data_9AV4
# 
_entry.id   9AV4 
# 
_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   9AV4         pdb_00009av4 10.2210/pdb9av4/pdb 
WWPDB D_1000282036 ?            ?                   
# 
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                        9AV4 
_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 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8G84 
_pdbx_database_related.content_type   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            Liu 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9400-3007 
# 
_audit_author.name               'Liu, S.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0001-9400-3007 
# 
_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'                    35350.141 2  ? ? ? 
'Dog HSD17B13 with 4 mutations to make it more human enzyme-like' 
2 non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE                            663.425   2  ? ? ? ? 
3 non-polymer syn '4-(3,4-dichlorobenzene-1-sulfonamido)-2-fluorobenzoic acid' 364.176   2  ? ? ? ? 
4 water       nat water                                                        18.015    56 ? ? ? ? 
# 
_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
IKRNHGHIVTVASVCGHEGIPYLIPYCSSKFAAVGFHRALTLELQALGITGIKTSCLCPVFVNTGFTKNPSTRLWPILET
DTVARSLIDGILTNKKMIFVPSYYNIYLILDKFLPERALAAINHLQNIQFEAVVGHKTRMKGSGHHHHHHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGNIILDLLLLLLTIIYSYLEALVKVFFPRKRKSVAGEIVLITGAGHGIGRWTAYEFAKQKSRLVLWDINKHGVEETAAE
CRKLGATVHTFVVDCGNREDIYNSVKQVKKEVGDVTILVNNAGTVYPADLLSTKDEEITKTFEINILGHFWITKALLPSM
IKRNHGHIVTVASVCGHEGIPYLIPYCSSKFAAVGFHRALTLELQALGITGIKTSCLCPVFVNTGFTKNPSTRLWPILET
DTVARSLIDGILTNKKMIFVPSYYNIYLILDKFLPERALAAINHLQNIQFEAVVGHKTRMKGSGHHHHHHHHHHH
;
_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 '4-(3,4-dichlorobenzene-1-sulfonamido)-2-fluorobenzoic acid' A1AG4 
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 ALA n 
1 200 LEU n 
1 201 THR n 
1 202 LEU 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 ILE 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 TYR n 
1 265 ASN n 
1 266 ILE n 
1 267 TYR 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 
A1AG4 non-polymer         . '4-(3,4-dichlorobenzene-1-sulfonamido)-2-fluorobenzoic acid' ? 'C13 H8 Cl2 F N O4 S' 364.176 
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   ?   ?   ?   A . n 
A 1 3   ASN 3   2   ?   ?   ?   A . n 
A 1 4   ILE 4   3   ?   ?   ?   A . n 
A 1 5   ILE 5   4   ?   ?   ?   A . n 
A 1 6   LEU 6   5   ?   ?   ?   A . n 
A 1 7   ASP 7   6   ?   ?   ?   A . n 
A 1 8   LEU 8   7   ?   ?   ?   A . n 
A 1 9   LEU 9   8   ?   ?   ?   A . n 
A 1 10  LEU 10  9   ?   ?   ?   A . n 
A 1 11  LEU 11  10  ?   ?   ?   A . n 
A 1 12  LEU 12  11  ?   ?   ?   A . n 
A 1 13  LEU 13  12  ?   ?   ?   A . n 
A 1 14  THR 14  13  ?   ?   ?   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 ALA 199 198 198 ALA ALA 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 LEU 202 201 201 LEU LEU 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 234 233 233 LEU LEU A . n 
A 1 235 TRP 235 234 ?   ?   ?   A . n 
A 1 236 PRO 236 235 ?   ?   ?   A . n 
A 1 237 ILE 237 236 236 ILE ILE 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 TYR 264 263 263 TYR TYR 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 TYR 267 266 266 TYR TYR 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 ALA 199 198 198 ALA ALA 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 LEU 202 201 201 LEU LEU 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 232 231 231 THR THR B . n 
B 1 233 ARG 233 232 232 ARG ARG B . n 
B 1 234 LEU 234 233 ?   ?   ?   B . n 
B 1 235 TRP 235 234 ?   ?   ?   B . n 
B 1 236 PRO 236 235 ?   ?   ?   B . n 
B 1 237 ILE 237 236 236 ILE ILE 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 TYR 264 263 263 TYR TYR 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 TYR 267 266 266 TYR TYR 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 A1AG4 ? ? A1AG4 ? ? '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 A1AG4 1  402 301 A1AG4 PFE A . 
E 2 NAD   1  401 296 NAD   NAD B . 
F 3 A1AG4 1  402 301 A1AG4 PFE B . 
G 4 HOH   1  501 34  HOH   HOH A . 
G 4 HOH   2  502 25  HOH   HOH A . 
G 4 HOH   3  503 36  HOH   HOH A . 
G 4 HOH   4  504 15  HOH   HOH A . 
G 4 HOH   5  505 13  HOH   HOH A . 
G 4 HOH   6  506 3   HOH   HOH A . 
G 4 HOH   7  507 51  HOH   HOH A . 
G 4 HOH   8  508 2   HOH   HOH A . 
G 4 HOH   9  509 6   HOH   HOH A . 
G 4 HOH   10 510 46  HOH   HOH A . 
G 4 HOH   11 511 53  HOH   HOH A . 
G 4 HOH   12 512 43  HOH   HOH A . 
G 4 HOH   13 513 23  HOH   HOH A . 
G 4 HOH   14 514 31  HOH   HOH A . 
G 4 HOH   15 515 42  HOH   HOH A . 
G 4 HOH   16 516 24  HOH   HOH A . 
G 4 HOH   17 517 45  HOH   HOH A . 
G 4 HOH   18 518 54  HOH   HOH A . 
G 4 HOH   19 519 4   HOH   HOH A . 
G 4 HOH   20 520 56  HOH   HOH A . 
G 4 HOH   21 521 10  HOH   HOH A . 
G 4 HOH   22 522 49  HOH   HOH A . 
G 4 HOH   23 523 37  HOH   HOH A . 
G 4 HOH   24 524 35  HOH   HOH A . 
G 4 HOH   25 525 28  HOH   HOH A . 
G 4 HOH   26 526 55  HOH   HOH A . 
G 4 HOH   27 527 18  HOH   HOH A . 
G 4 HOH   28 528 44  HOH   HOH A . 
G 4 HOH   29 529 38  HOH   HOH A . 
G 4 HOH   30 530 16  HOH   HOH A . 
G 4 HOH   31 531 21  HOH   HOH A . 
G 4 HOH   32 532 12  HOH   HOH A . 
G 4 HOH   33 533 27  HOH   HOH A . 
G 4 HOH   34 534 29  HOH   HOH A . 
G 4 HOH   35 535 8   HOH   HOH A . 
G 4 HOH   36 536 26  HOH   HOH A . 
G 4 HOH   37 537 19  HOH   HOH A . 
H 4 HOH   1  501 14  HOH   HOH B . 
H 4 HOH   2  502 11  HOH   HOH B . 
H 4 HOH   3  503 22  HOH   HOH B . 
H 4 HOH   4  504 41  HOH   HOH B . 
H 4 HOH   5  505 47  HOH   HOH B . 
H 4 HOH   6  506 40  HOH   HOH B . 
H 4 HOH   7  507 52  HOH   HOH B . 
H 4 HOH   8  508 20  HOH   HOH B . 
H 4 HOH   9  509 50  HOH   HOH B . 
H 4 HOH   10 510 1   HOH   HOH B . 
H 4 HOH   11 511 33  HOH   HOH B . 
H 4 HOH   12 512 30  HOH   HOH B . 
H 4 HOH   13 513 39  HOH   HOH B . 
H 4 HOH   14 514 48  HOH   HOH B . 
H 4 HOH   15 515 57  HOH   HOH B . 
H 4 HOH   16 516 32  HOH   HOH B . 
H 4 HOH   17 517 9   HOH   HOH B . 
H 4 HOH   18 518 17  HOH   HOH B . 
H 4 HOH   19 519 7   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'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.69 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9AV4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     186.97 
_cell.length_a_esd                 ? 
_cell.length_b                     76.06 
_cell.length_b_esd                 ? 
_cell.length_c                     65.24 
_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                         9AV4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   9AV4 
_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             3.27 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          62.38 
_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              ? 
_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% beta-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         2020-02-10 
_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                                       9AV4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.09 
_reflns.d_resolution_low                               93.17 
_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                                     28362 
_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                           87.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.9 
_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                                0.038 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.059 
_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                                    2.09 
_reflns_shell.d_res_low                                     2.36 
_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                             1419 
_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                               1.9 
_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                               0.330 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.763 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          56.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.359 
_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]                            5.9579 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0.3583 
_refine.aniso_B[2][2]                            0.9125 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -6.8704 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               45.53 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.916 
_refine.correlation_coeff_Fo_to_Fc_free          0.899 
_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                                 9AV4 
_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                            2.09 
_refine.ls_d_res_low                             33.47 
_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                     28372 
_refine.ls_number_reflns_R_free                  1410 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    46.5 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2126 
_refine.ls_R_factor_R_free                       0.2393 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2113 
_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          'MOLECULAR REPLACEMENT' 
_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   0.235 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.227 
_refine.pdbx_overall_SU_R_Blow_DPI               0.302 
_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             0.322 
_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                        9AV4 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.32 
_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                       2.09 
_refine_hist.d_res_low                        33.47 
_refine_hist.number_atoms_solvent             56 
_refine_hist.number_atoms_total               4128 
_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        3940 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         132 
_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' ? 0.008 ? 4190 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.94  ? 5709 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1439 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 733  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 4176 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 570  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 3172 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 3.2   ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 18.34 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.09 
_refine_ls_shell.d_res_low                        2.21 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             33 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               3.67 
_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                  0.3041 
_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                  0.3371 
# 
_struct.entry_id                     9AV4 
_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        9AV4 
_struct_keywords.text            'enzyme, substrate, HSd17B13, 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 3 ? 
G N N 4 ? 
H 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 9AV4 A 3 ? 301 ? A0A8C0PP93 2 ? 300 ? 2 300 
2 1 9AV4 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 9AV4 MET A 1   ? UNP A0A8C0PP93 ?   ?   'expression tag'      0   1  
1 9AV4 GLY A 2   ? UNP A0A8C0PP93 ?   ?   'expression tag'      1   2  
1 9AV4 GLU A 178 ? UNP A0A8C0PP93 GLY 177 'engineered mutation' 177 3  
1 9AV4 GLY A 179 ? UNP A0A8C0PP93 VAL 178 'engineered mutation' 178 4  
1 9AV4 ALA A 206 ? UNP A0A8C0PP93 THR 205 'engineered mutation' 205 5  
1 9AV4 VAL A 294 ? UNP A0A8C0PP93 ILE 293 'engineered mutation' 293 6  
1 9AV4 GLY A 302 ? UNP A0A8C0PP93 ?   ?   'expression tag'      301 7  
1 9AV4 SER A 303 ? UNP A0A8C0PP93 ?   ?   'expression tag'      302 8  
1 9AV4 GLY A 304 ? UNP A0A8C0PP93 ?   ?   'expression tag'      303 9  
1 9AV4 HIS A 305 ? UNP A0A8C0PP93 ?   ?   'expression tag'      304 10 
1 9AV4 HIS A 306 ? UNP A0A8C0PP93 ?   ?   'expression tag'      305 11 
1 9AV4 HIS A 307 ? UNP A0A8C0PP93 ?   ?   'expression tag'      306 12 
1 9AV4 HIS A 308 ? UNP A0A8C0PP93 ?   ?   'expression tag'      307 13 
1 9AV4 HIS A 309 ? UNP A0A8C0PP93 ?   ?   'expression tag'      308 14 
1 9AV4 HIS A 310 ? UNP A0A8C0PP93 ?   ?   'expression tag'      309 15 
1 9AV4 HIS A 311 ? UNP A0A8C0PP93 ?   ?   'expression tag'      310 16 
1 9AV4 HIS A 312 ? UNP A0A8C0PP93 ?   ?   'expression tag'      311 17 
1 9AV4 HIS A 313 ? UNP A0A8C0PP93 ?   ?   'expression tag'      312 18 
1 9AV4 HIS A 314 ? UNP A0A8C0PP93 ?   ?   'expression tag'      313 19 
1 9AV4 HIS A 315 ? UNP A0A8C0PP93 ?   ?   'expression tag'      314 20 
2 9AV4 MET B 1   ? UNP A0A8C0PP93 ?   ?   'expression tag'      0   21 
2 9AV4 GLY B 2   ? UNP A0A8C0PP93 ?   ?   'expression tag'      1   22 
2 9AV4 GLU B 178 ? UNP A0A8C0PP93 GLY 177 'engineered mutation' 177 23 
2 9AV4 GLY B 179 ? UNP A0A8C0PP93 VAL 178 'engineered mutation' 178 24 
2 9AV4 ALA B 206 ? UNP A0A8C0PP93 THR 205 'engineered mutation' 205 25 
2 9AV4 VAL B 294 ? UNP A0A8C0PP93 ILE 293 'engineered mutation' 293 26 
2 9AV4 GLY B 302 ? UNP A0A8C0PP93 ?   ?   'expression tag'      301 27 
2 9AV4 SER B 303 ? UNP A0A8C0PP93 ?   ?   'expression tag'      302 28 
2 9AV4 GLY B 304 ? UNP A0A8C0PP93 ?   ?   'expression tag'      303 29 
2 9AV4 HIS B 305 ? UNP A0A8C0PP93 ?   ?   'expression tag'      304 30 
2 9AV4 HIS B 306 ? UNP A0A8C0PP93 ?   ?   'expression tag'      305 31 
2 9AV4 HIS B 307 ? UNP A0A8C0PP93 ?   ?   'expression tag'      306 32 
2 9AV4 HIS B 308 ? UNP A0A8C0PP93 ?   ?   'expression tag'      307 33 
2 9AV4 HIS B 309 ? UNP A0A8C0PP93 ?   ?   'expression tag'      308 34 
2 9AV4 HIS B 310 ? UNP A0A8C0PP93 ?   ?   'expression tag'      309 35 
2 9AV4 HIS B 311 ? UNP A0A8C0PP93 ?   ?   'expression tag'      310 36 
2 9AV4 HIS B 312 ? UNP A0A8C0PP93 ?   ?   'expression tag'      311 37 
2 9AV4 HIS B 313 ? UNP A0A8C0PP93 ?   ?   'expression tag'      312 38 
2 9AV4 HIS B 314 ? UNP A0A8C0PP93 ?   ?   'expression tag'      313 39 
2 9AV4 HIS B 315 ? UNP A0A8C0PP93 ?   ?   'expression tag'      314 40 
# 
_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)' 6320  ? 
1 MORE         -45   ? 
1 'SSA (A^2)'  21530 ? 
# 
_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,H 
# 
_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 ILE A 15  ? PHE A 28  ? ILE A 14  PHE A 27  1 ? 14 
HELX_P HELX_P2  AA2 HIS A 47  ? GLN A 60  ? HIS A 46  GLN A 59  1 ? 14 
HELX_P HELX_P3  AA3 ASN A 70  ? LEU A 84  ? ASN A 69  LEU A 83  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 97  ? VAL A 112 ? ASN A 96  VAL A 111 1 ? 16 
HELX_P HELX_P5  AA5 ASP A 129 ? THR A 133 ? ASP A 128 THR A 132 5 ? 5  
HELX_P HELX_P6  AA6 LYS A 134 ? ILE A 146 ? LYS A 133 ILE A 145 1 ? 13 
HELX_P HELX_P7  AA7 ILE A 146 ? ARG A 163 ? ILE A 145 ARG A 162 1 ? 18 
HELX_P HELX_P8  AA8 SER A 173 ? HIS A 177 ? SER A 172 HIS A 176 5 ? 5  
HELX_P HELX_P9  AA9 LEU A 183 ? LEU A 207 ? LEU A 182 LEU A 206 1 ? 25 
HELX_P HELX_P10 AB1 GLU A 239 ? THR A 253 ? GLU A 238 THR A 252 1 ? 15 
HELX_P HELX_P11 AB2 TYR A 263 ? LYS A 272 ? TYR A 262 LYS A 271 1 ? 10 
HELX_P HELX_P12 AB3 HIS B 47  ? GLN B 60  ? HIS B 46  GLN B 59  1 ? 14 
HELX_P HELX_P13 AB4 ASN B 70  ? LEU B 84  ? ASN B 69  LEU B 83  1 ? 15 
HELX_P HELX_P14 AB5 ASN B 97  ? VAL B 112 ? ASN B 96  VAL B 111 1 ? 16 
HELX_P HELX_P15 AB6 ASP B 129 ? THR B 133 ? ASP B 128 THR B 132 5 ? 5  
HELX_P HELX_P16 AB7 LYS B 134 ? ILE B 146 ? LYS B 133 ILE B 145 1 ? 13 
HELX_P HELX_P17 AB8 ILE B 146 ? ASN B 164 ? ILE B 145 ASN B 163 1 ? 19 
HELX_P HELX_P18 AB9 SER B 173 ? HIS B 177 ? SER B 172 HIS B 176 5 ? 5  
HELX_P HELX_P19 AC1 LEU B 183 ? LEU B 207 ? LEU B 182 LEU B 206 1 ? 25 
HELX_P HELX_P20 AC2 GLU B 239 ? THR B 253 ? GLU B 238 THR B 252 1 ? 15 
HELX_P HELX_P21 AC3 PRO B 261 ? TYR B 264 ? PRO B 260 TYR B 263 5 ? 4  
HELX_P HELX_P22 AC4 ASN B 265 ? LYS B 272 ? ASN B 264 LYS B 271 1 ? 8  
# 
_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 -0.29 
2 VAL 260 B . ? VAL 259 B PRO 261 B ? PRO 260 B 1 0.11  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 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 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? parallel 
AA2 5 6 ? parallel 
AA2 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 VAL A 88  ? VAL A 92  ? VAL A 87  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 VAL B 88  ? VAL B 92  ? VAL B 87  VAL B 91  
AA2 2 ARG B 63  ? ASP B 68  ? ARG B 62  ASP B 67  
AA2 3 ILE B 39  ? THR B 43  ? ILE B 38  THR B 42  
AA2 4 ILE B 117 ? ASN B 120 ? ILE B 116 ASN B 119 
AA2 5 GLY B 166 ? VAL B 171 ? GLY B 165 VAL B 170 
AA2 6 ILE B 212 ? PRO B 219 ? ILE B 211 PRO B 218 
AA2 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 HIS A 89  ? O HIS A 88  N LEU A 66  ? N LEU A 65  
AA1 2 3 O VAL A 65  ? O VAL A 64  N VAL A 40  ? N VAL A 39  
AA1 3 4 N LEU A 41  ? N LEU A 40  O VAL A 119 ? O VAL A 118 
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 218 ? N CYS A 217 O ILE A 258 ? O ILE A 257 
AA2 1 2 O HIS B 89  ? O HIS B 88  N LEU B 66  ? N LEU B 65  
AA2 2 3 O VAL B 65  ? O VAL B 64  N VAL B 40  ? N VAL B 39  
AA2 3 4 N LEU B 41  ? N LEU B 40  O VAL B 119 ? O VAL B 118 
AA2 4 5 N LEU B 118 ? N LEU B 117 O VAL B 169 ? O VAL B 168 
AA2 5 6 N THR B 170 ? N THR B 169 O SER B 215 ? O SER B 214 
AA2 6 7 N CYS B 218 ? N CYS B 217 O ILE B 258 ? O ILE B 257 
# 
_pdbx_entry_details.entry_id                   9AV4 
_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 ALA A 127 ? ? 178.15  154.61  
2 1 ILE A 145 ? ? -140.96 -48.11  
3 1 HIS A 164 ? ? -160.09 115.72  
4 1 ALA A 171 ? ? -104.31 -112.21 
5 1 SER A 172 ? ? 172.00  167.80  
6 1 ILE B 145 ? ? -143.22 -48.24  
7 1 ALA B 171 ? ? -103.93 -112.68 
8 1 SER B 172 ? ? 171.68  167.09  
# 
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' ? ? 31.7688 -37.1811 -6.2274 -0.1042 ? -0.0316 ? -0.0019 ? -0.1099 ? 0.0302 ? -0.2323 ? 1.232 ? -0.1133 ? 
-0.1603 ? 2.2646 ? 0.4535 ? 5.0218 ? -0.0148 ? -0.1155 ? 0.2857  ? -0.1155 ? 0.0332  ? -0.54 ? 0.2857  ? -0.54 ? -0.0185 ? 
2 'X-RAY DIFFRACTION' ? ? 29.8582 -19.771  19.0559 -0.0137 ? 0.1105  ? 0.0474  ? -0.0977 ? 0.0124 ? -0.255  ? 1.485 ? 0.5113  ? 
-0.2812 ? 1.8403 ? 0.0677 ? 3.6159 ? 0.0249  ? 0.158   ? -0.5252 ? 0.158   ? -0.0034 ? -0.52 ? -0.5252 ? -0.52 ? -0.0215 ? 
# 
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 14  ? ? ? 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 301 ? ? '{ B|* }' 
# 
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 GLY 1   ? A GLY 2   
3   1 Y 1 A ASN 2   ? A ASN 3   
4   1 Y 1 A ILE 3   ? A ILE 4   
5   1 Y 1 A ILE 4   ? A ILE 5   
6   1 Y 1 A LEU 5   ? A LEU 6   
7   1 Y 1 A ASP 6   ? A ASP 7   
8   1 Y 1 A LEU 7   ? A LEU 8   
9   1 Y 1 A LEU 8   ? A LEU 9   
10  1 Y 1 A LEU 9   ? A LEU 10  
11  1 Y 1 A LEU 10  ? A LEU 11  
12  1 Y 1 A LEU 11  ? A LEU 12  
13  1 Y 1 A LEU 12  ? A LEU 13  
14  1 Y 1 A THR 13  ? A THR 14  
15  1 Y 1 A TRP 234 ? A TRP 235 
16  1 Y 1 A PRO 235 ? A PRO 236 
17  1 Y 1 A PRO 274 ? A PRO 275 
18  1 Y 1 A GLU 275 ? A GLU 276 
19  1 Y 1 A ARG 276 ? A ARG 277 
20  1 Y 1 A ALA 277 ? A ALA 278 
21  1 Y 1 A LEU 278 ? A LEU 279 
22  1 Y 1 A ALA 279 ? A ALA 280 
23  1 Y 1 A ALA 280 ? A ALA 281 
24  1 Y 1 A ILE 281 ? A ILE 282 
25  1 Y 1 A ASN 282 ? A ASN 283 
26  1 Y 1 A HIS 283 ? A HIS 284 
27  1 Y 1 A LEU 284 ? A LEU 285 
28  1 Y 1 A GLN 285 ? A GLN 286 
29  1 Y 1 A ASN 286 ? A ASN 287 
30  1 Y 1 A ILE 287 ? A ILE 288 
31  1 Y 1 A GLN 288 ? A GLN 289 
32  1 Y 1 A PHE 289 ? A PHE 290 
33  1 Y 1 A GLU 290 ? A GLU 291 
34  1 Y 1 A ALA 291 ? A ALA 292 
35  1 Y 1 A VAL 292 ? A VAL 293 
36  1 Y 1 A VAL 293 ? A VAL 294 
37  1 Y 1 A GLY 294 ? A GLY 295 
38  1 Y 1 A HIS 295 ? A HIS 296 
39  1 Y 1 A LYS 296 ? A LYS 297 
40  1 Y 1 A THR 297 ? A THR 298 
41  1 Y 1 A ARG 298 ? A ARG 299 
42  1 Y 1 A MET 299 ? A MET 300 
43  1 Y 1 A LYS 300 ? A LYS 301 
44  1 Y 1 A GLY 301 ? A GLY 302 
45  1 Y 1 A SER 302 ? A SER 303 
46  1 Y 1 A GLY 303 ? A GLY 304 
47  1 Y 1 A HIS 304 ? A HIS 305 
48  1 Y 1 A HIS 305 ? A HIS 306 
49  1 Y 1 A HIS 306 ? A HIS 307 
50  1 Y 1 A HIS 307 ? A HIS 308 
51  1 Y 1 A HIS 308 ? A HIS 309 
52  1 Y 1 A HIS 309 ? A HIS 310 
53  1 Y 1 A HIS 310 ? A HIS 311 
54  1 Y 1 A HIS 311 ? A HIS 312 
55  1 Y 1 A HIS 312 ? A HIS 313 
56  1 Y 1 A HIS 313 ? A HIS 314 
57  1 Y 1 A HIS 314 ? A HIS 315 
58  1 Y 1 B MET 0   ? B MET 1   
59  1 Y 1 B GLY 1   ? B GLY 2   
60  1 Y 1 B ASN 2   ? B ASN 3   
61  1 Y 1 B ILE 3   ? B ILE 4   
62  1 Y 1 B ILE 4   ? B ILE 5   
63  1 Y 1 B LEU 5   ? B LEU 6   
64  1 Y 1 B ASP 6   ? B ASP 7   
65  1 Y 1 B LEU 7   ? B LEU 8   
66  1 Y 1 B LEU 8   ? B LEU 9   
67  1 Y 1 B LEU 9   ? B LEU 10  
68  1 Y 1 B LEU 10  ? B LEU 11  
69  1 Y 1 B LEU 11  ? B LEU 12  
70  1 Y 1 B LEU 12  ? B LEU 13  
71  1 Y 1 B THR 13  ? B THR 14  
72  1 Y 1 B ILE 14  ? B ILE 15  
73  1 Y 1 B ILE 15  ? B ILE 16  
74  1 Y 1 B TYR 16  ? B TYR 17  
75  1 Y 1 B SER 17  ? B SER 18  
76  1 Y 1 B TYR 18  ? B TYR 19  
77  1 Y 1 B LEU 19  ? B LEU 20  
78  1 Y 1 B GLU 20  ? B GLU 21  
79  1 Y 1 B ALA 21  ? B ALA 22  
80  1 Y 1 B LEU 22  ? B LEU 23  
81  1 Y 1 B VAL 23  ? B VAL 24  
82  1 Y 1 B LYS 24  ? B LYS 25  
83  1 Y 1 B LEU 233 ? B LEU 234 
84  1 Y 1 B TRP 234 ? B TRP 235 
85  1 Y 1 B PRO 235 ? B PRO 236 
86  1 Y 1 B LEU 273 ? B LEU 274 
87  1 Y 1 B PRO 274 ? B PRO 275 
88  1 Y 1 B GLU 275 ? B GLU 276 
89  1 Y 1 B ARG 276 ? B ARG 277 
90  1 Y 1 B ALA 277 ? B ALA 278 
91  1 Y 1 B LEU 278 ? B LEU 279 
92  1 Y 1 B ALA 279 ? B ALA 280 
93  1 Y 1 B ALA 280 ? B ALA 281 
94  1 Y 1 B ILE 281 ? B ILE 282 
95  1 Y 1 B ASN 282 ? B ASN 283 
96  1 Y 1 B HIS 283 ? B HIS 284 
97  1 Y 1 B LEU 284 ? B LEU 285 
98  1 Y 1 B GLN 285 ? B GLN 286 
99  1 Y 1 B ASN 286 ? B ASN 287 
100 1 Y 1 B ILE 287 ? B ILE 288 
101 1 Y 1 B GLN 288 ? B GLN 289 
102 1 Y 1 B PHE 289 ? B PHE 290 
103 1 Y 1 B GLU 290 ? B GLU 291 
104 1 Y 1 B ALA 291 ? B ALA 292 
105 1 Y 1 B VAL 292 ? B VAL 293 
106 1 Y 1 B VAL 293 ? B VAL 294 
107 1 Y 1 B GLY 294 ? B GLY 295 
108 1 Y 1 B HIS 295 ? B HIS 296 
109 1 Y 1 B LYS 296 ? B LYS 297 
110 1 Y 1 B THR 297 ? B THR 298 
111 1 Y 1 B ARG 298 ? B ARG 299 
112 1 Y 1 B MET 299 ? B MET 300 
113 1 Y 1 B LYS 300 ? B LYS 301 
114 1 Y 1 B GLY 301 ? B GLY 302 
115 1 Y 1 B SER 302 ? B SER 303 
116 1 Y 1 B GLY 303 ? B GLY 304 
117 1 Y 1 B HIS 304 ? B HIS 305 
118 1 Y 1 B HIS 305 ? B HIS 306 
119 1 Y 1 B HIS 306 ? B HIS 307 
120 1 Y 1 B HIS 307 ? B HIS 308 
121 1 Y 1 B HIS 308 ? B HIS 309 
122 1 Y 1 B HIS 309 ? B HIS 310 
123 1 Y 1 B HIS 310 ? B HIS 311 
124 1 Y 1 B HIS 311 ? B HIS 312 
125 1 Y 1 B HIS 312 ? B HIS 313 
126 1 Y 1 B HIS 313 ? B HIS 314 
127 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 
A1AG4 C4   C  Y N 1   
A1AG4 C7   C  Y N 2   
A1AG4 C6   C  Y N 3   
A1AG4 C13  C  Y N 4   
A1AG4 C20  C  N N 5   
A1AG4 C16  C  Y N 6   
A1AG4 F1   F  N N 7   
A1AG4 C2   C  Y N 8   
A1AG4 C3   C  Y N 9   
A1AG4 C5   C  Y N 10  
A1AG4 N8   N  N N 11  
A1AG4 S9   S  N N 12  
A1AG4 O10  O  N N 13  
A1AG4 O11  O  N N 14  
A1AG4 C12  C  Y N 15  
A1AG4 C14  C  Y N 16  
A1AG4 C15  C  Y N 17  
A1AG4 C17  C  Y N 18  
A1AG4 CL18 CL N N 19  
A1AG4 CL19 CL N N 20  
A1AG4 O21  O  N N 21  
A1AG4 O22  O  N N 22  
A1AG4 H23  H  N N 23  
A1AG4 H25  H  N N 24  
A1AG4 H27  H  N N 25  
A1AG4 H28  H  N N 26  
A1AG4 H24  H  N N 27  
A1AG4 H26  H  N N 28  
A1AG4 H29  H  N N 29  
A1AG4 H30  H  N N 30  
ALA   N    N  N N 31  
ALA   CA   C  N S 32  
ALA   C    C  N N 33  
ALA   O    O  N N 34  
ALA   CB   C  N N 35  
ALA   OXT  O  N N 36  
ALA   H    H  N N 37  
ALA   H2   H  N N 38  
ALA   HA   H  N N 39  
ALA   HB1  H  N N 40  
ALA   HB2  H  N N 41  
ALA   HB3  H  N N 42  
ALA   HXT  H  N N 43  
ARG   N    N  N N 44  
ARG   CA   C  N S 45  
ARG   C    C  N N 46  
ARG   O    O  N N 47  
ARG   CB   C  N N 48  
ARG   CG   C  N N 49  
ARG   CD   C  N N 50  
ARG   NE   N  N N 51  
ARG   CZ   C  N N 52  
ARG   NH1  N  N N 53  
ARG   NH2  N  N N 54  
ARG   OXT  O  N N 55  
ARG   H    H  N N 56  
ARG   H2   H  N N 57  
ARG   HA   H  N N 58  
ARG   HB2  H  N N 59  
ARG   HB3  H  N N 60  
ARG   HG2  H  N N 61  
ARG   HG3  H  N N 62  
ARG   HD2  H  N N 63  
ARG   HD3  H  N N 64  
ARG   HE   H  N N 65  
ARG   HH11 H  N N 66  
ARG   HH12 H  N N 67  
ARG   HH21 H  N N 68  
ARG   HH22 H  N N 69  
ARG   HXT  H  N N 70  
ASN   N    N  N N 71  
ASN   CA   C  N S 72  
ASN   C    C  N N 73  
ASN   O    O  N N 74  
ASN   CB   C  N N 75  
ASN   CG   C  N N 76  
ASN   OD1  O  N N 77  
ASN   ND2  N  N N 78  
ASN   OXT  O  N N 79  
ASN   H    H  N N 80  
ASN   H2   H  N N 81  
ASN   HA   H  N N 82  
ASN   HB2  H  N N 83  
ASN   HB3  H  N N 84  
ASN   HD21 H  N N 85  
ASN   HD22 H  N N 86  
ASN   HXT  H  N N 87  
ASP   N    N  N N 88  
ASP   CA   C  N S 89  
ASP   C    C  N N 90  
ASP   O    O  N N 91  
ASP   CB   C  N N 92  
ASP   CG   C  N N 93  
ASP   OD1  O  N N 94  
ASP   OD2  O  N N 95  
ASP   OXT  O  N N 96  
ASP   H    H  N N 97  
ASP   H2   H  N N 98  
ASP   HA   H  N N 99  
ASP   HB2  H  N N 100 
ASP   HB3  H  N N 101 
ASP   HD2  H  N N 102 
ASP   HXT  H  N N 103 
CYS   N    N  N N 104 
CYS   CA   C  N R 105 
CYS   C    C  N N 106 
CYS   O    O  N N 107 
CYS   CB   C  N N 108 
CYS   SG   S  N N 109 
CYS   OXT  O  N N 110 
CYS   H    H  N N 111 
CYS   H2   H  N N 112 
CYS   HA   H  N N 113 
CYS   HB2  H  N N 114 
CYS   HB3  H  N N 115 
CYS   HG   H  N N 116 
CYS   HXT  H  N N 117 
GLN   N    N  N N 118 
GLN   CA   C  N S 119 
GLN   C    C  N N 120 
GLN   O    O  N N 121 
GLN   CB   C  N N 122 
GLN   CG   C  N N 123 
GLN   CD   C  N N 124 
GLN   OE1  O  N N 125 
GLN   NE2  N  N N 126 
GLN   OXT  O  N N 127 
GLN   H    H  N N 128 
GLN   H2   H  N N 129 
GLN   HA   H  N N 130 
GLN   HB2  H  N N 131 
GLN   HB3  H  N N 132 
GLN   HG2  H  N N 133 
GLN   HG3  H  N N 134 
GLN   HE21 H  N N 135 
GLN   HE22 H  N N 136 
GLN   HXT  H  N N 137 
GLU   N    N  N N 138 
GLU   CA   C  N S 139 
GLU   C    C  N N 140 
GLU   O    O  N N 141 
GLU   CB   C  N N 142 
GLU   CG   C  N N 143 
GLU   CD   C  N N 144 
GLU   OE1  O  N N 145 
GLU   OE2  O  N N 146 
GLU   OXT  O  N N 147 
GLU   H    H  N N 148 
GLU   H2   H  N N 149 
GLU   HA   H  N N 150 
GLU   HB2  H  N N 151 
GLU   HB3  H  N N 152 
GLU   HG2  H  N N 153 
GLU   HG3  H  N N 154 
GLU   HE2  H  N N 155 
GLU   HXT  H  N N 156 
GLY   N    N  N N 157 
GLY   CA   C  N N 158 
GLY   C    C  N N 159 
GLY   O    O  N N 160 
GLY   OXT  O  N N 161 
GLY   H    H  N N 162 
GLY   H2   H  N N 163 
GLY   HA2  H  N N 164 
GLY   HA3  H  N N 165 
GLY   HXT  H  N N 166 
HIS   N    N  N N 167 
HIS   CA   C  N S 168 
HIS   C    C  N N 169 
HIS   O    O  N N 170 
HIS   CB   C  N N 171 
HIS   CG   C  Y N 172 
HIS   ND1  N  Y N 173 
HIS   CD2  C  Y N 174 
HIS   CE1  C  Y N 175 
HIS   NE2  N  Y N 176 
HIS   OXT  O  N N 177 
HIS   H    H  N N 178 
HIS   H2   H  N N 179 
HIS   HA   H  N N 180 
HIS   HB2  H  N N 181 
HIS   HB3  H  N N 182 
HIS   HD1  H  N N 183 
HIS   HD2  H  N N 184 
HIS   HE1  H  N N 185 
HIS   HE2  H  N N 186 
HIS   HXT  H  N N 187 
HOH   O    O  N N 188 
HOH   H1   H  N N 189 
HOH   H2   H  N N 190 
ILE   N    N  N N 191 
ILE   CA   C  N S 192 
ILE   C    C  N N 193 
ILE   O    O  N N 194 
ILE   CB   C  N S 195 
ILE   CG1  C  N N 196 
ILE   CG2  C  N N 197 
ILE   CD1  C  N N 198 
ILE   OXT  O  N N 199 
ILE   H    H  N N 200 
ILE   H2   H  N N 201 
ILE   HA   H  N N 202 
ILE   HB   H  N N 203 
ILE   HG12 H  N N 204 
ILE   HG13 H  N N 205 
ILE   HG21 H  N N 206 
ILE   HG22 H  N N 207 
ILE   HG23 H  N N 208 
ILE   HD11 H  N N 209 
ILE   HD12 H  N N 210 
ILE   HD13 H  N N 211 
ILE   HXT  H  N N 212 
LEU   N    N  N N 213 
LEU   CA   C  N S 214 
LEU   C    C  N N 215 
LEU   O    O  N N 216 
LEU   CB   C  N N 217 
LEU   CG   C  N N 218 
LEU   CD1  C  N N 219 
LEU   CD2  C  N N 220 
LEU   OXT  O  N N 221 
LEU   H    H  N N 222 
LEU   H2   H  N N 223 
LEU   HA   H  N N 224 
LEU   HB2  H  N N 225 
LEU   HB3  H  N N 226 
LEU   HG   H  N N 227 
LEU   HD11 H  N N 228 
LEU   HD12 H  N N 229 
LEU   HD13 H  N N 230 
LEU   HD21 H  N N 231 
LEU   HD22 H  N N 232 
LEU   HD23 H  N N 233 
LEU   HXT  H  N N 234 
LYS   N    N  N N 235 
LYS   CA   C  N S 236 
LYS   C    C  N N 237 
LYS   O    O  N N 238 
LYS   CB   C  N N 239 
LYS   CG   C  N N 240 
LYS   CD   C  N N 241 
LYS   CE   C  N N 242 
LYS   NZ   N  N N 243 
LYS   OXT  O  N N 244 
LYS   H    H  N N 245 
LYS   H2   H  N N 246 
LYS   HA   H  N N 247 
LYS   HB2  H  N N 248 
LYS   HB3  H  N N 249 
LYS   HG2  H  N N 250 
LYS   HG3  H  N N 251 
LYS   HD2  H  N N 252 
LYS   HD3  H  N N 253 
LYS   HE2  H  N N 254 
LYS   HE3  H  N N 255 
LYS   HZ1  H  N N 256 
LYS   HZ2  H  N N 257 
LYS   HZ3  H  N N 258 
LYS   HXT  H  N N 259 
MET   N    N  N N 260 
MET   CA   C  N S 261 
MET   C    C  N N 262 
MET   O    O  N N 263 
MET   CB   C  N N 264 
MET   CG   C  N N 265 
MET   SD   S  N N 266 
MET   CE   C  N N 267 
MET   OXT  O  N N 268 
MET   H    H  N N 269 
MET   H2   H  N N 270 
MET   HA   H  N N 271 
MET   HB2  H  N N 272 
MET   HB3  H  N N 273 
MET   HG2  H  N N 274 
MET   HG3  H  N N 275 
MET   HE1  H  N N 276 
MET   HE2  H  N N 277 
MET   HE3  H  N N 278 
MET   HXT  H  N N 279 
NAD   PA   P  N S 280 
NAD   O1A  O  N N 281 
NAD   O2A  O  N N 282 
NAD   O5B  O  N N 283 
NAD   C5B  C  N N 284 
NAD   C4B  C  N R 285 
NAD   O4B  O  N N 286 
NAD   C3B  C  N S 287 
NAD   O3B  O  N N 288 
NAD   C2B  C  N R 289 
NAD   O2B  O  N N 290 
NAD   C1B  C  N R 291 
NAD   N9A  N  Y N 292 
NAD   C8A  C  Y N 293 
NAD   N7A  N  Y N 294 
NAD   C5A  C  Y N 295 
NAD   C6A  C  Y N 296 
NAD   N6A  N  N N 297 
NAD   N1A  N  Y N 298 
NAD   C2A  C  Y N 299 
NAD   N3A  N  Y N 300 
NAD   C4A  C  Y N 301 
NAD   O3   O  N N 302 
NAD   PN   P  N N 303 
NAD   O1N  O  N N 304 
NAD   O2N  O  N N 305 
NAD   O5D  O  N N 306 
NAD   C5D  C  N N 307 
NAD   C4D  C  N R 308 
NAD   O4D  O  N N 309 
NAD   C3D  C  N S 310 
NAD   O3D  O  N N 311 
NAD   C2D  C  N R 312 
NAD   O2D  O  N N 313 
NAD   C1D  C  N R 314 
NAD   N1N  N  Y N 315 
NAD   C2N  C  Y N 316 
NAD   C3N  C  Y N 317 
NAD   C7N  C  N N 318 
NAD   O7N  O  N N 319 
NAD   N7N  N  N N 320 
NAD   C4N  C  Y N 321 
NAD   C5N  C  Y N 322 
NAD   C6N  C  Y N 323 
NAD   HOA2 H  N N 324 
NAD   H51A H  N N 325 
NAD   H52A H  N N 326 
NAD   H4B  H  N N 327 
NAD   H3B  H  N N 328 
NAD   HO3A H  N N 329 
NAD   H2B  H  N N 330 
NAD   HO2A H  N N 331 
NAD   H1B  H  N N 332 
NAD   H8A  H  N N 333 
NAD   H61A H  N N 334 
NAD   H62A H  N N 335 
NAD   H2A  H  N N 336 
NAD   H51N H  N N 337 
NAD   H52N H  N N 338 
NAD   H4D  H  N N 339 
NAD   H3D  H  N N 340 
NAD   HO3N H  N N 341 
NAD   H2D  H  N N 342 
NAD   HO2N H  N N 343 
NAD   H1D  H  N N 344 
NAD   H2N  H  N N 345 
NAD   H71N H  N N 346 
NAD   H72N H  N N 347 
NAD   H4N  H  N N 348 
NAD   H5N  H  N N 349 
NAD   H6N  H  N N 350 
PHE   N    N  N N 351 
PHE   CA   C  N S 352 
PHE   C    C  N N 353 
PHE   O    O  N N 354 
PHE   CB   C  N N 355 
PHE   CG   C  Y N 356 
PHE   CD1  C  Y N 357 
PHE   CD2  C  Y N 358 
PHE   CE1  C  Y N 359 
PHE   CE2  C  Y N 360 
PHE   CZ   C  Y N 361 
PHE   OXT  O  N N 362 
PHE   H    H  N N 363 
PHE   H2   H  N N 364 
PHE   HA   H  N N 365 
PHE   HB2  H  N N 366 
PHE   HB3  H  N N 367 
PHE   HD1  H  N N 368 
PHE   HD2  H  N N 369 
PHE   HE1  H  N N 370 
PHE   HE2  H  N N 371 
PHE   HZ   H  N N 372 
PHE   HXT  H  N N 373 
PRO   N    N  N N 374 
PRO   CA   C  N S 375 
PRO   C    C  N N 376 
PRO   O    O  N N 377 
PRO   CB   C  N N 378 
PRO   CG   C  N N 379 
PRO   CD   C  N N 380 
PRO   OXT  O  N N 381 
PRO   H    H  N N 382 
PRO   HA   H  N N 383 
PRO   HB2  H  N N 384 
PRO   HB3  H  N N 385 
PRO   HG2  H  N N 386 
PRO   HG3  H  N N 387 
PRO   HD2  H  N N 388 
PRO   HD3  H  N N 389 
PRO   HXT  H  N N 390 
SER   N    N  N N 391 
SER   CA   C  N S 392 
SER   C    C  N N 393 
SER   O    O  N N 394 
SER   CB   C  N N 395 
SER   OG   O  N N 396 
SER   OXT  O  N N 397 
SER   H    H  N N 398 
SER   H2   H  N N 399 
SER   HA   H  N N 400 
SER   HB2  H  N N 401 
SER   HB3  H  N N 402 
SER   HG   H  N N 403 
SER   HXT  H  N N 404 
THR   N    N  N N 405 
THR   CA   C  N S 406 
THR   C    C  N N 407 
THR   O    O  N N 408 
THR   CB   C  N R 409 
THR   OG1  O  N N 410 
THR   CG2  C  N N 411 
THR   OXT  O  N N 412 
THR   H    H  N N 413 
THR   H2   H  N N 414 
THR   HA   H  N N 415 
THR   HB   H  N N 416 
THR   HG1  H  N N 417 
THR   HG21 H  N N 418 
THR   HG22 H  N N 419 
THR   HG23 H  N N 420 
THR   HXT  H  N N 421 
TRP   N    N  N N 422 
TRP   CA   C  N S 423 
TRP   C    C  N N 424 
TRP   O    O  N N 425 
TRP   CB   C  N N 426 
TRP   CG   C  Y N 427 
TRP   CD1  C  Y N 428 
TRP   CD2  C  Y N 429 
TRP   NE1  N  Y N 430 
TRP   CE2  C  Y N 431 
TRP   CE3  C  Y N 432 
TRP   CZ2  C  Y N 433 
TRP   CZ3  C  Y N 434 
TRP   CH2  C  Y N 435 
TRP   OXT  O  N N 436 
TRP   H    H  N N 437 
TRP   H2   H  N N 438 
TRP   HA   H  N N 439 
TRP   HB2  H  N N 440 
TRP   HB3  H  N N 441 
TRP   HD1  H  N N 442 
TRP   HE1  H  N N 443 
TRP   HE3  H  N N 444 
TRP   HZ2  H  N N 445 
TRP   HZ3  H  N N 446 
TRP   HH2  H  N N 447 
TRP   HXT  H  N N 448 
TYR   N    N  N N 449 
TYR   CA   C  N S 450 
TYR   C    C  N N 451 
TYR   O    O  N N 452 
TYR   CB   C  N N 453 
TYR   CG   C  Y N 454 
TYR   CD1  C  Y N 455 
TYR   CD2  C  Y N 456 
TYR   CE1  C  Y N 457 
TYR   CE2  C  Y N 458 
TYR   CZ   C  Y N 459 
TYR   OH   O  N N 460 
TYR   OXT  O  N N 461 
TYR   H    H  N N 462 
TYR   H2   H  N N 463 
TYR   HA   H  N N 464 
TYR   HB2  H  N N 465 
TYR   HB3  H  N N 466 
TYR   HD1  H  N N 467 
TYR   HD2  H  N N 468 
TYR   HE1  H  N N 469 
TYR   HE2  H  N N 470 
TYR   HH   H  N N 471 
TYR   HXT  H  N N 472 
VAL   N    N  N N 473 
VAL   CA   C  N S 474 
VAL   C    C  N N 475 
VAL   O    O  N N 476 
VAL   CB   C  N N 477 
VAL   CG1  C  N N 478 
VAL   CG2  C  N N 479 
VAL   OXT  O  N N 480 
VAL   H    H  N N 481 
VAL   H2   H  N N 482 
VAL   HA   H  N N 483 
VAL   HB   H  N N 484 
VAL   HG11 H  N N 485 
VAL   HG12 H  N N 486 
VAL   HG13 H  N N 487 
VAL   HG21 H  N N 488 
VAL   HG22 H  N N 489 
VAL   HG23 H  N N 490 
VAL   HXT  H  N N 491 
# 
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 
A1AG4 F1  C2   sing N N 1   
A1AG4 C2  C7   doub Y N 2   
A1AG4 C2  C3   sing Y N 3   
A1AG4 C3  C4   doub Y N 4   
A1AG4 C3  C20  sing N N 5   
A1AG4 C4  C5   sing Y N 6   
A1AG4 C5  C6   doub Y N 7   
A1AG4 C6  C7   sing Y N 8   
A1AG4 C6  N8   sing N N 9   
A1AG4 N8  S9   sing N N 10  
A1AG4 S9  O10  doub N N 11  
A1AG4 S9  O11  doub N N 12  
A1AG4 S9  C12  sing N N 13  
A1AG4 C12 C17  doub Y N 14  
A1AG4 C12 C13  sing Y N 15  
A1AG4 C13 C14  doub Y N 16  
A1AG4 C14 C15  sing Y N 17  
A1AG4 C14 CL19 sing N N 18  
A1AG4 C15 C16  doub Y N 19  
A1AG4 C15 CL18 sing N N 20  
A1AG4 C16 C17  sing Y N 21  
A1AG4 C20 O21  doub N N 22  
A1AG4 C20 O22  sing N N 23  
A1AG4 C4  H23  sing N N 24  
A1AG4 C7  H25  sing N N 25  
A1AG4 C13 H27  sing N N 26  
A1AG4 C16 H28  sing N N 27  
A1AG4 C5  H24  sing N N 28  
A1AG4 N8  H26  sing N N 29  
A1AG4 C17 H29  sing N N 30  
A1AG4 O22 H30  sing N N 31  
ALA   N   CA   sing N N 32  
ALA   N   H    sing N N 33  
ALA   N   H2   sing N N 34  
ALA   CA  C    sing N N 35  
ALA   CA  CB   sing N N 36  
ALA   CA  HA   sing N N 37  
ALA   C   O    doub N N 38  
ALA   C   OXT  sing N N 39  
ALA   CB  HB1  sing N N 40  
ALA   CB  HB2  sing N N 41  
ALA   CB  HB3  sing N N 42  
ALA   OXT HXT  sing N N 43  
ARG   N   CA   sing N N 44  
ARG   N   H    sing N N 45  
ARG   N   H2   sing N N 46  
ARG   CA  C    sing N N 47  
ARG   CA  CB   sing N N 48  
ARG   CA  HA   sing N N 49  
ARG   C   O    doub N N 50  
ARG   C   OXT  sing N N 51  
ARG   CB  CG   sing N N 52  
ARG   CB  HB2  sing N N 53  
ARG   CB  HB3  sing N N 54  
ARG   CG  CD   sing N N 55  
ARG   CG  HG2  sing N N 56  
ARG   CG  HG3  sing N N 57  
ARG   CD  NE   sing N N 58  
ARG   CD  HD2  sing N N 59  
ARG   CD  HD3  sing N N 60  
ARG   NE  CZ   sing N N 61  
ARG   NE  HE   sing N N 62  
ARG   CZ  NH1  sing N N 63  
ARG   CZ  NH2  doub N N 64  
ARG   NH1 HH11 sing N N 65  
ARG   NH1 HH12 sing N N 66  
ARG   NH2 HH21 sing N N 67  
ARG   NH2 HH22 sing N N 68  
ARG   OXT HXT  sing N N 69  
ASN   N   CA   sing N N 70  
ASN   N   H    sing N N 71  
ASN   N   H2   sing N N 72  
ASN   CA  C    sing N N 73  
ASN   CA  CB   sing N N 74  
ASN   CA  HA   sing N N 75  
ASN   C   O    doub N N 76  
ASN   C   OXT  sing N N 77  
ASN   CB  CG   sing N N 78  
ASN   CB  HB2  sing N N 79  
ASN   CB  HB3  sing N N 80  
ASN   CG  OD1  doub N N 81  
ASN   CG  ND2  sing N N 82  
ASN   ND2 HD21 sing N N 83  
ASN   ND2 HD22 sing N N 84  
ASN   OXT HXT  sing N N 85  
ASP   N   CA   sing N N 86  
ASP   N   H    sing N N 87  
ASP   N   H2   sing N N 88  
ASP   CA  C    sing N N 89  
ASP   CA  CB   sing N N 90  
ASP   CA  HA   sing N N 91  
ASP   C   O    doub N N 92  
ASP   C   OXT  sing N N 93  
ASP   CB  CG   sing N N 94  
ASP   CB  HB2  sing N N 95  
ASP   CB  HB3  sing N N 96  
ASP   CG  OD1  doub N N 97  
ASP   CG  OD2  sing N N 98  
ASP   OD2 HD2  sing N N 99  
ASP   OXT HXT  sing N N 100 
CYS   N   CA   sing N N 101 
CYS   N   H    sing N N 102 
CYS   N   H2   sing N N 103 
CYS   CA  C    sing N N 104 
CYS   CA  CB   sing N N 105 
CYS   CA  HA   sing N N 106 
CYS   C   O    doub N N 107 
CYS   C   OXT  sing N N 108 
CYS   CB  SG   sing N N 109 
CYS   CB  HB2  sing N N 110 
CYS   CB  HB3  sing N N 111 
CYS   SG  HG   sing N N 112 
CYS   OXT HXT  sing N N 113 
GLN   N   CA   sing N N 114 
GLN   N   H    sing N N 115 
GLN   N   H2   sing N N 116 
GLN   CA  C    sing N N 117 
GLN   CA  CB   sing N N 118 
GLN   CA  HA   sing N N 119 
GLN   C   O    doub N N 120 
GLN   C   OXT  sing N N 121 
GLN   CB  CG   sing N N 122 
GLN   CB  HB2  sing N N 123 
GLN   CB  HB3  sing N N 124 
GLN   CG  CD   sing N N 125 
GLN   CG  HG2  sing N N 126 
GLN   CG  HG3  sing N N 127 
GLN   CD  OE1  doub N N 128 
GLN   CD  NE2  sing N N 129 
GLN   NE2 HE21 sing N N 130 
GLN   NE2 HE22 sing N N 131 
GLN   OXT HXT  sing N N 132 
GLU   N   CA   sing N N 133 
GLU   N   H    sing N N 134 
GLU   N   H2   sing N N 135 
GLU   CA  C    sing N N 136 
GLU   CA  CB   sing N N 137 
GLU   CA  HA   sing N N 138 
GLU   C   O    doub N N 139 
GLU   C   OXT  sing N N 140 
GLU   CB  CG   sing N N 141 
GLU   CB  HB2  sing N N 142 
GLU   CB  HB3  sing N N 143 
GLU   CG  CD   sing N N 144 
GLU   CG  HG2  sing N N 145 
GLU   CG  HG3  sing N N 146 
GLU   CD  OE1  doub N N 147 
GLU   CD  OE2  sing N N 148 
GLU   OE2 HE2  sing N N 149 
GLU   OXT HXT  sing N N 150 
GLY   N   CA   sing N N 151 
GLY   N   H    sing N N 152 
GLY   N   H2   sing N N 153 
GLY   CA  C    sing N N 154 
GLY   CA  HA2  sing N N 155 
GLY   CA  HA3  sing N N 156 
GLY   C   O    doub N N 157 
GLY   C   OXT  sing N N 158 
GLY   OXT HXT  sing N N 159 
HIS   N   CA   sing N N 160 
HIS   N   H    sing N N 161 
HIS   N   H2   sing N N 162 
HIS   CA  C    sing N N 163 
HIS   CA  CB   sing N N 164 
HIS   CA  HA   sing N N 165 
HIS   C   O    doub N N 166 
HIS   C   OXT  sing N N 167 
HIS   CB  CG   sing N N 168 
HIS   CB  HB2  sing N N 169 
HIS   CB  HB3  sing N N 170 
HIS   CG  ND1  sing Y N 171 
HIS   CG  CD2  doub Y N 172 
HIS   ND1 CE1  doub Y N 173 
HIS   ND1 HD1  sing N N 174 
HIS   CD2 NE2  sing Y N 175 
HIS   CD2 HD2  sing N N 176 
HIS   CE1 NE2  sing Y N 177 
HIS   CE1 HE1  sing N N 178 
HIS   NE2 HE2  sing N N 179 
HIS   OXT HXT  sing N N 180 
HOH   O   H1   sing N N 181 
HOH   O   H2   sing N N 182 
ILE   N   CA   sing N N 183 
ILE   N   H    sing N N 184 
ILE   N   H2   sing N N 185 
ILE   CA  C    sing N N 186 
ILE   CA  CB   sing N N 187 
ILE   CA  HA   sing N N 188 
ILE   C   O    doub N N 189 
ILE   C   OXT  sing N N 190 
ILE   CB  CG1  sing N N 191 
ILE   CB  CG2  sing N N 192 
ILE   CB  HB   sing N N 193 
ILE   CG1 CD1  sing N N 194 
ILE   CG1 HG12 sing N N 195 
ILE   CG1 HG13 sing N N 196 
ILE   CG2 HG21 sing N N 197 
ILE   CG2 HG22 sing N N 198 
ILE   CG2 HG23 sing N N 199 
ILE   CD1 HD11 sing N N 200 
ILE   CD1 HD12 sing N N 201 
ILE   CD1 HD13 sing N N 202 
ILE   OXT HXT  sing N N 203 
LEU   N   CA   sing N N 204 
LEU   N   H    sing N N 205 
LEU   N   H2   sing N N 206 
LEU   CA  C    sing N N 207 
LEU   CA  CB   sing N N 208 
LEU   CA  HA   sing N N 209 
LEU   C   O    doub N N 210 
LEU   C   OXT  sing N N 211 
LEU   CB  CG   sing N N 212 
LEU   CB  HB2  sing N N 213 
LEU   CB  HB3  sing N N 214 
LEU   CG  CD1  sing N N 215 
LEU   CG  CD2  sing N N 216 
LEU   CG  HG   sing N N 217 
LEU   CD1 HD11 sing N N 218 
LEU   CD1 HD12 sing N N 219 
LEU   CD1 HD13 sing N N 220 
LEU   CD2 HD21 sing N N 221 
LEU   CD2 HD22 sing N N 222 
LEU   CD2 HD23 sing N N 223 
LEU   OXT HXT  sing N N 224 
LYS   N   CA   sing N N 225 
LYS   N   H    sing N N 226 
LYS   N   H2   sing N N 227 
LYS   CA  C    sing N N 228 
LYS   CA  CB   sing N N 229 
LYS   CA  HA   sing N N 230 
LYS   C   O    doub N N 231 
LYS   C   OXT  sing N N 232 
LYS   CB  CG   sing N N 233 
LYS   CB  HB2  sing N N 234 
LYS   CB  HB3  sing N N 235 
LYS   CG  CD   sing N N 236 
LYS   CG  HG2  sing N N 237 
LYS   CG  HG3  sing N N 238 
LYS   CD  CE   sing N N 239 
LYS   CD  HD2  sing N N 240 
LYS   CD  HD3  sing N N 241 
LYS   CE  NZ   sing N N 242 
LYS   CE  HE2  sing N N 243 
LYS   CE  HE3  sing N N 244 
LYS   NZ  HZ1  sing N N 245 
LYS   NZ  HZ2  sing N N 246 
LYS   NZ  HZ3  sing N N 247 
LYS   OXT HXT  sing N N 248 
MET   N   CA   sing N N 249 
MET   N   H    sing N N 250 
MET   N   H2   sing N N 251 
MET   CA  C    sing N N 252 
MET   CA  CB   sing N N 253 
MET   CA  HA   sing N N 254 
MET   C   O    doub N N 255 
MET   C   OXT  sing N N 256 
MET   CB  CG   sing N N 257 
MET   CB  HB2  sing N N 258 
MET   CB  HB3  sing N N 259 
MET   CG  SD   sing N N 260 
MET   CG  HG2  sing N N 261 
MET   CG  HG3  sing N N 262 
MET   SD  CE   sing N N 263 
MET   CE  HE1  sing N N 264 
MET   CE  HE2  sing N N 265 
MET   CE  HE3  sing N N 266 
MET   OXT HXT  sing N N 267 
NAD   PA  O1A  doub N N 268 
NAD   PA  O2A  sing N N 269 
NAD   PA  O5B  sing N N 270 
NAD   PA  O3   sing N N 271 
NAD   O2A HOA2 sing N N 272 
NAD   O5B C5B  sing N N 273 
NAD   C5B C4B  sing N N 274 
NAD   C5B H51A sing N N 275 
NAD   C5B H52A sing N N 276 
NAD   C4B O4B  sing N N 277 
NAD   C4B C3B  sing N N 278 
NAD   C4B H4B  sing N N 279 
NAD   O4B C1B  sing N N 280 
NAD   C3B O3B  sing N N 281 
NAD   C3B C2B  sing N N 282 
NAD   C3B H3B  sing N N 283 
NAD   O3B HO3A sing N N 284 
NAD   C2B O2B  sing N N 285 
NAD   C2B C1B  sing N N 286 
NAD   C2B H2B  sing N N 287 
NAD   O2B HO2A sing N N 288 
NAD   C1B N9A  sing N N 289 
NAD   C1B H1B  sing N N 290 
NAD   N9A C8A  sing Y N 291 
NAD   N9A C4A  sing Y N 292 
NAD   C8A N7A  doub Y N 293 
NAD   C8A H8A  sing N N 294 
NAD   N7A C5A  sing Y N 295 
NAD   C5A C6A  sing Y N 296 
NAD   C5A C4A  doub Y N 297 
NAD   C6A N6A  sing N N 298 
NAD   C6A N1A  doub Y N 299 
NAD   N6A H61A sing N N 300 
NAD   N6A H62A sing N N 301 
NAD   N1A C2A  sing Y N 302 
NAD   C2A N3A  doub Y N 303 
NAD   C2A H2A  sing N N 304 
NAD   N3A C4A  sing Y N 305 
NAD   O3  PN   sing N N 306 
NAD   PN  O1N  doub N N 307 
NAD   PN  O2N  sing N N 308 
NAD   PN  O5D  sing N N 309 
NAD   O5D C5D  sing N N 310 
NAD   C5D C4D  sing N N 311 
NAD   C5D H51N sing N N 312 
NAD   C5D H52N sing N N 313 
NAD   C4D O4D  sing N N 314 
NAD   C4D C3D  sing N N 315 
NAD   C4D H4D  sing N N 316 
NAD   O4D C1D  sing N N 317 
NAD   C3D O3D  sing N N 318 
NAD   C3D C2D  sing N N 319 
NAD   C3D H3D  sing N N 320 
NAD   O3D HO3N sing N N 321 
NAD   C2D O2D  sing N N 322 
NAD   C2D C1D  sing N N 323 
NAD   C2D H2D  sing N N 324 
NAD   O2D HO2N sing N N 325 
NAD   C1D N1N  sing N N 326 
NAD   C1D H1D  sing N N 327 
NAD   N1N C2N  sing Y N 328 
NAD   N1N C6N  doub Y N 329 
NAD   C2N C3N  doub Y N 330 
NAD   C2N H2N  sing N N 331 
NAD   C3N C7N  sing N N 332 
NAD   C3N C4N  sing Y N 333 
NAD   C7N O7N  doub N N 334 
NAD   C7N N7N  sing N N 335 
NAD   N7N H71N sing N N 336 
NAD   N7N H72N sing N N 337 
NAD   C4N C5N  doub Y N 338 
NAD   C4N H4N  sing N N 339 
NAD   C5N C6N  sing Y N 340 
NAD   C5N H5N  sing N N 341 
NAD   C6N H6N  sing N N 342 
PHE   N   CA   sing N N 343 
PHE   N   H    sing N N 344 
PHE   N   H2   sing N N 345 
PHE   CA  C    sing N N 346 
PHE   CA  CB   sing N N 347 
PHE   CA  HA   sing N N 348 
PHE   C   O    doub N N 349 
PHE   C   OXT  sing N N 350 
PHE   CB  CG   sing N N 351 
PHE   CB  HB2  sing N N 352 
PHE   CB  HB3  sing N N 353 
PHE   CG  CD1  doub Y N 354 
PHE   CG  CD2  sing Y N 355 
PHE   CD1 CE1  sing Y N 356 
PHE   CD1 HD1  sing N N 357 
PHE   CD2 CE2  doub Y N 358 
PHE   CD2 HD2  sing N N 359 
PHE   CE1 CZ   doub Y N 360 
PHE   CE1 HE1  sing N N 361 
PHE   CE2 CZ   sing Y N 362 
PHE   CE2 HE2  sing N N 363 
PHE   CZ  HZ   sing N N 364 
PHE   OXT HXT  sing N N 365 
PRO   N   CA   sing N N 366 
PRO   N   CD   sing N N 367 
PRO   N   H    sing N N 368 
PRO   CA  C    sing N N 369 
PRO   CA  CB   sing N N 370 
PRO   CA  HA   sing N N 371 
PRO   C   O    doub N N 372 
PRO   C   OXT  sing N N 373 
PRO   CB  CG   sing N N 374 
PRO   CB  HB2  sing N N 375 
PRO   CB  HB3  sing N N 376 
PRO   CG  CD   sing N N 377 
PRO   CG  HG2  sing N N 378 
PRO   CG  HG3  sing N N 379 
PRO   CD  HD2  sing N N 380 
PRO   CD  HD3  sing N N 381 
PRO   OXT HXT  sing N N 382 
SER   N   CA   sing N N 383 
SER   N   H    sing N N 384 
SER   N   H2   sing N N 385 
SER   CA  C    sing N N 386 
SER   CA  CB   sing N N 387 
SER   CA  HA   sing N N 388 
SER   C   O    doub N N 389 
SER   C   OXT  sing N N 390 
SER   CB  OG   sing N N 391 
SER   CB  HB2  sing N N 392 
SER   CB  HB3  sing N N 393 
SER   OG  HG   sing N N 394 
SER   OXT HXT  sing N N 395 
THR   N   CA   sing N N 396 
THR   N   H    sing N N 397 
THR   N   H2   sing N N 398 
THR   CA  C    sing N N 399 
THR   CA  CB   sing N N 400 
THR   CA  HA   sing N N 401 
THR   C   O    doub N N 402 
THR   C   OXT  sing N N 403 
THR   CB  OG1  sing N N 404 
THR   CB  CG2  sing N N 405 
THR   CB  HB   sing N N 406 
THR   OG1 HG1  sing N N 407 
THR   CG2 HG21 sing N N 408 
THR   CG2 HG22 sing N N 409 
THR   CG2 HG23 sing N N 410 
THR   OXT HXT  sing N N 411 
TRP   N   CA   sing N N 412 
TRP   N   H    sing N N 413 
TRP   N   H2   sing N N 414 
TRP   CA  C    sing N N 415 
TRP   CA  CB   sing N N 416 
TRP   CA  HA   sing N N 417 
TRP   C   O    doub N N 418 
TRP   C   OXT  sing N N 419 
TRP   CB  CG   sing N N 420 
TRP   CB  HB2  sing N N 421 
TRP   CB  HB3  sing N N 422 
TRP   CG  CD1  doub Y N 423 
TRP   CG  CD2  sing Y N 424 
TRP   CD1 NE1  sing Y N 425 
TRP   CD1 HD1  sing N N 426 
TRP   CD2 CE2  doub Y N 427 
TRP   CD2 CE3  sing Y N 428 
TRP   NE1 CE2  sing Y N 429 
TRP   NE1 HE1  sing N N 430 
TRP   CE2 CZ2  sing Y N 431 
TRP   CE3 CZ3  doub Y N 432 
TRP   CE3 HE3  sing N N 433 
TRP   CZ2 CH2  doub Y N 434 
TRP   CZ2 HZ2  sing N N 435 
TRP   CZ3 CH2  sing Y N 436 
TRP   CZ3 HZ3  sing N N 437 
TRP   CH2 HH2  sing N N 438 
TRP   OXT HXT  sing N N 439 
TYR   N   CA   sing N N 440 
TYR   N   H    sing N N 441 
TYR   N   H2   sing N N 442 
TYR   CA  C    sing N N 443 
TYR   CA  CB   sing N N 444 
TYR   CA  HA   sing N N 445 
TYR   C   O    doub N N 446 
TYR   C   OXT  sing N N 447 
TYR   CB  CG   sing N N 448 
TYR   CB  HB2  sing N N 449 
TYR   CB  HB3  sing N N 450 
TYR   CG  CD1  doub Y N 451 
TYR   CG  CD2  sing Y N 452 
TYR   CD1 CE1  sing Y N 453 
TYR   CD1 HD1  sing N N 454 
TYR   CD2 CE2  doub Y N 455 
TYR   CD2 HD2  sing N N 456 
TYR   CE1 CZ   doub Y N 457 
TYR   CE1 HE1  sing N N 458 
TYR   CE2 CZ   sing Y N 459 
TYR   CE2 HE2  sing N N 460 
TYR   CZ  OH   sing N N 461 
TYR   OH  HH   sing N N 462 
TYR   OXT HXT  sing N N 463 
VAL   N   CA   sing N N 464 
VAL   N   H    sing N N 465 
VAL   N   H2   sing N N 466 
VAL   CA  C    sing N N 467 
VAL   CA  CB   sing N N 468 
VAL   CA  HA   sing N N 469 
VAL   C   O    doub N N 470 
VAL   C   OXT  sing N N 471 
VAL   CB  CG1  sing N N 472 
VAL   CB  CG2  sing N N 473 
VAL   CB  HB   sing N N 474 
VAL   CG1 HG11 sing N N 475 
VAL   CG1 HG12 sing N N 476 
VAL   CG1 HG13 sing N N 477 
VAL   CG2 HG21 sing N N 478 
VAL   CG2 HG22 sing N N 479 
VAL   CG2 HG23 sing N N 480 
VAL   OXT HXT  sing N N 481 
# 
_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   8G84 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9AV4 
_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]   0.005348 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000439 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013148 
_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]   0.015380 
_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 
F  
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    . ILE   A 1 15  ? 6.854  -40.749 -4.34   1   128.79 ? 14  ILE   A N    1 1 
ATOM   2    C  CA   . ILE   A 1 15  ? 5.682  -41.261 -5.058  1   129.43 ? 14  ILE   A CA   1 1 
ATOM   3    C  C    . ILE   A 1 15  ? 5.007  -40.144 -5.871  1   129.72 ? 14  ILE   A C    1 1 
ATOM   4    O  O    . ILE   A 1 15  ? 4.751  -40.314 -7.067  1   129.77 ? 14  ILE   A O    1 1 
ATOM   5    C  CB   . ILE   A 1 15  ? 4.672  -41.963 -4.103  1   130.01 ? 14  ILE   A CB   1 1 
ATOM   6    C  CG1  . ILE   A 1 15  ? 5.375  -42.913 -3.11   1   130.87 ? 14  ILE   A CG1  1 1 
ATOM   7    C  CG2  . ILE   A 1 15  ? 3.582  -42.69  -4.895  1   130.5  ? 14  ILE   A CG2  1 1 
ATOM   8    C  CD1  . ILE   A 1 15  ? 4.483  -43.428 -1.99   1   131.91 ? 14  ILE   A CD1  1 1 
ATOM   9    N  N    . ILE   A 1 16  ? 4.716  -39.004 -5.212  1   129.61 ? 15  ILE   A N    1 1 
ATOM   10   C  CA   . ILE   A 1 16  ? 4.072  -37.841 -5.84   1   129.89 ? 15  ILE   A CA   1 1 
ATOM   11   C  C    . ILE   A 1 16  ? 5.087  -37.068 -6.685  1   130    ? 15  ILE   A C    1 1 
ATOM   12   O  O    . ILE   A 1 16  ? 4.746  -36.581 -7.761  1   130.14 ? 15  ILE   A O    1 1 
ATOM   13   C  CB   . ILE   A 1 16  ? 3.337  -36.889 -4.84   1   130.37 ? 15  ILE   A CB   1 1 
ATOM   14   C  CG1  . ILE   A 1 16  ? 2.874  -37.59  -3.531  1   131.29 ? 15  ILE   A CG1  1 1 
ATOM   15   C  CG2  . ILE   A 1 16  ? 2.172  -36.183 -5.535  1   130.77 ? 15  ILE   A CG2  1 1 
ATOM   16   C  CD1  . ILE   A 1 16  ? 3.833  -37.433 -2.317  1   132.35 ? 15  ILE   A CD1  1 1 
ATOM   17   N  N    . TYR   A 1 17  ? 6.332  -36.95  -6.186  1   129.73 ? 16  TYR   A N    1 1 
ATOM   18   C  CA   . TYR   A 1 17  ? 7.445  -36.282 -6.867  1   129.87 ? 16  TYR   A CA   1 1 
ATOM   19   C  C    . TYR   A 1 17  ? 8.005  -37.185 -7.975  1   129.56 ? 16  TYR   A C    1 1 
ATOM   20   O  O    . TYR   A 1 17  ? 8.421  -36.683 -9.01   1   129.55 ? 16  TYR   A O    1 1 
ATOM   21   C  CB   . TYR   A 1 17  ? 8.54   -35.953 -5.838  1   130.13 ? 16  TYR   A CB   1 1 
ATOM   22   C  CG   . TYR   A 1 17  ? 9.767  -35.227 -6.356  1   131.22 ? 16  TYR   A CG   1 1 
ATOM   23   C  CD1  . TYR   A 1 17  ? 10.857 -35.929 -6.856  1   132.08 ? 16  TYR   A CD1  1 1 
ATOM   24   C  CD2  . TYR   A 1 17  ? 9.898  -33.854 -6.208  1   132.23 ? 16  TYR   A CD2  1 1 
ATOM   25   C  CE1  . TYR   A 1 17  ? 12.014 -35.276 -7.265  1   132.91 ? 16  TYR   A CE1  1 1 
ATOM   26   C  CE2  . TYR   A 1 17  ? 11.061 -33.192 -6.592  1   133.09 ? 16  TYR   A CE2  1 1 
ATOM   27   C  CZ   . TYR   A 1 17  ? 12.115 -33.906 -7.127  1   133.85 ? 16  TYR   A CZ   1 1 
ATOM   28   O  OH   . TYR   A 1 17  ? 13.259 -33.255 -7.528  1   135.29 ? 16  TYR   A OH   1 1 
ATOM   29   N  N    . SER   A 1 18  ? 8.022  -38.51  -7.75   1   129.16 ? 17  SER   A N    1 1 
ATOM   30   C  CA   . SER   A 1 18  ? 8.531  -39.515 -8.689  1   129.26 ? 17  SER   A CA   1 1 
ATOM   31   C  C    . SER   A 1 18  ? 7.792  -39.503 -10.036 1   129.14 ? 17  SER   A C    1 1 
ATOM   32   O  O    . SER   A 1 18  ? 8.426  -39.629 -11.082 1   129.32 ? 17  SER   A O    1 1 
ATOM   33   C  CB   . SER   A 1 18  ? 8.446  -40.911 -8.074  1   130.54 ? 17  SER   A CB   1 1 
ATOM   34   O  OG   . SER   A 1 18  ? 8.82   -40.939 -6.706  1   132.72 ? 17  SER   A OG   1 1 
ATOM   35   N  N    . TYR   A 1 19  ? 6.457  -39.366 -10.015 1   128.6  ? 18  TYR   A N    1 1 
ATOM   36   C  CA   . TYR   A 1 19  ? 5.659  -39.336 -11.242 1   128.45 ? 18  TYR   A CA   1 1 
ATOM   37   C  C    . TYR   A 1 19  ? 5.575  -37.927 -11.849 1   127.68 ? 18  TYR   A C    1 1 
ATOM   38   O  O    . TYR   A 1 19  ? 5.391  -37.799 -13.057 1   127.94 ? 18  TYR   A O    1 1 
ATOM   39   C  CB   . TYR   A 1 19  ? 4.258  -39.898 -10.986 1   128.75 ? 18  TYR   A CB   1 1 
ATOM   40   C  CG   . TYR   A 1 19  ? 3.572  -40.436 -12.224 1   129.91 ? 18  TYR   A CG   1 1 
ATOM   41   C  CD1  . TYR   A 1 19  ? 4.106  -41.504 -12.93  1   130.88 ? 18  TYR   A CD1  1 1 
ATOM   42   C  CD2  . TYR   A 1 19  ? 2.35   -39.93  -12.639 1   131.06 ? 18  TYR   A CD2  1 1 
ATOM   43   C  CE1  . TYR   A 1 19  ? 3.465  -42.022 -14.051 1   131.88 ? 18  TYR   A CE1  1 1 
ATOM   44   C  CE2  . TYR   A 1 19  ? 1.691  -40.449 -13.749 1   132.05 ? 18  TYR   A CE2  1 1 
ATOM   45   C  CZ   . TYR   A 1 19  ? 2.254  -41.495 -14.456 1   132.86 ? 18  TYR   A CZ   1 1 
ATOM   46   O  OH   . TYR   A 1 19  ? 1.603  -42.004 -15.555 1   134.25 ? 18  TYR   A OH   1 1 
ATOM   47   N  N    . LEU   A 1 20  ? 5.709  -36.876 -11.018 1   126.59 ? 19  LEU   A N    1 1 
ATOM   48   C  CA   . LEU   A 1 20  ? 5.684  -35.483 -11.463 1   125.92 ? 19  LEU   A CA   1 1 
ATOM   49   C  C    . LEU   A 1 20  ? 7.007  -35.12  -12.153 1   125.06 ? 19  LEU   A C    1 1 
ATOM   50   O  O    . LEU   A 1 20  ? 6.986  -34.462 -13.192 1   125.25 ? 19  LEU   A O    1 1 
ATOM   51   C  CB   . LEU   A 1 20  ? 5.409  -34.544 -10.272 1   126.06 ? 19  LEU   A CB   1 1 
ATOM   52   C  CG   . LEU   A 1 20  ? 5.545  -33.044 -10.518 1   127.39 ? 19  LEU   A CG   1 1 
ATOM   53   C  CD1  . LEU   A 1 20  ? 4.267  -32.317 -10.17  1   127.77 ? 19  LEU   A CD1  1 1 
ATOM   54   C  CD2  . LEU   A 1 20  ? 6.707  -32.467 -9.727  1   128.09 ? 19  LEU   A CD2  1 1 
ATOM   55   N  N    . GLU   A 1 21  ? 8.154  -35.564 -11.595 1   123.88 ? 20  GLU   A N    1 1 
ATOM   56   C  CA   . GLU   A 1 21  ? 9.471  -35.297 -12.175 1   123.12 ? 20  GLU   A CA   1 1 
ATOM   57   C  C    . GLU   A 1 21  ? 9.666  -36.056 -13.486 1   121.88 ? 20  GLU   A C    1 1 
ATOM   58   O  O    . GLU   A 1 21  ? 10.178 -35.483 -14.445 1   122.03 ? 20  GLU   A O    1 1 
ATOM   59   C  CB   . GLU   A 1 21  ? 10.597 -35.643 -11.2   1   125.55 ? 20  GLU   A CB   1 1 
ATOM   60   C  CG   . GLU   A 1 21  ? 11.964 -35.28  -11.747 1   130.91 ? 20  GLU   A CG   1 1 
ATOM   61   C  CD   . GLU   A 1 21  ? 13.108 -36.092 -11.183 1   137.76 ? 20  GLU   A CD   1 1 
ATOM   62   O  OE1  . GLU   A 1 21  ? 13.727 -35.631 -10.199 1   139.37 ? 20  GLU   A OE1  1 1 
ATOM   63   O  OE2  . GLU   A 1 21  ? 13.39  -37.185 -11.726 1   139.84 ? 20  GLU   A OE2  1 1 
ATOM   64   N  N    . ALA   A 1 22  ? 9.227  -37.325 -13.551 1   120.41 ? 21  ALA   A N    1 1 
ATOM   65   C  CA   . ALA   A 1 22  ? 9.313  -38.112 -14.788 1   119.33 ? 21  ALA   A CA   1 1 
ATOM   66   C  C    . ALA   A 1 22  ? 8.485  -37.475 -15.931 1   117.8  ? 21  ALA   A C    1 1 
ATOM   67   O  O    . ALA   A 1 22  ? 8.808  -37.653 -17.107 1   117.84 ? 21  ALA   A O    1 1 
ATOM   68   C  CB   . ALA   A 1 22  ? 8.847  -39.537 -14.532 1   119.51 ? 21  ALA   A CB   1 1 
ATOM   69   N  N    . LEU   A 1 23  ? 7.427  -36.725 -15.568 1   116.26 ? 22  LEU   A N    1 1 
ATOM   70   C  CA   . LEU   A 1 23  ? 6.536  -35.99  -16.461 1   115.18 ? 22  LEU   A CA   1 1 
ATOM   71   C  C    . LEU   A 1 23  ? 7.236  -34.695 -16.931 1   113.83 ? 22  LEU   A C    1 1 
ATOM   72   O  O    . LEU   A 1 23  ? 7.157  -34.338 -18.109 1   113.75 ? 22  LEU   A O    1 1 
ATOM   73   C  CB   . LEU   A 1 23  ? 5.241  -35.672 -15.689 1   115.18 ? 22  LEU   A CB   1 1 
ATOM   74   C  CG   . LEU   A 1 23  ? 4.286  -34.672 -16.298 1   116.23 ? 22  LEU   A CG   1 1 
ATOM   75   C  CD1  . LEU   A 1 23  ? 3.589  -35.26  -17.507 1   116.54 ? 22  LEU   A CD1  1 1 
ATOM   76   C  CD2  . LEU   A 1 23  ? 3.285  -34.196 -15.261 1   116.71 ? 22  LEU   A CD2  1 1 
ATOM   77   N  N    . VAL   A 1 24  ? 7.945  -34.018 -16.011 1   112.45 ? 23  VAL   A N    1 1 
ATOM   78   C  CA   . VAL   A 1 24  ? 8.71   -32.805 -16.294 1   111.68 ? 23  VAL   A CA   1 1 
ATOM   79   C  C    . VAL   A 1 24  ? 9.964  -33.114 -17.155 1   110.73 ? 23  VAL   A C    1 1 
ATOM   80   O  O    . VAL   A 1 24  ? 10.383 -32.272 -17.941 1   110.99 ? 23  VAL   A O    1 1 
ATOM   81   C  CB   . VAL   A 1 24  ? 9.029  -32.039 -14.981 1   112.21 ? 23  VAL   A CB   1 1 
ATOM   82   C  CG1  . VAL   A 1 24  ? 10.155 -31.026 -15.158 1   112.6  ? 23  VAL   A CG1  1 1 
ATOM   83   C  CG2  . VAL   A 1 24  ? 7.779  -31.356 -14.443 1   112.77 ? 23  VAL   A CG2  1 1 
ATOM   84   N  N    . LYS   A 1 25  ? 10.513 -34.338 -17.068 1   109.38 ? 24  LYS   A N    1 1 
ATOM   85   C  CA   . LYS   A 1 25  ? 11.684 -34.718 -17.861 1   108.52 ? 24  LYS   A CA   1 1 
ATOM   86   C  C    . LYS   A 1 25  ? 11.371 -35.007 -19.341 1   107.62 ? 24  LYS   A C    1 1 
ATOM   87   O  O    . LYS   A 1 25  ? 12.29  -35.103 -20.149 1   107.88 ? 24  LYS   A O    1 1 
ATOM   88   C  CB   . LYS   A 1 25  ? 12.422 -35.897 -17.213 1   110.17 ? 24  LYS   A CB   1 1 
ATOM   89   C  CG   . LYS   A 1 25  ? 13.941 -35.776 -17.289 1   113.72 ? 24  LYS   A CG   1 1 
ATOM   90   C  CD   . LYS   A 1 25  ? 14.637 -36.615 -16.225 1   117.41 ? 24  LYS   A CD   1 1 
ATOM   91   C  CE   . LYS   A 1 25  ? 14.389 -36.078 -14.838 1   120.58 ? 24  LYS   A CE   1 1 
ATOM   92   N  NZ   . LYS   A 1 25  ? 15.224 -36.77  -13.821 1   122.63 ? 24  LYS   A NZ   1 1 
ATOM   93   N  N    . VAL   A 1 26  ? 10.09  -35.125 -19.705 1   106.43 ? 25  VAL   A N    1 1 
ATOM   94   C  CA   . VAL   A 1 26  ? 9.695  -35.372 -21.093 1   105.74 ? 25  VAL   A CA   1 1 
ATOM   95   C  C    . VAL   A 1 26  ? 9.218  -34.072 -21.759 1   104.68 ? 25  VAL   A C    1 1 
ATOM   96   O  O    . VAL   A 1 26  ? 9.678  -33.735 -22.854 1   104.73 ? 25  VAL   A O    1 1 
ATOM   97   C  CB   . VAL   A 1 26  ? 8.632  -36.494 -21.184 1   106.36 ? 25  VAL   A CB   1 1 
ATOM   98   C  CG1  . VAL   A 1 26  ? 8.171  -36.706 -22.62  1   106.9  ? 25  VAL   A CG1  1 1 
ATOM   99   C  CG2  . VAL   A 1 26  ? 9.166  -37.795 -20.596 1   106.84 ? 25  VAL   A CG2  1 1 
ATOM   100  N  N    . PHE   A 1 27  ? 8.299  -33.345 -21.094 1   103.54 ? 26  PHE   A N    1 1 
ATOM   101  C  CA   . PHE   A 1 27  ? 7.758  -32.07  -21.581 1   102.68 ? 26  PHE   A CA   1 1 
ATOM   102  C  C    . PHE   A 1 27  ? 8.859  -31.002 -21.547 1   100.53 ? 26  PHE   A C    1 1 
ATOM   103  O  O    . PHE   A 1 27  ? 9.003  -30.227 -22.489 1   100.87 ? 26  PHE   A O    1 1 
ATOM   104  C  CB   . PHE   A 1 27  ? 6.562  -31.633 -20.713 1   103.13 ? 26  PHE   A CB   1 1 
ATOM   105  C  CG   . PHE   A 1 27  ? 5.527  -30.764 -21.392 1   104.48 ? 26  PHE   A CG   1 1 
ATOM   106  C  CD1  . PHE   A 1 27  ? 4.931  -31.163 -22.576 1   105.61 ? 26  PHE   A CD1  1 1 
ATOM   107  C  CD2  . PHE   A 1 27  ? 5.082  -29.595 -20.797 1   105.69 ? 26  PHE   A CD2  1 1 
ATOM   108  C  CE1  . PHE   A 1 27  ? 3.938  -30.385 -23.178 1   106.4  ? 26  PHE   A CE1  1 1 
ATOM   109  C  CE2  . PHE   A 1 27  ? 4.088  -28.819 -21.4   1   106.52 ? 26  PHE   A CE2  1 1 
ATOM   110  C  CZ   . PHE   A 1 27  ? 3.524  -29.218 -22.587 1   106.21 ? 26  PHE   A CZ   1 1 
ATOM   111  N  N    . PHE   A 1 28  ? 9.654  -30.984 -20.478 1   98.22  ? 27  PHE   A N    1 1 
ATOM   112  C  CA   . PHE   A 1 28  ? 10.749 -30.026 -20.338 1   96.54  ? 27  PHE   A CA   1 1 
ATOM   113  C  C    . PHE   A 1 28  ? 12.095 -30.749 -20.14  1   92.9   ? 27  PHE   A C    1 1 
ATOM   114  O  O    . PHE   A 1 28  ? 12.588 -30.816 -19.013 1   93.04  ? 27  PHE   A O    1 1 
ATOM   115  C  CB   . PHE   A 1 28  ? 10.472 -29.071 -19.158 1   97.3   ? 27  PHE   A CB   1 1 
ATOM   116  C  CG   . PHE   A 1 28  ? 9.709  -27.825 -19.54  1   98.79  ? 27  PHE   A CG   1 1 
ATOM   117  C  CD1  . PHE   A 1 28  ? 8.43   -27.909 -20.069 1   99.85  ? 27  PHE   A CD1  1 1 
ATOM   118  C  CD2  . PHE   A 1 28  ? 10.264 -26.572 -19.355 1   99.92  ? 27  PHE   A CD2  1 1 
ATOM   119  C  CE1  . PHE   A 1 28  ? 7.735  -26.763 -20.431 1   100.74 ? 27  PHE   A CE1  1 1 
ATOM   120  C  CE2  . PHE   A 1 28  ? 9.564  -25.427 -19.71  1   100.82 ? 27  PHE   A CE2  1 1 
ATOM   121  C  CZ   . PHE   A 1 28  ? 8.306  -25.53  -20.25  1   100.67 ? 27  PHE   A CZ   1 1 
ATOM   122  N  N    . PRO   A 1 29  ? 12.699 -31.32  -21.203 1   89.44  ? 28  PRO   A N    1 1 
ATOM   123  C  CA   . PRO   A 1 29  ? 13.973 -32.025 -21.014 1   86.63  ? 28  PRO   A CA   1 1 
ATOM   124  C  C    . PRO   A 1 29  ? 15.18  -31.084 -20.965 1   82.95  ? 28  PRO   A C    1 1 
ATOM   125  O  O    . PRO   A 1 29  ? 15.171 -30.021 -21.579 1   83.13  ? 28  PRO   A O    1 1 
ATOM   126  C  CB   . PRO   A 1 29  ? 14.036 -32.992 -22.206 1   87.75  ? 28  PRO   A CB   1 1 
ATOM   127  C  CG   . PRO   A 1 29  ? 12.9   -32.605 -23.128 1   89     ? 28  PRO   A CG   1 1 
ATOM   128  C  CD   . PRO   A 1 29  ? 12.269 -31.351 -22.614 1   88.31  ? 28  PRO   A CD   1 1 
ATOM   129  N  N    . ARG   A 1 30  ? 16.214 -31.463 -20.213 1   79.43  ? 29  ARG   A N    1 1 
ATOM   130  C  CA   . ARG   A 1 30  ? 17.444 -30.677 -20.134 1   76.32  ? 29  ARG   A CA   1 1 
ATOM   131  C  C    . ARG   A 1 30  ? 18.388 -31.17  -21.234 1   73     ? 29  ARG   A C    1 1 
ATOM   132  O  O    . ARG   A 1 30  ? 18.466 -32.379 -21.474 1   72.5   ? 29  ARG   A O    1 1 
ATOM   133  C  CB   . ARG   A 1 30  ? 18.11  -30.845 -18.76  1   76.84  ? 29  ARG   A CB   1 1 
ATOM   134  C  CG   . ARG   A 1 30  ? 17.717 -29.803 -17.731 1   78.5   ? 29  ARG   A CG   1 1 
ATOM   135  C  CD   . ARG   A 1 30  ? 18.251 -30.187 -16.352 1   80.97  ? 29  ARG   A CD   1 1 
ATOM   136  N  NE   . ARG   A 1 30  ? 19.484 -29.475 -16.003 1   82.43  ? 29  ARG   A NE   1 1 
ATOM   137  C  CZ   . ARG   A 1 30  ? 19.567 -28.532 -15.07  1   83.63  ? 29  ARG   A CZ   1 1 
ATOM   138  N  NH1  . ARG   A 1 30  ? 18.497 -28.197 -14.358 1   83.18  ? 29  ARG   A NH1  1 1 
ATOM   139  N  NH2  . ARG   A 1 30  ? 20.721 -27.927 -14.831 1   83.43  ? 29  ARG   A NH2  1 1 
ATOM   140  N  N    . LYS   A 1 31  ? 19.098 -30.243 -21.901 1   70.55  ? 30  LYS   A N    1 1 
ATOM   141  C  CA   . LYS   A 1 31  ? 20.017 -30.598 -22.982 1   68.46  ? 30  LYS   A CA   1 1 
ATOM   142  C  C    . LYS   A 1 31  ? 21.267 -31.325 -22.487 1   64.76  ? 30  LYS   A C    1 1 
ATOM   143  O  O    . LYS   A 1 31  ? 21.856 -30.952 -21.464 1   64.79  ? 30  LYS   A O    1 1 
ATOM   144  C  CB   . LYS   A 1 31  ? 20.38  -29.381 -23.852 1   71.46  ? 30  LYS   A CB   1 1 
ATOM   145  C  CG   . LYS   A 1 31  ? 20.95  -29.79  -25.217 1   76.34  ? 30  LYS   A CG   1 1 
ATOM   146  C  CD   . LYS   A 1 31  ? 22.346 -29.243 -25.469 1   80.83  ? 30  LYS   A CD   1 1 
ATOM   147  C  CE   . LYS   A 1 31  ? 22.336 -28.065 -26.406 1   84.01  ? 30  LYS   A CE   1 1 
ATOM   148  N  NZ   . LYS   A 1 31  ? 22.414 -28.487 -27.833 1   85.89  ? 30  LYS   A NZ   1 1 
ATOM   149  N  N    . ARG   A 1 32  ? 21.639 -32.406 -23.2   1   61.23  ? 31  ARG   A N    1 1 
ATOM   150  C  CA   . ARG   A 1 32  ? 22.797 -33.221 -22.856 1   58.14  ? 31  ARG   A CA   1 1 
ATOM   151  C  C    . ARG   A 1 32  ? 24.01  -32.773 -23.645 1   54.07  ? 31  ARG   A C    1 1 
ATOM   152  O  O    . ARG   A 1 32  ? 23.954 -32.686 -24.866 1   54.56  ? 31  ARG   A O    1 1 
ATOM   153  C  CB   . ARG   A 1 32  ? 22.525 -34.708 -23.145 1   59.55  ? 31  ARG   A CB   1 1 
ATOM   154  C  CG   . ARG   A 1 32  ? 21.291 -35.282 -22.459 1   63.63  ? 31  ARG   A CG   1 1 
ATOM   155  C  CD   . ARG   A 1 32  ? 21.62  -36.466 -21.56  1   68.48  ? 31  ARG   A CD   1 1 
ATOM   156  N  NE   . ARG   A 1 32  ? 22.287 -37.543 -22.293 1   72.55  ? 31  ARG   A NE   1 1 
ATOM   157  C  CZ   . ARG   A 1 32  ? 22.716 -38.674 -21.74  1   75.39  ? 31  ARG   A CZ   1 1 
ATOM   158  N  NH1  . ARG   A 1 32  ? 22.547 -38.893 -20.443 1   74.28  ? 31  ARG   A NH1  1 1 
ATOM   159  N  NH2  . ARG   A 1 32  ? 23.327 -39.591 -22.478 1   76.24  ? 31  ARG   A NH2  1 1 
ATOM   160  N  N    . LYS   A 1 33  ? 25.107 -32.481 -22.952 1   50.16  ? 32  LYS   A N    1 1 
ATOM   161  C  CA   . LYS   A 1 33  ? 26.35  -32.101 -23.616 1   46.5   ? 32  LYS   A CA   1 1 
ATOM   162  C  C    . LYS   A 1 33  ? 27.172 -33.361 -23.902 1   44.24  ? 32  LYS   A C    1 1 
ATOM   163  O  O    . LYS   A 1 33  ? 26.846 -34.451 -23.406 1   44.21  ? 32  LYS   A O    1 1 
ATOM   164  C  CB   . LYS   A 1 33  ? 27.158 -31.128 -22.736 1   45.57  ? 32  LYS   A CB   1 1 
ATOM   165  C  CG   . LYS   A 1 33  ? 27.763 -31.765 -21.489 1   45.14  ? 32  LYS   A CG   1 1 
ATOM   166  C  CD   . LYS   A 1 33  ? 28.306 -30.711 -20.555 1   45.31  ? 32  LYS   A CD   1 1 
ATOM   167  C  CE   . LYS   A 1 33  ? 29.081 -31.291 -19.407 1   46.1   ? 32  LYS   A CE   1 1 
ATOM   168  N  NZ   . LYS   A 1 33  ? 29.6   -30.219 -18.524 1   45.9   ? 32  LYS   A NZ   1 1 
ATOM   169  N  N    . SER   A 1 34  ? 28.25  -33.214 -24.676 1   42.19  ? 33  SER   A N    1 1 
ATOM   170  C  CA   . SER   A 1 34  ? 29.145 -34.332 -24.916 1   40.63  ? 33  SER   A CA   1 1 
ATOM   171  C  C    . SER   A 1 34  ? 30.373 -34.207 -24.008 1   39.6   ? 33  SER   A C    1 1 
ATOM   172  O  O    . SER   A 1 34  ? 30.82  -33.098 -23.683 1   40.02  ? 33  SER   A O    1 1 
ATOM   173  C  CB   . SER   A 1 34  ? 29.554 -34.402 -26.381 1   40.39  ? 33  SER   A CB   1 1 
ATOM   174  O  OG   . SER   A 1 34  ? 30.362 -35.538 -26.633 1   40.99  ? 33  SER   A OG   1 1 
ATOM   175  N  N    . VAL   A 1 35  ? 30.87  -35.342 -23.53  1   37.85  ? 34  VAL   A N    1 1 
ATOM   176  C  CA   . VAL   A 1 35  ? 32.111 -35.376 -22.753 1   36.35  ? 34  VAL   A CA   1 1 
ATOM   177  C  C    . VAL   A 1 35  ? 33.19  -36.225 -23.473 1   35.41  ? 34  VAL   A C    1 1 
ATOM   178  O  O    . VAL   A 1 35  ? 34.215 -36.533 -22.873 1   35.84  ? 34  VAL   A O    1 1 
ATOM   179  C  CB   . VAL   A 1 35  ? 31.923 -35.817 -21.29  1   36.93  ? 34  VAL   A CB   1 1 
ATOM   180  C  CG1  . VAL   A 1 35  ? 31.146 -34.785 -20.494 1   37.09  ? 34  VAL   A CG1  1 1 
ATOM   181  C  CG2  . VAL   A 1 35  ? 31.254 -37.182 -21.212 1   37.88  ? 34  VAL   A CG2  1 1 
ATOM   182  N  N    . ALA   A 1 36  ? 32.958 -36.596 -24.755 1   34.11  ? 35  ALA   A N    1 1 
ATOM   183  C  CA   . ALA   A 1 36  ? 33.872 -37.36  -25.573 1   33.61  ? 35  ALA   A CA   1 1 
ATOM   184  C  C    . ALA   A 1 36  ? 35.175 -36.601 -25.722 1   33.45  ? 35  ALA   A C    1 1 
ATOM   185  O  O    . ALA   A 1 36  ? 35.157 -35.433 -26.08  1   33.38  ? 35  ALA   A O    1 1 
ATOM   186  C  CB   . ALA   A 1 36  ? 33.257 -37.57  -26.953 1   33.22  ? 35  ALA   A CB   1 1 
ATOM   187  N  N    . GLY   A 1 37  ? 36.285 -37.253 -25.437 1   33.21  ? 36  GLY   A N    1 1 
ATOM   188  C  CA   . GLY   A 1 37  ? 37.588 -36.636 -25.605 1   34.44  ? 36  GLY   A CA   1 1 
ATOM   189  C  C    . GLY   A 1 37  ? 38.041 -35.775 -24.453 1   36.51  ? 36  GLY   A C    1 1 
ATOM   190  O  O    . GLY   A 1 37  ? 39.177 -35.294 -24.476 1   38.22  ? 36  GLY   A O    1 1 
ATOM   191  N  N    . GLU   A 1 38  ? 37.165 -35.546 -23.455 1   35.82  ? 37  GLU   A N    1 1 
ATOM   192  C  CA   . GLU   A 1 38  ? 37.516 -34.788 -22.254 1   35.72  ? 37  GLU   A CA   1 1 
ATOM   193  C  C    . GLU   A 1 38  ? 38.493 -35.601 -21.417 1   34.25  ? 37  GLU   A C    1 1 
ATOM   194  O  O    . GLU   A 1 38  ? 38.4   -36.819 -21.435 1   35.25  ? 37  GLU   A O    1 1 
ATOM   195  C  CB   . GLU   A 1 38  ? 36.267 -34.515 -21.382 1   38.22  ? 37  GLU   A CB   1 1 
ATOM   196  C  CG   . GLU   A 1 38  ? 35.16  -33.709 -22.031 1   46.51  ? 37  GLU   A CG   1 1 
ATOM   197  C  CD   . GLU   A 1 38  ? 35.401 -32.235 -22.292 1   56.5   ? 37  GLU   A CD   1 1 
ATOM   198  O  OE1  . GLU   A 1 38  ? 36.558 -31.781 -22.166 1   58.81  ? 37  GLU   A OE1  1 1 
ATOM   199  O  OE2  . GLU   A 1 38  ? 34.428 -31.537 -22.656 1   60.17  ? 37  GLU   A OE2  1 1 
ATOM   200  N  N    . ILE   A 1 39  ? 39.382 -34.957 -20.65  1   31.95  ? 38  ILE   A N    1 1 
ATOM   201  C  CA   . ILE   A 1 39  ? 40.277 -35.694 -19.765 1   30.6   ? 38  ILE   A CA   1 1 
ATOM   202  C  C    . ILE   A 1 39  ? 39.642 -35.692 -18.364 1   29.89  ? 38  ILE   A C    1 1 
ATOM   203  O  O    . ILE   A 1 39  ? 39.624 -34.674 -17.69  1   29.92  ? 38  ILE   A O    1 1 
ATOM   204  C  CB   . ILE   A 1 39  ? 41.723 -35.155 -19.768 1   30.14  ? 38  ILE   A CB   1 1 
ATOM   205  C  CG1  . ILE   A 1 39  ? 42.36  -35.291 -21.158 1   29.21  ? 38  ILE   A CG1  1 1 
ATOM   206  C  CG2  . ILE   A 1 39  ? 42.541 -35.903 -18.693 1   30.61  ? 38  ILE   A CG2  1 1 
ATOM   207  C  CD1  . ILE   A 1 39  ? 43.727 -34.767 -21.264 1   29.41  ? 38  ILE   A CD1  1 1 
ATOM   208  N  N    . VAL   A 1 40  ? 39.064 -36.824 -17.958 1   29.12  ? 39  VAL   A N    1 1 
ATOM   209  C  CA   . VAL   A 1 40  ? 38.324 -36.987 -16.711 1   27.59  ? 39  VAL   A CA   1 1 
ATOM   210  C  C    . VAL   A 1 40  ? 39.166 -37.611 -15.639 1   27.96  ? 39  VAL   A C    1 1 
ATOM   211  O  O    . VAL   A 1 40  ? 39.622 -38.729 -15.802 1   28.29  ? 39  VAL   A O    1 1 
ATOM   212  C  CB   . VAL   A 1 40  ? 37.005 -37.783 -16.938 1   26.05  ? 39  VAL   A CB   1 1 
ATOM   213  C  CG1  . VAL   A 1 40  ? 36.178 -37.841 -15.665 1   26.11  ? 39  VAL   A CG1  1 1 
ATOM   214  C  CG2  . VAL   A 1 40  ? 36.19  -37.154 -18.06  1   25.68  ? 39  VAL   A CG2  1 1 
ATOM   215  N  N    . LEU   A 1 41  ? 39.351 -36.905 -14.524 1   28.08  ? 40  LEU   A N    1 1 
ATOM   216  C  CA   . LEU   A 1 41  ? 40.094 -37.443 -13.391 1   28.36  ? 40  LEU   A CA   1 1 
ATOM   217  C  C    . LEU   A 1 41  ? 39.118 -37.841 -12.308 1   27.95  ? 40  LEU   A C    1 1 
ATOM   218  O  O    . LEU   A 1 41  ? 38.381 -36.996 -11.814 1   27.67  ? 40  LEU   A O    1 1 
ATOM   219  C  CB   . LEU   A 1 41  ? 41.134 -36.463 -12.849 1   28.46  ? 40  LEU   A CB   1 1 
ATOM   220  C  CG   . LEU   A 1 41  ? 42.202 -37.068 -11.946 1   30.75  ? 40  LEU   A CG   1 1 
ATOM   221  C  CD1  . LEU   A 1 41  ? 43.473 -36.261 -12.028 1   32.49  ? 40  LEU   A CD1  1 1 
ATOM   222  C  CD2  . LEU   A 1 41  ? 41.758 -37.135 -10.513 1   31.07  ? 40  LEU   A CD2  1 1 
ATOM   223  N  N    . ILE   A 1 42  ? 39.087 -39.137 -11.962 1   27.59  ? 41  ILE   A N    1 1 
ATOM   224  C  CA   . ILE   A 1 42  ? 38.201 -39.655 -10.924 1   27.45  ? 41  ILE   A CA   1 1 
ATOM   225  C  C    . ILE   A 1 42  ? 39.027 -40.237 -9.788  1   27.85  ? 41  ILE   A C    1 1 
ATOM   226  O  O    . ILE   A 1 42  ? 39.802 -41.176 -10.008 1   27.71  ? 41  ILE   A O    1 1 
ATOM   227  C  CB   . ILE   A 1 42  ? 37.216 -40.707 -11.488 1   27.05  ? 41  ILE   A CB   1 1 
ATOM   228  C  CG1  . ILE   A 1 42  ? 36.417 -40.147 -12.669 1   27.58  ? 41  ILE   A CG1  1 1 
ATOM   229  C  CG2  . ILE   A 1 42  ? 36.293 -41.257 -10.393 1   26.77  ? 41  ILE   A CG2  1 1 
ATOM   230  C  CD1  . ILE   A 1 42  ? 35.755 -41.202 -13.459 1   28.79  ? 41  ILE   A CD1  1 1 
ATOM   231  N  N    . THR   A 1 43  ? 38.877 -39.657 -8.578  1   27.82  ? 42  THR   A N    1 1 
ATOM   232  C  CA   . THR   A 1 43  ? 39.548 -40.151 -7.375  1   28.21  ? 42  THR   A CA   1 1 
ATOM   233  C  C    . THR   A 1 43  ? 38.676 -41.242 -6.728  1   30.13  ? 42  THR   A C    1 1 
ATOM   234  O  O    . THR   A 1 43  ? 37.45  -41.243 -6.898  1   31.2   ? 42  THR   A O    1 1 
ATOM   235  C  CB   . THR   A 1 43  ? 39.906 -39.016 -6.428  1   27.73  ? 42  THR   A CB   1 1 
ATOM   236  O  OG1  . THR   A 1 43  ? 38.742 -38.566 -5.718  1   27.93  ? 42  THR   A OG1  1 1 
ATOM   237  C  CG2  . THR   A 1 43  ? 40.604 -37.86  -7.138  1   27.56  ? 42  THR   A CG2  1 1 
ATOM   238  N  N    . GLY   A 1 44  ? 39.294 -42.165 -6.007  1   30.13  ? 43  GLY   A N    1 1 
ATOM   239  C  CA   . GLY   A 1 44  ? 38.552 -43.278 -5.414  1   30.54  ? 43  GLY   A CA   1 1 
ATOM   240  C  C    . GLY   A 1 44  ? 37.934 -44.175 -6.485  1   30.27  ? 43  GLY   A C    1 1 
ATOM   241  O  O    . GLY   A 1 44  ? 36.891 -44.799 -6.274  1   30.31  ? 43  GLY   A O    1 1 
ATOM   242  N  N    . ALA   A 1 45  ? 38.584 -44.263 -7.639  1   29.92  ? 44  ALA   A N    1 1 
ATOM   243  C  CA   . ALA   A 1 45  ? 38.075 -45.049 -8.769  1   30.13  ? 44  ALA   A CA   1 1 
ATOM   244  C  C    . ALA   A 1 45  ? 38.291 -46.564 -8.661  1   31.43  ? 44  ALA   A C    1 1 
ATOM   245  O  O    . ALA   A 1 45  ? 37.904 -47.287 -9.582  1   31.6   ? 44  ALA   A O    1 1 
ATOM   246  C  CB   . ALA   A 1 45  ? 38.668 -44.532 -10.053 1   29.38  ? 44  ALA   A CB   1 1 
ATOM   247  N  N    . GLY   A 1 46  ? 38.9   -47.023 -7.558  1   31.5   ? 45  GLY   A N    1 1 
ATOM   248  C  CA   . GLY   A 1 46  ? 39.229 -48.422 -7.328  1   31.82  ? 45  GLY   A CA   1 1 
ATOM   249  C  C    . GLY   A 1 46  ? 38.084 -49.303 -6.875  1   32.34  ? 45  GLY   A C    1 1 
ATOM   250  O  O    . GLY   A 1 46  ? 38.232 -50.529 -6.85   1   33.69  ? 45  GLY   A O    1 1 
ATOM   251  N  N    . HIS   A 1 47  ? 36.929 -48.707 -6.548  1   30.78  ? 46  HIS   A N    1 1 
ATOM   252  C  CA   . HIS   A 1 47  ? 35.756 -49.454 -6.116  1   30.24  ? 46  HIS   A CA   1 1 
ATOM   253  C  C    . HIS   A 1 47  ? 34.506 -48.549 -6.126  1   31.28  ? 46  HIS   A C    1 1 
ATOM   254  O  O    . HIS   A 1 47  ? 34.635 -47.326 -6.199  1   32.37  ? 46  HIS   A O    1 1 
ATOM   255  C  CB   . HIS   A 1 47  ? 36.006 -49.983 -4.683  1   29.81  ? 46  HIS   A CB   1 1 
ATOM   256  C  CG   . HIS   A 1 47  ? 35.002 -50.996 -4.205  1   30.15  ? 46  HIS   A CG   1 1 
ATOM   257  N  ND1  . HIS   A 1 47  ? 34.98  -52.29  -4.702  1   31.34  ? 46  HIS   A ND1  1 1 
ATOM   258  C  CD2  . HIS   A 1 47  ? 34.032 -50.88  -3.274  1   31.16  ? 46  HIS   A CD2  1 1 
ATOM   259  C  CE1  . HIS   A 1 47  ? 33.992 -52.903 -4.075  1   31.96  ? 46  HIS   A CE1  1 1 
ATOM   260  N  NE2  . HIS   A 1 47  ? 33.402 -52.098 -3.198  1   32.3   ? 46  HIS   A NE2  1 1 
ATOM   261  N  N    . GLY   A 1 48  ? 33.321 -49.158 -6.018  1   30.77  ? 47  GLY   A N    1 1 
ATOM   262  C  CA   . GLY   A 1 48  ? 32.038 -48.501 -5.816  1   31.15  ? 47  GLY   A CA   1 1 
ATOM   263  C  C    . GLY   A 1 48  ? 31.69  -47.376 -6.745  1   32.55  ? 47  GLY   A C    1 1 
ATOM   264  O  O    . GLY   A 1 48  ? 31.818 -47.516 -7.962  1   32.95  ? 47  GLY   A O    1 1 
ATOM   265  N  N    . ILE   A 1 49  ? 31.236 -46.238 -6.179  1   32.68  ? 48  ILE   A N    1 1 
ATOM   266  C  CA   . ILE   A 1 49  ? 30.787 -45.107 -6.981  1   32.74  ? 48  ILE   A CA   1 1 
ATOM   267  C  C    . ILE   A 1 49  ? 31.855 -44.618 -7.975  1   32.75  ? 48  ILE   A C    1 1 
ATOM   268  O  O    . ILE   A 1 49  ? 31.536 -44.38  -9.132  1   32.86  ? 48  ILE   A O    1 1 
ATOM   269  C  CB   . ILE   A 1 49  ? 30.24  -43.991 -6.082  1   33.59  ? 48  ILE   A CB   1 1 
ATOM   270  C  CG1  . ILE   A 1 49  ? 29.06  -44.511 -5.249  1   34.36  ? 48  ILE   A CG1  1 1 
ATOM   271  C  CG2  . ILE   A 1 49  ? 29.825 -42.775 -6.908  1   34.56  ? 48  ILE   A CG2  1 1 
ATOM   272  C  CD1  . ILE   A 1 49  ? 28.648 -43.59  -4.156  1   36.06  ? 48  ILE   A CD1  1 1 
ATOM   273  N  N    . GLY   A 1 50  ? 33.108 -44.553 -7.541  1   32.04  ? 49  GLY   A N    1 1 
ATOM   274  C  CA   . GLY   A 1 50  ? 34.212 -44.114 -8.385  1   31.42  ? 49  GLY   A CA   1 1 
ATOM   275  C  C    . GLY   A 1 50  ? 34.478 -45.012 -9.564  1   30.72  ? 49  GLY   A C    1 1 
ATOM   276  O  O    . GLY   A 1 50  ? 34.724 -44.519 -10.664 1   30.62  ? 49  GLY   A O    1 1 
ATOM   277  N  N    . ARG   A 1 51  ? 34.415 -46.338 -9.341  1   30.25  ? 50  ARG   A N    1 1 
ATOM   278  C  CA   . ARG   A 1 51  ? 34.616 -47.374 -10.352 1   30.14  ? 50  ARG   A CA   1 1 
ATOM   279  C  C    . ARG   A 1 51  ? 33.485 -47.359 -11.374 1   30.83  ? 50  ARG   A C    1 1 
ATOM   280  O  O    . ARG   A 1 51  ? 33.747 -47.403 -12.568 1   31.23  ? 50  ARG   A O    1 1 
ATOM   281  C  CB   . ARG   A 1 51  ? 34.713 -48.76  -9.662  1   31.27  ? 50  ARG   A CB   1 1 
ATOM   282  C  CG   . ARG   A 1 51  ? 34.463 -49.98  -10.566 1   31.87  ? 50  ARG   A CG   1 1 
ATOM   283  C  CD   . ARG   A 1 51  ? 34.737 -51.274 -9.867  1   33.21  ? 50  ARG   A CD   1 1 
ATOM   284  N  NE   . ARG   A 1 51  ? 36.17  -51.483 -9.663  1   36.07  ? 50  ARG   A NE   1 1 
ATOM   285  C  CZ   . ARG   A 1 51  ? 36.695 -52.589 -9.134  1   38.35  ? 50  ARG   A CZ   1 1 
ATOM   286  N  NH1  . ARG   A 1 51  ? 35.908 -53.586 -8.742  1   35.62  ? 50  ARG   A NH1  1 1 
ATOM   287  N  NH2  . ARG   A 1 51  ? 38.007 -52.701 -8.981  1   38.73  ? 50  ARG   A NH2  1 1 
ATOM   288  N  N    . TRP   A 1 52  ? 32.232 -47.323 -10.917 1   31.7   ? 51  TRP   A N    1 1 
ATOM   289  C  CA   . TRP   A 1 52  ? 31.09  -47.334 -11.82  1   33.43  ? 51  TRP   A CA   1 1 
ATOM   290  C  C    . TRP   A 1 52  ? 30.901 -45.986 -12.514 1   34.3   ? 51  TRP   A C    1 1 
ATOM   291  O  O    . TRP   A 1 52  ? 30.384 -45.969 -13.628 1   35.21  ? 51  TRP   A O    1 1 
ATOM   292  C  CB   . TRP   A 1 52  ? 29.841 -47.849 -11.116 1   34.15  ? 51  TRP   A CB   1 1 
ATOM   293  C  CG   . TRP   A 1 52  ? 29.974 -49.314 -10.842 1   35.57  ? 51  TRP   A CG   1 1 
ATOM   294  C  CD1  . TRP   A 1 52  ? 30.683 -49.896 -9.831  1   36.72  ? 51  TRP   A CD1  1 1 
ATOM   295  C  CD2  . TRP   A 1 52  ? 29.524 -50.387 -11.684 1   36.24  ? 51  TRP   A CD2  1 1 
ATOM   296  N  NE1  . TRP   A 1 52  ? 30.667 -51.265 -9.965  1   37.22  ? 51  TRP   A NE1  1 1 
ATOM   297  C  CE2  . TRP   A 1 52  ? 29.946 -51.595 -11.087 1   37.16  ? 51  TRP   A CE2  1 1 
ATOM   298  C  CE3  . TRP   A 1 52  ? 28.787 -50.448 -12.878 1   37.12  ? 51  TRP   A CE3  1 1 
ATOM   299  C  CZ2  . TRP   A 1 52  ? 29.645 -52.853 -11.639 1   37.72  ? 51  TRP   A CZ2  1 1 
ATOM   300  C  CZ3  . TRP   A 1 52  ? 28.484 -51.691 -13.418 1   37.88  ? 51  TRP   A CZ3  1 1 
ATOM   301  C  CH2  . TRP   A 1 52  ? 28.9   -52.876 -12.793 1   37.67  ? 51  TRP   A CH2  1 1 
ATOM   302  N  N    . THR   A 1 53  ? 31.395 -44.871 -11.927 1   33.76  ? 52  THR   A N    1 1 
ATOM   303  C  CA   . THR   A 1 53  ? 31.389 -43.588 -12.623 1   33.84  ? 52  THR   A CA   1 1 
ATOM   304  C  C    . THR   A 1 53  ? 32.405 -43.656 -13.773 1   34.26  ? 52  THR   A C    1 1 
ATOM   305  O  O    . THR   A 1 53  ? 32.104 -43.192 -14.871 1   35.12  ? 52  THR   A O    1 1 
ATOM   306  C  CB   . THR   A 1 53  ? 31.715 -42.467 -11.669 1   34.38  ? 52  THR   A CB   1 1 
ATOM   307  O  OG1  . THR   A 1 53  ? 30.674 -42.433 -10.713 1   36.05  ? 52  THR   A OG1  1 1 
ATOM   308  C  CG2  . THR   A 1 53  ? 31.82  -41.136 -12.352 1   33.94  ? 52  THR   A CG2  1 1 
ATOM   309  N  N    . ALA   A 1 54  ? 33.578 -44.302 -13.543 1   33.48  ? 53  ALA   A N    1 1 
ATOM   310  C  CA   . ALA   A 1 54  ? 34.611 -44.505 -14.549 1   32.85  ? 53  ALA   A CA   1 1 
ATOM   311  C  C    . ALA   A 1 54  ? 34.048 -45.259 -15.735 1   32.64  ? 53  ALA   A C    1 1 
ATOM   312  O  O    . ALA   A 1 54  ? 34.29  -44.855 -16.861 1   32.84  ? 53  ALA   A O    1 1 
ATOM   313  C  CB   . ALA   A 1 54  ? 35.801 -45.244 -13.957 1   32.67  ? 53  ALA   A CB   1 1 
ATOM   314  N  N    . TYR   A 1 55  ? 33.231 -46.289 -15.497 1   32.85  ? 54  TYR   A N    1 1 
ATOM   315  C  CA   . TYR   A 1 55  ? 32.624 -47.067 -16.589 1   33.6   ? 54  TYR   A CA   1 1 
ATOM   316  C  C    . TYR   A 1 55  ? 31.656 -46.194 -17.377 1   34.65  ? 54  TYR   A C    1 1 
ATOM   317  O  O    . TYR   A 1 55  ? 31.588 -46.334 -18.592 1   34.84  ? 54  TYR   A O    1 1 
ATOM   318  C  CB   . TYR   A 1 55  ? 31.883 -48.334 -16.093 1   33.37  ? 54  TYR   A CB   1 1 
ATOM   319  C  CG   . TYR   A 1 55  ? 32.715 -49.33  -15.316 1   34.32  ? 54  TYR   A CG   1 1 
ATOM   320  C  CD1  . TYR   A 1 55  ? 34.101 -49.339 -15.415 1   34.93  ? 54  TYR   A CD1  1 1 
ATOM   321  C  CD2  . TYR   A 1 55  ? 32.113 -50.28  -14.492 1   35.8   ? 54  TYR   A CD2  1 1 
ATOM   322  C  CE1  . TYR   A 1 55  ? 34.869 -50.239 -14.689 1   36.06  ? 54  TYR   A CE1  1 1 
ATOM   323  C  CE2  . TYR   A 1 55  ? 32.87  -51.186 -13.76  1   36.6   ? 54  TYR   A CE2  1 1 
ATOM   324  C  CZ   . TYR   A 1 55  ? 34.248 -51.174 -13.877 1   37.61  ? 54  TYR   A CZ   1 1 
ATOM   325  O  OH   . TYR   A 1 55  ? 34.998 -52.082 -13.175 1   39.2   ? 54  TYR   A OH   1 1 
ATOM   326  N  N    . GLU   A 1 56  ? 30.921 -45.289 -16.707 1   35.08  ? 55  GLU   A N    1 1 
ATOM   327  C  CA   . GLU   A 1 56  ? 30.002 -44.391 -17.41  1   36.31  ? 55  GLU   A CA   1 1 
ATOM   328  C  C    . GLU   A 1 56  ? 30.746 -43.437 -18.349 1   36.53  ? 55  GLU   A C    1 1 
ATOM   329  O  O    . GLU   A 1 56  ? 30.311 -43.22  -19.47  1   36.65  ? 55  GLU   A O    1 1 
ATOM   330  C  CB   . GLU   A 1 56  ? 29.143 -43.58  -16.422 1   39.6   ? 55  GLU   A CB   1 1 
ATOM   331  C  CG   . GLU   A 1 56  ? 28.17  -44.419 -15.629 1   44.31  ? 55  GLU   A CG   1 1 
ATOM   332  C  CD   . GLU   A 1 56  ? 26.994 -45.005 -16.386 1   51.57  ? 55  GLU   A CD   1 1 
ATOM   333  O  OE1  . GLU   A 1 56  ? 26.846 -44.737 -17.601 1   52.06  ? 55  GLU   A OE1  1 1 
ATOM   334  O  OE2  . GLU   A 1 56  ? 26.209 -45.741 -15.747 1   56.37  ? 55  GLU   A OE2  1 1 
ATOM   335  N  N    . PHE   A 1 57  ? 31.865 -42.873 -17.887 1   36.88  ? 56  PHE   A N    1 1 
ATOM   336  C  CA   . PHE   A 1 57  ? 32.676 -41.964 -18.688 1   37.02  ? 56  PHE   A CA   1 1 
ATOM   337  C  C    . PHE   A 1 57  ? 33.411 -42.707 -19.794 1   38.19  ? 56  PHE   A C    1 1 
ATOM   338  O  O    . PHE   A 1 57  ? 33.583 -42.147 -20.878 1   38.83  ? 56  PHE   A O    1 1 
ATOM   339  C  CB   . PHE   A 1 57  ? 33.651 -41.189 -17.805 1   36.32  ? 56  PHE   A CB   1 1 
ATOM   340  C  CG   . PHE   A 1 57  ? 33.095 -39.956 -17.138 1   36.13  ? 56  PHE   A CG   1 1 
ATOM   341  C  CD1  . PHE   A 1 57  ? 32.929 -38.78  -17.851 1   36.43  ? 56  PHE   A CD1  1 1 
ATOM   342  C  CD2  . PHE   A 1 57  ? 32.817 -39.947 -15.779 1   36.47  ? 56  PHE   A CD2  1 1 
ATOM   343  C  CE1  . PHE   A 1 57  ? 32.469 -37.628 -17.226 1   36.51  ? 56  PHE   A CE1  1 1 
ATOM   344  C  CE2  . PHE   A 1 57  ? 32.346 -38.797 -15.159 1   36.51  ? 56  PHE   A CE2  1 1 
ATOM   345  C  CZ   . PHE   A 1 57  ? 32.184 -37.646 -15.885 1   36.3   ? 56  PHE   A CZ   1 1 
ATOM   346  N  N    . ALA   A 1 58  ? 33.767 -43.989 -19.577 1   38.3   ? 57  ALA   A N    1 1 
ATOM   347  C  CA   . ALA   A 1 58  ? 34.382 -44.807 -20.619 1   38.78  ? 57  ALA   A CA   1 1 
ATOM   348  C  C    . ALA   A 1 58  ? 33.386 -45.028 -21.76  1   39.5   ? 57  ALA   A C    1 1 
ATOM   349  O  O    . ALA   A 1 58  ? 33.78  -45.003 -22.937 1   40.14  ? 57  ALA   A O    1 1 
ATOM   350  C  CB   . ALA   A 1 58  ? 34.823 -46.138 -20.05  1   38.87  ? 57  ALA   A CB   1 1 
ATOM   351  N  N    . LYS   A 1 59  ? 32.088 -45.231 -21.433 1   39.31  ? 58  LYS   A N    1 1 
ATOM   352  C  CA   . LYS   A 1 59  ? 31.069 -45.377 -22.485 1   39.45  ? 58  LYS   A CA   1 1 
ATOM   353  C  C    . LYS   A 1 59  ? 30.803 -44.016 -23.172 1   39.42  ? 58  LYS   A C    1 1 
ATOM   354  O  O    . LYS   A 1 59  ? 30.431 -44.006 -24.325 1   40.02  ? 58  LYS   A O    1 1 
ATOM   355  C  CB   . LYS   A 1 59  ? 29.779 -46.035 -21.958 1   41.5   ? 58  LYS   A CB   1 1 
ATOM   356  C  CG   . LYS   A 1 59  ? 29.957 -47.529 -21.658 1   48.06  ? 58  LYS   A CG   1 1 
ATOM   357  C  CD   . LYS   A 1 59  ? 28.743 -48.217 -20.967 1   55.11  ? 58  LYS   A CD   1 1 
ATOM   358  C  CE   . LYS   A 1 59  ? 28.653 -47.914 -19.486 1   61.18  ? 58  LYS   A CE   1 1 
ATOM   359  N  NZ   . LYS   A 1 59  ? 27.559 -48.669 -18.808 1   65.11  ? 58  LYS   A NZ   1 1 
ATOM   360  N  N    . GLN   A 1 60  ? 31.063 -42.871 -22.494 1   39.22  ? 59  GLN   A N    1 1 
ATOM   361  C  CA   . GLN   A 1 60  ? 30.915 -41.519 -23.062 1   39.24  ? 59  GLN   A CA   1 1 
ATOM   362  C  C    . GLN   A 1 60  ? 32.079 -41.08  -23.978 1   38.72  ? 59  GLN   A C    1 1 
ATOM   363  O  O    . GLN   A 1 60  ? 32.079 -39.943 -24.47  1   39     ? 59  GLN   A O    1 1 
ATOM   364  C  CB   . GLN   A 1 60  ? 30.765 -40.488 -21.941 1   41.01  ? 59  GLN   A CB   1 1 
ATOM   365  C  CG   . GLN   A 1 60  ? 29.457 -40.583 -21.175 1   45.73  ? 59  GLN   A CG   1 1 
ATOM   366  C  CD   . GLN   A 1 60  ? 28.237 -40.312 -22.023 1   51.62  ? 59  GLN   A CD   1 1 
ATOM   367  O  OE1  . GLN   A 1 60  ? 28.241 -39.48  -22.942 1   53.53  ? 59  GLN   A OE1  1 1 
ATOM   368  N  NE2  . GLN   A 1 60  ? 27.154 -41.006 -21.719 1   52.49  ? 59  GLN   A NE2  1 1 
ATOM   369  N  N    . LYS   A 1 61  ? 33.069 -41.979 -24.185 1   37.79  ? 60  LYS   A N    1 1 
ATOM   370  C  CA   . LYS   A 1 61  ? 34.273 -41.825 -25.003 1   36.94  ? 60  LYS   A CA   1 1 
ATOM   371  C  C    . LYS   A 1 61  ? 35.258 -40.756 -24.44  1   36.35  ? 60  LYS   A C    1 1 
ATOM   372  O  O    . LYS   A 1 61  ? 35.997 -40.139 -25.208 1   37.12  ? 60  LYS   A O    1 1 
ATOM   373  C  CB   . LYS   A 1 61  ? 33.929 -41.585 -26.471 1   37.67  ? 60  LYS   A CB   1 1 
ATOM   374  C  CG   . LYS   A 1 61  ? 32.958 -42.598 -27.067 1   41.55  ? 60  LYS   A CG   1 1 
ATOM   375  C  CD   . LYS   A 1 61  ? 32.943 -42.45  -28.58  1   47.71  ? 60  LYS   A CD   1 1 
ATOM   376  C  CE   . LYS   A 1 61  ? 31.634 -42.767 -29.266 1   53.37  ? 60  LYS   A CE   1 1 
ATOM   377  N  NZ   . LYS   A 1 61  ? 31.69  -42.417 -30.728 1   56.39  ? 60  LYS   A NZ   1 1 
ATOM   378  N  N    . SER   A 1 62  ? 35.299 -40.584 -23.104 1   34.31  ? 61  SER   A N    1 1 
ATOM   379  C  CA   . SER   A 1 62  ? 36.231 -39.668 -22.437 1   33.77  ? 61  SER   A CA   1 1 
ATOM   380  C  C    . SER   A 1 62  ? 37.627 -40.313 -22.284 1   33.35  ? 61  SER   A C    1 1 
ATOM   381  O  O    . SER   A 1 62  ? 37.733 -41.531 -22.312 1   34.07  ? 61  SER   A O    1 1 
ATOM   382  C  CB   . SER   A 1 62  ? 35.729 -39.357 -21.023 1   34.39  ? 61  SER   A CB   1 1 
ATOM   383  O  OG   . SER   A 1 62  ? 34.606 -38.493 -20.958 1   35.08  ? 61  SER   A OG   1 1 
ATOM   384  N  N    . ARG   A 1 63  ? 38.683 -39.517 -22.076 1   32.18  ? 62  ARG   A N    1 1 
ATOM   385  C  CA   . ARG   A 1 63  ? 40.011 -40.05  -21.752 1   32.51  ? 62  ARG   A CA   1 1 
ATOM   386  C  C    . ARG   A 1 63  ? 40.05  -40.039 -20.215 1   33.99  ? 62  ARG   A C    1 1 
ATOM   387  O  O    . ARG   A 1 63  ? 39.731 -39.012 -19.592 1   34.06  ? 62  ARG   A O    1 1 
ATOM   388  C  CB   . ARG   A 1 63  ? 41.142 -39.189 -22.328 1   33.15  ? 62  ARG   A CB   1 1 
ATOM   389  C  CG   . ARG   A 1 63  ? 41.017 -38.987 -23.838 1   36.8   ? 62  ARG   A CG   1 1 
ATOM   390  C  CD   . ARG   A 1 63  ? 41.669 -37.702 -24.283 1   39.68  ? 62  ARG   A CD   1 1 
ATOM   391  N  NE   . ARG   A 1 63  ? 43.091 -37.733 -23.95  1   43.3   ? 62  ARG   A NE   1 1 
ATOM   392  C  CZ   . ARG   A 1 63  ? 43.942 -36.741 -24.171 1   45.3   ? 62  ARG   A CZ   1 1 
ATOM   393  N  NH1  . ARG   A 1 63  ? 43.521 -35.607 -24.72  1   45.47  ? 62  ARG   A NH1  1 1 
ATOM   394  N  NH2  . ARG   A 1 63  ? 45.218 -36.864 -23.821 1   44.57  ? 62  ARG   A NH2  1 1 
ATOM   395  N  N    . LEU   A 1 64  ? 40.383 -41.179 -19.598 1   33.9   ? 63  LEU   A N    1 1 
ATOM   396  C  CA   . LEU   A 1 64  ? 40.329 -41.27  -18.15  1   33.67  ? 63  LEU   A CA   1 1 
ATOM   397  C  C    . LEU   A 1 64  ? 41.649 -41.267 -17.434 1   32.87  ? 63  LEU   A C    1 1 
ATOM   398  O  O    . LEU   A 1 64  ? 42.602 -41.9   -17.852 1   32.15  ? 63  LEU   A O    1 1 
ATOM   399  C  CB   . LEU   A 1 64  ? 39.537 -42.51  -17.757 1   34.99  ? 63  LEU   A CB   1 1 
ATOM   400  C  CG   . LEU   A 1 64  ? 38.113 -42.583 -18.312 1   38.5   ? 63  LEU   A CG   1 1 
ATOM   401  C  CD1  . LEU   A 1 64  ? 37.472 -43.904 -17.973 1   39.67  ? 63  LEU   A CD1  1 1 
ATOM   402  C  CD2  . LEU   A 1 64  ? 37.266 -41.488 -17.738 1   40.06  ? 63  LEU   A CD2  1 1 
ATOM   403  N  N    . VAL   A 1 65  ? 41.676 -40.568 -16.29  1   33.06  ? 64  VAL   A N    1 1 
ATOM   404  C  CA   . VAL   A 1 65  ? 42.774 -40.551 -15.336 1   32.78  ? 64  VAL   A CA   1 1 
ATOM   405  C  C    . VAL   A 1 65  ? 42.158 -41.063 -14.026 1   32.16  ? 64  VAL   A C    1 1 
ATOM   406  O  O    . VAL   A 1 65  ? 41.24  -40.443 -13.507 1   32.52  ? 64  VAL   A O    1 1 
ATOM   407  C  CB   . VAL   A 1 65  ? 43.423 -39.177 -15.136 1   33.07  ? 64  VAL   A CB   1 1 
ATOM   408  C  CG1  . VAL   A 1 65  ? 44.653 -39.321 -14.251 1   34.15  ? 64  VAL   A CG1  1 1 
ATOM   409  C  CG2  . VAL   A 1 65  ? 43.787 -38.539 -16.463 1   32.41  ? 64  VAL   A CG2  1 1 
ATOM   410  N  N    . LEU   A 1 66  ? 42.584 -42.235 -13.551 1   30.92  ? 65  LEU   A N    1 1 
ATOM   411  C  CA   . LEU   A 1 66  ? 42.017 -42.83  -12.351 1   29.76  ? 65  LEU   A CA   1 1 
ATOM   412  C  C    . LEU   A 1 66  ? 43.027 -42.818 -11.211 1   30.07  ? 65  LEU   A C    1 1 
ATOM   413  O  O    . LEU   A 1 66  ? 44.193 -43.196 -11.396 1   30.3   ? 65  LEU   A O    1 1 
ATOM   414  C  CB   . LEU   A 1 66  ? 41.527 -44.251 -12.649 1   28.85  ? 65  LEU   A CB   1 1 
ATOM   415  C  CG   . LEU   A 1 66  ? 40.598 -44.409 -13.863 1   28.2   ? 65  LEU   A CG   1 1 
ATOM   416  C  CD1  . LEU   A 1 66  ? 40.255 -45.849 -14.065 1   27.83  ? 65  LEU   A CD1  1 1 
ATOM   417  C  CD2  . LEU   A 1 66  ? 39.329 -43.605 -13.69  1   28.28  ? 65  LEU   A CD2  1 1 
ATOM   418  N  N    . TRP   A 1 67  ? 42.57  -42.357 -10.034 1   29.76  ? 66  TRP   A N    1 1 
ATOM   419  C  CA   . TRP   A 1 67  ? 43.385 -42.24  -8.833  1   29.72  ? 66  TRP   A CA   1 1 
ATOM   420  C  C    . TRP   A 1 67  ? 42.821 -43.044 -7.685  1   29.62  ? 66  TRP   A C    1 1 
ATOM   421  O  O    . TRP   A 1 67  ? 41.611 -43.037 -7.468  1   30.49  ? 66  TRP   A O    1 1 
ATOM   422  C  CB   . TRP   A 1 67  ? 43.451 -40.772 -8.399  1   29.09  ? 66  TRP   A CB   1 1 
ATOM   423  C  CG   . TRP   A 1 67  ? 44.429 -39.921 -9.144  1   29.12  ? 66  TRP   A CG   1 1 
ATOM   424  C  CD1  . TRP   A 1 67  ? 45.008 -40.177 -10.353 1   30.38  ? 66  TRP   A CD1  1 1 
ATOM   425  C  CD2  . TRP   A 1 67  ? 44.869 -38.618 -8.756  1   29.16  ? 66  TRP   A CD2  1 1 
ATOM   426  N  NE1  . TRP   A 1 67  ? 45.829 -39.136 -10.712 1   30.73  ? 66  TRP   A NE1  1 1 
ATOM   427  C  CE2  . TRP   A 1 67  ? 45.762 -38.164 -9.743  1   29.79  ? 66  TRP   A CE2  1 1 
ATOM   428  C  CE3  . TRP   A 1 67  ? 44.599 -37.789 -7.655  1   29.36  ? 66  TRP   A CE3  1 1 
ATOM   429  C  CZ2  . TRP   A 1 67  ? 46.395 -36.927 -9.66   1   30.01  ? 66  TRP   A CZ2  1 1 
ATOM   430  C  CZ3  . TRP   A 1 67  ? 45.236 -36.57  -7.574  1   29.82  ? 66  TRP   A CZ3  1 1 
ATOM   431  C  CH2  . TRP   A 1 67  ? 46.122 -36.153 -8.567  1   30.15  ? 66  TRP   A CH2  1 1 
ATOM   432  N  N    . ASP   A 1 68  ? 43.695 -43.673 -6.907  1   28.37  ? 67  ASP   A N    1 1 
ATOM   433  C  CA   . ASP   A 1 68  ? 43.277 -44.428 -5.741  1   27.79  ? 67  ASP   A CA   1 1 
ATOM   434  C  C    . ASP   A 1 68  ? 44.49  -44.92  -4.956  1   27.87  ? 67  ASP   A C    1 1 
ATOM   435  O  O    . ASP   A 1 68  ? 45.554 -45.074 -5.524  1   27.54  ? 67  ASP   A O    1 1 
ATOM   436  C  CB   . ASP   A 1 68  ? 42.377 -45.608 -6.134  1   28.59  ? 67  ASP   A CB   1 1 
ATOM   437  C  CG   . ASP   A 1 68  ? 41.436 -46.065 -5.018  1   32.78  ? 67  ASP   A CG   1 1 
ATOM   438  O  OD1  . ASP   A 1 68  ? 41.935 -46.585 -3.979  1   33.92  ? 67  ASP   A OD1  1 1 
ATOM   439  O  OD2  . ASP   A 1 68  ? 40.212 -45.937 -5.19   1   33.15  ? 67  ASP   A OD2  1 1 
ATOM   440  N  N    . ILE   A 1 69  ? 44.342 -45.126 -3.637  1   28.03  ? 68  ILE   A N    1 1 
ATOM   441  C  CA   . ILE   A 1 69  ? 45.412 -45.695 -2.821  1   29.42  ? 68  ILE   A CA   1 1 
ATOM   442  C  C    . ILE   A 1 69  ? 45.493 -47.23  -3.021  1   30.8   ? 68  ILE   A C    1 1 
ATOM   443  O  O    . ILE   A 1 69  ? 46.522 -47.836 -2.681  1   31.71  ? 68  ILE   A O    1 1 
ATOM   444  C  CB   . ILE   A 1 69  ? 45.24  -45.372 -1.332  1   30.11  ? 68  ILE   A CB   1 1 
ATOM   445  C  CG1  . ILE   A 1 69  ? 43.823 -45.712 -0.855  1   30.23  ? 68  ILE   A CG1  1 1 
ATOM   446  C  CG2  . ILE   A 1 69  ? 45.609 -43.927 -1.05   1   31.36  ? 68  ILE   A CG2  1 1 
ATOM   447  C  CD1  . ILE   A 1 69  ? 43.651 -45.584 0.561   1   30.64  ? 68  ILE   A CD1  1 1 
ATOM   448  N  N    . ASN   A 1 70  ? 44.399 -47.85  -3.533  1   29.81  ? 69  ASN   A N    1 1 
ATOM   449  C  CA   . ASN   A 1 70  ? 44.285 -49.255 -3.851  1   30.14  ? 69  ASN   A CA   1 1 
ATOM   450  C  C    . ASN   A 1 70  ? 44.685 -49.463 -5.337  1   31.01  ? 69  ASN   A C    1 1 
ATOM   451  O  O    . ASN   A 1 70  ? 43.882 -49.265 -6.251  1   30.45  ? 69  ASN   A O    1 1 
ATOM   452  C  CB   . ASN   A 1 70  ? 42.86  -49.731 -3.569  1   30.43  ? 69  ASN   A CB   1 1 
ATOM   453  C  CG   . ASN   A 1 70  ? 42.599 -51.175 -3.928  1   33.67  ? 69  ASN   A CG   1 1 
ATOM   454  O  OD1  . ASN   A 1 70  ? 43.516 -51.987 -4.143  1   35.12  ? 69  ASN   A OD1  1 1 
ATOM   455  N  ND2  . ASN   A 1 70  ? 41.339 -51.543 -4.009  1   33.96  ? 69  ASN   A ND2  1 1 
ATOM   456  N  N    . LYS   A 1 71  ? 45.955 -49.829 -5.551  1   31.6   ? 70  LYS   A N    1 1 
ATOM   457  C  CA   . LYS   A 1 71  ? 46.552 -50.05  -6.852  1   32.21  ? 70  LYS   A CA   1 1 
ATOM   458  C  C    . LYS   A 1 71  ? 45.833 -51.152 -7.626  1   33.54  ? 70  LYS   A C    1 1 
ATOM   459  O  O    . LYS   A 1 71  ? 45.416 -50.924 -8.763  1   32.67  ? 70  LYS   A O    1 1 
ATOM   460  C  CB   . LYS   A 1 71  ? 48.048 -50.353 -6.682  1   33.48  ? 70  LYS   A CB   1 1 
ATOM   461  C  CG   . LYS   A 1 71  ? 48.813 -50.397 -7.993  1   37.93  ? 70  LYS   A CG   1 1 
ATOM   462  C  CD   . LYS   A 1 71  ? 50.311 -50.505 -7.741  1   43.46  ? 70  LYS   A CD   1 1 
ATOM   463  C  CE   . LYS   A 1 71  ? 51.14  -50.399 -9.002  1   47.55  ? 70  LYS   A CE   1 1 
ATOM   464  N  NZ   . LYS   A 1 71  ? 50.957 -51.57  -9.9    1   50.77  ? 70  LYS   A NZ   1 1 
ATOM   465  N  N    . HIS   A 1 72  ? 45.649 -52.333 -6.991  1   35.49  ? 71  HIS   A N    1 1 
ATOM   466  C  CA   . HIS   A 1 72  ? 44.976 -53.483 -7.589  1   37.56  ? 71  HIS   A CA   1 1 
ATOM   467  C  C    . HIS   A 1 72  ? 43.579 -53.143 -8.106  1   38.6   ? 71  HIS   A C    1 1 
ATOM   468  O  O    . HIS   A 1 72  ? 43.223 -53.531 -9.206  1   38.97  ? 71  HIS   A O    1 1 
ATOM   469  C  CB   . HIS   A 1 72  ? 44.879 -54.634 -6.586  1   39.86  ? 71  HIS   A CB   1 1 
ATOM   470  C  CG   . HIS   A 1 72  ? 44.094 -55.804 -7.102  1   45.07  ? 71  HIS   A CG   1 1 
ATOM   471  N  ND1  . HIS   A 1 72  ? 44.632 -56.689 -8.036  1   47.34  ? 71  HIS   A ND1  1 1 
ATOM   472  C  CD2  . HIS   A 1 72  ? 42.809 -56.151 -6.868  1   46.99  ? 71  HIS   A CD2  1 1 
ATOM   473  C  CE1  . HIS   A 1 72  ? 43.672 -57.558 -8.312  1   47.85  ? 71  HIS   A CE1  1 1 
ATOM   474  N  NE2  . HIS   A 1 72  ? 42.557 -57.276 -7.65   1   48.41  ? 71  HIS   A NE2  1 1 
ATOM   475  N  N    . GLY   A 1 73  ? 42.791 -52.466 -7.285  1   38.67  ? 72  GLY   A N    1 1 
ATOM   476  C  CA   . GLY   A 1 73  ? 41.426 -52.111 -7.628  1   38.57  ? 72  GLY   A CA   1 1 
ATOM   477  C  C    . GLY   A 1 73  ? 41.311 -51.084 -8.732  1   37.98  ? 72  GLY   A C    1 1 
ATOM   478  O  O    . GLY   A 1 73  ? 40.382 -51.16  -9.533  1   37.49  ? 72  GLY   A O    1 1 
ATOM   479  N  N    . VAL   A 1 74  ? 42.218 -50.096 -8.759  1   37.8   ? 73  VAL   A N    1 1 
ATOM   480  C  CA   . VAL   A 1 74  ? 42.135 -49.046 -9.769  1   37.71  ? 73  VAL   A CA   1 1 
ATOM   481  C  C    . VAL   A 1 74  ? 42.566 -49.624 -11.132 1   38.23  ? 73  VAL   A C    1 1 
ATOM   482  O  O    . VAL   A 1 74  ? 41.919 -49.344 -12.132 1   38.07  ? 73  VAL   A O    1 1 
ATOM   483  C  CB   . VAL   A 1 74  ? 42.829 -47.71  -9.363  1   37.24  ? 73  VAL   A CB   1 1 
ATOM   484  C  CG1  . VAL   A 1 74  ? 44.326 -47.712 -9.673  1   37.5   ? 73  VAL   A CG1  1 1 
ATOM   485  C  CG2  . VAL   A 1 74  ? 42.143 -46.527 -10.015 1   36.84  ? 73  VAL   A CG2  1 1 
ATOM   486  N  N    . GLU   A 1 75  ? 43.556 -50.533 -11.153 1   38.52  ? 74  GLU   A N    1 1 
ATOM   487  C  CA   . GLU   A 1 75  ? 43.968 -51.21  -12.382 1   38.85  ? 74  GLU   A CA   1 1 
ATOM   488  C  C    . GLU   A 1 75  ? 42.898 -52.176 -12.89  1   39.76  ? 74  GLU   A C    1 1 
ATOM   489  O  O    . GLU   A 1 75  ? 42.791 -52.398 -14.093 1   40.74  ? 74  GLU   A O    1 1 
ATOM   490  C  CB   . GLU   A 1 75  ? 45.308 -51.915 -12.175 1   40.23  ? 74  GLU   A CB   1 1 
ATOM   491  C  CG   . GLU   A 1 75  ? 46.362 -50.907 -11.76  1   44.65  ? 74  GLU   A CG   1 1 
ATOM   492  C  CD   . GLU   A 1 75  ? 47.766 -51.432 -11.569 1   51.11  ? 74  GLU   A CD   1 1 
ATOM   493  O  OE1  . GLU   A 1 75  ? 47.967 -52.667 -11.61  1   51.74  ? 74  GLU   A OE1  1 1 
ATOM   494  O  OE2  . GLU   A 1 75  ? 48.673 -50.59  -11.388 1   53.61  ? 74  GLU   A OE2  1 1 
ATOM   495  N  N    . GLU   A 1 76  ? 42.088 -52.728 -11.988 1   39.94  ? 75  GLU   A N    1 1 
ATOM   496  C  CA   . GLU   A 1 76  ? 40.966 -53.597 -12.326 1   40.8   ? 75  GLU   A CA   1 1 
ATOM   497  C  C    . GLU   A 1 76  ? 39.842 -52.745 -12.958 1   40.58  ? 75  GLU   A C    1 1 
ATOM   498  O  O    . GLU   A 1 76  ? 39.218 -53.175 -13.929 1   40.9   ? 75  GLU   A O    1 1 
ATOM   499  C  CB   . GLU   A 1 76  ? 40.475 -54.294 -11.066 1   44.54  ? 75  GLU   A CB   1 1 
ATOM   500  C  CG   . GLU   A 1 76  ? 39.554 -55.469 -11.315 1   52.84  ? 75  GLU   A CG   1 1 
ATOM   501  C  CD   . GLU   A 1 76  ? 39.076 -56.155 -10.047 1   64.19  ? 75  GLU   A CD   1 1 
ATOM   502  O  OE1  . GLU   A 1 76  ? 39.213 -55.569 -8.944  1   67.72  ? 75  GLU   A OE1  1 1 
ATOM   503  O  OE2  . GLU   A 1 76  ? 38.551 -57.285 -10.164 1   67.87  ? 75  GLU   A OE2  1 1 
ATOM   504  N  N    . THR   A 1 77  ? 39.625 -51.523 -12.444 1   39.83  ? 76  THR   A N    1 1 
ATOM   505  C  CA   . THR   A 1 77  ? 38.65  -50.601 -13.002 1   40.42  ? 76  THR   A CA   1 1 
ATOM   506  C  C    . THR   A 1 77  ? 39.107 -50.194 -14.413 1   40.5   ? 76  THR   A C    1 1 
ATOM   507  O  O    . THR   A 1 77  ? 38.305 -50.193 -15.334 1   40.72  ? 76  THR   A O    1 1 
ATOM   508  C  CB   . THR   A 1 77  ? 38.518 -49.359 -12.09  1   42.41  ? 76  THR   A CB   1 1 
ATOM   509  O  OG1  . THR   A 1 77  ? 37.878 -49.735 -10.871 1   44.24  ? 76  THR   A OG1  1 1 
ATOM   510  C  CG2  . THR   A 1 77  ? 37.748 -48.216 -12.747 1   42.6   ? 76  THR   A CG2  1 1 
ATOM   511  N  N    . ALA   A 1 78  ? 40.405 -49.876 -14.572 1   40.31  ? 77  ALA   A N    1 1 
ATOM   512  C  CA   . ALA   A 1 78  ? 41.025 -49.448 -15.822 1   40.74  ? 77  ALA   A CA   1 1 
ATOM   513  C  C    . ALA   A 1 78  ? 40.989 -50.522 -16.895 1   41.47  ? 77  ALA   A C    1 1 
ATOM   514  O  O    . ALA   A 1 78  ? 40.791 -50.195 -18.064 1   41.19  ? 77  ALA   A O    1 1 
ATOM   515  C  CB   . ALA   A 1 78  ? 42.453 -49.026 -15.577 1   40.62  ? 77  ALA   A CB   1 1 
ATOM   516  N  N    . ALA   A 1 79  ? 41.155 -51.804 -16.512 1   42.04  ? 78  ALA   A N    1 1 
ATOM   517  C  CA   . ALA   A 1 79  ? 41.089 -52.891 -17.49  1   42.66  ? 78  ALA   A CA   1 1 
ATOM   518  C  C    . ALA   A 1 79  ? 39.677 -52.991 -18.048 1   43.76  ? 78  ALA   A C    1 1 
ATOM   519  O  O    . ALA   A 1 79  ? 39.51  -53.129 -19.25  1   44.71  ? 78  ALA   A O    1 1 
ATOM   520  C  CB   . ALA   A 1 79  ? 41.495 -54.199 -16.848 1   42.68  ? 78  ALA   A CB   1 1 
ATOM   521  N  N    . GLU   A 1 80  ? 38.664 -52.834 -17.195 1   44.17  ? 79  GLU   A N    1 1 
ATOM   522  C  CA   . GLU   A 1 80  ? 37.286 -52.863 -17.612 1   44.65  ? 79  GLU   A CA   1 1 
ATOM   523  C  C    . GLU   A 1 80  ? 36.917 -51.633 -18.456 1   43.85  ? 79  GLU   A C    1 1 
ATOM   524  O  O    . GLU   A 1 80  ? 36.171 -51.775 -19.435 1   44.52  ? 79  GLU   A O    1 1 
ATOM   525  C  CB   . GLU   A 1 80  ? 36.359 -53.034 -16.404 1   48.38  ? 79  GLU   A CB   1 1 
ATOM   526  C  CG   . GLU   A 1 80  ? 34.903 -53.109 -16.801 1   55.83  ? 79  GLU   A CG   1 1 
ATOM   527  C  CD   . GLU   A 1 80  ? 34.539 -53.992 -17.97  1   64.91  ? 79  GLU   A CD   1 1 
ATOM   528  O  OE1  . GLU   A 1 80  ? 34.9   -55.189 -17.934 1   68.26  ? 79  GLU   A OE1  1 1 
ATOM   529  O  OE2  . GLU   A 1 80  ? 33.88  -53.49  -18.911 1   66.55  ? 79  GLU   A OE2  1 1 
ATOM   530  N  N    . CYS   A 1 81  ? 37.491 -50.448 -18.139 1   41.91  ? 80  CYS   A N    1 1 
ATOM   531  C  CA   . CYS   A 1 81  ? 37.266 -49.239 -18.937 1   40.91  ? 80  CYS   A CA   1 1 
ATOM   532  C  C    . CYS   A 1 81  ? 37.903 -49.413 -20.315 1   42.04  ? 80  CYS   A C    1 1 
ATOM   533  O  O    . CYS   A 1 81  ? 37.284 -49.052 -21.314 1   42.71  ? 80  CYS   A O    1 1 
ATOM   534  C  CB   . CYS   A 1 81  ? 37.81  -47.997 -18.242 1   39.77  ? 80  CYS   A CB   1 1 
ATOM   535  S  SG   . CYS   A 1 81  ? 36.797 -47.401 -16.872 1   38.49  ? 80  CYS   A SG   1 1 
ATOM   536  N  N    . ARG   A 1 82  ? 39.101 -50.015 -20.385 1   41.81  ? 81  ARG   A N    1 1 
ATOM   537  C  CA   . ARG   A 1 82  ? 39.735 -50.275 -21.665 1   41.91  ? 81  ARG   A CA   1 1 
ATOM   538  C  C    . ARG   A 1 82  ? 38.917 -51.269 -22.488 1   43.81  ? 81  ARG   A C    1 1 
ATOM   539  O  O    . ARG   A 1 82  ? 38.781 -51.07  -23.685 1   44.24  ? 81  ARG   A O    1 1 
ATOM   540  C  CB   . ARG   A 1 82  ? 41.17  -50.73  -21.475 1   41.43  ? 81  ARG   A CB   1 1 
ATOM   541  C  CG   . ARG   A 1 82  ? 42.032 -49.636 -20.902 1   40.69  ? 81  ARG   A CG   1 1 
ATOM   542  C  CD   . ARG   A 1 82  ? 43.482 -50.031 -20.874 1   41.19  ? 81  ARG   A CD   1 1 
ATOM   543  N  NE   . ARG   A 1 82  ? 44.237 -49.059 -20.106 1   43.08  ? 81  ARG   A NE   1 1 
ATOM   544  C  CZ   . ARG   A 1 82  ? 44.708 -49.273 -18.884 1   45.79  ? 81  ARG   A CZ   1 1 
ATOM   545  N  NH1  . ARG   A 1 82  ? 44.578 -50.462 -18.312 1   43.51  ? 81  ARG   A NH1  1 1 
ATOM   546  N  NH2  . ARG   A 1 82  ? 45.34  -48.31  -18.237 1   47.92  ? 81  ARG   A NH2  1 1 
ATOM   547  N  N    . LYS   A 1 83  ? 38.308 -52.294 -21.859 1   45.2   ? 82  LYS   A N    1 1 
ATOM   548  C  CA   . LYS   A 1 83  ? 37.434 -53.228 -22.595 1   46.46  ? 82  LYS   A CA   1 1 
ATOM   549  C  C    . LYS   A 1 83  ? 36.218 -52.475 -23.212 1   46.05  ? 82  LYS   A C    1 1 
ATOM   550  O  O    . LYS   A 1 83  ? 35.702 -52.891 -24.249 1   46.06  ? 82  LYS   A O    1 1 
ATOM   551  C  CB   . LYS   A 1 83  ? 36.955 -54.369 -21.691 1   50.13  ? 82  LYS   A CB   1 1 
ATOM   552  C  CG   . LYS   A 1 83  ? 38.05  -55.357 -21.34  1   57.67  ? 82  LYS   A CG   1 1 
ATOM   553  C  CD   . LYS   A 1 83  ? 37.628 -56.31  -20.216 1   64.1   ? 82  LYS   A CD   1 1 
ATOM   554  C  CE   . LYS   A 1 83  ? 36.341 -57.077 -20.495 1   68.83  ? 82  LYS   A CE   1 1 
ATOM   555  N  NZ   . LYS   A 1 83  ? 35.802 -57.698 -19.242 1   71.6   ? 82  LYS   A NZ   1 1 
ATOM   556  N  N    . LEU   A 1 84  ? 35.79  -51.356 -22.572 1   45.08  ? 83  LEU   A N    1 1 
ATOM   557  C  CA   . LEU   A 1 84  ? 34.717 -50.485 -23.033 1   44.46  ? 83  LEU   A CA   1 1 
ATOM   558  C  C    . LEU   A 1 84  ? 35.136 -49.532 -24.181 1   45.1   ? 83  LEU   A C    1 1 
ATOM   559  O  O    . LEU   A 1 84  ? 34.294 -48.765 -24.645 1   45.59  ? 83  LEU   A O    1 1 
ATOM   560  C  CB   . LEU   A 1 84  ? 34.164 -49.67  -21.867 1   43.46  ? 83  LEU   A CB   1 1 
ATOM   561  C  CG   . LEU   A 1 84  ? 33.388 -50.462 -20.834 1   43.47  ? 83  LEU   A CG   1 1 
ATOM   562  C  CD1  . LEU   A 1 84  ? 33.102 -49.612 -19.597 1   43.73  ? 83  LEU   A CD1  1 1 
ATOM   563  C  CD2  . LEU   A 1 84  ? 32.114 -51.031 -21.427 1   43.07  ? 83  LEU   A CD2  1 1 
ATOM   564  N  N    . GLY   A 1 85  ? 36.41  -49.57  -24.596 1   44.6   ? 84  GLY   A N    1 1 
ATOM   565  C  CA   . GLY   A 1 85  ? 36.962 -48.77  -25.684 1   44.31  ? 84  GLY   A CA   1 1 
ATOM   566  C  C    . GLY   A 1 85  ? 37.709 -47.505 -25.285 1   44.12  ? 84  GLY   A C    1 1 
ATOM   567  O  O    . GLY   A 1 85  ? 38.24  -46.805 -26.158 1   45.12  ? 84  GLY   A O    1 1 
ATOM   568  N  N    . ALA   A 1 86  ? 37.788 -47.197 -23.973 1   42.27  ? 85  ALA   A N    1 1 
ATOM   569  C  CA   . ALA   A 1 86  ? 38.437 -45.966 -23.505 1   41.21  ? 85  ALA   A CA   1 1 
ATOM   570  C  C    . ALA   A 1 86  ? 39.966 -46.013 -23.314 1   40.59  ? 85  ALA   A C    1 1 
ATOM   571  O  O    . ALA   A 1 86  ? 40.53  -47.061 -23.008 1   40.28  ? 85  ALA   A O    1 1 
ATOM   572  C  CB   . ALA   A 1 86  ? 37.789 -45.507 -22.202 1   40.72  ? 85  ALA   A CB   1 1 
ATOM   573  N  N    . THR   A 1 87  ? 40.63  -44.84  -23.434 1   40.17  ? 86  THR   A N    1 1 
ATOM   574  C  CA   . THR   A 1 87  ? 42.048 -44.699 -23.09  1   39.77  ? 86  THR   A CA   1 1 
ATOM   575  C  C    . THR   A 1 87  ? 42.097 -44.324 -21.569 1   39.8   ? 86  THR   A C    1 1 
ATOM   576  O  O    . THR   A 1 87  ? 41.378 -43.416 -21.119 1   39.76  ? 86  THR   A O    1 1 
ATOM   577  C  CB   . THR   A 1 87  ? 42.728 -43.652 -23.952 1   39.75  ? 86  THR   A CB   1 1 
ATOM   578  O  OG1  . THR   A 1 87  ? 42.73  -44.122 -25.3   1   40.67  ? 86  THR   A OG1  1 1 
ATOM   579  C  CG2  . THR   A 1 87  ? 44.163 -43.38  -23.488 1   39.46  ? 86  THR   A CG2  1 1 
ATOM   580  N  N    . VAL   A 1 88  ? 42.899 -45.058 -20.775 1   39.23  ? 87  VAL   A N    1 1 
ATOM   581  C  CA   . VAL   A 1 88  ? 42.955 -44.85  -19.322 1   39.03  ? 87  VAL   A CA   1 1 
ATOM   582  C  C    . VAL   A 1 88  ? 44.392 -44.81  -18.766 1   39.38  ? 87  VAL   A C    1 1 
ATOM   583  O  O    . VAL   A 1 88  ? 45.205 -45.67  -19.099 1   40.36  ? 87  VAL   A O    1 1 
ATOM   584  C  CB   . VAL   A 1 88  ? 42.181 -46     -18.62  1   38.97  ? 87  VAL   A CB   1 1 
ATOM   585  C  CG1  . VAL   A 1 88  ? 42.12  -45.777 -17.131 1   39.57  ? 87  VAL   A CG1  1 1 
ATOM   586  C  CG2  . VAL   A 1 88  ? 40.782 -46.176 -19.186 1   39.24  ? 87  VAL   A CG2  1 1 
ATOM   587  N  N    . HIS   A 1 89  ? 44.691 -43.859 -17.88  1   38.52  ? 88  HIS   A N    1 1 
ATOM   588  C  CA   . HIS   A 1 89  ? 45.972 -43.807 -17.169 1   37.94  ? 88  HIS   A CA   1 1 
ATOM   589  C  C    . HIS   A 1 89  ? 45.635 -43.932 -15.67  1   36.93  ? 88  HIS   A C    1 1 
ATOM   590  O  O    . HIS   A 1 89  ? 44.729 -43.251 -15.204 1   36.77  ? 88  HIS   A O    1 1 
ATOM   591  C  CB   . HIS   A 1 89  ? 46.715 -42.478 -17.408 1   39.18  ? 88  HIS   A CB   1 1 
ATOM   592  C  CG   . HIS   A 1 89  ? 47.497 -42.399 -18.687 1   43.83  ? 88  HIS   A CG   1 1 
ATOM   593  N  ND1  . HIS   A 1 89  ? 46.892 -42.037 -19.897 1   45.4   ? 88  HIS   A ND1  1 1 
ATOM   594  C  CD2  . HIS   A 1 89  ? 48.823 -42.594 -18.909 1   45.5   ? 88  HIS   A CD2  1 1 
ATOM   595  C  CE1  . HIS   A 1 89  ? 47.859 -42.044 -20.801 1   45.61  ? 88  HIS   A CE1  1 1 
ATOM   596  N  NE2  . HIS   A 1 89  ? 49.039 -42.373 -20.262 1   45.89  ? 88  HIS   A NE2  1 1 
ATOM   597  N  N    . THR   A 1 90  ? 46.329 -44.802 -14.929 1   36.42  ? 89  THR   A N    1 1 
ATOM   598  C  CA   . THR   A 1 90  ? 46.099 -44.93  -13.493 1   37.23  ? 89  THR   A CA   1 1 
ATOM   599  C  C    . THR   A 1 90  ? 47.292 -44.449 -12.702 1   36.35  ? 89  THR   A C    1 1 
ATOM   600  O  O    . THR   A 1 90  ? 48.433 -44.58  -13.148 1   37.31  ? 89  THR   A O    1 1 
ATOM   601  C  CB   . THR   A 1 90  ? 45.7   -46.335 -13.061 1   39.38  ? 89  THR   A CB   1 1 
ATOM   602  O  OG1  . THR   A 1 90  ? 46.853 -47.191 -13.045 1   40.88  ? 89  THR   A OG1  1 1 
ATOM   603  C  CG2  . THR   A 1 90  ? 44.579 -46.887 -13.89  1   39.93  ? 89  THR   A CG2  1 1 
ATOM   604  N  N    . PHE   A 1 91  ? 47.017 -43.904 -11.527 1   33.97  ? 90  PHE   A N    1 1 
ATOM   605  C  CA   . PHE   A 1 91  ? 48.036 -43.401 -10.635 1   32.19  ? 90  PHE   A CA   1 1 
ATOM   606  C  C    . PHE   A 1 91  ? 47.657 -43.813 -9.212  1   31.16  ? 90  PHE   A C    1 1 
ATOM   607  O  O    . PHE   A 1 91  ? 46.475 -43.769 -8.849  1   31.33  ? 90  PHE   A O    1 1 
ATOM   608  C  CB   . PHE   A 1 91  ? 48.141 -41.858 -10.761 1   31.84  ? 90  PHE   A CB   1 1 
ATOM   609  C  CG   . PHE   A 1 91  ? 48.596 -41.36  -12.116 1   32.25  ? 90  PHE   A CG   1 1 
ATOM   610  C  CD1  . PHE   A 1 91  ? 49.94  -41.214 -12.404 1   32.87  ? 90  PHE   A CD1  1 1 
ATOM   611  C  CD2  . PHE   A 1 91  ? 47.682 -41.087 -13.114 1   32.92  ? 90  PHE   A CD2  1 1 
ATOM   612  C  CE1  . PHE   A 1 91  ? 50.36  -40.817 -13.669 1   33.17  ? 90  PHE   A CE1  1 1 
ATOM   613  C  CE2  . PHE   A 1 91  ? 48.105 -40.689 -14.376 1   33.38  ? 90  PHE   A CE2  1 1 
ATOM   614  C  CZ   . PHE   A 1 91  ? 49.44  -40.546 -14.642 1   32.92  ? 90  PHE   A CZ   1 1 
ATOM   615  N  N    . VAL   A 1 92  ? 48.647 -44.251 -8.408  1   29.85  ? 91  VAL   A N    1 1 
ATOM   616  C  CA   . VAL   A 1 92  ? 48.376 -44.571 -7.016  1   28.97  ? 91  VAL   A CA   1 1 
ATOM   617  C  C    . VAL   A 1 92  ? 48.583 -43.279 -6.277  1   29.66  ? 91  VAL   A C    1 1 
ATOM   618  O  O    . VAL   A 1 92  ? 49.722 -42.834 -6.162  1   30.28  ? 91  VAL   A O    1 1 
ATOM   619  C  CB   . VAL   A 1 92  ? 49.253 -45.677 -6.407  1   27.75  ? 91  VAL   A CB   1 1 
ATOM   620  C  CG1  . VAL   A 1 92  ? 48.838 -45.932 -4.969  1   27.58  ? 91  VAL   A CG1  1 1 
ATOM   621  C  CG2  . VAL   A 1 92  ? 49.145 -46.942 -7.213  1   27.42  ? 91  VAL   A CG2  1 1 
ATOM   622  N  N    . VAL   A 1 93  ? 47.501 -42.631 -5.827  1   28.9   ? 92  VAL   A N    1 1 
ATOM   623  C  CA   . VAL   A 1 93  ? 47.618 -41.339 -5.158  1   28.03  ? 92  VAL   A CA   1 1 
ATOM   624  C  C    . VAL   A 1 93  ? 46.792 -41.322 -3.889  1   27.89  ? 92  VAL   A C    1 1 
ATOM   625  O  O    . VAL   A 1 93  ? 45.624 -41.698 -3.924  1   28.45  ? 92  VAL   A O    1 1 
ATOM   626  C  CB   . VAL   A 1 93  ? 47.178 -40.167 -6.096  1   28.03  ? 92  VAL   A CB   1 1 
ATOM   627  C  CG1  . VAL   A 1 93  ? 47.576 -38.81  -5.528  1   28.12  ? 92  VAL   A CG1  1 1 
ATOM   628  C  CG2  . VAL   A 1 93  ? 47.701 -40.332 -7.534  1   27.84  ? 92  VAL   A CG2  1 1 
ATOM   629  N  N    . ASP   A 1 94  ? 47.382 -40.851 -2.778  1   27.08  ? 93  ASP   A N    1 1 
ATOM   630  C  CA   . ASP   A 1 94  ? 46.692 -40.641 -1.511  1   26.44  ? 93  ASP   A CA   1 1 
ATOM   631  C  C    . ASP   A 1 94  ? 46.042 -39.275 -1.66   1   26.84  ? 93  ASP   A C    1 1 
ATOM   632  O  O    . ASP   A 1 94  ? 46.728 -38.252 -1.602  1   27.11  ? 93  ASP   A O    1 1 
ATOM   633  C  CB   . ASP   A 1 94  ? 47.688 -40.623 -0.358  1   26.73  ? 93  ASP   A CB   1 1 
ATOM   634  C  CG   . ASP   A 1 94  ? 47.107 -40.432 1.03    1   28.97  ? 93  ASP   A CG   1 1 
ATOM   635  O  OD1  . ASP   A 1 94  ? 45.884 -40.159 1.141   1   27.32  ? 93  ASP   A OD1  1 1 
ATOM   636  O  OD2  . ASP   A 1 94  ? 47.871 -40.555 2.005   1   32.56  ? 93  ASP   A OD2  1 1 
ATOM   637  N  N    . CYS   A 1 95  ? 44.715 -39.269 -1.862  1   26.54  ? 94  CYS   A N    1 1 
ATOM   638  C  CA   . CYS   A 1 95  ? 43.93  -38.074 -2.083  1   26.98  ? 94  CYS   A CA   1 1 
ATOM   639  C  C    . CYS   A 1 95  ? 43.569 -37.288 -0.801  1   27.96  ? 94  CYS   A C    1 1 
ATOM   640  O  O    . CYS   A 1 95  ? 42.712 -36.402 -0.839  1   29.06  ? 94  CYS   A O    1 1 
ATOM   641  C  CB   . CYS   A 1 95  ? 42.701 -38.413 -2.911  1   28.04  ? 94  CYS   A CB   1 1 
ATOM   642  S  SG   . CYS   A 1 95  ? 43.107 -39.151 -4.518  1   31.57  ? 94  CYS   A SG   1 1 
ATOM   643  N  N    . GLY   A 1 96  ? 44.256 -37.59  0.283   1   26.84  ? 95  GLY   A N    1 1 
ATOM   644  C  CA   . GLY   A 1 96  ? 44.197 -36.874 1.537   1   27.39  ? 95  GLY   A CA   1 1 
ATOM   645  C  C    . GLY   A 1 96  ? 45.544 -36.242 1.863   1   28.01  ? 95  GLY   A C    1 1 
ATOM   646  O  O    . GLY   A 1 96  ? 45.643 -35.492 2.837   1   28.62  ? 95  GLY   A O    1 1 
ATOM   647  N  N    . ASN   A 1 97  ? 46.595 -36.507 1.034   1   27.98  ? 96  ASN   A N    1 1 
ATOM   648  C  CA   . ASN   A 1 97  ? 47.973 -36.027 1.17    1   28.05  ? 96  ASN   A CA   1 1 
ATOM   649  C  C    . ASN   A 1 97  ? 48.285 -34.955 0.13    1   29.38  ? 96  ASN   A C    1 1 
ATOM   650  O  O    . ASN   A 1 97  ? 48.446 -35.27  -1.049  1   30.12  ? 96  ASN   A O    1 1 
ATOM   651  C  CB   . ASN   A 1 97  ? 48.934 -37.193 0.984   1   27.76  ? 96  ASN   A CB   1 1 
ATOM   652  C  CG   . ASN   A 1 97  ? 50.353 -36.871 1.346   1   29.66  ? 96  ASN   A CG   1 1 
ATOM   653  O  OD1  . ASN   A 1 97  ? 51.07  -36.182 0.645   1   30.7   ? 96  ASN   A OD1  1 1 
ATOM   654  N  ND2  . ASN   A 1 97  ? 50.803 -37.37  2.455   1   32.24  ? 96  ASN   A ND2  1 1 
ATOM   655  N  N    . ARG   A 1 98  ? 48.415 -33.704 0.573   1   29.58  ? 97  ARG   A N    1 1 
ATOM   656  C  CA   . ARG   A 1 98  ? 48.701 -32.545 -0.249  1   30.99  ? 97  ARG   A CA   1 1 
ATOM   657  C  C    . ARG   A 1 98  ? 49.951 -32.704 -1.146  1   32.65  ? 97  ARG   A C    1 1 
ATOM   658  O  O    . ARG   A 1 98  ? 49.893 -32.407 -2.336  1   32.56  ? 97  ARG   A O    1 1 
ATOM   659  C  CB   . ARG   A 1 98  ? 48.833 -31.321 0.657   1   32.55  ? 97  ARG   A CB   1 1 
ATOM   660  C  CG   . ARG   A 1 98  ? 48.777 -30.003 -0.095  1   37.36  ? 97  ARG   A CG   1 1 
ATOM   661  C  CD   . ARG   A 1 98  ? 48.959 -28.82  0.824   1   42.14  ? 97  ARG   A CD   1 1 
ATOM   662  N  NE   . ARG   A 1 98  ? 50.281 -28.85  1.442   1   47.98  ? 97  ARG   A NE   1 1 
ATOM   663  C  CZ   . ARG   A 1 98  ? 51.344 -28.187 0.994   1   52.43  ? 97  ARG   A CZ   1 1 
ATOM   664  N  NH1  . ARG   A 1 98  ? 51.244 -27.395 -0.069  1   51.51  ? 97  ARG   A NH1  1 1 
ATOM   665  N  NH2  . ARG   A 1 98  ? 52.515 -28.305 1.61    1   53.95  ? 97  ARG   A NH2  1 1 
ATOM   666  N  N    . GLU   A 1 99  ? 51.071 -33.172 -0.581  1   33.76  ? 98  GLU   A N    1 1 
ATOM   667  C  CA   . GLU   A 1 99  ? 52.318 -33.33  -1.315  1   35.2   ? 98  GLU   A CA   1 1 
ATOM   668  C  C    . GLU   A 1 99  ? 52.184 -34.38  -2.418  1   35.62  ? 98  GLU   A C    1 1 
ATOM   669  O  O    . GLU   A 1 99  ? 52.599 -34.142 -3.549  1   35.68  ? 98  GLU   A O    1 1 
ATOM   670  C  CB   . GLU   A 1 99  ? 53.454 -33.683 -0.355  1   39.68  ? 98  GLU   A CB   1 1 
ATOM   671  C  CG   . GLU   A 1 99  ? 54.815 -33.741 -1.03   1   49.12  ? 98  GLU   A CG   1 1 
ATOM   672  C  CD   . GLU   A 1 99  ? 55.998 -34.006 -0.109  1   60.03  ? 98  GLU   A CD   1 1 
ATOM   673  O  OE1  . GLU   A 1 99  ? 55.779 -34.163 1.116   1   62.04  ? 98  GLU   A OE1  1 1 
ATOM   674  O  OE2  . GLU   A 1 99  ? 57.144 -34.057 -0.618  1   63.56  ? 98  GLU   A OE2  1 1 
ATOM   675  N  N    . ASP   A 1 100 ? 51.563 -35.523 -2.098  1   35.42  ? 99  ASP   A N    1 1 
ATOM   676  C  CA   . ASP   A 1 100 ? 51.324 -36.606 -3.049  1   34.99  ? 99  ASP   A CA   1 1 
ATOM   677  C  C    . ASP   A 1 100 ? 50.429 -36.107 -4.191  1   34.53  ? 99  ASP   A C    1 1 
ATOM   678  O  O    . ASP   A 1 100 ? 50.735 -36.377 -5.352  1   35.88  ? 99  ASP   A O    1 1 
ATOM   679  C  CB   . ASP   A 1 100 ? 50.674 -37.81  -2.334  1   36.65  ? 99  ASP   A CB   1 1 
ATOM   680  C  CG   . ASP   A 1 100 ? 50.722 -39.124 -3.099  1   41.32  ? 99  ASP   A CG   1 1 
ATOM   681  O  OD1  . ASP   A 1 100 ? 51.162 -39.119 -4.258  1   41.87  ? 99  ASP   A OD1  1 1 
ATOM   682  O  OD2  . ASP   A 1 100 ? 50.327 -40.166 -2.524  1   44.56  ? 99  ASP   A OD2  1 1 
ATOM   683  N  N    . ILE   A 1 101 ? 49.352 -35.361 -3.879  1   33.08  ? 100 ILE   A N    1 1 
ATOM   684  C  CA   . ILE   A 1 101 ? 48.44  -34.82  -4.89   1   32.33  ? 100 ILE   A CA   1 1 
ATOM   685  C  C    . ILE   A 1 101 ? 49.176 -33.87  -5.874  1   33.26  ? 100 ILE   A C    1 1 
ATOM   686  O  O    . ILE   A 1 101 ? 49.07  -34.057 -7.089  1   34.07  ? 100 ILE   A O    1 1 
ATOM   687  C  CB   . ILE   A 1 101 ? 47.227 -34.151 -4.211  1   31.37  ? 100 ILE   A CB   1 1 
ATOM   688  C  CG1  . ILE   A 1 101 ? 46.294 -35.193 -3.558  1   31.15  ? 100 ILE   A CG1  1 1 
ATOM   689  C  CG2  . ILE   A 1 101 ? 46.472 -33.233 -5.165  1   31.49  ? 100 ILE   A CG2  1 1 
ATOM   690  C  CD1  . ILE   A 1 101 ? 45.3   -34.586 -2.591  1   31.9   ? 100 ILE   A CD1  1 1 
ATOM   691  N  N    . TYR   A 1 102 ? 49.959 -32.909 -5.363  1   32.83  ? 101 TYR   A N    1 1 
ATOM   692  C  CA   . TYR   A 1 102 ? 50.692 -31.988 -6.222  1   33.04  ? 101 TYR   A CA   1 1 
ATOM   693  C  C    . TYR   A 1 102 ? 51.715 -32.686 -7.115  1   34.87  ? 101 TYR   A C    1 1 
ATOM   694  O  O    . TYR   A 1 102 ? 51.801 -32.378 -8.319  1   34.39  ? 101 TYR   A O    1 1 
ATOM   695  C  CB   . TYR   A 1 102 ? 51.328 -30.857 -5.414  1   32.15  ? 101 TYR   A CB   1 1 
ATOM   696  C  CG   . TYR   A 1 102 ? 50.319 -29.91  -4.793  1   31.94  ? 101 TYR   A CG   1 1 
ATOM   697  C  CD1  . TYR   A 1 102 ? 49.099 -29.655 -5.409  1   32.02  ? 101 TYR   A CD1  1 1 
ATOM   698  C  CD2  . TYR   A 1 102 ? 50.605 -29.237 -3.613  1   32.32  ? 101 TYR   A CD2  1 1 
ATOM   699  C  CE1  . TYR   A 1 102 ? 48.17  -28.797 -4.841  1   32.71  ? 101 TYR   A CE1  1 1 
ATOM   700  C  CE2  . TYR   A 1 102 ? 49.695 -28.353 -3.051  1   33.07  ? 101 TYR   A CE2  1 1 
ATOM   701  C  CZ   . TYR   A 1 102 ? 48.472 -28.144 -3.661  1   33.71  ? 101 TYR   A CZ   1 1 
ATOM   702  O  OH   . TYR   A 1 102 ? 47.582 -27.242 -3.15   1   34.6   ? 101 TYR   A OH   1 1 
ATOM   703  N  N    . ASN   A 1 103 ? 52.47  -33.639 -6.549  1   35.77  ? 102 ASN   A N    1 1 
ATOM   704  C  CA   . ASN   A 1 103 ? 53.457 -34.399 -7.32   1   36.89  ? 102 ASN   A CA   1 1 
ATOM   705  C  C    . ASN   A 1 103 ? 52.771 -35.219 -8.403  1   36.72  ? 102 ASN   A C    1 1 
ATOM   706  O  O    . ASN   A 1 103 ? 53.321 -35.354 -9.484  1   36.64  ? 102 ASN   A O    1 1 
ATOM   707  C  CB   . ASN   A 1 103 ? 54.235 -35.335 -6.413  1   39.8   ? 102 ASN   A CB   1 1 
ATOM   708  C  CG   . ASN   A 1 103 ? 55.423 -34.677 -5.8    1   47.2   ? 102 ASN   A CG   1 1 
ATOM   709  O  OD1  . ASN   A 1 103 ? 56.239 -34.063 -6.5    1   50.83  ? 102 ASN   A OD1  1 1 
ATOM   710  N  ND2  . ASN   A 1 103 ? 55.556 -34.783 -4.481  1   48.12  ? 102 ASN   A ND2  1 1 
ATOM   711  N  N    . SER   A 1 104 ? 51.579 -35.782 -8.11   1   36.75  ? 103 SER   A N    1 1 
ATOM   712  C  CA   . SER   A 1 104 ? 50.822 -36.574 -9.074  1   36.8   ? 103 SER   A CA   1 1 
ATOM   713  C  C    . SER   A 1 104 ? 50.194 -35.718 -10.161 1   37.16  ? 103 SER   A C    1 1 
ATOM   714  O  O    . SER   A 1 104 ? 50.084 -36.176 -11.294 1   37.67  ? 103 SER   A O    1 1 
ATOM   715  C  CB   . SER   A 1 104 ? 49.782 -37.437 -8.382  1   37.82  ? 103 SER   A CB   1 1 
ATOM   716  O  OG   . SER   A 1 104 ? 50.455 -38.41  -7.599  1   40.63  ? 103 SER   A OG   1 1 
ATOM   717  N  N    . VAL   A 1 105 ? 49.83  -34.468 -9.852  1   37.16  ? 104 VAL   A N    1 1 
ATOM   718  C  CA   . VAL   A 1 105 ? 49.302 -33.554 -10.864 1   37.48  ? 104 VAL   A CA   1 1 
ATOM   719  C  C    . VAL   A 1 105 ? 50.396 -33.243 -11.887 1   38.58  ? 104 VAL   A C    1 1 
ATOM   720  O  O    . VAL   A 1 105 ? 50.108 -33.259 -13.082 1   39.04  ? 104 VAL   A O    1 1 
ATOM   721  C  CB   . VAL   A 1 105 ? 48.61  -32.293 -10.271 1   37.3   ? 104 VAL   A CB   1 1 
ATOM   722  C  CG1  . VAL   A 1 105 ? 48.367 -31.239 -11.342 1   37.47  ? 104 VAL   A CG1  1 1 
ATOM   723  C  CG2  . VAL   A 1 105 ? 47.296 -32.667 -9.597  1   37.29  ? 104 VAL   A CG2  1 1 
ATOM   724  N  N    . LYS   A 1 106 ? 51.667 -33.103 -11.44  1   38.99  ? 105 LYS   A N    1 1 
ATOM   725  C  CA   . LYS   A 1 106 ? 52.819 -32.896 -12.322 1   40.02  ? 105 LYS   A CA   1 1 
ATOM   726  C  C    . LYS   A 1 106 ? 52.959 -34.089 -13.303 1   40.87  ? 105 LYS   A C    1 1 
ATOM   727  O  O    . LYS   A 1 106 ? 53.237 -33.893 -14.484 1   41.02  ? 105 LYS   A O    1 1 
ATOM   728  C  CB   . LYS   A 1 106 ? 54.113 -32.756 -11.501 1   42.35  ? 105 LYS   A CB   1 1 
ATOM   729  C  CG   . LYS   A 1 106 ? 54.553 -31.321 -11.273 1   49.83  ? 105 LYS   A CG   1 1 
ATOM   730  C  CD   . LYS   A 1 106 ? 55.328 -31.124 -9.951  1   57.32  ? 105 LYS   A CD   1 1 
ATOM   731  C  CE   . LYS   A 1 106 ? 56.765 -31.628 -9.965  1   62.92  ? 105 LYS   A CE   1 1 
ATOM   732  N  NZ   . LYS   A 1 106 ? 57.371 -31.585 -8.591  1   66.18  ? 105 LYS   A NZ   1 1 
ATOM   733  N  N    . GLN   A 1 107 ? 52.768 -35.313 -12.793 1   40.89  ? 106 GLN   A N    1 1 
ATOM   734  C  CA   . GLN   A 1 107 ? 52.826 -36.548 -13.55  1   41.39  ? 106 GLN   A CA   1 1 
ATOM   735  C  C    . GLN   A 1 107 ? 51.697 -36.587 -14.588 1   41.43  ? 106 GLN   A C    1 1 
ATOM   736  O  O    . GLN   A 1 107 ? 51.976 -36.901 -15.74  1   42.83  ? 106 GLN   A O    1 1 
ATOM   737  C  CB   . GLN   A 1 107 ? 52.691 -37.726 -12.59  1   43.89  ? 106 GLN   A CB   1 1 
ATOM   738  C  CG   . GLN   A 1 107 ? 53.768 -38.781 -12.719 1   49.31  ? 106 GLN   A CG   1 1 
ATOM   739  C  CD   . GLN   A 1 107 ? 53.573 -39.883 -11.691 1   53.89  ? 106 GLN   A CD   1 1 
ATOM   740  O  OE1  . GLN   A 1 107 ? 53.576 -41.081 -12.019 1   54.81  ? 106 GLN   A OE1  1 1 
ATOM   741  N  NE2  . GLN   A 1 107 ? 53.4   -39.499 -10.42  1   54.38  ? 106 GLN   A NE2  1 1 
ATOM   742  N  N    . VAL   A 1 108 ? 50.443 -36.251 -14.203 1   40.06  ? 107 VAL   A N    1 1 
ATOM   743  C  CA   . VAL   A 1 108 ? 49.298 -36.239 -15.112 1   39.48  ? 107 VAL   A CA   1 1 
ATOM   744  C  C    . VAL   A 1 108 ? 49.496 -35.241 -16.248 1   41.01  ? 107 VAL   A C    1 1 
ATOM   745  O  O    . VAL   A 1 108 ? 49.216 -35.564 -17.4   1   41.65  ? 107 VAL   A O    1 1 
ATOM   746  C  CB   . VAL   A 1 108 ? 47.952 -36.036 -14.378 1   38.6   ? 107 VAL   A CB   1 1 
ATOM   747  C  CG1  . VAL   A 1 108 ? 46.791 -35.86  -15.356 1   37.92  ? 107 VAL   A CG1  1 1 
ATOM   748  C  CG2  . VAL   A 1 108 ? 47.676 -37.188 -13.421 1   38.71  ? 107 VAL   A CG2  1 1 
ATOM   749  N  N    . LYS   A 1 109 ? 50.028 -34.047 -15.954 1   41.33  ? 108 LYS   A N    1 1 
ATOM   750  C  CA   . LYS   A 1 109 ? 50.279 -33.046 -16.996 1   41.85  ? 108 LYS   A CA   1 1 
ATOM   751  C  C    . LYS   A 1 109 ? 51.326 -33.556 -17.991 1   43.3   ? 108 LYS   A C    1 1 
ATOM   752  O  O    . LYS   A 1 109 ? 51.199 -33.349 -19.189 1   43.85  ? 108 LYS   A O    1 1 
ATOM   753  C  CB   . LYS   A 1 109 ? 50.784 -31.746 -16.36  1   42.37  ? 108 LYS   A CB   1 1 
ATOM   754  C  CG   . LYS   A 1 109 ? 49.758 -30.982 -15.551 1   44.24  ? 108 LYS   A CG   1 1 
ATOM   755  C  CD   . LYS   A 1 109 ? 50.374 -29.677 -15.14  1   47.11  ? 108 LYS   A CD   1 1 
ATOM   756  C  CE   . LYS   A 1 109 ? 49.526 -28.869 -14.207 1   51.09  ? 108 LYS   A CE   1 1 
ATOM   757  N  NZ   . LYS   A 1 109 ? 50.27  -28.582 -12.938 1   55.14  ? 108 LYS   A NZ   1 1 
ATOM   758  N  N    . LYS   A 1 110 ? 52.373 -34.209 -17.487 1   44.06  ? 109 LYS   A N    1 1 
ATOM   759  C  CA   . LYS   A 1 110 ? 53.478 -34.722 -18.288 1   45     ? 109 LYS   A CA   1 1 
ATOM   760  C  C    . LYS   A 1 110 ? 53.112 -35.968 -19.105 1   45.39  ? 109 LYS   A C    1 1 
ATOM   761  O  O    . LYS   A 1 110 ? 53.695 -36.189 -20.158 1   46.35  ? 109 LYS   A O    1 1 
ATOM   762  C  CB   . LYS   A 1 110 ? 54.657 -35.056 -17.359 1   47.3   ? 109 LYS   A CB   1 1 
ATOM   763  C  CG   . LYS   A 1 110 ? 55.983 -35.181 -18.068 1   52.92  ? 109 LYS   A CG   1 1 
ATOM   764  C  CD   . LYS   A 1 110 ? 56.872 -36.274 -17.488 1   59.11  ? 109 LYS   A CD   1 1 
ATOM   765  C  CE   . LYS   A 1 110 ? 58.01  -36.585 -18.43  1   64.67  ? 109 LYS   A CE   1 1 
ATOM   766  N  NZ   . LYS   A 1 110 ? 57.545 -36.826 -19.846 1   68.25  ? 109 LYS   A NZ   1 1 
ATOM   767  N  N    . GLU   A 1 111 ? 52.174 -36.778 -18.629 1   44.7   ? 110 GLU   A N    1 1 
ATOM   768  C  CA   . GLU   A 1 111 ? 51.824 -38.023 -19.295 1   44.94  ? 110 GLU   A CA   1 1 
ATOM   769  C  C    . GLU   A 1 111 ? 50.506 -38.008 -20.043 1   43.17  ? 110 GLU   A C    1 1 
ATOM   770  O  O    . GLU   A 1 111 ? 50.325 -38.81  -20.948 1   43.06  ? 110 GLU   A O    1 1 
ATOM   771  C  CB   . GLU   A 1 111 ? 51.744 -39.144 -18.262 1   50.48  ? 110 GLU   A CB   1 1 
ATOM   772  C  CG   . GLU   A 1 111 ? 53.074 -39.553 -17.68  1   61.76  ? 110 GLU   A CG   1 1 
ATOM   773  C  CD   . GLU   A 1 111 ? 52.943 -40.774 -16.792 1   76.44  ? 110 GLU   A CD   1 1 
ATOM   774  O  OE1  . GLU   A 1 111 ? 52.102 -41.647 -17.114 1   79     ? 110 GLU   A OE1  1 1 
ATOM   775  O  OE2  . GLU   A 1 111 ? 53.672 -40.857 -15.773 1   82.03  ? 110 GLU   A OE2  1 1 
ATOM   776  N  N    . VAL   A 1 112 ? 49.541 -37.218 -19.589 1   41.51  ? 111 VAL   A N    1 1 
ATOM   777  C  CA   . VAL   A 1 112 ? 48.204 -37.218 -20.167 1   39.96  ? 111 VAL   A CA   1 1 
ATOM   778  C  C    . VAL   A 1 112 ? 47.828 -35.854 -20.766 1   38.6   ? 111 VAL   A C    1 1 
ATOM   779  O  O    . VAL   A 1 112 ? 47.46  -35.77  -21.939 1   38.54  ? 111 VAL   A O    1 1 
ATOM   780  C  CB   . VAL   A 1 112 ? 47.163 -37.728 -19.125 1   39.64  ? 111 VAL   A CB   1 1 
ATOM   781  C  CG1  . VAL   A 1 112 ? 45.767 -37.798 -19.722 1   40.08  ? 111 VAL   A CG1  1 1 
ATOM   782  C  CG2  . VAL   A 1 112 ? 47.57  -39.074 -18.554 1   39.48  ? 111 VAL   A CG2  1 1 
ATOM   783  N  N    . GLY   A 1 113 ? 47.923 -34.81  -19.954 1   37.35  ? 112 GLY   A N    1 1 
ATOM   784  C  CA   . GLY   A 1 113 ? 47.578 -33.459 -20.359 1   36.55  ? 112 GLY   A CA   1 1 
ATOM   785  C  C    . GLY   A 1 113 ? 46.83  -32.729 -19.269 1   36.04  ? 112 GLY   A C    1 1 
ATOM   786  O  O    . GLY   A 1 113 ? 46.959 -33.05  -18.081 1   36.16  ? 112 GLY   A O    1 1 
ATOM   787  N  N    . ASP   A 1 114 ? 46.015 -31.762 -19.672 1   34.86  ? 113 ASP   A N    1 1 
ATOM   788  C  CA   . ASP   A 1 114 ? 45.233 -30.968 -18.747 1   34.52  ? 113 ASP   A CA   1 1 
ATOM   789  C  C    . ASP   A 1 114 ? 43.868 -31.561 -18.446 1   32.56  ? 113 ASP   A C    1 1 
ATOM   790  O  O    . ASP   A 1 114 ? 43.044 -31.634 -19.356 1   33.28  ? 113 ASP   A O    1 1 
ATOM   791  C  CB   . ASP   A 1 114 ? 45.066 -29.568 -19.308 1   37.64  ? 113 ASP   A CB   1 1 
ATOM   792  C  CG   . ASP   A 1 114 ? 46.366 -28.795 -19.304 1   45.85  ? 113 ASP   A CG   1 1 
ATOM   793  O  OD1  . ASP   A 1 114 ? 47.095 -28.86  -18.277 1   48.34  ? 113 ASP   A OD1  1 1 
ATOM   794  O  OD2  . ASP   A 1 114 ? 46.635 -28.084 -20.297 1   48.92  ? 113 ASP   A OD2  1 1 
ATOM   795  N  N    . VAL   A 1 115 ? 43.604 -31.935 -17.169 1   29.37  ? 114 VAL   A N    1 1 
ATOM   796  C  CA   . VAL   A 1 115 ? 42.307 -32.472 -16.771 1   27.35  ? 114 VAL   A CA   1 1 
ATOM   797  C  C    . VAL   A 1 115 ? 41.196 -31.451 -17.049 1   27.88  ? 114 VAL   A C    1 1 
ATOM   798  O  O    . VAL   A 1 115 ? 41.365 -30.261 -16.761 1   29.13  ? 114 VAL   A O    1 1 
ATOM   799  C  CB   . VAL   A 1 115 ? 42.303 -32.89  -15.27  1   25.54  ? 114 VAL   A CB   1 1 
ATOM   800  C  CG1  . VAL   A 1 115 ? 40.9   -33.283 -14.794 1   24.4   ? 114 VAL   A CG1  1 1 
ATOM   801  C  CG2  . VAL   A 1 115 ? 43.293 -34.013 -15.02  1   25.52  ? 114 VAL   A CG2  1 1 
ATOM   802  N  N    . THR   A 1 116 ? 40.077 -31.899 -17.598 1   26.76  ? 115 THR   A N    1 1 
ATOM   803  C  CA   . THR   A 1 116 ? 38.954 -31.026 -17.898 1   26.85  ? 115 THR   A CA   1 1 
ATOM   804  C  C    . THR   A 1 116 ? 37.795 -31.272 -16.956 1   26.14  ? 115 THR   A C    1 1 
ATOM   805  O  O    . THR   A 1 116 ? 37.048 -30.347 -16.666 1   27.07  ? 115 THR   A O    1 1 
ATOM   806  C  CB   . THR   A 1 116 ? 38.503 -31.243 -19.333 1   28.93  ? 115 THR   A CB   1 1 
ATOM   807  O  OG1  . THR   A 1 116 ? 39.614 -31.08  -20.192 1   29.01  ? 115 THR   A OG1  1 1 
ATOM   808  C  CG2  . THR   A 1 116 ? 37.441 -30.25  -19.722 1   31.82  ? 115 THR   A CG2  1 1 
ATOM   809  N  N    . ILE   A 1 117 ? 37.586 -32.533 -16.531 1   24.59  ? 116 ILE   A N    1 1 
ATOM   810  C  CA   . ILE   A 1 117 ? 36.51  -32.856 -15.585 1   23.06  ? 116 ILE   A CA   1 1 
ATOM   811  C  C    . ILE   A 1 117 ? 37.119 -33.526 -14.382 1   22.86  ? 116 ILE   A C    1 1 
ATOM   812  O  O    . ILE   A 1 117 ? 37.766 -34.55  -14.534 1   22.91  ? 116 ILE   A O    1 1 
ATOM   813  C  CB   . ILE   A 1 117 ? 35.397 -33.742 -16.209 1   21.66  ? 116 ILE   A CB   1 1 
ATOM   814  C  CG1  . ILE   A 1 117 ? 34.722 -33.026 -17.393 1   20.5   ? 116 ILE   A CG1  1 1 
ATOM   815  C  CG2  . ILE   A 1 117 ? 34.38  -34.184 -15.135 1   20.92  ? 116 ILE   A CG2  1 1 
ATOM   816  C  CD1  . ILE   A 1 117 ? 33.76  -33.839 -18.123 1   20.56  ? 116 ILE   A CD1  1 1 
ATOM   817  N  N    . LEU   A 1 118 ? 36.932 -32.947 -13.194 1   22.7   ? 117 LEU   A N    1 1 
ATOM   818  C  CA   . LEU   A 1 118 ? 37.449 -33.5   -11.962 1   23.66  ? 117 LEU   A CA   1 1 
ATOM   819  C  C    . LEU   A 1 118 ? 36.293 -34.051 -11.137 1   24.57  ? 117 LEU   A C    1 1 
ATOM   820  O  O    . LEU   A 1 118 ? 35.355 -33.326 -10.835 1   25.42  ? 117 LEU   A O    1 1 
ATOM   821  C  CB   . LEU   A 1 118 ? 38.199 -32.443 -11.152 1   24.01  ? 117 LEU   A CB   1 1 
ATOM   822  C  CG   . LEU   A 1 118 ? 38.61  -32.836 -9.713  1   25.37  ? 117 LEU   A CG   1 1 
ATOM   823  C  CD1  . LEU   A 1 118 ? 39.493 -34.072 -9.702  1   25.3   ? 117 LEU   A CD1  1 1 
ATOM   824  C  CD2  . LEU   A 1 118 ? 39.295 -31.677 -9.02   1   26.02  ? 117 LEU   A CD2  1 1 
ATOM   825  N  N    . VAL   A 1 119 ? 36.374 -35.326 -10.767 1   23.57  ? 118 VAL   A N    1 1 
ATOM   826  C  CA   . VAL   A 1 119 ? 35.375 -35.949 -9.926  1   23.25  ? 118 VAL   A CA   1 1 
ATOM   827  C  C    . VAL   A 1 119 ? 36.03  -36.299 -8.61   1   23.11  ? 118 VAL   A C    1 1 
ATOM   828  O  O    . VAL   A 1 119 ? 36.816 -37.251 -8.554  1   22.9   ? 118 VAL   A O    1 1 
ATOM   829  C  CB   . VAL   A 1 119 ? 34.754 -37.197 -10.568 1   22.9   ? 118 VAL   A CB   1 1 
ATOM   830  C  CG1  . VAL   A 1 119 ? 33.636 -37.739 -9.665  1   22.75  ? 118 VAL   A CG1  1 1 
ATOM   831  C  CG2  . VAL   A 1 119 ? 34.257 -36.894 -11.994 1   22.21  ? 118 VAL   A CG2  1 1 
ATOM   832  N  N    . ASN   A 1 120 ? 35.778 -35.471 -7.583  1   23.08  ? 119 ASN   A N    1 1 
ATOM   833  C  CA   . ASN   A 1 120 ? 36.293 -35.628 -6.207  1   23.42  ? 119 ASN   A CA   1 1 
ATOM   834  C  C    . ASN   A 1 120 ? 35.448 -36.654 -5.439  1   23.89  ? 119 ASN   A C    1 1 
ATOM   835  O  O    . ASN   A 1 120 ? 34.597 -36.28  -4.639  1   23.95  ? 119 ASN   A O    1 1 
ATOM   836  C  CB   . ASN   A 1 120 ? 36.3   -34.289 -5.484  1   23.13  ? 119 ASN   A CB   1 1 
ATOM   837  C  CG   . ASN   A 1 120 ? 37.5   -33.442 -5.835  1   26.41  ? 119 ASN   A CG   1 1 
ATOM   838  O  OD1  . ASN   A 1 120 ? 37.381 -32.234 -6.105  1   28.76  ? 119 ASN   A OD1  1 1 
ATOM   839  N  ND2  . ASN   A 1 120 ? 38.689 -34.038 -5.83   1   26.1   ? 119 ASN   A ND2  1 1 
ATOM   840  N  N    . ASN   A 1 121 ? 35.669 -37.94  -5.715  1   23.76  ? 120 ASN   A N    1 1 
ATOM   841  C  CA   . ASN   A 1 121 ? 34.87  -39.003 -5.155  1   24.63  ? 120 ASN   A CA   1 1 
ATOM   842  C  C    . ASN   A 1 121 ? 35.483 -39.696 -3.94   1   26.13  ? 120 ASN   A C    1 1 
ATOM   843  O  O    . ASN   A 1 121 ? 34.723 -40.148 -3.097  1   27.37  ? 120 ASN   A O    1 1 
ATOM   844  C  CB   . ASN   A 1 121 ? 34.548 -40.013 -6.251  1   25.89  ? 120 ASN   A CB   1 1 
ATOM   845  C  CG   . ASN   A 1 121 ? 33.82  -41.241 -5.781  1   28.64  ? 120 ASN   A CG   1 1 
ATOM   846  O  OD1  . ASN   A 1 121 ? 32.61  -41.212 -5.526  1   30.38  ? 120 ASN   A OD1  1 1 
ATOM   847  N  ND2  . ASN   A 1 121 ? 34.558 -42.325 -5.61   1   28.16  ? 120 ASN   A ND2  1 1 
ATOM   848  N  N    . ALA   A 1 122 ? 36.822 -39.791 -3.816  1   26.02  ? 121 ALA   A N    1 1 
ATOM   849  C  CA   . ALA   A 1 122 ? 37.464 -40.469 -2.69   1   26.16  ? 121 ALA   A CA   1 1 
ATOM   850  C  C    . ALA   A 1 122 ? 36.917 -40.032 -1.331  1   27.72  ? 121 ALA   A C    1 1 
ATOM   851  O  O    . ALA   A 1 122 ? 36.703 -38.844 -1.091  1   28.46  ? 121 ALA   A O    1 1 
ATOM   852  C  CB   . ALA   A 1 122 ? 38.97  -40.281 -2.74   1   26.14  ? 121 ALA   A CB   1 1 
ATOM   853  N  N    . GLY   A 1 123 ? 36.599 -41.013 -0.503  1   27.36  ? 122 GLY   A N    1 1 
ATOM   854  C  CA   . GLY   A 1 123 ? 36.046 -40.773 0.804   1   27.3   ? 122 GLY   A CA   1 1 
ATOM   855  C  C    . GLY   A 1 123 ? 36.413 -41.859 1.788   1   27.9   ? 122 GLY   A C    1 1 
ATOM   856  O  O    . GLY   A 1 123 ? 36.78  -42.971 1.402   1   28.19  ? 122 GLY   A O    1 1 
ATOM   857  N  N    . THR   A 1 124 ? 36.304 -41.518 3.076   1   27.46  ? 123 THR   A N    1 1 
ATOM   858  C  CA   . THR   A 1 124 ? 36.604 -42.375 4.208   1   27.83  ? 123 THR   A CA   1 1 
ATOM   859  C  C    . THR   A 1 124 ? 35.607 -42.092 5.337   1   28.25  ? 123 THR   A C    1 1 
ATOM   860  O  O    . THR   A 1 124 ? 35.041 -40.991 5.422   1   27.62  ? 123 THR   A O    1 1 
ATOM   861  C  CB   . THR   A 1 124 ? 38.061 -42.184 4.657   1   28.5   ? 123 THR   A CB   1 1 
ATOM   862  O  OG1  . THR   A 1 124 ? 38.468 -43.276 5.481   1   30.76  ? 123 THR   A OG1  1 1 
ATOM   863  C  CG2  . THR   A 1 124 ? 38.268 -40.897 5.397   1   27.57  ? 123 THR   A CG2  1 1 
ATOM   864  N  N    . VAL   A 1 125 ? 35.368 -43.115 6.183   1   28.78  ? 124 VAL   A N    1 1 
ATOM   865  C  CA   . VAL   A 1 125 ? 34.439 -43.043 7.304   1   29.26  ? 124 VAL   A CA   1 1 
ATOM   866  C  C    . VAL   A 1 125 ? 34.886 -44.014 8.394   1   31.34  ? 124 VAL   A C    1 1 
ATOM   867  O  O    . VAL   A 1 125 ? 35.413 -45.077 8.088   1   32.51  ? 124 VAL   A O    1 1 
ATOM   868  C  CB   . VAL   A 1 125 ? 32.982 -43.32  6.839   1   29.1   ? 124 VAL   A CB   1 1 
ATOM   869  C  CG1  . VAL   A 1 125 ? 32.83  -44.726 6.289   1   29.85  ? 124 VAL   A CG1  1 1 
ATOM   870  C  CG2  . VAL   A 1 125 ? 31.979 -43.067 7.957   1   29.19  ? 124 VAL   A CG2  1 1 
ATOM   871  N  N    . TYR   A 1 126 ? 34.709 -43.645 9.673   1   31.53  ? 125 TYR   A N    1 1 
ATOM   872  C  CA   . TYR   A 1 126 ? 35.018 -44.514 10.802  1   32.64  ? 125 TYR   A CA   1 1 
ATOM   873  C  C    . TYR   A 1 126 ? 33.833 -44.397 11.755  1   33.96  ? 125 TYR   A C    1 1 
ATOM   874  O  O    . TYR   A 1 126 ? 33.881 -43.629 12.719  1   34.68  ? 125 TYR   A O    1 1 
ATOM   875  C  CB   . TYR   A 1 126 ? 36.342 -44.114 11.5    1   32.47  ? 125 TYR   A CB   1 1 
ATOM   876  C  CG   . TYR   A 1 126 ? 37.524 -44.144 10.555  1   33.31  ? 125 TYR   A CG   1 1 
ATOM   877  C  CD1  . TYR   A 1 126 ? 38.187 -45.335 10.278  1   33.96  ? 125 TYR   A CD1  1 1 
ATOM   878  C  CD2  . TYR   A 1 126 ? 37.901 -43.005 9.839   1   33.6   ? 125 TYR   A CD2  1 1 
ATOM   879  C  CE1  . TYR   A 1 126 ? 39.205 -45.388 9.331   1   34.58  ? 125 TYR   A CE1  1 1 
ATOM   880  C  CE2  . TYR   A 1 126 ? 38.953 -43.04  8.934   1   34.11  ? 125 TYR   A CE2  1 1 
ATOM   881  C  CZ   . TYR   A 1 126 ? 39.609 -44.234 8.697   1   35.02  ? 125 TYR   A CZ   1 1 
ATOM   882  O  OH   . TYR   A 1 126 ? 40.675 -44.301 7.864   1   38.03  ? 125 TYR   A OH   1 1 
ATOM   883  N  N    . PRO   A 1 127 ? 32.738 -45.13  11.478  1   34.17  ? 126 PRO   A N    1 1 
ATOM   884  C  CA   . PRO   A 1 127 ? 31.541 -45.007 12.313  1   34.57  ? 126 PRO   A CA   1 1 
ATOM   885  C  C    . PRO   A 1 127 ? 31.816 -45.292 13.78   1   36.02  ? 126 PRO   A C    1 1 
ATOM   886  O  O    . PRO   A 1 127 ? 32.539 -46.243 14.063  1   37.09  ? 126 PRO   A O    1 1 
ATOM   887  C  CB   . PRO   A 1 127 ? 30.603 -46.053 11.715  1   34.66  ? 126 PRO   A CB   1 1 
ATOM   888  C  CG   . PRO   A 1 127 ? 31.027 -46.17  10.294  1   34.86  ? 126 PRO   A CG   1 1 
ATOM   889  C  CD   . PRO   A 1 127 ? 32.518 -46.074 10.365  1   33.53  ? 126 PRO   A CD   1 1 
ATOM   890  N  N    . ALA   A 1 128 ? 31.329 -44.424 14.687  1   35.4   ? 127 ALA   A N    1 1 
ATOM   891  C  CA   . ALA   A 1 128 ? 31.463 -44.51  16.161  1   35.16  ? 127 ALA   A CA   1 1 
ATOM   892  C  C    . ALA   A 1 128 ? 30.796 -43.286 16.796  1   36.62  ? 127 ALA   A C    1 1 
ATOM   893  O  O    . ALA   A 1 128 ? 30.741 -42.213 16.165  1   37.41  ? 127 ALA   A O    1 1 
ATOM   894  C  CB   . ALA   A 1 128 ? 32.934 -44.539 16.574  1   34.14  ? 127 ALA   A CB   1 1 
ATOM   895  N  N    . ASP   A 1 129 ? 30.35  -43.405 18.05   1   37.22  ? 128 ASP   A N    1 1 
ATOM   896  C  CA   . ASP   A 1 129 ? 29.823 -42.233 18.744  1   38.25  ? 128 ASP   A CA   1 1 
ATOM   897  C  C    . ASP   A 1 129 ? 31.032 -41.317 19.087  1   38.51  ? 128 ASP   A C    1 1 
ATOM   898  O  O    . ASP   A 1 129 ? 32.165 -41.811 19.121  1   39.67  ? 128 ASP   A O    1 1 
ATOM   899  C  CB   . ASP   A 1 129 ? 28.962 -42.619 19.938  1   41.12  ? 128 ASP   A CB   1 1 
ATOM   900  C  CG   . ASP   A 1 129 ? 29.732 -43.083 21.136  1   47.14  ? 128 ASP   A CG   1 1 
ATOM   901  O  OD1  . ASP   A 1 129 ? 30.244 -44.215 21.102  1   48.51  ? 128 ASP   A OD1  1 1 
ATOM   902  O  OD2  . ASP   A 1 129 ? 29.811 -42.318 22.117  1   50.6   ? 128 ASP   A OD2  1 1 
ATOM   903  N  N    . LEU   A 1 130 ? 30.819 -39.994 19.239  1   37.1   ? 129 LEU   A N    1 1 
ATOM   904  C  CA   . LEU   A 1 130 ? 31.89  -39.013 19.422  1   36.86  ? 129 LEU   A CA   1 1 
ATOM   905  C  C    . LEU   A 1 130 ? 32.989 -39.413 20.414  1   37.2   ? 129 LEU   A C    1 1 
ATOM   906  O  O    . LEU   A 1 130 ? 34.173 -39.291 20.098  1   36.79  ? 129 LEU   A O    1 1 
ATOM   907  C  CB   . LEU   A 1 130 ? 31.316 -37.64  19.796  1   36.91  ? 129 LEU   A CB   1 1 
ATOM   908  C  CG   . LEU   A 1 130 ? 32.276 -36.469 19.652  1   38.1   ? 129 LEU   A CG   1 1 
ATOM   909  C  CD1  . LEU   A 1 130 ? 32.675 -36.266 18.219  1   37.71  ? 129 LEU   A CD1  1 1 
ATOM   910  C  CD2  . LEU   A 1 130 ? 31.695 -35.215 20.24   1   39.24  ? 129 LEU   A CD2  1 1 
ATOM   911  N  N    . LEU   A 1 131 ? 32.609 -39.916 21.594  1   37.79  ? 130 LEU   A N    1 1 
ATOM   912  C  CA   . LEU   A 1 131 ? 33.583 -40.274 22.615  1   38.27  ? 130 LEU   A CA   1 1 
ATOM   913  C  C    . LEU   A 1 131 ? 34.344 -41.58  22.327  1   39.01  ? 130 LEU   A C    1 1 
ATOM   914  O  O    . LEU   A 1 131 ? 35.369 -41.827 22.972  1   39.9   ? 130 LEU   A O    1 1 
ATOM   915  C  CB   . LEU   A 1 131 ? 32.92  -40.289 23.976  1   38.39  ? 130 LEU   A CB   1 1 
ATOM   916  C  CG   . LEU   A 1 131 ? 32.866 -38.932 24.71   1   39.93  ? 130 LEU   A CG   1 1 
ATOM   917  C  CD1  . LEU   A 1 131 ? 32.344 -37.78  23.864  1   40.43  ? 130 LEU   A CD1  1 1 
ATOM   918  C  CD2  . LEU   A 1 131 ? 32.09  -39.055 26.002  1   40.45  ? 130 LEU   A CD2  1 1 
ATOM   919  N  N    . SER   A 1 132 ? 33.878 -42.386 21.347  1   38.07  ? 131 SER   A N    1 1 
ATOM   920  C  CA   . SER   A 1 132 ? 34.559 -43.616 20.942  1   38.66  ? 131 SER   A CA   1 1 
ATOM   921  C  C    . SER   A 1 132 ? 35.424 -43.425 19.687  1   39.57  ? 131 SER   A C    1 1 
ATOM   922  O  O    . SER   A 1 132 ? 35.944 -44.417 19.179  1   41.28  ? 131 SER   A O    1 1 
ATOM   923  C  CB   . SER   A 1 132 ? 33.554 -44.715 20.624  1   40.02  ? 131 SER   A CB   1 1 
ATOM   924  O  OG   . SER   A 1 132 ? 32.907 -45.198 21.784  1   42.47  ? 131 SER   A OG   1 1 
ATOM   925  N  N    . THR   A 1 133 ? 35.537 -42.205 19.15   1   37.83  ? 132 THR   A N    1 1 
ATOM   926  C  CA   . THR   A 1 133 ? 36.338 -41.956 17.964  1   37.21  ? 132 THR   A CA   1 1 
ATOM   927  C  C    . THR   A 1 133 ? 37.823 -41.8   18.294  1   37.42  ? 132 THR   A C    1 1 
ATOM   928  O  O    . THR   A 1 133 ? 38.183 -41.426 19.415  1   36.54  ? 132 THR   A O    1 1 
ATOM   929  C  CB   . THR   A 1 133 ? 35.828 -40.702 17.243  1   37.5   ? 132 THR   A CB   1 1 
ATOM   930  O  OG1  . THR   A 1 133 ? 35.813 -39.628 18.169  1   38.87  ? 132 THR   A OG1  1 1 
ATOM   931  C  CG2  . THR   A 1 133 ? 34.442 -40.877 16.679  1   37.06  ? 132 THR   A CG2  1 1 
ATOM   932  N  N    . LYS   A 1 134 ? 38.698 -42.088 17.308  1   37.99  ? 133 LYS   A N    1 1 
ATOM   933  C  CA   . LYS   A 1 134 ? 40.136 -41.865 17.479  1   38.75  ? 133 LYS   A CA   1 1 
ATOM   934  C  C    . LYS   A 1 134 ? 40.416 -40.523 16.799  1   38.38  ? 133 LYS   A C    1 1 
ATOM   935  O  O    . LYS   A 1 134 ? 39.894 -40.286 15.703  1   39.19  ? 133 LYS   A O    1 1 
ATOM   936  C  CB   . LYS   A 1 134 ? 40.945 -43.01  16.841  1   41.85  ? 133 LYS   A CB   1 1 
ATOM   937  C  CG   . LYS   A 1 134 ? 40.7   -44.334 17.56   1   50.76  ? 133 LYS   A CG   1 1 
ATOM   938  C  CD   . LYS   A 1 134 ? 41.026 -45.567 16.734  1   58.31  ? 133 LYS   A CD   1 1 
ATOM   939  C  CE   . LYS   A 1 134 ? 40.207 -46.757 17.211  1   63.95  ? 133 LYS   A CE   1 1 
ATOM   940  N  NZ   . LYS   A 1 134 ? 38.845 -46.78  16.575  1   67.46  ? 133 LYS   A NZ   1 1 
ATOM   941  N  N    . ASP   A 1 135 ? 41.169 -39.622 17.444  1   37.07  ? 134 ASP   A N    1 1 
ATOM   942  C  CA   . ASP   A 1 135 ? 41.42  -38.296 16.869  1   36.97  ? 134 ASP   A CA   1 1 
ATOM   943  C  C    . ASP   A 1 135 ? 42.058 -38.364 15.443  1   37.21  ? 134 ASP   A C    1 1 
ATOM   944  O  O    . ASP   A 1 135 ? 41.771 -37.508 14.593  1   36.99  ? 134 ASP   A O    1 1 
ATOM   945  C  CB   . ASP   A 1 135 ? 42.26  -37.454 17.823  1   38.39  ? 134 ASP   A CB   1 1 
ATOM   946  C  CG   . ASP   A 1 135 ? 41.573 -37.106 19.135  1   42.22  ? 134 ASP   A CG   1 1 
ATOM   947  O  OD1  . ASP   A 1 135 ? 40.326 -37.129 19.179  1   42.5   ? 134 ASP   A OD1  1 1 
ATOM   948  O  OD2  . ASP   A 1 135 ? 42.28  -36.794 20.103  1   43.88  ? 134 ASP   A OD2  1 1 
ATOM   949  N  N    . GLU   A 1 136 ? 42.869 -39.429 15.181  1   36.93  ? 135 GLU   A N    1 1 
ATOM   950  C  CA   . GLU   A 1 136 ? 43.537 -39.711 13.898  1   36.72  ? 135 GLU   A CA   1 1 
ATOM   951  C  C    . GLU   A 1 136 ? 42.51  -40.018 12.824  1   35.7   ? 135 GLU   A C    1 1 
ATOM   952  O  O    . GLU   A 1 136 ? 42.708 -39.65  11.672  1   36.3   ? 135 GLU   A O    1 1 
ATOM   953  C  CB   . GLU   A 1 136 ? 44.533 -40.879 14.036  1   40.27  ? 135 GLU   A CB   1 1 
ATOM   954  C  CG   . GLU   A 1 136 ? 45.474 -40.759 15.231  1   51.11  ? 135 GLU   A CG   1 1 
ATOM   955  C  CD   . GLU   A 1 136 ? 44.926 -41.128 16.613  1   62.97  ? 135 GLU   A CD   1 1 
ATOM   956  O  OE1  . GLU   A 1 136 ? 44.298 -42.207 16.747  1   67.39  ? 135 GLU   A OE1  1 1 
ATOM   957  O  OE2  . GLU   A 1 136 ? 45.146 -40.347 17.568  1   63.84  ? 135 GLU   A OE2  1 1 
ATOM   958  N  N    . GLU   A 1 137 ? 41.414 -40.693 13.191  1   34.58  ? 136 GLU   A N    1 1 
ATOM   959  C  CA   . GLU   A 1 137 ? 40.321 -41.02  12.283  1   33.55  ? 136 GLU   A CA   1 1 
ATOM   960  C  C    . GLU   A 1 137 ? 39.551 -39.764 11.921  1   31.71  ? 136 GLU   A C    1 1 
ATOM   961  O  O    . GLU   A 1 137 ? 39.143 -39.618 10.769  1   31.79  ? 136 GLU   A O    1 1 
ATOM   962  C  CB   . GLU   A 1 137 ? 39.41  -42.046 12.916  1   38.3   ? 136 GLU   A CB   1 1 
ATOM   963  C  CG   . GLU   A 1 137 ? 40.056 -43.413 13.052  1   45.6   ? 136 GLU   A CG   1 1 
ATOM   964  C  CD   . GLU   A 1 137 ? 39.237 -44.389 13.875  1   56.53  ? 136 GLU   A CD   1 1 
ATOM   965  O  OE1  . GLU   A 1 137 ? 38.487 -43.931 14.773  1   61.74  ? 136 GLU   A OE1  1 1 
ATOM   966  O  OE2  . GLU   A 1 137 ? 39.358 -45.612 13.629  1   57.5   ? 136 GLU   A OE2  1 1 
ATOM   967  N  N    . ILE   A 1 138 ? 39.371 -38.835 12.881  1   30.56  ? 137 ILE   A N    1 1 
ATOM   968  C  CA   . ILE   A 1 138 ? 38.707 -37.55  12.627  1   29.71  ? 137 ILE   A CA   1 1 
ATOM   969  C  C    . ILE   A 1 138 ? 39.533 -36.729 11.642  1   29.95  ? 137 ILE   A C    1 1 
ATOM   970  O  O    . ILE   A 1 138 ? 38.998 -36.192 10.683  1   31.3   ? 137 ILE   A O    1 1 
ATOM   971  C  CB   . ILE   A 1 138 ? 38.486 -36.805 13.947  1   28.53  ? 137 ILE   A CB   1 1 
ATOM   972  C  CG1  . ILE   A 1 138 ? 37.535 -37.59  14.84   1   28.56  ? 137 ILE   A CG1  1 1 
ATOM   973  C  CG2  . ILE   A 1 138 ? 37.962 -35.41  13.691  1   29.06  ? 137 ILE   A CG2  1 1 
ATOM   974  C  CD1  . ILE   A 1 138 ? 37.393 -37.024 16.322  1   28.85  ? 137 ILE   A CD1  1 1 
ATOM   975  N  N    . THR   A 1 139 ? 40.847 -36.688 11.853  1   29.46  ? 138 THR   A N    1 1 
ATOM   976  C  CA   . THR   A 1 139 ? 41.802 -36.002 10.991  1   29.27  ? 138 THR   A CA   1 1 
ATOM   977  C  C    . THR   A 1 139 ? 41.792 -36.589 9.577   1   28.89  ? 138 THR   A C    1 1 
ATOM   978  O  O    . THR   A 1 139 ? 41.654 -35.84  8.608   1   29.18  ? 138 THR   A O    1 1 
ATOM   979  C  CB   . THR   A 1 139 ? 43.185 -36.069 11.647  1   30.82  ? 138 THR   A CB   1 1 
ATOM   980  O  OG1  . THR   A 1 139 ? 43.193 -35.187 12.759  1   31.51  ? 138 THR   A OG1  1 1 
ATOM   981  C  CG2  . THR   A 1 139 ? 44.3   -35.679 10.687  1   32.23  ? 138 THR   A CG2  1 1 
ATOM   982  N  N    . LYS   A 1 140 ? 41.887 -37.92  9.453   1   28.72  ? 139 LYS   A N    1 1 
ATOM   983  C  CA   . LYS   A 1 140 ? 41.852 -38.583 8.151   1   29.6   ? 139 LYS   A CA   1 1 
ATOM   984  C  C    . LYS   A 1 140 ? 40.53  -38.325 7.425   1   29.34  ? 139 LYS   A C    1 1 
ATOM   985  O  O    . LYS   A 1 140 ? 40.529 -38.1   6.223   1   30.78  ? 139 LYS   A O    1 1 
ATOM   986  C  CB   . LYS   A 1 140 ? 42.081 -40.085 8.327   1   33.48  ? 139 LYS   A CB   1 1 
ATOM   987  C  CG   . LYS   A 1 140 ? 43.512 -40.504 8.03    1   40.5   ? 139 LYS   A CG   1 1 
ATOM   988  C  CD   . LYS   A 1 140 ? 43.948 -41.732 8.846   1   45.64  ? 139 LYS   A CD   1 1 
ATOM   989  C  CE   . LYS   A 1 140 ? 43.734 -43.065 8.168   1   50.87  ? 139 LYS   A CE   1 1 
ATOM   990  N  NZ   . LYS   A 1 140 ? 43.788 -44.214 9.132   1   52.72  ? 139 LYS   A NZ   1 1 
ATOM   991  N  N    . THR   A 1 141 ? 39.405 -38.295 8.144   1   28.25  ? 140 THR   A N    1 1 
ATOM   992  C  CA   . THR   A 1 141 ? 38.1   -38.016 7.555   1   27.88  ? 140 THR   A CA   1 1 
ATOM   993  C  C    . THR   A 1 141 ? 38.101 -36.644 6.894   1   28.62  ? 140 THR   A C    1 1 
ATOM   994  O  O    . THR   A 1 141 ? 37.747 -36.541 5.739   1   28.91  ? 140 THR   A O    1 1 
ATOM   995  C  CB   . THR   A 1 141 ? 37.007 -38.131 8.605   1   28.66  ? 140 THR   A CB   1 1 
ATOM   996  O  OG1  . THR   A 1 141 ? 37.095 -39.418 9.229   1   30.58  ? 140 THR   A OG1  1 1 
ATOM   997  C  CG2  . THR   A 1 141 ? 35.624 -37.901 8.034   1   28.21  ? 140 THR   A CG2  1 1 
ATOM   998  N  N    . PHE   A 1 142 ? 38.613 -35.61  7.585   1   28.48  ? 141 PHE   A N    1 1 
ATOM   999  C  CA   . PHE   A 1 142 ? 38.693 -34.273 7.01    1   27.39  ? 141 PHE   A CA   1 1 
ATOM   1000 C  C    . PHE   A 1 142 ? 39.691 -34.167 5.865   1   27.39  ? 141 PHE   A C    1 1 
ATOM   1001 O  O    . PHE   A 1 142 ? 39.403 -33.543 4.836   1   28.04  ? 141 PHE   A O    1 1 
ATOM   1002 C  CB   . PHE   A 1 142 ? 38.975 -33.23  8.099   1   26.58  ? 141 PHE   A CB   1 1 
ATOM   1003 C  CG   . PHE   A 1 142 ? 37.671 -32.806 8.722   1   26.69  ? 141 PHE   A CG   1 1 
ATOM   1004 C  CD1  . PHE   A 1 142 ? 37.102 -33.546 9.744   1   27.5   ? 141 PHE   A CD1  1 1 
ATOM   1005 C  CD2  . PHE   A 1 142 ? 36.945 -31.757 8.195   1   27.07  ? 141 PHE   A CD2  1 1 
ATOM   1006 C  CE1  . PHE   A 1 142 ? 35.856 -33.204 10.265  1   27.89  ? 141 PHE   A CE1  1 1 
ATOM   1007 C  CE2  . PHE   A 1 142 ? 35.705 -31.422 8.708   1   27.79  ? 141 PHE   A CE2  1 1 
ATOM   1008 C  CZ   . PHE   A 1 142 ? 35.174 -32.135 9.753   1   27.83  ? 141 PHE   A CZ   1 1 
ATOM   1009 N  N    . GLU   A 1 143 ? 40.871 -34.753 6.043   1   26.44  ? 142 GLU   A N    1 1 
ATOM   1010 C  CA   . GLU   A 1 143 ? 41.925 -34.721 5.048   1   25.96  ? 142 GLU   A CA   1 1 
ATOM   1011 C  C    . GLU   A 1 143 ? 41.491 -35.297 3.719   1   25.98  ? 142 GLU   A C    1 1 
ATOM   1012 O  O    . GLU   A 1 143 ? 41.766 -34.692 2.688   1   27.31  ? 142 GLU   A O    1 1 
ATOM   1013 C  CB   . GLU   A 1 143 ? 43.165 -35.447 5.562   1   26.29  ? 142 GLU   A CB   1 1 
ATOM   1014 C  CG   . GLU   A 1 143 ? 43.975 -34.601 6.501   1   28.78  ? 142 GLU   A CG   1 1 
ATOM   1015 C  CD   . GLU   A 1 143 ? 45.101 -35.336 7.193   1   36.54  ? 142 GLU   A CD   1 1 
ATOM   1016 O  OE1  . GLU   A 1 143 ? 45.111 -36.592 7.175   1   37.89  ? 142 GLU   A OE1  1 1 
ATOM   1017 O  OE2  . GLU   A 1 143 ? 45.963 -34.646 7.784   1   39.41  ? 142 GLU   A OE2  1 1 
ATOM   1018 N  N    . ILE   A 1 144 ? 40.782 -36.421 3.729   1   25.22  ? 143 ILE   A N    1 1 
ATOM   1019 C  CA   . ILE   A 1 144 ? 40.313 -37.035 2.487   1   25.52  ? 143 ILE   A CA   1 1 
ATOM   1020 C  C    . ILE   A 1 144 ? 38.985 -36.47  2       1   25.86  ? 143 ILE   A C    1 1 
ATOM   1021 O  O    . ILE   A 1 144 ? 38.844 -36.234 0.821   1   26.88  ? 143 ILE   A O    1 1 
ATOM   1022 C  CB   . ILE   A 1 144 ? 40.212 -38.569 2.655   1   26.18  ? 143 ILE   A CB   1 1 
ATOM   1023 C  CG1  . ILE   A 1 144 ? 41.555 -39.154 3.119   1   27.4   ? 143 ILE   A CG1  1 1 
ATOM   1024 C  CG2  . ILE   A 1 144 ? 39.716 -39.228 1.374   1   26.45  ? 143 ILE   A CG2  1 1 
ATOM   1025 C  CD1  . ILE   A 1 144 ? 41.493 -40.515 3.583   1   28.76  ? 143 ILE   A CD1  1 1 
ATOM   1026 N  N    . ASN   A 1 145 ? 37.991 -36.305 2.877   1   25.8   ? 144 ASN   A N    1 1 
ATOM   1027 C  CA   . ASN   A 1 145 ? 36.649 -35.909 2.451   1   25.97  ? 144 ASN   A CA   1 1 
ATOM   1028 C  C    . ASN   A 1 145 ? 36.484 -34.448 2.086   1   26.78  ? 144 ASN   A C    1 1 
ATOM   1029 O  O    . ASN   A 1 145 ? 35.483 -34.138 1.432   1   27.68  ? 144 ASN   A O    1 1 
ATOM   1030 C  CB   . ASN   A 1 145 ? 35.588 -36.305 3.466   1   25.87  ? 144 ASN   A CB   1 1 
ATOM   1031 C  CG   . ASN   A 1 145 ? 35.437 -37.781 3.74    1   28.83  ? 144 ASN   A CG   1 1 
ATOM   1032 O  OD1  . ASN   A 1 145 ? 34.656 -38.188 4.611   1   30.87  ? 144 ASN   A OD1  1 1 
ATOM   1033 N  ND2  . ASN   A 1 145 ? 36.17  -38.634 3.043   1   27.87  ? 144 ASN   A ND2  1 1 
ATOM   1034 N  N    . ILE   A 1 146 ? 37.397 -33.535 2.519   1   25.88  ? 145 ILE   A N    1 1 
ATOM   1035 C  CA   . ILE   A 1 146 ? 37.244 -32.129 2.124   1   25.48  ? 145 ILE   A CA   1 1 
ATOM   1036 C  C    . ILE   A 1 146 ? 38.598 -31.431 1.795   1   25.23  ? 145 ILE   A C    1 1 
ATOM   1037 O  O    . ILE   A 1 146 ? 38.703 -30.81  0.734   1   24.83  ? 145 ILE   A O    1 1 
ATOM   1038 C  CB   . ILE   A 1 146 ? 36.377 -31.297 3.105   1   25.58  ? 145 ILE   A CB   1 1 
ATOM   1039 C  CG1  . ILE   A 1 146 ? 36.239 -29.819 2.64    1   25.74  ? 145 ILE   A CG1  1 1 
ATOM   1040 C  CG2  . ILE   A 1 146 ? 36.842 -31.401 4.542   1   26.43  ? 145 ILE   A CG2  1 1 
ATOM   1041 C  CD1  . ILE   A 1 146 ? 35.607 -29.665 1.288   1   25.65  ? 145 ILE   A CD1  1 1 
ATOM   1042 N  N    . LEU   A 1 147 ? 39.631 -31.56  2.653   1   24.86  ? 146 LEU   A N    1 1 
ATOM   1043 C  CA   . LEU   A 1 147 ? 40.907 -30.893 2.413   1   24.44  ? 146 LEU   A CA   1 1 
ATOM   1044 C  C    . LEU   A 1 147 ? 41.529 -31.309 1.086   1   24.52  ? 146 LEU   A C    1 1 
ATOM   1045 O  O    . LEU   A 1 147 ? 41.998 -30.46  0.345   1   24.4   ? 146 LEU   A O    1 1 
ATOM   1046 C  CB   . LEU   A 1 147 ? 41.863 -31.064 3.596   1   24.44  ? 146 LEU   A CB   1 1 
ATOM   1047 C  CG   . LEU   A 1 147 ? 41.412 -30.349 4.863   1   27.03  ? 146 LEU   A CG   1 1 
ATOM   1048 C  CD1  . LEU   A 1 147 ? 42.173 -30.845 6.096   1   27.85  ? 146 LEU   A CD1  1 1 
ATOM   1049 C  CD2  . LEU   A 1 147 ? 41.531 -28.844 4.713   1   27.69  ? 146 LEU   A CD2  1 1 
ATOM   1050 N  N    . GLY   A 1 148 ? 41.41  -32.587 0.749   1   24.86  ? 147 GLY   A N    1 1 
ATOM   1051 C  CA   . GLY   A 1 148 ? 41.904 -33.146 -0.498  1   25.2   ? 147 GLY   A CA   1 1 
ATOM   1052 C  C    . GLY   A 1 148 ? 41.23  -32.538 -1.705  1   26.07  ? 147 GLY   A C    1 1 
ATOM   1053 O  O    . GLY   A 1 148 ? 41.894 -32.266 -2.7    1   27.05  ? 147 GLY   A O    1 1 
ATOM   1054 N  N    . HIS   A 1 149 ? 39.92  -32.258 -1.624  1   25.63  ? 148 HIS   A N    1 1 
ATOM   1055 C  CA   . HIS   A 1 149 ? 39.199 -31.551 -2.693  1   25.49  ? 148 HIS   A CA   1 1 
ATOM   1056 C  C    . HIS   A 1 149 ? 39.877 -30.18  -2.98   1   25.6   ? 148 HIS   A C    1 1 
ATOM   1057 O  O    . HIS   A 1 149 ? 39.99  -29.786 -4.121  1   25.78  ? 148 HIS   A O    1 1 
ATOM   1058 C  CB   . HIS   A 1 149 ? 37.741 -31.256 -2.258  1   25.56  ? 148 HIS   A CB   1 1 
ATOM   1059 C  CG   . HIS   A 1 149 ? 36.859 -32.456 -2.12   1   25.81  ? 148 HIS   A CG   1 1 
ATOM   1060 N  ND1  . HIS   A 1 149 ? 35.496 -32.375 -2.37   1   27.11  ? 148 HIS   A ND1  1 1 
ATOM   1061 C  CD2  . HIS   A 1 149 ? 37.166 -33.727 -1.781  1   26.24  ? 148 HIS   A CD2  1 1 
ATOM   1062 C  CE1  . HIS   A 1 149 ? 35.019 -33.582 -2.143  1   27.38  ? 148 HIS   A CE1  1 1 
ATOM   1063 N  NE2  . HIS   A 1 149 ? 35.988 -34.433 -1.802  1   27.42  ? 148 HIS   A NE2  1 1 
ATOM   1064 N  N    . PHE   A 1 150 ? 40.293 -29.463 -1.943  1   25.73  ? 149 PHE   A N    1 1 
ATOM   1065 C  CA   . PHE   A 1 150 ? 40.953 -28.173 -2.091  1   26.54  ? 149 PHE   A CA   1 1 
ATOM   1066 C  C    . PHE   A 1 150 ? 42.271 -28.31  -2.833  1   26.75  ? 149 PHE   A C    1 1 
ATOM   1067 O  O    . PHE   A 1 150 ? 42.532 -27.528 -3.737  1   26.85  ? 149 PHE   A O    1 1 
ATOM   1068 C  CB   . PHE   A 1 150 ? 41.206 -27.536 -0.705  1   26.53  ? 149 PHE   A CB   1 1 
ATOM   1069 C  CG   . PHE   A 1 150 ? 40.012 -26.843 -0.112  1   27.2   ? 149 PHE   A CG   1 1 
ATOM   1070 C  CD1  . PHE   A 1 150 ? 39.723 -25.529 -0.436  1   28.64  ? 149 PHE   A CD1  1 1 
ATOM   1071 C  CD2  . PHE   A 1 150 ? 39.203 -27.488 0.798   1   27.62  ? 149 PHE   A CD2  1 1 
ATOM   1072 C  CE1  . PHE   A 1 150 ? 38.64  -24.88  0.146   1   29.71  ? 149 PHE   A CE1  1 1 
ATOM   1073 C  CE2  . PHE   A 1 150 ? 38.109 -26.851 1.351   1   28.49  ? 149 PHE   A CE2  1 1 
ATOM   1074 C  CZ   . PHE   A 1 150 ? 37.842 -25.548 1.041   1   28.85  ? 149 PHE   A CZ   1 1 
ATOM   1075 N  N    . TRP   A 1 151 ? 43.125 -29.282 -2.44   1   26.32  ? 150 TRP   A N    1 1 
ATOM   1076 C  CA   . TRP   A 1 151 ? 44.421 -29.426 -3.107  1   25.04  ? 150 TRP   A CA   1 1 
ATOM   1077 C  C    . TRP   A 1 151 ? 44.248 -29.845 -4.559  1   24.78  ? 150 TRP   A C    1 1 
ATOM   1078 O  O    . TRP   A 1 151 ? 44.915 -29.283 -5.433  1   24.79  ? 150 TRP   A O    1 1 
ATOM   1079 C  CB   . TRP   A 1 151 ? 45.392 -30.369 -2.344  1   23.82  ? 150 TRP   A CB   1 1 
ATOM   1080 C  CG   . TRP   A 1 151 ? 45.276 -30.384 -0.836  1   22.52  ? 150 TRP   A CG   1 1 
ATOM   1081 C  CD1  . TRP   A 1 151 ? 45.192 -31.491 -0.037  1   22.59  ? 150 TRP   A CD1  1 1 
ATOM   1082 C  CD2  . TRP   A 1 151 ? 45.29  -29.256 0.048   1   21.46  ? 150 TRP   A CD2  1 1 
ATOM   1083 N  NE1  . TRP   A 1 151 ? 45.112 -31.12  1.281   1   22.22  ? 150 TRP   A NE1  1 1 
ATOM   1084 C  CE2  . TRP   A 1 151 ? 45.145 -29.753 1.362   1   21.82  ? 150 TRP   A CE2  1 1 
ATOM   1085 C  CE3  . TRP   A 1 151 ? 45.342 -27.874 -0.145  1   21.62  ? 150 TRP   A CE3  1 1 
ATOM   1086 C  CZ2  . TRP   A 1 151 ? 45.081 -28.919 2.473   1   22.15  ? 150 TRP   A CZ2  1 1 
ATOM   1087 C  CZ3  . TRP   A 1 151 ? 45.245 -27.054 0.96    1   22.58  ? 150 TRP   A CZ3  1 1 
ATOM   1088 C  CH2  . TRP   A 1 151 ? 45.168 -27.58  2.255   1   22.53  ? 150 TRP   A CH2  1 1 
ATOM   1089 N  N    . ILE   A 1 152 ? 43.354 -30.814 -4.829  1   24.27  ? 151 ILE   A N    1 1 
ATOM   1090 C  CA   . ILE   A 1 152 ? 43.159 -31.263 -6.212  1   24.21  ? 151 ILE   A CA   1 1 
ATOM   1091 C  C    . ILE   A 1 152 ? 42.54  -30.17  -7.067  1   23.74  ? 151 ILE   A C    1 1 
ATOM   1092 O  O    . ILE   A 1 152 ? 43.01  -29.942 -8.174  1   25.1   ? 151 ILE   A O    1 1 
ATOM   1093 C  CB   . ILE   A 1 152 ? 42.401 -32.603 -6.336  1   24.01  ? 151 ILE   A CB   1 1 
ATOM   1094 C  CG1  . ILE   A 1 152 ? 42.961 -33.637 -5.347  1   24.38  ? 151 ILE   A CG1  1 1 
ATOM   1095 C  CG2  . ILE   A 1 152 ? 42.482 -33.099 -7.784  1   23.36  ? 151 ILE   A CG2  1 1 
ATOM   1096 C  CD1  . ILE   A 1 152 ? 42.156 -34.904 -5.148  1   25.88  ? 151 ILE   A CD1  1 1 
ATOM   1097 N  N    . THR   A 1 153 ? 41.543 -29.456 -6.547  1   22.71  ? 152 THR   A N    1 1 
ATOM   1098 C  CA   . THR   A 1 153 ? 40.907 -28.383 -7.304  1   23.24  ? 152 THR   A CA   1 1 
ATOM   1099 C  C    . THR   A 1 153 ? 41.9   -27.254 -7.574  1   24.07  ? 152 THR   A C    1 1 
ATOM   1100 O  O    . THR   A 1 153 ? 42.018 -26.821 -8.722  1   23.59  ? 152 THR   A O    1 1 
ATOM   1101 C  CB   . THR   A 1 153 ? 39.597 -27.931 -6.644  1   23.27  ? 152 THR   A CB   1 1 
ATOM   1102 O  OG1  . THR   A 1 153 ? 38.747 -29.077 -6.491  1   23.12  ? 152 THR   A OG1  1 1 
ATOM   1103 C  CG2  . THR   A 1 153 ? 38.881 -26.872 -7.446  1   23.68  ? 152 THR   A CG2  1 1 
ATOM   1104 N  N    . LYS   A 1 154 ? 42.684 -26.846 -6.561  1   24.45  ? 153 LYS   A N    1 1 
ATOM   1105 C  CA   . LYS   A 1 154 ? 43.681 -25.79  -6.77   1   25.65  ? 153 LYS   A CA   1 1 
ATOM   1106 C  C    . LYS   A 1 154 ? 44.736 -26.143 -7.833  1   26.72  ? 153 LYS   A C    1 1 
ATOM   1107 O  O    . LYS   A 1 154 ? 45.297 -25.247 -8.482  1   27.31  ? 153 LYS   A O    1 1 
ATOM   1108 C  CB   . LYS   A 1 154 ? 44.359 -25.389 -5.46   1   27.23  ? 153 LYS   A CB   1 1 
ATOM   1109 C  CG   . LYS   A 1 154 ? 43.431 -24.685 -4.508  1   31.29  ? 153 LYS   A CG   1 1 
ATOM   1110 C  CD   . LYS   A 1 154 ? 44.068 -23.465 -3.925  1   35.87  ? 153 LYS   A CD   1 1 
ATOM   1111 C  CE   . LYS   A 1 154 ? 45.32  -23.756 -3.153  1   39.76  ? 153 LYS   A CE   1 1 
ATOM   1112 N  NZ   . LYS   A 1 154 ? 45.727 -22.601 -2.316  1   40.46  ? 153 LYS   A NZ   1 1 
ATOM   1113 N  N    . ALA   A 1 155 ? 45.017 -27.434 -8      1   26.68  ? 154 ALA   A N    1 1 
ATOM   1114 C  CA   . ALA   A 1 155 ? 46.01  -27.884 -8.959  1   27.01  ? 154 ALA   A CA   1 1 
ATOM   1115 C  C    . ALA   A 1 155 ? 45.452 -27.945 -10.366 1   28.27  ? 154 ALA   A C    1 1 
ATOM   1116 O  O    . ALA   A 1 155 ? 46.188 -27.703 -11.325 1   28.42  ? 154 ALA   A O    1 1 
ATOM   1117 C  CB   . ALA   A 1 155 ? 46.546 -29.246 -8.549  1   26.86  ? 154 ALA   A CB   1 1 
ATOM   1118 N  N    . LEU   A 1 156 ? 44.158 -28.279 -10.505 1   28.75  ? 155 LEU   A N    1 1 
ATOM   1119 C  CA   . LEU   A 1 156 ? 43.565 -28.461 -11.824 1   28.64  ? 155 LEU   A CA   1 1 
ATOM   1120 C  C    . LEU   A 1 156 ? 42.786 -27.253 -12.356 1   29.28  ? 155 LEU   A C    1 1 
ATOM   1121 O  O    . LEU   A 1 156 ? 42.722 -27.089 -13.575 1   29.43  ? 155 LEU   A O    1 1 
ATOM   1122 C  CB   . LEU   A 1 156 ? 42.708 -29.729 -11.843 1   28.37  ? 155 LEU   A CB   1 1 
ATOM   1123 C  CG   . LEU   A 1 156 ? 43.444 -31.004 -11.386 1   29.46  ? 155 LEU   A CG   1 1 
ATOM   1124 C  CD1  . LEU   A 1 156 ? 42.524 -32.201 -11.431 1   30.23  ? 155 LEU   A CD1  1 1 
ATOM   1125 C  CD2  . LEU   A 1 156 ? 44.705 -31.268 -12.219 1   28.9   ? 155 LEU   A CD2  1 1 
ATOM   1126 N  N    . LEU   A 1 157 ? 42.296 -26.357 -11.489 1   29.69  ? 156 LEU   A N    1 1 
ATOM   1127 C  CA   . LEU   A 1 157 ? 41.533 -25.139 -11.87  1   30.44  ? 156 LEU   A CA   1 1 
ATOM   1128 C  C    . LEU   A 1 157 ? 42.246 -24.124 -12.81  1   31.15  ? 156 LEU   A C    1 1 
ATOM   1129 O  O    . LEU   A 1 157 ? 41.59  -23.598 -13.715 1   31.62  ? 156 LEU   A O    1 1 
ATOM   1130 C  CB   . LEU   A 1 157 ? 41.013 -24.402 -10.614 1   30.52  ? 156 LEU   A CB   1 1 
ATOM   1131 C  CG   . LEU   A 1 157 ? 39.669 -23.664 -10.727 1   31.8   ? 156 LEU   A CG   1 1 
ATOM   1132 C  CD1  . LEU   A 1 157 ? 38.615 -24.436 -11.558 1   32.34  ? 156 LEU   A CD1  1 1 
ATOM   1133 C  CD2  . LEU   A 1 157 ? 39.115 -23.342 -9.363  1   31.73  ? 156 LEU   A CD2  1 1 
ATOM   1134 N  N    . PRO   A 1 158 ? 43.558 -23.834 -12.656 1   31.19  ? 157 PRO   A N    1 1 
ATOM   1135 C  CA   . PRO   A 1 158 ? 44.206 -22.857 -13.555 1   31.06  ? 157 PRO   A CA   1 1 
ATOM   1136 C  C    . PRO   A 1 158 ? 44.051 -23.11  -15.062 1   33     ? 157 PRO   A C    1 1 
ATOM   1137 O  O    . PRO   A 1 158 ? 43.877 -22.183 -15.865 1   33.23  ? 157 PRO   A O    1 1 
ATOM   1138 C  CB   . PRO   A 1 158 ? 45.677 -22.954 -13.151 1   31.11  ? 157 PRO   A CB   1 1 
ATOM   1139 C  CG   . PRO   A 1 158 ? 45.673 -23.432 -11.767 1   31.46  ? 157 PRO   A CG   1 1 
ATOM   1140 C  CD   . PRO   A 1 158 ? 44.489 -24.304 -11.605 1   30.24  ? 157 PRO   A CD   1 1 
ATOM   1141 N  N    . SER   A 1 159 ? 44.167 -24.367 -15.45  1   33.81  ? 158 SER   A N    1 1 
ATOM   1142 C  CA   . SER   A 1 159 ? 44.086 -24.766 -16.839 1   34.8   ? 158 SER   A CA   1 1 
ATOM   1143 C  C    . SER   A 1 159 ? 42.64  -24.622 -17.354 1   36.79  ? 158 SER   A C    1 1 
ATOM   1144 O  O    . SER   A 1 159 ? 42.408 -24.184 -18.475 1   36.66  ? 158 SER   A O    1 1 
ATOM   1145 C  CB   . SER   A 1 159 ? 44.6   -26.191 -16.963 1   35.93  ? 158 SER   A CB   1 1 
ATOM   1146 O  OG   . SER   A 1 159 ? 44.382 -26.712 -18.255 1   40.06  ? 158 SER   A OG   1 1 
ATOM   1147 N  N    . MET   A 1 160 ? 41.663 -24.953 -16.501 1   38.23  ? 159 MET   A N    1 1 
ATOM   1148 C  CA   . MET   A 1 160 ? 40.24  -24.838 -16.798 1   38.44  ? 159 MET   A CA   1 1 
ATOM   1149 C  C    . MET   A 1 160 ? 39.859 -23.354 -16.947 1   39.58  ? 159 MET   A C    1 1 
ATOM   1150 O  O    . MET   A 1 160 ? 39.071 -23.019 -17.819 1   39.88  ? 159 MET   A O    1 1 
ATOM   1151 C  CB   . MET   A 1 160 ? 39.443 -25.478 -15.661 1   36.91  ? 159 MET   A CB   1 1 
ATOM   1152 C  CG   . MET   A 1 160 ? 39.727 -26.941 -15.467 1   36.16  ? 159 MET   A CG   1 1 
ATOM   1153 S  SD   . MET   A 1 160 ? 38.531 -27.608 -14.288 1   36.48  ? 159 MET   A SD   1 1 
ATOM   1154 C  CE   . MET   A 1 160 ? 39.079 -29.333 -14.11  1   31.93  ? 159 MET   A CE   1 1 
ATOM   1155 N  N    . ILE   A 1 161 ? 40.431 -22.471 -16.106 1   39.92  ? 160 ILE   A N    1 1 
ATOM   1156 C  CA   . ILE   A 1 161 ? 40.173 -21.021 -16.159 1   40.49  ? 160 ILE   A CA   1 1 
ATOM   1157 C  C    . ILE   A 1 161 ? 40.751 -20.441 -17.434 1   42.16  ? 160 ILE   A C    1 1 
ATOM   1158 O  O    . ILE   A 1 161 ? 40.062 -19.715 -18.157 1   42.81  ? 160 ILE   A O    1 1 
ATOM   1159 C  CB   . ILE   A 1 161 ? 40.729 -20.296 -14.9   1   39.98  ? 160 ILE   A CB   1 1 
ATOM   1160 C  CG1  . ILE   A 1 161 ? 39.923 -20.666 -13.652 1   39.56  ? 160 ILE   A CG1  1 1 
ATOM   1161 C  CG2  . ILE   A 1 161 ? 40.779 -18.778 -15.113 1   40.41  ? 160 ILE   A CG2  1 1 
ATOM   1162 C  CD1  . ILE   A 1 161 ? 40.501 -20.145 -12.389 1   40.56  ? 160 ILE   A CD1  1 1 
ATOM   1163 N  N    . LYS   A 1 162 ? 42.015 -20.806 -17.737 1   42.31  ? 161 LYS   A N    1 1 
ATOM   1164 C  CA   . LYS   A 1 162 ? 42.752 -20.397 -18.917 1   42.4   ? 161 LYS   A CA   1 1 
ATOM   1165 C  C    . LYS   A 1 162 ? 41.963 -20.731 -20.178 1   41.13  ? 161 LYS   A C    1 1 
ATOM   1166 O  O    . LYS   A 1 162 ? 41.893 -19.922 -21.076 1   41.87  ? 161 LYS   A O    1 1 
ATOM   1167 C  CB   . LYS   A 1 162 ? 44.107 -21.132 -18.948 1   46.69  ? 161 LYS   A CB   1 1 
ATOM   1168 C  CG   . LYS   A 1 162 ? 45.326 -20.229 -19.144 1   54.01  ? 161 LYS   A CG   1 1 
ATOM   1169 C  CD   . LYS   A 1 162 ? 46.649 -20.931 -18.807 1   60.78  ? 161 LYS   A CD   1 1 
ATOM   1170 C  CE   . LYS   A 1 162 ? 46.772 -21.484 -17.379 1   65.65  ? 161 LYS   A CE   1 1 
ATOM   1171 N  NZ   . LYS   A 1 162 ? 46.87  -20.437 -16.313 1   67.14  ? 161 LYS   A NZ   1 1 
ATOM   1172 N  N    . ARG   A 1 163 ? 41.337 -21.898 -20.229 1   39.62  ? 162 ARG   A N    1 1 
ATOM   1173 C  CA   . ARG   A 1 163 ? 40.548 -22.356 -21.381 1   38.84  ? 162 ARG   A CA   1 1 
ATOM   1174 C  C    . ARG   A 1 163 ? 39.048 -22.028 -21.296 1   38.34  ? 162 ARG   A C    1 1 
ATOM   1175 O  O    . ARG   A 1 163 ? 38.312 -22.361 -22.214 1   38.79  ? 162 ARG   A O    1 1 
ATOM   1176 C  CB   . ARG   A 1 163 ? 40.674 -23.889 -21.533 1   39.68  ? 162 ARG   A CB   1 1 
ATOM   1177 C  CG   . ARG   A 1 163 ? 42.058 -24.363 -21.918 1   43.55  ? 162 ARG   A CG   1 1 
ATOM   1178 C  CD   . ARG   A 1 163 ? 42.151 -25.858 -21.788 1   48.15  ? 162 ARG   A CD   1 1 
ATOM   1179 N  NE   . ARG   A 1 163 ? 43.476 -26.356 -22.158 1   52.28  ? 162 ARG   A NE   1 1 
ATOM   1180 C  CZ   . ARG   A 1 163 ? 43.705 -27.153 -23.196 1   55.21  ? 162 ARG   A CZ   1 1 
ATOM   1181 N  NH1  . ARG   A 1 163 ? 42.693 -27.616 -23.922 1   54.17  ? 162 ARG   A NH1  1 1 
ATOM   1182 N  NH2  . ARG   A 1 163 ? 44.94  -27.559 -23.467 1   55.59  ? 162 ARG   A NH2  1 1 
ATOM   1183 N  N    . ASN   A 1 164 ? 38.588 -21.451 -20.18  1   37.47  ? 163 ASN   A N    1 1 
ATOM   1184 C  CA   . ASN   A 1 164 ? 37.184 -21.191 -19.833 1   36.69  ? 163 ASN   A CA   1 1 
ATOM   1185 C  C    . ASN   A 1 164 ? 36.344 -22.444 -20.026 1   36.46  ? 163 ASN   A C    1 1 
ATOM   1186 O  O    . ASN   A 1 164 ? 35.322 -22.402 -20.702 1   37.13  ? 163 ASN   A O    1 1 
ATOM   1187 C  CB   . ASN   A 1 164 ? 36.593 -19.978 -20.556 1   35.51  ? 163 ASN   A CB   1 1 
ATOM   1188 C  CG   . ASN   A 1 164 ? 35.38  -19.471 -19.817 1   36.56  ? 163 ASN   A CG   1 1 
ATOM   1189 O  OD1  . ASN   A 1 164 ? 35.333 -19.512 -18.579 1   38.55  ? 163 ASN   A OD1  1 1 
ATOM   1190 N  ND2  . ASN   A 1 164 ? 34.338 -19.066 -20.519 1   34.78  ? 163 ASN   A ND2  1 1 
ATOM   1191 N  N    . HIS   A 1 165 ? 36.845 -23.579 -19.527 1   35.29  ? 164 HIS   A N    1 1 
ATOM   1192 C  CA   . HIS   A 1 165 ? 36.202 -24.859 -19.774 1   35.08  ? 164 HIS   A CA   1 1 
ATOM   1193 C  C    . HIS   A 1 165 ? 36.617 -25.909 -18.766 1   33.35  ? 164 HIS   A C    1 1 
ATOM   1194 O  O    . HIS   A 1 165 ? 37.77  -26.32  -18.743 1   33.95  ? 164 HIS   A O    1 1 
ATOM   1195 C  CB   . HIS   A 1 165 ? 36.543 -25.341 -21.202 1   36.83  ? 164 HIS   A CB   1 1 
ATOM   1196 C  CG   . HIS   A 1 165 ? 35.898 -26.637 -21.579 1   40.61  ? 164 HIS   A CG   1 1 
ATOM   1197 N  ND1  . HIS   A 1 165 ? 34.607 -26.68  -22.084 1   42.63  ? 164 HIS   A ND1  1 1 
ATOM   1198 C  CD2  . HIS   A 1 165 ? 36.394 -27.898 -21.53  1   42.07  ? 164 HIS   A CD2  1 1 
ATOM   1199 C  CE1  . HIS   A 1 165 ? 34.362 -27.96  -22.318 1   43.35  ? 164 HIS   A CE1  1 1 
ATOM   1200 N  NE2  . HIS   A 1 165 ? 35.413 -28.727 -22.009 1   43.36  ? 164 HIS   A NE2  1 1 
ATOM   1201 N  N    . GLY   A 1 166 ? 35.659 -26.369 -17.981 1   31.33  ? 165 GLY   A N    1 1 
ATOM   1202 C  CA   . GLY   A 1 166 ? 35.893 -27.408 -16.996 1   30.94  ? 165 GLY   A CA   1 1 
ATOM   1203 C  C    . GLY   A 1 166 ? 34.623 -27.835 -16.293 1   30.56  ? 165 GLY   A C    1 1 
ATOM   1204 O  O    . GLY   A 1 166 ? 33.546 -27.276 -16.527 1   31.58  ? 165 GLY   A O    1 1 
ATOM   1205 N  N    . HIS   A 1 167 ? 34.734 -28.839 -15.442 1   28.97  ? 166 HIS   A N    1 1 
ATOM   1206 C  CA   . HIS   A 1 167 ? 33.603 -29.315 -14.655 1   27.45  ? 166 HIS   A CA   1 1 
ATOM   1207 C  C    . HIS   A 1 167 ? 34.116 -29.896 -13.354 1   26.61  ? 166 HIS   A C    1 1 
ATOM   1208 O  O    . HIS   A 1 167 ? 34.848 -30.86  -13.41  1   26.73  ? 166 HIS   A O    1 1 
ATOM   1209 C  CB   . HIS   A 1 167 ? 32.768 -30.342 -15.427 1   26.2   ? 166 HIS   A CB   1 1 
ATOM   1210 C  CG   . HIS   A 1 167 ? 31.347 -30.436 -14.932 1   26.47  ? 166 HIS   A CG   1 1 
ATOM   1211 N  ND1  . HIS   A 1 167 ? 30.267 -30.47  -15.816 1   27.36  ? 166 HIS   A ND1  1 1 
ATOM   1212 C  CD2  . HIS   A 1 167 ? 30.869 -30.492 -13.662 1   26.31  ? 166 HIS   A CD2  1 1 
ATOM   1213 C  CE1  . HIS   A 1 167 ? 29.183 -30.543 -15.063 1   27.01  ? 166 HIS   A CE1  1 1 
ATOM   1214 N  NE2  . HIS   A 1 167 ? 29.495 -30.568 -13.76  1   27.13  ? 166 HIS   A NE2  1 1 
ATOM   1215 N  N    . ILE   A 1 168 ? 33.787 -29.281 -12.19  1   26.2   ? 167 ILE   A N    1 1 
ATOM   1216 C  CA   . ILE   A 1 168 ? 34.173 -29.762 -10.855 1   26.02  ? 167 ILE   A CA   1 1 
ATOM   1217 C  C    . ILE   A 1 168 ? 32.993 -30.519 -10.206 1   25.8   ? 167 ILE   A C    1 1 
ATOM   1218 O  O    . ILE   A 1 168 ? 31.968 -29.917 -9.86   1   25.5   ? 167 ILE   A O    1 1 
ATOM   1219 C  CB   . ILE   A 1 168 ? 34.609 -28.612 -9.922  1   26.4   ? 167 ILE   A CB   1 1 
ATOM   1220 C  CG1  . ILE   A 1 168 ? 35.594 -27.637 -10.625 1   27.38  ? 167 ILE   A CG1  1 1 
ATOM   1221 C  CG2  . ILE   A 1 168 ? 35.149 -29.162 -8.585  1   26.11  ? 167 ILE   A CG2  1 1 
ATOM   1222 C  CD1  . ILE   A 1 168 ? 36.923 -28.208 -10.931 1   28.58  ? 167 ILE   A CD1  1 1 
ATOM   1223 N  N    . VAL   A 1 169 ? 33.153 -31.829 -10.026 1   25.22  ? 168 VAL   A N    1 1 
ATOM   1224 C  CA   . VAL   A 1 169 ? 32.151 -32.682 -9.43   1   25.61  ? 168 VAL   A CA   1 1 
ATOM   1225 C  C    . VAL   A 1 169 ? 32.567 -33.03  -8.01   1   26.24  ? 168 VAL   A C    1 1 
ATOM   1226 O  O    . VAL   A 1 169 ? 33.629 -33.617 -7.808  1   26.9   ? 168 VAL   A O    1 1 
ATOM   1227 C  CB   . VAL   A 1 169 ? 31.994 -33.962 -10.268 1   26.62  ? 168 VAL   A CB   1 1 
ATOM   1228 C  CG1  . VAL   A 1 169 ? 31.081 -34.979 -9.565  1   27.8   ? 168 VAL   A CG1  1 1 
ATOM   1229 C  CG2  . VAL   A 1 169 ? 31.51  -33.641 -11.671 1   25.8   ? 168 VAL   A CG2  1 1 
ATOM   1230 N  N    . THR   A 1 170 ? 31.76  -32.645 -7.021  1   25.75  ? 169 THR   A N    1 1 
ATOM   1231 C  CA   . THR   A 1 170 ? 32.034 -32.967 -5.623  1   25.75  ? 169 THR   A CA   1 1 
ATOM   1232 C  C    . THR   A 1 170 ? 31.142 -34.116 -5.22   1   25.16  ? 169 THR   A C    1 1 
ATOM   1233 O  O    . THR   A 1 170 ? 29.926 -33.968 -5.313  1   25.75  ? 169 THR   A O    1 1 
ATOM   1234 C  CB   . THR   A 1 170 ? 31.638 -31.783 -4.738  1   27.18  ? 169 THR   A CB   1 1 
ATOM   1235 O  OG1  . THR   A 1 170 ? 32.41  -30.656 -5.139  1   28.77  ? 169 THR   A OG1  1 1 
ATOM   1236 C  CG2  . THR   A 1 170 ? 31.833 -32.08  -3.24   1   27.08  ? 169 THR   A CG2  1 1 
ATOM   1237 N  N    . VAL   A 1 171 ? 31.703 -35.248 -4.806  1   24.21  ? 170 VAL   A N    1 1 
ATOM   1238 C  CA   . VAL   A 1 171 ? 30.867 -36.344 -4.326  1   24.56  ? 170 VAL   A CA   1 1 
ATOM   1239 C  C    . VAL   A 1 171 ? 30.726 -36.164 -2.83   1   26.55  ? 170 VAL   A C    1 1 
ATOM   1240 O  O    . VAL   A 1 171 ? 31.702 -36.326 -2.077  1   27.41  ? 170 VAL   A O    1 1 
ATOM   1241 C  CB   . VAL   A 1 171 ? 31.348 -37.758 -4.713  1   23.99  ? 170 VAL   A CB   1 1 
ATOM   1242 C  CG1  . VAL   A 1 171 ? 30.536 -38.829 -3.971  1   23.87  ? 170 VAL   A CG1  1 1 
ATOM   1243 C  CG2  . VAL   A 1 171 ? 31.28  -37.95  -6.228  1   22.53  ? 170 VAL   A CG2  1 1 
ATOM   1244 N  N    . ALA   A 1 172 ? 29.547 -35.7   -2.399  1   26.26  ? 171 ALA   A N    1 1 
ATOM   1245 C  CA   . ALA   A 1 172 ? 29.307 -35.465 -0.99   1   25.65  ? 171 ALA   A CA   1 1 
ATOM   1246 C  C    . ALA   A 1 172 ? 28.397 -36.627 -0.424  1   26.69  ? 171 ALA   A C    1 1 
ATOM   1247 O  O    . ALA   A 1 172 ? 28.891 -37.753 -0.454  1   26.57  ? 171 ALA   A O    1 1 
ATOM   1248 C  CB   . ALA   A 1 172 ? 28.796 -34.028 -0.756  1   25.1   ? 171 ALA   A CB   1 1 
ATOM   1249 N  N    . SER   A 1 173 ? 27.111 -36.427 -0.007  1   27.2   ? 172 SER   A N    1 1 
ATOM   1250 C  CA   . SER   A 1 173 ? 26.235 -37.429 0.57    1   27.98  ? 172 SER   A CA   1 1 
ATOM   1251 C  C    . SER   A 1 173 ? 24.977 -36.699 1.064   1   29.55  ? 172 SER   A C    1 1 
ATOM   1252 O  O    . SER   A 1 173 ? 25.008 -35.462 1.196   1   29.13  ? 172 SER   A O    1 1 
ATOM   1253 C  CB   . SER   A 1 173 ? 26.945 -38.04  1.782   1   28.3   ? 172 SER   A CB   1 1 
ATOM   1254 O  OG   . SER   A 1 173 ? 26.111 -38.89  2.543   1   29.43  ? 172 SER   A OG   1 1 
ATOM   1255 N  N    . VAL   A 1 174 ? 23.89  -37.443 1.419   1   30.95  ? 173 VAL   A N    1 1 
ATOM   1256 C  CA   . VAL   A 1 174 ? 22.765 -36.79  2.119   1   32.97  ? 173 VAL   A CA   1 1 
ATOM   1257 C  C    . VAL   A 1 174 ? 23.251 -36.287 3.51    1   34.55  ? 173 VAL   A C    1 1 
ATOM   1258 O  O    . VAL   A 1 174 ? 22.685 -35.329 4.045   1   35.03  ? 173 VAL   A O    1 1 
ATOM   1259 C  CB   . VAL   A 1 174 ? 21.495 -37.64  2.252   1   33.9   ? 173 VAL   A CB   1 1 
ATOM   1260 C  CG1  . VAL   A 1 174 ? 20.766 -37.689 0.925   1   34.98  ? 173 VAL   A CG1  1 1 
ATOM   1261 C  CG2  . VAL   A 1 174 ? 21.833 -39.04  2.762   1   34.1   ? 173 VAL   A CG2  1 1 
ATOM   1262 N  N    . CYS   A 1 175 ? 24.349 -36.9   4.053   1   35.11  ? 174 CYS   A N    1 1 
ATOM   1263 C  CA   . CYS   A 1 175 ? 25.072 -36.506 5.268   1   35.65  ? 174 CYS   A CA   1 1 
ATOM   1264 C  C    . CYS   A 1 175 ? 25.643 -35.083 5.183   1   35.36  ? 174 CYS   A C    1 1 
ATOM   1265 O  O    . CYS   A 1 175 ? 26.041 -34.554 6.208   1   36.85  ? 174 CYS   A O    1 1 
ATOM   1266 C  CB   . CYS   A 1 175 ? 26.17  -37.509 5.597   1   37.14  ? 174 CYS   A CB   1 1 
ATOM   1267 S  SG   . CYS   A 1 175 ? 25.56  -39.15  6.041   1   44.91  ? 174 CYS   A SG   1 1 
ATOM   1268 N  N    . GLY   A 1 176 ? 25.707 -34.498 3.993   1   33.52  ? 175 GLY   A N    1 1 
ATOM   1269 C  CA   . GLY   A 1 176 ? 26.123 -33.116 3.799   1   33.25  ? 175 GLY   A CA   1 1 
ATOM   1270 C  C    . GLY   A 1 176 ? 24.985 -32.116 3.963   1   32.89  ? 175 GLY   A C    1 1 
ATOM   1271 O  O    . GLY   A 1 176 ? 25.204 -30.904 3.93    1   31.98  ? 175 GLY   A O    1 1 
ATOM   1272 N  N    . HIS   A 1 177 ? 23.752 -32.622 4.145   1   33.34  ? 176 HIS   A N    1 1 
ATOM   1273 C  CA   . HIS   A 1 177 ? 22.547 -31.838 4.309   1   34.84  ? 176 HIS   A CA   1 1 
ATOM   1274 C  C    . HIS   A 1 177 ? 21.87  -32.126 5.652   1   38.62  ? 176 HIS   A C    1 1 
ATOM   1275 O  O    . HIS   A 1 177 ? 21.214 -31.238 6.211   1   39.12  ? 176 HIS   A O    1 1 
ATOM   1276 C  CB   . HIS   A 1 177 ? 21.587 -32.147 3.171   1   34.01  ? 176 HIS   A CB   1 1 
ATOM   1277 C  CG   . HIS   A 1 177 ? 22.144 -31.785 1.837   1   33.92  ? 176 HIS   A CG   1 1 
ATOM   1278 N  ND1  . HIS   A 1 177 ? 21.998 -30.507 1.316   1   34.77  ? 176 HIS   A ND1  1 1 
ATOM   1279 C  CD2  . HIS   A 1 177 ? 22.875 -32.529 0.976   1   34.5   ? 176 HIS   A CD2  1 1 
ATOM   1280 C  CE1  . HIS   A 1 177 ? 22.621 -30.52  0.151   1   34.75  ? 176 HIS   A CE1  1 1 
ATOM   1281 N  NE2  . HIS   A 1 177 ? 23.162 -31.715 -0.102  1   35.08  ? 176 HIS   A NE2  1 1 
ATOM   1282 N  N    . GLU   A 1 178 ? 22.014 -33.362 6.168   1   40.74  ? 177 GLU   A N    1 1 
ATOM   1283 C  CA   . GLU   A 1 178 ? 21.409 -33.742 7.434   1   43.25  ? 177 GLU   A CA   1 1 
ATOM   1284 C  C    . GLU   A 1 178 ? 22.361 -34.649 8.232   1   44.43  ? 177 GLU   A C    1 1 
ATOM   1285 O  O    . GLU   A 1 178 ? 23.021 -35.499 7.65    1   45.36  ? 177 GLU   A O    1 1 
ATOM   1286 C  CB   . GLU   A 1 178 ? 20.046 -34.418 7.185   1   47.03  ? 177 GLU   A CB   1 1 
ATOM   1287 C  CG   . GLU   A 1 178 ? 19.305 -34.867 8.438   1   55.1   ? 177 GLU   A CG   1 1 
ATOM   1288 C  CD   . GLU   A 1 178 ? 18.856 -33.815 9.441   1   66.76  ? 177 GLU   A CD   1 1 
ATOM   1289 O  OE1  . GLU   A 1 178 ? 17.625 -33.622 9.583   1   72.69  ? 177 GLU   A OE1  1 1 
ATOM   1290 O  OE2  . GLU   A 1 178 ? 19.724 -33.22  10.121  1   67.64  ? 177 GLU   A OE2  1 1 
ATOM   1291 N  N    . GLY   A 1 179 ? 22.448 -34.429 9.537   1   44.27  ? 178 GLY   A N    1 1 
ATOM   1292 C  CA   . GLY   A 1 179 ? 23.307 -35.209 10.41   1   45     ? 178 GLY   A CA   1 1 
ATOM   1293 C  C    . GLY   A 1 179 ? 22.778 -36.593 10.706  1   45.68  ? 178 GLY   A C    1 1 
ATOM   1294 O  O    . GLY   A 1 179 ? 21.59  -36.874 10.521  1   46.19  ? 178 GLY   A O    1 1 
ATOM   1295 N  N    . ILE   A 1 180 ? 23.665 -37.48  11.163  1   45.23  ? 179 ILE   A N    1 1 
ATOM   1296 C  CA   . ILE   A 1 180 ? 23.322 -38.861 11.501  1   44.35  ? 179 ILE   A CA   1 1 
ATOM   1297 C  C    . ILE   A 1 180 ? 24.064 -39.265 12.758  1   42.36  ? 179 ILE   A C    1 1 
ATOM   1298 O  O    . ILE   A 1 180 ? 25.277 -39.138 12.811  1   41.8   ? 179 ILE   A O    1 1 
ATOM   1299 C  CB   . ILE   A 1 180 ? 23.734 -39.813 10.328  1   45.17  ? 179 ILE   A CB   1 1 
ATOM   1300 C  CG1  . ILE   A 1 180 ? 22.91  -39.563 9.064   1   46.29  ? 179 ILE   A CG1  1 1 
ATOM   1301 C  CG2  . ILE   A 1 180 ? 23.661 -41.287 10.738  1   45.5   ? 179 ILE   A CG2  1 1 
ATOM   1302 C  CD1  . ILE   A 1 180 ? 23.377 -40.353 7.902   1   48.05  ? 179 ILE   A CD1  1 1 
ATOM   1303 N  N    . PRO   A 1 181 ? 23.382 -39.872 13.733  1   41.81  ? 180 PRO   A N    1 1 
ATOM   1304 C  CA   . PRO   A 1 181 ? 24.087 -40.38  14.922  1   41.21  ? 180 PRO   A CA   1 1 
ATOM   1305 C  C    . PRO   A 1 181 ? 25.22  -41.357 14.572  1   40.88  ? 180 PRO   A C    1 1 
ATOM   1306 O  O    . PRO   A 1 181 ? 25.119 -42.104 13.582  1   41.07  ? 180 PRO   A O    1 1 
ATOM   1307 C  CB   . PRO   A 1 181 ? 22.98  -41.098 15.685  1   41.83  ? 180 PRO   A CB   1 1 
ATOM   1308 C  CG   . PRO   A 1 181 ? 21.727 -40.432 15.248  1   42.42  ? 180 PRO   A CG   1 1 
ATOM   1309 C  CD   . PRO   A 1 181 ? 21.934 -40.137 13.811  1   40.96  ? 180 PRO   A CD   1 1 
ATOM   1310 N  N    . TYR   A 1 182 ? 26.318 -41.315 15.351  1   39.87  ? 181 TYR   A N    1 1 
ATOM   1311 C  CA   . TYR   A 1 182 ? 27.512 -42.172 15.185  1   39.62  ? 181 TYR   A CA   1 1 
ATOM   1312 C  C    . TYR   A 1 182 ? 28.344 -41.845 13.925  1   37.64  ? 181 TYR   A C    1 1 
ATOM   1313 O  O    . TYR   A 1 182 ? 29.357 -42.501 13.682  1   37.5   ? 181 TYR   A O    1 1 
ATOM   1314 C  CB   . TYR   A 1 182 ? 27.192 -43.688 15.266  1   40.39  ? 181 TYR   A CB   1 1 
ATOM   1315 C  CG   . TYR   A 1 182 ? 26.112 -44.015 16.278  1   41.66  ? 181 TYR   A CG   1 1 
ATOM   1316 C  CD1  . TYR   A 1 182 ? 26.214 -43.588 17.592  1   42.81  ? 181 TYR   A CD1  1 1 
ATOM   1317 C  CD2  . TYR   A 1 182 ? 24.932 -44.633 15.889  1   42.58  ? 181 TYR   A CD2  1 1 
ATOM   1318 C  CE1  . TYR   A 1 182 ? 25.173 -43.774 18.493  1   43.71  ? 181 TYR   A CE1  1 1 
ATOM   1319 C  CE2  . TYR   A 1 182 ? 23.902 -44.862 16.794  1   43.63  ? 181 TYR   A CE2  1 1 
ATOM   1320 C  CZ   . TYR   A 1 182 ? 24.015 -44.411 18.09   1   45.07  ? 181 TYR   A CZ   1 1 
ATOM   1321 O  OH   . TYR   A 1 182 ? 22.985 -44.643 18.988  1   48.54  ? 181 TYR   A OH   1 1 
ATOM   1322 N  N    . LEU   A 1 183 ? 27.976 -40.804 13.178  1   36.13  ? 182 LEU   A N    1 1 
ATOM   1323 C  CA   . LEU   A 1 183 ? 28.73  -40.384 12.001  1   35.5   ? 182 LEU   A CA   1 1 
ATOM   1324 C  C    . LEU   A 1 183 ? 29.006 -38.869 12.086  1   34.39  ? 182 LEU   A C    1 1 
ATOM   1325 O  O    . LEU   A 1 183 ? 28.957 -38.198 11.059  1   35.14  ? 182 LEU   A O    1 1 
ATOM   1326 C  CB   . LEU   A 1 183 ? 27.973 -40.721 10.68   1   35.41  ? 182 LEU   A CB   1 1 
ATOM   1327 C  CG   . LEU   A 1 183 ? 27.835 -42.199 10.306  1   36.62  ? 182 LEU   A CG   1 1 
ATOM   1328 C  CD1  . LEU   A 1 183 ? 27.032 -42.37  9.028   1   36.95  ? 182 LEU   A CD1  1 1 
ATOM   1329 C  CD2  . LEU   A 1 183 ? 29.193 -42.86  10.171  1   37.1   ? 182 LEU   A CD2  1 1 
ATOM   1330 N  N    . ILE   A 1 184 ? 29.271 -38.331 13.294  1   32.49  ? 183 ILE   A N    1 1 
ATOM   1331 C  CA   . ILE   A 1 184 ? 29.508 -36.899 13.473  1   31.72  ? 183 ILE   A CA   1 1 
ATOM   1332 C  C    . ILE   A 1 184 ? 30.688 -36.393 12.643  1   31.79  ? 183 ILE   A C    1 1 
ATOM   1333 O  O    . ILE   A 1 184 ? 30.478 -35.491 11.829  1   32.36  ? 183 ILE   A O    1 1 
ATOM   1334 C  CB   . ILE   A 1 184 ? 29.613 -36.429 14.945  1   31.34  ? 183 ILE   A CB   1 1 
ATOM   1335 C  CG1  . ILE   A 1 184 ? 28.363 -36.812 15.755  1   32.08  ? 183 ILE   A CG1  1 1 
ATOM   1336 C  CG2  . ILE   A 1 184 ? 29.895 -34.911 15.006  1   31.34  ? 183 ILE   A CG2  1 1 
ATOM   1337 C  CD1  . ILE   A 1 184 ? 28.427 -36.434 17.227  1   32.74  ? 183 ILE   A CD1  1 1 
ATOM   1338 N  N    . PRO   A 1 185 ? 31.931 -36.923 12.794  1   30.85  ? 184 PRO   A N    1 1 
ATOM   1339 C  CA   . PRO   A 1 185 ? 33.038 -36.396 11.976  1   30.11  ? 184 PRO   A CA   1 1 
ATOM   1340 C  C    . PRO   A 1 185 ? 32.793 -36.531 10.494  1   30.25  ? 184 PRO   A C    1 1 
ATOM   1341 O  O    . PRO   A 1 185 ? 33.153 -35.64  9.754   1   31.36  ? 184 PRO   A O    1 1 
ATOM   1342 C  CB   . PRO   A 1 185 ? 34.253 -37.213 12.447  1   30.45  ? 184 PRO   A CB   1 1 
ATOM   1343 C  CG   . PRO   A 1 185 ? 33.887 -37.659 13.807  1   30.3   ? 184 PRO   A CG   1 1 
ATOM   1344 C  CD   . PRO   A 1 185 ? 32.421 -37.943 13.743  1   29.19  ? 184 PRO   A CD   1 1 
ATOM   1345 N  N    . TYR   A 1 186 ? 32.136 -37.597 10.064  1   29.64  ? 185 TYR   A N    1 1 
ATOM   1346 C  CA   . TYR   A 1 186 ? 31.856 -37.831 8.653   1   29.2   ? 185 TYR   A CA   1 1 
ATOM   1347 C  C    . TYR   A 1 186 ? 30.819 -36.843 8.132   1   30.23  ? 185 TYR   A C    1 1 
ATOM   1348 O  O    . TYR   A 1 186 ? 31.013 -36.269 7.061   1   31.25  ? 185 TYR   A O    1 1 
ATOM   1349 C  CB   . TYR   A 1 186 ? 31.399 -39.272 8.448   1   28.02  ? 185 TYR   A CB   1 1 
ATOM   1350 C  CG   . TYR   A 1 186 ? 30.941 -39.579 7.049   1   28.05  ? 185 TYR   A CG   1 1 
ATOM   1351 C  CD1  . TYR   A 1 186 ? 31.853 -39.905 6.055   1   28.96  ? 185 TYR   A CD1  1 1 
ATOM   1352 C  CD2  . TYR   A 1 186 ? 29.591 -39.598 6.728   1   28.58  ? 185 TYR   A CD2  1 1 
ATOM   1353 C  CE1  . TYR   A 1 186 ? 31.435 -40.223 4.771   1   29.96  ? 185 TYR   A CE1  1 1 
ATOM   1354 C  CE2  . TYR   A 1 186 ? 29.161 -39.902 5.444   1   29.77  ? 185 TYR   A CE2  1 1 
ATOM   1355 C  CZ   . TYR   A 1 186 ? 30.088 -40.224 4.471   1   31.18  ? 185 TYR   A CZ   1 1 
ATOM   1356 O  OH   . TYR   A 1 186 ? 29.666 -40.544 3.205   1   34.16  ? 185 TYR   A OH   1 1 
ATOM   1357 N  N    . CYS   A 1 187 ? 29.732 -36.627 8.877   1   29.72  ? 186 CYS   A N    1 1 
ATOM   1358 C  CA   . CYS   A 1 187 ? 28.69  -35.686 8.475   1   30.53  ? 186 CYS   A CA   1 1 
ATOM   1359 C  C    . CYS   A 1 187 ? 29.254 -34.274 8.35    1   30.16  ? 186 CYS   A C    1 1 
ATOM   1360 O  O    . CYS   A 1 187 ? 28.87  -33.533 7.461   1   29.86  ? 186 CYS   A O    1 1 
ATOM   1361 C  CB   . CYS   A 1 187 ? 27.536 -35.715 9.472   1   32.16  ? 186 CYS   A CB   1 1 
ATOM   1362 S  SG   . CYS   A 1 187 ? 26.483 -37.176 9.344   1   37.85  ? 186 CYS   A SG   1 1 
ATOM   1363 N  N    . SER   A 1 188 ? 30.139 -33.901 9.284   1   29.61  ? 187 SER   A N    1 1 
ATOM   1364 C  CA   . SER   A 1 188 ? 30.768 -32.598 9.332   1   28.57  ? 187 SER   A CA   1 1 
ATOM   1365 C  C    . SER   A 1 188 ? 31.636 -32.398 8.078   1   27.71  ? 187 SER   A C    1 1 
ATOM   1366 O  O    . SER   A 1 188 ? 31.566 -31.351 7.454   1   27.79  ? 187 SER   A O    1 1 
ATOM   1367 C  CB   . SER   A 1 188 ? 31.596 -32.495 10.602  1   28.8   ? 187 SER   A CB   1 1 
ATOM   1368 O  OG   . SER   A 1 188 ? 31.931 -31.15  10.869  1   30.36  ? 187 SER   A OG   1 1 
ATOM   1369 N  N    . SER   A 1 189 ? 32.423 -33.411 7.686   1   26.95  ? 188 SER   A N    1 1 
ATOM   1370 C  CA   . SER   A 1 189 ? 33.254 -33.341 6.49    1   26.72  ? 188 SER   A CA   1 1 
ATOM   1371 C  C    . SER   A 1 189 ? 32.39  -33.348 5.222   1   27.17  ? 188 SER   A C    1 1 
ATOM   1372 O  O    . SER   A 1 189 ? 32.782 -32.751 4.223   1   26.59  ? 188 SER   A O    1 1 
ATOM   1373 C  CB   . SER   A 1 189 ? 34.259 -34.489 6.446   1   27.19  ? 188 SER   A CB   1 1 
ATOM   1374 O  OG   . SER   A 1 189 ? 33.625 -35.727 6.158   1   27.72  ? 188 SER   A OG   1 1 
ATOM   1375 N  N    . LYS   A 1 190 ? 31.195 -33.991 5.265   1   26.92  ? 189 LYS   A N    1 1 
ATOM   1376 C  CA   . LYS   A 1 190 ? 30.284 -33.987 4.116   1   25.68  ? 189 LYS   A CA   1 1 
ATOM   1377 C  C    . LYS   A 1 190 ? 29.566 -32.65  3.979   1   24.94  ? 189 LYS   A C    1 1 
ATOM   1378 O  O    . LYS   A 1 190 ? 29.344 -32.191 2.864   1   26.22  ? 189 LYS   A O    1 1 
ATOM   1379 C  CB   . LYS   A 1 190 ? 29.322 -35.182 4.161   1   26.67  ? 189 LYS   A CB   1 1 
ATOM   1380 C  CG   . LYS   A 1 190 ? 29.987 -36.506 3.804   1   27.73  ? 189 LYS   A CG   1 1 
ATOM   1381 C  CD   . LYS   A 1 190 ? 30.608 -36.469 2.407   1   29.81  ? 189 LYS   A CD   1 1 
ATOM   1382 C  CE   . LYS   A 1 190 ? 31.526 -37.639 2.203   1   32.38  ? 189 LYS   A CE   1 1 
ATOM   1383 N  NZ   . LYS   A 1 190 ? 31.803 -37.9   0.757   1   32.67  ? 189 LYS   A NZ   1 1 
ATOM   1384 N  N    . PHE   A 1 191 ? 29.277 -31.98  5.088   1   23.91  ? 190 PHE   A N    1 1 
ATOM   1385 C  CA   . PHE   A 1 191 ? 28.7   -30.635 5.082   1   23.93  ? 190 PHE   A CA   1 1 
ATOM   1386 C  C    . PHE   A 1 191 ? 29.751 -29.677 4.503   1   23.92  ? 190 PHE   A C    1 1 
ATOM   1387 O  O    . PHE   A 1 191 ? 29.412 -28.81  3.713   1   23.91  ? 190 PHE   A O    1 1 
ATOM   1388 C  CB   . PHE   A 1 191 ? 28.36  -30.217 6.521   1   24.26  ? 190 PHE   A CB   1 1 
ATOM   1389 C  CG   . PHE   A 1 191 ? 26.909 -30.358 6.931   1   25.38  ? 190 PHE   A CG   1 1 
ATOM   1390 C  CD1  . PHE   A 1 191 ? 26.367 -31.602 7.208   1   26.47  ? 190 PHE   A CD1  1 1 
ATOM   1391 C  CD2  . PHE   A 1 191 ? 26.105 -29.243 7.097   1   25.63  ? 190 PHE   A CD2  1 1 
ATOM   1392 C  CE1  . PHE   A 1 191 ? 25.044 -31.73  7.625   1   27     ? 190 PHE   A CE1  1 1 
ATOM   1393 C  CE2  . PHE   A 1 191 ? 24.787 -29.376 7.522   1   26.48  ? 190 PHE   A CE2  1 1 
ATOM   1394 C  CZ   . PHE   A 1 191 ? 24.268 -30.617 7.798   1   26.43  ? 190 PHE   A CZ   1 1 
ATOM   1395 N  N    . ALA   A 1 192 ? 31.042 -29.861 4.881   1   24.04  ? 191 ALA   A N    1 1 
ATOM   1396 C  CA   . ALA   A 1 192 ? 32.161 -29.086 4.374   1   24.43  ? 191 ALA   A CA   1 1 
ATOM   1397 C  C    . ALA   A 1 192 ? 32.256 -29.252 2.833   1   26.04  ? 191 ALA   A C    1 1 
ATOM   1398 O  O    . ALA   A 1 192 ? 32.521 -28.282 2.134   1   26.96  ? 191 ALA   A O    1 1 
ATOM   1399 C  CB   . ALA   A 1 192 ? 33.446 -29.542 5.047   1   23.39  ? 191 ALA   A CB   1 1 
ATOM   1400 N  N    . ALA   A 1 193 ? 32.036 -30.461 2.312   1   26.27  ? 192 ALA   A N    1 1 
ATOM   1401 C  CA   . ALA   A 1 193 ? 32.065 -30.704 0.869   1   26.95  ? 192 ALA   A CA   1 1 
ATOM   1402 C  C    . ALA   A 1 193 ? 30.926 -29.949 0.151   1   27.91  ? 192 ALA   A C    1 1 
ATOM   1403 O  O    . ALA   A 1 193 ? 31.165 -29.338 -0.882  1   28.91  ? 192 ALA   A O    1 1 
ATOM   1404 C  CB   . ALA   A 1 193 ? 31.999 -32.205 0.589   1   26.51  ? 192 ALA   A CB   1 1 
ATOM   1405 N  N    . VAL   A 1 194 ? 29.702 -29.945 0.71    1   27.89  ? 193 VAL   A N    1 1 
ATOM   1406 C  CA   . VAL   A 1 194 ? 28.569 -29.218 0.11    1   27.84  ? 193 VAL   A CA   1 1 
ATOM   1407 C  C    . VAL   A 1 194 ? 28.854 -27.691 0.107   1   28.31  ? 193 VAL   A C    1 1 
ATOM   1408 O  O    . VAL   A 1 194 ? 28.535 -26.987 -0.846  1   29.63  ? 193 VAL   A O    1 1 
ATOM   1409 C  CB   . VAL   A 1 194 ? 27.252 -29.545 0.859   1   27.89  ? 193 VAL   A CB   1 1 
ATOM   1410 C  CG1  . VAL   A 1 194 ? 26.134 -28.61  0.442   1   28.4   ? 193 VAL   A CG1  1 1 
ATOM   1411 C  CG2  . VAL   A 1 194 ? 26.839 -30.988 0.655   1   27.63  ? 193 VAL   A CG2  1 1 
ATOM   1412 N  N    . GLY   A 1 195 ? 29.457 -27.205 1.168   1   27.63  ? 194 GLY   A N    1 1 
ATOM   1413 C  CA   . GLY   A 1 195 ? 29.796 -25.799 1.293   1   27.5   ? 194 GLY   A CA   1 1 
ATOM   1414 C  C    . GLY   A 1 195 ? 30.866 -25.373 0.326   1   27.1   ? 194 GLY   A C    1 1 
ATOM   1415 O  O    . GLY   A 1 195 ? 30.808 -24.261 -0.194  1   27.39  ? 194 GLY   A O    1 1 
ATOM   1416 N  N    . PHE   A 1 196 ? 31.85  -26.257 0.073   1   26.5   ? 195 PHE   A N    1 1 
ATOM   1417 C  CA   . PHE   A 1 196 ? 32.92  -26.008 -0.879  1   26.94  ? 195 PHE   A CA   1 1 
ATOM   1418 C  C    . PHE   A 1 196 ? 32.29  -25.908 -2.286  1   29.17  ? 195 PHE   A C    1 1 
ATOM   1419 O  O    . PHE   A 1 196 ? 32.607 -24.988 -3.042  1   29.3   ? 195 PHE   A O    1 1 
ATOM   1420 C  CB   . PHE   A 1 196 ? 33.968 -27.136 -0.817  1   26.1   ? 195 PHE   A CB   1 1 
ATOM   1421 C  CG   . PHE   A 1 196 ? 34.972 -27.144 -1.949  1   26.56  ? 195 PHE   A CG   1 1 
ATOM   1422 C  CD1  . PHE   A 1 196 ? 36.029 -26.252 -1.969  1   26.87  ? 195 PHE   A CD1  1 1 
ATOM   1423 C  CD2  . PHE   A 1 196 ? 34.827 -28.006 -3.027  1   27.28  ? 195 PHE   A CD2  1 1 
ATOM   1424 C  CE1  . PHE   A 1 196 ? 36.929 -26.237 -3.031  1   26.97  ? 195 PHE   A CE1  1 1 
ATOM   1425 C  CE2  . PHE   A 1 196 ? 35.741 -27.993 -4.081  1   26.88  ? 195 PHE   A CE2  1 1 
ATOM   1426 C  CZ   . PHE   A 1 196 ? 36.785 -27.116 -4.07   1   26.36  ? 195 PHE   A CZ   1 1 
ATOM   1427 N  N    . HIS   A 1 197 ? 31.367 -26.832 -2.619  1   30.38  ? 196 HIS   A N    1 1 
ATOM   1428 C  CA   . HIS   A 1 197 ? 30.667 -26.802 -3.906  1   31.49  ? 196 HIS   A CA   1 1 
ATOM   1429 C  C    . HIS   A 1 197 ? 29.843 -25.491 -4.063  1   33.1   ? 196 HIS   A C    1 1 
ATOM   1430 O  O    . HIS   A 1 197 ? 29.952 -24.828 -5.091  1   33.45  ? 196 HIS   A O    1 1 
ATOM   1431 C  CB   . HIS   A 1 197 ? 29.806 -28.069 -4.078  1   31.23  ? 196 HIS   A CB   1 1 
ATOM   1432 C  CG   . HIS   A 1 197 ? 28.731 -27.949 -5.108  1   32.05  ? 196 HIS   A CG   1 1 
ATOM   1433 N  ND1  . HIS   A 1 197 ? 29.021 -27.971 -6.464  1   33.47  ? 196 HIS   A ND1  1 1 
ATOM   1434 C  CD2  . HIS   A 1 197 ? 27.399 -27.794 -4.949  1   32.74  ? 196 HIS   A CD2  1 1 
ATOM   1435 C  CE1  . HIS   A 1 197 ? 27.862 -27.831 -7.083  1   33.39  ? 196 HIS   A CE1  1 1 
ATOM   1436 N  NE2  . HIS   A 1 197 ? 26.856 -27.724 -6.217  1   33.29  ? 196 HIS   A NE2  1 1 
ATOM   1437 N  N    . ARG   A 1 198 ? 29.087 -25.093 -3.04   1   34.06  ? 197 ARG   A N    1 1 
ATOM   1438 C  CA   . ARG   A 1 198 ? 28.287 -23.86  -3.102  1   36.14  ? 197 ARG   A CA   1 1 
ATOM   1439 C  C    . ARG   A 1 198 ? 29.12  -22.572 -3.273  1   35.51  ? 197 ARG   A C    1 1 
ATOM   1440 O  O    . ARG   A 1 198 ? 28.794 -21.731 -4.125  1   34.54  ? 197 ARG   A O    1 1 
ATOM   1441 C  CB   . ARG   A 1 198 ? 27.369 -23.745 -1.861  1   40.25  ? 197 ARG   A CB   1 1 
ATOM   1442 C  CG   . ARG   A 1 198 ? 25.984 -24.348 -2.104  1   47.93  ? 197 ARG   A CG   1 1 
ATOM   1443 C  CD   . ARG   A 1 198 ? 25.424 -25.046 -0.871  1   54.3   ? 197 ARG   A CD   1 1 
ATOM   1444 N  NE   . ARG   A 1 198 ? 24.266 -25.891 -1.19   1   59.54  ? 197 ARG   A NE   1 1 
ATOM   1445 C  CZ   . ARG   A 1 198 ? 23.021 -25.642 -0.791  1   62.41  ? 197 ARG   A CZ   1 1 
ATOM   1446 N  NH1  . ARG   A 1 198 ? 22.752 -24.561 -0.059  1   61.87  ? 197 ARG   A NH1  1 1 
ATOM   1447 N  NH2  . ARG   A 1 198 ? 22.031 -26.462 -1.133  1   61.93  ? 197 ARG   A NH2  1 1 
ATOM   1448 N  N    . ALA   A 1 199 ? 30.192 -22.42  -2.448  1   34.96  ? 198 ALA   A N    1 1 
ATOM   1449 C  CA   . ALA   A 1 199 ? 31.047 -21.239 -2.504  1   34.64  ? 198 ALA   A CA   1 1 
ATOM   1450 C  C    . ALA   A 1 199 ? 31.847 -21.194 -3.81   1   34.37  ? 198 ALA   A C    1 1 
ATOM   1451 O  O    . ALA   A 1 199 ? 32.028 -20.113 -4.385  1   34.4   ? 198 ALA   A O    1 1 
ATOM   1452 C  CB   . ALA   A 1 199 ? 31.961 -21.179 -1.296  1   34.31  ? 198 ALA   A CB   1 1 
ATOM   1453 N  N    . LEU   A 1 200 ? 32.272 -22.377 -4.307  1   33.97  ? 199 LEU   A N    1 1 
ATOM   1454 C  CA   . LEU   A 1 200 ? 32.98  -22.493 -5.584  1   33.31  ? 199 LEU   A CA   1 1 
ATOM   1455 C  C    . LEU   A 1 200 ? 32.057 -22.034 -6.706  1   33.87  ? 199 LEU   A C    1 1 
ATOM   1456 O  O    . LEU   A 1 200 ? 32.417 -21.104 -7.416  1   34.97  ? 199 LEU   A O    1 1 
ATOM   1457 C  CB   . LEU   A 1 200 ? 33.469 -23.926 -5.819  1   32.49  ? 199 LEU   A CB   1 1 
ATOM   1458 C  CG   . LEU   A 1 200 ? 34.36  -24.135 -7.027  1   33.41  ? 199 LEU   A CG   1 1 
ATOM   1459 C  CD1  . LEU   A 1 200 ? 35.597 -23.223 -6.993  1   33.79  ? 199 LEU   A CD1  1 1 
ATOM   1460 C  CD2  . LEU   A 1 200 ? 34.745 -25.599 -7.174  1   33.49  ? 199 LEU   A CD2  1 1 
ATOM   1461 N  N    . THR   A 1 201 ? 30.828 -22.59  -6.796  1   32.89  ? 200 THR   A N    1 1 
ATOM   1462 C  CA   . THR   A 1 201 ? 29.816 -22.196 -7.775  1   32.56  ? 200 THR   A CA   1 1 
ATOM   1463 C  C    . THR   A 1 201 ? 29.6   -20.67  -7.807  1   33.45  ? 200 THR   A C    1 1 
ATOM   1464 O  O    . THR   A 1 201 ? 29.623 -20.07  -8.871  1   33.71  ? 200 THR   A O    1 1 
ATOM   1465 C  CB   . THR   A 1 201 ? 28.503 -22.917 -7.473  1   32.59  ? 200 THR   A CB   1 1 
ATOM   1466 O  OG1  . THR   A 1 201 ? 28.743 -24.31  -7.405  1   33.61  ? 200 THR   A OG1  1 1 
ATOM   1467 C  CG2  . THR   A 1 201 ? 27.455 -22.655 -8.497  1   32.33  ? 200 THR   A CG2  1 1 
ATOM   1468 N  N    . LEU   A 1 202 ? 29.451 -20.038 -6.642  1   34.02  ? 201 LEU   A N    1 1 
ATOM   1469 C  CA   . LEU   A 1 202 ? 29.225 -18.605 -6.535  1   34.53  ? 201 LEU   A CA   1 1 
ATOM   1470 C  C    . LEU   A 1 202 ? 30.434 -17.77  -6.915  1   35.58  ? 201 LEU   A C    1 1 
ATOM   1471 O  O    . LEU   A 1 202 ? 30.261 -16.746 -7.575  1   36.2   ? 201 LEU   A O    1 1 
ATOM   1472 C  CB   . LEU   A 1 202 ? 28.725 -18.255 -5.132  1   34.47  ? 201 LEU   A CB   1 1 
ATOM   1473 C  CG   . LEU   A 1 202 ? 27.313 -18.744 -4.826  1   35.99  ? 201 LEU   A CG   1 1 
ATOM   1474 C  CD1  . LEU   A 1 202 ? 26.931 -18.441 -3.422  1   36.31  ? 201 LEU   A CD1  1 1 
ATOM   1475 C  CD2  . LEU   A 1 202 ? 26.3   -18.13  -5.74   1   36.54  ? 201 LEU   A CD2  1 1 
ATOM   1476 N  N    . GLU   A 1 203 ? 31.653 -18.206 -6.52   1   35.12  ? 202 GLU   A N    1 1 
ATOM   1477 C  CA   . GLU   A 1 203 ? 32.894 -17.502 -6.824  1   35.03  ? 202 GLU   A CA   1 1 
ATOM   1478 C  C    . GLU   A 1 203 ? 33.213 -17.504 -8.331  1   35.13  ? 202 GLU   A C    1 1 
ATOM   1479 O  O    . GLU   A 1 203 ? 33.539 -16.442 -8.871  1   35.68  ? 202 GLU   A O    1 1 
ATOM   1480 C  CB   . GLU   A 1 203 ? 34.054 -18.09  -6.03   1   36.9   ? 202 GLU   A CB   1 1 
ATOM   1481 C  CG   . GLU   A 1 203 ? 35.383 -17.416 -6.311  1   41.57  ? 202 GLU   A CG   1 1 
ATOM   1482 C  CD   . GLU   A 1 203 ? 36.489 -17.883 -5.392  1   47.11  ? 202 GLU   A CD   1 1 
ATOM   1483 O  OE1  . GLU   A 1 203 ? 37.442 -18.549 -5.86   1   48.95  ? 202 GLU   A OE1  1 1 
ATOM   1484 O  OE2  . GLU   A 1 203 ? 36.382 -17.594 -4.184  1   48.68  ? 202 GLU   A OE2  1 1 
ATOM   1485 N  N    . LEU   A 1 204 ? 33.09  -18.67  -9.019  1   34.05  ? 203 LEU   A N    1 1 
ATOM   1486 C  CA   . LEU   A 1 204 ? 33.308 -18.768 -10.468 1   33.78  ? 203 LEU   A CA   1 1 
ATOM   1487 C  C    . LEU   A 1 204 ? 32.386 -17.762 -11.207 1   36.57  ? 203 LEU   A C    1 1 
ATOM   1488 O  O    . LEU   A 1 204 ? 32.825 -17.043 -12.104 1   37.14  ? 203 LEU   A O    1 1 
ATOM   1489 C  CB   . LEU   A 1 204 ? 33     -20.2   -10.946 1   31.59  ? 203 LEU   A CB   1 1 
ATOM   1490 C  CG   . LEU   A 1 204 ? 33.973 -21.271 -10.52  1   30.37  ? 203 LEU   A CG   1 1 
ATOM   1491 C  CD1  . LEU   A 1 204 ? 33.462 -22.659 -10.863 1   30.1   ? 203 LEU   A CD1  1 1 
ATOM   1492 C  CD2  . LEU   A 1 204 ? 35.335 -21.03  -11.111 1   29.78  ? 203 LEU   A CD2  1 1 
ATOM   1493 N  N    . GLN   A 1 205 ? 31.123 -17.678 -10.771 1   38.2   ? 204 GLN   A N    1 1 
ATOM   1494 C  CA   . GLN   A 1 205 ? 30.104 -16.799 -11.333 1   39.84  ? 204 GLN   A CA   1 1 
ATOM   1495 C  C    . GLN   A 1 205 ? 30.473 -15.343 -11.035 1   40.46  ? 204 GLN   A C    1 1 
ATOM   1496 O  O    . GLN   A 1 205 ? 30.459 -14.532 -11.95  1   41.13  ? 204 GLN   A O    1 1 
ATOM   1497 C  CB   . GLN   A 1 205 ? 28.75  -17.198 -10.742 1   43.06  ? 204 GLN   A CB   1 1 
ATOM   1498 C  CG   . GLN   A 1 205 ? 27.545 -16.345 -11.073 1   50.05  ? 204 GLN   A CG   1 1 
ATOM   1499 C  CD   . GLN   A 1 205 ? 26.534 -16.563 -9.96   1   62.31  ? 204 GLN   A CD   1 1 
ATOM   1500 O  OE1  . GLN   A 1 205 ? 26.537 -15.865 -8.935  1   65.61  ? 204 GLN   A OE1  1 1 
ATOM   1501 N  NE2  . GLN   A 1 205 ? 25.697 -17.589 -10.079 1   65.76  ? 204 GLN   A NE2  1 1 
ATOM   1502 N  N    . ALA   A 1 206 ? 30.923 -15.034 -9.81   1   40.07  ? 205 ALA   A N    1 1 
ATOM   1503 C  CA   . ALA   A 1 206 ? 31.352 -13.681 -9.445  1   40.41  ? 205 ALA   A CA   1 1 
ATOM   1504 C  C    . ALA   A 1 206 ? 32.553 -13.222 -10.278 1   41.28  ? 205 ALA   A C    1 1 
ATOM   1505 O  O    . ALA   A 1 206 ? 32.673 -12.026 -10.585 1   42.13  ? 205 ALA   A O    1 1 
ATOM   1506 C  CB   . ALA   A 1 206 ? 31.71  -13.622 -7.966  1   40.3   ? 205 ALA   A CB   1 1 
ATOM   1507 N  N    . LEU   A 1 207 ? 33.448 -14.157 -10.634 1   40.44  ? 206 LEU   A N    1 1 
ATOM   1508 C  CA   . LEU   A 1 207 ? 34.638 -13.84  -11.416 1   40.37  ? 206 LEU   A CA   1 1 
ATOM   1509 C  C    . LEU   A 1 207 ? 34.411 -13.791 -12.929 1   41.28  ? 206 LEU   A C    1 1 
ATOM   1510 O  O    . LEU   A 1 207 ? 35.36  -13.546 -13.682 1   41.13  ? 206 LEU   A O    1 1 
ATOM   1511 C  CB   . LEU   A 1 207 ? 35.758 -14.841 -11.102 1   40.78  ? 206 LEU   A CB   1 1 
ATOM   1512 C  CG   . LEU   A 1 207 ? 36.292 -14.84  -9.672  1   42.13  ? 206 LEU   A CG   1 1 
ATOM   1513 C  CD1  . LEU   A 1 207 ? 37.287 -15.969 -9.467  1   42.77  ? 206 LEU   A CD1  1 1 
ATOM   1514 C  CD2  . LEU   A 1 207 ? 36.925 -13.523 -9.345  1   42.15  ? 206 LEU   A CD2  1 1 
ATOM   1515 N  N    . GLY   A 1 208 ? 33.173 -14.009 -13.371 1   41.49  ? 207 GLY   A N    1 1 
ATOM   1516 C  CA   . GLY   A 1 208 ? 32.829 -14.016 -14.779 1   41.4   ? 207 GLY   A CA   1 1 
ATOM   1517 C  C    . GLY   A 1 208 ? 33.29  -15.26  -15.509 1   42.44  ? 207 GLY   A C    1 1 
ATOM   1518 O  O    . GLY   A 1 208 ? 33.372 -15.243 -16.731 1   44.04  ? 207 GLY   A O    1 1 
ATOM   1519 N  N    . ILE   A 1 209 ? 33.6   -16.346 -14.79  1   42.4   ? 208 ILE   A N    1 1 
ATOM   1520 C  CA   . ILE   A 1 209 ? 34.031 -17.601 -15.388 1   42.97  ? 208 ILE   A CA   1 1 
ATOM   1521 C  C    . ILE   A 1 209 ? 32.801 -18.462 -15.684 1   44.71  ? 208 ILE   A C    1 1 
ATOM   1522 O  O    . ILE   A 1 209 ? 32.328 -19.221 -14.836 1   46.05  ? 208 ILE   A O    1 1 
ATOM   1523 C  CB   . ILE   A 1 209 ? 35.066 -18.312 -14.494 1   42.73  ? 208 ILE   A CB   1 1 
ATOM   1524 C  CG1  . ILE   A 1 209 ? 36.274 -17.405 -14.276 1   43.61  ? 208 ILE   A CG1  1 1 
ATOM   1525 C  CG2  . ILE   A 1 209 ? 35.482 -19.668 -15.076 1   43     ? 208 ILE   A CG2  1 1 
ATOM   1526 C  CD1  . ILE   A 1 209 ? 37.172 -17.873 -13.188 1   45.31  ? 208 ILE   A CD1  1 1 
ATOM   1527 N  N    . THR   A 1 210 ? 32.276 -18.326 -16.893 1   44.57  ? 209 THR   A N    1 1 
ATOM   1528 C  CA   . THR   A 1 210 ? 31.068 -18.995 -17.358 1   44.58  ? 209 THR   A CA   1 1 
ATOM   1529 C  C    . THR   A 1 210 ? 31.241 -20.447 -17.828 1   43.51  ? 209 THR   A C    1 1 
ATOM   1530 O  O    . THR   A 1 210 ? 30.27  -21.196 -17.846 1   43.98  ? 209 THR   A O    1 1 
ATOM   1531 C  CB   . THR   A 1 210 ? 30.465 -18.141 -18.482 1   46.32  ? 209 THR   A CB   1 1 
ATOM   1532 O  OG1  . THR   A 1 210 ? 31.45  -17.959 -19.514 1   46.9   ? 209 THR   A OG1  1 1 
ATOM   1533 C  CG2  . THR   A 1 210 ? 30     -16.782 -17.973 1   46.99  ? 209 THR   A CG2  1 1 
ATOM   1534 N  N    . GLY   A 1 211 ? 32.449 -20.824 -18.211 1   41.83  ? 210 GLY   A N    1 1 
ATOM   1535 C  CA   . GLY   A 1 211 ? 32.709 -22.134 -18.798 1   40.89  ? 210 GLY   A CA   1 1 
ATOM   1536 C  C    . GLY   A 1 211 ? 32.989 -23.289 -17.871 1   39.22  ? 210 GLY   A C    1 1 
ATOM   1537 O  O    . GLY   A 1 211 ? 33.081 -24.425 -18.333 1   39.33  ? 210 GLY   A O    1 1 
ATOM   1538 N  N    . ILE   A 1 212 ? 33.171 -23.02  -16.575 1   37.67  ? 211 ILE   A N    1 1 
ATOM   1539 C  CA   . ILE   A 1 212 ? 33.441 -24.071 -15.591 1   36.22  ? 211 ILE   A CA   1 1 
ATOM   1540 C  C    . ILE   A 1 212 ? 32.171 -24.438 -14.811 1   35.43  ? 211 ILE   A C    1 1 
ATOM   1541 O  O    . ILE   A 1 212 ? 31.633 -23.63  -14.054 1   36.13  ? 211 ILE   A O    1 1 
ATOM   1542 C  CB   . ILE   A 1 212 ? 34.626 -23.713 -14.656 1   36.36  ? 211 ILE   A CB   1 1 
ATOM   1543 C  CG1  . ILE   A 1 212 ? 35.897 -23.447 -15.468 1   37.12  ? 211 ILE   A CG1  1 1 
ATOM   1544 C  CG2  . ILE   A 1 212 ? 34.84  -24.809 -13.614 1   36.75  ? 211 ILE   A CG2  1 1 
ATOM   1545 C  CD1  . ILE   A 1 212 ? 37.063 -22.994 -14.655 1   38.95  ? 211 ILE   A CD1  1 1 
ATOM   1546 N  N    . LYS   A 1 213 ? 31.686 -25.66  -15.012 1   33.99  ? 212 LYS   A N    1 1 
ATOM   1547 C  CA   . LYS   A 1 213 ? 30.469 -26.131 -14.353 1   32.91  ? 212 LYS   A CA   1 1 
ATOM   1548 C  C    . LYS   A 1 213 ? 30.776 -26.839 -13.043 1   32.2   ? 212 LYS   A C    1 1 
ATOM   1549 O  O    . LYS   A 1 213 ? 31.911 -27.23  -12.799 1   31.94  ? 212 LYS   A O    1 1 
ATOM   1550 C  CB   . LYS   A 1 213 ? 29.652 -27.034 -15.295 1   33.87  ? 212 LYS   A CB   1 1 
ATOM   1551 C  CG   . LYS   A 1 213 ? 29.441 -26.433 -16.691 1   36.37  ? 212 LYS   A CG   1 1 
ATOM   1552 C  CD   . LYS   A 1 213 ? 28.546 -25.218 -16.595 1   40.16  ? 212 LYS   A CD   1 1 
ATOM   1553 C  CE   . LYS   A 1 213 ? 28.581 -24.364 -17.828 1   44.68  ? 212 LYS   A CE   1 1 
ATOM   1554 N  NZ   . LYS   A 1 213 ? 27.497 -23.338 -17.783 1   48.55  ? 212 LYS   A NZ   1 1 
ATOM   1555 N  N    . THR   A 1 214 ? 29.779 -26.941 -12.159 1   31.89  ? 213 THR   A N    1 1 
ATOM   1556 C  CA   . THR   A 1 214 ? 29.946 -27.607 -10.874 1   31.83  ? 213 THR   A CA   1 1 
ATOM   1557 C  C    . THR   A 1 214 ? 28.746 -28.526 -10.63  1   32     ? 213 THR   A C    1 1 
ATOM   1558 O  O    . THR   A 1 214 ? 27.618 -28.169 -10.965 1   32.29  ? 213 THR   A O    1 1 
ATOM   1559 C  CB   . THR   A 1 214 ? 30.072 -26.578 -9.729  1   32.12  ? 213 THR   A CB   1 1 
ATOM   1560 O  OG1  . THR   A 1 214 ? 28.894 -25.76  -9.687  1   32.76  ? 213 THR   A OG1  1 1 
ATOM   1561 C  CG2  . THR   A 1 214 ? 31.343 -25.715 -9.819  1   31.78  ? 213 THR   A CG2  1 1 
ATOM   1562 N  N    . SER   A 1 215 ? 28.987 -29.7   -10.046 1   31.36  ? 214 SER   A N    1 1 
ATOM   1563 C  CA   . SER   A 1 215 ? 27.922 -30.636 -9.68   1   31.12  ? 214 SER   A CA   1 1 
ATOM   1564 C  C    . SER   A 1 215 ? 28.244 -31.243 -8.312  1   31.16  ? 214 SER   A C    1 1 
ATOM   1565 O  O    . SER   A 1 215 ? 29.407 -31.496 -8.009  1   31.48  ? 214 SER   A O    1 1 
ATOM   1566 C  CB   . SER   A 1 215 ? 27.801 -31.758 -10.701 1   31.24  ? 214 SER   A CB   1 1 
ATOM   1567 O  OG   . SER   A 1 215 ? 27.133 -31.341 -11.88  1   32.21  ? 214 SER   A OG   1 1 
ATOM   1568 N  N    . CYS   A 1 216 ? 27.228 -31.489 -7.499  1   30.58  ? 215 CYS   A N    1 1 
ATOM   1569 C  CA   . CYS   A 1 216 ? 27.426 -32.106 -6.19   1   30.85  ? 215 CYS   A CA   1 1 
ATOM   1570 C  C    . CYS   A 1 216 ? 26.579 -33.344 -6.179  1   30.8   ? 215 CYS   A C    1 1 
ATOM   1571 O  O    . CYS   A 1 216 ? 25.385 -33.25  -6.454  1   30.95  ? 215 CYS   A O    1 1 
ATOM   1572 C  CB   . CYS   A 1 216 ? 27.03  -31.151 -5.069  1   30.87  ? 215 CYS   A CB   1 1 
ATOM   1573 S  SG   . CYS   A 1 216 ? 27.626 -31.636 -3.424  1   31.69  ? 215 CYS   A SG   1 1 
ATOM   1574 N  N    . LEU   A 1 217 ? 27.177 -34.502 -5.924  1   30.33  ? 216 LEU   A N    1 1 
ATOM   1575 C  CA   . LEU   A 1 217 ? 26.407 -35.743 -5.863  1   30.86  ? 216 LEU   A CA   1 1 
ATOM   1576 C  C    . LEU   A 1 217 ? 26.118 -36.063 -4.414  1   30.91  ? 216 LEU   A C    1 1 
ATOM   1577 O  O    . LEU   A 1 217 ? 27.044 -36.231 -3.63   1   31.2   ? 216 LEU   A O    1 1 
ATOM   1578 C  CB   . LEU   A 1 217 ? 27.163 -36.904 -6.508  1   31.15  ? 216 LEU   A CB   1 1 
ATOM   1579 C  CG   . LEU   A 1 217 ? 26.414 -38.21  -6.52   1   32.21  ? 216 LEU   A CG   1 1 
ATOM   1580 C  CD1  . LEU   A 1 217 ? 25.245 -38.148 -7.476  1   32.51  ? 216 LEU   A CD1  1 1 
ATOM   1581 C  CD2  . LEU   A 1 217 ? 27.347 -39.351 -6.855  1   33.11  ? 216 LEU   A CD2  1 1 
ATOM   1582 N  N    . CYS   A 1 218 ? 24.841 -36.139 -4.053  1   30.54  ? 217 CYS   A N    1 1 
ATOM   1583 C  CA   . CYS   A 1 218 ? 24.409 -36.444 -2.698  1   30.94  ? 217 CYS   A CA   1 1 
ATOM   1584 C  C    . CYS   A 1 218 ? 23.519 -37.687 -2.641  1   31.84  ? 217 CYS   A C    1 1 
ATOM   1585 O  O    . CYS   A 1 218 ? 22.298 -37.564 -2.523  1   32.22  ? 217 CYS   A O    1 1 
ATOM   1586 C  CB   . CYS   A 1 218 ? 23.707 -35.242 -2.081  1   31.08  ? 217 CYS   A CB   1 1 
ATOM   1587 S  SG   . CYS   A 1 218 ? 24.765 -33.793 -1.906  1   35.28  ? 217 CYS   A SG   1 1 
ATOM   1588 N  N    . PRO   A 1 219 ? 24.096 -38.894 -2.708  1   31.98  ? 218 PRO   A N    1 1 
ATOM   1589 C  CA   . PRO   A 1 219 ? 23.263 -40.099 -2.598  1   32.8   ? 218 PRO   A CA   1 1 
ATOM   1590 C  C    . PRO   A 1 219 ? 22.941 -40.459 -1.14   1   34.94  ? 218 PRO   A C    1 1 
ATOM   1591 O  O    . PRO   A 1 219 ? 23.657 -40.082 -0.205  1   33.84  ? 218 PRO   A O    1 1 
ATOM   1592 C  CB   . PRO   A 1 219 ? 24.146 -41.197 -3.212  1   32.96  ? 218 PRO   A CB   1 1 
ATOM   1593 C  CG   . PRO   A 1 219 ? 25.47  -40.521 -3.602  1   32.86  ? 218 PRO   A CG   1 1 
ATOM   1594 C  CD   . PRO   A 1 219 ? 25.522 -39.232 -2.861  1   31.23  ? 218 PRO   A CD   1 1 
ATOM   1595 N  N    . VAL   A 1 220 ? 21.859 -41.233 -0.95   1   36.92  ? 219 VAL   A N    1 1 
ATOM   1596 C  CA   . VAL   A 1 220 ? 21.529 -41.823 0.34    1   38.34  ? 219 VAL   A CA   1 1 
ATOM   1597 C  C    . VAL   A 1 220 ? 22.403 -43.132 0.415   1   40.08  ? 219 VAL   A C    1 1 
ATOM   1598 O  O    . VAL   A 1 220 ? 23.375 -43.246 -0.338  1   40.68  ? 219 VAL   A O    1 1 
ATOM   1599 C  CB   . VAL   A 1 220 ? 19.997 -42.057 0.493   1   39.06  ? 219 VAL   A CB   1 1 
ATOM   1600 C  CG1  . VAL   A 1 220 ? 19.227 -40.756 0.356   1   39.85  ? 219 VAL   A CG1  1 1 
ATOM   1601 C  CG2  . VAL   A 1 220 ? 19.5   -43.09  -0.498  1   38.99  ? 219 VAL   A CG2  1 1 
ATOM   1602 N  N    . PHE   A 1 221 ? 22.13  -44.076 1.324   1   40.91  ? 220 PHE   A N    1 1 
ATOM   1603 C  CA   . PHE   A 1 221 ? 22.907 -45.3   1.431   1   42.08  ? 220 PHE   A CA   1 1 
ATOM   1604 C  C    . PHE   A 1 221 ? 23.021 -46.084 0.105   1   42.7   ? 220 PHE   A C    1 1 
ATOM   1605 O  O    . PHE   A 1 221 ? 22.01  -46.478 -0.493  1   42.92  ? 220 PHE   A O    1 1 
ATOM   1606 C  CB   . PHE   A 1 221 ? 22.331 -46.183 2.521   1   42.67  ? 220 PHE   A CB   1 1 
ATOM   1607 C  CG   . PHE   A 1 221 ? 23.169 -47.392 2.796   1   44.26  ? 220 PHE   A CG   1 1 
ATOM   1608 C  CD1  . PHE   A 1 221 ? 22.729 -48.653 2.441   1   45.26  ? 220 PHE   A CD1  1 1 
ATOM   1609 C  CD2  . PHE   A 1 221 ? 24.416 -47.27  3.368   1   45.74  ? 220 PHE   A CD2  1 1 
ATOM   1610 C  CE1  . PHE   A 1 221 ? 23.508 -49.768 2.682   1   46.07  ? 220 PHE   A CE1  1 1 
ATOM   1611 C  CE2  . PHE   A 1 221 ? 25.193 -48.382 3.595   1   46.77  ? 220 PHE   A CE2  1 1 
ATOM   1612 C  CZ   . PHE   A 1 221 ? 24.731 -49.627 3.268   1   46.26  ? 220 PHE   A CZ   1 1 
ATOM   1613 N  N    . VAL   A 1 222 ? 24.259 -46.298 -0.348  1   42.36  ? 221 VAL   A N    1 1 
ATOM   1614 C  CA   . VAL   A 1 222 ? 24.57  -47.089 -1.537  1   42.63  ? 221 VAL   A CA   1 1 
ATOM   1615 C  C    . VAL   A 1 222 ? 25.24  -48.373 -1.037  1   43.74  ? 221 VAL   A C    1 1 
ATOM   1616 O  O    . VAL   A 1 222 ? 26.135 -48.298 -0.192  1   44.47  ? 221 VAL   A O    1 1 
ATOM   1617 C  CB   . VAL   A 1 222 ? 25.488 -46.344 -2.539  1   42.25  ? 221 VAL   A CB   1 1 
ATOM   1618 C  CG1  . VAL   A 1 222 ? 25.575 -47.105 -3.846  1   42.15  ? 221 VAL   A CG1  1 1 
ATOM   1619 C  CG2  . VAL   A 1 222 ? 25.011 -44.922 -2.78   1   42.24  ? 221 VAL   A CG2  1 1 
ATOM   1620 N  N    . ASN   A 1 223 ? 24.81  -49.534 -1.545  1   43.81  ? 222 ASN   A N    1 1 
ATOM   1621 C  CA   . ASN   A 1 223 ? 25.318 -50.854 -1.169  1   44.24  ? 222 ASN   A CA   1 1 
ATOM   1622 C  C    . ASN   A 1 223 ? 26.734 -51.108 -1.737  1   44.21  ? 222 ASN   A C    1 1 
ATOM   1623 O  O    . ASN   A 1 223 ? 26.895 -51.919 -2.643  1   45.31  ? 222 ASN   A O    1 1 
ATOM   1624 C  CB   . ASN   A 1 223 ? 24.318 -51.897 -1.687  1   46.28  ? 222 ASN   A CB   1 1 
ATOM   1625 C  CG   . ASN   A 1 223 ? 24.726 -53.345 -1.549  1   51.67  ? 222 ASN   A CG   1 1 
ATOM   1626 O  OD1  . ASN   A 1 223 ? 25.187 -53.796 -0.492  1   54.22  ? 222 ASN   A OD1  1 1 
ATOM   1627 N  ND2  . ASN   A 1 223 ? 24.566 -54.106 -2.628  1   52.58  ? 222 ASN   A ND2  1 1 
ATOM   1628 N  N    . THR   A 1 224 ? 27.755 -50.404 -1.241  1   42.91  ? 223 THR   A N    1 1 
ATOM   1629 C  CA   . THR   A 1 224 ? 29.135 -50.558 -1.735  1   42     ? 223 THR   A CA   1 1 
ATOM   1630 C  C    . THR   A 1 224 ? 30.1   -51.169 -0.701  1   41.5   ? 223 THR   A C    1 1 
ATOM   1631 O  O    . THR   A 1 224 ? 31.267 -51.403 -1.024  1   41.2   ? 223 THR   A O    1 1 
ATOM   1632 C  CB   . THR   A 1 224 ? 29.714 -49.185 -2.104  1   42.57  ? 223 THR   A CB   1 1 
ATOM   1633 O  OG1  . THR   A 1 224 ? 29.687 -48.358 -0.929  1   43.45  ? 223 THR   A OG1  1 1 
ATOM   1634 C  CG2  . THR   A 1 224 ? 28.981 -48.524 -3.246  1   42.24  ? 223 THR   A CG2  1 1 
ATOM   1635 N  N    . GLY   A 1 225 ? 29.626 -51.349 0.533   1   41.09  ? 224 GLY   A N    1 1 
ATOM   1636 C  CA   . GLY   A 1 225 ? 30.423 -51.815 1.657   1   41     ? 224 GLY   A CA   1 1 
ATOM   1637 C  C    . GLY   A 1 225 ? 31.121 -50.684 2.398   1   40.66  ? 224 GLY   A C    1 1 
ATOM   1638 O  O    . GLY   A 1 225 ? 31.881 -50.954 3.323   1   40.5   ? 224 GLY   A O    1 1 
ATOM   1639 N  N    . PHE   A 1 226 ? 30.898 -49.405 1.98    1   40.32  ? 225 PHE   A N    1 1 
ATOM   1640 C  CA   . PHE   A 1 226 ? 31.477 -48.217 2.597   1   40.72  ? 225 PHE   A CA   1 1 
ATOM   1641 C  C    . PHE   A 1 226 ? 31.117 -48.169 4.094   1   44.07  ? 225 PHE   A C    1 1 
ATOM   1642 O  O    . PHE   A 1 226 ? 31.991 -47.929 4.93    1   43.87  ? 225 PHE   A O    1 1 
ATOM   1643 C  CB   . PHE   A 1 226 ? 31.024 -46.971 1.838   1   38.74  ? 225 PHE   A CB   1 1 
ATOM   1644 C  CG   . PHE   A 1 226 ? 31.709 -45.688 2.234   1   37.09  ? 225 PHE   A CG   1 1 
ATOM   1645 C  CD1  . PHE   A 1 226 ? 33.061 -45.501 1.994   1   36.83  ? 225 PHE   A CD1  1 1 
ATOM   1646 C  CD2  . PHE   A 1 226 ? 30.997 -44.66  2.816   1   36.91  ? 225 PHE   A CD2  1 1 
ATOM   1647 C  CE1  . PHE   A 1 226 ? 33.682 -44.31  2.322   1   37.02  ? 225 PHE   A CE1  1 1 
ATOM   1648 C  CE2  . PHE   A 1 226 ? 31.626 -43.48  3.171   1   37.36  ? 225 PHE   A CE2  1 1 
ATOM   1649 C  CZ   . PHE   A 1 226 ? 32.966 -43.309 2.918   1   37.01  ? 225 PHE   A CZ   1 1 
ATOM   1650 N  N    . THR   A 1 227 ? 29.833 -48.416 4.423   1   46.93  ? 226 THR   A N    1 1 
ATOM   1651 C  CA   . THR   A 1 227 ? 29.297 -48.659 5.773   1   50.01  ? 226 THR   A CA   1 1 
ATOM   1652 C  C    . THR   A 1 227 ? 28.446 -49.936 5.701   1   53.05  ? 226 THR   A C    1 1 
ATOM   1653 O  O    . THR   A 1 227 ? 28.083 -50.363 4.604   1   53.46  ? 226 THR   A O    1 1 
ATOM   1654 C  CB   . THR   A 1 227 ? 28.57  -47.467 6.438   1   51.96  ? 226 THR   A CB   1 1 
ATOM   1655 O  OG1  . THR   A 1 227 ? 27.361 -47.156 5.752   1   53.72  ? 226 THR   A OG1  1 1 
ATOM   1656 C  CG2  . THR   A 1 227 ? 29.444 -46.249 6.604   1   52.54  ? 226 THR   A CG2  1 1 
ATOM   1657 N  N    . LYS   A 1 228 ? 28.128 -50.549 6.841   1   55.37  ? 227 LYS   A N    1 1 
ATOM   1658 C  CA   . LYS   A 1 228 ? 27.393 -51.817 6.874   1   58.69  ? 227 LYS   A CA   1 1 
ATOM   1659 C  C    . LYS   A 1 228 ? 25.909 -51.762 6.494   1   61.81  ? 227 LYS   A C    1 1 
ATOM   1660 O  O    . LYS   A 1 228 ? 25.459 -52.629 5.744   1   62.36  ? 227 LYS   A O    1 1 
ATOM   1661 C  CB   . LYS   A 1 228 ? 27.527 -52.507 8.241   1   60.98  ? 227 LYS   A CB   1 1 
ATOM   1662 C  CG   . LYS   A 1 228 ? 28.934 -52.967 8.536   1   66.6   ? 227 LYS   A CG   1 1 
ATOM   1663 C  CD   . LYS   A 1 228 ? 29.016 -53.569 9.92    1   72.96  ? 227 LYS   A CD   1 1 
ATOM   1664 C  CE   . LYS   A 1 228 ? 30.368 -54.197 10.18   1   77.97  ? 227 LYS   A CE   1 1 
ATOM   1665 N  NZ   . LYS   A 1 228 ? 30.685 -55.278 9.197   1   80.98  ? 227 LYS   A NZ   1 1 
ATOM   1666 N  N    . ASN   A 1 229 ? 25.14  -50.825 7.057   1   63.59  ? 228 ASN   A N    1 1 
ATOM   1667 C  CA   . ASN   A 1 229 ? 23.694 -50.744 6.83    1   65.97  ? 228 ASN   A CA   1 1 
ATOM   1668 C  C    . ASN   A 1 229 ? 23.233 -49.272 6.78    1   68.18  ? 228 ASN   A C    1 1 
ATOM   1669 O  O    . ASN   A 1 229 ? 23.927 -48.397 7.31    1   68.72  ? 228 ASN   A O    1 1 
ATOM   1670 C  CB   . ASN   A 1 229 ? 22.979 -51.437 8       1   67.79  ? 228 ASN   A CB   1 1 
ATOM   1671 C  CG   . ASN   A 1 229 ? 23.242 -52.915 8.129   1   72.43  ? 228 ASN   A CG   1 1 
ATOM   1672 O  OD1  . ASN   A 1 229 ? 23.031 -53.699 7.194   1   74.41  ? 228 ASN   A OD1  1 1 
ATOM   1673 N  ND2  . ASN   A 1 229 ? 23.704 -53.334 9.296   1   73.6   ? 228 ASN   A ND2  1 1 
ATOM   1674 N  N    . PRO   A 1 230 ? 22.051 -48.962 6.193   1   69.2   ? 229 PRO   A N    1 1 
ATOM   1675 C  CA   . PRO   A 1 230 ? 21.576 -47.562 6.21    1   70.14  ? 229 PRO   A CA   1 1 
ATOM   1676 C  C    . PRO   A 1 230 ? 21.181 -47.125 7.624   1   71.61  ? 229 PRO   A C    1 1 
ATOM   1677 O  O    . PRO   A 1 230 ? 20.7   -47.943 8.409   1   71.73  ? 229 PRO   A O    1 1 
ATOM   1678 C  CB   . PRO   A 1 230 ? 20.372 -47.573 5.263   1   70.55  ? 229 PRO   A CB   1 1 
ATOM   1679 C  CG   . PRO   A 1 230 ? 19.918 -48.968 5.232   1   70.65  ? 229 PRO   A CG   1 1 
ATOM   1680 C  CD   . PRO   A 1 230 ? 21.094 -49.858 5.514   1   68.76  ? 229 PRO   A CD   1 1 
ATOM   1681 N  N    . SER   A 1 231 ? 21.39  -45.84  7.959   1   72.59  ? 230 SER   A N    1 1 
ATOM   1682 C  CA   . SER   A 1 231 ? 21.099 -45.31  9.297   1   73.88  ? 230 SER   A CA   1 1 
ATOM   1683 C  C    . SER   A 1 231 ? 19.587 -45.146 9.62    1   75.61  ? 230 SER   A C    1 1 
ATOM   1684 O  O    . SER   A 1 231 ? 19.229 -44.821 10.756  1   75.67  ? 230 SER   A O    1 1 
ATOM   1685 C  CB   . SER   A 1 231 ? 21.843 -43.997 9.515   1   74.55  ? 230 SER   A CB   1 1 
ATOM   1686 O  OG   . SER   A 1 231 ? 21.293 -42.986 8.686   1   75.85  ? 230 SER   A OG   1 1 
ATOM   1687 N  N    . THR   A 1 232 ? 18.708 -45.363 8.622   1   76.81  ? 231 THR   A N    1 1 
ATOM   1688 C  CA   . THR   A 1 232 ? 17.245 -45.263 8.764   1   78.32  ? 231 THR   A CA   1 1 
ATOM   1689 C  C    . THR   A 1 232 ? 16.548 -46.525 8.168   1   79.76  ? 231 THR   A C    1 1 
ATOM   1690 O  O    . THR   A 1 232 ? 17.217 -47.361 7.546   1   79.86  ? 231 THR   A O    1 1 
ATOM   1691 C  CB   . THR   A 1 232 ? 16.724 -43.959 8.083   1   79.7   ? 231 THR   A CB   1 1 
ATOM   1692 O  OG1  . THR   A 1 232 ? 16.832 -44.077 6.663   1   80.68  ? 231 THR   A OG1  1 1 
ATOM   1693 C  CG2  . THR   A 1 232 ? 17.432 -42.695 8.567   1   80.23  ? 231 THR   A CG2  1 1 
ATOM   1694 N  N    . ARG   A 1 233 ? 15.205 -46.654 8.341   1   80.69  ? 232 ARG   A N    1 1 
ATOM   1695 C  CA   . ARG   A 1 233 ? 14.409 -47.756 7.772   1   82.1   ? 232 ARG   A CA   1 1 
ATOM   1696 C  C    . ARG   A 1 233 ? 14.122 -47.507 6.266   1   83.07  ? 232 ARG   A C    1 1 
ATOM   1697 O  O    . ARG   A 1 233 ? 12.968 -47.507 5.833   1   83.39  ? 232 ARG   A O    1 1 
ATOM   1698 C  CB   . ARG   A 1 233 ? 13.099 -47.965 8.563   1   83.79  ? 232 ARG   A CB   1 1 
ATOM   1699 C  CG   . ARG   A 1 233 ? 13.336 -48.198 10.05   1   87.87  ? 232 ARG   A CG   1 1 
ATOM   1700 C  CD   . ARG   A 1 233 ? 12.195 -48.936 10.742  1   91.81  ? 232 ARG   A CD   1 1 
ATOM   1701 N  NE   . ARG   A 1 233 ? 12.544 -49.272 12.127  1   95.78  ? 232 ARG   A NE   1 1 
ATOM   1702 C  CZ   . ARG   A 1 233 ? 11.738 -49.893 12.984  1   98.63  ? 232 ARG   A CZ   1 1 
ATOM   1703 N  NH1  . ARG   A 1 233 ? 10.513 -50.246 12.616  1   99.11  ? 232 ARG   A NH1  1 1 
ATOM   1704 N  NH2  . ARG   A 1 233 ? 12.148 -50.157 14.218  1   97.86  ? 232 ARG   A NH2  1 1 
ATOM   1705 N  N    . LEU   A 1 234 ? 15.194 -47.307 5.482   1   83.17  ? 233 LEU   A N    1 1 
ATOM   1706 C  CA   . LEU   A 1 234 ? 15.17  -47.024 4.054   1   83.82  ? 233 LEU   A CA   1 1 
ATOM   1707 C  C    . LEU   A 1 234 ? 14.775 -48.252 3.228   1   84.49  ? 233 LEU   A C    1 1 
ATOM   1708 O  O    . LEU   A 1 234 ? 15.528 -49.224 3.149   1   84.74  ? 233 LEU   A O    1 1 
ATOM   1709 C  CB   . LEU   A 1 234 ? 16.561 -46.512 3.643   1   83.98  ? 233 LEU   A CB   1 1 
ATOM   1710 C  CG   . LEU   A 1 234 ? 16.769 -46.137 2.182   1   85.35  ? 233 LEU   A CG   1 1 
ATOM   1711 C  CD1  . LEU   A 1 234 ? 15.775 -45.083 1.736   1   85.93  ? 233 LEU   A CD1  1 1 
ATOM   1712 C  CD2  . LEU   A 1 234 ? 18.193 -45.66  1.947   1   85.85  ? 233 LEU   A CD2  1 1 
ATOM   1713 N  N    . ILE   A 1 237 ? 17.322 -50.541 -1.357  1   55.39  ? 236 ILE   A N    1 1 
ATOM   1714 C  CA   . ILE   A 1 237 ? 18.61  -49.85  -1.172  1   55.26  ? 236 ILE   A CA   1 1 
ATOM   1715 C  C    . ILE   A 1 237 ? 19.269 -49.564 -2.526  1   54.43  ? 236 ILE   A C    1 1 
ATOM   1716 O  O    . ILE   A 1 237 ? 19.142 -50.378 -3.443  1   55.21  ? 236 ILE   A O    1 1 
ATOM   1717 C  CB   . ILE   A 1 237 ? 19.515 -50.661 -0.199  1   56.05  ? 236 ILE   A CB   1 1 
ATOM   1718 C  CG1  . ILE   A 1 237 ? 19.011 -50.527 1.248   1   57.13  ? 236 ILE   A CG1  1 1 
ATOM   1719 C  CG2  . ILE   A 1 237 ? 20.987 -50.289 -0.303  1   56.42  ? 236 ILE   A CG2  1 1 
ATOM   1720 C  CD1  . ILE   A 1 237 ? 19.641 -51.506 2.227   1   58.46  ? 236 ILE   A CD1  1 1 
ATOM   1721 N  N    . LEU   A 1 238 ? 19.93  -48.399 -2.667  1   52.75  ? 237 LEU   A N    1 1 
ATOM   1722 C  CA   . LEU   A 1 238 ? 20.603 -47.998 -3.911  1   51.79  ? 237 LEU   A CA   1 1 
ATOM   1723 C  C    . LEU   A 1 238 ? 21.711 -48.943 -4.344  1   51.63  ? 237 LEU   A C    1 1 
ATOM   1724 O  O    . LEU   A 1 238 ? 22.568 -49.307 -3.532  1   51.63  ? 237 LEU   A O    1 1 
ATOM   1725 C  CB   . LEU   A 1 238 ? 21.254 -46.607 -3.766  1   50.96  ? 237 LEU   A CB   1 1 
ATOM   1726 C  CG   . LEU   A 1 238 ? 20.372 -45.397 -3.874  1   50.81  ? 237 LEU   A CG   1 1 
ATOM   1727 C  CD1  . LEU   A 1 238 ? 21.168 -44.173 -3.637  1   50.87  ? 237 LEU   A CD1  1 1 
ATOM   1728 C  CD2  . LEU   A 1 238 ? 19.759 -45.314 -5.221  1   51.19  ? 237 LEU   A CD2  1 1 
ATOM   1729 N  N    . GLU   A 1 239 ? 21.746 -49.271 -5.645  1   51.19  ? 238 GLU   A N    1 1 
ATOM   1730 C  CA   . GLU   A 1 239 ? 22.85  -50.039 -6.205  1   51.36  ? 238 GLU   A CA   1 1 
ATOM   1731 C  C    . GLU   A 1 239 ? 23.881 -49.062 -6.771  1   50.72  ? 238 GLU   A C    1 1 
ATOM   1732 O  O    . GLU   A 1 239 ? 23.543 -47.925 -7.101  1   51.13  ? 238 GLU   A O    1 1 
ATOM   1733 C  CB   . GLU   A 1 239 ? 22.388 -51.057 -7.264  1   54.86  ? 238 GLU   A CB   1 1 
ATOM   1734 C  CG   . GLU   A 1 239 ? 21.933 -52.401 -6.7    1   62.62  ? 238 GLU   A CG   1 1 
ATOM   1735 C  CD   . GLU   A 1 239 ? 22.784 -53.057 -5.615  1   73.06  ? 238 GLU   A CD   1 1 
ATOM   1736 O  OE1  . GLU   A 1 239 ? 24     -52.76  -5.523  1   76.49  ? 238 GLU   A OE1  1 1 
ATOM   1737 O  OE2  . GLU   A 1 239 ? 22.224 -53.88  -4.853  1   74.74  ? 238 GLU   A OE2  1 1 
ATOM   1738 N  N    . THR   A 1 240 ? 25.138 -49.477 -6.864  1   49.85  ? 239 THR   A N    1 1 
ATOM   1739 C  CA   . THR   A 1 240 ? 26.212 -48.591 -7.353  1   49.34  ? 239 THR   A CA   1 1 
ATOM   1740 C  C    . THR   A 1 240 ? 26.03  -48.1   -8.808  1   49.09  ? 239 THR   A C    1 1 
ATOM   1741 O  O    . THR   A 1 240 ? 26.361 -46.963 -9.143  1   49.26  ? 239 THR   A O    1 1 
ATOM   1742 C  CB   . THR   A 1 240 ? 27.56  -49.267 -7.221  1   49.86  ? 239 THR   A CB   1 1 
ATOM   1743 O  OG1  . THR   A 1 240 ? 27.671 -49.962 -5.976  1   51.57  ? 239 THR   A OG1  1 1 
ATOM   1744 C  CG2  . THR   A 1 240 ? 28.664 -48.309 -7.386  1   49.25  ? 239 THR   A CG2  1 1 
ATOM   1745 N  N    . ASP   A 1 241 ? 25.532 -48.968 -9.667  1   48.56  ? 240 ASP   A N    1 1 
ATOM   1746 C  CA   . ASP   A 1 241 ? 25.32  -48.641 -11.076 1   48.7   ? 240 ASP   A CA   1 1 
ATOM   1747 C  C    . ASP   A 1 241 ? 24.242 -47.579 -11.278 1   47.88  ? 240 ASP   A C    1 1 
ATOM   1748 O  O    . ASP   A 1 241 ? 24.314 -46.815 -12.24  1   48.17  ? 240 ASP   A O    1 1 
ATOM   1749 C  CB   . ASP   A 1 241 ? 25.01  -49.905 -11.886 1   51.19  ? 240 ASP   A CB   1 1 
ATOM   1750 C  CG   . ASP   A 1 241 ? 24.002 -50.821 -11.228 1   58.28  ? 240 ASP   A CG   1 1 
ATOM   1751 O  OD1  . ASP   A 1 241 ? 24.337 -51.418 -10.178 1   59.91  ? 240 ASP   A OD1  1 1 
ATOM   1752 O  OD2  . ASP   A 1 241 ? 22.885 -50.951 -11.762 1   61.45  ? 240 ASP   A OD2  1 1 
ATOM   1753 N  N    . THR   A 1 242 ? 23.247 -47.531 -10.377 1   46.63  ? 241 THR   A N    1 1 
ATOM   1754 C  CA   . THR   A 1 242 ? 22.178 -46.536 -10.417 1   45.33  ? 241 THR   A CA   1 1 
ATOM   1755 C  C    . THR   A 1 242 ? 22.748 -45.157 -10.071 1   43.78  ? 241 THR   A C    1 1 
ATOM   1756 O  O    . THR   A 1 242 ? 22.43  -44.17  -10.731 1   43.63  ? 241 THR   A O    1 1 
ATOM   1757 C  CB   . THR   A 1 242 ? 21.079 -46.911 -9.42   1   45.73  ? 241 THR   A CB   1 1 
ATOM   1758 O  OG1  . THR   A 1 242 ? 20.549 -48.184 -9.782  1   46.58  ? 241 THR   A OG1  1 1 
ATOM   1759 C  CG2  . THR   A 1 242 ? 19.981 -45.865 -9.351  1   45.61  ? 241 THR   A CG2  1 1 
ATOM   1760 N  N    . VAL   A 1 243 ? 23.614 -45.102 -9.059  1   42.31  ? 242 VAL   A N    1 1 
ATOM   1761 C  CA   . VAL   A 1 243 ? 24.227 -43.872 -8.601  1   41.44  ? 242 VAL   A CA   1 1 
ATOM   1762 C  C    . VAL   A 1 243 ? 25.15  -43.312 -9.67   1   41.16  ? 242 VAL   A C    1 1 
ATOM   1763 O  O    . VAL   A 1 243 ? 25.143 -42.099 -9.916  1   41.39  ? 242 VAL   A O    1 1 
ATOM   1764 C  CB   . VAL   A 1 243 ? 24.924 -44.109 -7.245  1   41.52  ? 242 VAL   A CB   1 1 
ATOM   1765 C  CG1  . VAL   A 1 243 ? 25.629 -42.853 -6.745  1   42.02  ? 242 VAL   A CG1  1 1 
ATOM   1766 C  CG2  . VAL   A 1 243 ? 23.923 -44.616 -6.22   1   41.33  ? 242 VAL   A CG2  1 1 
ATOM   1767 N  N    . ALA   A 1 244 ? 25.899 -44.186 -10.349 1   40.48  ? 243 ALA   A N    1 1 
ATOM   1768 C  CA   . ALA   A 1 244 ? 26.777 -43.774 -11.44  1   40.76  ? 243 ALA   A CA   1 1 
ATOM   1769 C  C    . ALA   A 1 244 ? 25.951 -43.241 -12.633 1   40.36  ? 243 ALA   A C    1 1 
ATOM   1770 O  O    . ALA   A 1 244 ? 26.345 -42.255 -13.249 1   40.01  ? 243 ALA   A O    1 1 
ATOM   1771 C  CB   . ALA   A 1 244 ? 27.626 -44.951 -11.875 1   41.27  ? 243 ALA   A CB   1 1 
ATOM   1772 N  N    . ARG   A 1 245 ? 24.785 -43.861 -12.917 1   40.5   ? 244 ARG   A N    1 1 
ATOM   1773 C  CA   . ARG   A 1 245 ? 23.893 -43.391 -13.974 1   41.47  ? 244 ARG   A CA   1 1 
ATOM   1774 C  C    . ARG   A 1 245 ? 23.332 -42.022 -13.598 1   40.88  ? 244 ARG   A C    1 1 
ATOM   1775 O  O    . ARG   A 1 245 ? 23.292 -41.13  -14.434 1   41.19  ? 244 ARG   A O    1 1 
ATOM   1776 C  CB   . ARG   A 1 245 ? 22.766 -44.395 -14.26  1   44.54  ? 244 ARG   A CB   1 1 
ATOM   1777 C  CG   . ARG   A 1 245 ? 22.878 -45.006 -15.649 1   52.49  ? 244 ARG   A CG   1 1 
ATOM   1778 C  CD   . ARG   A 1 245 ? 21.742 -45.964 -16.006 1   60.34  ? 244 ARG   A CD   1 1 
ATOM   1779 N  NE   . ARG   A 1 245 ? 21.867 -47.288 -15.38  1   66.45  ? 244 ARG   A NE   1 1 
ATOM   1780 C  CZ   . ARG   A 1 245 ? 21.14  -47.704 -14.345 1   70.45  ? 244 ARG   A CZ   1 1 
ATOM   1781 N  NH1  . ARG   A 1 245 ? 20.229 -46.905 -13.798 1   70.59  ? 244 ARG   A NH1  1 1 
ATOM   1782 N  NH2  . ARG   A 1 245 ? 21.314 -48.923 -13.852 1   71.2   ? 244 ARG   A NH2  1 1 
ATOM   1783 N  N    . SER   A 1 246 ? 22.946 -41.837 -12.34  1   40.16  ? 245 SER   A N    1 1 
ATOM   1784 C  CA   . SER   A 1 246 ? 22.421 -40.559 -11.864 1   40.29  ? 245 SER   A CA   1 1 
ATOM   1785 C  C    . SER   A 1 246 ? 23.461 -39.46  -11.965 1   39.71  ? 245 SER   A C    1 1 
ATOM   1786 O  O    . SER   A 1 246 ? 23.143 -38.356 -12.423 1   39.88  ? 245 SER   A O    1 1 
ATOM   1787 C  CB   . SER   A 1 246 ? 21.924 -40.681 -10.435 1   42.3   ? 245 SER   A CB   1 1 
ATOM   1788 O  OG   . SER   A 1 246 ? 20.586 -41.145 -10.445 1   46.1   ? 245 SER   A OG   1 1 
ATOM   1789 N  N    . LEU   A 1 247 ? 24.713 -39.773 -11.567 1   38.68  ? 246 LEU   A N    1 1 
ATOM   1790 C  CA   . LEU   A 1 247 ? 25.823 -38.839 -11.643 1   37.94  ? 246 LEU   A CA   1 1 
ATOM   1791 C  C    . LEU   A 1 247 ? 26.091 -38.411 -13.091 1   38.58  ? 246 LEU   A C    1 1 
ATOM   1792 O  O    . LEU   A 1 247 ? 26.036 -37.211 -13.371 1   38.93  ? 246 LEU   A O    1 1 
ATOM   1793 C  CB   . LEU   A 1 247 ? 27.091 -39.409 -10.997 1   37.2   ? 246 LEU   A CB   1 1 
ATOM   1794 C  CG   . LEU   A 1 247 ? 28.333 -38.513 -11.083 1   37.75  ? 246 LEU   A CG   1 1 
ATOM   1795 C  CD1  . LEU   A 1 247 ? 28.084 -37.142 -10.466 1   38.39  ? 246 LEU   A CD1  1 1 
ATOM   1796 C  CD2  . LEU   A 1 247 ? 29.531 -39.148 -10.424 1   38     ? 246 LEU   A CD2  1 1 
ATOM   1797 N  N    . ILE   A 1 248 ? 26.326 -39.367 -14.023 1   38.2   ? 247 ILE   A N    1 1 
ATOM   1798 C  CA   . ILE   A 1 248 ? 26.624 -39.008 -15.404 1   38.92  ? 247 ILE   A CA   1 1 
ATOM   1799 C  C    . ILE   A 1 248 ? 25.494 -38.209 -16.043 1   38.77  ? 247 ILE   A C    1 1 
ATOM   1800 O  O    . ILE   A 1 248 ? 25.779 -37.208 -16.696 1   38.31  ? 247 ILE   A O    1 1 
ATOM   1801 C  CB   . ILE   A 1 248 ? 27.058 -40.216 -16.274 1   40.02  ? 247 ILE   A CB   1 1 
ATOM   1802 C  CG1  . ILE   A 1 248 ? 27.867 -39.747 -17.48  1   41.14  ? 247 ILE   A CG1  1 1 
ATOM   1803 C  CG2  . ILE   A 1 248 ? 25.887 -41.084 -16.706 1   40.44  ? 247 ILE   A CG2  1 1 
ATOM   1804 C  CD1  . ILE   A 1 248 ? 29.191 -39.296 -17.131 1   42.42  ? 247 ILE   A CD1  1 1 
ATOM   1805 N  N    . ASP   A 1 249 ? 24.221 -38.58  -15.772 1   38.65  ? 248 ASP   A N    1 1 
ATOM   1806 C  CA   . ASP   A 1 249 ? 23.066 -37.859 -16.307 1   38.84  ? 248 ASP   A CA   1 1 
ATOM   1807 C  C    . ASP   A 1 249 ? 23.02  -36.426 -15.808 1   38.84  ? 248 ASP   A C    1 1 
ATOM   1808 O  O    . ASP   A 1 249 ? 22.699 -35.535 -16.581 1   39.38  ? 248 ASP   A O    1 1 
ATOM   1809 C  CB   . ASP   A 1 249 ? 21.759 -38.601 -16.027 1   41.29  ? 248 ASP   A CB   1 1 
ATOM   1810 C  CG   . ASP   A 1 249 ? 21.609 -39.879 -16.852 1   49.21  ? 248 ASP   A CG   1 1 
ATOM   1811 O  OD1  . ASP   A 1 249 ? 22.003 -39.873 -18.052 1   49.8   ? 248 ASP   A OD1  1 1 
ATOM   1812 O  OD2  . ASP   A 1 249 ? 21.098 -40.884 -16.303 1   53.15  ? 248 ASP   A OD2  1 1 
ATOM   1813 N  N    . GLY   A 1 250 ? 23.405 -36.207 -14.548 1   37.99  ? 249 GLY   A N    1 1 
ATOM   1814 C  CA   . GLY   A 1 250 ? 23.478 -34.878 -13.959 1   37.56  ? 249 GLY   A CA   1 1 
ATOM   1815 C  C    . GLY   A 1 250 ? 24.606 -34.034 -14.523 1   37.01  ? 249 GLY   A C    1 1 
ATOM   1816 O  O    . GLY   A 1 250 ? 24.408 -32.846 -14.771 1   37.03  ? 249 GLY   A O    1 1 
ATOM   1817 N  N    . ILE   A 1 251 ? 25.802 -34.636 -14.734 1   36.14  ? 250 ILE   A N    1 1 
ATOM   1818 C  CA   . ILE   A 1 251 ? 26.959 -33.945 -15.309 1   35.71  ? 250 ILE   A CA   1 1 
ATOM   1819 C  C    . ILE   A 1 251 ? 26.658 -33.485 -16.736 1   36.92  ? 250 ILE   A C    1 1 
ATOM   1820 O  O    . ILE   A 1 251 ? 26.876 -32.319 -17.07  1   37.22  ? 250 ILE   A O    1 1 
ATOM   1821 C  CB   . ILE   A 1 251 ? 28.215 -34.839 -15.268 1   35.36  ? 250 ILE   A CB   1 1 
ATOM   1822 C  CG1  . ILE   A 1 251 ? 28.611 -35.139 -13.807 1   36.22  ? 250 ILE   A CG1  1 1 
ATOM   1823 C  CG2  . ILE   A 1 251 ? 29.376 -34.202 -16.039 1   35.17  ? 250 ILE   A CG2  1 1 
ATOM   1824 C  CD1  . ILE   A 1 251 ? 29.719 -36.158 -13.639 1   37.19  ? 250 ILE   A CD1  1 1 
ATOM   1825 N  N    . LEU   A 1 252 ? 26.107 -34.38  -17.56  1   36.79  ? 251 LEU   A N    1 1 
ATOM   1826 C  CA   . LEU   A 1 252 ? 25.774 -34.067 -18.939 1   36.97  ? 251 LEU   A CA   1 1 
ATOM   1827 C  C    . LEU   A 1 252 ? 24.715 -32.984 -19.079 1   37.6   ? 251 LEU   A C    1 1 
ATOM   1828 O  O    . LEU   A 1 252 ? 24.674 -32.318 -20.117 1   38.17  ? 251 LEU   A O    1 1 
ATOM   1829 C  CB   . LEU   A 1 252 ? 25.363 -35.341 -19.707 1   36.85  ? 251 LEU   A CB   1 1 
ATOM   1830 C  CG   . LEU   A 1 252 ? 26.378 -36.482 -19.718 1   37.43  ? 251 LEU   A CG   1 1 
ATOM   1831 C  CD1  . LEU   A 1 252 ? 25.877 -37.641 -20.525 1   37.51  ? 251 LEU   A CD1  1 1 
ATOM   1832 C  CD2  . LEU   A 1 252 ? 27.724 -36.033 -20.235 1   38.42  ? 251 LEU   A CD2  1 1 
ATOM   1833 N  N    . THR   A 1 253 ? 23.878 -32.782 -18.053 1   37.52  ? 252 THR   A N    1 1 
ATOM   1834 C  CA   . THR   A 1 253 ? 22.857 -31.731 -18.097 1   38.22  ? 252 THR   A CA   1 1 
ATOM   1835 C  C    . THR   A 1 253 ? 23.203 -30.511 -17.215 1   38.95  ? 252 THR   A C    1 1 
ATOM   1836 O  O    . THR   A 1 253 ? 22.354 -29.635 -17.043 1   39.68  ? 252 THR   A O    1 1 
ATOM   1837 C  CB   . THR   A 1 253 ? 21.504 -32.3   -17.699 1   39.17  ? 252 THR   A CB   1 1 
ATOM   1838 O  OG1  . THR   A 1 253 ? 21.64  -32.892 -16.397 1   40.87  ? 252 THR   A OG1  1 1 
ATOM   1839 C  CG2  . THR   A 1 253 ? 20.979 -33.301 -18.703 1   38.57  ? 252 THR   A CG2  1 1 
ATOM   1840 N  N    . ASN   A 1 254 ? 24.432 -30.462 -16.661 1   38.47  ? 253 ASN   A N    1 1 
ATOM   1841 C  CA   . ASN   A 1 254 ? 24.956 -29.401 -15.801 1   38.54  ? 253 ASN   A CA   1 1 
ATOM   1842 C  C    . ASN   A 1 254 ? 24.12  -29.169 -14.543 1   38.96  ? 253 ASN   A C    1 1 
ATOM   1843 O  O    . ASN   A 1 254 ? 23.961 -28.026 -14.117 1   39.58  ? 253 ASN   A O    1 1 
ATOM   1844 C  CB   . ASN   A 1 254 ? 25.196 -28.099 -16.564 1   38.8   ? 253 ASN   A CB   1 1 
ATOM   1845 C  CG   . ASN   A 1 254 ? 26.357 -28.139 -17.535 1   41.81  ? 253 ASN   A CG   1 1 
ATOM   1846 O  OD1  . ASN   A 1 254 ? 26.456 -27.304 -18.456 1   43.73  ? 253 ASN   A OD1  1 1 
ATOM   1847 N  ND2  . ASN   A 1 254 ? 27.265 -29.096 -17.372 1   41.63  ? 253 ASN   A ND2  1 1 
ATOM   1848 N  N    . LYS   A 1 255 ? 23.622 -30.255 -13.918 1   38.4   ? 254 LYS   A N    1 1 
ATOM   1849 C  CA   . LYS   A 1 255 ? 22.836 -30.14  -12.697 1   38.09  ? 254 LYS   A CA   1 1 
ATOM   1850 C  C    . LYS   A 1 255 ? 23.767 -29.866 -11.535 1   37.76  ? 254 LYS   A C    1 1 
ATOM   1851 O  O    . LYS   A 1 255 ? 24.756 -30.569 -11.36  1   37.72  ? 254 LYS   A O    1 1 
ATOM   1852 C  CB   . LYS   A 1 255 ? 22.009 -31.397 -12.447 1   40.24  ? 254 LYS   A CB   1 1 
ATOM   1853 C  CG   . LYS   A 1 255 ? 20.579 -31.067 -12.084 1   45.56  ? 254 LYS   A CG   1 1 
ATOM   1854 C  CD   . LYS   A 1 255 ? 19.953 -32.179 -11.279 1   53.01  ? 254 LYS   A CD   1 1 
ATOM   1855 C  CE   . LYS   A 1 255 ? 18.75  -31.705 -10.492 1   59.02  ? 254 LYS   A CE   1 1 
ATOM   1856 N  NZ   . LYS   A 1 255 ? 18.656 -32.387 -9.163  1   63.22  ? 254 LYS   A NZ   1 1 
ATOM   1857 N  N    . LYS   A 1 256 ? 23.48  -28.813 -10.759 1   37.53  ? 255 LYS   A N    1 1 
ATOM   1858 C  CA   . LYS   A 1 256 ? 24.323 -28.409 -9.643  1   37.29  ? 255 LYS   A CA   1 1 
ATOM   1859 C  C    . LYS   A 1 256 ? 24.185 -29.275 -8.407  1   38.3   ? 255 LYS   A C    1 1 
ATOM   1860 O  O    . LYS   A 1 256 ? 25.189 -29.544 -7.759  1   39.28  ? 255 LYS   A O    1 1 
ATOM   1861 C  CB   . LYS   A 1 256 ? 24.108 -26.939 -9.306  1   37.58  ? 255 LYS   A CB   1 1 
ATOM   1862 C  CG   . LYS   A 1 256 ? 24.51  -26.06  -10.46  1   41.61  ? 255 LYS   A CG   1 1 
ATOM   1863 C  CD   . LYS   A 1 256 ? 24.437 -24.589 -10.126 1   48.25  ? 255 LYS   A CD   1 1 
ATOM   1864 C  CE   . LYS   A 1 256 ? 24.989 -23.805 -11.288 1   54.92  ? 255 LYS   A CE   1 1 
ATOM   1865 N  NZ   . LYS   A 1 256 ? 24.715 -22.34  -11.169 1   59.18  ? 255 LYS   A NZ   1 1 
ATOM   1866 N  N    . MET   A 1 257 ? 22.972 -29.688 -8.043  1   38.35  ? 256 MET   A N    1 1 
ATOM   1867 C  CA   . MET   A 1 257 ? 22.788 -30.536 -6.859  1   38.78  ? 256 MET   A CA   1 1 
ATOM   1868 C  C    . MET   A 1 257 ? 22.059 -31.793 -7.283  1   39.84  ? 256 MET   A C    1 1 
ATOM   1869 O  O    . MET   A 1 257 ? 20.91  -31.728 -7.699  1   40.77  ? 256 MET   A O    1 1 
ATOM   1870 C  CB   . MET   A 1 257 ? 22.055 -29.786 -5.738  1   38.59  ? 256 MET   A CB   1 1 
ATOM   1871 C  CG   . MET   A 1 257 ? 22.03  -30.53  -4.41   1   40.51  ? 256 MET   A CG   1 1 
ATOM   1872 S  SD   . MET   A 1 257 ? 23.604 -30.762 -3.524  1   44.78  ? 256 MET   A SD   1 1 
ATOM   1873 C  CE   . MET   A 1 257 ? 24.201 -29.064 -3.49   1   38.27  ? 256 MET   A CE   1 1 
ATOM   1874 N  N    . ILE   A 1 258 ? 22.757 -32.918 -7.284  1   39.48  ? 257 ILE   A N    1 1 
ATOM   1875 C  CA   . ILE   A 1 258 ? 22.194 -34.185 -7.718  1   39.69  ? 257 ILE   A CA   1 1 
ATOM   1876 C  C    . ILE   A 1 258 ? 21.924 -35.048 -6.494  1   41.33  ? 257 ILE   A C    1 1 
ATOM   1877 O  O    . ILE   A 1 258 ? 22.858 -35.491 -5.842  1   41.58  ? 257 ILE   A O    1 1 
ATOM   1878 C  CB   . ILE   A 1 258 ? 23.161 -34.897 -8.709  1   39.15  ? 257 ILE   A CB   1 1 
ATOM   1879 C  CG1  . ILE   A 1 258 ? 23.551 -33.986 -9.895  1   39.47  ? 257 ILE   A CG1  1 1 
ATOM   1880 C  CG2  . ILE   A 1 258 ? 22.601 -36.23  -9.176  1   38.98  ? 257 ILE   A CG2  1 1 
ATOM   1881 C  CD1  . ILE   A 1 258 ? 24.878 -34.318 -10.486 1   40.1   ? 257 ILE   A CD1  1 1 
ATOM   1882 N  N    . PHE   A 1 259 ? 20.651 -35.28  -6.171  1   42.03  ? 258 PHE   A N    1 1 
ATOM   1883 C  CA   . PHE   A 1 259 ? 20.282 -36.142 -5.064  1   42.67  ? 258 PHE   A CA   1 1 
ATOM   1884 C  C    . PHE   A 1 259 ? 19.956 -37.51  -5.613  1   43.98  ? 258 PHE   A C    1 1 
ATOM   1885 O  O    . PHE   A 1 259 ? 19.276 -37.6   -6.629  1   43.97  ? 258 PHE   A O    1 1 
ATOM   1886 C  CB   . PHE   A 1 259 ? 19.047 -35.591 -4.349  1   42.27  ? 258 PHE   A CB   1 1 
ATOM   1887 C  CG   . PHE   A 1 259 ? 19.381 -34.455 -3.428  1   42.75  ? 258 PHE   A CG   1 1 
ATOM   1888 C  CD1  . PHE   A 1 259 ? 20.065 -34.681 -2.244  1   43.71  ? 258 PHE   A CD1  1 1 
ATOM   1889 C  CD2  . PHE   A 1 259 ? 19.03  -33.16  -3.748  1   43.26  ? 258 PHE   A CD2  1 1 
ATOM   1890 C  CE1  . PHE   A 1 259 ? 20.384 -33.63  -1.395  1   44.31  ? 258 PHE   A CE1  1 1 
ATOM   1891 C  CE2  . PHE   A 1 259 ? 19.341 -32.111 -2.892  1   44.13  ? 258 PHE   A CE2  1 1 
ATOM   1892 C  CZ   . PHE   A 1 259 ? 20.013 -32.351 -1.72   1   43.97  ? 258 PHE   A CZ   1 1 
ATOM   1893 N  N    . VAL   A 1 260 ? 20.418 -38.585 -4.955  1   44.94  ? 259 VAL   A N    1 1 
ATOM   1894 C  CA   . VAL   A 1 260 ? 20.073 -39.941 -5.398  1   45.89  ? 259 VAL   A CA   1 1 
ATOM   1895 C  C    . VAL   A 1 260 ? 19.445 -40.681 -4.233  1   47.09  ? 259 VAL   A C    1 1 
ATOM   1896 O  O    . VAL   A 1 260 ? 20.159 -40.998 -3.292  1   46.71  ? 259 VAL   A O    1 1 
ATOM   1897 C  CB   . VAL   A 1 260 ? 21.257 -40.739 -5.984  1   46.11  ? 259 VAL   A CB   1 1 
ATOM   1898 C  CG1  . VAL   A 1 260 ? 20.756 -41.988 -6.698  1   46.08  ? 259 VAL   A CG1  1 1 
ATOM   1899 C  CG2  . VAL   A 1 260 ? 22.096 -39.88  -6.923  1   46.53  ? 259 VAL   A CG2  1 1 
ATOM   1900 N  N    . PRO   A 1 261 ? 18.12  -40.958 -4.246  1   48.31  ? 260 PRO   A N    1 1 
ATOM   1901 C  CA   . PRO   A 1 261 ? 17.133 -40.622 -5.286  1   49.43  ? 260 PRO   A CA   1 1 
ATOM   1902 C  C    . PRO   A 1 261 ? 16.707 -39.162 -5.204  1   51.77  ? 260 PRO   A C    1 1 
ATOM   1903 O  O    . PRO   A 1 261 ? 16.678 -38.578 -4.112  1   52.14  ? 260 PRO   A O    1 1 
ATOM   1904 C  CB   . PRO   A 1 261 ? 15.987 -41.58  -4.978  1   49.32  ? 260 PRO   A CB   1 1 
ATOM   1905 C  CG   . PRO   A 1 261 ? 16.043 -41.735 -3.498  1   49.22  ? 260 PRO   A CG   1 1 
ATOM   1906 C  CD   . PRO   A 1 261 ? 17.491 -41.678 -3.123  1   47.61  ? 260 PRO   A CD   1 1 
ATOM   1907 N  N    . SER   A 1 262 ? 16.427 -38.562 -6.368  1   53.14  ? 261 SER   A N    1 1 
ATOM   1908 C  CA   . SER   A 1 262 ? 16.063 -37.153 -6.512  1   55.31  ? 261 SER   A CA   1 1 
ATOM   1909 C  C    . SER   A 1 262 ? 14.941 -36.687 -5.586  1   57.87  ? 261 SER   A C    1 1 
ATOM   1910 O  O    . SER   A 1 262 ? 14.967 -35.533 -5.142  1   57.88  ? 261 SER   A O    1 1 
ATOM   1911 C  CB   . SER   A 1 262 ? 15.737 -36.834 -7.961  1   56.65  ? 261 SER   A CB   1 1 
ATOM   1912 O  OG   . SER   A 1 262 ? 14.847 -37.801 -8.489  1   59.83  ? 261 SER   A OG   1 1 
ATOM   1913 N  N    . TYR   A 1 263 ? 14.001 -37.593 -5.229  1   59.69  ? 262 TYR   A N    1 1 
ATOM   1914 C  CA   . TYR   A 1 263 ? 12.916 -37.257 -4.304  1   61.79  ? 262 TYR   A CA   1 1 
ATOM   1915 C  C    . TYR   A 1 263 ? 13.384 -36.941 -2.888  1   65     ? 262 TYR   A C    1 1 
ATOM   1916 O  O    . TYR   A 1 263 ? 12.559 -36.518 -2.079  1   65.42  ? 262 TYR   A O    1 1 
ATOM   1917 C  CB   . TYR   A 1 263 ? 11.807 -38.32  -4.28   1   61.15  ? 262 TYR   A CB   1 1 
ATOM   1918 C  CG   . TYR   A 1 263 ? 12.215 -39.697 -3.799  1   61.18  ? 262 TYR   A CG   1 1 
ATOM   1919 C  CD1  . TYR   A 1 263 ? 12.463 -39.94  -2.456  1   61.94  ? 262 TYR   A CD1  1 1 
ATOM   1920 C  CD2  . TYR   A 1 263 ? 12.246 -40.776 -4.669  1   61.83  ? 262 TYR   A CD2  1 1 
ATOM   1921 C  CE1  . TYR   A 1 263 ? 12.793 -41.208 -2.002  1   62.99  ? 262 TYR   A CE1  1 1 
ATOM   1922 C  CE2  . TYR   A 1 263 ? 12.551 -42.054 -4.224  1   62.74  ? 262 TYR   A CE2  1 1 
ATOM   1923 C  CZ   . TYR   A 1 263 ? 12.823 -42.269 -2.887  1   63.99  ? 262 TYR   A CZ   1 1 
ATOM   1924 O  OH   . TYR   A 1 263 ? 13.15  -43.531 -2.442  1   65.87  ? 262 TYR   A OH   1 1 
ATOM   1925 N  N    . TYR   A 1 264 ? 14.677 -37.157 -2.567  1   67.18  ? 263 TYR   A N    1 1 
ATOM   1926 C  CA   . TYR   A 1 264 ? 15.173 -36.819 -1.232  1   70.14  ? 263 TYR   A CA   1 1 
ATOM   1927 C  C    . TYR   A 1 264 ? 15.315 -35.325 -0.986  1   73.18  ? 263 TYR   A C    1 1 
ATOM   1928 O  O    . TYR   A 1 264 ? 15.538 -34.915 0.147   1   73.41  ? 263 TYR   A O    1 1 
ATOM   1929 C  CB   . TYR   A 1 264 ? 16.461 -37.545 -0.891  1   70.32  ? 263 TYR   A CB   1 1 
ATOM   1930 C  CG   . TYR   A 1 264 ? 16.162 -38.685 0.035   1   71.39  ? 263 TYR   A CG   1 1 
ATOM   1931 C  CD1  . TYR   A 1 264 ? 16.026 -38.476 1.398   1   72.49  ? 263 TYR   A CD1  1 1 
ATOM   1932 C  CD2  . TYR   A 1 264 ? 15.84  -39.937 -0.462  1   72.57  ? 263 TYR   A CD2  1 1 
ATOM   1933 C  CE1  . TYR   A 1 264 ? 15.665 -39.505 2.252   1   73.69  ? 263 TYR   A CE1  1 1 
ATOM   1934 C  CE2  . TYR   A 1 264 ? 15.5   -40.983 0.382   1   73.78  ? 263 TYR   A CE2  1 1 
ATOM   1935 C  CZ   . TYR   A 1 264 ? 15.422 -40.766 1.743   1   75.04  ? 263 TYR   A CZ   1 1 
ATOM   1936 O  OH   . TYR   A 1 264 ? 15.083 -41.798 2.585   1   77.33  ? 263 TYR   A OH   1 1 
ATOM   1937 N  N    . ASN   A 1 265 ? 15.193 -34.519 -2.036  1   75.45  ? 264 ASN   A N    1 1 
ATOM   1938 C  CA   . ASN   A 1 265 ? 15.228 -33.081 -1.952  1   78.24  ? 264 ASN   A CA   1 1 
ATOM   1939 C  C    . ASN   A 1 265 ? 13.994 -32.597 -1.17   1   80.5   ? 264 ASN   A C    1 1 
ATOM   1940 O  O    . ASN   A 1 265 ? 14.118 -31.646 -0.405  1   81.01  ? 264 ASN   A O    1 1 
ATOM   1941 C  CB   . ASN   A 1 265 ? 15.228 -32.507 -3.369  1   80.21  ? 264 ASN   A CB   1 1 
ATOM   1942 C  CG   . ASN   A 1 265 ? 15.115 -31.01  -3.417  1   84.7   ? 264 ASN   A CG   1 1 
ATOM   1943 O  OD1  . ASN   A 1 265 ? 15.725 -30.289 -2.606  1   85.97  ? 264 ASN   A OD1  1 1 
ATOM   1944 N  ND2  . ASN   A 1 265 ? 14.312 -30.52  -4.363  1   85.73  ? 264 ASN   A ND2  1 1 
ATOM   1945 N  N    . ILE   A 1 266 ? 12.818 -33.245 -1.344  1   81.59  ? 265 ILE   A N    1 1 
ATOM   1946 C  CA   . ILE   A 1 266 ? 11.618 -32.814 -0.643  1   83.18  ? 265 ILE   A CA   1 1 
ATOM   1947 C  C    . ILE   A 1 266 ? 11.662 -33.192 0.839   1   84.48  ? 265 ILE   A C    1 1 
ATOM   1948 O  O    . ILE   A 1 266 ? 11.138 -32.435 1.649   1   84.82  ? 265 ILE   A O    1 1 
ATOM   1949 C  CB   . ILE   A 1 266 ? 10.308 -33.256 -1.345  1   83.94  ? 265 ILE   A CB   1 1 
ATOM   1950 C  CG1  . ILE   A 1 266 ? 9.957  -34.737 -1.082  1   84.97  ? 265 ILE   A CG1  1 1 
ATOM   1951 C  CG2  . ILE   A 1 266 ? 10.36  -32.938 -2.832  1   84.28  ? 265 ILE   A CG2  1 1 
ATOM   1952 C  CD1  . ILE   A 1 266 ? 8.57   -35.138 -1.563  1   86.24  ? 265 ILE   A CD1  1 1 
ATOM   1953 N  N    . TYR   A 1 267 ? 12.322 -34.31  1.212   1   85.21  ? 266 TYR   A N    1 1 
ATOM   1954 C  CA   . TYR   A 1 267 ? 12.449 -34.678 2.63    1   86.47  ? 266 TYR   A CA   1 1 
ATOM   1955 C  C    . TYR   A 1 267 ? 13.276 -33.618 3.362   1   87.21  ? 266 TYR   A C    1 1 
ATOM   1956 O  O    . TYR   A 1 267 ? 12.958 -33.26  4.488   1   87.5   ? 266 TYR   A O    1 1 
ATOM   1957 C  CB   . TYR   A 1 267 ? 13.146 -36.037 2.798   1   87.04  ? 266 TYR   A CB   1 1 
ATOM   1958 C  CG   . TYR   A 1 267 ? 12.304 -37.233 2.43    1   88.73  ? 266 TYR   A CG   1 1 
ATOM   1959 C  CD1  . TYR   A 1 267 ? 11.436 -37.802 3.348   1   90.13  ? 266 TYR   A CD1  1 1 
ATOM   1960 C  CD2  . TYR   A 1 267 ? 12.438 -37.847 1.194   1   89.96  ? 266 TYR   A CD2  1 1 
ATOM   1961 C  CE1  . TYR   A 1 267 ? 10.678 -38.922 3.026   1   91.26  ? 266 TYR   A CE1  1 1 
ATOM   1962 C  CE2  . TYR   A 1 267 ? 11.687 -38.968 0.861   1   91.1   ? 266 TYR   A CE2  1 1 
ATOM   1963 C  CZ   . TYR   A 1 267 ? 10.804 -39.502 1.779   1   92.1   ? 266 TYR   A CZ   1 1 
ATOM   1964 O  OH   . TYR   A 1 267 ? 10.053 -40.609 1.458   1   93.69  ? 266 TYR   A OH   1 1 
ATOM   1965 N  N    . LEU   A 1 268 ? 14.332 -33.11  2.711   1   87.56  ? 267 LEU   A N    1 1 
ATOM   1966 C  CA   . LEU   A 1 268 ? 15.218 -32.086 3.253   1   88.36  ? 267 LEU   A CA   1 1 
ATOM   1967 C  C    . LEU   A 1 268 ? 14.52  -30.73  3.345   1   89.46  ? 267 LEU   A C    1 1 
ATOM   1968 O  O    . LEU   A 1 268 ? 14.761 -29.981 4.289   1   89.52  ? 267 LEU   A O    1 1 
ATOM   1969 C  CB   . LEU   A 1 268 ? 16.486 -31.992 2.387   1   88.23  ? 267 LEU   A CB   1 1 
ATOM   1970 C  CG   . LEU   A 1 268 ? 17.726 -32.851 2.742   1   89.22  ? 267 LEU   A CG   1 1 
ATOM   1971 C  CD1  . LEU   A 1 268 ? 17.439 -34.036 3.674   1   89.69  ? 267 LEU   A CD1  1 1 
ATOM   1972 C  CD2  . LEU   A 1 268 ? 18.402 -33.329 1.508   1   89.67  ? 267 LEU   A CD2  1 1 
ATOM   1973 N  N    . ILE   A 1 269 ? 13.644 -30.424 2.383   1   90.24  ? 268 ILE   A N    1 1 
ATOM   1974 C  CA   . ILE   A 1 269 ? 12.875 -29.185 2.383   1   91.51  ? 268 ILE   A CA   1 1 
ATOM   1975 C  C    . ILE   A 1 269 ? 11.838 -29.205 3.517   1   93.01  ? 268 ILE   A C    1 1 
ATOM   1976 O  O    . ILE   A 1 269 ? 11.648 -28.192 4.192   1   93     ? 268 ILE   A O    1 1 
ATOM   1977 C  CB   . ILE   A 1 269 ? 12.254 -28.942 0.987   1   91.79  ? 268 ILE   A CB   1 1 
ATOM   1978 C  CG1  . ILE   A 1 269 ? 13.351 -28.548 -0.017  1   92.62  ? 268 ILE   A CG1  1 1 
ATOM   1979 C  CG2  . ILE   A 1 269 ? 11.159 -27.877 1.034   1   92.25  ? 268 ILE   A CG2  1 1 
ATOM   1980 C  CD1  . ILE   A 1 269 ? 12.907 -28.543 -1.455  1   93.74  ? 268 ILE   A CD1  1 1 
ATOM   1981 N  N    . LEU   A 1 270 ? 11.217 -30.372 3.766   1   94.13  ? 269 LEU   A N    1 1 
ATOM   1982 C  CA   . LEU   A 1 270 ? 10.245 -30.527 4.844   1   95.78  ? 269 LEU   A CA   1 1 
ATOM   1983 C  C    . LEU   A 1 270 ? 10.894 -30.394 6.223   1   97.27  ? 269 LEU   A C    1 1 
ATOM   1984 O  O    . LEU   A 1 270 ? 10.249 -29.897 7.142   1   97.52  ? 269 LEU   A O    1 1 
ATOM   1985 C  CB   . LEU   A 1 270 ? 9.488  -31.854 4.725   1   96.25  ? 269 LEU   A CB   1 1 
ATOM   1986 C  CG   . LEU   A 1 270 ? 8.524  -31.964 3.543   1   98.06  ? 269 LEU   A CG   1 1 
ATOM   1987 C  CD1  . LEU   A 1 270 ? 7.886  -33.333 3.496   1   98.84  ? 269 LEU   A CD1  1 1 
ATOM   1988 C  CD2  . LEU   A 1 270 ? 7.447  -30.895 3.603   1   98.75  ? 269 LEU   A CD2  1 1 
ATOM   1989 N  N    . ASP   A 1 271 ? 12.173 -30.809 6.36    1   98.12  ? 270 ASP   A N    1 1 
ATOM   1990 C  CA   . ASP   A 1 271 ? 12.946 -30.687 7.603   1   99.41  ? 270 ASP   A CA   1 1 
ATOM   1991 C  C    . ASP   A 1 271 ? 13.151 -29.217 7.981   1   100.4  ? 270 ASP   A C    1 1 
ATOM   1992 O  O    . ASP   A 1 271 ? 13.148 -28.885 9.162   1   100.38 ? 270 ASP   A O    1 1 
ATOM   1993 C  CB   . ASP   A 1 271 ? 14.317 -31.378 7.471   1   101.43 ? 270 ASP   A CB   1 1 
ATOM   1994 C  CG   . ASP   A 1 271 ? 14.304 -32.876 7.703   1   106.19 ? 270 ASP   A CG   1 1 
ATOM   1995 O  OD1  . ASP   A 1 271 ? 13.231 -33.414 8.076   1   106.91 ? 270 ASP   A OD1  1 1 
ATOM   1996 O  OD2  . ASP   A 1 271 ? 15.361 -33.513 7.508   1   108.22 ? 270 ASP   A OD2  1 1 
ATOM   1997 N  N    . LYS   A 1 272 ? 13.311 -28.335 6.979   1   101.2  ? 271 LYS   A N    1 1 
ATOM   1998 C  CA   . LYS   A 1 272 ? 13.476 -26.897 7.194   1   102.46 ? 271 LYS   A CA   1 1 
ATOM   1999 C  C    . LYS   A 1 272 ? 12.126 -26.18  7.438   1   103.75 ? 271 LYS   A C    1 1 
ATOM   2000 O  O    . LYS   A 1 272 ? 12.029 -24.978 7.2     1   103.79 ? 271 LYS   A O    1 1 
ATOM   2001 C  CB   . LYS   A 1 272 ? 14.198 -26.267 5.992   1   104.18 ? 271 LYS   A CB   1 1 
ATOM   2002 C  CG   . LYS   A 1 272 ? 15.64  -25.872 6.272   1   108.15 ? 271 LYS   A CG   1 1 
ATOM   2003 C  CD   . LYS   A 1 272 ? 15.814 -24.357 6.162   1   112.26 ? 271 LYS   A CD   1 1 
ATOM   2004 C  CE   . LYS   A 1 272 ? 17.212 -23.884 6.503   1   115.37 ? 271 LYS   A CE   1 1 
ATOM   2005 N  NZ   . LYS   A 1 272 ? 17.303 -22.397 6.512   1   117.1  ? 271 LYS   A NZ   1 1 
ATOM   2006 N  N    . PHE   A 1 273 ? 11.102 -26.915 7.92    1   104.59 ? 272 PHE   A N    1 1 
ATOM   2007 C  CA   . PHE   A 1 273 ? 9.755  -26.424 8.212   1   106.02 ? 272 PHE   A CA   1 1 
ATOM   2008 C  C    . PHE   A 1 273 ? 9.169  -27.266 9.375   1   106.74 ? 272 PHE   A C    1 1 
ATOM   2009 O  O    . PHE   A 1 273 ? 8.247  -28.063 9.165   1   106.88 ? 272 PHE   A O    1 1 
ATOM   2010 C  CB   . PHE   A 1 273 ? 8.857  -26.571 6.963   1   106.56 ? 272 PHE   A CB   1 1 
ATOM   2011 C  CG   . PHE   A 1 273 ? 8.877  -25.458 5.943   1   107.9  ? 272 PHE   A CG   1 1 
ATOM   2012 C  CD1  . PHE   A 1 273 ? 9.764  -25.485 4.881   1   108.92 ? 272 PHE   A CD1  1 1 
ATOM   2013 C  CD2  . PHE   A 1 273 ? 7.941  -24.44  5.988   1   109.08 ? 272 PHE   A CD2  1 1 
ATOM   2014 C  CE1  . PHE   A 1 273 ? 9.762  -24.478 3.925   1   109.85 ? 272 PHE   A CE1  1 1 
ATOM   2015 C  CE2  . PHE   A 1 273 ? 7.933  -23.44  5.024   1   109.95 ? 272 PHE   A CE2  1 1 
ATOM   2016 C  CZ   . PHE   A 1 273 ? 8.843  -23.465 3.999   1   109.79 ? 272 PHE   A CZ   1 1 
ATOM   2017 N  N    . LEU   A 1 274 ? 9.718  -27.121 10.593  1   107.1  ? 273 LEU   A N    1 1 
ATOM   2018 C  CA   . LEU   A 1 274 ? 9.24   -27.916 11.731  1   107.77 ? 273 LEU   A CA   1 1 
ATOM   2019 C  C    . LEU   A 1 274 ? 9.251  -27.138 13.051  1   108.06 ? 273 LEU   A C    1 1 
ATOM   2020 O  O    . LEU   A 1 274 ? 8.411  -27.375 13.921  1   108.13 ? 273 LEU   A O    1 1 
ATOM   2021 C  CB   . LEU   A 1 274 ? 10.082 -29.204 11.837  1   108.17 ? 273 LEU   A CB   1 1 
ATOM   2022 C  CG   . LEU   A 1 274 ? 9.36   -30.497 12.238  1   109.75 ? 273 LEU   A CG   1 1 
ATOM   2023 C  CD1  . LEU   A 1 274 ? 8.141  -30.76  11.357  1   110.23 ? 273 LEU   A CD1  1 1 
ATOM   2024 C  CD2  . LEU   A 1 274 ? 10.312 -31.685 12.178  1   110.35 ? 273 LEU   A CD2  1 1 
ATOM   2025 N  N    . VAL   B 1 26  ? 5.126  -13.341 22.297  1   110.5  ? 25  VAL   B N    1 2 
ATOM   2026 C  CA   . VAL   B 1 26  ? 4.262  -12.85  23.37   1   111.25 ? 25  VAL   B CA   1 2 
ATOM   2027 C  C    . VAL   B 1 26  ? 3.146  -13.858 23.693  1   111.48 ? 25  VAL   B C    1 2 
ATOM   2028 O  O    . VAL   B 1 26  ? 2.942  -14.21  24.86   1   111.76 ? 25  VAL   B O    1 2 
ATOM   2029 C  CB   . VAL   B 1 26  ? 3.691  -11.449 23.044  1   112.16 ? 25  VAL   B CB   1 2 
ATOM   2030 C  CG1  . VAL   B 1 26  ? 2.782  -10.952 24.169  1   112.63 ? 25  VAL   B CG1  1 2 
ATOM   2031 C  CG2  . VAL   B 1 26  ? 4.814  -10.454 22.761  1   112.75 ? 25  VAL   B CG2  1 2 
ATOM   2032 N  N    . PHE   B 1 27  ? 2.428  -14.321 22.654  1   110.91 ? 26  PHE   B N    1 2 
ATOM   2033 C  CA   . PHE   B 1 27  ? 1.346  -15.305 22.787  1   110.49 ? 26  PHE   B CA   1 2 
ATOM   2034 C  C    . PHE   B 1 27  ? 1.939  -16.663 23.187  1   108.77 ? 26  PHE   B C    1 2 
ATOM   2035 O  O    . PHE   B 1 27  ? 1.399  -17.348 24.055  1   108.78 ? 26  PHE   B O    1 2 
ATOM   2036 C  CB   . PHE   B 1 27  ? 0.582  -15.426 21.453  1   111.02 ? 26  PHE   B CB   1 2 
ATOM   2037 C  CG   . PHE   B 1 27  ? -0.865 -15.854 21.545  1   112.36 ? 26  PHE   B CG   1 2 
ATOM   2038 C  CD1  . PHE   B 1 27  ? -1.754 -15.188 22.377  1   113.47 ? 26  PHE   B CD1  1 2 
ATOM   2039 C  CD2  . PHE   B 1 27  ? -1.356 -16.871 20.743  1   113.41 ? 26  PHE   B CD2  1 2 
ATOM   2040 C  CE1  . PHE   B 1 27  ? -3.095 -15.567 22.439  1   114.2  ? 26  PHE   B CE1  1 2 
ATOM   2041 C  CE2  . PHE   B 1 27  ? -2.699 -17.238 20.798  1   114.19 ? 26  PHE   B CE2  1 2 
ATOM   2042 C  CZ   . PHE   B 1 27  ? -3.558 -16.587 21.649  1   114.06 ? 26  PHE   B CZ   1 2 
ATOM   2043 N  N    . PHE   B 1 28  ? 3.072  -17.035 22.573  1   107.02 ? 27  PHE   B N    1 2 
ATOM   2044 C  CA   . PHE   B 1 28  ? 3.747  -18.295 22.879  1   105.74 ? 27  PHE   B CA   1 2 
ATOM   2045 C  C    . PHE   B 1 28  ? 5.196  -18.042 23.32   1   102.79 ? 27  PHE   B C    1 2 
ATOM   2046 O  O    . PHE   B 1 28  ? 6.118  -18.23  22.522  1   103.2  ? 27  PHE   B O    1 2 
ATOM   2047 C  CB   . PHE   B 1 28  ? 3.712  -19.226 21.65   1   106.39 ? 27  PHE   B CB   1 2 
ATOM   2048 C  CG   . PHE   B 1 28  ? 2.501  -20.126 21.598  1   107.79 ? 27  PHE   B CG   1 2 
ATOM   2049 C  CD1  . PHE   B 1 28  ? 1.226  -19.595 21.493  1   108.87 ? 27  PHE   B CD1  1 2 
ATOM   2050 C  CD2  . PHE   B 1 28  ? 2.639  -21.503 21.651  1   108.9  ? 27  PHE   B CD2  1 2 
ATOM   2051 C  CE1  . PHE   B 1 28  ? 0.113  -20.422 21.451  1   109.75 ? 27  PHE   B CE1  1 2 
ATOM   2052 C  CE2  . PHE   B 1 28  ? 1.523  -22.328 21.607  1   109.84 ? 27  PHE   B CE2  1 2 
ATOM   2053 C  CZ   . PHE   B 1 28  ? 0.267  -21.783 21.508  1   109.69 ? 27  PHE   B CZ   1 2 
ATOM   2054 N  N    . PRO   B 1 29  ? 5.43   -17.606 24.574  1   99.51  ? 28  PRO   B N    1 2 
ATOM   2055 C  CA   . PRO   B 1 29  ? 6.81   -17.327 24.997  1   97.1   ? 28  PRO   B CA   1 2 
ATOM   2056 C  C    . PRO   B 1 29  ? 7.605  -18.563 25.387  1   93.73  ? 28  PRO   B C    1 2 
ATOM   2057 O  O    . PRO   B 1 29  ? 7.042  -19.542 25.865  1   93.89  ? 28  PRO   B O    1 2 
ATOM   2058 C  CB   . PRO   B 1 29  ? 6.643  -16.35  26.172  1   98.27  ? 28  PRO   B CB   1 2 
ATOM   2059 C  CG   . PRO   B 1 29  ? 5.173  -16.281 26.46   1   99.26  ? 28  PRO   B CG   1 2 
ATOM   2060 C  CD   . PRO   B 1 29  ? 4.47   -17.321 25.651  1   98.34  ? 28  PRO   B CD   1 2 
ATOM   2061 N  N    . ARG   B 1 30  ? 8.922  -18.519 25.166  1   90.55  ? 29  ARG   B N    1 2 
ATOM   2062 C  CA   . ARG   B 1 30  ? 9.809  -19.62  25.531  1   87.81  ? 29  ARG   B CA   1 2 
ATOM   2063 C  C    . ARG   B 1 30  ? 10.32  -19.38  26.954  1   84.9   ? 29  ARG   B C    1 2 
ATOM   2064 O  O    . ARG   B 1 30  ? 10.643 -18.242 27.313  1   85.06  ? 29  ARG   B O    1 2 
ATOM   2065 C  CB   . ARG   B 1 30  ? 10.992 -19.736 24.549  1   88.27  ? 29  ARG   B CB   1 2 
ATOM   2066 C  CG   . ARG   B 1 30  ? 10.73  -20.659 23.37   1   89.75  ? 29  ARG   B CG   1 2 
ATOM   2067 C  CD   . ARG   B 1 30  ? 11.842 -20.583 22.345  1   91.59  ? 29  ARG   B CD   1 2 
ATOM   2068 N  NE   . ARG   B 1 30  ? 12.755 -21.721 22.442  1   93.08  ? 29  ARG   B NE   1 2 
ATOM   2069 C  CZ   . ARG   B 1 30  ? 12.858 -22.686 21.532  1   94.09  ? 29  ARG   B CZ   1 2 
ATOM   2070 N  NH1  . ARG   B 1 30  ? 12.112 -22.655 20.435  1   93.25  ? 29  ARG   B NH1  1 2 
ATOM   2071 N  NH2  . ARG   B 1 30  ? 13.716 -23.682 21.707  1   93.71  ? 29  ARG   B NH2  1 2 
ATOM   2072 N  N    . LYS   B 1 31  ? 10.383 -20.44  27.768  1   81.89  ? 30  LYS   B N    1 2 
ATOM   2073 C  CA   . LYS   B 1 31  ? 10.852 -20.307 29.147  1   79.42  ? 30  LYS   B CA   1 2 
ATOM   2074 C  C    . LYS   B 1 31  ? 12.376 -20.082 29.217  1   75.71  ? 30  LYS   B C    1 2 
ATOM   2075 O  O    . LYS   B 1 31  ? 13.145 -20.736 28.507  1   75.76  ? 30  LYS   B O    1 2 
ATOM   2076 C  CB   . LYS   B 1 31  ? 10.357 -21.499 30.016  1   81.78  ? 30  LYS   B CB   1 2 
ATOM   2077 C  CG   . LYS   B 1 31  ? 11.371 -22.242 30.903  1   86.15  ? 30  LYS   B CG   1 2 
ATOM   2078 C  CD   . LYS   B 1 31  ? 11.26  -21.896 32.383  1   90.48  ? 30  LYS   B CD   1 2 
ATOM   2079 C  CE   . LYS   B 1 31  ? 10.407 -22.879 33.155  1   94.14  ? 30  LYS   B CE   1 2 
ATOM   2080 N  NZ   . LYS   B 1 31  ? 9.992  -22.316 34.464  1   96.17  ? 30  LYS   B NZ   1 2 
ATOM   2081 N  N    . ARG   B 1 32  ? 12.792 -19.143 30.074  1   72.27  ? 31  ARG   B N    1 2 
ATOM   2082 C  CA   . ARG   B 1 32  ? 14.197 -18.809 30.266  1   69.49  ? 31  ARG   B CA   1 2 
ATOM   2083 C  C    . ARG   B 1 32  ? 14.755 -19.565 31.457  1   66.09  ? 31  ARG   B C    1 2 
ATOM   2084 O  O    . ARG   B 1 32  ? 14.192 -19.505 32.551  1   66.23  ? 31  ARG   B O    1 2 
ATOM   2085 C  CB   . ARG   B 1 32  ? 14.373 -17.306 30.514  1   70.86  ? 31  ARG   B CB   1 2 
ATOM   2086 C  CG   . ARG   B 1 32  ? 13.813 -16.403 29.421  1   74.37  ? 31  ARG   B CG   1 2 
ATOM   2087 C  CD   . ARG   B 1 32  ? 14.878 -15.471 28.854  1   77.95  ? 31  ARG   B CD   1 2 
ATOM   2088 N  NE   . ARG   B 1 32  ? 15.54  -14.664 29.888  1   80.27  ? 31  ARG   B NE   1 2 
ATOM   2089 C  CZ   . ARG   B 1 32  ? 16.537 -13.815 29.658  1   81.72  ? 31  ARG   B CZ   1 2 
ATOM   2090 N  NH1  . ARG   B 1 32  ? 16.994 -13.636 28.424  1   80.37  ? 31  ARG   B NH1  1 2 
ATOM   2091 N  NH2  . ARG   B 1 32  ? 17.088 -13.142 30.661  1   81.9   ? 31  ARG   B NH2  1 2 
ATOM   2092 N  N    . LYS   B 1 33  ? 15.85  -20.289 31.25   1   62.86  ? 32  LYS   B N    1 2 
ATOM   2093 C  CA   . LYS   B 1 33  ? 16.495 -21.023 32.334  1   59.89  ? 32  LYS   B CA   1 2 
ATOM   2094 C  C    . LYS   B 1 33  ? 17.519 -20.111 33.03   1   58.26  ? 32  LYS   B C    1 2 
ATOM   2095 O  O    . LYS   B 1 33  ? 17.827 -19.023 32.533  1   58.71  ? 32  LYS   B O    1 2 
ATOM   2096 C  CB   . LYS   B 1 33  ? 17.183 -22.288 31.781  1   58.29  ? 32  LYS   B CB   1 2 
ATOM   2097 C  CG   . LYS   B 1 33  ? 18.424 -22.005 30.937  1   56.4   ? 32  LYS   B CG   1 2 
ATOM   2098 C  CD   . LYS   B 1 33  ? 18.867 -23.25  30.205  1   54.65  ? 32  LYS   B CD   1 2 
ATOM   2099 C  CE   . LYS   B 1 33  ? 20.181 -23.092 29.499  1   52.9   ? 32  LYS   B CE   1 2 
ATOM   2100 N  NZ   . LYS   B 1 33  ? 20.574 -24.351 28.821  1   51.89  ? 32  LYS   B NZ   1 2 
ATOM   2101 N  N    . SER   B 1 34  ? 18.061 -20.563 34.162  1   56.02  ? 33  SER   B N    1 2 
ATOM   2102 C  CA   . SER   B 1 34  ? 19.117 -19.834 34.841  1   54.74  ? 33  SER   B CA   1 2 
ATOM   2103 C  C    . SER   B 1 34  ? 20.467 -20.466 34.499  1   52.64  ? 33  SER   B C    1 2 
ATOM   2104 O  O    . SER   B 1 34  ? 20.576 -21.682 34.298  1   52.69  ? 33  SER   B O    1 2 
ATOM   2105 C  CB   . SER   B 1 34  ? 18.903 -19.867 36.354  1   57.09  ? 33  SER   B CB   1 2 
ATOM   2106 O  OG   . SER   B 1 34  ? 19.903 -19.159 37.071  1   60.11  ? 33  SER   B OG   1 2 
ATOM   2107 N  N    . VAL   B 1 35  ? 21.482 -19.635 34.366  1   50.99  ? 34  VAL   B N    1 2 
ATOM   2108 C  CA   . VAL   B 1 35  ? 22.858 -20.119 34.135  1   49.94  ? 34  VAL   B CA   1 2 
ATOM   2109 C  C    . VAL   B 1 35  ? 23.801 -19.667 35.28   1   49.22  ? 34  VAL   B C    1 2 
ATOM   2110 O  O    . VAL   B 1 35  ? 25.017 -19.796 35.154  1   49.41  ? 34  VAL   B O    1 2 
ATOM   2111 C  CB   . VAL   B 1 35  ? 23.442 -19.757 32.747  1   49.35  ? 34  VAL   B CB   1 2 
ATOM   2112 C  CG1  . VAL   B 1 35  ? 22.726 -20.504 31.629  1   50.03  ? 34  VAL   B CG1  1 2 
ATOM   2113 C  CG2  . VAL   B 1 35  ? 23.405 -18.259 32.51   1   48.83  ? 34  VAL   B CG2  1 2 
ATOM   2114 N  N    . ALA   B 1 36  ? 23.24  -19.131 36.38   1   48.02  ? 35  ALA   B N    1 2 
ATOM   2115 C  CA   . ALA   B 1 36  ? 23.967 -18.678 37.546  1   47.2   ? 35  ALA   B CA   1 2 
ATOM   2116 C  C    . ALA   B 1 36  ? 24.736 -19.839 38.148  1   46.33  ? 35  ALA   B C    1 2 
ATOM   2117 O  O    . ALA   B 1 36  ? 24.153 -20.895 38.389  1   46.62  ? 35  ALA   B O    1 2 
ATOM   2118 C  CB   . ALA   B 1 36  ? 22.987 -18.141 38.564  1   46.88  ? 35  ALA   B CB   1 2 
ATOM   2119 N  N    . GLY   B 1 37  ? 26.034 -19.654 38.347  1   45.17  ? 36  GLY   B N    1 2 
ATOM   2120 C  CA   . GLY   B 1 37  ? 26.864 -20.676 38.958  1   44.93  ? 36  GLY   B CA   1 2 
ATOM   2121 C  C    . GLY   B 1 37  ? 27.348 -21.76  38.029  1   45.04  ? 36  GLY   B C    1 2 
ATOM   2122 O  O    . GLY   B 1 37  ? 28.091 -22.639 38.467  1   45.98  ? 36  GLY   B O    1 2 
ATOM   2123 N  N    . GLU   B 1 38  ? 26.917 -21.736 36.754  1   43.89  ? 37  GLU   B N    1 2 
ATOM   2124 C  CA   . GLU   B 1 38  ? 27.392 -22.685 35.749  1   42.71  ? 37  GLU   B CA   1 2 
ATOM   2125 C  C    . GLU   B 1 38  ? 28.835 -22.341 35.412  1   41.04  ? 37  GLU   B C    1 2 
ATOM   2126 O  O    . GLU   B 1 38  ? 29.201 -21.172 35.464  1   41.13  ? 37  GLU   B O    1 2 
ATOM   2127 C  CB   . GLU   B 1 38  ? 26.578 -22.566 34.437  1   44.82  ? 37  GLU   B CB   1 2 
ATOM   2128 C  CG   . GLU   B 1 38  ? 25.09  -22.847 34.544  1   49.66  ? 37  GLU   B CG   1 2 
ATOM   2129 C  CD   . GLU   B 1 38  ? 24.653 -24.283 34.765  1   56.21  ? 37  GLU   B CD   1 2 
ATOM   2130 O  OE1  . GLU   B 1 38  ? 25.514 -25.13  35.088  1   57.42  ? 37  GLU   B OE1  1 2 
ATOM   2131 O  OE2  . GLU   B 1 38  ? 23.439 -24.56  34.628  1   58.66  ? 37  GLU   B OE2  1 2 
ATOM   2132 N  N    . ILE   B 1 39  ? 29.635 -23.329 35.016  1   39.44  ? 38  ILE   B N    1 2 
ATOM   2133 C  CA   . ILE   B 1 39  ? 30.986 -23.047 34.562  1   38.45  ? 38  ILE   B CA   1 2 
ATOM   2134 C  C    . ILE   B 1 39  ? 30.865 -22.905 33.05   1   38     ? 38  ILE   B C    1 2 
ATOM   2135 O  O    . ILE   B 1 39  ? 30.419 -23.829 32.385  1   38.02  ? 38  ILE   B O    1 2 
ATOM   2136 C  CB   . ILE   B 1 39  ? 32.009 -24.113 35.009  1   38.52  ? 38  ILE   B CB   1 2 
ATOM   2137 C  CG1  . ILE   B 1 39  ? 32.255 -24.008 36.542  1   38.8   ? 38  ILE   B CG1  1 2 
ATOM   2138 C  CG2  . ILE   B 1 39  ? 33.316 -23.958 34.241  1   38.72  ? 38  ILE   B CG2  1 2 
ATOM   2139 C  CD1  . ILE   B 1 39  ? 32.936 -25.18  37.079  1   39.44  ? 38  ILE   B CD1  1 2 
ATOM   2140 N  N    . VAL   B 1 40  ? 31.143 -21.706 32.531  1   37.06  ? 39  VAL   B N    1 2 
ATOM   2141 C  CA   . VAL   B 1 40  ? 31.038 -21.394 31.116  1   36.17  ? 39  VAL   B CA   1 2 
ATOM   2142 C  C    . VAL   B 1 40  ? 32.41  -21.175 30.521  1   36.27  ? 39  VAL   B C    1 2 
ATOM   2143 O  O    . VAL   B 1 40  ? 33.125 -20.266 30.939  1   35.65  ? 39  VAL   B O    1 2 
ATOM   2144 C  CB   . VAL   B 1 40  ? 30.134 -20.157 30.873  1   35.95  ? 39  VAL   B CB   1 2 
ATOM   2145 C  CG1  . VAL   B 1 40  ? 29.971 -19.882 29.374  1   36.05  ? 39  VAL   B CG1  1 2 
ATOM   2146 C  CG2  . VAL   B 1 40  ? 28.776 -20.339 31.533  1   35.91  ? 39  VAL   B CG2  1 2 
ATOM   2147 N  N    . LEU   B 1 41  ? 32.769 -21.992 29.509  1   36.29  ? 40  LEU   B N    1 2 
ATOM   2148 C  CA   . LEU   B 1 41  ? 34.038 -21.827 28.82   1   36.25  ? 40  LEU   B CA   1 2 
ATOM   2149 C  C    . LEU   B 1 41  ? 33.782 -21.191 27.466  1   35.79  ? 40  LEU   B C    1 2 
ATOM   2150 O  O    . LEU   B 1 41  ? 33.071 -21.76  26.643  1   35.64  ? 40  LEU   B O    1 2 
ATOM   2151 C  CB   . LEU   B 1 41  ? 34.78  -23.158 28.664  1   36.69  ? 40  LEU   B CB   1 2 
ATOM   2152 C  CG   . LEU   B 1 41  ? 36.278 -23.054 28.301  1   37.51  ? 40  LEU   B CG   1 2 
ATOM   2153 C  CD1  . LEU   B 1 41  ? 37.004 -24.272 28.754  1   38.02  ? 40  LEU   B CD1  1 2 
ATOM   2154 C  CD2  . LEU   B 1 41  ? 36.484 -22.939 26.807  1   37.78  ? 40  LEU   B CD2  1 2 
ATOM   2155 N  N    . ILE   B 1 42  ? 34.364 -20.001 27.243  1   35.3   ? 41  ILE   B N    1 2 
ATOM   2156 C  CA   . ILE   B 1 42  ? 34.228 -19.274 25.992  1   35.21  ? 41  ILE   B CA   1 2 
ATOM   2157 C  C    . ILE   B 1 42  ? 35.584 -19.119 25.316  1   34.75  ? 41  ILE   B C    1 2 
ATOM   2158 O  O    . ILE   B 1 42  ? 36.489 -18.51  25.883  1   35.28  ? 41  ILE   B O    1 2 
ATOM   2159 C  CB   . ILE   B 1 42  ? 33.557 -17.901 26.21   1   35.67  ? 41  ILE   B CB   1 2 
ATOM   2160 C  CG1  . ILE   B 1 42  ? 32.201 -18.057 26.907  1   36.59  ? 41  ILE   B CG1  1 2 
ATOM   2161 C  CG2  . ILE   B 1 42  ? 33.415 -17.145 24.894  1   36.22  ? 41  ILE   B CG2  1 2 
ATOM   2162 C  CD1  . ILE   B 1 42  ? 31.697 -16.781 27.45   1   38.08  ? 41  ILE   B CD1  1 2 
ATOM   2163 N  N    . THR   B 1 43  ? 35.734 -19.706 24.126  1   33.41  ? 42  THR   B N    1 2 
ATOM   2164 C  CA   . THR   B 1 43  ? 36.949 -19.588 23.323  1   32.71  ? 42  THR   B CA   1 2 
ATOM   2165 C  C    . THR   B 1 43  ? 36.855 -18.319 22.457  1   31.52  ? 42  THR   B C    1 2 
ATOM   2166 O  O    . THR   B 1 43  ? 35.753 -17.874 22.136  1   31.3   ? 42  THR   B O    1 2 
ATOM   2167 C  CB   . THR   B 1 43  ? 37.218 -20.865 22.507  1   33.18  ? 42  THR   B CB   1 2 
ATOM   2168 O  OG1  . THR   B 1 43  ? 36.342 -20.934 21.391  1   34.56  ? 42  THR   B OG1  1 2 
ATOM   2169 C  CG2  . THR   B 1 43  ? 37.103 -22.112 23.33   1   32.81  ? 42  THR   B CG2  1 2 
ATOM   2170 N  N    . GLY   B 1 44  ? 37.995 -17.739 22.113  1   30.8   ? 43  GLY   B N    1 2 
ATOM   2171 C  CA   . GLY   B 1 44  ? 38.012 -16.487 21.367  1   31.07  ? 43  GLY   B CA   1 2 
ATOM   2172 C  C    . GLY   B 1 44  ? 37.392 -15.343 22.155  1   31.32  ? 43  GLY   B C    1 2 
ATOM   2173 O  O    . GLY   B 1 44  ? 36.815 -14.41  21.589  1   30.77  ? 43  GLY   B O    1 2 
ATOM   2174 N  N    . ALA   B 1 45  ? 37.518 -15.396 23.483  1   32.56  ? 44  ALA   B N    1 2 
ATOM   2175 C  CA   . ALA   B 1 45  ? 36.932 -14.385 24.353  1   33.66  ? 44  ALA   B CA   1 2 
ATOM   2176 C  C    . ALA   B 1 45  ? 37.699 -13.061 24.434  1   34.45  ? 44  ALA   B C    1 2 
ATOM   2177 O  O    . ALA   B 1 45  ? 37.274 -12.169 25.158  1   35.23  ? 44  ALA   B O    1 2 
ATOM   2178 C  CB   . ALA   B 1 45  ? 36.734 -14.965 25.74   1   33.96  ? 44  ALA   B CB   1 2 
ATOM   2179 N  N    . GLY   B 1 46  ? 38.808 -12.95  23.716  1   34.53  ? 45  GLY   B N    1 2 
ATOM   2180 C  CA   . GLY   B 1 46  ? 39.674 -11.78  23.742  1   36.02  ? 45  GLY   B CA   1 2 
ATOM   2181 C  C    . GLY   B 1 46  ? 39.203 -10.584 22.942  1   37.58  ? 45  GLY   B C    1 2 
ATOM   2182 O  O    . GLY   B 1 46  ? 39.788 -9.506  23.054  1   38.88  ? 45  GLY   B O    1 2 
ATOM   2183 N  N    . HIS   B 1 47  ? 38.143 -10.75  22.139  1   36.98  ? 46  HIS   B N    1 2 
ATOM   2184 C  CA   . HIS   B 1 47  ? 37.596 -9.677  21.315  1   36.28  ? 46  HIS   B CA   1 2 
ATOM   2185 C  C    . HIS   B 1 47  ? 36.213 -10.08  20.761  1   36.04  ? 46  HIS   B C    1 2 
ATOM   2186 O  O    . HIS   B 1 47  ? 35.839 -11.25  20.816  1   36.5   ? 46  HIS   B O    1 2 
ATOM   2187 C  CB   . HIS   B 1 47  ? 38.579 -9.433  20.143  1   37.15  ? 46  HIS   B CB   1 2 
ATOM   2188 C  CG   . HIS   B 1 47  ? 38.328 -8.186  19.347  1   39.11  ? 46  HIS   B CG   1 2 
ATOM   2189 N  ND1  . HIS   B 1 47  ? 38.597 -6.938  19.865  1   41.32  ? 46  HIS   B ND1  1 2 
ATOM   2190 C  CD2  . HIS   B 1 47  ? 37.846 -8.042  18.095  1   40.18  ? 46  HIS   B CD2  1 2 
ATOM   2191 C  CE1  . HIS   B 1 47  ? 38.27  -6.082  18.92   1   41.81  ? 46  HIS   B CE1  1 2 
ATOM   2192 N  NE2  . HIS   B 1 47  ? 37.811 -6.702  17.838  1   41.56  ? 46  HIS   B NE2  1 2 
ATOM   2193 N  N    . GLY   B 1 48  ? 35.496 -9.116  20.2    1   35.54  ? 47  GLY   B N    1 2 
ATOM   2194 C  CA   . GLY   B 1 48  ? 34.248 -9.305  19.476  1   35.53  ? 47  GLY   B CA   1 2 
ATOM   2195 C  C    . GLY   B 1 48  ? 33.162 -10.136 20.119  1   36.1   ? 47  GLY   B C    1 2 
ATOM   2196 O  O    . GLY   B 1 48  ? 32.839 -9.953  21.294  1   35.85  ? 47  GLY   B O    1 2 
ATOM   2197 N  N    . ILE   B 1 49  ? 32.581 -11.062 19.345  1   36.2   ? 48  ILE   B N    1 2 
ATOM   2198 C  CA   . ILE   B 1 49  ? 31.48  -11.9   19.827  1   36.11  ? 48  ILE   B CA   1 2 
ATOM   2199 C  C    . ILE   B 1 49  ? 31.819 -12.651 21.13   1   36.22  ? 48  ILE   B C    1 2 
ATOM   2200 O  O    . ILE   B 1 49  ? 31.007 -12.665 22.038  1   35.93  ? 48  ILE   B O    1 2 
ATOM   2201 C  CB   . ILE   B 1 49  ? 30.972 -12.839 18.707  1   35.86  ? 48  ILE   B CB   1 2 
ATOM   2202 C  CG1  . ILE   B 1 49  ? 30.488 -12.005 17.495  1   36.02  ? 48  ILE   B CG1  1 2 
ATOM   2203 C  CG2  . ILE   B 1 49  ? 29.856 -13.733 19.207  1   36.31  ? 48  ILE   B CG2  1 2 
ATOM   2204 C  CD1  . ILE   B 1 49  ? 30.228 -12.8   16.284  1   36.17  ? 48  ILE   B CD1  1 2 
ATOM   2205 N  N    . GLY   B 1 50  ? 33.024 -13.196 21.228  1   36.36  ? 49  GLY   B N    1 2 
ATOM   2206 C  CA   . GLY   B 1 50  ? 33.475 -13.931 22.4    1   36.72  ? 49  GLY   B CA   1 2 
ATOM   2207 C  C    . GLY   B 1 50  ? 33.557 -13.077 23.648  1   37.28  ? 49  GLY   B C    1 2 
ATOM   2208 O  O    . GLY   B 1 50  ? 33.159 -13.53  24.722  1   37.48  ? 49  GLY   B O    1 2 
ATOM   2209 N  N    . ARG   B 1 51  ? 34.062 -11.828 23.507  1   36.83  ? 50  ARG   B N    1 2 
ATOM   2210 C  CA   . ARG   B 1 51  ? 34.21  -10.851 24.584  1   36.91  ? 50  ARG   B CA   1 2 
ATOM   2211 C  C    . ARG   B 1 51  ? 32.846 -10.384 25.075  1   37.88  ? 50  ARG   B C    1 2 
ATOM   2212 O  O    . ARG   B 1 51  ? 32.611 -10.336 26.274  1   37.46  ? 50  ARG   B O    1 2 
ATOM   2213 C  CB   . ARG   B 1 51  ? 35.059 -9.654  24.092  1   37.2   ? 50  ARG   B CB   1 2 
ATOM   2214 C  CG   . ARG   B 1 51  ? 34.931 -8.357  24.908  1   38.16  ? 50  ARG   B CG   1 2 
ATOM   2215 C  CD   . ARG   B 1 51  ? 35.909 -7.291  24.473  1   39.15  ? 50  ARG   B CD   1 2 
ATOM   2216 N  NE   . ARG   B 1 51  ? 37.279 -7.626  24.868  1   40.79  ? 50  ARG   B NE   1 2 
ATOM   2217 C  CZ   . ARG   B 1 51  ? 38.334 -6.84   24.664  1   42.97  ? 50  ARG   B CZ   1 2 
ATOM   2218 N  NH1  . ARG   B 1 51  ? 38.19  -5.668  24.056  1   43.48  ? 50  ARG   B NH1  1 2 
ATOM   2219 N  NH2  . ARG   B 1 51  ? 39.545 -7.229  25.046  1   42.31  ? 50  ARG   B NH2  1 2 
ATOM   2220 N  N    . TRP   B 1 52  ? 31.951 -10.018 24.154  1   38.74  ? 51  TRP   B N    1 2 
ATOM   2221 C  CA   . TRP   B 1 52  ? 30.626 -9.534  24.529  1   39.6   ? 51  TRP   B CA   1 2 
ATOM   2222 C  C    . TRP   B 1 52  ? 29.716 -10.667 24.995  1   40.63  ? 51  TRP   B C    1 2 
ATOM   2223 O  O    . TRP   B 1 52  ? 28.841 -10.416 25.805  1   41.45  ? 51  TRP   B O    1 2 
ATOM   2224 C  CB   . TRP   B 1 52  ? 30.029 -8.68   23.43   1   39.82  ? 51  TRP   B CB   1 2 
ATOM   2225 C  CG   . TRP   B 1 52  ? 30.776 -7.385  23.33   1   41.18  ? 51  TRP   B CG   1 2 
ATOM   2226 C  CD1  . TRP   B 1 52  ? 31.982 -7.172  22.717  1   42.32  ? 51  TRP   B CD1  1 2 
ATOM   2227 C  CD2  . TRP   B 1 52  ? 30.438 -6.16   23.989  1   41.22  ? 51  TRP   B CD2  1 2 
ATOM   2228 N  NE1  . TRP   B 1 52  ? 32.399 -5.878  22.938  1   42.67  ? 51  TRP   B NE1  1 2 
ATOM   2229 C  CE2  . TRP   B 1 52  ? 31.459 -5.231  23.7    1   42.13  ? 51  TRP   B CE2  1 2 
ATOM   2230 C  CE3  . TRP   B 1 52  ? 29.355 -5.749  24.765  1   41.95  ? 51  TRP   B CE3  1 2 
ATOM   2231 C  CZ2  . TRP   B 1 52  ? 31.422 -3.922  24.167  1   42.7   ? 51  TRP   B CZ2  1 2 
ATOM   2232 C  CZ3  . TRP   B 1 52  ? 29.321 -4.449  25.227  1   42.6   ? 51  TRP   B CZ3  1 2 
ATOM   2233 C  CH2  . TRP   B 1 52  ? 30.346 -3.555  24.929  1   42.7   ? 51  TRP   B CH2  1 2 
ATOM   2234 N  N    . THR   B 1 53  ? 29.971 -11.929 24.581  1   40.57  ? 52  THR   B N    1 2 
ATOM   2235 C  CA   . THR   B 1 53  ? 29.232 -13.07  25.123  1   40.15  ? 52  THR   B CA   1 2 
ATOM   2236 C  C    . THR   B 1 53  ? 29.671 -13.273 26.582  1   40.57  ? 52  THR   B C    1 2 
ATOM   2237 O  O    . THR   B 1 53  ? 28.822 -13.508 27.444  1   41.12  ? 52  THR   B O    1 2 
ATOM   2238 C  CB   . THR   B 1 53  ? 29.478 -14.297 24.295  1   40.31  ? 52  THR   B CB   1 2 
ATOM   2239 O  OG1  . THR   B 1 53  ? 28.957 -14.029 23.006  1   41.57  ? 52  THR   B OG1  1 2 
ATOM   2240 C  CG2  . THR   B 1 53  ? 28.811 -15.52  24.863  1   40.49  ? 52  THR   B CG2  1 2 
ATOM   2241 N  N    . ALA   B 1 54  ? 30.985 -13.107 26.875  1   40.26  ? 53  ALA   B N    1 2 
ATOM   2242 C  CA   . ALA   B 1 54  ? 31.532 -13.201 28.217  1   41.19  ? 53  ALA   B CA   1 2 
ATOM   2243 C  C    . ALA   B 1 54  ? 30.852 -12.193 29.145  1   42.08  ? 53  ALA   B C    1 2 
ATOM   2244 O  O    . ALA   B 1 54  ? 30.476 -12.559 30.256  1   42.52  ? 53  ALA   B O    1 2 
ATOM   2245 C  CB   . ALA   B 1 54  ? 33.038 -12.97  28.193  1   40.99  ? 53  ALA   B CB   1 2 
ATOM   2246 N  N    . TYR   B 1 55  ? 30.621 -10.952 28.666  1   41.95  ? 54  TYR   B N    1 2 
ATOM   2247 C  CA   . TYR   B 1 55  ? 29.955 -9.932  29.478  1   42.28  ? 54  TYR   B CA   1 2 
ATOM   2248 C  C    . TYR   B 1 55  ? 28.511 -10.342 29.754  1   43.48  ? 54  TYR   B C    1 2 
ATOM   2249 O  O    . TYR   B 1 55  ? 28.024 -10.094 30.852  1   44.21  ? 54  TYR   B O    1 2 
ATOM   2250 C  CB   . TYR   B 1 55  ? 29.975 -8.534  28.82   1   41.46  ? 54  TYR   B CB   1 2 
ATOM   2251 C  CG   . TYR   B 1 55  ? 31.342 -7.959  28.509  1   41.31  ? 54  TYR   B CG   1 2 
ATOM   2252 C  CD1  . TYR   B 1 55  ? 32.482 -8.43   29.149  1   42.04  ? 54  TYR   B CD1  1 2 
ATOM   2253 C  CD2  . TYR   B 1 55  ? 31.492 -6.936  27.582  1   41.67  ? 54  TYR   B CD2  1 2 
ATOM   2254 C  CE1  . TYR   B 1 55  ? 33.739 -7.917  28.855  1   42.86  ? 54  TYR   B CE1  1 2 
ATOM   2255 C  CE2  . TYR   B 1 55  ? 32.744 -6.415  27.279  1   42.5   ? 54  TYR   B CE2  1 2 
ATOM   2256 C  CZ   . TYR   B 1 55  ? 33.864 -6.887  27.939  1   43.72  ? 54  TYR   B CZ   1 2 
ATOM   2257 O  OH   . TYR   B 1 55  ? 35.106 -6.362  27.657  1   45.23  ? 54  TYR   B OH   1 2 
ATOM   2258 N  N    . GLU   B 1 56  ? 27.832 -10.987 28.783  1   43.4   ? 55  GLU   B N    1 2 
ATOM   2259 C  CA   . GLU   B 1 56  ? 26.458 -11.438 28.995  1   43.91  ? 55  GLU   B CA   1 2 
ATOM   2260 C  C    . GLU   B 1 56  ? 26.371 -12.5   30.09   1   44.3   ? 55  GLU   B C    1 2 
ATOM   2261 O  O    . GLU   B 1 56  ? 25.477 -12.441 30.936  1   45.19  ? 55  GLU   B O    1 2 
ATOM   2262 C  CB   . GLU   B 1 56  ? 25.826 -11.965 27.699  1   45.7   ? 55  GLU   B CB   1 2 
ATOM   2263 C  CG   . GLU   B 1 56  ? 25.62  -10.905 26.633  1   52.14  ? 55  GLU   B CG   1 2 
ATOM   2264 C  CD   . GLU   B 1 56  ? 24.541 -9.868  26.884  1   61.61  ? 55  GLU   B CD   1 2 
ATOM   2265 O  OE1  . GLU   B 1 56  ? 23.834 -9.959  27.914  1   63.47  ? 55  GLU   B OE1  1 2 
ATOM   2266 O  OE2  . GLU   B 1 56  ? 24.4   -8.958  26.035  1   66     ? 55  GLU   B OE2  1 2 
ATOM   2267 N  N    . PHE   B 1 57  ? 27.297 -13.46  30.075  1   43.57  ? 56  PHE   B N    1 2 
ATOM   2268 C  CA   . PHE   B 1 57  ? 27.337 -14.527 31.066  1   43.55  ? 56  PHE   B CA   1 2 
ATOM   2269 C  C    . PHE   B 1 57  ? 27.785 -14.003 32.43   1   44.49  ? 56  PHE   B C    1 2 
ATOM   2270 O  O    . PHE   B 1 57  ? 27.306 -14.501 33.447  1   44.77  ? 56  PHE   B O    1 2 
ATOM   2271 C  CB   . PHE   B 1 57  ? 28.229 -15.678 30.593  1   42.8   ? 56  PHE   B CB   1 2 
ATOM   2272 C  CG   . PHE   B 1 57  ? 27.572 -16.68  29.68   1   42.66  ? 56  PHE   B CG   1 2 
ATOM   2273 C  CD1  . PHE   B 1 57  ? 26.721 -17.649 30.185  1   43.11  ? 56  PHE   B CD1  1 2 
ATOM   2274 C  CD2  . PHE   B 1 57  ? 27.858 -16.699 28.322  1   43.04  ? 56  PHE   B CD2  1 2 
ATOM   2275 C  CE1  . PHE   B 1 57  ? 26.158 -18.609 29.344  1   43.52  ? 56  PHE   B CE1  1 2 
ATOM   2276 C  CE2  . PHE   B 1 57  ? 27.28  -17.645 27.486  1   43.09  ? 56  PHE   B CE2  1 2 
ATOM   2277 C  CZ   . PHE   B 1 57  ? 26.44  -18.596 28.002  1   42.75  ? 56  PHE   B CZ   1 2 
ATOM   2278 N  N    . ALA   B 1 58  ? 28.632 -12.958 32.462  1   45.05  ? 57  ALA   B N    1 2 
ATOM   2279 C  CA   . ALA   B 1 58  ? 29.04  -12.323 33.718  1   46.21  ? 57  ALA   B CA   1 2 
ATOM   2280 C  C    . ALA   B 1 58  ? 27.83  -11.675 34.379  1   47.68  ? 57  ALA   B C    1 2 
ATOM   2281 O  O    . ALA   B 1 58  ? 27.691 -11.744 35.61   1   48.55  ? 57  ALA   B O    1 2 
ATOM   2282 C  CB   . ALA   B 1 58  ? 30.108 -11.271 33.466  1   46.38  ? 57  ALA   B CB   1 2 
ATOM   2283 N  N    . LYS   B 1 59  ? 26.934 -11.052 33.58   1   47.92  ? 58  LYS   B N    1 2 
ATOM   2284 C  CA   . LYS   B 1 59  ? 25.713 -10.465 34.155  1   48.25  ? 58  LYS   B CA   1 2 
ATOM   2285 C  C    . LYS   B 1 59  ? 24.731 -11.585 34.596  1   47.56  ? 58  LYS   B C    1 2 
ATOM   2286 O  O    . LYS   B 1 59  ? 23.974 -11.371 35.507  1   46.94  ? 58  LYS   B O    1 2 
ATOM   2287 C  CB   . LYS   B 1 59  ? 25.068 -9.434  33.202  1   50.67  ? 58  LYS   B CB   1 2 
ATOM   2288 C  CG   . LYS   B 1 59  ? 25.879 -8.131  33.082  1   55.74  ? 58  LYS   B CG   1 2 
ATOM   2289 C  CD   . LYS   B 1 59  ? 25.358 -7.127  32.015  1   61.24  ? 58  LYS   B CD   1 2 
ATOM   2290 C  CE   . LYS   B 1 59  ? 25.753 -7.506  30.598  1   66.76  ? 58  LYS   B CE   1 2 
ATOM   2291 N  NZ   . LYS   B 1 59  ? 25.383 -6.479  29.57   1   69.34  ? 58  LYS   B NZ   1 2 
ATOM   2292 N  N    . GLN   B 1 60  ? 24.798 -12.795 33.99   1   47.76  ? 59  GLN   B N    1 2 
ATOM   2293 C  CA   . GLN   B 1 60  ? 23.964 -13.955 34.351  1   48.11  ? 59  GLN   B CA   1 2 
ATOM   2294 C  C    . GLN   B 1 60  ? 24.437 -14.712 35.628  1   48.76  ? 59  GLN   B C    1 2 
ATOM   2295 O  O    . GLN   B 1 60  ? 23.838 -15.734 35.998  1   48.86  ? 59  GLN   B O    1 2 
ATOM   2296 C  CB   . GLN   B 1 60  ? 23.909 -14.95  33.188  1   48.91  ? 59  GLN   B CB   1 2 
ATOM   2297 C  CG   . GLN   B 1 60  ? 23.143 -14.46  31.972  1   51.6   ? 59  GLN   B CG   1 2 
ATOM   2298 C  CD   . GLN   B 1 60  ? 21.681 -14.205 32.251  1   55.9   ? 59  GLN   B CD   1 2 
ATOM   2299 O  OE1  . GLN   B 1 60  ? 21.023 -14.904 33.039  1   56.32  ? 59  GLN   B OE1  1 2 
ATOM   2300 N  NE2  . GLN   B 1 60  ? 21.135 -13.197 31.587  1   57.35  ? 59  GLN   B NE2  1 2 
ATOM   2301 N  N    . LYS   B 1 61  ? 25.515 -14.211 36.272  1   48.45  ? 60  LYS   B N    1 2 
ATOM   2302 C  CA   . LYS   B 1 61  ? 26.161 -14.721 37.48   1   48.09  ? 60  LYS   B CA   1 2 
ATOM   2303 C  C    . LYS   B 1 61  ? 26.829 -16.11  37.282  1   47.08  ? 60  LYS   B C    1 2 
ATOM   2304 O  O    . LYS   B 1 61  ? 26.923 -16.89  38.241  1   47.83  ? 60  LYS   B O    1 2 
ATOM   2305 C  CB   . LYS   B 1 61  ? 25.211 -14.698 38.691  1   49.91  ? 60  LYS   B CB   1 2 
ATOM   2306 C  CG   . LYS   B 1 61  ? 24.592 -13.34  38.944  1   54.19  ? 60  LYS   B CG   1 2 
ATOM   2307 C  CD   . LYS   B 1 61  ? 23.785 -13.348 40.249  1   59.46  ? 60  LYS   B CD   1 2 
ATOM   2308 C  CE   . LYS   B 1 61  ? 23.09  -12.017 40.497  1   64.64  ? 60  LYS   B CE   1 2 
ATOM   2309 N  NZ   . LYS   B 1 61  ? 22.066 -12.074 41.591  1   68.41  ? 60  LYS   B NZ   1 2 
ATOM   2310 N  N    . SER   B 1 62  ? 27.331 -16.393 36.066  1   45     ? 61  SER   B N    1 2 
ATOM   2311 C  CA   . SER   B 1 62  ? 28.042 -17.647 35.746  1   43.65  ? 61  SER   B CA   1 2 
ATOM   2312 C  C    . SER   B 1 62  ? 29.525 -17.554 36.183  1   42.48  ? 61  SER   B C    1 2 
ATOM   2313 O  O    . SER   B 1 62  ? 30.057 -16.446 36.329  1   42.55  ? 61  SER   B O    1 2 
ATOM   2314 C  CB   . SER   B 1 62  ? 28.051 -17.869 34.232  1   43.91  ? 61  SER   B CB   1 2 
ATOM   2315 O  OG   . SER   B 1 62  ? 26.808 -18.269 33.684  1   45.69  ? 61  SER   B OG   1 2 
ATOM   2316 N  N    . ARG   B 1 63  ? 30.206 -18.713 36.321  1   41.03  ? 62  ARG   B N    1 2 
ATOM   2317 C  CA   . ARG   B 1 63  ? 31.632 -18.818 36.635  1   40.45  ? 62  ARG   B CA   1 2 
ATOM   2318 C  C    . ARG   B 1 63  ? 32.327 -18.95  35.274  1   40.03  ? 62  ARG   B C    1 2 
ATOM   2319 O  O    . ARG   B 1 63  ? 32.17  -19.97  34.604  1   40     ? 62  ARG   B O    1 2 
ATOM   2320 C  CB   . ARG   B 1 63  ? 31.899 -20.066 37.494  1   41.75  ? 62  ARG   B CB   1 2 
ATOM   2321 C  CG   . ARG   B 1 63  ? 31.689 -19.876 38.977  1   45.44  ? 62  ARG   B CG   1 2 
ATOM   2322 C  CD   . ARG   B 1 63  ? 30.97  -21.054 39.638  1   49.74  ? 62  ARG   B CD   1 2 
ATOM   2323 N  NE   . ARG   B 1 63  ? 31.878 -22.156 39.978  1   53.04  ? 62  ARG   B NE   1 2 
ATOM   2324 C  CZ   . ARG   B 1 63  ? 31.513 -23.435 40.045  1   54.83  ? 62  ARG   B CZ   1 2 
ATOM   2325 N  NH1  . ARG   B 1 63  ? 30.252 -23.787 39.813  1   53.36  ? 62  ARG   B NH1  1 2 
ATOM   2326 N  NH2  . ARG   B 1 63  ? 32.406 -24.372 40.349  1   54.98  ? 62  ARG   B NH2  1 2 
ATOM   2327 N  N    . LEU   B 1 64  ? 33.025 -17.902 34.823  1   39.25  ? 63  LEU   B N    1 2 
ATOM   2328 C  CA   . LEU   B 1 64  ? 33.616 -17.892 33.486  1   37.97  ? 63  LEU   B CA   1 2 
ATOM   2329 C  C    . LEU   B 1 64  ? 35.034 -18.435 33.392  1   37     ? 63  LEU   B C    1 2 
ATOM   2330 O  O    . LEU   B 1 64  ? 35.855 -18.242 34.286  1   37.24  ? 63  LEU   B O    1 2 
ATOM   2331 C  CB   . LEU   B 1 64  ? 33.615 -16.463 32.931  1   38.44  ? 63  LEU   B CB   1 2 
ATOM   2332 C  CG   . LEU   B 1 64  ? 32.27  -15.788 32.721  1   40.21  ? 63  LEU   B CG   1 2 
ATOM   2333 C  CD1  . LEU   B 1 64  ? 32.412 -14.281 32.812  1   41.13  ? 63  LEU   B CD1  1 2 
ATOM   2334 C  CD2  . LEU   B 1 64  ? 31.701 -16.142 31.37   1   40.53  ? 63  LEU   B CD2  1 2 
ATOM   2335 N  N    . VAL   B 1 65  ? 35.318 -19.107 32.274  1   36.15  ? 64  VAL   B N    1 2 
ATOM   2336 C  CA   . VAL   B 1 65  ? 36.623 -19.63  31.884  1   35.4   ? 64  VAL   B CA   1 2 
ATOM   2337 C  C    . VAL   B 1 65  ? 36.827 -19.096 30.467  1   35.03  ? 64  VAL   B C    1 2 
ATOM   2338 O  O    . VAL   B 1 65  ? 36.01  -19.355 29.583  1   35.41  ? 64  VAL   B O    1 2 
ATOM   2339 C  CB   . VAL   B 1 65  ? 36.754 -21.158 31.952  1   35.47  ? 64  VAL   B CB   1 2 
ATOM   2340 C  CG1  . VAL   B 1 65  ? 38.163 -21.577 31.553  1   36.25  ? 64  VAL   B CG1  1 2 
ATOM   2341 C  CG2  . VAL   B 1 65  ? 36.418 -21.681 33.343  1   35.69  ? 64  VAL   B CG2  1 2 
ATOM   2342 N  N    . LEU   B 1 66  ? 37.82  -18.232 30.287  1   33.91  ? 65  LEU   B N    1 2 
ATOM   2343 C  CA   . LEU   B 1 66  ? 38.044 -17.579 29.005  1   32.98  ? 65  LEU   B CA   1 2 
ATOM   2344 C  C    . LEU   B 1 66  ? 39.334 -18.059 28.358  1   32.77  ? 65  LEU   B C    1 2 
ATOM   2345 O  O    . LEU   B 1 66  ? 40.377 -18.122 29.007  1   32.57  ? 65  LEU   B O    1 2 
ATOM   2346 C  CB   . LEU   B 1 66  ? 38.033 -16.048 29.18   1   32.41  ? 65  LEU   B CB   1 2 
ATOM   2347 C  CG   . LEU   B 1 66  ? 36.836 -15.461 29.946  1   32.25  ? 65  LEU   B CG   1 2 
ATOM   2348 C  CD1  . LEU   B 1 66  ? 36.992 -13.979 30.123  1   32.38  ? 65  LEU   B CD1  1 2 
ATOM   2349 C  CD2  . LEU   B 1 66  ? 35.52  -15.779 29.239  1   32.01  ? 65  LEU   B CD2  1 2 
ATOM   2350 N  N    . TRP   B 1 67  ? 39.253 -18.412 27.069  1   32.86  ? 66  TRP   B N    1 2 
ATOM   2351 C  CA   . TRP   B 1 67  ? 40.381 -18.909 26.286  1   32.8   ? 66  TRP   B CA   1 2 
ATOM   2352 C  C    . TRP   B 1 67  ? 40.645 -18.049 25.084  1   34.85  ? 66  TRP   B C    1 2 
ATOM   2353 O  O    . TRP   B 1 67  ? 39.709 -17.639 24.407  1   35.94  ? 66  TRP   B O    1 2 
ATOM   2354 C  CB   . TRP   B 1 67  ? 40.081 -20.329 25.793  1   31.27  ? 66  TRP   B CB   1 2 
ATOM   2355 C  CG   . TRP   B 1 67  ? 40.292 -21.424 26.802  1   29.95  ? 66  TRP   B CG   1 2 
ATOM   2356 C  CD1  . TRP   B 1 67  ? 40.383 -21.301 28.16   1   30.2   ? 66  TRP   B CD1  1 2 
ATOM   2357 C  CD2  . TRP   B 1 67  ? 40.36  -22.821 26.519  1   29.11  ? 66  TRP   B CD2  1 2 
ATOM   2358 N  NE1  . TRP   B 1 67  ? 40.561 -22.535 28.734  1   30.16  ? 66  TRP   B NE1  1 2 
ATOM   2359 C  CE2  . TRP   B 1 67  ? 40.54  -23.49  27.748  1   29.93  ? 66  TRP   B CE2  1 2 
ATOM   2360 C  CE3  . TRP   B 1 67  ? 40.284 -23.574 25.344  1   29.35  ? 66  TRP   B CE3  1 2 
ATOM   2361 C  CZ2  . TRP   B 1 67  ? 40.665 -24.875 27.827  1   30.24  ? 66  TRP   B CZ2  1 2 
ATOM   2362 C  CZ3  . TRP   B 1 67  ? 40.398 -24.944 25.426  1   30.21  ? 66  TRP   B CZ3  1 2 
ATOM   2363 C  CH2  . TRP   B 1 67  ? 40.59  -25.581 26.654  1   30.27  ? 66  TRP   B CH2  1 2 
ATOM   2364 N  N    . ASP   B 1 68  ? 41.916 -17.838 24.761  1   35.2   ? 67  ASP   B N    1 2 
ATOM   2365 C  CA   . ASP   B 1 68  ? 42.301 -17.081 23.579  1   35.35  ? 67  ASP   B CA   1 2 
ATOM   2366 C  C    . ASP   B 1 68  ? 43.813 -17.135 23.381  1   36.38  ? 67  ASP   B C    1 2 
ATOM   2367 O  O    . ASP   B 1 68  ? 44.548 -17.329 24.342  1   36.62  ? 67  ASP   B O    1 2 
ATOM   2368 C  CB   . ASP   B 1 68  ? 41.827 -15.616 23.686  1   35.7   ? 67  ASP   B CB   1 2 
ATOM   2369 C  CG   . ASP   B 1 68  ? 41.636 -14.946 22.336  1   37.29  ? 67  ASP   B CG   1 2 
ATOM   2370 O  OD1  . ASP   B 1 68  ? 42.642 -14.736 21.632  1   36.58  ? 67  ASP   B OD1  1 2 
ATOM   2371 O  OD2  . ASP   B 1 68  ? 40.482 -14.616 21.998  1   38.07  ? 67  ASP   B OD2  1 2 
ATOM   2372 N  N    . ILE   B 1 69  ? 44.282 -16.987 22.135  1   37.1   ? 68  ILE   B N    1 2 
ATOM   2373 C  CA   . ILE   B 1 69  ? 45.722 -16.908 21.845  1   37.45  ? 68  ILE   B CA   1 2 
ATOM   2374 C  C    . ILE   B 1 69  ? 46.271 -15.518 22.183  1   37.77  ? 68  ILE   B C    1 2 
ATOM   2375 O  O    . ILE   B 1 69  ? 47.478 -15.372 22.342  1   38.13  ? 68  ILE   B O    1 2 
ATOM   2376 C  CB   . ILE   B 1 69  ? 46.032 -17.266 20.385  1   37.98  ? 68  ILE   B CB   1 2 
ATOM   2377 C  CG1  . ILE   B 1 69  ? 45.139 -16.466 19.419  1   38.87  ? 68  ILE   B CG1  1 2 
ATOM   2378 C  CG2  . ILE   B 1 69  ? 45.936 -18.755 20.156  1   38.42  ? 68  ILE   B CG2  1 2 
ATOM   2379 C  CD1  . ILE   B 1 69  ? 45.494 -16.588 18.031  1   39.95  ? 68  ILE   B CD1  1 2 
ATOM   2380 N  N    . ASN   B 1 70  ? 45.391 -14.504 22.267  1   38.15  ? 69  ASN   B N    1 2 
ATOM   2381 C  CA   . ASN   B 1 70  ? 45.693 -13.13  22.615  1   39.37  ? 69  ASN   B CA   1 2 
ATOM   2382 C  C    . ASN   B 1 70  ? 45.502 -12.956 24.15   1   39.69  ? 69  ASN   B C    1 2 
ATOM   2383 O  O    . ASN   B 1 70  ? 44.391 -12.781 24.652  1   40.03  ? 69  ASN   B O    1 2 
ATOM   2384 C  CB   . ASN   B 1 70  ? 44.794 -12.194 21.794  1   41.6   ? 69  ASN   B CB   1 2 
ATOM   2385 C  CG   . ASN   B 1 70  ? 44.938 -10.732 22.128  1   46.9   ? 69  ASN   B CG   1 2 
ATOM   2386 O  OD1  . ASN   B 1 70  ? 45.922 -10.294 22.732  1   46.93  ? 69  ASN   B OD1  1 2 
ATOM   2387 N  ND2  . ASN   B 1 70  ? 43.936 -9.936  21.743  1   49.75  ? 69  ASN   B ND2  1 2 
ATOM   2388 N  N    . LYS   B 1 71  ? 46.613 -13.043 24.878  1   39.41  ? 70  LYS   B N    1 2 
ATOM   2389 C  CA   . LYS   B 1 71  ? 46.683 -12.93  26.321  1   40     ? 70  LYS   B CA   1 2 
ATOM   2390 C  C    . LYS   B 1 71  ? 46.164 -11.58  26.82   1   41.4   ? 70  LYS   B C    1 2 
ATOM   2391 O  O    . LYS   B 1 71  ? 45.297 -11.541 27.701  1   41.73  ? 70  LYS   B O    1 2 
ATOM   2392 C  CB   . LYS   B 1 71  ? 48.126 -13.174 26.78   1   40.85  ? 70  LYS   B CB   1 2 
ATOM   2393 C  CG   . LYS   B 1 71  ? 48.29  -13.27  28.287  1   44.49  ? 70  LYS   B CG   1 2 
ATOM   2394 C  CD   . LYS   B 1 71  ? 49.714 -13.679 28.658  1   48.04  ? 70  LYS   B CD   1 2 
ATOM   2395 C  CE   . LYS   B 1 71  ? 49.896 -13.92  30.142  1   51.88  ? 70  LYS   B CE   1 2 
ATOM   2396 N  NZ   . LYS   B 1 71  ? 49.775 -12.66  30.919  1   53.72  ? 70  LYS   B NZ   1 2 
ATOM   2397 N  N    . HIS   B 1 72  ? 46.667 -10.482 26.238  1   41.66  ? 71  HIS   B N    1 2 
ATOM   2398 C  CA   . HIS   B 1 72  ? 46.292 -9.116  26.586  1   42.21  ? 71  HIS   B CA   1 2 
ATOM   2399 C  C    . HIS   B 1 72  ? 44.789 -8.892  26.476  1   42.45  ? 71  HIS   B C    1 2 
ATOM   2400 O  O    . HIS   B 1 72  ? 44.198 -8.29   27.37   1   43.12  ? 71  HIS   B O    1 2 
ATOM   2401 C  CB   . HIS   B 1 72  ? 47.04  -8.116  25.673  1   43.1   ? 71  HIS   B CB   1 2 
ATOM   2402 C  CG   . HIS   B 1 72  ? 46.601 -6.696  25.86   1   45.9   ? 71  HIS   B CG   1 2 
ATOM   2403 N  ND1  . HIS   B 1 72  ? 47.016 -5.952  26.958  1   47.5   ? 71  HIS   B ND1  1 2 
ATOM   2404 C  CD2  . HIS   B 1 72  ? 45.749 -5.947  25.118  1   46.83  ? 71  HIS   B CD2  1 2 
ATOM   2405 C  CE1  . HIS   B 1 72  ? 46.432 -4.772  26.827  1   47.89  ? 71  HIS   B CE1  1 2 
ATOM   2406 N  NE2  . HIS   B 1 72  ? 45.643 -4.729  25.752  1   48.07  ? 71  HIS   B NE2  1 2 
ATOM   2407 N  N    . GLY   B 1 73  ? 44.202 -9.331  25.371  1   41.86  ? 72  GLY   B N    1 2 
ATOM   2408 C  CA   . GLY   B 1 73  ? 42.786 -9.146  25.105  1   42.05  ? 72  GLY   B CA   1 2 
ATOM   2409 C  C    . GLY   B 1 73  ? 41.877 -9.953  25.999  1   42.11  ? 72  GLY   B C    1 2 
ATOM   2410 O  O    . GLY   B 1 73  ? 40.806 -9.467  26.379  1   43.05  ? 72  GLY   B O    1 2 
ATOM   2411 N  N    . VAL   B 1 74  ? 42.273 -11.198 26.318  1   40.76  ? 73  VAL   B N    1 2 
ATOM   2412 C  CA   . VAL   B 1 74  ? 41.425 -12.044 27.14   1   40.67  ? 73  VAL   B CA   1 2 
ATOM   2413 C  C    . VAL   B 1 74  ? 41.447 -11.543 28.595  1   41.31  ? 73  VAL   B C    1 2 
ATOM   2414 O  O    . VAL   B 1 74  ? 40.389 -11.489 29.235  1   41.69  ? 73  VAL   B O    1 2 
ATOM   2415 C  CB   . VAL   B 1 74  ? 41.688 -13.565 26.967  1   41.17  ? 73  VAL   B CB   1 2 
ATOM   2416 C  CG1  . VAL   B 1 74  ? 42.83  -14.071 27.85   1   41.55  ? 73  VAL   B CG1  1 2 
ATOM   2417 C  CG2  . VAL   B 1 74  ? 40.418 -14.367 27.202  1   41.42  ? 73  VAL   B CG2  1 2 
ATOM   2418 N  N    . GLU   B 1 75  ? 42.605 -11.05  29.075  1   40.83  ? 74  GLU   B N    1 2 
ATOM   2419 C  CA   . GLU   B 1 75  ? 42.696 -10.48  30.421  1   40.55  ? 74  GLU   B CA   1 2 
ATOM   2420 C  C    . GLU   B 1 75  ? 41.943 -9.156  30.515  1   41.87  ? 74  GLU   B C    1 2 
ATOM   2421 O  O    . GLU   B 1 75  ? 41.445 -8.812  31.576  1   42.52  ? 74  GLU   B O    1 2 
ATOM   2422 C  CB   . GLU   B 1 75  ? 44.159 -10.324 30.825  1   40.65  ? 74  GLU   B CB   1 2 
ATOM   2423 C  CG   . GLU   B 1 75  ? 44.852 -11.666 30.814  1   43.46  ? 74  GLU   B CG   1 2 
ATOM   2424 C  CD   . GLU   B 1 75  ? 46.303 -11.702 31.233  1   49.22  ? 74  GLU   B CD   1 2 
ATOM   2425 O  OE1  . GLU   B 1 75  ? 46.895 -10.615 31.434  1   50.97  ? 74  GLU   B OE1  1 2 
ATOM   2426 O  OE2  . GLU   B 1 75  ? 46.843 -12.827 31.367  1   50.55  ? 74  GLU   B OE2  1 2 
ATOM   2427 N  N    . GLU   B 1 76  ? 41.832 -8.42   29.401  1   42.53  ? 75  GLU   B N    1 2 
ATOM   2428 C  CA   . GLU   B 1 76  ? 41.079 -7.175  29.32   1   43.44  ? 75  GLU   B CA   1 2 
ATOM   2429 C  C    . GLU   B 1 76  ? 39.566 -7.499  29.403  1   43.86  ? 75  GLU   B C    1 2 
ATOM   2430 O  O    . GLU   B 1 76  ? 38.812 -6.787  30.067  1   44.56  ? 75  GLU   B O    1 2 
ATOM   2431 C  CB   . GLU   B 1 76  ? 41.434 -6.469  28.009  1   45.91  ? 75  GLU   B CB   1 2 
ATOM   2432 C  CG   . GLU   B 1 76  ? 40.996 -5.024  27.943  1   52.74  ? 75  GLU   B CG   1 2 
ATOM   2433 C  CD   . GLU   B 1 76  ? 41.344 -4.325  26.642  1   62.54  ? 75  GLU   B CD   1 2 
ATOM   2434 O  OE1  . GLU   B 1 76  ? 41.67  -5.017  25.646  1   65.11  ? 75  GLU   B OE1  1 2 
ATOM   2435 O  OE2  . GLU   B 1 76  ? 41.275 -3.074  26.617  1   66.15  ? 75  GLU   B OE2  1 2 
ATOM   2436 N  N    . THR   B 1 77  ? 39.136 -8.596  28.762  1   43.34  ? 76  THR   B N    1 2 
ATOM   2437 C  CA   . THR   B 1 77  ? 37.753 -9.056  28.824  1   43.18  ? 76  THR   B CA   1 2 
ATOM   2438 C  C    . THR   B 1 77  ? 37.435 -9.465  30.268  1   42.86  ? 76  THR   B C    1 2 
ATOM   2439 O  O    . THR   B 1 77  ? 36.396 -9.077  30.795  1   42.38  ? 76  THR   B O    1 2 
ATOM   2440 C  CB   . THR   B 1 77  ? 37.549 -10.249 27.856  1   43.69  ? 76  THR   B CB   1 2 
ATOM   2441 O  OG1  . THR   B 1 77  ? 37.622 -9.77   26.513  1   45.02  ? 76  THR   B OG1  1 2 
ATOM   2442 C  CG2  . THR   B 1 77  ? 36.225 -10.981 28.075  1   43.16  ? 76  THR   B CG2  1 2 
ATOM   2443 N  N    . ALA   B 1 78  ? 38.346 -10.22  30.903  1   43.24  ? 77  ALA   B N    1 2 
ATOM   2444 C  CA   . ALA   B 1 78  ? 38.198 -10.733 32.263  1   44.3   ? 77  ALA   B CA   1 2 
ATOM   2445 C  C    . ALA   B 1 78  ? 38.147 -9.631  33.312  1   45.74  ? 77  ALA   B C    1 2 
ATOM   2446 O  O    . ALA   B 1 78  ? 37.414 -9.758  34.29   1   46.47  ? 77  ALA   B O    1 2 
ATOM   2447 C  CB   . ALA   B 1 78  ? 39.332 -11.67  32.575  1   44.43  ? 77  ALA   B CB   1 2 
ATOM   2448 N  N    . ALA   B 1 79  ? 38.909 -8.536  33.114  1   46.02  ? 78  ALA   B N    1 2 
ATOM   2449 C  CA   . ALA   B 1 79  ? 38.879 -7.414  34.059  1   46.17  ? 78  ALA   B CA   1 2 
ATOM   2450 C  C    . ALA   B 1 79  ? 37.51  -6.769  34.031  1   46.94  ? 78  ALA   B C    1 2 
ATOM   2451 O  O    . ALA   B 1 79  ? 36.956 -6.482  35.084  1   48.26  ? 78  ALA   B O    1 2 
ATOM   2452 C  CB   . ALA   B 1 79  ? 39.952 -6.4    33.706  1   45.88  ? 78  ALA   B CB   1 2 
ATOM   2453 N  N    . GLU   B 1 80  ? 36.928 -6.613  32.836  1   47.18  ? 79  GLU   B N    1 2 
ATOM   2454 C  CA   . GLU   B 1 80  ? 35.606 -6.023  32.657  1   47.7   ? 79  GLU   B CA   1 2 
ATOM   2455 C  C    . GLU   B 1 80  ? 34.522 -6.975  33.201  1   47.43  ? 79  GLU   B C    1 2 
ATOM   2456 O  O    . GLU   B 1 80  ? 33.553 -6.496  33.799  1   48.03  ? 79  GLU   B O    1 2 
ATOM   2457 C  CB   . GLU   B 1 80  ? 35.341 -5.677  31.18   1   50.69  ? 79  GLU   B CB   1 2 
ATOM   2458 C  CG   . GLU   B 1 80  ? 35.648 -4.26   30.694  1   57.88  ? 79  GLU   B CG   1 2 
ATOM   2459 C  CD   . GLU   B 1 80  ? 35.322 -3.085  31.606  1   68.37  ? 79  GLU   B CD   1 2 
ATOM   2460 O  OE1  . GLU   B 1 80  ? 34.242 -3.062  32.242  1   71.05  ? 79  GLU   B OE1  1 2 
ATOM   2461 O  OE2  . GLU   B 1 80  ? 36.183 -2.182  31.703  1   71.45  ? 79  GLU   B OE2  1 2 
ATOM   2462 N  N    . CYS   B 1 81  ? 34.717 -8.309  33.068  1   46.54  ? 80  CYS   B N    1 2 
ATOM   2463 C  CA   . CYS   B 1 81  ? 33.796 -9.323  33.603  1   46.36  ? 80  CYS   B CA   1 2 
ATOM   2464 C  C    . CYS   B 1 81  ? 33.83  -9.319  35.13   1   47.86  ? 80  CYS   B C    1 2 
ATOM   2465 O  O    . CYS   B 1 81  ? 32.78  -9.442  35.769  1   48.55  ? 80  CYS   B O    1 2 
ATOM   2466 C  CB   . CYS   B 1 81  ? 34.112 -10.705 33.049  1   45.72  ? 80  CYS   B CB   1 2 
ATOM   2467 S  SG   . CYS   B 1 81  ? 33.696 -10.917 31.301  1   45.24  ? 80  CYS   B SG   1 2 
ATOM   2468 N  N    . ARG   B 1 82  ? 35.016 -9.122  35.722  1   48.09  ? 81  ARG   B N    1 2 
ATOM   2469 C  CA   . ARG   B 1 82  ? 35.133 -9.01   37.168  1   48.81  ? 81  ARG   B CA   1 2 
ATOM   2470 C  C    . ARG   B 1 82  ? 34.464 -7.733  37.655  1   50.64  ? 81  ARG   B C    1 2 
ATOM   2471 O  O    . ARG   B 1 82  ? 33.799 -7.767  38.687  1   50.5   ? 81  ARG   B O    1 2 
ATOM   2472 C  CB   . ARG   B 1 82  ? 36.591 -9.085  37.624  1   48.68  ? 81  ARG   B CB   1 2 
ATOM   2473 C  CG   . ARG   B 1 82  ? 37.158 -10.465 37.381  1   48.79  ? 81  ARG   B CG   1 2 
ATOM   2474 C  CD   . ARG   B 1 82  ? 38.543 -10.634 37.961  1   47.55  ? 81  ARG   B CD   1 2 
ATOM   2475 N  NE   . ARG   B 1 82  ? 39.115 -11.876 37.453  1   46.37  ? 81  ARG   B NE   1 2 
ATOM   2476 C  CZ   . ARG   B 1 82  ? 40.042 -11.949 36.503  1   42.75  ? 81  ARG   B CZ   1 2 
ATOM   2477 N  NH1  . ARG   B 1 82  ? 40.594 -10.843 36.021  1   40.67  ? 81  ARG   B NH1  1 2 
ATOM   2478 N  NH2  . ARG   B 1 82  ? 40.455 -13.131 36.06   1   39.48  ? 81  ARG   B NH2  1 2 
ATOM   2479 N  N    . LYS   B 1 83  ? 34.567 -6.619  36.897  1   51.94  ? 82  LYS   B N    1 2 
ATOM   2480 C  CA   . LYS   B 1 83  ? 33.872 -5.378  37.294  1   53.18  ? 82  LYS   B CA   1 2 
ATOM   2481 C  C    . LYS   B 1 83  ? 32.335 -5.583  37.311  1   53.32  ? 82  LYS   B C    1 2 
ATOM   2482 O  O    . LYS   B 1 83  ? 31.64  -4.924  38.083  1   53.79  ? 82  LYS   B O    1 2 
ATOM   2483 C  CB   . LYS   B 1 83  ? 34.267 -4.21   36.384  1   55.57  ? 82  LYS   B CB   1 2 
ATOM   2484 C  CG   . LYS   B 1 83  ? 35.697 -3.736  36.599  1   60.65  ? 82  LYS   B CG   1 2 
ATOM   2485 C  CD   . LYS   B 1 83  ? 36.163 -2.795  35.5    1   66.9   ? 82  LYS   B CD   1 2 
ATOM   2486 C  CE   . LYS   B 1 83  ? 35.316 -1.543  35.381  1   72.61  ? 82  LYS   B CE   1 2 
ATOM   2487 N  NZ   . LYS   B 1 83  ? 35.463 -0.898  34.025  1   76.35  ? 82  LYS   B NZ   1 2 
ATOM   2488 N  N    . LEU   B 1 84  ? 31.828 -6.535  36.493  1   52.82  ? 83  LEU   B N    1 2 
ATOM   2489 C  CA   . LEU   B 1 84  ? 30.423 -6.927  36.429  1   52.73  ? 83  LEU   B CA   1 2 
ATOM   2490 C  C    . LEU   B 1 84  ? 29.983 -7.871  37.577  1   52.83  ? 83  LEU   B C    1 2 
ATOM   2491 O  O    . LEU   B 1 84  ? 28.81  -8.252  37.62   1   53.64  ? 83  LEU   B O    1 2 
ATOM   2492 C  CB   . LEU   B 1 84  ? 30.127 -7.595  35.09   1   52.68  ? 83  LEU   B CB   1 2 
ATOM   2493 C  CG   . LEU   B 1 84  ? 30.167 -6.682  33.88   1   53.69  ? 83  LEU   B CG   1 2 
ATOM   2494 C  CD1  . LEU   B 1 84  ? 30.093 -7.487  32.599  1   53.78  ? 83  LEU   B CD1  1 2 
ATOM   2495 C  CD2  . LEU   B 1 84  ? 29.056 -5.664  33.944  1   54.17  ? 83  LEU   B CD2  1 2 
ATOM   2496 N  N    . GLY   B 1 85  ? 30.912 -8.254  38.459  1   51.66  ? 84  GLY   B N    1 2 
ATOM   2497 C  CA   . GLY   B 1 85  ? 30.646 -9.097  39.618  1   51.07  ? 84  GLY   B CA   1 2 
ATOM   2498 C  C    . GLY   B 1 85  ? 30.994 -10.572 39.496  1   50.47  ? 84  GLY   B C    1 2 
ATOM   2499 O  O    . GLY   B 1 85  ? 30.884 -11.311 40.481  1   50.79  ? 84  GLY   B O    1 2 
ATOM   2500 N  N    . ALA   B 1 86  ? 31.444 -11.013 38.311  1   48.87  ? 85  ALA   B N    1 2 
ATOM   2501 C  CA   . ALA   B 1 86  ? 31.748 -12.424 38.046  1   48.19  ? 85  ALA   B CA   1 2 
ATOM   2502 C  C    . ALA   B 1 86  ? 33.135 -12.927 38.443  1   47.6   ? 85  ALA   B C    1 2 
ATOM   2503 O  O    . ALA   B 1 86  ? 34.108 -12.174 38.405  1   48.09  ? 85  ALA   B O    1 2 
ATOM   2504 C  CB   . ALA   B 1 86  ? 31.539 -12.725 36.562  1   48.08  ? 85  ALA   B CB   1 2 
ATOM   2505 N  N    . THR   B 1 87  ? 33.235 -14.244 38.755  1   46.24  ? 86  THR   B N    1 2 
ATOM   2506 C  CA   . THR   B 1 87  ? 34.521 -14.908 38.98   1   44.78  ? 86  THR   B CA   1 2 
ATOM   2507 C  C    . THR   B 1 87  ? 35.021 -15.407 37.598  1   43.73  ? 86  THR   B C    1 2 
ATOM   2508 O  O    . THR   B 1 87  ? 34.263 -16.024 36.833  1   44.18  ? 86  THR   B O    1 2 
ATOM   2509 C  CB   . THR   B 1 87  ? 34.419 -15.98  40.039  1   44.71  ? 86  THR   B CB   1 2 
ATOM   2510 O  OG1  . THR   B 1 87  ? 34.249 -15.304 41.277  1   46.12  ? 86  THR   B OG1  1 2 
ATOM   2511 C  CG2  . THR   B 1 87  ? 35.675 -16.822 40.127  1   44.53  ? 86  THR   B CG2  1 2 
ATOM   2512 N  N    . VAL   B 1 88  ? 36.258 -15.034 37.234  1   41.8   ? 87  VAL   B N    1 2 
ATOM   2513 C  CA   . VAL   B 1 88  ? 36.797 -15.336 35.921  1   39.93  ? 87  VAL   B CA   1 2 
ATOM   2514 C  C    . VAL   B 1 88  ? 38.181 -15.918 35.959  1   38.36  ? 87  VAL   B C    1 2 
ATOM   2515 O  O    . VAL   B 1 88  ? 39.067 -15.346 36.583  1   37.45  ? 87  VAL   B O    1 2 
ATOM   2516 C  CB   . VAL   B 1 88  ? 36.839 -14.071 35.043  1   40.08  ? 87  VAL   B CB   1 2 
ATOM   2517 C  CG1  . VAL   B 1 88  ? 37.284 -14.43  33.637  1   40.27  ? 87  VAL   B CG1  1 2 
ATOM   2518 C  CG2  . VAL   B 1 88  ? 35.497 -13.353 35.017  1   40.35  ? 87  VAL   B CG2  1 2 
ATOM   2519 N  N    . HIS   B 1 89  ? 38.402 -16.969 35.152  1   37.73  ? 88  HIS   B N    1 2 
ATOM   2520 C  CA   . HIS   B 1 89  ? 39.709 -17.578 34.956  1   36.97  ? 88  HIS   B CA   1 2 
ATOM   2521 C  C    . HIS   B 1 89  ? 40.079 -17.467 33.495  1   36.27  ? 88  HIS   B C    1 2 
ATOM   2522 O  O    . HIS   B 1 89  ? 39.28  -17.83  32.643  1   36.73  ? 88  HIS   B O    1 2 
ATOM   2523 C  CB   . HIS   B 1 89  ? 39.674 -19.053 35.333  1   37.3   ? 88  HIS   B CB   1 2 
ATOM   2524 C  CG   . HIS   B 1 89  ? 39.681 -19.274 36.799  1   38.87  ? 88  HIS   B CG   1 2 
ATOM   2525 N  ND1  . HIS   B 1 89  ? 38.511 -19.257 37.526  1   40.97  ? 88  HIS   B ND1  1 2 
ATOM   2526 C  CD2  . HIS   B 1 89  ? 40.725 -19.488 37.635  1   39.85  ? 88  HIS   B CD2  1 2 
ATOM   2527 C  CE1  . HIS   B 1 89  ? 38.869 -19.471 38.786  1   41.51  ? 88  HIS   B CE1  1 2 
ATOM   2528 N  NE2  . HIS   B 1 89  ? 40.195 -19.629 38.9    1   41.32  ? 88  HIS   B NE2  1 2 
ATOM   2529 N  N    . THR   B 1 90  ? 41.294 -17.011 33.192  1   35.25  ? 89  THR   B N    1 2 
ATOM   2530 C  CA   . THR   B 1 90  ? 41.757 -16.933 31.814  1   34.72  ? 89  THR   B CA   1 2 
ATOM   2531 C  C    . THR   B 1 90  ? 42.867 -17.948 31.561  1   33.59  ? 89  THR   B C    1 2 
ATOM   2532 O  O    . THR   B 1 90  ? 43.668 -18.238 32.447  1   33.26  ? 89  THR   B O    1 2 
ATOM   2533 C  CB   . THR   B 1 90  ? 42.206 -15.494 31.452  1   35.5   ? 89  THR   B CB   1 2 
ATOM   2534 O  OG1  . THR   B 1 90  ? 43.345 -15.153 32.229  1   36.52  ? 89  THR   B OG1  1 2 
ATOM   2535 C  CG2  . THR   B 1 90  ? 41.112 -14.476 31.642  1   34.66  ? 89  THR   B CG2  1 2 
ATOM   2536 N  N    . PHE   B 1 91  ? 42.941 -18.442 30.333  1   33.38  ? 90  PHE   B N    1 2 
ATOM   2537 C  CA   . PHE   B 1 91  ? 43.975 -19.363 29.876  1   33.39  ? 90  PHE   B CA   1 2 
ATOM   2538 C  C    . PHE   B 1 91  ? 44.383 -18.938 28.46   1   33.84  ? 90  PHE   B C    1 2 
ATOM   2539 O  O    . PHE   B 1 91  ? 43.513 -18.59  27.648  1   34.54  ? 90  PHE   B O    1 2 
ATOM   2540 C  CB   . PHE   B 1 91  ? 43.465 -20.832 29.906  1   33.17  ? 90  PHE   B CB   1 2 
ATOM   2541 C  CG   . PHE   B 1 91  ? 43.114 -21.347 31.3    1   34.44  ? 90  PHE   B CG   1 2 
ATOM   2542 C  CD1  . PHE   B 1 91  ? 44.075 -21.945 32.1    1   35.31  ? 90  PHE   B CD1  1 2 
ATOM   2543 C  CD2  . PHE   B 1 91  ? 41.831 -21.199 31.814  1   35.13  ? 90  PHE   B CD2  1 2 
ATOM   2544 C  CE1  . PHE   B 1 91  ? 43.763 -22.381 33.384  1   36.55  ? 90  PHE   B CE1  1 2 
ATOM   2545 C  CE2  . PHE   B 1 91  ? 41.521 -21.635 33.093  1   36.56  ? 90  PHE   B CE2  1 2 
ATOM   2546 C  CZ   . PHE   B 1 91  ? 42.49  -22.22  33.876  1   36.49  ? 90  PHE   B CZ   1 2 
ATOM   2547 N  N    . VAL   B 1 92  ? 45.697 -18.926 28.159  1   33.28  ? 91  VAL   B N    1 2 
ATOM   2548 C  CA   . VAL   B 1 92  ? 46.146 -18.653 26.801  1   33.35  ? 91  VAL   B CA   1 2 
ATOM   2549 C  C    . VAL   B 1 92  ? 46.167 -20.002 26.092  1   34.11  ? 91  VAL   B C    1 2 
ATOM   2550 O  O    . VAL   B 1 92  ? 47.011 -20.847 26.41   1   35.15  ? 91  VAL   B O    1 2 
ATOM   2551 C  CB   . VAL   B 1 92  ? 47.517 -17.985 26.699  1   33.09  ? 91  VAL   B CB   1 2 
ATOM   2552 C  CG1  . VAL   B 1 92  ? 47.834 -17.706 25.232  1   32.65  ? 91  VAL   B CG1  1 2 
ATOM   2553 C  CG2  . VAL   B 1 92  ? 47.571 -16.71  27.525  1   33.52  ? 91  VAL   B CG2  1 2 
ATOM   2554 N  N    . VAL   B 1 93  ? 45.201 -20.246 25.198  1   32.87  ? 92  VAL   B N    1 2 
ATOM   2555 C  CA   . VAL   B 1 93  ? 45.089 -21.55  24.534  1   31.83  ? 92  VAL   B CA   1 2 
ATOM   2556 C  C    . VAL   B 1 93  ? 44.885 -21.374 23.032  1   31.23  ? 92  VAL   B C    1 2 
ATOM   2557 O  O    . VAL   B 1 93  ? 44.033 -20.594 22.63   1   31.03  ? 92  VAL   B O    1 2 
ATOM   2558 C  CB   . VAL   B 1 93  ? 43.921 -22.41  25.131  1   31.55  ? 92  VAL   B CB   1 2 
ATOM   2559 C  CG1  . VAL   B 1 93  ? 43.992 -23.867 24.675  1   31.21  ? 92  VAL   B CG1  1 2 
ATOM   2560 C  CG2  . VAL   B 1 93  ? 43.857 -22.319 26.666  1   31.72  ? 92  VAL   B CG2  1 2 
ATOM   2561 N  N    . ASP   B 1 94  ? 45.645 -22.122 22.211  1   30.48  ? 93  ASP   B N    1 2 
ATOM   2562 C  CA   . ASP   B 1 94  ? 45.487 -22.169 20.758  1   29.83  ? 93  ASP   B CA   1 2 
ATOM   2563 C  C    . ASP   B 1 94  ? 44.392 -23.186 20.534  1   29.97  ? 93  ASP   B C    1 2 
ATOM   2564 O  O    . ASP   B 1 94  ? 44.626 -24.39  20.679  1   29.99  ? 93  ASP   B O    1 2 
ATOM   2565 C  CB   . ASP   B 1 94  ? 46.779 -22.622 20.09   1   30.51  ? 93  ASP   B CB   1 2 
ATOM   2566 C  CG   . ASP   B 1 94  ? 46.762 -22.692 18.558  1   36.19  ? 93  ASP   B CG   1 2 
ATOM   2567 O  OD1  . ASP   B 1 94  ? 45.667 -22.538 17.953  1   35.28  ? 93  ASP   B OD1  1 2 
ATOM   2568 O  OD2  . ASP   B 1 94  ? 47.835 -22.929 17.968  1   39.04  ? 93  ASP   B OD2  1 2 
ATOM   2569 N  N    . CYS   B 1 95  ? 43.186 -22.697 20.2    1   29.96  ? 94  CYS   B N    1 2 
ATOM   2570 C  CA   . CYS   B 1 95  ? 41.999 -23.519 20.01   1   30.3   ? 94  CYS   B CA   1 2 
ATOM   2571 C  C    . CYS   B 1 95  ? 41.916 -24.228 18.639  1   31.1   ? 94  CYS   B C    1 2 
ATOM   2572 O  O    . CYS   B 1 95  ? 40.868 -24.755 18.27   1   31.32  ? 94  CYS   B O    1 2 
ATOM   2573 C  CB   . CYS   B 1 95  ? 40.748 -22.715 20.314  1   30.75  ? 94  CYS   B CB   1 2 
ATOM   2574 S  SG   . CYS   B 1 95  ? 40.75  -21.991 21.975  1   36.79  ? 94  CYS   B SG   1 2 
ATOM   2575 N  N    . GLY   B 1 96  ? 43.038 -24.271 17.933  1   31.31  ? 95  GLY   B N    1 2 
ATOM   2576 C  CA   . GLY   B 1 96  ? 43.235 -25.023 16.702  1   31.45  ? 95  GLY   B CA   1 2 
ATOM   2577 C  C    . GLY   B 1 96  ? 44.274 -26.127 16.891  1   31.64  ? 95  GLY   B C    1 2 
ATOM   2578 O  O    . GLY   B 1 96  ? 44.488 -26.938 15.984  1   32.37  ? 95  GLY   B O    1 2 
ATOM   2579 N  N    . ASN   B 1 97  ? 44.921 -26.183 18.098  1   30.85  ? 96  ASN   B N    1 2 
ATOM   2580 C  CA   . ASN   B 1 97  ? 45.954 -27.131 18.493  1   30.11  ? 96  ASN   B CA   1 2 
ATOM   2581 C  C    . ASN   B 1 97  ? 45.411 -28.166 19.485  1   30.39  ? 96  ASN   B C    1 2 
ATOM   2582 O  O    . ASN   B 1 97  ? 45.191 -27.839 20.641  1   30.33  ? 96  ASN   B O    1 2 
ATOM   2583 C  CB   . ASN   B 1 97  ? 47.121 -26.372 19.114  1   29.77  ? 96  ASN   B CB   1 2 
ATOM   2584 C  CG   . ASN   B 1 97  ? 48.344 -27.209 19.327  1   32.35  ? 96  ASN   B CG   1 2 
ATOM   2585 O  OD1  . ASN   B 1 97  ? 48.411 -28.072 20.195  1   32.55  ? 96  ASN   B OD1  1 2 
ATOM   2586 N  ND2  . ASN   B 1 97  ? 49.344 -26.983 18.518  1   34.56  ? 96  ASN   B ND2  1 2 
ATOM   2587 N  N    . ARG   B 1 98  ? 45.254 -29.419 19.038  1   30.58  ? 97  ARG   B N    1 2 
ATOM   2588 C  CA   . ARG   B 1 98  ? 44.751 -30.538 19.819  1   31.21  ? 97  ARG   B CA   1 2 
ATOM   2589 C  C    . ARG   B 1 98  ? 45.506 -30.765 21.145  1   32.64  ? 97  ARG   B C    1 2 
ATOM   2590 O  O    . ARG   B 1 98  ? 44.867 -30.92  22.185  1   33.24  ? 97  ARG   B O    1 2 
ATOM   2591 C  CB   . ARG   B 1 98  ? 44.789 -31.802 18.963  1   32.1   ? 97  ARG   B CB   1 2 
ATOM   2592 C  CG   . ARG   B 1 98  ? 43.986 -32.947 19.526  1   36.49  ? 97  ARG   B CG   1 2 
ATOM   2593 C  CD   . ARG   B 1 98  ? 44.09  -34.177 18.665  1   41.33  ? 97  ARG   B CD   1 2 
ATOM   2594 N  NE   . ARG   B 1 98  ? 45.456 -34.695 18.678  1   47.62  ? 97  ARG   B NE   1 2 
ATOM   2595 C  CZ   . ARG   B 1 98  ? 45.867 -35.708 19.436  1   52.6   ? 97  ARG   B CZ   1 2 
ATOM   2596 N  NH1  . ARG   B 1 98  ? 45.004 -36.368 20.202  1   52.1   ? 97  ARG   B NH1  1 2 
ATOM   2597 N  NH2  . ARG   B 1 98  ? 47.14  -36.087 19.414  1   54.1   ? 97  ARG   B NH2  1 2 
ATOM   2598 N  N    . GLU   B 1 99  ? 46.851 -30.774 21.113  1   33.12  ? 98  GLU   B N    1 2 
ATOM   2599 C  CA   . GLU   B 1 99  ? 47.682 -31.006 22.288  1   33.83  ? 98  GLU   B CA   1 2 
ATOM   2600 C  C    . GLU   B 1 99  ? 47.494 -29.902 23.316  1   34.26  ? 98  GLU   B C    1 2 
ATOM   2601 O  O    . GLU   B 1 99  ? 47.306 -30.19  24.503  1   34.7   ? 98  GLU   B O    1 2 
ATOM   2602 C  CB   . GLU   B 1 99  ? 49.151 -31.142 21.876  1   37.55  ? 98  GLU   B CB   1 2 
ATOM   2603 C  CG   . GLU   B 1 99  ? 50.082 -31.47  23.029  1   48.19  ? 98  GLU   B CG   1 2 
ATOM   2604 C  CD   . GLU   B 1 99  ? 51.548 -31.691 22.681  1   58.25  ? 98  GLU   B CD   1 2 
ATOM   2605 O  OE1  . GLU   B 1 99  ? 51.893 -31.604 21.478  1   59.45  ? 98  GLU   B OE1  1 2 
ATOM   2606 O  OE2  . GLU   B 1 99  ? 52.348 -31.955 23.613  1   61     ? 98  GLU   B OE2  1 2 
ATOM   2607 N  N    . ASP   B 1 100 ? 47.5   -28.635 22.859  1   34.06  ? 99  ASP   B N    1 2 
ATOM   2608 C  CA   . ASP   B 1 100 ? 47.313 -27.466 23.714  1   33.75  ? 99  ASP   B CA   1 2 
ATOM   2609 C  C    . ASP   B 1 100 ? 45.934 -27.521 24.375  1   32.65  ? 99  ASP   B C    1 2 
ATOM   2610 O  O    . ASP   B 1 100 ? 45.837 -27.292 25.582  1   33.35  ? 99  ASP   B O    1 2 
ATOM   2611 C  CB   . ASP   B 1 100 ? 47.48  -26.181 22.889  1   36.89  ? 99  ASP   B CB   1 2 
ATOM   2612 C  CG   . ASP   B 1 100 ? 47.696 -24.913 23.699  1   46.77  ? 99  ASP   B CG   1 2 
ATOM   2613 O  OD1  . ASP   B 1 100 ? 47.603 -24.98  24.953  1   49.53  ? 99  ASP   B OD1  1 2 
ATOM   2614 O  OD2  . ASP   B 1 100 ? 47.971 -23.843 23.08   1   50.43  ? 99  ASP   B OD2  1 2 
ATOM   2615 N  N    . ILE   B 1 101 ? 44.873 -27.856 23.605  1   30.77  ? 100 ILE   B N    1 2 
ATOM   2616 C  CA   . ILE   B 1 101 ? 43.509 -27.952 24.126  1   29.68  ? 100 ILE   B CA   1 2 
ATOM   2617 C  C    . ILE   B 1 101 ? 43.396 -29.02  25.244  1   31.57  ? 100 ILE   B C    1 2 
ATOM   2618 O  O    . ILE   B 1 101 ? 42.885 -28.715 26.318  1   31.71  ? 100 ILE   B O    1 2 
ATOM   2619 C  CB   . ILE   B 1 101 ? 42.508 -28.188 22.978  1   27.97  ? 100 ILE   B CB   1 2 
ATOM   2620 C  CG1  . ILE   B 1 101 ? 42.36  -26.925 22.064  1   27.56  ? 100 ILE   B CG1  1 2 
ATOM   2621 C  CG2  . ILE   B 1 101 ? 41.158 -28.688 23.468  1   27.39  ? 100 ILE   B CG2  1 2 
ATOM   2622 C  CD1  . ILE   B 1 101 ? 41.688 -27.216 20.754  1   27.02  ? 100 ILE   B CD1  1 2 
ATOM   2623 N  N    . TYR   B 1 102 ? 43.907 -30.239 25.013  1   32.14  ? 101 TYR   B N    1 2 
ATOM   2624 C  CA   . TYR   B 1 102 ? 43.846 -31.288 26.028  1   33.05  ? 101 TYR   B CA   1 2 
ATOM   2625 C  C    . TYR   B 1 102 ? 44.609 -30.928 27.298  1   34.86  ? 101 TYR   B C    1 2 
ATOM   2626 O  O    . TYR   B 1 102 ? 44.096 -31.147 28.391  1   35.89  ? 101 TYR   B O    1 2 
ATOM   2627 C  CB   . TYR   B 1 102 ? 44.309 -32.64  25.457  1   32.67  ? 101 TYR   B CB   1 2 
ATOM   2628 C  CG   . TYR   B 1 102 ? 43.375 -33.211 24.415  1   33.11  ? 101 TYR   B CG   1 2 
ATOM   2629 C  CD1  . TYR   B 1 102 ? 42.01  -32.973 24.473  1   34.25  ? 101 TYR   B CD1  1 2 
ATOM   2630 C  CD2  . TYR   B 1 102 ? 43.847 -34.039 23.411  1   33.47  ? 101 TYR   B CD2  1 2 
ATOM   2631 C  CE1  . TYR   B 1 102 ? 41.145 -33.497 23.526  1   34.91  ? 101 TYR   B CE1  1 2 
ATOM   2632 C  CE2  . TYR   B 1 102 ? 42.987 -34.604 22.482  1   34.54  ? 101 TYR   B CE2  1 2 
ATOM   2633 C  CZ   . TYR   B 1 102 ? 41.633 -34.322 22.534  1   35.92  ? 101 TYR   B CZ   1 2 
ATOM   2634 O  OH   . TYR   B 1 102 ? 40.766 -34.876 21.618  1   37.09  ? 101 TYR   B OH   1 2 
ATOM   2635 N  N    . ASN   B 1 103 ? 45.815 -30.372 27.164  1   35.46  ? 102 ASN   B N    1 2 
ATOM   2636 C  CA   . ASN   B 1 103 ? 46.614 -29.966 28.313  1   36.29  ? 102 ASN   B CA   1 2 
ATOM   2637 C  C    . ASN   B 1 103 ? 45.907 -28.866 29.103  1   35.81  ? 102 ASN   B C    1 2 
ATOM   2638 O  O    . ASN   B 1 103 ? 45.981 -28.861 30.329  1   35.49  ? 102 ASN   B O    1 2 
ATOM   2639 C  CB   . ASN   B 1 103 ? 47.968 -29.454 27.857  1   39.5   ? 102 ASN   B CB   1 2 
ATOM   2640 C  CG   . ASN   B 1 103 ? 48.99  -30.533 27.717  1   45.86  ? 102 ASN   B CG   1 2 
ATOM   2641 O  OD1  . ASN   B 1 103 ? 49.194 -31.339 28.633  1   48.97  ? 102 ASN   B OD1  1 2 
ATOM   2642 N  ND2  . ASN   B 1 103 ? 49.678 -30.556 26.581  1   47.39  ? 102 ASN   B ND2  1 2 
ATOM   2643 N  N    . SER   B 1 104 ? 45.226 -27.932 28.398  1   35.15  ? 103 SER   B N    1 2 
ATOM   2644 C  CA   . SER   B 1 104 ? 44.491 -26.846 29.038  1   35.13  ? 103 SER   B CA   1 2 
ATOM   2645 C  C    . SER   B 1 104 ? 43.215 -27.326 29.717  1   35.35  ? 103 SER   B C    1 2 
ATOM   2646 O  O    . SER   B 1 104 ? 42.836 -26.763 30.749  1   35.19  ? 103 SER   B O    1 2 
ATOM   2647 C  CB   . SER   B 1 104 ? 44.207 -25.717 28.058  1   35.85  ? 103 SER   B CB   1 2 
ATOM   2648 O  OG   . SER   B 1 104 ? 45.433 -25.114 27.683  1   38.43  ? 103 SER   B OG   1 2 
ATOM   2649 N  N    . VAL   B 1 105 ? 42.577 -28.379 29.183  1   35.23  ? 104 VAL   B N    1 2 
ATOM   2650 C  CA   . VAL   B 1 105 ? 41.399 -28.956 29.828  1   36.12  ? 104 VAL   B CA   1 2 
ATOM   2651 C  C    . VAL   B 1 105 ? 41.803 -29.571 31.179  1   37.34  ? 104 VAL   B C    1 2 
ATOM   2652 O  O    . VAL   B 1 105 ? 41.09  -29.381 32.154  1   37.82  ? 104 VAL   B O    1 2 
ATOM   2653 C  CB   . VAL   B 1 105 ? 40.593 -29.918 28.916  1   36.18  ? 104 VAL   B CB   1 2 
ATOM   2654 C  CG1  . VAL   B 1 105 ? 39.587 -30.741 29.719  1   36.62  ? 104 VAL   B CG1  1 2 
ATOM   2655 C  CG2  . VAL   B 1 105 ? 39.886 -29.143 27.813  1   35.98  ? 104 VAL   B CG2  1 2 
ATOM   2656 N  N    . LYS   B 1 106 ? 43     -30.177 31.269  1   38.09  ? 105 LYS   B N    1 2 
ATOM   2657 C  CA   . LYS   B 1 106 ? 43.535 -30.719 32.526  1   39.63  ? 105 LYS   B CA   1 2 
ATOM   2658 C  C    . LYS   B 1 106 ? 43.676 -29.6   33.572  1   39.71  ? 105 LYS   B C    1 2 
ATOM   2659 O  O    . LYS   B 1 106 ? 43.349 -29.787 34.756  1   40.63  ? 105 LYS   B O    1 2 
ATOM   2660 C  CB   . LYS   B 1 106 ? 44.908 -31.392 32.285  1   43.52  ? 105 LYS   B CB   1 2 
ATOM   2661 C  CG   . LYS   B 1 106 ? 44.847 -32.913 32.133  1   50.54  ? 105 LYS   B CG   1 2 
ATOM   2662 C  CD   . LYS   B 1 106 ? 45.923 -33.486 31.168  1   56.98  ? 105 LYS   B CD   1 2 
ATOM   2663 C  CE   . LYS   B 1 106 ? 47.32  -33.564 31.767  1   61.79  ? 105 LYS   B CE   1 2 
ATOM   2664 N  NZ   . LYS   B 1 106 ? 48.362 -33.917 30.75   1   63.21  ? 105 LYS   B NZ   1 2 
ATOM   2665 N  N    . GLN   B 1 107 ? 44.16  -28.44  33.13   1   39.12  ? 106 GLN   B N    1 2 
ATOM   2666 C  CA   . GLN   B 1 107 ? 44.345 -27.248 33.945  1   39.17  ? 106 GLN   B CA   1 2 
ATOM   2667 C  C    . GLN   B 1 107 ? 42.985 -26.722 34.441  1   38.09  ? 106 GLN   B C    1 2 
ATOM   2668 O  O    . GLN   B 1 107 ? 42.855 -26.442 35.628  1   37.39  ? 106 GLN   B O    1 2 
ATOM   2669 C  CB   . GLN   B 1 107 ? 45.048 -26.175 33.113  1   41.96  ? 106 GLN   B CB   1 2 
ATOM   2670 C  CG   . GLN   B 1 107 ? 46.286 -25.591 33.75   1   47.98  ? 106 GLN   B CG   1 2 
ATOM   2671 C  CD   . GLN   B 1 107 ? 46.93  -24.57  32.83   1   56.85  ? 106 GLN   B CD   1 2 
ATOM   2672 O  OE1  . GLN   B 1 107 ? 47.239 -23.434 33.241  1   59.68  ? 106 GLN   B OE1  1 2 
ATOM   2673 N  NE2  . GLN   B 1 107 ? 47.141 -24.944 31.551  1   58.15  ? 106 GLN   B NE2  1 2 
ATOM   2674 N  N    . VAL   B 1 108 ? 41.971 -26.618 33.549  1   37.48  ? 107 VAL   B N    1 2 
ATOM   2675 C  CA   . VAL   B 1 108 ? 40.631 -26.144 33.905  1   37.31  ? 107 VAL   B CA   1 2 
ATOM   2676 C  C    . VAL   B 1 108 ? 39.974 -27.049 34.939  1   37.46  ? 107 VAL   B C    1 2 
ATOM   2677 O  O    . VAL   B 1 108 ? 39.376 -26.553 35.886  1   37.52  ? 107 VAL   B O    1 2 
ATOM   2678 C  CB   . VAL   B 1 108 ? 39.731 -25.913 32.663  1   37.82  ? 107 VAL   B CB   1 2 
ATOM   2679 C  CG1  . VAL   B 1 108 ? 38.293 -25.585 33.069  1   38.34  ? 107 VAL   B CG1  1 2 
ATOM   2680 C  CG2  . VAL   B 1 108 ? 40.303 -24.815 31.777  1   38.1   ? 107 VAL   B CG2  1 2 
ATOM   2681 N  N    . LYS   B 1 109 ? 40.118 -28.37  34.801  1   37.5   ? 108 LYS   B N    1 2 
ATOM   2682 C  CA   . LYS   B 1 109 ? 39.548 -29.31  35.776  1   37.47  ? 108 LYS   B CA   1 2 
ATOM   2683 C  C    . LYS   B 1 109 ? 40.199 -29.116 37.146  1   38.95  ? 108 LYS   B C    1 2 
ATOM   2684 O  O    . LYS   B 1 109 ? 39.529 -29.145 38.177  1   39.85  ? 108 LYS   B O    1 2 
ATOM   2685 C  CB   . LYS   B 1 109 ? 39.781 -30.757 35.308  1   37.31  ? 108 LYS   B CB   1 2 
ATOM   2686 C  CG   . LYS   B 1 109 ? 38.995 -31.187 34.106  1   38.52  ? 108 LYS   B CG   1 2 
ATOM   2687 C  CD   . LYS   B 1 109 ? 39.234 -32.652 33.862  1   41.52  ? 108 LYS   B CD   1 2 
ATOM   2688 C  CE   . LYS   B 1 109 ? 38.615 -33.171 32.601  1   44.94  ? 108 LYS   B CE   1 2 
ATOM   2689 N  NZ   . LYS   B 1 109 ? 39.644 -33.799 31.716  1   48.89  ? 108 LYS   B NZ   1 2 
ATOM   2690 N  N    . LYS   B 1 110 ? 41.519 -28.926 37.164  1   39.24  ? 109 LYS   B N    1 2 
ATOM   2691 C  CA   . LYS   B 1 110 ? 42.293 -28.774 38.4    1   39.18  ? 109 LYS   B CA   1 2 
ATOM   2692 C  C    . LYS   B 1 110 ? 42.089 -27.42  39.081  1   40.6   ? 109 LYS   B C    1 2 
ATOM   2693 O  O    . LYS   B 1 110 ? 42.252 -27.316 40.296  1   41.96  ? 109 LYS   B O    1 2 
ATOM   2694 C  CB   . LYS   B 1 110 ? 43.783 -28.953 38.067  1   40.04  ? 109 LYS   B CB   1 2 
ATOM   2695 C  CG   . LYS   B 1 110 ? 44.658 -29.22  39.262  1   45.3   ? 109 LYS   B CG   1 2 
ATOM   2696 C  CD   . LYS   B 1 110 ? 46.053 -28.707 39.047  1   50.16  ? 109 LYS   B CD   1 2 
ATOM   2697 C  CE   . LYS   B 1 110 ? 46.757 -28.472 40.358  1   52.71  ? 109 LYS   B CE   1 2 
ATOM   2698 N  NZ   . LYS   B 1 110 ? 46.146 -27.308 41.054  1   54.75  ? 109 LYS   B NZ   1 2 
ATOM   2699 N  N    . GLU   B 1 111 ? 41.771 -26.372 38.319  1   40.71  ? 110 GLU   B N    1 2 
ATOM   2700 C  CA   . GLU   B 1 111 ? 41.657 -25.026 38.867  1   41.01  ? 110 GLU   B CA   1 2 
ATOM   2701 C  C    . GLU   B 1 111 ? 40.25  -24.508 38.994  1   40.93  ? 110 GLU   B C    1 2 
ATOM   2702 O  O    . GLU   B 1 111 ? 40.016 -23.632 39.809  1   41.99  ? 110 GLU   B O    1 2 
ATOM   2703 C  CB   . GLU   B 1 111 ? 42.424 -24.048 37.982  1   43.36  ? 110 GLU   B CB   1 2 
ATOM   2704 C  CG   . GLU   B 1 111 ? 43.927 -24.211 38.028  1   48.23  ? 110 GLU   B CG   1 2 
ATOM   2705 C  CD   . GLU   B 1 111 ? 44.629 -23.114 37.263  1   56.86  ? 110 GLU   B CD   1 2 
ATOM   2706 O  OE1  . GLU   B 1 111 ? 44.108 -21.976 37.246  1   59.2   ? 110 GLU   B OE1  1 2 
ATOM   2707 O  OE2  . GLU   B 1 111 ? 45.695 -23.393 36.67   1   60.1   ? 110 GLU   B OE2  1 2 
ATOM   2708 N  N    . VAL   B 1 112 ? 39.342 -24.941 38.132  1   39.49  ? 111 VAL   B N    1 2 
ATOM   2709 C  CA   . VAL   B 1 112 ? 37.976 -24.421 38.118  1   38.76  ? 111 VAL   B CA   1 2 
ATOM   2710 C  C    . VAL   B 1 112 ? 36.925 -25.51  38.405  1   38.78  ? 111 VAL   B C    1 2 
ATOM   2711 O  O    . VAL   B 1 112 ? 36.099 -25.354 39.29   1   38.61  ? 111 VAL   B O    1 2 
ATOM   2712 C  CB   . VAL   B 1 112 ? 37.703 -23.672 36.786  1   38.49  ? 111 VAL   B CB   1 2 
ATOM   2713 C  CG1  . VAL   B 1 112 ? 36.304 -23.069 36.777  1   38.93  ? 111 VAL   B CG1  1 2 
ATOM   2714 C  CG2  . VAL   B 1 112 ? 38.758 -22.606 36.527  1   38.18  ? 111 VAL   B CG2  1 2 
ATOM   2715 N  N    . GLY   B 1 113 ? 36.983 -26.604 37.658  1   39.14  ? 112 GLY   B N    1 2 
ATOM   2716 C  CA   . GLY   B 1 113 ? 36.067 -27.734 37.781  1   38.93  ? 112 GLY   B CA   1 2 
ATOM   2717 C  C    . GLY   B 1 113 ? 35.621 -28.213 36.41   1   39.04  ? 112 GLY   B C    1 2 
ATOM   2718 O  O    . GLY   B 1 113 ? 36.323 -28.039 35.405  1   38.55  ? 112 GLY   B O    1 2 
ATOM   2719 N  N    . ASP   B 1 114 ? 34.437 -28.807 36.356  1   38.64  ? 113 ASP   B N    1 2 
ATOM   2720 C  CA   . ASP   B 1 114 ? 33.89  -29.334 35.124  1   37.46  ? 113 ASP   B CA   1 2 
ATOM   2721 C  C    . ASP   B 1 114 ? 33.07  -28.31  34.391  1   36.98  ? 113 ASP   B C    1 2 
ATOM   2722 O  O    . ASP   B 1 114 ? 32.064 -27.86  34.922  1   37.16  ? 113 ASP   B O    1 2 
ATOM   2723 C  CB   . ASP   B 1 114 ? 33.031 -30.557 35.421  1   38.31  ? 113 ASP   B CB   1 2 
ATOM   2724 C  CG   . ASP   B 1 114 ? 33.854 -31.745 35.848  1   42.5   ? 113 ASP   B CG   1 2 
ATOM   2725 O  OD1  . ASP   B 1 114 ? 34.921 -31.975 35.244  1   41.61  ? 113 ASP   B OD1  1 2 
ATOM   2726 O  OD2  . ASP   B 1 114 ? 33.417 -32.465 36.771  1   47.32  ? 113 ASP   B OD2  1 2 
ATOM   2727 N  N    . VAL   B 1 115 ? 33.477 -27.961 33.148  1   36.5   ? 114 VAL   B N    1 2 
ATOM   2728 C  CA   . VAL   B 1 115 ? 32.73  -27.024 32.318  1   36.71  ? 114 VAL   B CA   1 2 
ATOM   2729 C  C    . VAL   B 1 115 ? 31.305 -27.548 32.065  1   37.25  ? 114 VAL   B C    1 2 
ATOM   2730 O  O    . VAL   B 1 115 ? 31.122 -28.732 31.788  1   36.96  ? 114 VAL   B O    1 2 
ATOM   2731 C  CB   . VAL   B 1 115 ? 33.471 -26.726 30.991  1   36.44  ? 114 VAL   B CB   1 2 
ATOM   2732 C  CG1  . VAL   B 1 115 ? 32.618 -25.895 30.066  1   36.66  ? 114 VAL   B CG1  1 2 
ATOM   2733 C  CG2  . VAL   B 1 115 ? 34.809 -26.048 31.241  1   36.59  ? 114 VAL   B CG2  1 2 
ATOM   2734 N  N    . THR   B 1 116 ? 30.307 -26.682 32.228  1   37.65  ? 115 THR   B N    1 2 
ATOM   2735 C  CA   . THR   B 1 116 ? 28.928 -27.046 32.008  1   38.83  ? 115 THR   B CA   1 2 
ATOM   2736 C  C    . THR   B 1 116 ? 28.416 -26.464 30.687  1   38.9   ? 115 THR   B C    1 2 
ATOM   2737 O  O    . THR   B 1 116 ? 27.598 -27.095 30.018  1   39.79  ? 115 THR   B O    1 2 
ATOM   2738 C  CB   . THR   B 1 116 ? 28.07  -26.579 33.155  1   42.18  ? 115 THR   B CB   1 2 
ATOM   2739 O  OG1  . THR   B 1 116 ? 28.601 -27.084 34.398  1   44.47  ? 115 THR   B OG1  1 2 
ATOM   2740 C  CG2  . THR   B 1 116 ? 26.661 -27.065 33.015  1   43.05  ? 115 THR   B CG2  1 2 
ATOM   2741 N  N    . ILE   B 1 117 ? 28.871 -25.253 30.306  1   37.05  ? 116 ILE   B N    1 2 
ATOM   2742 C  CA   . ILE   B 1 117 ? 28.459 -24.644 29.046  1   35.48  ? 116 ILE   B CA   1 2 
ATOM   2743 C  C    . ILE   B 1 117 ? 29.706 -24.334 28.231  1   34.28  ? 116 ILE   B C    1 2 
ATOM   2744 O  O    . ILE   B 1 117 ? 30.569 -23.592 28.696  1   33.78  ? 116 ILE   B O    1 2 
ATOM   2745 C  CB   . ILE   B 1 117 ? 27.604 -23.374 29.255  1   34.94  ? 116 ILE   B CB   1 2 
ATOM   2746 C  CG1  . ILE   B 1 117 ? 26.311 -23.698 30.012  1   35.14  ? 116 ILE   B CG1  1 2 
ATOM   2747 C  CG2  . ILE   B 1 117 ? 27.327 -22.691 27.899  1   34.62  ? 116 ILE   B CG2  1 2 
ATOM   2748 C  CD1  . ILE   B 1 117 ? 25.513 -22.514 30.39   1   36.16  ? 116 ILE   B CD1  1 2 
ATOM   2749 N  N    . LEU   B 1 118 ? 29.819 -24.927 27.039  1   33.73  ? 117 LEU   B N    1 2 
ATOM   2750 C  CA   . LEU   B 1 118 ? 30.937 -24.668 26.142  1   33.52  ? 117 LEU   B CA   1 2 
ATOM   2751 C  C    . LEU   B 1 118 ? 30.476 -23.794 24.984  1   33.27  ? 117 LEU   B C    1 2 
ATOM   2752 O  O    . LEU   B 1 118 ? 29.535 -24.154 24.296  1   34     ? 117 LEU   B O    1 2 
ATOM   2753 C  CB   . LEU   B 1 118 ? 31.51  -25.982 25.602  1   33.58  ? 117 LEU   B CB   1 2 
ATOM   2754 C  CG   . LEU   B 1 118 ? 32.559 -25.876 24.475  1   34.47  ? 117 LEU   B CG   1 2 
ATOM   2755 C  CD1  . LEU   B 1 118 ? 33.758 -25.005 24.904  1   35.03  ? 117 LEU   B CD1  1 2 
ATOM   2756 C  CD2  . LEU   B 1 118 ? 32.996 -27.266 24.007  1   34.6   ? 117 LEU   B CD2  1 2 
ATOM   2757 N  N    . VAL   B 1 119 ? 31.141 -22.655 24.763  1   32.3   ? 118 VAL   B N    1 2 
ATOM   2758 C  CA   . VAL   B 1 119 ? 30.862 -21.755 23.642  1   31.2   ? 118 VAL   B CA   1 2 
ATOM   2759 C  C    . VAL   B 1 119 ? 32.069 -21.794 22.705  1   30.14  ? 118 VAL   B C    1 2 
ATOM   2760 O  O    . VAL   B 1 119 ? 33.062 -21.116 22.965  1   30.16  ? 118 VAL   B O    1 2 
ATOM   2761 C  CB   . VAL   B 1 119 ? 30.562 -20.299 24.077  1   31.67  ? 118 VAL   B CB   1 2 
ATOM   2762 C  CG1  . VAL   B 1 119 ? 30.206 -19.439 22.87   1   32.19  ? 118 VAL   B CG1  1 2 
ATOM   2763 C  CG2  . VAL   B 1 119 ? 29.456 -20.247 25.125  1   31.98  ? 118 VAL   B CG2  1 2 
ATOM   2764 N  N    . ASN   B 1 120 ? 31.989 -22.621 21.641  1   28.94  ? 119 ASN   B N    1 2 
ATOM   2765 C  CA   . ASN   B 1 120 ? 33.003 -22.792 20.624  1   28.46  ? 119 ASN   B CA   1 2 
ATOM   2766 C  C    . ASN   B 1 120 ? 32.902 -21.587 19.635  1   29.55  ? 119 ASN   B C    1 2 
ATOM   2767 O  O    . ASN   B 1 120 ? 32.289 -21.679 18.563  1   29.56  ? 119 ASN   B O    1 2 
ATOM   2768 C  CB   . ASN   B 1 120 ? 32.772 -24.126 19.917  1   28.53  ? 119 ASN   B CB   1 2 
ATOM   2769 C  CG   . ASN   B 1 120 ? 33.393 -25.334 20.607  1   30.31  ? 119 ASN   B CG   1 2 
ATOM   2770 O  OD1  . ASN   B 1 120 ? 32.783 -26.427 20.712  1   30.08  ? 119 ASN   B OD1  1 2 
ATOM   2771 N  ND2  . ASN   B 1 120 ? 34.642 -25.188 21.05   1   29.82  ? 119 ASN   B ND2  1 2 
ATOM   2772 N  N    . ASN   B 1 121 ? 33.492 -20.453 20.03   1   29.48  ? 120 ASN   B N    1 2 
ATOM   2773 C  CA   . ASN   B 1 121 ? 33.42  -19.214 19.292  1   30     ? 120 ASN   B CA   1 2 
ATOM   2774 C  C    . ASN   B 1 121 ? 34.682 -18.888 18.488  1   30.97  ? 120 ASN   B C    1 2 
ATOM   2775 O  O    . ASN   B 1 121 ? 34.556 -18.321 17.385  1   30.97  ? 120 ASN   B O    1 2 
ATOM   2776 C  CB   . ASN   B 1 121 ? 33.049 -18.068 20.238  1   31.66  ? 120 ASN   B CB   1 2 
ATOM   2777 C  CG   . ASN   B 1 121 ? 33.192 -16.682 19.665  1   34.63  ? 120 ASN   B CG   1 2 
ATOM   2778 O  OD1  . ASN   B 1 121 ? 32.247 -16.116 19.103  1   35.64  ? 120 ASN   B OD1  1 2 
ATOM   2779 N  ND2  . ASN   B 1 121 ? 34.392 -16.127 19.777  1   34.78  ? 120 ASN   B ND2  1 2 
ATOM   2780 N  N    . ALA   B 1 122 ? 35.902 -19.258 18.978  1   30.51  ? 121 ALA   B N    1 2 
ATOM   2781 C  CA   . ALA   B 1 122 ? 37.151 -18.955 18.236  1   30.13  ? 121 ALA   B CA   1 2 
ATOM   2782 C  C    . ALA   B 1 122 ? 37.067 -19.295 16.747  1   30.22  ? 121 ALA   B C    1 2 
ATOM   2783 O  O    . ALA   B 1 122 ? 36.572 -20.367 16.366  1   30.5   ? 121 ALA   B O    1 2 
ATOM   2784 C  CB   . ALA   B 1 122 ? 38.345 -19.649 18.864  1   29.4   ? 121 ALA   B CB   1 2 
ATOM   2785 N  N    . GLY   B 1 123 ? 37.459 -18.334 15.931  1   30.04  ? 122 GLY   B N    1 2 
ATOM   2786 C  CA   . GLY   B 1 123 ? 37.428 -18.482 14.494  1   30.18  ? 122 GLY   B CA   1 2 
ATOM   2787 C  C    . GLY   B 1 123 ? 38.499 -17.663 13.809  1   30.84  ? 122 GLY   B C    1 2 
ATOM   2788 O  O    . GLY   B 1 123 ? 39.045 -16.71  14.385  1   31.33  ? 122 GLY   B O    1 2 
ATOM   2789 N  N    . THR   B 1 124 ? 38.787 -18.043 12.555  1   30.34  ? 123 THR   B N    1 2 
ATOM   2790 C  CA   . THR   B 1 124 ? 39.783 -17.446 11.688  1   30.44  ? 123 THR   B CA   1 2 
ATOM   2791 C  C    . THR   B 1 124 ? 39.267 -17.459 10.238  1   30.89  ? 123 THR   B C    1 2 
ATOM   2792 O  O    . THR   B 1 124 ? 38.42  -18.279 9.873   1   31.61  ? 123 THR   B O    1 2 
ATOM   2793 C  CB   . THR   B 1 124 ? 41.118 -18.18  11.834  1   31.57  ? 123 THR   B CB   1 2 
ATOM   2794 O  OG1  . THR   B 1 124 ? 42.16  -17.363 11.297  1   32.87  ? 123 THR   B OG1  1 2 
ATOM   2795 C  CG2  . THR   B 1 124 ? 41.124 -19.532 11.138  1   31.79  ? 123 THR   B CG2  1 2 
ATOM   2796 N  N    . VAL   B 1 125 ? 39.756 -16.513 9.424   1   30.23  ? 124 VAL   B N    1 2 
ATOM   2797 C  CA   . VAL   B 1 125 ? 39.377 -16.335 8.036   1   29.65  ? 124 VAL   B CA   1 2 
ATOM   2798 C  C    . VAL   B 1 125 ? 40.521 -15.67  7.291   1   31.23  ? 124 VAL   B C    1 2 
ATOM   2799 O  O    . VAL   B 1 125 ? 41.237 -14.857 7.866   1   31.5   ? 124 VAL   B O    1 2 
ATOM   2800 C  CB   . VAL   B 1 125 ? 38.073 -15.498 7.91    1   29.39  ? 124 VAL   B CB   1 2 
ATOM   2801 C  CG1  . VAL   B 1 125 ? 38.252 -14.084 8.457   1   29.48  ? 124 VAL   B CG1  1 2 
ATOM   2802 C  CG2  . VAL   B 1 125 ? 37.557 -15.463 6.467   1   29.48  ? 124 VAL   B CG2  1 2 
ATOM   2803 N  N    . TYR   B 1 126 ? 40.724 -16.047 6.019   1   31.87  ? 125 TYR   B N    1 2 
ATOM   2804 C  CA   . TYR   B 1 126 ? 41.735 -15.46  5.147   1   32.47  ? 125 TYR   B CA   1 2 
ATOM   2805 C  C    . TYR   B 1 126 ? 41.064 -15.223 3.812   1   32.75  ? 125 TYR   B C    1 2 
ATOM   2806 O  O    . TYR   B 1 126 ? 41.163 -16.049 2.902   1   33.01  ? 125 TYR   B O    1 2 
ATOM   2807 C  CB   . TYR   B 1 126 ? 42.974 -16.369 4.99    1   32.52  ? 125 TYR   B CB   1 2 
ATOM   2808 C  CG   . TYR   B 1 126 ? 43.63  -16.696 6.311   1   32.75  ? 125 TYR   B CG   1 2 
ATOM   2809 C  CD1  . TYR   B 1 126 ? 44.523 -15.814 6.9     1   33.63  ? 125 TYR   B CD1  1 2 
ATOM   2810 C  CD2  . TYR   B 1 126 ? 43.269 -17.828 7.026   1   33.45  ? 125 TYR   B CD2  1 2 
ATOM   2811 C  CE1  . TYR   B 1 126 ? 45.045 -16.054 8.166   1   34.84  ? 125 TYR   B CE1  1 2 
ATOM   2812 C  CE2  . TYR   B 1 126 ? 43.813 -18.099 8.274   1   34.69  ? 125 TYR   B CE2  1 2 
ATOM   2813 C  CZ   . TYR   B 1 126 ? 44.704 -17.213 8.841   1   35.96  ? 125 TYR   B CZ   1 2 
ATOM   2814 O  OH   . TYR   B 1 126 ? 45.214 -17.498 10.087  1   37.68  ? 125 TYR   B OH   1 2 
ATOM   2815 N  N    . PRO   B 1 127 ? 40.313 -14.114 3.696   1   32.83  ? 126 PRO   B N    1 2 
ATOM   2816 C  CA   . PRO   B 1 127 ? 39.605 -13.839 2.448   1   32.67  ? 126 PRO   B CA   1 2 
ATOM   2817 C  C    . PRO   B 1 127 ? 40.525 -13.8   1.237   1   32.43  ? 126 PRO   B C    1 2 
ATOM   2818 O  O    . PRO   B 1 127 ? 41.594 -13.224 1.331   1   33.06  ? 126 PRO   B O    1 2 
ATOM   2819 C  CB   . PRO   B 1 127 ? 38.982 -12.469 2.709   1   33.49  ? 126 PRO   B CB   1 2 
ATOM   2820 C  CG   . PRO   B 1 127 ? 38.818 -12.407 4.196   1   33.81  ? 126 PRO   B CG   1 2 
ATOM   2821 C  CD   . PRO   B 1 127 ? 40.064 -13.054 4.699   1   32.5   ? 126 PRO   B CD   1 2 
ATOM   2822 N  N    . ALA   B 1 128 ? 40.162 -14.513 0.154   1   31.99  ? 127 ALA   B N    1 2 
ATOM   2823 C  CA   . ALA   B 1 128 ? 40.879 -14.581 -1.136  1   32.26  ? 127 ALA   B CA   1 2 
ATOM   2824 C  C    . ALA   B 1 128 ? 40.124 -15.477 -2.086  1   33.94  ? 127 ALA   B C    1 2 
ATOM   2825 O  O    . ALA   B 1 128 ? 39.447 -16.407 -1.634  1   35.34  ? 127 ALA   B O    1 2 
ATOM   2826 C  CB   . ALA   B 1 128 ? 42.287 -15.153 -0.943  1   31.88  ? 127 ALA   B CB   1 2 
ATOM   2827 N  N    . ASP   B 1 129 ? 40.333 -15.315 -3.407  1   34.79  ? 128 ASP   B N    1 2 
ATOM   2828 C  CA   . ASP   B 1 129 ? 39.775 -16.284 -4.369  1   35.56  ? 128 ASP   B CA   1 2 
ATOM   2829 C  C    . ASP   B 1 129 ? 40.554 -17.612 -4.161  1   34.84  ? 128 ASP   B C    1 2 
ATOM   2830 O  O    . ASP   B 1 129 ? 41.662 -17.596 -3.618  1   34.16  ? 128 ASP   B O    1 2 
ATOM   2831 C  CB   . ASP   B 1 129 ? 39.884 -15.794 -5.818  1   38.69  ? 128 ASP   B CB   1 2 
ATOM   2832 C  CG   . ASP   B 1 129 ? 41.309 -15.529 -6.244  1   47.47  ? 128 ASP   B CG   1 2 
ATOM   2833 O  OD1  . ASP   B 1 129 ? 41.895 -14.562 -5.755  1   50.25  ? 128 ASP   B OD1  1 2 
ATOM   2834 O  OD2  . ASP   B 1 129 ? 41.842 -16.307 -7.051  1   51.62  ? 128 ASP   B OD2  1 2 
ATOM   2835 N  N    . LEU   B 1 130 ? 39.973 -18.753 -4.543  1   34.59  ? 129 LEU   B N    1 2 
ATOM   2836 C  CA   . LEU   B 1 130 ? 40.599 -20.056 -4.33   1   34.14  ? 129 LEU   B CA   1 2 
ATOM   2837 C  C    . LEU   B 1 130 ? 42.065 -20.143 -4.769  1   34.08  ? 129 LEU   B C    1 2 
ATOM   2838 O  O    . LEU   B 1 130 ? 42.906 -20.608 -4      1   34     ? 129 LEU   B O    1 2 
ATOM   2839 C  CB   . LEU   B 1 130 ? 39.777 -21.162 -4.997  1   33.77  ? 129 LEU   B CB   1 2 
ATOM   2840 C  CG   . LEU   B 1 130 ? 40.132 -22.59  -4.564  1   34.12  ? 129 LEU   B CG   1 2 
ATOM   2841 C  CD1  . LEU   B 1 130 ? 39.84  -22.797 -3.112  1   33.74  ? 129 LEU   B CD1  1 2 
ATOM   2842 C  CD2  . LEU   B 1 130 ? 39.397 -23.603 -5.391  1   34.33  ? 129 LEU   B CD2  1 2 
ATOM   2843 N  N    . LEU   B 1 131 ? 42.385 -19.628 -5.966  1   34.08  ? 130 LEU   B N    1 2 
ATOM   2844 C  CA   . LEU   B 1 131 ? 43.752 -19.71  -6.475  1   33.94  ? 130 LEU   B CA   1 2 
ATOM   2845 C  C    . LEU   B 1 131 ? 44.752 -18.748 -5.811  1   34.07  ? 130 LEU   B C    1 2 
ATOM   2846 O  O    . LEU   B 1 131 ? 45.953 -18.9   -6.008  1   33.99  ? 130 LEU   B O    1 2 
ATOM   2847 C  CB   . LEU   B 1 131 ? 43.785 -19.583 -7.992  1   33.53  ? 130 LEU   B CB   1 2 
ATOM   2848 C  CG   . LEU   B 1 131 ? 43.235 -20.786 -8.793  1   34.03  ? 130 LEU   B CG   1 2 
ATOM   2849 C  CD1  . LEU   B 1 131 ? 43.568 -20.678 -10.222 1   33.51  ? 130 LEU   B CD1  1 2 
ATOM   2850 C  CD2  . LEU   B 1 131 ? 43.647 -22.154 -8.195  1   34.4   ? 130 LEU   B CD2  1 2 
ATOM   2851 N  N    . SER   B 1 132 ? 44.267 -17.827 -4.968  1   34.05  ? 131 SER   B N    1 2 
ATOM   2852 C  CA   . SER   B 1 132 ? 45.086 -16.901 -4.179  1   33.85  ? 131 SER   B CA   1 2 
ATOM   2853 C  C    . SER   B 1 132 ? 45.224 -17.315 -2.714  1   34.32  ? 131 SER   B C    1 2 
ATOM   2854 O  O    . SER   B 1 132 ? 45.933 -16.649 -1.961  1   35.34  ? 131 SER   B O    1 2 
ATOM   2855 C  CB   . SER   B 1 132 ? 44.535 -15.488 -4.265  1   34.61  ? 131 SER   B CB   1 2 
ATOM   2856 O  OG   . SER   B 1 132 ? 44.627 -15.046 -5.611  1   38.1   ? 131 SER   B OG   1 2 
ATOM   2857 N  N    . THR   B 1 133 ? 44.543 -18.384 -2.29   1   33.04  ? 132 THR   B N    1 2 
ATOM   2858 C  CA   . THR   B 1 133 ? 44.659 -18.886 -0.929  1   31.93  ? 132 THR   B CA   1 2 
ATOM   2859 C  C    . THR   B 1 133 ? 46.01  -19.585 -0.8    1   31.86  ? 132 THR   B C    1 2 
ATOM   2860 O  O    . THR   B 1 133 ? 46.528 -20.145 -1.749  1   32.52  ? 132 THR   B O    1 2 
ATOM   2861 C  CB   . THR   B 1 133 ? 43.546 -19.924 -0.629  1   31.17  ? 132 THR   B CB   1 2 
ATOM   2862 O  OG1  . THR   B 1 133 ? 43.489 -20.851 -1.719  1   32.29  ? 132 THR   B OG1  1 2 
ATOM   2863 C  CG2  . THR   B 1 133 ? 42.198 -19.309 -0.454  1   30.16  ? 132 THR   B CG2  1 2 
ATOM   2864 N  N    . LYS   B 1 134 ? 46.544 -19.588 0.377   1   31.33  ? 133 LYS   B N    1 2 
ATOM   2865 C  CA   . LYS   B 1 134 ? 47.747 -20.312 0.735   1   31.29  ? 133 LYS   B CA   1 2 
ATOM   2866 C  C    . LYS   B 1 134 ? 47.241 -21.606 1.424   1   29.85  ? 133 LYS   B C    1 2 
ATOM   2867 O  O    . LYS   B 1 134 ? 46.291 -21.55  2.209   1   29.6   ? 133 LYS   B O    1 2 
ATOM   2868 C  CB   . LYS   B 1 134 ? 48.579 -19.458 1.697   1   34.66  ? 133 LYS   B CB   1 2 
ATOM   2869 C  CG   . LYS   B 1 134 ? 49.122 -18.211 1.023   1   40.25  ? 133 LYS   B CG   1 2 
ATOM   2870 C  CD   . LYS   B 1 134 ? 49.465 -17.065 1.997   1   46.02  ? 133 LYS   B CD   1 2 
ATOM   2871 C  CE   . LYS   B 1 134 ? 49.385 -15.716 1.297   1   50.57  ? 133 LYS   B CE   1 2 
ATOM   2872 N  NZ   . LYS   B 1 134 ? 50.109 -15.693 -0.028  1   53.61  ? 133 LYS   B NZ   1 2 
ATOM   2873 N  N    . ASP   B 1 135 ? 47.82  -22.767 1.092   1   28.93  ? 134 ASP   B N    1 2 
ATOM   2874 C  CA   . ASP   B 1 135 ? 47.368 -24.032 1.66    1   29.07  ? 134 ASP   B CA   1 2 
ATOM   2875 C  C    . ASP   B 1 135 ? 47.368 -24.035 3.224   1   30.08  ? 134 ASP   B C    1 2 
ATOM   2876 O  O    . ASP   B 1 135 ? 46.484 -24.645 3.836   1   30.45  ? 134 ASP   B O    1 2 
ATOM   2877 C  CB   . ASP   B 1 135 ? 48.182 -25.183 1.088   1   29.68  ? 134 ASP   B CB   1 2 
ATOM   2878 C  CG   . ASP   B 1 135 ? 47.943 -25.435 -0.395  1   35.24  ? 134 ASP   B CG   1 2 
ATOM   2879 O  OD1  . ASP   B 1 135 ? 46.9   -24.978 -0.923  1   35.26  ? 134 ASP   B OD1  1 2 
ATOM   2880 O  OD2  . ASP   B 1 135 ? 48.787 -26.105 -1.025  1   37.3   ? 134 ASP   B OD2  1 2 
ATOM   2881 N  N    . GLU   B 1 136 ? 48.319 -23.299 3.848   1   30.16  ? 135 GLU   B N    1 2 
ATOM   2882 C  CA   . GLU   B 1 136 ? 48.466 -23.141 5.307   1   31.03  ? 135 GLU   B CA   1 2 
ATOM   2883 C  C    . GLU   B 1 136 ? 47.268 -22.398 5.89    1   31.31  ? 135 GLU   B C    1 2 
ATOM   2884 O  O    . GLU   B 1 136 ? 46.846 -22.67  7.012   1   31.6   ? 135 GLU   B O    1 2 
ATOM   2885 C  CB   . GLU   B 1 136 ? 49.766 -22.387 5.669   1   34.5   ? 135 GLU   B CB   1 2 
ATOM   2886 C  CG   . GLU   B 1 136 ? 51.013 -22.892 4.941   1   44.31  ? 135 GLU   B CG   1 2 
ATOM   2887 C  CD   . GLU   B 1 136 ? 51.213 -22.5   3.471   1   53.49  ? 135 GLU   B CD   1 2 
ATOM   2888 O  OE1  . GLU   B 1 136 ? 51.094 -21.289 3.166   1   54.75  ? 135 GLU   B OE1  1 2 
ATOM   2889 O  OE2  . GLU   B 1 136 ? 51.501 -23.391 2.632   1   54.23  ? 135 GLU   B OE2  1 2 
ATOM   2890 N  N    . GLU   B 1 137 ? 46.725 -21.444 5.131   1   31.42  ? 136 GLU   B N    1 2 
ATOM   2891 C  CA   . GLU   B 1 137 ? 45.55  -20.689 5.545   1   31.59  ? 136 GLU   B CA   1 2 
ATOM   2892 C  C    . GLU   B 1 137 ? 44.314 -21.584 5.518   1   30.26  ? 136 GLU   B C    1 2 
ATOM   2893 O  O    . GLU   B 1 137 ? 43.47  -21.489 6.41    1   29.75  ? 136 GLU   B O    1 2 
ATOM   2894 C  CB   . GLU   B 1 137 ? 45.351 -19.477 4.617   1   33.81  ? 136 GLU   B CB   1 2 
ATOM   2895 C  CG   . GLU   B 1 137 ? 46.418 -18.428 4.827   1   40.3   ? 136 GLU   B CG   1 2 
ATOM   2896 C  CD   . GLU   B 1 137 ? 46.387 -17.309 3.804   1   45.84  ? 136 GLU   B CD   1 2 
ATOM   2897 O  OE1  . GLU   B 1 137 ? 45.947 -17.57  2.664   1   42.12  ? 136 GLU   B OE1  1 2 
ATOM   2898 O  OE2  . GLU   B 1 137 ? 46.793 -16.17  4.135   1   51.02  ? 136 GLU   B OE2  1 2 
ATOM   2899 N  N    . ILE   B 1 138 ? 44.216 -22.462 4.505   1   29.43  ? 137 ILE   B N    1 2 
ATOM   2900 C  CA   . ILE   B 1 138 ? 43.11  -23.41  4.403   1   28.98  ? 137 ILE   B CA   1 2 
ATOM   2901 C  C    . ILE   B 1 138 ? 43.142 -24.374 5.607   1   29.93  ? 137 ILE   B C    1 2 
ATOM   2902 O  O    . ILE   B 1 138 ? 42.122 -24.613 6.241   1   29.06  ? 137 ILE   B O    1 2 
ATOM   2903 C  CB   . ILE   B 1 138 ? 43.18  -24.167 3.072   1   27.67  ? 137 ILE   B CB   1 2 
ATOM   2904 C  CG1  . ILE   B 1 138 ? 43.014 -23.194 1.885   1   28.31  ? 137 ILE   B CG1  1 2 
ATOM   2905 C  CG2  . ILE   B 1 138 ? 42.127 -25.237 3.032   1   27.49  ? 137 ILE   B CG2  1 2 
ATOM   2906 C  CD1  . ILE   B 1 138 ? 43.248 -23.84  0.503   1   28.58  ? 137 ILE   B CD1  1 2 
ATOM   2907 N  N    . THR   B 1 139 ? 44.336 -24.885 5.928   1   30.71  ? 138 THR   B N    1 2 
ATOM   2908 C  CA   . THR   B 1 139 ? 44.569 -25.788 7.026   1   31.5   ? 138 THR   B CA   1 2 
ATOM   2909 C  C    . THR   B 1 139 ? 44.213 -25.128 8.357   1   32.46  ? 138 THR   B C    1 2 
ATOM   2910 O  O    . THR   B 1 139 ? 43.452 -25.706 9.136   1   32.33  ? 138 THR   B O    1 2 
ATOM   2911 C  CB   . THR   B 1 139 ? 46.017 -26.261 6.954   1   33.18  ? 138 THR   B CB   1 2 
ATOM   2912 O  OG1  . THR   B 1 139 ? 46.116 -27.201 5.884   1   33.46  ? 138 THR   B OG1  1 2 
ATOM   2913 C  CG2  . THR   B 1 139 ? 46.484 -26.922 8.245   1   34.26  ? 138 THR   B CG2  1 2 
ATOM   2914 N  N    . LYS   B 1 140 ? 44.717 -23.902 8.604   1   32.73  ? 139 LYS   B N    1 2 
ATOM   2915 C  CA   . LYS   B 1 140 ? 44.409 -23.172 9.827   1   32.77  ? 139 LYS   B CA   1 2 
ATOM   2916 C  C    . LYS   B 1 140 ? 42.922 -22.891 9.966   1   30.99  ? 139 LYS   B C    1 2 
ATOM   2917 O  O    . LYS   B 1 140 ? 42.379 -23.006 11.057  1   31.99  ? 139 LYS   B O    1 2 
ATOM   2918 C  CB   . LYS   B 1 140 ? 45.201 -21.88  9.874   1   37.91  ? 139 LYS   B CB   1 2 
ATOM   2919 C  CG   . LYS   B 1 140 ? 46.426 -21.982 10.765  1   47.92  ? 139 LYS   B CG   1 2 
ATOM   2920 C  CD   . LYS   B 1 140 ? 47.531 -21.04  10.319  1   58.03  ? 139 LYS   B CD   1 2 
ATOM   2921 C  CE   . LYS   B 1 140 ? 47.471 -19.713 11.076  1   65.52  ? 139 LYS   B CE   1 2 
ATOM   2922 N  NZ   . LYS   B 1 140 ? 48.317 -18.638 10.436  1   68.81  ? 139 LYS   B NZ   1 2 
ATOM   2923 N  N    . THR   B 1 141 ? 42.237 -22.574 8.866   1   28.93  ? 140 THR   B N    1 2 
ATOM   2924 C  CA   . THR   B 1 141 ? 40.8   -22.329 8.874   1   28.18  ? 140 THR   B CA   1 2 
ATOM   2925 C  C    . THR   B 1 141 ? 40.057 -23.549 9.382   1   28.04  ? 140 THR   B C    1 2 
ATOM   2926 O  O    . THR   B 1 141 ? 39.279 -23.416 10.308  1   29.43  ? 140 THR   B O    1 2 
ATOM   2927 C  CB   . THR   B 1 141 ? 40.317 -21.92  7.48    1   29.58  ? 140 THR   B CB   1 2 
ATOM   2928 O  OG1  . THR   B 1 141 ? 41.083 -20.808 7.006   1   29.51  ? 140 THR   B OG1  1 2 
ATOM   2929 C  CG2  . THR   B 1 141 ? 38.844 -21.589 7.456   1   30.28  ? 140 THR   B CG2  1 2 
ATOM   2930 N  N    . PHE   B 1 142 ? 40.399 -24.748 8.89    1   26.52  ? 141 PHE   B N    1 2 
ATOM   2931 C  CA   . PHE   B 1 142 ? 39.761 -25.976 9.353   1   25.92  ? 141 PHE   B CA   1 2 
ATOM   2932 C  C    . PHE   B 1 142 ? 40.129 -26.346 10.788  1   25.24  ? 141 PHE   B C    1 2 
ATOM   2933 O  O    . PHE   B 1 142 ? 39.258 -26.737 11.557  1   25.23  ? 141 PHE   B O    1 2 
ATOM   2934 C  CB   . PHE   B 1 142 ? 40.045 -27.136 8.397   1   25.9   ? 141 PHE   B CB   1 2 
ATOM   2935 C  CG   . PHE   B 1 142 ? 39.028 -27.115 7.28    1   27.11  ? 141 PHE   B CG   1 2 
ATOM   2936 C  CD1  . PHE   B 1 142 ? 39.21  -26.302 6.176   1   28.03  ? 141 PHE   B CD1  1 2 
ATOM   2937 C  CD2  . PHE   B 1 142 ? 37.834 -27.801 7.401   1   27.77  ? 141 PHE   B CD2  1 2 
ATOM   2938 C  CE1  . PHE   B 1 142 ? 38.254 -26.228 5.19    1   29.61  ? 141 PHE   B CE1  1 2 
ATOM   2939 C  CE2  . PHE   B 1 142 ? 36.873 -27.715 6.424   1   28.95  ? 141 PHE   B CE2  1 2 
ATOM   2940 C  CZ   . PHE   B 1 142 ? 37.092 -26.94  5.317   1   29.72  ? 141 PHE   B CZ   1 2 
ATOM   2941 N  N    . GLU   B 1 143 ? 41.413 -26.231 11.137  1   24.43  ? 142 GLU   B N    1 2 
ATOM   2942 C  CA   . GLU   B 1 143 ? 41.917 -26.555 12.442  1   24.67  ? 142 GLU   B CA   1 2 
ATOM   2943 C  C    . GLU   B 1 143 ? 41.235 -25.741 13.54   1   26.21  ? 142 GLU   B C    1 2 
ATOM   2944 O  O    . GLU   B 1 143 ? 40.851 -26.314 14.557  1   27.07  ? 142 GLU   B O    1 2 
ATOM   2945 C  CB   . GLU   B 1 143 ? 43.42  -26.353 12.491  1   25.57  ? 142 GLU   B CB   1 2 
ATOM   2946 C  CG   . GLU   B 1 143 ? 44.167 -27.498 11.863  1   28.24  ? 142 GLU   B CG   1 2 
ATOM   2947 C  CD   . GLU   B 1 143 ? 45.659 -27.287 11.712  1   33.76  ? 142 GLU   B CD   1 2 
ATOM   2948 O  OE1  . GLU   B 1 143 ? 46.117 -26.127 11.819  1   33.76  ? 142 GLU   B OE1  1 2 
ATOM   2949 O  OE2  . GLU   B 1 143 ? 46.371 -28.286 11.456  1   37.19  ? 142 GLU   B OE2  1 2 
ATOM   2950 N  N    . ILE   B 1 144 ? 41.034 -24.435 13.326  1   26.03  ? 143 ILE   B N    1 2 
ATOM   2951 C  CA   . ILE   B 1 144 ? 40.371 -23.604 14.321  1   26.33  ? 143 ILE   B CA   1 2 
ATOM   2952 C  C    . ILE   B 1 144 ? 38.848 -23.628 14.211  1   26.46  ? 143 ILE   B C    1 2 
ATOM   2953 O  O    . ILE   B 1 144 ? 38.185 -23.695 15.227  1   27.03  ? 143 ILE   B O    1 2 
ATOM   2954 C  CB   . ILE   B 1 144 ? 40.895 -22.145 14.24   1   27.17  ? 143 ILE   B CB   1 2 
ATOM   2955 C  CG1  . ILE   B 1 144 ? 42.424 -22.111 14.387  1   28.17  ? 143 ILE   B CG1  1 2 
ATOM   2956 C  CG2  . ILE   B 1 144 ? 40.205 -21.244 15.278  1   27.31  ? 143 ILE   B CG2  1 2 
ATOM   2957 C  CD1  . ILE   B 1 144 ? 43.036 -20.841 14.05   1   29.02  ? 143 ILE   B CD1  1 2 
ATOM   2958 N  N    . ASN   B 1 145 ? 38.283 -23.496 12.994  1   25.75  ? 144 ASN   B N    1 2 
ATOM   2959 C  CA   . ASN   B 1 145 ? 36.843 -23.353 12.838  1   25.05  ? 144 ASN   B CA   1 2 
ATOM   2960 C  C    . ASN   B 1 145 ? 36.035 -24.615 13.007  1   24.96  ? 144 ASN   B C    1 2 
ATOM   2961 O  O    . ASN   B 1 145 ? 34.814 -24.495 13.167  1   24.72  ? 144 ASN   B O    1 2 
ATOM   2962 C  CB   . ASN   B 1 145 ? 36.488 -22.689 11.512  1   26.1   ? 144 ASN   B CB   1 2 
ATOM   2963 C  CG   . ASN   B 1 145 ? 36.98  -21.272 11.322  1   29.12  ? 144 ASN   B CG   1 2 
ATOM   2964 O  OD1  . ASN   B 1 145 ? 36.795 -20.684 10.258  1   31.48  ? 144 ASN   B OD1  1 2 
ATOM   2965 N  ND2  . ASN   B 1 145 ? 37.632 -20.693 12.302  1   29.04  ? 144 ASN   B ND2  1 2 
ATOM   2966 N  N    . ILE   B 1 146 ? 36.653 -25.811 12.925  1   25.39  ? 145 ILE   B N    1 2 
ATOM   2967 C  CA   . ILE   B 1 146 ? 35.864 -27.048 13.099  1   26.12  ? 145 ILE   B CA   1 2 
ATOM   2968 C  C    . ILE   B 1 146 ? 36.641 -28.169 13.861  1   26.43  ? 145 ILE   B C    1 2 
ATOM   2969 O  O    . ILE   B 1 146 ? 36.098 -28.712 14.82   1   26.88  ? 145 ILE   B O    1 2 
ATOM   2970 C  CB   . ILE   B 1 146 ? 35.206 -27.576 11.788  1   25.5   ? 145 ILE   B CB   1 2 
ATOM   2971 C  CG1  . ILE   B 1 146 ? 34.388 -28.865 12.057  1   25.79  ? 145 ILE   B CG1  1 2 
ATOM   2972 C  CG2  . ILE   B 1 146 ? 36.197 -27.762 10.69   1   25.27  ? 145 ILE   B CG2  1 2 
ATOM   2973 C  CD1  . ILE   B 1 146 ? 33.278 -28.708 13.014  1   25.87  ? 145 ILE   B CD1  1 2 
ATOM   2974 N  N    . LEU   B 1 147 ? 37.897 -28.48  13.491  1   25.94  ? 146 LEU   B N    1 2 
ATOM   2975 C  CA   . LEU   B 1 147 ? 38.653 -29.537 14.167  1   25.48  ? 146 LEU   B CA   1 2 
ATOM   2976 C  C    . LEU   B 1 147 ? 38.809 -29.269 15.643  1   26.52  ? 146 LEU   B C    1 2 
ATOM   2977 O  O    . LEU   B 1 147 ? 38.59  -30.187 16.442  1   27.21  ? 146 LEU   B O    1 2 
ATOM   2978 C  CB   . LEU   B 1 147 ? 39.994 -29.81  13.476  1   24.72  ? 146 LEU   B CB   1 2 
ATOM   2979 C  CG   . LEU   B 1 147 ? 39.855 -30.422 12.074  1   24.1   ? 146 LEU   B CG   1 2 
ATOM   2980 C  CD1  . LEU   B 1 147 ? 41.143 -30.332 11.296  1   23.97  ? 146 LEU   B CD1  1 2 
ATOM   2981 C  CD2  . LEU   B 1 147 ? 39.402 -31.831 12.156  1   24.22  ? 146 LEU   B CD2  1 2 
ATOM   2982 N  N    . GLY   B 1 148 ? 39.033 -27.999 16.001  1   26.22  ? 147 GLY   B N    1 2 
ATOM   2983 C  CA   . GLY   B 1 148 ? 39.156 -27.558 17.386  1   26.18  ? 147 GLY   B CA   1 2 
ATOM   2984 C  C    . GLY   B 1 148 ? 37.884 -27.781 18.164  1   26.38  ? 147 GLY   B C    1 2 
ATOM   2985 O  O    . GLY   B 1 148 ? 37.94  -28.148 19.328  1   26.14  ? 147 GLY   B O    1 2 
ATOM   2986 N  N    . HIS   B 1 149 ? 36.716 -27.653 17.513  1   26.7   ? 148 HIS   B N    1 2 
ATOM   2987 C  CA   . HIS   B 1 149 ? 35.431 -27.92  18.167  1   26.75  ? 148 HIS   B CA   1 2 
ATOM   2988 C  C    . HIS   B 1 149 ? 35.377 -29.407 18.593  1   28.43  ? 148 HIS   B C    1 2 
ATOM   2989 O  O    . HIS   B 1 149 ? 34.947 -29.713 19.691  1   29.76  ? 148 HIS   B O    1 2 
ATOM   2990 C  CB   . HIS   B 1 149 ? 34.264 -27.607 17.223  1   26.3   ? 148 HIS   B CB   1 2 
ATOM   2991 C  CG   . HIS   B 1 149 ? 34.11  -26.151 16.876  1   28.02  ? 148 HIS   B CG   1 2 
ATOM   2992 N  ND1  . HIS   B 1 149 ? 32.867 -25.614 16.556  1   29.38  ? 148 HIS   B ND1  1 2 
ATOM   2993 C  CD2  . HIS   B 1 149 ? 35.031 -25.16  16.827  1   28.48  ? 148 HIS   B CD2  1 2 
ATOM   2994 C  CE1  . HIS   B 1 149 ? 33.076 -24.333 16.319  1   28.85  ? 148 HIS   B CE1  1 2 
ATOM   2995 N  NE2  . HIS   B 1 149 ? 34.362 -24.018 16.445  1   29     ? 148 HIS   B NE2  1 2 
ATOM   2996 N  N    . PHE   B 1 150 ? 35.887 -30.311 17.763  1   28.47  ? 149 PHE   B N    1 2 
ATOM   2997 C  CA   . PHE   B 1 150 ? 35.933 -31.726 18.077  1   28.5   ? 149 PHE   B CA   1 2 
ATOM   2998 C  C    . PHE   B 1 150 ? 36.801 -31.979 19.299  1   28.91  ? 149 PHE   B C    1 2 
ATOM   2999 O  O    . PHE   B 1 150 ? 36.377 -32.728 20.179  1   29.56  ? 149 PHE   B O    1 2 
ATOM   3000 C  CB   . PHE   B 1 150 ? 36.474 -32.537 16.882  1   28.13  ? 149 PHE   B CB   1 2 
ATOM   3001 C  CG   . PHE   B 1 150 ? 35.458 -32.809 15.796  1   28.36  ? 149 PHE   B CG   1 2 
ATOM   3002 C  CD1  . PHE   B 1 150 ? 34.613 -33.904 15.87   1   28.85  ? 149 PHE   B CD1  1 2 
ATOM   3003 C  CD2  . PHE   B 1 150 ? 35.365 -31.984 14.689  1   28.34  ? 149 PHE   B CD2  1 2 
ATOM   3004 C  CE1  . PHE   B 1 150 ? 33.688 -34.158 14.855  1   28.83  ? 149 PHE   B CE1  1 2 
ATOM   3005 C  CE2  . PHE   B 1 150 ? 34.438 -32.239 13.679  1   28.21  ? 149 PHE   B CE2  1 2 
ATOM   3006 C  CZ   . PHE   B 1 150 ? 33.612 -33.32  13.764  1   28.11  ? 149 PHE   B CZ   1 2 
ATOM   3007 N  N    . TRP   B 1 151 ? 38.021 -31.4   19.354  1   27.98  ? 150 TRP   B N    1 2 
ATOM   3008 C  CA   . TRP   B 1 151 ? 38.901 -31.674 20.499  1   27.5   ? 150 TRP   B CA   1 2 
ATOM   3009 C  C    . TRP   B 1 151 ? 38.337 -31.101 21.788  1   27.83  ? 150 TRP   B C    1 2 
ATOM   3010 O  O    . TRP   B 1 151 ? 38.347 -31.8   22.804  1   29.4   ? 150 TRP   B O    1 2 
ATOM   3011 C  CB   . TRP   B 1 151 ? 40.364 -31.229 20.262  1   26.43  ? 150 TRP   B CB   1 2 
ATOM   3012 C  CG   . TRP   B 1 151 ? 40.862 -31.29  18.839  1   24.83  ? 150 TRP   B CG   1 2 
ATOM   3013 C  CD1  . TRP   B 1 151 ? 41.501 -30.297 18.159  1   24.86  ? 150 TRP   B CD1  1 2 
ATOM   3014 C  CD2  . TRP   B 1 151 ? 40.834 -32.426 17.957  1   24.2   ? 150 TRP   B CD2  1 2 
ATOM   3015 N  NE1  . TRP   B 1 151 ? 41.83  -30.725 16.895  1   24.55  ? 150 TRP   B NE1  1 2 
ATOM   3016 C  CE2  . TRP   B 1 151 ? 41.409 -32.018 16.734  1   24.26  ? 150 TRP   B CE2  1 2 
ATOM   3017 C  CE3  . TRP   B 1 151 ? 40.32  -33.726 18.057  1   24.35  ? 150 TRP   B CE3  1 2 
ATOM   3018 C  CZ2  . TRP   B 1 151 ? 41.508 -32.871 15.631  1   24.18  ? 150 TRP   B CZ2  1 2 
ATOM   3019 C  CZ3  . TRP   B 1 151 ? 40.405 -34.558 16.961  1   24.96  ? 150 TRP   B CZ3  1 2 
ATOM   3020 C  CH2  . TRP   B 1 151 ? 41.018 -34.135 15.771  1   24.52  ? 150 TRP   B CH2  1 2 
ATOM   3021 N  N    . ILE   B 1 152 ? 37.81  -29.862 21.753  1   26.48  ? 151 ILE   B N    1 2 
ATOM   3022 C  CA   . ILE   B 1 152 ? 37.247 -29.25  22.941  1   26.42  ? 151 ILE   B CA   1 2 
ATOM   3023 C  C    . ILE   B 1 152 ? 36.008 -29.987 23.405  1   27.73  ? 151 ILE   B C    1 2 
ATOM   3024 O  O    . ILE   B 1 152 ? 35.899 -30.293 24.586  1   26.93  ? 151 ILE   B O    1 2 
ATOM   3025 C  CB   . ILE   B 1 152 ? 37.012 -27.728 22.836  1   26.27  ? 151 ILE   B CB   1 2 
ATOM   3026 C  CG1  . ILE   B 1 152 ? 38.254 -27.04  22.254  1   27.27  ? 151 ILE   B CG1  1 2 
ATOM   3027 C  CG2  . ILE   B 1 152 ? 36.695 -27.159 24.236  1   27.05  ? 151 ILE   B CG2  1 2 
ATOM   3028 C  CD1  . ILE   B 1 152 ? 38.119 -25.588 21.85   1   27.93  ? 151 ILE   B CD1  1 2 
ATOM   3029 N  N    . THR   B 1 153 ? 35.113 -30.338 22.481  1   28.77  ? 152 THR   B N    1 2 
ATOM   3030 C  CA   . THR   B 1 153 ? 33.893 -31.056 22.843  1   29.48  ? 152 THR   B CA   1 2 
ATOM   3031 C  C    . THR   B 1 153 ? 34.229 -32.435 23.387  1   30.01  ? 152 THR   B C    1 2 
ATOM   3032 O  O    . THR   B 1 153 ? 33.714 -32.789 24.427  1   31.58  ? 152 THR   B O    1 2 
ATOM   3033 C  CB   . THR   B 1 153 ? 32.89  -31.073 21.682  1   30.59  ? 152 THR   B CB   1 2 
ATOM   3034 O  OG1  . THR   B 1 153 ? 32.647 -29.729 21.267  1   31.19  ? 152 THR   B OG1  1 2 
ATOM   3035 C  CG2  . THR   B 1 153 ? 31.585 -31.724 22.059  1   31.12  ? 152 THR   B CG2  1 2 
ATOM   3036 N  N    . LYS   B 1 154 ? 35.152 -33.177 22.762  1   29.1   ? 153 LYS   B N    1 2 
ATOM   3037 C  CA   . LYS   B 1 154 ? 35.529 -34.502 23.272  1   28.63  ? 153 LYS   B CA   1 2 
ATOM   3038 C  C    . LYS   B 1 154 ? 36.119 -34.46  24.687  1   28.63  ? 153 LYS   B C    1 2 
ATOM   3039 O  O    . LYS   B 1 154 ? 36.036 -35.436 25.425  1   28.77  ? 153 LYS   B O    1 2 
ATOM   3040 C  CB   . LYS   B 1 154 ? 36.477 -35.225 22.305  1   28.73  ? 153 LYS   B CB   1 2 
ATOM   3041 C  CG   . LYS   B 1 154 ? 35.799 -35.62  21.018  1   31.43  ? 153 LYS   B CG   1 2 
ATOM   3042 C  CD   . LYS   B 1 154 ? 36.125 -37.036 20.61   1   35.1   ? 153 LYS   B CD   1 2 
ATOM   3043 C  CE   . LYS   B 1 154 ? 37.59  -37.288 20.444  1   37.13  ? 153 LYS   B CE   1 2 
ATOM   3044 N  NZ   . LYS   B 1 154 ? 37.854 -38.643 19.922  1   38.08  ? 153 LYS   B NZ   1 2 
ATOM   3045 N  N    . ALA   B 1 155 ? 36.75  -33.355 25.047  1   28.92  ? 154 ALA   B N    1 2 
ATOM   3046 C  CA   . ALA   B 1 155 ? 37.363 -33.21  26.371  1   29.22  ? 154 ALA   B CA   1 2 
ATOM   3047 C  C    . ALA   B 1 155 ? 36.334 -32.83  27.423  1   31.47  ? 154 ALA   B C    1 2 
ATOM   3048 O  O    . ALA   B 1 155 ? 36.466 -33.236 28.581  1   33.65  ? 154 ALA   B O    1 2 
ATOM   3049 C  CB   . ALA   B 1 155 ? 38.467 -32.167 26.329  1   27.91  ? 154 ALA   B CB   1 2 
ATOM   3050 N  N    . LEU   B 1 156 ? 35.32  -32.047 27.047  1   31.39  ? 155 LEU   B N    1 2 
ATOM   3051 C  CA   . LEU   B 1 156 ? 34.352 -31.552 28.015  1   32.07  ? 155 LEU   B CA   1 2 
ATOM   3052 C  C    . LEU   B 1 156 ? 33.053 -32.343 28.064  1   32.78  ? 155 LEU   B C    1 2 
ATOM   3053 O  O    . LEU   B 1 156 ? 32.42  -32.389 29.11   1   32.75  ? 155 LEU   B O    1 2 
ATOM   3054 C  CB   . LEU   B 1 156 ? 34.088 -30.053 27.768  1   31.51  ? 155 LEU   B CB   1 2 
ATOM   3055 C  CG   . LEU   B 1 156 ? 35.339 -29.176 27.755  1   31.55  ? 155 LEU   B CG   1 2 
ATOM   3056 C  CD1  . LEU   B 1 156 ? 34.977 -27.746 27.533  1   32.08  ? 155 LEU   B CD1  1 2 
ATOM   3057 C  CD2  . LEU   B 1 156 ? 36.159 -29.327 29.065  1   32     ? 155 LEU   B CD2  1 2 
ATOM   3058 N  N    . LEU   B 1 157 ? 32.648 -32.944 26.939  1   32.7   ? 156 LEU   B N    1 2 
ATOM   3059 C  CA   . LEU   B 1 157 ? 31.419 -33.734 26.882  1   33.46  ? 156 LEU   B CA   1 2 
ATOM   3060 C  C    . LEU   B 1 157 ? 31.346 -34.871 27.941  1   34.16  ? 156 LEU   B C    1 2 
ATOM   3061 O  O    . LEU   B 1 157 ? 30.264 -35.069 28.486  1   34.87  ? 156 LEU   B O    1 2 
ATOM   3062 C  CB   . LEU   B 1 157 ? 31.163 -34.281 25.457  1   33.68  ? 156 LEU   B CB   1 2 
ATOM   3063 C  CG   . LEU   B 1 157 ? 29.75  -34.798 25.17   1   35.11  ? 156 LEU   B CG   1 2 
ATOM   3064 C  CD1  . LEU   B 1 157 ? 28.729 -33.707 25.297  1   35.66  ? 156 LEU   B CD1  1 2 
ATOM   3065 C  CD2  . LEU   B 1 157 ? 29.657 -35.469 23.799  1   35.58  ? 156 LEU   B CD2  1 2 
ATOM   3066 N  N    . PRO   B 1 158 ? 32.434 -35.608 28.282  1   33.97  ? 157 PRO   B N    1 2 
ATOM   3067 C  CA   . PRO   B 1 158 ? 32.298 -36.702 29.257  1   34.62  ? 157 PRO   B CA   1 2 
ATOM   3068 C  C    . PRO   B 1 158 ? 31.691 -36.356 30.609  1   35.57  ? 157 PRO   B C    1 2 
ATOM   3069 O  O    . PRO   B 1 158 ? 30.952 -37.181 31.164  1   36.31  ? 157 PRO   B O    1 2 
ATOM   3070 C  CB   . PRO   B 1 158 ? 33.736 -37.197 29.414  1   34.99  ? 157 PRO   B CB   1 2 
ATOM   3071 C  CG   . PRO   B 1 158 ? 34.353 -36.91  28.086  1   34.65  ? 157 PRO   B CG   1 2 
ATOM   3072 C  CD   . PRO   B 1 158 ? 33.814 -35.56  27.758  1   33.1   ? 157 PRO   B CD   1 2 
ATOM   3073 N  N    . SER   B 1 159 ? 32.04  -35.194 31.187  1   36.1   ? 158 SER   B N    1 2 
ATOM   3074 C  CA   . SER   B 1 159 ? 31.502 -34.844 32.523  1   36.96  ? 158 SER   B CA   1 2 
ATOM   3075 C  C    . SER   B 1 159 ? 30.031 -34.413 32.428  1   36.59  ? 158 SER   B C    1 2 
ATOM   3076 O  O    . SER   B 1 159 ? 29.261 -34.63  33.368  1   36.45  ? 158 SER   B O    1 2 
ATOM   3077 C  CB   . SER   B 1 159 ? 32.368 -33.791 33.207  1   39.44  ? 158 SER   B CB   1 2 
ATOM   3078 O  OG   . SER   B 1 159 ? 31.626 -32.73  33.797  1   43.74  ? 158 SER   B OG   1 2 
ATOM   3079 N  N    . MET   B 1 160 ? 29.671 -33.773 31.302  1   36.07  ? 159 MET   B N    1 2 
ATOM   3080 C  CA   . MET   B 1 160 ? 28.323 -33.332 30.964  1   35.89  ? 159 MET   B CA   1 2 
ATOM   3081 C  C    . MET   B 1 160 ? 27.439 -34.58  30.857  1   36.33  ? 159 MET   B C    1 2 
ATOM   3082 O  O    . MET   B 1 160 ? 26.325 -34.572 31.37   1   36     ? 159 MET   B O    1 2 
ATOM   3083 C  CB   . MET   B 1 160 ? 28.326 -32.586 29.604  1   35.32  ? 159 MET   B CB   1 2 
ATOM   3084 C  CG   . MET   B 1 160 ? 29.013 -31.25  29.621  1   35.71  ? 159 MET   B CG   1 2 
ATOM   3085 S  SD   . MET   B 1 160 ? 28.902 -30.5   27.98   1   39.63  ? 159 MET   B SD   1 2 
ATOM   3086 C  CE   . MET   B 1 160 ? 29.859 -29.001 28.224  1   35.22  ? 159 MET   B CE   1 2 
ATOM   3087 N  N    . ILE   B 1 161 ? 27.939 -35.646 30.187  1   36.55  ? 160 ILE   B N    1 2 
ATOM   3088 C  CA   . ILE   B 1 161 ? 27.217 -36.904 30.025  1   36.89  ? 160 ILE   B CA   1 2 
ATOM   3089 C  C    . ILE   B 1 161 ? 27.03  -37.548 31.375  1   37.76  ? 160 ILE   B C    1 2 
ATOM   3090 O  O    . ILE   B 1 161 ? 25.905 -37.912 31.721  1   38.03  ? 160 ILE   B O    1 2 
ATOM   3091 C  CB   . ILE   B 1 161 ? 27.939 -37.849 29.023  1   36.75  ? 160 ILE   B CB   1 2 
ATOM   3092 C  CG1  . ILE   B 1 161 ? 27.836 -37.313 27.598  1   37.35  ? 160 ILE   B CG1  1 2 
ATOM   3093 C  CG2  . ILE   B 1 161 ? 27.393 -39.269 29.107  1   36.97  ? 160 ILE   B CG2  1 2 
ATOM   3094 C  CD1  . ILE   B 1 161 ? 28.594 -38.127 26.549  1   37.8   ? 160 ILE   B CD1  1 2 
ATOM   3095 N  N    . LYS   B 1 162 ? 28.129 -37.65  32.159  1   38.37  ? 161 LYS   B N    1 2 
ATOM   3096 C  CA   . LYS   B 1 162 ? 28.159 -38.213 33.515  1   39.35  ? 161 LYS   B CA   1 2 
ATOM   3097 C  C    . LYS   B 1 162 ? 27.088 -37.545 34.386  1   39.18  ? 161 LYS   B C    1 2 
ATOM   3098 O  O    . LYS   B 1 162 ? 26.366 -38.25  35.093  1   39.17  ? 161 LYS   B O    1 2 
ATOM   3099 C  CB   . LYS   B 1 162 ? 29.533 -37.934 34.141  1   42.47  ? 161 LYS   B CB   1 2 
ATOM   3100 C  CG   . LYS   B 1 162 ? 30.281 -39.102 34.735  1   48.24  ? 161 LYS   B CG   1 2 
ATOM   3101 C  CD   . LYS   B 1 162 ? 31.696 -38.644 35.248  1   54.9   ? 161 LYS   B CD   1 2 
ATOM   3102 C  CE   . LYS   B 1 162 ? 32.58  -37.971 34.194  1   60.98  ? 161 LYS   B CE   1 2 
ATOM   3103 N  NZ   . LYS   B 1 162 ? 33.019 -38.885 33.089  1   63.47  ? 161 LYS   B NZ   1 2 
ATOM   3104 N  N    . ARG   B 1 163 ? 26.964 -36.198 34.296  1   39.26  ? 162 ARG   B N    1 2 
ATOM   3105 C  CA   . ARG   B 1 163 ? 26.011 -35.428 35.089  1   40.71  ? 162 ARG   B CA   1 2 
ATOM   3106 C  C    . ARG   B 1 163 ? 24.643 -35.224 34.442  1   40.55  ? 162 ARG   B C    1 2 
ATOM   3107 O  O    . ARG   B 1 163 ? 23.781 -34.606 35.066  1   40.25  ? 162 ARG   B O    1 2 
ATOM   3108 C  CB   . ARG   B 1 163 ? 26.596 -34.045 35.397  1   43.78  ? 162 ARG   B CB   1 2 
ATOM   3109 C  CG   . ARG   B 1 163 ? 27.84  -34.056 36.261  1   49.7   ? 162 ARG   B CG   1 2 
ATOM   3110 C  CD   . ARG   B 1 163 ? 28.187 -32.636 36.653  1   56.18  ? 162 ARG   B CD   1 2 
ATOM   3111 N  NE   . ARG   B 1 163 ? 29.482 -32.508 37.324  1   62.71  ? 162 ARG   B NE   1 2 
ATOM   3112 C  CZ   . ARG   B 1 163 ? 29.657 -32.405 38.648  1   67.48  ? 162 ARG   B CZ   1 2 
ATOM   3113 N  NH1  . ARG   B 1 163 ? 28.615 -32.493 39.477  1   65.2   ? 162 ARG   B NH1  1 2 
ATOM   3114 N  NH2  . ARG   B 1 163 ? 30.879 -32.268 39.155  1   69.38  ? 162 ARG   B NH2  1 2 
ATOM   3115 N  N    . ASN   B 1 164 ? 24.463 -35.672 33.181  1   40.57  ? 163 ASN   B N    1 2 
ATOM   3116 C  CA   . ASN   B 1 164 ? 23.29  -35.44  32.331  1   40.81  ? 163 ASN   B CA   1 2 
ATOM   3117 C  C    . ASN   B 1 164 ? 22.929 -33.955 32.308  1   41.28  ? 163 ASN   B C    1 2 
ATOM   3118 O  O    . ASN   B 1 164 ? 21.78  -33.581 32.551  1   42.01  ? 163 ASN   B O    1 2 
ATOM   3119 C  CB   . ASN   B 1 164 ? 22.086 -36.303 32.69   1   41.07  ? 163 ASN   B CB   1 2 
ATOM   3120 C  CG   . ASN   B 1 164 ? 21.156 -36.402 31.499  1   43.81  ? 163 ASN   B CG   1 2 
ATOM   3121 O  OD1  . ASN   B 1 164 ? 21.601 -36.446 30.342  1   44.24  ? 163 ASN   B OD1  1 2 
ATOM   3122 N  ND2  . ASN   B 1 164 ? 19.845 -36.384 31.734  1   43.93  ? 163 ASN   B ND2  1 2 
ATOM   3123 N  N    . HIS   B 1 165 ? 23.947 -33.102 32.123  1   40.53  ? 164 HIS   B N    1 2 
ATOM   3124 C  CA   . HIS   B 1 165 ? 23.744 -31.663 32.209  1   40.83  ? 164 HIS   B CA   1 2 
ATOM   3125 C  C    . HIS   B 1 165 ? 24.848 -30.903 31.51   1   40.29  ? 164 HIS   B C    1 2 
ATOM   3126 O  O    . HIS   B 1 165 ? 25.993 -30.943 31.94   1   40.7   ? 164 HIS   B O    1 2 
ATOM   3127 C  CB   . HIS   B 1 165 ? 23.699 -31.251 33.692  1   42.95  ? 164 HIS   B CB   1 2 
ATOM   3128 C  CG   . HIS   B 1 165 ? 23.443 -29.795 33.927  1   46.92  ? 164 HIS   B CG   1 2 
ATOM   3129 N  ND1  . HIS   B 1 165 ? 22.167 -29.287 33.959  1   49.25  ? 164 HIS   B ND1  1 2 
ATOM   3130 C  CD2  . HIS   B 1 165 ? 24.317 -28.788 34.156  1   48.27  ? 164 HIS   B CD2  1 2 
ATOM   3131 C  CE1  . HIS   B 1 165 ? 22.301 -27.994 34.202  1   49.62  ? 164 HIS   B CE1  1 2 
ATOM   3132 N  NE2  . HIS   B 1 165 ? 23.575 -27.65  34.331  1   49.32  ? 164 HIS   B NE2  1 2 
ATOM   3133 N  N    . GLY   B 1 166 ? 24.492 -30.2   30.45   1   39.17  ? 165 GLY   B N    1 2 
ATOM   3134 C  CA   . GLY   B 1 166 ? 25.441 -29.397 29.711  1   39     ? 165 GLY   B CA   1 2 
ATOM   3135 C  C    . GLY   B 1 166 ? 24.814 -28.617 28.578  1   38.76  ? 165 GLY   B C    1 2 
ATOM   3136 O  O    . GLY   B 1 166 ? 23.621 -28.747 28.305  1   38.96  ? 165 GLY   B O    1 2 
ATOM   3137 N  N    . HIS   B 1 167 ? 25.608 -27.795 27.912  1   38.32  ? 166 HIS   B N    1 2 
ATOM   3138 C  CA   . HIS   B 1 167 ? 25.125 -27.009 26.77   1   37.88  ? 166 HIS   B CA   1 2 
ATOM   3139 C  C    . HIS   B 1 167 ? 26.283 -26.749 25.833  1   36.98  ? 166 HIS   B C    1 2 
ATOM   3140 O  O    . HIS   B 1 167 ? 27.219 -26.08  26.238  1   37.4   ? 166 HIS   B O    1 2 
ATOM   3141 C  CB   . HIS   B 1 167 ? 24.482 -25.675 27.23   1   38.62  ? 166 HIS   B CB   1 2 
ATOM   3142 C  CG   . HIS   B 1 167 ? 23.515 -25.114 26.231  1   40.41  ? 166 HIS   B CG   1 2 
ATOM   3143 N  ND1  . HIS   B 1 167 ? 22.286 -24.609 26.62   1   42.02  ? 166 HIS   B ND1  1 2 
ATOM   3144 C  CD2  . HIS   B 1 167 ? 23.626 -24.994 24.885  1   40.56  ? 166 HIS   B CD2  1 2 
ATOM   3145 C  CE1  . HIS   B 1 167 ? 21.693 -24.207 25.504  1   41.89  ? 166 HIS   B CE1  1 2 
ATOM   3146 N  NE2  . HIS   B 1 167 ? 22.462 -24.418 24.435  1   41.15  ? 166 HIS   B NE2  1 2 
ATOM   3147 N  N    . ILE   B 1 168 ? 26.25  -27.306 24.601  1   36.15  ? 167 ILE   B N    1 2 
ATOM   3148 C  CA   . ILE   B 1 168 ? 27.272 -27.093 23.572  1   35.68  ? 167 ILE   B CA   1 2 
ATOM   3149 C  C    . ILE   B 1 168 ? 26.805 -26.014 22.576  1   35.19  ? 167 ILE   B C    1 2 
ATOM   3150 O  O    . ILE   B 1 168 ? 25.862 -26.238 21.812  1   35.75  ? 167 ILE   B O    1 2 
ATOM   3151 C  CB   . ILE   B 1 168 ? 27.608 -28.395 22.799  1   36.05  ? 167 ILE   B CB   1 2 
ATOM   3152 C  CG1  . ILE   B 1 168 ? 27.823 -29.593 23.75   1   37.65  ? 167 ILE   B CG1  1 2 
ATOM   3153 C  CG2  . ILE   B 1 168 ? 28.785 -28.18  21.842  1   35.64  ? 167 ILE   B CG2  1 2 
ATOM   3154 C  CD1  . ILE   B 1 168 ? 29.028 -29.514 24.6    1   39.24  ? 167 ILE   B CD1  1 2 
ATOM   3155 N  N    . VAL   B 1 169 ? 27.481 -24.866 22.565  1   33.73  ? 168 VAL   B N    1 2 
ATOM   3156 C  CA   . VAL   B 1 169 ? 27.178 -23.757 21.675  1   32.89  ? 168 VAL   B CA   1 2 
ATOM   3157 C  C    . VAL   B 1 169 ? 28.21  -23.699 20.565  1   32.44  ? 168 VAL   B C    1 2 
ATOM   3158 O  O    . VAL   B 1 169 ? 29.39  -23.525 20.831  1   32.4   ? 168 VAL   B O    1 2 
ATOM   3159 C  CB   . VAL   B 1 169 ? 27.168 -22.434 22.47   1   32.97  ? 168 VAL   B CB   1 2 
ATOM   3160 C  CG1  . VAL   B 1 169 ? 27.01  -21.232 21.545  1   33.03  ? 168 VAL   B CG1  1 2 
ATOM   3161 C  CG2  . VAL   B 1 169 ? 26.091 -22.454 23.535  1   32.88  ? 168 VAL   B CG2  1 2 
ATOM   3162 N  N    . THR   B 1 170 ? 27.785 -23.852 19.326  1   32.46  ? 169 THR   B N    1 2 
ATOM   3163 C  CA   . THR   B 1 170 ? 28.677 -23.77  18.173  1   33.08  ? 169 THR   B CA   1 2 
ATOM   3164 C  C    . THR   B 1 170 ? 28.487 -22.427 17.534  1   33.66  ? 169 THR   B C    1 2 
ATOM   3165 O  O    . THR   B 1 170 ? 27.374 -22.139 17.093  1   33.85  ? 169 THR   B O    1 2 
ATOM   3166 C  CB   . THR   B 1 170 ? 28.285 -24.832 17.121  1   34.26  ? 169 THR   B CB   1 2 
ATOM   3167 O  OG1  . THR   B 1 170 ? 28.394 -26.13  17.724  1   35.6   ? 169 THR   B OG1  1 2 
ATOM   3168 C  CG2  . THR   B 1 170 ? 29.134 -24.749 15.853  1   34.24  ? 169 THR   B CG2  1 2 
ATOM   3169 N  N    . VAL   B 1 171 ? 29.538 -21.604 17.467  1   34.03  ? 170 VAL   B N    1 2 
ATOM   3170 C  CA   . VAL   B 1 171 ? 29.417 -20.327 16.768  1   35.11  ? 170 VAL   B CA   1 2 
ATOM   3171 C  C    . VAL   B 1 171 ? 29.817 -20.574 15.331  1   35.49  ? 170 VAL   B C    1 2 
ATOM   3172 O  O    . VAL   B 1 171 ? 30.987 -20.829 15.047  1   36.26  ? 170 VAL   B O    1 2 
ATOM   3173 C  CB   . VAL   B 1 171 ? 30.183 -19.147 17.416  1   36.25  ? 170 VAL   B CB   1 2 
ATOM   3174 C  CG1  . VAL   B 1 171 ? 30.163 -17.928 16.502  1   36.86  ? 170 VAL   B CG1  1 2 
ATOM   3175 C  CG2  . VAL   B 1 171 ? 29.599 -18.807 18.782  1   36.73  ? 170 VAL   B CG2  1 2 
ATOM   3176 N  N    . ALA   B 1 172 ? 28.829 -20.621 14.439  1   34.76  ? 171 ALA   B N    1 2 
ATOM   3177 C  CA   . ALA   B 1 172 ? 29.085 -20.866 13.032  1   33.88  ? 171 ALA   B CA   1 2 
ATOM   3178 C  C    . ALA   B 1 172 ? 28.959 -19.51  12.239  1   34.08  ? 171 ALA   B C    1 2 
ATOM   3179 O  O    . ALA   B 1 172 ? 29.776 -18.643 12.539  1   34.58  ? 171 ALA   B O    1 2 
ATOM   3180 C  CB   . ALA   B 1 172 ? 28.232 -22.045 12.511  1   33.62  ? 171 ALA   B CB   1 2 
ATOM   3181 N  N    . SER   B 1 173 ? 27.968 -19.268 11.336  1   33.76  ? 172 SER   B N    1 2 
ATOM   3182 C  CA   . SER   B 1 173 ? 27.815 -18.07  10.527  1   33.72  ? 172 SER   B CA   1 2 
ATOM   3183 C  C    . SER   B 1 173 ? 26.692 -18.328 9.518   1   34.36  ? 172 SER   B C    1 2 
ATOM   3184 O  O    . SER   B 1 173 ? 26.329 -19.497 9.31    1   34.33  ? 172 SER   B O    1 2 
ATOM   3185 C  CB   . SER   B 1 173 ? 29.113 -17.84  9.756   1   34.09  ? 172 SER   B CB   1 2 
ATOM   3186 O  OG   . SER   B 1 173 ? 29.007 -16.806 8.789   1   35.56  ? 172 SER   B OG   1 2 
ATOM   3187 N  N    . VAL   B 1 174 ? 26.176 -17.272 8.824   1   34.74  ? 173 VAL   B N    1 2 
ATOM   3188 C  CA   . VAL   B 1 174 ? 25.267 -17.534 7.687   1   35.84  ? 173 VAL   B CA   1 2 
ATOM   3189 C  C    . VAL   B 1 174 ? 26.031 -18.298 6.57    1   36.65  ? 173 VAL   B C    1 2 
ATOM   3190 O  O    . VAL   B 1 174 ? 25.407 -19.016 5.777   1   36.74  ? 173 VAL   B O    1 2 
ATOM   3191 C  CB   . VAL   B 1 174 ? 24.554 -16.294 7.13    1   36.61  ? 173 VAL   B CB   1 2 
ATOM   3192 C  CG1  . VAL   B 1 174 ? 23.431 -15.881 8.068   1   37.73  ? 173 VAL   B CG1  1 2 
ATOM   3193 C  CG2  . VAL   B 1 174 ? 25.536 -15.156 6.9     1   36.37  ? 173 VAL   B CG2  1 2 
ATOM   3194 N  N    . CYS   B 1 175 ? 27.399 -18.181 6.559   1   36.67  ? 174 CYS   B N    1 2 
ATOM   3195 C  CA   . CYS   B 1 175 ? 28.348 -18.903 5.713   1   36.66  ? 174 CYS   B CA   1 2 
ATOM   3196 C  C    . CYS   B 1 175 ? 28.289 -20.421 5.906   1   36.34  ? 174 CYS   B C    1 2 
ATOM   3197 O  O    . CYS   B 1 175 ? 28.845 -21.139 5.081   1   37.13  ? 174 CYS   B O    1 2 
ATOM   3198 C  CB   . CYS   B 1 175 ? 29.761 -18.378 5.925   1   37.9   ? 174 CYS   B CB   1 2 
ATOM   3199 S  SG   . CYS   B 1 175 ? 29.993 -16.669 5.381   1   44.39  ? 174 CYS   B SG   1 2 
ATOM   3200 N  N    . GLY   B 1 176 ? 27.665 -20.893 6.984   1   35.42  ? 175 GLY   B N    1 2 
ATOM   3201 C  CA   . GLY   B 1 176 ? 27.445 -22.313 7.232   1   35.35  ? 175 GLY   B CA   1 2 
ATOM   3202 C  C    . GLY   B 1 176 ? 26.189 -22.846 6.554   1   35.07  ? 175 GLY   B C    1 2 
ATOM   3203 O  O    . GLY   B 1 176 ? 25.923 -24.052 6.583   1   34.81  ? 175 GLY   B O    1 2 
ATOM   3204 N  N    . HIS   B 1 177 ? 25.411 -21.95  5.925   1   34.97  ? 176 HIS   B N    1 2 
ATOM   3205 C  CA   . HIS   B 1 177 ? 24.171 -22.254 5.237   1   36.23  ? 176 HIS   B CA   1 2 
ATOM   3206 C  C    . HIS   B 1 177 ? 24.234 -21.874 3.771   1   37.55  ? 176 HIS   B C    1 2 
ATOM   3207 O  O    . HIS   B 1 177 ? 23.588 -22.521 2.948   1   37.96  ? 176 HIS   B O    1 2 
ATOM   3208 C  CB   . HIS   B 1 177 ? 23.007 -21.517 5.923   1   37.15  ? 176 HIS   B CB   1 2 
ATOM   3209 C  CG   . HIS   B 1 177 ? 22.821 -21.939 7.341   1   39.03  ? 176 HIS   B CG   1 2 
ATOM   3210 N  ND1  . HIS   B 1 177 ? 22.042 -23.031 7.667   1   40.74  ? 176 HIS   B ND1  1 2 
ATOM   3211 C  CD2  . HIS   B 1 177 ? 23.373 -21.439 8.471   1   40.27  ? 176 HIS   B CD2  1 2 
ATOM   3212 C  CE1  . HIS   B 1 177 ? 22.136 -23.154 8.979   1   41.25  ? 176 HIS   B CE1  1 2 
ATOM   3213 N  NE2  . HIS   B 1 177 ? 22.924 -22.215 9.505   1   41.34  ? 176 HIS   B NE2  1 2 
ATOM   3214 N  N    . GLU   B 1 178 ? 24.996 -20.82  3.433   1   38.26  ? 177 GLU   B N    1 2 
ATOM   3215 C  CA   . GLU   B 1 178 ? 25.123 -20.355 2.067   1   39.03  ? 177 GLU   B CA   1 2 
ATOM   3216 C  C    . GLU   B 1 178 ? 26.563 -19.916 1.783   1   39.78  ? 177 GLU   B C    1 2 
ATOM   3217 O  O    . GLU   B 1 178 ? 27.205 -19.318 2.642   1   40.01  ? 177 GLU   B O    1 2 
ATOM   3218 C  CB   . GLU   B 1 178 ? 24.118 -19.223 1.808   1   42.69  ? 177 GLU   B CB   1 2 
ATOM   3219 C  CG   . GLU   B 1 178 ? 24.156 -18.641 0.396   1   52.18  ? 177 GLU   B CG   1 2 
ATOM   3220 C  CD   . GLU   B 1 178 ? 23.782 -19.537 -0.779  1   62.94  ? 177 GLU   B CD   1 2 
ATOM   3221 O  OE1  . GLU   B 1 178 ? 22.731 -19.266 -1.407  1   66.56  ? 177 GLU   B OE1  1 2 
ATOM   3222 O  OE2  . GLU   B 1 178 ? 24.551 -20.477 -1.101  1   64.26  ? 177 GLU   B OE2  1 2 
ATOM   3223 N  N    . GLY   B 1 179 ? 27.073 -20.264 0.601   1   40.02  ? 178 GLY   B N    1 2 
ATOM   3224 C  CA   . GLY   B 1 179 ? 28.417 -19.92  0.156   1   40.58  ? 178 GLY   B CA   1 2 
ATOM   3225 C  C    . GLY   B 1 179 ? 28.58  -18.453 -0.2    1   40.84  ? 178 GLY   B C    1 2 
ATOM   3226 O  O    . GLY   B 1 179 ? 27.599 -17.744 -0.438  1   41.23  ? 178 GLY   B O    1 2 
ATOM   3227 N  N    . ILE   B 1 180 ? 29.827 -17.973 -0.203  1   40.35  ? 179 ILE   B N    1 2 
ATOM   3228 C  CA   . ILE   B 1 180 ? 30.142 -16.581 -0.518  1   39.96  ? 179 ILE   B CA   1 2 
ATOM   3229 C  C    . ILE   B 1 180 ? 31.418 -16.552 -1.335  1   37.32  ? 179 ILE   B C    1 2 
ATOM   3230 O  O    . ILE   B 1 180 ? 32.428 -17.108 -0.899  1   36.83  ? 179 ILE   B O    1 2 
ATOM   3231 C  CB   . ILE   B 1 180 ? 30.361 -15.763 0.794   1   42.15  ? 179 ILE   B CB   1 2 
ATOM   3232 C  CG1  . ILE   B 1 180 ? 29.079 -15.585 1.584   1   44.37  ? 179 ILE   B CG1  1 2 
ATOM   3233 C  CG2  . ILE   B 1 180 ? 30.988 -14.398 0.515   1   42.99  ? 179 ILE   B CG2  1 2 
ATOM   3234 C  CD1  . ILE   B 1 180 ? 29.32  -14.938 2.919   1   46.51  ? 179 ILE   B CD1  1 2 
ATOM   3235 N  N    . PRO   B 1 181 ? 31.438 -15.811 -2.447  1   35.62  ? 180 PRO   B N    1 2 
ATOM   3236 C  CA   . PRO   B 1 181 ? 32.686 -15.679 -3.217  1   35.15  ? 180 PRO   B CA   1 2 
ATOM   3237 C  C    . PRO   B 1 181 ? 33.848 -15.14  -2.368  1   34.92  ? 180 PRO   B C    1 2 
ATOM   3238 O  O    . PRO   B 1 181 ? 33.633 -14.347 -1.461  1   34.6   ? 180 PRO   B O    1 2 
ATOM   3239 C  CB   . PRO   B 1 181 ? 32.309 -14.681 -4.322  1   35.94  ? 180 PRO   B CB   1 2 
ATOM   3240 C  CG   . PRO   B 1 181 ? 30.826 -14.798 -4.463  1   36.19  ? 180 PRO   B CG   1 2 
ATOM   3241 C  CD   . PRO   B 1 181 ? 30.329 -15.067 -3.065  1   34.78  ? 180 PRO   B CD   1 2 
ATOM   3242 N  N    . TYR   B 1 182 ? 35.071 -15.609 -2.633  1   34.4   ? 181 TYR   B N    1 2 
ATOM   3243 C  CA   . TYR   B 1 182 ? 36.311 -15.211 -1.941  1   33.86  ? 181 TYR   B CA   1 2 
ATOM   3244 C  C    . TYR   B 1 182 ? 36.397 -15.726 -0.505  1   33.81  ? 181 TYR   B C    1 2 
ATOM   3245 O  O    . TYR   B 1 182 ? 37.385 -15.444 0.169   1   34.66  ? 181 TYR   B O    1 2 
ATOM   3246 C  CB   . TYR   B 1 182 ? 36.59  -13.697 -2.021  1   34.32  ? 181 TYR   B CB   1 2 
ATOM   3247 C  CG   . TYR   B 1 182 ? 36.21  -13.092 -3.369  1   36.37  ? 181 TYR   B CG   1 2 
ATOM   3248 C  CD1  . TYR   B 1 182 ? 36.675 -13.643 -4.557  1   37.77  ? 181 TYR   B CD1  1 2 
ATOM   3249 C  CD2  . TYR   B 1 182 ? 35.28  -12.069 -3.453  1   37.34  ? 181 TYR   B CD2  1 2 
ATOM   3250 C  CE1  . TYR   B 1 182 ? 36.243 -13.178 -5.789  1   39.21  ? 181 TYR   B CE1  1 2 
ATOM   3251 C  CE2  . TYR   B 1 182 ? 34.871 -11.568 -4.682  1   38.94  ? 181 TYR   B CE2  1 2 
ATOM   3252 C  CZ   . TYR   B 1 182 ? 35.346 -12.131 -5.852  1   40.58  ? 181 TYR   B CZ   1 2 
ATOM   3253 O  OH   . TYR   B 1 182 ? 34.973 -11.627 -7.089  1   43.17  ? 181 TYR   B OH   1 2 
ATOM   3254 N  N    . LEU   B 1 183 ? 35.421 -16.528 -0.038  1   32.14  ? 182 LEU   B N    1 2 
ATOM   3255 C  CA   . LEU   B 1 183 ? 35.468 -17.095 1.304   1   30.91  ? 182 LEU   B CA   1 2 
ATOM   3256 C  C    . LEU   B 1 183 ? 35.204 -18.611 1.223   1   30.3   ? 182 LEU   B C    1 2 
ATOM   3257 O  O    . LEU   B 1 183 ? 34.517 -19.144 2.098   1   30.23  ? 182 LEU   B O    1 2 
ATOM   3258 C  CB   . LEU   B 1 183 ? 34.423 -16.421 2.239   1   30.27  ? 182 LEU   B CB   1 2 
ATOM   3259 C  CG   . LEU   B 1 183 ? 34.668 -14.961 2.643   1   30.24  ? 182 LEU   B CG   1 2 
ATOM   3260 C  CD1  . LEU   B 1 183 ? 33.544 -14.432 3.52    1   28.96  ? 182 LEU   B CD1  1 2 
ATOM   3261 C  CD2  . LEU   B 1 183 ? 35.989 -14.802 3.342   1   30.74  ? 182 LEU   B CD2  1 2 
ATOM   3262 N  N    . ILE   B 1 184 ? 35.709 -19.297 0.173   1   29.18  ? 183 ILE   B N    1 2 
ATOM   3263 C  CA   . ILE   B 1 184 ? 35.469 -20.732 -0.013  1   28.51  ? 183 ILE   B CA   1 2 
ATOM   3264 C  C    . ILE   B 1 184 ? 35.959 -21.57  1.163   1   28.52  ? 183 ILE   B C    1 2 
ATOM   3265 O  O    . ILE   B 1 184 ? 35.135 -22.274 1.751   1   28.97  ? 183 ILE   B O    1 2 
ATOM   3266 C  CB   . ILE   B 1 184 ? 35.982 -21.301 -1.369  1   28.59  ? 183 ILE   B CB   1 2 
ATOM   3267 C  CG1  . ILE   B 1 184 ? 35.371 -20.562 -2.564  1   28.6   ? 183 ILE   B CG1  1 2 
ATOM   3268 C  CG2  . ILE   B 1 184 ? 35.709 -22.816 -1.446  1   29.04  ? 183 ILE   B CG2  1 2 
ATOM   3269 C  CD1  . ILE   B 1 184 ? 35.895 -21.008 -3.952  1   29.35  ? 183 ILE   B CD1  1 2 
ATOM   3270 N  N    . PRO   B 1 185 ? 37.264 -21.525 1.567   1   27.61  ? 184 PRO   B N    1 2 
ATOM   3271 C  CA   . PRO   B 1 185 ? 37.683 -22.349 2.7     1   25.98  ? 184 PRO   B CA   1 2 
ATOM   3272 C  C    . PRO   B 1 185 ? 36.942 -22.024 3.973   1   24.62  ? 184 PRO   B C    1 2 
ATOM   3273 O  O    . PRO   B 1 185 ? 36.652 -22.929 4.738   1   25.38  ? 184 PRO   B O    1 2 
ATOM   3274 C  CB   . PRO   B 1 185 ? 39.181 -22.067 2.813   1   27.14  ? 184 PRO   B CB   1 2 
ATOM   3275 C  CG   . PRO   B 1 185 ? 39.587 -21.587 1.468   1   27.91  ? 184 PRO   B CG   1 2 
ATOM   3276 C  CD   . PRO   B 1 185 ? 38.418 -20.795 0.988   1   26.77  ? 184 PRO   B CD   1 2 
ATOM   3277 N  N    . TYR   B 1 186 ? 36.591 -20.765 4.187   1   23.35  ? 185 TYR   B N    1 2 
ATOM   3278 C  CA   . TYR   B 1 186 ? 35.882 -20.35  5.396   1   23.05  ? 185 TYR   B CA   1 2 
ATOM   3279 C  C    . TYR   B 1 186 ? 34.454 -20.863 5.391   1   23.92  ? 185 TYR   B C    1 2 
ATOM   3280 O  O    . TYR   B 1 186 ? 33.998 -21.382 6.39    1   24.36  ? 185 TYR   B O    1 2 
ATOM   3281 C  CB   . TYR   B 1 186 ? 35.923 -18.828 5.515   1   22.35  ? 185 TYR   B CB   1 2 
ATOM   3282 C  CG   . TYR   B 1 186 ? 35.095 -18.271 6.639   1   22.75  ? 185 TYR   B CG   1 2 
ATOM   3283 C  CD1  . TYR   B 1 186 ? 35.595 -18.218 7.936   1   23.22  ? 185 TYR   B CD1  1 2 
ATOM   3284 C  CD2  . TYR   B 1 186 ? 33.824 -17.757 6.405   1   23.49  ? 185 TYR   B CD2  1 2 
ATOM   3285 C  CE1  . TYR   B 1 186 ? 34.851 -17.681 8.972   1   24.09  ? 185 TYR   B CE1  1 2 
ATOM   3286 C  CE2  . TYR   B 1 186 ? 33.066 -17.225 7.438   1   24.2   ? 185 TYR   B CE2  1 2 
ATOM   3287 C  CZ   . TYR   B 1 186 ? 33.588 -17.183 8.72    1   25.42  ? 185 TYR   B CZ   1 2 
ATOM   3288 O  OH   . TYR   B 1 186 ? 32.861 -16.645 9.752   1   27.27  ? 185 TYR   B OH   1 2 
ATOM   3289 N  N    . CYS   B 1 187 ? 33.744 -20.738 4.27    1   24.45  ? 186 CYS   B N    1 2 
ATOM   3290 C  CA   . CYS   B 1 187 ? 32.368 -21.212 4.144   1   25.77  ? 186 CYS   B CA   1 2 
ATOM   3291 C  C    . CYS   B 1 187 ? 32.304 -22.713 4.375   1   26.92  ? 186 CYS   B C    1 2 
ATOM   3292 O  O    . CYS   B 1 187 ? 31.363 -23.191 4.988   1   27.67  ? 186 CYS   B O    1 2 
ATOM   3293 C  CB   . CYS   B 1 187 ? 31.803 -20.86  2.768   1   27.03  ? 186 CYS   B CB   1 2 
ATOM   3294 S  SG   . CYS   B 1 187 ? 31.361 -19.128 2.574   1   31.53  ? 186 CYS   B SG   1 2 
ATOM   3295 N  N    . SER   B 1 188 ? 33.284 -23.453 3.837   1   26.9   ? 187 SER   B N    1 2 
ATOM   3296 C  CA   . SER   B 1 188 ? 33.385 -24.895 3.941   1   27     ? 187 SER   B CA   1 2 
ATOM   3297 C  C    . SER   B 1 188 ? 33.549 -25.288 5.415   1   27.34  ? 187 SER   B C    1 2 
ATOM   3298 O  O    . SER   B 1 188 ? 32.855 -26.188 5.889   1   28.48  ? 187 SER   B O    1 2 
ATOM   3299 C  CB   . SER   B 1 188 ? 34.567 -25.372 3.106   1   27.61  ? 187 SER   B CB   1 2 
ATOM   3300 O  OG   . SER   B 1 188 ? 34.53  -26.768 2.896   1   29.79  ? 187 SER   B OG   1 2 
ATOM   3301 N  N    . SER   B 1 189 ? 34.424 -24.587 6.157   1   26.26  ? 188 SER   B N    1 2 
ATOM   3302 C  CA   . SER   B 1 189 ? 34.62  -24.851 7.595   1   24.88  ? 188 SER   B CA   1 2 
ATOM   3303 C  C    . SER   B 1 189 ? 33.385 -24.436 8.409   1   24.25  ? 188 SER   B C    1 2 
ATOM   3304 O  O    . SER   B 1 189 ? 33.1   -25.047 9.437   1   25     ? 188 SER   B O    1 2 
ATOM   3305 C  CB   . SER   B 1 189 ? 35.868 -24.146 8.118   1   25.03  ? 188 SER   B CB   1 2 
ATOM   3306 O  OG   . SER   B 1 189 ? 35.665 -22.745 8.214   1   26.69  ? 188 SER   B OG   1 2 
ATOM   3307 N  N    . LYS   B 1 190 ? 32.635 -23.424 7.953   1   23.18  ? 189 LYS   B N    1 2 
ATOM   3308 C  CA   . LYS   B 1 190 ? 31.411 -23.016 8.637   1   23.18  ? 189 LYS   B CA   1 2 
ATOM   3309 C  C    . LYS   B 1 190 ? 30.262 -24.007 8.377   1   24.33  ? 189 LYS   B C    1 2 
ATOM   3310 O  O    . LYS   B 1 190 ? 29.468 -24.272 9.269   1   25.4   ? 189 LYS   B O    1 2 
ATOM   3311 C  CB   . LYS   B 1 190 ? 31.035 -21.563 8.302   1   22.7   ? 189 LYS   B CB   1 2 
ATOM   3312 C  CG   . LYS   B 1 190 ? 31.921 -20.548 8.998   1   23.11  ? 189 LYS   B CG   1 2 
ATOM   3313 C  CD   . LYS   B 1 190 ? 31.894 -20.699 10.526  1   26.07  ? 189 LYS   B CD   1 2 
ATOM   3314 C  CE   . LYS   B 1 190 ? 33.017 -19.923 11.174  1   28.98  ? 189 LYS   B CE   1 2 
ATOM   3315 N  NZ   . LYS   B 1 190 ? 32.777 -19.634 12.62   1   31.34  ? 189 LYS   B NZ   1 2 
ATOM   3316 N  N    . PHE   B 1 191 ? 30.216 -24.608 7.196   1   24.5   ? 190 PHE   B N    1 2 
ATOM   3317 C  CA   . PHE   B 1 191 ? 29.251 -25.654 6.876   1   24.87  ? 190 PHE   B CA   1 2 
ATOM   3318 C  C    . PHE   B 1 191 ? 29.578 -26.888 7.75    1   25.73  ? 190 PHE   B C    1 2 
ATOM   3319 O  O    . PHE   B 1 191 ? 28.674 -27.531 8.271   1   26.53  ? 190 PHE   B O    1 2 
ATOM   3320 C  CB   . PHE   B 1 191 ? 29.383 -26.035 5.398   1   24.7   ? 190 PHE   B CB   1 2 
ATOM   3321 C  CG   . PHE   B 1 191 ? 28.37  -25.42  4.457   1   24.79  ? 190 PHE   B CG   1 2 
ATOM   3322 C  CD1  . PHE   B 1 191 ? 28.463 -24.09  4.086   1   25.19  ? 190 PHE   B CD1  1 2 
ATOM   3323 C  CD2  . PHE   B 1 191 ? 27.359 -26.185 3.91    1   25     ? 190 PHE   B CD2  1 2 
ATOM   3324 C  CE1  . PHE   B 1 191 ? 27.558 -23.536 3.195   1   25.9   ? 190 PHE   B CE1  1 2 
ATOM   3325 C  CE2  . PHE   B 1 191 ? 26.453 -25.626 3.024   1   25.88  ? 190 PHE   B CE2  1 2 
ATOM   3326 C  CZ   . PHE   B 1 191 ? 26.568 -24.31  2.652   1   25.64  ? 190 PHE   B CZ   1 2 
ATOM   3327 N  N    . ALA   B 1 192 ? 30.881 -27.192 7.941   1   25.22  ? 191 ALA   B N    1 2 
ATOM   3328 C  CA   . ALA   B 1 192 ? 31.356 -28.268 8.799   1   24.59  ? 191 ALA   B CA   1 2 
ATOM   3329 C  C    . ALA   B 1 192 ? 30.895 -28.027 10.245  1   25.23  ? 191 ALA   B C    1 2 
ATOM   3330 O  O    . ALA   B 1 192 ? 30.507 -28.977 10.92   1   26.03  ? 191 ALA   B O    1 2 
ATOM   3331 C  CB   . ALA   B 1 192 ? 32.873 -28.347 8.734   1   24.03  ? 191 ALA   B CB   1 2 
ATOM   3332 N  N    . ALA   B 1 193 ? 30.925 -26.776 10.728  1   25.16  ? 192 ALA   B N    1 2 
ATOM   3333 C  CA   . ALA   B 1 193 ? 30.473 -26.448 12.075  1   25.66  ? 192 ALA   B CA   1 2 
ATOM   3334 C  C    . ALA   B 1 193 ? 28.949 -26.693 12.228  1   27.96  ? 192 ALA   B C    1 2 
ATOM   3335 O  O    . ALA   B 1 193 ? 28.527 -27.267 13.223  1   29.19  ? 192 ALA   B O    1 2 
ATOM   3336 C  CB   . ALA   B 1 193 ? 30.835 -25.011 12.42   1   25.06  ? 192 ALA   B CB   1 2 
ATOM   3337 N  N    . VAL   B 1 194 ? 28.133 -26.304 11.242  1   28.46  ? 193 VAL   B N    1 2 
ATOM   3338 C  CA   . VAL   B 1 194 ? 26.682 -26.529 11.287  1   28.64  ? 193 VAL   B CA   1 2 
ATOM   3339 C  C    . VAL   B 1 194 ? 26.391 -28.045 11.3    1   29.83  ? 193 VAL   B C    1 2 
ATOM   3340 O  O    . VAL   B 1 194 ? 25.512 -28.506 12.036  1   30.79  ? 193 VAL   B O    1 2 
ATOM   3341 C  CB   . VAL   B 1 194 ? 25.977 -25.831 10.077  1   27.96  ? 193 VAL   B CB   1 2 
ATOM   3342 C  CG1  . VAL   B 1 194 ? 24.528 -26.271 9.947   1   27.78  ? 193 VAL   B CG1  1 2 
ATOM   3343 C  CG2  . VAL   B 1 194 ? 26.063 -24.311 10.197  1   28.14  ? 193 VAL   B CG2  1 2 
ATOM   3344 N  N    . GLY   B 1 195 ? 27.132 -28.801 10.489  1   29.04  ? 194 GLY   B N    1 2 
ATOM   3345 C  CA   . GLY   B 1 195 ? 26.981 -30.246 10.398  1   28.4   ? 194 GLY   B CA   1 2 
ATOM   3346 C  C    . GLY   B 1 195 ? 27.343 -30.949 11.679  1   27.76  ? 194 GLY   B C    1 2 
ATOM   3347 O  O    . GLY   B 1 195 ? 26.674 -31.915 12.057  1   27.58  ? 194 GLY   B O    1 2 
ATOM   3348 N  N    . PHE   B 1 196 ? 28.395 -30.46  12.362  1   27.42  ? 195 PHE   B N    1 2 
ATOM   3349 C  CA   . PHE   B 1 196 ? 28.834 -31.005 13.65   1   27.76  ? 195 PHE   B CA   1 2 
ATOM   3350 C  C    . PHE   B 1 196 ? 27.717 -30.773 14.683  1   28.96  ? 195 PHE   B C    1 2 
ATOM   3351 O  O    . PHE   B 1 196 ? 27.367 -31.677 15.431  1   29.67  ? 195 PHE   B O    1 2 
ATOM   3352 C  CB   . PHE   B 1 196 ? 30.15  -30.335 14.088  1   27.43  ? 195 PHE   B CB   1 2 
ATOM   3353 C  CG   . PHE   B 1 196 ? 30.553 -30.595 15.517  1   27.99  ? 195 PHE   B CG   1 2 
ATOM   3354 C  CD1  . PHE   B 1 196 ? 31.141 -31.788 15.877  1   28.49  ? 195 PHE   B CD1  1 2 
ATOM   3355 C  CD2  . PHE   B 1 196 ? 30.315 -29.649 16.508  1   29.11  ? 195 PHE   B CD2  1 2 
ATOM   3356 C  CE1  . PHE   B 1 196 ? 31.481 -32.036 17.201  1   29.63  ? 195 PHE   B CE1  1 2 
ATOM   3357 C  CE2  . PHE   B 1 196 ? 30.673 -29.889 17.83   1   29.61  ? 195 PHE   B CE2  1 2 
ATOM   3358 C  CZ   . PHE   B 1 196 ? 31.252 -31.079 18.169  1   29.57  ? 195 PHE   B CZ   1 2 
ATOM   3359 N  N    . HIS   B 1 197 ? 27.151 -29.57  14.712  1   29.08  ? 196 HIS   B N    1 2 
ATOM   3360 C  CA   . HIS   B 1 197 ? 26.047 -29.232 15.595  1   29.8   ? 196 HIS   B CA   1 2 
ATOM   3361 C  C    . HIS   B 1 197 ? 24.803 -30.135 15.344  1   31.54  ? 196 HIS   B C    1 2 
ATOM   3362 O  O    . HIS   B 1 197 ? 24.158 -30.56  16.295  1   32.91  ? 196 HIS   B O    1 2 
ATOM   3363 C  CB   . HIS   B 1 197 ? 25.681 -27.733 15.429  1   29.27  ? 196 HIS   B CB   1 2 
ATOM   3364 C  CG   . HIS   B 1 197 ? 24.314 -27.382 15.938  1   29.46  ? 196 HIS   B CG   1 2 
ATOM   3365 N  ND1  . HIS   B 1 197 ? 24.028 -27.379 17.292  1   30.38  ? 196 HIS   B ND1  1 2 
ATOM   3366 C  CD2  . HIS   B 1 197 ? 23.175 -27.13  15.25   1   29.95  ? 196 HIS   B CD2  1 2 
ATOM   3367 C  CE1  . HIS   B 1 197 ? 22.736 -27.099 17.384  1   30.72  ? 196 HIS   B CE1  1 2 
ATOM   3368 N  NE2  . HIS   B 1 197 ? 22.184 -26.928 16.18   1   30.42  ? 196 HIS   B NE2  1 2 
ATOM   3369 N  N    A ARG   B 1 198 ? 24.457 -30.386 14.086  0.5 31.76  ? 197 ARG   B N    1 2 
ATOM   3370 N  N    B ARG   B 1 198 ? 24.468 -30.382 14.086  0.5 31.53  ? 197 ARG   B N    1 2 
ATOM   3371 C  CA   A ARG   B 1 198 ? 23.295 -31.201 13.741  0.5 32.78  ? 197 ARG   B CA   1 2 
ATOM   3372 C  CA   B ARG   B 1 198 ? 23.314 -31.196 13.737  0.5 32.37  ? 197 ARG   B CA   1 2 
ATOM   3373 C  C    A ARG   B 1 198 ? 23.471 -32.699 14.04   0.5 33.15  ? 197 ARG   B C    1 2 
ATOM   3374 C  C    B ARG   B 1 198 ? 23.487 -32.688 14.065  0.5 32.94  ? 197 ARG   B C    1 2 
ATOM   3375 O  O    A ARG   B 1 198 ? 22.521 -33.351 14.474  0.5 33.32  ? 197 ARG   B O    1 2 
ATOM   3376 O  O    B ARG   B 1 198 ? 22.548 -33.326 14.54   0.5 33.15  ? 197 ARG   B O    1 2 
ATOM   3377 C  CB   A ARG   B 1 198 ? 22.909 -30.995 12.262  0.5 34.44  ? 197 ARG   B CB   1 2 
ATOM   3378 C  CB   B ARG   B 1 198 ? 22.951 -31.022 12.241  0.5 33.39  ? 197 ARG   B CB   1 2 
ATOM   3379 C  CG   A ARG   B 1 198 ? 22.392 -29.597 11.979  0.5 37.63  ? 197 ARG   B CG   1 2 
ATOM   3380 C  CG   B ARG   B 1 198 ? 21.518 -30.54  11.974  0.5 35.46  ? 197 ARG   B CG   1 2 
ATOM   3381 C  CD   A ARG   B 1 198 ? 21.708 -29.497 10.632  0.5 40.45  ? 197 ARG   B CD   1 2 
ATOM   3382 C  CD   B ARG   B 1 198 ? 20.48  -31.277 12.796  0.5 37.51  ? 197 ARG   B CD   1 2 
ATOM   3383 N  NE   A ARG   B 1 198 ? 21.258 -28.129 10.384  0.5 43.09  ? 197 ARG   B NE   1 2 
ATOM   3384 N  NE   B ARG   B 1 198 ? 19.142 -31.194 12.228  0.5 39.68  ? 197 ARG   B NE   1 2 
ATOM   3385 C  CZ   A ARG   B 1 198 ? 20.353 -27.787 9.476   0.5 45.23  ? 197 ARG   B CZ   1 2 
ATOM   3386 C  CZ   B ARG   B 1 198 ? 18.051 -31.673 12.816  0.5 41.48  ? 197 ARG   B CZ   1 2 
ATOM   3387 N  NH1  A ARG   B 1 198 ? 19.773 -28.716 8.722   0.5 45.07  ? 197 ARG   B NH1  1 2 
ATOM   3388 N  NH1  B ARG   B 1 198 ? 18.132 -32.266 14.001  0.5 40.97  ? 197 ARG   B NH1  1 2 
ATOM   3389 N  NH2  A ARG   B 1 198 ? 20.013 -26.515 9.318   0.5 44.77  ? 197 ARG   B NH2  1 2 
ATOM   3390 N  NH2  B ARG   B 1 198 ? 16.869 -31.56  12.224  0.5 41.43  ? 197 ARG   B NH2  1 2 
ATOM   3391 N  N    . ALA   B 1 199 ? 24.65  -33.257 13.739  1   32.94  ? 198 ALA   B N    1 2 
ATOM   3392 C  CA   . ALA   B 1 199 ? 24.911 -34.665 13.995  1   32.84  ? 198 ALA   B CA   1 2 
ATOM   3393 C  C    . ALA   B 1 199 ? 25.074 -34.882 15.506  1   33.52  ? 198 ALA   B C    1 2 
ATOM   3394 O  O    . ALA   B 1 199 ? 24.622 -35.92  16.003  1   33.71  ? 198 ALA   B O    1 2 
ATOM   3395 C  CB   . ALA   B 1 199 ? 26.144 -35.129 13.241  1   32.43  ? 198 ALA   B CB   1 2 
ATOM   3396 N  N    . LEU   B 1 200 ? 25.646 -33.883 16.251  1   33.27  ? 199 LEU   B N    1 2 
ATOM   3397 C  CA   . LEU   B 1 200 ? 25.791 -33.959 17.706  1   33.2   ? 199 LEU   B CA   1 2 
ATOM   3398 C  C    . LEU   B 1 200 ? 24.418 -33.987 18.375  1   34.9   ? 199 LEU   B C    1 2 
ATOM   3399 O  O    . LEU   B 1 200 ? 24.162 -34.872 19.193  1   36.28  ? 199 LEU   B O    1 2 
ATOM   3400 C  CB   . LEU   B 1 200 ? 26.64  -32.813 18.266  1   32.54  ? 199 LEU   B CB   1 2 
ATOM   3401 C  CG   . LEU   B 1 200 ? 26.781 -32.77  19.803  1   32.91  ? 199 LEU   B CG   1 2 
ATOM   3402 C  CD1  . LEU   B 1 200 ? 27.459 -34.042 20.349  1   32.67  ? 199 LEU   B CD1  1 2 
ATOM   3403 C  CD2  . LEU   B 1 200 ? 27.509 -31.511 20.256  1   33.35  ? 199 LEU   B CD2  1 2 
ATOM   3404 N  N    . THR   B 1 201 ? 23.515 -33.056 18.004  1   34.8   ? 200 THR   B N    1 2 
ATOM   3405 C  CA   . THR   B 1 201 ? 22.133 -32.973 18.496  1   35.03  ? 200 THR   B CA   1 2 
ATOM   3406 C  C    . THR   B 1 201 ? 21.437 -34.317 18.296  1   35.56  ? 200 THR   B C    1 2 
ATOM   3407 O  O    . THR   B 1 201 ? 20.948 -34.9   19.261  1   36.46  ? 200 THR   B O    1 2 
ATOM   3408 C  CB   . THR   B 1 201 ? 21.384 -31.861 17.738  1   36.26  ? 200 THR   B CB   1 2 
ATOM   3409 O  OG1  . THR   B 1 201 ? 22.069 -30.629 17.917  1   38.36  ? 200 THR   B OG1  1 2 
ATOM   3410 C  CG2  . THR   B 1 201 ? 19.948 -31.73  18.158  1   36.06  ? 200 THR   B CG2  1 2 
ATOM   3411 N  N    . LEU   B 1 202 ? 21.514 -34.866 17.081  1   35.28  ? 201 LEU   B N    1 2 
ATOM   3412 C  CA   . LEU   B 1 202 ? 20.873 -36.133 16.79   1   35.55  ? 201 LEU   B CA   1 2 
ATOM   3413 C  C    . LEU   B 1 202 ? 21.47  -37.3   17.557  1   35.91  ? 201 LEU   B C    1 2 
ATOM   3414 O  O    . LEU   B 1 202 ? 20.714 -38.162 17.993  1   36.1   ? 201 LEU   B O    1 2 
ATOM   3415 C  CB   . LEU   B 1 202 ? 20.85  -36.389 15.287  1   35.15  ? 201 LEU   B CB   1 2 
ATOM   3416 C  CG   . LEU   B 1 202 ? 19.934 -35.438 14.515  1   36.17  ? 201 LEU   B CG   1 2 
ATOM   3417 C  CD1  . LEU   B 1 202 ? 20.04  -35.646 13.045  1   36.32  ? 201 LEU   B CD1  1 2 
ATOM   3418 C  CD2  . LEU   B 1 202 ? 18.513 -35.647 14.89   1   36.62  ? 201 LEU   B CD2  1 2 
ATOM   3419 N  N    . GLU   B 1 203 ? 22.806 -37.312 17.755  1   35.77  ? 202 GLU   B N    1 2 
ATOM   3420 C  CA   . GLU   B 1 203 ? 23.494 -38.382 18.471  1   36.3   ? 202 GLU   B CA   1 2 
ATOM   3421 C  C    . GLU   B 1 203 ? 23.158 -38.381 19.966  1   37.44  ? 202 GLU   B C    1 2 
ATOM   3422 O  O    . GLU   B 1 203 ? 22.839 -39.44  20.509  1   37.52  ? 202 GLU   B O    1 2 
ATOM   3423 C  CB   . GLU   B 1 203 ? 25.003 -38.313 18.258  1   38.04  ? 202 GLU   B CB   1 2 
ATOM   3424 C  CG   . GLU   B 1 203 ? 25.756 -39.425 18.972  1   42.66  ? 202 GLU   B CG   1 2 
ATOM   3425 C  CD   . GLU   B 1 203 ? 27.218 -39.481 18.596  1   46.63  ? 202 GLU   B CD   1 2 
ATOM   3426 O  OE1  . GLU   B 1 203 ? 28.078 -39.287 19.487  1   44.63  ? 202 GLU   B OE1  1 2 
ATOM   3427 O  OE2  . GLU   B 1 203 ? 27.505 -39.694 17.395  1   49.59  ? 202 GLU   B OE2  1 2 
ATOM   3428 N  N    . LEU   B 1 204 ? 23.187 -37.195 20.628  1   37.73  ? 203 LEU   B N    1 2 
ATOM   3429 C  CA   . LEU   B 1 204 ? 22.806 -37.055 22.041  1   38.64  ? 203 LEU   B CA   1 2 
ATOM   3430 C  C    . LEU   B 1 204 ? 21.373 -37.615 22.263  1   40.41  ? 203 LEU   B C    1 2 
ATOM   3431 O  O    . LEU   B 1 204 ? 21.136 -38.373 23.199  1   40.6   ? 203 LEU   B O    1 2 
ATOM   3432 C  CB   . LEU   B 1 204 ? 22.849 -35.567 22.452  1   37.99  ? 203 LEU   B CB   1 2 
ATOM   3433 C  CG   . LEU   B 1 204 ? 24.217 -34.934 22.528  1   38.1   ? 203 LEU   B CG   1 2 
ATOM   3434 C  CD1  . LEU   B 1 204 ? 24.125 -33.449 22.782  1   37.86  ? 203 LEU   B CD1  1 2 
ATOM   3435 C  CD2  . LEU   B 1 204 ? 25.021 -35.567 23.609  1   38.66  ? 203 LEU   B CD2  1 2 
ATOM   3436 N  N    . GLN   B 1 205 ? 20.454 -37.29  21.34   1   41.37  ? 204 GLN   B N    1 2 
ATOM   3437 C  CA   . GLN   B 1 205 ? 19.069 -37.709 21.364  1   42.89  ? 204 GLN   B CA   1 2 
ATOM   3438 C  C    . GLN   B 1 205 ? 18.988 -39.218 21.136  1   44.17  ? 204 GLN   B C    1 2 
ATOM   3439 O  O    . GLN   B 1 205 ? 18.323 -39.897 21.909  1   45.77  ? 204 GLN   B O    1 2 
ATOM   3440 C  CB   . GLN   B 1 205 ? 18.311 -36.911 20.31   1   45.56  ? 204 GLN   B CB   1 2 
ATOM   3441 C  CG   . GLN   B 1 205 ? 16.851 -37.231 20.097  1   51.99  ? 204 GLN   B CG   1 2 
ATOM   3442 C  CD   . GLN   B 1 205 ? 16.486 -36.782 18.698  1   61.01  ? 204 GLN   B CD   1 2 
ATOM   3443 O  OE1  . GLN   B 1 205 ? 16.621 -35.601 18.317  1   63.94  ? 204 GLN   B OE1  1 2 
ATOM   3444 N  NE2  . GLN   B 1 205 ? 16.072 -37.727 17.875  1   62.57  ? 204 GLN   B NE2  1 2 
ATOM   3445 N  N    . ALA   B 1 206 ? 19.748 -39.765 20.181  1   43.58  ? 205 ALA   B N    1 2 
ATOM   3446 C  CA   . ALA   B 1 206 ? 19.789 -41.211 19.926  1   43.79  ? 205 ALA   B CA   1 2 
ATOM   3447 C  C    . ALA   B 1 206 ? 20.307 -41.994 21.135  1   44.55  ? 205 ALA   B C    1 2 
ATOM   3448 O  O    . ALA   B 1 206 ? 19.873 -43.12  21.365  1   44.64  ? 205 ALA   B O    1 2 
ATOM   3449 C  CB   . ALA   B 1 206 ? 20.67  -41.509 18.728  1   43.66  ? 205 ALA   B CB   1 2 
ATOM   3450 N  N    . LEU   B 1 207 ? 21.241 -41.402 21.899  1   44.72  ? 206 LEU   B N    1 2 
ATOM   3451 C  CA   . LEU   B 1 207 ? 21.814 -42.041 23.084  1   45.07  ? 206 LEU   B CA   1 2 
ATOM   3452 C  C    . LEU   B 1 207 ? 20.977 -41.878 24.361  1   46.07  ? 206 LEU   B C    1 2 
ATOM   3453 O  O    . LEU   B 1 207 ? 21.381 -42.378 25.415  1   46.68  ? 206 LEU   B O    1 2 
ATOM   3454 C  CB   . LEU   B 1 207 ? 23.236 -41.525 23.331  1   44.78  ? 206 LEU   B CB   1 2 
ATOM   3455 C  CG   . LEU   B 1 207 ? 24.261 -41.829 22.256  1   45.81  ? 206 LEU   B CG   1 2 
ATOM   3456 C  CD1  . LEU   B 1 207 ? 25.576 -41.164 22.569  1   46.06  ? 206 LEU   B CD1  1 2 
ATOM   3457 C  CD2  . LEU   B 1 207 ? 24.462 -43.309 22.101  1   46.73  ? 206 LEU   B CD2  1 2 
ATOM   3458 N  N    . GLY   B 1 208 ? 19.837 -41.193 24.268  1   46.06  ? 207 GLY   B N    1 2 
ATOM   3459 C  CA   . GLY   B 1 208 ? 18.969 -40.948 25.411  1   46.47  ? 207 GLY   B CA   1 2 
ATOM   3460 C  C    . GLY   B 1 208 ? 19.504 -39.897 26.366  1   46.83  ? 207 GLY   B C    1 2 
ATOM   3461 O  O    . GLY   B 1 208 ? 19.091 -39.864 27.527  1   48.16  ? 207 GLY   B O    1 2 
ATOM   3462 N  N    . ILE   B 1 209 ? 20.434 -39.045 25.912  1   45.96  ? 208 ILE   B N    1 2 
ATOM   3463 C  CA   . ILE   B 1 209 ? 21.005 -37.983 26.73   1   46.35  ? 208 ILE   B CA   1 2 
ATOM   3464 C  C    . ILE   B 1 209 ? 20.15  -36.722 26.596  1   47.63  ? 208 ILE   B C    1 2 
ATOM   3465 O  O    . ILE   B 1 209 ? 20.326 -35.914 25.68   1   48.94  ? 208 ILE   B O    1 2 
ATOM   3466 C  CB   . ILE   B 1 209 ? 22.494 -37.758 26.385  1   46.28  ? 208 ILE   B CB   1 2 
ATOM   3467 C  CG1  . ILE   B 1 209 ? 23.289 -39.048 26.601  1   46.97  ? 208 ILE   B CG1  1 2 
ATOM   3468 C  CG2  . ILE   B 1 209 ? 23.095 -36.606 27.198  1   46.3   ? 208 ILE   B CG2  1 2 
ATOM   3469 C  CD1  . ILE   B 1 209 ? 24.634 -39.019 26.014  1   47.94  ? 208 ILE   B CD1  1 2 
ATOM   3470 N  N    . THR   B 1 210 ? 19.214 -36.572 27.522  1   47.32  ? 209 THR   B N    1 2 
ATOM   3471 C  CA   . THR   B 1 210 ? 18.227 -35.498 27.571  1   47.42  ? 209 THR   B CA   1 2 
ATOM   3472 C  C    . THR   B 1 210 ? 18.699 -34.168 28.192  1   47.26  ? 209 THR   B C    1 2 
ATOM   3473 O  O    . THR   B 1 210 ? 18.127 -33.11  27.917  1   47.52  ? 209 THR   B O    1 2 
ATOM   3474 C  CB   . THR   B 1 210 ? 16.994 -36.01  28.318  1   48.48  ? 209 THR   B CB   1 2 
ATOM   3475 O  OG1  . THR   B 1 210 ? 17.404 -36.47  29.605  1   50.37  ? 209 THR   B OG1  1 2 
ATOM   3476 C  CG2  . THR   B 1 210 ? 16.306 -37.15  27.597  1   48.51  ? 209 THR   B CG2  1 2 
ATOM   3477 N  N    . GLY   B 1 211 ? 19.717 -34.225 29.03   1   46.65  ? 210 GLY   B N    1 2 
ATOM   3478 C  CA   . GLY   B 1 211 ? 20.189 -33.055 29.76   1   46.14  ? 210 GLY   B CA   1 2 
ATOM   3479 C  C    . GLY   B 1 211 ? 21.195 -32.143 29.088  1   45.42  ? 210 GLY   B C    1 2 
ATOM   3480 O  O    . GLY   B 1 211 ? 21.499 -31.074 29.634  1   45.99  ? 210 GLY   B O    1 2 
ATOM   3481 N  N    . ILE   B 1 212 ? 21.745 -32.559 27.935  1   43.83  ? 211 ILE   B N    1 2 
ATOM   3482 C  CA   . ILE   B 1 212 ? 22.725 -31.755 27.202  1   43.19  ? 211 ILE   B CA   1 2 
ATOM   3483 C  C    . ILE   B 1 212 ? 22.087 -31.023 26.014  1   42.4   ? 211 ILE   B C    1 2 
ATOM   3484 O  O    . ILE   B 1 212 ? 21.635 -31.643 25.056  1   41.4   ? 211 ILE   B O    1 2 
ATOM   3485 C  CB   . ILE   B 1 212 ? 23.971 -32.575 26.783  1   43.33  ? 211 ILE   B CB   1 2 
ATOM   3486 C  CG1  . ILE   B 1 212 ? 24.635 -33.221 28.01   1   44.61  ? 211 ILE   B CG1  1 2 
ATOM   3487 C  CG2  . ILE   B 1 212 ? 24.956 -31.712 26      1   43.24  ? 211 ILE   B CG2  1 2 
ATOM   3488 C  CD1  . ILE   B 1 212 ? 25.779 -34.113 27.678  1   46.15  ? 211 ILE   B CD1  1 2 
ATOM   3489 N  N    . LYS   B 1 213 ? 22.033 -29.69  26.097  1   42.11  ? 212 LYS   B N    1 2 
ATOM   3490 C  CA   . LYS   B 1 213 ? 21.434 -28.86  25.05   1   40.96  ? 212 LYS   B CA   1 2 
ATOM   3491 C  C    . LYS   B 1 213 ? 22.47  -28.415 24.024  1   39.96  ? 212 LYS   B C    1 2 
ATOM   3492 O  O    . LYS   B 1 213 ? 23.672 -28.475 24.281  1   40.08  ? 212 LYS   B O    1 2 
ATOM   3493 C  CB   . LYS   B 1 213 ? 20.715 -27.647 25.68   1   42.2   ? 212 LYS   B CB   1 2 
ATOM   3494 C  CG   . LYS   B 1 213 ? 19.786 -28.014 26.85   1   44.56  ? 212 LYS   B CG   1 2 
ATOM   3495 C  CD   . LYS   B 1 213 ? 18.618 -28.821 26.351  1   48.14  ? 212 LYS   B CD   1 2 
ATOM   3496 C  CE   . LYS   B 1 213 ? 17.872 -29.533 27.432  1   51.39  ? 212 LYS   B CE   1 2 
ATOM   3497 N  NZ   . LYS   B 1 213 ? 16.605 -30.102 26.901  1   53.95  ? 212 LYS   B NZ   1 2 
ATOM   3498 N  N    . THR   B 1 214 ? 22.012 -28.036 22.832  1   38.84  ? 213 THR   B N    1 2 
ATOM   3499 C  CA   . THR   B 1 214 ? 22.909 -27.589 21.77   1   38.18  ? 213 THR   B CA   1 2 
ATOM   3500 C  C    . THR   B 1 214 ? 22.336 -26.333 21.128  1   37.49  ? 213 THR   B C    1 2 
ATOM   3501 O  O    . THR   B 1 214 ? 21.127 -26.234 20.955  1   37.66  ? 213 THR   B O    1 2 
ATOM   3502 C  CB   . THR   B 1 214 ? 23.118 -28.697 20.697  1   39.31  ? 213 THR   B CB   1 2 
ATOM   3503 O  OG1  . THR   B 1 214 ? 21.866 -29.058 20.11   1   40.37  ? 213 THR   B OG1  1 2 
ATOM   3504 C  CG2  . THR   B 1 214 ? 23.84  -29.938 21.222  1   39.04  ? 213 THR   B CG2  1 2 
ATOM   3505 N  N    . SER   B 1 215 ? 23.191 -25.378 20.767  1   36.96  ? 214 SER   B N    1 2 
ATOM   3506 C  CA   . SER   B 1 215 ? 22.769 -24.153 20.078  1   36.91  ? 214 SER   B CA   1 2 
ATOM   3507 C  C    . SER   B 1 215 ? 23.8   -23.827 19.004  1   36.69  ? 214 SER   B C    1 2 
ATOM   3508 O  O    . SER   B 1 215 ? 24.994 -24.038 19.215  1   37.11  ? 214 SER   B O    1 2 
ATOM   3509 C  CB   . SER   B 1 215 ? 22.673 -22.972 21.039  1   39.24  ? 214 SER   B CB   1 2 
ATOM   3510 O  OG   . SER   B 1 215 ? 21.504 -23.007 21.84   1   42.77  ? 214 SER   B OG   1 2 
ATOM   3511 N  N    . CYS   B 1 216 ? 23.347 -23.292 17.865  1   35.42  ? 215 CYS   B N    1 2 
ATOM   3512 C  CA   . CYS   B 1 216 ? 24.215 -22.908 16.773  1   34.95  ? 215 CYS   B CA   1 2 
ATOM   3513 C  C    . CYS   B 1 216 ? 23.982 -21.44  16.495  1   34.76  ? 215 CYS   B C    1 2 
ATOM   3514 O  O    . CYS   B 1 216 ? 22.867 -21.081 16.132  1   35.07  ? 215 CYS   B O    1 2 
ATOM   3515 C  CB   . CYS   B 1 216 ? 23.893 -23.747 15.543  1   35.33  ? 215 CYS   B CB   1 2 
ATOM   3516 S  SG   . CYS   B 1 216 ? 25.079 -23.571 14.184  1   36.36  ? 215 CYS   B SG   1 2 
ATOM   3517 N  N    . LEU   B 1 217 ? 25.004 -20.589 16.642  1   34.15  ? 216 LEU   B N    1 2 
ATOM   3518 C  CA   . LEU   B 1 217 ? 24.826 -19.163 16.365  1   34     ? 216 LEU   B CA   1 2 
ATOM   3519 C  C    . LEU   B 1 217 ? 25.267 -18.875 14.949  1   34.46  ? 216 LEU   B C    1 2 
ATOM   3520 O  O    . LEU   B 1 217 ? 26.419 -19.102 14.615  1   34.89  ? 216 LEU   B O    1 2 
ATOM   3521 C  CB   . LEU   B 1 217 ? 25.622 -18.304 17.34   1   33.35  ? 216 LEU   B CB   1 2 
ATOM   3522 C  CG   . LEU   B 1 217 ? 25.454 -16.806 17.149  1   33.1   ? 216 LEU   B CG   1 2 
ATOM   3523 C  CD1  . LEU   B 1 217 ? 24.073 -16.365 17.552  1   32.37  ? 216 LEU   B CD1  1 2 
ATOM   3524 C  CD2  . LEU   B 1 217 ? 26.529 -16.038 17.905  1   33.47  ? 216 LEU   B CD2  1 2 
ATOM   3525 N  N    . CYS   B 1 218 ? 24.362 -18.368 14.123  1   34.43  ? 217 CYS   B N    1 2 
ATOM   3526 C  CA   . CYS   B 1 218 ? 24.633 -18.045 12.725  1   35.29  ? 217 CYS   B CA   1 2 
ATOM   3527 C  C    . CYS   B 1 218 ? 24.347 -16.584 12.411  1   35.94  ? 217 CYS   B C    1 2 
ATOM   3528 O  O    . CYS   B 1 218 ? 23.314 -16.274 11.824  1   35.91  ? 217 CYS   B O    1 2 
ATOM   3529 C  CB   . CYS   B 1 218 ? 23.848 -18.968 11.801  1   35.81  ? 217 CYS   B CB   1 2 
ATOM   3530 S  SG   . CYS   B 1 218 ? 24.3   -20.708 11.957  1   41.44  ? 217 CYS   B SG   1 2 
ATOM   3531 N  N    . PRO   B 1 219 ? 25.244 -15.664 12.784  1   36.29  ? 218 PRO   B N    1 2 
ATOM   3532 C  CA   . PRO   B 1 219 ? 25.016 -14.252 12.44   1   36.85  ? 218 PRO   B CA   1 2 
ATOM   3533 C  C    . PRO   B 1 219 ? 25.45  -13.914 11.008  1   37.33  ? 218 PRO   B C    1 2 
ATOM   3534 O  O    . PRO   B 1 219 ? 26.287 -14.6   10.414  1   37.16  ? 218 PRO   B O    1 2 
ATOM   3535 C  CB   . PRO   B 1 219 ? 25.911 -13.493 13.439  1   37.46  ? 218 PRO   B CB   1 2 
ATOM   3536 C  CG   . PRO   B 1 219 ? 26.634 -14.565 14.27   1   37.61  ? 218 PRO   B CG   1 2 
ATOM   3537 C  CD   . PRO   B 1 219 ? 26.512 -15.848 13.51   1   35.71  ? 218 PRO   B CD   1 2 
ATOM   3538 N  N    . VAL   B 1 220 ? 24.894 -12.82  10.466  1   37.71  ? 219 VAL   B N    1 2 
ATOM   3539 C  CA   . VAL   B 1 220 ? 25.341 -12.251 9.21    1   38.64  ? 219 VAL   B CA   1 2 
ATOM   3540 C  C    . VAL   B 1 220 ? 26.589 -11.361 9.578   1   39.28  ? 219 VAL   B C    1 2 
ATOM   3541 O  O    . VAL   B 1 220 ? 27.161 -11.559 10.646  1   40.08  ? 219 VAL   B O    1 2 
ATOM   3542 C  CB   . VAL   B 1 220 ? 24.195 -11.495 8.46    1   39.93  ? 219 VAL   B CB   1 2 
ATOM   3543 C  CG1  . VAL   B 1 220 ? 23.024 -12.411 8.158   1   40.89  ? 219 VAL   B CG1  1 2 
ATOM   3544 C  CG2  . VAL   B 1 220 ? 23.743 -10.282 9.235   1   40.17  ? 219 VAL   B CG2  1 2 
ATOM   3545 N  N    . PHE   B 1 221 ? 27.049 -10.459 8.717   1   39.7   ? 220 PHE   B N    1 2 
ATOM   3546 C  CA   . PHE   B 1 221 ? 28.193 -9.61   9.004   1   40.57  ? 220 PHE   B CA   1 2 
ATOM   3547 C  C    . PHE   B 1 221 ? 28.059 -8.823  10.326  1   41.25  ? 220 PHE   B C    1 2 
ATOM   3548 O  O    . PHE   B 1 221 ? 27.105 -8.066  10.534  1   41.61  ? 220 PHE   B O    1 2 
ATOM   3549 C  CB   . PHE   B 1 221 ? 28.466 -8.67   7.818   1   40.28  ? 220 PHE   B CB   1 2 
ATOM   3550 C  CG   . PHE   B 1 221 ? 29.737 -7.883  7.979   1   40.88  ? 220 PHE   B CG   1 2 
ATOM   3551 C  CD1  . PHE   B 1 221 ? 30.967 -8.449  7.676   1   41.23  ? 220 PHE   B CD1  1 2 
ATOM   3552 C  CD2  . PHE   B 1 221 ? 29.708 -6.58   8.455   1   41.57  ? 220 PHE   B CD2  1 2 
ATOM   3553 C  CE1  . PHE   B 1 221 ? 32.137 -7.72   7.84    1   42     ? 220 PHE   B CE1  1 2 
ATOM   3554 C  CE2  . PHE   B 1 221 ? 30.883 -5.85   8.605   1   42.16  ? 220 PHE   B CE2  1 2 
ATOM   3555 C  CZ   . PHE   B 1 221 ? 32.087 -6.431  8.325   1   42.01  ? 220 PHE   B CZ   1 2 
ATOM   3556 N  N    . VAL   B 1 222 ? 29.024 -9.019  11.219  1   41.13  ? 221 VAL   B N    1 2 
ATOM   3557 C  CA   . VAL   B 1 222 ? 29.105 -8.304  12.492  1   41.3   ? 221 VAL   B CA   1 2 
ATOM   3558 C  C    . VAL   B 1 222 ? 30.338 -7.4    12.389  1   42.26  ? 221 VAL   B C    1 2 
ATOM   3559 O  O    . VAL   B 1 222 ? 31.408 -7.849  11.947  1   42.55  ? 221 VAL   B O    1 2 
ATOM   3560 C  CB   . VAL   B 1 222 ? 29.213 -9.245  13.727  1   40.92  ? 221 VAL   B CB   1 2 
ATOM   3561 C  CG1  . VAL   B 1 222 ? 29.045 -8.464  15.018  1   40.36  ? 221 VAL   B CG1  1 2 
ATOM   3562 C  CG2  . VAL   B 1 222 ? 28.204 -10.386 13.651  1   41.47  ? 221 VAL   B CG2  1 2 
ATOM   3563 N  N    . ASN   B 1 223 ? 30.186 -6.133  12.784  1   42.52  ? 222 ASN   B N    1 2 
ATOM   3564 C  CA   . ASN   B 1 223 ? 31.24  -5.125  12.736  1   44.27  ? 222 ASN   B CA   1 2 
ATOM   3565 C  C    . ASN   B 1 223 ? 32.296 -5.339  13.84   1   44.96  ? 222 ASN   B C    1 2 
ATOM   3566 O  O    . ASN   B 1 223 ? 32.362 -4.553  14.793  1   46.39  ? 222 ASN   B O    1 2 
ATOM   3567 C  CB   . ASN   B 1 223 ? 30.586 -3.736  12.855  1   47.02  ? 222 ASN   B CB   1 2 
ATOM   3568 C  CG   . ASN   B 1 223 ? 31.528 -2.566  12.935  1   51.81  ? 222 ASN   B CG   1 2 
ATOM   3569 O  OD1  . ASN   B 1 223 ? 32.48  -2.444  12.151  1   53.49  ? 222 ASN   B OD1  1 2 
ATOM   3570 N  ND2  . ASN   B 1 223 ? 31.278 -1.694  13.899  1   52.97  ? 222 ASN   B ND2  1 2 
ATOM   3571 N  N    . THR   B 1 224 ? 33.105 -6.401  13.738  1   43.85  ? 223 THR   B N    1 2 
ATOM   3572 C  CA   . THR   B 1 224 ? 34.121 -6.698  14.762  1   43.74  ? 223 THR   B CA   1 2 
ATOM   3573 C  C    . THR   B 1 224 ? 35.563 -6.558  14.263  1   43.5   ? 223 THR   B C    1 2 
ATOM   3574 O  O    . THR   B 1 224 ? 36.493 -6.727  15.052  1   44.47  ? 223 THR   B O    1 2 
ATOM   3575 C  CB   . THR   B 1 224 ? 33.969 -8.15   15.241  1   44.82  ? 223 THR   B CB   1 2 
ATOM   3576 O  OG1  . THR   B 1 224 ? 34.108 -9.024  14.116  1   46.29  ? 223 THR   B OG1  1 2 
ATOM   3577 C  CG2  . THR   B 1 224 ? 32.658 -8.409  15.919  1   44.81  ? 223 THR   B CG2  1 2 
ATOM   3578 N  N    . GLY   B 1 225 ? 35.739 -6.327  12.973  1   42.2   ? 224 GLY   B N    1 2 
ATOM   3579 C  CA   . GLY   B 1 225 ? 37.047 -6.277  12.344  1   41.95  ? 224 GLY   B CA   1 2 
ATOM   3580 C  C    . GLY   B 1 225 ? 37.498 -7.632  11.82   1   41.86  ? 224 GLY   B C    1 2 
ATOM   3581 O  O    . GLY   B 1 225 ? 38.589 -7.726  11.267  1   41.96  ? 224 GLY   B O    1 2 
ATOM   3582 N  N    . PHE   B 1 226 ? 36.69  -8.707  12.021  1   41.42  ? 225 PHE   B N    1 2 
ATOM   3583 C  CA   . PHE   B 1 226 ? 36.985 -10.07  11.584  1   41.33  ? 225 PHE   B CA   1 2 
ATOM   3584 C  C    . PHE   B 1 226 ? 37.209 -10.088 10.066  1   44.42  ? 225 PHE   B C    1 2 
ATOM   3585 O  O    . PHE   B 1 226 ? 38.158 -10.701 9.587   1   45.35  ? 225 PHE   B O    1 2 
ATOM   3586 C  CB   . PHE   B 1 226 ? 35.84  -11     11.996  1   39.13  ? 225 PHE   B CB   1 2 
ATOM   3587 C  CG   . PHE   B 1 226 ? 36.103 -12.47  11.803  1   37.6   ? 225 PHE   B CG   1 2 
ATOM   3588 C  CD1  . PHE   B 1 226 ? 37.066 -13.117 12.551  1   37.47  ? 225 PHE   B CD1  1 2 
ATOM   3589 C  CD2  . PHE   B 1 226 ? 35.344 -13.216 10.915  1   37.09  ? 225 PHE   B CD2  1 2 
ATOM   3590 C  CE1  . PHE   B 1 226 ? 37.279 -14.47  12.404  1   37.9   ? 225 PHE   B CE1  1 2 
ATOM   3591 C  CE2  . PHE   B 1 226 ? 35.568 -14.566 10.756  1   37.57  ? 225 PHE   B CE2  1 2 
ATOM   3592 C  CZ   . PHE   B 1 226 ? 36.539 -15.187 11.495  1   37.74  ? 225 PHE   B CZ   1 2 
ATOM   3593 N  N    . THR   B 1 227 ? 36.35  -9.376  9.324   1   45.99  ? 226 THR   B N    1 2 
ATOM   3594 C  CA   . THR   B 1 227 ? 36.425 -9.142  7.875   1   48     ? 226 THR   B CA   1 2 
ATOM   3595 C  C    . THR   B 1 227 ? 36.152 -7.647  7.653   1   49.36  ? 226 THR   B C    1 2 
ATOM   3596 O  O    . THR   B 1 227 ? 35.457 -7.021  8.462   1   49.22  ? 226 THR   B O    1 2 
ATOM   3597 C  CB   . THR   B 1 227 ? 35.504 -10.09  7.068   1   51.13  ? 226 THR   B CB   1 2 
ATOM   3598 O  OG1  . THR   B 1 227 ? 34.27  -10.286 7.767   1   54.78  ? 226 THR   B OG1  1 2 
ATOM   3599 C  CG2  . THR   B 1 227 ? 36.133 -11.46  6.842   1   51.19  ? 226 THR   B CG2  1 2 
ATOM   3600 N  N    . LYS   B 1 228 ? 36.725 -7.048  6.591   1   50.47  ? 227 LYS   B N    1 2 
ATOM   3601 C  CA   . LYS   B 1 228 ? 36.594 -5.611  6.372   1   51.24  ? 227 LYS   B CA   1 2 
ATOM   3602 C  C    . LYS   B 1 228 ? 35.195 -5.102  6.05    1   53     ? 227 LYS   B C    1 2 
ATOM   3603 O  O    . LYS   B 1 228 ? 34.808 -4.053  6.558   1   53.85  ? 227 LYS   B O    1 2 
ATOM   3604 C  CB   . LYS   B 1 228 ? 37.562 -5.147  5.293   1   52.45  ? 227 LYS   B CB   1 2 
ATOM   3605 C  CG   . LYS   B 1 228 ? 39.028 -5.235  5.696   1   54.81  ? 227 LYS   B CG   1 2 
ATOM   3606 C  CD   . LYS   B 1 228 ? 39.892 -4.711  4.578   1   58.04  ? 227 LYS   B CD   1 2 
ATOM   3607 C  CE   . LYS   B 1 228 ? 41.29  -4.502  5.023   1   61.25  ? 227 LYS   B CE   1 2 
ATOM   3608 N  NZ   . LYS   B 1 228 ? 41.39  -3.353  5.945   1   63.51  ? 227 LYS   B NZ   1 2 
ATOM   3609 N  N    . ASN   B 1 229 ? 34.455 -5.787  5.19    1   54.06  ? 228 ASN   B N    1 2 
ATOM   3610 C  CA   . ASN   B 1 229 ? 33.135 -5.323  4.757   1   55.97  ? 228 ASN   B CA   1 2 
ATOM   3611 C  C    . ASN   B 1 229 ? 32.181 -6.508  4.551   1   57.2   ? 228 ASN   B C    1 2 
ATOM   3612 O  O    . ASN   B 1 229 ? 32.643 -7.625  4.286   1   56.78  ? 228 ASN   B O    1 2 
ATOM   3613 C  CB   . ASN   B 1 229 ? 33.3   -4.604  3.391   1   58.32  ? 228 ASN   B CB   1 2 
ATOM   3614 C  CG   . ASN   B 1 229 ? 34.152 -3.354  3.4     1   63.53  ? 228 ASN   B CG   1 2 
ATOM   3615 O  OD1  . ASN   B 1 229 ? 33.89  -2.392  4.142   1   65.59  ? 228 ASN   B OD1  1 2 
ATOM   3616 N  ND2  . ASN   B 1 229 ? 35.189 -3.338  2.565   1   64.48  ? 228 ASN   B ND2  1 2 
ATOM   3617 N  N    . PRO   B 1 230 ? 30.846 -6.292  4.586   1   58.42  ? 229 PRO   B N    1 2 
ATOM   3618 C  CA   . PRO   B 1 230 ? 29.926 -7.396  4.257   1   59.66  ? 229 PRO   B CA   1 2 
ATOM   3619 C  C    . PRO   B 1 230 ? 30.129 -7.846  2.805   1   61.59  ? 229 PRO   B C    1 2 
ATOM   3620 O  O    . PRO   B 1 230 ? 30.571 -7.061  1.96    1   61.22  ? 229 PRO   B O    1 2 
ATOM   3621 C  CB   . PRO   B 1 230 ? 28.533 -6.766  4.427   1   59.88  ? 229 PRO   B CB   1 2 
ATOM   3622 C  CG   . PRO   B 1 230 ? 28.749 -5.536  5.23    1   59.77  ? 229 PRO   B CG   1 2 
ATOM   3623 C  CD   . PRO   B 1 230 ? 30.109 -5.046  4.857   1   57.94  ? 229 PRO   B CD   1 2 
ATOM   3624 N  N    . SER   B 1 231 ? 29.828 -9.116  2.515   1   63.22  ? 230 SER   B N    1 2 
ATOM   3625 C  CA   . SER   B 1 231 ? 29.985 -9.645  1.157   1   64.92  ? 230 SER   B CA   1 2 
ATOM   3626 C  C    . SER   B 1 231 ? 28.835 -9.3    0.207   1   66.28  ? 230 SER   B C    1 2 
ATOM   3627 O  O    . SER   B 1 231 ? 28.99  -9.435  -1.009  1   66.47  ? 230 SER   B O    1 2 
ATOM   3628 C  CB   . SER   B 1 231 ? 30.147 -11.15  1.209   1   66.54  ? 230 SER   B CB   1 2 
ATOM   3629 O  OG   . SER   B 1 231 ? 28.936 -11.778 1.594   1   69.12  ? 230 SER   B OG   1 2 
ATOM   3630 N  N    . THR   B 1 232 ? 27.66  -8.946  0.772   1   67.12  ? 231 THR   B N    1 2 
ATOM   3631 C  CA   . THR   B 1 232 ? 26.438 -8.56   0.056   1   68.33  ? 231 THR   B CA   1 2 
ATOM   3632 C  C    . THR   B 1 232 ? 26.05  -7.1    0.422   1   69.8   ? 231 THR   B C    1 2 
ATOM   3633 O  O    . THR   B 1 232 ? 26.608 -6.528  1.358   1   69.61  ? 231 THR   B O    1 2 
ATOM   3634 C  CB   . THR   B 1 232 ? 25.284 -9.569  0.33    1   69.36  ? 231 THR   B CB   1 2 
ATOM   3635 O  OG1  . THR   B 1 232 ? 24.647 -9.265  1.577   1   70.44  ? 231 THR   B OG1  1 2 
ATOM   3636 C  CG2  . THR   B 1 232 ? 25.733 -11.035 0.287   1   69.43  ? 231 THR   B CG2  1 2 
ATOM   3637 N  N    . ARG   B 1 233 ? 25.082 -6.508  -0.301  1   71.09  ? 232 ARG   B N    1 2 
ATOM   3638 C  CA   . ARG   B 1 233 ? 24.662 -5.136  -0.046  1   72.57  ? 232 ARG   B CA   1 2 
ATOM   3639 C  C    . ARG   B 1 233 ? 23.323 -5.081  0.698   1   72.91  ? 232 ARG   B C    1 2 
ATOM   3640 O  O    . ARG   B 1 233 ? 23.14  -5.773  1.701   1   73.13  ? 232 ARG   B O    1 2 
ATOM   3641 C  CB   . ARG   B 1 233 ? 24.584 -4.364  -1.366  1   74.83  ? 232 ARG   B CB   1 2 
ATOM   3642 C  CG   . ARG   B 1 233 ? 25.891 -4.38   -2.166  1   79.93  ? 232 ARG   B CG   1 2 
ATOM   3643 C  CD   . ARG   B 1 233 ? 25.822 -3.441  -3.37   1   85.42  ? 232 ARG   B CD   1 2 
ATOM   3644 N  NE   . ARG   B 1 233 ? 27.137 -3.209  -3.97   1   89.98  ? 232 ARG   B NE   1 2 
ATOM   3645 C  CZ   . ARG   B 1 233 ? 27.369 -2.357  -4.968  1   93.38  ? 232 ARG   B CZ   1 2 
ATOM   3646 N  NH1  . ARG   B 1 233 ? 26.374 -1.646  -5.49   1   93.47  ? 232 ARG   B NH1  1 2 
ATOM   3647 N  NH2  . ARG   B 1 233 ? 28.596 -2.21   -5.452  1   93.61  ? 232 ARG   B NH2  1 2 
ATOM   3648 N  N    . ILE   B 1 237 ? 24.559 -5.359  8.71    1   60.26  ? 236 ILE   B N    1 2 
ATOM   3649 C  CA   . ILE   B 1 237 ? 25.512 -4.544  9.471   1   61.02  ? 236 ILE   B CA   1 2 
ATOM   3650 C  C    . ILE   B 1 237 ? 25.22  -4.569  10.973  1   60.81  ? 236 ILE   B C    1 2 
ATOM   3651 O  O    . ILE   B 1 237 ? 24.766 -3.569  11.541  1   61.65  ? 236 ILE   B O    1 2 
ATOM   3652 C  CB   . ILE   B 1 237 ? 25.63  -3.106  8.911   1   62.46  ? 236 ILE   B CB   1 2 
ATOM   3653 C  CG1  . ILE   B 1 237 ? 24.238 -2.517  8.437   1   64.36  ? 236 ILE   B CG1  1 2 
ATOM   3654 C  CG2  . ILE   B 1 237 ? 26.665 -3.084  7.766   1   62.88  ? 236 ILE   B CG2  1 2 
ATOM   3655 C  CD1  . ILE   B 1 237 ? 23.499 -1.428  9.393   1   65.64  ? 236 ILE   B CD1  1 2 
ATOM   3656 N  N    . LEU   B 1 238 ? 25.485 -5.726  11.62   1   59.4   ? 237 LEU   B N    1 2 
ATOM   3657 C  CA   . LEU   B 1 238 ? 25.231 -5.936  13.047  1   58.28  ? 237 LEU   B CA   1 2 
ATOM   3658 C  C    . LEU   B 1 238 ? 26.293 -5.342  13.944  1   57.07  ? 237 LEU   B C    1 2 
ATOM   3659 O  O    . LEU   B 1 238 ? 27.464 -5.272  13.582  1   57.12  ? 237 LEU   B O    1 2 
ATOM   3660 C  CB   . LEU   B 1 238 ? 25.166 -7.437  13.371  1   58.48  ? 237 LEU   B CB   1 2 
ATOM   3661 C  CG   . LEU   B 1 238 ? 24.214 -8.284  12.577  1   59.99  ? 237 LEU   B CG   1 2 
ATOM   3662 C  CD1  . LEU   B 1 238 ? 24.508 -9.737  12.817  1   60.48  ? 237 LEU   B CD1  1 2 
ATOM   3663 C  CD2  . LEU   B 1 238 ? 22.791 -7.984  12.96   1   60.52  ? 237 LEU   B CD2  1 2 
ATOM   3664 N  N    . GLU   B 1 239 ? 25.894 -5.01   15.164  1   55.93  ? 238 GLU   B N    1 2 
ATOM   3665 C  CA   . GLU   B 1 239 ? 26.814 -4.541  16.177  1   55.1   ? 238 GLU   B CA   1 2 
ATOM   3666 C  C    . GLU   B 1 239 ? 27.1   -5.706  17.138  1   53.45  ? 238 GLU   B C    1 2 
ATOM   3667 O  O    . GLU   B 1 239 ? 26.19  -6.456  17.492  1   53.41  ? 238 GLU   B O    1 2 
ATOM   3668 C  CB   . GLU   B 1 239 ? 26.213 -3.336  16.911  1   57.78  ? 238 GLU   B CB   1 2 
ATOM   3669 C  CG   . GLU   B 1 239 ? 26.136 -2.086  16.056  1   63.46  ? 238 GLU   B CG   1 2 
ATOM   3670 C  CD   . GLU   B 1 239 ? 27.458 -1.647  15.454  1   72.02  ? 238 GLU   B CD   1 2 
ATOM   3671 O  OE1  . GLU   B 1 239 ? 27.541 -1.545  14.205  1   73.92  ? 238 GLU   B OE1  1 2 
ATOM   3672 O  OE2  . GLU   B 1 239 ? 28.415 -1.419  16.231  1   73.89  ? 238 GLU   B OE2  1 2 
ATOM   3673 N  N    . THR   B 1 240 ? 28.361 -5.863  17.544  1   51.95  ? 239 THR   B N    1 2 
ATOM   3674 C  CA   . THR   B 1 240 ? 28.817 -6.927  18.435  1   51.18  ? 239 THR   B CA   1 2 
ATOM   3675 C  C    . THR   B 1 240 ? 27.871 -7.279  19.603  1   51.4   ? 239 THR   B C    1 2 
ATOM   3676 O  O    . THR   B 1 240 ? 27.578 -8.457  19.8    1   51.17  ? 239 THR   B O    1 2 
ATOM   3677 C  CB   . THR   B 1 240 ? 30.205 -6.598  18.975  1   51.46  ? 239 THR   B CB   1 2 
ATOM   3678 O  OG1  . THR   B 1 240 ? 31.083 -6.247  17.911  1   51.81  ? 239 THR   B OG1  1 2 
ATOM   3679 C  CG2  . THR   B 1 240 ? 30.783 -7.729  19.763  1   51.87  ? 239 THR   B CG2  1 2 
ATOM   3680 N  N    . ASP   B 1 241 ? 27.407 -6.254  20.373  1   51.82  ? 240 ASP   B N    1 2 
ATOM   3681 C  CA   . ASP   B 1 241 ? 26.539 -6.35   21.56   1   52.26  ? 240 ASP   B CA   1 2 
ATOM   3682 C  C    . ASP   B 1 241 ? 25.159 -6.92   21.263  1   51.69  ? 240 ASP   B C    1 2 
ATOM   3683 O  O    . ASP   B 1 241 ? 24.567 -7.563  22.134  1   52.3   ? 240 ASP   B O    1 2 
ATOM   3684 C  CB   . ASP   B 1 241 ? 26.409 -4.989  22.266  1   54.78  ? 240 ASP   B CB   1 2 
ATOM   3685 C  CG   . ASP   B 1 241 ? 26.169 -3.84   21.316  1   60.5   ? 240 ASP   B CG   1 2 
ATOM   3686 O  OD1  . ASP   B 1 241 ? 27.091 -3.519  20.53   1   60.49  ? 240 ASP   B OD1  1 2 
ATOM   3687 O  OD2  . ASP   B 1 241 ? 25.059 -3.257  21.359  1   64.27  ? 240 ASP   B OD2  1 2 
ATOM   3688 N  N    . THR   B 1 242 ? 24.646 -6.681  20.044  1   50.31  ? 241 THR   B N    1 2 
ATOM   3689 C  CA   . THR   B 1 242 ? 23.359 -7.213  19.596  1   49.45  ? 241 THR   B CA   1 2 
ATOM   3690 C  C    . THR   B 1 242 ? 23.479 -8.72   19.411  1   48.42  ? 241 THR   B C    1 2 
ATOM   3691 O  O    . THR   B 1 242 ? 22.59  -9.46   19.824  1   49.37  ? 241 THR   B O    1 2 
ATOM   3692 C  CB   . THR   B 1 242 ? 22.949 -6.555  18.28   1   50.63  ? 241 THR   B CB   1 2 
ATOM   3693 O  OG1  . THR   B 1 242 ? 22.791 -5.165  18.517  1   53.17  ? 241 THR   B OG1  1 2 
ATOM   3694 C  CG2  . THR   B 1 242 ? 21.667 -7.12   17.728  1   50.3   ? 241 THR   B CG2  1 2 
ATOM   3695 N  N    . VAL   B 1 243 ? 24.587 -9.176  18.817  1   46.57  ? 242 VAL   B N    1 2 
ATOM   3696 C  CA   . VAL   B 1 243 ? 24.837 -10.578 18.558  1   45.73  ? 242 VAL   B CA   1 2 
ATOM   3697 C  C    . VAL   B 1 243 ? 24.997 -11.334 19.866  1   45.71  ? 242 VAL   B C    1 2 
ATOM   3698 O  O    . VAL   B 1 243 ? 24.453 -12.429 19.998  1   45.83  ? 242 VAL   B O    1 2 
ATOM   3699 C  CB   . VAL   B 1 243 ? 26.048 -10.726 17.618  1   45.89  ? 242 VAL   B CB   1 2 
ATOM   3700 C  CG1  . VAL   B 1 243 ? 26.384 -12.191 17.357  1   46.27  ? 242 VAL   B CG1  1 2 
ATOM   3701 C  CG2  . VAL   B 1 243 ? 25.795 -9.983  16.317  1   46.01  ? 242 VAL   B CG2  1 2 
ATOM   3702 N  N    . ALA   B 1 244 ? 25.683 -10.728 20.859  1   45.4   ? 243 ALA   B N    1 2 
ATOM   3703 C  CA   . ALA   B 1 244 ? 25.851 -11.328 22.188  1   45.42  ? 243 ALA   B CA   1 2 
ATOM   3704 C  C    . ALA   B 1 244 ? 24.491 -11.425 22.906  1   45.38  ? 243 ALA   B C    1 2 
ATOM   3705 O  O    . ALA   B 1 244 ? 24.214 -12.433 23.549  1   45.06  ? 243 ALA   B O    1 2 
ATOM   3706 C  CB   . ALA   B 1 244 ? 26.827 -10.516 23.009  1   45.21  ? 243 ALA   B CB   1 2 
ATOM   3707 N  N    . ARG   B 1 245 ? 23.626 -10.413 22.745  1   45.81  ? 244 ARG   B N    1 2 
ATOM   3708 C  CA   . ARG   B 1 245 ? 22.289 -10.442 23.326  1   47.26  ? 244 ARG   B CA   1 2 
ATOM   3709 C  C    . ARG   B 1 245 ? 21.462 -11.545 22.664  1   47.31  ? 244 ARG   B C    1 2 
ATOM   3710 O  O    . ARG   B 1 245 ? 20.782 -12.292 23.354  1   47.96  ? 244 ARG   B O    1 2 
ATOM   3711 C  CB   . ARG   B 1 245 ? 21.587 -9.077  23.207  1   50.47  ? 244 ARG   B CB   1 2 
ATOM   3712 C  CG   . ARG   B 1 245 ? 21.364 -8.427  24.561  1   58.91  ? 244 ARG   B CG   1 2 
ATOM   3713 C  CD   . ARG   B 1 245 ? 20.614 -7.091  24.52   1   66.18  ? 244 ARG   B CD   1 2 
ATOM   3714 N  NE   . ARG   B 1 245 ? 21.451 -5.96   24.09   1   71.91  ? 244 ARG   B NE   1 2 
ATOM   3715 C  CZ   . ARG   B 1 245 ? 21.391 -5.399  22.883  1   75.78  ? 244 ARG   B CZ   1 2 
ATOM   3716 N  NH1  . ARG   B 1 245 ? 20.536 -5.854  21.972  1   75.47  ? 244 ARG   B NH1  1 2 
ATOM   3717 N  NH2  . ARG   B 1 245 ? 22.181 -4.374  22.581  1   76.39  ? 244 ARG   B NH2  1 2 
ATOM   3718 N  N    . SER   B 1 246 ? 21.556 -11.682 21.344  1   46.55  ? 245 SER   B N    1 2 
ATOM   3719 C  CA   . SER   B 1 246 ? 20.839 -12.725 20.615  1   46.57  ? 245 SER   B CA   1 2 
ATOM   3720 C  C    . SER   B 1 246 ? 21.294 -14.116 21.043  1   46.81  ? 245 SER   B C    1 2 
ATOM   3721 O  O    . SER   B 1 246 ? 20.451 -14.992 21.25   1   46.97  ? 245 SER   B O    1 2 
ATOM   3722 C  CB   . SER   B 1 246 ? 21.032 -12.559 19.112  1   47.03  ? 245 SER   B CB   1 2 
ATOM   3723 O  OG   . SER   B 1 246 ? 20.075 -11.643 18.612  1   49.56  ? 245 SER   B OG   1 2 
ATOM   3724 N  N    . LEU   B 1 247 ? 22.622 -14.306 21.196  1   46.5   ? 246 LEU   B N    1 2 
ATOM   3725 C  CA   . LEU   B 1 247 ? 23.196 -15.562 21.631  1   46.95  ? 246 LEU   B CA   1 2 
ATOM   3726 C  C    . LEU   B 1 247 ? 22.713 -15.935 23.033  1   48.59  ? 246 LEU   B C    1 2 
ATOM   3727 O  O    . LEU   B 1 247 ? 22.132 -17.007 23.182  1   49.29  ? 246 LEU   B O    1 2 
ATOM   3728 C  CB   . LEU   B 1 247 ? 24.734 -15.531 21.571  1   46.65  ? 246 LEU   B CB   1 2 
ATOM   3729 C  CG   . LEU   B 1 247 ? 25.441 -16.8   22.085  1   47.88  ? 246 LEU   B CG   1 2 
ATOM   3730 C  CD1  . LEU   B 1 247 ? 24.979 -18.046 21.339  1   48.58  ? 246 LEU   B CD1  1 2 
ATOM   3731 C  CD2  . LEU   B 1 247 ? 26.942 -16.682 21.996  1   47.85  ? 246 LEU   B CD2  1 2 
ATOM   3732 N  N    . ILE   B 1 248 ? 22.889 -15.056 24.049  1   49.12  ? 247 ILE   B N    1 2 
ATOM   3733 C  CA   . ILE   B 1 248 ? 22.472 -15.389 25.408  1   50.22  ? 247 ILE   B CA   1 2 
ATOM   3734 C  C    . ILE   B 1 248 ? 20.976 -15.678 25.486  1   51.47  ? 247 ILE   B C    1 2 
ATOM   3735 O  O    . ILE   B 1 248 ? 20.594 -16.651 26.127  1   52.24  ? 247 ILE   B O    1 2 
ATOM   3736 C  CB   . ILE   B 1 248 ? 22.934 -14.353 26.463  1   50.95  ? 247 ILE   B CB   1 2 
ATOM   3737 C  CG1  . ILE   B 1 248 ? 22.95  -14.972 27.874  1   52.31  ? 247 ILE   B CG1  1 2 
ATOM   3738 C  CG2  . ILE   B 1 248 ? 22.087 -13.085 26.449  1   51.28  ? 247 ILE   B CG2  1 2 
ATOM   3739 C  CD1  . ILE   B 1 248 ? 24.029 -15.895 28.068  1   53.74  ? 247 ILE   B CD1  1 2 
ATOM   3740 N  N    . ASP   B 1 249 ? 20.141 -14.902 24.762  1   51.4   ? 248 ASP   B N    1 2 
ATOM   3741 C  CA   . ASP   B 1 249 ? 18.695 -15.111 24.749  1   51.52  ? 248 ASP   B CA   1 2 
ATOM   3742 C  C    . ASP   B 1 249 ? 18.333 -16.468 24.169  1   50.34  ? 248 ASP   B C    1 2 
ATOM   3743 O  O    . ASP   B 1 249 ? 17.437 -17.119 24.697  1   50.69  ? 248 ASP   B O    1 2 
ATOM   3744 C  CB   . ASP   B 1 249 ? 17.966 -13.962 24.039  1   54.45  ? 248 ASP   B CB   1 2 
ATOM   3745 C  CG   . ASP   B 1 249 ? 17.978 -12.666 24.843  1   62.22  ? 248 ASP   B CG   1 2 
ATOM   3746 O  OD1  . ASP   B 1 249 ? 17.832 -12.732 26.093  1   62.87  ? 248 ASP   B OD1  1 2 
ATOM   3747 O  OD2  . ASP   B 1 249 ? 18.137 -11.585 24.227  1   66.06  ? 248 ASP   B OD2  1 2 
ATOM   3748 N  N    . GLY   B 1 250 ? 19.069 -16.91  23.147  1   48.69  ? 249 GLY   B N    1 2 
ATOM   3749 C  CA   . GLY   B 1 250 ? 18.89  -18.223 22.538  1   47.82  ? 249 GLY   B CA   1 2 
ATOM   3750 C  C    . GLY   B 1 250 ? 19.315 -19.368 23.446  1   46.72  ? 249 GLY   B C    1 2 
ATOM   3751 O  O    . GLY   B 1 250 ? 18.617 -20.378 23.524  1   47.1   ? 249 GLY   B O    1 2 
ATOM   3752 N  N    . ILE   B 1 251 ? 20.459 -19.221 24.149  1   45.13  ? 250 ILE   B N    1 2 
ATOM   3753 C  CA   . ILE   B 1 251 ? 20.963 -20.225 25.086  1   43.98  ? 250 ILE   B CA   1 2 
ATOM   3754 C  C    . ILE   B 1 251 ? 19.981 -20.425 26.239  1   44.64  ? 250 ILE   B C    1 2 
ATOM   3755 O  O    . ILE   B 1 251 ? 19.615 -21.56  26.537  1   44.98  ? 250 ILE   B O    1 2 
ATOM   3756 C  CB   . ILE   B 1 251 ? 22.367 -19.844 25.613  1   42.56  ? 250 ILE   B CB   1 2 
ATOM   3757 C  CG1  . ILE   B 1 251 ? 23.387 -19.825 24.465  1   41.93  ? 250 ILE   B CG1  1 2 
ATOM   3758 C  CG2  . ILE   B 1 251 ? 22.811 -20.79  26.737  1   42.23  ? 250 ILE   B CG2  1 2 
ATOM   3759 C  CD1  . ILE   B 1 251 ? 24.749 -19.277 24.829  1   41.78  ? 250 ILE   B CD1  1 2 
ATOM   3760 N  N    . LEU   B 1 252 ? 19.511 -19.326 26.845  1   44.67  ? 251 LEU   B N    1 2 
ATOM   3761 C  CA   . LEU   B 1 252 ? 18.58  -19.389 27.956  1   45.35  ? 251 LEU   B CA   1 2 
ATOM   3762 C  C    . LEU   B 1 252 ? 17.236 -20.013 27.578  1   46.67  ? 251 LEU   B C    1 2 
ATOM   3763 O  O    . LEU   B 1 252 ? 16.548 -20.538 28.454  1   47.66  ? 251 LEU   B O    1 2 
ATOM   3764 C  CB   . LEU   B 1 252 ? 18.389 -18.004 28.583  1   45.46  ? 251 LEU   B CB   1 2 
ATOM   3765 C  CG   . LEU   B 1 252 ? 19.651 -17.306 29.094  1   46.58  ? 251 LEU   B CG   1 2 
ATOM   3766 C  CD1  . LEU   B 1 252 ? 19.319 -15.981 29.725  1   46.65  ? 251 LEU   B CD1  1 2 
ATOM   3767 C  CD2  . LEU   B 1 252 ? 20.419 -18.162 30.084  1   46.81  ? 251 LEU   B CD2  1 2 
ATOM   3768 N  N    . THR   B 1 253 ? 16.852 -19.966 26.286  1   46.76  ? 252 THR   B N    1 2 
ATOM   3769 C  CA   . THR   B 1 253 ? 15.595 -20.572 25.815  1   47.21  ? 252 THR   B CA   1 2 
ATOM   3770 C  C    . THR   B 1 253 ? 15.793 -21.927 25.11   1   47.76  ? 252 THR   B C    1 2 
ATOM   3771 O  O    . THR   B 1 253 ? 14.816 -22.488 24.616  1   48.68  ? 252 THR   B O    1 2 
ATOM   3772 C  CB   . THR   B 1 253 ? 14.786 -19.608 24.923  1   47.99  ? 252 THR   B CB   1 2 
ATOM   3773 O  OG1  . THR   B 1 253 ? 15.533 -19.285 23.752  1   48.84  ? 252 THR   B OG1  1 2 
ATOM   3774 C  CG2  . THR   B 1 253 ? 14.39  -18.343 25.643  1   48.45  ? 252 THR   B CG2  1 2 
ATOM   3775 N  N    . ASN   B 1 254 ? 17.038 -22.451 25.074  1   46.91  ? 253 ASN   B N    1 2 
ATOM   3776 C  CA   . ASN   B 1 254 ? 17.433 -23.705 24.438  1   46.28  ? 253 ASN   B CA   1 2 
ATOM   3777 C  C    . ASN   B 1 254 ? 17.142 -23.73  22.938  1   45.92  ? 253 ASN   B C    1 2 
ATOM   3778 O  O    . ASN   B 1 254 ? 16.765 -24.777 22.412  1   46.41  ? 253 ASN   B O    1 2 
ATOM   3779 C  CB   . ASN   B 1 254 ? 16.851 -24.934 25.152  1   46.74  ? 253 ASN   B CB   1 2 
ATOM   3780 C  CG   . ASN   B 1 254 ? 17.457 -25.231 26.505  1   50.47  ? 253 ASN   B CG   1 2 
ATOM   3781 O  OD1  . ASN   B 1 254 ? 16.882 -25.964 27.315  1   51.11  ? 253 ASN   B OD1  1 2 
ATOM   3782 N  ND2  . ASN   B 1 254 ? 18.629 -24.682 26.792  1   52     ? 253 ASN   B ND2  1 2 
ATOM   3783 N  N    . LYS   B 1 255 ? 17.353 -22.595 22.243  1   44.68  ? 254 LYS   B N    1 2 
ATOM   3784 C  CA   . LYS   B 1 255 ? 17.132 -22.52  20.805  1   43.79  ? 254 LYS   B CA   1 2 
ATOM   3785 C  C    . LYS   B 1 255 ? 18.265 -23.217 20.089  1   43.86  ? 254 LYS   B C    1 2 
ATOM   3786 O  O    . LYS   B 1 255 ? 19.429 -22.935 20.371  1   44.23  ? 254 LYS   B O    1 2 
ATOM   3787 C  CB   . LYS   B 1 255 ? 16.995 -21.075 20.336  1   44.6   ? 254 LYS   B CB   1 2 
ATOM   3788 C  CG   . LYS   B 1 255 ? 15.809 -20.903 19.407  1   48.62  ? 254 LYS   B CG   1 2 
ATOM   3789 C  CD   . LYS   B 1 255 ? 15.978 -19.715 18.504  1   54.29  ? 254 LYS   B CD   1 2 
ATOM   3790 C  CE   . LYS   B 1 255 ? 15.098 -19.797 17.275  1   59.06  ? 254 LYS   B CE   1 2 
ATOM   3791 N  NZ   . LYS   B 1 255 ? 15.782 -19.269 16.054  1   62.08  ? 254 LYS   B NZ   1 2 
ATOM   3792 N  N    . LYS   B 1 256 ? 17.936 -24.156 19.189  1   43.22  ? 255 LYS   B N    1 2 
ATOM   3793 C  CA   . LYS   B 1 256 ? 18.937 -24.937 18.475  1   42.93  ? 255 LYS   B CA   1 2 
ATOM   3794 C  C    . LYS   B 1 256 ? 19.631 -24.186 17.346  1   42.13  ? 255 LYS   B C    1 2 
ATOM   3795 O  O    . LYS   B 1 256 ? 20.83  -24.356 17.172  1   42.07  ? 255 LYS   B O    1 2 
ATOM   3796 C  CB   . LYS   B 1 256 ? 18.34  -26.259 17.98   1   45.01  ? 255 LYS   B CB   1 2 
ATOM   3797 C  CG   . LYS   B 1 256 ? 17.92  -27.121 19.15   1   50.2   ? 255 LYS   B CG   1 2 
ATOM   3798 C  CD   . LYS   B 1 256 ? 17.496 -28.52  18.767  1   56.69  ? 255 LYS   B CD   1 2 
ATOM   3799 C  CE   . LYS   B 1 256 ? 17.272 -29.312 20.043  1   62.98  ? 255 LYS   B CE   1 2 
ATOM   3800 N  NZ   . LYS   B 1 256 ? 16.605 -30.626 19.822  1   67.24  ? 255 LYS   B NZ   1 2 
ATOM   3801 N  N    . MET   B 1 257 ? 18.91  -23.384 16.57   1   41.73  ? 256 MET   B N    1 2 
ATOM   3802 C  CA   . MET   B 1 257 ? 19.529 -22.632 15.471  1   41.62  ? 256 MET   B CA   1 2 
ATOM   3803 C  C    . MET   B 1 257 ? 19.196 -21.172 15.654  1   42.23  ? 256 MET   B C    1 2 
ATOM   3804 O  O    . MET   B 1 257 ? 18.032 -20.792 15.583  1   43.06  ? 256 MET   B O    1 2 
ATOM   3805 C  CB   . MET   B 1 257 ? 19.081 -23.172 14.099  1   41.27  ? 256 MET   B CB   1 2 
ATOM   3806 C  CG   . MET   B 1 257 ? 19.841 -22.572 12.918  1   42.46  ? 256 MET   B CG   1 2 
ATOM   3807 S  SD   . MET   B 1 257 ? 21.608 -22.966 12.742  1   41.8   ? 256 MET   B SD   1 2 
ATOM   3808 C  CE   . MET   B 1 257 ? 21.559 -24.759 12.863  1   37.54  ? 256 MET   B CE   1 2 
ATOM   3809 N  N    . ILE   B 1 258 ? 20.188 -20.374 16.007  1   41.96  ? 257 ILE   B N    1 2 
ATOM   3810 C  CA   . ILE   B 1 258 ? 19.987 -18.956 16.264  1   42.5   ? 257 ILE   B CA   1 2 
ATOM   3811 C  C    . ILE   B 1 258 ? 20.531 -18.153 15.102  1   43.77  ? 257 ILE   B C    1 2 
ATOM   3812 O  O    . ILE   B 1 258 ? 21.735 -18.114 14.914  1   44.17  ? 257 ILE   B O    1 2 
ATOM   3813 C  CB   . ILE   B 1 258 ? 20.665 -18.54  17.603  1   42.02  ? 257 ILE   B CB   1 2 
ATOM   3814 C  CG1  . ILE   B 1 258 ? 20.214 -19.437 18.79   1   41.62  ? 257 ILE   B CG1  1 2 
ATOM   3815 C  CG2  . ILE   B 1 258 ? 20.476 -17.045 17.899  1   42.04  ? 257 ILE   B CG2  1 2 
ATOM   3816 C  CD1  . ILE   B 1 258 ? 21.236 -19.551 19.886  1   41.19  ? 257 ILE   B CD1  1 2 
ATOM   3817 N  N    . PHE   B 1 259 ? 19.66  -17.523 14.32   1   44.31  ? 258 PHE   B N    1 2 
ATOM   3818 C  CA   . PHE   B 1 259 ? 20.091 -16.67  13.222  1   45.64  ? 258 PHE   B CA   1 2 
ATOM   3819 C  C    . PHE   B 1 259 ? 20.09  -15.227 13.686  1   47.28  ? 258 PHE   B C    1 2 
ATOM   3820 O  O    . PHE   B 1 259 ? 19.145 -14.816 14.348  1   47.43  ? 258 PHE   B O    1 2 
ATOM   3821 C  CB   . PHE   B 1 259 ? 19.132 -16.805 12.037  1   45.29  ? 258 PHE   B CB   1 2 
ATOM   3822 C  CG   . PHE   B 1 259 ? 19.372 -18.056 11.246  1   45.77  ? 258 PHE   B CG   1 2 
ATOM   3823 C  CD1  . PHE   B 1 259 ? 20.497 -18.188 10.457  1   47.01  ? 258 PHE   B CD1  1 2 
ATOM   3824 C  CD2  . PHE   B 1 259 ? 18.482 -19.109 11.304  1   46.32  ? 258 PHE   B CD2  1 2 
ATOM   3825 C  CE1  . PHE   B 1 259 ? 20.729 -19.351 9.737   1   47.92  ? 258 PHE   B CE1  1 2 
ATOM   3826 C  CE2  . PHE   B 1 259 ? 18.701 -20.26  10.568  1   47.36  ? 258 PHE   B CE2  1 2 
ATOM   3827 C  CZ   . PHE   B 1 259 ? 19.822 -20.375 9.785   1   47.54  ? 258 PHE   B CZ   1 2 
ATOM   3828 N  N    . VAL   B 1 260 ? 21.127 -14.448 13.351  1   48.53  ? 259 VAL   B N    1 2 
ATOM   3829 C  CA   . VAL   B 1 260 ? 21.142 -13.023 13.704  1   49.89  ? 259 VAL   B CA   1 2 
ATOM   3830 C  C    . VAL   B 1 260 ? 21.325 -12.215 12.423  1   51.74  ? 259 VAL   B C    1 2 
ATOM   3831 O  O    . VAL   B 1 260 ? 22.411 -12.25  11.864  1   51.82  ? 259 VAL   B O    1 2 
ATOM   3832 C  CB   . VAL   B 1 260 ? 22.208 -12.649 14.761  1   50.07  ? 259 VAL   B CB   1 2 
ATOM   3833 C  CG1  . VAL   B 1 260 ? 21.955 -11.24  15.302  1   50.38  ? 259 VAL   B CG1  1 2 
ATOM   3834 C  CG2  . VAL   B 1 260 ? 22.25  -13.668 15.896  1   49.98  ? 259 VAL   B CG2  1 2 
ATOM   3835 N  N    . PRO   B 1 261 ? 20.3   -11.502 11.918  1   53.27  ? 260 PRO   B N    1 2 
ATOM   3836 C  CA   . PRO   B 1 261 ? 18.938 -11.375 12.454  1   54.82  ? 260 PRO   B CA   1 2 
ATOM   3837 C  C    . PRO   B 1 261 ? 18.085 -12.596 12.14   1   57.29  ? 260 PRO   B C    1 2 
ATOM   3838 O  O    . PRO   B 1 261 ? 18.275 -13.232 11.114  1   57.1   ? 260 PRO   B O    1 2 
ATOM   3839 C  CB   . PRO   B 1 261 ? 18.422 -10.102 11.772  1   54.83  ? 260 PRO   B CB   1 2 
ATOM   3840 C  CG   . PRO   B 1 261 ? 19.091 -10.115 10.435  1   54.92  ? 260 PRO   B CG   1 2 
ATOM   3841 C  CD   . PRO   B 1 261 ? 20.46  -10.717 10.678  1   53.25  ? 260 PRO   B CD   1 2 
ATOM   3842 N  N    . SER   B 1 262 ? 17.176 -12.945 13.057  1   59.5   ? 261 SER   B N    1 2 
ATOM   3843 C  CA   . SER   B 1 262 ? 16.302 -14.117 12.984  1   62.02  ? 261 SER   B CA   1 2 
ATOM   3844 C  C    . SER   B 1 262 ? 15.521 -14.24  11.687  1   64.88  ? 261 SER   B C    1 2 
ATOM   3845 O  O    . SER   B 1 262 ? 15.306 -15.354 11.194  1   65.19  ? 261 SER   B O    1 2 
ATOM   3846 C  CB   . SER   B 1 262 ? 15.363 -14.145 14.18   1   63.1   ? 261 SER   B CB   1 2 
ATOM   3847 O  OG   . SER   B 1 262 ? 14.726 -12.889 14.333  1   65.25  ? 261 SER   B OG   1 2 
ATOM   3848 N  N    . TYR   B 1 263 ? 15.116 -13.102 11.116  1   66.6   ? 262 TYR   B N    1 2 
ATOM   3849 C  CA   . TYR   B 1 263 ? 14.408 -13.101 9.845   1   68.73  ? 262 TYR   B CA   1 2 
ATOM   3850 C  C    . TYR   B 1 263 ? 15.271 -13.592 8.668   1   71.7   ? 262 TYR   B C    1 2 
ATOM   3851 O  O    . TYR   B 1 263 ? 14.734 -13.885 7.601   1   71.93  ? 262 TYR   B O    1 2 
ATOM   3852 C  CB   . TYR   B 1 263 ? 13.796 -11.723 9.562   1   68.45  ? 262 TYR   B CB   1 2 
ATOM   3853 C  CG   . TYR   B 1 263 ? 14.776 -10.614 9.244   1   68.77  ? 262 TYR   B CG   1 2 
ATOM   3854 C  CD1  . TYR   B 1 263 ? 15.389 -10.54  8.003   1   69.56  ? 262 TYR   B CD1  1 2 
ATOM   3855 C  CD2  . TYR   B 1 263 ? 14.967 -9.555  10.122  1   69.57  ? 262 TYR   B CD2  1 2 
ATOM   3856 C  CE1  . TYR   B 1 263 ? 16.246 -9.498  7.678   1   70.57  ? 262 TYR   B CE1  1 2 
ATOM   3857 C  CE2  . TYR   B 1 263 ? 15.805 -8.492  9.8     1   70.55  ? 262 TYR   B CE2  1 2 
ATOM   3858 C  CZ   . TYR   B 1 263 ? 16.445 -8.468  8.573   1   71.44  ? 262 TYR   B CZ   1 2 
ATOM   3859 O  OH   . TYR   B 1 263 ? 17.292 -7.445  8.221   1   72.87  ? 262 TYR   B OH   1 2 
ATOM   3860 N  N    . TYR   B 1 264 ? 16.609 -13.677 8.846   1   73.69  ? 263 TYR   B N    1 2 
ATOM   3861 C  CA   . TYR   B 1 264 ? 17.495 -14.174 7.789   1   75.83  ? 263 TYR   B CA   1 2 
ATOM   3862 C  C    . TYR   B 1 264 ? 17.4   -15.697 7.6     1   78.15  ? 263 TYR   B C    1 2 
ATOM   3863 O  O    . TYR   B 1 264 ? 18.285 -16.304 7.003   1   78.54  ? 263 TYR   B O    1 2 
ATOM   3864 C  CB   . TYR   B 1 264 ? 18.952 -13.708 7.986   1   75.85  ? 263 TYR   B CB   1 2 
ATOM   3865 C  CG   . TYR   B 1 264 ? 19.422 -12.825 6.85    1   76.73  ? 263 TYR   B CG   1 2 
ATOM   3866 C  CD1  . TYR   B 1 264 ? 19.855 -13.374 5.652   1   77.53  ? 263 TYR   B CD1  1 2 
ATOM   3867 C  CD2  . TYR   B 1 264 ? 19.345 -11.441 6.94    1   77.53  ? 263 TYR   B CD2  1 2 
ATOM   3868 C  CE1  . TYR   B 1 264 ? 20.214 -12.571 4.578   1   78.17  ? 263 TYR   B CE1  1 2 
ATOM   3869 C  CE2  . TYR   B 1 264 ? 19.724 -10.626 5.878   1   78.22  ? 263 TYR   B CE2  1 2 
ATOM   3870 C  CZ   . TYR   B 1 264 ? 20.174 -11.196 4.702   1   79     ? 263 TYR   B CZ   1 2 
ATOM   3871 O  OH   . TYR   B 1 264 ? 20.554 -10.412 3.639   1   80.45  ? 263 TYR   B OH   1 2 
ATOM   3872 N  N    . ASN   B 1 265 ? 16.317 -16.296 8.11    1   79.57  ? 264 ASN   B N    1 2 
ATOM   3873 C  CA   . ASN   B 1 265 ? 15.946 -17.694 8.018   1   81.54  ? 264 ASN   B CA   1 2 
ATOM   3874 C  C    . ASN   B 1 265 ? 15.04  -17.859 6.793   1   83.43  ? 264 ASN   B C    1 2 
ATOM   3875 O  O    . ASN   B 1 265 ? 15.163 -18.848 6.078   1   83.97  ? 264 ASN   B O    1 2 
ATOM   3876 C  CB   . ASN   B 1 265 ? 15.19  -18.09  9.281   1   83.14  ? 264 ASN   B CB   1 2 
ATOM   3877 C  CG   . ASN   B 1 265 ? 15.006 -19.567 9.436   1   86.81  ? 264 ASN   B CG   1 2 
ATOM   3878 O  OD1  . ASN   B 1 265 ? 15.728 -20.369 8.833   1   88.44  ? 264 ASN   B OD1  1 2 
ATOM   3879 N  ND2  . ASN   B 1 265 ? 14.037 -19.957 10.254  1   87.29  ? 264 ASN   B ND2  1 2 
ATOM   3880 N  N    . ILE   B 1 266 ? 14.135 -16.889 6.543   1   84.27  ? 265 ILE   B N    1 2 
ATOM   3881 C  CA   . ILE   B 1 266 ? 13.266 -16.917 5.378   1   85.61  ? 265 ILE   B CA   1 2 
ATOM   3882 C  C    . ILE   B 1 266 ? 14.061 -16.682 4.09    1   86.88  ? 265 ILE   B C    1 2 
ATOM   3883 O  O    . ILE   B 1 266 ? 13.687 -17.235 3.061   1   87.05  ? 265 ILE   B O    1 2 
ATOM   3884 C  CB   . ILE   B 1 266 ? 12.038 -15.981 5.515   1   86.38  ? 265 ILE   B CB   1 2 
ATOM   3885 C  CG1  . ILE   B 1 266 ? 12.386 -14.501 5.275   1   87.38  ? 265 ILE   B CG1  1 2 
ATOM   3886 C  CG2  . ILE   B 1 266 ? 11.346 -16.186 6.858   1   86.93  ? 265 ILE   B CG2  1 2 
ATOM   3887 C  CD1  . ILE   B 1 266 ? 11.166 -13.586 5.173   1   88.56  ? 265 ILE   B CD1  1 2 
ATOM   3888 N  N    . TYR   B 1 267 ? 15.179 -15.922 4.14    1   87.63  ? 266 TYR   B N    1 2 
ATOM   3889 C  CA   . TYR   B 1 267 ? 16.014 -15.725 2.946   1   88.87  ? 266 TYR   B CA   1 2 
ATOM   3890 C  C    . TYR   B 1 267 ? 16.62  -17.061 2.519   1   89.93  ? 266 TYR   B C    1 2 
ATOM   3891 O  O    . TYR   B 1 267 ? 16.689 -17.348 1.332   1   90.39  ? 266 TYR   B O    1 2 
ATOM   3892 C  CB   . TYR   B 1 267 ? 17.148 -14.72  3.196   1   89.08  ? 266 TYR   B CB   1 2 
ATOM   3893 C  CG   . TYR   B 1 267 ? 16.703 -13.276 3.291   1   90.28  ? 266 TYR   B CG   1 2 
ATOM   3894 C  CD1  . TYR   B 1 267 ? 16.517 -12.507 2.151   1   91.32  ? 266 TYR   B CD1  1 2 
ATOM   3895 C  CD2  . TYR   B 1 267 ? 16.515 -12.666 4.522   1   91.52  ? 266 TYR   B CD2  1 2 
ATOM   3896 C  CE1  . TYR   B 1 267 ? 16.124 -11.174 2.234   1   92.41  ? 266 TYR   B CE1  1 2 
ATOM   3897 C  CE2  . TYR   B 1 267 ? 16.127 -11.335 4.619   1   92.52  ? 266 TYR   B CE2  1 2 
ATOM   3898 C  CZ   . TYR   B 1 267 ? 15.931 -10.59  3.473   1   93.51  ? 266 TYR   B CZ   1 2 
ATOM   3899 O  OH   . TYR   B 1 267 ? 15.544 -9.275  3.578   1   95.15  ? 266 TYR   B OH   1 2 
ATOM   3900 N  N    . LEU   B 1 268 ? 17.04  -17.879 3.489   1   90.36  ? 267 LEU   B N    1 2 
ATOM   3901 C  CA   . LEU   B 1 268 ? 17.625 -19.195 3.254   1   91.28  ? 267 LEU   B CA   1 2 
ATOM   3902 C  C    . LEU   B 1 268 ? 16.582 -20.191 2.742   1   92.63  ? 267 LEU   B C    1 2 
ATOM   3903 O  O    . LEU   B 1 268 ? 16.9   -21.033 1.906   1   92.86  ? 267 LEU   B O    1 2 
ATOM   3904 C  CB   . LEU   B 1 268 ? 18.29  -19.704 4.554   1   91.13  ? 267 LEU   B CB   1 2 
ATOM   3905 C  CG   . LEU   B 1 268 ? 19.809 -19.444 4.8     1   92.24  ? 267 LEU   B CG   1 2 
ATOM   3906 C  CD1  . LEU   B 1 268 ? 20.39  -18.301 3.946   1   92.67  ? 267 LEU   B CD1  1 2 
ATOM   3907 C  CD2  . LEU   B 1 268 ? 20.072 -19.154 6.246   1   92.86  ? 267 LEU   B CD2  1 2 
ATOM   3908 N  N    . ILE   B 1 269 ? 15.337 -20.08  3.223   1   93.39  ? 268 ILE   B N    1 2 
ATOM   3909 C  CA   . ILE   B 1 269 ? 14.241 -20.936 2.781   1   94.59  ? 268 ILE   B CA   1 2 
ATOM   3910 C  C    . ILE   B 1 269 ? 13.851 -20.603 1.333   1   95.65  ? 268 ILE   B C    1 2 
ATOM   3911 O  O    . ILE   B 1 269 ? 13.6   -21.512 0.541   1   95.7   ? 268 ILE   B O    1 2 
ATOM   3912 C  CB   . ILE   B 1 269 ? 13.059 -20.84  3.77    1   95.25  ? 268 ILE   B CB   1 2 
ATOM   3913 C  CG1  . ILE   B 1 269 ? 13.419 -21.546 5.092   1   96.38  ? 268 ILE   B CG1  1 2 
ATOM   3914 C  CG2  . ILE   B 1 269 ? 11.768 -21.411 3.172   1   95.64  ? 268 ILE   B CG2  1 2 
ATOM   3915 C  CD1  . ILE   B 1 269 ? 12.453 -21.287 6.225   1   97.73  ? 268 ILE   B CD1  1 2 
ATOM   3916 N  N    . LEU   B 1 270 ? 13.867 -19.308 0.973   1   96.33  ? 269 LEU   B N    1 2 
ATOM   3917 C  CA   . LEU   B 1 270 ? 13.559 -18.873 -0.39   1   97.44  ? 269 LEU   B CA   1 2 
ATOM   3918 C  C    . LEU   B 1 270 ? 14.619 -19.333 -1.392  1   98.42  ? 269 LEU   B C    1 2 
ATOM   3919 O  O    . LEU   B 1 270 ? 14.281 -19.613 -2.542  1   98.46  ? 269 LEU   B O    1 2 
ATOM   3920 C  CB   . LEU   B 1 270 ? 13.382 -17.351 -0.461  1   97.75  ? 269 LEU   B CB   1 2 
ATOM   3921 C  CG   . LEU   B 1 270 ? 12.142 -16.788 0.22    1   99.31  ? 269 LEU   B CG   1 2 
ATOM   3922 C  CD1  . LEU   B 1 270 ? 12.12  -15.274 0.13    1   99.83  ? 269 LEU   B CD1  1 2 
ATOM   3923 C  CD2  . LEU   B 1 270 ? 10.868 -17.377 -0.37   1   100    ? 269 LEU   B CD2  1 2 
ATOM   3924 N  N    . ASP   B 1 271 ? 15.892 -19.429 -0.952  1   99.01  ? 270 ASP   B N    1 2 
ATOM   3925 C  CA   . ASP   B 1 271 ? 17.004 -19.907 -1.777  1   100.13 ? 270 ASP   B CA   1 2 
ATOM   3926 C  C    . ASP   B 1 271 ? 16.798 -21.368 -2.183  1   100.84 ? 270 ASP   B C    1 2 
ATOM   3927 O  O    . ASP   B 1 271 ? 17.167 -21.75  -3.292  1   101.13 ? 270 ASP   B O    1 2 
ATOM   3928 C  CB   . ASP   B 1 271 ? 18.338 -19.771 -1.027  1   102.14 ? 270 ASP   B CB   1 2 
ATOM   3929 C  CG   . ASP   B 1 271 ? 18.973 -18.395 -1.085  1   107.08 ? 270 ASP   B CG   1 2 
ATOM   3930 O  OD1  . ASP   B 1 271 ? 18.432 -17.516 -1.801  1   108.01 ? 270 ASP   B OD1  1 2 
ATOM   3931 O  OD2  . ASP   B 1 271 ? 20.015 -18.195 -0.414  1   108.97 ? 270 ASP   B OD2  1 2 
ATOM   3932 N  N    . LYS   B 1 272 ? 16.194 -22.18  -1.296  1   101    ? 271 LYS   B N    1 2 
ATOM   3933 C  CA   . LYS   B 1 272 ? 15.897 -23.587 -1.566  1   101.65 ? 271 LYS   B CA   1 2 
ATOM   3934 C  C    . LYS   B 1 272 ? 14.618 -23.771 -2.4    1   102.19 ? 271 LYS   B C    1 2 
ATOM   3935 O  O    . LYS   B 1 272 ? 14.003 -24.834 -2.331  1   102.26 ? 271 LYS   B O    1 2 
ATOM   3936 C  CB   . LYS   B 1 272 ? 15.787 -24.379 -0.252  1   103.36 ? 271 LYS   B CB   1 2 
ATOM   3937 C  CG   . LYS   B 1 272 ? 17.003 -25.264 0.036   1   107.05 ? 271 LYS   B CG   1 2 
ATOM   3938 C  CD   . LYS   B 1 272 ? 16.707 -26.76  -0.156  1   110.62 ? 271 LYS   B CD   1 2 
ATOM   3939 C  CE   . LYS   B 1 272 ? 17.925 -27.63  0.055   1   113.14 ? 271 LYS   B CE   1 2 
ATOM   3940 N  NZ   . LYS   B 1 272 ? 17.593 -29.074 -0.05   1   114.58 ? 271 LYS   B NZ   1 2 
ATOM   3941 N  N    . PHE   B 1 273 ? 14.234 -22.745 -3.191  1   102.34 ? 272 PHE   B N    1 2 
ATOM   3942 C  CA   . PHE   B 1 273 ? 13.058 -22.723 -4.056  1   102.93 ? 272 PHE   B CA   1 2 
ATOM   3943 C  C    . PHE   B 1 273 ? 13.363 -21.851 -5.289  1   103.03 ? 272 PHE   B C    1 2 
ATOM   3944 O  O    . PHE   B 1 273 ? 12.845 -20.739 -5.423  1   102.91 ? 272 PHE   B O    1 2 
ATOM   3945 C  CB   . PHE   B 1 273 ? 11.842 -22.156 -3.294  1   103.29 ? 272 PHE   B CB   1 2 
ATOM   3946 C  CG   . PHE   B 1 273 ? 11.027 -23.131 -2.469  1   104.3  ? 272 PHE   B CG   1 2 
ATOM   3947 C  CD1  . PHE   B 1 273 ? 11.326 -23.356 -1.134  1   105.17 ? 272 PHE   B CD1  1 2 
ATOM   3948 C  CD2  . PHE   B 1 273 ? 9.909  -23.753 -3.004  1   105.27 ? 272 PHE   B CD2  1 2 
ATOM   3949 C  CE1  . PHE   B 1 273 ? 10.559 -24.23  -0.368  1   105.9  ? 272 PHE   B CE1  1 2 
ATOM   3950 C  CE2  . PHE   B 1 273 ? 9.14   -24.625 -2.234  1   105.99 ? 272 PHE   B CE2  1 2 
ATOM   3951 C  CZ   . PHE   B 1 273 ? 9.47   -24.856 -0.921  1   105.77 ? 272 PHE   B CZ   1 2 
HETATM 3952 P  PA   . NAD   C 2 .   ? 34.047 -47.518 -1.595  1   34.07  ? 401 NAD   A PA   1 1 
HETATM 3953 O  O1A  . NAD   C 2 .   ? 33.383 -48.413 -2.569  1   34.48  ? 401 NAD   A O1A  1 1 
HETATM 3954 O  O2A  . NAD   C 2 .   ? 34.441 -48.035 -0.266  1   32.91  ? 401 NAD   A O2A  1 1 
HETATM 3955 O  O5B  . NAD   C 2 .   ? 35.294 -46.899 -2.39   1   33.8   ? 401 NAD   A O5B  1 1 
HETATM 3956 C  C5B  . NAD   C 2 .   ? 35.855 -45.606 -2.071  1   33.14  ? 401 NAD   A C5B  1 1 
HETATM 3957 C  C4B  . NAD   C 2 .   ? 37.215 -45.593 -2.716  1   32.77  ? 401 NAD   A C4B  1 1 
HETATM 3958 O  O4B  . NAD   C 2 .   ? 37.99  -44.467 -2.233  1   32.38  ? 401 NAD   A O4B  1 1 
HETATM 3959 C  C3B  . NAD   C 2 .   ? 38.035 -46.855 -2.426  1   32.54  ? 401 NAD   A C3B  1 1 
HETATM 3960 O  O3B  . NAD   C 2 .   ? 38.468 -47.476 -3.629  1   32.99  ? 401 NAD   A O3B  1 1 
HETATM 3961 C  C2B  . NAD   C 2 .   ? 39.191 -46.339 -1.566  1   32.5   ? 401 NAD   A C2B  1 1 
HETATM 3962 O  O2B  . NAD   C 2 .   ? 40.415 -47.018 -1.811  1   33.09  ? 401 NAD   A O2B  1 1 
HETATM 3963 C  C1B  . NAD   C 2 .   ? 39.318 -44.914 -2.062  1   32.5   ? 401 NAD   A C1B  1 1 
HETATM 3964 N  N9A  . NAD   C 2 .   ? 40.032 -44.03  -1.147  1   32.74  ? 401 NAD   A N9A  1 1 
HETATM 3965 C  C8A  . NAD   C 2 .   ? 39.942 -44.009 0.219   1   32.67  ? 401 NAD   A C8A  1 1 
HETATM 3966 N  N7A  . NAD   C 2 .   ? 40.838 -43.25  0.803   1   32.6   ? 401 NAD   A N7A  1 1 
HETATM 3967 C  C5A  . NAD   C 2 .   ? 41.571 -42.733 -0.255  1   32.56  ? 401 NAD   A C5A  1 1 
HETATM 3968 C  C6A  . NAD   C 2 .   ? 42.698 -41.887 -0.31   1   32.46  ? 401 NAD   A C6A  1 1 
HETATM 3969 N  N6A  . NAD   C 2 .   ? 43.273 -41.33  0.762   1   31.4   ? 401 NAD   A N6A  1 1 
HETATM 3970 N  N1A  . NAD   C 2 .   ? 43.208 -41.601 -1.53   1   33.33  ? 401 NAD   A N1A  1 1 
HETATM 3971 C  C2A  . NAD   C 2 .   ? 42.624 -42.12  -2.612  1   33.18  ? 401 NAD   A C2A  1 1 
HETATM 3972 N  N3A  . NAD   C 2 .   ? 41.562 -42.926 -2.681  1   33.18  ? 401 NAD   A N3A  1 1 
HETATM 3973 C  C4A  . NAD   C 2 .   ? 41.082 -43.202 -1.463  1   33     ? 401 NAD   A C4A  1 1 
HETATM 3974 O  O3   . NAD   C 2 .   ? 33.126 -46.222 -1.402  1   33.8   ? 401 NAD   A O3   1 1 
HETATM 3975 P  PN   . NAD   C 2 .   ? 31.803 -45.639 -2.091  1   32.62  ? 401 NAD   A PN   1 1 
HETATM 3976 O  O1N  . NAD   C 2 .   ? 31.924 -45.708 -3.569  1   33.02  ? 401 NAD   A O1N  1 1 
HETATM 3977 O  O2N  . NAD   C 2 .   ? 30.608 -46.193 -1.417  1   31.91  ? 401 NAD   A O2N  1 1 
HETATM 3978 O  O5D  . NAD   C 2 .   ? 31.932 -44.105 -1.696  1   31.91  ? 401 NAD   A O5D  1 1 
HETATM 3979 C  C5D  . NAD   C 2 .   ? 32.534 -43.156 -2.6    1   31.23  ? 401 NAD   A C5D  1 1 
HETATM 3980 C  C4D  . NAD   C 2 .   ? 32.164 -41.765 -2.16   1   30.92  ? 401 NAD   A C4D  1 1 
HETATM 3981 O  O4D  . NAD   C 2 .   ? 30.726 -41.649 -2.069  1   31.54  ? 401 NAD   A O4D  1 1 
HETATM 3982 C  C3D  . NAD   C 2 .   ? 32.713 -41.327 -0.796  1   30.27  ? 401 NAD   A C3D  1 1 
HETATM 3983 O  O3D  . NAD   C 2 .   ? 33.093 -39.96  -0.843  1   29.42  ? 401 NAD   A O3D  1 1 
HETATM 3984 C  C2D  . NAD   C 2 .   ? 31.509 -41.495 0.13    1   30.81  ? 401 NAD   A C2D  1 1 
HETATM 3985 O  O2D  . NAD   C 2 .   ? 31.579 -40.642 1.264   1   31.19  ? 401 NAD   A O2D  1 1 
HETATM 3986 C  C1D  . NAD   C 2 .   ? 30.38  -41.1   -0.825  1   31.22  ? 401 NAD   A C1D  1 1 
HETATM 3987 N  N1N  . NAD   C 2 .   ? 29.037 -41.631 -0.406  1   31.04  ? 401 NAD   A N1N  1 1 
HETATM 3988 C  C2N  . NAD   C 2 .   ? 28.892 -42.927 -0.086  1   30.85  ? 401 NAD   A C2N  1 1 
HETATM 3989 C  C3N  . NAD   C 2 .   ? 27.652 -43.425 0.266   1   30.94  ? 401 NAD   A C3N  1 1 
HETATM 3990 C  C7N  . NAD   C 2 .   ? 27.44  -44.886 0.545   1   31.21  ? 401 NAD   A C7N  1 1 
HETATM 3991 O  O7N  . NAD   C 2 .   ? 26.457 -45.24  1.196   1   30.78  ? 401 NAD   A O7N  1 1 
HETATM 3992 N  N7N  . NAD   C 2 .   ? 28.294 -45.752 0.015   1   31.84  ? 401 NAD   A N7N  1 1 
HETATM 3993 C  C4N  . NAD   C 2 .   ? 26.575 -42.553 0.298   1   30.89  ? 401 NAD   A C4N  1 1 
HETATM 3994 C  C5N  . NAD   C 2 .   ? 26.75  -41.222 -0.037  1   30.87  ? 401 NAD   A C5N  1 1 
HETATM 3995 C  C6N  . NAD   C 2 .   ? 27.998 -40.774 -0.383  1   30.91  ? 401 NAD   A C6N  1 1 
HETATM 3996 C  C4   . A1AG4 D 3 .   ? 25.501 -43.518 5.38    1   48.92  ? 402 A1AG4 A C4   1 1 
HETATM 3997 C  C7   . A1AG4 D 3 .   ? 23.201 -42.469 4.241   1   50.25  ? 402 A1AG4 A C7   1 1 
HETATM 3998 C  C6   . A1AG4 D 3 .   ? 23.11  -43.307 5.344   1   51     ? 402 A1AG4 A C6   1 1 
HETATM 3999 C  C13  . A1AG4 D 3 .   ? 20.543 -40.862 5.977   1   58.27  ? 402 A1AG4 A C13  1 1 
HETATM 4000 C  C20  . A1AG4 D 3 .   ? 26.967 -42.336 3.757   1   47.62  ? 402 A1AG4 A C20  1 1 
HETATM 4001 C  C16  . A1AG4 D 3 .   ? 18.442 -40.081 4.333   1   59.53  ? 402 A1AG4 A C16  1 1 
HETATM 4002 F  F1   . A1AG4 D 3 .   ? 24.496 -41.339 2.696   1   50.07  ? 402 A1AG4 A F1   1 1 
HETATM 4003 C  C2   . A1AG4 D 3 .   ? 24.438 -42.174 3.746   1   49.59  ? 402 A1AG4 A C2   1 1 
HETATM 4004 C  C3   . A1AG4 D 3 .   ? 25.617 -42.67  4.281   1   48.68  ? 402 A1AG4 A C3   1 1 
HETATM 4005 C  C5   . A1AG4 D 3 .   ? 24.265 -43.836 5.905   1   49.68  ? 402 A1AG4 A C5   1 1 
HETATM 4006 N  N8   . A1AG4 D 3 .   ? 21.838 -43.575 5.93    1   53.35  ? 402 A1AG4 A N8   1 1 
HETATM 4007 S  S9   . A1AG4 D 3 .   ? 20.379 -43.477 5.199   1   55.87  ? 402 A1AG4 A S9   1 1 
HETATM 4008 O  O10  . A1AG4 D 3 .   ? 19.476 -44.167 6.068   1   56.13  ? 402 A1AG4 A O10  1 1 
HETATM 4009 O  O11  . A1AG4 D 3 .   ? 20.521 -43.918 3.846   1   56.07  ? 402 A1AG4 A O11  1 1 
HETATM 4010 C  C12  . A1AG4 D 3 .   ? 19.905 -41.779 5.152   1   57.63  ? 402 A1AG4 A C12  1 1 
HETATM 4011 C  C14  . A1AG4 D 3 .   ? 20.113 -39.547 5.97    1   59.39  ? 402 A1AG4 A C14  1 1 
HETATM 4012 C  C15  . A1AG4 D 3 .   ? 19.042 -39.165 5.172   1   60.35  ? 402 A1AG4 A C15  1 1 
HETATM 4013 C  C17  . A1AG4 D 3 .   ? 18.875 -41.39  4.313   1   58.68  ? 402 A1AG4 A C17  1 1 
HETATM 4014 CL CL18 . A1AG4 D 3 .   ? 18.39  -37.556 5.247   1   61.99  ? 402 A1AG4 A CL18 1 1 
HETATM 4015 CL CL19 . A1AG4 D 3 .   ? 20.978 -38.373 6.918   1   59.81  ? 402 A1AG4 A CL19 1 1 
HETATM 4016 O  O21  . A1AG4 D 3 .   ? 27.886 -43.142 3.765   1   47.64  ? 402 A1AG4 A O21  1 1 
HETATM 4017 O  O22  . A1AG4 D 3 .   ? 27.084 -41.127 3.289   1   46.75  ? 402 A1AG4 A O22  1 1 
HETATM 4018 H  H23  . A1AG4 D 3 .   ? 26.387 -43.947 5.847   0   50.1   ? 402 A1AG4 A H23  1 1 
HETATM 4019 H  H25  . A1AG4 D 3 .   ? 22.323 -42.034 3.768   0   54.77  ? 402 A1AG4 A H25  1 1 
HETATM 4020 H  H27  . A1AG4 D 3 .   ? 21.364 -41.138 6.635   0   65.2   ? 402 A1AG4 A H27  1 1 
HETATM 4021 H  H28  . A1AG4 D 3 .   ? 17.632 -39.758 3.687   0   71.74  ? 402 A1AG4 A H28  1 1 
HETATM 4022 H  H24  . A1AG4 D 3 .   ? 24.228 -44.508 6.76    0   55.17  ? 402 A1AG4 A H24  1 1 
HETATM 4023 H  H26  . A1AG4 D 3 .   ? 21.949 -43.847 6.901   0   62.02  ? 402 A1AG4 A H26  1 1 
HETATM 4024 H  H29  . A1AG4 D 3 .   ? 18.407 -42.107 3.641   0   71.1   ? 402 A1AG4 A H29  1 1 
HETATM 4025 P  PA   . NAD   E 2 .   ? 37.23  -11.319 16.387  1   34.81  ? 401 NAD   B PA   1 2 
HETATM 4026 O  O1A  . NAD   E 2 .   ? 36.635 -10.149 17.061  1   35.37  ? 401 NAD   B O1A  1 2 
HETATM 4027 O  O2A  . NAD   E 2 .   ? 38.274 -11.126 15.346  1   34.53  ? 401 NAD   B O2A  1 2 
HETATM 4028 O  O5B  . NAD   E 2 .   ? 37.739 -12.241 17.572  1   34.23  ? 401 NAD   B O5B  1 2 
HETATM 4029 C  C5B  . NAD   E 2 .   ? 37.88  -13.669 17.407  1   34.3   ? 401 NAD   B C5B  1 2 
HETATM 4030 C  C4B  . NAD   E 2 .   ? 38.765 -14.096 18.55   1   33.9   ? 401 NAD   B C4B  1 2 
HETATM 4031 O  O4B  . NAD   E 2 .   ? 39.206 -15.459 18.35   1   34.08  ? 401 NAD   B O4B  1 2 
HETATM 4032 C  C3B  . NAD   E 2 .   ? 40.029 -13.237 18.704  1   33.44  ? 401 NAD   B C3B  1 2 
HETATM 4033 O  O3B  . NAD   E 2 .   ? 40.169 -12.691 20.008  1   33.6   ? 401 NAD   B O3B  1 2 
HETATM 4034 C  C2B  . NAD   E 2 .   ? 41.162 -14.192 18.332  1   33.37  ? 401 NAD   B C2B  1 2 
HETATM 4035 O  O2B  . NAD   E 2 .   ? 42.357 -13.959 19.064  1   33.3   ? 401 NAD   B O2B  1 2 
HETATM 4036 C  C1B  . NAD   E 2 .   ? 40.564 -15.525 18.731  1   33.42  ? 401 NAD   B C1B  1 2 
HETATM 4037 N  N9A  . NAD   E 2 .   ? 41.205 -16.66  18.08   1   32.99  ? 401 NAD   B N9A  1 2 
HETATM 4038 C  C8A  . NAD   E 2 .   ? 41.644 -16.752 16.784  1   32.18  ? 401 NAD   B C8A  1 2 
HETATM 4039 N  N7A  . NAD   E 2 .   ? 42.359 -17.823 16.536  1   31.95  ? 401 NAD   B N7A  1 2 
HETATM 4040 C  C5A  . NAD   E 2 .   ? 42.391 -18.485 17.756  1   31.92  ? 401 NAD   B C5A  1 2 
HETATM 4041 C  C6A  . NAD   E 2 .   ? 43.021 -19.669 18.179  1   31.03  ? 401 NAD   B C6A  1 2 
HETATM 4042 N  N6A  . NAD   E 2 .   ? 43.749 -20.453 17.382  1   30.39  ? 401 NAD   B N6A  1 2 
HETATM 4043 N  N1A  . NAD   E 2 .   ? 42.878 -20.025 19.474  1   30.74  ? 401 NAD   B N1A  1 2 
HETATM 4044 C  C2A  . NAD   E 2 .   ? 42.158 -19.245 20.28   1   31.19  ? 401 NAD   B C2A  1 2 
HETATM 4045 N  N3A  . NAD   E 2 .   ? 41.524 -18.108 19.999  1   31.91  ? 401 NAD   B N3A  1 2 
HETATM 4046 C  C4A  . NAD   E 2 .   ? 41.68  -17.779 18.715  1   32.45  ? 401 NAD   B C4A  1 2 
HETATM 4047 O  O3   . NAD   E 2 .   ? 36.056 -12.197 15.749  1   34.33  ? 401 NAD   B O3   1 2 
HETATM 4048 P  PN   . NAD   E 2 .   ? 34.457 -12.195 15.807  1   34.01  ? 401 NAD   B PN   1 2 
HETATM 4049 O  O1N  . NAD   E 2 .   ? 33.999 -12.038 17.204  1   34.09  ? 401 NAD   B O1N  1 2 
HETATM 4050 O  O2N  . NAD   E 2 .   ? 33.936 -11.309 14.737  1   34.17  ? 401 NAD   B O2N  1 2 
HETATM 4051 O  O5D  . NAD   E 2 .   ? 34.167 -13.711 15.391  1   33.6   ? 401 NAD   B O5D  1 2 
HETATM 4052 C  C5D  . NAD   E 2 .   ? 33.976 -14.734 16.38   1   32.56  ? 401 NAD   B C5D  1 2 
HETATM 4053 C  C4D  . NAD   E 2 .   ? 33.333 -15.922 15.717  1   32.67  ? 401 NAD   B C4D  1 2 
HETATM 4054 O  O4D  . NAD   E 2 .   ? 32.107 -15.523 15.063  1   32.94  ? 401 NAD   B O4D  1 2 
HETATM 4055 C  C3D  . NAD   E 2 .   ? 34.169 -16.644 14.652  1   32.31  ? 401 NAD   B C3D  1 2 
HETATM 4056 O  O3D  . NAD   E 2 .   ? 33.984 -18.054 14.745  1   32.12  ? 401 NAD   B O3D  1 2 
HETATM 4057 C  C2D  . NAD   E 2 .   ? 33.565 -16.139 13.347  1   32.38  ? 401 NAD   B C2D  1 2 
HETATM 4058 O  O2D  . NAD   E 2 .   ? 33.742 -17.064 12.28   1   32.68  ? 401 NAD   B O2D  1 2 
HETATM 4059 C  C1D  . NAD   E 2 .   ? 32.096 -16.013 13.753  1   32.61  ? 401 NAD   B C1D  1 2 
HETATM 4060 N  N1N  . NAD   E 2 .   ? 31.311 -15.073 12.885  1   32.82  ? 401 NAD   B N1N  1 2 
HETATM 4061 C  C2N  . NAD   E 2 .   ? 31.786 -13.842 12.63   1   32.99  ? 401 NAD   B C2N  1 2 
HETATM 4062 C  C3N  . NAD   E 2 .   ? 31.07  -12.968 11.835  1   33.73  ? 401 NAD   B C3N  1 2 
HETATM 4063 C  C7N  . NAD   E 2 .   ? 31.534 -11.558 11.602  1   34.26  ? 401 NAD   B C7N  1 2 
HETATM 4064 O  O7N  . NAD   E 2 .   ? 31.104 -10.93  10.621  1   34.88  ? 401 NAD   B O7N  1 2 
HETATM 4065 N  N7N  . NAD   E 2 .   ? 32.367 -11.023 12.488  1   34.12  ? 401 NAD   B N7N  1 2 
HETATM 4066 C  C4N  . NAD   E 2 .   ? 29.86  -13.398 11.297  1   33.7   ? 401 NAD   B C4N  1 2 
HETATM 4067 C  C5N  . NAD   E 2 .   ? 29.389 -14.669 11.582  1   33.41  ? 401 NAD   B C5N  1 2 
HETATM 4068 C  C6N  . NAD   E 2 .   ? 30.136 -15.5   12.381  1   32.98  ? 401 NAD   B C6N  1 2 
HETATM 4069 C  C4   . A1AG4 F 3 .   ? 31.305 -12.4   6.217   1   45.69  ? 402 A1AG4 B C4   1 2 
HETATM 4070 C  C7   . A1AG4 F 3 .   ? 28.539 -12.552 6.381   1   46.21  ? 402 A1AG4 B C7   1 2 
HETATM 4071 C  C6   . A1AG4 F 3 .   ? 29.138 -11.845 5.341   1   47.52  ? 402 A1AG4 B C6   1 2 
HETATM 4072 C  C13  . A1AG4 F 3 .   ? 26.374 -13.258 3.692   1   55.5   ? 402 A1AG4 B C13  1 2 
HETATM 4073 C  C20  . A1AG4 F 3 .   ? 31.618 -13.724 8.293   1   44.2   ? 402 A1AG4 B C20  1 2 
HETATM 4074 C  C16  . A1AG4 F 3 .   ? 23.605 -13.014 3.833   1   57.03  ? 402 A1AG4 B C16  1 2 
HETATM 4075 F  F1   . A1AG4 F 3 .   ? 28.748 -13.899 8.273   1   44.57  ? 402 A1AG4 B F1   1 2 
HETATM 4076 C  C2   . A1AG4 F 3 .   ? 29.345 -13.162 7.308   1   45.28  ? 402 A1AG4 B C2   1 2 
HETATM 4077 C  C3   . A1AG4 F 3 .   ? 30.73  -13.099 7.275   1   45.05  ? 402 A1AG4 B C3   1 2 
HETATM 4078 C  C5   . A1AG4 F 3 .   ? 30.523 -11.783 5.26    1   46.61  ? 402 A1AG4 B C5   1 2 
HETATM 4079 N  N8   . A1AG4 F 3 .   ? 28.361 -11.181 4.344   1   49.78  ? 402 A1AG4 B N8   1 2 
HETATM 4080 S  S9   . A1AG4 F 3 .   ? 26.81  -10.688 4.473   1   52.36  ? 402 A1AG4 B S9   1 2 
HETATM 4081 O  O10  . A1AG4 F 3 .   ? 26.625 -9.711  3.446   1   52.1   ? 402 A1AG4 B O10  1 2 
HETATM 4082 O  O11  . A1AG4 F 3 .   ? 26.58  -10.324 5.838   1   53.27  ? 402 A1AG4 B O11  1 2 
HETATM 4083 C  C12  . A1AG4 F 3 .   ? 25.785 -12.071 4.106   1   54.7   ? 402 A1AG4 B C12  1 2 
HETATM 4084 C  C14  . A1AG4 F 3 .   ? 25.561 -14.328 3.368   1   56.56  ? 402 A1AG4 B C14  1 2 
HETATM 4085 C  C15  . A1AG4 F 3 .   ? 24.179 -14.208 3.429   1   58     ? 402 A1AG4 B C15  1 2 
HETATM 4086 C  C17  . A1AG4 F 3 .   ? 24.406 -11.945 4.189   1   55.93  ? 402 A1AG4 B C17  1 2 
HETATM 4087 CL CL18 . A1AG4 F 3 .   ? 23.148 -15.561 3.065   1   59.84  ? 402 A1AG4 B CL18 1 2 
HETATM 4088 CL CL19 . A1AG4 F 3 .   ? 26.302 -15.843 2.985   1   56.29  ? 402 A1AG4 B CL19 1 2 
HETATM 4089 O  O21  . A1AG4 F 3 .   ? 32.654 -13.186 8.664   1   44.23  ? 402 A1AG4 B O21  1 2 
HETATM 4090 O  O22  . A1AG4 F 3 .   ? 31.203 -14.877 8.739   1   43.44  ? 402 A1AG4 B O22  1 2 
HETATM 4091 H  H23  . A1AG4 F 3 .   ? 32.388 -12.328 6.123   0   43.28  ? 402 A1AG4 B H23  1 2 
HETATM 4092 H  H25  . A1AG4 F 3 .   ? 27.458 -12.642 6.471   0   47.26  ? 402 A1AG4 B H25  1 2 
HETATM 4093 H  H27  . A1AG4 F 3 .   ? 27.451 -13.387 3.61    0   57.36  ? 402 A1AG4 B H27  1 2 
HETATM 4094 H  H28  . A1AG4 F 3 .   ? 22.524 -12.925 3.852   0   65.44  ? 402 A1AG4 B H28  1 2 
HETATM 4095 H  H24  . A1AG4 F 3 .   ? 31.028 -11.253 4.454   0   47.39  ? 402 A1AG4 B H24  1 2 
HETATM 4096 H  H26  . A1AG4 F 3 .   ? 28.908 -11.047 3.5     0   53.21  ? 402 A1AG4 B H26  1 2 
HETATM 4097 H  H29  . A1AG4 F 3 .   ? 23.953 -11.016 4.532   0   64.44  ? 402 A1AG4 B H29  1 2 
HETATM 4098 O  O    . HOH   G 4 .   ? 37.306 -45.308 1.971   1   34.29  ? 501 HOH   A O    1 ? 
HETATM 4099 O  O    . HOH   G 4 .   ? 24.354 -28.583 4.066   1   29.05  ? 502 HOH   A O    1 ? 
HETATM 4100 O  O    . HOH   G 4 .   ? 36.415 -42.542 14.448  1   34.41  ? 503 HOH   A O    1 ? 
HETATM 4101 O  O    . HOH   G 4 .   ? 36.224 -47.767 1.591   1   23.25  ? 504 HOH   A O    1 ? 
HETATM 4102 O  O    . HOH   G 4 .   ? 38.913 -36.147 -4.291  1   15.35  ? 505 HOH   A O    1 ? 
HETATM 4103 O  O    . HOH   G 4 .   ? 27.95  -49.137 2.255   1   32.38  ? 506 HOH   A O    1 ? 
HETATM 4104 O  O    . HOH   G 4 .   ? 44.285 -41.635 -20.186 1   37.04  ? 507 HOH   A O    1 ? 
HETATM 4105 O  O    . HOH   G 4 .   ? 34.2   -44.874 -4.952  1   24.34  ? 508 HOH   A O    1 ? 
HETATM 4106 O  O    . HOH   G 4 .   ? 31.507 -29.169 -7.183  1   23.76  ? 509 HOH   A O    1 ? 
HETATM 4107 O  O    . HOH   G 4 .   ? 51.447 -40.678 -8.688  1   35.93  ? 510 HOH   A O    1 ? 
HETATM 4108 O  O    . HOH   G 4 .   ? 33.687 -35.897 0.434   1   31.24  ? 511 HOH   A O    1 ? 
HETATM 4109 O  O    . HOH   G 4 .   ? 41.94  -27.862 -18.487 1   33.49  ? 512 HOH   A O    1 ? 
HETATM 4110 O  O    . HOH   G 4 .   ? 46.158 -32.098 -15.667 1   26     ? 513 HOH   A O    1 ? 
HETATM 4111 O  O    . HOH   G 4 .   ? 45.744 -32     8.417   1   30.69  ? 514 HOH   A O    1 ? 
HETATM 4112 O  O    . HOH   G 4 .   ? 44.264 -53.139 -18.788 1   24.91  ? 515 HOH   A O    1 ? 
HETATM 4113 O  O    . HOH   G 4 .   ? 33.728 -50.986 0.104   1   29.99  ? 516 HOH   A O    1 ? 
HETATM 4114 O  O    . HOH   G 4 .   ? 34.757 -36.961 -1.983  1   26.19  ? 517 HOH   A O    1 ? 
HETATM 4115 O  O    . HOH   G 4 .   ? 41.823 -44.014 3.251   1   26.3   ? 518 HOH   A O    1 ? 
HETATM 4116 O  O    . HOH   G 4 .   ? 32.505 -41.53  13.844  1   26.11  ? 519 HOH   A O    1 ? 
HETATM 4117 O  O    . HOH   G 4 .   ? 39.029 -50.156 -3.175  1   30.96  ? 520 HOH   A O    1 ? 
HETATM 4118 O  O    . HOH   G 4 .   ? 35.15  -31.15  -4.858  1   21.81  ? 521 HOH   A O    1 ? 
HETATM 4119 O  O    . HOH   G 4 .   ? 39.043 -42.667 -24.484 1   30.34  ? 522 HOH   A O    1 ? 
HETATM 4120 O  O    . HOH   G 4 .   ? 27.466 -43.352 -19.93  1   31.54  ? 523 HOH   A O    1 ? 
HETATM 4121 O  O    . HOH   G 4 .   ? 43.622 -29.189 -15.449 1   21.39  ? 524 HOH   A O    1 ? 
HETATM 4122 O  O    . HOH   G 4 .   ? 29.186 -39.609 22.785  1   37.93  ? 525 HOH   A O    1 ? 
HETATM 4123 O  O    . HOH   G 4 .   ? 44.613 -47.295 -22.429 1   35.19  ? 526 HOH   A O    1 ? 
HETATM 4124 O  O    . HOH   G 4 .   ? 38.624 -19.137 -8.491  1   32.89  ? 527 HOH   A O    1 ? 
HETATM 4125 O  O    . HOH   G 4 .   ? 42.253 -40.5   20.083  1   23.5   ? 528 HOH   A O    1 ? 
HETATM 4126 O  O    . HOH   G 4 .   ? 46.329 -29.414 -15.385 1   19.5   ? 529 HOH   A O    1 ? 
HETATM 4127 O  O    . HOH   G 4 .   ? 45.091 -39.747 -22.844 1   24.22  ? 530 HOH   A O    1 ? 
HETATM 4128 O  O    . HOH   G 4 .   ? 26.66  -52.853 -8.792  1   42.44  ? 531 HOH   A O    1 ? 
HETATM 4129 O  O    . HOH   G 4 .   ? 35.027 -47.441 4.832   1   19.56  ? 532 HOH   A O    1 ? 
HETATM 4130 O  O    . HOH   G 4 .   ? 37.479 -46.319 5.358   1   23.11  ? 533 HOH   A O    1 ? 
HETATM 4131 O  O    . HOH   G 4 .   ? 32.049 -51.993 -6.98   1   28.69  ? 534 HOH   A O    1 ? 
HETATM 4132 O  O    . HOH   G 4 .   ? 48.229 -34.668 4.653   1   34.73  ? 535 HOH   A O    1 ? 
HETATM 4133 O  O    . HOH   G 4 .   ? 32.278 -54.107 -9.209  1   28.91  ? 536 HOH   A O    1 ? 
HETATM 4134 O  O    . HOH   G 4 .   ? 39.421 -27.951 -22.883 1   21.68  ? 537 HOH   A O    1 ? 
HETATM 4135 O  O    . HOH   H 4 .   ? 32.615 -30.675 31.23   1   21.32  ? 501 HOH   B O    1 ? 
HETATM 4136 O  O    . HOH   H 4 .   ? 26.312 -27.075 18.963  1   21.56  ? 502 HOH   B O    1 ? 
HETATM 4137 O  O    . HOH   H 4 .   ? 42.858 -28.792 15.135  1   21.66  ? 503 HOH   B O    1 ? 
HETATM 4138 O  O    . HOH   H 4 .   ? 43.23  -17.388 2.028   1   24     ? 504 HOH   B O    1 ? 
HETATM 4139 O  O    . HOH   H 4 .   ? 34.067 -21.162 16.158  1   21.43  ? 505 HOH   B O    1 ? 
HETATM 4140 O  O    . HOH   H 4 .   ? 30.927 -26.584 18.537  1   28.59  ? 506 HOH   B O    1 ? 
HETATM 4141 O  O    . HOH   H 4 .   ? 35.857 -19.089 37.016  1   45.72  ? 507 HOH   B O    1 ? 
HETATM 4142 O  O    . HOH   H 4 .   ? 39.617 -17.499 1.206   1   22.32  ? 508 HOH   B O    1 ? 
HETATM 4143 O  O    . HOH   H 4 .   ? 34.185 -7.747  10.782  1   44.34  ? 509 HOH   B O    1 ? 
HETATM 4144 O  O    . HOH   H 4 .   ? 35.096 -13.517 19.306  1   30.01  ? 510 HOH   B O    1 ? 
HETATM 4145 O  O    . HOH   H 4 .   ? 30.626 -3.778  16.775  1   45.12  ? 511 HOH   B O    1 ? 
HETATM 4146 O  O    . HOH   H 4 .   ? 36.409 -23.299 19.977  1   27.95  ? 512 HOH   B O    1 ? 
HETATM 4147 O  O    . HOH   H 4 .   ? 45.489 -30.852 10.449  1   44.27  ? 513 HOH   B O    1 ? 
HETATM 4148 O  O    . HOH   H 4 .   ? 38.01  -18.337 3.315   1   29.96  ? 514 HOH   B O    1 ? 
HETATM 4149 O  O    . HOH   H 4 .   ? 29.111 -31.046 33.822  1   47.67  ? 515 HOH   B O    1 ? 
HETATM 4150 O  O    . HOH   H 4 .   ? 18.718 -27.316 22.551  1   34.14  ? 516 HOH   B O    1 ? 
HETATM 4151 O  O    . HOH   H 4 .   ? 30.32  -3.173  20.439  1   36.9   ? 517 HOH   B O    1 ? 
HETATM 4152 O  O    . HOH   H 4 .   ? 47.236 -29.093 15.335  1   34.5   ? 518 HOH   B O    1 ? 
HETATM 4153 O  O    . HOH   H 4 .   ? 35.604 -20.571 39.571  1   28.15  ? 519 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    . ILE   A 15  ? 1.0142 2.3825 1.4969 -0.3301 -0.0026 -0.0348 14  ILE   A N    
2    C  CA   . ILE   A 15  ? 0.9757 2.4426 1.4993 -0.3649 -0.0192 -0.0464 14  ILE   A CA   
3    C  C    . ILE   A 15  ? 0.9333 2.495  1.5003 -0.3125 -0.0414 -0.0516 14  ILE   A C    
4    O  O    . ILE   A 15  ? 0.9233 2.5112 1.4964 -0.3175 -0.0688 -0.0587 14  ILE   A O    
5    C  CB   . ILE   A 15  ? 0.9457 2.4909 1.5032 -0.4228 0.0021  -0.051  14  ILE   A CB   
6    C  CG1  . ILE   A 15  ? 1.0055 2.4518 1.5152 -0.4618 0.0293  -0.0425 14  ILE   A CG1  
7    C  CG2  . ILE   A 15  ? 0.9185 2.5368 1.5032 -0.4741 -0.0167 -0.0635 14  ILE   A CG2  
8    C  CD1  . ILE   A 15  ? 0.9864 2.5021 1.5235 -0.5142 0.0553  -0.0446 14  ILE   A CD1  
9    N  N    . ILE   A 16  ? 0.9077 2.5168 1.5003 -0.2607 -0.0299 -0.0482 15  ILE   A N    
10   C  CA   . ILE   A 16  ? 0.8722 2.563  1.5    -0.2017 -0.0488 -0.0518 15  ILE   A CA   
11   C  C    . ILE   A 16  ? 0.9223 2.5148 1.5021 -0.1546 -0.0683 -0.0455 15  ILE   A C    
12   O  O    . ILE   A 16  ? 0.9087 2.5379 1.4982 -0.1265 -0.0951 -0.0492 15  ILE   A O    
13   C  CB   . ILE   A 16  ? 0.8395 2.6085 1.5056 -0.1593 -0.0287 -0.051  15  ILE   A CB   
14   C  CG1  . ILE   A 16  ? 0.8239 2.647  1.5174 -0.2067 0.0025  -0.0529 15  ILE   A CG1  
15   C  CG2  . ILE   A 16  ? 0.7885 2.6759 1.5041 -0.1122 -0.0495 -0.0581 15  ILE   A CG2  
16   C  CD1  . ILE   A 16  ? 0.8778 2.6163 1.5345 -0.1968 0.033   -0.043  15  ILE   A CD1  
17   N  N    . TYR   A 17  ? 0.9774 2.447  1.5046 -0.1467 -0.0545 -0.0359 16  TYR   A N    
18   C  CA   . TYR   A 17  ? 1.0299 2.3969 1.5075 -0.1091 -0.0678 -0.0293 16  TYR   A CA   
19   C  C    . TYR   A 17  ? 1.0568 2.3637 1.5023 -0.1453 -0.0861 -0.0316 16  TYR   A C    
20   O  O    . TYR   A 17  ? 1.0758 2.3483 1.4984 -0.1178 -0.1072 -0.0306 16  TYR   A O    
21   C  CB   . TYR   A 17  ? 1.0791 2.348  1.5174 -0.0954 -0.0448 -0.0199 16  TYR   A CB   
22   C  CG   . TYR   A 17  ? 1.1442 2.3089 1.5328 -0.0579 -0.0537 -0.0129 16  TYR   A CG   
23   C  CD1  . TYR   A 17  ? 1.202  2.2701 1.5463 -0.0825 -0.0588 -0.0102 16  TYR   A CD1  
24   C  CD2  . TYR   A 17  ? 1.1613 2.3191 1.5439 0.0008  -0.0537 -0.009  16  TYR   A CD2  
25   C  CE1  . TYR   A 17  ? 1.2573 2.2346 1.5581 -0.0515 -0.0641 -0.004  16  TYR   A CE1  
26   C  CE2  . TYR   A 17  ? 1.221  2.28   1.5557 0.0297  -0.0589 -0.0024 16  TYR   A CE2  
27   C  CZ   . TYR   A 17  ? 1.2721 2.2452 1.5684 0.0024  -0.0639 0.0001  16  TYR   A CZ   
28   O  OH   . TYR   A 17  ? 1.335  2.2183 1.587  0.0284  -0.0681 0.006   16  TYR   A OH   
29   N  N    . SER   A 18  ? 1.06   2.3489 1.4988 -0.2064 -0.0771 -0.0346 17  SER   A N    
30   C  CA   . SER   A 18  ? 1.0936 2.3201 1.4975 -0.2452 -0.0915 -0.038  17  SER   A CA   
31   C  C    . SER   A 18  ? 1.063  2.3567 1.487  -0.2469 -0.1219 -0.0474 17  SER   A C    
32   O  O    . SER   A 18  ? 1.0977 2.3305 1.4853 -0.2441 -0.1401 -0.0481 17  SER   A O    
33   C  CB   . SER   A 18  ? 1.1189 2.3261 1.5149 -0.3106 -0.0748 -0.0403 17  SER   A CB   
34   O  OG   . SER   A 18  ? 1.1608 2.3337 1.5481 -0.3115 -0.0462 -0.0324 17  SER   A OG   
35   N  N    . TYR   A 19  ? 0.9942 2.4161 1.476  -0.2515 -0.1273 -0.055  18  TYR   A N    
36   C  CA   . TYR   A 19  ? 0.9575 2.4589 1.4641 -0.2522 -0.1578 -0.0647 18  TYR   A CA   
37   C  C    . TYR   A 19  ? 0.9349 2.467  1.4493 -0.1809 -0.1765 -0.0615 18  TYR   A C    
38   O  O    . TYR   A 19  ? 0.9269 2.4916 1.4427 -0.1718 -0.2053 -0.0669 18  TYR   A O    
39   C  CB   . TYR   A 19  ? 0.8977 2.5296 1.4647 -0.2945 -0.1561 -0.0755 18  TYR   A CB   
40   C  CG   . TYR   A 19  ? 0.8865 2.5808 1.4685 -0.3246 -0.1864 -0.0881 18  TYR   A CG   
41   C  CD1  . TYR   A 19  ? 0.939  2.5569 1.4771 -0.374  -0.1957 -0.0928 18  TYR   A CD1  
42   C  CD2  . TYR   A 19  ? 0.8355 2.6685 1.4757 -0.3052 -0.2056 -0.0962 18  TYR   A CD2  
43   C  CE1  . TYR   A 19  ? 0.9294 2.6033 1.4783 -0.405  -0.224  -0.1057 18  TYR   A CE1  
44   C  CE2  . TYR   A 19  ? 0.8219 2.7185 1.4771 -0.3356 -0.2349 -0.1088 18  TYR   A CE2  
45   C  CZ   . TYR   A 19  ? 0.875  2.6899 1.4833 -0.3868 -0.2442 -0.1137 18  TYR   A CZ   
46   O  OH   . TYR   A 19  ? 0.8687 2.7439 1.4882 -0.418  -0.2742 -0.1272 18  TYR   A OH   
47   N  N    . LEU   A 20  ? 0.9257 2.4436 1.4407 -0.1305 -0.1608 -0.0528 19  LEU   A N    
48   C  CA   . LEU   A 20  ? 0.9143 2.4433 1.4269 -0.0602 -0.1749 -0.0482 19  LEU   A CA   
49   C  C    . LEU   A 20  ? 0.9683 2.3686 1.415  -0.0391 -0.1834 -0.0402 19  LEU   A C    
50   O  O    . LEU   A 20  ? 0.9756 2.3759 1.4076 -0.0057 -0.2077 -0.0396 19  LEU   A O    
51   C  CB   . LEU   A 20  ? 0.9003 2.4559 1.4336 -0.0189 -0.1522 -0.0431 19  LEU   A CB   
52   C  CG   . LEU   A 20  ? 0.9247 2.4709 1.4449 0.0565  -0.1618 -0.0372 19  LEU   A CG   
53   C  CD1  . LEU   A 20  ? 0.8675 2.5424 1.445  0.0921  -0.1616 -0.0423 19  LEU   A CD1  
54   C  CD2  . LEU   A 20  ? 0.9872 2.4189 1.4606 0.0814  -0.1413 -0.0268 19  LEU   A CD2  
55   N  N    . GLU   A 21  ? 1.0025 2.2956 1.409  -0.0593 -0.1636 -0.034  20  GLU   A N    
56   C  CA   . GLU   A 21  ? 1.0524 2.2263 1.3991 -0.0443 -0.1679 -0.0269 20  GLU   A CA   
57   C  C    . GLU   A 21  ? 1.0531 2.2022 1.3755 -0.0738 -0.1899 -0.0325 20  GLU   A C    
58   O  O    . GLU   A 21  ? 1.0819 2.1846 1.3699 -0.0454 -0.2058 -0.0291 20  GLU   A O    
59   C  CB   . GLU   A 21  ? 1.1251 2.2044 1.441  -0.0596 -0.1418 -0.0204 20  GLU   A CB   
60   C  CG   . GLU   A 21  ? 1.2497 2.2155 1.5089 -0.0434 -0.1447 -0.0137 20  GLU   A CG   
61   C  CD   . GLU   A 21  ? 1.3766 2.2531 1.6045 -0.0724 -0.1253 -0.0102 20  GLU   A CD   
62   O  OE1  . GLU   A 21  ? 1.4099 2.2535 1.6319 -0.0557 -0.1063 -0.004  20  GLU   A OE1  
63   O  OE2  . GLU   A 21  ? 1.4226 2.261  1.6298 -0.1104 -0.1297 -0.0141 20  GLU   A OE2  
64   N  N    . ALA   A 22  ? 1.0203 2.1978 1.3569 -0.1309 -0.1905 -0.0413 21  ALA   A N    
65   C  CA   . ALA   A 22  ? 1.0222 2.178  1.334  -0.1615 -0.2118 -0.0486 21  ALA   A CA   
66   C  C    . ALA   A 22  ? 0.9727 2.2028 1.3005 -0.1336 -0.2431 -0.0534 21  ALA   A C    
67   O  O    . ALA   A 22  ? 0.9983 2.1887 1.2905 -0.1351 -0.2629 -0.0558 21  ALA   A O    
68   C  CB   . ALA   A 22  ? 1.0123 2.191  1.3375 -0.2287 -0.2062 -0.0581 21  ALA   A CB   
69   N  N    . LEU   A 23  ? 0.9002 2.2377 1.2794 -0.1055 -0.247  -0.0546 22  LEU   A N    
70   C  CA   . LEU   A 23  ? 0.8512 2.273  1.2521 -0.0699 -0.2761 -0.0583 22  LEU   A CA   
71   C  C    . LEU   A 23  ? 0.8701 2.2257 1.2294 -0.0051 -0.2832 -0.0469 22  LEU   A C    
72   O  O    . LEU   A 23  ? 0.8765 2.2318 1.2138 0.0164  -0.3096 -0.0474 22  LEU   A O    
73   C  CB   . LEU   A 23  ? 0.7828 2.3395 1.2541 -0.0604 -0.2722 -0.0631 22  LEU   A CB   
74   C  CG   . LEU   A 23  ? 0.754  2.4075 1.2547 -0.008  -0.2978 -0.065  22  LEU   A CG   
75   C  CD1  . LEU   A 23  ? 0.7353 2.4486 1.2442 -0.0332 -0.3312 -0.0761 22  LEU   A CD1  
76   C  CD2  . LEU   A 23  ? 0.7    2.469  1.2656 0.0106  -0.2847 -0.0677 22  LEU   A CD2  
77   N  N    . VAL   A 24  ? 0.8781 2.1723 1.2221 0.0231  -0.2593 -0.0367 23  VAL   A N    
78   C  CA   . VAL   A 24  ? 0.9088 2.1262 1.2081 0.078   -0.2606 -0.0255 23  VAL   A CA   
79   C  C    . VAL   A 24  ? 0.9562 2.0586 1.1926 0.0635  -0.2645 -0.0217 23  VAL   A C    
80   O  O    . VAL   A 24  ? 0.9887 2.0431 1.1852 0.1008  -0.2767 -0.015  23  VAL   A O    
81   C  CB   . VAL   A 24  ? 0.9232 2.1139 1.2265 0.1058  -0.2331 -0.0178 23  VAL   A CB   
82   C  CG1  . VAL   A 24  ? 0.9844 2.0643 1.2297 0.1444  -0.2283 -0.0065 23  VAL   A CG1  
83   C  CG2  . VAL   A 24  ? 0.8767 2.1769 1.2313 0.1413  -0.2342 -0.0204 23  VAL   A CG2  
84   N  N    . LYS   A 25  ? 0.957  2.0167 1.1824 0.0099  -0.2546 -0.0263 24  LYS   A N    
85   C  CA   . LYS   A 25  ? 0.9993 1.9562 1.168  -0.0046 -0.2563 -0.0243 24  LYS   A CA   
86   C  C    . LYS   A 25  ? 0.99   1.9602 1.139  -0.0128 -0.2855 -0.0308 24  LYS   A C    
87   O  O    . LYS   A 25  ? 1.0375 1.9257 1.1356 -0.0151 -0.2888 -0.0286 24  LYS   A O    
88   C  CB   . LYS   A 25  ? 1.0416 1.943  1.2013 -0.0531 -0.2348 -0.0267 24  LYS   A CB   
89   C  CG   . LYS   A 25  ? 1.1431 1.9277 1.2499 -0.0463 -0.2216 -0.0193 24  LYS   A CG   
90   C  CD   . LYS   A 25  ? 1.206  1.9438 1.3112 -0.0776 -0.1962 -0.0187 24  LYS   A CD   
91   C  CE   . LYS   A 25  ? 1.2259 1.993  1.3627 -0.0612 -0.1774 -0.0134 24  LYS   A CE   
92   N  NZ   . LYS   A 25  ? 1.2751 1.9837 1.4007 -0.0852 -0.1535 -0.0109 24  LYS   A NZ   
93   N  N    . VAL   A 26  ? 0.9267 2.0019 1.1153 -0.0167 -0.3067 -0.0391 25  VAL   A N    
94   C  CA   . VAL   A 26  ? 0.9165 2.0133 1.0877 -0.0237 -0.3372 -0.0463 25  VAL   A CA   
95   C  C    . VAL   A 26  ? 0.8931 2.025  1.0593 0.0362  -0.3593 -0.0401 25  VAL   A C    
96   O  O    . VAL   A 26  ? 0.9272 2.0079 1.0442 0.0539  -0.3756 -0.0368 25  VAL   A O    
97   C  CB   . VAL   A 26  ? 0.8799 2.0677 1.0936 -0.0752 -0.3491 -0.0614 25  VAL   A CB   
98   C  CG1  . VAL   A 26  ? 0.884  2.0986 1.0792 -0.0821 -0.3832 -0.07   25  VAL   A CG1  
99   C  CG2  . VAL   A 26  ? 0.9055 2.0418 1.1122 -0.1336 -0.3271 -0.0664 25  VAL   A CG2  
100  N  N    . PHE   A 27  ? 0.8346 2.0512 1.0482 0.0691  -0.3588 -0.0384 26  PHE   A N    
101  C  CA   . PHE   A 27  ? 0.8122 2.0662 1.0231 0.132   -0.3787 -0.0323 26  PHE   A CA   
102  C  C    . PHE   A 27  ? 0.8414 1.9832 0.9951 0.1756  -0.3661 -0.0172 26  PHE   A C    
103  O  O    . PHE   A 27  ? 0.8707 1.9799 0.9819 0.2134  -0.3844 -0.0106 26  PHE   A O    
104  C  CB   . PHE   A 27  ? 0.7558 2.1285 1.0342 0.1546  -0.3768 -0.0354 26  PHE   A CB   
105  C  CG   . PHE   A 27  ? 0.7406 2.1959 1.0333 0.2084  -0.4063 -0.0353 26  PHE   A CG   
106  C  CD1  . PHE   A 27  ? 0.7334 2.2494 1.03   0.1979  -0.4399 -0.0438 26  PHE   A CD1  
107  C  CD2  . PHE   A 27  ? 0.7448 2.2227 1.0485 0.2697  -0.401  -0.0277 26  PHE   A CD2  
108  C  CE1  . PHE   A 27  ? 0.7108 2.3098 1.0222 0.2501  -0.469  -0.0438 26  PHE   A CE1  
109  C  CE2  . PHE   A 27  ? 0.7245 2.2814 1.0412 0.3234  -0.4289 -0.0277 26  PHE   A CE2  
110  C  CZ   . PHE   A 27  ? 0.6983 2.3173 1.0198 0.314   -0.4633 -0.0354 26  PHE   A CZ   
111  N  N    . PHE   A 28  ? 0.834  1.9144 0.9836 0.1678  -0.3351 -0.0119 27  PHE   A N    
112  C  CA   . PHE   A 28  ? 0.8657 1.8394 0.9629 0.2011  -0.3207 0.001   27  PHE   A CA   
113  C  C    . PHE   A 28  ? 0.8628 1.7387 0.9281 0.1606  -0.2992 0.0022  27  PHE   A C    
114  O  O    . PHE   A 28  ? 0.8702 1.7185 0.9464 0.1512  -0.2737 0.0045  27  PHE   A O    
115  C  CB   . PHE   A 28  ? 0.8618 1.8535 0.9814 0.2403  -0.3039 0.0067  27  PHE   A CB   
116  C  CG   . PHE   A 28  ? 0.8713 1.8978 0.9846 0.3032  -0.3225 0.0119  27  PHE   A CG   
117  C  CD1  . PHE   A 28  ? 0.8348 1.9726 0.9864 0.3162  -0.3487 0.0048  27  PHE   A CD1  
118  C  CD2  . PHE   A 28  ? 0.927  1.8749 0.9945 0.3498  -0.3143 0.0237  27  PHE   A CD2  
119  C  CE1  . PHE   A 28  ? 0.8386 2.0075 0.9817 0.3791  -0.3672 0.0099  27  PHE   A CE1  
120  C  CE2  . PHE   A 28  ? 0.9349 1.9062 0.9896 0.4106  -0.3316 0.029   27  PHE   A CE2  
121  C  CZ   . PHE   A 28  ? 0.8836 1.9654 0.9759 0.4273  -0.3583 0.0224  27  PHE   A CZ   
122  N  N    . PRO   A 29  ? 0.8491 1.6744 0.8749 0.1369  -0.3091 0       28  PRO   A N    
123  C  CA   . PRO   A 29  ? 0.8524 1.5897 0.8494 0.1021  -0.2884 0.0004  28  PRO   A CA   
124  C  C    . PRO   A 29  ? 0.8543 1.4939 0.8035 0.1296  -0.2729 0.0125  28  PRO   A C    
125  O  O    . PRO   A 29  ? 0.8737 1.4926 0.7922 0.1701  -0.2831 0.0205  28  PRO   A O    
126  C  CB   . PRO   A 29  ? 0.8783 1.6051 0.8509 0.0698  -0.3057 -0.0079 28  PRO   A CB   
127  C  CG   . PRO   A 29  ? 0.8656 1.668  0.8479 0.0911  -0.3373 -0.0111 28  PRO   A CG   
128  C  CD   . PRO   A 29  ? 0.8359 1.6805 0.8389 0.1427  -0.3392 -0.0031 28  PRO   A CD   
129  N  N    . ARG   A 30  ? 0.8321 1.4121 0.7739 0.1075  -0.2484 0.0138  29  ARG   A N    
130  C  CA   . ARG   A 30  ? 0.8364 1.3273 0.736  0.1259  -0.2323 0.0236  29  ARG   A CA   
131  C  C    . ARG   A 30  ? 0.8328 1.2566 0.6844 0.108   -0.2343 0.0231  29  ARG   A C    
132  O  O    . ARG   A 30  ? 0.8237 1.251  0.6799 0.0713  -0.2355 0.0143  29  ARG   A O    
133  C  CB   . ARG   A 30  ? 0.8443 1.3125 0.7628 0.1119  -0.2058 0.0245  29  ARG   A CB   
134  C  CG   . ARG   A 30  ? 0.8652 1.3288 0.7887 0.1477  -0.1951 0.032   29  ARG   A CG   
135  C  CD   . ARG   A 30  ? 0.8929 1.3451 0.8386 0.1287  -0.1714 0.0309  29  ARG   A CD   
136  N  NE   . ARG   A 30  ? 0.9473 1.3238 0.861  0.1424  -0.1549 0.0381  29  ARG   A NE   
137  C  CZ   . ARG   A 30  ? 0.9618 1.3342 0.8817 0.1649  -0.1432 0.0419  29  ARG   A CZ   
138  N  NH1  . ARG   A 30  ? 0.9207 1.3613 0.8785 0.179   -0.1445 0.0394  29  ARG   A NH1  
139  N  NH2  . ARG   A 30  ? 0.9935 1.2951 0.8814 0.1728  -0.1296 0.0473  29  ARG   A NH2  
140  N  N    . LYS   A 31  ? 0.8392 1.1997 0.6418 0.1333  -0.2336 0.0322  30  LYS   A N    
141  C  CA   . LYS   A 31  ? 0.8498 1.1474 0.604  0.1194  -0.2334 0.0322  30  LYS   A CA   
142  C  C    . LYS   A 31  ? 0.8219 1.0674 0.5713 0.0898  -0.2098 0.0296  30  LYS   A C    
143  O  O    . LYS   A 31  ? 0.8269 1.0489 0.5859 0.0936  -0.1906 0.0339  30  LYS   A O    
144  C  CB   . LYS   A 31  ? 0.9233 1.1683 0.6237 0.1529  -0.2381 0.0434  30  LYS   A CB   
145  C  CG   . LYS   A 31  ? 1.0159 1.2176 0.6671 0.1405  -0.245  0.042   30  LYS   A CG   
146  C  CD   . LYS   A 31  ? 1.1169 1.2328 0.7215 0.1405  -0.2245 0.0496  30  LYS   A CD   
147  C  CE   . LYS   A 31  ? 1.1899 1.2645 0.7378 0.1703  -0.234  0.0605  30  LYS   A CE   
148  N  NZ   . LYS   A 31  ? 1.2286 1.2957 0.7391 0.1622  -0.2501 0.0569  30  LYS   A NZ   
149  N  N    . ARG   A 32  ? 0.7875 1.0171 0.5218 0.061   -0.2122 0.0216  31  ARG   A N    
150  C  CA   . ARG   A 32  ? 0.7663 0.9492 0.4935 0.0352  -0.1921 0.0178  31  ARG   A CA   
151  C  C    . ARG   A 32  ? 0.7547 0.8681 0.4316 0.0422  -0.1825 0.0228  31  ARG   A C    
152  O  O    . ARG   A 32  ? 0.778  0.8767 0.4183 0.0467  -0.1947 0.0226  31  ARG   A O    
153  C  CB   . ARG   A 32  ? 0.776  0.9757 0.511  0.0005  -0.1987 0.0052  31  ARG   A CB   
154  C  CG   . ARG   A 32  ? 0.788  1.0582 0.5716 -0.0149 -0.2072 -0.001  31  ARG   A CG   
155  C  CD   . ARG   A 32  ? 0.847  1.1062 0.6485 -0.0468 -0.1917 -0.0072 31  ARG   A CD   
156  N  NE   . ARG   A 32  ? 0.9263 1.137  0.6934 -0.0702 -0.19   -0.0152 31  ARG   A NE   
157  C  CZ   . ARG   A 32  ? 0.9697 1.1564 0.7385 -0.0971 -0.1783 -0.0214 31  ARG   A CZ   
158  N  NH1  . ARG   A 32  ? 0.9375 1.1444 0.7405 -0.1063 -0.1673 -0.0199 31  ARG   A NH1  
159  N  NH2  . ARG   A 32  ? 1.0087 1.1471 0.741  -0.1132 -0.1769 -0.029  31  ARG   A NH2  
160  N  N    . LYS   A 33  ? 0.7195 0.7924 0.3939 0.042   -0.1604 0.027   32  LYS   A N    
161  C  CA   . LYS   A 33  ? 0.7079 0.7199 0.3391 0.0443  -0.1477 0.031   32  LYS   A CA   
162  C  C    . LYS   A 33  ? 0.6898 0.6788 0.3125 0.0185  -0.1381 0.0215  32  LYS   A C    
163  O  O    . LYS   A 33  ? 0.6728 0.6848 0.3219 -0.0005 -0.1397 0.0131  32  LYS   A O    
164  C  CB   . LYS   A 33  ? 0.705  0.6885 0.3381 0.0559  -0.1291 0.0393  32  LYS   A CB   
165  C  CG   . LYS   A 33  ? 0.6875 0.6737 0.3539 0.04    -0.1124 0.0352  32  LYS   A CG   
166  C  CD   . LYS   A 33  ? 0.6938 0.6624 0.3654 0.0526  -0.0989 0.0426  32  LYS   A CD   
167  C  CE   . LYS   A 33  ? 0.6963 0.6618 0.3934 0.0381  -0.0826 0.0389  32  LYS   A CE   
168  N  NZ   . LYS   A 33  ? 0.6995 0.6468 0.3979 0.0489  -0.0709 0.0451  32  LYS   A NZ   
169  N  N    . SER   A 34  ? 0.6925 0.634  0.2764 0.0183  -0.1268 0.0229  33  SER   A N    
170  C  CA   . SER   A 34  ? 0.6843 0.6014 0.2581 -0.0007 -0.1152 0.0139  33  SER   A CA   
171  C  C    . SER   A 34  ? 0.6737 0.57   0.2608 -0.0022 -0.0919 0.0161  33  SER   A C    
172  O  O    . SER   A 34  ? 0.6843 0.5678 0.2684 0.0097  -0.0828 0.0249  33  SER   A O    
173  C  CB   . SER   A 34  ? 0.7089 0.5935 0.2323 -0.001  -0.1171 0.0117  33  SER   A CB   
174  O  OG   . SER   A 34  ? 0.7274 0.5903 0.2397 -0.017  -0.1067 0.0013  33  SER   A OG   
175  N  N    . VAL   A 35  ? 0.6478 0.541  0.2493 -0.0166 -0.0833 0.0078  34  VAL   A N    
176  C  CA   . VAL   A 35  ? 0.6305 0.5073 0.2433 -0.0175 -0.0628 0.0083  34  VAL   A CA   
177  C  C    . VAL   A 35  ? 0.6368 0.4843 0.2242 -0.0244 -0.0511 0.0001  34  VAL   A C    
178  O  O    . VAL   A 35  ? 0.6412 0.4806 0.2398 -0.0252 -0.0356 -0.002  34  VAL   A O    
179  C  CB   . VAL   A 35  ? 0.6172 0.5152 0.2708 -0.0222 -0.06   0.0075  34  VAL   A CB   
180  C  CG1  . VAL   A 35  ? 0.6029 0.5268 0.2796 -0.0118 -0.066  0.0158  34  VAL   A CG1  
181  C  CG2  . VAL   A 35  ? 0.6236 0.5309 0.2846 -0.0377 -0.0686 -0.0013 34  VAL   A CG2  
182  N  N    . ALA   A 36  ? 0.6369 0.4701 0.1889 -0.0274 -0.0588 -0.0049 35  ALA   A N    
183  C  CA   . ALA   A 36  ? 0.6502 0.4547 0.1721 -0.0313 -0.0482 -0.0134 35  ALA   A CA   
184  C  C    . ALA   A 36  ? 0.6567 0.446  0.1682 -0.024  -0.0277 -0.0086 35  ALA   A C    
185  O  O    . ALA   A 36  ? 0.6617 0.4472 0.1595 -0.0179 -0.0273 0.0006  35  ALA   A O    
186  C  CB   . ALA   A 36  ? 0.6624 0.4554 0.1443 -0.0343 -0.0622 -0.0178 35  ALA   A CB   
187  N  N    . GLY   A 37  ? 0.6543 0.4358 0.1718 -0.0246 -0.0109 -0.0147 36  GLY   A N    
188  C  CA   . GLY   A 37  ? 0.6741 0.4491 0.1852 -0.0206 0.0098  -0.0121 36  GLY   A CA   
189  C  C    . GLY   A 37  ? 0.6833 0.4756 0.2284 -0.0189 0.0179  -0.0044 36  GLY   A C    
190  O  O    . GLY   A 37  ? 0.7051 0.4972 0.2498 -0.0191 0.0356  -0.0033 36  GLY   A O    
191  N  N    . GLU   A 38  ? 0.6595 0.4682 0.2331 -0.0184 0.0056  0.0003  37  GLU   A N    
192  C  CA   . GLU   A 38  ? 0.6434 0.4663 0.2476 -0.0168 0.0119  0.0063  37  GLU   A CA   
193  C  C    . GLU   A 38  ? 0.6132 0.4459 0.2421 -0.0171 0.023   -0.0003 37  GLU   A C    
194  O  O    . GLU   A 38  ? 0.6273 0.4563 0.2557 -0.0172 0.02    -0.0081 37  GLU   A O    
195  C  CB   . GLU   A 38  ? 0.6618 0.5012 0.289  -0.0145 -0.0036 0.0114  37  GLU   A CB   
196  C  CG   . GLU   A 38  ? 0.7738 0.6111 0.3822 -0.0093 -0.0179 0.0179  37  GLU   A CG   
197  C  CD   . GLU   A 38  ? 0.9119 0.7333 0.5014 -0.0028 -0.0133 0.0277  37  GLU   A CD   
198  O  OE1  . GLU   A 38  ? 0.9455 0.7558 0.533  -0.0068 0.0033  0.0291  37  GLU   A OE1  
199  O  OE2  . GLU   A 38  ? 0.9639 0.7835 0.5389 0.0062  -0.0266 0.0339  37  GLU   A OE2  
200  N  N    . ILE   A 39  ? 0.574  0.4177 0.2224 -0.0171 0.0345  0.0024  38  ILE   A N    
201  C  CA   . ILE   A 39  ? 0.5439 0.4016 0.2172 -0.0145 0.0424  -0.0035 38  ILE   A CA   
202  C  C    . ILE   A 39  ? 0.5212 0.3912 0.2233 -0.0137 0.0331  0       38  ILE   A C    
203  O  O    . ILE   A 39  ? 0.515  0.3925 0.2294 -0.0151 0.0337  0.0061  38  ILE   A O    
204  C  CB   . ILE   A 39  ? 0.5319 0.4018 0.2113 -0.016  0.0603  -0.005  38  ILE   A CB   
205  C  CG1  . ILE   A 39  ? 0.5334 0.3932 0.1832 -0.0168 0.0719  -0.0095 38  ILE   A CG1  
206  C  CG2  . ILE   A 39  ? 0.5212 0.4116 0.2303 -0.0096 0.0645  -0.0108 38  ILE   A CG2  
207  C  CD1  . ILE   A 39  ? 0.528  0.4053 0.184  -0.0211 0.0909  -0.0113 38  ILE   A CD1  
208  N  N    . VAL   A 40  ? 0.5102 0.3781 0.2182 -0.0126 0.0247  -0.0038 39  VAL   A N    
209  C  CA   . VAL   A 40  ? 0.48   0.3578 0.2107 -0.0135 0.0164  -0.0006 39  VAL   A CA   
210  C  C    . VAL   A 40  ? 0.4767 0.3603 0.2255 -0.0086 0.0221  -0.0034 39  VAL   A C    
211  O  O    . VAL   A 40  ? 0.4874 0.3596 0.2278 -0.0046 0.0245  -0.0098 39  VAL   A O    
212  C  CB   . VAL   A 40  ? 0.4647 0.3369 0.1882 -0.0195 0.0031  -0.002  39  VAL   A CB   
213  C  CG1  . VAL   A 40  ? 0.4529 0.3394 0.2    -0.0224 -0.0034 0.002   39  VAL   A CG1  
214  C  CG2  . VAL   A 40  ? 0.4665 0.3375 0.1717 -0.0217 -0.005  0.0006  39  VAL   A CG2  
215  N  N    . LEU   A 41  ? 0.466  0.3647 0.236  -0.0076 0.0235  0.001   40  LEU   A N    
216  C  CA   . LEU   A 41  ? 0.4615 0.3679 0.2481 -0.0018 0.0265  -0.0009 40  LEU   A CA   
217  C  C    . LEU   A 41  ? 0.4536 0.3589 0.2495 -0.004  0.0182  0.0027  40  LEU   A C    
218  O  O    . LEU   A 41  ? 0.4438 0.3585 0.2491 -0.0074 0.0145  0.0081  40  LEU   A O    
219  C  CB   . LEU   A 41  ? 0.4513 0.3766 0.2535 -0.0007 0.034   -0.0001 40  LEU   A CB   
220  C  CG   . LEU   A 41  ? 0.471  0.409  0.2883 0.008   0.0367  -0.0039 40  LEU   A CG   
221  C  CD1  . LEU   A 41  ? 0.482  0.4429 0.3095 0.008   0.0465  -0.0075 40  LEU   A CD1  
222  C  CD2  . LEU   A 41  ? 0.4691 0.4115 0.3001 0.0083  0.0303  0.0003  40  LEU   A CD2  
223  N  N    . ILE   A 42  ? 0.4557 0.3468 0.2457 -0.0017 0.0161  -0.0003 41  ILE   A N    
224  C  CA   . ILE   A 42  ? 0.4536 0.3407 0.2485 -0.0064 0.0103  0.0033  41  ILE   A CA   
225  C  C    . ILE   A 42  ? 0.4584 0.3418 0.2578 0.003   0.0128  0.0033  41  ILE   A C    
226  O  O    . ILE   A 42  ? 0.4664 0.3333 0.253  0.0122  0.0153  -0.0015 41  ILE   A O    
227  C  CB   . ILE   A 42  ? 0.4612 0.3282 0.2383 -0.0167 0.0045  0.001   41  ILE   A CB   
228  C  CG1  . ILE   A 42  ? 0.4671 0.3418 0.239  -0.0245 -0.0005 0.0006  41  ILE   A CG1  
229  C  CG2  . ILE   A 42  ? 0.457  0.3215 0.2388 -0.0255 0.0007  0.0051  41  ILE   A CG2  
230  C  CD1  . ILE   A 42  ? 0.4961 0.351  0.247  -0.035  -0.0062 -0.0045 41  ILE   A CD1  
231  N  N    . THR   A 43  ? 0.4481 0.3458 0.2631 0.0031  0.0119  0.0083  42  THR   A N    
232  C  CA   . THR   A 43  ? 0.4532 0.3482 0.2706 0.0122  0.0122  0.0092  42  THR   A CA   
233  C  C    . THR   A 43  ? 0.4903 0.3611 0.2934 0.0064  0.0089  0.0124  42  THR   A C    
234  O  O    . THR   A 43  ? 0.5044 0.3745 0.3064 -0.0076 0.0067  0.0148  42  THR   A O    
235  C  CB   . THR   A 43  ? 0.4332 0.3517 0.2688 0.014   0.0127  0.0119  42  THR   A CB   
236  O  OG1  . THR   A 43  ? 0.4333 0.3549 0.2732 0.0057  0.0104  0.0174  42  THR   A OG1  
237  C  CG2  . THR   A 43  ? 0.4216 0.3589 0.2669 0.0132  0.0168  0.0091  42  THR   A CG2  
238  N  N    . GLY   A 44  ? 0.5008 0.3525 0.2916 0.0166  0.0087  0.0127  43  GLY   A N    
239  C  CA   . GLY   A 44  ? 0.5237 0.3435 0.2932 0.0094  0.0071  0.0163  43  GLY   A CA   
240  C  C    . GLY   A 44  ? 0.5368 0.3285 0.2849 -0.0016 0.0064  0.0125  43  GLY   A C    
241  O  O    . GLY   A 44  ? 0.548  0.3209 0.2828 -0.0184 0.0053  0.0151  43  GLY   A O    
242  N  N    . ALA   A 45  ? 0.5352 0.3237 0.2779 0.0063  0.0076  0.0056  44  ALA   A N    
243  C  CA   . ALA   A 45  ? 0.5549 0.3157 0.2741 -0.0037 0.0065  0.0002  44  ALA   A CA   
244  C  C    . ALA   A 45  ? 0.6019 0.309  0.2833 0.0008  0.0067  -0.0023 44  ALA   A C    
245  O  O    . ALA   A 45  ? 0.6224 0.2995 0.2786 -0.0088 0.0055  -0.0079 44  ALA   A O    
246  C  CB   . ALA   A 45  ? 0.5393 0.3145 0.2626 0.0033  0.0088  -0.0061 44  ALA   A CB   
247  N  N    . GLY   A 46  ? 0.6105 0.3023 0.2841 0.0158  0.0075  0.0016  45  GLY   A N    
248  C  CA   . GLY   A 46  ? 0.6475 0.2819 0.2798 0.0256  0.0077  0.0005  45  GLY   A CA   
249  C  C    . GLY   A 46  ? 0.6778 0.2696 0.2813 0.0016  0.0065  0.0048  45  GLY   A C    
250  O  O    . GLY   A 46  ? 0.7292 0.2614 0.2894 0.0056  0.007   0.0035  45  GLY   A O    
251  N  N    . HIS   A 47  ? 0.6414 0.2619 0.2664 -0.0239 0.0057  0.0097  46  HIS   A N    
252  C  CA   . HIS   A 47  ? 0.6517 0.2425 0.2549 -0.0519 0.0061  0.0136  46  HIS   A CA   
253  C  C    . HIS   A 47  ? 0.6355 0.2787 0.2742 -0.0768 0.0051  0.0161  46  HIS   A C    
254  O  O    . HIS   A 47  ? 0.62   0.3144 0.2956 -0.0679 0.0043  0.0167  46  HIS   A O    
255  C  CB   . HIS   A 47  ? 0.6633 0.2235 0.2457 -0.0443 0.0087  0.0224  46  HIS   A CB   
256  C  CG   . HIS   A 47  ? 0.6942 0.2092 0.2422 -0.0728 0.0114  0.0269  46  HIS   A CG   
257  N  ND1  . HIS   A 47  ? 0.7488 0.1951 0.2468 -0.0808 0.0115  0.0227  46  HIS   A ND1  
258  C  CD2  . HIS   A 47  ? 0.7004 0.2284 0.2551 -0.0957 0.0153  0.0347  46  HIS   A CD2  
259  C  CE1  . HIS   A 47  ? 0.7727 0.1924 0.2491 -0.1112 0.0153  0.0284  46  HIS   A CE1  
260  N  NE2  . HIS   A 47  ? 0.7487 0.2189 0.2595 -0.1208 0.0182  0.0358  46  HIS   A NE2  
261  N  N    . GLY   A 48  ? 0.6382 0.2674 0.2636 -0.1074 0.0056  0.0172  47  GLY   A N    
262  C  CA   . GLY   A 48  ? 0.616  0.295  0.2725 -0.1314 0.0055  0.02    47  GLY   A CA   
263  C  C    . GLY   A 48  ? 0.603  0.3377 0.2959 -0.1298 0.0002  0.0157  47  GLY   A C    
264  O  O    . GLY   A 48  ? 0.6135 0.3405 0.2979 -0.1296 -0.0049 0.0081  47  GLY   A O    
265  N  N    . ILE   A 49  ? 0.5747 0.3628 0.3044 -0.1272 0.0013  0.0205  48  ILE   A N    
266  C  CA   . ILE   A 49  ? 0.5481 0.3868 0.3091 -0.1241 -0.004  0.0178  48  ILE   A CA   
267  C  C    . ILE   A 49  ? 0.5508 0.3837 0.3096 -0.1024 -0.007  0.0132  48  ILE   A C    
268  O  O    . ILE   A 49  ? 0.548  0.3924 0.3082 -0.1065 -0.0131 0.0081  48  ILE   A O    
269  C  CB   . ILE   A 49  ? 0.5318 0.4187 0.3257 -0.1193 -0.0009 0.0238  48  ILE   A CB   
270  C  CG1  . ILE   A 49  ? 0.5361 0.4361 0.3333 -0.1441 0.0036  0.0272  48  ILE   A CG1  
271  C  CG2  . ILE   A 49  ? 0.5203 0.452  0.3407 -0.111  -0.0068 0.0218  48  ILE   A CG2  
272  C  CD1  . ILE   A 49  ? 0.5371 0.4743 0.3586 -0.1372 0.0096  0.0331  48  ILE   A CD1  
273  N  N    . GLY   A 50  ? 0.55   0.3647 0.3028 -0.0811 -0.0028 0.0146  49  GLY   A N    
274  C  CA   . GLY   A 50  ? 0.543  0.3557 0.295  -0.062  -0.003  0.0102  49  GLY   A CA   
275  C  C    . GLY   A 50  ? 0.5547 0.3338 0.2785 -0.0646 -0.0051 0.0025  49  GLY   A C    
276  O  O    . GLY   A 50  ? 0.5494 0.3391 0.275  -0.0597 -0.007  -0.002  49  GLY   A O    
277  N  N    . ARG   A 51  ? 0.5742 0.3079 0.2671 -0.0728 -0.0044 0.0008  50  ARG   A N    
278  C  CA   . ARG   A 51  ? 0.5993 0.2893 0.2565 -0.076  -0.0059 -0.0076 50  ARG   A CA   
279  C  C    . ARG   A 51  ? 0.6042 0.3067 0.2606 -0.0997 -0.0131 -0.0126 50  ARG   A C    
280  O  O    . ARG   A 51  ? 0.6172 0.3103 0.2592 -0.0963 -0.0156 -0.02   50  ARG   A O    
281  C  CB   . ARG   A 51  ? 0.6458 0.2771 0.2651 -0.0803 -0.0033 -0.0068 50  ARG   A CB   
282  C  CG   . ARG   A 51  ? 0.6865 0.2631 0.2613 -0.0938 -0.0056 -0.0156 50  ARG   A CG   
283  C  CD   . ARG   A 51  ? 0.7405 0.2498 0.2714 -0.0925 -0.002  -0.0141 50  ARG   A CD   
284  N  NE   . ARG   A 51  ? 0.7884 0.2756 0.3067 -0.0553 0.0021  -0.0147 50  ARG   A NE   
285  C  CZ   . ARG   A 51  ? 0.8522 0.277  0.328  -0.0425 0.0046  -0.0137 50  ARG   A CZ   
286  N  NH1  . ARG   A 51  ? 0.8481 0.2194 0.286  -0.0669 0.0047  -0.0113 50  ARG   A NH1  
287  N  NH2  . ARG   A 51  ? 0.862  0.2778 0.3319 -0.0051 0.0072  -0.0149 50  ARG   A NH2  
288  N  N    . TRP   A 52  ? 0.6027 0.3285 0.2734 -0.1236 -0.0165 -0.0091 51  TRP   A N    
289  C  CA   . TRP   A 52  ? 0.6172 0.3628 0.2902 -0.1471 -0.0252 -0.0143 51  TRP   A CA   
290  C  C    . TRP   A 52  ? 0.6008 0.3987 0.3038 -0.1365 -0.0306 -0.0137 51  TRP   A C    
291  O  O    . TRP   A 52  ? 0.6119 0.418  0.308  -0.1459 -0.0392 -0.0198 51  TRP   A O    
292  C  CB   . TRP   A 52  ? 0.6218 0.3767 0.299  -0.1779 -0.0262 -0.0119 51  TRP   A CB   
293  C  CG   . TRP   A 52  ? 0.6771 0.3648 0.3098 -0.1927 -0.0225 -0.0144 51  TRP   A CG   
294  C  CD1  . TRP   A 52  ? 0.713  0.3574 0.3249 -0.1815 -0.014  -0.009  51  TRP   A CD1  
295  C  CD2  . TRP   A 52  ? 0.7113 0.3586 0.307  -0.2178 -0.0277 -0.0238 51  TRP   A CD2  
296  N  NE1  . TRP   A 52  ? 0.7585 0.3346 0.321  -0.1972 -0.013  -0.0135 51  TRP   A NE1  
297  C  CE2  . TRP   A 52  ? 0.7617 0.3372 0.3131 -0.2215 -0.0209 -0.023  51  TRP   A CE2  
298  C  CE3  . TRP   A 52  ? 0.7184 0.3809 0.3109 -0.2377 -0.0383 -0.033  51  TRP   A CE3  
299  C  CZ2  . TRP   A 52  ? 0.8058 0.3197 0.3079 -0.2461 -0.0233 -0.0314 51  TRP   A CZ2  
300  C  CZ3  . TRP   A 52  ? 0.7617 0.3689 0.3086 -0.2638 -0.0415 -0.0421 51  TRP   A CZ3  
301  C  CH2  . TRP   A 52  ? 0.7995 0.3311 0.3009 -0.2687 -0.0335 -0.0413 51  TRP   A CH2  
302  N  N    . THR   A 53  ? 0.5752 0.4021 0.3052 -0.116  -0.0261 -0.0068 52  THR   A N    
303  C  CA   . THR   A 53  ? 0.5581 0.4208 0.3068 -0.1033 -0.0299 -0.0058 52  THR   A CA   
304  C  C    . THR   A 53  ? 0.58   0.4164 0.3053 -0.0907 -0.0287 -0.0117 52  THR   A C    
305  O  O    . THR   A 53  ? 0.5881 0.4368 0.3094 -0.091  -0.0351 -0.0145 52  THR   A O    
306  C  CB   . THR   A 53  ? 0.5475 0.4361 0.3228 -0.087  -0.0242 0.0019  52  THR   A CB   
307  O  OG1  . THR   A 53  ? 0.5537 0.4677 0.3482 -0.0985 -0.0245 0.0064  52  THR   A OG1  
308  C  CG2  . THR   A 53  ? 0.5296 0.4434 0.3165 -0.0735 -0.0268 0.0036  52  THR   A CG2  
309  N  N    . ALA   A 54  ? 0.5881 0.3883 0.2956 -0.0789 -0.0205 -0.0139 53  ALA   A N    
310  C  CA   . ALA   A 54  ? 0.5957 0.372  0.2805 -0.0656 -0.0166 -0.0204 53  ALA   A CA   
311  C  C    . ALA   A 54  ? 0.6107 0.3638 0.2656 -0.08   -0.0236 -0.029  53  ALA   A C    
312  O  O    . ALA   A 54  ? 0.6156 0.3718 0.2604 -0.0747 -0.0248 -0.0328 53  ALA   A O    
313  C  CB   . ALA   A 54  ? 0.608  0.3532 0.28   -0.0497 -0.0078 -0.0219 53  ALA   A CB   
314  N  N    . TYR   A 55  ? 0.626  0.3569 0.2654 -0.1007 -0.0286 -0.0319 54  TYR   A N    
315  C  CA   . TYR   A 55  ? 0.6541 0.3606 0.262  -0.119  -0.0368 -0.0415 54  TYR   A CA   
316  C  C    . TYR   A 55  ? 0.6469 0.3982 0.2714 -0.1288 -0.0484 -0.0414 54  TYR   A C    
317  O  O    . TYR   A 55  ? 0.6614 0.401  0.2615 -0.1321 -0.0544 -0.0489 54  TYR   A O    
318  C  CB   . TYR   A 55  ? 0.6694 0.3421 0.2564 -0.1448 -0.0396 -0.0445 54  TYR   A CB   
319  C  CG   . TYR   A 55  ? 0.708  0.3267 0.2694 -0.1351 -0.0299 -0.0442 54  TYR   A CG   
320  C  CD1  . TYR   A 55  ? 0.7265 0.3239 0.2769 -0.1043 -0.021  -0.0455 54  TYR   A CD1  
321  C  CD2  . TYR   A 55  ? 0.7419 0.3307 0.2877 -0.1565 -0.0295 -0.0425 54  TYR   A CD2  
322  C  CE1  . TYR   A 55  ? 0.7644 0.3147 0.2909 -0.0907 -0.0138 -0.045  54  TYR   A CE1  
323  C  CE2  . TYR   A 55  ? 0.7803 0.3135 0.2967 -0.1448 -0.0215 -0.041  54  TYR   A CE2  
324  C  CZ   . TYR   A 55  ? 0.8029 0.3169 0.3092 -0.1099 -0.0146 -0.0425 54  TYR   A CZ   
325  O  OH   . TYR   A 55  ? 0.8509 0.3116 0.3268 -0.0941 -0.0084 -0.0411 54  TYR   A OH   
326  N  N    . GLU   A 56  ? 0.6229 0.4242 0.2858 -0.1307 -0.0517 -0.033  55  GLU   A N    
327  C  CA   . GLU   A 56  ? 0.6181 0.4644 0.2971 -0.134  -0.0635 -0.032  55  GLU   A CA   
328  C  C    . GLU   A 56  ? 0.6231 0.4707 0.2943 -0.1124 -0.062  -0.0309 55  GLU   A C    
329  O  O    . GLU   A 56  ? 0.6269 0.4816 0.2839 -0.1154 -0.0721 -0.0347 55  GLU   A O    
330  C  CB   . GLU   A 56  ? 0.6286 0.5267 0.3492 -0.1351 -0.0655 -0.0234 55  GLU   A CB   
331  C  CG   . GLU   A 56  ? 0.6817 0.5899 0.4119 -0.1611 -0.0676 -0.0244 55  GLU   A CG   
332  C  CD   . GLU   A 56  ? 0.7709 0.6947 0.494  -0.1885 -0.0816 -0.0324 55  GLU   A CD   
333  O  OE1  . GLU   A 56  ? 0.7794 0.709  0.4896 -0.1858 -0.0924 -0.0375 55  GLU   A OE1  
334  O  OE2  . GLU   A 56  ? 0.8272 0.7582 0.5564 -0.2145 -0.0817 -0.0338 55  GLU   A OE2  
335  N  N    . PHE   A 57  ? 0.6271 0.4683 0.306  -0.0923 -0.0495 -0.0258 56  PHE   A N    
336  C  CA   . PHE   A 57  ? 0.6319 0.4723 0.3024 -0.0749 -0.0447 -0.0242 56  PHE   A CA   
337  C  C    . PHE   A 57  ? 0.6721 0.4745 0.3044 -0.0733 -0.041  -0.0335 56  PHE   A C    
338  O  O    . PHE   A 57  ? 0.686  0.4881 0.3013 -0.0674 -0.0421 -0.0344 56  PHE   A O    
339  C  CB   . PHE   A 57  ? 0.6138 0.4612 0.3047 -0.0588 -0.0321 -0.0174 56  PHE   A CB   
340  C  CG   . PHE   A 57  ? 0.5903 0.4726 0.3099 -0.0539 -0.0347 -0.0082 56  PHE   A CG   
341  C  CD1  . PHE   A 57  ? 0.591  0.4859 0.3071 -0.0459 -0.0382 -0.004  56  PHE   A CD1  
342  C  CD2  . PHE   A 57  ? 0.5811 0.4784 0.3263 -0.0553 -0.0326 -0.0037 56  PHE   A CD2  
343  C  CE1  . PHE   A 57  ? 0.5768 0.4964 0.3139 -0.0381 -0.0399 0.004   56  PHE   A CE1  
344  C  CE2  . PHE   A 57  ? 0.5644 0.4905 0.3325 -0.0484 -0.0339 0.0037  56  PHE   A CE2  
345  C  CZ   . PHE   A 57  ? 0.56   0.4957 0.3235 -0.0391 -0.0375 0.0072  56  PHE   A CZ   
346  N  N    . ALA   A 58  ? 0.6916 0.4586 0.3052 -0.0782 -0.0369 -0.0406 57  ALA   A N    
347  C  CA   . ALA   A 58  ? 0.7247 0.4512 0.2975 -0.0754 -0.0333 -0.0511 57  ALA   A CA   
348  C  C    . ALA   A 58  ? 0.7432 0.4662 0.2914 -0.0921 -0.0478 -0.0576 57  ALA   A C    
349  O  O    . ALA   A 58  ? 0.767  0.4732 0.285  -0.0864 -0.0465 -0.0635 57  ALA   A O    
350  C  CB   . ALA   A 58  ? 0.7458 0.4304 0.3007 -0.076  -0.0275 -0.0568 57  ALA   A CB   
351  N  N    . LYS   A 59  ? 0.7301 0.4724 0.2911 -0.1132 -0.0615 -0.0571 58  LYS   A N    
352  C  CA   . LYS   A 59  ? 0.7357 0.4848 0.2781 -0.1305 -0.0781 -0.0637 58  LYS   A CA   
353  C  C    . LYS   A 59  ? 0.7196 0.5061 0.2723 -0.1185 -0.085  -0.0572 58  LYS   A C    
354  O  O    . LYS   A 59  ? 0.7375 0.5199 0.2632 -0.1226 -0.0954 -0.0627 58  LYS   A O    
355  C  CB   . LYS   A 59  ? 0.7519 0.5176 0.3074 -0.1588 -0.0904 -0.066  58  LYS   A CB   
356  C  CG   . LYS   A 59  ? 0.8625 0.5747 0.3888 -0.1756 -0.0858 -0.0745 58  LYS   A CG   
357  C  CD   . LYS   A 59  ? 0.9426 0.669  0.4823 -0.2082 -0.0942 -0.0755 58  LYS   A CD   
358  C  CE   . LYS   A 59  ? 0.9969 0.7507 0.5771 -0.2049 -0.0858 -0.0641 58  LYS   A CE   
359  N  NZ   . LYS   A 59  ? 1.0409 0.8038 0.6292 -0.2384 -0.0904 -0.0654 58  LYS   A NZ   
360  N  N    . GLN   A 60  ? 0.696  0.5124 0.2816 -0.1025 -0.0788 -0.0456 59  GLN   A N    
361  C  CA   . GLN   A 60  ? 0.6864 0.5283 0.2763 -0.0884 -0.0833 -0.0378 59  GLN   A CA   
362  C  C    . GLN   A 60  ? 0.6989 0.5134 0.259  -0.073  -0.0715 -0.0378 59  GLN   A C    
363  O  O    . GLN   A 60  ? 0.7    0.5258 0.256  -0.0618 -0.0731 -0.0305 59  GLN   A O    
364  C  CB   . GLN   A 60  ? 0.684  0.5596 0.3144 -0.0782 -0.0798 -0.0264 59  GLN   A CB   
365  C  CG   . GLN   A 60  ? 0.7203 0.6354 0.3819 -0.0905 -0.0918 -0.0249 59  GLN   A CG   
366  C  CD   . GLN   A 60  ? 0.7851 0.7322 0.444  -0.0946 -0.1118 -0.0262 59  GLN   A CD   
367  O  OE1  . GLN   A 60  ? 0.8149 0.7626 0.4562 -0.0805 -0.1173 -0.0228 59  GLN   A OE1  
368  N  NE2  . GLN   A 60  ? 0.781  0.7569 0.4565 -0.1146 -0.1233 -0.031  59  GLN   A NE2  
369  N  N    . LYS   A 61  ? 0.7069 0.4845 0.2444 -0.072  -0.0589 -0.0458 60  LYS   A N    
370  C  CA   . LYS   A 61  ? 0.7138 0.4666 0.2232 -0.0592 -0.0443 -0.0484 60  LYS   A CA   
371  C  C    . LYS   A 61  ? 0.6939 0.4611 0.2262 -0.0444 -0.0283 -0.0388 60  LYS   A C    
372  O  O    . LYS   A 61  ? 0.7125 0.4723 0.2257 -0.0364 -0.0181 -0.0373 60  LYS   A O    
373  C  CB   . LYS   A 61  ? 0.7395 0.4822 0.2096 -0.0607 -0.0529 -0.0516 60  LYS   A CB   
374  C  CG   . LYS   A 61  ? 0.8008 0.5313 0.2467 -0.0779 -0.0704 -0.0623 60  LYS   A CG   
375  C  CD   . LYS   A 61  ? 0.9004 0.6131 0.2993 -0.0764 -0.0758 -0.0671 60  LYS   A CD   
376  C  CE   . LYS   A 61  ? 0.974  0.697  0.3569 -0.0922 -0.101  -0.0725 60  LYS   A CE   
377  N  NZ   . LYS   A 61  ? 1.0329 0.7409 0.3689 -0.0868 -0.1065 -0.0745 60  LYS   A NZ   
378  N  N    . SER   A 62  ? 0.6491 0.4352 0.2194 -0.0429 -0.0254 -0.033  61  SER   A N    
379  C  CA   . SER   A 62  ? 0.6305 0.4298 0.2227 -0.0322 -0.0115 -0.0257 61  SER   A CA   
380  C  C    . SER   A 62  ? 0.6309 0.4164 0.22   -0.0238 0.0057  -0.032  61  SER   A C    
381  O  O    . SER   A 62  ? 0.6516 0.4157 0.2271 -0.0243 0.0057  -0.0407 61  SER   A O    
382  C  CB   . SER   A 62  ? 0.6176 0.4407 0.2484 -0.0335 -0.0156 -0.0188 61  SER   A CB   
383  O  OG   . SER   A 62  ? 0.6156 0.4601 0.2571 -0.0357 -0.0283 -0.0117 61  SER   A OG   
384  N  N    . ARG   A 63  ? 0.6077 0.4058 0.2092 -0.0159 0.02    -0.0281 62  ARG   A N    
385  C  CA   . ARG   A 63  ? 0.6095 0.408  0.2178 -0.0059 0.0355  -0.0338 62  ARG   A CA   
386  C  C    . ARG   A 63  ? 0.6102 0.4261 0.2551 -0.0039 0.0337  -0.0294 62  ARG   A C    
387  O  O    . ARG   A 63  ? 0.5978 0.4324 0.2638 -0.0077 0.0306  -0.0209 62  ARG   A O    
388  C  CB   . ARG   A 63  ? 0.615  0.4251 0.2194 -0.002  0.0523  -0.0327 62  ARG   A CB   
389  C  CG   . ARG   A 63  ? 0.6804 0.4725 0.2452 -0.0051 0.0543  -0.0347 62  ARG   A CG   
390  C  CD   . ARG   A 63  ? 0.7147 0.5175 0.2755 -0.0084 0.0672  -0.0281 62  ARG   A CD   
391  N  NE   . ARG   A 63  ? 0.747  0.5714 0.3269 -0.0031 0.0863  -0.0322 62  ARG   A NE   
392  C  CZ   . ARG   A 63  ? 0.7666 0.6061 0.3487 -0.0088 0.1017  -0.0284 62  ARG   A CZ   
393  N  NH1  . ARG   A 63  ? 0.78   0.6065 0.341  -0.0189 0.1007  -0.0194 62  ARG   A NH1  
394  N  NH2  . ARG   A 63  ? 0.7403 0.6083 0.345  -0.0048 0.1179  -0.0336 62  ARG   A NH2  
395  N  N    . LEU   A 64  ? 0.6119 0.417  0.2593 0.003   0.0348  -0.0351 63  LEU   A N    
396  C  CA   . LEU   A 64  ? 0.5959 0.4122 0.2713 0.0047  0.0315  -0.0307 63  LEU   A CA   
397  C  C    . LEU   A 64  ? 0.5735 0.4071 0.2683 0.0185  0.0424  -0.032  63  LEU   A C    
398  O  O    . LEU   A 64  ? 0.5696 0.3982 0.2539 0.0313  0.0515  -0.0395 63  LEU   A O    
399  C  CB   . LEU   A 64  ? 0.626  0.415  0.2885 0.0001  0.0222  -0.0338 63  LEU   A CB   
400  C  CG   . LEU   A 64  ? 0.6762 0.4587 0.3277 -0.0173 0.0088  -0.0325 63  LEU   A CG   
401  C  CD1  . LEU   A 64  ? 0.7074 0.459  0.3407 -0.0261 0.0018  -0.0375 63  LEU   A CD1  
402  C  CD2  . LEU   A 64  ? 0.6764 0.4888 0.3567 -0.0241 0.0022  -0.0228 63  LEU   A CD2  
403  N  N    . VAL   A 65  ? 0.5588 0.4152 0.2823 0.0169  0.0405  -0.0252 64  VAL   A N    
404  C  CA   . VAL   A 65  ? 0.5406 0.4182 0.2866 0.0282  0.0465  -0.0258 64  VAL   A CA   
405  C  C    . VAL   A 65  ? 0.5325 0.4019 0.2874 0.0283  0.0371  -0.0216 64  VAL   A C    
406  O  O    . VAL   A 65  ? 0.5319 0.4068 0.2971 0.0174  0.0304  -0.0148 64  VAL   A O    
407  C  CB   . VAL   A 65  ? 0.5261 0.4364 0.2939 0.0234  0.0532  -0.0222 64  VAL   A CB   
408  C  CG1  . VAL   A 65  ? 0.5232 0.4604 0.3139 0.035   0.0583  -0.0253 64  VAL   A CG1  
409  C  CG2  . VAL   A 65  ? 0.5217 0.4346 0.275  0.018   0.0628  -0.0241 64  VAL   A CG2  
410  N  N    . LEU   A 66  ? 0.5256 0.3777 0.2717 0.0413  0.0368  -0.0255 65  LEU   A N    
411  C  CA   . LEU   A 66  ? 0.5157 0.3526 0.2624 0.0407  0.0291  -0.021  65  LEU   A CA   
412  C  C    . LEU   A 66  ? 0.5069 0.3637 0.2722 0.056   0.0306  -0.0199 65  LEU   A C    
413  O  O    . LEU   A 66  ? 0.5065 0.3726 0.2724 0.0741  0.0364  -0.0258 65  LEU   A O    
414  C  CB   . LEU   A 66  ? 0.5308 0.3214 0.2441 0.0415  0.0258  -0.025  65  LEU   A CB   
415  C  CG   . LEU   A 66  ? 0.5363 0.3072 0.2278 0.026   0.0228  -0.0283 65  LEU   A CG   
416  C  CD1  . LEU   A 66  ? 0.5604 0.2813 0.2156 0.0253  0.02    -0.0336 65  LEU   A CD1  
417  C  CD2  . LEU   A 66  ? 0.5269 0.3146 0.2329 0.0057  0.0153  -0.0215 65  LEU   A CD2  
418  N  N    . TRP   A 67  ? 0.4945 0.3612 0.275  0.0495  0.0253  -0.0128 66  TRP   A N    
419  C  CA   . TRP   A 67  ? 0.482  0.3683 0.2788 0.0616  0.0241  -0.0111 66  TRP   A CA   
420  C  C    . TRP   A 67  ? 0.494  0.3536 0.278  0.0635  0.0175  -0.0058 66  TRP   A C    
421  O  O    . TRP   A 67  ? 0.5119 0.3566 0.29   0.0474  0.0143  -0.0007 66  TRP   A O    
422  C  CB   . TRP   A 67  ? 0.4533 0.3753 0.2766 0.0513  0.0246  -0.0079 66  TRP   A CB   
423  C  CG   . TRP   A 67  ? 0.4385 0.3916 0.2763 0.0511  0.0324  -0.0127 66  TRP   A CG   
424  C  CD1  . TRP   A 67  ? 0.4564 0.4112 0.2867 0.0559  0.0401  -0.019  66  TRP   A CD1  
425  C  CD2  . TRP   A 67  ? 0.4216 0.4058 0.2804 0.0424  0.0344  -0.0117 66  TRP   A CD2  
426  N  NE1  . TRP   A 67  ? 0.4439 0.4325 0.2912 0.0502  0.0477  -0.0214 66  TRP   A NE1  
427  C  CE2  . TRP   A 67  ? 0.4208 0.4262 0.2851 0.0407  0.044   -0.0172 66  TRP   A CE2  
428  C  CE3  . TRP   A 67  ? 0.4172 0.4109 0.2876 0.0349  0.0298  -0.0073 66  TRP   A CE3  
429  C  CZ2  . TRP   A 67  ? 0.4084 0.4427 0.2891 0.029   0.049   -0.0179 66  TRP   A CZ2  
430  C  CZ3  . TRP   A 67  ? 0.4095 0.429  0.2945 0.0253  0.0336  -0.0089 66  TRP   A CZ3  
431  C  CH2  . TRP   A 67  ? 0.4056 0.4445 0.2955 0.021   0.0431  -0.014  66  TRP   A CH2  
432  N  N    . ASP   A 68  ? 0.4802 0.3372 0.2604 0.0833  0.0157  -0.0066 67  ASP   A N    
433  C  CA   . ASP   A 68  ? 0.4885 0.3162 0.2513 0.0866  0.01    -0.0005 67  ASP   A CA   
434  C  C    . ASP   A 68  ? 0.4877 0.3219 0.2492 0.1134  0.0069  -0.0018 67  ASP   A C    
435  O  O    . ASP   A 68  ? 0.4755 0.3276 0.2432 0.1314  0.0097  -0.0089 67  ASP   A O    
436  C  CB   . ASP   A 68  ? 0.5285 0.3022 0.2555 0.0792  0.0097  0.0004  67  ASP   A CB   
437  C  CG   . ASP   A 68  ? 0.5964 0.3419 0.3072 0.0676  0.0061  0.0089  67  ASP   A CG   
438  O  OD1  . ASP   A 68  ? 0.6202 0.3507 0.318  0.0831  0.0031  0.0128  67  ASP   A OD1  
439  O  OD2  . ASP   A 68  ? 0.6034 0.3429 0.3131 0.0438  0.0065  0.0118  67  ASP   A OD2  
440  N  N    . ILE   A 69  ? 0.4957 0.3195 0.2498 0.117   0.0009  0.005   68  ILE   A N    
441  C  CA   . ILE   A 69  ? 0.5149 0.3407 0.2622 0.145   -0.0048 0.0047  68  ILE   A CA   
442  C  C    . ILE   A 69  ? 0.5661 0.3337 0.2703 0.1639  -0.0053 0.0045  68  ILE   A C    
443  O  O    . ILE   A 69  ? 0.5807 0.3481 0.276  0.1946  -0.0095 0.0023  68  ILE   A O    
444  C  CB   . ILE   A 69  ? 0.5216 0.3526 0.27   0.1431  -0.0116 0.0122  68  ILE   A CB   
445  C  CG1  . ILE   A 69  ? 0.5457 0.3335 0.2696 0.122   -0.0102 0.0209  68  ILE   A CG1  
446  C  CG2  . ILE   A 69  ? 0.5052 0.3938 0.2927 0.1334  -0.0124 0.0097  68  ILE   A CG2  
447  C  CD1  . ILE   A 69  ? 0.5541 0.3393 0.2709 0.1222  -0.015  0.0283  68  ILE   A CD1  
448  N  N    . ASN   A 70  ? 0.5796 0.2977 0.2554 0.1457  -0.0018 0.0066  69  ASN   A N    
449  C  CA   . ASN   A 70  ? 0.6213 0.2738 0.2499 0.1561  -0.0011 0.0057  69  ASN   A CA   
450  C  C    . ASN   A 70  ? 0.6329 0.2855 0.2598 0.1625  0.0048  -0.005  69  ASN   A C    
451  O  O    . ASN   A 70  ? 0.6275 0.2747 0.2549 0.1385  0.0087  -0.0076 69  ASN   A O    
452  C  CB   . ASN   A 70  ? 0.6512 0.2543 0.2508 0.127   -0.0004 0.0129  69  ASN   A CB   
453  C  CG   . ASN   A 70  ? 0.7364 0.2622 0.2807 0.1308  0.0008  0.0118  69  ASN   A CG   
454  O  OD1  . ASN   A 70  ? 0.7728 0.2703 0.2914 0.162   0       0.0073  69  ASN   A OD1  
455  N  ND2  . ASN   A 70  ? 0.7594 0.2487 0.2823 0.099   0.0029  0.0151  69  ASN   A ND2  
456  N  N    . LYS   A 71  ? 0.6374 0.3003 0.2631 0.1967  0.0053  -0.0116 70  LYS   A N    
457  C  CA   . LYS   A 71  ? 0.6443 0.3117 0.2677 0.2097  0.0124  -0.0226 70  LYS   A CA   
458  C  C    . LYS   A 71  ? 0.7029 0.2957 0.2756 0.2024  0.0151  -0.0256 70  LYS   A C    
459  O  O    . LYS   A 71  ? 0.6911 0.2852 0.265  0.1849  0.0203  -0.0314 70  LYS   A O    
460  C  CB   . LYS   A 71  ? 0.6488 0.3438 0.2797 0.2518  0.0119  -0.0285 70  LYS   A CB   
461  C  CG   . LYS   A 71  ? 0.6947 0.4131 0.3333 0.2665  0.0218  -0.0407 70  LYS   A CG   
462  C  CD   . LYS   A 71  ? 0.7424 0.5082 0.4006 0.3071  0.0217  -0.0469 70  LYS   A CD   
463  C  CE   . LYS   A 71  ? 0.7783 0.5789 0.4496 0.3211  0.034   -0.0594 70  LYS   A CE   
464  N  NZ   . LYS   A 71  ? 0.8599 0.5904 0.4786 0.3364  0.0395  -0.0659 70  LYS   A NZ   
465  N  N    . HIS   A 72  ? 0.7666 0.2907 0.291  0.2137  0.011   -0.0213 71  HIS   A N    
466  C  CA   . HIS   A 72  ? 0.8387 0.2814 0.3069 0.2049  0.0129  -0.0242 71  HIS   A CA   
467  C  C    . HIS   A 72  ? 0.8532 0.2893 0.324  0.1587  0.0138  -0.0229 71  HIS   A C    
468  O  O    . HIS   A 72  ? 0.875  0.2824 0.3234 0.1482  0.017   -0.031  71  HIS   A O    
469  C  CB   . HIS   A 72  ? 0.9099 0.279  0.3257 0.2175  0.0082  -0.0167 71  HIS   A CB   
470  C  CG   . HIS   A 72  ? 1.0269 0.3053 0.3804 0.2012  0.0102  -0.019  71  HIS   A CG   
471  N  ND1  . HIS   A 72  ? 1.0864 0.3145 0.3977 0.225   0.0139  -0.0298 71  HIS   A ND1  
472  C  CD2  . HIS   A 72  ? 1.0739 0.3088 0.4028 0.1611  0.0096  -0.0132 71  HIS   A CD2  
473  C  CE1  . HIS   A 72  ? 1.1364 0.2862 0.3954 0.1978  0.0145  -0.0302 71  HIS   A CE1  
474  N  NE2  . HIS   A 72  ? 1.1387 0.2927 0.4081 0.1575  0.012   -0.0205 71  HIS   A NE2  
475  N  N    . GLY   A 73  ? 0.8372 0.2991 0.3328 0.1331  0.0106  -0.0134 72  GLY   A N    
476  C  CA   . GLY   A 73  ? 0.8326 0.2974 0.3353 0.0918  0.0104  -0.0116 72  GLY   A CA   
477  C  C    . GLY   A 73  ? 0.7946 0.3139 0.3345 0.0808  0.0126  -0.0178 72  GLY   A C    
478  O  O    . GLY   A 73  ? 0.7953 0.303  0.3263 0.055   0.012   -0.0211 72  GLY   A O    
479  N  N    . VAL   A 74  ? 0.7589 0.3381 0.3391 0.0983  0.0146  -0.019  73  VAL   A N    
480  C  CA   . VAL   A 74  ? 0.7315 0.3584 0.3427 0.0874  0.0176  -0.0234 73  VAL   A CA   
481  C  C    . VAL   A 74  ? 0.7547 0.3578 0.3402 0.0974  0.0226  -0.0346 73  VAL   A C    
482  O  O    . VAL   A 74  ? 0.7526 0.3579 0.336  0.0782  0.0229  -0.0383 73  VAL   A O    
483  C  CB   . VAL   A 74  ? 0.6869 0.3817 0.3463 0.0948  0.0191  -0.0208 73  VAL   A CB   
484  C  CG1  . VAL   A 74  ? 0.6791 0.3982 0.3474 0.1248  0.0245  -0.028  73  VAL   A CG1  
485  C  CG2  . VAL   A 74  ? 0.661  0.3922 0.3465 0.0714  0.0198  -0.0198 73  VAL   A CG2  
486  N  N    . GLU   A 75  ? 0.7764 0.3506 0.3364 0.1279  0.0257  -0.0401 74  GLU   A N    
487  C  CA   . GLU   A 75  ? 0.801  0.3453 0.3298 0.1406  0.0315  -0.0517 74  GLU   A CA   
488  C  C    . GLU   A 75  ? 0.8518 0.327  0.332  0.1185  0.0281  -0.0548 74  GLU   A C    
489  O  O    . GLU   A 75  ? 0.8762 0.3353 0.3362 0.1135  0.0311  -0.064  74  GLU   A O    
490  C  CB   . GLU   A 75  ? 0.8267 0.3606 0.3414 0.1832  0.0358  -0.057  74  GLU   A CB   
491  C  CG   . GLU   A 75  ? 0.8391 0.4515 0.4061 0.2003  0.0388  -0.0557 74  GLU   A CG   
492  C  CD   . GLU   A 75  ? 0.9181 0.5412 0.4828 0.2443  0.0423  -0.0615 74  GLU   A CD   
493  O  OE1  . GLU   A 75  ? 0.9623 0.5238 0.4799 0.2676  0.042   -0.0655 74  GLU   A OE1  
494  O  OE2  . GLU   A 75  ? 0.9109 0.6053 0.5207 0.2555  0.0454  -0.0625 74  GLU   A OE2  
495  N  N    . GLU   A 76  ? 0.8737 0.3095 0.3344 0.1025  0.022   -0.0474 75  GLU   A N    
496  C  CA   . GLU   A 76  ? 0.9197 0.2936 0.337  0.0739  0.0183  -0.0495 75  GLU   A CA   
497  C  C    . GLU   A 76  ? 0.8945 0.3082 0.339  0.0375  0.0143  -0.0492 75  GLU   A C    
498  O  O    . GLU   A 76  ? 0.9176 0.3021 0.3345 0.0188  0.0122  -0.057  75  GLU   A O    
499  C  CB   . GLU   A 76  ? 0.989  0.3197 0.3836 0.0652  0.0148  -0.04   75  GLU   A CB   
500  C  CG   . GLU   A 76  ? 1.1393 0.3913 0.4773 0.0386  0.0126  -0.043  75  GLU   A CG   
501  C  CD   . GLU   A 76  ? 1.3069 0.5134 0.6188 0.0275  0.0112  -0.0324 75  GLU   A CD   
502  O  OE1  . GLU   A 76  ? 1.3274 0.5734 0.6721 0.034   0.0106  -0.0218 75  GLU   A OE1  
503  O  OE2  . GLU   A 76  ? 1.3988 0.5265 0.6533 0.0106  0.011   -0.0349 75  GLU   A OE2  
504  N  N    . THR   A 77  ? 0.8458 0.3255 0.3421 0.0297  0.0128  -0.041  76  THR   A N    
505  C  CA   . THR   A 77  ? 0.8302 0.3517 0.3537 0.0023  0.0086  -0.04   76  THR   A CA   
506  C  C    . THR   A 77  ? 0.826  0.3635 0.3492 0.0101  0.0116  -0.0491 76  THR   A C    
507  O  O    . THR   A 77  ? 0.8348 0.3666 0.3457 -0.0105 0.0069  -0.0538 76  THR   A O    
508  C  CB   . THR   A 77  ? 0.8181 0.4009 0.3922 -0.0003 0.0077  -0.0297 76  THR   A CB   
509  O  OG1  . THR   A 77  ? 0.8472 0.4152 0.4184 -0.0127 0.0053  -0.0216 76  THR   A OG1  
510  C  CG2  . THR   A 77  ? 0.7947 0.4254 0.3984 -0.0185 0.004   -0.0288 76  THR   A CG2  
511  N  N    . ALA   A 78  ? 0.8127 0.3712 0.3477 0.0395  0.0195  -0.0517 77  ALA   A N    
512  C  CA   . ALA   A 78  ? 0.8119 0.389  0.347  0.0494  0.0258  -0.0595 77  ALA   A CA   
513  C  C    . ALA   A 78  ? 0.8567 0.3782 0.3408 0.0508  0.027   -0.0713 77  ALA   A C    
514  O  O    . ALA   A 78  ? 0.8534 0.382  0.3296 0.0425  0.0276  -0.0771 77  ALA   A O    
515  C  CB   . ALA   A 78  ? 0.7908 0.403  0.3495 0.0793  0.0352  -0.0601 77  ALA   A CB   
516  N  N    . ALA   A 79  ? 0.8972 0.3583 0.3417 0.0613  0.0271  -0.075  78  ALA   A N    
517  C  CA   . ALA   A 79  ? 0.9451 0.3426 0.3333 0.0622  0.0282  -0.0873 78  ALA   A CA   
518  C  C    . ALA   A 79  ? 0.9705 0.3502 0.3421 0.0226  0.0179  -0.0892 78  ALA   A C    
519  O  O    . ALA   A 79  ? 0.9972 0.3597 0.3417 0.0161  0.0174  -0.0991 78  ALA   A O    
520  C  CB   . ALA   A 79  ? 0.982  0.3121 0.3274 0.0811  0.0297  -0.0894 78  ALA   A CB   
521  N  N    . GLU   A 80  ? 0.9656 0.3566 0.356  -0.0038 0.0097  -0.0799 79  GLU   A N    
522  C  CA   . GLU   A 80  ? 0.9748 0.363  0.3585 -0.0423 -0.0009 -0.0812 79  GLU   A CA   
523  C  C    . GLU   A 80  ? 0.9333 0.3828 0.35   -0.0514 -0.0051 -0.0807 79  GLU   A C    
524  O  O    . GLU   A 80  ? 0.9521 0.3916 0.3478 -0.0719 -0.0128 -0.088  79  GLU   A O    
525  C  CB   . GLU   A 80  ? 1.0188 0.4054 0.414  -0.0661 -0.0061 -0.0716 79  GLU   A CB   
526  C  CG   . GLU   A 80  ? 1.113  0.5037 0.5046 -0.108  -0.0169 -0.0737 79  GLU   A CG   
527  C  CD   . GLU   A 80  ? 1.2613 0.6024 0.6025 -0.1231 -0.0218 -0.0878 79  GLU   A CD   
528  O  OE1  . GLU   A 80  ? 1.3467 0.6121 0.6347 -0.1184 -0.018  -0.0945 79  GLU   A OE1  
529  O  OE2  . GLU   A 80  ? 1.2672 0.6424 0.6189 -0.1373 -0.0298 -0.0924 79  GLU   A OE2  
530  N  N    . CYS   A 81  ? 0.8741 0.3819 0.3365 -0.0349 -0.0002 -0.0728 80  CYS   A N    
531  C  CA   . CYS   A 81  ? 0.8367 0.3941 0.3235 -0.0393 -0.0027 -0.0713 80  CYS   A CA   
532  C  C    . CYS   A 81  ? 0.8688 0.4059 0.3227 -0.0273 0.0028  -0.0822 80  CYS   A C    
533  O  O    . CYS   A 81  ? 0.8782 0.423  0.3217 -0.0413 -0.004  -0.0857 80  CYS   A O    
534  C  CB   . CYS   A 81  ? 0.788  0.4005 0.3227 -0.0256 0.0028  -0.061  80  CYS   A CB   
535  S  SG   . CYS   A 81  ? 0.7467 0.3938 0.3218 -0.0418 -0.0044 -0.0483 80  CYS   A SG   
536  N  N    . ARG   A 82  ? 0.881  0.3918 0.3157 -0.0006 0.0148  -0.0882 81  ARG   A N    
537  C  CA   . ARG   A 82  ? 0.9008 0.3905 0.301  0.0127  0.0224  -0.0997 81  ARG   A CA   
538  C  C    . ARG   A 82  ? 0.9612 0.3943 0.3089 -0.0062 0.0137  -0.1107 81  ARG   A C    
539  O  O    . ARG   A 82  ? 0.9745 0.4058 0.3007 -0.0111 0.0126  -0.1176 81  ARG   A O    
540  C  CB   . ARG   A 82  ? 0.9003 0.3794 0.2942 0.0478  0.0373  -0.1043 81  ARG   A CB   
541  C  CG   . ARG   A 82  ? 0.8527 0.3955 0.2978 0.0631  0.0459  -0.0959 81  ARG   A CG   
542  C  CD   . ARG   A 82  ? 0.8595 0.4041 0.3015 0.0982  0.0605  -0.1022 81  ARG   A CD   
543  N  NE   . ARG   A 82  ? 0.8456 0.4518 0.3393 0.1081  0.0661  -0.0939 81  ARG   A NE   
544  C  CZ   . ARG   A 82  ? 0.87   0.4856 0.3844 0.123   0.0652  -0.0892 81  ARG   A CZ   
545  N  NH1  . ARG   A 82  ? 0.8685 0.4318 0.3531 0.1329  0.0603  -0.0911 81  ARG   A NH1  
546  N  NH2  . ARG   A 82  ? 0.862  0.5359 0.4229 0.1276  0.0687  -0.0825 81  ARG   A NH2  
547  N  N    . LYS   A 83  ? 1.0023 0.3884 0.3269 -0.0201 0.0069  -0.1121 82  LYS   A N    
548  C  CA   . LYS   A 83  ? 1.0533 0.3848 0.327  -0.045  -0.0028 -0.1231 82  LYS   A CA   
549  C  C    . LYS   A 83  ? 1.0288 0.4014 0.3196 -0.0764 -0.0174 -0.1214 82  LYS   A C    
550  O  O    . LYS   A 83  ? 1.0509 0.396  0.3031 -0.0928 -0.0253 -0.1323 82  LYS   A O    
551  C  CB   . LYS   A 83  ? 1.1272 0.4027 0.375  -0.0595 -0.0068 -0.1231 82  LYS   A CB   
552  C  CG   . LYS   A 83  ? 1.2553 0.4701 0.4656 -0.0278 0.0048  -0.1279 82  LYS   A CG   
553  C  CD   . LYS   A 83  ? 1.3612 0.524  0.5504 -0.0402 0.0017  -0.1233 82  LYS   A CD   
554  C  CE   . LYS   A 83  ? 1.45   0.5652 0.6    -0.0843 -0.0097 -0.1296 82  LYS   A CE   
555  N  NZ   . LYS   A 83  ? 1.4986 0.5807 0.641  -0.1028 -0.0115 -0.1211 82  LYS   A NZ   
556  N  N    . LEU   A 84  ? 0.9759 0.4142 0.3226 -0.0822 -0.0215 -0.1083 83  LEU   A N    
557  C  CA   . LEU   A 84  ? 0.9444 0.4307 0.3141 -0.1038 -0.035  -0.1046 83  LEU   A CA   
558  C  C    . LEU   A 84  ? 0.9437 0.4571 0.3128 -0.0904 -0.0328 -0.1055 83  LEU   A C    
559  O  O    . LEU   A 84  ? 0.9331 0.4831 0.3161 -0.1039 -0.045  -0.1021 83  LEU   A O    
560  C  CB   . LEU   A 84  ? 0.8956 0.4354 0.3203 -0.1103 -0.0384 -0.0905 83  LEU   A CB   
561  C  CG   . LEU   A 84  ? 0.9007 0.4237 0.3275 -0.1323 -0.043  -0.0884 83  LEU   A CG   
562  C  CD1  . LEU   A 84  ? 0.8689 0.4438 0.349  -0.131  -0.0419 -0.0745 83  LEU   A CD1  
563  C  CD2  . LEU   A 84  ? 0.9061 0.419  0.3113 -0.1679 -0.0581 -0.0964 83  LEU   A CD2  
564  N  N    . GLY   A 85  ? 0.9478 0.4454 0.3013 -0.0635 -0.0172 -0.1094 84  GLY   A N    
565  C  CA   . GLY   A 85  ? 0.9403 0.4566 0.2865 -0.0509 -0.0109 -0.1105 84  GLY   A CA   
566  C  C    . GLY   A 85  ? 0.9069 0.4733 0.2961 -0.0341 0.0001  -0.0988 84  GLY   A C    
567  O  O    . GLY   A 85  ? 0.9179 0.4974 0.2989 -0.025  0.0078  -0.0988 84  GLY   A O    
568  N  N    . ALA   A 86  ? 0.8608 0.4527 0.2925 -0.031  0.0018  -0.089  85  ALA   A N    
569  C  CA   . ALA   A 86  ? 0.8185 0.4565 0.2906 -0.0189 0.0109  -0.0784 85  ALA   A CA   
570  C  C    . ALA   A 86  ? 0.8074 0.4492 0.2857 0.0058  0.03    -0.0807 85  ALA   A C    
571  O  O    . ALA   A 86  ? 0.8184 0.4309 0.2813 0.0186  0.0355  -0.0878 85  ALA   A O    
572  C  CB   . ALA   A 86  ? 0.7889 0.4556 0.3028 -0.0276 0.0031  -0.0674 85  ALA   A CB   
573  N  N    . THR   A 87  ? 0.7816 0.4616 0.2832 0.0126  0.0398  -0.0744 86  THR   A N    
574  C  CA   . THR   A 87  ? 0.7638 0.4641 0.2833 0.0326  0.0573  -0.0755 86  THR   A CA   
575  C  C    . THR   A 87  ? 0.7404 0.468  0.3039 0.0334  0.054   -0.0663 86  THR   A C    
576  O  O    . THR   A 87  ? 0.7255 0.4739 0.3113 0.0199  0.0456  -0.0567 86  THR   A O    
577  C  CB   . THR   A 87  ? 0.7548 0.4809 0.2748 0.0342  0.0703  -0.0738 86  THR   A CB   
578  O  OG1  . THR   A 87  ? 0.7909 0.4883 0.266  0.0356  0.0742  -0.0832 86  THR   A OG1  
579  C  CG2  . THR   A 87  ? 0.7302 0.4909 0.2783 0.0502  0.0878  -0.0745 86  THR   A CG2  
580  N  N    . VAL   A 88  ? 0.7312 0.456  0.3033 0.0508  0.0596  -0.0696 87  VAL   A N    
581  C  CA   . VAL   A 88  ? 0.7103 0.4554 0.3172 0.0529  0.0555  -0.0619 87  VAL   A CA   
582  C  C    . VAL   A 88  ? 0.6973 0.4719 0.3271 0.0751  0.0675  -0.064  87  VAL   A C    
583  O  O    . VAL   A 88  ? 0.7201 0.481  0.3324 0.0956  0.0756  -0.0731 87  VAL   A O    
584  C  CB   . VAL   A 88  ? 0.7287 0.4332 0.3189 0.0494  0.0445  -0.0624 87  VAL   A CB   
585  C  CG1  . VAL   A 88  ? 0.7198 0.4424 0.3412 0.0494  0.0398  -0.0535 87  VAL   A CG1  
586  C  CG2  . VAL   A 88  ? 0.748  0.4273 0.3157 0.026   0.0325  -0.0627 87  VAL   A CG2  
587  N  N    . HIS   A 89  ? 0.6603 0.4752 0.3281 0.0722  0.0677  -0.0564 88  HIS   A N    
588  C  CA   . HIS   A 89  ? 0.6324 0.4824 0.3269 0.0905  0.0756  -0.0583 88  HIS   A CA   
589  C  C    . HIS   A 89  ? 0.6133 0.4638 0.3262 0.0909  0.0646  -0.0512 88  HIS   A C    
590  O  O    . HIS   A 89  ? 0.6062 0.4603 0.3307 0.0726  0.0568  -0.043  88  HIS   A O    
591  C  CB   . HIS   A 89  ? 0.6224 0.5219 0.3443 0.0828  0.086   -0.0563 88  HIS   A CB   
592  C  CG   . HIS   A 89  ? 0.6824 0.5922 0.3908 0.0875  0.1015  -0.0639 88  HIS   A CG   
593  N  ND1  . HIS   A 89  ? 0.7183 0.6074 0.3995 0.073   0.1037  -0.0634 88  HIS   A ND1  
594  C  CD2  . HIS   A 89  ? 0.6894 0.6313 0.4082 0.1052  0.1158  -0.0721 88  HIS   A CD2  
595  C  CE1  . HIS   A 89  ? 0.7184 0.6233 0.3914 0.0813  0.1201  -0.0709 88  HIS   A CE1  
596  N  NE2  . HIS   A 89  ? 0.7025 0.6418 0.3992 0.1006  0.1287  -0.0768 88  HIS   A NE2  
597  N  N    . THR   A 90  ? 0.6087 0.4539 0.3211 0.1133  0.064   -0.0543 89  THR   A N    
598  C  CA   . THR   A 90  ? 0.6148 0.4594 0.3405 0.1151  0.0543  -0.0472 89  THR   A CA   
599  C  C    . THR   A 90  ? 0.5754 0.4708 0.335  0.1296  0.0573  -0.0477 89  THR   A C    
600  O  O    . THR   A 90  ? 0.5759 0.4987 0.343  0.1475  0.0666  -0.0555 89  THR   A O    
601  C  CB   . THR   A 90  ? 0.6712 0.4613 0.3637 0.1261  0.0475  -0.0477 89  THR   A CB   
602  O  OG1  . THR   A 90  ? 0.6952 0.4811 0.377  0.1582  0.0525  -0.0551 89  THR   A OG1  
603  C  CG2  . THR   A 90  ? 0.7059 0.4474 0.364  0.1085  0.0441  -0.0491 89  THR   A CG2  
604  N  N    . PHE   A 91  ? 0.5334 0.4438 0.3135 0.1214  0.0495  -0.0401 90  PHE   A N    
605  C  CA   . PHE   A 91  ? 0.4843 0.4427 0.2962 0.1312  0.049   -0.0403 90  PHE   A CA   
606  C  C    . PHE   A 91  ? 0.4782 0.4189 0.2869 0.1363  0.0371  -0.0334 90  PHE   A C    
607  O  O    . PHE   A 91  ? 0.4939 0.4049 0.2914 0.1193  0.0313  -0.0263 90  PHE   A O    
608  C  CB   . PHE   A 91  ? 0.4564 0.4567 0.2967 0.1086  0.0535  -0.0382 90  PHE   A CB   
609  C  CG   . PHE   A 91  ? 0.4558 0.4732 0.2964 0.1017  0.0666  -0.0438 90  PHE   A CG   
610  C  CD1  . PHE   A 91  ? 0.4415 0.5057 0.3018 0.1124  0.0769  -0.0515 90  PHE   A CD1  
611  C  CD2  . PHE   A 91  ? 0.481  0.4693 0.3006 0.0853  0.0688  -0.0415 90  PHE   A CD2  
612  C  CE1  . PHE   A 91  ? 0.4417 0.5199 0.2986 0.1053  0.0912  -0.0564 90  PHE   A CE1  
613  C  CE2  . PHE   A 91  ? 0.4853 0.4843 0.2987 0.08    0.0812  -0.046  90  PHE   A CE2  
614  C  CZ   . PHE   A 91  ? 0.459  0.5014 0.2902 0.0891  0.0934  -0.0532 90  PHE   A CZ   
615  N  N    . VAL   A 92  ? 0.4526 0.4122 0.2695 0.1609  0.0335  -0.0356 91  VAL   A N    
616  C  CA   . VAL   A 92  ? 0.4486 0.3924 0.2597 0.1666  0.0223  -0.0286 91  VAL   A CA   
617  C  C    . VAL   A 92  ? 0.4302 0.4214 0.2752 0.1515  0.0195  -0.026  91  VAL   A C    
618  O  O    . VAL   A 92  ? 0.4119 0.4549 0.2839 0.1603  0.0208  -0.0317 91  VAL   A O    
619  C  CB   . VAL   A 92  ? 0.44   0.3765 0.238  0.2022  0.0171  -0.031  91  VAL   A CB   
620  C  CG1  . VAL   A 92  ? 0.4492 0.3634 0.2354 0.2044  0.0056  -0.0219 91  VAL   A CG1  
621  C  CG2  . VAL   A 92  ? 0.4661 0.3503 0.2254 0.2193  0.0211  -0.035  91  VAL   A CG2  
622  N  N    . VAL   A 93  ? 0.4258 0.4024 0.2699 0.128   0.0163  -0.0187 92  VAL   A N    
623  C  CA   . VAL   A 93  ? 0.3937 0.4071 0.264  0.1127  0.0142  -0.0169 92  VAL   A CA   
624  C  C    . VAL   A 93  ? 0.4025 0.3941 0.2632 0.1068  0.0059  -0.0087 92  VAL   A C    
625  O  O    . VAL   A 93  ? 0.429  0.3821 0.27   0.0972  0.0057  -0.0031 92  VAL   A O    
626  C  CB   . VAL   A 93  ? 0.3867 0.4109 0.2673 0.0881  0.0221  -0.0173 92  VAL   A CB   
627  C  CG1  . VAL   A 93  ? 0.3679 0.4285 0.2721 0.0738  0.0215  -0.0177 92  VAL   A CG1  
628  C  CG2  . VAL   A 93  ? 0.382  0.4142 0.2615 0.0911  0.0324  -0.024  92  VAL   A CG2  
629  N  N    . ASP   A 94  ? 0.3782 0.3976 0.253  0.1107  -0.0007 -0.0087 93  ASP   A N    
630  C  CA   . ASP   A 94  ? 0.3779 0.3825 0.2443 0.1044  -0.0075 -0.0017 93  ASP   A CA   
631  C  C    . ASP   A 94  ? 0.3755 0.3899 0.2543 0.0796  -0.0033 -0.0007 93  ASP   A C    
632  O  O    . ASP   A 94  ? 0.3608 0.4096 0.2595 0.0718  -0.0028 -0.0054 93  ASP   A O    
633  C  CB   . ASP   A 94  ? 0.369  0.4023 0.2442 0.1188  -0.017  -0.0037 93  ASP   A CB   
634  C  CG   . ASP   A 94  ? 0.407  0.4247 0.2692 0.1149  -0.0242 0.0029  93  ASP   A CG   
635  O  OD1  . ASP   A 94  ? 0.3994 0.3888 0.2498 0.0988  -0.0203 0.0089  93  ASP   A OD1  
636  O  OD2  . ASP   A 94  ? 0.4457 0.4822 0.3093 0.1286  -0.0338 0.0017  93  ASP   A OD2  
637  N  N    . CYS   A 95  ? 0.3864 0.3701 0.2518 0.0672  -0.0005 0.0051  94  CYS   A N    
638  C  CA   . CYS   A 95  ? 0.3887 0.3756 0.2609 0.0485  0.0032  0.0067  94  CYS   A CA   
639  C  C    . CYS   A 95  ? 0.3997 0.3901 0.2727 0.0426  -0.0005 0.0097  94  CYS   A C    
640  O  O    . CYS   A 95  ? 0.4152 0.4008 0.2882 0.0308  0.0023  0.012   94  CYS   A O    
641  C  CB   . CYS   A 95  ? 0.4144 0.3757 0.275  0.0402  0.0068  0.0104  94  CYS   A CB   
642  S  SG   . CYS   A 95  ? 0.4633 0.4177 0.3184 0.0449  0.0115  0.0053  94  CYS   A SG   
643  N  N    . GLY   A 96  ? 0.3832 0.3819 0.2548 0.053   -0.0071 0.0091  95  GLY   A N    
644  C  CA   . GLY   A 96  ? 0.3888 0.3931 0.2588 0.0493  -0.0115 0.01    95  GLY   A CA   
645  C  C    . GLY   A 96  ? 0.3794 0.4194 0.2654 0.0503  -0.0166 0.0023  95  GLY   A C    
646  O  O    . GLY   A 96  ? 0.3854 0.4323 0.2698 0.0447  -0.021  0.0008  95  GLY   A O    
647  N  N    . ASN   A 97  ? 0.3654 0.4308 0.267  0.0561  -0.0157 -0.0035 96  ASN   A N    
648  C  CA   . ASN   A 97  ? 0.3443 0.4545 0.2668 0.0559  -0.0196 -0.012  96  ASN   A CA   
649  C  C    . ASN   A 97  ? 0.3504 0.4782 0.2878 0.0361  -0.0104 -0.0172 96  ASN   A C    
650  O  O    . ASN   A 97  ? 0.3569 0.4879 0.2995 0.0374  -0.0026 -0.0185 96  ASN   A O    
651  C  CB   . ASN   A 97  ? 0.332  0.4619 0.261  0.0793  -0.0235 -0.015  96  ASN   A CB   
652  C  CG   . ASN   A 97  ? 0.3296 0.5146 0.2826 0.083   -0.0302 -0.0239 96  ASN   A CG   
653  O  OD1  . ASN   A 97  ? 0.3234 0.5445 0.2986 0.0702  -0.0242 -0.0311 96  ASN   A OD1  
654  N  ND2  . ASN   A 97  ? 0.3606 0.5555 0.309  0.0998  -0.0429 -0.0237 96  ASN   A ND2  
655  N  N    . ARG   A 98  ? 0.3494 0.4852 0.2894 0.0175  -0.011  -0.0204 97  ARG   A N    
656  C  CA   . ARG   A 98  ? 0.3624 0.5062 0.3089 -0.0047 -0.0023 -0.0245 97  ARG   A CA   
657  C  C    . ARG   A 98  ? 0.3614 0.5483 0.3307 -0.0065 0.0033  -0.0317 97  ARG   A C    
658  O  O    . ARG   A 98  ? 0.3625 0.5436 0.3309 -0.0158 0.0144  -0.0314 97  ARG   A O    
659  C  CB   . ARG   A 98  ? 0.3838 0.5277 0.3251 -0.0226 -0.0063 -0.0284 97  ARG   A CB   
660  C  CG   . ARG   A 98  ? 0.4517 0.5818 0.386  -0.0472 0.0034  -0.0301 97  ARG   A CG   
661  C  CD   . ARG   A 98  ? 0.5179 0.6416 0.4416 -0.0656 -0.0007 -0.0352 97  ARG   A CD   
662  N  NE   . ARG   A 98  ? 0.5684 0.7417 0.5128 -0.0718 -0.0086 -0.0447 97  ARG   A NE   
663  C  CZ   . ARG   A 98  ? 0.6093 0.8148 0.568  -0.0945 -0.0042 -0.0529 97  ARG   A CZ   
664  N  NH1  . ARG   A 98  ? 0.6077 0.7928 0.5567 -0.1141 0.0089  -0.0519 97  ARG   A NH1  
665  N  NH2  . ARG   A 98  ? 0.6028 0.8624 0.5845 -0.0985 -0.0131 -0.0622 97  ARG   A NH2  
666  N  N    . GLU   A 99  ? 0.3538 0.5861 0.3428 0.0036  -0.0043 -0.0382 98  GLU   A N    
667  C  CA   . GLU   A 99  ? 0.346  0.6302 0.361  0.0039  0.0012  -0.0463 98  GLU   A CA   
668  C  C    . GLU   A 99  ? 0.3551 0.6303 0.3679 0.0231  0.0092  -0.044  98  GLU   A C    
669  O  O    . GLU   A 99  ? 0.3474 0.6394 0.369  0.0143  0.0215  -0.0476 98  GLU   A O    
670  C  CB   . GLU   A 99  ? 0.3773 0.7158 0.4144 0.0156  -0.0114 -0.0538 98  GLU   A CB   
671  C  CG   . GLU   A 99  ? 0.4632 0.8694 0.5335 0.0118  -0.0054 -0.0641 98  GLU   A CG   
672  C  CD   . GLU   A 99  ? 0.5712 1.042  0.6677 0.0254  -0.0194 -0.0726 98  GLU   A CD   
673  O  OE1  . GLU   A 99  ? 0.6042 1.0635 0.6895 0.0359  -0.0351 -0.0702 98  GLU   A OE1  
674  O  OE2  . GLU   A 99  ? 0.5838 1.1195 0.7119 0.0262  -0.0147 -0.0817 98  GLU   A OE2  
675  N  N    . ASP   A 100 ? 0.3684 0.6122 0.365  0.0474  0.0029  -0.0381 99  ASP   A N    
676  C  CA   . ASP   A 100 ? 0.3728 0.5971 0.3596 0.0655  0.0091  -0.0362 99  ASP   A CA   
677  C  C    . ASP   A 100 ? 0.3831 0.5732 0.3557 0.0478  0.0205  -0.0322 99  ASP   A C    
678  O  O    . ASP   A 100 ? 0.3976 0.5941 0.3716 0.0502  0.0305  -0.0354 99  ASP   A O    
679  C  CB   . ASP   A 100 ? 0.414  0.6    0.3786 0.089   -0.0004 -0.0297 99  ASP   A CB   
680  C  CG   . ASP   A 100 ? 0.4834 0.6511 0.4353 0.1124  0.0033  -0.0301 99  ASP   A CG   
681  O  OD1  . ASP   A 100 ? 0.4827 0.6657 0.4425 0.1113  0.0139  -0.0352 99  ASP   A OD1  
682  O  OD2  . ASP   A 100 ? 0.5428 0.6772 0.4731 0.1315  -0.004  -0.0253 99  ASP   A OD2  
683  N  N    . ILE   A 101 ? 0.3812 0.5369 0.339  0.032   0.0191  -0.0258 100 ILE   A N    
684  C  CA   . ILE   A 101 ? 0.387  0.5114 0.3299 0.0179  0.0274  -0.0215 100 ILE   A CA   
685  C  C    . ILE   A 101 ? 0.3886 0.5353 0.3399 -0.0003 0.0389  -0.0263 100 ILE   A C    
686  O  O    . ILE   A 101 ? 0.4046 0.5421 0.3479 -0.0008 0.0479  -0.0261 100 ILE   A O    
687  C  CB   . ILE   A 101 ? 0.3908 0.482  0.319  0.0083  0.0228  -0.0147 100 ILE   A CB   
688  C  CG1  . ILE   A 101 ? 0.4012 0.4655 0.3168 0.0229  0.0155  -0.0088 100 ILE   A CG1  
689  C  CG2  . ILE   A 101 ? 0.4048 0.472  0.3197 -0.007  0.0301  -0.0112 100 ILE   A CG2  
690  C  CD1  . ILE   A 101 ? 0.4205 0.4651 0.3266 0.0163  0.0111  -0.0037 100 ILE   A CD1  
691  N  N    . TYR   A 102 ? 0.3689 0.5443 0.334  -0.0164 0.0391  -0.0309 101 TYR   A N    
692  C  CA   . TYR   A 102 ? 0.3631 0.5584 0.3337 -0.0381 0.0513  -0.0352 101 TYR   A CA   
693  C  C    . TYR   A 102 ? 0.3673 0.6028 0.3549 -0.0295 0.0606  -0.0418 101 TYR   A C    
694  O  O    . TYR   A 102 ? 0.3657 0.596  0.3449 -0.0401 0.0738  -0.0417 101 TYR   A O    
695  C  CB   . TYR   A 102 ? 0.3417 0.5583 0.3216 -0.0602 0.0489  -0.0399 101 TYR   A CB   
696  C  CG   . TYR   A 102 ? 0.3625 0.5324 0.3186 -0.0718 0.0441  -0.0342 101 TYR   A CG   
697  C  CD1  . TYR   A 102 ? 0.389  0.5088 0.3189 -0.071  0.0475  -0.0259 101 TYR   A CD1  
698  C  CD2  . TYR   A 102 ? 0.3639 0.5417 0.3225 -0.0827 0.0361  -0.0381 101 TYR   A CD2  
699  C  CE1  . TYR   A 102 ? 0.4182 0.4982 0.3266 -0.0771 0.0436  -0.0212 101 TYR   A CE1  
700  C  CE2  . TYR   A 102 ? 0.3967 0.5295 0.3303 -0.091  0.0329  -0.0339 101 TYR   A CE2  
701  C  CZ   . TYR   A 102 ? 0.429  0.5137 0.3382 -0.0865 0.0371  -0.0253 101 TYR   A CZ   
702  O  OH   . TYR   A 102 ? 0.4625 0.5052 0.347  -0.091  0.0349  -0.0217 101 TYR   A OH   
703  N  N    . ASN   A 103 ? 0.3589 0.6328 0.3675 -0.0082 0.0541  -0.0473 102 ASN   A N    
704  C  CA   . ASN   A 103 ? 0.3536 0.669  0.3791 0.0064  0.0628  -0.0546 102 ASN   A CA   
705  C  C    . ASN   A 103 ? 0.3723 0.6483 0.3745 0.0208  0.0693  -0.051  102 ASN   A C    
706  O  O    . ASN   A 103 ? 0.3645 0.6586 0.3692 0.021   0.0828  -0.0556 102 ASN   A O    
707  C  CB   . ASN   A 103 ? 0.3698 0.7258 0.4166 0.0334  0.0517  -0.06   102 ASN   A CB   
708  C  CG   . ASN   A 103 ? 0.4307 0.8528 0.51   0.0204  0.0492  -0.0684 102 ASN   A CG   
709  O  OD1  . ASN   A 103 ? 0.4562 0.9214 0.5538 0.0017  0.0621  -0.075  102 ASN   A OD1  
710  N  ND2  . ASN   A 103 ? 0.4365 0.8695 0.5225 0.0279  0.0327  -0.0687 102 ASN   A ND2  
711  N  N    . SER   A 104 ? 0.398  0.6215 0.3769 0.0315  0.0602  -0.0435 103 SER   A N    
712  C  CA   . SER   A 104 ? 0.4205 0.603  0.3745 0.0419  0.064   -0.0406 103 SER   A CA   
713  C  C    . SER   A 104 ? 0.4396 0.5966 0.3759 0.0203  0.0733  -0.0367 103 SER   A C    
714  O  O    . SER   A 104 ? 0.4557 0.5989 0.3768 0.0251  0.0813  -0.0381 103 SER   A O    
715  C  CB   . SER   A 104 ? 0.4537 0.5933 0.3898 0.0558  0.0516  -0.0344 103 SER   A CB   
716  O  OG   . SER   A 104 ? 0.4807 0.6378 0.4254 0.0803  0.0446  -0.0379 103 SER   A OG   
717  N  N    . VAL   A 105 ? 0.4429 0.5918 0.3774 -0.002  0.0725  -0.0322 104 VAL   A N    
718  C  CA   . VAL   A 105 ? 0.4627 0.5851 0.3763 -0.0208 0.0808  -0.0278 104 VAL   A CA   
719  C  C    . VAL   A 105 ? 0.4649 0.6174 0.3836 -0.031  0.0972  -0.0336 104 VAL   A C    
720  O  O    . VAL   A 105 ? 0.4848 0.6165 0.3821 -0.0333 0.1057  -0.032  104 VAL   A O    
721  C  CB   . VAL   A 105 ? 0.4712 0.5703 0.3757 -0.0388 0.076   -0.0216 104 VAL   A CB   
722  C  CG1  . VAL   A 105 ? 0.4896 0.5638 0.3703 -0.0572 0.0858  -0.0175 104 VAL   A CG1  
723  C  CG2  . VAL   A 105 ? 0.4851 0.5517 0.3799 -0.0278 0.0631  -0.0153 104 VAL   A CG2  
724  N  N    . LYS   A 106 ? 0.4427 0.6485 0.3903 -0.0353 0.1015  -0.0412 105 LYS   A N    
725  C  CA   . LYS   A 106 ? 0.4381 0.6854 0.3969 -0.0452 0.1187  -0.0482 105 LYS   A CA   
726  C  C    . LYS   A 106 ? 0.451  0.6995 0.4026 -0.0218 0.126   -0.0521 105 LYS   A C    
727  O  O    . LYS   A 106 ? 0.4568 0.7062 0.3956 -0.0303 0.1416  -0.0536 105 LYS   A O    
728  C  CB   . LYS   A 106 ? 0.4323 0.7469 0.43   -0.0484 0.1184  -0.0571 105 LYS   A CB   
729  C  CG   . LYS   A 106 ? 0.5196 0.8506 0.523  -0.0847 0.1247  -0.058  105 LYS   A CG   
730  C  CD   . LYS   A 106 ? 0.5875 0.967  0.6235 -0.0886 0.1136  -0.0646 105 LYS   A CD   
731  C  CE   . LYS   A 106 ? 0.6171 1.0799 0.6938 -0.0798 0.1188  -0.0763 105 LYS   A CE   
732  N  NZ   . LYS   A 106 ? 0.6341 1.141  0.7396 -0.0784 0.1031  -0.0821 105 LYS   A NZ   
733  N  N    . GLN   A 107 ? 0.4514 0.6955 0.4069 0.0075  0.115   -0.0539 106 GLN   A N    
734  C  CA   . GLN   A 107 ? 0.4647 0.7    0.4081 0.0329  0.1193  -0.0584 106 GLN   A CA   
735  C  C    . GLN   A 107 ? 0.4973 0.6746 0.4022 0.0276  0.1211  -0.0527 106 GLN   A C    
736  O  O    . GLN   A 107 ? 0.5205 0.6962 0.4106 0.0319  0.1336  -0.0569 106 GLN   A O    
737  C  CB   . GLN   A 107 ? 0.497  0.7257 0.4449 0.0619  0.1046  -0.0594 106 GLN   A CB   
738  C  CG   . GLN   A 107 ? 0.5504 0.8135 0.5098 0.0922  0.1098  -0.0693 106 GLN   A CG   
739  C  CD   . GLN   A 107 ? 0.6147 0.8615 0.5714 0.1209  0.0941  -0.0686 106 GLN   A CD   
740  O  OE1  . GLN   A 107 ? 0.6407 0.8635 0.5781 0.1483  0.0941  -0.0721 106 GLN   A OE1  
741  N  NE2  . GLN   A 107 ? 0.6137 0.8679 0.5845 0.1151  0.0806  -0.0639 106 GLN   A NE2  
742  N  N    . VAL   A 108 ? 0.5    0.6332 0.3887 0.0188  0.1088  -0.0436 107 VAL   A N    
743  C  CA   . VAL   A 108 ? 0.5204 0.6045 0.3753 0.0136  0.1074  -0.0382 107 VAL   A CA   
744  C  C    . VAL   A 108 ? 0.5454 0.6281 0.3847 -0.006  0.1214  -0.0366 107 VAL   A C    
745  O  O    . VAL   A 108 ? 0.5696 0.6304 0.3825 -0.0034 0.1272  -0.0375 107 VAL   A O    
746  C  CB   . VAL   A 108 ? 0.5236 0.5726 0.3704 0.0091  0.0917  -0.0295 107 VAL   A CB   
747  C  CG1  . VAL   A 108 ? 0.539  0.5472 0.3545 0.002   0.0893  -0.0241 107 VAL   A CG1  
748  C  CG2  . VAL   A 108 ? 0.5254 0.5671 0.3785 0.0276  0.0798  -0.0304 107 VAL   A CG2  
749  N  N    . LYS   A 109 ? 0.5387 0.6417 0.3899 -0.0266 0.1274  -0.0346 108 LYS   A N    
750  C  CA   . LYS   A 109 ? 0.5541 0.6506 0.3854 -0.0479 0.1422  -0.0321 108 LYS   A CA   
751  C  C    . LYS   A 109 ? 0.5618 0.6892 0.3944 -0.0433 0.1604  -0.0405 108 LYS   A C    
752  O  O    . LYS   A 109 ? 0.5857 0.692  0.3884 -0.0498 0.171   -0.0389 108 LYS   A O    
753  C  CB   . LYS   A 109 ? 0.5511 0.6637 0.3949 -0.0726 0.146   -0.0299 108 LYS   A CB   
754  C  CG   . LYS   A 109 ? 0.5904 0.6664 0.4243 -0.0791 0.1317  -0.0214 108 LYS   A CG   
755  C  CD   . LYS   A 109 ? 0.6212 0.7083 0.4605 -0.1052 0.1381  -0.021  108 LYS   A CD   
756  C  CE   . LYS   A 109 ? 0.6881 0.738  0.5151 -0.111  0.1257  -0.0139 108 LYS   A CE   
757  N  NZ   . LYS   A 109 ? 0.7206 0.8008 0.5736 -0.1229 0.1228  -0.019  108 LYS   A NZ   
758  N  N    . LYS   A 110 ? 0.5427 0.722  0.4093 -0.0305 0.1641  -0.0498 109 LYS   A N    
759  C  CA   . LYS   A 110 ? 0.5383 0.7585 0.4129 -0.0223 0.1822  -0.0596 109 LYS   A CA   
760  C  C    . LYS   A 110 ? 0.5609 0.7534 0.4105 0.0037  0.1826  -0.0637 109 LYS   A C    
761  O  O    . LYS   A 110 ? 0.5722 0.7782 0.4107 0.0068  0.2     -0.0697 109 LYS   A O    
762  C  CB   . LYS   A 110 ? 0.5293 0.8174 0.4504 -0.0119 0.1825  -0.0685 109 LYS   A CB   
763  C  CG   . LYS   A 110 ? 0.5743 0.923  0.5135 -0.0105 0.2043  -0.0789 109 LYS   A CG   
764  C  CD   . LYS   A 110 ? 0.623  1.026  0.5969 0.0224  0.2012  -0.0896 109 LYS   A CD   
765  C  CE   . LYS   A 110 ? 0.6717 1.1285 0.6568 0.0318  0.224   -0.1007 109 LYS   A CE   
766  N  NZ   . LYS   A 110 ? 0.7478 1.1573 0.6882 0.0348  0.237   -0.0999 109 LYS   A NZ   
767  N  N    . GLU   A 111 ? 0.5687 0.7224 0.4075 0.0209  0.1648  -0.0612 110 GLU   A N    
768  C  CA   . GLU   A 111 ? 0.5907 0.7135 0.4032 0.0439  0.1637  -0.0663 110 GLU   A CA   
769  C  C    . GLU   A 111 ? 0.6022 0.6645 0.3736 0.0361  0.1559  -0.06   110 GLU   A C    
770  O  O    . GLU   A 111 ? 0.6189 0.6559 0.3612 0.0476  0.1594  -0.0652 110 GLU   A O    
771  C  CB   . GLU   A 111 ? 0.6579 0.7772 0.4828 0.0697  0.1494  -0.0693 110 GLU   A CB   
772  C  CG   . GLU   A 111 ? 0.7698 0.9474 0.6295 0.089   0.1554  -0.078  110 GLU   A CG   
773  C  CD   . GLU   A 111 ? 0.9607 1.1224 0.8215 0.1177  0.1407  -0.0799 110 GLU   A CD   
774  O  OE1  . GLU   A 111 ? 1.0232 1.1284 0.8499 0.1279  0.1337  -0.0793 110 GLU   A OE1  
775  O  OE2  . GLU   A 111 ? 1.0068 1.2102 0.8997 0.1287  0.1357  -0.0818 110 GLU   A OE2  
776  N  N    . VAL   A 112 ? 0.5899 0.6289 0.3584 0.0198  0.1432  -0.0498 111 VAL   A N    
777  C  CA   . VAL   A 112 ? 0.5982 0.5873 0.3329 0.0143  0.1324  -0.0438 111 VAL   A CA   
778  C  C    . VAL   A 112 ? 0.5912 0.5673 0.3082 -0.0077 0.1361  -0.035  111 VAL   A C    
779  O  O    . VAL   A 112 ? 0.6107 0.5608 0.2928 -0.0114 0.1397  -0.0339 111 VAL   A O    
780  C  CB   . VAL   A 112 ? 0.5987 0.5667 0.3405 0.02    0.1122  -0.0398 111 VAL   A CB   
781  C  CG1  . VAL   A 112 ? 0.6284 0.5545 0.3398 0.0139  0.1002  -0.0349 111 VAL   A CG1  
782  C  CG2  . VAL   A 112 ? 0.5927 0.564  0.3433 0.042   0.1092  -0.0474 111 VAL   A CG2  
783  N  N    . GLY   A 113 ? 0.5641 0.5541 0.3007 -0.0212 0.1347  -0.0289 112 GLY   A N    
784  C  CA   . GLY   A 113 ? 0.5671 0.5378 0.2837 -0.0409 0.1376  -0.0199 112 GLY   A CA   
785  C  C    . GLY   A 113 ? 0.5603 0.5206 0.2884 -0.0465 0.1236  -0.0122 112 GLY   A C    
786  O  O    . GLY   A 113 ? 0.5447 0.5256 0.3035 -0.0407 0.1167  -0.0145 112 GLY   A O    
787  N  N    . ASP   A 114 ? 0.566  0.4921 0.2664 -0.0553 0.1192  -0.0031 113 ASP   A N    
788  C  CA   . ASP   A 114 ? 0.5648 0.4767 0.2701 -0.0583 0.1072  0.0042  113 ASP   A CA   
789  C  C    . ASP   A 114 ? 0.5454 0.4417 0.25   -0.0445 0.0885  0.0069  113 ASP   A C    
790  O  O    . ASP   A 114 ? 0.5716 0.4441 0.2489 -0.0408 0.0826  0.0103  113 ASP   A O    
791  C  CB   . ASP   A 114 ? 0.6257 0.5064 0.2981 -0.0726 0.1125  0.0128  113 ASP   A CB   
792  C  CG   . ASP   A 114 ? 0.7236 0.6195 0.3991 -0.0931 0.1308  0.0109  113 ASP   A CG   
793  O  OD1  . ASP   A 114 ? 0.7321 0.662  0.4425 -0.0975 0.1326  0.0053  113 ASP   A OD1  
794  O  OD2  . ASP   A 114 ? 0.7812 0.6548 0.4228 -0.1061 0.1428  0.0152  113 ASP   A OD2  
795  N  N    . VAL   A 115 ? 0.4907 0.4013 0.2239 -0.0381 0.0791  0.0057  114 VAL   A N    
796  C  CA   . VAL   A 115 ? 0.4679 0.3683 0.203  -0.0284 0.0631  0.0082  114 VAL   A CA   
797  C  C    . VAL   A 115 ? 0.4896 0.3661 0.2038 -0.0293 0.0551  0.017   114 VAL   A C    
798  O  O    . VAL   A 115 ? 0.5107 0.3775 0.2185 -0.0356 0.059   0.0218  114 VAL   A O    
799  C  CB   . VAL   A 115 ? 0.4286 0.3471 0.1947 -0.0237 0.057   0.0065  114 VAL   A CB   
800  C  CG1  . VAL   A 115 ? 0.4161 0.3264 0.1845 -0.0175 0.0427  0.01    114 VAL   A CG1  
801  C  CG2  . VAL   A 115 ? 0.4159 0.3551 0.1988 -0.0173 0.0623  -0.0016 114 VAL   A CG2  
802  N  N    . THR   A 116 ? 0.483  0.3495 0.1845 -0.0228 0.0438  0.0187  115 THR   A N    
803  C  CA   . THR   A 116 ? 0.4958 0.3453 0.179  -0.0186 0.0339  0.0266  115 THR   A CA   
804  C  C    . THR   A 116 ? 0.4755 0.3381 0.1796 -0.0112 0.0205  0.028   115 THR   A C    
805  O  O    . THR   A 116 ? 0.4911 0.3472 0.1902 -0.0051 0.0144  0.0341  115 THR   A O    
806  C  CB   . THR   A 116 ? 0.54   0.3709 0.1884 -0.0168 0.0304  0.0286  115 THR   A CB   
807  O  OG1  . THR   A 116 ? 0.5437 0.3754 0.1833 -0.0215 0.0397  0.0219  115 THR   A OG1  
808  C  CG2  . THR   A 116 ? 0.5969 0.3995 0.2128 -0.018  0.0347  0.0372  115 THR   A CG2  
809  N  N    . ILE   A 117 ? 0.4439 0.3228 0.1676 -0.0111 0.0162  0.0224  116 ILE   A N    
810  C  CA   . ILE   A 117 ? 0.4127 0.3067 0.1569 -0.0076 0.0058  0.0235  116 ILE   A CA   
811  C  C    . ILE   A 117 ? 0.3984 0.3037 0.1666 -0.0095 0.0105  0.0199  116 ILE   A C    
812  O  O    . ILE   A 117 ? 0.3988 0.3034 0.1681 -0.0114 0.0143  0.0143  116 ILE   A O    
813  C  CB   . ILE   A 117 ? 0.3943 0.2942 0.1342 -0.0085 -0.0063 0.0213  116 ILE   A CB   
814  C  CG1  . ILE   A 117 ? 0.3908 0.2824 0.1056 -0.0039 -0.0139 0.0252  116 ILE   A CG1  
815  C  CG2  . ILE   A 117 ? 0.3697 0.2907 0.1344 -0.009  -0.0141 0.0218  116 ILE   A CG2  
816  C  CD1  . ILE   A 117 ? 0.3908 0.2908 0.0995 -0.0068 -0.0266 0.0218  116 ILE   A CD1  
817  N  N    . LEU   A 118 ? 0.3886 0.3017 0.1723 -0.0071 0.0102  0.0231  117 LEU   A N    
818  C  CA   . LEU   A 118 ? 0.3909 0.3138 0.1942 -0.0077 0.0133  0.0206  117 LEU   A CA   
819  C  C    . LEU   A 118 ? 0.3945 0.3283 0.2108 -0.0068 0.0058  0.0222  117 LEU   A C    
820  O  O    . LEU   A 118 ? 0.4019 0.3425 0.2215 -0.0031 0.0016  0.0263  117 LEU   A O    
821  C  CB   . LEU   A 118 ? 0.3935 0.3167 0.202  -0.008  0.0193  0.022   117 LEU   A CB   
822  C  CG   . LEU   A 118 ? 0.4006 0.3354 0.2278 -0.0071 0.02    0.0201  117 LEU   A CG   
823  C  CD1  . LEU   A 118 ? 0.3959 0.3364 0.2291 -0.0063 0.0225  0.0148  117 LEU   A CD1  
824  C  CD2  . LEU   A 118 ? 0.4088 0.3427 0.2373 -0.0098 0.0244  0.0203  117 LEU   A CD2  
825  N  N    . VAL   A 119 ? 0.38   0.3141 0.2015 -0.0098 0.0051  0.019   118 VAL   A N    
826  C  CA   . VAL   A 119 ? 0.3698 0.3124 0.2013 -0.0131 0.0005  0.0206  118 VAL   A CA   
827  C  C    . VAL   A 119 ? 0.3654 0.3071 0.2056 -0.0109 0.0047  0.0207  118 VAL   A C    
828  O  O    . VAL   A 119 ? 0.3682 0.2986 0.2032 -0.0101 0.0067  0.0175  118 VAL   A O    
829  C  CB   . VAL   A 119 ? 0.3702 0.3066 0.1934 -0.0216 -0.0046 0.0174  118 VAL   A CB   
830  C  CG1  . VAL   A 119 ? 0.3607 0.309  0.1947 -0.0294 -0.0079 0.0196  118 VAL   A CG1  
831  C  CG2  . VAL   A 119 ? 0.3653 0.3022 0.1762 -0.0233 -0.0102 0.0162  118 VAL   A CG2  
832  N  N    . ASN   A 120 ? 0.3584 0.3102 0.2084 -0.0077 0.0057  0.0241  119 ASN   A N    
833  C  CA   . ASN   A 120 ? 0.3605 0.3127 0.2166 -0.0051 0.0084  0.0247  119 ASN   A CA   
834  C  C    . ASN   A 120 ? 0.3661 0.3184 0.2233 -0.0102 0.007   0.0269  119 ASN   A C    
835  O  O    . ASN   A 120 ? 0.3605 0.3247 0.2246 -0.011  0.0074  0.0301  119 ASN   A O    
836  C  CB   . ASN   A 120 ? 0.3534 0.3117 0.2137 -0.0008 0.0102  0.0265  119 ASN   A CB   
837  C  CG   . ASN   A 120 ? 0.3977 0.3513 0.2544 0       0.0135  0.0238  119 ASN   A CG   
838  O  OD1  . ASN   A 120 ? 0.431  0.38   0.2818 0.0006  0.0148  0.0249  119 ASN   A OD1  
839  N  ND2  . ASN   A 120 ? 0.3928 0.3474 0.2516 -0.0001 0.0154  0.02    119 ASN   A ND2  
840  N  N    . ASN   A 121 ? 0.3728 0.3095 0.2203 -0.014  0.0062  0.0251  120 ASN   A N    
841  C  CA   . ASN   A 121 ? 0.3883 0.3172 0.2302 -0.0232 0.0057  0.0272  120 ASN   A CA   
842  C  C    . ASN   A 121 ? 0.4159 0.3282 0.2488 -0.019  0.008   0.0293  120 ASN   A C    
843  O  O    . ASN   A 121 ? 0.4337 0.3433 0.2631 -0.0268 0.0097  0.0332  120 ASN   A O    
844  C  CB   . ASN   A 121 ? 0.4136 0.3274 0.2426 -0.0326 0.0027  0.0238  120 ASN   A CB   
845  C  CG   . ASN   A 121 ? 0.4583 0.355  0.2748 -0.0464 0.0028  0.0252  120 ASN   A CG   
846  O  OD1  . ASN   A 121 ? 0.4716 0.386  0.2966 -0.0596 0.0024  0.0275  120 ASN   A OD1  
847  N  ND2  . ASN   A 121 ? 0.471  0.3331 0.266  -0.0432 0.004   0.0238  120 ASN   A ND2  
848  N  N    . ALA   A 122 ? 0.4188 0.3222 0.2475 -0.0067 0.0082  0.0268  121 ALA   A N    
849  C  CA   . ALA   A 122 ? 0.4295 0.3173 0.247  0.0011  0.0081  0.0289  121 ALA   A CA   
850  C  C    . ALA   A 122 ? 0.4454 0.3416 0.2661 -0.0013 0.0096  0.0341  121 ALA   A C    
851  O  O    . ALA   A 122 ? 0.4426 0.3609 0.2779 -0.001  0.0105  0.0341  121 ALA   A O    
852  C  CB   . ALA   A 122 ? 0.4263 0.3196 0.2473 0.0166  0.0069  0.0247  121 ALA   A CB   
853  N  N    . GLY   A 123 ? 0.4542 0.3284 0.2569 -0.0047 0.0106  0.0386  122 GLY   A N    
854  C  CA   . GLY   A 123 ? 0.4528 0.3314 0.2531 -0.0078 0.0136  0.0439  122 GLY   A CA   
855  C  C    . GLY   A 123 ? 0.4802 0.3267 0.2531 -0.0034 0.0133  0.0486  122 GLY   A C    
856  O  O    . GLY   A 123 ? 0.501  0.3164 0.2536 -0.0008 0.0115  0.0485  122 GLY   A O    
857  N  N    . THR   A 124 ? 0.4751 0.3254 0.2429 -0.0013 0.0152  0.0527  123 THR   A N    
858  C  CA   . THR   A 124 ? 0.4998 0.3197 0.2378 0.004   0.0147  0.0587  123 THR   A CA   
859  C  C    . THR   A 124 ? 0.5052 0.3307 0.2374 -0.007  0.0224  0.0644  123 THR   A C    
860  O  O    . THR   A 124 ? 0.4789 0.3371 0.2333 -0.0106 0.026   0.0621  123 THR   A O    
861  C  CB   . THR   A 124 ? 0.5088 0.3302 0.244  0.0261  0.0061  0.0561  123 THR   A CB   
862  O  OG1  . THR   A 124 ? 0.5614 0.3455 0.2617 0.0358  0.0032  0.062   123 THR   A OG1  
863  C  CG2  . THR   A 124 ? 0.4816 0.3332 0.2326 0.0297  0.0048  0.0537  123 THR   A CG2  
864  N  N    . VAL   A 125 ? 0.5347 0.3253 0.2335 -0.0117 0.0259  0.0719  124 VAL   A N    
865  C  CA   . VAL   A 125 ? 0.5443 0.336  0.2313 -0.0233 0.0354  0.0782  124 VAL   A CA   
866  C  C    . VAL   A 125 ? 0.6008 0.3469 0.2431 -0.0172 0.0346  0.0863  124 VAL   A C    
867  O  O    . VAL   A 125 ? 0.6374 0.3435 0.2543 -0.0122 0.03    0.0886  124 VAL   A O    
868  C  CB   . VAL   A 125 ? 0.5353 0.3387 0.2316 -0.0494 0.0459  0.0796  124 VAL   A CB   
869  C  CG1  . VAL   A 125 ? 0.5675 0.3289 0.2379 -0.0631 0.0464  0.0826  124 VAL   A CG1  
870  C  CG2  . VAL   A 125 ? 0.5333 0.3509 0.2248 -0.0611 0.0581  0.0848  124 VAL   A CG2  
871  N  N    . TYR   A 126 ? 0.6069 0.3556 0.2356 -0.015  0.0387  0.0906  125 TYR   A N    
872  C  CA   . TYR   A 126 ? 0.6515 0.3557 0.2328 -0.0096 0.0385  0.0996  125 TYR   A CA   
873  C  C    . TYR   A 126 ? 0.6706 0.3796 0.2402 -0.0283 0.0538  0.1057  125 TYR   A C    
874  O  O    . TYR   A 126 ? 0.6749 0.4003 0.2426 -0.0207 0.0553  0.1054  125 TYR   A O    
875  C  CB   . TYR   A 126 ? 0.652  0.3569 0.2251 0.0177  0.0248  0.0976  125 TYR   A CB   
876  C  CG   . TYR   A 126 ? 0.6544 0.366  0.2451 0.0359  0.0114  0.0905  125 TYR   A CG   
877  C  CD1  . TYR   A 126 ? 0.6859 0.3561 0.2484 0.0482  0.0049  0.0939  125 TYR   A CD1  
878  C  CD2  . TYR   A 126 ? 0.6283 0.3859 0.2625 0.0396  0.007   0.0803  125 TYR   A CD2  
879  C  CE1  . TYR   A 126 ? 0.6841 0.3649 0.2649 0.0651  -0.0049 0.0865  125 TYR   A CE1  
880  C  CE2  . TYR   A 126 ? 0.6259 0.3933 0.277  0.0536  -0.0027 0.0737  125 TYR   A CE2  
881  C  CZ   . TYR   A 126 ? 0.6574 0.3896 0.2836 0.0671  -0.0083 0.0765  125 TYR   A CZ   
882  O  OH   . TYR   A 126 ? 0.6858 0.431  0.3283 0.0834  -0.0165 0.0695  125 TYR   A OH   
883  N  N    . PRO   A 127 ? 0.6792 0.3774 0.2418 -0.0544 0.0661  0.1101  126 PRO   A N    
884  C  CA   . PRO   A 127 ? 0.6813 0.3939 0.2382 -0.0746 0.0832  0.1151  126 PRO   A CA   
885  C  C    . PRO   A 127 ? 0.7273 0.4048 0.2366 -0.0681 0.0867  0.1241  126 PRO   A C    
886  O  O    . PRO   A 127 ? 0.7734 0.396  0.2399 -0.0598 0.0797  0.1308  126 PRO   A O    
887  C  CB   . PRO   A 127 ? 0.6904 0.3867 0.2397 -0.1052 0.093   0.1187  126 PRO   A CB   
888  C  CG   . PRO   A 127 ? 0.685  0.3829 0.2568 -0.1007 0.0812  0.1113  126 PRO   A CG   
889  C  CD   . PRO   A 127 ? 0.6795 0.3549 0.2396 -0.0685 0.0656  0.1097  126 PRO   A CD   
890  N  N    . ALA   A 128 ? 0.7076 0.4151 0.2223 -0.0677 0.0959  0.1236  127 ALA   A N    
891  C  CA   . ALA   A 128 ? 0.7283 0.4095 0.1981 -0.0623 0.101   0.1313  127 ALA   A CA   
892  C  C    . ALA   A 128 ? 0.7235 0.453  0.2148 -0.0616 0.112   0.126   127 ALA   A C    
893  O  O    . ALA   A 128 ? 0.7032 0.4784 0.2397 -0.0534 0.108   0.1155  127 ALA   A O    
894  C  CB   . ALA   A 128 ? 0.7335 0.385  0.1785 -0.0329 0.0812  0.1314  127 ALA   A CB   
895  N  N    . ASP   A 129 ? 0.7479 0.4636 0.2026 -0.0676 0.1254  0.133   128 ASP   A N    
896  C  CA   . ASP   A 129 ? 0.7429 0.4992 0.2112 -0.0622 0.1357  0.1272  128 ASP   A CA   
897  C  C    . ASP   A 129 ? 0.7473 0.5021 0.2139 -0.0332 0.1169  0.1195  128 ASP   A C    
898  O  O    . ASP   A 129 ? 0.7808 0.501  0.2253 -0.0201 0.0994  0.122   128 ASP   A O    
899  C  CB   . ASP   A 129 ? 0.7966 0.5404 0.2255 -0.0775 0.1572  0.1362  128 ASP   A CB   
900  C  CG   . ASP   A 129 ? 0.9114 0.6012 0.2785 -0.0657 0.1512  0.1445  128 ASP   A CG   
901  O  OD1  . ASP   A 129 ? 0.9587 0.5956 0.2887 -0.0687 0.1443  0.1542  128 ASP   A OD1  
902  O  OD2  . ASP   A 129 ? 0.9574 0.6555 0.3097 -0.052  0.1529  0.1409  128 ASP   A OD2  
903  N  N    . LEU   A 130 ? 0.7086 0.5016 0.1995 -0.0232 0.1194  0.1093  129 LEU   A N    
904  C  CA   . LEU   A 130 ? 0.7041 0.4991 0.1974 -0.0012 0.1021  0.0999  129 LEU   A CA   
905  C  C    . LEU   A 130 ? 0.7376 0.4924 0.1833 0.0115  0.0884  0.1042  129 LEU   A C    
906  O  O    . LEU   A 130 ? 0.7324 0.4817 0.1836 0.0253  0.0677  0.0998  129 LEU   A O    
907  C  CB   . LEU   A 130 ? 0.6891 0.5166 0.1966 0.0056  0.1115  0.09    129 LEU   A CB   
908  C  CG   . LEU   A 130 ? 0.6988 0.5318 0.217  0.0229  0.0947  0.0779  129 LEU   A CG   
909  C  CD1  . LEU   A 130 ? 0.674  0.5238 0.2349 0.0236  0.0832  0.0727  129 LEU   A CD1  
910  C  CD2  . LEU   A 130 ? 0.7082 0.5583 0.2245 0.0304  0.1054  0.0691  129 LEU   A CD2  
911  N  N    . LEU   A 131 ? 0.7696 0.4982 0.1682 0.0067  0.0997  0.1132  130 LEU   A N    
912  C  CA   . LEU   A 131 ? 0.8052 0.4954 0.1535 0.0206  0.0861  0.1178  130 LEU   A CA   
913  C  C    . LEU   A 131 ? 0.8359 0.4853 0.1612 0.0247  0.0727  0.1278  130 LEU   A C    
914  O  O    . LEU   A 131 ? 0.8671 0.4907 0.1583 0.0423  0.0553  0.1301  130 LEU   A O    
915  C  CB   . LEU   A 131 ? 0.8277 0.5017 0.1292 0.0158  0.1029  0.1237  130 LEU   A CB   
916  C  CG   . LEU   A 131 ? 0.8401 0.5366 0.1406 0.0264  0.1043  0.1117  130 LEU   A CG   
917  C  CD1  . LEU   A 131 ? 0.8119 0.5556 0.1685 0.0262  0.1095  0.0985  130 LEU   A CD1  
918  C  CD2  . LEU   A 131 ? 0.8679 0.5487 0.1204 0.0206  0.1246  0.1179  130 LEU   A CD2  
919  N  N    . SER   A 132 ? 0.8194 0.464  0.163  0.0104  0.0791  0.1326  131 SER   A N    
920  C  CA   . SER   A 132 ? 0.8484 0.4506 0.1699 0.0159  0.0672  0.1407  131 SER   A CA   
921  C  C    . SER   A 132 ? 0.8376 0.4618 0.204  0.0282  0.0494  0.1313  131 SER   A C    
922  O  O    . SER   A 132 ? 0.874  0.4669 0.2275 0.034   0.0409  0.1363  131 SER   A O    
923  C  CB   . SER   A 132 ? 0.8803 0.4543 0.1859 -0.0096 0.0852  0.1514  131 SER   A CB   
924  O  OG   . SER   A 132 ? 0.9405 0.4806 0.1926 -0.0217 0.101   0.163   131 SER   A OG   
925  N  N    . THR   A 133 ? 0.7828 0.4566 0.198  0.0316  0.0455  0.1182  132 THR   A N    
926  C  CA   . THR   A 133 ? 0.7538 0.4499 0.2101 0.0409  0.031   0.1095  132 THR   A CA   
927  C  C    . THR   A 133 ? 0.7594 0.4551 0.2075 0.0651  0.0082  0.105   132 THR   A C    
928  O  O    . THR   A 133 ? 0.7586 0.4502 0.1798 0.0742  0.0021  0.1046  132 THR   A O    
929  C  CB   . THR   A 133 ? 0.7245 0.469  0.2315 0.0332  0.037   0.0983  132 THR   A CB   
930  O  OG1  . THR   A 133 ? 0.7389 0.4985 0.2394 0.0381  0.038   0.0925  132 THR   A OG1  
931  C  CG2  . THR   A 133 ? 0.709  0.465  0.234  0.012   0.0561  0.1011  132 THR   A CG2  
932  N  N    . LYS   A 134 ? 0.7563 0.4594 0.2277 0.0755  -0.0047 0.101   133 LYS   A N    
933  C  CA   . LYS   A 134 ? 0.7602 0.4776 0.2346 0.0978  -0.0264 0.0947  133 LYS   A CA   
934  C  C    . LYS   A 134 ? 0.722  0.4896 0.2469 0.0929  -0.0293 0.0805  133 LYS   A C    
935  O  O    . LYS   A 134 ? 0.7159 0.4986 0.2744 0.081   -0.0203 0.0773  133 LYS   A O    
936  C  CB   . LYS   A 134 ? 0.808  0.5056 0.2764 0.1143  -0.0372 0.0983  133 LYS   A CB   
937  C  CG   . LYS   A 134 ? 0.9609 0.5977 0.3702 0.1203  -0.0349 0.113   133 LYS   A CG   
938  C  CD   . LYS   A 134 ? 1.0707 0.675  0.4697 0.1313  -0.0387 0.1174  133 LYS   A CD   
939  C  CE   . LYS   A 134 ? 1.1837 0.7201 0.526  0.122   -0.0268 0.1323  133 LYS   A CE   
940  N  NZ   . LYS   A 134 ? 1.2234 0.7574 0.5822 0.0892  -0.006  0.1334  133 LYS   A NZ   
941  N  N    . ASP   A 135 ? 0.6972 0.4875 0.224  0.1     -0.0415 0.072   134 ASP   A N    
942  C  CA   . ASP   A 135 ? 0.6692 0.499  0.2364 0.0923  -0.0432 0.0588  134 ASP   A CA   
943  C  C    . ASP   A 135 ? 0.6505 0.5044 0.259  0.0935  -0.0479 0.0534  134 ASP   A C    
944  O  O    . ASP   A 135 ? 0.6301 0.5047 0.2707 0.0816  -0.0412 0.0466  134 ASP   A O    
945  C  CB   . ASP   A 135 ? 0.6853 0.5311 0.2422 0.0977  -0.0575 0.05    134 ASP   A CB   
946  C  CG   . ASP   A 135 ? 0.7537 0.5787 0.2719 0.0944  -0.0507 0.0524  134 ASP   A CG   
947  O  OD1  . ASP   A 135 ? 0.7649 0.5741 0.2756 0.0844  -0.0315 0.0582  134 ASP   A OD1  
948  O  OD2  . ASP   A 135 ? 0.7811 0.6089 0.2773 0.1016  -0.0645 0.0478  134 ASP   A OD2  
949  N  N    . GLU   A 136 ? 0.6509 0.4982 0.254  0.1096  -0.0583 0.057   135 GLU   A N    
950  C  CA   . GLU   A 136 ? 0.631  0.4977 0.2664 0.1149  -0.0622 0.0526  135 GLU   A CA   
951  C  C    . GLU   A 136 ? 0.6186 0.4711 0.2666 0.1014  -0.0464 0.0564  135 GLU   A C    
952  O  O    . GLU   A 136 ? 0.6076 0.4827 0.2889 0.0966  -0.0447 0.0501  135 GLU   A O    
953  C  CB   . GLU   A 136 ? 0.6855 0.5415 0.303  0.14    -0.0759 0.0566  135 GLU   A CB   
954  C  CG   . GLU   A 136 ? 0.8252 0.6933 0.4235 0.1563  -0.0938 0.0546  135 GLU   A CG   
955  C  CD   . GLU   A 136 ? 1.0057 0.8342 0.5526 0.159   -0.0935 0.0644  135 GLU   A CD   
956  O  OE1  . GLU   A 136 ? 1.0894 0.8696 0.6014 0.1619  -0.0855 0.0768  135 GLU   A OE1  
957  O  OE2  . GLU   A 136 ? 1.0144 0.8582 0.5528 0.157   -0.1011 0.0595  135 GLU   A OE2  
958  N  N    . GLU   A 137 ? 0.6257 0.4421 0.2461 0.0936  -0.0349 0.0666  136 GLU   A N    
959  C  CA   . GLU   A 137 ? 0.613  0.4184 0.2435 0.0777  -0.0204 0.07    136 GLU   A CA   
960  C  C    . GLU   A 137 ? 0.5702 0.4044 0.2302 0.0619  -0.0111 0.0639  136 GLU   A C    
961  O  O    . GLU   A 137 ? 0.5589 0.4044 0.2445 0.0531  -0.0055 0.0613  136 GLU   A O    
962  C  CB   . GLU   A 137 ? 0.7005 0.4629 0.2918 0.0708  -0.0108 0.082   136 GLU   A CB   
963  C  CG   . GLU   A 137 ? 0.8185 0.54   0.3743 0.0868  -0.0187 0.0892  136 GLU   A CG   
964  C  CD   . GLU   A 137 ? 0.99   0.661  0.4968 0.0786  -0.0093 0.1021  136 GLU   A CD   
965  O  OE1  . GLU   A 137 ? 1.0591 0.7324 0.5544 0.0668  0       0.1053  136 GLU   A OE1  
966  O  OE2  . GLU   A 137 ? 1.0274 0.6537 0.5038 0.0842  -0.0103 0.1088  136 GLU   A OE2  
967  N  N    . ILE   A 138 ? 0.5547 0.3984 0.208  0.0601  -0.01   0.0613  137 ILE   A N    
968  C  CA   . ILE   A 138 ? 0.5291 0.3953 0.2046 0.0499  -0.0019 0.0549  137 ILE   A CA   
969  C  C    . ILE   A 138 ? 0.5129 0.4047 0.2203 0.0507  -0.0093 0.0451  137 ILE   A C    
970  O  O    . ILE   A 138 ? 0.5185 0.4219 0.2487 0.0429  -0.0026 0.0424  137 ILE   A O    
971  C  CB   . ILE   A 138 ? 0.5222 0.386  0.1758 0.0509  0       0.0533  137 ILE   A CB   
972  C  CG1  . ILE   A 138 ? 0.5412 0.3809 0.163  0.0472  0.0111  0.0636  137 ILE   A CG1  
973  C  CG2  . ILE   A 138 ? 0.5169 0.3986 0.1888 0.0448  0.0069  0.0454  137 ILE   A CG2  
974  C  CD1  . ILE   A 138 ? 0.5581 0.3898 0.1482 0.0507  0.0128  0.0628  137 ILE   A CD1  
975  N  N    . THR   A 139 ? 0.5032 0.4051 0.2112 0.06    -0.0231 0.0401  138 THR   A N    
976  C  CA   . THR   A 139 ? 0.4822 0.4111 0.2187 0.0589  -0.03   0.0308  138 THR   A CA   
977  C  C    . THR   A 139 ? 0.4694 0.4016 0.2268 0.058   -0.0263 0.032   138 THR   A C    
978  O  O    . THR   A 139 ? 0.4614 0.4067 0.2406 0.0492  -0.0217 0.0274  138 THR   A O    
979  C  CB   . THR   A 139 ? 0.4982 0.4425 0.2303 0.0697  -0.046  0.026   138 THR   A CB   
980  O  OG1  . THR   A 139 ? 0.5127 0.4566 0.2278 0.0664  -0.0496 0.0219  138 THR   A OG1  
981  C  CG2  . THR   A 139 ? 0.4944 0.4721 0.258  0.0683  -0.0524 0.0169  138 THR   A CG2  
982  N  N    . LYS   A 140 ? 0.4768 0.3918 0.2225 0.0672  -0.0279 0.0385  139 LYS   A N    
983  C  CA   . LYS   A 140 ? 0.4844 0.3966 0.2435 0.0671  -0.0245 0.0391  139 LYS   A CA   
984  C  C    . LYS   A 140 ? 0.4804 0.3868 0.2477 0.0517  -0.0122 0.0415  139 LYS   A C    
985  O  O    . LYS   A 140 ? 0.4882 0.4056 0.2756 0.0469  -0.0097 0.0378  139 LYS   A O    
986  C  CB   . LYS   A 140 ? 0.5514 0.4348 0.2859 0.0803  -0.028  0.0458  139 LYS   A CB   
987  C  CG   . LYS   A 140 ? 0.6329 0.5321 0.3739 0.0998  -0.0397 0.0409  139 LYS   A CG   
988  C  CD   . LYS   A 140 ? 0.7201 0.5883 0.4258 0.1199  -0.0474 0.0479  139 LYS   A CD   
989  C  CE   . LYS   A 140 ? 0.8047 0.6356 0.4924 0.1264  -0.0434 0.0526  139 LYS   A CE   
990  N  NZ   . LYS   A 140 ? 0.859  0.6437 0.5004 0.1426  -0.0484 0.062   139 LYS   A NZ   
991  N  N    . THR   A 141 ? 0.4759 0.3692 0.2285 0.0441  -0.0046 0.0471  140 THR   A N    
992  C  CA   . THR   A 141 ? 0.4664 0.3632 0.2297 0.0309  0.0062  0.0488  140 THR   A CA   
993  C  C    . THR   A 141 ? 0.46   0.3803 0.2471 0.0279  0.0071  0.0417  140 THR   A C    
994  O  O    . THR   A 141 ? 0.4561 0.3834 0.2591 0.0228  0.0097  0.0404  140 THR   A O    
995  C  CB   . THR   A 141 ? 0.4854 0.3728 0.2308 0.0246  0.015   0.0549  140 THR   A CB   
996  O  OG1  . THR   A 141 ? 0.5291 0.3871 0.2456 0.0263  0.0144  0.0625  140 THR   A OG1  
997  C  CG2  . THR   A 141 ? 0.4704 0.3708 0.2305 0.0121  0.0258  0.0562  140 THR   A CG2  
998  N  N    . PHE   A 142 ? 0.456  0.3845 0.2415 0.031   0.0036  0.0367  141 PHE   A N    
999  C  CA   . PHE   A 142 ? 0.4332 0.3743 0.2332 0.0275  0.0045  0.03    141 PHE   A CA   
1000 C  C    . PHE   A 142 ? 0.4238 0.3758 0.241  0.0264  -0.0003 0.0252  141 PHE   A C    
1001 O  O    . PHE   A 142 ? 0.4268 0.3828 0.2556 0.0215  0.0034  0.0234  141 PHE   A O    
1002 C  CB   . PHE   A 142 ? 0.4274 0.3674 0.2149 0.0287  0.0023  0.0251  141 PHE   A CB   
1003 C  CG   . PHE   A 142 ? 0.4346 0.3682 0.2115 0.0288  0.0121  0.0278  141 PHE   A CG   
1004 C  CD1  . PHE   A 142 ? 0.4532 0.379  0.2127 0.0307  0.0164  0.0336  141 PHE   A CD1  
1005 C  CD2  . PHE   A 142 ? 0.4362 0.3722 0.2201 0.0281  0.0183  0.0251  141 PHE   A CD2  
1006 C  CE1  . PHE   A 142 ? 0.4599 0.3867 0.2129 0.0307  0.0277  0.0358  141 PHE   A CE1  
1007 C  CE2  . PHE   A 142 ? 0.4473 0.3838 0.2247 0.0317  0.028   0.0271  141 PHE   A CE2  
1008 C  CZ   . PHE   A 142 ? 0.4529 0.3879 0.2168 0.0324  0.0333  0.032   141 PHE   A CZ   
1009 N  N    . GLU   A 143 ? 0.4097 0.3678 0.2273 0.0323  -0.0084 0.0232  142 GLU   A N    
1010 C  CA   . GLU   A 143 ? 0.3922 0.3669 0.2271 0.0323  -0.0117 0.0179  142 GLU   A CA   
1011 C  C    . GLU   A 143 ? 0.3913 0.3613 0.2344 0.0308  -0.0065 0.0203  142 GLU   A C    
1012 O  O    . GLU   A 143 ? 0.4008 0.3804 0.2566 0.0251  -0.004  0.0165  142 GLU   A O    
1013 C  CB   . GLU   A 143 ? 0.3926 0.3795 0.2268 0.0435  -0.0215 0.0156  142 GLU   A CB   
1014 C  CG   . GLU   A 143 ? 0.419  0.4223 0.2524 0.0413  -0.029  0.0092  142 GLU   A CG   
1015 C  CD   . GLU   A 143 ? 0.5126 0.5319 0.3438 0.0553  -0.0411 0.0074  142 GLU   A CD   
1016 O  OE1  . GLU   A 143 ? 0.5367 0.5441 0.3589 0.0699  -0.0431 0.013   142 GLU   A OE1  
1017 O  OE2  . GLU   A 143 ? 0.5398 0.582  0.3756 0.0518  -0.0493 0.0001  142 GLU   A OE2  
1018 N  N    . ILE   A 144 ? 0.391  0.3435 0.2237 0.0338  -0.0045 0.0266  143 ILE   A N    
1019 C  CA   . ILE   A 144 ? 0.3958 0.3411 0.2326 0.0306  -0.0006 0.028   143 ILE   A CA   
1020 C  C    . ILE   A 144 ? 0.3989 0.3438 0.24   0.0204  0.0056  0.0302  143 ILE   A C    
1021 O  O    . ILE   A 144 ? 0.4074 0.3567 0.2573 0.0166  0.0073  0.0283  143 ILE   A O    
1022 C  CB   . ILE   A 144 ? 0.4177 0.3398 0.2371 0.0365  -0.0018 0.0326  143 ILE   A CB   
1023 C  CG1  . ILE   A 144 ? 0.4345 0.3582 0.2483 0.0526  -0.0094 0.0304  143 ILE   A CG1  
1024 C  CG2  . ILE   A 144 ? 0.4249 0.3358 0.2444 0.031   0.0016  0.0327  143 ILE   A CG2  
1025 C  CD1  . ILE   A 144 ? 0.4705 0.3636 0.2588 0.0615  -0.0115 0.0359  143 ILE   A CD1  
1026 N  N    . ASN   A 145 ? 0.4015 0.343  0.2358 0.0173  0.009   0.0343  144 ASN   A N    
1027 C  CA   . ASN   A 145 ? 0.3995 0.3473 0.2401 0.0104  0.0145  0.0364  144 ASN   A CA   
1028 C  C    . ASN   A 145 ? 0.4034 0.3618 0.2524 0.0116  0.0158  0.033   144 ASN   A C    
1029 O  O    . ASN   A 145 ? 0.4101 0.376  0.2658 0.0095  0.0184  0.0343  144 ASN   A O    
1030 C  CB   . ASN   A 145 ? 0.4018 0.3475 0.2337 0.0066  0.0198  0.0416  144 ASN   A CB   
1031 C  CG   . ASN   A 145 ? 0.4502 0.3776 0.2676 0.0015  0.0205  0.0465  144 ASN   A CG   
1032 O  OD1  . ASN   A 145 ? 0.4811 0.4042 0.2877 -0.0043 0.0261  0.0514  144 ASN   A OD1  
1033 N  ND2  . ASN   A 145 ? 0.4446 0.3573 0.2572 0.0035  0.0159  0.0455  144 ASN   A ND2  
1034 N  N    . ILE   A 146 ? 0.393  0.3508 0.2394 0.0146  0.0135  0.0287  145 ILE   A N    
1035 C  CA   . ILE   A 146 ? 0.388  0.3453 0.2349 0.0146  0.0154  0.0257  145 ILE   A CA   
1036 C  C    . ILE   A 146 ? 0.3853 0.3411 0.2322 0.0108  0.0124  0.0199  145 ILE   A C    
1037 O  O    . ILE   A 146 ? 0.3808 0.3334 0.2291 0.0074  0.0139  0.0187  145 ILE   A O    
1038 C  CB   . ILE   A 146 ? 0.3934 0.3477 0.2311 0.0194  0.0195  0.0261  145 ILE   A CB   
1039 C  CG1  . ILE   A 146 ? 0.4009 0.345  0.232  0.0221  0.0211  0.023   145 ILE   A CG1  
1040 C  CG2  . ILE   A 146 ? 0.4095 0.3593 0.2354 0.0208  0.0182  0.0247  145 ILE   A CG2  
1041 C  CD1  . ILE   A 146 ? 0.3965 0.3436 0.2344 0.0237  0.0216  0.0255  145 ILE   A CD1  
1042 N  N    . LEU   A 147 ? 0.3799 0.3399 0.2247 0.0103  0.008   0.0164  146 LEU   A N    
1043 C  CA   . LEU   A 147 ? 0.3713 0.3379 0.2194 0.0034  0.0054  0.0098  146 LEU   A CA   
1044 C  C    . LEU   A 147 ? 0.3647 0.3416 0.2255 0.0004  0.0066  0.0089  146 LEU   A C    
1045 O  O    . LEU   A 147 ? 0.3633 0.3393 0.2243 -0.0083 0.0096  0.0058  146 LEU   A O    
1046 C  CB   . LEU   A 147 ? 0.3684 0.3456 0.2146 0.0043  -0.0015 0.0057  146 LEU   A CB   
1047 C  CG   . LEU   A 147 ? 0.4114 0.3756 0.24   0.0048  -0.0022 0.0045  146 LEU   A CG   
1048 C  CD1  . LEU   A 147 ? 0.4201 0.3943 0.2436 0.0086  -0.0108 0.0021  146 LEU   A CD1  
1049 C  CD2  . LEU   A 147 ? 0.4278 0.3781 0.2461 -0.0049 0.0005  -0.0009 146 LEU   A CD2  
1050 N  N    . GLY   A 148 ? 0.3657 0.3468 0.2321 0.0073  0.0056  0.012   147 GLY   A N    
1051 C  CA   . GLY   A 148 ? 0.365  0.353  0.2397 0.0073  0.0075  0.0107  147 GLY   A CA   
1052 C  C    . GLY   A 148 ? 0.3802 0.3584 0.252  0.0015  0.0126  0.0125  147 GLY   A C    
1053 O  O    . GLY   A 148 ? 0.3898 0.3733 0.2648 -0.0033 0.0158  0.0096  147 GLY   A O    
1054 N  N    . HIS   A 149 ? 0.381  0.3469 0.2459 0.0027  0.0135  0.0171  148 HIS   A N    
1055 C  CA   . HIS   A 149 ? 0.3841 0.341  0.2436 0.0005  0.0162  0.0192  148 HIS   A CA   
1056 C  C    . HIS   A 149 ? 0.391  0.3394 0.2422 -0.0065 0.0193  0.0162  148 HIS   A C    
1057 O  O    . HIS   A 149 ? 0.3975 0.3391 0.2429 -0.0105 0.0222  0.0167  148 HIS   A O    
1058 C  CB   . HIS   A 149 ? 0.3876 0.3402 0.2432 0.0058  0.016   0.0235  148 HIS   A CB   
1059 C  CG   . HIS   A 149 ? 0.3862 0.3465 0.2479 0.0074  0.0146  0.0268  148 HIS   A CG   
1060 N  ND1  . HIS   A 149 ? 0.4    0.3664 0.2638 0.0097  0.0146  0.0301  148 HIS   A ND1  
1061 C  CD2  . HIS   A 149 ? 0.3905 0.352  0.2546 0.0063  0.0133  0.0271  148 HIS   A CD2  
1062 C  CE1  . HIS   A 149 ? 0.3998 0.3724 0.2682 0.0057  0.014   0.0319  148 HIS   A CE1  
1063 N  NE2  . HIS   A 149 ? 0.4039 0.3686 0.2694 0.004   0.0133  0.0306  148 HIS   A NE2  
1064 N  N    . PHE   A 150 ? 0.3953 0.3404 0.2419 -0.0093 0.0188  0.0133  149 PHE   A N    
1065 C  CA   . PHE   A 150 ? 0.4141 0.3458 0.2484 -0.0199 0.0218  0.0098  149 PHE   A CA   
1066 C  C    . PHE   A 150 ? 0.4085 0.3558 0.2518 -0.0314 0.0246  0.0056  149 PHE   A C    
1067 O  O    . PHE   A 150 ? 0.418  0.3521 0.25   -0.0408 0.03    0.0057  149 PHE   A O    
1068 C  CB   . PHE   A 150 ? 0.4184 0.3445 0.245  -0.0226 0.0195  0.0057  149 PHE   A CB   
1069 C  CG   . PHE   A 150 ? 0.4399 0.3437 0.2498 -0.0129 0.0202  0.0084  149 PHE   A CG   
1070 C  CD1  . PHE   A 150 ? 0.4766 0.3488 0.2627 -0.0145 0.0237  0.0083  149 PHE   A CD1  
1071 C  CD2  . PHE   A 150 ? 0.4407 0.3532 0.2556 -0.0018 0.0183  0.0108  149 PHE   A CD2  
1072 C  CE1  . PHE   A 150 ? 0.5022 0.3549 0.2719 -0.0013 0.0247  0.0098  149 PHE   A CE1  
1073 C  CE2  . PHE   A 150 ? 0.461  0.359  0.2625 0.0085  0.0207  0.0124  149 PHE   A CE2  
1074 C  CZ   . PHE   A 150 ? 0.4823 0.3518 0.2621 0.0105  0.0235  0.0114  149 PHE   A CZ   
1075 N  N    . TRP   A 151 ? 0.3876 0.3631 0.2494 -0.0296 0.0215  0.0019  150 TRP   A N    
1076 C  CA   . TRP   A 151 ? 0.3595 0.3585 0.2335 -0.0383 0.0251  -0.0033 150 TRP   A CA   
1077 C  C    . TRP   A 151 ? 0.3578 0.3534 0.2303 -0.0365 0.0309  -0.0006 150 TRP   A C    
1078 O  O    . TRP   A 151 ? 0.358  0.3563 0.2276 -0.0486 0.0382  -0.0028 150 TRP   A O    
1079 C  CB   . TRP   A 151 ? 0.326  0.3591 0.2199 -0.0318 0.0194  -0.0082 150 TRP   A CB   
1080 C  CG   . TRP   A 151 ? 0.3099 0.3437 0.202  -0.0269 0.011   -0.0089 150 TRP   A CG   
1081 C  CD1  . TRP   A 151 ? 0.307  0.3482 0.2033 -0.0116 0.0042  -0.0072 150 TRP   A CD1  
1082 C  CD2  . TRP   A 151 ? 0.3039 0.327  0.1845 -0.0374 0.0088  -0.0119 150 TRP   A CD2  
1083 N  NE1  . TRP   A 151 ? 0.306  0.3436 0.1945 -0.0117 -0.002  -0.0082 150 TRP   A NE1  
1084 C  CE2  . TRP   A 151 ? 0.3077 0.3345 0.1869 -0.0271 0.0006  -0.0117 150 TRP   A CE2  
1085 C  CE3  . TRP   A 151 ? 0.3173 0.3212 0.1831 -0.0544 0.0133  -0.0145 150 TRP   A CE3  
1086 C  CZ2  . TRP   A 151 ? 0.3203 0.3359 0.1855 -0.0329 -0.0033 -0.0149 150 TRP   A CZ2  
1087 C  CZ3  . TRP   A 151 ? 0.3394 0.3283 0.1901 -0.0601 0.0094  -0.0179 150 TRP   A CZ3  
1088 C  CH2  . TRP   A 151 ? 0.3355 0.3332 0.1874 -0.0495 0.0009  -0.0187 150 TRP   A CH2  
1089 N  N    . ILE   A 152 ? 0.3538 0.3424 0.2259 -0.0236 0.0281  0.0038  151 ILE   A N    
1090 C  CA   . ILE   A 152 ? 0.3563 0.3399 0.2236 -0.0221 0.0323  0.0053  151 ILE   A CA   
1091 C  C    . ILE   A 152 ? 0.3649 0.3242 0.2128 -0.029  0.0361  0.0093  151 ILE   A C    
1092 O  O    . ILE   A 152 ? 0.3854 0.3426 0.2257 -0.0358 0.0427  0.0086  151 ILE   A O    
1093 C  CB   . ILE   A 152 ? 0.3546 0.3345 0.2232 -0.0101 0.0278  0.0078  151 ILE   A CB   
1094 C  CG1  . ILE   A 152 ? 0.3506 0.345  0.2307 -0.0011 0.0236  0.0051  151 ILE   A CG1  
1095 C  CG2  . ILE   A 152 ? 0.3501 0.3259 0.2116 -0.0098 0.032   0.0069  151 ILE   A CG2  
1096 C  CD1  . ILE   A 152 ? 0.3754 0.3573 0.2506 0.0079  0.0192  0.0082  151 ILE   A CD1  
1097 N  N    . THR   A 153 ? 0.3618 0.3022 0.199  -0.0262 0.0325  0.0135  152 THR   A N    
1098 C  CA   . THR   A 153 ? 0.3851 0.2984 0.1994 -0.0279 0.0347  0.0179  152 THR   A CA   
1099 C  C    . THR   A 153 ? 0.4045 0.3051 0.2048 -0.0438 0.0422  0.0157  152 THR   A C    
1100 O  O    . THR   A 153 ? 0.4096 0.2945 0.1922 -0.0495 0.0477  0.0181  152 THR   A O    
1101 C  CB   . THR   A 153 ? 0.3925 0.292  0.1995 -0.0168 0.0293  0.0222  152 THR   A CB   
1102 O  OG1  . THR   A 153 ? 0.3802 0.2963 0.2018 -0.0073 0.0239  0.0238  152 THR   A OG1  
1103 C  CG2  . THR   A 153 ? 0.4161 0.2866 0.197  -0.0129 0.0299  0.0272  152 THR   A CG2  
1104 N  N    . LYS   A 154 ? 0.4045 0.313  0.2114 -0.0531 0.0428  0.0107  153 LYS   A N    
1105 C  CA   . LYS   A 154 ? 0.4275 0.3259 0.2213 -0.0736 0.0504  0.0074  153 LYS   A CA   
1106 C  C    . LYS   A 154 ? 0.4309 0.3513 0.2331 -0.0853 0.0591  0.0046  153 LYS   A C    
1107 O  O    . LYS   A 154 ? 0.4498 0.3545 0.2335 -0.1035 0.0682  0.0045  153 LYS   A O    
1108 C  CB   . LYS   A 154 ? 0.4417 0.3501 0.2429 -0.0834 0.0476  0.0008  153 LYS   A CB   
1109 C  CG   . LYS   A 154 ? 0.5093 0.3871 0.2924 -0.0753 0.0425  0.0027  153 LYS   A CG   
1110 C  CD   . LYS   A 154 ? 0.5811 0.4371 0.3446 -0.0944 0.0448  -0.0026 153 LYS   A CD   
1111 C  CE   . LYS   A 154 ? 0.6097 0.5046 0.3962 -0.11   0.0428  -0.0117 153 LYS   A CE   
1112 N  NZ   . LYS   A 154 ? 0.6328 0.5053 0.3993 -0.1259 0.0411  -0.0179 153 LYS   A NZ   
1113 N  N    . ALA   A 155 ? 0.4111 0.3648 0.2377 -0.075  0.0574  0.0022  154 ALA   A N    
1114 C  CA   . ALA   A 155 ? 0.4039 0.3826 0.2399 -0.0814 0.0663  -0.0016 154 ALA   A CA   
1115 C  C    . ALA   A 155 ? 0.4347 0.3903 0.2491 -0.0781 0.0712  0.0037  154 ALA   A C    
1116 O  O    . ALA   A 155 ? 0.4377 0.3977 0.2446 -0.0901 0.0824  0.0023  154 ALA   A O    
1117 C  CB   . ALA   A 155 ? 0.379  0.397  0.2444 -0.0677 0.0623  -0.0069 154 ALA   A CB   
1118 N  N    . LEU   A 156 ? 0.4514 0.3854 0.2556 -0.0628 0.063   0.0095  155 LEU   A N    
1119 C  CA   . LEU   A 156 ? 0.4629 0.3786 0.2469 -0.0581 0.0646  0.0139  155 LEU   A CA   
1120 C  C    . LEU   A 156 ? 0.4961 0.3706 0.2458 -0.0604 0.0645  0.0215  155 LEU   A C    
1121 O  O    . LEU   A 156 ? 0.5113 0.3691 0.2378 -0.0625 0.0691  0.0247  155 LEU   A O    
1122 C  CB   . LEU   A 156 ? 0.4537 0.3766 0.2478 -0.0414 0.0554  0.0141  155 LEU   A CB   
1123 C  CG   . LEU   A 156 ? 0.4486 0.4022 0.2683 -0.0355 0.0553  0.0074  155 LEU   A CG   
1124 C  CD1  . LEU   A 156 ? 0.4592 0.4088 0.2806 -0.0227 0.0467  0.0082  155 LEU   A CD1  
1125 C  CD2  . LEU   A 156 ? 0.4344 0.4067 0.257  -0.0408 0.0668  0.0016  155 LEU   A CD2  
1126 N  N    . LEU   A 157 ? 0.5105 0.3654 0.2521 -0.0598 0.0603  0.0241  156 LEU   A N    
1127 C  CA   . LEU   A 157 ? 0.5471 0.3575 0.252  -0.0572 0.0593  0.0314  156 LEU   A CA   
1128 C  C    . LEU   A 157 ? 0.5784 0.3569 0.2485 -0.0747 0.071   0.0343  156 LEU   A C    
1129 O  O    . LEU   A 157 ? 0.607  0.3511 0.2432 -0.0679 0.0699  0.0416  156 LEU   A O    
1130 C  CB   . LEU   A 157 ? 0.5537 0.3493 0.2564 -0.0519 0.054   0.0317  156 LEU   A CB   
1131 C  CG   . LEU   A 157 ? 0.5892 0.3523 0.2666 -0.0332 0.0468  0.0387  156 LEU   A CG   
1132 C  CD1  . LEU   A 157 ? 0.5899 0.3667 0.2721 -0.0162 0.0385  0.0428  156 LEU   A CD1  
1133 C  CD2  . LEU   A 157 ? 0.5854 0.3488 0.2713 -0.0237 0.0418  0.0368  156 LEU   A CD2  
1134 N  N    . PRO   A 158 ? 0.5731 0.3629 0.249  -0.0977 0.0821  0.0289  157 PRO   A N    
1135 C  CA   . PRO   A 158 ? 0.5942 0.3518 0.2341 -0.1186 0.0953  0.032   157 PRO   A CA   
1136 C  C    . PRO   A 158 ? 0.6307 0.376  0.247  -0.1158 0.1005  0.0374  157 PRO   A C    
1137 O  O    . PRO   A 158 ? 0.6647 0.3625 0.2353 -0.122  0.106   0.0448  157 PRO   A O    
1138 C  CB   . PRO   A 158 ? 0.5732 0.3695 0.2393 -0.1432 0.1057  0.0229  157 PRO   A CB   
1139 C  CG   . PRO   A 158 ? 0.5551 0.3831 0.2573 -0.1352 0.0956  0.0165  157 PRO   A CG   
1140 C  CD   . PRO   A 158 ? 0.5345 0.3666 0.2478 -0.1066 0.0828  0.0198  157 PRO   A CD   
1141 N  N    . SER   A 159 ? 0.619  0.4035 0.2621 -0.1067 0.0993  0.0333  158 SER   A N    
1142 C  CA   . SER   A 159 ? 0.6406 0.4183 0.2634 -0.1036 0.1038  0.0363  158 SER   A CA   
1143 C  C    . SER   A 159 ? 0.6862 0.4302 0.2813 -0.0826 0.0902  0.0447  158 SER   A C    
1144 O  O    . SER   A 159 ? 0.7088 0.4203 0.264  -0.0825 0.0931  0.0513  158 SER   A O    
1145 C  CB   . SER   A 159 ? 0.6267 0.4533 0.2853 -0.0977 0.1052  0.0279  158 SER   A CB   
1146 O  OG   . SER   A 159 ? 0.6882 0.5071 0.3266 -0.0908 0.1069  0.0295  158 SER   A OG   
1147 N  N    . MET   A 160 ? 0.6939 0.4485 0.31   -0.0647 0.0754  0.0445  159 MET   A N    
1148 C  CA   . MET   A 160 ? 0.7082 0.4443 0.3079 -0.0436 0.0609  0.051   159 MET   A CA   
1149 C  C    . MET   A 160 ? 0.7553 0.4384 0.3101 -0.0414 0.0612  0.0598  159 MET   A C    
1150 O  O    . MET   A 160 ? 0.7789 0.4354 0.3009 -0.0283 0.0545  0.0671  159 MET   A O    
1151 C  CB   . MET   A 160 ? 0.6671 0.4321 0.3034 -0.0298 0.0488  0.0477  159 MET   A CB   
1152 C  CG   . MET   A 160 ? 0.6316 0.4381 0.3044 -0.0308 0.0479  0.0401  159 MET   A CG   
1153 S  SD   . MET   A 160 ? 0.6172 0.448  0.3209 -0.0151 0.0334  0.039   159 MET   A SD   
1154 C  CE   . MET   A 160 ? 0.5372 0.4032 0.2728 -0.0186 0.0344  0.0306  159 MET   A CE   
1155 N  N    . ILE   A 161 ? 0.7672 0.4324 0.3172 -0.054  0.0683  0.0588  160 ILE   A N    
1156 C  CA   . ILE   A 161 ? 0.8108 0.4157 0.3119 -0.0535 0.0702  0.0664  160 ILE   A CA   
1157 C  C    . ILE   A 161 ? 0.8605 0.4266 0.3149 -0.0686 0.082   0.0725  160 ILE   A C    
1158 O  O    . ILE   A 161 ? 0.9008 0.4184 0.3073 -0.0557 0.0777  0.0821  160 ILE   A O    
1159 C  CB   . ILE   A 161 ? 0.8061 0.4004 0.3124 -0.0672 0.0753  0.0618  160 ILE   A CB   
1160 C  CG1  . ILE   A 161 ? 0.781  0.4014 0.3207 -0.0476 0.0631  0.058   160 ILE   A CG1  
1161 C  CG2  . ILE   A 161 ? 0.8557 0.3775 0.3023 -0.0743 0.0814  0.0686  160 ILE   A CG2  
1162 C  CD1  . ILE   A 161 ? 0.7915 0.4095 0.3403 -0.0609 0.067   0.0517  160 ILE   A CD1  
1163 N  N    . LYS   A 162 ? 0.8499 0.4398 0.3178 -0.0946 0.0969  0.067   161 LYS   A N    
1164 C  CA   . LYS   A 162 ? 0.8729 0.4361 0.3021 -0.1141 0.1122  0.0713  161 LYS   A CA   
1165 C  C    . LYS   A 162 ? 0.8714 0.4194 0.272  -0.0951 0.1051  0.0785  161 LYS   A C    
1166 O  O    . LYS   A 162 ? 0.9171 0.4122 0.2618 -0.0981 0.1101  0.0878  161 LYS   A O    
1167 C  CB   . LYS   A 162 ? 0.8975 0.5131 0.3634 -0.1381 0.1274  0.0615  161 LYS   A CB   
1168 C  CG   . LYS   A 162 ? 1.003  0.6008 0.4482 -0.174  0.1474  0.0608  161 LYS   A CG   
1169 C  CD   . LYS   A 162 ? 1.0496 0.7151 0.5448 -0.1943 0.1596  0.0488  161 LYS   A CD   
1170 C  CE   . LYS   A 162 ? 1.0764 0.7906 0.6275 -0.1878 0.1493  0.0391  161 LYS   A CE   
1171 N  NZ   . LYS   A 162 ? 1.1073 0.7946 0.6493 -0.2013 0.1469  0.0385  161 LYS   A NZ   
1172 N  N    . ARG   A 163 ? 0.8267 0.4172 0.2614 -0.0763 0.0927  0.0742  162 ARG   A N    
1173 C  CA   . ARG   A 163 ? 0.8265 0.4104 0.2387 -0.0591 0.0832  0.0788  162 ARG   A CA   
1174 C  C    . ARG   A 163 ? 0.8313 0.3966 0.229  -0.0297 0.0624  0.0857  162 ARG   A C    
1175 O  O    . ARG   A 163 ? 0.8441 0.4066 0.2232 -0.0146 0.0515  0.0892  162 ARG   A O    
1176 C  CB   . ARG   A 163 ? 0.8045 0.4438 0.2593 -0.0562 0.0805  0.0691  162 ARG   A CB   
1177 C  CG   . ARG   A 163 ? 0.8417 0.5045 0.3084 -0.0781 0.1002  0.0619  162 ARG   A CG   
1178 C  CD   . ARG   A 163 ? 0.8688 0.5818 0.3788 -0.0712 0.0964  0.0515  162 ARG   A CD   
1179 N  NE   . ARG   A 163 ? 0.9088 0.6477 0.4301 -0.0868 0.1154  0.0439  162 ARG   A NE   
1180 C  CZ   . ARG   A 163 ? 0.9474 0.6935 0.4568 -0.0846 0.1208  0.04    162 ARG   A CZ   
1181 N  NH1  . ARG   A 163 ? 0.9466 0.6771 0.4344 -0.0693 0.107   0.0423  162 ARG   A NH1  
1182 N  NH2  . ARG   A 163 ? 0.9388 0.7126 0.4606 -0.0965 0.1395  0.0325  162 ARG   A NH2  
1183 N  N    . ASN   A 164 ? 0.8187 0.3774 0.2277 -0.0207 0.0562  0.0862  163 ASN   A N    
1184 C  CA   . ASN   A 164 ? 0.8105 0.3654 0.2181 0.0092  0.0375  0.0905  163 ASN   A CA   
1185 C  C    . ASN   A 164 ? 0.7784 0.3852 0.2218 0.0235  0.0226  0.0859  163 ASN   A C    
1186 O  O    . ASN   A 164 ? 0.7947 0.397  0.2189 0.0437  0.0082  0.091   163 ASN   A O    
1187 C  CB   . ASN   A 164 ? 0.838  0.3297 0.1815 0.0253  0.0329  0.1025  163 ASN   A CB   
1188 C  CG   . ASN   A 164 ? 0.8511 0.3401 0.1979 0.0556  0.0176  0.1052  163 ASN   A CG   
1189 O  OD1  . ASN   A 164 ? 0.8573 0.368  0.2394 0.0561  0.018   0.0992  163 ASN   A OD1  
1190 N  ND2  . ASN   A 164 ? 0.846  0.3156 0.1599 0.0835  0.0031  0.1132  163 ASN   A ND2  
1191 N  N    . HIS   A 165 ? 0.732  0.3858 0.2231 0.0111  0.0264  0.0762  164 HIS   A N    
1192 C  CA   . HIS   A 165 ? 0.7054 0.4019 0.2256 0.0183  0.0148  0.0709  164 HIS   A CA   
1193 C  C    . HIS   A 165 ? 0.6521 0.3914 0.2237 0.009   0.018   0.0614  164 HIS   A C    
1194 O  O    . HIS   A 165 ? 0.6537 0.4008 0.2357 -0.0075 0.0311  0.0561  164 HIS   A O    
1195 C  CB   . HIS   A 165 ? 0.7393 0.4276 0.2326 0.0119  0.0174  0.0709  164 HIS   A CB   
1196 C  CG   . HIS   A 165 ? 0.7678 0.4923 0.283  0.0166  0.0053  0.0645  164 HIS   A CG   
1197 N  ND1  . HIS   A 165 ? 0.7943 0.5256 0.3    0.0336  -0.0139 0.0674  164 HIS   A ND1  
1198 C  CD2  . HIS   A 165 ? 0.7673 0.5204 0.3107 0.006   0.0096  0.055   164 HIS   A CD2  
1199 C  CE1  . HIS   A 165 ? 0.7854 0.5482 0.3135 0.0287  -0.0202 0.0591  164 HIS   A CE1  
1200 N  NE2  . HIS   A 165 ? 0.7757 0.5479 0.3238 0.0132  -0.0061 0.0518  164 HIS   A NE2  
1201 N  N    . GLY   A 166 ? 0.6067 0.3751 0.2088 0.0206  0.0061  0.0593  165 GLY   A N    
1202 C  CA   . GLY   A 166 ? 0.5753 0.3795 0.2208 0.0137  0.0076  0.0516  165 GLY   A CA   
1203 C  C    . GLY   A 166 ? 0.5518 0.3854 0.2238 0.0259  -0.0056 0.0508  165 GLY   A C    
1204 O  O    . GLY   A 166 ? 0.5687 0.4012 0.2299 0.0415  -0.0164 0.0556  165 GLY   A O    
1205 N  N    . HIS   A 167 ? 0.5112 0.3725 0.217  0.0194  -0.0046 0.0448  166 HIS   A N    
1206 C  CA   . HIS   A 167 ? 0.4731 0.3644 0.2056 0.0262  -0.014  0.0438  166 HIS   A CA   
1207 C  C    . HIS   A 167 ? 0.4485 0.3538 0.2088 0.0187  -0.0074 0.0396  166 HIS   A C    
1208 O  O    . HIS   A 167 ? 0.4463 0.3553 0.2142 0.0085  -0.003  0.0348  166 HIS   A O    
1209 C  CB   . HIS   A 167 ? 0.4487 0.361  0.1859 0.0247  -0.0252 0.041   166 HIS   A CB   
1210 C  CG   . HIS   A 167 ? 0.4342 0.3793 0.1921 0.0331  -0.0364 0.0418  166 HIS   A CG   
1211 N  ND1  . HIS   A 167 ? 0.442  0.4039 0.1937 0.0403  -0.0504 0.0427  166 HIS   A ND1  
1212 C  CD2  . HIS   A 167 ? 0.416  0.3832 0.2005 0.035   -0.035  0.0413  166 HIS   A CD2  
1213 C  CE1  . HIS   A 167 ? 0.4166 0.4147 0.1949 0.0459  -0.0565 0.0425  166 HIS   A CE1  
1214 N  NE2  . HIS   A 167 ? 0.4107 0.4117 0.2082 0.0427  -0.0466 0.0418  166 HIS   A NE2  
1215 N  N    . ILE   A 168 ? 0.4382 0.3479 0.2092 0.0255  -0.0064 0.0414  167 ILE   A N    
1216 C  CA   . ILE   A 168 ? 0.4243 0.3463 0.218  0.0201  -0.0014 0.0382  167 ILE   A CA   
1217 C  C    . ILE   A 168 ? 0.4039 0.3561 0.2201 0.0227  -0.0077 0.0377  167 ILE   A C    
1218 O  O    . ILE   A 168 ? 0.3947 0.3591 0.2149 0.0343  -0.0116 0.0403  167 ILE   A O    
1219 C  CB   . ILE   A 168 ? 0.4369 0.3421 0.224  0.0235  0.0047  0.0394  167 ILE   A CB   
1220 C  CG1  . ILE   A 168 ? 0.4688 0.3421 0.2293 0.0179  0.0112  0.0406  167 ILE   A CG1  
1221 C  CG2  . ILE   A 168 ? 0.4225 0.34   0.2297 0.0175  0.0088  0.0357  167 ILE   A CG2  
1222 C  CD1  . ILE   A 168 ? 0.4818 0.3576 0.2467 0.0033  0.0183  0.0363  167 ILE   A CD1  
1223 N  N    . VAL   A 169 ? 0.3886 0.3519 0.2177 0.012   -0.0076 0.0341  168 VAL   A N    
1224 C  CA   . VAL   A 169 ? 0.3791 0.3673 0.2265 0.0083  -0.0114 0.0334  168 VAL   A CA   
1225 C  C    . VAL   A 169 ? 0.3832 0.3721 0.2418 0.0052  -0.0048 0.0329  168 VAL   A C    
1226 O  O    . VAL   A 169 ? 0.3971 0.3723 0.2529 -0.0001 -0.0006 0.0306  168 VAL   A O    
1227 C  CB   . VAL   A 169 ? 0.3919 0.3822 0.2372 -0.0035 -0.0161 0.0299  168 VAL   A CB   
1228 C  CG1  . VAL   A 169 ? 0.3947 0.4056 0.256  -0.0138 -0.018  0.0288  168 VAL   A CG1  
1229 C  CG2  . VAL   A 169 ? 0.3856 0.3771 0.2177 -0.0004 -0.0243 0.0301  168 VAL   A CG2  
1230 N  N    . THR   A 170 ? 0.3675 0.3734 0.2373 0.0107  -0.0039 0.035   169 THR   A N    
1231 C  CA   . THR   A 170 ? 0.3652 0.3713 0.2417 0.0081  0.0021  0.0349  169 THR   A CA   
1232 C  C    . THR   A 170 ? 0.3474 0.3729 0.2357 -0.0023 0.0015  0.0352  169 THR   A C    
1233 O  O    . THR   A 170 ? 0.342  0.3949 0.2415 -0.0009 -0.001  0.0362  169 THR   A O    
1234 C  CB   . THR   A 170 ? 0.3817 0.3922 0.2588 0.0206  0.0053  0.0366  169 THR   A CB   
1235 O  OG1  . THR   A 170 ? 0.415  0.4017 0.2763 0.0275  0.0061  0.0363  169 THR   A OG1  
1236 C  CG2  . THR   A 170 ? 0.379  0.3902 0.2599 0.0183  0.0113  0.0365  169 THR   A CG2  
1237 N  N    . VAL   A 171 ? 0.341  0.3531 0.2255 -0.0125 0.0039  0.0344  170 VAL   A N    
1238 C  CA   . VAL   A 171 ? 0.3403 0.3631 0.2299 -0.0257 0.005   0.0353  170 VAL   A CA   
1239 C  C    . VAL   A 171 ? 0.3628 0.3904 0.2554 -0.0231 0.012   0.0382  170 VAL   A C    
1240 O  O    . VAL   A 171 ? 0.3843 0.3904 0.2667 -0.0204 0.015   0.0387  170 VAL   A O    
1241 C  CB   . VAL   A 171 ? 0.3457 0.3437 0.2219 -0.0381 0.0038  0.0334  170 VAL   A CB   
1242 C  CG1  . VAL   A 171 ? 0.3439 0.3442 0.219  -0.0545 0.007   0.0354  170 VAL   A CG1  
1243 C  CG2  . VAL   A 171 ? 0.3301 0.3249 0.2009 -0.0415 -0.0028 0.0297  170 VAL   A CG2  
1244 N  N    . ALA   A 172 ? 0.3444 0.4028 0.2506 -0.0211 0.0145  0.0396  171 ALA   A N    
1245 C  CA   . ALA   A 172 ? 0.3343 0.399  0.2413 -0.0179 0.0226  0.0419  171 ALA   A CA   
1246 C  C    . ALA   A 172 ? 0.3415 0.4203 0.2523 -0.0369 0.028   0.0441  171 ALA   A C    
1247 O  O    . ALA   A 172 ? 0.3536 0.4055 0.2504 -0.0497 0.0274  0.0449  171 ALA   A O    
1248 C  CB   . ALA   A 172 ? 0.3185 0.4023 0.2329 0.0004  0.0244  0.0413  171 ALA   A CB   
1249 N  N    . SER   A 173 ? 0.3289 0.448  0.2567 -0.04   0.0333  0.0448  172 SER   A N    
1250 C  CA   . SER   A 173 ? 0.3319 0.4679 0.2634 -0.0615 0.0406  0.0469  172 SER   A CA   
1251 C  C    . SER   A 173 ? 0.3262 0.5156 0.2808 -0.0551 0.0476  0.0465  172 SER   A C    
1252 O  O    . SER   A 173 ? 0.3161 0.515  0.2756 -0.0309 0.0474  0.0451  172 SER   A O    
1253 C  CB   . SER   A 173 ? 0.3562 0.4552 0.2637 -0.0662 0.0482  0.051   172 SER   A CB   
1254 O  OG   . SER   A 173 ? 0.3674 0.4779 0.2727 -0.0864 0.0585  0.0544  172 SER   A OG   
1255 N  N    . VAL   A 174 ? 0.3287 0.5519 0.2955 -0.0764 0.0552  0.0474  173 VAL   A N    
1256 C  CA   . VAL   A 174 ? 0.3288 0.6063 0.3177 -0.0688 0.0652  0.0468  173 VAL   A CA   
1257 C  C    . VAL   A 174 ? 0.3625 0.617  0.3331 -0.0545 0.0764  0.0495  173 VAL   A C    
1258 O  O    . VAL   A 174 ? 0.3547 0.6401 0.3362 -0.0353 0.0832  0.0478  173 VAL   A O    
1259 C  CB   . VAL   A 174 ? 0.318  0.6439 0.3262 -0.0971 0.0729  0.0467  173 VAL   A CB   
1260 C  CG1  . VAL   A 174 ? 0.3089 0.6775 0.3428 -0.1035 0.0606  0.0419  173 VAL   A CG1  
1261 C  CG2  . VAL   A 174 ? 0.3434 0.627  0.3252 -0.1283 0.0794  0.0511  173 VAL   A CG2  
1262 N  N    . CYS   A 175 ? 0.3983 0.5969 0.3387 -0.0611 0.0771  0.053   174 CYS   A N    
1263 C  CA   . CYS   A 175 ? 0.4231 0.5911 0.3403 -0.0484 0.0834  0.0551  174 CYS   A CA   
1264 C  C    . CYS   A 175 ? 0.4224 0.5826 0.3385 -0.0194 0.0781  0.0511  174 CYS   A C    
1265 O  O    . CYS   A 175 ? 0.4521 0.5963 0.3518 -0.008  0.0837  0.051   174 CYS   A O    
1266 C  CB   . CYS   A 175 ? 0.4703 0.5835 0.3572 -0.0593 0.0807  0.0592  174 CYS   A CB   
1267 S  SG   . CYS   A 175 ? 0.5766 0.6808 0.4491 -0.0933 0.0903  0.0653  174 CYS   A SG   
1268 N  N    . GLY   A 176 ? 0.3927 0.5594 0.3215 -0.0094 0.0674  0.0479  175 GLY   A N    
1269 C  CA   . GLY   A 176 ? 0.3942 0.5506 0.3187 0.0157  0.063   0.0445  175 GLY   A CA   
1270 C  C    . GLY   A 176 ? 0.3711 0.5679 0.3106 0.0348  0.0685  0.0419  175 GLY   A C    
1271 O  O    . GLY   A 176 ? 0.3673 0.5505 0.2974 0.0575  0.0665  0.0391  175 GLY   A O    
1272 N  N    . HIS   A 177 ? 0.3528 0.5995 0.3143 0.0257  0.076   0.0426  176 HIS   A N    
1273 C  CA   . HIS   A 177 ? 0.3483 0.6458 0.3294 0.0443  0.0822  0.0397  176 HIS   A CA   
1274 C  C    . HIS   A 177 ? 0.3869 0.7107 0.3699 0.0386  0.1     0.0404  176 HIS   A C    
1275 O  O    . HIS   A 177 ? 0.3832 0.733  0.3704 0.0614  0.1087  0.0372  176 HIS   A O    
1276 C  CB   . HIS   A 177 ? 0.3105 0.659  0.3226 0.0386  0.0745  0.0387  176 HIS   A CB   
1277 C  CG   . HIS   A 177 ? 0.3189 0.6436 0.3262 0.0466  0.0579  0.0381  176 HIS   A CG   
1278 N  ND1  . HIS   A 177 ? 0.3304 0.6556 0.335  0.0777  0.0516  0.0361  176 HIS   A ND1  
1279 C  CD2  . HIS   A 177 ? 0.3385 0.634  0.3385 0.0283  0.0479  0.0394  176 HIS   A CD2  
1280 C  CE1  . HIS   A 177 ? 0.342  0.6401 0.3382 0.0752  0.0384  0.0369  176 HIS   A CE1  
1281 N  NE2  . HIS   A 177 ? 0.3521 0.634  0.3468 0.0462  0.036   0.0384  176 HIS   A NE2  
1282 N  N    . GLU   A 178 ? 0.4191 0.7334 0.3953 0.0091  0.1063  0.0447  177 GLU   A N    
1283 C  CA   . GLU   A 178 ? 0.4453 0.7798 0.4182 -0.0005 0.1245  0.0465  177 GLU   A CA   
1284 C  C    . GLU   A 178 ? 0.4902 0.7691 0.4289 -0.0192 0.1276  0.052   177 GLU   A C    
1285 O  O    . GLU   A 178 ? 0.5157 0.762  0.4457 -0.0359 0.1178  0.0549  177 GLU   A O    
1286 C  CB   . GLU   A 178 ? 0.4593 0.8617 0.4657 -0.0213 0.132   0.0465  177 GLU   A CB   
1287 C  CG   . GLU   A 178 ? 0.5526 0.9832 0.5576 -0.0356 0.1537  0.0487  177 GLU   A CG   
1288 C  CD   . GLU   A 178 ? 0.6938 1.1464 0.6964 -0.0069 0.1678  0.0452  177 GLU   A CD   
1289 O  OE1  . GLU   A 178 ? 0.7346 1.259  0.7683 -0.0017 0.1787  0.0417  177 GLU   A OE1  
1290 O  OE2  . GLU   A 178 ? 0.7337 1.1338 0.7027 0.0095  0.1684  0.0453  177 GLU   A OE2  
1291 N  N    . GLY   A 179 ? 0.4996 0.7662 0.4164 -0.0133 0.1403  0.0531  178 GLY   A N    
1292 C  CA   . GLY   A 179 ? 0.5379 0.7532 0.4186 -0.0268 0.1428  0.0587  178 GLY   A CA   
1293 C  C    . GLY   A 179 ? 0.5462 0.7667 0.4226 -0.0599 0.1527  0.0654  178 GLY   A C    
1294 O  O    . GLY   A 179 ? 0.5261 0.7997 0.4291 -0.0747 0.1623  0.0649  178 GLY   A O    
1295 N  N    . ILE   A 180 ? 0.5709 0.7356 0.4121 -0.0723 0.1499  0.0716  179 ILE   A N    
1296 C  CA   . ILE   A 180 ? 0.5704 0.7206 0.3942 -0.1044 0.1589  0.0792  179 ILE   A CA   
1297 C  C    . ILE   A 180 ? 0.5788 0.6758 0.3548 -0.1039 0.1638  0.0859  179 ILE   A C    
1298 O  O    . ILE   A 180 ? 0.5938 0.6459 0.3485 -0.0884 0.1503  0.086   179 ILE   A O    
1299 C  CB   . ILE   A 180 ? 0.5889 0.7132 0.4142 -0.121  0.1447  0.0805  179 ILE   A CB   
1300 C  CG1  . ILE   A 180 ? 0.5708 0.7483 0.4396 -0.1265 0.1396  0.0744  179 ILE   A CG1  
1301 C  CG2  . ILE   A 180 ? 0.6177 0.7019 0.4092 -0.1517 0.1519  0.089   179 ILE   A CG2  
1302 C  CD1  . ILE   A 180 ? 0.6032 0.7527 0.4697 -0.1403 0.1255  0.0741  179 ILE   A CD1  
1303 N  N    . PRO   A 181 ? 0.5773 0.6775 0.3339 -0.123  0.1825  0.0921  180 PRO   A N    
1304 C  CA   . PRO   A 181 ? 0.6062 0.6495 0.3102 -0.1233 0.1862  0.1     180 PRO   A CA   
1305 C  C    . PRO   A 181 ? 0.634  0.6119 0.3075 -0.1274 0.1704  0.1055  180 PRO   A C    
1306 O  O    . PRO   A 181 ? 0.6346 0.6069 0.3188 -0.1442 0.1644  0.1061  180 PRO   A O    
1307 C  CB   . PRO   A 181 ? 0.6126 0.6727 0.3042 -0.1521 0.2101  0.1066  180 PRO   A CB   
1308 C  CG   . PRO   A 181 ? 0.576  0.7168 0.3189 -0.1545 0.2207  0.0993  180 PRO   A CG   
1309 C  CD   . PRO   A 181 ? 0.5394 0.6969 0.3198 -0.1463 0.2015  0.0924  180 PRO   A CD   
1310 N  N    . TYR   A 182 ? 0.6495 0.58   0.2852 -0.1096 0.1623  0.1085  181 TYR   A N    
1311 C  CA   . TYR   A 182 ? 0.6775 0.547  0.281  -0.1058 0.1466  0.1135  181 TYR   A CA   
1312 C  C    . TYR   A 182 ? 0.6419 0.5141 0.2741 -0.091  0.1266  0.1059  181 TYR   A C    
1313 O  O    . TYR   A 182 ? 0.6616 0.4907 0.2726 -0.0845 0.1135  0.1085  181 TYR   A O    
1314 C  CB   . TYR   A 182 ? 0.7126 0.5404 0.2815 -0.134  0.1544  0.124   181 TYR   A CB   
1315 C  CG   . TYR   A 182 ? 0.7327 0.569  0.2812 -0.1569 0.1782  0.131   181 TYR   A CG   
1316 C  CD1  . TYR   A 182 ? 0.7595 0.5881 0.2789 -0.1451 0.1864  0.1342  181 TYR   A CD1  
1317 C  CD2  . TYR   A 182 ? 0.7315 0.5923 0.2941 -0.1911 0.1933  0.1329  181 TYR   A CD2  
1318 C  CE1  . TYR   A 182 ? 0.7712 0.6148 0.2747 -0.1654 0.2106  0.1397  181 TYR   A CE1  
1319 C  CE2  . TYR   A 182 ? 0.7437 0.6217 0.2923 -0.2142 0.2174  0.1385  181 TYR   A CE2  
1320 C  CZ   . TYR   A 182 ? 0.7742 0.6445 0.2938 -0.2004 0.227   0.142   181 TYR   A CZ   
1321 O  OH   . TYR   A 182 ? 0.817  0.706  0.3213 -0.2237 0.2531  0.1475  181 TYR   A OH   
1322 N  N    . LEU   A 183 ? 0.5917 0.5126 0.2684 -0.0829 0.1245  0.0969  182 LEU   A N    
1323 C  CA   . LEU   A 183 ? 0.5742 0.4987 0.2758 -0.0697 0.1077  0.09    182 LEU   A CA   
1324 C  C    . LEU   A 183 ? 0.5451 0.4956 0.266  -0.0468 0.1034  0.0816  182 LEU   A C    
1325 O  O    . LEU   A 183 ? 0.536  0.511  0.2882 -0.0405 0.0971  0.0752  182 LEU   A O    
1326 C  CB   . LEU   A 183 ? 0.5536 0.5047 0.287  -0.0862 0.1077  0.0874  182 LEU   A CB   
1327 C  CG   . LEU   A 183 ? 0.5865 0.5049 0.3    -0.1103 0.1087  0.0934  182 LEU   A CG   
1328 C  CD1  . LEU   A 183 ? 0.5689 0.5199 0.3151 -0.1269 0.1076  0.0888  182 LEU   A CD1  
1329 C  CD2  . LEU   A 183 ? 0.6213 0.4835 0.305  -0.0986 0.0951  0.0956  182 LEU   A CD2  
1330 N  N    . ILE   A 184 ? 0.5318 0.4729 0.2298 -0.0353 0.1069  0.0816  183 ILE   A N    
1331 C  CA   . ILE   A 184 ? 0.5131 0.4706 0.2215 -0.0156 0.1038  0.073   183 ILE   A CA   
1332 C  C    . ILE   A 184 ? 0.5136 0.4608 0.2335 -0.0036 0.0859  0.0669  183 ILE   A C    
1333 O  O    . ILE   A 184 ? 0.5046 0.4741 0.2507 0.003   0.0837  0.0606  183 ILE   A O    
1334 C  CB   . ILE   A 184 ? 0.5231 0.4682 0.1996 -0.0065 0.1103  0.0728  183 ILE   A CB   
1335 C  CG1  . ILE   A 184 ? 0.5304 0.4915 0.1969 -0.0189 0.1314  0.0783  183 ILE   A CG1  
1336 C  CG2  . ILE   A 184 ? 0.5172 0.4724 0.2013 0.0125  0.1061  0.0624  183 ILE   A CG2  
1337 C  CD1  . ILE   A 184 ? 0.5559 0.5025 0.1856 -0.0103 0.1397  0.0784  183 ILE   A CD1  
1338 N  N    . PRO   A 185 ? 0.5186 0.4342 0.2193 0.0002  0.0733  0.0686  184 PRO   A N    
1339 C  CA   . PRO   A 185 ? 0.5047 0.419  0.2203 0.0098  0.0582  0.062   184 PRO   A CA   
1340 C  C    . PRO   A 185 ? 0.4916 0.4207 0.237  0.0041  0.0559  0.0605  184 PRO   A C    
1341 O  O    . PRO   A 185 ? 0.496  0.4359 0.2595 0.0106  0.05    0.0541  184 PRO   A O    
1342 C  CB   . PRO   A 185 ? 0.5273 0.412  0.2179 0.0147  0.0468  0.0652  184 PRO   A CB   
1343 C  CG   . PRO   A 185 ? 0.5426 0.4098 0.1987 0.013   0.0545  0.0716  184 PRO   A CG   
1344 C  CD   . PRO   A 185 ? 0.5215 0.4029 0.1847 -0.0017 0.0718  0.0762  184 PRO   A CD   
1345 N  N    . TYR   A 186 ? 0.4838 0.4113 0.2311 -0.0095 0.061   0.0662  185 TYR   A N    
1346 C  CA   . TYR   A 186 ? 0.4659 0.4058 0.2376 -0.0165 0.058   0.0644  185 TYR   A CA   
1347 C  C    . TYR   A 186 ? 0.4572 0.4349 0.2564 -0.0156 0.0636  0.0603  185 TYR   A C    
1348 O  O    . TYR   A 186 ? 0.4606 0.4484 0.2785 -0.0104 0.0569  0.0557  185 TYR   A O    
1349 C  CB   . TYR   A 186 ? 0.4603 0.3838 0.2207 -0.0339 0.0618  0.0709  185 TYR   A CB   
1350 C  CG   . TYR   A 186 ? 0.449  0.3855 0.2311 -0.0441 0.0592  0.0684  185 TYR   A CG   
1351 C  CD1  . TYR   A 186 ? 0.466  0.3852 0.2492 -0.0391 0.0485  0.0655  185 TYR   A CD1  
1352 C  CD2  . TYR   A 186 ? 0.4389 0.4073 0.2396 -0.0589 0.0675  0.0686  185 TYR   A CD2  
1353 C  CE1  . TYR   A 186 ? 0.4708 0.3985 0.2689 -0.0488 0.0459  0.0629  185 TYR   A CE1  
1354 C  CE2  . TYR   A 186 ? 0.4438 0.4251 0.2623 -0.0692 0.0632  0.0658  185 TYR   A CE2  
1355 C  CZ   . TYR   A 186 ? 0.4708 0.4283 0.2856 -0.0643 0.0523  0.0631  185 TYR   A CZ   
1356 O  OH   . TYR   A 186 ? 0.501  0.4682 0.3288 -0.0746 0.048   0.0598  185 TYR   A OH   
1357 N  N    . CYS   A 187 ? 0.4434 0.4422 0.2435 -0.019  0.0761  0.062   186 CYS   A N    
1358 C  CA   . CYS   A 187 ? 0.432  0.4705 0.2577 -0.0134 0.0815  0.058   186 CYS   A CA   
1359 C  C    . CYS   A 187 ? 0.428  0.4628 0.2552 0.0069  0.0755  0.0514  186 CYS   A C    
1360 O  O    . CYS   A 187 ? 0.4119 0.4647 0.2578 0.0145  0.0726  0.0478  186 CYS   A O    
1361 C  CB   . CYS   A 187 ? 0.4448 0.5083 0.2689 -0.0181 0.0976  0.0603  186 CYS   A CB   
1362 S  SG   . CYS   A 187 ? 0.5095 0.5896 0.3392 -0.0479 0.1073  0.0669  186 CYS   A SG   
1363 N  N    . SER   A 188 ? 0.4374 0.4465 0.2412 0.0147  0.0735  0.0499  187 SER   A N    
1364 C  CA   . SER   A 188 ? 0.4298 0.4279 0.2277 0.0294  0.0682  0.0431  187 SER   A CA   
1365 C  C    . SER   A 188 ? 0.4179 0.4075 0.2275 0.0292  0.0562  0.0404  187 SER   A C    
1366 O  O    . SER   A 188 ? 0.4158 0.408  0.232  0.0378  0.0543  0.0362  187 SER   A O    
1367 C  CB   . SER   A 188 ? 0.4507 0.4238 0.2199 0.0325  0.0665  0.0418  187 SER   A CB   
1368 O  OG   . SER   A 188 ? 0.4771 0.4402 0.2361 0.0443  0.0647  0.0342  187 SER   A OG   
1369 N  N    . SER   A 189 ? 0.4123 0.39   0.2216 0.0205  0.049   0.0431  188 SER   A N    
1370 C  CA   . SER   A 189 ? 0.4076 0.3802 0.2276 0.0198  0.0397  0.0405  188 SER   A CA   
1371 C  C    . SER   A 189 ? 0.4003 0.3914 0.2405 0.017   0.0407  0.0413  188 SER   A C    
1372 O  O    . SER   A 189 ? 0.3913 0.3805 0.2385 0.0201  0.0355  0.0383  188 SER   A O    
1373 C  CB   . SER   A 189 ? 0.4209 0.3781 0.2342 0.0148  0.033   0.0427  188 SER   A CB   
1374 O  OG   . SER   A 189 ? 0.4274 0.3843 0.2417 0.0053  0.0362  0.0482  188 SER   A OG   
1375 N  N    . LYS   A 190 ? 0.388  0.3982 0.2365 0.0099  0.0473  0.0451  189 LYS   A N    
1376 C  CA   . LYS   A 190 ? 0.3576 0.3919 0.2263 0.0069  0.0466  0.0451  189 LYS   A CA   
1377 C  C    . LYS   A 190 ? 0.3393 0.3923 0.2161 0.0222  0.0489  0.0421  189 LYS   A C    
1378 O  O    . LYS   A 190 ? 0.3494 0.4105 0.2362 0.027   0.0435  0.0407  189 LYS   A O    
1379 C  CB   . LYS   A 190 ? 0.3623 0.4134 0.2378 -0.0096 0.0518  0.0492  189 LYS   A CB   
1380 C  CG   . LYS   A 190 ? 0.3879 0.4129 0.2526 -0.0233 0.0472  0.0515  189 LYS   A CG   
1381 C  CD   . LYS   A 190 ? 0.4148 0.4323 0.2857 -0.0215 0.0375  0.0483  189 LYS   A CD   
1382 C  CE   . LYS   A 190 ? 0.4634 0.4487 0.3183 -0.0276 0.0333  0.0492  189 LYS   A CE   
1383 N  NZ   . LYS   A 190 ? 0.4666 0.448  0.3267 -0.0302 0.0265  0.046   189 LYS   A NZ   
1384 N  N    . PHE   A 191 ? 0.3287 0.3833 0.1963 0.032   0.0563  0.0409  190 PHE   A N    
1385 C  CA   . PHE   A 191 ? 0.3262 0.3892 0.1938 0.051   0.0589  0.0373  190 PHE   A CA   
1386 C  C    . PHE   A 191 ? 0.3415 0.3717 0.1956 0.0582  0.0508  0.0339  190 PHE   A C    
1387 O  O    . PHE   A 191 ? 0.3407 0.3714 0.1963 0.07    0.0481  0.0326  190 PHE   A O    
1388 C  CB   . PHE   A 191 ? 0.3351 0.3981 0.1885 0.0592  0.0694  0.0358  190 PHE   A CB   
1389 C  CG   . PHE   A 191 ? 0.3298 0.4357 0.1987 0.0629  0.0808  0.037   190 PHE   A CG   
1390 C  CD1  . PHE   A 191 ? 0.332  0.4613 0.2123 0.0438  0.0868  0.0416  190 PHE   A CD1  
1391 C  CD2  . PHE   A 191 ? 0.3272 0.4494 0.1971 0.0853  0.0865  0.0331  190 PHE   A CD2  
1392 C  CE1  . PHE   A 191 ? 0.3181 0.4932 0.2147 0.0438  0.0989  0.0422  190 PHE   A CE1  
1393 C  CE2  . PHE   A 191 ? 0.3163 0.4863 0.2036 0.0899  0.0983  0.0334  190 PHE   A CE2  
1394 C  CZ   . PHE   A 191 ? 0.3009 0.5002 0.2033 0.0675  0.1048  0.0378  190 PHE   A CZ   
1395 N  N    . ALA   A 192 ? 0.357  0.3594 0.197  0.0503  0.0468  0.0325  191 ALA   A N    
1396 C  CA   . ALA   A 192 ? 0.3747 0.35   0.2035 0.0508  0.0402  0.0289  191 ALA   A CA   
1397 C  C    . ALA   A 192 ? 0.3897 0.3689 0.231  0.047   0.0344  0.0306  191 ALA   A C    
1398 O  O    . ALA   A 192 ? 0.4094 0.3727 0.2422 0.0524  0.032   0.0288  191 ALA   A O    
1399 C  CB   . ALA   A 192 ? 0.37   0.3296 0.1891 0.0414  0.0363  0.0272  191 ALA   A CB   
1400 N  N    . ALA   A 193 ? 0.3819 0.3776 0.2384 0.0372  0.0325  0.0339  192 ALA   A N    
1401 C  CA   . ALA   A 193 ? 0.3865 0.3857 0.2517 0.0335  0.0271  0.0348  192 ALA   A CA   
1402 C  C    . ALA   A 193 ? 0.3919 0.4062 0.2623 0.0453  0.0266  0.0357  192 ALA   A C    
1403 O  O    . ALA   A 193 ? 0.4108 0.4129 0.2749 0.0496  0.0222  0.0354  192 ALA   A O    
1404 C  CB   . ALA   A 193 ? 0.3742 0.3835 0.2495 0.0204  0.0256  0.0372  192 ALA   A CB   
1405 N  N    . VAL   A 194 ? 0.3792 0.4209 0.2596 0.052   0.0312  0.0367  193 VAL   A N    
1406 C  CA   . VAL   A 194 ? 0.369  0.4324 0.2565 0.0677  0.0298  0.037   193 VAL   A CA   
1407 C  C    . VAL   A 194 ? 0.3929 0.4255 0.2574 0.0866  0.0298  0.0351  193 VAL   A C    
1408 O  O    . VAL   A 194 ? 0.4132 0.441  0.2717 0.0989  0.0248  0.0361  193 VAL   A O    
1409 C  CB   . VAL   A 194 ? 0.3492 0.4556 0.255  0.071   0.0366  0.0375  193 VAL   A CB   
1410 C  CG1  . VAL   A 194 ? 0.3448 0.477  0.2573 0.094   0.0354  0.0368  193 VAL   A CG1  
1411 C  CG2  . VAL   A 194 ? 0.3304 0.4639 0.2553 0.0493  0.036   0.0395  193 VAL   A CG2  
1412 N  N    . GLY   A 195 ? 0.398  0.406  0.2457 0.0881  0.0351  0.0324  194 GLY   A N    
1413 C  CA   . GLY   A 195 ? 0.4182 0.3886 0.2379 0.1019  0.0359  0.0296  194 GLY   A CA   
1414 C  C    . GLY   A 195 ? 0.4298 0.3659 0.234  0.0936  0.0303  0.0297  194 GLY   A C    
1415 O  O    . GLY   A 195 ? 0.4503 0.3582 0.2323 0.1058  0.0291  0.0298  194 GLY   A O    
1416 N  N    . PHE   A 196 ? 0.4188 0.3559 0.2322 0.0735  0.0277  0.0298  195 PHE   A N    
1417 C  CA   . PHE   A 196 ? 0.4359 0.3488 0.2388 0.063   0.0244  0.0296  195 PHE   A CA   
1418 C  C    . PHE   A 196 ? 0.4623 0.3799 0.2661 0.0701  0.0199  0.0337  195 PHE   A C    
1419 O  O    . PHE   A 196 ? 0.4815 0.3688 0.2628 0.0733  0.0189  0.0346  195 PHE   A O    
1420 C  CB   . PHE   A 196 ? 0.4172 0.3402 0.2342 0.0447  0.023   0.0284  195 PHE   A CB   
1421 C  CG   . PHE   A 196 ? 0.4284 0.3392 0.2415 0.0337  0.0209  0.028   195 PHE   A CG   
1422 C  CD1  . PHE   A 196 ? 0.4469 0.3315 0.2424 0.0259  0.0228  0.0247  195 PHE   A CD1  
1423 C  CD2  . PHE   A 196 ? 0.4288 0.3541 0.2538 0.03    0.018   0.0304  195 PHE   A CD2  
1424 C  CE1  . PHE   A 196 ? 0.4517 0.3291 0.244  0.0145  0.0232  0.0244  195 PHE   A CE1  
1425 C  CE2  . PHE   A 196 ? 0.4291 0.3437 0.2484 0.021   0.018   0.0297  195 PHE   A CE2  
1426 C  CZ   . PHE   A 196 ? 0.4348 0.3278 0.2391 0.0133  0.0213  0.027   195 PHE   A CZ   
1427 N  N    . HIS   A 197 ? 0.458  0.4119 0.2846 0.0717  0.0169  0.036   196 HIS   A N    
1428 C  CA   . HIS   A 197 ? 0.468  0.4323 0.2963 0.0789  0.0106  0.0392  196 HIS   A CA   
1429 C  C    . HIS   A 197 ? 0.4983 0.4509 0.3085 0.1037  0.0093  0.0409  196 HIS   A C    
1430 O  O    . HIS   A 197 ? 0.5178 0.4459 0.3071 0.1103  0.0052  0.0435  196 HIS   A O    
1431 C  CB   . HIS   A 197 ? 0.4407 0.4487 0.2971 0.0721  0.0072  0.0399  196 HIS   A CB   
1432 C  CG   . HIS   A 197 ? 0.4415 0.4728 0.3034 0.0832  -0.0006 0.042   196 HIS   A CG   
1433 N  ND1  . HIS   A 197 ? 0.4674 0.4862 0.3183 0.0805  -0.0076 0.0435  196 HIS   A ND1  
1434 C  CD2  . HIS   A 197 ? 0.4326 0.5015 0.3097 0.0977  -0.0027 0.0424  196 HIS   A CD2  
1435 C  CE1  . HIS   A 197 ? 0.4544 0.5018 0.3126 0.0936  -0.0155 0.045   196 HIS   A CE1  
1436 N  NE2  . HIS   A 197 ? 0.4357 0.5171 0.312  0.1045  -0.013  0.0442  196 HIS   A NE2  
1437 N  N    . ARG   A 198 ? 0.5049 0.4705 0.3186 0.1186  0.0136  0.0394  197 ARG   A N    
1438 C  CA   . ARG   A 198 ? 0.5414 0.4953 0.3363 0.1471  0.0129  0.0403  197 ARG   A CA   
1439 C  C    . ARG   A 198 ? 0.5695 0.4587 0.321  0.152   0.0145  0.0403  197 ARG   A C    
1440 O  O    . ARG   A 198 ? 0.5732 0.4385 0.3006 0.1694  0.0099  0.0438  197 ARG   A O    
1441 C  CB   . ARG   A 198 ? 0.5806 0.5616 0.387  0.1622  0.0197  0.0373  197 ARG   A CB   
1442 C  CG   . ARG   A 198 ? 0.6459 0.6902 0.485  0.1732  0.0166  0.0385  197 ARG   A CG   
1443 C  CD   . ARG   A 198 ? 0.7041 0.7899 0.5693 0.1659  0.0256  0.0359  197 ARG   A CD   
1444 N  NE   . ARG   A 198 ? 0.7364 0.888  0.638  0.1638  0.0228  0.0366  197 ARG   A NE   
1445 C  CZ   . ARG   A 198 ? 0.7507 0.9504 0.6704 0.1836  0.0265  0.035   197 ARG   A CZ   
1446 N  NH1  . ARG   A 198 ? 0.7547 0.9397 0.6564 0.2106  0.0338  0.0326  197 ARG   A NH1  
1447 N  NH2  . ARG   A 198 ? 0.7112 0.9754 0.6664 0.1761  0.0234  0.035   197 ARG   A NH2  
1448 N  N    . ALA   A 199 ? 0.5764 0.4362 0.3157 0.1358  0.0207  0.0364  198 ALA   A N    
1449 C  CA   . ALA   A 199 ? 0.6067 0.405  0.3044 0.1337  0.0233  0.0351  198 ALA   A CA   
1450 C  C    . ALA   A 199 ? 0.6154 0.3905 0.3001 0.1185  0.0201  0.0387  198 ALA   A C    
1451 O  O    . ALA   A 199 ? 0.6453 0.3708 0.291  0.1246  0.0205  0.0411  198 ALA   A O    
1452 C  CB   . ALA   A 199 ? 0.6098 0.3922 0.3017 0.1176  0.029   0.0287  198 ALA   A CB   
1453 N  N    . LEU   A 200 ? 0.5896 0.3978 0.3033 0.0999  0.0178  0.0394  199 LEU   A N    
1454 C  CA   . LEU   A 200 ? 0.589  0.3831 0.2936 0.0861  0.0161  0.0423  199 LEU   A CA   
1455 C  C    . LEU   A 200 ? 0.6041 0.3905 0.2921 0.1059  0.0098  0.0485  199 LEU   A C    
1456 O  O    . LEU   A 200 ? 0.6458 0.3861 0.2967 0.1068  0.0108  0.0518  199 LEU   A O    
1457 C  CB   . LEU   A 200 ? 0.5547 0.3871 0.2926 0.0676  0.015   0.0408  199 LEU   A CB   
1458 C  CG   . LEU   A 200 ? 0.5729 0.394  0.3028 0.0523  0.0156  0.0422  199 LEU   A CG   
1459 C  CD1  . LEU   A 200 ? 0.6    0.3807 0.303  0.0372  0.0227  0.0404  199 LEU   A CD1  
1460 C  CD2  . LEU   A 200 ? 0.5515 0.4086 0.3122 0.0391  0.0146  0.0398  199 LEU   A CD2  
1461 N  N    . THR   A 201 ? 0.5692 0.3992 0.2815 0.1226  0.0031  0.0499  200 THR   A N    
1462 C  CA   . THR   A 201 ? 0.5678 0.4009 0.2684 0.1453  -0.0056 0.0551  200 THR   A CA   
1463 C  C    . THR   A 201 ? 0.6125 0.3915 0.2671 0.1686  -0.0048 0.0582  200 THR   A C    
1464 O  O    . THR   A 201 ? 0.6381 0.383  0.2596 0.1765  -0.0091 0.0638  200 THR   A O    
1465 C  CB   . THR   A 201 ? 0.5349 0.4306 0.2729 0.1589  -0.0116 0.054   200 THR   A CB   
1466 O  OG1  . THR   A 201 ? 0.5232 0.4577 0.2961 0.1353  -0.0114 0.0511  200 THR   A OG1  
1467 C  CG2  . THR   A 201 ? 0.528  0.4398 0.2606 0.1811  -0.0232 0.0583  200 THR   A CG2  
1468 N  N    . LEU   A 202 ? 0.6272 0.3916 0.2738 0.1793  0.0013  0.0545  201 LEU   A N    
1469 C  CA   . LEU   A 202 ? 0.6689 0.3757 0.2675 0.2031  0.0029  0.0563  201 LEU   A CA   
1470 C  C    . LEU   A 202 ? 0.7225 0.3559 0.2737 0.1843  0.0086  0.0577  201 LEU   A C    
1471 O  O    . LEU   A 202 ? 0.7637 0.3438 0.2677 0.2007  0.0066  0.0632  201 LEU   A O    
1472 C  CB   . LEU   A 202 ? 0.6641 0.3779 0.2676 0.2193  0.0086  0.0504  201 LEU   A CB   
1473 C  CG   . LEU   A 202 ? 0.6477 0.4301 0.2897 0.2442  0.0045  0.0497  201 LEU   A CG   
1474 C  CD1  . LEU   A 202 ? 0.6484 0.4375 0.2936 0.2576  0.0129  0.0436  201 LEU   A CD1  
1475 C  CD2  . LEU   A 202 ? 0.659  0.4434 0.2859 0.2787  -0.0052 0.0552  201 LEU   A CD2  
1476 N  N    . GLU   A 203 ? 0.7132 0.3452 0.2758 0.1499  0.0154  0.0531  202 GLU   A N    
1477 C  CA   . GLU   A 203 ? 0.7445 0.3178 0.2688 0.1255  0.0221  0.0532  202 GLU   A CA   
1478 C  C    . GLU   A 203 ? 0.7573 0.314  0.2634 0.1176  0.0201  0.0605  202 GLU   A C    
1479 O  O    . GLU   A 203 ? 0.8034 0.295  0.2571 0.1165  0.0235  0.0648  202 GLU   A O    
1480 C  CB   . GLU   A 203 ? 0.7533 0.3456 0.303  0.0928  0.0282  0.0457  202 GLU   A CB   
1481 C  CG   . GLU   A 203 ? 0.8396 0.3831 0.3566 0.0632  0.0356  0.0443  202 GLU   A CG   
1482 C  CD   . GLU   A 203 ? 0.8938 0.4604 0.4359 0.0345  0.0399  0.0357  202 GLU   A CD   
1483 O  OE1  . GLU   A 203 ? 0.902  0.4932 0.4645 0.0102  0.0423  0.0346  202 GLU   A OE1  
1484 O  OE2  . GLU   A 203 ? 0.9155 0.4776 0.4564 0.0384  0.0403  0.0296  202 GLU   A OE2  
1485 N  N    . LEU   A 204 ? 0.7135 0.3234 0.2568 0.1123  0.015   0.062   203 LEU   A N    
1486 C  CA   . LEU   A 204 ? 0.7197 0.3181 0.2458 0.1066  0.0127  0.0683  203 LEU   A CA   
1487 C  C    . LEU   A 204 ? 0.7845 0.3407 0.2644 0.1374  0.0058  0.0767  203 LEU   A C    
1488 O  O    . LEU   A 204 ? 0.8253 0.3276 0.2582 0.1323  0.0086  0.0829  203 LEU   A O    
1489 C  CB   . LEU   A 204 ? 0.6546 0.3184 0.2272 0.1031  0.0061  0.0672  203 LEU   A CB   
1490 C  CG   . LEU   A 204 ? 0.6153 0.3136 0.2252 0.0752  0.0121  0.0606  203 LEU   A CG   
1491 C  CD1  . LEU   A 204 ? 0.5799 0.3344 0.2293 0.0755  0.0049  0.0591  203 LEU   A CD1  
1492 C  CD2  . LEU   A 204 ? 0.6247 0.2933 0.2136 0.0491  0.0217  0.0606  203 LEU   A CD2  
1493 N  N    . GLN   A 205 ? 0.7931 0.3734 0.2849 0.1702  -0.0025 0.0768  204 GLN   A N    
1494 C  CA   . GLN   A 205 ? 0.8354 0.3879 0.2904 0.2076  -0.0114 0.0838  204 GLN   A CA   
1495 C  C    . GLN   A 205 ? 0.894  0.3583 0.2853 0.2137  -0.0039 0.0861  204 GLN   A C    
1496 O  O    . GLN   A 205 ? 0.9396 0.3461 0.2771 0.224   -0.006  0.0944  204 GLN   A O    
1497 C  CB   . GLN   A 205 ? 0.8426 0.4563 0.3373 0.237   -0.0193 0.0804  204 GLN   A CB   
1498 C  CG   . GLN   A 205 ? 0.9362 0.5527 0.4127 0.2812  -0.0317 0.0859  204 GLN   A CG   
1499 C  CD   . GLN   A 205 ? 1.0571 0.7339 0.5764 0.3027  -0.0329 0.0796  204 GLN   A CD   
1500 O  OE1  . GLN   A 205 ? 1.1144 0.7629 0.6156 0.3198  -0.0262 0.0766  204 GLN   A OE1  
1501 N  NE2  . GLN   A 205 ? 1.0539 0.8145 0.6302 0.2986  -0.0397 0.0766  204 GLN   A NE2  
1502 N  N    . ALA   A 206 ? 0.8939 0.3422 0.2864 0.2032  0.0054  0.0788  205 ALA   A N    
1503 C  CA   . ALA   A 206 ? 0.948  0.309  0.2784 0.2034  0.0133  0.0789  205 ALA   A CA   
1504 C  C    . ALA   A 206 ? 0.9936 0.2943 0.2806 0.17    0.0212  0.0833  205 ALA   A C    
1505 O  O    . ALA   A 206 ? 1.0554 0.271  0.2744 0.1755  0.0248  0.0883  205 ALA   A O    
1506 C  CB   . ALA   A 206 ? 0.9394 0.3055 0.2862 0.1913  0.021   0.0683  205 ALA   A CB   
1507 N  N    . LEU   A 207 ? 0.957  0.2993 0.2804 0.135   0.025   0.0812  206 LEU   A N    
1508 C  CA   . LEU   A 207 ? 0.9814 0.2805 0.2721 0.1002  0.0347  0.0844  206 LEU   A CA   
1509 C  C    . LEU   A 207 ? 1.0093 0.2893 0.2698 0.1085  0.0306  0.0954  206 LEU   A C    
1510 O  O    . LEU   A 207 ? 1.0286 0.2743 0.2599 0.0797  0.0401  0.0989  206 LEU   A O    
1511 C  CB   . LEU   A 207 ? 0.9509 0.3053 0.2933 0.0615  0.0417  0.0763  206 LEU   A CB   
1512 C  CG   . LEU   A 207 ? 0.9559 0.3235 0.3214 0.0463  0.0463  0.0655  206 LEU   A CG   
1513 C  CD1  . LEU   A 207 ? 0.9244 0.3559 0.3446 0.0159  0.05    0.0586  206 LEU   A CD1  
1514 C  CD2  . LEU   A 207 ? 1.0019 0.29   0.3097 0.0298  0.055   0.0639  206 LEU   A CD2  
1515 N  N    . GLY   A 208 ? 1.002  0.3059 0.2686 0.1468  0.0168  0.1005  207 GLY   A N    
1516 C  CA   . GLY   A 208 ? 1.014  0.3058 0.2531 0.1592  0.0095  0.1105  207 GLY   A CA   
1517 C  C    . GLY   A 208 ? 0.993  0.3449 0.2746 0.1365  0.0091  0.1087  207 GLY   A C    
1518 O  O    . GLY   A 208 ? 1.0284 0.3635 0.2814 0.1373  0.0063  0.1162  207 GLY   A O    
1519 N  N    . ILE   A 209 ? 0.9495 0.3671 0.2943 0.1172  0.0121  0.099   208 ILE   A N    
1520 C  CA   . ILE   A 209 ? 0.9253 0.3977 0.3097 0.0977  0.0122  0.096   208 ILE   A CA   
1521 C  C    . ILE   A 209 ? 0.9172 0.4468 0.3348 0.1236  -0.0044 0.0962  208 ILE   A C    
1522 O  O    . ILE   A 209 ? 0.8998 0.4834 0.3663 0.1301  -0.0092 0.0898  208 ILE   A O    
1523 C  CB   . ILE   A 209 ? 0.8943 0.4044 0.3248 0.0674  0.0224  0.0859  208 ILE   A CB   
1524 C  CG1  . ILE   A 209 ? 0.934  0.3918 0.3311 0.0394  0.0375  0.085   208 ILE   A CG1  
1525 C  CG2  . ILE   A 209 ? 0.8663 0.4312 0.3363 0.0519  0.0223  0.082   208 ILE   A CG2  
1526 C  CD1  . ILE   A 209 ? 0.9305 0.4226 0.3687 0.0153  0.0449  0.0748  208 ILE   A CD1  
1527 N  N    . THR   A 210 ? 0.9294 0.4464 0.3178 0.137   -0.0131 0.1035  209 THR   A N    
1528 C  CA   . THR   A 210 ? 0.9049 0.4725 0.3166 0.161   -0.0309 0.1041  209 THR   A CA   
1529 C  C    . THR   A 210 ? 0.8571 0.4837 0.3123 0.1418  -0.0337 0.0979  209 THR   A C    
1530 O  O    . THR   A 210 ? 0.8328 0.5147 0.3236 0.1541  -0.0469 0.0946  209 THR   A O    
1531 C  CB   . THR   A 210 ? 0.9617 0.4837 0.3148 0.1863  -0.0411 0.115   209 THR   A CB   
1532 O  OG1  . THR   A 210 ? 0.9984 0.4742 0.3093 0.1631  -0.0311 0.1199  209 THR   A OG1  
1533 C  CG2  . THR   A 210 ? 1.0029 0.4694 0.3133 0.2147  -0.0418 0.1208  209 THR   A CG2  
1534 N  N    . GLY   A 211 ? 0.8414 0.4557 0.2921 0.112   -0.021  0.0958  210 GLY   A N    
1535 C  CA   . GLY   A 211 ? 0.8059 0.4625 0.2854 0.0955  -0.0222 0.0901  210 GLY   A CA   
1536 C  C    . GLY   A 211 ? 0.7486 0.4563 0.2852 0.0801  -0.0185 0.0801  210 GLY   A C    
1537 O  O    . GLY   A 211 ? 0.7324 0.472  0.29   0.0698  -0.0211 0.075   210 GLY   A O    
1538 N  N    . ILE   A 212 ? 0.7211 0.4321 0.2782 0.0782  -0.0122 0.0771  211 ILE   A N    
1539 C  CA   . ILE   A 212 ? 0.6715 0.4265 0.2781 0.0653  -0.009  0.0686  211 ILE   A CA   
1540 C  C    . ILE   A 212 ? 0.6369 0.4331 0.276  0.0824  -0.02   0.0668  211 ILE   A C    
1541 O  O    . ILE   A 212 ? 0.6495 0.4379 0.2854 0.0983  -0.021  0.0687  211 ILE   A O    
1542 C  CB   . ILE   A 212 ? 0.6772 0.4162 0.2883 0.0478  0.0054  0.0652  211 ILE   A CB   
1543 C  CG1  . ILE   A 212 ? 0.7058 0.4147 0.29   0.0274  0.0178  0.066   211 ILE   A CG1  
1544 C  CG2  . ILE   A 212 ? 0.6518 0.4346 0.3101 0.0386  0.0068  0.0574  211 ILE   A CG2  
1545 C  CD1  . ILE   A 212 ? 0.7326 0.4284 0.319  0.0086  0.0306  0.0624  211 ILE   A CD1  
1546 N  N    . LYS   A 213 ? 0.5946 0.4339 0.263  0.0781  -0.0275 0.0626  212 LYS   A N    
1547 C  CA   . LYS   A 213 ? 0.5546 0.4397 0.2562 0.089   -0.0368 0.0604  212 LYS   A CA   
1548 C  C    . LYS   A 213 ? 0.5265 0.4342 0.2629 0.0767  -0.0292 0.0549  212 LYS   A C    
1549 O  O    . LYS   A 213 ? 0.5265 0.4216 0.2653 0.0596  -0.0195 0.0518  212 LYS   A O    
1550 C  CB   . LYS   A 213 ? 0.5526 0.4708 0.2635 0.0883  -0.0501 0.0586  212 LYS   A CB   
1551 C  CG   . LYS   A 213 ? 0.6054 0.4995 0.2772 0.0997  -0.0588 0.064   212 LYS   A CG   
1552 C  CD   . LYS   A 213 ? 0.6602 0.549  0.3165 0.1293  -0.067  0.0703  212 LYS   A CD   
1553 C  CE   . LYS   A 213 ? 0.749  0.5945 0.3542 0.1432  -0.0723 0.078   212 LYS   A CE   
1554 N  NZ   . LYS   A 213 ? 0.802  0.649  0.3938 0.1776  -0.0838 0.0836  212 LYS   A NZ   
1555 N  N    . THR   A 214 ? 0.5027 0.4442 0.2645 0.0868  -0.0329 0.0538  213 THR   A N    
1556 C  CA   . THR   A 214 ? 0.4857 0.4474 0.2764 0.0762  -0.0259 0.0495  213 THR   A CA   
1557 C  C    . THR   A 214 ? 0.4603 0.4732 0.2823 0.0756  -0.033  0.0472  213 THR   A C    
1558 O  O    . THR   A 214 ? 0.4544 0.4923 0.2802 0.0917  -0.042  0.0489  213 THR   A O    
1559 C  CB   . THR   A 214 ? 0.4975 0.4413 0.2818 0.0872  -0.0185 0.0504  213 THR   A CB   
1560 O  OG1  . THR   A 214 ? 0.5035 0.4578 0.2834 0.1124  -0.0245 0.0532  213 THR   A OG1  
1561 C  CG2  . THR   A 214 ? 0.5197 0.4134 0.2742 0.0809  -0.0103 0.0514  213 THR   A CG2  
1562 N  N    . SER   A 215 ? 0.4399 0.4686 0.2829 0.0571  -0.029  0.0433  214 SER   A N    
1563 C  CA   . SER   A 215 ? 0.4126 0.4864 0.2835 0.0501  -0.0331 0.0409  214 SER   A CA   
1564 C  C    . SER   A 215 ? 0.407  0.4839 0.2929 0.039   -0.023  0.0393  214 SER   A C    
1565 O  O    . SER   A 215 ? 0.4238 0.4716 0.3008 0.0306  -0.0164 0.0385  214 SER   A O    
1566 C  CB   . SER   A 215 ? 0.411  0.4934 0.2827 0.0334  -0.0407 0.0378  214 SER   A CB   
1567 O  OG   . SER   A 215 ? 0.4234 0.5155 0.285  0.0433  -0.0527 0.0388  214 SER   A OG   
1568 N  N    . CYS   A 216 ? 0.3798 0.4941 0.2879 0.0392  -0.0217 0.0389  215 CYS   A N    
1569 C  CA   . CYS   A 216 ? 0.3793 0.4956 0.2974 0.0284  -0.012  0.0383  215 CYS   A CA   
1570 C  C    . CYS   A 216 ? 0.3615 0.5108 0.2981 0.0092  -0.0138 0.0365  215 CYS   A C    
1571 O  O    . CYS   A 216 ? 0.3434 0.5356 0.2972 0.0121  -0.0191 0.0358  215 CYS   A O    
1572 C  CB   . CYS   A 216 ? 0.3753 0.5004 0.2972 0.0454  -0.0051 0.0396  215 CYS   A CB   
1573 S  SG   . CYS   A 216 ? 0.3897 0.5024 0.3121 0.0353  0.0071  0.0394  215 CYS   A SG   
1574 N  N    . LEU   A 217 ? 0.3639 0.4934 0.2953 -0.0103 -0.0101 0.0354  216 LEU   A N    
1575 C  CA   . LEU   A 217 ? 0.3598 0.5108 0.302  -0.0328 -0.0107 0.0337  216 LEU   A CA   
1576 C  C    . LEU   A 217 ? 0.3547 0.5153 0.3046 -0.0393 0.0003  0.0359  216 LEU   A C    
1577 O  O    . LEU   A 217 ? 0.374  0.5014 0.3102 -0.0388 0.007   0.0376  216 LEU   A O    
1578 C  CB   . LEU   A 217 ? 0.3814 0.4967 0.3055 -0.0498 -0.0131 0.0313  216 LEU   A CB   
1579 C  CG   . LEU   A 217 ? 0.39   0.5165 0.3172 -0.0762 -0.0141 0.0289  216 LEU   A CG   
1580 C  CD1  . LEU   A 217 ? 0.3745 0.544  0.3168 -0.0822 -0.0249 0.0255  216 LEU   A CD1  
1581 C  CD2  . LEU   A 217 ? 0.4261 0.5041 0.3278 -0.0887 -0.0139 0.0266  216 LEU   A CD2  
1582 N  N    . CYS   A 218 ? 0.3268 0.5353 0.2984 -0.0454 0.0024  0.0356  217 CYS   A N    
1583 C  CA   . CYS   A 218 ? 0.3246 0.5476 0.3033 -0.0534 0.0148  0.0378  217 CYS   A CA   
1584 C  C    . CYS   A 218 ? 0.3248 0.5722 0.3128 -0.0845 0.017   0.0367  217 CYS   A C    
1585 O  O    . CYS   A 218 ? 0.302  0.6065 0.3157 -0.0891 0.0187  0.0353  217 CYS   A O    
1586 C  CB   . CYS   A 218 ? 0.3086 0.5688 0.3036 -0.0306 0.0197  0.0384  217 CYS   A CB   
1587 S  SG   . CYS   A 218 ? 0.3813 0.6019 0.3571 0.001   0.0194  0.0394  217 CYS   A SG   
1588 N  N    . PRO   A 219 ? 0.3477 0.5532 0.3142 -0.1062 0.0176  0.0371  218 PRO   A N    
1589 C  CA   . PRO   A 219 ? 0.3526 0.5723 0.3213 -0.1398 0.021   0.0361  218 PRO   A CA   
1590 C  C    . PRO   A 219 ? 0.3796 0.6023 0.3458 -0.1508 0.0369  0.0409  218 PRO   A C    
1591 O  O    . PRO   A 219 ? 0.3788 0.575  0.3319 -0.1345 0.044   0.045   218 PRO   A O    
1592 C  CB   . PRO   A 219 ? 0.3852 0.5448 0.3224 -0.1542 0.016   0.0347  218 PRO   A CB   
1593 C  CG   . PRO   A 219 ? 0.4012 0.523  0.3244 -0.1264 0.0111  0.035   218 PRO   A CG   
1594 C  CD   . PRO   A 219 ? 0.3686 0.5119 0.3062 -0.1012 0.0158  0.0379  218 PRO   A CD   
1595 N  N    . VAL   A 220 ? 0.3904 0.6454 0.367  -0.1813 0.0426  0.0401  219 VAL   A N    
1596 C  CA   . VAL   A 220 ? 0.4129 0.6638 0.38   -0.1997 0.0591  0.0452  219 VAL   A CA   
1597 C  C    . VAL   A 220 ? 0.4763 0.6481 0.3986 -0.219  0.0596  0.0482  219 VAL   A C    
1598 O  O    . VAL   A 220 ? 0.5042 0.6324 0.4089 -0.2075 0.0488  0.0463  219 VAL   A O    
1599 C  CB   . VAL   A 220 ? 0.3876 0.7108 0.3856 -0.2261 0.0663  0.0428  219 VAL   A CB   
1600 C  CG1  . VAL   A 220 ? 0.3585 0.7574 0.3982 -0.1998 0.0644  0.0394  219 VAL   A CG1  
1601 C  CG2  . VAL   A 220 ? 0.3861 0.7123 0.383  -0.261  0.0576  0.0376  219 VAL   A CG2  
1602 N  N    . PHE   A 221 ? 0.5013 0.6511 0.402  -0.2454 0.0724  0.0532  220 PHE   A N    
1603 C  CA   . PHE   A 221 ? 0.5585 0.6288 0.4117 -0.2603 0.0729  0.0566  220 PHE   A CA   
1604 C  C    . PHE   A 221 ? 0.5795 0.6229 0.42   -0.2765 0.0603  0.0502  220 PHE   A C    
1605 O  O    . PHE   A 221 ? 0.5658 0.6438 0.4212 -0.3058 0.0582  0.045   220 PHE   A O    
1606 C  CB   . PHE   A 221 ? 0.5785 0.6335 0.4091 -0.2909 0.0893  0.0631  220 PHE   A CB   
1607 C  CG   . PHE   A 221 ? 0.648  0.6121 0.4217 -0.3007 0.0906  0.0684  220 PHE   A CG   
1608 C  CD1  . PHE   A 221 ? 0.6817 0.6105 0.4275 -0.3392 0.0924  0.0675  220 PHE   A CD1  
1609 C  CD2  . PHE   A 221 ? 0.6931 0.6057 0.4393 -0.2704 0.0889  0.0736  220 PHE   A CD2  
1610 C  CE1  . PHE   A 221 ? 0.7418 0.5793 0.4292 -0.3445 0.0934  0.0726  220 PHE   A CE1  
1611 C  CE2  . PHE   A 221 ? 0.7513 0.5814 0.4442 -0.2744 0.0888  0.0785  220 PHE   A CE2  
1612 C  CZ   . PHE   A 221 ? 0.7689 0.5585 0.4304 -0.3101 0.0916  0.0784  220 PHE   A CZ   
1613 N  N    . VAL   A 222 ? 0.6041 0.5882 0.4172 -0.2569 0.052   0.0497  221 VAL   A N    
1614 C  CA   . VAL   A 222 ? 0.6276 0.5728 0.4192 -0.2675 0.0415  0.0435  221 VAL   A CA   
1615 C  C    . VAL   A 222 ? 0.6881 0.5488 0.4249 -0.2778 0.0469  0.0481  221 VAL   A C    
1616 O  O    . VAL   A 222 ? 0.7151 0.5415 0.4331 -0.2553 0.051   0.0545  221 VAL   A O    
1617 C  CB   . VAL   A 222 ? 0.6206 0.5637 0.4209 -0.2353 0.029   0.0386  221 VAL   A CB   
1618 C  CG1  . VAL   A 222 ? 0.6353 0.5495 0.4165 -0.2492 0.0189  0.0307  221 VAL   A CG1  
1619 C  CG2  . VAL   A 222 ? 0.5815 0.5959 0.4276 -0.2167 0.025   0.0368  221 VAL   A CG2  
1620 N  N    . ASN   A 223 ? 0.7101 0.5357 0.4189 -0.3109 0.0461  0.0445  222 ASN   A N    
1621 C  CA   . ASN   A 223 ? 0.7652 0.5017 0.4141 -0.3234 0.0509  0.0483  222 ASN   A CA   
1622 C  C    . ASN   A 223 ? 0.7952 0.4705 0.414  -0.2908 0.042   0.0458  222 ASN   A C    
1623 O  O    . ASN   A 223 ? 0.833  0.465  0.4235 -0.3009 0.0359  0.0389  222 ASN   A O    
1624 C  CB   . ASN   A 223 ? 0.8016 0.5246 0.4322 -0.3718 0.0518  0.0431  222 ASN   A CB   
1625 C  CG   . ASN   A 223 ? 0.927  0.5483 0.4879 -0.3895 0.0557  0.0454  222 ASN   A CG   
1626 O  OD1  . ASN   A 223 ? 0.9888 0.558  0.5134 -0.3833 0.0651  0.0554  222 ASN   A OD1  
1627 N  ND2  . ASN   A 223 ? 0.9581 0.545  0.4946 -0.4107 0.0479  0.036   222 ASN   A ND2  
1628 N  N    . THR   A 224 ? 0.7762 0.4519 0.4023 -0.252  0.0413  0.0501  223 THR   A N    
1629 C  CA   . THR   A 224 ? 0.7866 0.4177 0.3913 -0.2189 0.034   0.0473  223 THR   A CA   
1630 C  C    . THR   A 224 ? 0.8149 0.3841 0.3777 -0.1992 0.038   0.0555  223 THR   A C    
1631 O  O    . THR   A 224 ? 0.829  0.3631 0.3733 -0.1699 0.0324  0.0532  223 THR   A O    
1632 C  CB   . THR   A 224 ? 0.7604 0.4472 0.4097 -0.1872 0.0279  0.0444  223 THR   A CB   
1633 O  OG1  . THR   A 224 ? 0.7534 0.4737 0.4239 -0.1758 0.0336  0.0517  223 THR   A OG1  
1634 C  CG2  . THR   A 224 ? 0.7261 0.4676 0.4115 -0.1972 0.0214  0.0367  223 THR   A CG2  
1635 N  N    . GLY   A 225 ? 0.8161 0.3785 0.3665 -0.2127 0.0476  0.0648  224 GLY   A N    
1636 C  CA   . GLY   A 225 ? 0.8456 0.3557 0.3566 -0.1938 0.0509  0.0741  224 GLY   A CA   
1637 C  C    . GLY   A 225 ? 0.817  0.3695 0.3583 -0.1609 0.0488  0.0772  224 GLY   A C    
1638 O  O    . GLY   A 225 ? 0.8368 0.3531 0.3489 -0.1405 0.0488  0.084   224 GLY   A O    
1639 N  N    . PHE   A 226 ? 0.7698 0.396  0.3662 -0.1546 0.046   0.0718  225 PHE   A N    
1640 C  CA   . PHE   A 226 ? 0.7514 0.4188 0.3769 -0.1277 0.0441  0.0731  225 PHE   A CA   
1641 C  C    . PHE   A 226 ? 0.7988 0.4645 0.4111 -0.1325 0.0533  0.0826  225 PHE   A C    
1642 O  O    . PHE   A 226 ? 0.8037 0.4582 0.4051 -0.1083 0.0508  0.0865  225 PHE   A O    
1643 C  CB   . PHE   A 226 ? 0.6861 0.4221 0.3638 -0.1267 0.0411  0.0662  225 PHE   A CB   
1644 C  CG   . PHE   A 226 ? 0.6438 0.4166 0.349  -0.1002 0.0382  0.0656  225 PHE   A CG   
1645 C  CD1  . PHE   A 226 ? 0.6454 0.4059 0.3481 -0.0733 0.0305  0.0626  225 PHE   A CD1  
1646 C  CD2  . PHE   A 226 ? 0.6162 0.437  0.3491 -0.1029 0.0436  0.0669  225 PHE   A CD2  
1647 C  CE1  . PHE   A 226 ? 0.6288 0.4224 0.3554 -0.0539 0.0278  0.0611  225 PHE   A CE1  
1648 C  CE2  . PHE   A 226 ? 0.6069 0.4536 0.3589 -0.0805 0.0409  0.0655  225 PHE   A CE2  
1649 C  CZ   . PHE   A 226 ? 0.6086 0.4407 0.3569 -0.0582 0.0328  0.0626  225 PHE   A CZ   
1650 N  N    . THR   A 227 ? 0.8306 0.5094 0.4433 -0.1646 0.0641  0.0859  226 THR   A N    
1651 C  CA   . THR   A 227 ? 0.8802 0.5489 0.471  -0.1776 0.0765  0.0955  226 THR   A CA   
1652 C  C    . THR   A 227 ? 0.9436 0.5722 0.5    -0.2162 0.0854  0.099   226 THR   A C    
1653 O  O    . THR   A 227 ? 0.947  0.5748 0.5094 -0.2343 0.0816  0.0924  226 THR   A O    
1654 C  CB   . THR   A 227 ? 0.8689 0.6063 0.4992 -0.1778 0.0843  0.0955  226 THR   A CB   
1655 O  OG1  . THR   A 227 ? 0.8608 0.6524 0.528  -0.2019 0.0886  0.0902  226 THR   A OG1  
1656 C  CG2  . THR   A 227 ? 0.8581 0.6246 0.5138 -0.143  0.0761  0.092   226 THR   A CG2  
1657 N  N    . LYS   A 228 ? 0.9976 0.591  0.5153 -0.231  0.0972  0.1092  227 LYS   A N    
1658 C  CA   . LYS   A 228 ? 1.07   0.6143 0.5458 -0.2707 0.1071  0.1137  227 LYS   A CA   
1659 C  C    . LYS   A 228 ? 1.0792 0.6808 0.5886 -0.3135 0.1171  0.1094  227 LYS   A C    
1660 O  O    . LYS   A 228 ? 1.1005 0.6756 0.5933 -0.3439 0.1168  0.1057  227 LYS   A O    
1661 C  CB   . LYS   A 228 ? 1.1386 0.6221 0.5561 -0.2745 0.1178  0.1272  227 LYS   A CB   
1662 C  CG   . LYS   A 228 ? 1.251  0.6598 0.6198 -0.2384 0.1066  0.1319  227 LYS   A CG   
1663 C  CD   . LYS   A 228 ? 1.3732 0.7194 0.6795 -0.2413 0.1162  0.1462  227 LYS   A CD   
1664 C  CE   . LYS   A 228 ? 1.4795 0.7495 0.7335 -0.2032 0.1035  0.1512  227 LYS   A CE   
1665 N  NZ   . LYS   A 228 ? 1.5511 0.7552 0.7707 -0.2057 0.0967  0.1473  227 LYS   A NZ   
1666 N  N    . ASN   A 229 ? 1.0622 0.7393 0.6144 -0.3167 0.1263  0.1095  228 ASN   A N    
1667 C  CA   . ASN   A 229 ? 1.059  0.8011 0.6465 -0.3551 0.1368  0.1056  228 ASN   A CA   
1668 C  C    . ASN   A 229 ? 1.032  0.8722 0.6864 -0.3358 0.136   0.0994  228 ASN   A C    
1669 O  O    . ASN   A 229 ? 1.0331 0.8816 0.6962 -0.299  0.1325  0.1007  228 ASN   A O    
1670 C  CB   . ASN   A 229 ? 1.1005 0.8221 0.6531 -0.3886 0.1576  0.1158  228 ASN   A CB   
1671 C  CG   . ASN   A 229 ? 1.2173 0.8374 0.6972 -0.4127 0.161   0.123   228 ASN   A CG   
1672 O  OD1  . ASN   A 229 ? 1.2567 0.8479 0.7228 -0.4385 0.156   0.1177  228 ASN   A OD1  
1673 N  ND2  . ASN   A 229 ? 1.2702 0.8292 0.6971 -0.4041 0.169   0.1351  228 ASN   A ND2  
1674 N  N    . PRO   A 230 ? 1.0045 0.9198 0.705  -0.3594 0.139   0.0924  229 PRO   A N    
1675 C  CA   . PRO   A 230 ? 0.9673 0.9716 0.7261 -0.3372 0.139   0.0872  229 PRO   A CA   
1676 C  C    . PRO   A 230 ? 0.9778 1.007  0.736  -0.3342 0.1576  0.0938  229 PRO   A C    
1677 O  O    . PRO   A 230 ? 0.9958 1.0046 0.7249 -0.3655 0.1738  0.1007  229 PRO   A O    
1678 C  CB   . PRO   A 230 ? 0.9354 1.0088 0.7364 -0.3657 0.1371  0.0786  229 PRO   A CB   
1679 C  CG   . PRO   A 230 ? 0.9624 0.9943 0.7277 -0.4134 0.1446  0.0811  229 PRO   A CG   
1680 C  CD   . PRO   A 230 ? 0.9968 0.9196 0.6963 -0.4068 0.1422  0.0885  229 PRO   A CD   
1681 N  N    . SER   A 231 ? 0.968  1.0364 0.7536 -0.2973 0.156   0.0917  230 SER   A N    
1682 C  CA   . SER   A 231 ? 0.9784 1.0677 0.7608 -0.2888 0.1728  0.0965  230 SER   A CA   
1683 C  C    . SER   A 231 ? 0.9618 1.1322 0.7788 -0.3139 0.1913  0.0945  230 SER   A C    
1684 O  O    . SER   A 231 ? 0.9591 1.1466 0.7694 -0.3121 0.2089  0.0987  230 SER   A O    
1685 C  CB   . SER   A 231 ? 0.9787 1.0788 0.7753 -0.2428 0.1645  0.0933  230 SER   A CB   
1686 O  OG   . SER   A 231 ? 0.9544 1.1244 0.8033 -0.2286 0.158   0.0842  230 SER   A OG   
1687 N  N    . THR   A 232 ? 0.947  1.1704 0.801  -0.3368 0.1873  0.0876  231 THR   A N    
1688 C  CA   . THR   A 232 ? 0.9229 1.2356 0.8175 -0.3622 0.2026  0.0839  231 THR   A CA   
1689 C  C    . THR   A 232 ? 0.9433 1.2547 0.8325 -0.4163 0.2049  0.083   231 THR   A C    
1690 O  O    . THR   A 232 ? 0.9804 1.2194 0.8346 -0.4285 0.1928  0.0842  231 THR   A O    
1691 C  CB   . THR   A 232 ? 0.8907 1.2911 0.8466 -0.3313 0.193   0.0738  231 THR   A CB   
1692 O  OG1  . THR   A 232 ? 0.8973 1.2988 0.8695 -0.3336 0.1717  0.0673  231 THR   A OG1  
1693 C  CG2  . THR   A 232 ? 0.8995 1.2928 0.856  -0.2801 0.1897  0.0736  231 THR   A CG2  
1694 N  N    . ARG   A 233 ? 0.9166 1.3094 0.84   -0.449  0.2204  0.0798  232 ARG   A N    
1695 C  CA   . ARG   A 233 ? 0.9297 1.3353 0.8543 -0.5051 0.2229  0.077   232 ARG   A CA   
1696 C  C    . ARG   A 233 ? 0.9115 1.3654 0.8794 -0.5022 0.1995  0.0651  232 ARG   A C    
1697 O  O    . ARG   A 233 ? 0.8681 1.4154 0.8848 -0.5243 0.2011  0.0573  232 ARG   A O    
1698 C  CB   . ARG   A 233 ? 0.9173 1.4009 0.8657 -0.5425 0.2492  0.0775  232 ARG   A CB   
1699 C  CG   . ARG   A 233 ? 0.9986 1.4376 0.9023 -0.5451 0.2736  0.0893  232 ARG   A CG   
1700 C  CD   . ARG   A 233 ? 1.0367 1.5137 0.938  -0.6019 0.3013  0.0925  232 ARG   A CD   
1701 N  NE   . ARG   A 233 ? 1.1284 1.5396 0.9712 -0.6064 0.3232  0.1057  232 ARG   A NE   
1702 C  CZ   . ARG   A 233 ? 1.1649 1.5916 0.9911 -0.6519 0.3516  0.1115  232 ARG   A CZ   
1703 N  NH1  . ARG   A 233 ? 1.1289 1.6404 0.9966 -0.6994 0.3622  0.1047  232 ARG   A NH1  
1704 N  NH2  . ARG   A 233 ? 1.1975 1.5563 0.9643 -0.6512 0.3696  0.1243  232 ARG   A NH2  
1705 N  N    . LEU   A 234 ? 0.9399 1.3316 0.8886 -0.4744 0.1779  0.0638  233 LEU   A N    
1706 C  CA   . LEU   A 234 ? 0.9286 1.349  0.9072 -0.4656 0.1545  0.0538  233 LEU   A CA   
1707 C  C    . LEU   A 234 ? 0.9532 1.3452 0.9119 -0.5153 0.1476  0.0493  233 LEU   A C    
1708 O  O    . LEU   A 234 ? 1.0085 1.3016 0.9097 -0.5305 0.1472  0.0541  233 LEU   A O    
1709 C  CB   . LEU   A 234 ? 0.9561 1.3174 0.9172 -0.4163 0.1376  0.0549  233 LEU   A CB   
1710 C  CG   . LEU   A 234 ? 0.961  1.3379 0.9438 -0.4004 0.1137  0.0461  233 LEU   A CG   
1711 C  CD1  . LEU   A 234 ? 0.9104 1.3986 0.9558 -0.3889 0.1089  0.0384  233 LEU   A CD1  
1712 C  CD2  . LEU   A 234 ? 0.9949 1.3106 0.9564 -0.3556 0.1018  0.0483  233 LEU   A CD2  
1713 N  N    . ILE   A 237 ? 0.6983 0.8569 0.5493 -0.524  0.0745  0.0275  236 ILE   A N    
1714 C  CA   . ILE   A 237 ? 0.7167 0.8291 0.554  -0.4706 0.0704  0.0331  236 ILE   A CA   
1715 C  C    . ILE   A 237 ? 0.7116 0.8078 0.5486 -0.4468 0.0497  0.0253  236 ILE   A C    
1716 O  O    . ILE   A 237 ? 0.7381 0.806  0.5536 -0.4735 0.0405  0.0178  236 ILE   A O    
1717 C  CB   . ILE   A 237 ? 0.7806 0.7924 0.5567 -0.4712 0.0824  0.0432  236 ILE   A CB   
1718 C  CG1  . ILE   A 237 ? 0.7844 0.8204 0.5657 -0.4793 0.1031  0.0526  236 ILE   A CG1  
1719 C  CG2  . ILE   A 237 ? 0.8134 0.7642 0.566  -0.4235 0.074   0.0461  236 ILE   A CG2  
1720 C  CD1  . ILE   A 237 ? 0.8548 0.7951 0.5712 -0.4909 0.1156  0.063   236 ILE   A CD1  
1721 N  N    . LEU   A 238 ? 0.6774 0.791  0.5359 -0.3988 0.043   0.0266  237 LEU   A N    
1722 C  CA   . LEU   A 238 ? 0.6699 0.7702 0.5278 -0.3736 0.0255  0.0203  237 LEU   A CA   
1723 C  C    . LEU   A 238 ? 0.7187 0.7216 0.5216 -0.3728 0.0218  0.0194  237 LEU   A C    
1724 O  O    . LEU   A 238 ? 0.7503 0.6914 0.5199 -0.3614 0.0307  0.0267  237 LEU   A O    
1725 C  CB   . LEU   A 238 ? 0.643  0.7675 0.5258 -0.3242 0.0229  0.0238  237 LEU   A CB   
1726 C  CG   . LEU   A 238 ? 0.5928 0.8094 0.5283 -0.3099 0.0194  0.0218  237 LEU   A CG   
1727 C  CD1  . LEU   A 238 ? 0.5902 0.8073 0.5354 -0.2645 0.019   0.0259  237 LEU   A CD1  
1728 C  CD2  . LEU   A 238 ? 0.5788 0.8345 0.5318 -0.3183 0.0027  0.0127  237 LEU   A CD2  
1729 N  N    . GLU   A 239 ? 0.7205 0.7111 0.5134 -0.3801 0.0077  0.0101  238 GLU   A N    
1730 C  CA   . GLU   A 239 ? 0.7685 0.6716 0.5113 -0.3721 0.0033  0.0074  238 GLU   A CA   
1731 C  C    . GLU   A 239 ? 0.7558 0.6615 0.5099 -0.3263 -0.0043 0.0069  238 GLU   A C    
1732 O  O    . GLU   A 239 ? 0.7253 0.6967 0.5207 -0.3095 -0.0107 0.0059  238 GLU   A O    
1733 C  CB   . GLU   A 239 ? 0.8309 0.7071 0.5464 -0.4081 -0.0058 -0.0034 238 GLU   A CB   
1734 C  CG   . GLU   A 239 ? 0.9609 0.7834 0.6348 -0.4524 0.0038  -0.0026 238 GLU   A CG   
1735 C  CD   . GLU   A 239 ? 1.1355 0.8767 0.7637 -0.4434 0.0176  0.0076  238 GLU   A CD   
1736 O  OE1  . GLU   A 239 ? 1.1939 0.9012 0.8112 -0.4009 0.0175  0.0118  238 GLU   A OE1  
1737 O  OE2  . GLU   A 239 ? 1.1755 0.8872 0.777  -0.4802 0.0284  0.0113  238 GLU   A OE2  
1738 N  N    . THR   A 240 ? 0.7806 0.6159 0.4975 -0.3054 -0.0032 0.0079  239 THR   A N    
1739 C  CA   . THR   A 240 ? 0.7711 0.607  0.4968 -0.2644 -0.008  0.0076  239 THR   A CA   
1740 C  C    . THR   A 240 ? 0.7539 0.6188 0.4926 -0.26   -0.0213 -0.001  239 THR   A C    
1741 O  O    . THR   A 240 ? 0.7356 0.636  0.5001 -0.2331 -0.0251 0.0001  239 THR   A O    
1742 C  CB   . THR   A 240 ? 0.8175 0.5766 0.5005 -0.2453 -0.0042 0.0089  239 THR   A CB   
1743 O  OG1  . THR   A 240 ? 0.8603 0.58   0.519  -0.2534 0.0062  0.0165  239 THR   A OG1  
1744 C  CG2  . THR   A 240 ? 0.8016 0.5704 0.4992 -0.206  -0.0054 0.0103  239 THR   A CG2  
1745 N  N    . ASP   A 241 ? 0.7614 0.6062 0.4773 -0.2871 -0.0284 -0.0096 240 ASP   A N    
1746 C  CA   . ASP   A 241 ? 0.7544 0.6211 0.475  -0.2858 -0.0421 -0.0184 240 ASP   A CA   
1747 C  C    . ASP   A 241 ? 0.6983 0.6531 0.468  -0.287  -0.0502 -0.018  240 ASP   A C    
1748 O  O    . ASP   A 241 ? 0.69   0.67   0.4702 -0.2694 -0.0604 -0.0211 240 ASP   A O    
1749 C  CB   . ASP   A 241 ? 0.8152 0.6354 0.4946 -0.318  -0.0483 -0.0288 240 ASP   A CB   
1750 C  CG   . ASP   A 241 ? 0.9083 0.7257 0.5804 -0.3616 -0.0441 -0.0291 240 ASP   A CG   
1751 O  OD1  . ASP   A 241 ? 0.9496 0.7247 0.602  -0.3652 -0.0313 -0.0221 240 ASP   A OD1  
1752 O  OD2  . ASP   A 241 ? 0.9313 0.7884 0.6153 -0.3931 -0.0536 -0.0365 240 ASP   A OD2  
1753 N  N    . THR   A 242 ? 0.6577 0.6588 0.4552 -0.3062 -0.045  -0.0142 241 THR   A N    
1754 C  CA   . THR   A 242 ? 0.5953 0.6854 0.4418 -0.3039 -0.0512 -0.0137 241 THR   A CA   
1755 C  C    . THR   A 242 ? 0.5603 0.6729 0.4304 -0.261  -0.0482 -0.0062 241 THR   A C    
1756 O  O    . THR   A 242 ? 0.5355 0.6939 0.4284 -0.2426 -0.0582 -0.0073 241 THR   A O    
1757 C  CB   . THR   A 242 ? 0.5795 0.7107 0.4475 -0.3347 -0.0427 -0.0116 241 THR   A CB   
1758 O  OG1  . THR   A 242 ? 0.6077 0.7125 0.4495 -0.3787 -0.0452 -0.0189 241 THR   A OG1  
1759 C  CG2  . THR   A 242 ? 0.5274 0.7567 0.4488 -0.3282 -0.0478 -0.0115 241 THR   A CG2  
1760 N  N    . VAL   A 243 ? 0.5571 0.6333 0.4173 -0.2455 -0.0351 0.0011  242 VAL   A N    
1761 C  CA   . VAL   A 243 ? 0.536  0.6253 0.4133 -0.2094 -0.0309 0.0076  242 VAL   A CA   
1762 C  C    . VAL   A 243 ? 0.5445 0.6107 0.4088 -0.1847 -0.0386 0.0053  242 VAL   A C    
1763 O  O    . VAL   A 243 ? 0.5307 0.6281 0.4139 -0.1608 -0.0424 0.0075  242 VAL   A O    
1764 C  CB   . VAL   A 243 ? 0.5525 0.6067 0.4184 -0.2036 -0.0164 0.0148  242 VAL   A CB   
1765 C  CG1  . VAL   A 243 ? 0.5505 0.6152 0.431  -0.1692 -0.0126 0.0202  242 VAL   A CG1  
1766 C  CG2  . VAL   A 243 ? 0.5389 0.6167 0.4146 -0.2305 -0.0074 0.0176  242 VAL   A CG2  
1767 N  N    . ALA   A 244 ? 0.566  0.5768 0.3954 -0.1906 -0.0405 0.0005  243 ALA   A N    
1768 C  CA   . ALA   A 244 ? 0.582  0.5706 0.3959 -0.1703 -0.0459 -0.0025 243 ALA   A CA   
1769 C  C    . ALA   A 244 ? 0.5602 0.5889 0.3845 -0.1722 -0.0603 -0.0072 243 ALA   A C    
1770 O  O    . ALA   A 244 ? 0.5524 0.5888 0.3789 -0.1492 -0.064  -0.0056 243 ALA   A O    
1771 C  CB   . ALA   A 244 ? 0.624  0.5471 0.397  -0.177  -0.0438 -0.0079 243 ALA   A CB   
1772 N  N    . ARG   A 245 ? 0.5508 0.6069 0.3809 -0.2003 -0.0686 -0.0125 244 ARG   A N    
1773 C  CA   . ARG   A 245 ? 0.5437 0.6462 0.3859 -0.2024 -0.0846 -0.0172 244 ARG   A CA   
1774 C  C    . ARG   A 245 ? 0.5033 0.6666 0.3833 -0.1791 -0.0864 -0.0106 244 ARG   A C    
1775 O  O    . ARG   A 245 ? 0.5013 0.6814 0.3825 -0.1587 -0.0962 -0.0101 244 ARG   A O    
1776 C  CB   . ARG   A 245 ? 0.5754 0.6991 0.418  -0.241  -0.0933 -0.0254 244 ARG   A CB   
1777 C  CG   . ARG   A 245 ? 0.6975 0.7909 0.5059 -0.2526 -0.1061 -0.0354 244 ARG   A CG   
1778 C  CD   . ARG   A 245 ? 0.7898 0.9058 0.5969 -0.2941 -0.1169 -0.0451 244 ARG   A CD   
1779 N  NE   . ARG   A 245 ? 0.8929 0.9577 0.6743 -0.3258 -0.1066 -0.0479 244 ARG   A NE   
1780 C  CZ   . ARG   A 245 ? 0.9289 1.0183 0.7296 -0.3515 -0.0987 -0.0454 244 ARG   A CZ   
1781 N  NH1  . ARG   A 245 ? 0.887  1.0576 0.7373 -0.3478 -0.0992 -0.0409 244 ARG   A NH1  
1782 N  NH2  . ARG   A 245 ? 0.9688 0.9998 0.7366 -0.38   -0.0893 -0.0473 244 ARG   A NH2  
1783 N  N    . SER   A 246 ? 0.4767 0.6668 0.3824 -0.18   -0.0762 -0.0053 245 SER   A N    
1784 C  CA   . SER   A 246 ? 0.4498 0.693  0.3881 -0.1557 -0.0758 0.0003  245 SER   A CA   
1785 C  C    . SER   A 246 ? 0.456  0.6697 0.3831 -0.1212 -0.0726 0.0059  245 SER   A C    
1786 O  O    . SER   A 246 ? 0.4457 0.6872 0.3822 -0.0981 -0.0802 0.0082  245 SER   A O    
1787 C  CB   . SER   A 246 ? 0.459  0.7277 0.4204 -0.1644 -0.0626 0.0042  245 SER   A CB   
1788 O  OG   . SER   A 246 ? 0.4785 0.8076 0.4653 -0.1892 -0.068  -0.0004 245 SER   A OG   
1789 N  N    . LEU   A 247 ? 0.4694 0.6259 0.3743 -0.1181 -0.0616 0.0081  246 LEU   A N    
1790 C  CA   . LEU   A 247 ? 0.474  0.6006 0.3671 -0.0914 -0.057  0.0124  246 LEU   A CA   
1791 C  C    . LEU   A 247 ? 0.4924 0.6072 0.3664 -0.0813 -0.0674 0.0101  246 LEU   A C    
1792 O  O    . LEU   A 247 ? 0.492  0.6184 0.3686 -0.0592 -0.0705 0.0142  246 LEU   A O    
1793 C  CB   . LEU   A 247 ? 0.4874 0.5632 0.3628 -0.0928 -0.0449 0.0135  246 LEU   A CB   
1794 C  CG   . LEU   A 247 ? 0.5074 0.5553 0.3717 -0.07   -0.0396 0.0165  246 LEU   A CG   
1795 C  CD1  . LEU   A 247 ? 0.5017 0.5739 0.3832 -0.0506 -0.0372 0.0221  246 LEU   A CD1  
1796 C  CD2  . LEU   A 247 ? 0.5281 0.5366 0.3793 -0.0708 -0.0295 0.0167  246 LEU   A CD2  
1797 N  N    . ILE   A 248 ? 0.5037 0.593  0.3546 -0.0971 -0.0727 0.0035  247 ILE   A N    
1798 C  CA   . ILE   A 248 ? 0.5252 0.6003 0.3531 -0.0882 -0.0814 0.0012  247 ILE   A CA   
1799 C  C    . ILE   A 248 ? 0.5035 0.6257 0.3437 -0.0797 -0.0965 0.0021  247 ILE   A C    
1800 O  O    . ILE   A 248 ? 0.5043 0.6196 0.3317 -0.0589 -0.1    0.0059  247 ILE   A O    
1801 C  CB   . ILE   A 248 ? 0.5624 0.5989 0.3594 -0.1058 -0.0838 -0.0072 247 ILE   A CB   
1802 C  CG1  . ILE   A 248 ? 0.5962 0.6032 0.3639 -0.0912 -0.0848 -0.008  247 ILE   A CG1  
1803 C  CG2  . ILE   A 248 ? 0.559  0.6199 0.3576 -0.1314 -0.097  -0.0146 247 ILE   A CG2  
1804 C  CD1  . ILE   A 248 ? 0.6258 0.6002 0.386  -0.0763 -0.0699 -0.0043 247 ILE   A CD1  
1805 N  N    . ASP   A 249 ? 0.477  0.6489 0.3425 -0.0945 -0.1045 -0.0007 248 ASP   A N    
1806 C  CA   . ASP   A 249 ? 0.4554 0.6828 0.3376 -0.0841 -0.1202 -0.0005 248 ASP   A CA   
1807 C  C    . ASP   A 249 ? 0.4455 0.6892 0.3409 -0.0514 -0.1168 0.0081  248 ASP   A C    
1808 O  O    . ASP   A 249 ? 0.4508 0.7069 0.3384 -0.0301 -0.1282 0.0107  248 ASP   A O    
1809 C  CB   . ASP   A 249 ? 0.4579 0.7423 0.3687 -0.1094 -0.128  -0.0064 248 ASP   A CB   
1810 C  CG   . ASP   A 249 ? 0.5703 0.8388 0.4606 -0.1418 -0.1368 -0.0164 248 ASP   A CG   
1811 O  OD1  . ASP   A 249 ? 0.5985 0.8366 0.457  -0.1371 -0.1458 -0.0195 248 ASP   A OD1  
1812 O  OD2  . ASP   A 249 ? 0.6114 0.8944 0.5137 -0.1728 -0.1342 -0.0213 248 ASP   A OD2  
1813 N  N    . GLY   A 250 ? 0.4328 0.6687 0.3418 -0.0468 -0.1013 0.0125  249 GLY   A N    
1814 C  CA   . GLY   A 250 ? 0.4237 0.6641 0.3395 -0.0172 -0.0959 0.0197  249 GLY   A CA   
1815 C  C    . GLY   A 250 ? 0.4453 0.6327 0.3284 0.0014  -0.0927 0.0243  249 GLY   A C    
1816 O  O    . GLY   A 250 ? 0.4472 0.6369 0.323  0.0269  -0.0971 0.0293  249 GLY   A O    
1817 N  N    . ILE   A 251 ? 0.4576 0.5963 0.3192 -0.0109 -0.0843 0.0226  250 ILE   A N    
1818 C  CA   . ILE   A 251 ? 0.478  0.5695 0.3094 0.0013  -0.079  0.026   250 ILE   A CA   
1819 C  C    . ILE   A 251 ? 0.5025 0.5909 0.3094 0.0108  -0.0924 0.0266  250 ILE   A C    
1820 O  O    . ILE   A 251 ? 0.5187 0.5888 0.3067 0.0308  -0.0924 0.0328  250 ILE   A O    
1821 C  CB   . ILE   A 251 ? 0.4913 0.5431 0.3093 -0.0139 -0.0679 0.0223  250 ILE   A CB   
1822 C  CG1  . ILE   A 251 ? 0.4965 0.5463 0.3333 -0.0184 -0.0554 0.0232  250 ILE   A CG1  
1823 C  CG2  . ILE   A 251 ? 0.5122 0.5237 0.3004 -0.005  -0.0623 0.0245  250 ILE   A CG2  
1824 C  CD1  . ILE   A 251 ? 0.5232 0.5402 0.3495 -0.0308 -0.0465 0.0194  250 ILE   A CD1  
1825 N  N    . LEU   A 252 ? 0.4966 0.6007 0.3004 -0.0042 -0.1042 0.0204  251 LEU   A N    
1826 C  CA   . LEU   A 252 ? 0.5079 0.6107 0.286  0.0033  -0.1188 0.0201  251 LEU   A CA   
1827 C  C    . LEU   A 252 ? 0.5018 0.6398 0.2869 0.0278  -0.1319 0.0256  251 LEU   A C    
1828 O  O    . LEU   A 252 ? 0.524  0.6471 0.2791 0.0432  -0.1415 0.0292  251 LEU   A O    
1829 C  CB   . LEU   A 252 ? 0.5046 0.6179 0.2776 -0.0207 -0.1298 0.0105  251 LEU   A CB   
1830 C  CG   . LEU   A 252 ? 0.5319 0.6021 0.2881 -0.0409 -0.1182 0.0043  251 LEU   A CG   
1831 C  CD1  . LEU   A 252 ? 0.5356 0.61   0.2797 -0.0634 -0.1302 -0.0058 251 LEU   A CD1  
1832 C  CD2  . LEU   A 252 ? 0.5721 0.5924 0.2954 -0.03   -0.1071 0.0074  251 LEU   A CD2  
1833 N  N    . THR   A 253 ? 0.4739 0.6566 0.2953 0.0339  -0.1319 0.0266  252 THR   A N    
1834 C  CA   . THR   A 253 ? 0.4675 0.6873 0.2976 0.0623  -0.1436 0.0312  252 THR   A CA   
1835 C  C    . THR   A 253 ? 0.4849 0.6827 0.3122 0.0874  -0.1314 0.039   252 THR   A C    
1836 O  O    . THR   A 253 ? 0.4818 0.7086 0.3172 0.1142  -0.1386 0.0426  252 THR   A O    
1837 C  CB   . THR   A 253 ? 0.4401 0.7354 0.3128 0.0538  -0.1537 0.0255  252 THR   A CB   
1838 O  OG1  . THR   A 253 ? 0.4492 0.7535 0.3504 0.036   -0.1378 0.0233  252 THR   A OG1  
1839 C  CG2  . THR   A 253 ? 0.4249 0.7447 0.2957 0.0312  -0.1702 0.0174  252 THR   A CG2  
1840 N  N    . ASN   A 254 ? 0.4996 0.6475 0.3146 0.0795  -0.1136 0.0409  253 ASN   A N    
1841 C  CA   . ASN   A 254 ? 0.513  0.631  0.3206 0.0965  -0.1007 0.0467  253 ASN   A CA   
1842 C  C    . ASN   A 254 ? 0.4928 0.6528 0.3348 0.1068  -0.0973 0.0462  253 ASN   A C    
1843 O  O    . ASN   A 254 ? 0.5074 0.6561 0.3403 0.1322  -0.0945 0.0509  253 ASN   A O    
1844 C  CB   . ASN   A 254 ? 0.5437 0.6207 0.3099 0.1214  -0.1044 0.0543  253 ASN   A CB   
1845 C  CG   . ASN   A 254 ? 0.6125 0.6356 0.3404 0.1097  -0.0995 0.0559  253 ASN   A CG   
1846 O  OD1  . ASN   A 254 ? 0.6605 0.6515 0.3494 0.1247  -0.1048 0.0619  253 ASN   A OD1  
1847 N  ND2  . ASN   A 254 ? 0.6118 0.6229 0.3469 0.084   -0.0887 0.0508  253 ASN   A ND2  
1848 N  N    . LYS   A 255 ? 0.4593 0.6629 0.3367 0.0861  -0.0959 0.0404  254 LYS   A N    
1849 C  CA   . LYS   A 255 ? 0.4301 0.6768 0.3404 0.0926  -0.0903 0.0396  254 LYS   A CA   
1850 C  C    . LYS   A 255 ? 0.4402 0.6489 0.3455 0.091   -0.0725 0.0415  254 LYS   A C    
1851 O  O    . LYS   A 255 ? 0.4527 0.6295 0.3511 0.0697  -0.0644 0.04    254 LYS   A O    
1852 C  CB   . LYS   A 255 ? 0.4268 0.7298 0.3723 0.0671  -0.0934 0.0333  254 LYS   A CB   
1853 C  CG   . LYS   A 255 ? 0.459  0.8343 0.4378 0.0825  -0.0995 0.0321  254 LYS   A CG   
1854 C  CD   . LYS   A 255 ? 0.5252 0.9493 0.5397 0.0532  -0.0937 0.0267  254 LYS   A CD   
1855 C  CE   . LYS   A 255 ? 0.568  1.0575 0.617  0.0697  -0.0899 0.0262  254 LYS   A CE   
1856 N  NZ   . LYS   A 255 ? 0.6088 1.1138 0.6794 0.0446  -0.0732 0.0243  254 LYS   A NZ   
1857 N  N    . LYS   A 256 ? 0.4366 0.6468 0.3426 0.1156  -0.0672 0.0443  255 LYS   A N    
1858 C  CA   . LYS   A 256 ? 0.4488 0.622  0.3461 0.1161  -0.052  0.0454  255 LYS   A CA   
1859 C  C    . LYS   A 256 ? 0.4436 0.643  0.3688 0.0981  -0.0415 0.0422  255 LYS   A C    
1860 O  O    . LYS   A 256 ? 0.47   0.6353 0.387  0.0853  -0.0314 0.042   255 LYS   A O    
1861 C  CB   . LYS   A 256 ? 0.4648 0.6196 0.3437 0.1491  -0.0502 0.0488  255 LYS   A CB   
1862 C  CG   . LYS   A 256 ? 0.5439 0.6532 0.3837 0.1636  -0.0576 0.0535  255 LYS   A CG   
1863 C  CD   . LYS   A 256 ? 0.6495 0.7234 0.4605 0.1944  -0.0547 0.0572  255 LYS   A CD   
1864 C  CE   . LYS   A 256 ? 0.7677 0.7859 0.533  0.2028  -0.0602 0.0629  255 LYS   A CE   
1865 N  NZ   . LYS   A 256 ? 0.8473 0.825  0.5763 0.2363  -0.0597 0.0673  255 LYS   A NZ   
1866 N  N    . MET   A 257 ? 0.4133 0.6736 0.3701 0.0971  -0.0435 0.0398  256 MET   A N    
1867 C  CA   . MET   A 257 ? 0.4036 0.6868 0.3829 0.0778  -0.032  0.0376  256 MET   A CA   
1868 C  C    . MET   A 257 ? 0.3944 0.722  0.3972 0.0516  -0.0381 0.0341  256 MET   A C    
1869 O  O    . MET   A 257 ? 0.3804 0.7641 0.4047 0.0578  -0.0468 0.0321  256 MET   A O    
1870 C  CB   . MET   A 257 ? 0.387  0.6994 0.3796 0.0991  -0.0232 0.0376  256 MET   A CB   
1871 C  CG   . MET   A 257 ? 0.4022 0.7275 0.4095 0.0803  -0.0089 0.0364  256 MET   A CG   
1872 S  SD   . MET   A 257 ? 0.4881 0.7446 0.4687 0.0669  0.0023  0.0381  256 MET   A SD   
1873 C  CE   . MET   A 257 ? 0.4304 0.642  0.3818 0.0993  0.0028  0.0394  256 MET   A CE   
1874 N  N    . ILE   A 258 ? 0.4013 0.7019 0.397  0.023   -0.0349 0.0329  257 ILE   A N    
1875 C  CA   . ILE   A 258 ? 0.3901 0.7185 0.3994 -0.0062 -0.0402 0.029   257 ILE   A CA   
1876 C  C    . ILE   A 258 ? 0.4016 0.7441 0.4248 -0.0284 -0.0271 0.0286  257 ILE   A C    
1877 O  O    . ILE   A 258 ? 0.4255 0.7225 0.4317 -0.0376 -0.0178 0.0305  257 ILE   A O    
1878 C  CB   . ILE   A 258 ? 0.4082 0.6879 0.3915 -0.0216 -0.0462 0.0274  257 ILE   A CB   
1879 C  CG1  . ILE   A 258 ? 0.4258 0.6849 0.3891 -0.0001 -0.0568 0.0287  257 ILE   A CG1  
1880 C  CG2  . ILE   A 258 ? 0.3975 0.6961 0.3875 -0.0534 -0.052  0.0222  257 ILE   A CG2  
1881 C  CD1  . ILE   A 258 ? 0.4629 0.6639 0.3969 -0.0072 -0.0554 0.0285  257 ILE   A CD1  
1882 N  N    . PHE   A 259 ? 0.3789 0.7858 0.4321 -0.037  -0.0262 0.0264  258 PHE   A N    
1883 C  CA   . PHE   A 259 ? 0.3781 0.8005 0.4425 -0.062  -0.0126 0.0265  258 PHE   A CA   
1884 C  C    . PHE   A 259 ? 0.3932 0.8203 0.4577 -0.1004 -0.0176 0.0226  258 PHE   A C    
1885 O  O    . PHE   A 259 ? 0.3767 0.8402 0.4537 -0.106  -0.0314 0.0181  258 PHE   A O    
1886 C  CB   . PHE   A 259 ? 0.3379 0.8324 0.4356 -0.0512 -0.006  0.0258  258 PHE   A CB   
1887 C  CG   . PHE   A 259 ? 0.3513 0.8307 0.4423 -0.0187 0.004   0.0291  258 PHE   A CG   
1888 C  CD1  . PHE   A 259 ? 0.3826 0.8218 0.4566 -0.0246 0.0188  0.0324  258 PHE   A CD1  
1889 C  CD2  . PHE   A 259 ? 0.3488 0.8492 0.4456 0.0184  -0.0021 0.0289  258 PHE   A CD2  
1890 C  CE1  . PHE   A 259 ? 0.3989 0.8216 0.4632 0.0036  0.0272  0.0342  258 PHE   A CE1  
1891 C  CE2  . PHE   A 259 ? 0.371  0.8501 0.4558 0.0472  0.0074  0.031   258 PHE   A CE2  
1892 C  CZ   . PHE   A 259 ? 0.3867 0.8281 0.456  0.0384  0.0219  0.0331  258 PHE   A CZ   
1893 N  N    . VAL   A 260 ? 0.4242 0.812  0.4713 -0.1268 -0.0073 0.0242  259 VAL   A N    
1894 C  CA   . VAL   A 260 ? 0.4397 0.8235 0.4805 -0.1659 -0.0105 0.0202  259 VAL   A CA   
1895 C  C    . VAL   A 260 ? 0.4461 0.8486 0.4946 -0.1932 0.005   0.022   259 VAL   A C    
1896 O  O    . VAL   A 260 ? 0.4646 0.8193 0.4907 -0.1944 0.0173  0.0273  259 VAL   A O    
1897 C  CB   . VAL   A 260 ? 0.4815 0.7874 0.483  -0.1748 -0.0146 0.0196  259 VAL   A CB   
1898 C  CG1  . VAL   A 260 ? 0.485  0.7882 0.4775 -0.2128 -0.0211 0.0135  259 VAL   A CG1  
1899 C  CG2  . VAL   A 260 ? 0.4986 0.7803 0.489  -0.1451 -0.0252 0.0192  259 VAL   A CG2  
1900 N  N    . PRO   A 261 ? 0.4273 0.9014 0.507  -0.2153 0.0053  0.018   260 PRO   A N    
1901 C  CA   . PRO   A 261 ? 0.4079 0.9517 0.5184 -0.2146 -0.0105 0.0113  260 PRO   A CA   
1902 C  C    . PRO   A 261 ? 0.41   1.008  0.5493 -0.1718 -0.0132 0.0123  260 PRO   A C    
1903 O  O    . PRO   A 261 ? 0.4087 1.0167 0.5558 -0.1541 0.0013  0.0165  260 PRO   A O    
1904 C  CB   . PRO   A 261 ? 0.3818 0.979  0.5132 -0.2588 -0.0044 0.0072  260 PRO   A CB   
1905 C  CG   . PRO   A 261 ? 0.385  0.9722 0.5128 -0.2641 0.0183  0.0136  260 PRO   A CG   
1906 C  CD   . PRO   A 261 ? 0.4097 0.9036 0.4956 -0.2452 0.0227  0.0202  260 PRO   A CD   
1907 N  N    . SER   A 262 ? 0.4147 1.0404 0.5638 -0.1532 -0.032  0.0085  261 SER   A N    
1908 C  CA   . SER   A 262 ? 0.4222 1.0893 0.5903 -0.1087 -0.0381 0.0096  261 SER   A CA   
1909 C  C    . SER   A 262 ? 0.4144 1.1624 0.622  -0.0988 -0.0271 0.0089  261 SER   A C    
1910 O  O    . SER   A 262 ? 0.4112 1.1657 0.6222 -0.0586 -0.0229 0.0118  261 SER   A O    
1911 C  CB   . SER   A 262 ? 0.4295 1.1216 0.6013 -0.0985 -0.0614 0.0052  261 SER   A CB   
1912 O  OG   . SER   A 262 ? 0.4438 1.1919 0.6377 -0.1354 -0.0697 -0.0022 261 SER   A OG   
1913 N  N    . TYR   A 263 ? 0.4095 1.2149 0.6437 -0.1365 -0.0205 0.0048  262 TYR   A N    
1914 C  CA   . TYR   A 263 ? 0.3948 1.284  0.6688 -0.1316 -0.007  0.0034  262 TYR   A CA   
1915 C  C    . TYR   A 263 ? 0.4513 1.3065 0.7119 -0.1195 0.0163  0.0095  262 TYR   A C    
1916 O  O    . TYR   A 263 ? 0.4252 1.3455 0.7149 -0.1085 0.0293  0.0085  262 TYR   A O    
1917 C  CB   . TYR   A 263 ? 0.3518 1.3139 0.6577 -0.1802 -0.0044 -0.0029 262 TYR   A CB   
1918 C  CG   . TYR   A 263 ? 0.3795 1.2865 0.6586 -0.232  0.0083  -0.0011 262 TYR   A CG   
1919 C  CD1  . TYR   A 263 ? 0.4024 1.2821 0.6689 -0.2412 0.0325  0.0049  262 TYR   A CD1  
1920 C  CD2  . TYR   A 263 ? 0.3995 1.2853 0.6645 -0.273  -0.0037 -0.0058 262 TYR   A CD2  
1921 C  CE1  . TYR   A 263 ? 0.4432 1.2694 0.6806 -0.2873 0.0439  0.0074  262 TYR   A CE1  
1922 C  CE2  . TYR   A 263 ? 0.4386 1.2706 0.6747 -0.3201 0.0082  -0.0043 262 TYR   A CE2  
1923 C  CZ   . TYR   A 263 ? 0.4694 1.2709 0.6912 -0.3266 0.032   0.0029  262 TYR   A CZ   
1924 O  OH   . TYR   A 263 ? 0.5255 1.2653 0.7118 -0.3707 0.0434  0.0056  262 TYR   A OH   
1925 N  N    . TYR   A 264 ? 0.5257 1.284  0.7428 -0.1212 0.0217  0.0153  263 TYR   A N    
1926 C  CA   . TYR   A 264 ? 0.58   1.3042 0.781  -0.1086 0.0414  0.0206  263 TYR   A CA   
1927 C  C    . TYR   A 264 ? 0.6174 1.344  0.819  -0.0569 0.0418  0.0217  263 TYR   A C    
1928 O  O    . TYR   A 264 ? 0.6272 1.3415 0.8204 -0.0438 0.0581  0.0243  263 TYR   A O    
1929 C  CB   . TYR   A 264 ? 0.629  1.2572 0.7857 -0.1258 0.0461  0.0259  263 TYR   A CB   
1930 C  CG   . TYR   A 264 ? 0.6441 1.2722 0.7961 -0.1659 0.0632  0.0281  263 TYR   A CG   
1931 C  CD1  . TYR   A 264 ? 0.6563 1.2913 0.8067 -0.1608 0.0834  0.0318  263 TYR   A CD1  
1932 C  CD2  . TYR   A 264 ? 0.6595 1.2883 0.8094 -0.2101 0.0599  0.0258  263 TYR   A CD2  
1933 C  CE1  . TYR   A 264 ? 0.673  1.31   0.8167 -0.1987 0.1004  0.0346  263 TYR   A CE1  
1934 C  CE2  . TYR   A 264 ? 0.6788 1.3043 0.8202 -0.2496 0.0766  0.0283  263 TYR   A CE2  
1935 C  CZ   . TYR   A 264 ? 0.6948 1.3238 0.8326 -0.2437 0.0972  0.0334  263 TYR   A CZ   
1936 O  OH   . TYR   A 264 ? 0.7307 1.3525 0.855  -0.2838 0.1149  0.037   263 TYR   A OH   
1937 N  N    . ASN   A 265 ? 0.6406 1.379  0.8473 -0.028  0.0239  0.0196  264 ASN   A N    
1938 C  CA   . ASN   A 265 ? 0.6772 1.4154 0.8804 0.0216  0.0219  0.0202  264 ASN   A CA   
1939 C  C    . ASN   A 265 ? 0.6655 1.4886 0.9045 0.0387  0.0342  0.0169  264 ASN   A C    
1940 O  O    . ASN   A 265 ? 0.6804 1.4894 0.9085 0.0716  0.0445  0.0179  264 ASN   A O    
1941 C  CB   . ASN   A 265 ? 0.7017 1.4426 0.9032 0.0425  -0.001  0.0189  264 ASN   A CB   
1942 C  CG   . ASN   A 265 ? 0.7602 1.5026 0.9555 0.0949  -0.005  0.0197  264 ASN   A CG   
1943 O  OD1  . ASN   A 265 ? 0.8014 1.4935 0.9715 0.1166  0.0058  0.0225  264 ASN   A OD1  
1944 N  ND2  . ASN   A 265 ? 0.7477 1.5465 0.9631 0.1164  -0.0213 0.0169  264 ASN   A ND2  
1945 N  N    . ILE   A 266 ? 0.6359 1.5475 0.9165 0.0156  0.0337  0.0122  265 ILE   A N    
1946 C  CA   . ILE   A 266 ? 0.6125 1.6161 0.932  0.0318  0.046   0.0082  265 ILE   A CA   
1947 C  C    . ILE   A 266 ? 0.6331 1.6295 0.9472 0.0142  0.0733  0.0103  265 ILE   A C    
1948 O  O    . ILE   A 266 ? 0.6199 1.6561 0.9468 0.0433  0.0872  0.0084  265 ILE   A O    
1949 C  CB   . ILE   A 266 ? 0.5688 1.6814 0.939  0.0154  0.0356  0.0013  265 ILE   A CB   
1950 C  CG1  . ILE   A 266 ? 0.5682 1.707  0.9535 -0.0481 0.0452  -0.0003 265 ILE   A CG1  
1951 C  CG2  . ILE   A 266 ? 0.575  1.6848 0.9426 0.0315  0.007   -0.0002 265 ILE   A CG2  
1952 C  CD1  . ILE   A 266 ? 0.5258 1.7849 0.966  -0.0681 0.0384  -0.0084 265 ILE   A CD1  
1953 N  N    . TYR   A 267 ? 0.6687 1.6095 0.9592 -0.0294 0.0811  0.0143  266 TYR   A N    
1954 C  CA   . TYR   A 267 ? 0.695  1.6186 0.9719 -0.0453 0.1062  0.0177  266 TYR   A CA   
1955 C  C    . TYR   A 267 ? 0.7366 1.5975 0.9797 -0.0048 0.1127  0.0206  266 TYR   A C    
1956 O  O    . TYR   A 267 ? 0.7338 1.6135 0.9773 0.0072  0.1321  0.0202  266 TYR   A O    
1957 C  CB   . TYR   A 267 ? 0.7325 1.5937 0.9809 -0.0949 0.1102  0.0225  266 TYR   A CB   
1958 C  CG   . TYR   A 267 ? 0.7273 1.6427 1.0014 -0.1441 0.1103  0.0196  266 TYR   A CG   
1959 C  CD1  . TYR   A 267 ? 0.719  1.6925 1.0132 -0.1734 0.1318  0.0191  266 TYR   A CD1  
1960 C  CD2  . TYR   A 267 ? 0.7468 1.6505 1.0207 -0.1647 0.0898  0.0171  266 TYR   A CD2  
1961 C  CE1  . TYR   A 267 ? 0.7108 1.731  1.0257 -0.2242 0.1326  0.016   266 TYR   A CE1  
1962 C  CE2  . TYR   A 267 ? 0.7401 1.6881 1.0331 -0.2136 0.0893  0.0133  266 TYR   A CE2  
1963 C  CZ   . TYR   A 267 ? 0.7264 1.7327 1.0403 -0.2446 0.1106  0.0128  266 TYR   A CZ   
1964 O  OH   . TYR   A 267 ? 0.7264 1.7758 1.0577 -0.2975 0.1105  0.0085  266 TYR   A OH   
1965 N  N    . LEU   A 268 ? 0.7756 1.563  0.9883 0.0148  0.0969  0.0227  267 LEU   A N    
1966 C  CA   . LEU   A 268 ? 0.8192 1.5411 0.9969 0.0494  0.0999  0.0246  267 LEU   A CA   
1967 C  C    . LEU   A 268 ? 0.8148 1.5788 1.0055 0.098   0.1013  0.0202  267 LEU   A C    
1968 O  O    . LEU   A 268 ? 0.831  1.5694 1.001  0.1221  0.1138  0.0197  267 LEU   A O    
1969 C  CB   . LEU   A 268 ? 0.8551 1.4963 1.001  0.0516  0.0823  0.0275  267 LEU   A CB   
1970 C  CG   . LEU   A 268 ? 0.9045 1.4686 1.0168 0.0229  0.0844  0.0322  267 LEU   A CG   
1971 C  CD1  . LEU   A 268 ? 0.905  1.4822 1.0205 -0.0163 0.0992  0.0346  267 LEU   A CD1  
1972 C  CD2  . LEU   A 268 ? 0.9264 1.4523 1.0285 0.0121  0.0662  0.0332  267 LEU   A CD2  
1973 N  N    . ILE   A 269 ? 0.7927 1.6207 1.0152 0.1136  0.088   0.0166  268 ILE   A N    
1974 C  CA   . ILE   A 269 ? 0.789  1.6629 1.025  0.1635  0.0878  0.0123  268 ILE   A CA   
1975 C  C    . ILE   A 269 ? 0.7724 1.7238 1.0377 0.1664  0.1106  0.0082  268 ILE   A C    
1976 O  O    . ILE   A 269 ? 0.775  1.7281 1.0306 0.2068  0.1208  0.0054  268 ILE   A O    
1977 C  CB   . ILE   A 269 ? 0.7688 1.6899 1.0288 0.1798  0.0648  0.0102  268 ILE   A CB   
1978 C  CG1  . ILE   A 269 ? 0.8219 1.6551 1.0421 0.1896  0.0457  0.0145  268 ILE   A CG1  
1979 C  CG2  . ILE   A 269 ? 0.7429 1.7356 1.0267 0.23    0.0654  0.0052  268 ILE   A CG2  
1980 C  CD1  . ILE   A 269 ? 0.8197 1.6863 1.0557 0.1952  0.022   0.0136  268 ILE   A CD1  
1981 N  N    . LEU   A 270 ? 0.7573 1.7661 1.0532 0.1216  0.1202  0.0078  269 LEU   A N    
1982 C  CA   . LEU   A 270 ? 0.7436 1.8283 1.0673 0.1161  0.1446  0.0044  269 LEU   A CA   
1983 C  C    . LEU   A 270 ? 0.7962 1.8189 1.0809 0.1171  0.1665  0.0073  269 LEU   A C    
1984 O  O    . LEU   A 270 ? 0.7808 1.8492 1.0755 0.1364  0.1865  0.0035  269 LEU   A O    
1985 C  CB   . LEU   A 270 ? 0.714  1.868  1.0751 0.0614  0.1495  0.0036  269 LEU   A CB   
1986 C  CG   . LEU   A 270 ? 0.6885 1.9375 1.0998 0.0602  0.132   -0.0021 269 LEU   A CG   
1987 C  CD1  . LEU   A 270 ? 0.6693 1.9757 1.1106 -0.0015 0.1383  -0.0034 269 LEU   A CD1  
1988 C  CD2  . LEU   A 270 ? 0.654  1.9961 1.1019 0.1104  0.1354  -0.009  269 LEU   A CD2  
1989 N  N    . ASP   A 271 ? 0.8557 1.7769 1.0954 0.0982  0.1623  0.0134  270 ASP   A N    
1990 C  CA   . ASP   A 271 ? 0.9086 1.7627 1.1059 0.0991  0.1786  0.0162  270 ASP   A CA   
1991 C  C    . ASP   A 271 ? 0.9386 1.7639 1.1122 0.153   0.1805  0.0121  270 ASP   A C    
1992 O  O    . ASP   A 271 ? 0.9497 1.7617 1.1026 0.1634  0.1994  0.0108  270 ASP   A O    
1993 C  CB   . ASP   A 271 ? 0.9795 1.7372 1.1373 0.0709  0.1691  0.0229  270 ASP   A CB   
1994 C  CG   . ASP   A 271 ? 1.0379 1.798  1.1988 0.0175  0.1754  0.0279  270 ASP   A CG   
1995 O  OD1  . ASP   A 271 ? 1.0124 1.8462 1.2033 -0.0035 0.1905  0.0265  270 ASP   A OD1  
1996 O  OD2  . ASP   A 271 ? 1.0972 1.7853 1.2292 -0.0034 0.1659  0.0329  270 ASP   A OD2  
1997 N  N    . LYS   A 272 ? 0.9535 1.7657 1.1258 0.1869  0.1613  0.0101  271 LYS   A N    
1998 C  CA   . LYS   A 272 ? 0.9903 1.7676 1.135  0.2387  0.1611  0.0061  271 LYS   A CA   
1999 C  C    . LYS   A 272 ? 0.9668 1.8323 1.1429 0.2782  0.1713  -0.0009 271 LYS   A C    
2000 O  O    . LYS   A 272 ? 0.9783 1.8268 1.1383 0.3265  0.1653  -0.0045 271 LYS   A O    
2001 C  CB   . LYS   A 272 ? 1.0391 1.7568 1.1624 0.2563  0.1368  0.0081  271 LYS   A CB   
2002 C  CG   . LYS   A 272 ? 1.1439 1.7525 1.2129 0.2555  0.1337  0.0105  271 LYS   A CG   
2003 C  CD   . LYS   A 272 ? 1.2223 1.7854 1.2577 0.3045  0.1295  0.0068  271 LYS   A CD   
2004 C  CE   . LYS   A 272 ? 1.3142 1.7734 1.2959 0.3014  0.1272  0.0078  271 LYS   A CE   
2005 N  NZ   . LYS   A 272 ? 1.365  1.7755 1.3087 0.3465  0.1252  0.0035  271 LYS   A NZ   
2006 N  N    . PHE   A 273 ? 0.9323 1.8905 1.1511 0.2577  0.1874  -0.0029 272 PHE   A N    
2007 C  CA   . PHE   A 273 ? 0.9036 1.9635 1.1611 0.2898  0.1999  -0.0102 272 PHE   A CA   
2008 C  C    . PHE   A 273 ? 0.8874 2.004  1.1642 0.2571  0.2283  -0.011  272 PHE   A C    
2009 O  O    . PHE   A 273 ? 0.8396 2.054  1.1674 0.2316  0.2338  -0.0125 272 PHE   A O    
2010 C  CB   . PHE   A 273 ? 0.864  2.0114 1.1735 0.2935  0.1815  -0.0122 272 PHE   A CB   
2011 C  CG   . PHE   A 273 ? 0.8912 2.0185 1.1902 0.3436  0.1585  -0.0135 272 PHE   A CG   
2012 C  CD1  . PHE   A 273 ? 0.9359 1.9919 1.2109 0.3338  0.1344  -0.0079 272 PHE   A CD1  
2013 C  CD2  . PHE   A 273 ? 0.8818 2.067  1.1959 0.4005  0.161   -0.0201 272 PHE   A CD2  
2014 C  CE1  . PHE   A 273 ? 0.9594 1.9942 1.2203 0.378   0.114   -0.008  272 PHE   A CE1  
2015 C  CE2  . PHE   A 273 ? 0.9054 2.0674 1.2046 0.4476  0.1391  -0.0202 272 PHE   A CE2  
2016 C  CZ   . PHE   A 273 ? 0.9383 2.0235 1.2096 0.4347  0.1158  -0.0137 272 PHE   A CZ   
2017 N  N    . LEU   A 274 ? 0.9275 1.9809 1.1611 0.254   0.2461  -0.0097 273 LEU   A N    
2018 C  CA   . LEU   A 274 ? 0.9198 2.0136 1.1615 0.2217  0.274   -0.009  273 LEU   A CA   
2019 C  C    . LEU   A 274 ? 0.9457 2.0101 1.1498 0.2529  0.2966  -0.0134 273 LEU   A C    
2020 O  O    . LEU   A 274 ? 0.9166 2.0519 1.14   0.2533  0.3224  -0.0173 273 LEU   A O    
2021 C  CB   . LEU   A 274 ? 0.9508 1.9865 1.1724 0.1623  0.2713  0.0003  273 LEU   A CB   
2022 C  CG   . LEU   A 274 ? 0.938  2.0409 1.1909 0.1087  0.288   0.0034  273 LEU   A CG   
2023 C  CD1  . LEU   A 274 ? 0.8835 2.1025 1.2025 0.1033  0.2822  -0.0015 273 LEU   A CD1  
2024 C  CD2  . LEU   A 274 ? 0.9804 2.0077 1.2046 0.0578  0.2799  0.0129  273 LEU   A CD2  
2025 N  N    . VAL   B 26  ? 1.0422 1.8886 1.2678 0.5651  0.1842  -0.0147 25  VAL   B N    
2026 C  CA   . VAL   B 26  ? 1.0342 1.917  1.2758 0.5944  0.2102  -0.0258 25  VAL   B CA   
2027 C  C    . VAL   B 26  ? 0.9808 1.9776 1.2771 0.5743  0.2201  -0.0293 25  VAL   B C    
2028 O  O    . VAL   B 26  ? 0.9785 1.9926 1.2753 0.5611  0.2442  -0.0403 25  VAL   B O    
2029 C  CB   . VAL   B 26  ? 1.0459 1.9236 1.2921 0.6575  0.2097  -0.0236 25  VAL   B CB   
2030 C  CG1  . VAL   B 26  ? 1.0341 1.9489 1.2964 0.6897  0.2389  -0.0367 25  VAL   B CG1  
2031 C  CG2  . VAL   B 26  ? 1.1119 1.8721 1.2999 0.6732  0.2005  -0.0199 25  VAL   B CG2  
2032 N  N    . PHE   B 27  ? 0.9332 2.0075 1.2735 0.5698  0.2013  -0.0199 26  PHE   B N    
2033 C  CA   . PHE   B 27  ? 0.8718 2.0598 1.2666 0.5469  0.2071  -0.0219 26  PHE   B CA   
2034 C  C    . PHE   B 27  ? 0.8594 2.0345 1.2391 0.4837  0.2102  -0.0245 26  PHE   B C    
2035 O  O    . PHE   B 27  ? 0.8354 2.0634 1.2344 0.4607  0.2297  -0.0321 26  PHE   B O    
2036 C  CB   . PHE   B 27  ? 0.8382 2.1026 1.2775 0.5571  0.182   -0.0104 26  PHE   B CB   
2037 C  CG   . PHE   B 27  ? 0.7892 2.1859 1.2942 0.5565  0.1888  -0.0128 26  PHE   B CG   
2038 C  CD1  . PHE   B 27  ? 0.7753 2.2265 1.3095 0.5961  0.2113  -0.0208 26  PHE   B CD1  
2039 C  CD2  . PHE   B 27  ? 0.7676 2.2359 1.3056 0.5174  0.1726  -0.0074 26  PHE   B CD2  
2040 C  CE1  . PHE   B 27  ? 0.7202 2.3004 1.3186 0.5955  0.2177  -0.023  26  PHE   B CE1  
2041 C  CE2  . PHE   B 27  ? 0.7146 2.3093 1.3147 0.515   0.178   -0.0096 26  PHE   B CE2  
2042 C  CZ   . PHE   B 27  ? 0.6832 2.3357 1.3148 0.554   0.2006  -0.0171 26  PHE   B CZ   
2043 N  N    . PHE   B 28  ? 0.8738 1.9756 1.217  0.4566  0.1922  -0.0182 27  PHE   B N    
2044 C  CA   . PHE   B 28  ? 0.8721 1.9496 1.1959 0.4004  0.1935  -0.0196 27  PHE   B CA   
2045 C  C    . PHE   B 28  ? 0.8934 1.8552 1.1569 0.393   0.195   -0.0213 27  PHE   B C    
2046 O  O    . PHE   B 28  ? 0.9249 1.8322 1.1641 0.3786  0.1758  -0.0144 27  PHE   B O    
2047 C  CB   . PHE   B 28  ? 0.8636 1.9735 1.2053 0.3682  0.1694  -0.0109 27  PHE   B CB   
2048 C  CG   . PHE   B 28  ? 0.8279 2.0471 1.2206 0.3447  0.1729  -0.0123 27  PHE   B CG   
2049 C  CD1  . PHE   B 28  ? 0.794  2.1064 1.2364 0.3771  0.1762  -0.0128 27  PHE   B CD1  
2050 C  CD2  . PHE   B 28  ? 0.8393 2.0684 1.23   0.2899  0.173   -0.0131 27  PHE   B CD2  
2051 C  CE1  . PHE   B 28  ? 0.7535 2.1719 1.2447 0.3528  0.1795  -0.0145 27  PHE   B CE1  
2052 C  CE2  . PHE   B 28  ? 0.8032 2.1316 1.2387 0.2646  0.1767  -0.0148 27  PHE   B CE2  
2053 C  CZ   . PHE   B 28  ? 0.7521 2.177  1.2385 0.2949  0.1799  -0.0157 27  PHE   B CZ   
2054 N  N    . PRO   B 29  ? 0.8729 1.7972 1.111  0.403   0.2173  -0.0306 28  PRO   B N    
2055 C  CA   . PRO   B 29  ? 0.8967 1.7147 1.078  0.3957  0.2173  -0.0323 28  PRO   B CA   
2056 C  C    . PRO   B 29  ? 0.8714 1.6594 1.0305 0.3442  0.2164  -0.0317 28  PRO   B C    
2057 O  O    . PRO   B 29  ? 0.849  1.6901 1.0284 0.3148  0.2257  -0.0336 28  PRO   B O    
2058 C  CB   . PRO   B 29  ? 0.925  1.7206 1.0883 0.426   0.2415  -0.0433 28  PRO   B CB   
2059 C  CG   . PRO   B 29  ? 0.8884 1.7819 1.101  0.4471  0.2562  -0.0478 28  PRO   B CG   
2060 C  CD   . PRO   B 29  ? 0.8335 1.8107 1.0921 0.4209  0.2436  -0.0406 28  PRO   B CD   
2061 N  N    . ARG   B 30  ? 0.8734 1.5764 0.9909 0.3334  0.205   -0.0286 29  ARG   B N    
2062 C  CA   . ARG   B 30  ? 0.8591 1.5251 0.9522 0.2893  0.2029  -0.0273 29  ARG   B CA   
2063 C  C    . ARG   B 30  ? 0.8505 1.4684 0.9068 0.2857  0.2215  -0.0353 29  ARG   B C    
2064 O  O    . ARG   B 30  ? 0.8762 1.4479 0.9077 0.3143  0.2271  -0.0402 29  ARG   B O    
2065 C  CB   . ARG   B 30  ? 0.8925 1.4984 0.9629 0.2794  0.1805  -0.0198 29  ARG   B CB   
2066 C  CG   . ARG   B 30  ? 0.8938 1.5321 0.9844 0.2475  0.1655  -0.0131 29  ARG   B CG   
2067 C  CD   . ARG   B 30  ? 0.9425 1.5252 1.012  0.2439  0.1449  -0.0066 29  ARG   B CD   
2068 N  NE   . ARG   B 30  ? 0.9766 1.5302 1.0298 0.2041  0.1397  -0.0046 29  ARG   B NE   
2069 C  CZ   . ARG   B 30  ? 0.981  1.5491 1.045  0.182   0.1253  0.0003  29  ARG   B CZ   
2070 N  NH1  . ARG   B 30  ? 0.946  1.5602 1.037  0.1934  0.1133  0.004   29  ARG   B NH1  
2071 N  NH2  . ARG   B 30  ? 0.993  1.5285 1.0392 0.149   0.1225  0.0013  29  ARG   B NH2  
2072 N  N    . LYS   B 31  ? 0.8116 1.4381 0.8616 0.2502  0.2312  -0.0366 30  LYS   B N    
2073 C  CA   . LYS   B 31  ? 0.8067 1.3911 0.82   0.2437  0.2482  -0.0434 30  LYS   B CA   
2074 C  C    . LYS   B 31  ? 0.8055 1.2989 0.7721 0.2371  0.237   -0.0416 30  LYS   B C    
2075 O  O    . LYS   B 31  ? 0.8164 1.2848 0.7774 0.2157  0.2197  -0.0341 30  LYS   B O    
2076 C  CB   . LYS   B 31  ? 0.8214 1.445  0.8409 0.2081  0.2624  -0.044  30  LYS   B CB   
2077 C  CG   . LYS   B 31  ? 0.91   1.4761 0.8873 0.1753  0.264   -0.0422 30  LYS   B CG   
2078 C  CD   . LYS   B 31  ? 0.9794 1.5302 0.9282 0.1782  0.2864  -0.0505 30  LYS   B CD   
2079 C  CE   . LYS   B 31  ? 1.0052 1.6074 0.9645 0.1511  0.3045  -0.0512 30  LYS   B CE   
2080 N  NZ   . LYS   B 31  ? 1.0356 1.6415 0.9768 0.1638  0.3295  -0.0615 30  LYS   B NZ   
2081 N  N    . ARG   B 32  ? 0.7887 1.235  0.7222 0.2555  0.2474  -0.0492 31  ARG   B N    
2082 C  CA   . ARG   B 32  ? 0.7956 1.16   0.6846 0.2498  0.2385  -0.049  31  ARG   B CA   
2083 C  C    . ARG   B 32  ? 0.7709 1.1107 0.6294 0.2202  0.2469  -0.0506 31  ARG   B C    
2084 O  O    . ARG   B 32  ? 0.7692 1.1268 0.6206 0.2212  0.2667  -0.0577 31  ARG   B O    
2085 C  CB   . ARG   B 32  ? 0.8353 1.1565 0.7004 0.285   0.2442  -0.057  31  ARG   B CB   
2086 C  CG   . ARG   B 32  ? 0.8671 1.2031 0.7556 0.3193  0.2362  -0.0547 31  ARG   B CG   
2087 C  CD   . ARG   B 32  ? 0.9478 1.2094 0.8044 0.3304  0.2221  -0.0529 31  ARG   B CD   
2088 N  NE   . ARG   B 32  ? 1.014  1.2118 0.8242 0.3351  0.2324  -0.0624 31  ARG   B NE   
2089 C  CZ   . ARG   B 32  ? 1.0671 1.195  0.8427 0.3418  0.2238  -0.0632 31  ARG   B CZ   
2090 N  NH1  . ARG   B 32  ? 1.0534 1.1652 0.835  0.3459  0.2055  -0.0545 31  ARG   B NH1  
2091 N  NH2  . ARG   B 32  ? 1.1019 1.1753 0.8346 0.3423  0.2335  -0.073  31  ARG   B NH2  
2092 N  N    . LYS   B 33  ? 0.7493 1.0496 0.5896 0.1946  0.232   -0.0437 32  LYS   B N    
2093 C  CA   . LYS   B 33  ? 0.7315 1.0038 0.5404 0.1675  0.2366  -0.043  32  LYS   B CA   
2094 C  C    . LYS   B 33  ? 0.7478 0.9537 0.5121 0.1757  0.2361  -0.0488 32  LYS   B C    
2095 O  O    . LYS   B 33  ? 0.7651 0.9424 0.523  0.1986  0.2304  -0.0523 32  LYS   B O    
2096 C  CB   . LYS   B 33  ? 0.7127 0.9769 0.5251 0.1371  0.2206  -0.0323 32  LYS   B CB   
2097 C  CG   . LYS   B 33  ? 0.7094 0.9239 0.5096 0.1387  0.2002  -0.028  32  LYS   B CG   
2098 C  CD   . LYS   B 33  ? 0.682  0.9001 0.4942 0.114   0.1864  -0.0185 32  LYS   B CD   
2099 C  CE   . LYS   B 33  ? 0.6804 0.8508 0.4789 0.1124  0.1683  -0.0145 32  LYS   B CE   
2100 N  NZ   . LYS   B 33  ? 0.6632 0.8363 0.4721 0.0895  0.1571  -0.0065 32  LYS   B NZ   
2101 N  N    . SER   B 34  ? 0.7391 0.919  0.4705 0.1555  0.2411  -0.0493 33  SER   B N    
2102 C  CA   . SER   B 34  ? 0.7578 0.8767 0.4455 0.1574  0.2382  -0.0544 33  SER   B CA   
2103 C  C    . SER   B 34  ? 0.748  0.8298 0.4225 0.1359  0.2175  -0.0451 33  SER   B C    
2104 O  O    . SER   B 34  ? 0.7393 0.8369 0.4257 0.1143  0.211   -0.0358 33  SER   B O    
2105 C  CB   . SER   B 34  ? 0.7999 0.9135 0.4559 0.15    0.2564  -0.0613 33  SER   B CB   
2106 O  OG   . SER   B 34  ? 0.8722 0.9283 0.4833 0.1509  0.2539  -0.0676 33  SER   B OG   
2107 N  N    . VAL   B 35  ? 0.751  0.7843 0.4022 0.1426  0.2072  -0.0479 34  VAL   B N    
2108 C  CA   . VAL   B 35  ? 0.7536 0.7525 0.3912 0.124   0.1883  -0.0404 34  VAL   B CA   
2109 C  C    . VAL   B 35  ? 0.775  0.7281 0.3669 0.1165  0.1879  -0.0457 34  VAL   B C    
2110 O  O    . VAL   B 35  ? 0.792  0.715  0.3704 0.1047  0.1722  -0.0414 34  VAL   B O    
2111 C  CB   . VAL   B 35  ? 0.7443 0.7313 0.3994 0.1315  0.1721  -0.0365 34  VAL   B CB   
2112 C  CG1  . VAL   B 35  ? 0.7243 0.7556 0.421  0.1316  0.1688  -0.0295 34  VAL   B CG1  
2113 C  CG2  . VAL   B 35  ? 0.7506 0.711  0.3938 0.1553  0.1748  -0.0451 34  VAL   B CG2  
2114 N  N    . ALA   B 36  ? 0.7687 0.7189 0.3369 0.1231  0.2052  -0.0555 35  ALA   B N    
2115 C  CA   . ALA   B 36  ? 0.7872 0.6972 0.309  0.1154  0.2068  -0.0621 35  ALA   B CA   
2116 C  C    . ALA   B 36  ? 0.7823 0.6882 0.2898 0.0886  0.197   -0.052  35  ALA   B C    
2117 O  O    . ALA   B 36  ? 0.7715 0.7083 0.2914 0.0778  0.203   -0.0451 35  ALA   B O    
2118 C  CB   . ALA   B 36  ? 0.7865 0.7044 0.2904 0.1268  0.2302  -0.074  35  ALA   B CB   
2119 N  N    . GLY   B 37  ? 0.7881 0.6572 0.2709 0.0779  0.1814  -0.0505 36  GLY   B N    
2120 C  CA   . GLY   B 37  ? 0.7926 0.6551 0.2595 0.0555  0.17    -0.0403 36  GLY   B CA   
2121 C  C    . GLY   B 37  ? 0.7796 0.6551 0.2767 0.0468  0.1541  -0.0266 36  GLY   B C    
2122 O  O    . GLY   B 37  ? 0.7981 0.6657 0.2831 0.0309  0.1432  -0.0172 36  GLY   B O    
2123 N  N    . GLU   B 38  ? 0.7459 0.6408 0.2807 0.0577  0.1528  -0.0253 37  GLU   B N    
2124 C  CA   . GLU   B 38  ? 0.7186 0.6231 0.281  0.0505  0.1385  -0.0142 37  GLU   B CA   
2125 C  C    . GLU   B 38  ? 0.71   0.5856 0.2639 0.0472  0.1205  -0.0127 37  GLU   B C    
2126 O  O    . GLU   B 38  ? 0.7237 0.577  0.262  0.0545  0.1198  -0.0214 37  GLU   B O    
2127 C  CB   . GLU   B 38  ? 0.7233 0.6549 0.3248 0.0632  0.1413  -0.0147 37  GLU   B CB   
2128 C  CG   . GLU   B 38  ? 0.7661 0.7359 0.3848 0.0678  0.1584  -0.0167 37  GLU   B CG   
2129 C  CD   . GLU   B 38  ? 0.8379 0.8313 0.4665 0.0499  0.1611  -0.0076 37  GLU   B CD   
2130 O  OE1  . GLU   B 38  ? 0.8638 0.8386 0.4793 0.0343  0.1507  0.001   37  GLU   B OE1  
2131 O  OE2  . GLU   B 38  ? 0.8496 0.8805 0.4986 0.0514  0.1739  -0.0089 37  GLU   B OE2  
2132 N  N    . ILE   B 39  ? 0.6858 0.562  0.2507 0.0367  0.1067  -0.0023 38  ILE   B N    
2133 C  CA   . ILE   B 39  ? 0.6797 0.5371 0.244  0.0341  0.0901  -0.0007 38  ILE   B CA   
2134 C  C    . ILE   B 39  ? 0.6593 0.5278 0.2568 0.043   0.0872  -0.0004 38  ILE   B C    
2135 O  O    . ILE   B 39  ? 0.6447 0.5333 0.2665 0.0416  0.0875  0.0057  38  ILE   B O    
2136 C  CB   . ILE   B 39  ? 0.6849 0.537  0.2418 0.0208  0.0766  0.01    38  ILE   B CB   
2137 C  CG1  . ILE   B 39  ? 0.7064 0.544  0.2239 0.0122  0.0775  0.0093  38  ILE   B CG1  
2138 C  CG2  . ILE   B 39  ? 0.6866 0.5304 0.2543 0.0198  0.0604  0.012   38  ILE   B CG2  
2139 C  CD1  . ILE   B 39  ? 0.7178 0.5534 0.2274 0.0014  0.0664  0.0219  38  ILE   B CD1  
2140 N  N    . VAL   B 40  ? 0.653  0.5069 0.2482 0.0516  0.0858  -0.0077 39  VAL   B N    
2141 C  CA   . VAL   B 40  ? 0.631  0.4915 0.2517 0.0605  0.0831  -0.0076 39  VAL   B CA   
2142 C  C    . VAL   B 40  ? 0.6374 0.4819 0.2588 0.0543  0.069   -0.0058 39  VAL   B C    
2143 O  O    . VAL   B 40  ? 0.6449 0.4655 0.2441 0.0516  0.0657  -0.0113 39  VAL   B O    
2144 C  CB   . VAL   B 40  ? 0.6307 0.4869 0.2486 0.0776  0.094   -0.0162 39  VAL   B CB   
2145 C  CG1  . VAL   B 40  ? 0.6213 0.4846 0.2638 0.0872  0.09    -0.0143 39  VAL   B CG1  
2146 C  CG2  . VAL   B 40  ? 0.6222 0.5004 0.2418 0.0846  0.1094  -0.0189 39  VAL   B CG2  
2147 N  N    . LEU   B 41  ? 0.6247 0.483  0.2714 0.0512  0.0614  0.001   40  LEU   B N    
2148 C  CA   . LEU   B 41  ? 0.6255 0.4746 0.2772 0.046   0.0497  0.0025  40  LEU   B CA   
2149 C  C    . LEU   B 41  ? 0.6148 0.464  0.2813 0.0544  0.0507  0.0006  40  LEU   B C    
2150 O  O    . LEU   B 41  ? 0.5994 0.4674 0.2874 0.059   0.053   0.0037  40  LEU   B O    
2151 C  CB   . LEU   B 41  ? 0.6224 0.4831 0.2888 0.0377  0.0407  0.0108  40  LEU   B CB   
2152 C  CG   . LEU   B 41  ? 0.6332 0.4886 0.3034 0.0314  0.0288  0.0119  40  LEU   B CG   
2153 C  CD1  . LEU   B 41  ? 0.6372 0.4988 0.3088 0.0249  0.0201  0.019   40  LEU   B CD1  
2154 C  CD2  . LEU   B 41  ? 0.6264 0.4893 0.3198 0.0345  0.0273  0.0126  40  LEU   B CD2  
2155 N  N    . ILE   B 42  ? 0.6207 0.4474 0.273  0.0548  0.0485  -0.0044 41  ILE   B N    
2156 C  CA   . ILE   B 42  ? 0.6191 0.4396 0.2791 0.062   0.0487  -0.0052 41  ILE   B CA   
2157 C  C    . ILE   B 42  ? 0.615  0.4277 0.2776 0.0511  0.0392  -0.0038 41  ILE   B C    
2158 O  O    . ILE   B 42  ? 0.634  0.4286 0.2778 0.0416  0.0353  -0.0073 41  ILE   B O    
2159 C  CB   . ILE   B 42  ? 0.6399 0.4365 0.2788 0.074   0.0566  -0.0119 41  ILE   B CB   
2160 C  CG1  . ILE   B 42  ? 0.6469 0.4572 0.2862 0.0861  0.0676  -0.0141 41  ILE   B CG1  
2161 C  CG2  . ILE   B 42  ? 0.6484 0.4354 0.2924 0.0824  0.0558  -0.0108 41  ILE   B CG2  
2162 C  CD1  . ILE   B 42  ? 0.6828 0.467  0.2971 0.0982  0.0764  -0.0222 41  ILE   B CD1  
2163 N  N    . THR   B 43  ? 0.5853 0.4136 0.2705 0.0509  0.036   0.0008  42  THR   B N    
2164 C  CA   . THR   B 43  ? 0.5755 0.4011 0.2662 0.0414  0.0292  0.0019  42  THR   B CA   
2165 C  C    . THR   B 43  ? 0.5718 0.3753 0.2505 0.0451  0.0315  -0.0003 42  THR   B C    
2166 O  O    . THR   B 43  ? 0.5716 0.3703 0.2474 0.0584  0.037   -0.0006 42  THR   B O    
2167 C  CB   . THR   B 43  ? 0.5645 0.4145 0.2817 0.0394  0.0259  0.007   42  THR   B CB   
2168 O  OG1  . THR   B 43  ? 0.5759 0.433  0.3041 0.0476  0.0295  0.0084  42  THR   B OG1  
2169 C  CG2  . THR   B 43  ? 0.552  0.4172 0.2773 0.0382  0.0248  0.0103  42  THR   B CG2  
2170 N  N    . GLY   B 44  ? 0.5694 0.3602 0.2405 0.0334  0.0273  -0.0015 43  GLY   B N    
2171 C  CA   . GLY   B 44  ? 0.588  0.3509 0.2417 0.0342  0.0295  -0.0029 43  GLY   B CA   
2172 C  C    . GLY   B 44  ? 0.6119 0.342  0.2362 0.0415  0.0348  -0.0081 43  GLY   B C    
2173 O  O    . GLY   B 44  ? 0.6179 0.3235 0.2277 0.0514  0.0387  -0.0081 43  GLY   B O    
2174 N  N    . ALA   B 45  ? 0.6324 0.3596 0.245  0.0372  0.0349  -0.0126 44  ALA   B N    
2175 C  CA   . ALA   B 45  ? 0.6669 0.3625 0.2495 0.0442  0.0414  -0.0193 44  ALA   B CA   
2176 C  C    . ALA   B 45  ? 0.7021 0.3551 0.2519 0.0324  0.0409  -0.0249 44  ALA   B C    
2177 O  O    . ALA   B 45  ? 0.7328 0.3528 0.2531 0.038   0.0469  -0.0316 44  ALA   B O    
2178 C  CB   . ALA   B 45  ? 0.6679 0.3755 0.2469 0.0428  0.0425  -0.0222 44  ALA   B CB   
2179 N  N    . GLY   B 46  ? 0.7016 0.3551 0.2553 0.0156  0.0346  -0.0226 45  GLY   B N    
2180 C  CA   . GLY   B 46  ? 0.7429 0.3591 0.2667 -0.0014 0.0336  -0.0276 45  GLY   B CA   
2181 C  C    . GLY   B 46  ? 0.7853 0.3577 0.2849 0.0071  0.0396  -0.0274 45  GLY   B C    
2182 O  O    . GLY   B 46  ? 0.8259 0.3577 0.2935 -0.0067 0.0404  -0.0321 45  GLY   B O    
2183 N  N    . HIS   B 47  ? 0.7711 0.3502 0.284  0.0293  0.0433  -0.0216 46  HIS   B N    
2184 C  CA   . HIS   B 47  ? 0.7827 0.322  0.2737 0.0415  0.0478  -0.0192 46  HIS   B CA   
2185 C  C    . HIS   B 47  ? 0.766  0.326  0.2774 0.0696  0.0506  -0.0133 46  HIS   B C    
2186 O  O    . HIS   B 47  ? 0.7455 0.3518 0.2894 0.0742  0.0488  -0.0107 46  HIS   B O    
2187 C  CB   . HIS   B 47  ? 0.7967 0.3288 0.2861 0.0233  0.0437  -0.014  46  HIS   B CB   
2188 C  CG   . HIS   B 47  ? 0.8491 0.3301 0.3067 0.0294  0.0472  -0.0109 46  HIS   B CG   
2189 N  ND1  . HIS   B 47  ? 0.9106 0.3342 0.3252 0.0225  0.0512  -0.017  46  HIS   B ND1  
2190 C  CD2  . HIS   B 47  ? 0.8627 0.3405 0.3234 0.0413  0.047   -0.0019 46  HIS   B CD2  
2191 C  CE1  . HIS   B 47  ? 0.937  0.322  0.3298 0.0316  0.0535  -0.0108 46  HIS   B CE1  
2192 N  NE2  . HIS   B 47  ? 0.9141 0.3313 0.3337 0.0434  0.0505  -0.0012 46  HIS   B NE2  
2193 N  N    . GLY   B 48  ? 0.7779 0.3033 0.2692 0.0873  0.0545  -0.0108 47  GLY   B N    
2194 C  CA   . GLY   B 48  ? 0.7661 0.3095 0.2743 0.1137  0.0555  -0.004  47  GLY   B CA   
2195 C  C    . GLY   B 48  ? 0.7506 0.3358 0.2854 0.1309  0.0588  -0.0058 47  GLY   B C    
2196 O  O    . GLY   B 48  ? 0.7533 0.3311 0.2778 0.1359  0.065   -0.0135 47  GLY   B O    
2197 N  N    . ILE   B 49  ? 0.7261 0.3556 0.2937 0.1382  0.0551  0.001   48  ILE   B N    
2198 C  CA   . ILE   B 49  ? 0.7013 0.3746 0.2962 0.1521  0.0583  0.0003  48  ILE   B CA   
2199 C  C    . ILE   B 49  ? 0.6952 0.3852 0.2958 0.139   0.0612  -0.0064 48  ILE   B C    
2200 O  O    . ILE   B 49  ? 0.6892 0.3867 0.2893 0.151   0.0685  -0.0111 48  ILE   B O    
2201 C  CB   . ILE   B 49  ? 0.6726 0.39   0.2999 0.1549  0.0525  0.0082  48  ILE   B CB   
2202 C  CG1  . ILE   B 49  ? 0.6834 0.384  0.3013 0.1714  0.0493  0.0155  48  ILE   B CG1  
2203 C  CG2  . ILE   B 49  ? 0.6534 0.4174 0.3087 0.1646  0.056   0.0071  48  ILE   B CG2  
2204 C  CD1  . ILE   B 49  ? 0.6659 0.4011 0.3072 0.1693  0.0421  0.0228  48  ILE   B CD1  
2205 N  N    . GLY   B 50  ? 0.6948 0.3886 0.2982 0.1154  0.0556  -0.0066 49  GLY   B N    
2206 C  CA   . GLY   B 50  ? 0.6935 0.4016 0.3002 0.1023  0.0558  -0.011  49  GLY   B CA   
2207 C  C    . GLY   B 50  ? 0.7222 0.397  0.2973 0.1024  0.0616  -0.0196 49  GLY   B C    
2208 O  O    . GLY   B 50  ? 0.7199 0.4085 0.2958 0.1041  0.0661  -0.0234 49  GLY   B O    
2209 N  N    . ARG   B 51  ? 0.7424 0.3706 0.2864 0.0996  0.0621  -0.0229 50  ARG   B N    
2210 C  CA   . ARG   B 51  ? 0.7694 0.3564 0.2764 0.0979  0.0678  -0.0325 50  ARG   B CA   
2211 C  C    . ARG   B 51  ? 0.7869 0.3663 0.286  0.1245  0.079   -0.0368 50  ARG   B C    
2212 O  O    . ARG   B 51  ? 0.7885 0.3623 0.2726 0.1253  0.0856  -0.0448 50  ARG   B O    
2213 C  CB   . ARG   B 51  ? 0.8006 0.3368 0.2758 0.0868  0.0657  -0.0341 50  ARG   B CB   
2214 C  CG   . ARG   B 51  ? 0.8468 0.3264 0.2769 0.0908  0.0735  -0.0443 50  ARG   B CG   
2215 C  CD   . ARG   B 51  ? 0.887  0.3162 0.2842 0.0729  0.0708  -0.0459 50  ARG   B CD   
2216 N  NE   . ARG   B 51  ? 0.9044 0.3443 0.3011 0.0403  0.0626  -0.0485 50  ARG   B NE   
2217 C  CZ   . ARG   B 51  ? 0.9521 0.3575 0.323  0.0166  0.0594  -0.051  50  ARG   B CZ   
2218 N  NH1  . ARG   B 51  ? 0.987  0.3384 0.3267 0.0211  0.0639  -0.0508 50  ARG   B NH1  
2219 N  NH2  . ARG   B 51  ? 0.9354 0.3608 0.3115 -0.012  0.0513  -0.0533 50  ARG   B NH2  
2220 N  N    . TRP   B 52  ? 0.7945 0.3748 0.3026 0.147   0.0813  -0.0316 51  TRP   B N    
2221 C  CA   . TRP   B 52  ? 0.8076 0.3852 0.3119 0.1758  0.0922  -0.0353 51  TRP   B CA   
2222 C  C    . TRP   B 52  ? 0.7903 0.4253 0.3282 0.183   0.0962  -0.0345 51  TRP   B C    
2223 O  O    . TRP   B 52  ? 0.802  0.439  0.334  0.1993  0.1073  -0.041  51  TRP   B O    
2224 C  CB   . TRP   B 52  ? 0.8191 0.3753 0.3185 0.1984  0.0921  -0.0295 51  TRP   B CB   
2225 C  CG   . TRP   B 52  ? 0.874  0.3616 0.3291 0.1924  0.0924  -0.0329 51  TRP   B CG   
2226 C  CD1  . TRP   B 52  ? 0.9009 0.3645 0.3427 0.1677  0.0842  -0.0296 51  TRP   B CD1  
2227 C  CD2  . TRP   B 52  ? 0.906  0.3386 0.3216 0.2079  0.1025  -0.0417 51  TRP   B CD2  
2228 N  NE1  . TRP   B 52  ? 0.9429 0.3394 0.3388 0.1649  0.0881  -0.0353 51  TRP   B NE1  
2229 C  CE2  . TRP   B 52  ? 0.95   0.3231 0.3275 0.1902  0.0992  -0.0429 51  TRP   B CE2  
2230 C  CE3  . TRP   B 52  ? 0.9195 0.3468 0.3276 0.2353  0.115   -0.0491 51  TRP   B CE3  
2231 C  CZ2  . TRP   B 52  ? 0.9963 0.3003 0.326  0.1984  0.1076  -0.0513 51  TRP   B CZ2  
2232 C  CZ3  . TRP   B 52  ? 0.9656 0.3256 0.3275 0.2462  0.1238  -0.0578 51  TRP   B CZ3  
2233 C  CH2  . TRP   B 52  ? 1.0012 0.2979 0.3232 0.2274  0.1198  -0.0589 51  TRP   B CH2  
2234 N  N    . THR   B 53  ? 0.7641 0.4432 0.334  0.1688  0.0885  -0.0277 52  THR   B N    
2235 C  CA   . THR   B 53  ? 0.7334 0.4617 0.3303 0.1697  0.0925  -0.0271 52  THR   B CA   
2236 C  C    . THR   B 53  ? 0.7481 0.4676 0.3257 0.1561  0.0971  -0.0346 52  THR   B C    
2237 O  O    . THR   B 53  ? 0.7481 0.4861 0.3281 0.1645  0.1071  -0.0388 52  THR   B O    
2238 C  CB   . THR   B 53  ? 0.7122 0.4785 0.3408 0.1566  0.0831  -0.0186 52  THR   B CB   
2239 O  OG1  . THR   B 53  ? 0.7211 0.4949 0.3634 0.1697  0.0792  -0.0124 52  THR   B OG1  
2240 C  CG2  . THR   B 53  ? 0.6915 0.5028 0.344  0.1534  0.087   -0.0176 52  THR   B CG2  
2241 N  N    . ALA   B 54  ? 0.7603 0.4521 0.3173 0.1351  0.09    -0.0365 53  ALA   B N    
2242 C  CA   . ALA   B 54  ? 0.7835 0.4637 0.3178 0.1206  0.0916  -0.0432 53  ALA   B CA   
2243 C  C    . ALA   B 54  ? 0.815  0.4656 0.3184 0.1351  0.1049  -0.054  53  ALA   B C    
2244 O  O    . ALA   B 54  ? 0.8188 0.4813 0.3154 0.1341  0.1123  -0.0587 53  ALA   B O    
2245 C  CB   . ALA   B 54  ? 0.7946 0.4504 0.3124 0.0974  0.0807  -0.0436 53  ALA   B CB   
2246 N  N    . TYR   B 55  ? 0.8328 0.4445 0.3168 0.1502  0.109   -0.0577 54  TYR   B N    
2247 C  CA   . TYR   B 55  ? 0.8587 0.4366 0.3112 0.1673  0.1229  -0.069  54  TYR   B CA   
2248 C  C    . TYR   B 55  ? 0.8529 0.4706 0.3284 0.1908  0.1352  -0.0695 54  TYR   B C    
2249 O  O    . TYR   B 55  ? 0.8712 0.4814 0.3273 0.1976  0.1479  -0.0793 54  TYR   B O    
2250 C  CB   . TYR   B 55  ? 0.8751 0.3989 0.3014 0.1809  0.1246  -0.0714 54  TYR   B CB   
2251 C  CG   . TYR   B 55  ? 0.8961 0.377  0.2964 0.1568  0.1144  -0.0717 54  TYR   B CG   
2252 C  CD1  . TYR   B 55  ? 0.9068 0.3913 0.2992 0.1264  0.1064  -0.0739 54  TYR   B CD1  
2253 C  CD2  . TYR   B 55  ? 0.9209 0.3586 0.3039 0.164   0.1128  -0.0693 54  TYR   B CD2  
2254 C  CE1  . TYR   B 55  ? 0.9348 0.3869 0.3066 0.1027  0.0973  -0.0744 54  TYR   B CE1  
2255 C  CE2  . TYR   B 55  ? 0.9518 0.3521 0.3109 0.1389  0.1046  -0.0696 54  TYR   B CE2  
2256 C  CZ   . TYR   B 55  ? 0.9659 0.3751 0.3203 0.1078  0.0972  -0.0729 54  TYR   B CZ   
2257 O  OH   . TYR   B 55  ? 1.0025 0.3805 0.3356 0.0815  0.0894  -0.0737 54  TYR   B OH   
2258 N  N    . GLU   B 56  ? 0.8235 0.4859 0.3397 0.2014  0.1319  -0.0596 55  GLU   B N    
2259 C  CA   . GLU   B 56  ? 0.8057 0.5144 0.3484 0.2207  0.1428  -0.0597 55  GLU   B CA   
2260 C  C    . GLU   B 56  ? 0.798  0.5388 0.3464 0.2046  0.1477  -0.0616 55  GLU   B C    
2261 O  O    . GLU   B 56  ? 0.8055 0.5607 0.3509 0.2165  0.1624  -0.0684 55  GLU   B O    
2262 C  CB   . GLU   B 56  ? 0.8003 0.5517 0.3843 0.2308  0.1361  -0.0487 55  GLU   B CB   
2263 C  CG   . GLU   B 56  ? 0.8922 0.6174 0.4714 0.2527  0.1329  -0.0455 55  GLU   B CG   
2264 C  CD   . GLU   B 56  ? 1.0199 0.7323 0.5889 0.2867  0.1461  -0.0518 55  GLU   B CD   
2265 O  OE1  . GLU   B 56  ? 1.0378 0.7674 0.6063 0.2951  0.1601  -0.06   55  GLU   B OE1  
2266 O  OE2  . GLU   B 56  ? 1.0878 0.7718 0.6481 0.3059  0.1429  -0.0483 55  GLU   B OE2  
2267 N  N    . PHE   B 57  ? 0.7829 0.5341 0.3383 0.1784  0.1359  -0.0553 56  PHE   B N    
2268 C  CA   . PHE   B 57  ? 0.7737 0.5498 0.331  0.1614  0.1382  -0.0548 56  PHE   B CA   
2269 C  C    . PHE   B 57  ? 0.8113 0.5527 0.3262 0.1536  0.1445  -0.065  56  PHE   B C    
2270 O  O    . PHE   B 57  ? 0.8109 0.5699 0.3201 0.1499  0.154   -0.0679 56  PHE   B O    
2271 C  CB   . PHE   B 57  ? 0.7528 0.5452 0.3281 0.1391  0.123   -0.0446 56  PHE   B CB   
2272 C  CG   . PHE   B 57  ? 0.7224 0.5603 0.3383 0.141   0.1203  -0.0355 56  PHE   B CG   
2273 C  CD1  . PHE   B 57  ? 0.71   0.5862 0.3419 0.1382  0.1282  -0.0336 56  PHE   B CD1  
2274 C  CD2  . PHE   B 57  ? 0.7195 0.5608 0.355  0.1424  0.1099  -0.0291 56  PHE   B CD2  
2275 C  CE1  . PHE   B 57  ? 0.6901 0.6062 0.357  0.1362  0.1252  -0.0259 56  PHE   B CE1  
2276 C  CE2  . PHE   B 57  ? 0.6954 0.5769 0.365  0.1419  0.107   -0.0219 56  PHE   B CE2  
2277 C  CZ   . PHE   B 57  ? 0.6737 0.5919 0.3588 0.1383  0.1143  -0.0206 56  PHE   B CZ   
2278 N  N    . ALA   B 58  ? 0.8457 0.5373 0.3286 0.1504  0.1403  -0.0711 57  ALA   B N    
2279 C  CA   . ALA   B 58  ? 0.8879 0.5419 0.326  0.1423  0.146   -0.0826 57  ALA   B CA   
2280 C  C    . ALA   B 58  ? 0.9128 0.562  0.3369 0.1654  0.1664  -0.0934 57  ALA   B C    
2281 O  O    . ALA   B 58  ? 0.9334 0.5786 0.3325 0.1595  0.1758  -0.1012 57  ALA   B O    
2282 C  CB   . ALA   B 58  ? 0.9176 0.5189 0.3255 0.1335  0.1378  -0.0873 57  ALA   B CB   
2283 N  N    . LYS   B 59  ? 0.91   0.5611 0.3497 0.1929  0.1735  -0.0938 58  LYS   B N    
2284 C  CA   . LYS   B 59  ? 0.9161 0.5691 0.3482 0.2194  0.1938  -0.1039 58  LYS   B CA   
2285 C  C    . LYS   B 59  ? 0.876  0.592  0.339  0.2203  0.2033  -0.1005 58  LYS   B C    
2286 O  O    . LYS   B 59  ? 0.8709 0.5921 0.3206 0.2306  0.2208  -0.1101 58  LYS   B O    
2287 C  CB   . LYS   B 59  ? 0.9497 0.5865 0.3892 0.2509  0.1976  -0.1042 58  LYS   B CB   
2288 C  CG   . LYS   B 59  ? 1.053  0.6158 0.4492 0.2513  0.194   -0.1108 58  LYS   B CG   
2289 C  CD   . LYS   B 59  ? 1.1286 0.6688 0.5294 0.2816  0.1947  -0.1079 58  LYS   B CD   
2290 C  CE   . LYS   B 59  ? 1.1814 0.7413 0.6139 0.2755  0.1771  -0.0925 58  LYS   B CE   
2291 N  NZ   . LYS   B 59  ? 1.2255 0.7551 0.6542 0.3021  0.1758  -0.0885 58  LYS   B NZ   
2292 N  N    . GLN   B 60  ? 0.8509 0.6119 0.3517 0.207   0.1924  -0.0875 59  GLN   B N    
2293 C  CA   . GLN   B 60  ? 0.827  0.6452 0.3558 0.2021  0.1997  -0.0829 59  GLN   B CA   
2294 C  C    . GLN   B 60  ? 0.8434 0.6606 0.3485 0.1766  0.2015  -0.0839 59  GLN   B C    
2295 O  O    . GLN   B 60  ? 0.8248 0.6839 0.3476 0.1684  0.2076  -0.0793 59  GLN   B O    
2296 C  CB   . GLN   B 60  ? 0.8091 0.6675 0.3818 0.1955  0.1867  -0.0692 59  GLN   B CB   
2297 C  CG   . GLN   B 60  ? 0.8274 0.7037 0.4294 0.2207  0.1862  -0.0665 59  GLN   B CG   
2298 C  CD   . GLN   B 60  ? 0.8625 0.7786 0.4829 0.2443  0.2042  -0.0717 59  GLN   B CD   
2299 O  OE1  . GLN   B 60  ? 0.8529 0.8056 0.4815 0.2366  0.2157  -0.0732 59  GLN   B OE1  
2300 N  NE2  . GLN   B 60  ? 0.88   0.7912 0.5077 0.274   0.207   -0.0739 59  GLN   B NE2  
2301 N  N    . LYS   B 61  ? 0.8693 0.6384 0.3331 0.1632  0.1955  -0.0894 60  LYS   B N    
2302 C  CA   . LYS   B 61  ? 0.8786 0.637  0.3116 0.1396  0.1939  -0.0905 60  LYS   B CA   
2303 C  C    . LYS   B 61  ? 0.8512 0.6339 0.3036 0.1163  0.1779  -0.0759 60  LYS   B C    
2304 O  O    . LYS   B 61  ? 0.8626 0.6541 0.3004 0.1002  0.1794  -0.0731 60  LYS   B O    
2305 C  CB   . LYS   B 61  ? 0.9038 0.6741 0.3182 0.1451  0.2156  -0.0998 60  LYS   B CB   
2306 C  CG   . LYS   B 61  ? 0.9743 0.7176 0.367  0.1701  0.2327  -0.1154 60  LYS   B CG   
2307 C  CD   . LYS   B 61  ? 1.0458 0.7987 0.4146 0.1722  0.2547  -0.1257 60  LYS   B CD   
2308 C  CE   . LYS   B 61  ? 1.1263 0.8546 0.4752 0.2008  0.2745  -0.1423 60  LYS   B CE   
2309 N  NZ   . LYS   B 61  ? 1.1733 0.9204 0.5055 0.2056  0.2991  -0.1527 60  LYS   B NZ   
2310 N  N    . SER   B 62  ? 0.8129 0.6025 0.2944 0.1147  0.1628  -0.0666 61  SER   B N    
2311 C  CA   . SER   B 62  ? 0.7837 0.5912 0.2835 0.0956  0.1475  -0.0535 61  SER   B CA   
2312 C  C    . SER   B 62  ? 0.7886 0.5645 0.2609 0.0772  0.1321  -0.0527 61  SER   B C    
2313 O  O    . SER   B 62  ? 0.8102 0.5504 0.256  0.0784  0.1306  -0.0616 61  SER   B O    
2314 C  CB   . SER   B 62  ? 0.7687 0.5928 0.307  0.1017  0.1381  -0.0458 61  SER   B CB   
2315 O  OG   . SER   B 62  ? 0.7677 0.6303 0.3381 0.114   0.1473  -0.0433 61  SER   B OG   
2316 N  N    . ARG   B 63  ? 0.7634 0.5525 0.243  0.0603  0.1199  -0.0418 62  ARG   B N    
2317 C  CA   . ARG   B 63  ? 0.7678 0.5387 0.2305 0.0435  0.1028  -0.0384 62  ARG   B CA   
2318 C  C    . ARG   B 63  ? 0.7507 0.5266 0.2439 0.0438  0.0894  -0.0321 62  ARG   B C    
2319 O  O    . ARG   B 63  ? 0.7321 0.5327 0.2552 0.0431  0.0853  -0.0223 62  ARG   B O    
2320 C  CB   . ARG   B 63  ? 0.7818 0.5667 0.2379 0.0292  0.0977  -0.0285 62  ARG   B CB   
2321 C  CG   . ARG   B 63  ? 0.8468 0.6185 0.2614 0.0221  0.1053  -0.0342 62  ARG   B CG   
2322 C  CD   . ARG   B 63  ? 0.8942 0.6874 0.3085 0.0168  0.1133  -0.0259 62  ARG   B CD   
2323 N  NE   . ARG   B 63  ? 0.9366 0.7317 0.347  0.0023  0.0971  -0.0124 62  ARG   B NE   
2324 C  CZ   . ARG   B 63  ? 0.95   0.7621 0.3712 -0.003  0.0981  -0.0004 62  ARG   B CZ   
2325 N  NH1  . ARG   B 63  ? 0.9191 0.7517 0.3567 0.002   0.1147  -0.0007 62  ARG   B NH1  
2326 N  NH2  . ARG   B 63  ? 0.9551 0.7636 0.3702 -0.0133 0.0825  0.0123  62  ARG   B NH2  
2327 N  N    . LEU   B 64  ? 0.752  0.503  0.2361 0.0443  0.0842  -0.0382 63  LEU   B N    
2328 C  CA   . LEU   B 64  ? 0.7259 0.4804 0.2363 0.0449  0.0741  -0.0334 63  LEU   B CA   
2329 C  C    . LEU   B 64  ? 0.7107 0.4691 0.2263 0.0286  0.0566  -0.0267 63  LEU   B C    
2330 O  O    . LEU   B 64  ? 0.7261 0.4721 0.2168 0.0158  0.0494  -0.0291 63  LEU   B O    
2331 C  CB   . LEU   B 64  ? 0.7462 0.4705 0.2439 0.0531  0.0778  -0.0424 63  LEU   B CB   
2332 C  CG   . LEU   B 64  ? 0.769  0.4902 0.2685 0.0748  0.0935  -0.048  63  LEU   B CG   
2333 C  CD1  . LEU   B 64  ? 0.8061 0.4829 0.2738 0.0806  0.0983  -0.059  63  LEU   B CD1  
2334 C  CD2  . LEU   B 64  ? 0.7527 0.4978 0.2897 0.0862  0.0924  -0.0407 63  LEU   B CD2  
2335 N  N    . VAL   B 65  ? 0.6824 0.46   0.231  0.0297  0.0499  -0.0187 64  VAL   B N    
2336 C  CA   . VAL   B 65  ? 0.6657 0.452  0.2275 0.0185  0.0349  -0.0124 64  VAL   B CA   
2337 C  C    . VAL   B 65  ? 0.6555 0.4394 0.2362 0.0227  0.0338  -0.0132 64  VAL   B C    
2338 O  O    . VAL   B 65  ? 0.6496 0.4448 0.2512 0.0336  0.0396  -0.0107 64  VAL   B O    
2339 C  CB   . VAL   B 65  ? 0.6518 0.4627 0.2331 0.0164  0.0293  -0.0013 64  VAL   B CB   
2340 C  CG1  . VAL   B 65  ? 0.6537 0.474  0.2498 0.0084  0.0144  0.0041  64  VAL   B CG1  
2341 C  CG2  . VAL   B 65  ? 0.6625 0.4725 0.2209 0.012   0.0312  0.0007  64  VAL   B CG2  
2342 N  N    . LEU   B 66  ? 0.6504 0.418  0.2199 0.0133  0.0272  -0.0174 65  LEU   B N    
2343 C  CA   . LEU   B 66  ? 0.6377 0.3975 0.218  0.0151  0.0272  -0.0184 65  LEU   B CA   
2344 C  C    . LEU   B 66  ? 0.6223 0.3997 0.2231 0.0039  0.0156  -0.0132 65  LEU   B C    
2345 O  O    . LEU   B 66  ? 0.6205 0.4025 0.2145 -0.0094 0.0062  -0.0133 65  LEU   B O    
2346 C  CB   . LEU   B 66  ? 0.654  0.3754 0.2021 0.0131  0.0318  -0.028  65  LEU   B CB   
2347 C  CG   . LEU   B 66  ? 0.6667 0.3678 0.1909 0.0258  0.0444  -0.0351 65  LEU   B CG   
2348 C  CD1  . LEU   B 66  ? 0.6947 0.3518 0.1837 0.023   0.0483  -0.045  65  LEU   B CD1  
2349 C  CD2  . LEU   B 66  ? 0.6514 0.3675 0.1972 0.0462  0.0538  -0.0317 65  LEU   B CD2  
2350 N  N    . TRP   B 67  ? 0.6107 0.4007 0.2371 0.0095  0.0164  -0.0089 66  TRP   B N    
2351 C  CA   . TRP   B 67  ? 0.5962 0.4053 0.2449 0.0014  0.0082  -0.0047 66  TRP   B CA   
2352 C  C    . TRP   B 67  ? 0.6257 0.4229 0.2755 -0.0012 0.0103  -0.0068 66  TRP   B C    
2353 O  O    . TRP   B 67  ? 0.644  0.4294 0.2921 0.0095  0.0176  -0.0072 66  TRP   B O    
2354 C  CB   . TRP   B 67  ? 0.5585 0.3938 0.2357 0.0095  0.0079  0.0025  66  TRP   B CB   
2355 C  CG   . TRP   B 67  ? 0.5362 0.3858 0.216  0.0085  0.0025  0.0074  66  TRP   B CG   
2356 C  CD1  . TRP   B 67  ? 0.5489 0.3917 0.2069 0.0037  -0.0005 0.0064  66  TRP   B CD1  
2357 C  CD2  . TRP   B 67  ? 0.5116 0.3807 0.2137 0.013   0       0.0146  66  TRP   B CD2  
2358 N  NE1  . TRP   B 67  ? 0.5408 0.3986 0.2064 0.0049  -0.0058 0.0138  66  TRP   B NE1  
2359 C  CE2  . TRP   B 67  ? 0.5242 0.3964 0.2166 0.0111  -0.0053 0.0189  66  TRP   B CE2  
2360 C  CE3  . TRP   B 67  ? 0.5026 0.3837 0.2288 0.0182  0.0019  0.0176  66  TRP   B CE3  
2361 C  CZ2  . TRP   B 67  ? 0.5195 0.4038 0.2255 0.0152  -0.0088 0.0269  66  TRP   B CZ2  
2362 C  CZ3  . TRP   B 67  ? 0.5051 0.3979 0.2448 0.0217  -0.0009 0.0239  66  TRP   B CZ3  
2363 C  CH2  . TRP   B 67  ? 0.5092 0.4021 0.2387 0.0207  -0.0062 0.029   66  TRP   B CH2  
2364 N  N    . ASP   B 68  ? 0.6266 0.4301 0.2808 -0.0155 0.0037  -0.0073 67  ASP   B N    
2365 C  CA   . ASP   B 68  ? 0.6318 0.4251 0.2862 -0.0213 0.006   -0.0083 67  ASP   B CA   
2366 C  C    . ASP   B 68  ? 0.6345 0.4474 0.3005 -0.0387 -0.0015 -0.0083 67  ASP   B C    
2367 O  O    . ASP   B 68  ? 0.6338 0.4593 0.2984 -0.0478 -0.0092 -0.0093 67  ASP   B O    
2368 C  CB   . ASP   B 68  ? 0.6618 0.4126 0.2821 -0.0225 0.0117  -0.0141 67  ASP   B CB   
2369 C  CG   . ASP   B 68  ? 0.6883 0.4223 0.3062 -0.0202 0.0166  -0.0125 67  ASP   B CG   
2370 O  OD1  . ASP   B 68  ? 0.676  0.415  0.299  -0.0346 0.0141  -0.0118 67  ASP   B OD1  
2371 O  OD2  . ASP   B 68  ? 0.7062 0.4234 0.3168 -0.0039 0.0229  -0.0116 67  ASP   B OD2  
2372 N  N    . ILE   B 69  ? 0.6377 0.4564 0.3157 -0.0433 0.0007  -0.0071 68  ILE   B N    
2373 C  CA   . ILE   B 69  ? 0.6309 0.471  0.3209 -0.0611 -0.0043 -0.0079 68  ILE   B CA   
2374 C  C    . ILE   B 69  ? 0.6538 0.467  0.3143 -0.0812 -0.005  -0.0138 68  ILE   B C    
2375 O  O    . ILE   B 69  ? 0.6497 0.4826 0.3165 -0.0996 -0.0108 -0.0157 68  ILE   B O    
2376 C  CB   . ILE   B 69  ? 0.625  0.4815 0.3366 -0.0602 0.0002  -0.0051 68  ILE   B CB   
2377 C  CG1  . ILE   B 69  ? 0.6535 0.4767 0.3465 -0.0552 0.0084  -0.0046 68  ILE   B CG1  
2378 C  CG2  . ILE   B 69  ? 0.6096 0.4978 0.3522 -0.0458 -0.0008 -0.0008 68  ILE   B CG2  
2379 C  CD1  . ILE   B 69  ? 0.6595 0.4932 0.3652 -0.0581 0.0129  -0.0025 68  ILE   B CD1  
2380 N  N    . ASN   B 70  ? 0.6844 0.4527 0.3126 -0.0777 0.001   -0.0168 69  ASN   B N    
2381 C  CA   . ASN   B 70  ? 0.7246 0.4545 0.3168 -0.0947 0.0021  -0.0231 69  ASN   B CA   
2382 C  C    . ASN   B 70  ? 0.74   0.4576 0.3106 -0.0961 -0.0019 -0.0286 69  ASN   B C    
2383 O  O    . ASN   B 70  ? 0.7582 0.4511 0.3117 -0.0801 0.0034  -0.0303 69  ASN   B O    
2384 C  CB   . ASN   B 70  ? 0.776  0.4607 0.3439 -0.0861 0.0113  -0.0226 69  ASN   B CB   
2385 C  CG   . ASN   B 70  ? 0.8748 0.508  0.3992 -0.101  0.014   -0.0291 69  ASN   B CG   
2386 O  OD1  . ASN   B 70  ? 0.8793 0.5119 0.3919 -0.1249 0.0091  -0.0345 69  ASN   B OD1  
2387 N  ND2  . ASN   B 70  ? 0.9347 0.5224 0.4331 -0.0868 0.0217  -0.0288 69  ASN   B ND2  
2388 N  N    . LYS   B 71  ? 0.7287 0.4675 0.3013 -0.1156 -0.0112 -0.0314 70  LYS   B N    
2389 C  CA   . LYS   B 71  ? 0.7451 0.4779 0.2968 -0.1219 -0.0171 -0.0366 70  LYS   B CA   
2390 C  C    . LYS   B 71  ? 0.7983 0.4729 0.302  -0.1277 -0.0106 -0.0455 70  LYS   B C    
2391 O  O    . LYS   B 71  ? 0.8156 0.4703 0.2996 -0.1152 -0.0071 -0.0489 70  LYS   B O    
2392 C  CB   . LYS   B 71  ? 0.7387 0.5098 0.3038 -0.1444 -0.03   -0.0372 70  LYS   B CB   
2393 C  CG   . LYS   B 71  ? 0.789  0.5644 0.337  -0.1505 -0.0392 -0.0406 70  LYS   B CG   
2394 C  CD   . LYS   B 71  ? 0.8109 0.6349 0.3796 -0.1691 -0.0541 -0.0391 70  LYS   B CD   
2395 C  CE   . LYS   B 71  ? 0.8618 0.6947 0.4145 -0.1738 -0.0654 -0.0405 70  LYS   B CE   
2396 N  NZ   . LYS   B 71  ? 0.9168 0.7043 0.4199 -0.1927 -0.064  -0.052  70  LYS   B NZ   
2397 N  N    . HIS   B 72  ? 0.8183 0.4633 0.3015 -0.146  -0.0077 -0.0496 71  HIS   B N    
2398 C  CA   . HIS   B 72  ? 0.8626 0.4446 0.2964 -0.153  -0.0009 -0.0584 71  HIS   B CA   
2399 C  C    . HIS   B 72  ? 0.8825 0.4287 0.3019 -0.1231 0.0105  -0.058  71  HIS   B C    
2400 O  O    . HIS   B 72  ? 0.9147 0.4237 0.2999 -0.1185 0.0151  -0.0658 71  HIS   B O    
2401 C  CB   . HIS   B 72  ? 0.8876 0.4441 0.306  -0.1759 0.0016  -0.0597 71  HIS   B CB   
2402 C  CG   . HIS   B 72  ? 0.9655 0.4483 0.3303 -0.1808 0.0099  -0.0677 71  HIS   B CG   
2403 N  ND1  . HIS   B 72  ? 1.0085 0.4614 0.3348 -0.2023 0.0071  -0.079  71  HIS   B ND1  
2404 C  CD2  . HIS   B 72  ? 1.0012 0.4341 0.3441 -0.1645 0.0205  -0.0659 71  HIS   B CD2  
2405 C  CE1  . HIS   B 72  ? 1.0519 0.4345 0.3334 -0.1988 0.0173  -0.0842 71  HIS   B CE1  
2406 N  NE2  . HIS   B 72  ? 1.0558 0.4245 0.3462 -0.1747 0.0253  -0.076  71  HIS   B NE2  
2407 N  N    . GLY   B 73  ? 0.8628 0.4208 0.307  -0.104  0.0151  -0.0496 72  GLY   B N    
2408 C  CA   . GLY   B 73  ? 0.8763 0.4088 0.3128 -0.0752 0.0248  -0.0479 72  GLY   B CA   
2409 C  C    . GLY   B 73  ? 0.866  0.4201 0.314  -0.0555 0.0261  -0.0482 72  GLY   B C    
2410 O  O    . GLY   B 73  ? 0.8944 0.4193 0.3221 -0.0371 0.0348  -0.052  72  GLY   B O    
2411 N  N    . VAL   B 74  ? 0.8212 0.426  0.3014 -0.0582 0.0184  -0.0437 73  VAL   B N    
2412 C  CA   . VAL   B 74  ? 0.8101 0.4351 0.3001 -0.0418 0.02    -0.0426 73  VAL   B CA   
2413 C  C    . VAL   B 74  ? 0.8375 0.4396 0.2923 -0.0497 0.0203  -0.052  73  VAL   B C    
2414 O  O    . VAL   B 74  ? 0.851  0.4405 0.2926 -0.0334 0.0286  -0.0553 73  VAL   B O    
2415 C  CB   . VAL   B 74  ? 0.7846 0.4634 0.3163 -0.039  0.0129  -0.0338 73  VAL   B CB   
2416 C  CG1  . VAL   B 74  ? 0.7803 0.4835 0.315  -0.0571 0.0013  -0.0342 73  VAL   B CG1  
2417 C  CG2  . VAL   B 74  ? 0.7787 0.4716 0.3235 -0.017  0.019   -0.0303 73  VAL   B CG2  
2418 N  N    . GLU   B 75  ? 0.8403 0.4343 0.2766 -0.0753 0.0123  -0.0573 74  GLU   B N    
2419 C  CA   . GLU   B 75  ? 0.8582 0.4268 0.2557 -0.0861 0.012   -0.0675 74  GLU   B CA   
2420 C  C    . GLU   B 75  ? 0.9094 0.4166 0.2647 -0.0787 0.0247  -0.0772 74  GLU   B C    
2421 O  O    . GLU   B 75  ? 0.9355 0.4196 0.2606 -0.0748 0.0303  -0.0857 74  GLU   B O    
2422 C  CB   . GLU   B 75  ? 0.8576 0.4384 0.2487 -0.1172 -0.0013 -0.0704 74  GLU   B CB   
2423 C  CG   . GLU   B 75  ? 0.8587 0.5007 0.2917 -0.1192 -0.0136 -0.0605 74  GLU   B CG   
2424 C  CD   . GLU   B 75  ? 0.9219 0.5904 0.3578 -0.1467 -0.0286 -0.0615 74  GLU   B CD   
2425 O  OE1  . GLU   B 75  ? 0.9638 0.6039 0.3691 -0.1698 -0.03   -0.0706 74  GLU   B OE1  
2426 O  OE2  . GLU   B 75  ? 0.9113 0.6294 0.38   -0.1451 -0.0392 -0.0531 74  GLU   B OE2  
2427 N  N    . GLU   B 76  ? 0.9284 0.4077 0.2801 -0.0751 0.03    -0.0758 75  GLU   B N    
2428 C  CA   . GLU   B 76  ? 0.9732 0.3909 0.2862 -0.0637 0.0421  -0.0831 75  GLU   B CA   
2429 C  C    . GLU   B 76  ? 0.9738 0.3959 0.2968 -0.0287 0.0531  -0.0813 75  GLU   B C    
2430 O  O    . GLU   B 76  ? 1.0062 0.39   0.2967 -0.0162 0.0636  -0.0903 75  GLU   B O    
2431 C  CB   . GLU   B 76  ? 1.0134 0.4065 0.3243 -0.0691 0.0428  -0.0786 75  GLU   B CB   
2432 C  CG   . GLU   B 76  ? 1.1406 0.4599 0.4032 -0.0639 0.0531  -0.086  75  GLU   B CG   
2433 C  CD   . GLU   B 76  ? 1.2761 0.5675 0.5326 -0.0702 0.0537  -0.0799 75  GLU   B CD   
2434 O  OE1  . GLU   B 76  ? 1.2821 0.6154 0.5766 -0.0717 0.0483  -0.0692 75  GLU   B OE1  
2435 O  OE2  . GLU   B 76  ? 1.3595 0.5837 0.5702 -0.0734 0.0604  -0.0859 75  GLU   B OE2  
2436 N  N    . THR   B 77  ? 0.936  0.4067 0.3039 -0.014  0.0511  -0.0703 76  THR   B N    
2437 C  CA   . THR   B 77  ? 0.9237 0.4099 0.3071 0.0154  0.0603  -0.0679 76  THR   B CA   
2438 C  C    . THR   B 77  ? 0.9201 0.4165 0.292  0.0156  0.0634  -0.0744 76  THR   B C    
2439 O  O    . THR   B 77  ? 0.9256 0.4039 0.2807 0.0343  0.0754  -0.0806 76  THR   B O    
2440 C  CB   . THR   B 77  ? 0.8964 0.4344 0.3291 0.0241  0.0556  -0.0554 76  THR   B CB   
2441 O  OG1  . THR   B 77  ? 0.9159 0.4406 0.3542 0.0275  0.0551  -0.0499 76  THR   B OG1  
2442 C  CG2  . THR   B 77  ? 0.8734 0.4398 0.3267 0.0482  0.0632  -0.0527 76  THR   B CG2  
2443 N  N    . ALA   B 78  ? 0.9128 0.4378 0.2923 -0.0049 0.0526  -0.0727 77  ALA   B N    
2444 C  CA   . ALA   B 78  ? 0.9257 0.4638 0.2938 -0.0083 0.0529  -0.0766 77  ALA   B CA   
2445 C  C    . ALA   B 78  ? 0.9772 0.4671 0.2936 -0.0142 0.0598  -0.091  77  ALA   B C    
2446 O  O    . ALA   B 78  ? 0.9921 0.4806 0.2931 -0.005  0.0685  -0.0964 77  ALA   B O    
2447 C  CB   . ALA   B 78  ? 0.9094 0.4843 0.2945 -0.029  0.0374  -0.0704 77  ALA   B CB   
2448 N  N    . ALA   B 79  ? 1.0043 0.4527 0.2915 -0.0307 0.0571  -0.098  78  ALA   B N    
2449 C  CA   . ALA   B 79  ? 1.0423 0.4367 0.2752 -0.0378 0.0644  -0.1133 78  ALA   B CA   
2450 C  C    . ALA   B 79  ? 1.0682 0.4296 0.2856 -0.0073 0.0828  -0.1193 78  ALA   B C    
2451 O  O    . ALA   B 79  ? 1.1025 0.4425 0.2885 -0.0014 0.0929  -0.1302 78  ALA   B O    
2452 C  CB   . ALA   B 79  ? 1.0607 0.4158 0.2667 -0.063  0.0581  -0.1188 78  ALA   B CB   
2453 N  N    . GLU   B 80  ? 1.0635 0.4247 0.3044 0.0134  0.0872  -0.1118 79  GLU   B N    
2454 C  CA   . GLU   B 80  ? 1.0811 0.4175 0.3139 0.0462  0.1032  -0.1153 79  GLU   B CA   
2455 C  C    . GLU   B 80  ? 1.0538 0.4359 0.3123 0.0667  0.1113  -0.1131 79  GLU   B C    
2456 O  O    . GLU   B 80  ? 1.075  0.437  0.3131 0.087   0.1265  -0.1223 79  GLU   B O    
2457 C  CB   . GLU   B 80  ? 1.1169 0.4424 0.3667 0.0608  0.1029  -0.1064 79  GLU   B CB   
2458 C  CG   . GLU   B 80  ? 1.2458 0.5007 0.4526 0.0541  0.105   -0.1124 79  GLU   B CG   
2459 C  CD   . GLU   B 80  ? 1.4188 0.6072 0.5715 0.0641  0.1189  -0.1279 79  GLU   B CD   
2460 O  OE1  . GLU   B 80  ? 1.4517 0.6455 0.6026 0.0892  0.1315  -0.1337 79  GLU   B OE1  
2461 O  OE2  . GLU   B 80  ? 1.4918 0.6211 0.6019 0.0455  0.118   -0.1349 79  GLU   B OE2  
2462 N  N    . CYS   B 81  ? 1.0093 0.4503 0.3086 0.0597  0.102   -0.102  80  CYS   B N    
2463 C  CA   . CYS   B 81  ? 0.9846 0.47   0.3068 0.0728  0.1087  -0.099  80  CYS   B CA   
2464 C  C    . CYS   B 81  ? 1.0188 0.4936 0.3062 0.0625  0.1138  -0.1094 80  CYS   B C    
2465 O  O    . CYS   B 81  ? 1.0262 0.5091 0.3094 0.0791  0.128   -0.1142 80  CYS   B O    
2466 C  CB   . CYS   B 81  ? 0.9427 0.4836 0.3109 0.0653  0.097   -0.0847 80  CYS   B CB   
2467 S  SG   . CYS   B 81  ? 0.9157 0.4769 0.3264 0.081   0.0939  -0.0729 80  CYS   B SG   
2468 N  N    . ARG   B 82  ? 1.0365 0.4934 0.2972 0.0349  0.1027  -0.1135 81  ARG   B N    
2469 C  CA   . ARG   B 82  ? 1.0639 0.5058 0.2848 0.0227  0.106   -0.1241 81  ARG   B CA   
2470 C  C    . ARG   B 82  ? 1.1204 0.5071 0.2964 0.0359  0.1233  -0.1406 81  ARG   B C    
2471 O  O    . ARG   B 82  ? 1.1267 0.511  0.281  0.0427  0.1357  -0.149  81  ARG   B O    
2472 C  CB   . ARG   B 82  ? 1.0685 0.5082 0.2731 -0.0106 0.0879  -0.1242 81  ARG   B CB   
2473 C  CG   . ARG   B 82  ? 1.037  0.5334 0.2834 -0.0197 0.0727  -0.1086 81  ARG   B CG   
2474 C  CD   . ARG   B 82  ? 1.0239 0.5266 0.2563 -0.0497 0.0545  -0.1082 81  ARG   B CD   
2475 N  NE   . ARG   B 82  ? 0.9769 0.5305 0.2544 -0.0537 0.0401  -0.0924 81  ARG   B NE   
2476 C  CZ   . ARG   B 82  ? 0.9179 0.4853 0.221  -0.0635 0.028   -0.086  81  ARG   B CZ   
2477 N  NH1  . ARG   B 82  ? 0.9084 0.4427 0.1943 -0.0746 0.0272  -0.0935 81  ARG   B NH1  
2478 N  NH2  . ARG   B 82  ? 0.8479 0.4606 0.1917 -0.0631 0.0172  -0.0724 81  ARG   B NH2  
2479 N  N    . LYS   B 83  ? 1.1572 0.4979 0.3182 0.0414  0.1258  -0.1451 82  LYS   B N    
2480 C  CA   . LYS   B 83  ? 1.2071 0.4891 0.3242 0.0584  0.1436  -0.1607 82  LYS   B CA   
2481 C  C    . LYS   B 83  ? 1.1949 0.499  0.3322 0.0952  0.162   -0.1608 82  LYS   B C    
2482 O  O    . LYS   B 83  ? 1.2224 0.4953 0.3261 0.11    0.1791  -0.1748 82  LYS   B O    
2483 C  CB   . LYS   B 83  ? 1.2622 0.4888 0.3603 0.0586  0.1421  -0.163  82  LYS   B CB   
2484 C  CG   . LYS   B 83  ? 1.3486 0.5422 0.4135 0.0206  0.1287  -0.1682 82  LYS   B CG   
2485 C  CD   . LYS   B 83  ? 1.446  0.5948 0.501  0.0171  0.1255  -0.166  82  LYS   B CD   
2486 C  CE   . LYS   B 83  ? 1.5535 0.6344 0.571  0.0434  0.143   -0.1761 82  LYS   B CE   
2487 N  NZ   . LYS   B 83  ? 1.6102 0.6597 0.6313 0.0491  0.1402  -0.1678 82  LYS   B NZ   
2488 N  N    . LEU   B 84  ? 1.1513 0.5122 0.3436 0.1084  0.1585  -0.1459 83  LEU   B N    
2489 C  CA   . LEU   B 84  ? 1.1285 0.5255 0.3497 0.139   0.173   -0.1436 83  LEU   B CA   
2490 C  C    . LEU   B 84  ? 1.1152 0.5524 0.3398 0.1342  0.1801  -0.1452 83  LEU   B C    
2491 O  O    . LEU   B 84  ? 1.1059 0.5777 0.3545 0.1564  0.1934  -0.1441 83  LEU   B O    
2492 C  CB   . LEU   B 84  ? 1.095  0.5358 0.3706 0.1499  0.1649  -0.1273 83  LEU   B CB   
2493 C  CG   . LEU   B 84  ? 1.119  0.5261 0.3949 0.163   0.1618  -0.1242 83  LEU   B CG   
2494 C  CD1  . LEU   B 84  ? 1.0877 0.5411 0.4146 0.166   0.1505  -0.1078 83  LEU   B CD1  
2495 C  CD2  . LEU   B 84  ? 1.1416 0.517  0.3998 0.1971  0.1796  -0.1333 83  LEU   B CD2  
2496 N  N    . GLY   B 85  ? 1.1086 0.5438 0.3105 0.1049  0.1706  -0.1469 84  GLY   B N    
2497 C  CA   . GLY   B 85  ? 1.093  0.5584 0.289  0.0966  0.1758  -0.1477 84  GLY   B CA   
2498 C  C    . GLY   B 85  ? 1.0548 0.5749 0.288  0.0815  0.162   -0.1313 84  GLY   B C    
2499 O  O    . GLY   B 85  ? 1.0551 0.5959 0.2788 0.0715  0.1644  -0.1304 84  GLY   B O    
2500 N  N    . ALA   B 86  ? 1.0148 0.5553 0.2868 0.0792  0.1475  -0.1184 85  ALA   B N    
2501 C  CA   . ALA   B 86  ? 0.9777 0.5665 0.2867 0.0679  0.1349  -0.1027 85  ALA   B CA   
2502 C  C    . ALA   B 86  ? 0.9735 0.5631 0.272  0.0398  0.1154  -0.0974 85  ALA   B C    
2503 O  O    . ALA   B 86  ? 0.9977 0.5559 0.2735 0.0263  0.1062  -0.1028 85  ALA   B O    
2504 C  CB   . ALA   B 86  ? 0.953  0.565  0.3086 0.0797  0.1296  -0.092  85  ALA   B CB   
2505 N  N    . THR   B 87  ? 0.9373 0.5649 0.2548 0.0311  0.1085  -0.0857 86  THR   B N    
2506 C  CA   . THR   B 87  ? 0.9157 0.5529 0.233  0.0088  0.0881  -0.0773 86  THR   B CA   
2507 C  C    . THR   B 87  ? 0.8804 0.5389 0.2423 0.0103  0.0761  -0.0659 86  THR   B C    
2508 O  O    . THR   B 87  ? 0.8662 0.5496 0.2627 0.024   0.0815  -0.0589 86  THR   B O    
2509 C  CB   . THR   B 87  ? 0.9104 0.5693 0.2191 0.0002  0.0867  -0.0703 86  THR   B CB   
2510 O  OG1  . THR   B 87  ? 0.9533 0.5857 0.2135 -0.0053 0.0954  -0.0828 86  THR   B OG1  
2511 C  CG2  . THR   B 87  ? 0.8999 0.5751 0.2168 -0.0174 0.0645  -0.0585 86  THR   B CG2  
2512 N  N    . VAL   B 88  ? 0.8602 0.5082 0.2199 -0.004  0.0611  -0.0657 87  VAL   B N    
2513 C  CA   . VAL   B 88  ? 0.8184 0.483  0.2159 -0.0033 0.0515  -0.0571 87  VAL   B CA   
2514 C  C    . VAL   B 88  ? 0.7894 0.4717 0.1964 -0.0215 0.0322  -0.0496 87  VAL   B C    
2515 O  O    . VAL   B 88  ? 0.7919 0.4589 0.1721 -0.0383 0.0237  -0.0554 87  VAL   B O    
2516 C  CB   . VAL   B 88  ? 0.8325 0.4662 0.2241 0.0013  0.0556  -0.0648 87  VAL   B CB   
2517 C  CG1  . VAL   B 88  ? 0.8157 0.4686 0.2458 0.0028  0.0477  -0.0555 87  VAL   B CG1  
2518 C  CG2  . VAL   B 88  ? 0.8466 0.4598 0.2267 0.0227  0.0743  -0.0728 87  VAL   B CG2  
2519 N  N    . HIS   B 89  ? 0.7576 0.4717 0.2041 -0.0178 0.0253  -0.0376 88  HIS   B N    
2520 C  CA   . HIS   B 89  ? 0.7352 0.4708 0.1989 -0.0304 0.0078  -0.0297 88  HIS   B CA   
2521 C  C    . HIS   B 89  ? 0.713  0.4567 0.2084 -0.0273 0.0056  -0.027  88  HIS   B C    
2522 O  O    . HIS   B 89  ? 0.7082 0.4603 0.227  -0.0132 0.0134  -0.0232 88  HIS   B O    
2523 C  CB   . HIS   B 89  ? 0.7243 0.4883 0.2044 -0.0277 0.0021  -0.0174 88  HIS   B CB   
2524 C  CG   . HIS   B 89  ? 0.7567 0.516  0.2042 -0.0354 -0.0006 -0.0174 88  HIS   B CG   
2525 N  ND1  . HIS   B 89  ? 0.7938 0.5423 0.2205 -0.0288 0.0139  -0.0209 88  HIS   B ND1  
2526 C  CD2  . HIS   B 89  ? 0.772  0.5379 0.2042 -0.0493 -0.0162 -0.0144 88  HIS   B CD2  
2527 C  CE1  . HIS   B 89  ? 0.8117 0.5574 0.2083 -0.0396 0.0073  -0.0198 88  HIS   B CE1  
2528 N  NE2  . HIS   B 89  ? 0.805  0.5612 0.2037 -0.0518 -0.0118 -0.0154 88  HIS   B NE2  
2529 N  N    . THR   B 90  ? 0.6996 0.4437 0.196  -0.0418 -0.0052 -0.0287 89  THR   B N    
2530 C  CA   . THR   B 90  ? 0.6803 0.4338 0.2052 -0.0413 -0.0071 -0.0259 89  THR   B CA   
2531 C  C    . THR   B 90  ? 0.6436 0.4343 0.1983 -0.0473 -0.021  -0.0168 89  THR   B C    
2532 O  O    . THR   B 90  ? 0.6378 0.4413 0.1848 -0.058  -0.0327 -0.015  89  THR   B O    
2533 C  CB   . THR   B 90  ? 0.7075 0.4302 0.2112 -0.0528 -0.0053 -0.0354 89  THR   B CB   
2534 O  OG1  . THR   B 90  ? 0.7262 0.4494 0.2119 -0.0744 -0.0168 -0.0394 89  THR   B OG1  
2535 C  CG2  . THR   B 90  ? 0.7201 0.4024 0.1943 -0.0428 0.009   -0.0442 89  THR   B CG2  
2536 N  N    . PHE   B 91  ? 0.6243 0.432  0.2119 -0.0399 -0.0198 -0.0114 90  PHE   B N    
2537 C  CA   . PHE   B 91  ? 0.6026 0.4444 0.2215 -0.0421 -0.0303 -0.0038 90  PHE   B CA   
2538 C  C    . PHE   B 91  ? 0.6007 0.4459 0.2391 -0.0443 -0.0273 -0.0053 90  PHE   B C    
2539 O  O    . PHE   B 91  ? 0.6148 0.4437 0.2538 -0.0354 -0.0167 -0.0069 90  PHE   B O    
2540 C  CB   . PHE   B 91  ? 0.5874 0.447  0.226  -0.0274 -0.03   0.0058  90  PHE   B CB   
2541 C  CG   . PHE   B 91  ? 0.6116 0.4678 0.2292 -0.0266 -0.0328 0.009   90  PHE   B CG   
2542 C  CD1  . PHE   B 91  ? 0.6167 0.4909 0.2339 -0.0321 -0.0469 0.015   90  PHE   B CD1  
2543 C  CD2  . PHE   B 91  ? 0.6337 0.4701 0.2312 -0.0202 -0.0213 0.0062  90  PHE   B CD2  
2544 C  CE1  . PHE   B 91  ? 0.6424 0.5108 0.2355 -0.0325 -0.0499 0.0188  90  PHE   B CE1  
2545 C  CE2  . PHE   B 91  ? 0.6603 0.4931 0.2356 -0.0213 -0.0226 0.009   90  PHE   B CE2  
2546 C  CZ   . PHE   B 91  ? 0.6562 0.503  0.2274 -0.028  -0.0371 0.0155  90  PHE   B CZ   
2547 N  N    . VAL   B 92  ? 0.5812 0.4487 0.2344 -0.0568 -0.0363 -0.0048 91  VAL   B N    
2548 C  CA   . VAL   B 92  ? 0.5733 0.4479 0.2458 -0.06   -0.0327 -0.0055 91  VAL   B CA   
2549 C  C    . VAL   B 92  ? 0.562  0.4646 0.2692 -0.0457 -0.0326 0.0021  91  VAL   B C    
2550 O  O    . VAL   B 92  ? 0.5589 0.4915 0.2851 -0.045  -0.0419 0.0069  91  VAL   B O    
2551 C  CB   . VAL   B 92  ? 0.5644 0.4537 0.2392 -0.0812 -0.0402 -0.0091 91  VAL   B CB   
2552 C  CG1  . VAL   B 92  ? 0.5517 0.4454 0.2435 -0.0843 -0.0336 -0.0096 91  VAL   B CG1  
2553 C  CG2  . VAL   B 92  ? 0.5928 0.4516 0.2291 -0.0984 -0.0414 -0.0174 91  VAL   B CG2  
2554 N  N    . VAL   B 93  ? 0.5477 0.4398 0.2616 -0.0331 -0.0227 0.0033  92  VAL   B N    
2555 C  CA   . VAL   B 93  ? 0.5182 0.4308 0.2602 -0.0203 -0.0215 0.0092  92  VAL   B CA   
2556 C  C    . VAL   B 93  ? 0.5073 0.4179 0.2612 -0.0178 -0.0133 0.0079  92  VAL   B C    
2557 O  O    . VAL   B 93  ? 0.5178 0.4048 0.2563 -0.0162 -0.0062 0.0052  92  VAL   B O    
2558 C  CB   . VAL   B 93  ? 0.5188 0.4237 0.2561 -0.0071 -0.0185 0.0135  92  VAL   B CB   
2559 C  CG1  . VAL   B 93  ? 0.5002 0.4233 0.2625 0.0034  -0.0192 0.0197  92  VAL   B CG1  
2560 C  CG2  . VAL   B 93  ? 0.5307 0.4288 0.2459 -0.0106 -0.0242 0.0141  92  VAL   B CG2  
2561 N  N    . ASP   B 94  ? 0.4809 0.4161 0.2611 -0.0161 -0.0141 0.0099  93  ASP   B N    
2562 C  CA   . ASP   B 94  ? 0.4686 0.4047 0.2601 -0.0135 -0.0063 0.0089  93  ASP   B CA   
2563 C  C    . ASP   B 94  ? 0.47   0.4017 0.2669 0.0008  -0.0021 0.0119  93  ASP   B C    
2564 O  O    . ASP   B 94  ? 0.4602 0.4063 0.273  0.0083  -0.0044 0.0153  93  ASP   B O    
2565 C  CB   . ASP   B 94  ? 0.4587 0.4249 0.2757 -0.017  -0.0078 0.0088  93  ASP   B CB   
2566 C  CG   . ASP   B 94  ? 0.5265 0.4952 0.3533 -0.0164 0.001   0.007   93  ASP   B CG   
2567 O  OD1  . ASP   B 94  ? 0.5258 0.4736 0.341  -0.0117 0.0069  0.0068  93  ASP   B OD1  
2568 O  OD2  . ASP   B 94  ? 0.5478 0.5416 0.394  -0.0202 0.0018  0.0056  93  ASP   B OD2  
2569 N  N    . CYS   B 95  ? 0.4813 0.3928 0.2643 0.0046  0.0039  0.0109  94  CYS   B N    
2570 C  CA   . CYS   B 95  ? 0.4853 0.3943 0.2719 0.0153  0.0081  0.0131  94  CYS   B CA   
2571 C  C    . CYS   B 95  ? 0.4871 0.405  0.2896 0.0187  0.0124  0.013   94  CYS   B C    
2572 O  O    . CYS   B 95  ? 0.4903 0.4058 0.294  0.0246  0.0161  0.0138  94  CYS   B O    
2573 C  CB   . CYS   B 95  ? 0.5034 0.3937 0.2713 0.0191  0.0121  0.0119  94  CYS   B CB   
2574 S  SG   . CYS   B 95  ? 0.5921 0.4687 0.3372 0.0157  0.009   0.0104  94  CYS   B SG   
2575 N  N    . GLY   B 96  ? 0.4817 0.412  0.296  0.0138  0.0122  0.0115  95  GLY   B N    
2576 C  CA   . GLY   B 96  ? 0.4754 0.4155 0.3041 0.0163  0.0167  0.0102  95  GLY   B CA   
2577 C  C    . GLY   B 96  ? 0.4651 0.4237 0.3134 0.0202  0.0145  0.0108  95  GLY   B C    
2578 O  O    . GLY   B 96  ? 0.4681 0.4335 0.3283 0.0242  0.019   0.0089  95  GLY   B O    
2579 N  N    . ASN   B 97  ? 0.4519 0.4181 0.3023 0.0201  0.0071  0.0135  96  ASN   B N    
2580 C  CA   . ASN   B 97  ? 0.4301 0.4154 0.2987 0.0263  0.0025  0.0158  96  ASN   B CA   
2581 C  C    . ASN   B 97  ? 0.4382 0.4138 0.3027 0.0358  -0.0014 0.0215  96  ASN   B C    
2582 O  O    . ASN   B 97  ? 0.4437 0.4134 0.2953 0.0335  -0.0073 0.0247  96  ASN   B O    
2583 C  CB   . ASN   B 97  ? 0.4182 0.4219 0.2908 0.0179  -0.0046 0.0156  96  ASN   B CB   
2584 C  CG   . ASN   B 97  ? 0.4338 0.4656 0.3299 0.0251  -0.0097 0.0178  96  ASN   B CG   
2585 O  OD1  . ASN   B 97  ? 0.435  0.4681 0.3338 0.0352  -0.0163 0.0233  96  ASN   B OD1  
2586 N  ND2  . ASN   B 97  ? 0.448  0.5036 0.3616 0.0209  -0.0063 0.0138  96  ASN   B ND2  
2587 N  N    . ARG   B 98  ? 0.4389 0.4109 0.312  0.0454  0.0022  0.0224  97  ARG   B N    
2588 C  CA   . ARG   B 98  ? 0.4535 0.4115 0.3208 0.0534  -0.0001 0.0283  97  ARG   B CA   
2589 C  C    . ARG   B 98  ? 0.4692 0.4347 0.3361 0.0577  -0.0108 0.0352  97  ARG   B C    
2590 O  O    . ARG   B 98  ? 0.4869 0.4387 0.3372 0.0567  -0.0142 0.0403  97  ARG   B O    
2591 C  CB   . ARG   B 98  ? 0.4636 0.4154 0.3405 0.0623  0.0058  0.0269  97  ARG   B CB   
2592 C  CG   . ARG   B 98  ? 0.531  0.4595 0.3961 0.0669  0.0062  0.0321  97  ARG   B CG   
2593 C  CD   . ARG   B 98  ? 0.594  0.5111 0.4652 0.0748  0.0125  0.0295  97  ARG   B CD   
2594 N  NE   . ARG   B 98  ? 0.6639 0.5938 0.5518 0.0881  0.0091  0.031   97  ARG   B NE   
2595 C  CZ   . ARG   B 98  ? 0.7309 0.6501 0.6177 0.1007  0.0041  0.0384  97  ARG   B CZ   
2596 N  NH1  . ARG   B 98  ? 0.7403 0.6317 0.6074 0.0992  0.0031  0.0448  97  ARG   B NH1  
2597 N  NH2  . ARG   B 98  ? 0.738  0.6744 0.6432 0.1151  0.0006  0.0398  97  ARG   B NH2  
2598 N  N    . GLU   B 99  ? 0.4611 0.451  0.3461 0.0618  -0.0162 0.0355  98  GLU   B N    
2599 C  CA   . GLU   B 99  ? 0.465  0.468  0.3523 0.0667  -0.0285 0.0426  98  GLU   B CA   
2600 C  C    . GLU   B 99  ? 0.4767 0.4794 0.3458 0.0539  -0.0352 0.0431  98  GLU   B C    
2601 O  O    . GLU   B 99  ? 0.4897 0.4846 0.3442 0.0556  -0.0429 0.0499  98  GLU   B O    
2602 C  CB   . GLU   B 99  ? 0.4916 0.5285 0.4065 0.0734  -0.0321 0.0415  98  GLU   B CB   
2603 C  CG   . GLU   B 99  ? 0.6183 0.6732 0.5395 0.0823  -0.0462 0.0501  98  GLU   B CG   
2604 C  CD   . GLU   B 99  ? 0.7213 0.8179 0.6741 0.0904  -0.0507 0.0493  98  GLU   B CD   
2605 O  OE1  . GLU   B 99  ? 0.7261 0.836  0.6968 0.0902  -0.0406 0.0416  98  GLU   B OE1  
2606 O  OE2  . GLU   B 99  ? 0.7466 0.8648 0.7064 0.097   -0.0644 0.0566  98  GLU   B OE2  
2607 N  N    . ASP   B 100 ? 0.4735 0.4807 0.3398 0.0406  -0.0316 0.036   99  ASP   B N    
2608 C  CA   . ASP   B 100 ? 0.4783 0.4798 0.3242 0.0276  -0.036  0.0343  99  ASP   B CA   
2609 C  C    . ASP   B 100 ? 0.4822 0.455  0.3034 0.0283  -0.0324 0.0362  99  ASP   B C    
2610 O  O    . ASP   B 100 ? 0.4988 0.4661 0.3021 0.0246  -0.0388 0.039   99  ASP   B O    
2611 C  CB   . ASP   B 100 ? 0.5177 0.5212 0.3629 0.0145  -0.0306 0.0263  99  ASP   B CB   
2612 C  CG   . ASP   B 100 ? 0.6506 0.6503 0.4763 -0.0005 -0.0361 0.0232  99  ASP   B CG   
2613 O  OD1  . ASP   B 100 ? 0.6923 0.6869 0.5027 -0.0011 -0.0437 0.0266  99  ASP   B OD1  
2614 O  OD2  . ASP   B 100 ? 0.6981 0.6971 0.521  -0.0129 -0.0325 0.0173  99  ASP   B OD2  
2615 N  N    . ILE   B 101 ? 0.4639 0.4211 0.2842 0.0322  -0.0221 0.0345  100 ILE   B N    
2616 C  CA   . ILE   B 101 ? 0.4633 0.3997 0.2646 0.0325  -0.0172 0.0359  100 ILE   B CA   
2617 C  C    . ILE   B 101 ? 0.4922 0.4224 0.2848 0.0378  -0.0223 0.0443  100 ILE   B C    
2618 O  O    . ILE   B 101 ? 0.5041 0.4248 0.276  0.0338  -0.0237 0.0461  100 ILE   B O    
2619 C  CB   . ILE   B 101 ? 0.4426 0.371  0.249  0.0349  -0.0067 0.0327  100 ILE   B CB   
2620 C  CG1  . ILE   B 101 ? 0.4378 0.366  0.2435 0.0293  -0.0019 0.0258  100 ILE   B CG1  
2621 C  CG2  . ILE   B 101 ? 0.4442 0.3585 0.2378 0.0361  -0.0016 0.0353  100 ILE   B CG2  
2622 C  CD1  . ILE   B 101 ? 0.4286 0.3552 0.2429 0.0318  0.0057  0.0232  100 ILE   B CD1  
2623 N  N    . TYR   B 102 ? 0.4939 0.4273 0.2998 0.0471  -0.0248 0.0496  101 TYR   B N    
2624 C  CA   . TYR   B 102 ? 0.5127 0.4354 0.3077 0.0528  -0.0301 0.0591  101 TYR   B CA   
2625 C  C    . TYR   B 102 ? 0.5362 0.4679 0.3203 0.0508  -0.0426 0.0642  101 TYR   B C    
2626 O  O    . TYR   B 102 ? 0.5613 0.4794 0.3229 0.0485  -0.0448 0.0698  101 TYR   B O    
2627 C  CB   . TYR   B 102 ? 0.5038 0.4236 0.3137 0.0652  -0.0301 0.0635  101 TYR   B CB   
2628 C  CG   . TYR   B 102 ? 0.5137 0.418  0.3262 0.065   -0.0182 0.0594  101 TYR   B CG   
2629 C  CD1  . TYR   B 102 ? 0.5372 0.4288 0.3353 0.0561  -0.0103 0.0572  101 TYR   B CD1  
2630 C  CD2  . TYR   B 102 ? 0.5132 0.4168 0.3419 0.0738  -0.0149 0.0575  101 TYR   B CD2  
2631 C  CE1  . TYR   B 102 ? 0.548  0.4296 0.3489 0.054   -0.0009 0.0534  101 TYR   B CE1  
2632 C  CE2  . TYR   B 102 ? 0.5321 0.4202 0.3599 0.0716  -0.0047 0.0532  101 TYR   B CE2  
2633 C  CZ   . TYR   B 102 ? 0.5575 0.4358 0.3717 0.0607  0.0016  0.0513  101 TYR   B CZ   
2634 O  OH   . TYR   B 102 ? 0.5762 0.4432 0.3899 0.0564  0.0103  0.0469  101 TYR   B OH   
2635 N  N    . ASN   B 103 ? 0.5308 0.4869 0.3298 0.05    -0.0507 0.062   102 ASN   B N    
2636 C  CA   . ASN   B 103 ? 0.5399 0.5094 0.3296 0.0459  -0.0643 0.0658  102 ASN   B CA   
2637 C  C    . ASN   B 103 ? 0.5476 0.5039 0.3092 0.0321  -0.0624 0.0611  102 ASN   B C    
2638 O  O    . ASN   B 103 ? 0.5517 0.5045 0.2923 0.0288  -0.0706 0.0661  102 ASN   B O    
2639 C  CB   . ASN   B 103 ? 0.5615 0.5641 0.3751 0.044   -0.0716 0.0623  102 ASN   B CB   
2640 C  CG   . ASN   B 103 ? 0.6274 0.6502 0.465  0.0599  -0.0792 0.0695  102 ASN   B CG   
2641 O  OD1  . ASN   B 103 ? 0.6702 0.6904 0.4999 0.0693  -0.0892 0.08    102 ASN   B OD1  
2642 N  ND2  . ASN   B 103 ? 0.6305 0.6736 0.4966 0.0642  -0.0745 0.0644  102 ASN   B ND2  
2643 N  N    . SER   B 104 ? 0.5428 0.4905 0.3023 0.025   -0.0514 0.0516  103 SER   B N    
2644 C  CA   . SER   B 104 ? 0.5566 0.4884 0.2896 0.0148  -0.0472 0.0457  103 SER   B CA   
2645 C  C    . SER   B 104 ? 0.573  0.4844 0.2857 0.0175  -0.04   0.0491  103 SER   B C    
2646 O  O    . SER   B 104 ? 0.5832 0.4841 0.2696 0.0111  -0.0401 0.0474  103 SER   B O    
2647 C  CB   . SER   B 104 ? 0.5661 0.4934 0.3028 0.0093  -0.0384 0.0358  103 SER   B CB   
2648 O  OG   . SER   B 104 ? 0.5886 0.534  0.3377 0.0019  -0.0453 0.0325  103 SER   B OG   
2649 N  N    . VAL   B 105 ? 0.5698 0.4758 0.2928 0.0255  -0.0335 0.0534  104 VAL   B N    
2650 C  CA   . VAL   B 105 ? 0.5924 0.4823 0.2976 0.0258  -0.0264 0.0574  104 VAL   B CA   
2651 C  C    . VAL   B 105 ? 0.6161 0.5014 0.3014 0.0253  -0.036  0.0671  104 VAL   B C    
2652 O  O    . VAL   B 105 ? 0.6344 0.5085 0.2939 0.0198  -0.0323 0.0676  104 VAL   B O    
2653 C  CB   . VAL   B 105 ? 0.5903 0.4749 0.3094 0.0308  -0.0172 0.0591  104 VAL   B CB   
2654 C  CG1  . VAL   B 105 ? 0.6069 0.4769 0.3074 0.0286  -0.0115 0.0654  104 VAL   B CG1  
2655 C  CG2  . VAL   B 105 ? 0.5828 0.4709 0.3134 0.0298  -0.0075 0.0498  104 VAL   B CG2  
2656 N  N    . LYS   B 106 ? 0.6185 0.5142 0.3145 0.0313  -0.0488 0.0743  105 LYS   B N    
2657 C  CA   . LYS   B 106 ? 0.6449 0.5385 0.3223 0.0324  -0.0611 0.085   105 LYS   B CA   
2658 C  C    . LYS   B 106 ? 0.6535 0.5495 0.3059 0.0208  -0.0663 0.0805  105 LYS   B C    
2659 O  O    . LYS   B 106 ? 0.679  0.563  0.3017 0.0167  -0.0687 0.0861  105 LYS   B O    
2660 C  CB   . LYS   B 106 ? 0.6807 0.5927 0.3802 0.0433  -0.075  0.0919  105 LYS   B CB   
2661 C  CG   . LYS   B 106 ? 0.7732 0.6709 0.4763 0.0566  -0.0757 0.1035  105 LYS   B CG   
2662 C  CD   . LYS   B 106 ? 0.8375 0.7529 0.5745 0.0709  -0.0807 0.1045  105 LYS   B CD   
2663 C  CE   . LYS   B 106 ? 0.8865 0.8286 0.6327 0.0784  -0.099  0.1112  105 LYS   B CE   
2664 N  NZ   . LYS   B 106 ? 0.8841 0.8504 0.6672 0.092   -0.1012 0.1095  105 LYS   B NZ   
2665 N  N    . GLN   B 107 ? 0.6387 0.5475 0.3002 0.0143  -0.0674 0.0701  106 GLN   B N    
2666 C  CA   . GLN   B 107 ? 0.6476 0.5554 0.2854 0.0015  -0.0713 0.0629  106 GLN   B CA   
2667 C  C    . GLN   B 107 ? 0.651  0.5352 0.261  -0.0034 -0.057  0.0567  106 GLN   B C    
2668 O  O    . GLN   B 107 ? 0.6556 0.5308 0.2342 -0.0107 -0.0597 0.0567  106 GLN   B O    
2669 C  CB   . GLN   B 107 ? 0.6726 0.5941 0.3276 -0.0049 -0.0726 0.0529  106 GLN   B CB   
2670 C  CG   . GLN   B 107 ? 0.7456 0.6842 0.3932 -0.0162 -0.088  0.0514  106 GLN   B CG   
2671 C  CD   . GLN   B 107 ? 0.8481 0.799  0.513  -0.0251 -0.0874 0.0418  106 GLN   B CD   
2672 O  OE1  . GLN   B 107 ? 0.8916 0.8382 0.5377 -0.0407 -0.0903 0.0333  106 GLN   B OE1  
2673 N  NE2  . GLN   B 107 ? 0.849  0.8131 0.5474 -0.0167 -0.0829 0.0424  106 GLN   B NE2  
2674 N  N    . VAL   B 108 ? 0.6421 0.5185 0.2634 0.001   -0.0418 0.0516  107 VAL   B N    
2675 C  CA   . VAL   B 108 ? 0.6521 0.5123 0.2533 -0.0007 -0.0271 0.0456  107 VAL   B CA   
2676 C  C    . VAL   B 108 ? 0.6639 0.5156 0.2439 -0.0011 -0.0244 0.054   107 VAL   B C    
2677 O  O    . VAL   B 108 ? 0.6779 0.5189 0.2289 -0.0066 -0.0184 0.0501  107 VAL   B O    
2678 C  CB   . VAL   B 108 ? 0.6517 0.5117 0.2738 0.0055  -0.0137 0.0398  107 VAL   B CB   
2679 C  CG1  . VAL   B 108 ? 0.6669 0.5169 0.2728 0.0064  0.0015  0.0351  107 VAL   B CG1  
2680 C  CG2  . VAL   B 108 ? 0.6504 0.5129 0.2842 0.0039  -0.0151 0.0312  107 VAL   B CG2  
2681 N  N    . LYS   B 109 ? 0.6601 0.5137 0.251  0.0042  -0.0283 0.0655  108 LYS   B N    
2682 C  CA   . LYS   B 109 ? 0.6714 0.513  0.2391 0.0021  -0.0259 0.0753  108 LYS   B CA   
2683 C  C    . LYS   B 109 ? 0.702  0.5398 0.2381 -0.0042 -0.0377 0.0797  108 LYS   B C    
2684 O  O    . LYS   B 109 ? 0.7277 0.5539 0.2325 -0.0106 -0.0317 0.0811  108 LYS   B O    
2685 C  CB   . LYS   B 109 ? 0.6651 0.504  0.2485 0.0093  -0.03   0.0874  108 LYS   B CB   
2686 C  CG   . LYS   B 109 ? 0.6724 0.5114 0.2797 0.0127  -0.0179 0.0842  108 LYS   B CG   
2687 C  CD   . LYS   B 109 ? 0.7112 0.5404 0.3259 0.0186  -0.0223 0.0958  108 LYS   B CD   
2688 C  CE   . LYS   B 109 ? 0.7479 0.5755 0.3841 0.0201  -0.0116 0.0926  108 LYS   B CE   
2689 N  NZ   . LYS   B 109 ? 0.7909 0.6179 0.4488 0.0305  -0.0194 0.0964  108 LYS   B NZ   
2690 N  N    . LYS   B 110 ? 0.6988 0.5492 0.2429 -0.0032 -0.0547 0.0818  109 LYS   B N    
2691 C  CA   . LYS   B 110 ? 0.7068 0.5586 0.2233 -0.0096 -0.0696 0.0867  109 LYS   B CA   
2692 C  C    . LYS   B 110 ? 0.736  0.582  0.2246 -0.0219 -0.0659 0.0737  109 LYS   B C    
2693 O  O    . LYS   B 110 ? 0.7667 0.6068 0.221  -0.0299 -0.0729 0.0764  109 LYS   B O    
2694 C  CB   . LYS   B 110 ? 0.7022 0.5768 0.2424 -0.0046 -0.0889 0.0917  109 LYS   B CB   
2695 C  CG   . LYS   B 110 ? 0.7742 0.6553 0.2915 -0.0076 -0.1081 0.1016  109 LYS   B CG   
2696 C  CD   . LYS   B 110 ? 0.8191 0.7302 0.3566 -0.0094 -0.1254 0.0992  109 LYS   B CD   
2697 C  CE   . LYS   B 110 ? 0.8587 0.7779 0.3661 -0.0186 -0.1435 0.104   109 LYS   B CE   
2698 N  NZ   . LYS   B 110 ? 0.9027 0.8046 0.373  -0.036  -0.1353 0.0911  109 LYS   B NZ   
2699 N  N    . GLU   B 111 ? 0.7337 0.579  0.234  -0.0235 -0.0556 0.0597  110 GLU   B N    
2700 C  CA   . GLU   B 111 ? 0.7502 0.5847 0.2234 -0.034  -0.0518 0.0462  110 GLU   B CA   
2701 C  C    . GLU   B 111 ? 0.7605 0.5772 0.2174 -0.0328 -0.0308 0.0369  110 GLU   B C    
2702 O  O    . GLU   B 111 ? 0.7898 0.5921 0.2136 -0.0405 -0.0262 0.0276  110 GLU   B O    
2703 C  CB   . GLU   B 111 ? 0.7708 0.6133 0.2635 -0.0375 -0.0563 0.0366  110 GLU   B CB   
2704 C  CG   . GLU   B 111 ? 0.8208 0.6859 0.3256 -0.0425 -0.0773 0.0421  110 GLU   B CG   
2705 C  CD   . GLU   B 111 ? 0.9227 0.7948 0.4429 -0.05   -0.0795 0.0316  110 GLU   B CD   
2706 O  OE1  . GLU   B 111 ? 0.9656 0.8164 0.4674 -0.0566 -0.0688 0.0188  110 GLU   B OE1  
2707 O  OE2  . GLU   B 111 ? 0.9453 0.8433 0.4952 -0.049  -0.0911 0.0362  110 GLU   B OE2  
2708 N  N    . VAL   B 112 ? 0.7335 0.5524 0.2144 -0.0232 -0.0178 0.0377  111 VAL   B N    
2709 C  CA   . VAL   B 112 ? 0.7302 0.5396 0.2029 -0.0197 0.0024  0.0287  111 VAL   B CA   
2710 C  C    . VAL   B 112 ? 0.7298 0.5419 0.2016 -0.0172 0.0131  0.037   111 VAL   B C    
2711 O  O    . VAL   B 112 ? 0.7388 0.5437 0.1843 -0.0204 0.0249  0.0337  111 VAL   B O    
2712 C  CB   . VAL   B 112 ? 0.7168 0.5285 0.2172 -0.012  0.0095  0.02    111 VAL   B CB   
2713 C  CG1  . VAL   B 112 ? 0.7266 0.5318 0.2205 -0.0053 0.0293  0.011   111 VAL   B CG1  
2714 C  CG2  . VAL   B 112 ? 0.7158 0.5216 0.2133 -0.0177 -0.0002 0.0124  111 VAL   B CG2  
2715 N  N    . GLY   B 113 ? 0.7224 0.5439 0.2211 -0.0127 0.0096  0.0472  112 GLY   B N    
2716 C  CA   . GLY   B 113 ? 0.719  0.5413 0.2187 -0.0129 0.0189  0.0557  112 GLY   B CA   
2717 C  C    . GLY   B 113 ? 0.7046 0.5374 0.2414 -0.0062 0.024   0.0562  112 GLY   B C    
2718 O  O    . GLY   B 113 ? 0.6881 0.5267 0.2498 -0.0009 0.016   0.0548  112 GLY   B O    
2719 N  N    . ASP   B 114 ? 0.6972 0.534  0.2368 -0.008  0.0379  0.0577  113 ASP   B N    
2720 C  CA   . ASP   B 114 ? 0.6682 0.5157 0.2394 -0.0044 0.0432  0.058   113 ASP   B CA   
2721 C  C    . ASP   B 114 ? 0.6521 0.5133 0.2398 0.0018  0.0542  0.046   113 ASP   B C    
2722 O  O    . ASP   B 114 ? 0.6556 0.5231 0.2331 0.0011  0.0678  0.0407  113 ASP   B O    
2723 C  CB   . ASP   B 114 ? 0.6814 0.5272 0.2469 -0.0123 0.0516  0.0666  113 ASP   B CB   
2724 C  CG   . ASP   B 114 ? 0.7448 0.5725 0.2976 -0.0156 0.0399  0.0806  113 ASP   B CG   
2725 O  OD1  . ASP   B 114 ? 0.7297 0.554  0.2971 -0.0087 0.0266  0.0838  113 ASP   B OD1  
2726 O  OD2  . ASP   B 114 ? 0.8179 0.6347 0.3456 -0.0246 0.0446  0.0888  113 ASP   B OD2  
2727 N  N    . VAL   B 115 ? 0.6356 0.5023 0.2491 0.0087  0.049   0.0421  114 VAL   B N    
2728 C  CA   . VAL   B 115 ? 0.629  0.5071 0.2587 0.0164  0.0576  0.0326  114 VAL   B CA   
2729 C  C    . VAL   B 115 ? 0.6256 0.522  0.2678 0.0153  0.0709  0.0328  114 VAL   B C    
2730 O  O    . VAL   B 115 ? 0.6177 0.5175 0.269  0.0087  0.0701  0.0399  114 VAL   B O    
2731 C  CB   . VAL   B 115 ? 0.6174 0.4969 0.2704 0.0219  0.0489  0.0308  114 VAL   B CB   
2732 C  CG1  . VAL   B 115 ? 0.6116 0.5016 0.2799 0.0304  0.0567  0.0233  114 VAL   B CG1  
2733 C  CG2  . VAL   B 115 ? 0.627  0.4938 0.2694 0.021   0.0372  0.0293  114 VAL   B CG2  
2734 N  N    . THR   B 116 ? 0.6272 0.5352 0.2683 0.0213  0.0832  0.0248  115 THR   B N    
2735 C  CA   . THR   B 116 ? 0.6285 0.5618 0.2851 0.0205  0.0957  0.0241  115 THR   B CA   
2736 C  C    . THR   B 116 ? 0.6144 0.5649 0.2987 0.0318  0.0963  0.0188  115 THR   B C    
2737 O  O    . THR   B 116 ? 0.6109 0.5843 0.3165 0.0288  0.1001  0.0204  115 THR   B O    
2738 C  CB   . THR   B 116 ? 0.6744 0.6155 0.3127 0.0201  0.1103  0.0199  115 THR   B CB   
2739 O  OG1  . THR   B 116 ? 0.7162 0.6445 0.3288 0.0067  0.1106  0.027   115 THR   B OG1  
2740 C  CG2  . THR   B 116 ? 0.667  0.6422 0.3264 0.0222  0.1241  0.0168  115 THR   B CG2  
2741 N  N    . ILE   B 117 ? 0.5956 0.5345 0.2778 0.0436  0.0925  0.0126  116 ILE   B N    
2742 C  CA   . ILE   B 117 ? 0.5643 0.5154 0.2686 0.055   0.0919  0.0091  116 ILE   B CA   
2743 C  C    . ILE   B 117 ? 0.555  0.4864 0.2611 0.0556  0.0789  0.0102  116 ILE   B C    
2744 O  O    . ILE   B 117 ? 0.5626 0.471  0.2499 0.0563  0.0746  0.0074  116 ILE   B O    
2745 C  CB   . ILE   B 117 ? 0.557  0.5132 0.2572 0.071   0.1022  0.0009  116 ILE   B CB   
2746 C  CG1  . ILE   B 117 ? 0.5496 0.533  0.2523 0.0707  0.1169  -0.0007 116 ILE   B CG1  
2747 C  CG2  . ILE   B 117 ? 0.5438 0.5079 0.2638 0.0842  0.0988  -0.0007 116 ILE   B CG2  
2748 C  CD1  . ILE   B 117 ? 0.5629 0.5511 0.2599 0.0882  0.1286  -0.0093 116 ILE   B CD1  
2749 N  N    . LEU   B 118 ? 0.5376 0.4789 0.265  0.0534  0.0731  0.0137  117 LEU   B N    
2750 C  CA   . LEU   B 118 ? 0.5383 0.4655 0.2698 0.0537  0.0627  0.0143  117 LEU   B CA   
2751 C  C    . LEU   B 118 ? 0.5293 0.4626 0.2723 0.0647  0.063   0.0111  117 LEU   B C    
2752 O  O    . LEU   B 118 ? 0.5252 0.4811 0.2857 0.067   0.0659  0.0119  117 LEU   B O    
2753 C  CB   . LEU   B 118 ? 0.5342 0.464  0.2778 0.044   0.0562  0.0201  117 LEU   B CB   
2754 C  CG   . LEU   B 118 ? 0.5451 0.4671 0.2976 0.0443  0.0474  0.0203  117 LEU   B CG   
2755 C  CD1  . LEU   B 118 ? 0.5633 0.4664 0.3013 0.0445  0.0415  0.0185  117 LEU   B CD1  
2756 C  CD2  . LEU   B 118 ? 0.5423 0.4664 0.306  0.0369  0.0435  0.0249  117 LEU   B CD2  
2757 N  N    . VAL   B 119 ? 0.5276 0.4401 0.2593 0.0702  0.0596  0.0079  118 VAL   B N    
2758 C  CA   . VAL   B 119 ? 0.5124 0.4232 0.2497 0.0807  0.0587  0.0064  118 VAL   B CA   
2759 C  C    . VAL   B 119 ? 0.502  0.401  0.2421 0.0737  0.0497  0.0084  118 VAL   B C    
2760 O  O    . VAL   B 119 ? 0.515  0.3913 0.2397 0.0703  0.0463  0.0065  118 VAL   B O    
2761 C  CB   . VAL   B 119 ? 0.5312 0.4227 0.2495 0.0935  0.0639  0.0011  118 VAL   B CB   
2762 C  CG1  . VAL   B 119 ? 0.5371 0.4257 0.2603 0.1061  0.0624  0.0016  118 VAL   B CG1  
2763 C  CG2  . VAL   B 119 ? 0.5323 0.4361 0.2466 0.1008  0.0748  -0.0022 118 VAL   B CG2  
2764 N  N    . ASN   B 120 ? 0.4752 0.3906 0.234  0.0701  0.0464  0.0116  119 ASN   B N    
2765 C  CA   . ASN   B 120 ? 0.4693 0.3788 0.2333 0.0641  0.04    0.013   119 ASN   B CA   
2766 C  C    . ASN   B 120 ? 0.4887 0.3873 0.2467 0.0721  0.039   0.0123  119 ASN   B C    
2767 O  O    . ASN   B 120 ? 0.4813 0.3925 0.2493 0.0763  0.0381  0.014   119 ASN   B O    
2768 C  CB   . ASN   B 120 ? 0.4579 0.3862 0.2399 0.0581  0.0388  0.0154  119 ASN   B CB   
2769 C  CG   . ASN   B 120 ? 0.4799 0.4075 0.264  0.049   0.0375  0.0175  119 ASN   B CG   
2770 O  OD1  . ASN   B 120 ? 0.4708 0.4097 0.2625 0.0445  0.0398  0.0193  119 ASN   B OD1  
2771 N  ND2  . ASN   B 120 ? 0.4808 0.3948 0.2575 0.0456  0.0332  0.0177  119 ASN   B ND2  
2772 N  N    . ASN   B 121 ? 0.5027 0.3758 0.2415 0.0733  0.0388  0.0099  120 ASN   B N    
2773 C  CA   . ASN   B 121 ? 0.52   0.3738 0.2461 0.0806  0.0387  0.0098  120 ASN   B CA   
2774 C  C    . ASN   B 121 ? 0.5391 0.3778 0.2596 0.0699  0.034   0.0107  120 ASN   B C    
2775 O  O    . ASN   B 121 ? 0.543  0.3742 0.2595 0.0737  0.0329  0.0131  120 ASN   B O    
2776 C  CB   . ASN   B 121 ? 0.5562 0.3865 0.2603 0.0897  0.0435  0.0059  120 ASN   B CB   
2777 C  CG   . ASN   B 121 ? 0.6113 0.4095 0.2947 0.0961  0.0434  0.0057  120 ASN   B CG   
2778 O  OD1  . ASN   B 121 ? 0.6247 0.4219 0.3074 0.1119  0.0451  0.0079  120 ASN   B OD1  
2779 N  ND2  . ASN   B 121 ? 0.6278 0.3998 0.2938 0.0832  0.041   0.0037  120 ASN   B ND2  
2780 N  N    . ALA   B 122 ? 0.534  0.3707 0.2544 0.0564  0.0311  0.0092  121 ALA   B N    
2781 C  CA   . ALA   B 122 ? 0.5329 0.3612 0.2507 0.0448  0.0279  0.0094  121 ALA   B CA   
2782 C  C    . ALA   B 122 ? 0.5268 0.3656 0.2556 0.045   0.0274  0.0124  121 ALA   B C    
2783 O  O    . ALA   B 122 ? 0.5171 0.3781 0.2637 0.0476  0.0273  0.0137  121 ALA   B O    
2784 C  CB   . ALA   B 122 ? 0.5175 0.3563 0.2433 0.0327  0.0242  0.0082  121 ALA   B CB   
2785 N  N    . GLY   B 123 ? 0.5357 0.3555 0.2502 0.0418  0.0274  0.0134  122 GLY   B N    
2786 C  CA   . GLY   B 123 ? 0.534  0.3598 0.2528 0.0409  0.0271  0.0164  122 GLY   B CA   
2787 C  C    . GLY   B 123 ? 0.5533 0.3608 0.2576 0.0287  0.0275  0.0169  122 GLY   B C    
2788 O  O    . GLY   B 123 ? 0.5732 0.3573 0.2597 0.0222  0.028   0.0152  122 GLY   B O    
2789 N  N    . THR   B 124 ? 0.5416 0.3594 0.2519 0.0238  0.028   0.0186  123 THR   B N    
2790 C  CA   . THR   B 124 ? 0.5506 0.3568 0.2491 0.0105  0.03    0.0195  123 THR   B CA   
2791 C  C    . THR   B 124 ? 0.5584 0.3646 0.2508 0.0138  0.0302  0.0238  123 THR   B C    
2792 O  O    . THR   B 124 ? 0.557  0.382  0.2621 0.0227  0.0285  0.0244  123 THR   B O    
2793 C  CB   . THR   B 124 ? 0.5516 0.3797 0.2683 -0.0032 0.0315  0.0152  123 THR   B CB   
2794 O  OG1  . THR   B 124 ? 0.5765 0.3926 0.2798 -0.0189 0.0343  0.0153  123 THR   B OG1  
2795 C  CG2  . THR   B 124 ? 0.5375 0.394  0.2765 -0.0011 0.0328  0.0138  123 THR   B CG2  
2796 N  N    . VAL   B 125 ? 0.5649 0.3485 0.2351 0.0051  0.0321  0.027   124 VAL   B N    
2797 C  CA   . VAL   B 125 ? 0.5636 0.342  0.2209 0.0062  0.0319  0.0323  124 VAL   B CA   
2798 C  C    . VAL   B 125 ? 0.5948 0.3576 0.2344 -0.0123 0.0367  0.0335  124 VAL   B C    
2799 O  O    . VAL   B 125 ? 0.6091 0.3516 0.2361 -0.0226 0.0387  0.0325  124 VAL   B O    
2800 C  CB   . VAL   B 125 ? 0.5741 0.3303 0.2123 0.0238  0.0272  0.0392  124 VAL   B CB   
2801 C  CG1  . VAL   B 125 ? 0.5988 0.3126 0.2088 0.0238  0.0282  0.0416  124 VAL   B CG1  
2802 C  CG2  . VAL   B 125 ? 0.579  0.3356 0.2055 0.0268  0.0246  0.0456  124 VAL   B CG2  
2803 N  N    . TYR   B 126 ? 0.5998 0.3734 0.2378 -0.0186 0.0392  0.0347  125 TYR   B N    
2804 C  CA   . TYR   B 126 ? 0.6176 0.379  0.2373 -0.0372 0.0453  0.0363  125 TYR   B CA   
2805 C  C    . TYR   B 126 ? 0.6323 0.3821 0.2299 -0.0334 0.0436  0.0436  125 TYR   B C    
2806 O  O    . TYR   B 126 ? 0.6256 0.3977 0.231  -0.037  0.0461  0.0412  125 TYR   B O    
2807 C  CB   . TYR   B 126 ? 0.5989 0.3937 0.243  -0.0515 0.0524  0.0284  125 TYR   B CB   
2808 C  CG   . TYR   B 126 ? 0.5889 0.3993 0.2561 -0.0537 0.052   0.0224  125 TYR   B CG   
2809 C  CD1  . TYR   B 126 ? 0.6077 0.4048 0.2654 -0.0685 0.0537  0.0217  125 TYR   B CD1  
2810 C  CD2  . TYR   B 126 ? 0.5803 0.4155 0.2752 -0.0414 0.0487  0.0181  125 TYR   B CD2  
2811 C  CE1  . TYR   B 126 ? 0.6123 0.4232 0.2882 -0.0702 0.0511  0.0168  125 TYR   B CE1  
2812 C  CE2  . TYR   B 126 ? 0.5861 0.4334 0.2986 -0.0423 0.0468  0.0141  125 TYR   B CE2  
2813 C  CZ   . TYR   B 126 ? 0.6086 0.4455 0.3121 -0.0563 0.0475  0.0134  125 TYR   B CZ   
2814 O  OH   . TYR   B 126 ? 0.6203 0.4713 0.34   -0.0574 0.044   0.0097  125 TYR   B OH   
2815 N  N    . PRO   B 127 ? 0.6549 0.369  0.2235 -0.0241 0.0387  0.0524  126 PRO   B N    
2816 C  CA   . PRO   B 127 ? 0.6643 0.3671 0.2098 -0.0182 0.0347  0.0612  126 PRO   B CA   
2817 C  C    . PRO   B 127 ? 0.668  0.3681 0.1962 -0.0386 0.0418  0.0624  126 PRO   B C    
2818 O  O    . PRO   B 127 ? 0.6846 0.3695 0.2019 -0.0566 0.0492  0.0614  126 PRO   B O    
2819 C  CB   . PRO   B 127 ? 0.7    0.3577 0.2146 -0.0062 0.0299  0.0706  126 PRO   B CB   
2820 C  CG   . PRO   B 127 ? 0.699  0.3558 0.2299 0.0021  0.0294  0.0648  126 PRO   B CG   
2821 C  CD   . PRO   B 127 ? 0.6671 0.3473 0.2204 -0.0174 0.0364  0.0549  126 PRO   B CD   
2822 N  N    . ALA   B 128 ? 0.656  0.3754 0.184  -0.0378 0.0406  0.0631  127 ALA   B N    
2823 C  CA   . ALA   B 128 ? 0.6656 0.3853 0.1749 -0.0556 0.0478  0.064   127 ALA   B CA   
2824 C  C    . ALA   B 128 ? 0.6783 0.421  0.1901 -0.0491 0.0433  0.0633  127 ALA   B C    
2825 O  O    . ALA   B 128 ? 0.6779 0.4474 0.2175 -0.0371 0.0383  0.0576  127 ALA   B O    
2826 C  CB   . ALA   B 128 ? 0.646  0.3889 0.1763 -0.0745 0.0604  0.0532  127 ALA   B CB   
2827 N  N    . ASP   B 129 ? 0.7013 0.436  0.1845 -0.0603 0.0462  0.0677  128 ASP   B N    
2828 C  CA   . ASP   B 129 ? 0.7026 0.4617 0.187  -0.0586 0.0432  0.0645  128 ASP   B CA   
2829 C  C    . ASP   B 129 ? 0.6706 0.4645 0.1888 -0.0667 0.0538  0.0486  128 ASP   B C    
2830 O  O    . ASP   B 129 ? 0.6558 0.4538 0.1883 -0.0765 0.0641  0.0427  128 ASP   B O    
2831 C  CB   . ASP   B 129 ? 0.7621 0.5034 0.2046 -0.0701 0.0446  0.0725  128 ASP   B CB   
2832 C  CG   . ASP   B 129 ? 0.8795 0.6141 0.3102 -0.0936 0.0608  0.0689  128 ASP   B CG   
2833 O  OD1  . ASP   B 129 ? 0.9271 0.6358 0.3464 -0.1006 0.0646  0.0741  128 ASP   B OD1  
2834 O  OD2  . ASP   B 129 ? 0.9239 0.6802 0.3573 -0.1055 0.0704  0.06    128 ASP   B OD2  
2835 N  N    . LEU   B 130 ? 0.655  0.4734 0.1858 -0.0622 0.051   0.0417  129 LEU   B N    
2836 C  CA   . LEU   B 130 ? 0.6303 0.476  0.1907 -0.0665 0.0605  0.0269  129 LEU   B CA   
2837 C  C    . LEU   B 130 ? 0.6284 0.4788 0.1875 -0.0831 0.077   0.02    129 LEU   B C    
2838 O  O    . LEU   B 130 ? 0.6128 0.4786 0.2006 -0.0839 0.0848  0.012   129 LEU   B O    
2839 C  CB   . LEU   B 130 ? 0.6197 0.4824 0.181  -0.0638 0.0561  0.0208  129 LEU   B CB   
2840 C  CG   . LEU   B 130 ? 0.6065 0.4913 0.1985 -0.0634 0.0636  0.0061  129 LEU   B CG   
2841 C  CD1  . LEU   B 130 ? 0.5893 0.4806 0.2122 -0.0513 0.0587  0.0057  129 LEU   B CD1  
2842 C  CD2  . LEU   B 130 ? 0.6083 0.5033 0.1929 -0.0654 0.0606  -0.0005 129 LEU   B CD2  
2843 N  N    . LEU   B 131 ? 0.6439 0.4818 0.1691 -0.0961 0.0822  0.0242  130 LEU   B N    
2844 C  CA   . LEU   B 131 ? 0.6398 0.4863 0.1633 -0.1131 0.0996  0.0172  130 LEU   B CA   
2845 C  C    . LEU   B 131 ? 0.6427 0.4814 0.1705 -0.1227 0.1059  0.021   130 LEU   B C    
2846 O  O    . LEU   B 131 ? 0.633  0.4883 0.1701 -0.1361 0.1206  0.0136  130 LEU   B O    
2847 C  CB   . LEU   B 131 ? 0.6503 0.4884 0.1353 -0.1259 0.1048  0.0192  130 LEU   B CB   
2848 C  CG   . LEU   B 131 ? 0.6523 0.5056 0.1349 -0.1234 0.1048  0.0095  130 LEU   B CG   
2849 C  CD1  . LEU   B 131 ? 0.6596 0.5077 0.1058 -0.1394 0.1145  0.0086  130 LEU   B CD1  
2850 C  CD2  . LEU   B 131 ? 0.6346 0.5148 0.1578 -0.1165 0.1125  -0.0068 130 LEU   B CD2  
2851 N  N    . SER   B 132 ? 0.6512 0.4675 0.1751 -0.1157 0.0952  0.0308  131 SER   B N    
2852 C  CA   . SER   B 132 ? 0.6514 0.4567 0.178  -0.1252 0.099   0.0336  131 SER   B CA   
2853 C  C    . SER   B 132 ? 0.6385 0.4612 0.2045 -0.115  0.0956  0.0274  131 SER   B C    
2854 O  O    . SER   B 132 ? 0.6508 0.4694 0.2224 -0.124  0.0984  0.0278  131 SER   B O    
2855 C  CB   . SER   B 132 ? 0.6887 0.4494 0.1768 -0.1261 0.091   0.0484  131 SER   B CB   
2856 O  OG   . SER   B 132 ? 0.7517 0.4953 0.2007 -0.1391 0.0958  0.0551  131 SER   B OG   
2857 N  N    . THR   B 133 ? 0.608  0.4486 0.1987 -0.098  0.0892  0.022   132 THR   B N    
2858 C  CA   . THR   B 133 ? 0.577  0.4338 0.2026 -0.0883 0.086   0.0166  132 THR   B CA   
2859 C  C    . THR   B 133 ? 0.5564 0.4447 0.2095 -0.097  0.0981  0.0061  132 THR   B C    
2860 O  O    . THR   B 133 ? 0.5599 0.4634 0.2123 -0.1036 0.1084  0.0001  132 THR   B O    
2861 C  CB   . THR   B 133 ? 0.5584 0.4257 0.2003 -0.0702 0.0775  0.0137  132 THR   B CB   
2862 O  OG1  . THR   B 133 ? 0.569  0.4496 0.2081 -0.0723 0.0827  0.0075  132 THR   B OG1  
2863 C  CG2  . THR   B 133 ? 0.5582 0.4042 0.1835 -0.0584 0.0647  0.0232  132 THR   B CG2  
2864 N  N    . LYS   B 134 ? 0.5378 0.4375 0.2151 -0.0954 0.0967  0.0038  133 LYS   B N    
2865 C  CA   . LYS   B 134 ? 0.5149 0.4494 0.2246 -0.0986 0.1051  -0.0054 133 LYS   B CA   
2866 C  C    . LYS   B 134 ? 0.4827 0.4318 0.2196 -0.0792 0.0999  -0.0107 133 LYS   B C    
2867 O  O    . LYS   B 134 ? 0.4845 0.4194 0.2208 -0.0683 0.0889  -0.0064 133 LYS   B O    
2868 C  CB   . LYS   B 134 ? 0.5542 0.4914 0.2716 -0.1092 0.1039  -0.0034 133 LYS   B CB   
2869 C  CG   . LYS   B 134 ? 0.6403 0.5602 0.3289 -0.1314 0.1101  0.0016  133 LYS   B CG   
2870 C  CD   . LYS   B 134 ? 0.7206 0.625  0.4028 -0.1427 0.1051  0.0057  133 LYS   B CD   
2871 C  CE   . LYS   B 134 ? 0.8061 0.6704 0.4448 -0.1598 0.1074  0.0142  133 LYS   B CE   
2872 N  NZ   . LYS   B 134 ? 0.8454 0.7197 0.4717 -0.1771 0.1211  0.0132  133 LYS   B NZ   
2873 N  N    . ASP   B 135 ? 0.4556 0.4302 0.2136 -0.0749 0.1084  -0.0199 134 ASP   B N    
2874 C  CA   . ASP   B 135 ? 0.4479 0.43   0.2267 -0.0578 0.1044  -0.0246 134 ASP   B CA   
2875 C  C    . ASP   B 135 ? 0.4527 0.4385 0.2518 -0.0493 0.0946  -0.0215 134 ASP   B C    
2876 O  O    . ASP   B 135 ? 0.4585 0.4363 0.2621 -0.0371 0.087   -0.0205 134 ASP   B O    
2877 C  CB   . ASP   B 135 ? 0.4419 0.4472 0.2387 -0.054  0.1167  -0.0353 134 ASP   B CB   
2878 C  CG   . ASP   B 135 ? 0.5222 0.5205 0.2964 -0.0598 0.1257  -0.0401 134 ASP   B CG   
2879 O  OD1  . ASP   B 135 ? 0.5392 0.5148 0.2855 -0.0636 0.1194  -0.0345 134 ASP   B OD1  
2880 O  OD2  . ASP   B 135 ? 0.5388 0.5554 0.3229 -0.0597 0.139   -0.0495 134 ASP   B OD2  
2881 N  N    . GLU   B 136 ? 0.4468 0.4442 0.255  -0.058  0.0948  -0.0198 135 GLU   B N    
2882 C  CA   . GLU   B 136 ? 0.4512 0.4531 0.2746 -0.0536 0.0855  -0.017  135 GLU   B CA   
2883 C  C    . GLU   B 136 ? 0.4722 0.443  0.2746 -0.0508 0.0751  -0.0099 135 GLU   B C    
2884 O  O    . GLU   B 136 ? 0.4735 0.4423 0.2848 -0.0412 0.0671  -0.0083 135 GLU   B O    
2885 C  CB   . GLU   B 136 ? 0.4855 0.507  0.3183 -0.0685 0.0882  -0.0174 135 GLU   B CB   
2886 C  CG   . GLU   B 136 ? 0.5912 0.6481 0.4442 -0.0736 0.1007  -0.0244 135 GLU   B CG   
2887 C  CD   . GLU   B 136 ? 0.7152 0.7684 0.5488 -0.0868 0.1131  -0.0264 135 GLU   B CD   
2888 O  OE1  . GLU   B 136 ? 0.7476 0.7789 0.5539 -0.103  0.113   -0.0209 135 GLU   B OE1  
2889 O  OE2  . GLU   B 136 ? 0.7159 0.7854 0.559  -0.081  0.1235  -0.0333 135 GLU   B OE2  
2890 N  N    . GLU   B 137 ? 0.4913 0.4378 0.2648 -0.0584 0.0755  -0.0053 136 GLU   B N    
2891 C  CA   . GLU   B 137 ? 0.5102 0.4272 0.263  -0.0529 0.0667  0.0015  136 GLU   B CA   
2892 C  C    . GLU   B 137 ? 0.4926 0.4081 0.249  -0.0375 0.062   0.0015  136 GLU   B C    
2893 O  O    . GLU   B 137 ? 0.4893 0.3954 0.2456 -0.028  0.0546  0.0045  136 GLU   B O    
2894 C  CB   . GLU   B 137 ? 0.5581 0.4487 0.2778 -0.0634 0.0686  0.0074  136 GLU   B CB   
2895 C  CG   . GLU   B 137 ? 0.6449 0.53   0.3561 -0.0814 0.0724  0.0083  136 GLU   B CG   
2896 C  CD   . GLU   B 137 ? 0.7364 0.5931 0.4121 -0.0942 0.0762  0.0144  136 GLU   B CD   
2897 O  OE1  . GLU   B 137 ? 0.6945 0.5481 0.3579 -0.0921 0.0789  0.0161  136 GLU   B OE1  
2898 O  OE2  . GLU   B 137 ? 0.8154 0.6503 0.4728 -0.1074 0.0763  0.0177  136 GLU   B OE2  
2899 N  N    . ILE   B 138 ? 0.478  0.4034 0.2368 -0.0363 0.0671  -0.0027 137 ILE   B N    
2900 C  CA   . ILE   B 138 ? 0.4712 0.397  0.2331 -0.0255 0.0632  -0.0041 137 ILE   B CA   
2901 C  C    . ILE   B 138 ? 0.4714 0.4083 0.2576 -0.0161 0.0605  -0.0069 137 ILE   B C    
2902 O  O    . ILE   B 138 ? 0.4618 0.3934 0.249  -0.0081 0.054   -0.0045 137 ILE   B O    
2903 C  CB   . ILE   B 138 ? 0.4542 0.3863 0.2108 -0.0292 0.0703  -0.0097 137 ILE   B CB   
2904 C  CG1  . ILE   B 138 ? 0.4764 0.3952 0.2042 -0.0387 0.0717  -0.0052 137 ILE   B CG1  
2905 C  CG2  . ILE   B 138 ? 0.4505 0.3835 0.2106 -0.0213 0.0664  -0.0124 137 ILE   B CG2  
2906 C  CD1  . ILE   B 138 ? 0.4808 0.406  0.1992 -0.0454 0.0804  -0.0115 137 ILE   B CD1  
2907 N  N    . THR   B 139 ? 0.4694 0.4228 0.2746 -0.017  0.0655  -0.0115 138 THR   B N    
2908 C  CA   . THR   B 139 ? 0.469  0.4323 0.2955 -0.0078 0.0629  -0.0131 138 THR   B CA   
2909 C  C    . THR   B 139 ? 0.4841 0.4398 0.3094 -0.0055 0.0541  -0.0073 138 THR   B C    
2910 O  O    . THR   B 139 ? 0.4825 0.434  0.3117 0.0028  0.0493  -0.0057 138 THR   B O    
2911 C  CB   . THR   B 139 ? 0.4763 0.4618 0.3225 -0.0088 0.0697  -0.0181 138 THR   B CB   
2912 O  OG1  . THR   B 139 ? 0.4782 0.4677 0.3256 -0.0068 0.0785  -0.0249 138 THR   B OG1  
2913 C  CG2  . THR   B 139 ? 0.4792 0.476  0.3467 0.0009  0.0648  -0.0173 138 THR   B CG2  
2914 N  N    . LYS   B 140 ? 0.4917 0.4434 0.3086 -0.0142 0.0528  -0.0045 139 LYS   B N    
2915 C  CA   . LYS   B 140 ? 0.4977 0.4385 0.3088 -0.0132 0.0456  -0.0004 139 LYS   B CA   
2916 C  C    . LYS   B 140 ? 0.4866 0.4084 0.2826 -0.0058 0.0414  0.0034  139 LYS   B C    
2917 O  O    . LYS   B 140 ? 0.4996 0.418  0.2978 0.0009  0.0366  0.005   139 LYS   B O    
2918 C  CB   . LYS   B 140 ? 0.5685 0.5034 0.3683 -0.0266 0.0462  0.0007  139 LYS   B CB   
2919 C  CG   . LYS   B 140 ? 0.682  0.6387 0.5001 -0.0322 0.0448  -0.0016 139 LYS   B CG   
2920 C  CD   . LYS   B 140 ? 0.8102 0.7718 0.6227 -0.0502 0.0491  -0.0027 139 LYS   B CD   
2921 C  CE   . LYS   B 140 ? 0.9201 0.8584 0.711  -0.0607 0.0443  -0.0002 139 LYS   B CE   
2922 N  NZ   . LYS   B 140 ? 0.9683 0.9012 0.745  -0.0815 0.0498  -0.0006 139 LYS   B NZ   
2923 N  N    . THR   B 141 ? 0.4686 0.3807 0.2499 -0.0064 0.043   0.0049  140 THR   B N    
2924 C  CA   . THR   B 141 ? 0.4667 0.3673 0.2368 0.0022  0.0386  0.0087  140 THR   B CA   
2925 C  C    . THR   B 141 ? 0.456  0.3683 0.2411 0.0102  0.0367  0.0069  140 THR   B C    
2926 O  O    . THR   B 141 ? 0.4747 0.3838 0.2597 0.0169  0.0331  0.0092  140 THR   B O    
2927 C  CB   . THR   B 141 ? 0.4925 0.3858 0.2458 0       0.0396  0.011   140 THR   B CB   
2928 O  OG1  . THR   B 141 ? 0.502  0.3809 0.2384 -0.0096 0.0423  0.0133  140 THR   B OG1  
2929 C  CG2  . THR   B 141 ? 0.5065 0.3933 0.2505 0.0104  0.0338  0.0156  140 THR   B CG2  
2930 N  N    . PHE   B 142 ? 0.4287 0.3532 0.2259 0.0088  0.0403  0.0024  141 PHE   B N    
2931 C  CA   . PHE   B 142 ? 0.4154 0.3459 0.2236 0.014   0.0394  0.0007  141 PHE   B CA   
2932 C  C    . PHE   B 142 ? 0.4026 0.3348 0.2217 0.0181  0.0372  0.0018  141 PHE   B C    
2933 O  O    . PHE   B 142 ? 0.4023 0.3335 0.2227 0.0222  0.0346  0.0037  141 PHE   B O    
2934 C  CB   . PHE   B 142 ? 0.4116 0.3475 0.2248 0.0115  0.0446  -0.0052 141 PHE   B CB   
2935 C  CG   . PHE   B 142 ? 0.4315 0.3663 0.2324 0.0085  0.0437  -0.0057 141 PHE   B CG   
2936 C  CD1  . PHE   B 142 ? 0.4488 0.3809 0.2355 0.0036  0.0449  -0.0049 141 PHE   B CD1  
2937 C  CD2  . PHE   B 142 ? 0.4386 0.3762 0.2404 0.0098  0.0405  -0.0058 141 PHE   B CD2  
2938 C  CE1  . PHE   B 142 ? 0.4729 0.4055 0.2467 0.0015  0.0421  -0.0041 141 PHE   B CE1  
2939 C  CE2  . PHE   B 142 ? 0.4556 0.3971 0.2472 0.0066  0.0378  -0.0058 141 PHE   B CE2  
2940 C  CZ   . PHE   B 142 ? 0.4708 0.41   0.2483 0.0032  0.0379  -0.0048 141 PHE   B CZ   
2941 N  N    . GLU   B 143 ? 0.3881 0.3254 0.2149 0.016   0.0381  0.0008  142 GLU   B N    
2942 C  CA   . GLU   B 143 ? 0.3869 0.3278 0.2228 0.0195  0.0346  0.0025  142 GLU   B CA   
2943 C  C    . GLU   B 143 ? 0.4129 0.3445 0.2383 0.0207  0.0298  0.0064  142 GLU   B C    
2944 O  O    . GLU   B 143 ? 0.4233 0.3542 0.2512 0.0251  0.0272  0.0084  142 GLU   B O    
2945 C  CB   . GLU   B 143 ? 0.3906 0.3441 0.237  0.0158  0.0354  0.0009  142 GLU   B CB   
2946 C  CG   . GLU   B 143 ? 0.4153 0.3808 0.277  0.0197  0.0404  -0.0032 142 GLU   B CG   
2947 C  CD   . GLU   B 143 ? 0.4738 0.4594 0.3496 0.0165  0.0428  -0.0055 142 GLU   B CD   
2948 O  OE1  . GLU   B 143 ? 0.4743 0.4634 0.345  0.0068  0.0413  -0.0045 142 GLU   B OE1  
2949 O  OE2  . GLU   B 143 ? 0.5078 0.5057 0.3994 0.0234  0.0467  -0.0088 142 GLU   B OE2  
2950 N  N    . ILE   B 144 ? 0.4187 0.3405 0.23   0.0172  0.0294  0.0074  143 ILE   B N    
2951 C  CA   . ILE   B 144 ? 0.4307 0.3404 0.2296 0.02    0.0264  0.0097  143 ILE   B CA   
2952 C  C    . ILE   B 144 ? 0.4352 0.3415 0.2288 0.0275  0.0269  0.0114  143 ILE   B C    
2953 O  O    . ILE   B 144 ? 0.4432 0.3485 0.2353 0.0322  0.0259  0.0125  143 ILE   B O    
2954 C  CB   . ILE   B 144 ? 0.4514 0.3466 0.2344 0.0133  0.0262  0.0097  143 ILE   B CB   
2955 C  CG1  . ILE   B 144 ? 0.4579 0.3634 0.249  0.0033  0.0255  0.0077  143 ILE   B CG1  
2956 C  CG2  . ILE   B 144 ? 0.4645 0.3421 0.2311 0.0174  0.0244  0.0108  143 ILE   B CG2  
2957 C  CD1  . ILE   B 144 ? 0.4779 0.3707 0.254  -0.0076 0.0266  0.0073  143 ILE   B CD1  
2958 N  N    . ASN   B 145 ? 0.427  0.3338 0.2173 0.0283  0.0282  0.0117  144 ASN   B N    
2959 C  CA   . ASN   B 145 ? 0.4188 0.3276 0.2055 0.0357  0.0273  0.0137  144 ASN   B CA   
2960 C  C    . ASN   B 145 ? 0.4084 0.3325 0.2075 0.0369  0.0278  0.0128  144 ASN   B C    
2961 O  O    . ASN   B 145 ? 0.403  0.3342 0.2021 0.0425  0.0271  0.0143  144 ASN   B O    
2962 C  CB   . ASN   B 145 ? 0.4369 0.3415 0.2133 0.0365  0.0267  0.0155  144 ASN   B CB   
2963 C  CG   . ASN   B 145 ? 0.4884 0.3716 0.2464 0.0357  0.0265  0.0178  144 ASN   B CG   
2964 O  OD1  . ASN   B 145 ? 0.5249 0.4005 0.2706 0.036   0.0257  0.0207  144 ASN   B OD1  
2965 N  ND2  . ASN   B 145 ? 0.4934 0.3642 0.2459 0.0333  0.027   0.0169  144 ASN   B ND2  
2966 N  N    . ILE   B 146 ? 0.4087 0.3378 0.218  0.0317  0.0292  0.0103  145 ILE   B N    
2967 C  CA   . ILE   B 146 ? 0.4127 0.3503 0.2296 0.0305  0.0302  0.0096  145 ILE   B CA   
2968 C  C    . ILE   B 146 ? 0.4156 0.3492 0.2395 0.0287  0.0313  0.009   145 ILE   B C    
2969 O  O    . ILE   B 146 ? 0.421  0.3546 0.2456 0.0291  0.0315  0.0111  145 ILE   B O    
2970 C  CB   . ILE   B 146 ? 0.4019 0.3476 0.2194 0.0264  0.0306  0.0071  145 ILE   B CB   
2971 C  CG1  . ILE   B 146 ? 0.4015 0.3537 0.2248 0.0216  0.0319  0.0058  145 ILE   B CG1  
2972 C  CG2  . ILE   B 146 ? 0.4011 0.3423 0.2168 0.0221  0.0326  0.0036  145 ILE   B CG2  
2973 C  CD1  . ILE   B 146 ? 0.3986 0.3604 0.2241 0.024   0.0314  0.0088  145 ILE   B CD1  
2974 N  N    . LEU   B 147 ? 0.4089 0.3396 0.2372 0.0277  0.0323  0.0069  146 LEU   B N    
2975 C  CA   . LEU   B 147 ? 0.4019 0.3291 0.2372 0.0296  0.0325  0.0073  146 LEU   B CA   
2976 C  C    . LEU   B 147 ? 0.4164 0.3415 0.2496 0.0324  0.0287  0.0119  146 LEU   B C    
2977 O  O    . LEU   B 147 ? 0.4271 0.347  0.2598 0.0335  0.0283  0.0147  146 LEU   B O    
2978 C  CB   . LEU   B 147 ? 0.3887 0.3187 0.232  0.0305  0.0346  0.004   146 LEU   B CB   
2979 C  CG   . LEU   B 147 ? 0.3814 0.3103 0.2242 0.0276  0.0399  -0.0017 146 LEU   B CG   
2980 C  CD1  . LEU   B 147 ? 0.3752 0.3107 0.2249 0.0282  0.0438  -0.0058 146 LEU   B CD1  
2981 C  CD2  . LEU   B 147 ? 0.3863 0.3052 0.2286 0.0278  0.0421  -0.0032 146 LEU   B CD2  
2982 N  N    . GLY   B 148 ? 0.4141 0.3401 0.2419 0.0322  0.0264  0.0127  147 GLY   B N    
2983 C  CA   . GLY   B 148 ? 0.4169 0.3396 0.2384 0.0333  0.0228  0.0158  147 GLY   B CA   
2984 C  C    . GLY   B 148 ? 0.4226 0.3426 0.2371 0.0346  0.0242  0.018   147 GLY   B C    
2985 O  O    . GLY   B 148 ? 0.4222 0.3389 0.2323 0.0351  0.0224  0.0212  147 GLY   B O    
2986 N  N    . HIS   B 149 ? 0.4254 0.3494 0.2395 0.0347  0.0276  0.0167  148 HIS   B N    
2987 C  CA   . HIS   B 149 ? 0.4258 0.354  0.2368 0.035   0.0303  0.0182  148 HIS   B CA   
2988 C  C    . HIS   B 149 ? 0.4472 0.3725 0.2607 0.0308  0.0314  0.0206  148 HIS   B C    
2989 O  O    . HIS   B 149 ? 0.4668 0.39   0.274  0.0296  0.0326  0.0237  148 HIS   B O    
2990 C  CB   . HIS   B 149 ? 0.4151 0.3547 0.2293 0.0359  0.0324  0.0165  148 HIS   B CB   
2991 C  CG   . HIS   B 149 ? 0.4394 0.3776 0.2474 0.0424  0.0316  0.0158  148 HIS   B CG   
2992 N  ND1  . HIS   B 149 ? 0.4525 0.4024 0.2614 0.048   0.0328  0.016   148 HIS   B ND1  
2993 C  CD2  . HIS   B 149 ? 0.4522 0.3776 0.2522 0.044   0.0296  0.0153  148 HIS   B CD2  
2994 C  CE1  . HIS   B 149 ? 0.4525 0.3919 0.2519 0.0547  0.0316  0.0161  148 HIS   B CE1  
2995 N  NE2  . HIS   B 149 ? 0.4621 0.3851 0.2547 0.0509  0.03    0.0155  148 HIS   B NE2  
2996 N  N    . PHE   B 150 ? 0.4467 0.3685 0.2666 0.0286  0.0315  0.0191  149 PHE   B N    
2997 C  CA   . PHE   B 150 ? 0.4509 0.3624 0.2698 0.0254  0.0328  0.0212  149 PHE   B CA   
2998 C  C    . PHE   B 150 ? 0.4608 0.3627 0.275  0.0295  0.029   0.0265  149 PHE   B C    
2999 O  O    . PHE   B 150 ? 0.4746 0.3679 0.2805 0.0268  0.03    0.0311  149 PHE   B O    
3000 C  CB   . PHE   B 150 ? 0.4463 0.3518 0.2708 0.0245  0.0343  0.0171  149 PHE   B CB   
3001 C  CG   . PHE   B 150 ? 0.447  0.3586 0.2719 0.0171  0.0375  0.0125  149 PHE   B CG   
3002 C  CD1  . PHE   B 150 ? 0.4569 0.362  0.2772 0.0083  0.0406  0.0124  149 PHE   B CD1  
3003 C  CD2  . PHE   B 150 ? 0.442  0.3648 0.2699 0.0173  0.037   0.0086  149 PHE   B CD2  
3004 C  CE1  . PHE   B 150 ? 0.4537 0.3673 0.2742 -0.0008 0.0424  0.0075  149 PHE   B CE1  
3005 C  CE2  . PHE   B 150 ? 0.438  0.3687 0.2652 0.0102  0.0383  0.0048  149 PHE   B CE2  
3006 C  CZ   . PHE   B 150 ? 0.4386 0.3664 0.2631 0.0008  0.0406  0.0038  149 PHE   B CZ   
3007 N  N    . TRP   B 151 ? 0.4467 0.3511 0.2652 0.0349  0.0245  0.0264  150 TRP   B N    
3008 C  CA   . TRP   B 151 ? 0.4435 0.3429 0.2583 0.0388  0.0189  0.0319  150 TRP   B CA   
3009 C  C    . TRP   B 151 ? 0.4526 0.3511 0.2536 0.0364  0.0176  0.0353  150 TRP   B C    
3010 O  O    . TRP   B 151 ? 0.4787 0.368  0.2702 0.0365  0.0155  0.0413  150 TRP   B O    
3011 C  CB   . TRP   B 151 ? 0.4234 0.3322 0.2486 0.0435  0.0137  0.0307  150 TRP   B CB   
3012 C  CG   . TRP   B 151 ? 0.3967 0.3118 0.2349 0.0446  0.0173  0.025   150 TRP   B CG   
3013 C  CD1  . TRP   B 151 ? 0.391  0.318  0.2354 0.0425  0.0172  0.0208  150 TRP   B CD1  
3014 C  CD2  . TRP   B 151 ? 0.3893 0.2972 0.2329 0.047   0.022   0.0225  150 TRP   B CD2  
3015 N  NE1  . TRP   B 151 ? 0.3831 0.313  0.2368 0.0436  0.0221  0.0161  150 TRP   B NE1  
3016 C  CE2  . TRP   B 151 ? 0.3835 0.3015 0.2366 0.0466  0.0251  0.0164  150 TRP   B CE2  
3017 C  CE3  . TRP   B 151 ? 0.3988 0.2895 0.2369 0.0478  0.0247  0.0244  150 TRP   B CE3  
3018 C  CZ2  . TRP   B 151 ? 0.3828 0.2958 0.2402 0.0481  0.0311  0.0113  150 TRP   B CZ2  
3019 C  CZ3  . TRP   B 151 ? 0.4078 0.2908 0.2496 0.0487  0.0302  0.0192  150 TRP   B CZ3  
3020 C  CH2  . TRP   B 151 ? 0.3951 0.2898 0.2466 0.0496  0.0334  0.0123  150 TRP   B CH2  
3021 N  N    . ILE   B 152 ? 0.4346 0.3397 0.2318 0.0347  0.0195  0.0315  151 ILE   B N    
3022 C  CA   . ILE   B 152 ? 0.4395 0.3425 0.222  0.0334  0.0202  0.0328  151 ILE   B CA   
3023 C  C    . ILE   B 152 ? 0.4586 0.3601 0.235  0.0299  0.0263  0.0354  151 ILE   B C    
3024 O  O    . ILE   B 152 ? 0.455  0.3501 0.218  0.0278  0.0259  0.0399  151 ILE   B O    
3025 C  CB   . ILE   B 152 ? 0.4386 0.3439 0.2158 0.0345  0.0216  0.0277  151 ILE   B CB   
3026 C  CG1  . ILE   B 152 ? 0.4494 0.3553 0.2316 0.0342  0.0164  0.0252  151 ILE   B CG1  
3027 C  CG2  . ILE   B 152 ? 0.4565 0.3561 0.2152 0.0338  0.0225  0.0281  151 ILE   B CG2  
3028 C  CD1  . ILE   B 152 ? 0.4613 0.3631 0.2369 0.0342  0.0181  0.0204  151 ILE   B CD1  
3029 N  N    . THR   B 153 ? 0.4666 0.3749 0.2518 0.0275  0.0315  0.0329  152 THR   B N    
3030 C  CA   . THR   B 153 ? 0.4757 0.387  0.2572 0.021   0.0379  0.0348  152 THR   B CA   
3031 C  C    . THR   B 153 ? 0.4906 0.3851 0.2644 0.0164  0.0368  0.0411  152 THR   B C    
3032 O  O    . THR   B 153 ? 0.5164 0.4065 0.2772 0.0115  0.0399  0.0455  152 THR   B O    
3033 C  CB   . THR   B 153 ? 0.4808 0.4071 0.2744 0.0181  0.0421  0.0303  152 THR   B CB   
3034 O  OG1  . THR   B 153 ? 0.4831 0.4212 0.2807 0.0252  0.0421  0.0262  152 THR   B OG1  
3035 C  CG2  . THR   B 153 ? 0.4849 0.4207 0.2768 0.009   0.049   0.0316  152 THR   B CG2  
3036 N  N    . LYS   B 154 ? 0.481  0.3643 0.2605 0.0191  0.0328  0.0419  153 LYS   B N    
3037 C  CA   . LYS   B 154 ? 0.4854 0.3473 0.2553 0.0177  0.0315  0.0488  153 LYS   B CA   
3038 C  C    . LYS   B 154 ? 0.493  0.3464 0.2483 0.0212  0.0259  0.0564  153 LYS   B C    
3039 O  O    . LYS   B 154 ? 0.5058 0.3409 0.2465 0.0184  0.0258  0.0641  153 LYS   B O    
3040 C  CB   . LYS   B 154 ? 0.487  0.3384 0.2664 0.0236  0.0289  0.0472  153 LYS   B CB   
3041 C  CG   . LYS   B 154 ? 0.5182 0.3713 0.3048 0.0171  0.0347  0.0403  153 LYS   B CG   
3042 C  CD   . LYS   B 154 ? 0.5747 0.4023 0.3565 0.0167  0.0365  0.0411  153 LYS   B CD   
3043 C  CE   . LYS   B 154 ? 0.6015 0.4203 0.3892 0.0311  0.0314  0.0426  153 LYS   B CE   
3044 N  NZ   . LYS   B 154 ? 0.6243 0.4157 0.4067 0.033   0.0348  0.0417  153 LYS   B NZ   
3045 N  N    . ALA   B 155 ? 0.4924 0.3571 0.2492 0.0264  0.0208  0.0547  154 ALA   B N    
3046 C  CA   . ALA   B 155 ? 0.503  0.3625 0.2447 0.0284  0.014   0.061   154 ALA   B CA   
3047 C  C    . ALA   B 155 ? 0.5374 0.3973 0.2608 0.0212  0.0198  0.062   154 ALA   B C    
3048 O  O    . ALA   B 155 ? 0.5752 0.4241 0.2794 0.0192  0.017   0.0694  154 ALA   B O    
3049 C  CB   . ALA   B 155 ? 0.48   0.3516 0.2291 0.0338  0.0063  0.0575  154 ALA   B CB   
3050 N  N    . LEU   B 156 ? 0.5304 0.4036 0.2587 0.0183  0.028   0.0548  155 LEU   B N    
3051 C  CA   . LEU   B 156 ? 0.5426 0.4203 0.2558 0.0137  0.0352  0.054   155 LEU   B CA   
3052 C  C    . LEU   B 156 ? 0.5511 0.4321 0.2624 0.0046  0.0454  0.0557  155 LEU   B C    
3053 O  O    . LEU   B 156 ? 0.5564 0.437  0.2508 -0.0012 0.0514  0.0582  155 LEU   B O    
3054 C  CB   . LEU   B 156 ? 0.5298 0.4202 0.2473 0.0186  0.0378  0.0451  155 LEU   B CB   
3055 C  CG   . LEU   B 156 ? 0.5319 0.4182 0.2486 0.0236  0.0286  0.0427  155 LEU   B CG   
3056 C  CD1  . LEU   B 156 ? 0.5373 0.4284 0.2533 0.0276  0.0326  0.0344  155 LEU   B CD1  
3057 C  CD2  . LEU   B 156 ? 0.5479 0.4238 0.2443 0.0213  0.0211  0.0482  155 LEU   B CD2  
3058 N  N    . LEU   B 157 ? 0.5433 0.4286 0.2705 0.0016  0.048   0.0538  156 LEU   B N    
3059 C  CA   . LEU   B 157 ? 0.5511 0.4422 0.278  -0.0104 0.0573  0.0547  156 LEU   B CA   
3060 C  C    . LEU   B 157 ? 0.5748 0.4443 0.2789 -0.0205 0.0594  0.0642  156 LEU   B C    
3061 O  O    . LEU   B 157 ? 0.5831 0.4617 0.28   -0.0315 0.0691  0.065   156 LEU   B O    
3062 C  CB   . LEU   B 157 ? 0.5463 0.4422 0.2911 -0.0137 0.0576  0.0507  156 LEU   B CB   
3063 C  CG   . LEU   B 157 ? 0.5575 0.4694 0.307  -0.0277 0.0668  0.0488  156 LEU   B CG   
3064 C  CD1  . LEU   B 157 ? 0.5504 0.4953 0.3092 -0.0253 0.0732  0.0437  156 LEU   B CD1  
3065 C  CD2  . LEU   B 157 ? 0.5593 0.471  0.3216 -0.0328 0.0653  0.0447  156 LEU   B CD2  
3066 N  N    . PRO   B 158 ? 0.5855 0.4277 0.2774 -0.0168 0.051   0.0721  157 PRO   B N    
3067 C  CA   . PRO   B 158 ? 0.6103 0.428  0.277  -0.0261 0.053   0.0826  157 PRO   B CA   
3068 C  C    . PRO   B 158 ? 0.628  0.4503 0.2733 -0.0331 0.059   0.086   157 PRO   B C    
3069 O  O    . PRO   B 158 ? 0.6466 0.4583 0.2746 -0.0471 0.0668  0.092   157 PRO   B O    
3070 C  CB   . PRO   B 158 ? 0.6254 0.4186 0.2855 -0.0144 0.0404  0.0901  157 PRO   B CB   
3071 C  CG   . PRO   B 158 ? 0.6093 0.4119 0.2955 -0.0044 0.0359  0.0824  157 PRO   B CG   
3072 C  CD   . PRO   B 158 ? 0.5746 0.4078 0.2753 -0.0039 0.0398  0.0725  157 PRO   B CD   
3073 N  N    . SER   B 159 ? 0.6314 0.4661 0.2741 -0.0248 0.056   0.0825  158 SER   B N    
3074 C  CA   . SER   B 159 ? 0.6496 0.4867 0.2681 -0.0311 0.0626  0.0846  158 SER   B CA   
3075 C  C    . SER   B 159 ? 0.6327 0.4973 0.2601 -0.0389 0.0782  0.0769  158 SER   B C    
3076 O  O    . SER   B 159 ? 0.6365 0.5031 0.2452 -0.0497 0.0884  0.0798  158 SER   B O    
3077 C  CB   . SER   B 159 ? 0.6839 0.5218 0.2929 -0.0213 0.0544  0.0822  158 SER   B CB   
3078 O  OG   . SER   B 159 ? 0.7356 0.5897 0.3368 -0.0224 0.0642  0.0745  158 SER   B OG   
3079 N  N    . MET   B 160 ? 0.6091 0.4965 0.2649 -0.0326 0.0799  0.0673  159 MET   B N    
3080 C  CA   . MET   B 160 ? 0.5907 0.5104 0.2627 -0.036  0.0923  0.0597  159 MET   B CA   
3081 C  C    . MET   B 160 ? 0.5956 0.5175 0.2673 -0.0544 0.1003  0.0642  159 MET   B C    
3082 O  O    . MET   B 160 ? 0.585  0.5282 0.2545 -0.0642 0.1131  0.0628  159 MET   B O    
3083 C  CB   . MET   B 160 ? 0.5677 0.5055 0.2687 -0.0246 0.0884  0.0513  159 MET   B CB   
3084 C  CG   . MET   B 160 ? 0.5732 0.5093 0.2742 -0.009  0.0827  0.0458  159 MET   B CG   
3085 S  SD   . MET   B 160 ? 0.6069 0.5609 0.3378 0.0017  0.079   0.0382  159 MET   B SD   
3086 C  CE   . MET   B 160 ? 0.558  0.5002 0.2802 0.0164  0.073   0.0331  159 MET   B CE   
3087 N  N    . ILE   B 161 ? 0.6055 0.5049 0.2782 -0.0597 0.0936  0.0691  160 ILE   B N    
3088 C  CA   . ILE   B 161 ? 0.6137 0.5065 0.2816 -0.0793 0.1003  0.0733  160 ILE   B CA   
3089 C  C    . ILE   B 161 ? 0.6418 0.5152 0.2777 -0.0922 0.1065  0.0829  160 ILE   B C    
3090 O  O    . ILE   B 161 ? 0.6412 0.5304 0.2735 -0.1097 0.1192  0.0831  160 ILE   B O    
3091 C  CB   . ILE   B 161 ? 0.6199 0.485  0.2914 -0.0795 0.0915  0.0754  160 ILE   B CB   
3092 C  CG1  . ILE   B 161 ? 0.6095 0.4983 0.3112 -0.0722 0.0883  0.0653  160 ILE   B CG1  
3093 C  CG2  . ILE   B 161 ? 0.6356 0.4783 0.2908 -0.1011 0.0978  0.0815  160 ILE   B CG2  
3094 C  CD1  . ILE   B 161 ? 0.6226 0.4857 0.3277 -0.0703 0.0807  0.0653  160 ILE   B CD1  
3095 N  N    . LYS   B 162 ? 0.6678 0.5097 0.2803 -0.0838 0.0975  0.0911  161 LYS   B N    
3096 C  CA   . LYS   B 162 ? 0.7001 0.5183 0.2765 -0.0936 0.1007  0.1022  161 LYS   B CA   
3097 C  C    . LYS   B 162 ? 0.6902 0.5381 0.2605 -0.1016 0.1152  0.0979  161 LYS   B C    
3098 O  O    . LYS   B 162 ? 0.6985 0.5413 0.2483 -0.1203 0.1262  0.1039  161 LYS   B O    
3099 C  CB   . LYS   B 162 ? 0.7534 0.5476 0.3128 -0.0781 0.0863  0.1088  161 LYS   B CB   
3100 C  CG   . LYS   B 162 ? 0.8506 0.6003 0.3821 -0.08   0.0778  0.1237  161 LYS   B CG   
3101 C  CD   . LYS   B 162 ? 0.942  0.6797 0.4642 -0.0619 0.0612  0.1289  161 LYS   B CD   
3102 C  CE   . LYS   B 162 ? 1.0035 0.7556 0.5578 -0.0441 0.0505  0.1203  161 LYS   B CE   
3103 N  NZ   . LYS   B 162 ? 1.0356 0.7707 0.6053 -0.0397 0.0463  0.1217  161 LYS   B NZ   
3104 N  N    . ARG   B 163 ? 0.6756 0.5534 0.2628 -0.0876 0.1165  0.0871  162 ARG   B N    
3105 C  CA   . ARG   B 163 ? 0.6859 0.5923 0.2685 -0.0905 0.131   0.0811  162 ARG   B CA   
3106 C  C    . ARG   B 163 ? 0.6596 0.6098 0.2713 -0.0965 0.1445  0.0722  162 ARG   B C    
3107 O  O    . ARG   B 163 ? 0.6465 0.625  0.2579 -0.0973 0.1583  0.0665  162 ARG   B O    
3108 C  CB   . ARG   B 163 ? 0.7235 0.6347 0.3053 -0.0713 0.1261  0.0736  162 ARG   B CB   
3109 C  CG   . ARG   B 163 ? 0.8198 0.6967 0.3717 -0.0665 0.1133  0.0811  162 ARG   B CG   
3110 C  CD   . ARG   B 163 ? 0.9007 0.7849 0.4488 -0.0526 0.1116  0.0717  162 ARG   B CD   
3111 N  NE   . ARG   B 163 ? 1.0004 0.8579 0.5244 -0.048  0.0968  0.0772  162 ARG   B NE   
3112 C  CZ   . ARG   B 163 ? 1.0774 0.9218 0.5649 -0.0533 0.0979  0.0808  162 ARG   B CZ   
3113 N  NH1  . ARG   B 163 ? 1.0515 0.9048 0.5208 -0.064  0.1148  0.0799  162 ARG   B NH1  
3114 N  NH2  . ARG   B 163 ? 1.1143 0.9387 0.5829 -0.049  0.0819  0.0858  162 ARG   B NH2  
3115 N  N    . ASN   B 164 ? 0.6484 0.6069 0.2862 -0.0992 0.1404  0.0702  163 ASN   B N    
3116 C  CA   . ASN   B 164 ? 0.6254 0.6292 0.2959 -0.1028 0.1486  0.0617  163 ASN   B CA   
3117 C  C    . ASN   B 164 ? 0.6141 0.6518 0.3025 -0.0827 0.1527  0.0512  163 ASN   B C    
3118 O  O    . ASN   B 164 ? 0.6062 0.6835 0.3063 -0.0851 0.1665  0.0459  163 ASN   B O    
3119 C  CB   . ASN   B 164 ? 0.6231 0.6465 0.2907 -0.1284 0.1634  0.0641  163 ASN   B CB   
3120 C  CG   . ASN   B 164 ? 0.6326 0.6963 0.3355 -0.1347 0.1656  0.0573  163 ASN   B CG   
3121 O  OD1  . ASN   B 164 ? 0.6347 0.6923 0.3539 -0.1279 0.1539  0.0548  163 ASN   B OD1  
3122 N  ND2  . ASN   B 164 ? 0.6143 0.7242 0.3307 -0.1474 0.1804  0.0534  163 ASN   B ND2  
3123 N  N    . HIS   B 165 ? 0.6112 0.6305 0.2982 -0.0629 0.1413  0.0488  164 HIS   B N    
3124 C  CA   . HIS   B 165 ? 0.6057 0.6444 0.3014 -0.0432 0.1447  0.0395  164 HIS   B CA   
3125 C  C    . HIS   B 165 ? 0.6035 0.6228 0.3046 -0.0258 0.1301  0.0369  164 HIS   B C    
3126 O  O    . HIS   B 165 ? 0.6265 0.6125 0.3075 -0.0239 0.1206  0.041   164 HIS   B O    
3127 C  CB   . HIS   B 165 ? 0.6453 0.6755 0.3113 -0.0432 0.154   0.0392  164 HIS   B CB   
3128 C  CG   . HIS   B 165 ? 0.6901 0.7338 0.3587 -0.0234 0.1597  0.0287  164 HIS   B CG   
3129 N  ND1  . HIS   B 165 ? 0.7004 0.785  0.3858 -0.018  0.1752  0.0212  164 HIS   B ND1  
3130 C  CD2  . HIS   B 165 ? 0.7197 0.7394 0.3748 -0.0085 0.1522  0.0246  164 HIS   B CD2  
3131 C  CE1  . HIS   B 165 ? 0.7085 0.7885 0.3885 0.002   0.177   0.0128  164 HIS   B CE1  
3132 N  NE2  . HIS   B 165 ? 0.7245 0.7645 0.385  0.0067  0.1635  0.0143  164 HIS   B NE2  
3133 N  N    . GLY   B 166 ? 0.5729 0.6147 0.3007 -0.0137 0.1282  0.0305  165 GLY   B N    
3134 C  CA   . GLY   B 166 ? 0.5746 0.5999 0.3074 0.0014  0.1161  0.0277  165 GLY   B CA   
3135 C  C    . GLY   B 166 ? 0.5535 0.6059 0.3132 0.0145  0.1159  0.0216  165 GLY   B C    
3136 O  O    . GLY   B 166 ? 0.5377 0.6265 0.316  0.0125  0.124   0.0194  165 GLY   B O    
3137 N  N    . HIS   B 167 ? 0.5527 0.589  0.3141 0.0277  0.1064  0.0192  166 HIS   B N    
3138 C  CA   . HIS   B 167 ? 0.5334 0.5895 0.3163 0.0414  0.1042  0.015   166 HIS   B CA   
3139 C  C    . HIS   B 167 ? 0.5304 0.5617 0.3131 0.0455  0.0912  0.0159  166 HIS   B C    
3140 O  O    . HIS   B 167 ? 0.5503 0.5544 0.3162 0.051   0.0872  0.0148  166 HIS   B O    
3141 C  CB   . HIS   B 167 ? 0.5401 0.6066 0.3208 0.0599  0.1128  0.0085  166 HIS   B CB   
3142 C  CG   . HIS   B 167 ? 0.5437 0.6424 0.3494 0.0735  0.1135  0.0059  166 HIS   B CG   
3143 N  ND1  . HIS   B 167 ? 0.549  0.6818 0.3658 0.0847  0.1254  0.0017  166 HIS   B ND1  
3144 C  CD2  . HIS   B 167 ? 0.539  0.6419 0.3599 0.0782  0.1035  0.0073  166 HIS   B CD2  
3145 C  CE1  . HIS   B 167 ? 0.5317 0.689  0.3711 0.0967  0.1208  0.0015  166 HIS   B CE1  
3146 N  NE2  . HIS   B 167 ? 0.5278 0.667  0.3687 0.0925  0.1075  0.005   166 HIS   B NE2  
3147 N  N    . ILE   B 168 ? 0.5108 0.5519 0.3108 0.0409  0.0849  0.0176  167 ILE   B N    
3148 C  CA   . ILE   B 168 ? 0.5107 0.5329 0.3122 0.044   0.0741  0.0181  167 ILE   B CA   
3149 C  C    . ILE   B 168 ? 0.4963 0.5317 0.309  0.0587  0.072   0.0151  167 ILE   B C    
3150 O  O    . ILE   B 168 ? 0.4878 0.5523 0.3183 0.0586  0.0723  0.015   167 ILE   B O    
3151 C  CB   . ILE   B 168 ? 0.5139 0.5333 0.3226 0.0299  0.069   0.0211  167 ILE   B CB   
3152 C  CG1  . ILE   B 168 ? 0.5427 0.5485 0.3394 0.0161  0.0716  0.0255  167 ILE   B CG1  
3153 C  CG2  . ILE   B 168 ? 0.5151 0.5151 0.3239 0.0333  0.0596  0.0209  167 ILE   B CG2  
3154 C  CD1  . ILE   B 168 ? 0.5784 0.5556 0.3568 0.0185  0.0678  0.028   167 ILE   B CD1  
3155 N  N    . VAL   B 169 ? 0.4893 0.5023 0.2901 0.0704  0.0692  0.0132  168 VAL   B N    
3156 C  CA   . VAL   B 169 ? 0.4764 0.492  0.2814 0.0856  0.0666  0.0118  168 VAL   B CA   
3157 C  C    . VAL   B 169 ? 0.4773 0.4746 0.2809 0.0822  0.0571  0.0135  168 VAL   B C    
3158 O  O    . VAL   B 169 ? 0.4899 0.4606 0.2804 0.0777  0.0538  0.0134  168 VAL   B O    
3159 C  CB   . VAL   B 169 ? 0.4892 0.4865 0.2769 0.1002  0.0717  0.0081  168 VAL   B CB   
3160 C  CG1  . VAL   B 169 ? 0.4933 0.4822 0.2794 0.1167  0.0683  0.0077  168 VAL   B CG1  
3161 C  CG2  . VAL   B 169 ? 0.4804 0.499  0.27   0.1051  0.0831  0.0053  168 VAL   B CG2  
3162 N  N    . THR   B 170 ? 0.4675 0.4815 0.2844 0.0832  0.0527  0.015   169 THR   B N    
3163 C  CA   . THR   B 170 ? 0.4813 0.4801 0.2957 0.08    0.0451  0.0162  169 THR   B CA   
3164 C  C    . THR   B 170 ? 0.4934 0.4842 0.3011 0.0952  0.0427  0.017   169 THR   B C    
3165 O  O    . THR   B 170 ? 0.4847 0.499  0.3025 0.1054  0.0425  0.0182  169 THR   B O    
3166 C  CB   . THR   B 170 ? 0.484  0.5045 0.3133 0.0699  0.0416  0.0171  169 THR   B CB   
3167 O  OG1  . THR   B 170 ? 0.4989 0.5222 0.3317 0.0557  0.0445  0.0168  169 THR   B OG1  
3168 C  CG2  . THR   B 170 ? 0.4897 0.4963 0.315  0.0668  0.0352  0.0177  169 THR   B CG2  
3169 N  N    . VAL   B 171 ? 0.5146 0.4732 0.3052 0.0965  0.0406  0.0168  170 VAL   B N    
3170 C  CA   . VAL   B 171 ? 0.537  0.4804 0.3165 0.1097  0.0382  0.0186  170 VAL   B CA   
3171 C  C    . VAL   B 171 ? 0.5405 0.4853 0.3226 0.1032  0.0315  0.0216  170 VAL   B C    
3172 O  O    . VAL   B 171 ? 0.5577 0.4861 0.3338 0.0914  0.0297  0.021   170 VAL   B O    
3173 C  CB   . VAL   B 171 ? 0.5723 0.4773 0.3276 0.1134  0.0402  0.0166  170 VAL   B CB   
3174 C  CG1  . VAL   B 171 ? 0.5927 0.4751 0.3328 0.1245  0.0373  0.0196  170 VAL   B CG1  
3175 C  CG2  . VAL   B 171 ? 0.5809 0.4843 0.3304 0.1217  0.0477  0.0126  170 VAL   B CG2  
3176 N  N    . ALA   B 172 ? 0.5198 0.4886 0.3123 0.1099  0.028   0.0245  171 ALA   B N    
3177 C  CA   . ALA   B 172 ? 0.5078 0.4792 0.3001 0.1034  0.0217  0.0271  171 ALA   B CA   
3178 C  C    . ALA   B 172 ? 0.5227 0.4747 0.2977 0.1176  0.0176  0.0323  171 ALA   B C    
3179 O  O    . ALA   B 172 ? 0.5468 0.464  0.3029 0.1186  0.0197  0.0322  171 ALA   B O    
3180 C  CB   . ALA   B 172 ? 0.4855 0.4945 0.2974 0.096   0.0191  0.0265  171 ALA   B CB   
3181 N  N    . SER   B 173 ? 0.5106 0.4823 0.2899 0.1286  0.0116  0.0371  172 SER   B N    
3182 C  CA   . SER   B 173 ? 0.5227 0.4747 0.2837 0.143   0.0066  0.0439  172 SER   B CA   
3183 C  C    . SER   B 173 ? 0.5145 0.5032 0.2878 0.15    -0.002  0.0487  172 SER   B C    
3184 O  O    . SER   B 173 ? 0.496  0.5195 0.2887 0.1375  -0.0035 0.0456  172 SER   B O    
3185 C  CB   . SER   B 173 ? 0.5455 0.4643 0.2856 0.1292  0.0054  0.0451  172 SER   B CB   
3186 O  OG   . SER   B 173 ? 0.5779 0.4764 0.297  0.139   -0.0002 0.053   172 SER   B OG   
3187 N  N    . VAL   B 174 ? 0.5267 0.5066 0.2868 0.1686  -0.0084 0.0568  173 VAL   B N    
3188 C  CA   . VAL   B 174 ? 0.5259 0.541  0.2949 0.1728  -0.0192 0.0625  173 VAL   B CA   
3189 C  C    . VAL   B 174 ? 0.5396 0.5522 0.3006 0.1494  -0.0231 0.0615  173 VAL   B C    
3190 O  O    . VAL   B 174 ? 0.5253 0.5731 0.2974 0.1427  -0.0304 0.062   173 VAL   B O    
3191 C  CB   . VAL   B 174 ? 0.5431 0.5495 0.2985 0.1993  -0.0268 0.0728  173 VAL   B CB   
3192 C  CG1  . VAL   B 174 ? 0.5434 0.5734 0.3169 0.224   -0.0238 0.0725  173 VAL   B CG1  
3193 C  CG2  . VAL   B 174 ? 0.5727 0.5175 0.2917 0.2023  -0.0249 0.0774  173 VAL   B CG2  
3194 N  N    . CYS   B 175 ? 0.5595 0.5323 0.3017 0.1358  -0.0174 0.0591  174 CYS   B N    
3195 C  CA   . CYS   B 175 ? 0.5639 0.5303 0.2986 0.1138  -0.0171 0.056   174 CYS   B CA   
3196 C  C    . CYS   B 175 ? 0.5424 0.539  0.2994 0.097   -0.0146 0.0475  174 CYS   B C    
3197 O  O    . CYS   B 175 ? 0.5538 0.5509 0.3061 0.081   -0.0149 0.0443  174 CYS   B O    
3198 C  CB   . CYS   B 175 ? 0.6005 0.5241 0.3156 0.1051  -0.0101 0.0547  174 CYS   B CB   
3199 S  SG   . CYS   B 175 ? 0.7094 0.5882 0.3891 0.118   -0.0129 0.0651  174 CYS   B SG   
3200 N  N    . GLY   B 176 ? 0.5166 0.5344 0.2949 0.1002  -0.011  0.0436  175 GLY   B N    
3201 C  CA   . GLY   B 176 ? 0.5006 0.5446 0.2979 0.0848  -0.0086 0.0366  175 GLY   B CA   
3202 C  C    . GLY   B 176 ? 0.4787 0.5646 0.2891 0.0834  -0.0165 0.0376  175 GLY   B C    
3203 O  O    . GLY   B 176 ? 0.4643 0.5711 0.2873 0.0677  -0.0152 0.0317  175 GLY   B O    
3204 N  N    . HIS   B 177 ? 0.4748 0.5729 0.2811 0.0993  -0.0252 0.0452  176 HIS   B N    
3205 C  CA   . HIS   B 177 ? 0.4714 0.6144 0.2907 0.1005  -0.0352 0.0476  176 HIS   B CA   
3206 C  C    . HIS   B 177 ? 0.4963 0.6348 0.2956 0.1003  -0.0459 0.0536  176 HIS   B C    
3207 O  O    . HIS   B 177 ? 0.4891 0.6598 0.2934 0.09    -0.0543 0.0527  176 HIS   B O    
3208 C  CB   . HIS   B 177 ? 0.4681 0.6389 0.3046 0.1239  -0.0369 0.0524  176 HIS   B CB   
3209 C  CG   . HIS   B 177 ? 0.4827 0.6626 0.3377 0.1226  -0.0259 0.0464  176 HIS   B CG   
3210 N  ND1  . HIS   B 177 ? 0.4827 0.7044 0.361  0.1088  -0.0244 0.0412  176 HIS   B ND1  
3211 C  CD2  . HIS   B 177 ? 0.51   0.6602 0.3599 0.1307  -0.016  0.0447  176 HIS   B CD2  
3212 C  CE1  . HIS   B 177 ? 0.4886 0.7042 0.3746 0.1099  -0.0134 0.0374  176 HIS   B CE1  
3213 N  NE2  . HIS   B 177 ? 0.5091 0.683  0.3786 0.1233  -0.0084 0.0391  176 HIS   B NE2  
3214 N  N    . GLU   B 178 ? 0.5271 0.6251 0.3013 0.1099  -0.0458 0.0597  177 GLU   B N    
3215 C  CA   . GLU   B 178 ? 0.5483 0.6363 0.2983 0.11    -0.0552 0.0668  177 GLU   B CA   
3216 C  C    . GLU   B 178 ? 0.5838 0.6212 0.3062 0.1017  -0.0481 0.0668  177 GLU   B C    
3217 O  O    . GLU   B 178 ? 0.598  0.6054 0.3167 0.1075  -0.0397 0.0664  177 GLU   B O    
3218 C  CB   . GLU   B 178 ? 0.5923 0.6908 0.3392 0.137   -0.066  0.079   177 GLU   B CB   
3219 C  CG   . GLU   B 178 ? 0.7261 0.8124 0.444  0.1395  -0.0774 0.089   177 GLU   B CG   
3220 C  CD   . GLU   B 178 ? 0.852  0.9709 0.5686 0.1216  -0.0874 0.0871  177 GLU   B CD   
3221 O  OE1  . GLU   B 178 ? 0.8846 1.0386 0.6057 0.1332  -0.1018 0.0948  177 GLU   B OE1  
3222 O  OE2  . GLU   B 178 ? 0.8745 0.9831 0.5838 0.0968  -0.0811 0.0779  177 GLU   B OE2  
3223 N  N    . GLY   B 179 ? 0.5955 0.6262 0.2991 0.0864  -0.0508 0.0663  178 GLY   B N    
3224 C  CA   . GLY   B 179 ? 0.6247 0.6144 0.3026 0.076   -0.0436 0.066   178 GLY   B CA   
3225 C  C    . GLY   B 179 ? 0.6486 0.6043 0.2987 0.0904  -0.047  0.0783  178 GLY   B C    
3226 O  O    . GLY   B 179 ? 0.6521 0.6163 0.2983 0.1095  -0.0576 0.0883  178 GLY   B O    
3227 N  N    . ILE   B 180 ? 0.6621 0.5784 0.2927 0.0818  -0.0379 0.0779  179 ILE   B N    
3228 C  CA   . ILE   B 180 ? 0.6816 0.5564 0.2804 0.0909  -0.039  0.089   179 ILE   B CA   
3229 C  C    . ILE   B 180 ? 0.6653 0.5139 0.2388 0.07    -0.0317 0.0878  179 ILE   B C    
3230 O  O    . ILE   B 180 ? 0.6565 0.5024 0.2405 0.0547  -0.0204 0.0778  179 ILE   B O    
3231 C  CB   . ILE   B 180 ? 0.7167 0.5655 0.3195 0.1028  -0.0324 0.0889  179 ILE   B CB   
3232 C  CG1  . ILE   B 180 ? 0.7308 0.6012 0.3537 0.1268  -0.0382 0.0912  179 ILE   B CG1  
3233 C  CG2  . ILE   B 180 ? 0.7573 0.5533 0.323  0.1048  -0.0301 0.0977  179 ILE   B CG2  
3234 C  CD1  . ILE   B 180 ? 0.7659 0.6104 0.3909 0.1368  -0.0302 0.0888  179 ILE   B CD1  
3235 N  N    . PRO   B 181 ? 0.6625 0.4896 0.2015 0.0702  -0.0372 0.0986  180 PRO   B N    
3236 C  CA   . PRO   B 181 ? 0.6738 0.4751 0.1865 0.0491  -0.0283 0.0978  180 PRO   B CA   
3237 C  C    . PRO   B 181 ? 0.6819 0.4522 0.1927 0.0413  -0.0156 0.0941  180 PRO   B C    
3238 O  O    . PRO   B 181 ? 0.6843 0.4347 0.1956 0.0548  -0.0162 0.0978  180 PRO   B O    
3239 C  CB   . PRO   B 181 ? 0.7056 0.482  0.1778 0.0558  -0.0378 0.1135  180 PRO   B CB   
3240 C  CG   . PRO   B 181 ? 0.6949 0.5016 0.1785 0.0765  -0.0537 0.1197  180 PRO   B CG   
3241 C  CD   . PRO   B 181 ? 0.6575 0.4843 0.1796 0.0898  -0.0518 0.1126  180 PRO   B CD   
3242 N  N    . TYR   B 182 ? 0.6759 0.4453 0.186  0.0193  -0.0039 0.0859  181 TYR   B N    
3243 C  CA   . TYR   B 182 ? 0.676  0.4241 0.1864 0.0074  0.008   0.0815  181 TYR   B CA   
3244 C  C    . TYR   B 182 ? 0.6579 0.4224 0.2041 0.0123  0.0113  0.0719  181 TYR   B C    
3245 O  O    . TYR   B 182 ? 0.672  0.4236 0.2212 0.0028  0.0195  0.0678  181 TYR   B O    
3246 C  CB   . TYR   B 182 ? 0.7105 0.4096 0.184  0.0081  0.0083  0.093   181 TYR   B CB   
3247 C  CG   . TYR   B 182 ? 0.7561 0.4355 0.1905 0.0087  0.0017  0.106   181 TYR   B CG   
3248 C  CD1  . TYR   B 182 ? 0.7737 0.4655 0.1959 -0.0086 0.0056  0.104   181 TYR   B CD1  
3249 C  CD2  . TYR   B 182 ? 0.7856 0.4371 0.1961 0.029   -0.0091 0.1199  181 TYR   B CD2  
3250 C  CE1  . TYR   B 182 ? 0.8094 0.4859 0.1946 -0.0079 -0.0018 0.1161  181 TYR   B CE1  
3251 C  CE2  . TYR   B 182 ? 0.8235 0.4583 0.1976 0.0315  -0.017  0.1332  181 TYR   B CE2  
3252 C  CZ   . TYR   B 182 ? 0.8444 0.4922 0.2052 0.0121  -0.0139 0.1315  181 TYR   B CZ   
3253 O  OH   . TYR   B 182 ? 0.8966 0.5266 0.2171 0.0131  -0.0222 0.1453  181 TYR   B OH   
3254 N  N    . LEU   B 183 ? 0.6177 0.4127 0.1907 0.0247  0.0052  0.0681  182 LEU   B N    
3255 C  CA   . LEU   B 183 ? 0.5866 0.3971 0.1909 0.0285  0.0084  0.0598  182 LEU   B CA   
3256 C  C    . LEU   B 183 ? 0.5573 0.4054 0.1883 0.0243  0.0087  0.0505  182 LEU   B C    
3257 O  O    . LEU   B 183 ? 0.5425 0.4093 0.1966 0.0331  0.0061  0.0473  182 LEU   B O    
3258 C  CB   . LEU   B 183 ? 0.5793 0.3836 0.1874 0.0497  0.0019  0.0649  182 LEU   B CB   
3259 C  CG   . LEU   B 183 ? 0.6019 0.3629 0.1843 0.0559  0.003   0.0719  182 LEU   B CG   
3260 C  CD1  . LEU   B 183 ? 0.5848 0.3431 0.1727 0.0796  -0.0022 0.0753  182 LEU   B CD1  
3261 C  CD2  . LEU   B 183 ? 0.6135 0.3583 0.1962 0.0399  0.0126  0.0655  182 LEU   B CD2  
3262 N  N    . ILE   B 184 ? 0.5421 0.399  0.1675 0.0103  0.0125  0.0461  183 ILE   B N    
3263 C  CA   . ILE   B 184 ? 0.5177 0.403  0.1625 0.0052  0.0134  0.0368  183 ILE   B CA   
3264 C  C    . ILE   B 184 ? 0.5048 0.4006 0.1783 0.0043  0.0198  0.0279  183 ILE   B C    
3265 O  O    . ILE   B 184 ? 0.4985 0.4119 0.1904 0.0103  0.0159  0.0252  183 ILE   B O    
3266 C  CB   . ILE   B 184 ? 0.5228 0.4113 0.1523 -0.0094 0.018   0.0322  183 ILE   B CB   
3267 C  CG1  . ILE   B 184 ? 0.5363 0.4158 0.1345 -0.0086 0.0098  0.0421  183 ILE   B CG1  
3268 C  CG2  . ILE   B 184 ? 0.5146 0.4267 0.1623 -0.0143 0.0195  0.0212  183 ILE   B CG2  
3269 C  CD1  . ILE   B 184 ? 0.5527 0.4329 0.1297 -0.0243 0.0149  0.0378  183 ILE   B CD1  
3270 N  N    . PRO   B 185 ? 0.4946 0.3818 0.1728 -0.0032 0.029   0.0237  184 PRO   B N    
3271 C  CA   . PRO   B 185 ? 0.4615 0.3596 0.1661 -0.0022 0.033   0.0167  184 PRO   B CA   
3272 C  C    . PRO   B 185 ? 0.4409 0.3386 0.1561 0.0097  0.0276  0.0202  184 PRO   B C    
3273 O  O    . PRO   B 185 ? 0.4396 0.3507 0.1743 0.0125  0.0276  0.0159  184 PRO   B O    
3274 C  CB   . PRO   B 185 ? 0.4782 0.3695 0.1835 -0.0115 0.0419  0.0138  184 PRO   B CB   
3275 C  CG   . PRO   B 185 ? 0.4987 0.3813 0.1804 -0.0214 0.0455  0.0159  184 PRO   B CG   
3276 C  CD   . PRO   B 185 ? 0.4954 0.3661 0.1558 -0.0142 0.036   0.0252  184 PRO   B CD   
3277 N  N    . TYR   B 186 ? 0.4355 0.3158 0.1359 0.0168  0.0235  0.0279  185 TYR   B N    
3278 C  CA   . TYR   B 186 ? 0.4301 0.308  0.1377 0.0293  0.0199  0.0304  185 TYR   B CA   
3279 C  C    . TYR   B 186 ? 0.4304 0.3298 0.1486 0.0392  0.0136  0.0315  185 TYR   B C    
3280 O  O    . TYR   B 186 ? 0.4259 0.338  0.1616 0.0437  0.0138  0.0287  185 TYR   B O    
3281 C  CB   . TYR   B 186 ? 0.4387 0.287  0.1235 0.0348  0.0184  0.0375  185 TYR   B CB   
3282 C  CG   . TYR   B 186 ? 0.4447 0.2873 0.1325 0.0499  0.0156  0.0396  185 TYR   B CG   
3283 C  CD1  . TYR   B 186 ? 0.45   0.2868 0.1455 0.0486  0.0193  0.0353  185 TYR   B CD1  
3284 C  CD2  . TYR   B 186 ? 0.4555 0.2996 0.1375 0.0662  0.0093  0.0459  185 TYR   B CD2  
3285 C  CE1  . TYR   B 186 ? 0.4635 0.2932 0.1585 0.062   0.0183  0.0363  185 TYR   B CE1  
3286 C  CE2  . TYR   B 186 ? 0.4649 0.3047 0.1497 0.0818  0.0086  0.0469  185 TYR   B CE2  
3287 C  CZ   . TYR   B 186 ? 0.4816 0.3126 0.1716 0.0791  0.0138  0.0416  185 TYR   B CZ   
3288 O  OH   . TYR   B 186 ? 0.5069 0.3322 0.197  0.094   0.0146  0.0415  185 TYR   B OH   
3289 N  N    . CYS   B 187 ? 0.4388 0.3444 0.146  0.0412  0.0078  0.0358  186 CYS   B N    
3290 C  CA   . CYS   B 187 ? 0.4429 0.375  0.1611 0.0486  0.0007  0.0369  186 CYS   B CA   
3291 C  C    . CYS   B 187 ? 0.4434 0.3976 0.1818 0.0386  0.0036  0.0282  186 CYS   B C    
3292 O  O    . CYS   B 187 ? 0.4407 0.4152 0.1955 0.043   0.0014  0.0271  186 CYS   B O    
3293 C  CB   . CYS   B 187 ? 0.4636 0.3995 0.1641 0.0499  -0.0072 0.043   186 CYS   B CB   
3294 S  SG   . CYS   B 187 ? 0.5368 0.4478 0.2133 0.0679  -0.0136 0.056   186 CYS   B SG   
3295 N  N    . SER   B 188 ? 0.4457 0.3947 0.1815 0.0252  0.0094  0.0219  187 SER   B N    
3296 C  CA   . SER   B 188 ? 0.4384 0.3993 0.1881 0.0158  0.0134  0.0132  187 SER   B CA   
3297 C  C    . SER   B 188 ? 0.4367 0.3978 0.2044 0.0194  0.0172  0.0112  187 SER   B C    
3298 O  O    . SER   B 188 ? 0.4422 0.4173 0.2224 0.0176  0.0165  0.0084  187 SER   B O    
3299 C  CB   . SER   B 188 ? 0.4524 0.4029 0.1937 0.0047  0.0206  0.0072  187 SER   B CB   
3300 O  OG   . SER   B 188 ? 0.4752 0.4332 0.2234 -0.0037 0.024   -0.0014 187 SER   B OG   
3301 N  N    . SER   B 189 ? 0.4285 0.3738 0.1954 0.023   0.0206  0.0129  188 SER   B N    
3302 C  CA   . SER   B 189 ? 0.4069 0.3513 0.1872 0.0264  0.0231  0.0118  188 SER   B CA   
3303 C  C    . SER   B 189 ? 0.3943 0.3479 0.1792 0.0365  0.0192  0.0159  188 SER   B C    
3304 O  O    . SER   B 189 ? 0.3976 0.3581 0.1941 0.0371  0.0209  0.0143  188 SER   B O    
3305 C  CB   . SER   B 189 ? 0.4157 0.3435 0.192  0.026   0.0264  0.0124  188 SER   B CB   
3306 O  OG   . SER   B 189 ? 0.4458 0.36   0.2081 0.0322  0.0239  0.0179  188 SER   B OG   
3307 N  N    . LYS   B 190 ? 0.3838 0.3379 0.1592 0.0452  0.0144  0.0213  189 LYS   B N    
3308 C  CA   . LYS   B 190 ? 0.3773 0.3444 0.1591 0.0574  0.0115  0.0246  189 LYS   B CA   
3309 C  C    . LYS   B 190 ? 0.3765 0.3751 0.1728 0.0538  0.0087  0.0228  189 LYS   B C    
3310 O  O    . LYS   B 190 ? 0.3804 0.3952 0.1895 0.0575  0.01    0.0224  189 LYS   B O    
3311 C  CB   . LYS   B 190 ? 0.3804 0.3352 0.147  0.0711  0.0075  0.0314  189 LYS   B CB   
3312 C  CG   . LYS   B 190 ? 0.4008 0.3238 0.1536 0.0744  0.0114  0.0323  189 LYS   B CG   
3313 C  CD   . LYS   B 190 ? 0.4349 0.3584 0.1973 0.0776  0.0159  0.029   189 LYS   B CD   
3314 C  CE   . LYS   B 190 ? 0.4863 0.3798 0.235  0.074   0.0194  0.0278  189 LYS   B CE   
3315 N  NZ   . LYS   B 190 ? 0.5177 0.406  0.267  0.0808  0.0226  0.0257  189 LYS   B NZ   
3316 N  N    . PHE   B 191 ? 0.3771 0.3838 0.1701 0.0442  0.0056  0.0209  190 PHE   B N    
3317 C  CA   . PHE   B 191 ? 0.3689 0.4032 0.1728 0.0356  0.0029  0.0177  190 PHE   B CA   
3318 C  C    . PHE   B 191 ? 0.3773 0.4086 0.1916 0.0251  0.0098  0.0117  190 PHE   B C    
3319 O  O    . PHE   B 191 ? 0.3768 0.4282 0.2032 0.0212  0.0101  0.0105  190 PHE   B O    
3320 C  CB   . PHE   B 191 ? 0.3702 0.4059 0.1624 0.0252  -0.0009 0.0155  190 PHE   B CB   
3321 C  CG   . PHE   B 191 ? 0.3661 0.4225 0.1532 0.031   -0.0111 0.0211  190 PHE   B CG   
3322 C  CD1  . PHE   B 191 ? 0.3798 0.4241 0.1533 0.0449  -0.0154 0.0293  190 PHE   B CD1  
3323 C  CD2  . PHE   B 191 ? 0.3562 0.4432 0.1503 0.0217  -0.0171 0.0186  190 PHE   B CD2  
3324 C  CE1  . PHE   B 191 ? 0.3849 0.4471 0.1522 0.0523  -0.026  0.0359  190 PHE   B CE1  
3325 C  CE2  . PHE   B 191 ? 0.3612 0.4711 0.1512 0.0276  -0.0283 0.0245  190 PHE   B CE2  
3326 C  CZ   . PHE   B 191 ? 0.3667 0.4641 0.1433 0.0441  -0.0331 0.0336  190 PHE   B CZ   
3327 N  N    . ALA   B 192 ? 0.3808 0.3875 0.1901 0.0211  0.0154  0.0087  191 ALA   B N    
3328 C  CA   . ALA   B 192 ? 0.3733 0.3716 0.1895 0.0146  0.0211  0.0047  191 ALA   B CA   
3329 C  C    . ALA   B 192 ? 0.377  0.38   0.2015 0.0215  0.0227  0.0081  191 ALA   B C    
3330 O  O    . ALA   B 192 ? 0.3833 0.3915 0.2144 0.015   0.0254  0.0065  191 ALA   B O    
3331 C  CB   . ALA   B 192 ? 0.3754 0.3512 0.1865 0.0138  0.0255  0.0024  191 ALA   B CB   
3332 N  N    . ALA   B 193 ? 0.3786 0.3774 0.1999 0.0337  0.0217  0.0123  192 ALA   B N    
3333 C  CA   . ALA   B 193 ? 0.3822 0.3846 0.2082 0.0408  0.0242  0.0144  192 ALA   B CA   
3334 C  C    . ALA   B 193 ? 0.3974 0.4303 0.2347 0.0413  0.0235  0.015   192 ALA   B C    
3335 O  O    . ALA   B 193 ? 0.4082 0.4489 0.2521 0.0376  0.0278  0.0144  192 ALA   B O    
3336 C  CB   . ALA   B 193 ? 0.3828 0.3703 0.199  0.0533  0.0236  0.0174  192 ALA   B CB   
3337 N  N    . VAL   B 194 ? 0.3964 0.4488 0.236  0.045   0.018   0.0166  193 VAL   B N    
3338 C  CA   . VAL   B 194 ? 0.3817 0.471  0.2356 0.0451  0.0164  0.0171  193 VAL   B CA   
3339 C  C    . VAL   B 194 ? 0.3908 0.491  0.2514 0.0251  0.0188  0.0127  193 VAL   B C    
3340 O  O    . VAL   B 194 ? 0.392  0.514  0.2638 0.0205  0.0224  0.0123  193 VAL   B O    
3341 C  CB   . VAL   B 194 ? 0.3664 0.4755 0.2205 0.0532  0.0077  0.0205  193 VAL   B CB   
3342 C  CG1  . VAL   B 194 ? 0.3428 0.4978 0.2149 0.0497  0.0045  0.0204  193 VAL   B CG1  
3343 C  CG2  . VAL   B 194 ? 0.3759 0.4718 0.2216 0.0747  0.0063  0.0258  193 VAL   B CG2  
3344 N  N    . GLY   B 195 ? 0.3895 0.4724 0.2416 0.0131  0.0178  0.0091  194 GLY   B N    
3345 C  CA   . GLY   B 195 ? 0.3812 0.464  0.234  -0.006  0.0204  0.0042  194 GLY   B CA   
3346 C  C    . GLY   B 195 ? 0.3788 0.4447 0.2314 -0.0102 0.0278  0.0042  194 GLY   B C    
3347 O  O    . GLY   B 195 ? 0.3722 0.4472 0.2284 -0.0239 0.0309  0.0026  194 GLY   B O    
3348 N  N    . PHE   B 196 ? 0.3845 0.4259 0.2316 0.0002  0.0302  0.0064  195 PHE   B N    
3349 C  CA   . PHE   B 196 ? 0.3952 0.4197 0.2398 -0.0016 0.0356  0.0078  195 PHE   B CA   
3350 C  C    . PHE   B 196 ? 0.4004 0.4477 0.2524 -0.0003 0.039   0.0105  195 PHE   B C    
3351 O  O    . PHE   B 196 ? 0.4098 0.4564 0.2612 -0.0111 0.0437  0.0109  195 PHE   B O    
3352 C  CB   . PHE   B 196 ? 0.4011 0.4019 0.2392 0.0096  0.0355  0.0097  195 PHE   B CB   
3353 C  CG   . PHE   B 196 ? 0.4139 0.4012 0.2483 0.0107  0.0389  0.0126  195 PHE   B CG   
3354 C  CD1  . PHE   B 196 ? 0.4281 0.3966 0.2579 0.0032  0.041   0.0127  195 PHE   B CD1  
3355 C  CD2  . PHE   B 196 ? 0.4272 0.4188 0.2602 0.0198  0.0402  0.0152  195 PHE   B CD2  
3356 C  CE1  . PHE   B 196 ? 0.4485 0.4046 0.2725 0.0045  0.0428  0.0168  195 PHE   B CE1  
3357 C  CE2  . PHE   B 196 ? 0.4397 0.4191 0.2661 0.0196  0.0428  0.0179  195 PHE   B CE2  
3358 C  CZ   . PHE   B 196 ? 0.4463 0.4091 0.2683 0.0118  0.0435  0.0193  195 PHE   B CZ   
3359 N  N    . HIS   B 197 ? 0.3937 0.4599 0.2515 0.0131  0.0373  0.0123  196 HIS   B N    
3360 C  CA   . HIS   B 197 ? 0.3912 0.4834 0.2578 0.0173  0.0417  0.0137  196 HIS   B CA   
3361 C  C    . HIS   B 197 ? 0.3979 0.5236 0.2769 0.0019  0.043   0.0121  196 HIS   B C    
3362 O  O    . HIS   B 197 ? 0.4096 0.5482 0.2925 -0.0051 0.0498  0.0126  196 HIS   B O    
3363 C  CB   . HIS   B 197 ? 0.3794 0.4836 0.2492 0.0376  0.0393  0.0154  196 HIS   B CB   
3364 C  CG   . HIS   B 197 ? 0.3647 0.5063 0.2485 0.0441  0.0432  0.0158  196 HIS   B CG   
3365 N  ND1  . HIS   B 197 ? 0.3759 0.5195 0.2589 0.0457  0.0521  0.0156  196 HIS   B ND1  
3366 C  CD2  . HIS   B 197 ? 0.3523 0.5336 0.252  0.0483  0.0397  0.0162  196 HIS   B CD2  
3367 C  CE1  . HIS   B 197 ? 0.3609 0.5457 0.2604 0.0514  0.0551  0.0153  196 HIS   B CE1  
3368 N  NE2  . HIS   B 197 ? 0.3446 0.5549 0.2561 0.054   0.0472  0.016   196 HIS   B NE2  
3369 N  N    A ARG   B 198 ? 0.3941 0.5349 0.2778 -0.0046 0.0367  0.01    197 ARG   B N    
3370 N  N    B ARG   B 198 ? 0.3913 0.5318 0.2748 -0.0045 0.0367  0.0101  197 ARG   B N    
3371 C  CA   A ARG   B 198 ? 0.3919 0.5669 0.2869 -0.0217 0.0364  0.0078  197 ARG   B CA   
3372 C  CA   B ARG   B 198 ? 0.3869 0.5614 0.2817 -0.0216 0.0364  0.0078  197 ARG   B CA   
3373 C  C    A ARG   B 198 ? 0.406  0.5615 0.292  -0.0453 0.0415  0.0051  197 ARG   B C    
3374 C  C    B ARG   B 198 ? 0.4036 0.5586 0.2895 -0.0451 0.0416  0.0052  197 ARG   B C    
3375 O  O    A ARG   B 198 ? 0.398  0.5768 0.2911 -0.0605 0.046   0.0045  197 ARG   B O    
3376 O  O    B ARG   B 198 ? 0.3963 0.5741 0.2891 -0.0598 0.0464  0.0047  197 ARG   B O    
3377 C  CB   A ARG   B 198 ? 0.4044 0.6002 0.3037 -0.0227 0.0266  0.0062  197 ARG   B CB   
3378 C  CB   B ARG   B 198 ? 0.3918 0.5863 0.2905 -0.0231 0.0265  0.0061  197 ARG   B CB   
3379 C  CG   A ARG   B 198 ? 0.4336 0.6537 0.3423 0.0004  0.0211  0.0103  197 ARG   B CG   
3380 C  CG   B ARG   B 198 ? 0.3926 0.6428 0.312  -0.019  0.0223  0.0075  197 ARG   B CG   
3381 C  CD   A ARG   B 198 ? 0.4566 0.7085 0.3718 -0.0027 0.0105  0.0101  197 ARG   B CD   
3382 C  CD   B ARG   B 198 ? 0.4033 0.6855 0.3364 -0.0347 0.0294  0.0061  197 ARG   B CD   
3383 N  NE   A ARG   B 198 ? 0.4818 0.7521 0.4033 0.0223  0.0045  0.0155  197 ARG   B NE   
3384 N  NE   B ARG   B 198 ? 0.4042 0.7451 0.3585 -0.0388 0.0237  0.0057  197 ARG   B NE   
3385 C  CZ   A ARG   B 198 ? 0.4923 0.8018 0.4243 0.0265  -0.0056 0.0178  197 ARG   B CZ   
3386 C  CZ   B ARG   B 198 ? 0.4073 0.7899 0.3788 -0.0518 0.0292  0.0045  197 ARG   B CZ   
3387 N  NH1  A ARG   B 198 ? 0.4787 0.8169 0.417  0.0049  -0.0108 0.0142  197 ARG   B NH1  
3388 N  NH1  B ARG   B 198 ? 0.4073 0.7752 0.3742 -0.0621 0.0413  0.0042  197 ARG   B NH1  
3389 N  NH2  A ARG   B 198 ? 0.4821 0.8017 0.4171 0.0524  -0.0109 0.024   197 ARG   B NH2  
3390 N  NH2  B ARG   B 198 ? 0.3798 0.8213 0.3732 -0.0551 0.0227  0.0042  197 ARG   B NH2  
3391 N  N    . ALA   B 199 ? 0.4226 0.5362 0.2927 -0.0488 0.041   0.0035  198 ALA   B N    
3392 C  CA   . ALA   B 199 ? 0.4344 0.5212 0.2924 -0.0679 0.0458  0.0015  198 ALA   B CA   
3393 C  C    . ALA   B 199 ? 0.4495 0.5216 0.3024 -0.0668 0.0532  0.0063  198 ALA   B C    
3394 O  O    . ALA   B 199 ? 0.4557 0.5225 0.3026 -0.085  0.0586  0.0066  198 ALA   B O    
3395 C  CB   . ALA   B 199 ? 0.4469 0.4946 0.2907 -0.0673 0.0438  -0.0017 198 ALA   B CB   
3396 N  N    . LEU   B 200 ? 0.4484 0.5142 0.3014 -0.0474 0.0535  0.0102  199 LEU   B N    
3397 C  CA   . LEU   B 200 ? 0.4541 0.5076 0.2998 -0.0456 0.0597  0.0147  199 LEU   B CA   
3398 C  C    . LEU   B 200 ? 0.4607 0.5496 0.3156 -0.0543 0.0663  0.0155  199 LEU   B C    
3399 O  O    . LEU   B 200 ? 0.4842 0.5641 0.3302 -0.0688 0.0729  0.0179  199 LEU   B O    
3400 C  CB   . LEU   B 200 ? 0.4506 0.4925 0.2932 -0.025  0.0579  0.0171  199 LEU   B CB   
3401 C  CG   . LEU   B 200 ? 0.4624 0.493  0.2948 -0.0229 0.0635  0.0215  199 LEU   B CG   
3402 C  CD1  . LEU   B 200 ? 0.476  0.4727 0.2926 -0.0339 0.0648  0.0251  199 LEU   B CD1  
3403 C  CD2  . LEU   B 200 ? 0.4723 0.4941 0.3007 -0.0044 0.0611  0.0222  199 LEU   B CD2  
3404 N  N    . THR   B 201 ? 0.4398 0.57   0.3125 -0.0456 0.0649  0.0137  200 THR   B N    
3405 C  CA   . THR   B 201 ? 0.4228 0.5977 0.3104 -0.0513 0.0713  0.0135  200 THR   B CA   
3406 C  C    . THR   B 201 ? 0.4261 0.611  0.3139 -0.08   0.0743  0.0119  200 THR   B C    
3407 O  O    . THR   B 201 ? 0.4372 0.627  0.3212 -0.0937 0.0834  0.0138  200 THR   B O    
3408 C  CB   . THR   B 201 ? 0.4175 0.6345 0.3256 -0.0353 0.0662  0.0118  200 THR   B CB   
3409 O  OG1  . THR   B 201 ? 0.4518 0.6511 0.3547 -0.0105 0.0639  0.0133  200 THR   B OG1  
3410 C  CG2  . THR   B 201 ? 0.3903 0.6612 0.3186 -0.0383 0.0726  0.0112  200 THR   B CG2  
3411 N  N    . LEU   B 202 ? 0.4242 0.605  0.3115 -0.0908 0.0673  0.0084  201 LEU   B N    
3412 C  CA   . LEU   B 202 ? 0.4268 0.6129 0.3111 -0.1202 0.0696  0.0056  201 LEU   B CA   
3413 C  C    . LEU   B 202 ? 0.4557 0.5931 0.3157 -0.1353 0.0764  0.0081  201 LEU   B C    
3414 O  O    . LEU   B 202 ? 0.4566 0.6019 0.313  -0.1588 0.0834  0.0085  201 LEU   B O    
3415 C  CB   . LEU   B 202 ? 0.4197 0.6102 0.3055 -0.1279 0.0603  0       201 LEU   B CB   
3416 C  CG   . LEU   B 202 ? 0.406  0.6526 0.3158 -0.118  0.0527  -0.0013 201 LEU   B CG   
3417 C  CD1  . LEU   B 202 ? 0.409  0.6557 0.3154 -0.1253 0.0427  -0.0062 201 LEU   B CD1  
3418 C  CD2  . LEU   B 202 ? 0.3864 0.6887 0.3162 -0.132  0.0571  -0.0017 201 LEU   B CD2  
3419 N  N    . GLU   B 203 ? 0.4757 0.5643 0.319  -0.1219 0.0745  0.0106  202 GLU   B N    
3420 C  CA   . GLU   B 203 ? 0.5071 0.546  0.3262 -0.1314 0.0792  0.0145  202 GLU   B CA   
3421 C  C    . GLU   B 203 ? 0.5228 0.564  0.3357 -0.1338 0.0877  0.0211  202 GLU   B C    
3422 O  O    . GLU   B 203 ? 0.5351 0.5583 0.3323 -0.1547 0.0943  0.0239  202 GLU   B O    
3423 C  CB   . GLU   B 203 ? 0.5475 0.5427 0.355  -0.1136 0.0739  0.0156  202 GLU   B CB   
3424 C  CG   . GLU   B 203 ? 0.6314 0.575  0.4144 -0.1197 0.0774  0.0206  202 GLU   B CG   
3425 C  CD   . GLU   B 203 ? 0.6964 0.6032 0.472  -0.1022 0.072   0.0208  202 GLU   B CD   
3426 O  OE1  . GLU   B 203 ? 0.6801 0.5674 0.4483 -0.0885 0.071   0.0273  202 GLU   B OE1  
3427 O  OE2  . GLU   B 203 ? 0.7353 0.6358 0.5129 -0.1023 0.0687  0.0141  202 GLU   B OE2  
3428 N  N    . LEU   B 204 ? 0.5165 0.5782 0.3389 -0.1138 0.0883  0.0232  203 LEU   B N    
3429 C  CA   . LEU   B 204 ? 0.5281 0.596  0.3439 -0.115  0.0973  0.0282  203 LEU   B CA   
3430 C  C    . LEU   B 204 ? 0.5358 0.6405 0.3592 -0.1393 0.1067  0.0271  203 LEU   B C    
3431 O  O    . LEU   B 204 ? 0.5484 0.6391 0.3551 -0.1557 0.1152  0.0318  203 LEU   B O    
3432 C  CB   . LEU   B 204 ? 0.5083 0.5994 0.3358 -0.09   0.0968  0.0274  203 LEU   B CB   
3433 C  CG   . LEU   B 204 ? 0.5241 0.5817 0.3419 -0.0693 0.0896  0.029   203 LEU   B CG   
3434 C  CD1  . LEU   B 204 ? 0.5105 0.5898 0.3381 -0.0477 0.0896  0.0268  203 LEU   B CD1  
3435 C  CD2  . LEU   B 204 ? 0.5528 0.5705 0.3458 -0.0728 0.0915  0.0357  203 LEU   B CD2  
3436 N  N    . GLN   B 205 ? 0.5239 0.676  0.372  -0.1428 0.1043  0.0212  204 GLN   B N    
3437 C  CA   . GLN   B 205 ? 0.5226 0.7219 0.3852 -0.1651 0.1113  0.0188  204 GLN   B CA   
3438 C  C    . GLN   B 205 ? 0.5552 0.7247 0.3985 -0.1977 0.1136  0.0191  204 GLN   B C    
3439 O  O    . GLN   B 205 ? 0.5763 0.7512 0.4114 -0.2201 0.1241  0.0218  204 GLN   B O    
3440 C  CB   . GLN   B 205 ? 0.529  0.7808 0.4215 -0.1563 0.1038  0.0131  204 GLN   B CB   
3441 C  CG   . GLN   B 205 ? 0.5787 0.8993 0.4975 -0.1698 0.109   0.0102  204 GLN   B CG   
3442 C  CD   . GLN   B 205 ? 0.6738 1.0298 0.6144 -0.1627 0.0966  0.0056  204 GLN   B CD   
3443 O  OE1  . GLN   B 205 ? 0.7026 1.0712 0.6555 -0.1334 0.0897  0.0056  204 GLN   B OE1  
3444 N  NE2  . GLN   B 205 ? 0.6905 1.0557 0.6314 -0.19   0.0926  0.0018  204 GLN   B NE2  
3445 N  N    . ALA   B 206 ? 0.5644 0.6956 0.396  -0.2002 0.1052  0.0165  205 ALA   B N    
3446 C  CA   . ALA   B 206 ? 0.588  0.6794 0.3962 -0.2287 0.1073  0.0158  205 ALA   B CA   
3447 C  C    . ALA   B 206 ? 0.6253 0.6647 0.4028 -0.2358 0.1152  0.0242  205 ALA   B C    
3448 O  O    . ALA   B 206 ? 0.6398 0.6581 0.3982 -0.2647 0.1218  0.0256  205 ALA   B O    
3449 C  CB   . ALA   B 206 ? 0.6011 0.6569 0.401  -0.2224 0.0977  0.0109  205 ALA   B CB   
3450 N  N    . LEU   B 207 ? 0.6375 0.6539 0.4077 -0.2103 0.1138  0.0302  206 LEU   B N    
3451 C  CA   . LEU   B 207 ? 0.6681 0.6363 0.4083 -0.213  0.119   0.0397  206 LEU   B CA   
3452 C  C    . LEU   B 207 ? 0.6728 0.6671 0.4106 -0.2232 0.1305  0.0448  206 LEU   B C    
3453 O  O    . LEU   B 207 ? 0.7024 0.6585 0.4126 -0.2264 0.135   0.0537  206 LEU   B O    
3454 C  CB   . LEU   B 207 ? 0.6783 0.6123 0.4109 -0.1828 0.1111  0.0438  206 LEU   B CB   
3455 C  CG   . LEU   B 207 ? 0.7028 0.6043 0.4334 -0.1721 0.1018  0.0398  206 LEU   B CG   
3456 C  CD1  . LEU   B 207 ? 0.713  0.5947 0.4423 -0.143  0.0945  0.0435  206 LEU   B CD1  
3457 C  CD2  . LEU   B 207 ? 0.7408 0.5903 0.4445 -0.191  0.1041  0.0415  206 LEU   B CD2  
3458 N  N    . GLY   B 208 ? 0.6419 0.7008 0.4074 -0.2273 0.1354  0.0395  207 GLY   B N    
3459 C  CA   . GLY   B 208 ? 0.6352 0.7277 0.4027 -0.2356 0.1482  0.0424  207 GLY   B CA   
3460 C  C    . GLY   B 208 ? 0.6403 0.7331 0.4057 -0.2079 0.1491  0.0457  207 GLY   B C    
3461 O  O    . GLY   B 208 ? 0.6565 0.7607 0.4127 -0.2139 0.1605  0.0494  207 GLY   B O    
3462 N  N    . ILE   B 209 ? 0.6323 0.7108 0.4034 -0.1793 0.1379  0.044   208 ILE   B N    
3463 C  CA   . ILE   B 209 ? 0.6392 0.7153 0.4067 -0.1542 0.1376  0.0457  208 ILE   B CA   
3464 C  C    . ILE   B 209 ? 0.6255 0.7612 0.4229 -0.1399 0.1416  0.0386  208 ILE   B C    
3465 O  O    . ILE   B 209 ? 0.6292 0.7825 0.4477 -0.1229 0.1332  0.0333  208 ILE   B O    
3466 C  CB   . ILE   B 209 ? 0.6556 0.6886 0.4141 -0.1332 0.1243  0.0474  208 ILE   B CB   
3467 C  CG1  . ILE   B 209 ? 0.6932 0.6689 0.4226 -0.1449 0.1212  0.0551  208 ILE   B CG1  
3468 C  CG2  . ILE   B 209 ? 0.6578 0.6894 0.412  -0.1096 0.123   0.048   208 ILE   B CG2  
3469 C  CD1  . ILE   B 209 ? 0.718  0.659  0.4443 -0.1272 0.1089  0.0556  208 ILE   B CD1  
3470 N  N    . THR   B 210 ? 0.6114 0.7772 0.4092 -0.1464 0.1552  0.0388  209 THR   B N    
3471 C  CA   . THR   B 210 ? 0.5836 0.809  0.4091 -0.1335 0.1625  0.0322  209 THR   B CA   
3472 C  C    . THR   B 210 ? 0.5841 0.8053 0.4064 -0.1032 0.1627  0.0298  209 THR   B C    
3473 O  O    . THR   B 210 ? 0.5663 0.8266 0.4126 -0.0839 0.164   0.0237  209 THR   B O    
3474 C  CB   . THR   B 210 ? 0.5838 0.8466 0.4116 -0.1568 0.1793  0.0326  209 THR   B CB   
3475 O  OG1  . THR   B 210 ? 0.6326 0.8564 0.4248 -0.1659 0.1871  0.0394  209 THR   B OG1  
3476 C  CG2  . THR   B 210 ? 0.5762 0.8546 0.4124 -0.1882 0.1798  0.0327  209 THR   B CG2  
3477 N  N    . GLY   B 211 ? 0.6026 0.7758 0.3942 -0.0992 0.161   0.0348  210 GLY   B N    
3478 C  CA   . GLY   B 211 ? 0.6025 0.7663 0.3844 -0.0755 0.1619  0.0322  210 GLY   B CA   
3479 C  C    . GLY   B 211 ? 0.5995 0.7416 0.3849 -0.0519 0.148   0.0296  210 GLY   B C    
3480 O  O    . GLY   B 211 ? 0.6113 0.7473 0.3889 -0.0333 0.1494  0.0261  210 GLY   B O    
3481 N  N    . ILE   B 212 ? 0.5813 0.7089 0.3752 -0.0539 0.1355  0.0309  211 ILE   B N    
3482 C  CA   . ILE   B 212 ? 0.5787 0.6866 0.3757 -0.0342 0.123   0.0288  211 ILE   B CA   
3483 C  C    . ILE   B 212 ? 0.5471 0.6908 0.3732 -0.0222 0.1197  0.0231  211 ILE   B C    
3484 O  O    . ILE   B 212 ? 0.5234 0.6845 0.3653 -0.033  0.1162  0.0228  211 ILE   B O    
3485 C  CB   . ILE   B 212 ? 0.5992 0.6639 0.3833 -0.0402 0.1113  0.0339  211 ILE   B CB   
3486 C  CG1  . ILE   B 212 ? 0.637  0.6665 0.3914 -0.0485 0.1128  0.041   211 ILE   B CG1  
3487 C  CG2  . ILE   B 212 ? 0.6013 0.6513 0.3904 -0.0217 0.1     0.0312  211 ILE   B CG2  
3488 C  CD1  . ILE   B 212 ? 0.6733 0.6636 0.4165 -0.0528 0.1025  0.0466  211 ILE   B CD1  
3489 N  N    . LYS   B 213 ? 0.5391 0.6915 0.3695 0.0001  0.1207  0.0188  212 LYS   B N    
3490 C  CA   . LYS   B 213 ? 0.5061 0.6894 0.3609 0.0157  0.1171  0.0147  212 LYS   B CA   
3491 C  C    . LYS   B 213 ? 0.5035 0.6587 0.3561 0.0257  0.1033  0.0152  212 LYS   B C    
3492 O  O    . LYS   B 213 ? 0.5248 0.6395 0.3584 0.0248  0.098   0.0172  212 LYS   B O    
3493 C  CB   . LYS   B 213 ? 0.5131 0.7185 0.372  0.0364  0.1268  0.0099  212 LYS   B CB   
3494 C  CG   . LYS   B 213 ? 0.5346 0.7663 0.3923 0.0269  0.1429  0.0087  212 LYS   B CG   
3495 C  CD   . LYS   B 213 ? 0.5539 0.8367 0.4384 0.0119  0.1468  0.009   212 LYS   B CD   
3496 C  CE   . LYS   B 213 ? 0.5898 0.8929 0.4698 -0.0075 0.1619  0.0097  212 LYS   B CE   
3497 N  NZ   . LYS   B 213 ? 0.5923 0.9547 0.5028 -0.0208 0.1664  0.0085  212 LYS   B NZ   
3498 N  N    . THR   B 214 ? 0.4749 0.6538 0.3471 0.0335  0.0972  0.0138  213 THR   B N    
3499 C  CA   . THR   B 214 ? 0.4754 0.6304 0.3449 0.0419  0.0853  0.0143  213 THR   B CA   
3500 C  C    . THR   B 214 ? 0.4557 0.6314 0.3375 0.0641  0.0829  0.0125  213 THR   B C    
3501 O  O    . THR   B 214 ? 0.4365 0.6562 0.3383 0.0681  0.0863  0.0115  213 THR   B O    
3502 C  CB   . THR   B 214 ? 0.488  0.6421 0.3634 0.0244  0.0776  0.0157  213 THR   B CB   
3503 O  OG1  . THR   B 214 ? 0.4793 0.6788 0.3759 0.0172  0.0785  0.0145  213 THR   B OG1  
3504 C  CG2  . THR   B 214 ? 0.4997 0.6238 0.3598 0.0057  0.0788  0.0181  213 THR   B CG2  
3505 N  N    . SER   B 215 ? 0.4634 0.6082 0.3329 0.0784  0.0768  0.0126  214 SER   B N    
3506 C  CA   . SER   B 215 ? 0.4577 0.6117 0.3332 0.1007  0.0734  0.0124  214 SER   B CA   
3507 C  C    . SER   B 215 ? 0.4684 0.5918 0.3339 0.1018  0.0624  0.0146  214 SER   B C    
3508 O  O    . SER   B 215 ? 0.4907 0.5789 0.3403 0.0932  0.0604  0.0146  214 SER   B O    
3509 C  CB   . SER   B 215 ? 0.496  0.636  0.359  0.1202  0.0814  0.0094  214 SER   B CB   
3510 O  OG   . SER   B 215 ? 0.525  0.7004 0.3998 0.1249  0.0929  0.0067  214 SER   B OG   
3511 N  N    . CYS   B 216 ? 0.4443 0.5828 0.3187 0.1128  0.0554  0.0167  215 CYS   B N    
3512 C  CA   . CYS   B 216 ? 0.4508 0.5627 0.3143 0.114   0.0459  0.0191  215 CYS   B CA   
3513 C  C    . CYS   B 216 ? 0.4547 0.5558 0.3102 0.1384  0.044   0.0212  215 CYS   B C    
3514 O  O    . CYS   B 216 ? 0.4429 0.5768 0.3129 0.1525  0.0425  0.0231  215 CYS   B O    
3515 C  CB   . CYS   B 216 ? 0.4434 0.5794 0.3197 0.1015  0.0381  0.0207  215 CYS   B CB   
3516 S  SG   . CYS   B 216 ? 0.4723 0.576  0.3331 0.0975  0.0284  0.0229  215 CYS   B SG   
3517 N  N    . LEU   B 217 ? 0.4698 0.5258 0.3021 0.1434  0.0437  0.0211  216 LEU   B N    
3518 C  CA   . LEU   B 217 ? 0.4788 0.515  0.2979 0.1659  0.0424  0.0233  216 LEU   B CA   
3519 C  C    . LEU   B 217 ? 0.4914 0.5148 0.3031 0.1652  0.0322  0.0286  216 LEU   B C    
3520 O  O    . LEU   B 217 ? 0.5097 0.5068 0.3092 0.1503  0.0296  0.0284  216 LEU   B O    
3521 C  CB   . LEU   B 217 ? 0.4941 0.4852 0.2879 0.1697  0.0484  0.0197  216 LEU   B CB   
3522 C  CG   . LEU   B 217 ? 0.5068 0.4689 0.2818 0.1928  0.0487  0.0212  216 LEU   B CG   
3523 C  CD1  . LEU   B 217 ? 0.4838 0.4744 0.2717 0.2166  0.0546  0.0204  216 LEU   B CD1  
3524 C  CD2  . LEU   B 217 ? 0.5387 0.4492 0.2838 0.1892  0.0529  0.0171  216 LEU   B CD2  
3525 N  N    . CYS   B 218 ? 0.4823 0.5252 0.3006 0.1818  0.0266  0.0336  217 CYS   B N    
3526 C  CA   . CYS   B 218 ? 0.4999 0.5324 0.3085 0.1825  0.0162  0.0399  217 CYS   B CA   
3527 C  C    . CYS   B 218 ? 0.5225 0.5299 0.3133 0.2083  0.0138  0.0456  217 CYS   B C    
3528 O  O    . CYS   B 218 ? 0.5094 0.5445 0.3107 0.226   0.0078  0.0509  217 CYS   B O    
3529 C  CB   . CYS   B 218 ? 0.4832 0.5634 0.3138 0.175   0.0085  0.0421  217 CYS   B CB   
3530 S  SG   . CYS   B 218 ? 0.5444 0.6418 0.3886 0.1431  0.011   0.0358  217 CYS   B SG   
3531 N  N    . PRO   B 219 ? 0.5539 0.5083 0.3165 0.2108  0.0177  0.0448  218 PRO   B N    
3532 C  CA   . PRO   B 219 ? 0.5798 0.5008 0.3197 0.2348  0.0156  0.0507  218 PRO   B CA   
3533 C  C    . PRO   B 219 ? 0.5979 0.4999 0.3205 0.231   0.0054  0.0595  218 PRO   B C    
3534 O  O    . PRO   B 219 ? 0.5963 0.4978 0.3177 0.2074  0.0025  0.0589  218 PRO   B O    
3535 C  CB   . PRO   B 219 ? 0.614  0.4821 0.3271 0.2326  0.0245  0.0451  218 PRO   B CB   
3536 C  CG   . PRO   B 219 ? 0.6088 0.4875 0.3327 0.2073  0.0296  0.0372  218 PRO   B CG   
3537 C  CD   . PRO   B 219 ? 0.5622 0.4837 0.3109 0.1916  0.0236  0.0389  218 PRO   B CD   
3538 N  N    . VAL   B 220 ? 0.6141 0.498  0.3208 0.2556  0.0005  0.0677  219 VAL   B N    
3539 C  CA   . VAL   B 220 ? 0.6444 0.4983 0.3254 0.2542  -0.0081 0.0773  219 VAL   B CA   
3540 C  C    . VAL   B 220 ? 0.6877 0.473  0.3316 0.245   -0.0012 0.0754  219 VAL   B C    
3541 O  O    . VAL   B 220 ? 0.7008 0.4758 0.3463 0.2338  0.0078  0.066   219 VAL   B O    
3542 C  CB   . VAL   B 220 ? 0.6584 0.5219 0.3368 0.2852  -0.0175 0.0886  219 VAL   B CB   
3543 C  CG1  . VAL   B 220 ? 0.6334 0.57   0.3502 0.2901  -0.0247 0.0894  219 VAL   B CG1  
3544 C  CG2  . VAL   B 220 ? 0.6773 0.508  0.341  0.3151  -0.0112 0.089   219 VAL   B CG2  
3545 N  N    . PHE   B 221 ? 0.7193 0.4595 0.3297 0.2465  -0.0054 0.084   220 PHE   B N    
3546 C  CA   . PHE   B 221 ? 0.7633 0.4403 0.3378 0.2347  0.0009  0.0822  220 PHE   B CA   
3547 C  C    . PHE   B 221 ? 0.7867 0.4314 0.3494 0.2488  0.0105  0.0753  220 PHE   B C    
3548 O  O    . PHE   B 221 ? 0.7965 0.4312 0.3533 0.2792  0.0109  0.0785  220 PHE   B O    
3549 C  CB   . PHE   B 221 ? 0.7867 0.4194 0.3242 0.2375  -0.0052 0.0945  220 PHE   B CB   
3550 C  CG   . PHE   B 221 ? 0.8275 0.3979 0.3277 0.2181  0.0014  0.0929  220 PHE   B CG   
3551 C  CD1  . PHE   B 221 ? 0.8309 0.4041 0.3315 0.1848  0.0037  0.0889  220 PHE   B CD1  
3552 C  CD2  . PHE   B 221 ? 0.8684 0.3779 0.3332 0.2326  0.0058  0.0946  220 PHE   B CD2  
3553 C  CE1  . PHE   B 221 ? 0.8686 0.3902 0.3372 0.1649  0.0097  0.0871  220 PHE   B CE1  
3554 C  CE2  . PHE   B 221 ? 0.9071 0.3589 0.3359 0.2111  0.0118  0.0926  220 PHE   B CE2  
3555 C  CZ   . PHE   B 221 ? 0.9007 0.3621 0.3335 0.1766  0.0136  0.0887  220 PHE   B CZ   
3556 N  N    . VAL   B 222 ? 0.7914 0.4211 0.3504 0.2271  0.0182  0.0654  221 VAL   B N    
3557 C  CA   . VAL   B 222 ? 0.8108 0.4054 0.353  0.2339  0.0275  0.0571  221 VAL   B CA   
3558 C  C    . VAL   B 222 ? 0.8581 0.3885 0.3591 0.2149  0.03    0.0571  221 VAL   B C    
3559 O  O    . VAL   B 222 ? 0.8607 0.394  0.3618 0.1865  0.0281  0.057   221 VAL   B O    
3560 C  CB   . VAL   B 222 ? 0.7858 0.4149 0.354  0.2225  0.0339  0.0454  221 VAL   B CB   
3561 C  CG1  . VAL   B 222 ? 0.7962 0.3917 0.3454 0.2345  0.0435  0.037   221 VAL   B CG1  
3562 C  CG2  . VAL   B 222 ? 0.7559 0.4533 0.3666 0.2304  0.0311  0.0458  221 VAL   B CG2  
3563 N  N    . ASN   B 223 ? 0.8925 0.3652 0.3579 0.2303  0.0348  0.0569  222 ASN   B N    
3564 C  CA   . ASN   B 223 ? 0.9522 0.3568 0.373  0.2129  0.0379  0.0567  222 ASN   B CA   
3565 C  C    . ASN   B 223 ? 0.9641 0.3619 0.3823 0.185   0.0442  0.0437  222 ASN   B C    
3566 O  O    . ASN   B 223 ? 1.0047 0.3606 0.3973 0.1889  0.0513  0.0358  222 ASN   B O    
3567 C  CB   . ASN   B 223 ? 1.0203 0.3633 0.4028 0.2418  0.0413  0.0602  222 ASN   B CB   
3568 C  CG   . ASN   B 223 ? 1.1253 0.3879 0.4551 0.2255  0.0458  0.0592  222 ASN   B CG   
3569 O  OD1  . ASN   B 223 ? 1.1588 0.4021 0.4715 0.1995  0.0429  0.0647  222 ASN   B OD1  
3570 N  ND2  . ASN   B 223 ? 1.1653 0.3797 0.4676 0.2393  0.0541  0.0513  222 ASN   B ND2  
3571 N  N    . THR   B 224 ? 0.9276 0.3669 0.3718 0.1581  0.0416  0.0411  223 THR   B N    
3572 C  CA   . THR   B 224 ? 0.9251 0.3661 0.3708 0.1323  0.0453  0.0301  223 THR   B CA   
3573 C  C    . THR   B 224 ? 0.9326 0.3565 0.3639 0.0987  0.044   0.0308  223 THR   B C    
3574 O  O    . THR   B 224 ? 0.9433 0.3706 0.3757 0.076   0.0457  0.0224  223 THR   B O    
3575 C  CB   . THR   B 224 ? 0.9013 0.4093 0.3922 0.1286  0.0437  0.0258  223 THR   B CB   
3576 O  OG1  . THR   B 224 ? 0.8991 0.4454 0.4144 0.1212  0.0378  0.0326  223 THR   B OG1  
3577 C  CG2  . THR   B 224 ? 0.8871 0.4197 0.3956 0.1556  0.0466  0.0233  223 THR   B CG2  
3578 N  N    . GLY   B 225 ? 0.9234 0.336  0.3441 0.095   0.0408  0.0406  224 GLY   B N    
3579 C  CA   . GLY   B 225 ? 0.9261 0.3308 0.3369 0.0633  0.0406  0.042   224 GLY   B CA   
3580 C  C    . GLY   B 225 ? 0.8906 0.358  0.342  0.0505  0.0374  0.0421  224 GLY   B C    
3581 O  O    . GLY   B 225 ? 0.8913 0.3621 0.3408 0.0252  0.0382  0.0425  224 GLY   B O    
3582 N  N    . PHE   B 226 ? 0.8562 0.3735 0.3441 0.0667  0.0346  0.0409  225 PHE   B N    
3583 C  CA   . PHE   B 226 ? 0.8242 0.3972 0.3491 0.0573  0.032   0.0403  225 PHE   B CA   
3584 C  C    . PHE   B 226 ? 0.8651 0.4391 0.3837 0.0509  0.0299  0.0487  225 PHE   B C    
3585 O  O    . PHE   B 226 ? 0.8651 0.4617 0.3963 0.0309  0.031   0.047   225 PHE   B O    
3586 C  CB   . PHE   B 226 ? 0.7719 0.3865 0.3282 0.0777  0.0299  0.0388  225 PHE   B CB   
3587 C  CG   . PHE   B 226 ? 0.7231 0.39   0.3156 0.0687  0.028   0.0365  225 PHE   B CG   
3588 C  CD1  . PHE   B 226 ? 0.7106 0.395  0.3182 0.0518  0.0296  0.0296  225 PHE   B CD1  
3589 C  CD2  . PHE   B 226 ? 0.7006 0.398  0.3105 0.078   0.0242  0.0411  225 PHE   B CD2  
3590 C  CE1  . PHE   B 226 ? 0.6916 0.4185 0.33   0.0463  0.0284  0.0277  225 PHE   B CE1  
3591 C  CE2  . PHE   B 226 ? 0.6832 0.422  0.3223 0.0695  0.0234  0.038   225 PHE   B CE2  
3592 C  CZ   . PHE   B 226 ? 0.6767 0.4279 0.3293 0.0546  0.0259  0.0315  225 PHE   B CZ   
3593 N  N    . THR   B 227 ? 0.9007 0.4491 0.3977 0.0688  0.0271  0.0577  226 THR   B N    
3594 C  CA   . THR   B 227 ? 0.9346 0.4739 0.4154 0.0654  0.0243  0.0676  226 THR   B CA   
3595 C  C    . THR   B 227 ? 0.9884 0.4637 0.4235 0.075   0.0244  0.0758  226 THR   B C    
3596 O  O    . THR   B 227 ? 0.9984 0.4487 0.4231 0.0945  0.0251  0.0745  226 THR   B O    
3597 C  CB   . THR   B 227 ? 0.9504 0.5353 0.4569 0.0798  0.0178  0.0718  226 THR   B CB   
3598 O  OG1  . THR   B 227 ? 0.9833 0.5887 0.5095 0.1043  0.0152  0.0698  226 THR   B OG1  
3599 C  CG2  . THR   B 227 ? 0.9252 0.5574 0.4626 0.0615  0.0191  0.0657  226 THR   B CG2  
3600 N  N    . LYS   B 228 ? 1.0227 0.4676 0.4275 0.0607  0.0249  0.0839  227 LYS   B N    
3601 C  CA   . LYS   B 228 ? 1.0718 0.4477 0.4276 0.067   0.0256  0.0924  227 LYS   B CA   
3602 C  C    . LYS   B 228 ? 1.1032 0.4633 0.4474 0.1036  0.0187  0.1026  227 LYS   B C    
3603 O  O    . LYS   B 228 ? 1.1408 0.4495 0.456  0.1196  0.0203  0.1045  227 LYS   B O    
3604 C  CB   . LYS   B 228 ? 1.1068 0.4547 0.4315 0.0409  0.0284  0.0994  227 LYS   B CB   
3605 C  CG   . LYS   B 228 ? 1.1368 0.484  0.4618 0.0046  0.0366  0.0901  227 LYS   B CG   
3606 C  CD   . LYS   B 228 ? 1.1997 0.5156 0.4898 -0.0207 0.0408  0.0979  227 LYS   B CD   
3607 C  CE   . LYS   B 228 ? 1.2431 0.5543 0.5297 -0.0566 0.0491  0.0894  227 LYS   B CE   
3608 N  NZ   . LYS   B 228 ? 1.3021 0.5548 0.556  -0.0602 0.0518  0.0861  227 LYS   B NZ   
3609 N  N    . ASN   B 229 ? 1.096  0.4977 0.4602 0.1169  0.0109  0.1092  228 ASN   B N    
3610 C  CA   . ASN   B 229 ? 1.1257 0.5198 0.4811 0.1517  0.0024  0.1204  228 ASN   B CA   
3611 C  C    . ASN   B 229 ? 1.1019 0.5684 0.5028 0.1662  -0.0051 0.1193  228 ASN   B C    
3612 O  O    . ASN   B 229 ? 1.0724 0.5845 0.5006 0.1462  -0.0045 0.1131  228 ASN   B O    
3613 C  CB   . ASN   B 229 ? 1.1829 0.537  0.4961 0.1485  -0.0023 0.136   228 ASN   B CB   
3614 C  CG   . ASN   B 229 ? 1.2917 0.5688 0.5535 0.1327  0.0047  0.1397  228 ASN   B CG   
3615 O  OD1  . ASN   B 229 ? 1.343  0.5689 0.5802 0.1475  0.0078  0.1393  228 ASN   B OD1  
3616 N  ND2  . ASN   B 229 ? 1.3136 0.5799 0.5565 0.1012  0.0082  0.1426  228 ASN   B ND2  
3617 N  N    . PRO   B 230 ? 1.1107 0.5895 0.5195 0.2004  -0.0123 0.1253  229 PRO   B N    
3618 C  CA   . PRO   B 230 ? 1.0893 0.6385 0.5391 0.2104  -0.0203 0.125   229 PRO   B CA   
3619 C  C    . PRO   B 230 ? 1.111  0.6762 0.5531 0.1964  -0.0281 0.1333  229 PRO   B C    
3620 O  O    . PRO   B 230 ? 1.1349 0.6545 0.5366 0.1914  -0.0298 0.1439  229 PRO   B O    
3621 C  CB   . PRO   B 230 ? 1.091  0.6417 0.5425 0.2505  -0.0267 0.1323  229 PRO   B CB   
3622 C  CG   . PRO   B 230 ? 1.1228 0.6071 0.5413 0.2619  -0.019  0.1318  229 PRO   B CG   
3623 C  CD   . PRO   B 230 ? 1.1302 0.5607 0.5107 0.2315  -0.0136 0.1329  229 PRO   B CD   
3624 N  N    . SER   B 231 ? 1.0993 0.7261 0.5767 0.1884  -0.032  0.1283  230 SER   B N    
3625 C  CA   . SER   B 231 ? 1.1171 0.7622 0.5875 0.1741  -0.0387 0.134   230 SER   B CA   
3626 C  C    . SER   B 231 ? 1.1344 0.7898 0.5943 0.1978  -0.0535 0.1484  230 SER   B C    
3627 O  O    . SER   B 231 ? 1.1437 0.7983 0.5834 0.1874  -0.0598 0.1561  230 SER   B O    
3628 C  CB   . SER   B 231 ? 1.1058 0.8078 0.6145 0.1558  -0.0368 0.122   230 SER   B CB   
3629 O  OG   . SER   B 231 ? 1.1105 0.8622 0.6536 0.1735  -0.0433 0.1197  230 SER   B OG   
3630 N  N    . THR   B 232 ? 1.1337 0.8061 0.6105 0.2292  -0.0591 0.1511  231 THR   B N    
3631 C  CA   . THR   B 232 ? 1.1442 0.834  0.618  0.258   -0.0743 0.1648  231 THR   B CA   
3632 C  C    . THR   B 232 ? 1.19   0.826  0.6359 0.2901  -0.0746 0.1748  231 THR   B C    
3633 O  O    . THR   B 232 ? 1.2044 0.7995 0.6409 0.2897  -0.0625 0.1681  231 THR   B O    
3634 C  CB   . THR   B 232 ? 1.1146 0.8824 0.6383 0.2683  -0.0809 0.1589  231 THR   B CB   
3635 O  OG1  . THR   B 232 ? 1.1182 0.8938 0.6644 0.2918  -0.0753 0.1537  231 THR   B OG1  
3636 C  CG2  . THR   B 232 ? 1.0915 0.9032 0.6432 0.2363  -0.0766 0.1455  231 THR   B CG2  
3637 N  N    . ARG   B 233 ? 1.211  0.8471 0.6431 0.3186  -0.0887 0.1906  232 ARG   B N    
3638 C  CA   . ARG   B 233 ? 1.2574 0.8395 0.6606 0.3527  -0.0896 0.2012  232 ARG   B CA   
3639 C  C    . ARG   B 233 ? 1.2347 0.8604 0.6752 0.3905  -0.0929 0.1995  232 ARG   B C    
3640 O  O    . ARG   B 233 ? 1.2125 0.875  0.691  0.3865  -0.0836 0.1844  232 ARG   B O    
3641 C  CB   . ARG   B 233 ? 1.3142 0.8577 0.6714 0.3626  -0.1026 0.2219  232 ARG   B CB   
3642 C  CG   . ARG   B 233 ? 1.4063 0.9066 0.724  0.3245  -0.0978 0.2241  232 ARG   B CG   
3643 C  CD   . ARG   B 233 ? 1.5114 0.9595 0.7747 0.3355  -0.1088 0.2459  232 ARG   B CD   
3644 N  NE   . ARG   B 233 ? 1.6008 0.997  0.8211 0.2991  -0.1005 0.2478  232 ARG   B NE   
3645 C  CZ   . ARG   B 233 ? 1.6805 1.0219 0.8458 0.2987  -0.1064 0.2658  232 ARG   B CZ   
3646 N  NH1  . ARG   B 233 ? 1.6923 1.0214 0.8378 0.3348  -0.1223 0.2846  232 ARG   B NH1  
3647 N  NH2  . ARG   B 233 ? 1.709  1.009  0.8388 0.2623  -0.0966 0.2658  232 ARG   B NH2  
3648 N  N    . ILE   B 237 ? 1.066  0.6474 0.5762 0.3773  -0.0077 0.1129  236 ILE   B N    
3649 C  CA   . ILE   B 237 ? 1.1124 0.6216 0.5846 0.366   0.0038  0.1057  236 ILE   B CA   
3650 C  C    . ILE   B 237 ? 1.1024 0.6192 0.5889 0.3745  0.0167  0.0909  236 ILE   B C    
3651 O  O    . ILE   B 237 ? 1.1333 0.6102 0.5991 0.4022  0.0234  0.0893  236 ILE   B O    
3652 C  CB   . ILE   B 237 ? 1.1748 0.604  0.5943 0.3834  0.0019  0.117   236 ILE   B CB   
3653 C  CG1  . ILE   B 237 ? 1.1943 0.6338 0.6173 0.4314  -0.006  0.1291  236 ILE   B CG1  
3654 C  CG2  . ILE   B 237 ? 1.1985 0.5998 0.5907 0.3539  -0.0048 0.1264  236 ILE   B CG2  
3655 C  CD1  . ILE   B 237 ? 1.2297 0.628  0.6363 0.4715  0.0041  0.1248  236 ILE   B CD1  
3656 N  N    . LEU   B 238 ? 1.057  0.6231 0.5769 0.3507  0.0206  0.0802  237 LEU   B N    
3657 C  CA   . LEU   B 238 ? 1.033  0.6136 0.5677 0.3544  0.0325  0.0665  237 LEU   B CA   
3658 C  C    . LEU   B 238 ? 1.05   0.5689 0.5496 0.3362  0.0425  0.0566  237 LEU   B C    
3659 O  O    . LEU   B 238 ? 1.0688 0.5548 0.5466 0.3077  0.0403  0.0576  237 LEU   B O    
3660 C  CB   . LEU   B 238 ? 0.9962 0.6496 0.5762 0.3341  0.0321  0.0603  237 LEU   B CB   
3661 C  CG   . LEU   B 238 ? 0.9793 0.7023 0.5979 0.3427  0.0225  0.0674  237 LEU   B CG   
3662 C  CD1  . LEU   B 238 ? 0.9573 0.7323 0.6085 0.314   0.0226  0.0611  237 LEU   B CD1  
3663 C  CD2  . LEU   B 238 ? 0.9683 0.724  0.6071 0.3791  0.0255  0.0674  237 LEU   B CD2  
3664 N  N    . GLU   B 239 ? 1.0397 0.5491 0.5362 0.3502  0.0538  0.0459  238 GLU   B N    
3665 C  CA   . GLU   B 239 ? 1.0568 0.5147 0.5219 0.3317  0.0632  0.0344  238 GLU   B CA   
3666 C  C    . GLU   B 239 ? 1.0099 0.5163 0.5045 0.3092  0.0675  0.0238  238 GLU   B C    
3667 O  O    . GLU   B 239 ? 0.9782 0.5426 0.5087 0.3216  0.0697  0.0217  238 GLU   B O    
3668 C  CB   . GLU   B 239 ? 1.1186 0.5243 0.5524 0.3622  0.0738  0.0289  238 GLU   B CB   
3669 C  CG   . GLU   B 239 ? 1.2256 0.5659 0.6195 0.3812  0.0702  0.0393  238 GLU   B CG   
3670 C  CD   . GLU   B 239 ? 1.3652 0.6493 0.7218 0.3483  0.0657  0.0433  238 GLU   B CD   
3671 O  OE1  . GLU   B 239 ? 1.3925 0.6721 0.7441 0.3472  0.0556  0.0571  238 GLU   B OE1  
3672 O  OE2  . GLU   B 239 ? 1.4093 0.6566 0.7416 0.3223  0.0724  0.0324  238 GLU   B OE2  
3673 N  N    . THR   B 240 ? 1.0034 0.4876 0.4827 0.2756  0.0681  0.0179  239 THR   B N    
3674 C  CA   . THR   B 240 ? 0.9733 0.4961 0.4751 0.2524  0.0704  0.0095  239 THR   B CA   
3675 C  C    . THR   B 240 ? 0.9595 0.5144 0.479  0.2687  0.0799  0.0009  239 THR   B C    
3676 O  O    . THR   B 240 ? 0.9252 0.5386 0.4806 0.2619  0.0788  0.0007  239 THR   B O    
3677 C  CB   . THR   B 240 ? 1.0012 0.4808 0.4731 0.2219  0.0716  0.0025  239 THR   B CB   
3678 O  OG1  . THR   B 240 ? 1.0215 0.4714 0.4757 0.2056  0.0647  0.0099  239 THR   B OG1  
3679 C  CG2  . THR   B 240 ? 0.9852 0.5055 0.4803 0.1977  0.0711  -0.0035 239 THR   B CG2  
3680 N  N    . ASP   B 241 ? 0.9878 0.5017 0.4795 0.2895  0.0903  -0.0064 240 ASP   B N    
3681 C  CA   . ASP   B 241 ? 0.9839 0.518  0.4836 0.3065  0.1025  -0.0162 240 ASP   B CA   
3682 C  C    . ASP   B 241 ? 0.9412 0.5401 0.4829 0.3322  0.1032  -0.0113 240 ASP   B C    
3683 O  O    . ASP   B 241 ? 0.9275 0.5688 0.4909 0.3344  0.1112  -0.0177 240 ASP   B O    
3684 C  CB   . ASP   B 241 ? 1.0533 0.52   0.5082 0.3248  0.1137  -0.0252 240 ASP   B CB   
3685 C  CG   . ASP   B 241 ? 1.1506 0.5677 0.5805 0.3483  0.1109  -0.0173 240 ASP   B CG   
3686 O  OD1  . ASP   B 241 ? 1.1685 0.5508 0.579  0.3297  0.1019  -0.0103 240 ASP   B OD1  
3687 O  OD2  . ASP   B 241 ? 1.2    0.613  0.6291 0.3859  0.118   -0.0177 240 ASP   B OD2  
3688 N  N    . THR   B 242 ? 0.9171 0.5251 0.4695 0.3503  0.0947  0.0003  241 THR   B N    
3689 C  CA   . THR   B 242 ? 0.87   0.5445 0.4642 0.373   0.0926  0.0061  241 THR   B CA   
3690 C  C    . THR   B 242 ? 0.8228 0.5614 0.4556 0.3464  0.0863  0.0083  241 THR   B C    
3691 O  O    . THR   B 242 ? 0.8041 0.6013 0.4703 0.3522  0.0909  0.006   241 THR   B O    
3692 C  CB   . THR   B 242 ? 0.89   0.5531 0.4805 0.3956  0.0823  0.0191  241 THR   B CB   
3693 O  OG1  . THR   B 242 ? 0.9571 0.5545 0.5085 0.4214  0.089   0.0172  241 THR   B OG1  
3694 C  CG2  . THR   B 242 ? 0.8469 0.583  0.4814 0.4176  0.0777  0.0258  241 THR   B CG2  
3695 N  N    . VAL   B 243 ? 0.8054 0.5316 0.4324 0.317   0.0768  0.0124  242 VAL   B N    
3696 C  CA   . VAL   B 243 ? 0.7677 0.5441 0.4257 0.2917  0.0706  0.0145  242 VAL   B CA   
3697 C  C    . VAL   B 243 ? 0.7589 0.5532 0.4246 0.2758  0.0795  0.0049  242 VAL   B C    
3698 O  O    . VAL   B 243 ? 0.7316 0.5804 0.4293 0.2693  0.0799  0.0051  242 VAL   B O    
3699 C  CB   . VAL   B 243 ? 0.782  0.5341 0.4277 0.2674  0.0602  0.0202  242 VAL   B CB   
3700 C  CG1  . VAL   B 243 ? 0.7614 0.5601 0.4366 0.2425  0.0547  0.0215  242 VAL   B CG1  
3701 C  CG2  . VAL   B 243 ? 0.7933 0.527  0.4279 0.2836  0.0519  0.0307  242 VAL   B CG2  
3702 N  N    . ALA   B 244 ? 0.7811 0.5287 0.4151 0.2696  0.0867  -0.0034 243 ALA   B N    
3703 C  CA   . ALA   B 244 ? 0.7775 0.5363 0.412  0.2555  0.0949  -0.0122 243 ALA   B CA   
3704 C  C    . ALA   B 244 ? 0.7586 0.5548 0.4107 0.2772  0.1067  -0.0168 243 ALA   B C    
3705 O  O    . ALA   B 244 ? 0.7347 0.5709 0.4064 0.2655  0.1109  -0.0192 243 ALA   B O    
3706 C  CB   . ALA   B 244 ? 0.8083 0.5077 0.4017 0.2452  0.0989  -0.0201 243 ALA   B CB   
3707 N  N    . ARG   B 245 ? 0.7697 0.555  0.4159 0.3092  0.1122  -0.0173 244 ARG   B N    
3708 C  CA   . ARG   B 245 ? 0.7675 0.5941 0.4342 0.333   0.1241  -0.0217 244 ARG   B CA   
3709 C  C    . ARG   B 245 ? 0.7276 0.6286 0.4414 0.331   0.1183  -0.0143 244 ARG   B C    
3710 O  O    . ARG   B 245 ? 0.7125 0.6607 0.4489 0.3275  0.1268  -0.0182 244 ARG   B O    
3711 C  CB   . ARG   B 245 ? 0.8236 0.6203 0.4738 0.3711  0.1305  -0.0233 244 ARG   B CB   
3712 C  CG   . ARG   B 245 ? 0.9482 0.7172 0.573  0.3831  0.1482  -0.0368 244 ARG   B CG   
3713 C  CD   . ARG   B 245 ? 1.0559 0.7943 0.6642 0.4246  0.1567  -0.0396 244 ARG   B CD   
3714 N  NE   . ARG   B 245 ? 1.1707 0.8276 0.7341 0.4275  0.1516  -0.0382 244 ARG   B NE   
3715 C  CZ   . ARG   B 245 ? 1.2266 0.8653 0.7874 0.4433  0.1406  -0.0269 244 ARG   B CZ   
3716 N  NH1  . ARG   B 245 ? 1.1893 0.8877 0.7907 0.4582  0.1322  -0.0161 244 ARG   B NH1  
3717 N  NH2  . ARG   B 245 ? 1.2756 0.8358 0.7912 0.4426  0.1376  -0.0259 244 ARG   B NH2  
3718 N  N    . SER   B 246 ? 0.7108 0.621  0.4368 0.3299  0.1042  -0.004  245 SER   B N    
3719 C  CA   . SER   B 246 ? 0.6752 0.6523 0.4421 0.3247  0.097   0.0025  245 SER   B CA   
3720 C  C    . SER   B 246 ? 0.665  0.6681 0.4456 0.2909  0.0969  0.0006  245 SER   B C    
3721 O  O    . SER   B 246 ? 0.6381 0.6978 0.4489 0.2867  0.1006  0.0002  245 SER   B O    
3722 C  CB   . SER   B 246 ? 0.6821 0.654  0.4508 0.3267  0.0812  0.0133  245 SER   B CB   
3723 O  OG   . SER   B 246 ? 0.7094 0.6903 0.4834 0.3619  0.08    0.0178  245 SER   B OG   
3724 N  N    . LEU   B 247 ? 0.6827 0.644  0.4402 0.267   0.0931  -0.0004 246 LEU   B N    
3725 C  CA   . LEU   B 247 ? 0.6809 0.6569 0.446  0.2371  0.0923  -0.0015 246 LEU   B CA   
3726 C  C    . LEU   B 247 ? 0.6954 0.689  0.462  0.2346  0.106   -0.0088 246 LEU   B C    
3727 O  O    . LEU   B 247 ? 0.6809 0.72   0.4719 0.2231  0.1082  -0.0077 246 LEU   B O    
3728 C  CB   . LEU   B 247 ? 0.7017 0.6295 0.4413 0.2168  0.0855  -0.0013 246 LEU   B CB   
3729 C  CG   . LEU   B 247 ? 0.7124 0.6499 0.457  0.1887  0.0841  -0.0019 246 LEU   B CG   
3730 C  CD1  . LEU   B 247 ? 0.6957 0.679  0.4712 0.1777  0.0788  0.0032  246 LEU   B CD1  
3731 C  CD2  . LEU   B 247 ? 0.733  0.6291 0.4561 0.172   0.0772  -0.0017 246 LEU   B CD2  
3732 N  N    . ILE   B 248 ? 0.7233 0.681  0.4622 0.2445  0.116   -0.0164 247 ILE   B N    
3733 C  CA   . ILE   B 248 ? 0.7334 0.7054 0.4692 0.2413  0.1298  -0.0237 247 ILE   B CA   
3734 C  C    . ILE   B 248 ? 0.7188 0.7503 0.4864 0.2566  0.1392  -0.0243 247 ILE   B C    
3735 O  O    . ILE   B 248 ? 0.7125 0.7789 0.4934 0.2419  0.146   -0.0254 247 ILE   B O    
3736 C  CB   . ILE   B 248 ? 0.7732 0.6931 0.4695 0.2483  0.139   -0.0331 247 ILE   B CB   
3737 C  CG1  . ILE   B 248 ? 0.7918 0.7184 0.4773 0.2324  0.1493  -0.0392 247 ILE   B CG1  
3738 C  CG2  . ILE   B 248 ? 0.7831 0.6927 0.4727 0.2828  0.1485  -0.038  247 ILE   B CG2  
3739 C  CD1  . ILE   B 248 ? 0.8171 0.7306 0.4941 0.2028  0.1397  -0.0356 247 ILE   B CD1  
3740 N  N    . ASP   B 249 ? 0.7087 0.7545 0.4897 0.2848  0.1386  -0.0223 248 ASP   B N    
3741 C  CA   . ASP   B 249 ? 0.6774 0.7872 0.493  0.3014  0.1464  -0.0226 248 ASP   B CA   
3742 C  C    . ASP   B 249 ? 0.6322 0.7981 0.4823 0.2792  0.1391  -0.0162 248 ASP   B C    
3743 O  O    . ASP   B 249 ? 0.612  0.8292 0.4849 0.2746  0.149   -0.0186 248 ASP   B O    
3744 C  CB   . ASP   B 249 ? 0.7119 0.8233 0.5337 0.3387  0.145   -0.0207 248 ASP   B CB   
3745 C  CG   . ASP   B 249 ? 0.8372 0.9002 0.6268 0.3641  0.1578  -0.0295 248 ASP   B CG   
3746 O  OD1  . ASP   B 249 ? 0.8501 0.9109 0.6278 0.36    0.1733  -0.039  248 ASP   B OD1  
3747 O  OD2  . ASP   B 249 ? 0.9043 0.9284 0.6772 0.3874  0.1527  -0.027  248 ASP   B OD2  
3748 N  N    . GLY   B 250 ? 0.6154 0.7684 0.4661 0.2634  0.1232  -0.009  249 GLY   B N    
3749 C  CA   . GLY   B 250 ? 0.5816 0.7767 0.4584 0.2396  0.1156  -0.0039 249 GLY   B CA   
3750 C  C    . GLY   B 250 ? 0.5696 0.7647 0.4411 0.2098  0.1214  -0.0061 249 GLY   B C    
3751 O  O    . GLY   B 250 ? 0.551  0.793  0.4457 0.1952  0.1247  -0.0053 249 GLY   B O    
3752 N  N    . ILE   B 251 ? 0.5775 0.72   0.4172 0.1999  0.1223  -0.0086 250 ILE   B N    
3753 C  CA   . ILE   B 251 ? 0.5687 0.7043 0.3981 0.1743  0.1266  -0.0095 250 ILE   B CA   
3754 C  C    . ILE   B 251 ? 0.5646 0.7323 0.3992 0.1758  0.1436  -0.0145 250 ILE   B C    
3755 O  O    . ILE   B 251 ? 0.5554 0.7522 0.4017 0.1554  0.1474  -0.0126 250 ILE   B O    
3756 C  CB   . ILE   B 251 ? 0.5823 0.6582 0.3767 0.1673  0.123   -0.0112 250 ILE   B CB   
3757 C  CG1  . ILE   B 251 ? 0.5839 0.6338 0.3754 0.1609  0.1074  -0.006  250 ILE   B CG1  
3758 C  CG2  . ILE   B 251 ? 0.5848 0.6542 0.3656 0.145   0.1278  -0.0116 250 ILE   B CG2  
3759 C  CD1  . ILE   B 251 ? 0.61   0.6067 0.3706 0.1557  0.1031  -0.0078 250 ILE   B CD1  
3760 N  N    . LEU   B 252 ? 0.57   0.732  0.3952 0.1998  0.1547  -0.0212 251 LEU   B N    
3761 C  CA   . LEU   B 252 ? 0.5675 0.7596 0.3959 0.2038  0.173   -0.0274 251 LEU   B CA   
3762 C  C    . LEU   B 252 ? 0.5467 0.8109 0.4158 0.2035  0.178   -0.0254 251 LEU   B C    
3763 O  O    . LEU   B 252 ? 0.5465 0.8429 0.4215 0.1943  0.1924  -0.0286 251 LEU   B O    
3764 C  CB   . LEU   B 252 ? 0.5839 0.751  0.3923 0.2327  0.1842  -0.0362 251 LEU   B CB   
3765 C  CG   . LEU   B 252 ? 0.6364 0.733  0.4006 0.23    0.1816  -0.0402 251 LEU   B CG   
3766 C  CD1  . LEU   B 252 ? 0.6526 0.7245 0.3955 0.2575  0.1947  -0.0503 251 LEU   B CD1  
3767 C  CD2  . LEU   B 252 ? 0.6517 0.7325 0.3945 0.2011  0.1835  -0.0403 251 LEU   B CD2  
3768 N  N    . THR   B 253 ? 0.5296 0.8212 0.4259 0.2118  0.1662  -0.0202 252 THR   B N    
3769 C  CA   . THR   B 253 ? 0.4974 0.8621 0.4344 0.2094  0.1682  -0.0182 252 THR   B CA   
3770 C  C    . THR   B 253 ? 0.4948 0.8753 0.4446 0.1771  0.1566  -0.0116 252 THR   B C    
3771 O  O    . THR   B 253 ? 0.476  0.9154 0.4582 0.171   0.1557  -0.0098 252 THR   B O    
3772 C  CB   . THR   B 253 ? 0.489  0.8845 0.4499 0.2427  0.1637  -0.0173 252 THR   B CB   
3773 O  OG1  . THR   B 253 ? 0.5139 0.8753 0.4667 0.2469  0.1453  -0.0111 252 THR   B OG1  
3774 C  CG2  . THR   B 253 ? 0.5016 0.8867 0.4525 0.2766  0.1777  -0.0245 252 THR   B CG2  
3775 N  N    . ASN   B 254 ? 0.5096 0.8388 0.4342 0.1569  0.1482  -0.0086 253 ASN   B N    
3776 C  CA   . ASN   B 254 ? 0.4998 0.8293 0.4291 0.128   0.1378  -0.0033 253 ASN   B CA   
3777 C  C    . ASN   B 254 ? 0.4796 0.8334 0.4315 0.1315  0.1234  0.0007  253 ASN   B C    
3778 O  O    . ASN   B 254 ? 0.4707 0.8537 0.4388 0.1096  0.1191  0.003   253 ASN   B O    
3779 C  CB   . ASN   B 254 ? 0.4931 0.8532 0.4296 0.101   0.1481  -0.0032 253 ASN   B CB   
3780 C  CG   . ASN   B 254 ? 0.5625 0.8864 0.4687 0.0892  0.1581  -0.0043 253 ASN   B CG   
3781 O  OD1  . ASN   B 254 ? 0.5626 0.9094 0.4698 0.0725  0.1703  -0.0048 253 ASN   B OD1  
3782 N  ND2  . ASN   B 254 ? 0.6104 0.8779 0.4877 0.096   0.1528  -0.0045 253 ASN   B ND2  
3783 N  N    . LYS   B 255 ? 0.4703 0.8078 0.4194 0.1573  0.1155  0.0016  254 LYS   B N    
3784 C  CA   . LYS   B 255 ? 0.4474 0.8037 0.4129 0.1621  0.1008  0.0062  254 LYS   B CA   
3785 C  C    . LYS   B 255 ? 0.4661 0.7841 0.4163 0.1409  0.089   0.0094  254 LYS   B C    
3786 O  O    . LYS   B 255 ? 0.4976 0.7616 0.4213 0.1402  0.0879  0.0092  254 LYS   B O    
3787 C  CB   . LYS   B 255 ? 0.4617 0.8081 0.4248 0.1969  0.0968  0.0074  254 LYS   B CB   
3788 C  CG   . LYS   B 255 ? 0.4818 0.8882 0.4773 0.2107  0.0898  0.0107  254 LYS   B CG   
3789 C  CD   . LYS   B 255 ? 0.5641 0.9478 0.5509 0.2398  0.0795  0.0154  254 LYS   B CD   
3790 C  CE   . LYS   B 255 ? 0.5995 1.0324 0.6119 0.2446  0.0653  0.0215  254 LYS   B CE   
3791 N  NZ   . LYS   B 255 ? 0.6581 1.0502 0.6506 0.2541  0.0503  0.0281  254 LYS   B NZ   
3792 N  N    . LYS   B 256 ? 0.4428 0.7899 0.4094 0.1224  0.0808  0.0117  255 LYS   B N    
3793 C  CA   . LYS   B 256 ? 0.4546 0.7688 0.4078 0.1016  0.0713  0.0136  255 LYS   B CA   
3794 C  C    . LYS   B 256 ? 0.4573 0.7434 0.3999 0.1144  0.0588  0.0167  255 LYS   B C    
3795 O  O    . LYS   B 256 ? 0.4782 0.7194 0.4009 0.1056  0.055   0.0172  255 LYS   B O    
3796 C  CB   . LYS   B 256 ? 0.4633 0.8137 0.4332 0.0749  0.0688  0.0133  255 LYS   B CB   
3797 C  CG   . LYS   B 256 ? 0.524  0.8876 0.4959 0.0565  0.0818  0.0111  255 LYS   B CG   
3798 C  CD   . LYS   B 256 ? 0.5962 0.9813 0.5765 0.0252  0.0804  0.0106  255 LYS   B CD   
3799 C  CE   . LYS   B 256 ? 0.6782 1.0626 0.6522 0.0068  0.0943  0.0097  255 LYS   B CE   
3800 N  NZ   . LYS   B 256 ? 0.7211 1.1304 0.7033 -0.0254 0.0957  0.009   255 LYS   B NZ   
3801 N  N    . MET   B 257 ? 0.4393 0.7518 0.3944 0.1345  0.0523  0.0194  256 MET   B N    
3802 C  CA   . MET   B 257 ? 0.452  0.7359 0.3934 0.1462  0.0406  0.0237  256 MET   B CA   
3803 C  C    . MET   B 257 ? 0.4634 0.7405 0.4007 0.1791  0.0422  0.0257  256 MET   B C    
3804 O  O    . MET   B 257 ? 0.4518 0.7741 0.4103 0.1963  0.0424  0.027   256 MET   B O    
3805 C  CB   . MET   B 257 ? 0.4324 0.7487 0.3869 0.1361  0.028   0.0266  256 MET   B CB   
3806 C  CG   . MET   B 257 ? 0.4647 0.748  0.4006 0.1428  0.0164  0.0312  256 MET   B CG   
3807 S  SD   . MET   B 257 ? 0.4875 0.7065 0.3942 0.1244  0.0163  0.0295  256 MET   B SD   
3808 C  CE   . MET   B 257 ? 0.424  0.6611 0.3411 0.0913  0.019   0.0243  256 MET   B CE   
3809 N  N    . ILE   B 258 ? 0.4875 0.7092 0.3978 0.1877  0.0446  0.0253  257 ILE   B N    
3810 C  CA   . ILE   B 258 ? 0.5043 0.7066 0.4037 0.2182  0.0475  0.0264  257 ILE   B CA   
3811 C  C    . ILE   B 258 ? 0.5377 0.7067 0.4187 0.2283  0.0359  0.0328  257 ILE   B C    
3812 O  O    . ILE   B 258 ? 0.5658 0.6887 0.4238 0.2158  0.0336  0.0329  257 ILE   B O    
3813 C  CB   . ILE   B 258 ? 0.5195 0.68   0.397  0.2195  0.0597  0.0204  257 ILE   B CB   
3814 C  CG1  . ILE   B 258 ? 0.5001 0.6902 0.3912 0.2061  0.0715  0.0148  257 ILE   B CG1  
3815 C  CG2  . ILE   B 258 ? 0.5347 0.667  0.3957 0.2506  0.0641  0.02    257 ILE   B CG2  
3816 C  CD1  . ILE   B 258 ? 0.517  0.6642 0.3838 0.1938  0.079   0.0102  257 ILE   B CD1  
3817 N  N    . PHE   B 259 ? 0.5331 0.7265 0.424  0.2506  0.0285  0.0387  258 PHE   B N    
3818 C  CA   . PHE   B 259 ? 0.5682 0.728  0.438  0.2621  0.0176  0.0464  258 PHE   B CA   
3819 C  C    . PHE   B 259 ? 0.6097 0.7284 0.4581 0.2917  0.0229  0.0475  258 PHE   B C    
3820 O  O    . PHE   B 259 ? 0.5991 0.7419 0.4611 0.3143  0.0301  0.0452  258 PHE   B O    
3821 C  CB   . PHE   B 259 ? 0.5411 0.7493 0.4306 0.2699  0.0042  0.0538  258 PHE   B CB   
3822 C  CG   . PHE   B 259 ? 0.5364 0.7675 0.435  0.2391  -0.0034 0.0533  258 PHE   B CG   
3823 C  CD1  . PHE   B 259 ? 0.5736 0.764  0.4484 0.2222  -0.0091 0.0551  258 PHE   B CD1  
3824 C  CD2  . PHE   B 259 ? 0.5127 0.8048 0.4424 0.2258  -0.0038 0.0501  258 PHE   B CD2  
3825 C  CE1  . PHE   B 259 ? 0.5773 0.7853 0.4581 0.195   -0.0146 0.0532  258 PHE   B CE1  
3826 C  CE2  . PHE   B 259 ? 0.5194 0.8265 0.4533 0.1968  -0.0103 0.0486  258 PHE   B CE2  
3827 C  CZ   . PHE   B 259 ? 0.5445 0.8084 0.4535 0.1826  -0.0155 0.0499  258 PHE   B CZ   
3828 N  N    . VAL   B 260 ? 0.658  0.7142 0.4718 0.2914  0.0204  0.0503  259 VAL   B N    
3829 C  CA   . VAL   B 260 ? 0.6999 0.7085 0.4875 0.3185  0.0251  0.0514  259 VAL   B CA   
3830 C  C    . VAL   B 260 ? 0.7403 0.7193 0.5063 0.3299  0.013   0.0626  259 VAL   B C    
3831 O  O    . VAL   B 260 ? 0.7608 0.7032 0.5047 0.3096  0.0088  0.0647  259 VAL   B O    
3832 C  CB   . VAL   B 260 ? 0.7301 0.6825 0.4896 0.3076  0.0361  0.0433  259 VAL   B CB   
3833 C  CG1  . VAL   B 260 ? 0.7573 0.6655 0.4914 0.3373  0.0432  0.0423  259 VAL   B CG1  
3834 C  CG2  . VAL   B 260 ? 0.7139 0.694  0.4913 0.2892  0.0458  0.0339  259 VAL   B CG2  
3835 N  N    . PRO   B 261 ? 0.7522 0.7481 0.5239 0.3617  0.0069  0.0705  260 PRO   B N    
3836 C  CA   . PRO   B 261 ? 0.7452 0.7913 0.5462 0.3898  0.0113  0.0689  260 PRO   B CA   
3837 C  C    . PRO   B 261 ? 0.7344 0.8633 0.5791 0.3778  0.0056  0.0687  260 PRO   B C    
3838 O  O    . PRO   B 261 ? 0.725  0.8709 0.5738 0.3591  -0.0066 0.0738  260 PRO   B O    
3839 C  CB   . PRO   B 261 ? 0.7586 0.7816 0.5429 0.4272  0.0037  0.0799  260 PRO   B CB   
3840 C  CG   . PRO   B 261 ? 0.7742 0.7744 0.5382 0.4121  -0.011  0.0902  260 PRO   B CG   
3841 C  CD   . PRO   B 261 ? 0.7704 0.7353 0.5175 0.3732  -0.0057 0.083   260 PRO   B CD   
3842 N  N    . SER   B 262 ? 0.7356 0.9142 0.6107 0.386   0.0155  0.0618  261 SER   B N    
3843 C  CA   . SER   B 262 ? 0.7267 0.9857 0.644  0.3721  0.0133  0.0597  261 SER   B CA   
3844 C  C    . SER   B 262 ? 0.7404 1.048  0.6767 0.3795  -0.0045 0.0698  261 SER   B C    
3845 O  O    . SER   B 262 ? 0.7216 1.076  0.6793 0.3537  -0.0113 0.0691  261 SER   B O    
3846 C  CB   . SER   B 262 ? 0.7178 1.0187 0.6609 0.3877  0.0281  0.0521  261 SER   B CB   
3847 O  OG   . SER   B 262 ? 0.7482 1.0426 0.6883 0.4308  0.0301  0.0556  261 SER   B OG   
3848 N  N    . TYR   B 263 ? 0.7703 1.0642 0.696  0.4143  -0.0126 0.0794  262 TYR   B N    
3849 C  CA   . TYR   B 263 ? 0.7787 1.1151 0.7178 0.4244  -0.0316 0.0908  262 TYR   B CA   
3850 C  C    . TYR   B 263 ? 0.8321 1.1431 0.7489 0.3954  -0.0451 0.0961  262 TYR   B C    
3851 O  O    . TYR   B 263 ? 0.8175 1.1697 0.7457 0.3941  -0.0614 0.1038  262 TYR   B O    
3852 C  CB   . TYR   B 263 ? 0.7823 1.1056 0.7127 0.4722  -0.0368 0.1009  262 TYR   B CB   
3853 C  CG   . TYR   B 263 ? 0.8349 1.0645 0.7136 0.4836  -0.0377 0.1072  262 TYR   B CG   
3854 C  CD1  . TYR   B 263 ? 0.8644 1.0627 0.7158 0.4719  -0.0528 0.1176  262 TYR   B CD1  
3855 C  CD2  . TYR   B 263 ? 0.8709 1.0455 0.7271 0.5087  -0.0239 0.1034  262 TYR   B CD2  
3856 C  CE1  . TYR   B 263 ? 0.9216 1.035  0.7246 0.4808  -0.0533 0.1242  262 TYR   B CE1  
3857 C  CE2  . TYR   B 263 ? 0.9287 1.0161 0.7356 0.5183  -0.0249 0.1096  262 TYR   B CE2  
3858 C  CZ   . TYR   B 263 ? 0.9587 1.0164 0.7395 0.5037  -0.0397 0.1204  262 TYR   B CZ   
3859 O  OH   . TYR   B 263 ? 1.0223 0.9938 0.7527 0.5093  -0.0402 0.127   262 TYR   B OH   
3860 N  N    . TYR   B 264 ? 0.8899 1.1355 0.7747 0.372   -0.0385 0.0917  263 TYR   B N    
3861 C  CA   . TYR   B 264 ? 0.9315 1.1539 0.7958 0.3439  -0.0484 0.0951  263 TYR   B CA   
3862 C  C    . TYR   B 264 ? 0.936  1.2081 0.8252 0.3086  -0.0503 0.0882  263 TYR   B C    
3863 O  O    . TYR   B 264 ? 0.954  1.2031 0.827  0.2808  -0.0532 0.0866  263 TYR   B O    
3864 C  CB   . TYR   B 264 ? 0.9727 1.1132 0.7962 0.3323  -0.041  0.0933  263 TYR   B CB   
3865 C  CG   . TYR   B 264 ? 1.0108 1.1058 0.7988 0.3411  -0.0522 0.1054  263 TYR   B CG   
3866 C  CD1  . TYR   B 264 ? 1.0224 1.1222 0.8011 0.3192  -0.0635 0.1098  263 TYR   B CD1  
3867 C  CD2  . TYR   B 264 ? 1.0452 1.0932 0.8073 0.3724  -0.0514 0.1127  263 TYR   B CD2  
3868 C  CE1  . TYR   B 264 ? 1.0549 1.1158 0.7994 0.3269  -0.0737 0.1219  263 TYR   B CE1  
3869 C  CE2  . TYR   B 264 ? 1.0804 1.0846 0.8069 0.3801  -0.0618 0.1253  263 TYR   B CE2  
3870 C  CZ   . TYR   B 264 ? 1.0908 1.1023 0.8084 0.3564  -0.0728 0.1301  263 TYR   B CZ   
3871 O  OH   . TYR   B 264 ? 1.1363 1.1045 0.816  0.362   -0.0825 0.1431  263 TYR   B OH   
3872 N  N    . ASN   B 265 ? 0.9186 1.2581 0.8464 0.3101  -0.0479 0.0838  264 ASN   B N    
3873 C  CA   . ASN   B 265 ? 0.9164 1.3105 0.8711 0.2798  -0.0492 0.0774  264 ASN   B CA   
3874 C  C    . ASN   B 265 ? 0.9165 1.3665 0.8869 0.2835  -0.0679 0.0851  264 ASN   B C    
3875 O  O    . ASN   B 265 ? 0.9164 1.3855 0.8886 0.2541  -0.0754 0.0828  264 ASN   B O    
3876 C  CB   . ASN   B 265 ? 0.9123 1.3484 0.8981 0.2814  -0.0354 0.0692  264 ASN   B CB   
3877 C  CG   . ASN   B 265 ? 0.9382 1.4153 0.9449 0.2453  -0.0328 0.0615  264 ASN   B CG   
3878 O  OD1  . ASN   B 265 ? 0.9699 1.4278 0.9628 0.2164  -0.0374 0.0595  264 ASN   B OD1  
3879 N  ND2  . ASN   B 265 ? 0.9151 1.4475 0.954  0.246   -0.0243 0.0566  264 ASN   B ND2  
3880 N  N    . ILE   B 266 ? 0.9152 1.3911 0.8956 0.32    -0.0758 0.0943  265 ILE   B N    
3881 C  CA   . ILE   B 266 ? 0.9098 1.4395 0.9036 0.3269  -0.0958 0.1034  265 ILE   B CA   
3882 C  C    . ILE   B 266 ? 0.954  1.4378 0.9093 0.3191  -0.1097 0.1118  265 ILE   B C    
3883 O  O    . ILE   B 266 ? 0.9417 1.464  0.9018 0.3049  -0.1252 0.1152  265 ILE   B O    
3884 C  CB   . ILE   B 266 ? 0.8957 1.4718 0.9144 0.3708  -0.1008 0.1113  265 ILE   B CB   
3885 C  CG1  . ILE   B 266 ? 0.9404 1.4539 0.9256 0.4089  -0.1041 0.1227  265 ILE   B CG1  
3886 C  CG2  . ILE   B 266 ? 0.8772 1.4945 0.9312 0.3777  -0.0836 0.1016  265 ILE   B CG2  
3887 C  CD1  . ILE   B 266 ? 0.9332 1.4914 0.9403 0.4557  -0.1124 0.1326  265 ILE   B CD1  
3888 N  N    . TYR   B 267 ? 1.0036 1.4062 0.9195 0.3247  -0.1035 0.1144  266 TYR   B N    
3889 C  CA   . TYR   B 267 ? 1.0473 1.4045 0.9247 0.3139  -0.1141 0.1217  266 TYR   B CA   
3890 C  C    . TYR   B 267 ? 1.0596 1.4224 0.935  0.2703  -0.1134 0.1124  266 TYR   B C    
3891 O  O    . TYR   B 267 ? 1.0679 1.4375 0.9291 0.2571  -0.1268 0.1169  266 TYR   B O    
3892 C  CB   . TYR   B 267 ? 1.0924 1.3631 0.9293 0.3238  -0.1051 0.1248  266 TYR   B CB   
3893 C  CG   . TYR   B 267 ? 1.1191 1.367  0.9442 0.367   -0.1081 0.1361  266 TYR   B CG   
3894 C  CD1  . TYR   B 267 ? 1.1453 1.3787 0.9459 0.3854  -0.1244 0.1515  266 TYR   B CD1  
3895 C  CD2  . TYR   B 267 ? 1.1361 1.371  0.9702 0.3897  -0.094  0.1314  266 TYR   B CD2  
3896 C  CE1  . TYR   B 267 ? 1.1726 1.3793 0.9594 0.4271  -0.1271 0.1628  266 TYR   B CE1  
3897 C  CE2  . TYR   B 267 ? 1.1622 1.3705 0.9827 0.431   -0.0955 0.1408  266 TYR   B CE2  
3898 C  CZ   . TYR   B 267 ? 1.1877 1.3806 0.9846 0.4504  -0.1122 0.1569  266 TYR   B CZ   
3899 O  OH   . TYR   B 267 ? 1.2244 1.3855 1.0053 0.4933  -0.1135 0.1668  266 TYR   B OH   
3900 N  N    . LEU   B 268 ? 1.0624 1.4208 0.95   0.2489  -0.0979 0.0996  267 LEU   B N    
3901 C  CA   . LEU   B 268 ? 1.0741 1.4334 0.9605 0.2098  -0.0949 0.0897  267 LEU   B CA   
3902 C  C    . LEU   B 268 ? 1.0583 1.4893 0.9719 0.1935  -0.1053 0.087   267 LEU   B C    
3903 O  O    . LEU   B 268 ? 1.0647 1.4965 0.9669 0.1663  -0.1111 0.0833  267 LEU   B O    
3904 C  CB   . LEU   B 268 ? 1.0782 1.4135 0.9707 0.1966  -0.076  0.0785  267 LEU   B CB   
3905 C  CG   . LEU   B 268 ? 1.1272 1.3894 0.9883 0.1888  -0.0658 0.0759  267 LEU   B CG   
3906 C  CD1  . LEU   B 268 ? 1.1592 1.3746 0.9872 0.2066  -0.0719 0.0864  267 LEU   B CD1  
3907 C  CD2  . LEU   B 268 ? 1.1387 1.3826 1.007  0.1947  -0.0504 0.07    267 LEU   B CD2  
3908 N  N    . ILE   B 269 ? 1.0361 1.5277 0.9845 0.2096  -0.1075 0.0883  268 ILE   B N    
3909 C  CA   . ILE   B 269 ? 1.0164 1.5838 0.9937 0.1943  -0.1183 0.0861  268 ILE   B CA   
3910 C  C    . ILE   B 269 ? 1.0272 1.6148 0.9924 0.2008  -0.1404 0.0967  268 ILE   B C    
3911 O  O    . ILE   B 269 ? 1.0163 1.6365 0.9833 0.1736  -0.1505 0.093   268 ILE   B O    
3912 C  CB   . ILE   B 269 ? 0.9898 1.6195 1.0097 0.2103  -0.1126 0.0844  268 ILE   B CB   
3913 C  CG1  . ILE   B 269 ? 1.0057 1.6212 1.0349 0.1916  -0.0917 0.0724  268 ILE   B CG1  
3914 C  CG2  . ILE   B 269 ? 0.9549 1.6724 1.0068 0.2013  -0.1274 0.0854  268 ILE   B CG2  
3915 C  CD1  . ILE   B 269 ? 0.9959 1.6575 1.0599 0.2103  -0.0813 0.0705  268 ILE   B CD1  
3916 N  N    . LEU   B 270 ? 1.0504 1.6118 0.9978 0.2352  -0.1478 0.1097  269 LEU   B N    
3917 C  CA   . LEU   B 270 ? 1.0667 1.6391 0.9964 0.2443  -0.1693 0.1221  269 LEU   B CA   
3918 C  C    . LEU   B 270 ? 1.1086 1.6331 0.9978 0.2151  -0.1724 0.1201  269 LEU   B C    
3919 O  O    . LEU   B 270 ? 1.1043 1.6538 0.9831 0.2054  -0.1897 0.1249  269 LEU   B O    
3920 C  CB   . LEU   B 270 ? 1.0836 1.6304 0.9999 0.2897  -0.1748 0.1373  269 LEU   B CB   
3921 C  CG   . LEU   B 270 ? 1.0707 1.6765 1.0262 0.3254  -0.1775 0.1422  269 LEU   B CG   
3922 C  CD1  . LEU   B 270 ? 1.0977 1.6633 1.0322 0.3706  -0.1819 0.157   269 LEU   B CD1  
3923 C  CD2  . LEU   B 270 ? 1.0373 1.7362 1.0259 0.3199  -0.1962 0.1446  269 LEU   B CD2  
3924 N  N    . ASP   B 271 ? 1.1455 1.604  1.0124 0.2011  -0.1555 0.1128  270 ASP   B N    
3925 C  CA   . ASP   B 271 ? 1.1869 1.5995 1.0181 0.1735  -0.1543 0.1089  270 ASP   B CA   
3926 C  C    . ASP   B 271 ? 1.1806 1.6294 1.0216 0.1362  -0.1567 0.0969  270 ASP   B C    
3927 O  O    . ASP   B 271 ? 1.1974 1.6334 1.0117 0.1168  -0.1639 0.096   270 ASP   B O    
3928 C  CB   . ASP   B 271 ? 1.2411 1.5851 1.0545 0.1684  -0.1348 0.1028  270 ASP   B CB   
3929 C  CG   . ASP   B 271 ? 1.3321 1.6195 1.1168 0.1942  -0.1332 0.114   270 ASP   B CG   
3930 O  OD1  . ASP   B 271 ? 1.3463 1.639  1.1187 0.2168  -0.1476 0.1277  270 ASP   B OD1  
3931 O  OD2  . ASP   B 271 ? 1.3768 1.6136 1.15   0.1914  -0.1179 0.1093  270 ASP   B OD2  
3932 N  N    . LYS   B 272 ? 1.1562 1.6482 1.033  0.1253  -0.1501 0.0874  271 LYS   B N    
3933 C  CA   . LYS   B 272 ? 1.15   1.6756 1.0368 0.0889  -0.1513 0.0754  271 LYS   B CA   
3934 C  C    . LYS   B 272 ? 1.1269 1.7255 1.0301 0.0857  -0.1719 0.0796  271 LYS   B C    
3935 O  O    . LYS   B 272 ? 1.1066 1.7493 1.0296 0.0592  -0.1727 0.07    271 LYS   B O    
3936 C  CB   . LYS   B 272 ? 1.1591 1.6947 1.0733 0.0761  -0.1345 0.0642  271 LYS   B CB   
3937 C  CG   . LYS   B 272 ? 1.2311 1.7108 1.1255 0.0503  -0.1189 0.0527  271 LYS   B CG   
3938 C  CD   . LYS   B 272 ? 1.2666 1.7696 1.1667 0.0127  -0.118  0.0403  271 LYS   B CD   
3939 C  CE   . LYS   B 272 ? 1.3247 1.7698 1.2044 -0.0085 -0.1028 0.0297  271 LYS   B CE   
3940 N  NZ   . LYS   B 272 ? 1.3366 1.7975 1.2196 -0.0437 -0.1005 0.0175  271 LYS   B NZ   
3941 N  N    . PHE   B 273 ? 1.1283 1.7386 1.0217 0.1117  -0.1889 0.0942  272 PHE   B N    
3942 C  CA   . PHE   B 273 ? 1.108  1.7881 1.0147 0.1141  -0.2116 0.1011  272 PHE   B CA   
3943 C  C    . PHE   B 273 ? 1.1314 1.7839 0.9992 0.129   -0.2279 0.1151  272 PHE   B C    
3944 O  O    . PHE   B 273 ? 1.1231 1.7922 0.9947 0.1642  -0.2404 0.1305  272 PHE   B O    
3945 C  CB   . PHE   B 273 ? 1.0762 1.8202 1.028  0.1446  -0.2154 0.1078  272 PHE   B CB   
3946 C  CG   . PHE   B 273 ? 1.0544 1.8592 1.0493 0.1249  -0.2078 0.096   272 PHE   B CG   
3947 C  CD1  . PHE   B 273 ? 1.067  1.8513 1.0778 0.1246  -0.1855 0.0878  272 PHE   B CD1  
3948 C  CD2  . PHE   B 273 ? 1.0316 1.9171 1.0512 0.1075  -0.2236 0.0942  272 PHE   B CD2  
3949 C  CE1  . PHE   B 273 ? 1.0458 1.8846 1.0934 0.1057  -0.1778 0.0781  272 PHE   B CE1  
3950 C  CE2  . PHE   B 273 ? 1.0088 1.951  1.0674 0.0873  -0.2157 0.0838  272 PHE   B CE2  
3951 C  CZ   . PHE   B 273 ? 1.01   1.9271 1.0816 0.0866  -0.1923 0.0761  272 PHE   B CZ   
3952 P  PA   . NAD   C .   ? 0.6497 0.3318 0.3131 -0.0734 0.0171  0.0443  401 NAD   A PA   
3953 O  O1A  . NAD   C .   ? 0.6706 0.3252 0.3142 -0.0958 0.0165  0.0396  401 NAD   A O1A  
3954 O  O2A  . NAD   C .   ? 0.6548 0.3043 0.2914 -0.0645 0.0199  0.0523  401 NAD   A O2A  
3955 O  O5B  . NAD   C .   ? 0.635  0.334  0.3151 -0.046  0.0119  0.0377  401 NAD   A O5B  
3956 C  C5B  . NAD   C .   ? 0.6006 0.3449 0.3135 -0.0299 0.0108  0.0378  401 NAD   A C5B  
3957 C  C4B  . NAD   C .   ? 0.597  0.3383 0.3098 -0.0063 0.0077  0.0318  401 NAD   A C4B  
3958 O  O4B  . NAD   C .   ? 0.5707 0.3497 0.3098 0.0088  0.0065  0.0318  401 NAD   A O4B  
3959 C  C3B  . NAD   C .   ? 0.6231 0.3144 0.299  0.0099  0.0065  0.0321  401 NAD   A C3B  
3960 O  O3B  . NAD   C .   ? 0.6411 0.3102 0.3022 0.0163  0.006   0.0245  401 NAD   A O3B  
3961 C  C2B  . NAD   C .   ? 0.6116 0.3237 0.2994 0.0346  0.0036  0.0335  401 NAD   A C2B  
3962 O  O2B  . NAD   C .   ? 0.6309 0.3238 0.3026 0.0606  0.0009  0.0294  401 NAD   A O2B  
3963 C  C1B  . NAD   C .   ? 0.5798 0.3467 0.3084 0.0324  0.0039  0.0295  401 NAD   A C1B  
3964 N  N9A  . NAD   C .   ? 0.566  0.3643 0.3137 0.0443  0.0016  0.0307  401 NAD   A N9A  
3965 C  C8A  . NAD   C .   ? 0.569  0.3634 0.309  0.0464  0       0.037   401 NAD   A C8A  
3966 N  N7A  . NAD   C .   ? 0.5529 0.3766 0.3093 0.0591  -0.0039 0.0352  401 NAD   A N7A  
3967 C  C5A  . NAD   C .   ? 0.5365 0.3864 0.3142 0.0642  -0.0036 0.0276  401 NAD   A C5A  
3968 C  C6A  . NAD   C .   ? 0.5146 0.4028 0.316  0.0738  -0.0059 0.0218  401 NAD   A C6A  
3969 N  N6A  . NAD   C .   ? 0.4918 0.4006 0.3008 0.0801  -0.011  0.0221  401 NAD   A N6A  
3970 N  N1A  . NAD   C .   ? 0.5149 0.4206 0.3307 0.0745  -0.0026 0.0151  401 NAD   A N1A  
3971 C  C2A  . NAD   C .   ? 0.5236 0.4081 0.329  0.068   0.0015  0.0142  401 NAD   A C2A  
3972 N  N3A  . NAD   C .   ? 0.5428 0.3914 0.3263 0.0585  0.0024  0.0183  401 NAD   A N3A  
3973 C  C4A  . NAD   C .   ? 0.5495 0.3832 0.3211 0.0562  0.0002  0.0251  401 NAD   A C4A  
3974 O  O3   . NAD   C .   ? 0.6106 0.3568 0.3171 -0.0835 0.0191  0.0455  401 NAD   A O3   
3975 P  PN   . NAD   C .   ? 0.5703 0.3629 0.3064 -0.1047 0.0188  0.0424  401 NAD   A PN   
3976 O  O1N  . NAD   C .   ? 0.5752 0.3668 0.3127 -0.1053 0.0124  0.0345  401 NAD   A O1N  
3977 O  O2N  . NAD   C .   ? 0.5631 0.3567 0.2927 -0.1319 0.0253  0.047   401 NAD   A O2N  
3978 O  O5D  . NAD   C .   ? 0.5332 0.3751 0.3042 -0.0878 0.019   0.0436  401 NAD   A O5D  
3979 C  C5D  . NAD   C .   ? 0.5109 0.3744 0.3011 -0.0719 0.0138  0.0386  401 NAD   A C5D  
3980 C  C4D  . NAD   C .   ? 0.4834 0.3899 0.3016 -0.0648 0.0154  0.0403  401 NAD   A C4D  
3981 O  O4D  . NAD   C .   ? 0.4763 0.4132 0.3088 -0.0816 0.0178  0.0416  401 NAD   A O4D  
3982 C  C3D  . NAD   C .   ? 0.4762 0.3813 0.2927 -0.0525 0.0193  0.0445  401 NAD   A C3D  
3983 O  O3D  . NAD   C .   ? 0.451  0.3809 0.2861 -0.0383 0.0179  0.0426  401 NAD   A O3D  
3984 C  C2D  . NAD   C .   ? 0.4779 0.3967 0.2961 -0.0673 0.0262  0.0493  401 NAD   A C2D  
3985 O  O2D  . NAD   C .   ? 0.4756 0.4094 0.3    -0.0569 0.0304  0.0521  401 NAD   A O2D  
3986 C  C1D  . NAD   C .   ? 0.4637 0.4184 0.3042 -0.0782 0.0243  0.0461  401 NAD   A C1D  
3987 N  N1N  . NAD   C .   ? 0.4537 0.4272 0.2983 -0.1006 0.0304  0.0486  401 NAD   A N1N  
3988 C  C2N  . NAD   C .   ? 0.4704 0.4113 0.2904 -0.1197 0.0341  0.0512  401 NAD   A C2N  
3989 C  C3N  . NAD   C .   ? 0.4638 0.4241 0.2876 -0.1451 0.0411  0.0532  401 NAD   A C3N  
3990 C  C7N  . NAD   C .   ? 0.4927 0.4099 0.2834 -0.1711 0.0459  0.0562  401 NAD   A C7N  
3991 O  O7N  . NAD   C .   ? 0.4815 0.4149 0.2732 -0.1939 0.0554  0.0595  401 NAD   A O7N  
3992 N  N7N  . NAD   C .   ? 0.5291 0.3914 0.2891 -0.1691 0.0404  0.0547  401 NAD   A N7N  
3993 C  C4N  . NAD   C .   ? 0.4318 0.4526 0.2894 -0.1468 0.0437  0.0519  401 NAD   A C4N  
3994 C  C5N  . NAD   C .   ? 0.4137 0.4647 0.2946 -0.1223 0.0387  0.0493  401 NAD   A C5N  
3995 C  C6N  . NAD   C .   ? 0.4264 0.4496 0.2984 -0.101  0.0324  0.0479  401 NAD   A C6N  
3996 C  C4   . A1AG4 D .   ? 0.6855 0.6844 0.4891 -0.1756 0.0922  0.076   402 A1AG4 A C4   
3997 C  C7   . A1AG4 D .   ? 0.6307 0.7638 0.5149 -0.1907 0.0943  0.0656  402 A1AG4 A C7   
3998 C  C6   . A1AG4 D .   ? 0.6602 0.7633 0.5142 -0.2099 0.1079  0.0727  402 A1AG4 A C6   
3999 C  C13  . A1AG4 D .   ? 0.6576 0.9485 0.6078 -0.1873 0.1275  0.0642  402 A1AG4 A C13  
4000 C  C20  . A1AG4 D .   ? 0.6627 0.6584 0.4884 -0.1345 0.0681  0.0664  402 A1AG4 A C20  
4001 C  C16  . A1AG4 D .   ? 0.5963 1.033  0.6324 -0.1896 0.1176  0.0512  402 A1AG4 A C16  
4002 F  F1   . A1AG4 D .   ? 0.629  0.7479 0.5257 -0.1505 0.0704  0.0583  402 A1AG4 A F1   
4003 C  C2   . A1AG4 D .   ? 0.64   0.7326 0.5116 -0.1672 0.0818  0.0643  402 A1AG4 A C2   
4004 C  C3   . A1AG4 D .   ? 0.6619 0.6912 0.4964 -0.1594 0.0806  0.0688  402 A1AG4 A C3   
4005 C  C5   . A1AG4 D .   ? 0.6815 0.7136 0.4926 -0.2017 0.1064  0.0784  402 A1AG4 A C5   
4006 N  N8   . A1AG4 D .   ? 0.6707 0.8188 0.5374 -0.2364 0.1237  0.0743  402 A1AG4 A N8   
4007 S  S9   . A1AG4 D .   ? 0.6596 0.8906 0.5727 -0.2582 0.1254  0.0677  402 A1AG4 A S9   
4008 O  O10  . A1AG4 D .   ? 0.6592 0.9077 0.5659 -0.2914 0.1445  0.0719  402 A1AG4 A O10  
4009 O  O11  . A1AG4 D .   ? 0.6643 0.8848 0.5813 -0.2682 0.1093  0.0623  402 A1AG4 A O11  
4010 C  C12  . A1AG4 D .   ? 0.6406 0.9479 0.6011 -0.2199 0.1237  0.062   402 A1AG4 A C12  
4011 C  C14  . A1AG4 D .   ? 0.6443 0.9873 0.625  -0.1574 0.1273  0.0595  402 A1AG4 A C14  
4012 C  C15  . A1AG4 D .   ? 0.6184 1.0335 0.6412 -0.1573 0.1231  0.0535  402 A1AG4 A C15  
4013 C  C17  . A1AG4 D .   ? 0.6149 0.9957 0.6189 -0.2225 0.1182  0.0551  402 A1AG4 A C17  
4014 CL CL18 . A1AG4 D .   ? 0.6066 1.0859 0.6628 -0.1165 0.1245  0.0481  402 A1AG4 A CL18 
4015 CL CL19 . A1AG4 D .   ? 0.6663 0.9785 0.6278 -0.1184 0.1298  0.0605  402 A1AG4 A CL19 
4016 O  O21  . A1AG4 D .   ? 0.6905 0.6337 0.486  -0.1336 0.064   0.0685  402 A1AG4 A O21  
4017 O  O22  . A1AG4 D .   ? 0.6327 0.6596 0.484  -0.1137 0.0624  0.0618  402 A1AG4 A O22  
4025 P  PA   . NAD   E .   ? 0.7158 0.33   0.2767 0.0529  0.0375  0.0115  401 NAD   B PA   
4026 O  O1A  . NAD   E .   ? 0.7482 0.3179 0.2777 0.066   0.0419  0.0085  401 NAD   B O1A  
4027 O  O2A  . NAD   E .   ? 0.7165 0.324  0.2717 0.0335  0.0359  0.0151  401 NAD   B O2A  
4028 O  O5B  . NAD   E .   ? 0.692  0.3364 0.2723 0.0427  0.0364  0.0051  401 NAD   B O5B  
4029 C  C5B  . NAD   E .   ? 0.6652 0.3574 0.2806 0.0395  0.0333  0.0067  401 NAD   B C5B  
4030 C  C4B  . NAD   E .   ? 0.6548 0.3584 0.2749 0.0252  0.0311  0.0013  401 NAD   B C4B  
4031 O  O4B  . NAD   E .   ? 0.6329 0.3777 0.2845 0.0201  0.0277  0.0032  401 NAD   B O4B  
4032 C  C3B  . NAD   E .   ? 0.664  0.3434 0.2632 0.0039  0.0298  -0.0022 401 NAD   B C3B  
4033 O  O3B  . NAD   E .   ? 0.6797 0.3389 0.258  -0.0008 0.03    -0.0087 401 NAD   B O3B  
4034 C  C2B  . NAD   E .   ? 0.642  0.3582 0.2678 -0.0113 0.0256  -0.0009 401 NAD   B C2B  
4035 O  O2B  . NAD   E .   ? 0.6426 0.3599 0.2629 -0.0312 0.022   -0.0054 401 NAD   B O2B  
4036 C  C1B  . NAD   E .   ? 0.6219 0.3729 0.275  0.0012  0.0241  0.0005  401 NAD   B C1B  
4037 N  N9A  . NAD   E .   ? 0.5952 0.3811 0.2771 -0.0038 0.0218  0.003   401 NAD   B N9A  
4038 C  C8A  . NAD   E .   ? 0.5798 0.3732 0.2698 -0.0089 0.0232  0.0055  401 NAD   B C8A  
4039 N  N7A  . NAD   E .   ? 0.5577 0.3829 0.2731 -0.0132 0.0215  0.0057  401 NAD   B N7A  
4040 C  C5A  . NAD   E .   ? 0.5501 0.3884 0.2743 -0.0102 0.0177  0.0045  401 NAD   B C5A  
4041 C  C6A  . NAD   E .   ? 0.5214 0.3889 0.2686 -0.0107 0.0139  0.005   401 NAD   B C6A  
4042 N  N6A  . NAD   E .   ? 0.4983 0.3892 0.267  -0.013  0.0144  0.0056  401 NAD   B N6A  
4043 N  N1A  . NAD   E .   ? 0.5173 0.3876 0.2629 -0.0077 0.0098  0.005   401 NAD   B N1A  
4044 C  C2A  . NAD   E .   ? 0.5384 0.3854 0.2614 -0.0053 0.0108  0.0032  401 NAD   B C2A  
4045 N  N3A  . NAD   E .   ? 0.5641 0.3828 0.2654 -0.0033 0.0152  0.0015  401 NAD   B N3A  
4046 C  C4A  . NAD   E .   ? 0.5715 0.3867 0.2747 -0.0056 0.0179  0.0029  401 NAD   B C4A  
4047 O  O3   . NAD   E .   ? 0.6881 0.3397 0.2767 0.0725  0.0359  0.0169  401 NAD   B O3   
4048 P  PN   . NAD   E .   ? 0.6778 0.3404 0.2741 0.1006  0.0373  0.0193  401 NAD   B PN   
4049 O  O1N  . NAD   E .   ? 0.6819 0.3395 0.2737 0.1089  0.0423  0.0124  401 NAD   B O1N  
4050 O  O2N  . NAD   E .   ? 0.6939 0.3319 0.2725 0.1141  0.0358  0.0267  401 NAD   B O2N  
4051 O  O5D  . NAD   E .   ? 0.6419 0.3588 0.2759 0.0983  0.034   0.0211  401 NAD   B O5D  
4052 C  C5D  . NAD   E .   ? 0.6112 0.3591 0.2667 0.0967  0.0355  0.0166  401 NAD   B C5D  
4053 C  C4D  . NAD   E .   ? 0.5892 0.3787 0.2733 0.0996  0.0328  0.0199  401 NAD   B C4D  
4054 O  O4D  . NAD   E .   ? 0.5903 0.3857 0.2755 0.1186  0.0319  0.0245  401 NAD   B O4D  
4055 C  C3D  . NAD   E .   ? 0.5769 0.3793 0.2715 0.0845  0.029   0.0221  401 NAD   B C3D  
4056 O  O3D  . NAD   E .   ? 0.5542 0.3919 0.2745 0.08    0.0284  0.0209  401 NAD   B O3D  
4057 C  C2D  . NAD   E .   ? 0.5815 0.3797 0.2692 0.0937  0.026   0.0283  401 NAD   B C2D  
4058 O  O2D  . NAD   E .   ? 0.5725 0.3944 0.2747 0.0852  0.0229  0.0301  401 NAD   B O2D  
4059 C  C1D  . NAD   E .   ? 0.5774 0.3895 0.2721 0.1145  0.0268  0.0293  401 NAD   B C1D  
4060 N  N1N  . NAD   E .   ? 0.5887 0.3882 0.2702 0.1318  0.0236  0.0359  401 NAD   B N1N  
4061 C  C2N  . NAD   E .   ? 0.6155 0.3709 0.2671 0.1338  0.024   0.0387  401 NAD   B C2N  
4062 C  C3N  . NAD   E .   ? 0.6351 0.3749 0.2717 0.1515  0.0204  0.0463  401 NAD   B C3N  
4063 C  C7N  . NAD   E .   ? 0.6733 0.3565 0.2719 0.1545  0.0214  0.0501  401 NAD   B C7N  
4064 O  O7N  . NAD   E .   ? 0.6912 0.3596 0.2746 0.1665  0.0166  0.059   401 NAD   B O7N  
4065 N  N7N  . NAD   E .   ? 0.6889 0.3382 0.2691 0.1438  0.027   0.044   401 NAD   B N7N  
4066 C  C4N  . NAD   E .   ? 0.6157 0.3928 0.2721 0.167   0.0155  0.0506  401 NAD   B C4N  
4067 C  C5N  . NAD   E .   ? 0.5851 0.4107 0.2736 0.1621  0.0155  0.0466  401 NAD   B C5N  
4068 C  C6N  . NAD   E .   ? 0.5736 0.4068 0.2728 0.1443  0.0201  0.0394  401 NAD   B C6N  
4069 C  C4   . A1AG4 F .   ? 0.8073 0.5326 0.3961 0.1408  -0.0043 0.0792  402 A1AG4 B C4   
4070 C  C7   . A1AG4 F .   ? 0.782  0.5686 0.4051 0.1878  -0.0161 0.0857  402 A1AG4 B C7   
4071 C  C6   . A1AG4 F .   ? 0.8225 0.571  0.412  0.1821  -0.0194 0.0941  402 A1AG4 B C6   
4072 C  C13  . A1AG4 F .   ? 0.8677 0.7355 0.5054 0.2071  -0.0452 0.1049  402 A1AG4 B C13  
4073 C  C20  . A1AG4 F .   ? 0.7612 0.5241 0.394  0.1302  0.0058  0.0612  402 A1AG4 B C20  
4074 C  C16  . A1AG4 F .   ? 0.8472 0.7937 0.5259 0.258   -0.0606 0.114   402 A1AG4 B C16  
4075 F  F1   . A1AG4 F .   ? 0.7349 0.5588 0.3996 0.1742  -0.0042 0.0679  402 A1AG4 B F1   
4076 C  C2   . A1AG4 F .   ? 0.7656 0.5539 0.4008 0.17    -0.0074 0.075   402 A1AG4 B C2   
4077 C  C3   . A1AG4 F .   ? 0.7779 0.5366 0.3972 0.1474  -0.002  0.0717  402 A1AG4 B C3   
4078 C  C5   . A1AG4 F .   ? 0.827  0.5448 0.3992 0.1573  -0.0127 0.0906  402 A1AG4 B C5   
4079 N  N8   . A1AG4 F .   ? 0.8593 0.6009 0.4311 0.201   -0.0296 0.107   402 A1AG4 B N8   
4080 S  S9   . A1AG4 F .   ? 0.8818 0.6437 0.464  0.2376  -0.0375 0.1143  402 A1AG4 B S9   
4081 O  O10  . A1AG4 F .   ? 0.9011 0.6294 0.4492 0.2512  -0.0461 0.1287  402 A1AG4 B O10  
4082 O  O11  . A1AG4 F .   ? 0.8933 0.6461 0.4845 0.2512  -0.0285 0.1071  402 A1AG4 B O11  
4083 C  C12  . A1AG4 F .   ? 0.8698 0.7131 0.4955 0.2359  -0.046  0.1116  402 A1AG4 B C12  
4084 C  C14  . A1AG4 F .   ? 0.8517 0.7782 0.5191 0.2033  -0.0518 0.1022  402 A1AG4 B C14  
4085 C  C15  . A1AG4 F .   ? 0.8498 0.8164 0.5375 0.227   -0.0598 0.1068  402 A1AG4 B C15  
4086 C  C17  . A1AG4 F .   ? 0.8658 0.7473 0.5119 0.2631  -0.0533 0.1162  402 A1AG4 B C17  
4087 CL CL18 . A1AG4 F .   ? 0.8352 0.8782 0.5602 0.2177  -0.0681 0.1027  402 A1AG4 B CL18 
4088 CL CL19 . A1AG4 F .   ? 0.8363 0.7859 0.5165 0.1685  -0.0485 0.0917  402 A1AG4 B CL19 
4089 O  O21  . A1AG4 F .   ? 0.7785 0.5081 0.3938 0.1182  0.0108  0.0586  402 A1AG4 B O21  
4090 O  O22  . A1AG4 F .   ? 0.7274 0.5323 0.3909 0.1282  0.0061  0.0556  402 A1AG4 B O22  
# 
