   . ALA   B 192 ? 0.8634 0.6782 0.2657 -0.1213 -0.2368 0.1259  191 ALA   B CB   
3421 N  N    . ALA   B 193 ? 0.8583 0.6947 0.2557 -0.1591 -0.2623 0.143   192 ALA   B N    
3422 C  CA   . ALA   B 193 ? 0.8612 0.7154 0.2563 -0.1777 -0.2681 0.1529  192 ALA   B CA   
3423 C  C    . ALA   B 193 ? 0.8723 0.7113 0.2704 -0.1829 -0.2811 0.1678  192 ALA   B C    
3424 O  O    . ALA   B 193 ? 0.8711 0.7193 0.2693 -0.19   -0.2869 0.1809  192 ALA   B O    
3425 C  CB   . ALA   B 193 ? 0.8593 0.7295 0.2477 -0.1872 -0.2633 0.1476  192 ALA   B CB   
3426 N  N    . VAL   B 194 ? 0.8807 0.6956 0.2808 -0.178  -0.2853 0.1654  193 VAL   B N    
3427 C  CA   . VAL   B 194 ? 0.887  0.6784 0.2909 -0.1817 -0.2946 0.1779  193 VAL   B CA   
3428 C  C    . VAL   B 194 ? 0.8932 0.6723 0.304  -0.1689 -0.2981 0.1877  193 VAL   B C    
3429 O  O    . VAL   B 194 ? 0.8944 0.6648 0.3076 -0.1721 -0.3047 0.2049  193 VAL   B O    
3430 C  CB   . VAL   B 194 ? 0.895  0.6635 0.3    -0.1805 -0.2969 0.1672  193 VAL   B CB   
3431 C  CG1  . VAL   B 194 ? 0.9117 0.6472 0.3221 -0.1821 -0.3035 0.1775  193 VAL   B CG1  
3432 C  CG2  . VAL   B 194 ? 0.8898 0.677  0.2929 -0.1955 -0.2957 0.1605  193 VAL   B CG2  
3433 N  N    . GLY   B 195 ? 0.894  0.674  0.3088 -0.1536 -0.2924 0.1779  194 GLY   B N    
3434 C  CA   . GLY   B 195 ? 0.8987 0.6739 0.3243 -0.1404 -0.2939 0.1849  194 GLY   B CA   
3435 C  C    . GLY   B 195 ? 0.8878 0.6947 0.3177 -0.1465 -0.2963 0.1937  194 GLY   B C    
3436 O  O    . GLY   B 195 ? 0.8843 0.6939 0.3234 -0.1404 -0.3031 0.2069  194 GLY   B O    
3437 N  N    . PHE   B 196 ? 0.8798 0.7126 0.3031 -0.1579 -0.2909 0.1859  195 PHE   B N    
3438 C  CA   . PHE   B 196 ? 0.8761 0.7419 0.3004 -0.1669 -0.2936 0.1904  195 PHE   B CA   
3439 C  C    . PHE   B 196 ? 0.8878 0.7589 0.3042 -0.1764 -0.3053 0.2104  195 PHE   B C    
3440 O  O    . PHE   B 196 ? 0.8851 0.7748 0.3051 -0.1751 -0.3135 0.2222  195 PHE   B O    
3441 C  CB   . PHE   B 196 ? 0.8693 0.7554 0.2857 -0.1775 -0.2831 0.1755  195 PHE   B CB   
3442 C  CG   . PHE   B 196 ? 0.8659 0.7862 0.2773 -0.1913 -0.2862 0.1773  195 PHE   B CG   
3443 C  CD1  . PHE   B 196 ? 0.8608 0.803  0.2841 -0.1902 -0.287  0.1725  195 PHE   B CD1  
3444 C  CD2  . PHE   B 196 ? 0.8758 0.8089 0.271  -0.206  -0.2882 0.1827  195 PHE   B CD2  
3445 C  CE1  . PHE   B 196 ? 0.8572 0.8338 0.2742 -0.2038 -0.291  0.1707  195 PHE   B CE1  
3446 C  CE2  . PHE   B 196 ? 0.8733 0.8389 0.2599 -0.218  -0.291  0.183   195 PHE   B CE2  
3447 C  CZ   . PHE   B 196 ? 0.8572 0.8447 0.2539 -0.2169 -0.2932 0.176   195 PHE   B CZ   
3448 N  N    . HIS   B 197 ? 0.8999 0.7558 0.3062 -0.1853 -0.3054 0.2148  196 HIS   B N    
3449 C  CA   . HIS   B 197 ? 0.9178 0.7715 0.3158 -0.1947 -0.3126 0.2353  196 HIS   B CA   
3450 C  C    . HIS   B 197 ? 0.937  0.7664 0.3437 -0.1816 -0.3204 0.2526  196 HIS   B C    
3451 O  O    . HIS   B 197 ? 0.9418 0.7808 0.3443 -0.1817 -0.3278 0.2731  196 HIS   B O    
3452 C  CB   . HIS   B 197 ? 0.934  0.774  0.3257 -0.2072 -0.3082 0.2326  196 HIS   B CB   
3453 C  CG   . HIS   B 197 ? 0.963  0.7929 0.3483 -0.2175 -0.3123 0.2548  196 HIS   B CG   
3454 N  ND1  . HIS   B 197 ? 0.9779 0.8341 0.3495 -0.2285 -0.3135 0.2687  196 HIS   B ND1  
3455 C  CD2  . HIS   B 197 ? 0.985  0.7794 0.3753 -0.2175 -0.314  0.2654  196 HIS   B CD2  
3456 C  CE1  . HIS   B 197 ? 0.9933 0.829  0.3615 -0.2343 -0.3149 0.2895  196 HIS   B CE1  
3457 N  NE2  . HIS   B 197 ? 1.0014 0.7981 0.3821 -0.2288 -0.3148 0.2878  196 HIS   B NE2  
3458 N  N    . ARG   B 198 ? 0.9486 0.7469 0.3656 -0.1688 -0.3181 0.2449  197 ARG   B N    
3459 C  CA   . ARG   B 198 ? 0.9679 0.7379 0.3941 -0.1543 -0.3229 0.2589  197 ARG   B CA   
3460 C  C    . ARG   B 198 ? 0.9603 0.7515 0.3983 -0.1392 -0.328  0.2668  197 ARG   B C    
3461 O  O    . ARG   B 198 ? 0.9636 0.7463 0.4062 -0.1292 -0.3345 0.2874  197 ARG   B O    
3462 C  CB   . ARG   B 198 ? 1.0047 0.7359 0.4363 -0.1453 -0.3179 0.2447  197 ARG   B CB   
3463 C  CG   . ARG   B 198 ? 1.0735 0.7653 0.5032 -0.1504 -0.3191 0.2551  197 ARG   B CG   
3464 C  CD   . ARG   B 198 ? 1.142  0.7935 0.5784 -0.137  -0.316  0.2434  197 ARG   B CD   
3465 N  NE   . ARG   B 198 ? 1.1993 0.8429 0.6303 -0.1447 -0.3123 0.2195  197 ARG   B NE   
3466 C  CZ   . ARG   B 198 ? 1.2437 0.8677 0.6722 -0.1605 -0.3124 0.2153  197 ARG   B CZ   
3467 N  NH1  . ARG   B 198 ? 1.2504 0.856  0.6805 -0.1713 -0.3134 0.2346  197 ARG   B NH1  
3468 N  NH2  . ARG   B 198 ? 1.2401 0.8645 0.6652 -0.1654 -0.3109 0.1922  197 ARG   B NH2  
3469 N  N    . GLY   B 199 ? 0.9479 0.7666 0.3924 -0.1373 -0.3242 0.2505  198 GLY   B N    
3470 C  CA   . GLY   B 199 ? 0.9412 0.7884 0.4014 -0.1265 -0.3284 0.2536  198 GLY   B CA   
3471 C  C    . GLY   B 199 ? 0.941  0.8266 0.3937 -0.1361 -0.3387 0.2676  198 GLY   B C    
3472 O  O    . GLY   B 199 ? 0.9366 0.838  0.3976 -0.1255 -0.3487 0.2849  198 GLY   B O    
3473 N  N    . LEU   B 200 ? 0.9409 0.8425 0.3761 -0.155  -0.3364 0.2615  199 LEU   B N    
3474 C  CA   . LEU   B 200 ? 0.9378 0.8754 0.359  -0.1658 -0.3449 0.2729  199 LEU   B CA   
3475 C  C    . LEU   B 200 ? 0.9559 0.8792 0.3684 -0.1602 -0.3537 0.3032  199 LEU   B C    
3476 O  O    . LEU   B 200 ? 0.9558 0.908  0.3664 -0.1547 -0.3648 0.3194  199 LEU   B O    
3477 C  CB   . LEU   B 200 ? 0.942  0.8898 0.3446 -0.1858 -0.3373 0.2604  199 LEU   B CB   
3478 C  CG   . LEU   B 200 ? 0.9586 0.9394 0.3401 -0.1986 -0.3436 0.2715  199 LEU   B CG   
3479 C  CD1  . LEU   B 200 ? 0.9463 0.9734 0.3325 -0.1971 -0.3531 0.2678  199 LEU   B CD1  
3480 C  CD2  . LEU   B 200 ? 0.9734 0.9593 0.339  -0.2162 -0.3327 0.2573  199 LEU   B CD2  
3481 N  N    . THR   B 201 ? 0.9705 0.849  0.3795 -0.1603 -0.3484 0.3106  200 THR   B N    
3482 C  CA   . THR   B 201 ? 0.9892 0.8438 0.3912 -0.1554 -0.3527 0.3398  200 THR   B CA   
3483 C  C    . THR   B 201 ? 1.0091 0.8607 0.427  -0.1314 -0.3607 0.3561  200 THR   B C    
3484 O  O    . THR   B 201 ? 1.0112 0.881  0.4222 -0.1242 -0.3699 0.3814  200 THR   B O    
3485 C  CB   . THR   B 201 ? 1.0042 0.8112 0.403  -0.1644 -0.3434 0.3383  200 THR   B CB   
3486 O  OG1  . THR   B 201 ? 1.0073 0.8277 0.3884 -0.1854 -0.3394 0.339   200 THR   B OG1  
3487 C  CG2  . THR   B 201 ? 1.0197 0.7836 0.4213 -0.154  -0.3438 0.3626  200 THR   B CG2  
3488 N  N    . SER   B 202 ? 1.0197 0.8537 0.4582 -0.1175 -0.3569 0.3419  201 SER   B N    
3489 C  CA   . SER   B 202 ? 1.0366 0.8682 0.4939 -0.0929 -0.3624 0.3556  201 SER   B CA   
3490 C  C    . SER   B 202 ? 1.0309 0.9219 0.4964 -0.0866 -0.3743 0.361   201 SER   B C    
3491 O  O    . SER   B 202 ? 1.0275 0.9287 0.4987 -0.0693 -0.3836 0.3855  201 SER   B O    
3492 C  CB   . SER   B 202 ? 1.0679 0.8707 0.5442 -0.0798 -0.3537 0.3371  201 SER   B CB   
3493 O  OG   . SER   B 202 ? 1.1167 0.9029 0.5875 -0.0925 -0.3436 0.3109  201 SER   B OG   
3494 N  N    . GLU   B 203 ? 1.0242 0.955  0.4903 -0.1006 -0.374  0.3382  202 GLU   B N    
3495 C  CA   . GLU   B 203 ? 1.0097 1.0011 0.4851 -0.0993 -0.3854 0.3373  202 GLU   B CA   
3496 C  C    . GLU   B 203 ? 1.0156 1.0378 0.4669 -0.106  -0.3976 0.3581  202 GLU   B C    
3497 O  O    . GLU   B 203 ? 1.0031 1.0663 0.4607 -0.0944 -0.4117 0.3726  202 GLU   B O    
3498 C  CB   . GLU   B 203 ? 1.0196 1.0385 0.5038 -0.114  -0.3785 0.3046  202 GLU   B CB   
3499 C  CG   . GLU   B 203 ? 1.0377 1.1155 0.5427 -0.1112 -0.3885 0.2984  202 GLU   B CG   
3500 C  CD   . GLU   B 203 ? 1.091  1.193  0.6056 -0.1281 -0.3794 0.266   202 GLU   B CD   
3501 O  OE1  . GLU   B 203 ? 1.0874 1.2208 0.586  -0.1467 -0.3827 0.2562  202 GLU   B OE1  
3502 O  OE2  . GLU   B 203 ? 1.1242 1.2112 0.6612 -0.1224 -0.3673 0.2506  202 GLU   B OE2  
3503 N  N    . LEU   B 204 ? 1.0351 1.0383 0.4589 -0.1227 -0.3921 0.3617  203 LEU   B N    
3504 C  CA   . LEU   B 204 ? 1.0512 1.0786 0.4472 -0.1291 -0.4006 0.3834  203 LEU   B CA   
3505 C  C    . LEU   B 204 ? 1.072  1.0865 0.4671 -0.1068 -0.409  0.4209  203 LEU   B C    
3506 O  O    . LEU   B 204 ? 1.0581 1.1144 0.4435 -0.0988 -0.4229 0.4396  203 LEU   B O    
3507 C  CB   . LEU   B 204 ? 1.0684 1.0695 0.4392 -0.1496 -0.3892 0.3821  203 LEU   B CB   
3508 C  CG   . LEU   B 204 ? 1.0772 1.1043 0.4377 -0.1717 -0.383  0.3534  203 LEU   B CG   
3509 C  CD1  . LEU   B 204 ? 1.0988 1.0989 0.4399 -0.1883 -0.3711 0.3549  203 LEU   B CD1  
3510 C  CD2  . LEU   B 204 ? 1.0676 1.1546 0.4149 -0.1772 -0.3943 0.3511  203 LEU   B CD2  
3511 N  N    . GLN   B 205 ? 1.1022 1.0593 0.5082 -0.0953 -0.4005 0.4304  204 GLN   B N    
3512 C  CA   . GLN   B 205 ? 1.1281 1.0589 0.5364 -0.0722 -0.4038 0.4649  204 GLN   B CA   
3513 C  C    . GLN   B 205 ? 1.1213 1.0864 0.5554 -0.0465 -0.4158 0.4709  204 GLN   B C    
3514 O  O    . GLN   B 205 ? 1.12   1.1046 0.5494 -0.0279 -0.4268 0.5017  204 GLN   B O    
3515 C  CB   . GLN   B 205 ? 1.1724 1.0292 0.5873 -0.0705 -0.3889 0.465   204 GLN   B CB   
3516 C  CG   . GLN   B 205 ? 1.2318 1.0484 0.6484 -0.0478 -0.3878 0.5004  204 GLN   B CG   
3517 C  CD   . GLN   B 205 ? 1.2915 1.0901 0.7377 -0.0218 -0.3871 0.4976  204 GLN   B CD   
3518 O  OE1  . GLN   B 205 ? 1.3029 1.1049 0.7572 0.0045  -0.3933 0.5251  204 GLN   B OE1  
3519 N  NE2  . GLN   B 205 ? 1.3062 1.0863 0.7686 -0.0269 -0.3789 0.4653  204 GLN   B NE2  
3520 N  N    . ALA   B 206 ? 1.1135 1.0886 0.5749 -0.0446 -0.4132 0.4426  205 ALA   B N    
3521 C  CA   . ALA   B 206 ? 1.1004 1.1109 0.5926 -0.0219 -0.4223 0.4443  205 ALA   B CA   
3522 C  C    . ALA   B 206 ? 1.0769 1.1656 0.5685 -0.0228 -0.4406 0.4473  205 ALA   B C    
3523 O  O    . ALA   B 206 ? 1.0613 1.1842 0.5729 0.0001  -0.4526 0.4628  205 ALA   B O    
3524 C  CB   . ALA   B 206 ? 1.0988 1.1018 0.6185 -0.0233 -0.4118 0.4119  205 ALA   B CB   
3525 N  N    . LEU   B 207 ? 1.0725 1.1919 0.5422 -0.0484 -0.443  0.4317  206 LEU   B N    
3526 C  CA   . LEU   B 207 ? 1.054  1.2497 0.52   -0.0522 -0.461  0.4302  206 LEU   B CA   
3527 C  C    . LEU   B 207 ? 1.0672 1.2825 0.4996 -0.0452 -0.474  0.4653  206 LEU   B C    
3528 O  O    . LEU   B 207 ? 1.0481 1.3292 0.471  -0.0486 -0.4903 0.4643  206 LEU   B O    
3529 C  CB   . LEU   B 207 ? 1.0451 1.2685 0.5058 -0.0821 -0.4566 0.3925  206 LEU   B CB   
3530 C  CG   . LEU   B 207 ? 1.0476 1.2616 0.54   -0.089  -0.4438 0.3586  206 LEU   B CG   
3531 C  CD1  . LEU   B 207 ? 1.0447 1.2869 0.5294 -0.117  -0.4392 0.3253  206 LEU   B CD1  
3532 C  CD2  . LEU   B 207 ? 1.0304 1.2779 0.5639 -0.0697 -0.4514 0.3577  206 LEU   B CD2  
3533 N  N    . GLY   B 208 ? 1.0981 1.257  0.5121 -0.0358 -0.466  0.4954  207 GLY   B N    
3534 C  CA   . GLY   B 208 ? 1.1181 1.2861 0.4981 -0.0276 -0.4741 0.5329  207 GLY   B CA   
3535 C  C    . GLY   B 208 ? 1.1426 1.3142 0.4827 -0.0544 -0.4692 0.5287  207 GLY   B C    
3536 O  O    . GLY   B 208 ? 1.1604 1.3411 0.468  -0.0492 -0.474  0.5598  207 GLY   B O    
3537 N  N    . ILE   B 209 ? 1.1449 1.3102 0.486  -0.0815 -0.4584 0.4918  208 ILE   B N    
3538 C  CA   . ILE   B 209 ? 1.1613 1.3309 0.4674 -0.1068 -0.4515 0.4846  208 ILE   B CA   
3539 C  C    . ILE   B 209 ? 1.1988 1.3024 0.4883 -0.1115 -0.4347 0.5059  208 ILE   B C    
3540 O  O    . ILE   B 209 ? 1.2125 1.2631 0.5203 -0.1151 -0.4211 0.4951  208 ILE   B O    
3541 C  CB   . ILE   B 209 ? 1.1541 1.3445 0.4672 -0.1321 -0.4454 0.4387  208 ILE   B CB   
3542 C  CG1  . ILE   B 209 ? 1.1409 1.4068 0.4569 -0.1349 -0.4624 0.4206  208 ILE   B CG1  
3543 C  CG2  . ILE   B 209 ? 1.1721 1.3458 0.4552 -0.1562 -0.4316 0.4313  208 ILE   B CG2  
3544 C  CD1  . ILE   B 209 ? 1.1359 1.4264 0.4925 -0.1201 -0.472  0.4103  208 ILE   B CD1  
3545 N  N    . THR   B 210 ? 1.215  1.3236 0.4697 -0.1115 -0.4354 0.5362  209 THR   B N    
3546 C  CA   . THR   B 210 ? 1.2518 1.3015 0.4908 -0.1178 -0.4183 0.5591  209 THR   B CA   
3547 C  C    . THR   B 210 ? 1.2574 1.3109 0.4722 -0.1469 -0.4061 0.5439  209 THR   B C    
3548 O  O    . THR   B 210 ? 1.2741 1.2822 0.4971 -0.162  -0.3896 0.5333  209 THR   B O    
3549 C  CB   . THR   B 210 ? 1.2899 1.3291 0.5092 -0.0955 -0.422  0.6094  209 THR   B CB   
3550 O  OG1  . THR   B 210 ? 1.2891 1.3974 0.4868 -0.0836 -0.4415 0.6224  209 THR   B OG1  
3551 C  CG2  . THR   B 210 ? 1.3061 1.297  0.5537 -0.0704 -0.4202 0.6277  209 THR   B CG2  
3552 N  N    . GLY   B 211 ? 1.2385 1.3491 0.4248 -0.154  -0.4146 0.5408  210 GLY   B N    
3553 C  CA   . GLY   B 211 ? 1.2407 1.3641 0.4    -0.1791 -0.4034 0.5277  210 GLY   B CA   
3554 C  C    . GLY   B 211 ? 1.2333 1.3427 0.4104 -0.2008 -0.3905 0.487   210 GLY   B C    
3555 O  O    . GLY   B 211 ? 1.24   1.3443 0.3999 -0.2199 -0.3764 0.4813  210 GLY   B O    
3556 N  N    . ILE   B 212 ? 1.2158 1.3202 0.4273 -0.1968 -0.3939 0.4597  211 ILE   B N    
3557 C  CA   . ILE   B 212 ? 1.2116 1.3012 0.4396 -0.2136 -0.3812 0.4234  211 ILE   B CA   
3558 C  C    . ILE   B 212 ? 1.2123 1.2411 0.4617 -0.2128 -0.3694 0.4263  211 ILE   B C    
3559 O  O    . ILE   B 212 ? 1.211  1.216  0.4855 -0.1977 -0.3735 0.427   211 ILE   B O    
3560 C  CB   . ILE   B 212 ? 1.2034 1.3242 0.4523 -0.2132 -0.3881 0.3889  211 ILE   B CB   
3561 C  CG1  . ILE   B 212 ? 1.2083 1.3921 0.4362 -0.2175 -0.4002 0.3815  211 ILE   B CG1  
3562 C  CG2  . ILE   B 212 ? 1.2085 1.3097 0.4707 -0.2279 -0.3727 0.356   211 ILE   B CG2  
3563 C  CD1  . ILE   B 212 ? 1.2098 1.4262 0.4614 -0.2175 -0.4075 0.3502  211 ILE   B CD1  
3564 N  N    . LYS   B 213 ? 1.2125 1.2183 0.4527 -0.2295 -0.3545 0.427   212 LYS   B N    
3565 C  CA   . LYS   B 213 ? 1.2211 1.1734 0.4811 -0.2327 -0.3435 0.4263  212 LYS   B CA   
3566 C  C    . LYS   B 213 ? 1.2044 1.1535 0.4838 -0.2415 -0.3367 0.3883  212 LYS   B C    
3567 O  O    . LYS   B 213 ? 1.1984 1.1828 0.4732 -0.2473 -0.337  0.3655  212 LYS   B O    
3568 C  CB   . LYS   B 213 ? 1.2572 1.1879 0.5011 -0.2468 -0.3305 0.4486  212 LYS   B CB   
3569 C  CG   . LYS   B 213 ? 1.3151 1.2546 0.5316 -0.2397 -0.3339 0.4875  212 LYS   B CG   
3570 C  CD   . LYS   B 213 ? 1.3869 1.2988 0.6123 -0.2164 -0.3424 0.5146  212 LYS   B CD   
3571 C  CE   . LYS   B 213 ? 1.461  1.3823 0.6554 -0.2081 -0.3439 0.5562  212 LYS   B CE   
3572 N  NZ   . LYS   B 213 ? 1.506  1.4028 0.7073 -0.1816 -0.3517 0.5867  212 LYS   B NZ   
3573 N  N    . THR   B 214 ? 1.1943 1.1008 0.4943 -0.2416 -0.3303 0.3813  213 THR   B N    
3574 C  CA   . THR   B 214 ? 1.1798 1.0826 0.4957 -0.247  -0.324  0.3487  213 THR   B CA   
3575 C  C    . THR   B 214 ? 1.1742 1.0433 0.4993 -0.2588 -0.3137 0.346   213 THR   B C    
3576 O  O    . THR   B 214 ? 1.1886 1.02   0.5205 -0.2564 -0.3131 0.3624  213 THR   B O    
3577 C  CB   . THR   B 214 ? 1.1883 1.0826 0.5249 -0.2297 -0.3302 0.3336  213 THR   B CB   
3578 O  OG1  . THR   B 214 ? 1.2076 1.0689 0.5535 -0.2152 -0.3354 0.3533  213 THR   B OG1  
3579 C  CG2  . THR   B 214 ? 1.1781 1.114  0.5131 -0.2239 -0.3372 0.3224  213 THR   B CG2  
3580 N  N    . SER   B 215 ? 1.1501 1.0331 0.4769 -0.2714 -0.3053 0.3246  214 SER   B N    
3581 C  CA   . SER   B 215 ? 1.1416 1.0026 0.4808 -0.2835 -0.2969 0.3172  214 SER   B CA   
3582 C  C    . SER   B 215 ? 1.1253 0.9932 0.4773 -0.2799 -0.2948 0.2863  214 SER   B C    
3583 O  O    . SER   B 215 ? 1.1182 1.0147 0.4643 -0.2768 -0.2934 0.2721  214 SER   B O    
3584 C  CB   . SER   B 215 ? 1.1538 1.0318 0.4818 -0.3031 -0.2867 0.3267  214 SER   B CB   
3585 O  OG   . SER   B 215 ? 1.1918 1.0457 0.5148 -0.3087 -0.2845 0.356   214 SER   B OG   
3586 N  N    . CYS   B 216 ? 1.1198 0.9608 0.4883 -0.2798 -0.2942 0.2755  215 CYS   B N    
3587 C  CA   . CYS   B 216 ? 1.108  0.955  0.4862 -0.2737 -0.2925 0.2483  215 CYS   B CA   
3588 C  C    . CYS   B 216 ? 1.0958 0.9422 0.4847 -0.2878 -0.2874 0.2389  215 CYS   B C    
3589 O  O    . CYS   B 216 ? 1.1018 0.9193 0.501  -0.2935 -0.2893 0.2424  215 CYS   B O    
3590 C  CB   . CYS   B 216 ? 1.1208 0.9412 0.5076 -0.2552 -0.2988 0.2406  215 CYS   B CB   
3591 S  SG   . CYS   B 216 ? 1.1636 0.9867 0.5585 -0.2447 -0.2961 0.2106  215 CYS   B SG   
3592 N  N    . LEU   B 217 ? 1.0785 0.9569 0.4669 -0.2935 -0.2806 0.226   216 LEU   B N    
3593 C  CA   . LEU   B 217 ? 1.0732 0.96   0.4757 -0.3063 -0.2765 0.2158  216 LEU   B CA   
3594 C  C    . LEU   B 217 ? 1.0647 0.946  0.4782 -0.294  -0.2809 0.1927  216 LEU   B C    
3595 O  O    . LEU   B 217 ? 1.0574 0.9531 0.466  -0.2791 -0.2791 0.1801  216 LEU   B O    
3596 C  CB   . LEU   B 217 ? 1.0691 0.9954 0.4674 -0.3166 -0.2662 0.2143  216 LEU   B CB   
3597 C  CG   . LEU   B 217 ? 1.084  1.0273 0.5006 -0.3315 -0.2613 0.2062  216 LEU   B CG   
3598 C  CD1  . LEU   B 217 ? 1.0943 1.0236 0.5177 -0.3528 -0.2583 0.224   216 LEU   B CD1  
3599 C  CD2  . LEU   B 217 ? 1.0835 1.0682 0.4977 -0.3332 -0.2506 0.1989  216 LEU   B CD2  
3600 N  N    . CYS   B 218 ? 1.0647 0.9239 0.4919 -0.3001 -0.2859 0.1872  217 CYS   B N    
3601 C  CA   . CYS   B 218 ? 1.0676 0.9219 0.5025 -0.2892 -0.2917 0.1651  217 CYS   B CA   
3602 C  C    . CYS   B 218 ? 1.0609 0.9329 0.5137 -0.3052 -0.2925 0.1519  217 CYS   B C    
3603 O  O    . CYS   B 218 ? 1.0658 0.9141 0.5301 -0.3151 -0.2974 0.1465  217 CYS   B O    
3604 C  CB   . CYS   B 218 ? 1.085  0.8963 0.5186 -0.2787 -0.2986 0.1651  217 CYS   B CB   
3605 S  SG   . CYS   B 218 ? 1.123  0.924  0.5418 -0.2531 -0.2991 0.17    217 CYS   B SG   
3606 N  N    . PRO   B 219 ? 1.0474 0.9617 0.505  -0.3075 -0.2874 0.1447  218 PRO   B N    
3607 C  CA   . PRO   B 219 ? 1.034  0.9731 0.5131 -0.3226 -0.2891 0.1314  218 PRO   B CA   
3608 C  C    . PRO   B 219 ? 1.0286 0.9835 0.5119 -0.3067 -0.2975 0.1076  218 PRO   B C    
3609 O  O    . PRO   B 219 ? 1.0388 0.9852 0.5062 -0.2827 -0.2993 0.1029  218 PRO   B O    
3610 C  CB   . PRO   B 219 ? 1.0296 1.0093 0.512  -0.3319 -0.2778 0.139   218 PRO   B CB   
3611 C  CG   . PRO   B 219 ? 1.0421 1.0237 0.5019 -0.3135 -0.2719 0.146   218 PRO   B CG   
3612 C  CD   . PRO   B 219 ? 1.0384 0.9812 0.4843 -0.2977 -0.2789 0.1478  218 PRO   B CD   
3613 N  N    . VAL   B 220 ? 1.0112 0.9911 0.516  -0.3202 -0.3024 0.0927  219 VAL   B N    
3614 C  CA   . VAL   B 220 ? 1.0084 1.0124 0.5168 -0.3051 -0.3121 0.0699  219 VAL   B CA   
3615 C  C    . VAL   B 220 ? 0.9907 1.0485 0.503  -0.294  -0.3058 0.068   219 VAL   B C    
3616 O  O    . VAL   B 220 ? 0.9964 1.0552 0.4965 -0.2873 -0.2943 0.0823  219 VAL   B O    
3617 C  CB   . VAL   B 220 ? 1.0149 1.016  0.544  -0.3242 -0.3233 0.0514  219 VAL   B CB   
3618 C  CG1  . VAL   B 220 ? 1.046  0.9877 0.5666 -0.328  -0.3269 0.0529  219 VAL   B CG1  
3619 C  CG2  . VAL   B 220 ? 1.0041 1.0324 0.5625 -0.3556 -0.3184 0.0535  219 VAL   B CG2  
3620 N  N    . PHE   B 221 ? 0.9709 1.073  0.4992 -0.2908 -0.3127 0.0509  220 PHE   B N    
3621 C  CA   . PHE   B 221 ? 0.9644 1.1155 0.4973 -0.2774 -0.3051 0.0516  220 PHE   B CA   
3622 C  C    . PHE   B 221 ? 0.9522 1.1283 0.5031 -0.2999 -0.2929 0.063   220 PHE   B C    
3623 O  O    . PHE   B 221 ? 0.9364 1.1296 0.5136 -0.3262 -0.2954 0.0588  220 PHE   B O    
3624 C  CB   . PHE   B 221 ? 0.9522 1.1487 0.4966 -0.2632 -0.3167 0.032   220 PHE   B CB   
3625 C  CG   . PHE   B 221 ? 0.9469 1.1923 0.4952 -0.2433 -0.3081 0.0342  220 PHE   B CG   
3626 C  CD1  . PHE   B 221 ? 0.9286 1.2292 0.5078 -0.2563 -0.307  0.0299  220 PHE   B CD1  
3627 C  CD2  . PHE   B 221 ? 0.9695 1.2053 0.4925 -0.2109 -0.2999 0.0403  220 PHE   B CD2  
3628 C  CE1  . PHE   B 221 ? 0.9208 1.2658 0.5046 -0.2353 -0.2979 0.0325  220 PHE   B CE1  
3629 C  CE2  . PHE   B 221 ? 0.9637 1.2396 0.4903 -0.1908 -0.2899 0.0429  220 PHE   B CE2  
3630 C  CZ   . PHE   B 221 ? 0.9327 1.263  0.4892 -0.202  -0.2892 0.0393  220 PHE   B CZ   
3631 N  N    . VAL   B 222 ? 0.9584 1.136  0.4949 -0.2901 -0.2783 0.0764  221 VAL   B N    
3632 C  CA   . VAL   B 222 ? 0.9543 1.1564 0.5013 -0.3067 -0.264  0.0875  221 VAL   B CA   
3633 C  C    . VAL   B 222 ? 0.9401 1.1934 0.4964 -0.2882 -0.2569 0.0809  221 VAL   B C    
3634 O  O    . VAL   B 222 ? 0.95   1.2006 0.4891 -0.2595 -0.2546 0.0782  221 VAL   B O    
3635 C  CB   . VAL   B 222 ? 0.9854 1.1538 0.5068 -0.3082 -0.2524 0.1054  221 VAL   B CB   
3636 C  CG1  . VAL   B 222 ? 0.9829 1.1744 0.5116 -0.3278 -0.2375 0.1173  221 VAL   B CG1  
3637 C  CG2  . VAL   B 222 ? 1.0131 1.1294 0.5221 -0.3162 -0.2607 0.1128  221 VAL   B CG2  
3638 N  N    . ASN   B 223 ? 0.9164 1.2158 0.5012 -0.3038 -0.2523 0.0788  222 ASN   B N    
3639 C  CA   . ASN   B 223 ? 0.9041 1.258  0.5035 -0.2872 -0.2449 0.0735  222 ASN   B CA   
3640 C  C    . ASN   B 223 ? 0.9183 1.2691 0.4985 -0.2752 -0.2238 0.0849  222 ASN   B C    
3641 O  O    . ASN   B 223 ? 0.912  1.2857 0.5032 -0.2908 -0.2098 0.0918  222 ASN   B O    
3642 C  CB   . ASN   B 223 ? 0.891  1.2958 0.5309 -0.3118 -0.2454 0.0682  222 ASN   B CB   
3643 C  CG   . ASN   B 223 ? 0.9109 1.38   0.5731 -0.2945 -0.2405 0.0614  222 ASN   B CG   
3644 O  OD1  . ASN   B 223 ? 0.9279 1.4062 0.5774 -0.2609 -0.2413 0.0578  222 ASN   B OD1  
3645 N  ND2  . ASN   B 223 ? 0.8982 1.4137 0.5953 -0.3163 -0.2338 0.0609  222 ASN   B ND2  
3646 N  N    . THR   B 224 ? 0.936  1.2574 0.4876 -0.2491 -0.22   0.0861  223 THR   B N    
3647 C  CA   . THR   B 224 ? 0.948  1.2622 0.4806 -0.2385 -0.1995 0.093   223 THR   B CA   
3648 C  C    . THR   B 224 ? 0.949  1.2761 0.4755 -0.2034 -0.1906 0.0878  223 THR   B C    
3649 O  O    . THR   B 224 ? 0.9472 1.2749 0.4636 -0.1941 -0.1712 0.0905  223 THR   B O    
3650 C  CB   . THR   B 224 ? 0.9871 1.2475 0.4896 -0.2436 -0.1981 0.1008  223 THR   B CB   
3651 O  OG1  . THR   B 224 ? 1.0157 1.2451 0.5048 -0.2251 -0.2088 0.0962  223 THR   B OG1  
3652 C  CG2  . THR   B 224 ? 0.9922 1.2361 0.4957 -0.2747 -0.2033 0.1105  223 THR   B CG2  
3653 N  N    . GLY   B 225 ? 0.9531 1.2875 0.4836 -0.1835 -0.2036 0.0806  224 GLY   B N    
3654 C  CA   . GLY   B 225 ? 0.9674 1.3088 0.4892 -0.1468 -0.1953 0.0787  224 GLY   B CA   
3655 C  C    . GLY   B 225 ? 1.0037 1.291  0.4942 -0.13   -0.1912 0.0812  224 GLY   B C    
3656 O  O    . GLY   B 225 ? 1.0113 1.2935 0.4906 -0.0998 -0.1795 0.0821  224 GLY   B O    
3657 N  N    . PHE   B 226 ? 1.0205 1.2669 0.4982 -0.149  -0.1995 0.0834  225 PHE   B N    
3658 C  CA   . PHE   B 226 ? 1.0482 1.245  0.501  -0.1381 -0.1978 0.0853  225 PHE   B CA   
3659 C  C    . PHE   B 226 ? 1.0647 1.2613 0.512  -0.1098 -0.2063 0.0808  225 PHE   B C    
3660 O  O    . PHE   B 226 ? 1.0783 1.2564 0.5097 -0.0837 -0.1938 0.083   225 PHE   B O    
3661 C  CB   . PHE   B 226 ? 1.0477 1.2144 0.4963 -0.1645 -0.2101 0.0884  225 PHE   B CB   
3662 C  CG   . PHE   B 226 ? 1.0674 1.1869 0.495  -0.1588 -0.2092 0.091   225 PHE   B CG   
3663 C  CD1  . PHE   B 226 ? 1.0837 1.1846 0.4972 -0.1533 -0.1921 0.0934  225 PHE   B CD1  
3664 C  CD2  . PHE   B 226 ? 1.0823 1.1771 0.5066 -0.1618 -0.2249 0.0901  225 PHE   B CD2  
3665 C  CE1  . PHE   B 226 ? 1.1082 1.171  0.5074 -0.1505 -0.1915 0.0948  225 PHE   B CE1  
3666 C  CE2  . PHE   B 226 ? 1.1075 1.1629 0.5161 -0.1567 -0.2233 0.0929  225 PHE   B CE2  
3667 C  CZ   . PHE   B 226 ? 1.1122 1.154  0.5098 -0.1514 -0.207  0.0955  225 PHE   B CZ   
3668 N  N    . THR   B 227 ? 1.0584 1.2783 0.5195 -0.1158 -0.2266 0.0741  226 THR   B N    
3669 C  CA   . THR   B 227 ? 1.0677 1.2987 0.525  -0.0936 -0.24   0.0672  226 THR   B CA   
3670 C  C    . THR   B 227 ? 1.0448 1.3374 0.5286 -0.0943 -0.2505 0.0596  226 THR   B C    
3671 O  O    . THR   B 227 ? 1.0297 1.3463 0.5371 -0.1222 -0.2534 0.0577  226 THR   B O    
3672 C  CB   . THR   B 227 ? 1.1031 1.2997 0.5505 -0.1035 -0.2564 0.0621  226 THR   B CB   
3673 O  OG1  . THR   B 227 ? 1.1169 1.3046 0.5777 -0.1388 -0.2636 0.062   226 THR   B OG1  
3674 C  CG2  . THR   B 227 ? 1.1325 1.2788 0.5534 -0.0879 -0.2471 0.068   226 THR   B CG2  
3675 N  N    . LYS   B 228 ? 1.0383 1.3592 0.5188 -0.0634 -0.2556 0.0561  227 LYS   B N    
3676 C  CA   . LYS   B 228 ? 1.0165 1.4041 0.5237 -0.0593 -0.2655 0.0489  227 LYS   B CA   
3677 C  C    . LYS   B 228 ? 1.0097 1.4223 0.5401 -0.0895 -0.2892 0.0339  227 LYS   B C    
3678 O  O    . LYS   B 228 ? 0.9895 1.437  0.5507 -0.1144 -0.2899 0.0309  227 LYS   B O    
3679 C  CB   . LYS   B 228 ? 1.0319 1.4449 0.5268 -0.0151 -0.2659 0.0506  227 LYS   B CB   
3680 C  CG   . LYS   B 228 ? 1.0646 1.5016 0.565  0.0101  -0.2441 0.0618  227 LYS   B CG   
3681 C  CD   . LYS   B 228 ? 1.0815 1.5811 0.6212 -0.006  -0.2454 0.0577  227 LYS   B CD   
3682 C  CE   . LYS   B 228 ? 1.1246 1.6072 0.6708 -0.0244 -0.2222 0.0651  227 LYS   B CE   
3683 N  NZ   . LYS   B 228 ? 1.112  1.6444 0.6956 -0.0534 -0.2251 0.06    227 LYS   B NZ   
3684 N  N    . ASN   B 229 ? 1.0249 1.4182 0.5415 -0.0884 -0.3066 0.0238  228 ASN   B N    
3685 C  CA   . ASN   B 229 ? 1.0218 1.4345 0.5596 -0.1166 -0.3284 0.0062  228 ASN   B CA   
3686 C  C    . ASN   B 229 ? 1.0526 1.4033 0.5763 -0.1388 -0.3332 0.0037  228 ASN   B C    
3687 O  O    . ASN   B 229 ? 1.0782 1.3783 0.5723 -0.1241 -0.3248 0.0128  228 ASN   B O    
3688 C  CB   . ASN   B 229 ? 1.0244 1.4846 0.5624 -0.0945 -0.3484 -0.0091 228 ASN   B CB   
3689 C  CG   . ASN   B 229 ? 1.0368 1.5612 0.5882 -0.0669 -0.3447 -0.0047 228 ASN   B CG   
3690 O  OD1  . ASN   B 229 ? 1.0287 1.5932 0.612  -0.0802 -0.3379 -0.0022 228 ASN   B OD1  
3691 N  ND2  . ASN   B 229 ? 1.0435 1.5793 0.5704 -0.026  -0.348  -0.0025 228 ASN   B ND2  
3692 N  N    . PRO   B 230 ? 1.0481 1.4011 0.5946 -0.174  -0.3452 -0.0081 229 PRO   B N    
3693 C  CA   . PRO   B 230 ? 1.0764 1.3684 0.6107 -0.193  -0.3481 -0.009  229 PRO   B CA   
3694 C  C    . PRO   B 230 ? 1.0979 1.3641 0.6052 -0.1732 -0.3603 -0.0205 229 PRO   B C    
3695 O  O    . PRO   B 230 ? 1.0888 1.3926 0.5927 -0.1539 -0.3728 -0.034  229 PRO   B O    
3696 C  CB   . PRO   B 230 ? 1.0682 1.3744 0.6367 -0.2335 -0.3562 -0.0198 229 PRO   B CB   
3697 C  CG   . PRO   B 230 ? 1.0393 1.4188 0.6349 -0.2316 -0.3665 -0.0342 229 PRO   B CG   
3698 C  CD   . PRO   B 230 ? 1.0109 1.4207 0.5978 -0.1988 -0.3545 -0.0207 229 PRO   B CD   
3699 N  N    . SER   B 231 ? 1.1235 1.328  0.6112 -0.1769 -0.3564 -0.015  230 SER   B N    
3700 C  CA   . SER   B 231 ? 1.1426 1.3157 0.6033 -0.1589 -0.3646 -0.0247 230 SER   B CA   
3701 C  C    . SER   B 231 ? 1.1328 1.3077 0.6046 -0.1792 -0.3836 -0.0493 230 SER   B C    
3702 O  O    . SER   B 231 ? 1.1374 1.3008 0.5881 -0.1636 -0.3934 -0.0634 230 SER   B O    
3703 C  CB   . SER   B 231 ? 1.1856 1.2956 0.6257 -0.1555 -0.3522 -0.0094 230 SER   B CB   
3704 O  OG   . SER   B 231 ? 1.2061 1.2895 0.6621 -0.1863 -0.3474 -0.0005 230 SER   B OG   
3705 N  N    . PRO   B 236 ? 1.1118 1.3111 0.797  -0.4257 -0.3599 -0.046  235 PRO   B N    
3706 C  CA   . PRO   B 236 ? 1.0927 1.3097 0.8066 -0.4545 -0.3441 -0.0304 235 PRO   B CA   
3707 C  C    . PRO   B 236 ? 1.0733 1.3305 0.7815 -0.4364 -0.3324 -0.0112 235 PRO   B C    
3708 O  O    . PRO   B 236 ? 1.0467 1.3523 0.7855 -0.4532 -0.3244 -0.0092 235 PRO   B O    
3709 C  CB   . PRO   B 236 ? 1.1314 1.2741 0.834  -0.4718 -0.3318 -0.0105 235 PRO   B CB   
3710 C  CG   . PRO   B 236 ? 1.1693 1.261  0.8329 -0.4436 -0.3385 -0.0089 235 PRO   B CG   
3711 C  CD   . PRO   B 236 ? 1.1412 1.2627 0.8009 -0.4245 -0.3576 -0.0383 235 PRO   B CD   
3712 N  N    . VAL   B 237 ? 1.0831 1.3202 0.7537 -0.4024 -0.3302 0.0015  236 VAL   B N    
3713 C  CA   . VAL   B 237 ? 1.0752 1.3394 0.734  -0.3816 -0.3179 0.018   236 VAL   B CA   
3714 C  C    . VAL   B 237 ? 1.0694 1.3309 0.7372 -0.4043 -0.2985 0.0401  236 VAL   B C    
3715 O  O    . VAL   B 237 ? 1.0482 1.3459 0.7499 -0.4297 -0.2931 0.0376  236 VAL   B O    
3716 C  CB   . VAL   B 237 ? 1.0559 1.3898 0.7285 -0.3614 -0.3245 0.004   236 VAL   B CB   
3717 C  CG1  . VAL   B 237 ? 1.0564 1.4172 0.7231 -0.345  -0.3076 0.0208  236 VAL   B CG1  
3718 C  CG2  . VAL   B 237 ? 1.0716 1.4003 0.7212 -0.3304 -0.3404 -0.0107 236 VAL   B CG2  
3719 N  N    . LEU   B 238 ? 1.0853 1.3046 0.7223 -0.3953 -0.2881 0.0613  237 LEU   B N    
3720 C  CA   . LEU   B 238 ? 1.0851 1.2951 0.7198 -0.4127 -0.2703 0.0844  237 LEU   B CA   
3721 C  C    . LEU   B 238 ? 1.0714 1.3275 0.7056 -0.4011 -0.2569 0.0908  237 LEU   B C    
3722 O  O    . LEU   B 238 ? 1.0708 1.3457 0.6934 -0.3724 -0.2594 0.0836  237 LEU   B O    
3723 C  CB   . LEU   B 238 ? 1.1132 1.2623 0.7132 -0.4059 -0.2672 0.1032  237 LEU   B CB   
3724 C  CG   . LEU   B 238 ? 1.1439 1.242  0.7323 -0.4004 -0.2805 0.0967  237 LEU   B CG   
3725 C  CD1  . LEU   B 238 ? 1.1712 1.2344 0.7247 -0.3762 -0.2802 0.1081  237 LEU   B CD1  
3726 C  CD2  . LEU   B 238 ? 1.156  1.2194 0.7594 -0.4299 -0.2792 0.102   237 LEU   B CD2  
3727 N  N    . GLU   B 239 ? 1.0601 1.3303 0.7044 -0.4223 -0.2405 0.1055  238 GLU   B N    
3728 C  CA   . GLU   B 239 ? 1.0505 1.3606 0.6925 -0.4131 -0.2247 0.112   238 GLU   B CA   
3729 C  C    . GLU   B 239 ? 1.0778 1.3547 0.6788 -0.3989 -0.2151 0.1285  238 GLU   B C    
3730 O  O    . GLU   B 239 ? 1.1061 1.3331 0.6845 -0.4007 -0.2198 0.1385  238 GLU   B O    
3731 C  CB   . GLU   B 239 ? 1.0502 1.3977 0.7233 -0.4418 -0.2099 0.1183  238 GLU   B CB   
3732 C  CG   . GLU   B 239 ? 1.0613 1.4709 0.7787 -0.4471 -0.215  0.099   238 GLU   B CG   
3733 C  CD   . GLU   B 239 ? 1.1158 1.5658 0.8338 -0.4133 -0.222  0.0844  238 GLU   B CD   
3734 O  OE1  . GLU   B 239 ? 1.1275 1.5879 0.8566 -0.4043 -0.241  0.0662  238 GLU   B OE1  
3735 O  OE2  . GLU   B 239 ? 1.1323 1.6033 0.8389 -0.3952 -0.2077 0.0909  238 GLU   B OE2  
3736 N  N    . THR   B 240 ? 1.0651 1.3712 0.6576 -0.3842 -0.2018 0.1299  239 THR   B N    
3737 C  CA   . THR   B 240 ? 1.0844 1.3667 0.6401 -0.3719 -0.192  0.1407  239 THR   B CA   
3738 C  C    . THR   B 240 ? 1.0954 1.3498 0.635  -0.3942 -0.185  0.1614  239 THR   B C    
3739 O  O    . THR   B 240 ? 1.1163 1.3286 0.6296 -0.3899 -0.1911 0.1698  239 THR   B O    
3740 C  CB   . THR   B 240 ? 1.0868 1.4094 0.6419 -0.3564 -0.1757 0.1361  239 THR   B CB   
3741 O  OG1  . THR   B 240 ? 1.0811 1.4354 0.6565 -0.3365 -0.1818 0.12    239 THR   B OG1  
3742 C  CG2  . THR   B 240 ? 1.1114 1.4099 0.6294 -0.3407 -0.1669 0.14    239 THR   B CG2  
3743 N  N    . ASP   B 241 ? 1.0795 1.3584 0.6375 -0.418  -0.1726 0.1702  240 ASP   B N    
3744 C  CA   . ASP   B 241 ? 1.0928 1.3523 0.6365 -0.4393 -0.162  0.1928  240 ASP   B CA   
3745 C  C    . ASP   B 241 ? 1.109  1.3224 0.6541 -0.4548 -0.1722 0.2036  240 ASP   B C    
3746 O  O    . ASP   B 241 ? 1.1306 1.3132 0.6503 -0.4609 -0.168  0.2245  240 ASP   B O    
3747 C  CB   . ASP   B 241 ? 1.084  1.3866 0.6496 -0.4591 -0.1425 0.1987  240 ASP   B CB   
3748 C  CG   . ASP   B 241 ? 1.0997 1.4296 0.7134 -0.4774 -0.1454 0.1884  240 ASP   B CG   
3749 O  OD1  . ASP   B 241 ? 1.0929 1.4383 0.7264 -0.4649 -0.1599 0.1678  240 ASP   B OD1  
3750 O  OD2  . ASP   B 241 ? 1.1139 1.4514 0.7456 -0.5045 -0.1327 0.2005  240 ASP   B OD2  
3751 N  N    . THR   B 242 ? 1.0965 1.306  0.6706 -0.4606 -0.1849 0.1895  241 THR   B N    
3752 C  CA   . THR   B 242 ? 1.1114 1.2743 0.6904 -0.4755 -0.1933 0.1962  241 THR   B CA   
3753 C  C    . THR   B 242 ? 1.1383 1.2522 0.6833 -0.4567 -0.2043 0.2033  241 THR   B C    
3754 O  O    . THR   B 242 ? 1.1583 1.2313 0.6904 -0.4654 -0.203  0.2227  241 THR   B O    
3755 C  CB   . THR   B 242 ? 1.1091 1.2843 0.7258 -0.4844 -0.205  0.1732  241 THR   B CB   
3756 O  OG1  . THR   B 242 ? 1.0938 1.3149 0.746  -0.507  -0.1933 0.17    241 THR   B OG1  
3757 C  CG2  . THR   B 242 ? 1.1299 1.2515 0.7502 -0.4962 -0.2146 0.1744  241 THR   B CG2  
3758 N  N    . VAL   B 243 ? 1.1344 1.2538 0.6657 -0.43   -0.2135 0.1891  242 VAL   B N    
3759 C  CA   . VAL   B 243 ? 1.1571 1.2378 0.6602 -0.4104 -0.2232 0.1928  242 VAL   B CA   
3760 C  C    . VAL   B 243 ? 1.1664 1.2377 0.6382 -0.409  -0.2147 0.2143  242 VAL   B C    
3761 O  O    . VAL   B 243 ? 1.1826 1.2166 0.6366 -0.405  -0.2209 0.2275  242 VAL   B O    
3762 C  CB   . VAL   B 243 ? 1.1639 1.2578 0.6635 -0.384  -0.2313 0.1721  242 VAL   B CB   
3763 C  CG1  . VAL   B 243 ? 1.1938 1.2536 0.6659 -0.3642 -0.238  0.1758  242 VAL   B CG1  
3764 C  CG2  . VAL   B 243 ? 1.1585 1.2588 0.6836 -0.3837 -0.243  0.1522  242 VAL   B CG2  
3765 N  N    . ALA   B 244 ? 1.1551 1.2622 0.6205 -0.4123 -0.2004 0.2175  243 ALA   B N    
3766 C  CA   . ALA   B 244 ? 1.1724 1.2789 0.606  -0.4122 -0.1915 0.235   243 ALA   B CA   
3767 C  C    . ALA   B 244 ? 1.1861 1.2693 0.6132 -0.4311 -0.187  0.2617  243 ALA   B C    
3768 O  O    . ALA   B 244 ? 1.2023 1.2664 0.6006 -0.4262 -0.189  0.279   243 ALA   B O    
3769 C  CB   . ALA   B 244 ? 1.161  1.3117 0.5917 -0.4127 -0.1753 0.2294  243 ALA   B CB   
3770 N  N    . ARG   B 245 ? 1.1749 1.2604 0.6297 -0.4523 -0.1805 0.2655  244 ARG   B N    
3771 C  CA   . ARG   B 245 ? 1.1898 1.2475 0.6423 -0.4712 -0.1731 0.2919  244 ARG   B CA   
3772 C  C    . ARG   B 245 ? 1.2117 1.2162 0.6582 -0.4638 -0.1875 0.2994  244 ARG   B C    
3773 O  O    . ARG   B 245 ? 1.2274 1.2037 0.6533 -0.4653 -0.1848 0.3256  244 ARG   B O    
3774 C  CB   . ARG   B 245 ? 1.1907 1.2625 0.6807 -0.4974 -0.1618 0.2899  244 ARG   B CB   
3775 C  CG   . ARG   B 245 ? 1.212  1.3366 0.7097 -0.5066 -0.144  0.2878  244 ARG   B CG   
3776 C  CD   . ARG   B 245 ? 1.2457 1.3774 0.7757 -0.5371 -0.1285 0.2967  244 ARG   B CD   
3777 N  NE   . ARG   B 245 ? 1.2595 1.4367 0.8325 -0.5456 -0.1274 0.2718  244 ARG   B NE   
3778 C  CZ   . ARG   B 245 ? 1.2779 1.4519 0.8839 -0.5499 -0.1415 0.2503  244 ARG   B CZ   
3779 N  NH1  . ARG   B 245 ? 1.297  1.4202 0.8974 -0.5464 -0.1563 0.2495  244 ARG   B NH1  
3780 N  NH2  . ARG   B 245 ? 1.2427 1.4664 0.8872 -0.5566 -0.1411 0.2287  244 ARG   B NH2  
3781 N  N    . SER   B 246 ? 1.2096 1.2015 0.6731 -0.454  -0.2021 0.2772  245 SER   B N    
3782 C  CA   . SER   B 246 ? 1.2314 1.174  0.6904 -0.4445 -0.2149 0.2809  245 SER   B CA   
3783 C  C    . SER   B 246 ? 1.2479 1.1808 0.6734 -0.4222 -0.222  0.2916  245 SER   B C    
3784 O  O    . SER   B 246 ? 1.2656 1.1618 0.6789 -0.4175 -0.2259 0.3108  245 SER   B O    
3785 C  CB   . SER   B 246 ? 1.2405 1.1787 0.7217 -0.4375 -0.2278 0.252   245 SER   B CB   
3786 O  OG   . SER   B 246 ? 1.2554 1.1956 0.7692 -0.4603 -0.2242 0.2424  245 SER   B OG   
3787 N  N    . LEU   B 247 ? 1.2399 1.2064 0.6521 -0.4087 -0.2228 0.2792  246 LEU   B N    
3788 C  CA   . LEU   B 247 ? 1.2555 1.2195 0.6394 -0.3904 -0.2292 0.2852  246 LEU   B CA   
3789 C  C    . LEU   B 247 ? 1.2754 1.2441 0.6333 -0.397  -0.2216 0.3125  246 LEU   B C    
3790 O  O    . LEU   B 247 ? 1.2943 1.2431 0.6341 -0.387  -0.2293 0.3288  246 LEU   B O    
3791 C  CB   . LEU   B 247 ? 1.2445 1.2399 0.6232 -0.3765 -0.2294 0.2624  246 LEU   B CB   
3792 C  CG   . LEU   B 247 ? 1.2648 1.2604 0.6191 -0.3598 -0.2357 0.2629  246 LEU   B CG   
3793 C  CD1  . LEU   B 247 ? 1.2818 1.242  0.6379 -0.3468 -0.2496 0.2664  246 LEU   B CD1  
3794 C  CD2  . LEU   B 247 ? 1.263  1.2837 0.6159 -0.3486 -0.2321 0.2394  246 LEU   B CD2  
3795 N  N    . ILE   B 248 ? 1.2692 1.2652 0.6252 -0.413  -0.2062 0.319   247 ILE   B N    
3796 C  CA   . ILE   B 248 ? 1.2852 1.287  0.612  -0.4188 -0.1976 0.3465  247 ILE   B CA   
3797 C  C    . ILE   B 248 ? 1.3008 1.2607 0.6267 -0.4246 -0.1979 0.3757  247 ILE   B C    
3798 O  O    . ILE   B 248 ? 1.3161 1.269  0.6135 -0.4173 -0.2    0.3996  247 ILE   B O    
3799 C  CB   . ILE   B 248 ? 1.2833 1.3242 0.6047 -0.4334 -0.1785 0.3479  247 ILE   B CB   
3800 C  CG1  . ILE   B 248 ? 1.3026 1.357  0.5827 -0.4319 -0.1726 0.3702  247 ILE   B CG1  
3801 C  CG2  . ILE   B 248 ? 1.2835 1.3206 0.6331 -0.4559 -0.165  0.3554  247 ILE   B CG2  
3802 C  CD1  . ILE   B 248 ? 1.3163 1.3995 0.5734 -0.4191 -0.1764 0.3533  247 ILE   B CD1  
3803 N  N    . ASP   B 249 ? 1.2961 1.2277 0.6529 -0.4361 -0.1964 0.3729  248 ASP   B N    
3804 C  CA   . ASP   B 249 ? 1.3151 1.1998 0.6734 -0.4419 -0.1938 0.3996  248 ASP   B CA   
3805 C  C    . ASP   B 249 ? 1.3249 1.173  0.6769 -0.4205 -0.2105 0.4033  248 ASP   B C    
3806 O  O    . ASP   B 249 ? 1.3417 1.1556 0.6822 -0.4167 -0.2092 0.4319  248 ASP   B O    
3807 C  CB   . ASP   B 249 ? 1.337  1.2041 0.7318 -0.4658 -0.1835 0.3939  248 ASP   B CB   
3808 C  CG   . ASP   B 249 ? 1.3892 1.2888 0.7912 -0.4887 -0.1633 0.3999  248 ASP   B CG   
3809 O  OD1  . ASP   B 249 ? 1.4038 1.3107 0.7782 -0.4911 -0.1514 0.4277  248 ASP   B OD1  
3810 O  OD2  . ASP   B 249 ? 1.399  1.3201 0.8339 -0.5035 -0.1595 0.3768  248 ASP   B OD2  
3811 N  N    . GLY   B 250 ? 1.3148 1.171  0.6737 -0.4054 -0.2244 0.3763  249 GLY   B N    
3812 C  CA   . GLY   B 250 ? 1.3273 1.1547 0.6828 -0.3842 -0.2392 0.3766  249 GLY   B CA   
3813 C  C    . GLY   B 250 ? 1.3281 1.1732 0.6533 -0.3667 -0.2467 0.391   249 GLY   B C    
3814 O  O    . GLY   B 250 ? 1.3395 1.1599 0.6578 -0.3513 -0.2553 0.4067  249 GLY   B O    
3815 N  N    . ILE   B 251 ? 1.3131 1.203  0.6211 -0.3686 -0.2435 0.3841  250 ILE   B N    
3816 C  CA   . ILE   B 251 ? 1.3188 1.2327 0.5974 -0.3553 -0.2509 0.3936  250 ILE   B CA   
3817 C  C    . ILE   B 251 ? 1.3394 1.2458 0.5938 -0.3573 -0.2461 0.4318  250 ILE   B C    
3818 O  O    . ILE   B 251 ? 1.3511 1.256  0.5882 -0.3413 -0.257  0.4489  250 ILE   B O    
3819 C  CB   . ILE   B 251 ? 1.3094 1.2703 0.5767 -0.3584 -0.2466 0.3717  250 ILE   B CB   
3820 C  CG1  . ILE   B 251 ? 1.3125 1.2775 0.6007 -0.3511 -0.2514 0.3377  250 ILE   B CG1  
3821 C  CG2  . ILE   B 251 ? 1.3149 1.3042 0.5494 -0.3496 -0.2529 0.3807  250 ILE   B CG2  
3822 C  CD1  . ILE   B 251 ? 1.316  1.3184 0.5988 -0.3552 -0.2428 0.316   250 ILE   B CD1  
3823 N  N    . LEU   B 252 ? 1.3394 1.2412 0.5941 -0.3764 -0.2293 0.4465  251 LEU   B N    
3824 C  CA   . LEU   B 252 ? 1.3502 1.242  0.5813 -0.3802 -0.2199 0.4854  251 LEU   B CA   
3825 C  C    . LEU   B 252 ? 1.3723 1.2117 0.6095 -0.371  -0.223  0.5121  251 LEU   B C    
3826 O  O    . LEU   B 252 ? 1.3898 1.2225 0.6008 -0.3625 -0.2217 0.5469  251 LEU   B O    
3827 C  CB   . LEU   B 252 ? 1.3435 1.2448 0.5778 -0.4046 -0.198  0.4915  251 LEU   B CB   
3828 C  CG   . LEU   B 252 ? 1.3465 1.3008 0.5672 -0.4113 -0.1914 0.4726  251 LEU   B CG   
3829 C  CD1  . LEU   B 252 ? 1.348  1.3115 0.5769 -0.4347 -0.1684 0.4798  251 LEU   B CD1  
3830 C  CD2  . LEU   B 252 ? 1.3596 1.3457 0.5371 -0.3983 -0.1979 0.4833  251 LEU   B CD2  
3831 N  N    . THR   B 253 ? 1.3712 1.1735 0.6409 -0.3711 -0.2266 0.4966  252 THR   B N    
3832 C  CA   . THR   B 253 ? 1.3893 1.1382 0.6657 -0.3599 -0.229  0.5187  252 THR   B CA   
3833 C  C    . THR   B 253 ? 1.3889 1.1352 0.6673 -0.3332 -0.2492 0.5085  252 THR   B C    
3834 O  O    . THR   B 253 ? 1.4062 1.111  0.6897 -0.3193 -0.2522 0.5259  252 THR   B O    
3835 C  CB   . THR   B 253 ? 1.4087 1.1116 0.7172 -0.3789 -0.2166 0.513   252 THR   B CB   
3836 O  OG1  . THR   B 253 ? 1.4108 1.1181 0.7462 -0.3814 -0.2248 0.4727  252 THR   B OG1  
3837 C  CG2  . THR   B 253 ? 1.4106 1.1192 0.7206 -0.406  -0.1955 0.5246  252 THR   B CG2  
3838 N  N    . ASN   B 254 ? 1.3661 1.1558 0.6408 -0.3259 -0.2609 0.4815  253 ASN   B N    
3839 C  CA   . ASN   B 254 ? 1.3571 1.154  0.6355 -0.3035 -0.2781 0.4683  253 ASN   B CA   
3840 C  C    . ASN   B 254 ? 1.3516 1.1073 0.6595 -0.2975 -0.2813 0.451   253 ASN   B C    
3841 O  O    . ASN   B 254 ? 1.3589 1.0954 0.6711 -0.2772 -0.2905 0.4582  253 ASN   B O    
3842 C  CB   . ASN   B 254 ? 1.3737 1.1788 0.6296 -0.2832 -0.2878 0.4988  253 ASN   B CB   
3843 C  CG   . ASN   B 254 ? 1.4051 1.2595 0.6278 -0.2861 -0.2885 0.5101  253 ASN   B CG   
3844 O  OD1  . ASN   B 254 ? 1.4284 1.2838 0.6269 -0.2793 -0.2878 0.5448  253 ASN   B OD1  
3845 N  ND2  . ASN   B 254 ? 1.4001 1.2957 0.6191 -0.2951 -0.2892 0.4812  253 ASN   B ND2  
3846 N  N    . LYS   B 255 ? 1.3352 1.0802 0.6634 -0.3143 -0.2738 0.4275  254 LYS   B N    
3847 C  CA   . LYS   B 255 ? 1.3333 1.0418 0.6863 -0.3099 -0.2768 0.4078  254 LYS   B CA   
3848 C  C    . LYS   B 255 ? 1.3155 1.0465 0.674  -0.2949 -0.288  0.3791  254 LYS   B C    
3849 O  O    . LYS   B 255 ? 1.3042 1.0759 0.6575 -0.2988 -0.2885 0.3617  254 LYS   B O    
3850 C  CB   . LYS   B 255 ? 1.356  1.0473 0.7292 -0.3337 -0.2662 0.3933  254 LYS   B CB   
3851 C  CG   . LYS   B 255 ? 1.4175 1.0609 0.8124 -0.3306 -0.2681 0.3791  254 LYS   B CG   
3852 C  CD   . LYS   B 255 ? 1.4785 1.0891 0.8907 -0.3554 -0.2553 0.3809  254 LYS   B CD   
3853 C  CE   . LYS   B 255 ? 1.5383 1.0923 0.9671 -0.3511 -0.2558 0.3727  254 LYS   B CE   
3854 N  NZ   . LYS   B 255 ? 1.5597 1.1211 0.9988 -0.3413 -0.2668 0.3361  254 LYS   B NZ   
3855 N  N    . LYS   B 256 ? 1.3126 1.015  0.6811 -0.2769 -0.295  0.3752  255 LYS   B N    
3856 C  CA   . LYS   B 256 ? 1.303  1.0213 0.6774 -0.2609 -0.3035 0.3513  255 LYS   B CA   
3857 C  C    . LYS   B 256 ? 1.292  1.0153 0.6789 -0.2687 -0.301  0.3183  255 LYS   B C    
3858 O  O    . LYS   B 256 ? 1.2833 1.0363 0.6686 -0.2623 -0.3036 0.2996  255 LYS   B O    
3859 C  CB   . LYS   B 256 ? 1.3323 1.0163 0.7154 -0.2391 -0.3091 0.3578  255 LYS   B CB   
3860 C  CG   . LYS   B 256 ? 1.3788 1.0567 0.7516 -0.227  -0.3123 0.3925  255 LYS   B CG   
3861 C  CD   . LYS   B 256 ? 1.4158 1.1441 0.7768 -0.2167 -0.3216 0.3962  255 LYS   B CD   
3862 C  CE   . LYS   B 256 ? 1.4646 1.1907 0.816  -0.2012 -0.3271 0.4309  255 LYS   B CE   
3863 N  NZ   . LYS   B 256 ? 1.4992 1.2134 0.8342 -0.2147 -0.3188 0.4583  255 LYS   B NZ   
3864 N  N    . MET   B 257 ? 1.2896 0.9837 0.6895 -0.2818 -0.296  0.3108  256 MET   B N    
3865 C  CA   . MET   B 257 ? 1.2819 0.984  0.6935 -0.2877 -0.2957 0.2798  256 MET   B CA   
3866 C  C    . MET   B 257 ? 1.2838 0.9949 0.7037 -0.3131 -0.2882 0.2759  256 MET   B C    
3867 O  O    . MET   B 257 ? 1.2913 0.9697 0.7227 -0.3263 -0.284  0.2799  256 MET   B O    
3868 C  CB   . MET   B 257 ? 1.2859 0.9492 0.7088 -0.2767 -0.2995 0.2645  256 MET   B CB   
3869 C  CG   . MET   B 257 ? 1.2785 0.9586 0.7065 -0.2727 -0.3023 0.2331  256 MET   B CG   
3870 S  SD   . MET   B 257 ? 1.2379 0.9525 0.6552 -0.2509 -0.3053 0.225   256 MET   B SD   
3871 C  CE   . MET   B 257 ? 1.2053 0.8827 0.6247 -0.227  -0.3095 0.2287  256 MET   B CE   
3872 N  N    . ILE   B 258 ? 1.2754 1.0305 0.692  -0.3201 -0.2853 0.2668  257 ILE   B N    
3873 C  CA   . ILE   B 258 ? 1.278  1.0517 0.7052 -0.3434 -0.2773 0.2625  257 ILE   B CA   
3874 C  C    . ILE   B 258 ? 1.2793 1.0643 0.7239 -0.3456 -0.2807 0.2315  257 ILE   B C    
3875 O  O    . ILE   B 258 ? 1.2691 1.0911 0.712  -0.3399 -0.2808 0.2166  257 ILE   B O    
3876 C  CB   . ILE   B 258 ? 1.2747 1.0914 0.6884 -0.3501 -0.2701 0.2722  257 ILE   B CB   
3877 C  CG1  . ILE   B 258 ? 1.2942 1.108  0.6852 -0.3427 -0.2703 0.2996  257 ILE   B CG1  
3878 C  CG2  . ILE   B 258 ? 1.2729 1.1049 0.6991 -0.3755 -0.2591 0.2746  257 ILE   B CG2  
3879 C  CD1  . ILE   B 258 ? 1.3022 1.1591 0.6756 -0.3459 -0.2648 0.3036  257 ILE   B CD1  
3880 N  N    . PHE   B 259 ? 1.2908 1.0441 0.7512 -0.3534 -0.283  0.2217  258 PHE   B N    
3881 C  CA   . PHE   B 259 ? 1.2937 1.0603 0.7696 -0.3561 -0.2883 0.1915  258 PHE   B CA   
3882 C  C    . PHE   B 259 ? 1.293  1.094  0.7867 -0.3803 -0.282  0.1861  258 PHE   B C    
3883 O  O    . PHE   B 259 ? 1.3012 1.0889 0.8043 -0.4021 -0.2734 0.2013  258 PHE   B O    
3884 C  CB   . PHE   B 259 ? 1.3001 1.0204 0.7861 -0.358  -0.2929 0.1806  258 PHE   B CB   
3885 C  CG   . PHE   B 259 ? 1.3138 1.009  0.7865 -0.3311 -0.3    0.175   258 PHE   B CG   
3886 C  CD1  . PHE   B 259 ? 1.3148 1.0366 0.7782 -0.3107 -0.3054 0.1594  258 PHE   B CD1  
3887 C  CD2  . PHE   B 259 ? 1.3378 0.9818 0.8086 -0.3252 -0.2995 0.186   258 PHE   B CD2  
3888 C  CE1  . PHE   B 259 ? 1.3331 1.0327 0.7858 -0.2867 -0.3096 0.1549  258 PHE   B CE1  
3889 C  CE2  . PHE   B 259 ? 1.3551 0.9789 0.8161 -0.2999 -0.3046 0.1806  258 PHE   B CE2  
3890 C  CZ   . PHE   B 259 ? 1.3458 0.9983 0.7981 -0.2817 -0.3095 0.1649  258 PHE   B CZ   
3891 N  N    . VAL   B 260 ? 1.2796 1.1251 0.7793 -0.376  -0.2849 0.166   259 VAL   B N    
3892 C  CA   . VAL   B 260 ? 1.2715 1.1569 0.7921 -0.3972 -0.2791 0.1597  259 VAL   B CA   
3893 C  C    . VAL   B 260 ? 1.2712 1.1768 0.811  -0.3981 -0.2889 0.1293  259 VAL   B C    
3894 O  O    . VAL   B 260 ? 1.267  1.1984 0.7993 -0.3771 -0.2951 0.115   259 VAL   B O    
3895 C  CB   . VAL   B 260 ? 1.2694 1.1999 0.7808 -0.3923 -0.2707 0.1676  259 VAL   B CB   
3896 C  CG1  . VAL   B 260 ? 1.256  1.2255 0.7911 -0.4158 -0.2618 0.1656  259 VAL   B CG1  
3897 C  CG2  . VAL   B 260 ? 1.291  1.2054 0.7777 -0.3873 -0.2641 0.1941  259 VAL   B CG2  
3898 N  N    . PRO   B 261 ? 1.2749 1.1664 0.838  -0.4207 -0.2909 0.1183  260 PRO   B N    
3899 C  CA   . PRO   B 261 ? 1.2886 1.1441 0.864  -0.4475 -0.2812 0.134   260 PRO   B CA   
3900 C  C    . PRO   B 261 ? 1.3248 1.1139 0.8863 -0.4401 -0.2825 0.144   260 PRO   B C    
3901 O  O    . PRO   B 261 ? 1.335  1.1066 0.884  -0.4186 -0.2928 0.1309  260 PRO   B O    
3902 C  CB   . PRO   B 261 ? 1.2766 1.1546 0.8876 -0.4743 -0.2833 0.1099  260 PRO   B CB   
3903 C  CG   . PRO   B 261 ? 1.2607 1.1926 0.8756 -0.458  -0.2963 0.0829  260 PRO   B CG   
3904 C  CD   . PRO   B 261 ? 1.2558 1.1724 0.8373 -0.4229 -0.3025 0.0865  260 PRO   B CD   
3905 N  N    . SER   B 262 ? 1.3435 1.0959 0.9064 -0.4559 -0.2706 0.1692  261 SER   B N    
3906 C  CA   . SER   B 262 ? 1.3827 1.0709 0.9335 -0.4483 -0.2686 0.1854  261 SER   B CA   
3907 C  C    . SER   B 262 ? 1.4084 1.0562 0.9667 -0.4453 -0.2768 0.1608  261 SER   B C    
3908 O  O    . SER   B 262 ? 1.4298 1.0339 0.9729 -0.4263 -0.2788 0.1689  261 SER   B O    
3909 C  CB   . SER   B 262 ? 1.4045 1.0629 0.9615 -0.4706 -0.2521 0.2144  261 SER   B CB   
3910 O  OG   . SER   B 262 ? 1.4224 1.071  1.0108 -0.5019 -0.2458 0.1992  261 SER   B OG   
3911 N  N    . TYR   B 263 ? 1.4046 1.0682 0.9871 -0.4644 -0.2812 0.1305  262 TYR   B N    
3912 C  CA   . TYR   B 263 ? 1.4289 1.0578 1.0184 -0.4651 -0.2891 0.1022  262 TYR   B CA   
3913 C  C    . TYR   B 263 ? 1.4491 1.0889 1.0187 -0.4337 -0.3038 0.0821  262 TYR   B C    
3914 O  O    . TYR   B 263 ? 1.4669 1.0693 1.0335 -0.4276 -0.309  0.0634  262 TYR   B O    
3915 C  CB   . TYR   B 263 ? 1.4115 1.0586 1.0347 -0.4986 -0.2899 0.0738  262 TYR   B CB   
3916 C  CG   . TYR   B 263 ? 1.3905 1.1157 1.0272 -0.5036 -0.2972 0.0578  262 TYR   B CG   
3917 C  CD1  . TYR   B 263 ? 1.3934 1.1576 1.0192 -0.4806 -0.3133 0.0341  262 TYR   B CD1  
3918 C  CD2  . TYR   B 263 ? 1.3824 1.1418 1.0446 -0.5315 -0.2868 0.0658  262 TYR   B CD2  
3919 C  CE1  . TYR   B 263 ? 1.3778 1.2134 1.0165 -0.4821 -0.3194 0.0212  262 TYR   B CE1  
3920 C  CE2  . TYR   B 263 ? 1.3647 1.1977 1.0424 -0.5346 -0.2928 0.051   262 TYR   B CE2  
3921 C  CZ   . TYR   B 263 ? 1.3685 1.2393 1.0345 -0.509  -0.3096 0.0289  262 TYR   B CZ   
3922 O  OH   . TYR   B 263 ? 1.3589 1.3025 1.0401 -0.5085 -0.3148 0.0169  262 TYR   B OH   
3923 N  N    . ILE   B 264 ? 1.4468 1.1352 1.0024 -0.414  -0.3089 0.0851  263 ILE   B N    
3924 C  CA   . ILE   B 264 ? 1.4666 1.1652 1.0027 -0.3836 -0.32   0.0689  263 ILE   B CA   
3925 C  C    . ILE   B 264 ? 1.5061 1.1519 1.0215 -0.36   -0.3187 0.0813  263 ILE   B C    
3926 O  O    . ILE   B 264 ? 1.5096 1.1554 1.0089 -0.3348 -0.3253 0.0692  263 ILE   B O    
3927 C  CB   . ILE   B 264 ? 1.4598 1.2174 0.9873 -0.3689 -0.322  0.072   263 ILE   B CB   
3928 C  CG1  . ILE   B 264 ? 1.4715 1.2586 0.9918 -0.3499 -0.3338 0.0441  263 ILE   B CG1  
3929 C  CG2  . ILE   B 264 ? 1.4747 1.2253 0.9819 -0.3508 -0.3156 0.0996  263 ILE   B CG2  
3930 C  CD1  . ILE   B 264 ? 1.467  1.303  1.0108 -0.3679 -0.3418 0.0178  263 ILE   B CD1  
3931 N  N    . ASN   B 265 ? 1.5352 1.1369 1.0519 -0.3673 -0.3091 0.1064  264 ASN   B N    
3932 C  CA   . ASN   B 265 ? 1.5783 1.1309 1.081  -0.3464 -0.3069 0.1202  264 ASN   B CA   
3933 C  C    . ASN   B 265 ? 1.6064 1.1135 1.1144 -0.3481 -0.3091 0.0954  264 ASN   B C    
3934 O  O    . ASN   B 265 ? 1.6177 1.1035 1.1118 -0.3235 -0.3124 0.0884  264 ASN   B O    
3935 C  CB   . ASN   B 265 ? 1.6116 1.1362 1.1146 -0.3536 -0.2958 0.1569  264 ASN   B CB   
3936 C  CG   . ASN   B 265 ? 1.6859 1.1613 1.1781 -0.3314 -0.2933 0.174   264 ASN   B CG   
3937 O  OD1  . ASN   B 265 ? 1.7087 1.1814 1.1897 -0.3059 -0.2993 0.1644  264 ASN   B OD1  
3938 N  ND2  . ASN   B 265 ? 1.7103 1.1466 1.206  -0.3393 -0.2831 0.2015  264 ASN   B ND2  
3939 N  N    . ILE   B 266 ? 1.6159 1.1079 1.1447 -0.3779 -0.3061 0.081   265 ILE   B N    
3940 C  CA   . ILE   B 266 ? 1.6455 1.0933 1.1797 -0.3829 -0.3077 0.0529  265 ILE   B CA   
3941 C  C    . ILE   B 266 ? 1.6556 1.1352 1.1802 -0.3697 -0.3219 0.0165  265 ILE   B C    
3942 O  O    . ILE   B 266 ? 1.6733 1.1173 1.1884 -0.3575 -0.3242 -0.0028 265 ILE   B O    
3943 C  CB   . ILE   B 266 ? 1.6526 1.0723 1.2138 -0.4208 -0.2992 0.0451  265 ILE   B CB   
3944 C  CG1  . ILE   B 266 ? 1.6378 1.1142 1.2197 -0.4473 -0.3068 0.0184  265 ILE   B CG1  
3945 C  CG2  . ILE   B 266 ? 1.6683 1.0581 1.2351 -0.4312 -0.2832 0.0859  265 ILE   B CG2  
3946 C  CD1  . ILE   B 266 ? 1.6538 1.1182 1.2485 -0.4636 -0.3139 -0.0248 265 ILE   B CD1  
3947 N  N    . PHE   B 267 ? 1.645  1.1903 1.1695 -0.369  -0.3304 0.0089  266 PHE   B N    
3948 C  CA   . PHE   B 267 ? 1.6554 1.236  1.1675 -0.3526 -0.3435 -0.021  266 PHE   B CA   
3949 C  C    . PHE   B 267 ? 1.682  1.2485 1.1661 -0.3152 -0.3438 -0.0142 266 PHE   B C    
3950 O  O    . PHE   B 267 ? 1.6901 1.25   1.16   -0.2999 -0.3503 -0.0388 266 PHE   B O    
3951 C  CB   . PHE   B 267 ? 1.632  1.2849 1.1511 -0.3571 -0.3499 -0.0243 266 PHE   B CB   
3952 C  CG   . PHE   B 267 ? 1.6255 1.3036 1.1744 -0.392  -0.3532 -0.0435 266 PHE   B CG   
3953 C  CD1  . PHE   B 267 ? 1.6395 1.2972 1.1989 -0.4085 -0.3594 -0.0761 266 PHE   B CD1  
3954 C  CD2  . PHE   B 267 ? 1.6152 1.3394 1.1828 -0.4089 -0.3496 -0.0307 266 PHE   B CD2  
3955 C  CE1  . PHE   B 267 ? 1.6297 1.3144 1.2209 -0.4432 -0.3625 -0.096  266 PHE   B CE1  
3956 C  CE2  . PHE   B 267 ? 1.6059 1.3576 1.2053 -0.4419 -0.3517 -0.0487 266 PHE   B CE2  
3957 C  CZ   . PHE   B 267 ? 1.6054 1.3384 1.2178 -0.4597 -0.3586 -0.0815 266 PHE   B CZ   
3958 N  N    . LEU   B 268 ? 1.6928 1.2559 1.1694 -0.3012 -0.3363 0.0184  267 LEU   B N    
3959 C  CA   . LEU   B 268 ? 1.7165 1.2674 1.172  -0.2681 -0.3347 0.0269  267 LEU   B CA   
3960 C  C    . LEU   B 268 ? 1.7497 1.2382 1.201  -0.2585 -0.33   0.0246  267 LEU   B C    
3961 O  O    . LEU   B 268 ? 1.7607 1.2387 1.1956 -0.232  -0.33   0.0183  267 LEU   B O    
3962 C  CB   . LEU   B 268 ? 1.7153 1.2834 1.1676 -0.2597 -0.3288 0.0598  267 LEU   B CB   
3963 C  CG   . LEU   B 268 ? 1.716  1.343  1.1681 -0.2623 -0.3311 0.0612  267 LEU   B CG   
3964 C  CD1  . LEU   B 268 ? 1.7216 1.3606 1.1725 -0.2613 -0.3244 0.0919  267 LEU   B CD1  
3965 C  CD2  . LEU   B 268 ? 1.7204 1.3739 1.1563 -0.2381 -0.3357 0.0441  267 LEU   B CD2  
3966 N  N    . ILE   B 269 ? 1.7639 1.2098 1.2304 -0.2793 -0.3241 0.0302  268 ILE   B N    
3967 C  CA   . ILE   B 269 ? 1.7977 1.1795 1.2631 -0.2719 -0.3176 0.0276  268 ILE   B CA   
3968 C  C    . ILE   B 269 ? 1.8145 1.1861 1.2722 -0.2701 -0.3239 -0.0137 268 ILE   B C    
3969 O  O    . ILE   B 269 ? 1.8288 1.1742 1.2712 -0.2456 -0.322  -0.0221 268 ILE   B O    
3970 C  CB   . ILE   B 269 ? 1.8134 1.1533 1.2981 -0.2974 -0.3077 0.0447  268 ILE   B CB   
3971 C  CG1  . ILE   B 269 ? 1.8234 1.1684 1.3084 -0.2915 -0.3011 0.0885  268 ILE   B CG1  
3972 C  CG2  . ILE   B 269 ? 1.8436 1.1123 1.3306 -0.2957 -0.2998 0.0333  268 ILE   B CG2  
3973 C  CD1  . ILE   B 269 ? 1.8427 1.1598 1.3439 -0.3175 -0.2908 0.1098  268 ILE   B CD1  
3974 N  N    . LEU   B 270 ? 1.8091 1.2087 1.2768 -0.2949 -0.332  -0.0402 269 LEU   B N    
3975 C  CA   . LEU   B 270 ? 1.8246 1.225  1.2846 -0.2966 -0.341  -0.083  269 LEU   B CA   
3976 C  C    . LEU   B 270 ? 1.8337 1.2691 1.266  -0.2645 -0.3489 -0.0951 269 LEU   B C    
3977 O  O    . LEU   B 270 ? 1.8422 1.2677 1.2592 -0.2559 -0.3541 -0.1264 269 LEU   B O    
3978 C  CB   . LEU   B 270 ? 1.8099 1.2443 1.2909 -0.3314 -0.3495 -0.1068 269 LEU   B CB   
3979 C  CG   . LEU   B 270 ? 1.829  1.2378 1.3402 -0.3669 -0.3398 -0.0935 269 LEU   B CG   
3980 C  CD1  . LEU   B 270 ? 1.813  1.2674 1.348  -0.4003 -0.3484 -0.1179 269 LEU   B CD1  
3981 C  CD2  . LEU   B 270 ? 1.864  1.1915 1.3796 -0.373  -0.3274 -0.0958 269 LEU   B CD2  
3982 N  N    . ASP   B 271 ? 1.8303 1.3052 1.2552 -0.2472 -0.3486 -0.0708 270 ASP   B N    
3983 C  CA   . ASP   B 271 ? 1.8405 1.345  1.2401 -0.2159 -0.352  -0.0761 270 ASP   B CA   
3984 C  C    . ASP   B 271 ? 1.8673 1.3266 1.25   -0.1885 -0.3433 -0.0734 270 ASP   B C    
3985 O  O    . ASP   B 271 ? 1.8747 1.3417 1.2342 -0.1659 -0.3453 -0.0906 270 ASP   B O    
3986 C  CB   . ASP   B 271 ? 1.8484 1.3984 1.2479 -0.207  -0.3502 -0.0494 270 ASP   B CB   
3987 C  CG   . ASP   B 271 ? 1.883  1.4925 1.2885 -0.219  -0.3595 -0.0588 270 ASP   B CG   
3988 O  OD1  . ASP   B 271 ? 1.8822 1.5076 1.2883 -0.2291 -0.3699 -0.0886 270 ASP   B OD1  
3989 O  OD2  . ASP   B 271 ? 1.9013 1.5434 1.3112 -0.2177 -0.3563 -0.0375 270 ASP   B OD2  
3990 N  N    . LYS   B 272 ? 1.8795 1.293  1.2734 -0.1889 -0.3331 -0.0511 271 LYS   B N    
3991 C  CA   . LYS   B 272 ? 1.9048 1.2767 1.2876 -0.1626 -0.3239 -0.0473 271 LYS   B CA   
3992 C  C    . LYS   B 272 ? 1.9334 1.2514 1.3138 -0.1673 -0.3214 -0.0744 271 LYS   B C    
3993 O  O    . LYS   B 272 ? 1.9498 1.2169 1.3348 -0.1579 -0.3108 -0.0635 271 LYS   B O    
3994 C  CB   . LYS   B 272 ? 1.9228 1.2791 1.3176 -0.154  -0.3147 -0.0086 271 LYS   B CB   
3995 C  CG   . LYS   B 272 ? 1.9482 1.3485 1.336  -0.1345 -0.3138 0.0105  271 LYS   B CG   
3996 C  CD   . LYS   B 272 ? 1.9894 1.3725 1.3843 -0.1162 -0.3051 0.0396  271 LYS   B CD   
3997 C  CE   . LYS   B 272 ? 2.01   1.4342 1.3992 -0.0978 -0.3029 0.0523  271 LYS   B CE   
3998 N  NZ   . LYS   B 272 ? 2.0311 1.4637 1.4007 -0.076  -0.3001 0.0317  271 LYS   B NZ   
3999 N  N    . PHE   B 273 ? 1.9367 1.2681 1.3097 -0.1808 -0.3312 -0.1109 272 PHE   B N    
4000 C  CA   . PHE   B 273 ? 1.9638 1.2514 1.3316 -0.1886 -0.3309 -0.146  272 PHE   B CA   
4001 C  C    . PHE   B 273 ? 1.9604 1.2868 1.3047 -0.1834 -0.3439 -0.1836 272 PHE   B C    
4002 O  O    . PHE   B 273 ? 1.9462 1.3069 1.2989 -0.2078 -0.3564 -0.2035 272 PHE   B O    
4003 C  CB   . PHE   B 273 ? 1.9672 1.2271 1.3624 -0.2271 -0.3305 -0.1525 272 PHE   B CB   
4004 C  CG   . PHE   B 273 ? 1.9885 1.1958 1.4033 -0.2319 -0.3158 -0.1197 272 PHE   B CG   
4005 C  CD1  . PHE   B 273 ? 2.0231 1.1603 1.4375 -0.2238 -0.3033 -0.1245 272 PHE   B CD1  
4006 C  CD2  . PHE   B 273 ? 1.9849 1.2131 1.4172 -0.243  -0.3141 -0.0837 272 PHE   B CD2  
4007 C  CE1  . PHE   B 273 ? 2.0424 1.1321 1.474  -0.225  -0.2896 -0.0914 272 PHE   B CE1  
4008 C  CE2  . PHE   B 273 ? 2.0047 1.1873 1.4516 -0.2449 -0.3013 -0.0516 272 PHE   B CE2  
4009 C  CZ   . PHE   B 273 ? 2.0262 1.14   1.473  -0.2352 -0.2893 -0.0544 272 PHE   B CZ   
4010 P  PA   . NAD   C .   ? 0.7443 1.192  0.3339 0.0527  -0.3353 0.071   401 NAD   A PA   
4011 O  O1A  . NAD   C .   ? 0.7239 1.2119 0.3378 0.0801  -0.338  0.0679  401 NAD   A O1A  
4012 O  O2A  . NAD   C .   ? 0.7373 1.2087 0.3228 0.0253  -0.3387 0.0783  401 NAD   A O2A  
4013 O  O5B  . NAD   C .   ? 0.7547 1.1775 0.3247 0.0396  -0.3157 0.0606  401 NAD   A O5B  
4014 C  C5B  . NAD   C .   ? 0.7794 1.1545 0.3226 0.0217  -0.3096 0.0615  401 NAD   A C5B  
4015 C  C4B  . NAD   C .   ? 0.7913 1.1626 0.3162 0.0053  -0.2882 0.0546  401 NAD   A C4B  
4016 O  O4B  . NAD   C .   ? 0.8185 1.1461 0.3149 -0.012  -0.2808 0.0569  401 NAD   A O4B  
4017 C  C3B  . NAD   C .   ? 0.7759 1.1945 0.3065 -0.0171 -0.278  0.0528  401 NAD   A C3B  
4018 O  O3B  . NAD   C .   ? 0.7669 1.2097 0.305  -0.0082 -0.2655 0.0453  401 NAD   A O3B  
4019 C  C2B  . NAD   C .   ? 0.7957 1.1853 0.2959 -0.0496 -0.2643 0.0537  401 NAD   A C2B  
4020 O  O2B  . NAD   C .   ? 0.7924 1.1953 0.2813 -0.0712 -0.2429 0.0478  401 NAD   A O2B  
4021 C  C1B  . NAD   C .   ? 0.8264 1.1579 0.3046 -0.0371 -0.2616 0.0544  401 NAD   A C1B  
4022 N  N9A  . NAD   C .   ? 0.8545 1.1495 0.3057 -0.0576 -0.2563 0.0585  401 NAD   A N9A  
4023 C  C8A  . NAD   C .   ? 0.8578 1.1547 0.3085 -0.073  -0.2669 0.0645  401 NAD   A C8A  
4024 N  N7A  . NAD   C .   ? 0.8811 1.142  0.3025 -0.0908 -0.2565 0.066   401 NAD   A N7A  
4025 C  C5A  . NAD   C .   ? 0.8999 1.1323 0.3005 -0.0852 -0.2376 0.0618  401 NAD   A C5A  
4026 C  C6A  . NAD   C .   ? 0.9317 1.1192 0.2953 -0.094  -0.2182 0.062   401 NAD   A C6A  
4027 N  N6A  . NAD   C .   ? 0.9518 1.1139 0.2927 -0.1128 -0.2138 0.0651  401 NAD   A N6A  
4028 N  N1A  . NAD   C .   ? 0.9413 1.1104 0.2893 -0.0815 -0.2019 0.0592  401 NAD   A N1A  
4029 C  C2A  . NAD   C .   ? 0.9267 1.1223 0.2954 -0.0636 -0.205  0.0553  401 NAD   A C2A  
4030 N  N3A  . NAD   C .   ? 0.8996 1.1373 0.3036 -0.0543 -0.222  0.0533  401 NAD   A N3A  
4031 C  C4A  . NAD   C .   ? 0.8847 1.1386 0.3032 -0.0654 -0.2377 0.0573  401 NAD   A C4A  
4032 O  O3   . NAD   C .   ? 0.7763 1.1641 0.3561 0.0669  -0.3453 0.075   401 NAD   A O3   
4033 P  PN   . NAD   C .   ? 0.7983 1.1484 0.3816 0.0973  -0.3513 0.0706  401 NAD   A PN   
4034 O  O1N  . NAD   C .   ? 0.8016 1.1483 0.3822 0.1059  -0.3392 0.0566  401 NAD   A O1N  
4035 O  O2N  . NAD   C .   ? 0.7858 1.1508 0.3858 0.1216  -0.3646 0.079   401 NAD   A O2N  
4036 O  O5D  . NAD   C .   ? 0.8278 1.123  0.3917 0.0844  -0.3541 0.0737  401 NAD   A O5D  
4037 C  C5D  . NAD   C .   ? 0.8406 1.1183 0.3851 0.0629  -0.3424 0.0691  401 NAD   A C5D  
4038 C  C4D  . NAD   C .   ? 0.8585 1.0886 0.3912 0.0628  -0.3457 0.0679  401 NAD   A C4D  
4039 O  O4D  . NAD   C .   ? 0.8627 1.0739 0.4063 0.0836  -0.357  0.0678  401 NAD   A O4D  
4040 C  C3D  . NAD   C .   ? 0.8688 1.0812 0.3881 0.041   -0.348  0.0781  401 NAD   A C3D  
4041 O  O3D  . NAD   C .   ? 0.8814 1.0637 0.385  0.0338  -0.3418 0.0732  401 NAD   A O3D  
4042 C  C2D  . NAD   C .   ? 0.8739 1.0746 0.4025 0.0506  -0.3627 0.0883  401 NAD   A C2D  
4043 O  O2D  . NAD   C .   ? 0.8886 1.0599 0.4052 0.0365  -0.366  0.096   401 NAD   A O2D  
4044 C  C1D  . NAD   C .   ? 0.8782 1.0629 0.4167 0.0754  -0.3655 0.0784  401 NAD   A C1D  
4045 N  N1N  . NAD   C .   ? 0.8802 1.062  0.4304 0.0952  -0.3767 0.0867  401 NAD   A N1N  
4046 C  C2N  . NAD   C .   ? 0.8658 1.089  0.4283 0.1048  -0.38   0.0933  401 NAD   A C2N  
4047 C  C3N  . NAD   C .   ? 0.8657 1.0877 0.4363 0.1265  -0.3901 0.1036  401 NAD   A C3N  
4048 C  C7N  . NAD   C .   ? 0.8443 1.1223 0.4307 0.1406  -0.3946 0.111   401 NAD   A C7N  
4049 O  O7N  . NAD   C .   ? 0.8393 1.1219 0.4275 0.153   -0.4046 0.1262  401 NAD   A O7N  
4050 N  N7N  . NAD   C .   ? 0.8277 1.1512 0.4251 0.1394  -0.3869 0.1013  401 NAD   A N7N  
4051 C  C4N  . NAD   C .   ? 0.8828 1.0516 0.446  0.1357  -0.395  0.1068  401 NAD   A C4N  
4052 C  C5N  . NAD   C .   ? 0.898  1.0246 0.4498 0.1212  -0.3909 0.098   401 NAD   A C5N  
4053 C  C6N  . NAD   C .   ? 0.8958 1.0335 0.4424 0.1021  -0.3825 0.088   401 NAD   A C6N  
4054 C  C4   . A1AG6 D .   ? 1.3216 1.5125 0.8586 0.1271  -0.4287 0.1856  402 A1AG6 A C4   
4055 N  N2   . A1AG6 D .   ? 1.2991 1.5607 0.8347 0.1327  -0.4439 0.2112  402 A1AG6 A N2   
4056 C  C7   . A1AG6 D .   ? 1.3701 1.4368 0.8954 0.1558  -0.4233 0.1803  402 A1AG6 A C7   
4057 C  C6   . A1AG6 D .   ? 1.3535 1.4509 0.8855 0.1325  -0.4178 0.1649  402 A1AG6 A C6   
4058 C  C9   . A1AG6 D .   ? 1.3351 1.5007 0.8661 0.1538  -0.4359 0.2028  402 A1AG6 A C9   
4059 C  C20  . A1AG6 D .   ? 1.4561 1.3683 0.9367 0.1669  -0.4229 0.2137  402 A1AG6 A C20  
4060 C  C8   . A1AG6 D .   ? 1.364  1.4629 0.8879 0.1683  -0.4321 0.2005  402 A1AG6 A C8   
4061 C  C18  . A1AG6 D .   ? 1.5086 1.2912 0.9658 0.162   -0.4105 0.2064  402 A1AG6 A C18  
4062 C  C16  . A1AG6 D .   ? 1.4841 1.3291 0.959  0.2233  -0.4191 0.2119  402 A1AG6 A C16  
4063 C  C19  . A1AG6 D .   ? 1.4797 1.329  0.947  0.1475  -0.416  0.21    402 A1AG6 A C19  
4064 C  C26  . A1AG6 D .   ? 1.5945 1.1717 0.99   0.0887  -0.386  0.2276  402 A1AG6 A C26  
4065 C  C1   . A1AG6 D .   ? 1.2808 1.5991 0.8143 0.1249  -0.4529 0.2233  402 A1AG6 A C1   
4066 C  C3   . A1AG6 D .   ? 1.3012 1.5518 0.8403 0.1135  -0.4333 0.1918  402 A1AG6 A C3   
4067 C  C5   . A1AG6 D .   ? 1.3296 1.4846 0.8662 0.1184  -0.4194 0.1678  402 A1AG6 A C5   
4068 N  N10  . A1AG6 D .   ? 1.3187 1.5283 0.8486 0.1597  -0.4453 0.2198  402 A1AG6 A N10  
4069 N  N11  . A1AG6 D .   ? 1.3878 1.4512 0.8995 0.1939  -0.4368 0.2199  402 A1AG6 A N11  
4070 S  S12  . A1AG6 D .   ? 1.4169 1.4205 0.9233 0.2281  -0.4333 0.2193  402 A1AG6 A S12  
4071 O  O13  . A1AG6 D .   ? 1.4069 1.429  0.9304 0.2396  -0.4289 0.1978  402 A1AG6 A O13  
4072 O  O14  . A1AG6 D .   ? 1.4206 1.4258 0.9176 0.2585  -0.4402 0.244   402 A1AG6 A O14  
4073 C  C15  . A1AG6 D .   ? 1.4562 1.3693 0.9421 0.2046  -0.4247 0.2149  402 A1AG6 A C15  
4074 C  C17  . A1AG6 D .   ? 1.5116 1.2891 0.9711 0.2005  -0.4117 0.2072  402 A1AG6 A C17  
4075 CL CL21 . A1AG6 D .   ? 1.4737 1.3285 0.9361 0.1034  -0.4126 0.2081  402 A1AG6 A CL21 
4076 C  C28  . A1AG6 D .   ? 1.3149 1.4904 0.8541 0.0957  -0.4102 0.1512  402 A1AG6 A C28  
4077 O  O29  . A1AG6 D .   ? 1.3236 1.4669 0.8585 0.0878  -0.4033 0.1388  402 A1AG6 A O29  
4078 O  O30  . A1AG6 D .   ? 1.2949 1.5217 0.838  0.0833  -0.4095 0.1512  402 A1AG6 A O30  
4079 O  O22  . A1AG6 D .   ? 1.5318 1.2581 0.9766 0.1363  -0.4032 0.2018  402 A1AG6 A O22  
4080 C  C23  . A1AG6 D .   ? 1.5607 1.2113 0.9908 0.1473  -0.3961 0.1987  402 A1AG6 A C23  
4081 C  C24  . A1AG6 D .   ? 1.5778 1.1827 0.9987 0.1101  -0.388  0.1908  402 A1AG6 A C24  
4082 C  C25  . A1AG6 D .   ? 1.5666 1.2013 0.9877 0.0778  -0.389  0.2005  402 A1AG6 A C25  
4083 C  C27  . A1AG6 D .   ? 1.6114 1.1413 1.0049 0.11    -0.3813 0.2114  402 A1AG6 A C27  
4085 P  PA   . NAD   E .   ? 0.8764 1.0448 0.3012 -0.2019 -0.1608 0.1002  401 NAD   B PA   
4086 O  O1A  . NAD   E .   ? 0.8541 1.063  0.298  -0.2157 -0.1596 0.1025  401 NAD   B O1A  
4087 O  O2A  . NAD   E .   ? 0.8771 1.0393 0.3001 -0.1716 -0.154  0.0938  401 NAD   B O2A  
4088 O  O5B  . NAD   E .   ? 0.8994 1.0502 0.3032 -0.2127 -0.1485 0.101   401 NAD   B O5B  
4089 C  C5B  . NAD   E .   ? 0.9225 1.037  0.3099 -0.2092 -0.1503 0.0993  401 NAD   B C5B  
4090 C  C4B  . NAD   E .   ? 0.9328 1.0434 0.3042 -0.213  -0.1327 0.0931  401 NAD   B C4B  
4091 O  O4B  . NAD   E .   ? 0.9534 1.032  0.3135 -0.2081 -0.1325 0.0885  401 NAD   B O4B  
4092 C  C3B  . NAD   E .   ? 0.9268 1.0518 0.3002 -0.1976 -0.1102 0.0842  401 NAD   B C3B  
4093 O  O3B  . NAD   E .   ? 0.9182 1.068  0.2876 -0.2116 -0.0991 0.0835  401 NAD   B O3B  
4094 C  C2B  . NAD   E .   ? 0.947  1.0398 0.3084 -0.1845 -0.0967 0.0744  401 NAD   B C2B  
4095 O  O2B  . NAD   E .   ? 0.9488 1.0437 0.3018 -0.1823 -0.0729 0.0637  401 NAD   B O2B  
4096 C  C1B  . NAD   E .   ? 0.9645 1.0376 0.3158 -0.2012 -0.1108 0.0767  401 NAD   B C1B  
4097 N  N9A  . NAD   E .   ? 0.9895 1.0304 0.3373 -0.1901 -0.107  0.0707  401 NAD   B N9A  
4098 C  C8A  . NAD   E .   ? 0.9964 1.0198 0.3509 -0.1684 -0.1065 0.072   401 NAD   B C8A  
4099 N  N7A  . NAD   E .   ? 1.0091 1.0042 0.3593 -0.1625 -0.0977 0.0658  401 NAD   B N7A  
4100 C  C5A  . NAD   E .   ? 1.0127 1.0092 0.3544 -0.1826 -0.0939 0.0579  401 NAD   B C5A  
4101 C  C6A  . NAD   E .   ? 1.0219 0.9995 0.3589 -0.1895 -0.0844 0.0463  401 NAD   B C6A  
4102 N  N6A  . NAD   E .   ? 1.0322 0.9814 0.374  -0.1767 -0.0739 0.042   401 NAD   B N6A  
4103 N  N1A  . NAD   E .   ? 1.0192 1.01   0.3462 -0.2106 -0.0845 0.0382  401 NAD   B N1A  
4104 C  C2A  . NAD   E .   ? 1.0125 1.0307 0.3326 -0.2224 -0.0916 0.0438  401 NAD   B C2A  
4105 N  N3A  . NAD   E .   ? 1.0022 1.0379 0.3278 -0.2183 -0.0985 0.0559  401 NAD   B N3A  
4106 C  C4A  . NAD   E .   ? 1.0017 1.0263 0.3393 -0.1987 -0.1    0.0614  401 NAD   B C4A  
4107 O  O3   . NAD   E .   ? 0.8837 1.025  0.3067 -0.2133 -0.1818 0.1053  401 NAD   B O3   
4108 P  PN   . NAD   E .   ? 0.8774 1.0147 0.3075 -0.2395 -0.1971 0.1142  401 NAD   B PN   
4109 O  O1N  . NAD   E .   ? 0.8844 1.0259 0.3049 -0.2594 -0.189  0.123   401 NAD   B O1N  
4110 O  O2N  . NAD   E .   ? 0.8639 1.0259 0.3175 -0.2429 -0.207  0.1105  401 NAD   B O2N  
4111 O  O5D  . NAD   E .   ? 0.8801 0.9755 0.298  -0.2347 -0.2089 0.1161  401 NAD   B O5D  
4112 C  C5D  . NAD   E .   ? 0.8837 0.9566 0.2831 -0.2297 -0.202  0.1169  401 NAD   B C5D  
4113 C  C4D  . NAD   E .   ? 0.8904 0.9321 0.2845 -0.2342 -0.2157 0.1234  401 NAD   B C4D  
4114 O  O4D  . NAD   E .   ? 0.8863 0.9264 0.2927 -0.2465 -0.2291 0.1287  401 NAD   B O4D  
4115 C  C3D  . NAD   E .   ? 0.897  0.9133 0.2869 -0.2136 -0.2179 0.1172  401 NAD   B C3D  
4116 O  O3D  . NAD   E .   ? 0.9057 0.8986 0.2869 -0.2164 -0.2215 0.1222  401 NAD   B O3D  
4117 C  C2D  . NAD   E .   ? 0.8977 0.9106 0.2985 -0.2097 -0.2314 0.1148  401 NAD   B C2D  
4118 O  O2D  . NAD   E .   ? 0.9076 0.8912 0.3033 -0.1965 -0.238  0.1128  401 NAD   B O2D  
4119 C  C1D  . NAD   E .   ? 0.8982 0.9155 0.307  -0.2345 -0.2399 0.124   401 NAD   B C1D  
4120 N  N1N  . NAD   E .   ? 0.8991 0.9293 0.3247 -0.2397 -0.2491 0.1185  401 NAD   B N1N  
4121 C  C2N  . NAD   E .   ? 0.8873 0.9522 0.3237 -0.2355 -0.2442 0.1109  401 NAD   B C2N  
4122 C  C3N  . NAD   E .   ? 0.876  0.9587 0.3303 -0.24   -0.2543 0.1028  401 NAD   B C3N  
4123 C  C7N  . NAD   E .   ? 0.8535 0.9825 0.3234 -0.2343 -0.2503 0.0946  401 NAD   B C7N  
4124 O  O7N  . NAD   E .   ? 0.8445 0.9899 0.3253 -0.227  -0.2609 0.0833  401 NAD   B O7N  
4125 N  N7N  . NAD   E .   ? 0.8445 0.9972 0.3154 -0.2363 -0.2355 0.0992  401 NAD   B N7N  
4126 C  C4N  . NAD   E .   ? 0.8847 0.9432 0.3438 -0.2502 -0.2679 0.1014  401 NAD   B C4N  
4127 C  C5N  . NAD   E .   ? 0.9026 0.9207 0.3494 -0.2534 -0.2707 0.1107  401 NAD   B C5N  
4128 C  C6N  . NAD   E .   ? 0.9093 0.9162 0.34   -0.2475 -0.2618 0.12    401 NAD   B C6N  
# 
