data_8YK4
# 
_entry.id   8YK4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8YK4         pdb_00008yk4 10.2210/pdb8yk4/pdb 
WWPDB D_1300045268 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-12 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YK4 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              maenaka@pharm.hokudai.ac.jp 
_pdbx_contact_author.name_first         Katsumi 
_pdbx_contact_author.name_last          Maenaka 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5459-521X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Anraku, Y.'     1  0000-0002-5731-0902 
'Kita, S.'       2  0000-0003-3969-302X 
'Onodera, T.'    3  0000-0002-7079-3339 
'Sato, A.'       4  0000-0001-6625-1679 
'Tadokoro, T.'   5  0000-0002-3390-4861 
'Adachi, Y.'     6  ?                   
'Ito, S.'        7  0000-0002-3562-9322 
'Suzuki, T.'     8  0000-0002-6946-3850 
'Sasaki, J.'     9  0000-0002-5129-2336 
'Shiwa, N.'      10 0000-0002-4135-322X 
'Iwata, N.'      11 ?                   
'Nagata, N.'     12 0000-0001-9147-1438 
'Kazuki, Y.'     13 0000-0003-4818-4710 
'Oshimura, M.'   14 ?                   
'Sasaki, M.'     15 0000-0003-1607-2175 
'Orba, Y.'       16 0000-0001-9910-3912 
'Suzuki, T.'     17 0000-0002-3820-9542 
'Sawa, H.'       18 0000-0003-2569-2755 
'Hashiguchi, T.' 19 0000-0001-7578-7571 
'Fukuhara, H.'   20 0000-0002-7035-8206 
'Takahashi, Y.'  21 0000-0001-6342-4087 
'Maenaka, K.'    22 0000-0002-5459-521X 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structural Basis for Potent Neutralization Activity of SARS-CoV-2 Antibody, NT-108' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Anraku, Y.'     1  0000-0002-5731-0902 
primary 'Tadokoro, T.'   2  0000-0002-3390-4861 
primary 'Suzuki, T.'     3  0000-0002-6946-3850 
primary 'Sasaki, J.'     4  0000-0002-5129-2336 
primary 'Hashiguchi, T.' 5  0000-0001-7578-7571 
primary 'Kita, S.'       6  0000-0003-3969-302X 
primary 'Shiwa, N.'      7  0000-0002-4135-322X 
primary 'Iwata, N.'      8  ?                   
primary 'Nagata, N.'     9  0000-0001-9147-1438 
primary 'Suzuki, T.'     10 0000-0002-3820-9542 
primary 'Kazuki, Y.'     11 0000-0003-4818-4710 
primary 'Fukuhara, H.'   12 0000-0002-7035-8206 
primary 'Oshimura, M.'   13 ?                   
primary 'Sato, A.'       14 0000-0001-6625-1679 
primary 'Sasaki, M.'     15 0000-0003-1607-2175 
primary 'Orba, Y.'       16 0000-0001-9910-3912 
primary 'Sawa, H.'       17 0000-0003-2569-2755 
primary 'Maenaka, K.'    18 0000-0002-5459-521X 
# 
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 'antibody NT-108, single chain Fv fragment' 29873.400 1 ? ? ? ? 
2 polymer man 'Spike protein S1'                          24145.156 1 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MGILPSPGMPALLSLVSLLSVLLMGCVAETGEIVLTQSPGTLSLSPGERATLSCRASQSVSSTFLAWYQQKPGQAPRLLI
YGASYMATGIPDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSLTFGGGTKLEIKGGGGSGGGGSGGGGSQVQLQQS
GPGLVKPSQTLSLTCSISGDSVSSNSAAWNWIRQSPSRGLEWLGRTYYRSKWYNDYAGTVKSRIAINPDTSKNQFSLHLN
SVTPEDTAVYFCARVISVAGYAFDIWGQGTMVTVSSHHHHHH
;
;MGILPSPGMPALLSLVSLLSVLLMGCVAETGEIVLTQSPGTLSLSPGERATLSCRASQSVSSTFLAWYQQKPGQAPRLLI
YGASYMATGIPDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSLTFGGGTKLEIKGGGGSGGGGSGGGGSQVQLQQS
GPGLVKPSQTLSLTCSISGDSVSSNSAAWNWIRQSPSRGLEWLGRTYYRSKWYNDYAGTVKSRIAINPDTSKNQFSLHLN
SVTPEDTAVYFCARVISVAGYAFDIWGQGTMVTVSSHHHHHH
;
A ? 
2 'polypeptide(L)' no no 
;PTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFV
IRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCN
GVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKN
;
;PTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFV
IRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCN
GVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKN
;
C ? 
# 
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   ILE n 
1 4   LEU n 
1 5   PRO n 
1 6   SER n 
1 7   PRO n 
1 8   GLY n 
1 9   MET n 
1 10  PRO n 
1 11  ALA n 
1 12  LEU n 
1 13  LEU n 
1 14  SER n 
1 15  LEU n 
1 16  VAL n 
1 17  SER n 
1 18  LEU n 
1 19  LEU n 
1 20  SER n 
1 21  VAL n 
1 22  LEU n 
1 23  LEU n 
1 24  MET n 
1 25  GLY n 
1 26  CYS n 
1 27  VAL n 
1 28  ALA n 
1 29  GLU n 
1 30  THR n 
1 31  GLY n 
1 32  GLU n 
1 33  ILE n 
1 34  VAL n 
1 35  LEU n 
1 36  THR n 
1 37  GLN n 
1 38  SER n 
1 39  PRO n 
1 40  GLY n 
1 41  THR n 
1 42  LEU n 
1 43  SER n 
1 44  LEU n 
1 45  SER n 
1 46  PRO n 
1 47  GLY n 
1 48  GLU n 
1 49  ARG n 
1 50  ALA n 
1 51  THR n 
1 52  LEU n 
1 53  SER n 
1 54  CYS n 
1 55  ARG n 
1 56  ALA n 
1 57  SER n 
1 58  GLN n 
1 59  SER n 
1 60  VAL n 
1 61  SER n 
1 62  SER n 
1 63  THR n 
1 64  PHE n 
1 65  LEU n 
1 66  ALA n 
1 67  TRP n 
1 68  TYR n 
1 69  GLN n 
1 70  GLN n 
1 71  LYS n 
1 72  PRO n 
1 73  GLY n 
1 74  GLN n 
1 75  ALA n 
1 76  PRO n 
1 77  ARG n 
1 78  LEU n 
1 79  LEU n 
1 80  ILE n 
1 81  TYR n 
1 82  GLY n 
1 83  ALA n 
1 84  SER n 
1 85  TYR n 
1 86  MET n 
1 87  ALA n 
1 88  THR n 
1 89  GLY n 
1 90  ILE n 
1 91  PRO n 
1 92  ASP n 
1 93  ARG n 
1 94  PHE n 
1 95  SER n 
1 96  GLY n 
1 97  SER n 
1 98  GLY n 
1 99  SER n 
1 100 GLY n 
1 101 THR n 
1 102 ASP n 
1 103 PHE n 
1 104 THR n 
1 105 LEU n 
1 106 THR n 
1 107 ILE n 
1 108 SER n 
1 109 ARG n 
1 110 LEU n 
1 111 GLU n 
1 112 PRO n 
1 113 GLU n 
1 114 ASP n 
1 115 PHE n 
1 116 ALA n 
1 117 VAL n 
1 118 TYR n 
1 119 TYR n 
1 120 CYS n 
1 121 GLN n 
1 122 GLN n 
1 123 TYR n 
1 124 GLY n 
1 125 SER n 
1 126 SER n 
1 127 LEU n 
1 128 THR n 
1 129 PHE n 
1 130 GLY n 
1 131 GLY n 
1 132 GLY n 
1 133 THR n 
1 134 LYS n 
1 135 LEU n 
1 136 GLU n 
1 137 ILE n 
1 138 LYS n 
1 139 GLY n 
1 140 GLY n 
1 141 GLY n 
1 142 GLY n 
1 143 SER n 
1 144 GLY n 
1 145 GLY n 
1 146 GLY n 
1 147 GLY n 
1 148 SER n 
1 149 GLY n 
1 150 GLY n 
1 151 GLY n 
1 152 GLY n 
1 153 SER n 
1 154 GLN n 
1 155 VAL n 
1 156 GLN n 
1 157 LEU n 
1 158 GLN n 
1 159 GLN n 
1 160 SER n 
1 161 GLY n 
1 162 PRO n 
1 163 GLY n 
1 164 LEU n 
1 165 VAL n 
1 166 LYS n 
1 167 PRO n 
1 168 SER n 
1 169 GLN n 
1 170 THR n 
1 171 LEU n 
1 172 SER n 
1 173 LEU n 
1 174 THR n 
1 175 CYS n 
1 176 SER n 
1 177 ILE n 
1 178 SER n 
1 179 GLY n 
1 180 ASP n 
1 181 SER n 
1 182 VAL n 
1 183 SER n 
1 184 SER n 
1 185 ASN n 
1 186 SER n 
1 187 ALA n 
1 188 ALA n 
1 189 TRP n 
1 190 ASN n 
1 191 TRP n 
1 192 ILE n 
1 193 ARG n 
1 194 GLN n 
1 195 SER n 
1 196 PRO n 
1 197 SER n 
1 198 ARG n 
1 199 GLY n 
1 200 LEU n 
1 201 GLU n 
1 202 TRP n 
1 203 LEU n 
1 204 GLY n 
1 205 ARG n 
1 206 THR n 
1 207 TYR n 
1 208 TYR n 
1 209 ARG n 
1 210 SER n 
1 211 LYS n 
1 212 TRP n 
1 213 TYR n 
1 214 ASN n 
1 215 ASP n 
1 216 TYR n 
1 217 ALA n 
1 218 GLY n 
1 219 THR n 
1 220 VAL n 
1 221 LYS n 
1 222 SER n 
1 223 ARG n 
1 224 ILE n 
1 225 ALA n 
1 226 ILE n 
1 227 ASN n 
1 228 PRO n 
1 229 ASP n 
1 230 THR n 
1 231 SER n 
1 232 LYS n 
1 233 ASN n 
1 234 GLN n 
1 235 PHE n 
1 236 SER n 
1 237 LEU n 
1 238 HIS n 
1 239 LEU n 
1 240 ASN n 
1 241 SER n 
1 242 VAL n 
1 243 THR n 
1 244 PRO n 
1 245 GLU n 
1 246 ASP n 
1 247 THR n 
1 248 ALA n 
1 249 VAL n 
1 250 TYR n 
1 251 PHE n 
1 252 CYS n 
1 253 ALA n 
1 254 ARG n 
1 255 VAL n 
1 256 ILE n 
1 257 SER n 
1 258 VAL n 
1 259 ALA n 
1 260 GLY n 
1 261 TYR n 
1 262 ALA n 
1 263 PHE n 
1 264 ASP n 
1 265 ILE n 
1 266 TRP n 
1 267 GLY n 
1 268 GLN n 
1 269 GLY n 
1 270 THR n 
1 271 MET n 
1 272 VAL n 
1 273 THR n 
1 274 VAL n 
1 275 SER n 
1 276 SER n 
1 277 HIS n 
1 278 HIS n 
1 279 HIS n 
1 280 HIS n 
1 281 HIS n 
1 282 HIS n 
2 1   PRO n 
2 2   THR n 
2 3   GLU n 
2 4   SER n 
2 5   ILE n 
2 6   VAL n 
2 7   ARG n 
2 8   PHE n 
2 9   PRO n 
2 10  ASN n 
2 11  ILE n 
2 12  THR n 
2 13  ASN n 
2 14  LEU n 
2 15  CYS n 
2 16  PRO n 
2 17  PHE n 
2 18  GLY n 
2 19  GLU n 
2 20  VAL n 
2 21  PHE n 
2 22  ASN n 
2 23  ALA n 
2 24  THR n 
2 25  ARG n 
2 26  PHE n 
2 27  ALA n 
2 28  SER n 
2 29  VAL n 
2 30  TYR n 
2 31  ALA n 
2 32  TRP n 
2 33  ASN n 
2 34  ARG n 
2 35  LYS n 
2 36  ARG n 
2 37  ILE n 
2 38  SER n 
2 39  ASN n 
2 40  CYS n 
2 41  VAL n 
2 42  ALA n 
2 43  ASP n 
2 44  TYR n 
2 45  SER n 
2 46  VAL n 
2 47  LEU n 
2 48  TYR n 
2 49  ASN n 
2 50  SER n 
2 51  ALA n 
2 52  SER n 
2 53  PHE n 
2 54  SER n 
2 55  THR n 
2 56  PHE n 
2 57  LYS n 
2 58  CYS n 
2 59  TYR n 
2 60  GLY n 
2 61  VAL n 
2 62  SER n 
2 63  PRO n 
2 64  THR n 
2 65  LYS n 
2 66  LEU n 
2 67  ASN n 
2 68  ASP n 
2 69  LEU n 
2 70  CYS n 
2 71  PHE n 
2 72  THR n 
2 73  ASN n 
2 74  VAL n 
2 75  TYR n 
2 76  ALA n 
2 77  ASP n 
2 78  SER n 
2 79  PHE n 
2 80  VAL n 
2 81  ILE n 
2 82  ARG n 
2 83  GLY n 
2 84  ASP n 
2 85  GLU n 
2 86  VAL n 
2 87  ARG n 
2 88  GLN n 
2 89  ILE n 
2 90  ALA n 
2 91  PRO n 
2 92  GLY n 
2 93  GLN n 
2 94  THR n 
2 95  GLY n 
2 96  LYS n 
2 97  ILE n 
2 98  ALA n 
2 99  ASP n 
2 100 TYR n 
2 101 ASN n 
2 102 TYR n 
2 103 LYS n 
2 104 LEU n 
2 105 PRO n 
2 106 ASP n 
2 107 ASP n 
2 108 PHE n 
2 109 THR n 
2 110 GLY n 
2 111 CYS n 
2 112 VAL n 
2 113 ILE n 
2 114 ALA n 
2 115 TRP n 
2 116 ASN n 
2 117 SER n 
2 118 ASN n 
2 119 ASN n 
2 120 LEU n 
2 121 ASP n 
2 122 SER n 
2 123 LYS n 
2 124 VAL n 
2 125 GLY n 
2 126 GLY n 
2 127 ASN n 
2 128 TYR n 
2 129 ASN n 
2 130 TYR n 
2 131 LEU n 
2 132 TYR n 
2 133 ARG n 
2 134 LEU n 
2 135 PHE n 
2 136 ARG n 
2 137 LYS n 
2 138 SER n 
2 139 ASN n 
2 140 LEU n 
2 141 LYS n 
2 142 PRO n 
2 143 PHE n 
2 144 GLU n 
2 145 ARG n 
2 146 ASP n 
2 147 ILE n 
2 148 SER n 
2 149 THR n 
2 150 GLU n 
2 151 ILE n 
2 152 TYR n 
2 153 GLN n 
2 154 ALA n 
2 155 GLY n 
2 156 SER n 
2 157 THR n 
2 158 PRO n 
2 159 CYS n 
2 160 ASN n 
2 161 GLY n 
2 162 VAL n 
2 163 GLU n 
2 164 GLY n 
2 165 PHE n 
2 166 ASN n 
2 167 CYS n 
2 168 TYR n 
2 169 PHE n 
2 170 PRO n 
2 171 LEU n 
2 172 GLN n 
2 173 SER n 
2 174 TYR n 
2 175 GLY n 
2 176 PHE n 
2 177 GLN n 
2 178 PRO n 
2 179 THR n 
2 180 ASN n 
2 181 GLY n 
2 182 VAL n 
2 183 GLY n 
2 184 TYR n 
2 185 GLN n 
2 186 PRO n 
2 187 TYR n 
2 188 ARG n 
2 189 VAL n 
2 190 VAL n 
2 191 VAL n 
2 192 LEU n 
2 193 SER n 
2 194 PHE n 
2 195 GLU n 
2 196 LEU n 
2 197 LEU n 
2 198 HIS n 
2 199 ALA n 
2 200 PRO n 
2 201 ALA n 
2 202 THR n 
2 203 VAL n 
2 204 CYS n 
2 205 GLY n 
2 206 PRO n 
2 207 LYS n 
2 208 LYS n 
2 209 SER n 
2 210 THR n 
2 211 ASN n 
2 212 LEU n 
2 213 VAL n 
2 214 LYS n 
2 215 ASN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 282 ? ? ? ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 215 ? ? ? ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
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 
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 
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   -29 ?   ?   ?   A . n 
A 1 2   GLY 2   -28 ?   ?   ?   A . n 
A 1 3   ILE 3   -27 ?   ?   ?   A . n 
A 1 4   LEU 4   -26 ?   ?   ?   A . n 
A 1 5   PRO 5   -25 ?   ?   ?   A . n 
A 1 6   SER 6   -24 ?   ?   ?   A . n 
A 1 7   PRO 7   -23 ?   ?   ?   A . n 
A 1 8   GLY 8   -22 ?   ?   ?   A . n 
A 1 9   MET 9   -21 ?   ?   ?   A . n 
A 1 10  PRO 10  -20 ?   ?   ?   A . n 
A 1 11  ALA 11  -19 ?   ?   ?   A . n 
A 1 12  LEU 12  -18 ?   ?   ?   A . n 
A 1 13  LEU 13  -17 ?   ?   ?   A . n 
A 1 14  SER 14  -16 ?   ?   ?   A . n 
A 1 15  LEU 15  -15 ?   ?   ?   A . n 
A 1 16  VAL 16  -14 ?   ?   ?   A . n 
A 1 17  SER 17  -13 ?   ?   ?   A . n 
A 1 18  LEU 18  -12 ?   ?   ?   A . n 
A 1 19  LEU 19  -11 ?   ?   ?   A . n 
A 1 20  SER 20  -10 ?   ?   ?   A . n 
A 1 21  VAL 21  -9  ?   ?   ?   A . n 
A 1 22  LEU 22  -8  ?   ?   ?   A . n 
A 1 23  LEU 23  -7  ?   ?   ?   A . n 
A 1 24  MET 24  -6  ?   ?   ?   A . n 
A 1 25  GLY 25  -5  ?   ?   ?   A . n 
A 1 26  CYS 26  -4  ?   ?   ?   A . n 
A 1 27  VAL 27  -3  ?   ?   ?   A . n 
A 1 28  ALA 28  -2  ?   ?   ?   A . n 
A 1 29  GLU 29  -1  ?   ?   ?   A . n 
A 1 30  THR 30  0   ?   ?   ?   A . n 
A 1 31  GLY 31  1   ?   ?   ?   A . n 
A 1 32  GLU 32  2   ?   ?   ?   A . n 
A 1 33  ILE 33  3   3   ILE ILE A . n 
A 1 34  VAL 34  4   4   VAL VAL A . n 
A 1 35  LEU 35  5   5   LEU LEU A . n 
A 1 36  THR 36  6   6   THR THR A . n 
A 1 37  GLN 37  7   7   GLN GLN A . n 
A 1 38  SER 38  8   8   SER SER A . n 
A 1 39  PRO 39  9   9   PRO PRO A . n 
A 1 40  GLY 40  10  10  GLY GLY A . n 
A 1 41  THR 41  11  11  THR THR A . n 
A 1 42  LEU 42  12  12  LEU LEU A . n 
A 1 43  SER 43  13  13  SER SER A . n 
A 1 44  LEU 44  14  14  LEU LEU A . n 
A 1 45  SER 45  15  15  SER SER A . n 
A 1 46  PRO 46  16  16  PRO PRO A . n 
A 1 47  GLY 47  17  17  GLY GLY A . n 
A 1 48  GLU 48  18  18  GLU GLU A . n 
A 1 49  ARG 49  19  19  ARG ARG A . n 
A 1 50  ALA 50  20  20  ALA ALA A . n 
A 1 51  THR 51  21  21  THR THR A . n 
A 1 52  LEU 52  22  22  LEU LEU A . n 
A 1 53  SER 53  23  23  SER SER A . n 
A 1 54  CYS 54  24  24  CYS CYS A . n 
A 1 55  ARG 55  25  25  ARG ARG A . n 
A 1 56  ALA 56  26  26  ALA ALA A . n 
A 1 57  SER 57  27  27  SER SER A . n 
A 1 58  GLN 58  28  28  GLN GLN A . n 
A 1 59  SER 59  29  29  SER SER A . n 
A 1 60  VAL 60  30  30  VAL VAL A . n 
A 1 61  SER 61  31  31  SER SER A . n 
A 1 62  SER 62  32  32  SER SER A . n 
A 1 63  THR 63  33  33  THR THR A . n 
A 1 64  PHE 64  34  34  PHE PHE A . n 
A 1 65  LEU 65  35  35  LEU LEU A . n 
A 1 66  ALA 66  36  36  ALA ALA A . n 
A 1 67  TRP 67  37  37  TRP TRP A . n 
A 1 68  TYR 68  38  38  TYR TYR A . n 
A 1 69  GLN 69  39  39  GLN GLN A . n 
A 1 70  GLN 70  40  40  GLN GLN A . n 
A 1 71  LYS 71  41  41  LYS LYS A . n 
A 1 72  PRO 72  42  42  PRO PRO A . n 
A 1 73  GLY 73  43  43  GLY GLY A . n 
A 1 74  GLN 74  44  44  GLN GLN A . n 
A 1 75  ALA 75  45  45  ALA ALA A . n 
A 1 76  PRO 76  46  46  PRO PRO A . n 
A 1 77  ARG 77  47  47  ARG ARG A . n 
A 1 78  LEU 78  48  48  LEU LEU A . n 
A 1 79  LEU 79  49  49  LEU LEU A . n 
A 1 80  ILE 80  50  50  ILE ILE A . n 
A 1 81  TYR 81  51  51  TYR TYR A . n 
A 1 82  GLY 82  52  52  GLY GLY A . n 
A 1 83  ALA 83  53  53  ALA ALA A . n 
A 1 84  SER 84  54  54  SER SER A . n 
A 1 85  TYR 85  55  55  TYR TYR A . n 
A 1 86  MET 86  56  56  MET MET A . n 
A 1 87  ALA 87  57  57  ALA ALA A . n 
A 1 88  THR 88  58  58  THR THR A . n 
A 1 89  GLY 89  59  59  GLY GLY A . n 
A 1 90  ILE 90  60  60  ILE ILE A . n 
A 1 91  PRO 91  61  61  PRO PRO A . n 
A 1 92  ASP 92  62  62  ASP ASP A . n 
A 1 93  ARG 93  63  63  ARG ARG A . n 
A 1 94  PHE 94  64  64  PHE PHE A . n 
A 1 95  SER 95  65  65  SER SER A . n 
A 1 96  GLY 96  66  66  GLY GLY A . n 
A 1 97  SER 97  67  67  SER SER A . n 
A 1 98  GLY 98  68  68  GLY GLY A . n 
A 1 99  SER 99  69  69  SER SER A . n 
A 1 100 GLY 100 70  70  GLY GLY A . n 
A 1 101 THR 101 71  71  THR THR A . n 
A 1 102 ASP 102 72  72  ASP ASP A . n 
A 1 103 PHE 103 73  73  PHE PHE A . n 
A 1 104 THR 104 74  74  THR THR A . n 
A 1 105 LEU 105 75  75  LEU LEU A . n 
A 1 106 THR 106 76  76  THR THR A . n 
A 1 107 ILE 107 77  77  ILE ILE A . n 
A 1 108 SER 108 78  78  SER SER A . n 
A 1 109 ARG 109 79  79  ARG ARG A . n 
A 1 110 LEU 110 80  80  LEU LEU A . n 
A 1 111 GLU 111 81  81  GLU GLU A . n 
A 1 112 PRO 112 82  82  PRO PRO A . n 
A 1 113 GLU 113 83  83  GLU GLU A . n 
A 1 114 ASP 114 84  84  ASP ASP A . n 
A 1 115 PHE 115 85  85  PHE PHE A . n 
A 1 116 ALA 116 86  86  ALA ALA A . n 
A 1 117 VAL 117 87  87  VAL VAL A . n 
A 1 118 TYR 118 88  88  TYR TYR A . n 
A 1 119 TYR 119 89  89  TYR TYR A . n 
A 1 120 CYS 120 90  90  CYS CYS A . n 
A 1 121 GLN 121 91  91  GLN GLN A . n 
A 1 122 GLN 122 92  92  GLN GLN A . n 
A 1 123 TYR 123 93  93  TYR TYR A . n 
A 1 124 GLY 124 94  94  GLY GLY A . n 
A 1 125 SER 125 95  95  SER SER A . n 
A 1 126 SER 126 96  96  SER SER A . n 
A 1 127 LEU 127 97  97  LEU LEU A . n 
A 1 128 THR 128 98  98  THR THR A . n 
A 1 129 PHE 129 99  99  PHE PHE A . n 
A 1 130 GLY 130 100 100 GLY GLY A . n 
A 1 131 GLY 131 101 101 GLY GLY A . n 
A 1 132 GLY 132 102 102 GLY GLY A . n 
A 1 133 THR 133 103 103 THR THR A . n 
A 1 134 LYS 134 104 104 LYS LYS A . n 
A 1 135 LEU 135 105 105 LEU LEU A . n 
A 1 136 GLU 136 106 106 GLU GLU A . n 
A 1 137 ILE 137 107 107 ILE ILE A . n 
A 1 138 LYS 138 108 108 LYS LYS A . n 
A 1 139 GLY 139 109 ?   ?   ?   A . n 
A 1 140 GLY 140 110 ?   ?   ?   A . n 
A 1 141 GLY 141 111 ?   ?   ?   A . n 
A 1 142 GLY 142 112 ?   ?   ?   A . n 
A 1 143 SER 143 113 ?   ?   ?   A . n 
A 1 144 GLY 144 114 ?   ?   ?   A . n 
A 1 145 GLY 145 115 ?   ?   ?   A . n 
A 1 146 GLY 146 116 ?   ?   ?   A . n 
A 1 147 GLY 147 117 ?   ?   ?   A . n 
A 1 148 SER 148 118 ?   ?   ?   A . n 
A 1 149 GLY 149 119 ?   ?   ?   A . n 
A 1 150 GLY 150 120 ?   ?   ?   A . n 
A 1 151 GLY 151 121 ?   ?   ?   A . n 
A 1 152 GLY 152 122 ?   ?   ?   A . n 
A 1 153 SER 153 123 123 SER SER A . n 
A 1 154 GLN 154 124 124 GLN GLN A . n 
A 1 155 VAL 155 125 125 VAL VAL A . n 
A 1 156 GLN 156 126 126 GLN GLN A . n 
A 1 157 LEU 157 127 127 LEU LEU A . n 
A 1 158 GLN 158 128 128 GLN GLN A . n 
A 1 159 GLN 159 129 129 GLN GLN A . n 
A 1 160 SER 160 130 130 SER SER A . n 
A 1 161 GLY 161 131 131 GLY GLY A . n 
A 1 162 PRO 162 132 132 PRO PRO A . n 
A 1 163 GLY 163 133 133 GLY GLY A . n 
A 1 164 LEU 164 134 134 LEU LEU A . n 
A 1 165 VAL 165 135 135 VAL VAL A . n 
A 1 166 LYS 166 136 136 LYS LYS A . n 
A 1 167 PRO 167 137 137 PRO PRO A . n 
A 1 168 SER 168 138 138 SER SER A . n 
A 1 169 GLN 169 139 139 GLN GLN A . n 
A 1 170 THR 170 140 140 THR THR A . n 
A 1 171 LEU 171 141 141 LEU LEU A . n 
A 1 172 SER 172 142 142 SER SER A . n 
A 1 173 LEU 173 143 143 LEU LEU A . n 
A 1 174 THR 174 144 144 THR THR A . n 
A 1 175 CYS 175 145 145 CYS CYS A . n 
A 1 176 SER 176 146 146 SER SER A . n 
A 1 177 ILE 177 147 147 ILE ILE A . n 
A 1 178 SER 178 148 148 SER SER A . n 
A 1 179 GLY 179 149 149 GLY GLY A . n 
A 1 180 ASP 180 150 150 ASP ASP A . n 
A 1 181 SER 181 151 151 SER SER A . n 
A 1 182 VAL 182 152 152 VAL VAL A . n 
A 1 183 SER 183 153 153 SER SER A . n 
A 1 184 SER 184 154 154 SER SER A . n 
A 1 185 ASN 185 155 155 ASN ASN A . n 
A 1 186 SER 186 156 156 SER SER A . n 
A 1 187 ALA 187 157 157 ALA ALA A . n 
A 1 188 ALA 188 158 158 ALA ALA A . n 
A 1 189 TRP 189 159 159 TRP TRP A . n 
A 1 190 ASN 190 160 160 ASN ASN A . n 
A 1 191 TRP 191 161 161 TRP TRP A . n 
A 1 192 ILE 192 162 162 ILE ILE A . n 
A 1 193 ARG 193 163 163 ARG ARG A . n 
A 1 194 GLN 194 164 164 GLN GLN A . n 
A 1 195 SER 195 165 165 SER SER A . n 
A 1 196 PRO 196 166 166 PRO PRO A . n 
A 1 197 SER 197 167 167 SER SER A . n 
A 1 198 ARG 198 168 168 ARG ARG A . n 
A 1 199 GLY 199 169 169 GLY GLY A . n 
A 1 200 LEU 200 170 170 LEU LEU A . n 
A 1 201 GLU 201 171 171 GLU GLU A . n 
A 1 202 TRP 202 172 172 TRP TRP A . n 
A 1 203 LEU 203 173 173 LEU LEU A . n 
A 1 204 GLY 204 174 174 GLY GLY A . n 
A 1 205 ARG 205 175 175 ARG ARG A . n 
A 1 206 THR 206 176 176 THR THR A . n 
A 1 207 TYR 207 177 177 TYR TYR A . n 
A 1 208 TYR 208 178 178 TYR TYR A . n 
A 1 209 ARG 209 179 179 ARG ARG A . n 
A 1 210 SER 210 180 180 SER SER A . n 
A 1 211 LYS 211 181 181 LYS LYS A . n 
A 1 212 TRP 212 182 182 TRP TRP A . n 
A 1 213 TYR 213 183 183 TYR TYR A . n 
A 1 214 ASN 214 184 184 ASN ASN A . n 
A 1 215 ASP 215 185 185 ASP ASP A . n 
A 1 216 TYR 216 186 186 TYR TYR A . n 
A 1 217 ALA 217 187 187 ALA ALA A . n 
A 1 218 GLY 218 188 188 GLY GLY A . n 
A 1 219 THR 219 189 189 THR THR A . n 
A 1 220 VAL 220 190 190 VAL VAL A . n 
A 1 221 LYS 221 191 191 LYS LYS A . n 
A 1 222 SER 222 192 192 SER SER A . n 
A 1 223 ARG 223 193 193 ARG ARG A . n 
A 1 224 ILE 224 194 194 ILE ILE A . n 
A 1 225 ALA 225 195 195 ALA ALA A . n 
A 1 226 ILE 226 196 196 ILE ILE A . n 
A 1 227 ASN 227 197 197 ASN ASN A . n 
A 1 228 PRO 228 198 198 PRO PRO A . n 
A 1 229 ASP 229 199 199 ASP ASP A . n 
A 1 230 THR 230 200 200 THR THR A . n 
A 1 231 SER 231 201 201 SER SER A . n 
A 1 232 LYS 232 202 202 LYS LYS A . n 
A 1 233 ASN 233 203 203 ASN ASN A . n 
A 1 234 GLN 234 204 204 GLN GLN A . n 
A 1 235 PHE 235 205 205 PHE PHE A . n 
A 1 236 SER 236 206 206 SER SER A . n 
A 1 237 LEU 237 207 207 LEU LEU A . n 
A 1 238 HIS 238 208 208 HIS HIS A . n 
A 1 239 LEU 239 209 209 LEU LEU A . n 
A 1 240 ASN 240 210 210 ASN ASN A . n 
A 1 241 SER 241 211 211 SER SER A . n 
A 1 242 VAL 242 212 212 VAL VAL A . n 
A 1 243 THR 243 213 213 THR THR A . n 
A 1 244 PRO 244 214 214 PRO PRO A . n 
A 1 245 GLU 245 215 215 GLU GLU A . n 
A 1 246 ASP 246 216 216 ASP ASP A . n 
A 1 247 THR 247 217 217 THR THR A . n 
A 1 248 ALA 248 218 218 ALA ALA A . n 
A 1 249 VAL 249 219 219 VAL VAL A . n 
A 1 250 TYR 250 220 220 TYR TYR A . n 
A 1 251 PHE 251 221 221 PHE PHE A . n 
A 1 252 CYS 252 222 222 CYS CYS A . n 
A 1 253 ALA 253 223 223 ALA ALA A . n 
A 1 254 ARG 254 224 224 ARG ARG A . n 
A 1 255 VAL 255 225 225 VAL VAL A . n 
A 1 256 ILE 256 226 226 ILE ILE A . n 
A 1 257 SER 257 227 227 SER SER A . n 
A 1 258 VAL 258 228 228 VAL VAL A . n 
A 1 259 ALA 259 229 229 ALA ALA A . n 
A 1 260 GLY 260 230 230 GLY GLY A . n 
A 1 261 TYR 261 231 231 TYR TYR A . n 
A 1 262 ALA 262 232 232 ALA ALA A . n 
A 1 263 PHE 263 233 233 PHE PHE A . n 
A 1 264 ASP 264 234 234 ASP ASP A . n 
A 1 265 ILE 265 235 235 ILE ILE A . n 
A 1 266 TRP 266 236 236 TRP TRP A . n 
A 1 267 GLY 267 237 237 GLY GLY A . n 
A 1 268 GLN 268 238 238 GLN GLN A . n 
A 1 269 GLY 269 239 239 GLY GLY A . n 
A 1 270 THR 270 240 240 THR THR A . n 
A 1 271 MET 271 241 241 MET MET A . n 
A 1 272 VAL 272 242 242 VAL VAL A . n 
A 1 273 THR 273 243 243 THR THR A . n 
A 1 274 VAL 274 244 244 VAL VAL A . n 
A 1 275 SER 275 245 245 SER SER A . n 
A 1 276 SER 276 246 246 SER SER A . n 
A 1 277 HIS 277 247 ?   ?   ?   A . n 
A 1 278 HIS 278 248 ?   ?   ?   A . n 
A 1 279 HIS 279 249 ?   ?   ?   A . n 
A 1 280 HIS 280 250 ?   ?   ?   A . n 
A 1 281 HIS 281 251 ?   ?   ?   A . n 
A 1 282 HIS 282 252 ?   ?   ?   A . n 
B 2 1   PRO 1   322 ?   ?   ?   C . n 
B 2 2   THR 2   323 ?   ?   ?   C . n 
B 2 3   GLU 3   324 ?   ?   ?   C . n 
B 2 4   SER 4   325 ?   ?   ?   C . n 
B 2 5   ILE 5   326 ?   ?   ?   C . n 
B 2 6   VAL 6   327 ?   ?   ?   C . n 
B 2 7   ARG 7   328 ?   ?   ?   C . n 
B 2 8   PHE 8   329 ?   ?   ?   C . n 
B 2 9   PRO 9   330 ?   ?   ?   C . n 
B 2 10  ASN 10  331 ?   ?   ?   C . n 
B 2 11  ILE 11  332 ?   ?   ?   C . n 
B 2 12  THR 12  333 ?   ?   ?   C . n 
B 2 13  ASN 13  334 ?   ?   ?   C . n 
B 2 14  LEU 14  335 ?   ?   ?   C . n 
B 2 15  CYS 15  336 ?   ?   ?   C . n 
B 2 16  PRO 16  337 ?   ?   ?   C . n 
B 2 17  PHE 17  338 338 PHE PHE C . n 
B 2 18  GLY 18  339 339 GLY GLY C . n 
B 2 19  GLU 19  340 340 GLU GLU C . n 
B 2 20  VAL 20  341 341 VAL VAL C . n 
B 2 21  PHE 21  342 342 PHE PHE C . n 
B 2 22  ASN 22  343 343 ASN ASN C . n 
B 2 23  ALA 23  344 344 ALA ALA C . n 
B 2 24  THR 24  345 345 THR THR C . n 
B 2 25  ARG 25  346 346 ARG ARG C . n 
B 2 26  PHE 26  347 347 PHE PHE C . n 
B 2 27  ALA 27  348 348 ALA ALA C . n 
B 2 28  SER 28  349 349 SER SER C . n 
B 2 29  VAL 29  350 350 VAL VAL C . n 
B 2 30  TYR 30  351 351 TYR TYR C . n 
B 2 31  ALA 31  352 352 ALA ALA C . n 
B 2 32  TRP 32  353 353 TRP TRP C . n 
B 2 33  ASN 33  354 354 ASN ASN C . n 
B 2 34  ARG 34  355 355 ARG ARG C . n 
B 2 35  LYS 35  356 356 LYS LYS C . n 
B 2 36  ARG 36  357 357 ARG ARG C . n 
B 2 37  ILE 37  358 358 ILE ILE C . n 
B 2 38  SER 38  359 359 SER SER C . n 
B 2 39  ASN 39  360 360 ASN ASN C . n 
B 2 40  CYS 40  361 361 CYS CYS C . n 
B 2 41  VAL 41  362 362 VAL VAL C . n 
B 2 42  ALA 42  363 363 ALA ALA C . n 
B 2 43  ASP 43  364 364 ASP ASP C . n 
B 2 44  TYR 44  365 365 TYR TYR C . n 
B 2 45  SER 45  366 366 SER SER C . n 
B 2 46  VAL 46  367 367 VAL VAL C . n 
B 2 47  LEU 47  368 368 LEU LEU C . n 
B 2 48  TYR 48  369 369 TYR TYR C . n 
B 2 49  ASN 49  370 370 ASN ASN C . n 
B 2 50  SER 50  371 371 SER SER C . n 
B 2 51  ALA 51  372 372 ALA ALA C . n 
B 2 52  SER 52  373 373 SER SER C . n 
B 2 53  PHE 53  374 374 PHE PHE C . n 
B 2 54  SER 54  375 375 SER SER C . n 
B 2 55  THR 55  376 376 THR THR C . n 
B 2 56  PHE 56  377 377 PHE PHE C . n 
B 2 57  LYS 57  378 378 LYS LYS C . n 
B 2 58  CYS 58  379 379 CYS CYS C . n 
B 2 59  TYR 59  380 380 TYR TYR C . n 
B 2 60  GLY 60  381 381 GLY GLY C . n 
B 2 61  VAL 61  382 382 VAL VAL C . n 
B 2 62  SER 62  383 383 SER SER C . n 
B 2 63  PRO 63  384 384 PRO PRO C . n 
B 2 64  THR 64  385 385 THR THR C . n 
B 2 65  LYS 65  386 386 LYS LYS C . n 
B 2 66  LEU 66  387 387 LEU LEU C . n 
B 2 67  ASN 67  388 388 ASN ASN C . n 
B 2 68  ASP 68  389 ?   ?   ?   C . n 
B 2 69  LEU 69  390 ?   ?   ?   C . n 
B 2 70  CYS 70  391 ?   ?   ?   C . n 
B 2 71  PHE 71  392 ?   ?   ?   C . n 
B 2 72  THR 72  393 ?   ?   ?   C . n 
B 2 73  ASN 73  394 394 ASN ASN C . n 
B 2 74  VAL 74  395 395 VAL VAL C . n 
B 2 75  TYR 75  396 396 TYR TYR C . n 
B 2 76  ALA 76  397 397 ALA ALA C . n 
B 2 77  ASP 77  398 398 ASP ASP C . n 
B 2 78  SER 78  399 399 SER SER C . n 
B 2 79  PHE 79  400 400 PHE PHE C . n 
B 2 80  VAL 80  401 401 VAL VAL C . n 
B 2 81  ILE 81  402 402 ILE ILE C . n 
B 2 82  ARG 82  403 403 ARG ARG C . n 
B 2 83  GLY 83  404 404 GLY GLY C . n 
B 2 84  ASP 84  405 405 ASP ASP C . n 
B 2 85  GLU 85  406 406 GLU GLU C . n 
B 2 86  VAL 86  407 407 VAL VAL C . n 
B 2 87  ARG 87  408 408 ARG ARG C . n 
B 2 88  GLN 88  409 409 GLN GLN C . n 
B 2 89  ILE 89  410 410 ILE ILE C . n 
B 2 90  ALA 90  411 411 ALA ALA C . n 
B 2 91  PRO 91  412 412 PRO PRO C . n 
B 2 92  GLY 92  413 413 GLY GLY C . n 
B 2 93  GLN 93  414 414 GLN GLN C . n 
B 2 94  THR 94  415 415 THR THR C . n 
B 2 95  GLY 95  416 416 GLY GLY C . n 
B 2 96  LYS 96  417 417 LYS LYS C . n 
B 2 97  ILE 97  418 418 ILE ILE C . n 
B 2 98  ALA 98  419 419 ALA ALA C . n 
B 2 99  ASP 99  420 420 ASP ASP C . n 
B 2 100 TYR 100 421 421 TYR TYR C . n 
B 2 101 ASN 101 422 422 ASN ASN C . n 
B 2 102 TYR 102 423 423 TYR TYR C . n 
B 2 103 LYS 103 424 424 LYS LYS C . n 
B 2 104 LEU 104 425 425 LEU LEU C . n 
B 2 105 PRO 105 426 426 PRO PRO C . n 
B 2 106 ASP 106 427 427 ASP ASP C . n 
B 2 107 ASP 107 428 428 ASP ASP C . n 
B 2 108 PHE 108 429 429 PHE PHE C . n 
B 2 109 THR 109 430 430 THR THR C . n 
B 2 110 GLY 110 431 431 GLY GLY C . n 
B 2 111 CYS 111 432 432 CYS CYS C . n 
B 2 112 VAL 112 433 433 VAL VAL C . n 
B 2 113 ILE 113 434 434 ILE ILE C . n 
B 2 114 ALA 114 435 435 ALA ALA C . n 
B 2 115 TRP 115 436 436 TRP TRP C . n 
B 2 116 ASN 116 437 437 ASN ASN C . n 
B 2 117 SER 117 438 438 SER SER C . n 
B 2 118 ASN 118 439 439 ASN ASN C . n 
B 2 119 ASN 119 440 440 ASN ASN C . n 
B 2 120 LEU 120 441 441 LEU LEU C . n 
B 2 121 ASP 121 442 442 ASP ASP C . n 
B 2 122 SER 122 443 443 SER SER C . n 
B 2 123 LYS 123 444 444 LYS LYS C . n 
B 2 124 VAL 124 445 445 VAL VAL C . n 
B 2 125 GLY 125 446 446 GLY GLY C . n 
B 2 126 GLY 126 447 447 GLY GLY C . n 
B 2 127 ASN 127 448 448 ASN ASN C . n 
B 2 128 TYR 128 449 449 TYR TYR C . n 
B 2 129 ASN 129 450 450 ASN ASN C . n 
B 2 130 TYR 130 451 451 TYR TYR C . n 
B 2 131 LEU 131 452 452 LEU LEU C . n 
B 2 132 TYR 132 453 453 TYR TYR C . n 
B 2 133 ARG 133 454 454 ARG ARG C . n 
B 2 134 LEU 134 455 455 LEU LEU C . n 
B 2 135 PHE 135 456 456 PHE PHE C . n 
B 2 136 ARG 136 457 457 ARG ARG C . n 
B 2 137 LYS 137 458 458 LYS LYS C . n 
B 2 138 SER 138 459 459 SER SER C . n 
B 2 139 ASN 139 460 460 ASN ASN C . n 
B 2 140 LEU 140 461 461 LEU LEU C . n 
B 2 141 LYS 141 462 462 LYS LYS C . n 
B 2 142 PRO 142 463 463 PRO PRO C . n 
B 2 143 PHE 143 464 464 PHE PHE C . n 
B 2 144 GLU 144 465 465 GLU GLU C . n 
B 2 145 ARG 145 466 466 ARG ARG C . n 
B 2 146 ASP 146 467 467 ASP ASP C . n 
B 2 147 ILE 147 468 468 ILE ILE C . n 
B 2 148 SER 148 469 469 SER SER C . n 
B 2 149 THR 149 470 470 THR THR C . n 
B 2 150 GLU 150 471 471 GLU GLU C . n 
B 2 151 ILE 151 472 472 ILE ILE C . n 
B 2 152 TYR 152 473 473 TYR TYR C . n 
B 2 153 GLN 153 474 474 GLN GLN C . n 
B 2 154 ALA 154 475 475 ALA ALA C . n 
B 2 155 GLY 155 476 476 GLY GLY C . n 
B 2 156 SER 156 477 477 SER SER C . n 
B 2 157 THR 157 478 478 THR THR C . n 
B 2 158 PRO 158 479 479 PRO PRO C . n 
B 2 159 CYS 159 480 480 CYS CYS C . n 
B 2 160 ASN 160 481 481 ASN ASN C . n 
B 2 161 GLY 161 482 482 GLY GLY C . n 
B 2 162 VAL 162 483 483 VAL VAL C . n 
B 2 163 GLU 163 484 484 GLU GLU C . n 
B 2 164 GLY 164 485 485 GLY GLY C . n 
B 2 165 PHE 165 486 486 PHE PHE C . n 
B 2 166 ASN 166 487 487 ASN ASN C . n 
B 2 167 CYS 167 488 488 CYS CYS C . n 
B 2 168 TYR 168 489 489 TYR TYR C . n 
B 2 169 PHE 169 490 490 PHE PHE C . n 
B 2 170 PRO 170 491 491 PRO PRO C . n 
B 2 171 LEU 171 492 492 LEU LEU C . n 
B 2 172 GLN 172 493 493 GLN GLN C . n 
B 2 173 SER 173 494 494 SER SER C . n 
B 2 174 TYR 174 495 495 TYR TYR C . n 
B 2 175 GLY 175 496 496 GLY GLY C . n 
B 2 176 PHE 176 497 497 PHE PHE C . n 
B 2 177 GLN 177 498 498 GLN GLN C . n 
B 2 178 PRO 178 499 499 PRO PRO C . n 
B 2 179 THR 179 500 500 THR THR C . n 
B 2 180 ASN 180 501 501 ASN ASN C . n 
B 2 181 GLY 181 502 502 GLY GLY C . n 
B 2 182 VAL 182 503 503 VAL VAL C . n 
B 2 183 GLY 183 504 504 GLY GLY C . n 
B 2 184 TYR 184 505 505 TYR TYR C . n 
B 2 185 GLN 185 506 506 GLN GLN C . n 
B 2 186 PRO 186 507 507 PRO PRO C . n 
B 2 187 TYR 187 508 508 TYR TYR C . n 
B 2 188 ARG 188 509 509 ARG ARG C . n 
B 2 189 VAL 189 510 510 VAL VAL C . n 
B 2 190 VAL 190 511 511 VAL VAL C . n 
B 2 191 VAL 191 512 512 VAL VAL C . n 
B 2 192 LEU 192 513 513 LEU LEU C . n 
B 2 193 SER 193 514 514 SER SER C . n 
B 2 194 PHE 194 515 515 PHE PHE C . n 
B 2 195 GLU 195 516 516 GLU GLU C . n 
B 2 196 LEU 196 517 ?   ?   ?   C . n 
B 2 197 LEU 197 518 ?   ?   ?   C . n 
B 2 198 HIS 198 519 ?   ?   ?   C . n 
B 2 199 ALA 199 520 ?   ?   ?   C . n 
B 2 200 PRO 200 521 ?   ?   ?   C . n 
B 2 201 ALA 201 522 522 ALA ALA C . n 
B 2 202 THR 202 523 523 THR THR C . n 
B 2 203 VAL 203 524 524 VAL VAL C . n 
B 2 204 CYS 204 525 525 CYS CYS C . n 
B 2 205 GLY 205 526 ?   ?   ?   C . n 
B 2 206 PRO 206 527 ?   ?   ?   C . n 
B 2 207 LYS 207 528 ?   ?   ?   C . n 
B 2 208 LYS 208 529 ?   ?   ?   C . n 
B 2 209 SER 209 530 ?   ?   ?   C . n 
B 2 210 THR 210 531 ?   ?   ?   C . n 
B 2 211 ASN 211 532 ?   ?   ?   C . n 
B 2 212 LEU 212 533 ?   ?   ?   C . n 
B 2 213 VAL 213 534 ?   ?   ?   C . n 
B 2 214 LYS 214 535 ?   ?   ?   C . n 
B 2 215 ASN 215 536 ?   ?   ?   C . n 
# 
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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? 1.18_3845 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 1.18_3845 2 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1    3 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YK4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     55.152 
_cell.length_a_esd                 ? 
_cell.length_b                     149.641 
_cell.length_b_esd                 ? 
_cell.length_c                     253.429 
_cell.length_c_esd                 ? 
_cell.volume                       2091549.646 
_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                         8YK4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8YK4 
_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             4.84 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          74.59 
_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    '0.1M CHES pH9.5, 20% PEG8000' 
_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 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-07-21 
_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   1.00000 
_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                        'SPRING-8 BEAMLINE BL32XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL32XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          59.17 
_reflns.entry_id                                       8YK4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.20 
_reflns.d_resolution_low                               48.35 
_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                                     17765 
_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                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.7 
_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                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.987 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    3.20 
_reflns_shell.d_res_low                                     3.42 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3153 
_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                               ? 
_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                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.522 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               74.12 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_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                                 8YK4 
_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                            3.20 
_refine.ls_d_res_low                             48.35 
_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                     17738 
_refine.ls_number_reflns_R_free                  861 
_refine.ls_number_reflns_R_work                  16877 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.27 
_refine.ls_percent_reflns_R_free                 4.85 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2440 
_refine.ls_R_factor_R_free                       0.2671 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2429 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.33 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 25.2935 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.4561 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.20 
_refine_hist.d_res_low                        48.35 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               3179 
_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        3179 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.0011  ? 3258 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4014  ? 4426 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0417  ? 476  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0032  ? 570  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.9849 ? 1151 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_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 
'X-RAY DIFFRACTION' 3.20 3.40  . . 151 2735 98.94 . . . . 0.3223 . . . . . . . . . . . 0.3472 
'X-RAY DIFFRACTION' 3.40 3.66  . . 158 2764 99.19 . . . . 0.2886 . . . . . . . . . . . 0.3301 
'X-RAY DIFFRACTION' 3.66 4.03  . . 138 2761 99.18 . . . . 0.2637 . . . . . . . . . . . 0.3033 
'X-RAY DIFFRACTION' 4.03 4.61  . . 133 2810 99.53 . . . . 0.2035 . . . . . . . . . . . 0.2083 
'X-RAY DIFFRACTION' 4.61 5.81  . . 146 2817 99.40 . . . . 0.2006 . . . . . . . . . . . 0.2324 
'X-RAY DIFFRACTION' 5.81 48.35 . . 135 2990 99.40 . . . . 0.2427 . . . . . . . . . . . 0.2487 
# 
_struct.entry_id                     8YK4 
_struct.title                        'Structure of SARS-CoV-2 RBD and antibody NT-108' 
_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        8YK4 
_struct_keywords.text            'SARS-CoV-2, spike, RBD, antibody, IgG, scFv, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
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 2 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 8YK4             8YK4       ? 1 ? 1   
2 UNP A0A7U3DZD0_SARS2 A0A7U3DZD0 ? 2 
;PTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFV
IRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCN
GVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKN
;
322 
# 
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 8YK4 A 1 ? 282 ? 8YK4       -29 ? 252 ? -29 252 
2 2 8YK4 C 1 ? 215 ? A0A7U3DZD0 322 ? 536 ? 322 536 
# 
_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)' 2090  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  18420 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 GLU A 111 ? PHE A 115 ? GLU A 81  PHE A 85  5 ? 5 
HELX_P HELX_P2 AA2 VAL A 220 ? SER A 222 ? VAL A 190 SER A 192 5 ? 3 
HELX_P HELX_P3 AA3 THR A 243 ? THR A 247 ? THR A 213 THR A 217 5 ? 5 
HELX_P HELX_P4 AA4 GLY B 18  ? ASN B 22  ? GLY C 339 ASN C 343 1 ? 5 
HELX_P HELX_P5 AA5 GLY B 83  ? ILE B 89  ? GLY C 404 ILE C 410 5 ? 7 
HELX_P HELX_P6 AA6 GLY B 95  ? ASN B 101 ? GLY C 416 ASN C 422 1 ? 7 
HELX_P HELX_P7 AA7 GLY B 181 ? GLN B 185 ? GLY C 502 GLN C 506 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 54  SG ? ? ? 1_555 A CYS 120 SG ? ? A CYS 24  A CYS 90  1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf2 disulf ? ? A CYS 175 SG ? ? ? 1_555 A CYS 252 SG ? ? A CYS 145 A CYS 222 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
disulf3 disulf ? ? B CYS 58  SG ? ? ? 1_555 B CYS 111 SG ? ? C CYS 379 C CYS 432 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf4 disulf ? ? B CYS 159 SG ? ? ? 1_555 B CYS 167 SG ? ? C CYS 480 C CYS 488 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 54  ? CYS A 120 ? CYS A 24  ? 1_555 CYS A 90  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 175 ? CYS A 252 ? CYS A 145 ? 1_555 CYS A 222 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS B 58  ? CYS B 111 ? CYS C 379 ? 1_555 CYS C 432 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS B 159 ? CYS B 167 ? CYS C 480 ? 1_555 CYS C 488 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          SER 
_struct_mon_prot_cis.label_seq_id           38 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           SER 
_struct_mon_prot_cis.auth_seq_id            8 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    39 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     9 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -0.36 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
# 
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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? parallel      
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-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 LEU A 35  ? SER A 38  ? LEU A 5   SER A 8   
AA1 2 ALA A 50  ? ALA A 56  ? ALA A 20  ALA A 26  
AA1 3 ASP A 102 ? ILE A 107 ? ASP A 72  ILE A 77  
AA1 4 PHE A 94  ? SER A 99  ? PHE A 64  SER A 69  
AA2 1 THR A 41  ? LEU A 44  ? THR A 11  LEU A 14  
AA2 2 THR A 133 ? ILE A 137 ? THR A 103 ILE A 107 
AA2 3 ALA A 116 ? TYR A 123 ? ALA A 86  TYR A 93  
AA2 4 ALA A 66  ? GLN A 70  ? ALA A 36  GLN A 40  
AA2 5 ARG A 77  ? TYR A 81  ? ARG A 47  TYR A 51  
AA2 6 TYR A 85  ? MET A 86  ? TYR A 55  MET A 56  
AA3 1 THR A 41  ? LEU A 44  ? THR A 11  LEU A 14  
AA3 2 THR A 133 ? ILE A 137 ? THR A 103 ILE A 107 
AA3 3 ALA A 116 ? TYR A 123 ? ALA A 86  TYR A 93  
AA3 4 LEU A 127 ? PHE A 129 ? LEU A 97  PHE A 99  
AA4 1 GLN A 156 ? SER A 160 ? GLN A 126 SER A 130 
AA4 2 LEU A 171 ? SER A 178 ? LEU A 141 SER A 148 
AA4 3 GLN A 234 ? LEU A 239 ? GLN A 204 LEU A 209 
AA4 4 ILE A 224 ? ASP A 229 ? ILE A 194 ASP A 199 
AA5 1 LEU A 164 ? VAL A 165 ? LEU A 134 VAL A 135 
AA5 2 THR A 270 ? VAL A 274 ? THR A 240 VAL A 244 
AA5 3 ALA A 248 ? VAL A 255 ? ALA A 218 VAL A 225 
AA5 4 ALA A 188 ? SER A 195 ? ALA A 158 SER A 165 
AA5 5 GLY A 199 ? TYR A 208 ? GLY A 169 TYR A 178 
AA5 6 TRP A 212 ? TYR A 216 ? TRP A 182 TYR A 186 
AA6 1 LEU A 164 ? VAL A 165 ? LEU A 134 VAL A 135 
AA6 2 THR A 270 ? VAL A 274 ? THR A 240 VAL A 244 
AA6 3 ALA A 248 ? VAL A 255 ? ALA A 218 VAL A 225 
AA6 4 PHE A 263 ? TRP A 266 ? PHE A 233 TRP A 236 
AA7 1 ASN B 33  ? ILE B 37  ? ASN C 354 ILE C 358 
AA7 2 VAL B 74  ? ILE B 81  ? VAL C 395 ILE C 402 
AA7 3 TYR B 187 ? PHE B 194 ? TYR C 508 PHE C 515 
AA7 4 GLY B 110 ? ASN B 116 ? GLY C 431 ASN C 437 
AA7 5 THR B 55  ? CYS B 58  ? THR C 376 CYS C 379 
AA8 1 CYS B 40  ? VAL B 41  ? CYS C 361 VAL C 362 
AA8 2 VAL B 203 ? CYS B 204 ? VAL C 524 CYS C 525 
AA9 1 LEU B 131 ? ARG B 133 ? LEU C 452 ARG C 454 
AA9 2 LEU B 171 ? SER B 173 ? LEU C 492 SER C 494 
AB1 1 TYR B 152 ? GLN B 153 ? TYR C 473 GLN C 474 
AB1 2 CYS B 167 ? TYR B 168 ? CYS C 488 TYR C 489 
# 
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 N THR A 36  ? N THR A 6   O ARG A 55  ? O ARG A 25  
AA1 2 3 N LEU A 52  ? N LEU A 22  O LEU A 105 ? O LEU A 75  
AA1 3 4 O THR A 104 ? O THR A 74  N SER A 97  ? N SER A 67  
AA2 1 2 N LEU A 42  ? N LEU A 12  O GLU A 136 ? O GLU A 106 
AA2 2 3 O THR A 133 ? O THR A 103 N TYR A 118 ? N TYR A 88  
AA2 3 4 O GLN A 121 ? O GLN A 91  N ALA A 66  ? N ALA A 36  
AA2 4 5 N GLN A 69  ? N GLN A 39  O ARG A 77  ? O ARG A 47  
AA2 5 6 N TYR A 81  ? N TYR A 51  O TYR A 85  ? O TYR A 55  
AA3 1 2 N LEU A 42  ? N LEU A 12  O GLU A 136 ? O GLU A 106 
AA3 2 3 O THR A 133 ? O THR A 103 N TYR A 118 ? N TYR A 88  
AA3 3 4 N GLN A 122 ? N GLN A 92  O THR A 128 ? O THR A 98  
AA4 1 2 N GLN A 158 ? N GLN A 128 O SER A 176 ? O SER A 146 
AA4 2 3 N LEU A 173 ? N LEU A 143 O LEU A 237 ? O LEU A 207 
AA4 3 4 O GLN A 234 ? O GLN A 204 N ASP A 229 ? N ASP A 199 
AA5 1 2 N VAL A 165 ? N VAL A 135 O THR A 273 ? O THR A 243 
AA5 2 3 O VAL A 272 ? O VAL A 242 N ALA A 248 ? N ALA A 218 
AA5 3 4 O PHE A 251 ? O PHE A 221 N ILE A 192 ? N ILE A 162 
AA5 4 5 N SER A 195 ? N SER A 165 O GLY A 199 ? O GLY A 169 
AA5 5 6 N TYR A 207 ? N TYR A 177 O TYR A 213 ? O TYR A 183 
AA6 1 2 N VAL A 165 ? N VAL A 135 O THR A 273 ? O THR A 243 
AA6 2 3 O VAL A 272 ? O VAL A 242 N ALA A 248 ? N ALA A 218 
AA6 3 4 N ARG A 254 ? N ARG A 224 O ILE A 265 ? O ILE A 235 
AA7 1 2 N ILE B 37  ? N ILE C 358 O VAL B 74  ? O VAL C 395 
AA7 2 3 N ASP B 77  ? N ASP C 398 O VAL B 191 ? O VAL C 512 
AA7 3 4 O VAL B 190 ? O VAL C 511 N ILE B 113 ? N ILE C 434 
AA7 4 5 O ALA B 114 ? O ALA C 435 N THR B 55  ? N THR C 376 
AA8 1 2 O CYS B 40  ? O CYS C 361 N CYS B 204 ? N CYS C 525 
AA9 1 2 N TYR B 132 ? N TYR C 453 O GLN B 172 ? O GLN C 493 
AB1 1 2 N TYR B 152 ? N TYR C 473 O TYR B 168 ? O TYR C 489 
# 
_pdbx_entry_details.entry_id                   8YK4 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 53  ? ? 65.16   -63.41  
2  1 SER A 153 ? ? -96.72  30.59   
3  1 SER A 156 ? ? -112.90 53.28   
4  1 LEU A 173 ? ? -100.89 -61.74  
5  1 ARG A 179 ? ? -113.85 -90.33  
6  1 LYS A 181 ? ? -127.78 -165.58 
7  1 ARG A 193 ? ? -159.30 13.54   
8  1 ASN A 210 ? ? -61.11  -74.94  
9  1 ALA A 229 ? ? -99.59  43.59   
10 1 ASN C 343 ? ? -83.31  38.95   
11 1 ALA C 352 ? ? -101.74 47.95   
12 1 ASN C 422 ? ? -123.21 -62.78  
13 1 SER C 443 ? ? -161.62 100.04  
14 1 PHE C 497 ? ? 60.11   80.61   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
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' ? refined 3.68572864362   11.1377520545 74.6013633283 0.441865907824 ? 0.076066104452    ? -0.0322451802809 
? 0.352576560742 ? 0.116528596671   ? 0.957961475575 ? 2.42055292541 ? 3.07010731984    ? -0.619499388065 ? 4.3403995427    ? 
0.0980418408647  ? 1.90561098412  ? 0.079161063864   ? -0.407082276341  ? -1.47888678342   ? 0.618673705528   ? 0.117865248465   ? 
0.225022683252   ? 0.328765380676   ? 0.130904033637   ? -0.151231811031  ? 
2  'X-RAY DIFFRACTION' ? refined -3.04704380319  16.4962868924 76.6268337647 0.524531501064 ? -0.0565688968253  ? 0.0949654067727  
? 0.301491015215 ? 0.0454444994886  ? 0.662695501804 ? 4.14865676027 ? 0.882084410053   ? 1.31657237485   ? 5.17893845433   ? 
0.303320612668   ? 4.98323211709  ? 0.223620700783   ? -0.308359304496  ? -0.49614163088   ? 0.550105986157   ? 0.0616246510864  ? 
0.999801017623   ? 0.244560691689   ? -0.298932308813  ? -0.355032392664  ? 
3  'X-RAY DIFFRACTION' ? refined -0.270168753766 13.4730496835 70.1908084516 0.393826878782 ? 0.0839537533397   ? -0.101250802492  
? 0.347371963737 ? 0.122653565137   ? 1.0419734851   ? 6.85347025639 ? 5.03329711498    ? -0.39554857629  ? 4.49128911701   ? 
0.657922397184   ? 1.18145959506  ? -0.437494361768  ? -0.0234459189385 ? -0.636259449965  ? -0.613676141556  ? 0.168557082285   ? 
0.544979348353   ? -0.100182076295  ? 0.0771885981291  ? 0.260748841679   ? 
4  'X-RAY DIFFRACTION' ? refined 1.49404551454   29.6336686744 54.9982475231 0.36853309539  ? 0.0623250029534   ? -0.0491844776758 
? 0.440677649005 ? 0.0529136411615  ? 0.345436701829 ? 1.60305554071 ? -1.83377032305   ? 0.309204850154  ? 5.8998049259    ? 
1.70131232728    ? 1.27873378451  ? -0.0997933449034 ? 0.536100256768   ? 0.634913051369   ? -0.373652367413  ? 0.126573522461   ? 
-0.492428058893  ? 0.381956541703   ? -0.341384471     ? 0.0676127074464  ? 
5  'X-RAY DIFFRACTION' ? refined 8.33512399381   34.3499346111 64.3076734516 0.372465034114 ? -0.00503192049588 ? -0.05371205824   
? 0.161287255207 ? -0.010483114999  ? 0.442427913808 ? 5.02666314935 ? 0.377348091145   ? -0.580392951896 ? 1.03697668007   ? 
-0.487887161112  ? 4.47413830731  ? 0.0149381416483  ? -0.0702838761906 ? 0.131637850533   ? -0.313109653986  ? 0.052034271045   ? 
0.0231740255872  ? -0.0495794440276 ? 0.137090867492   ? -0.0871578632168 ? 
6  'X-RAY DIFFRACTION' ? refined 5.47841083653   26.7250529949 60.8943810405 0.344402228499 ? -0.00340734339481 ? 0.0140255002132  
? 0.177587829458 ? 0.0506974769285  ? 0.508249463968 ? 2.5397101331  ? -0.920590709121  ? -1.82222368241  ? 2.49603227483   ? 
3.8011110309     ? 9.31973036504  ? 0.0263365956867  ? 0.0662636745174  ? -0.0750284991822 ? -0.0293400414633 ? 0.110781107395   ? 
-0.0853487489688 ? 0.274828630634   ? -0.0362513349767 ? -0.22198747377   ? 
7  'X-RAY DIFFRACTION' ? refined -10.1047228403  36.5514997995 99.429407868  0.793781226973 ? 0.192129756766    ? -0.082116757017  
? 0.8653794203   ? -0.12333544726   ? 0.50739647706  ? 6.0469950215  ? 1.11388919342    ? -0.192202829461 ? 8.75192782159   ? 
-0.990561161488  ? 1.99721978792  ? -0.23113790709   ? -1.3713532927    ? 0.593710637121   ? -0.348466617157  ? 0.948400879866   ? 
0.667969209853   ? -0.451965326357  ? 0.530624202365   ? -0.774600249645  ? 
8  'X-RAY DIFFRACTION' ? refined -12.0781262882  38.7110753323 112.543075364 1.00339068573  ? 0.00201390420182  ? 0.366188833871   
? 1.67442207516  ? -0.443963554879  ? 0.840591568065 ? 2.74818302907 ? -1.39186674044   ? -0.875145976684 ? 3.63507375078   ? 
-2.05140488179   ? 3.07262517998  ? -0.574317639786  ? -0.976743873693  ? -1.36064742803   ? 1.15966598605    ? -0.400806806881  ? 
0.872661126806   ? -0.4496096121    ? 0.0145063366876  ? 0.782258432499   ? 
9  'X-RAY DIFFRACTION' ? refined -15.7891871939  23.7970536213 108.156244051 1.46881834895  ? -0.139745334933   ? 0.607123680621   
? 1.31059851872  ? 0.400479359031   ? 1.51001757367  ? 7.80966660636 ? -4.47192851499   ? 1.60396618154   ? 4.00848949844   ? 
-0.0864649398508 ? 0.807831829066 ? 0.396444969209   ? -1.68114650269   ? 0.333549860236   ? 1.7655988734     ? 0.717570292313   ? 
2.360643871      ? 0.327843793703   ? -1.25458817875   ? -0.951885283706  ? 
10 'X-RAY DIFFRACTION' ? refined -10.1133917569  27.0864000583 118.878453049 1.37557553804  ? -0.152735714534   ? -0.124158432521  
? 1.73458538051  ? 0.00503860679062 ? 0.732740272111 ? 3.64657385113 ? -1.20719717467   ? -4.53503544899  ? 0.408974279859  ? 
1.4818613134     ? 5.67055781735  ? -0.976445658239  ? -1.66973918053   ? 0.482822223042   ? 0.212193732346   ? 0.707918177653   ? 
0.0158903981621  ? 0.130152656022   ? 1.51299310912    ? 0.309078168914   ? 
11 'X-RAY DIFFRACTION' ? refined -4.44130204716  27.5286240049 100.556485849 0.94376968873  ? -0.00705946427547 ? 0.0108640377168  
? 1.14402385416  ? 0.153059400969   ? 0.484737593427 ? 6.66317094212 ? 0.98291352777    ? -0.455006247089 ? 5.63556604496   ? 
1.51944451578    ? 6.77584308485  ? -0.45126282493   ? -0.942111268048  ? -0.256329190838  ? 0.753958641283   ? -0.0750879090632 ? 
-0.230952621134  ? 0.123797730876   ? 0.5445598064     ? 0.469257128397   ? 
12 'X-RAY DIFFRACTION' ? refined -4.1985004152   27.4790800855 98.4700709748 0.731738272222 ? 0.0419619944092   ? 0.121844810994   
? 0.982455912094 ? 0.117462844552   ? 0.438933005449 ? 2.4302660308  ? 0.664762172956   ? -0.840410226827 ? 3.81844375465   ? 
0.964566832188   ? 0.685754553906 ? -0.19198841566   ? -0.835062685723  ? -0.192486452945  ? 0.89001946773    ? -0.0112024470326 ? 
0.221766906414   ? 0.242107807988   ? -0.363953782957  ? 0.172308733255   ? 
13 'X-RAY DIFFRACTION' ? refined 7.8379451904    31.9285640567 88.9695360946 0.559781172308 ? 0.0809587665845   ? -0.155200209197  
? 0.507616465647 ? 0.00718591247826 ? 0.583457462947 ? 3.75680911455 ? 0.328841232853   ? -2.55428428622  ? 3.28925397158   ? 
-0.504644959777  ? 6.11840769642  ? -0.217703598045  ? -0.687013091407  ? 0.0789681522562  ? 0.534292042211   ? 0.193969635896   ? 
0.0308813384171  ? -0.529682435066  ? 0.492582578966   ? 0.0152257590492  ? 
14 'X-RAY DIFFRACTION' ? refined -8.91379914952  29.8362725724 104.947241487 1.26688588926  ? -0.0220392363578  ? 0.0362266576745  
? 1.04023325606  ? -0.0913497024748 ? 0.368576985888 ? 2.31750203139 ? -0.0860253559482 ? -0.617214530893 ? 0.0305124529712 ? 
0.314428917395   ? 2.97530934674  ? 0.17706768347    ? -0.615046713314  ? 0.151226102814   ? 1.29557151985    ? 0.0374374468706  ? 
-0.108857461842  ? -0.140746432828  ? -0.0252343920039 ? -0.149086497378  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  A 1   A 3   ? A 38  A 40  ? ? 
;chain 'A' and (resid 3 through 40 )
;
2  'X-RAY DIFFRACTION' 2  A 39  A 41  ? A 75  A 77  ? ? 
;chain 'A' and (resid 41 through 77 )
;
3  'X-RAY DIFFRACTION' 3  A 76  A 78  ? A 105 A 107 ? ? 
;chain 'A' and (resid 78 through 107 )
;
4  'X-RAY DIFFRACTION' 4  A 106 A 108 ? A 124 A 140 ? ? 
;chain 'A' and (resid 108 through 140 )
;
5  'X-RAY DIFFRACTION' 5  A 125 A 141 ? A 193 A 209 ? ? 
;chain 'A' and (resid 141 through 209 )
;
6  'X-RAY DIFFRACTION' 6  A 194 A 210 ? A 230 A 246 ? ? 
;chain 'A' and (resid 210 through 246 )
;
7  'X-RAY DIFFRACTION' 7  B 1   C 338 ? B 16  C 353 ? ? 
;chain 'C' and (resid 338 through 353 )
;
8  'X-RAY DIFFRACTION' 8  B 17  C 354 ? B 30  C 367 ? ? 
;chain 'C' and (resid 354 through 367 )
;
9  'X-RAY DIFFRACTION' 9  B 31  C 368 ? B 42  C 379 ? ? 
;chain 'C' and (resid 368 through 379 )
;
10 'X-RAY DIFFRACTION' 10 B 43  C 380 ? B 52  C 394 ? ? 
;chain 'C' and (resid 380 through 394 )
;
11 'X-RAY DIFFRACTION' 11 B 53  C 395 ? B 67  C 409 ? ? 
;chain 'C' and (resid 395 through 409 )
;
12 'X-RAY DIFFRACTION' 12 B 68  C 410 ? B 109 C 451 ? ? 
;chain 'C' and (resid 410 through 451 )
;
13 'X-RAY DIFFRACTION' 13 B 110 C 452 ? B 160 C 502 ? ? 
;chain 'C' and (resid 452 through 502 )
;
14 'X-RAY DIFFRACTION' 14 B 161 C 503 ? B 178 C 525 ? ? 
;chain 'C' and (resid 503 through 525 )
;
# 
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 -29 ? A MET 1   
2  1 Y 1 A GLY -28 ? A GLY 2   
3  1 Y 1 A ILE -27 ? A ILE 3   
4  1 Y 1 A LEU -26 ? A LEU 4   
5  1 Y 1 A PRO -25 ? A PRO 5   
6  1 Y 1 A SER -24 ? A SER 6   
7  1 Y 1 A PRO -23 ? A PRO 7   
8  1 Y 1 A GLY -22 ? A GLY 8   
9  1 Y 1 A MET -21 ? A MET 9   
10 1 Y 1 A PRO -20 ? A PRO 10  
11 1 Y 1 A ALA -19 ? A ALA 11  
12 1 Y 1 A LEU -18 ? A LEU 12  
13 1 Y 1 A LEU -17 ? A LEU 13  
14 1 Y 1 A SER -16 ? A SER 14  
15 1 Y 1 A LEU -15 ? A LEU 15  
16 1 Y 1 A VAL -14 ? A VAL 16  
17 1 Y 1 A SER -13 ? A SER 17  
18 1 Y 1 A LEU -12 ? A LEU 18  
19 1 Y 1 A LEU -11 ? A LEU 19  
20 1 Y 1 A SER -10 ? A SER 20  
21 1 Y 1 A VAL -9  ? A VAL 21  
22 1 Y 1 A LEU -8  ? A LEU 22  
23 1 Y 1 A LEU -7  ? A LEU 23  
24 1 Y 1 A MET -6  ? A MET 24  
25 1 Y 1 A GLY -5  ? A GLY 25  
26 1 Y 1 A CYS -4  ? A CYS 26  
27 1 Y 1 A VAL -3  ? A VAL 27  
28 1 Y 1 A ALA -2  ? A ALA 28  
29 1 Y 1 A GLU -1  ? A GLU 29  
30 1 Y 1 A THR 0   ? A THR 30  
31 1 Y 1 A GLY 1   ? A GLY 31  
32 1 Y 1 A GLU 2   ? A GLU 32  
33 1 Y 1 A GLY 109 ? A GLY 139 
34 1 Y 1 A GLY 110 ? A GLY 140 
35 1 Y 1 A GLY 111 ? A GLY 141 
36 1 Y 1 A GLY 112 ? A GLY 142 
37 1 Y 1 A SER 113 ? A SER 143 
38 1 Y 1 A GLY 114 ? A GLY 144 
39 1 Y 1 A GLY 115 ? A GLY 145 
40 1 Y 1 A GLY 116 ? A GLY 146 
41 1 Y 1 A GLY 117 ? A GLY 147 
42 1 Y 1 A SER 118 ? A SER 148 
43 1 Y 1 A GLY 119 ? A GLY 149 
44 1 Y 1 A GLY 120 ? A GLY 150 
45 1 Y 1 A GLY 121 ? A GLY 151 
46 1 Y 1 A GLY 122 ? A GLY 152 
47 1 Y 1 A HIS 247 ? A HIS 277 
48 1 Y 1 A HIS 248 ? A HIS 278 
49 1 Y 1 A HIS 249 ? A HIS 279 
50 1 Y 1 A HIS 250 ? A HIS 280 
51 1 Y 1 A HIS 251 ? A HIS 281 
52 1 Y 1 A HIS 252 ? A HIS 282 
53 1 Y 1 C PRO 322 ? B PRO 1   
54 1 Y 1 C THR 323 ? B THR 2   
55 1 Y 1 C GLU 324 ? B GLU 3   
56 1 Y 1 C SER 325 ? B SER 4   
57 1 Y 1 C ILE 326 ? B ILE 5   
58 1 Y 1 C VAL 327 ? B VAL 6   
59 1 Y 1 C ARG 328 ? B ARG 7   
60 1 Y 1 C PHE 329 ? B PHE 8   
61 1 Y 1 C PRO 330 ? B PRO 9   
62 1 Y 1 C ASN 331 ? B ASN 10  
63 1 Y 1 C ILE 332 ? B ILE 11  
64 1 Y 1 C THR 333 ? B THR 12  
65 1 Y 1 C ASN 334 ? B ASN 13  
66 1 Y 1 C LEU 335 ? B LEU 14  
67 1 Y 1 C CYS 336 ? B CYS 15  
68 1 Y 1 C PRO 337 ? B PRO 16  
69 1 Y 1 C ASP 389 ? B ASP 68  
70 1 Y 1 C LEU 390 ? B LEU 69  
71 1 Y 1 C CYS 391 ? B CYS 70  
72 1 Y 1 C PHE 392 ? B PHE 71  
73 1 Y 1 C THR 393 ? B THR 72  
74 1 Y 1 C LEU 517 ? B LEU 196 
75 1 Y 1 C LEU 518 ? B LEU 197 
76 1 Y 1 C HIS 519 ? B HIS 198 
77 1 Y 1 C ALA 520 ? B ALA 199 
78 1 Y 1 C PRO 521 ? B PRO 200 
79 1 Y 1 C GLY 526 ? B GLY 205 
80 1 Y 1 C PRO 527 ? B PRO 206 
81 1 Y 1 C LYS 528 ? B LYS 207 
82 1 Y 1 C LYS 529 ? B LYS 208 
83 1 Y 1 C SER 530 ? B SER 209 
84 1 Y 1 C THR 531 ? B THR 210 
85 1 Y 1 C ASN 532 ? B ASN 211 
86 1 Y 1 C LEU 533 ? B LEU 212 
87 1 Y 1 C VAL 534 ? B VAL 213 
88 1 Y 1 C LYS 535 ? B LYS 214 
89 1 Y 1 C ASN 536 ? B ASN 215 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Agency for Medical Research and Development (AMED)' Japan JP20fk0108298 1 
'Japan Agency for Medical Research and Development (AMED)' Japan JP20ae0101047 2 
'Japan Agency for Medical Research and Development (AMED)' Japan JP20am0101093 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8YK4 
_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]   0.018132 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006683 
_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]   0.003946 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 6.96715 ?       ? ? 11.43723 ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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 1    N N   . ILE A 1 33  ? 17.69191  18.31928 74.35751  1.000 53.09834  ?  3   ILE A N   1 
ATOM 2    C CA  . ILE A 1 33  ? 16.76876  17.29427 74.82900  1.000 55.79730  ?  3   ILE A CA  1 
ATOM 3    C C   . ILE A 1 33  ? 16.13378  16.57655 73.64273  1.000 57.22530  ?  3   ILE A C   1 
ATOM 4    O O   . ILE A 1 33  ? 15.68612  17.21268 72.68984  1.000 49.97389  ?  3   ILE A O   1 
ATOM 5    C CB  . ILE A 1 33  ? 15.68992  17.89606 75.74589  1.000 39.94028  ?  3   ILE A CB  1 
ATOM 6    C CG1 . ILE A 1 33  ? 16.33652  18.73627 76.84898  1.000 62.57972  ?  3   ILE A CG1 1 
ATOM 7    C CG2 . ILE A 1 33  ? 14.82944  16.79735 76.34997  1.000 41.97536  ?  3   ILE A CG2 1 
ATOM 8    C CD1 . ILE A 1 33  ? 15.34350  19.35362 77.81005  1.000 75.54448  ?  3   ILE A CD1 1 
ATOM 9    N N   . VAL A 1 34  ? 16.09843  15.24817 73.70620  1.000 66.07131  ?  4   VAL A N   1 
ATOM 10   C CA  . VAL A 1 34  ? 15.53843  14.41359 72.64890  1.000 52.33685  ?  4   VAL A CA  1 
ATOM 11   C C   . VAL A 1 34  ? 14.29902  13.72214 73.19914  1.000 60.87522  ?  4   VAL A C   1 
ATOM 12   O O   . VAL A 1 34  ? 14.38108  12.97257 74.18025  1.000 57.88066  ?  4   VAL A O   1 
ATOM 13   C CB  . VAL A 1 34  ? 16.56018  13.38824 72.13512  1.000 46.01929  ?  4   VAL A CB  1 
ATOM 14   C CG1 . VAL A 1 34  ? 15.94468  12.52800 71.04211  1.000 46.41314  ?  4   VAL A CG1 1 
ATOM 15   C CG2 . VAL A 1 34  ? 17.80948  14.09359 71.62922  1.000 47.96788  ?  4   VAL A CG2 1 
ATOM 16   N N   . LEU A 1 35  ? 13.15413  13.97072 72.56857  1.000 54.89865  ?  5   LEU A N   1 
ATOM 17   C CA  . LEU A 1 35  ? 11.88505  13.38095 72.97538  1.000 42.80721  ?  5   LEU A CA  1 
ATOM 18   C C   . LEU A 1 35  ? 11.60255  12.15698 72.11285  1.000 49.98664  ?  5   LEU A C   1 
ATOM 19   O O   . LEU A 1 35  ? 11.49468  12.26798 70.88665  1.000 59.97722  ?  5   LEU A O   1 
ATOM 20   C CB  . LEU A 1 35  ? 10.74879  14.39604 72.85593  1.000 47.61268  ?  5   LEU A CB  1 
ATOM 21   C CG  . LEU A 1 35  ? 10.86080  15.64999 73.72433  1.000 43.58796  ?  5   LEU A CG  1 
ATOM 22   C CD1 . LEU A 1 35  ? 9.66594   16.56128 73.50170  1.000 48.36589  ?  5   LEU A CD1 1 
ATOM 23   C CD2 . LEU A 1 35  ? 10.98491  15.27638 75.19128  1.000 41.00597  ?  5   LEU A CD2 1 
ATOM 24   N N   . THR A 1 36  ? 11.48108  10.99633 72.75395  1.000 63.09289  ?  6   THR A N   1 
ATOM 25   C CA  . THR A 1 36  ? 11.21159  9.73346  72.07271  1.000 61.52362  ?  6   THR A CA  1 
ATOM 26   C C   . THR A 1 36  ? 9.86462   9.21006  72.55348  1.000 53.64248  ?  6   THR A C   1 
ATOM 27   O O   . THR A 1 36  ? 9.72115   8.83421  73.72208  1.000 57.45474  ?  6   THR A O   1 
ATOM 28   C CB  . THR A 1 36  ? 12.32036  8.71543  72.33829  1.000 52.30649  ?  6   THR A CB  1 
ATOM 29   O OG1 . THR A 1 36  ? 13.58289  9.26617  71.94276  1.000 51.92084  ?  6   THR A OG1 1 
ATOM 30   C CG2 . THR A 1 36  ? 12.06520  7.43661  71.55575  1.000 54.42281  ?  6   THR A CG2 1 
ATOM 31   N N   . GLN A 1 37  ? 8.88339   9.18596  71.65808  1.000 48.43267  ?  7   GLN A N   1 
ATOM 32   C CA  . GLN A 1 37  ? 7.54453   8.73477  72.00168  1.000 48.98786  ?  7   GLN A CA  1 
ATOM 33   C C   . GLN A 1 37  ? 7.37789   7.25012  71.69517  1.000 62.50392  ?  7   GLN A C   1 
ATOM 34   O O   . GLN A 1 37  ? 8.06851   6.68136  70.84668  1.000 65.96454  ?  7   GLN A O   1 
ATOM 35   C CB  . GLN A 1 37  ? 6.48898   9.54228  71.24560  1.000 52.49167  ?  7   GLN A CB  1 
ATOM 36   C CG  . GLN A 1 37  ? 6.53332   11.03414 71.51396  1.000 51.59262  ?  7   GLN A CG  1 
ATOM 37   C CD  . GLN A 1 37  ? 5.39537   11.77480 70.84235  1.000 53.40731  ?  7   GLN A CD  1 
ATOM 38   O OE1 . GLN A 1 37  ? 5.58311   12.86334 70.30055  1.000 58.82194  ?  7   GLN A OE1 1 
ATOM 39   N NE2 . GLN A 1 37  ? 4.20400   11.18799 70.87785  1.000 54.76770  ?  7   GLN A NE2 1 
ATOM 40   N N   . SER A 1 38  ? 6.43602   6.62485  72.40466  1.000 66.70840  ?  8   SER A N   1 
ATOM 41   C CA  . SER A 1 38  ? 6.12927   5.21583  72.23669  1.000 62.25727  ?  8   SER A CA  1 
ATOM 42   C C   . SER A 1 38  ? 4.68557   4.98259  72.65336  1.000 72.44680  ?  8   SER A C   1 
ATOM 43   O O   . SER A 1 38  ? 4.24635   5.54342  73.66818  1.000 72.71507  ?  8   SER A O   1 
ATOM 44   C CB  . SER A 1 38  ? 7.06128   4.32535  73.06285  1.000 67.28139  ?  8   SER A CB  1 
ATOM 45   O OG  . SER A 1 38  ? 6.97351   4.63397  74.44285  1.000 84.77842  ?  8   SER A OG  1 
ATOM 46   N N   . PRO A 1 39  ? 3.92440   4.16865  71.90478  1.000 58.73909  ?  9   PRO A N   1 
ATOM 47   C CA  . PRO A 1 39  ? 4.37166   3.47649  70.69090  1.000 58.17330  ?  9   PRO A CA  1 
ATOM 48   C C   . PRO A 1 39  ? 4.38865   4.37415  69.45720  1.000 61.84510  ?  9   PRO A C   1 
ATOM 49   O O   . PRO A 1 39  ? 4.03315   5.54831  69.54445  1.000 67.03305  ?  9   PRO A O   1 
ATOM 50   C CB  . PRO A 1 39  ? 3.33595   2.36473  70.53043  1.000 60.26561  ?  9   PRO A CB  1 
ATOM 51   C CG  . PRO A 1 39  ? 2.09715   2.94215  71.11391  1.000 59.06727  ?  9   PRO A CG  1 
ATOM 52   C CD  . PRO A 1 39  ? 2.54390   3.80156  72.26748  1.000 58.01847  ?  9   PRO A CD  1 
ATOM 53   N N   . GLY A 1 40  ? 4.80659   3.82043  68.32227  1.000 69.98672  ?  10  GLY A N   1 
ATOM 54   C CA  . GLY A 1 40  ? 4.81142   4.56462  67.07913  1.000 74.32517  ?  10  GLY A CA  1 
ATOM 55   C C   . GLY A 1 40  ? 3.46506   4.53021  66.38820  1.000 75.92058  ?  10  GLY A C   1 
ATOM 56   O O   . GLY A 1 40  ? 2.97738   5.55561  65.90329  1.000 69.45882  ?  10  GLY A O   1 
ATOM 57   N N   . THR A 1 41  ? 2.85423   3.34866  66.34089  1.000 67.13246  ?  11  THR A N   1 
ATOM 58   C CA  . THR A 1 41  ? 1.53568   3.16121  65.75201  1.000 64.02245  ?  11  THR A CA  1 
ATOM 59   C C   . THR A 1 41  ? 0.68815   2.33600  66.70711  1.000 60.71895  ?  11  THR A C   1 
ATOM 60   O O   . THR A 1 41  ? 1.12448   1.27819  67.17214  1.000 61.28510  ?  11  THR A O   1 
ATOM 61   C CB  . THR A 1 41  ? 1.62491   2.46912  64.38744  1.000 72.04240  ?  11  THR A CB  1 
ATOM 62   O OG1 . THR A 1 41  ? 2.46381   3.23613  63.51485  1.000 63.24106  ?  11  THR A OG1 1 
ATOM 63   C CG2 . THR A 1 41  ? 0.24255   2.33728  63.76500  1.000 89.20172  ?  11  THR A CG2 1 
ATOM 64   N N   . LEU A 1 42  ? -0.51661  2.82098  67.00019  1.000 67.02536  ?  12  LEU A N   1 
ATOM 65   C CA  . LEU A 1 42  ? -1.42388  2.16237  67.93202  1.000 61.20076  ?  12  LEU A CA  1 
ATOM 66   C C   . LEU A 1 42  ? -2.80764  2.10128  67.30551  1.000 60.12170  ?  12  LEU A C   1 
ATOM 67   O O   . LEU A 1 42  ? -3.39224  3.14154  66.98589  1.000 79.58630  ?  12  LEU A O   1 
ATOM 68   C CB  . LEU A 1 42  ? -1.46859  2.90243  69.27277  1.000 58.55803  ?  12  LEU A CB  1 
ATOM 69   C CG  . LEU A 1 42  ? -2.24291  2.23294  70.40960  1.000 60.52424  ?  12  LEU A CG  1 
ATOM 70   C CD1 . LEU A 1 42  ? -1.64173  0.87775  70.73781  1.000 63.31285  ?  12  LEU A CD1 1 
ATOM 71   C CD2 . LEU A 1 42  ? -2.26212  3.12278  71.64203  1.000 59.42256  ?  12  LEU A CD2 1 
ATOM 72   N N   . SER A 1 43  ? -3.32582  0.88894  67.12917  1.000 62.70030  ?  13  SER A N   1 
ATOM 73   C CA  . SER A 1 43  ? -4.65103  0.66395  66.56503  1.000 63.68356  ?  13  SER A CA  1 
ATOM 74   C C   . SER A 1 43  ? -5.56427  0.12966  67.65911  1.000 65.26531  ?  13  SER A C   1 
ATOM 75   O O   . SER A 1 43  ? -5.28224  -0.91769 68.25098  1.000 67.31015  ?  13  SER A O   1 
ATOM 76   C CB  . SER A 1 43  ? -4.59066  -0.31126 65.38933  1.000 72.91875  ?  13  SER A CB  1 
ATOM 77   O OG  . SER A 1 43  ? -3.79243  0.20450  64.33857  1.000 108.58297 ?  13  SER A OG  1 
ATOM 78   N N   . LEU A 1 44  ? -6.65301  0.84760  67.92401  1.000 64.59428  ?  14  LEU A N   1 
ATOM 79   C CA  . LEU A 1 44  ? -7.60035  0.46864  68.96056  1.000 75.80606  ?  14  LEU A CA  1 
ATOM 80   C C   . LEU A 1 44  ? -9.01807  0.69141  68.45341  1.000 66.83172  ?  14  LEU A C   1 
ATOM 81   O O   . LEU A 1 44  ? -9.23954  1.26640  67.38450  1.000 65.93377  ?  14  LEU A O   1 
ATOM 82   C CB  . LEU A 1 44  ? -7.35925  1.25563  70.25546  1.000 67.02139  ?  14  LEU A CB  1 
ATOM 83   C CG  . LEU A 1 44  ? -6.13287  0.85899  71.07891  1.000 65.20394  ?  14  LEU A CG  1 
ATOM 84   C CD1 . LEU A 1 44  ? -5.88570  1.85863  72.19395  1.000 63.79996  ?  14  LEU A CD1 1 
ATOM 85   C CD2 . LEU A 1 44  ? -6.31718  -0.53397 71.64956  1.000 68.28742  ?  14  LEU A CD2 1 
ATOM 86   N N   . SER A 1 45  ? -9.98098  0.22399  69.23631  1.000 68.71005  ?  15  SER A N   1 
ATOM 87   C CA  . SER A 1 45  ? -11.39650 0.35744  68.94209  1.000 70.40993  ?  15  SER A CA  1 
ATOM 88   C C   . SER A 1 45  ? -12.03414 1.40555  69.84545  1.000 84.11726  ?  15  SER A C   1 
ATOM 89   O O   . SER A 1 45  ? -11.50959 1.71482  70.92076  1.000 82.01161  ?  15  SER A O   1 
ATOM 90   C CB  . SER A 1 45  ? -12.11323 -0.98797 69.12508  1.000 73.01289  ?  15  SER A CB  1 
ATOM 91   O OG  . SER A 1 45  ? -11.62788 -1.95194 68.20736  1.000 82.49964  ?  15  SER A OG  1 
ATOM 92   N N   . PRO A 1 46  ? -13.15930 1.98926  69.43225  1.000 69.66441  ?  16  PRO A N   1 
ATOM 93   C CA  . PRO A 1 46  ? -13.83945 2.96564  70.29391  1.000 69.49517  ?  16  PRO A CA  1 
ATOM 94   C C   . PRO A 1 46  ? -14.27383 2.33544  71.60943  1.000 71.50731  ?  16  PRO A C   1 
ATOM 95   O O   . PRO A 1 46  ? -14.85169 1.24661  71.63719  1.000 73.90812  ?  16  PRO A O   1 
ATOM 96   C CB  . PRO A 1 46  ? -15.04278 3.40378  69.45142  1.000 70.57319  ?  16  PRO A CB  1 
ATOM 97   C CG  . PRO A 1 46  ? -14.63941 3.12927  68.04559  1.000 70.08409  ?  16  PRO A CG  1 
ATOM 98   C CD  . PRO A 1 46  ? -13.78404 1.89995  68.10102  1.000 70.46963  ?  16  PRO A CD  1 
ATOM 99   N N   . GLY A 1 47  ? -13.98493 3.03247  72.70689  1.000 70.69166  ?  17  GLY A N   1 
ATOM 100  C CA  . GLY A 1 47  ? -14.32699 2.58559  74.03944  1.000 72.66295  ?  17  GLY A CA  1 
ATOM 101  C C   . GLY A 1 47  ? -13.14803 2.11426  74.86300  1.000 72.30924  ?  17  GLY A C   1 
ATOM 102  O O   . GLY A 1 47  ? -13.26011 2.04234  76.09404  1.000 77.39363  ?  17  GLY A O   1 
ATOM 103  N N   . GLU A 1 48  ? -12.02396 1.79433  74.22672  1.000 70.86453  ?  18  GLU A N   1 
ATOM 104  C CA  . GLU A 1 48  ? -10.85383 1.30598  74.93581  1.000 70.88593  ?  18  GLU A CA  1 
ATOM 105  C C   . GLU A 1 48  ? -10.01461 2.47937  75.43915  1.000 71.52683  ?  18  GLU A C   1 
ATOM 106  O O   . GLU A 1 48  ? -10.35856 3.64954  75.25734  1.000 73.20160  ?  18  GLU A O   1 
ATOM 107  C CB  . GLU A 1 48  ? -10.03128 0.38592  74.03529  1.000 70.88595  ?  18  GLU A CB  1 
ATOM 108  C CG  . GLU A 1 48  ? -10.86684 -0.54195 73.17055  1.000 85.91585  ?  18  GLU A CG  1 
ATOM 109  C CD  . GLU A 1 48  ? -10.05230 -1.66919 72.57137  1.000 92.10827  ?  18  GLU A CD  1 
ATOM 110  O OE1 . GLU A 1 48  ? -9.66508  -2.58410 73.32664  1.000 93.71146  ?  18  GLU A OE1 1 
ATOM 111  O OE2 . GLU A 1 48  ? -9.79302  -1.63758 71.34990  1.000 89.98654  -1 18  GLU A OE2 1 
ATOM 112  N N   . ARG A 1 49  ? -8.89292  2.16147  76.08088  1.000 88.77950  ?  19  ARG A N   1 
ATOM 113  C CA  . ARG A 1 49  ? -7.98954  3.15883  76.63808  1.000 66.76327  ?  19  ARG A CA  1 
ATOM 114  C C   . ARG A 1 49  ? -6.65227  3.09349  75.91613  1.000 68.05499  ?  19  ARG A C   1 
ATOM 115  O O   . ARG A 1 49  ? -6.08352  2.00916  75.74958  1.000 71.42754  ?  19  ARG A O   1 
ATOM 116  C CB  . ARG A 1 49  ? -7.79029  2.94614  78.14186  1.000 68.67003  ?  19  ARG A CB  1 
ATOM 117  C CG  . ARG A 1 49  ? -6.77195  3.88492  78.76902  1.000 67.12117  ?  19  ARG A CG  1 
ATOM 118  C CD  . ARG A 1 49  ? -6.63160  3.63975  80.26215  1.000 69.49571  ?  19  ARG A CD  1 
ATOM 119  N NE  . ARG A 1 49  ? -7.85850  3.95429  80.98782  1.000 73.57948  ?  19  ARG A NE  1 
ATOM 120  C CZ  . ARG A 1 49  ? -7.99066  3.85991  82.30682  1.000 89.07017  ?  19  ARG A CZ  1 
ATOM 121  N NH1 . ARG A 1 49  ? -6.96867  3.45824  83.05027  1.000 85.80159  ?  19  ARG A NH1 1 
ATOM 122  N NH2 . ARG A 1 49  ? -9.14447  4.16743  82.88342  1.000 102.13547 ?  19  ARG A NH2 1 
ATOM 123  N N   . ALA A 1 50  ? -6.15620  4.25221  75.49180  1.000 73.93812  ?  20  ALA A N   1 
ATOM 124  C CA  . ALA A 1 50  ? -4.86424  4.37065  74.82865  1.000 60.69971  ?  20  ALA A CA  1 
ATOM 125  C C   . ALA A 1 50  ? -3.87884  5.01433  75.79377  1.000 68.81937  ?  20  ALA A C   1 
ATOM 126  O O   . ALA A 1 50  ? -4.11586  6.12684  76.27701  1.000 59.52420  ?  20  ALA A O   1 
ATOM 127  C CB  . ALA A 1 50  ? -4.97808  5.19185  73.54445  1.000 58.33966  ?  20  ALA A CB  1 
ATOM 128  N N   . THR A 1 51  ? -2.78231  4.31607  76.07432  1.000 80.25991  ?  21  THR A N   1 
ATOM 129  C CA  . THR A 1 51  ? -1.74526  4.79771  76.98356  1.000 60.74385  ?  21  THR A CA  1 
ATOM 130  C C   . THR A 1 51  ? -0.50601  5.12740  76.15757  1.000 58.90559  ?  21  THR A C   1 
ATOM 131  O O   . THR A 1 51  ? 0.22290   4.22926  75.72677  1.000 60.07471  ?  21  THR A O   1 
ATOM 132  C CB  . THR A 1 51  ? -1.43660  3.76461  78.06276  1.000 63.92453  ?  21  THR A CB  1 
ATOM 133  O OG1 . THR A 1 51  ? -2.62589  3.48343  78.81099  1.000 65.74174  ?  21  THR A OG1 1 
ATOM 134  C CG2 . THR A 1 51  ? -0.36513  4.28963  79.00614  1.000 63.99985  ?  21  THR A CG2 1 
ATOM 135  N N   . LEU A 1 52  ? -0.27488  6.41668  75.93905  1.000 56.85188  ?  22  LEU A N   1 
ATOM 136  C CA  . LEU A 1 52  ? 0.87571   6.90323  75.19411  1.000 60.70054  ?  22  LEU A CA  1 
ATOM 137  C C   . LEU A 1 52  ? 1.98276   7.32263  76.15453  1.000 59.10425  ?  22  LEU A C   1 
ATOM 138  O O   . LEU A 1 52  ? 1.74257   7.60733  77.32986  1.000 61.04536  ?  22  LEU A O   1 
ATOM 139  C CB  . LEU A 1 52  ? 0.48533   8.07961  74.29291  1.000 60.20872  ?  22  LEU A CB  1 
ATOM 140  C CG  . LEU A 1 52  ? -0.22100  7.79204  72.96247  1.000 60.21747  ?  22  LEU A CG  1 
ATOM 141  C CD1 . LEU A 1 52  ? -1.59306  7.16005  73.15738  1.000 55.74587  ?  22  LEU A CD1 1 
ATOM 142  C CD2 . LEU A 1 52  ? -0.33877  9.06995  72.14942  1.000 71.33093  ?  22  LEU A CD2 1 
ATOM 143  N N   . SER A 1 53  ? 3.20930   7.35724  75.63703  1.000 53.89477  ?  23  SER A N   1 
ATOM 144  C CA  . SER A 1 53  ? 4.37327   7.68293  76.44718  1.000 61.49607  ?  23  SER A CA  1 
ATOM 145  C C   . SER A 1 53  ? 5.29103   8.62398  75.68136  1.000 61.18347  ?  23  SER A C   1 
ATOM 146  O O   . SER A 1 53  ? 5.28927   8.65496  74.44802  1.000 66.07924  ?  23  SER A O   1 
ATOM 147  C CB  . SER A 1 53  ? 5.14400   6.42162  76.86106  1.000 57.49968  ?  23  SER A CB  1 
ATOM 148  O OG  . SER A 1 53  ? 4.34382   5.57957  77.67263  1.000 69.23871  ?  23  SER A OG  1 
ATOM 149  N N   . CYS A 1 54  ? 6.07924   9.39324  76.43441  1.000 57.88930  ?  24  CYS A N   1 
ATOM 150  C CA  . CYS A 1 54  ? 7.03531   10.33531 75.85311  1.000 53.59155  ?  24  CYS A CA  1 
ATOM 151  C C   . CYS A 1 54  ? 8.23230   10.40674 76.79742  1.000 65.04420  ?  24  CYS A C   1 
ATOM 152  O O   . CYS A 1 54  ? 8.15555   11.04645 77.85053  1.000 77.40025  ?  24  CYS A O   1 
ATOM 153  C CB  . CYS A 1 54  ? 6.40360   11.70576 75.64359  1.000 51.50220  ?  24  CYS A CB  1 
ATOM 154  S SG  . CYS A 1 54  ? 7.55817   12.99946 75.12288  1.000 49.97515  ?  24  CYS A SG  1 
ATOM 155  N N   . ARG A 1 55  ? 9.32470   9.74915  76.41848  1.000 51.98174  ?  25  ARG A N   1 
ATOM 156  C CA  . ARG A 1 55  ? 10.54375  9.72858  77.21567  1.000 53.78649  ?  25  ARG A CA  1 
ATOM 157  C C   . ARG A 1 55  ? 11.52930  10.75693 76.67714  1.000 59.68522  ?  25  ARG A C   1 
ATOM 158  O O   . ARG A 1 55  ? 11.76155  10.82779 75.46563  1.000 68.26822  ?  25  ARG A O   1 
ATOM 159  C CB  . ARG A 1 55  ? 11.17942  8.33702  77.21442  1.000 57.28055  ?  25  ARG A CB  1 
ATOM 160  C CG  . ARG A 1 55  ? 12.54927  8.28841  77.87596  1.000 70.98376  ?  25  ARG A CG  1 
ATOM 161  C CD  . ARG A 1 55  ? 13.07583  6.86712  77.98619  1.000 93.29597  ?  25  ARG A CD  1 
ATOM 162  N NE  . ARG A 1 55  ? 12.28424  6.06054  78.91048  1.000 120.73213 ?  25  ARG A NE  1 
ATOM 163  C CZ  . ARG A 1 55  ? 12.60421  4.82688  79.28722  1.000 114.41626 ?  25  ARG A CZ  1 
ATOM 164  N NH1 . ARG A 1 55  ? 13.70520  4.25387  78.82030  1.000 105.46487 ?  25  ARG A NH1 1 
ATOM 165  N NH2 . ARG A 1 55  ? 11.82516  4.16639  80.13303  1.000 97.59415  ?  25  ARG A NH2 1 
ATOM 166  N N   . ALA A 1 56  ? 12.10304  11.54806 77.57792  1.000 51.62823  ?  26  ALA A N   1 
ATOM 167  C CA  . ALA A 1 56  ? 13.08516  12.56053 77.22527  1.000 49.86697  ?  26  ALA A CA  1 
ATOM 168  C C   . ALA A 1 56  ? 14.49351  12.05086 77.50466  1.000 60.31138  ?  26  ALA A C   1 
ATOM 169  O O   . ALA A 1 56  ? 14.71078  11.22954 78.39938  1.000 64.80964  ?  26  ALA A O   1 
ATOM 170  C CB  . ALA A 1 56  ? 12.83610  13.85588 77.99998  1.000 53.60260  ?  26  ALA A CB  1 
ATOM 171  N N   . SER A 1 57  ? 15.45470  12.54989 76.72225  1.000 61.73523  ?  27  SER A N   1 
ATOM 172  C CA  . SER A 1 57  ? 16.84182  12.13368 76.90254  1.000 57.30610  ?  27  SER A CA  1 
ATOM 173  C C   . SER A 1 57  ? 17.40680  12.62043 78.23063  1.000 59.85470  ?  27  SER A C   1 
ATOM 174  O O   . SER A 1 57  ? 18.26098  11.95009 78.82171  1.000 68.76772  ?  27  SER A O   1 
ATOM 175  C CB  . SER A 1 57  ? 17.69982  12.63919 75.74288  1.000 52.59584  ?  27  SER A CB  1 
ATOM 176  O OG  . SER A 1 57  ? 17.70963  14.05421 75.69399  1.000 51.08775  ?  27  SER A OG  1 
ATOM 177  N N   . GLN A 1 58  ? 16.94868  13.77463 78.71240  1.000 61.85200  ?  28  GLN A N   1 
ATOM 178  C CA  . GLN A 1 58  ? 17.35032  14.29968 80.00880  1.000 60.76069  ?  28  GLN A CA  1 
ATOM 179  C C   . GLN A 1 58  ? 16.13036  14.91868 80.67926  1.000 55.45603  ?  28  GLN A C   1 
ATOM 180  O O   . GLN A 1 58  ? 15.05003  15.01098 80.08886  1.000 59.65126  ?  28  GLN A O   1 
ATOM 181  C CB  . GLN A 1 58  ? 18.49776  15.30818 79.87071  1.000 53.67510  ?  28  GLN A CB  1 
ATOM 182  C CG  . GLN A 1 58  ? 18.21327  16.45381 78.91686  1.000 92.66929  ?  28  GLN A CG  1 
ATOM 183  C CD  . GLN A 1 58  ? 19.41940  17.34925 78.70853  1.000 88.99622  ?  28  GLN A CD  1 
ATOM 184  O OE1 . GLN A 1 58  ? 20.18996  17.16242 77.76667  1.000 91.18323  ?  28  GLN A OE1 1 
ATOM 185  N NE2 . GLN A 1 58  ? 19.58984  18.32809 79.58996  1.000 87.67421  ?  28  GLN A NE2 1 
ATOM 186  N N   . SER A 1 59  ? 16.30815  15.34561 81.92594  1.000 55.93955  ?  29  SER A N   1 
ATOM 187  C CA  . SER A 1 59  ? 15.18923  15.84115 82.71477  1.000 57.72839  ?  29  SER A CA  1 
ATOM 188  C C   . SER A 1 59  ? 14.71610  17.19602 82.20303  1.000 62.13233  ?  29  SER A C   1 
ATOM 189  O O   . SER A 1 59  ? 15.51920  18.08793 81.91546  1.000 85.54986  ?  29  SER A O   1 
ATOM 190  C CB  . SER A 1 59  ? 15.58412  15.94997 84.18658  1.000 57.24809  ?  29  SER A CB  1 
ATOM 191  O OG  . SER A 1 59  ? 14.49185  16.38998 84.97420  1.000 61.36891  ?  29  SER A OG  1 
ATOM 192  N N   . VAL A 1 60  ? 13.39727  17.34449 82.09248  1.000 68.38581  ?  30  VAL A N   1 
ATOM 193  C CA  . VAL A 1 60  ? 12.77959  18.61815 81.71747  1.000 67.57589  ?  30  VAL A CA  1 
ATOM 194  C C   . VAL A 1 60  ? 12.56998  19.38347 83.02110  1.000 65.04544  ?  30  VAL A C   1 
ATOM 195  O O   . VAL A 1 60  ? 11.51097  19.31802 83.64722  1.000 62.52191  ?  30  VAL A O   1 
ATOM 196  C CB  . VAL A 1 60  ? 11.48016  18.41878 80.94072  1.000 51.34403  ?  30  VAL A CB  1 
ATOM 197  C CG1 . VAL A 1 60  ? 10.95562  19.75148 80.42914  1.000 46.80067  ?  30  VAL A CG1 1 
ATOM 198  C CG2 . VAL A 1 60  ? 11.69232  17.44446 79.79102  1.000 55.42414  ?  30  VAL A CG2 1 
ATOM 199  N N   . SER A 1 61  ? 13.60409  20.12061 83.43624  1.000 78.32109  ?  31  SER A N   1 
ATOM 200  C CA  . SER A 1 61  ? 13.55687  20.81430 84.71978  1.000 78.51556  ?  31  SER A CA  1 
ATOM 201  C C   . SER A 1 61  ? 12.53307  21.94204 84.72169  1.000 87.46432  ?  31  SER A C   1 
ATOM 202  O O   . SER A 1 61  ? 11.96035  22.25388 85.77216  1.000 83.62824  ?  31  SER A O   1 
ATOM 203  C CB  . SER A 1 61  ? 14.94053  21.36008 85.07179  1.000 81.30303  ?  31  SER A CB  1 
ATOM 204  O OG  . SER A 1 61  ? 15.35406  22.33707 84.13244  1.000 95.60128  ?  31  SER A OG  1 
ATOM 205  N N   . SER A 1 62  ? 12.28933  22.56275 83.56631  1.000 66.75345  ?  32  SER A N   1 
ATOM 206  C CA  . SER A 1 62  ? 11.33481  23.66126 83.48878  1.000 45.87567  ?  32  SER A CA  1 
ATOM 207  C C   . SER A 1 62  ? 9.88833   23.19951 83.60685  1.000 60.00754  ?  32  SER A C   1 
ATOM 208  O O   . SER A 1 62  ? 9.00498   24.04389 83.79357  1.000 75.07435  ?  32  SER A O   1 
ATOM 209  C CB  . SER A 1 62  ? 11.52887  24.42739 82.18016  1.000 41.01621  ?  32  SER A CB  1 
ATOM 210  O OG  . SER A 1 62  ? 11.37058  23.57242 81.06198  1.000 43.15846  ?  32  SER A OG  1 
ATOM 211  N N   . THR A 1 63  ? 9.63185   21.89315 83.50255  1.000 64.30000  ?  33  THR A N   1 
ATOM 212  C CA  . THR A 1 63  ? 8.28808   21.32402 83.62817  1.000 64.12941  ?  33  THR A CA  1 
ATOM 213  C C   . THR A 1 63  ? 7.33044   21.94661 82.61211  1.000 45.45561  ?  33  THR A C   1 
ATOM 214  O O   . THR A 1 63  ? 6.22395   22.37730 82.94333  1.000 71.47604  ?  33  THR A O   1 
ATOM 215  C CB  . THR A 1 63  ? 7.75305   21.47586 85.05565  1.000 66.37386  ?  33  THR A CB  1 
ATOM 216  O OG1 . THR A 1 63  ? 8.83478   21.35045 85.98666  1.000 84.10242  ?  33  THR A OG1 1 
ATOM 217  C CG2 . THR A 1 63  ? 6.71807   20.39675 85.35529  1.000 80.03585  ?  33  THR A CG2 1 
ATOM 218  N N   . PHE A 1 64  ? 7.77242   21.99547 81.35650  1.000 39.47576  ?  34  PHE A N   1 
ATOM 219  C CA  . PHE A 1 64  ? 6.94884   22.53668 80.28293  1.000 61.16774  ?  34  PHE A CA  1 
ATOM 220  C C   . PHE A 1 64  ? 6.66281   21.46689 79.23738  1.000 64.79671  ?  34  PHE A C   1 
ATOM 221  O O   . PHE A 1 64  ? 6.82949   21.70106 78.03587  1.000 53.51786  ?  34  PHE A O   1 
ATOM 222  C CB  . PHE A 1 64  ? 7.62803   23.74927 79.64196  1.000 55.66784  ?  34  PHE A CB  1 
ATOM 223  C CG  . PHE A 1 64  ? 7.78204   24.92001 80.57236  1.000 57.85421  ?  34  PHE A CG  1 
ATOM 224  C CD1 . PHE A 1 64  ? 6.86049   25.14720 81.58157  1.000 44.34561  ?  34  PHE A CD1 1 
ATOM 225  C CD2 . PHE A 1 64  ? 8.85002   25.79101 80.43982  1.000 55.72635  ?  34  PHE A CD2 1 
ATOM 226  C CE1 . PHE A 1 64  ? 7.00147   26.22083 82.44029  1.000 37.55571  ?  34  PHE A CE1 1 
ATOM 227  C CE2 . PHE A 1 64  ? 8.99708   26.86548 81.29727  1.000 44.28954  ?  34  PHE A CE2 1 
ATOM 228  C CZ  . PHE A 1 64  ? 8.07100   27.08096 82.29730  1.000 36.20792  ?  34  PHE A CZ  1 
ATOM 229  N N   . LEU A 1 65  ? 6.23608   20.28991 79.68912  1.000 51.56681  ?  35  LEU A N   1 
ATOM 230  C CA  . LEU A 1 65  ? 5.88563   19.20502 78.78424  1.000 56.58969  ?  35  LEU A CA  1 
ATOM 231  C C   . LEU A 1 65  ? 4.45599   19.39520 78.29398  1.000 54.80586  ?  35  LEU A C   1 
ATOM 232  O O   . LEU A 1 65  ? 3.52656   19.52287 79.09729  1.000 55.00721  ?  35  LEU A O   1 
ATOM 233  C CB  . LEU A 1 65  ? 6.04152   17.85569 79.48603  1.000 61.75921  ?  35  LEU A CB  1 
ATOM 234  C CG  . LEU A 1 65  ? 6.34766   16.62717 78.62261  1.000 54.62235  ?  35  LEU A CG  1 
ATOM 235  C CD1 . LEU A 1 65  ? 5.11730   16.14072 77.86704  1.000 66.74908  ?  35  LEU A CD1 1 
ATOM 236  C CD2 . LEU A 1 65  ? 7.48838   16.92677 77.65972  1.000 41.02153  ?  35  LEU A CD2 1 
ATOM 237  N N   . ALA A 1 66  ? 4.28237   19.41677 76.97503  1.000 53.72024  ?  36  ALA A N   1 
ATOM 238  C CA  . ALA A 1 66  ? 2.98806   19.66426 76.36069  1.000 41.40119  ?  36  ALA A CA  1 
ATOM 239  C C   . ALA A 1 66  ? 2.61994   18.52722 75.41702  1.000 50.76514  ?  36  ALA A C   1 
ATOM 240  O O   . ALA A 1 66  ? 3.48649   17.90645 74.79371  1.000 50.58885  ?  36  ALA A O   1 
ATOM 241  C CB  . ALA A 1 66  ? 2.97918   20.99542 75.59772  1.000 34.52050  ?  36  ALA A CB  1 
ATOM 242  N N   . TRP A 1 67  ? 1.31949   18.26268 75.32020  1.000 50.91506  ?  37  TRP A N   1 
ATOM 243  C CA  . TRP A 1 67  ? 0.77404   17.24493 74.43416  1.000 40.92937  ?  37  TRP A CA  1 
ATOM 244  C C   . TRP A 1 67  ? -0.11430  17.90577 73.39003  1.000 46.35155  ?  37  TRP A C   1 
ATOM 245  O O   . TRP A 1 67  ? -0.83610  18.86156 73.69155  1.000 41.41040  ?  37  TRP A O   1 
ATOM 246  C CB  . TRP A 1 67  ? -0.02684  16.19878 75.21573  1.000 41.11309  ?  37  TRP A CB  1 
ATOM 247  C CG  . TRP A 1 67  ? 0.81229   15.33165 76.10196  1.000 42.50534  ?  37  TRP A CG  1 
ATOM 248  C CD1 . TRP A 1 67  ? 1.10897   15.54399 77.41695  1.000 48.19775  ?  37  TRP A CD1 1 
ATOM 249  C CD2 . TRP A 1 67  ? 1.46082   14.10810 75.73690  1.000 43.36984  ?  37  TRP A CD2 1 
ATOM 250  N NE1 . TRP A 1 67  ? 1.90342   14.52841 77.89293  1.000 45.11338  ?  37  TRP A NE1 1 
ATOM 251  C CE2 . TRP A 1 67  ? 2.13366   13.63445 76.88046  1.000 45.02225  ?  37  TRP A CE2 1 
ATOM 252  C CE3 . TRP A 1 67  ? 1.53889   13.36784 74.55320  1.000 43.19854  ?  37  TRP A CE3 1 
ATOM 253  C CZ2 . TRP A 1 67  ? 2.87347   12.45432 76.87500  1.000 53.30484  ?  37  TRP A CZ2 1 
ATOM 254  C CZ3 . TRP A 1 67  ? 2.27333   12.19687 74.55010  1.000 44.64982  ?  37  TRP A CZ3 1 
ATOM 255  C CH2 . TRP A 1 67  ? 2.92981   11.75121 75.70300  1.000 46.32718  ?  37  TRP A CH2 1 
ATOM 256  N N   . TYR A 1 68  ? -0.06100  17.39269 72.16284  1.000 42.12732  ?  38  TYR A N   1 
ATOM 257  C CA  . TYR A 1 68  ? -0.80628  17.95934 71.04983  1.000 39.56970  ?  38  TYR A CA  1 
ATOM 258  C C   . TYR A 1 68  ? -1.53191  16.85808 70.29095  1.000 48.30034  ?  38  TYR A C   1 
ATOM 259  O O   . TYR A 1 68  ? -1.10164  15.70194 70.27584  1.000 46.13070  ?  38  TYR A O   1 
ATOM 260  C CB  . TYR A 1 68  ? 0.11452   18.72876 70.08960  1.000 36.98190  ?  38  TYR A CB  1 
ATOM 261  C CG  . TYR A 1 68  ? 0.81437   19.91009 70.72242  1.000 35.84725  ?  38  TYR A CG  1 
ATOM 262  C CD1 . TYR A 1 68  ? 2.00036   19.74449 71.42518  1.000 44.19399  ?  38  TYR A CD1 1 
ATOM 263  C CD2 . TYR A 1 68  ? 0.29137   21.19168 70.61399  1.000 46.43861  ?  38  TYR A CD2 1 
ATOM 264  C CE1 . TYR A 1 68  ? 2.64308   20.82031 72.00542  1.000 45.80324  ?  38  TYR A CE1 1 
ATOM 265  C CE2 . TYR A 1 68  ? 0.92916   22.27490 71.19020  1.000 44.01592  ?  38  TYR A CE2 1 
ATOM 266  C CZ  . TYR A 1 68  ? 2.10460   22.08266 71.88505  1.000 44.25012  ?  38  TYR A CZ  1 
ATOM 267  O OH  . TYR A 1 68  ? 2.74570   23.15460 72.46231  1.000 39.95677  ?  38  TYR A OH  1 
ATOM 268  N N   . GLN A 1 69  ? -2.64301  17.23383 69.66225  1.000 45.46209  ?  39  GLN A N   1 
ATOM 269  C CA  . GLN A 1 69  ? -3.41448  16.34897 68.80030  1.000 40.18301  ?  39  GLN A CA  1 
ATOM 270  C C   . GLN A 1 69  ? -3.47869  16.96017 67.40941  1.000 43.72988  ?  39  GLN A C   1 
ATOM 271  O O   . GLN A 1 69  ? -3.78334  18.14889 67.26538  1.000 57.13976  ?  39  GLN A O   1 
ATOM 272  C CB  . GLN A 1 69  ? -4.82783  16.13172 69.34725  1.000 42.18228  ?  39  GLN A CB  1 
ATOM 273  C CG  . GLN A 1 69  ? -5.69851  15.23686 68.48020  1.000 48.70820  ?  39  GLN A CG  1 
ATOM 274  C CD  . GLN A 1 69  ? -7.14073  15.19322 68.94724  1.000 59.27593  ?  39  GLN A CD  1 
ATOM 275  O OE1 . GLN A 1 69  ? -7.89380  16.15023 68.76486  1.000 57.52771  ?  39  GLN A OE1 1 
ATOM 276  N NE2 . GLN A 1 69  ? -7.53264  14.07925 69.55497  1.000 63.36756  ?  39  GLN A NE2 1 
ATOM 277  N N   . GLN A 1 70  ? -3.19274  16.15300 66.38993  1.000 39.86976  ?  40  GLN A N   1 
ATOM 278  C CA  . GLN A 1 70  ? -3.18531  16.61786 65.00362  1.000 49.84573  ?  40  GLN A CA  1 
ATOM 279  C C   . GLN A 1 70  ? -4.03035  15.66912 64.15929  1.000 41.63442  ?  40  GLN A C   1 
ATOM 280  O O   . GLN A 1 70  ? -3.54573  14.62510 63.71227  1.000 42.24472  ?  40  GLN A O   1 
ATOM 281  C CB  . GLN A 1 70  ? -1.76290  16.71687 64.46229  1.000 38.04522  ?  40  GLN A CB  1 
ATOM 282  C CG  . GLN A 1 70  ? -1.68140  17.31325 63.06673  1.000 37.79557  ?  40  GLN A CG  1 
ATOM 283  C CD  . GLN A 1 70  ? -0.26355  17.37074 62.53914  1.000 45.53303  ?  40  GLN A CD  1 
ATOM 284  O OE1 . GLN A 1 70  ? 0.37780   18.42120 62.56386  1.000 34.92969  ?  40  GLN A OE1 1 
ATOM 285  N NE2 . GLN A 1 70  ? 0.23416   16.23823 62.05487  1.000 52.95774  ?  40  GLN A NE2 1 
ATOM 286  N N   . LYS A 1 71  ? -5.29073  16.03461 63.94350  1.000 46.77509  ?  41  LYS A N   1 
ATOM 287  C CA  . LYS A 1 71  ? -6.13376  15.28220 63.03263  1.000 46.65407  ?  41  LYS A CA  1 
ATOM 288  C C   . LYS A 1 71  ? -5.66292  15.49709 61.59357  1.000 47.71716  ?  41  LYS A C   1 
ATOM 289  O O   . LYS A 1 71  ? -5.08244  16.53788 61.27306  1.000 47.82613  ?  41  LYS A O   1 
ATOM 290  C CB  . LYS A 1 71  ? -7.59482  15.70006 63.19005  1.000 48.39205  ?  41  LYS A CB  1 
ATOM 291  C CG  . LYS A 1 71  ? -8.24764  15.15379 64.45465  1.000 54.66154  ?  41  LYS A CG  1 
ATOM 292  C CD  . LYS A 1 71  ? -9.71226  15.54883 64.56384  1.000 53.24401  ?  41  LYS A CD  1 
ATOM 293  C CE  . LYS A 1 71  ? -9.86934  17.02814 64.87529  1.000 97.31091  ?  41  LYS A CE  1 
ATOM 294  N NZ  . LYS A 1 71  ? -11.29547 17.40003 65.09435  1.000 73.50887  ?  41  LYS A NZ  1 
ATOM 295  N N   . PRO A 1 72  ? -5.88454  14.52084 60.71264  1.000 56.20811  ?  42  PRO A N   1 
ATOM 296  C CA  . PRO A 1 72  ? -5.34024  14.61931 59.35043  1.000 56.70620  ?  42  PRO A CA  1 
ATOM 297  C C   . PRO A 1 72  ? -5.89344  15.82437 58.60219  1.000 52.63902  ?  42  PRO A C   1 
ATOM 298  O O   . PRO A 1 72  ? -7.10677  16.02954 58.52529  1.000 61.99638  ?  42  PRO A O   1 
ATOM 299  C CB  . PRO A 1 72  ? -5.77231  13.29860 58.70015  1.000 62.67251  ?  42  PRO A CB  1 
ATOM 300  C CG  . PRO A 1 72  ? -6.92318  12.81980 59.52478  1.000 57.32082  ?  42  PRO A CG  1 
ATOM 301  C CD  . PRO A 1 72  ? -6.61579  13.25939 60.92132  1.000 60.55184  ?  42  PRO A CD  1 
ATOM 302  N N   . GLY A 1 73  ? -4.98453  16.62421 58.05016  1.000 60.67631  ?  43  GLY A N   1 
ATOM 303  C CA  . GLY A 1 73  ? -5.34968  17.80902 57.30459  1.000 73.20452  ?  43  GLY A CA  1 
ATOM 304  C C   . GLY A 1 73  ? -5.53454  19.06262 58.12810  1.000 61.40979  ?  43  GLY A C   1 
ATOM 305  O O   . GLY A 1 73  ? -5.95641  20.08671 57.57743  1.000 68.15153  ?  43  GLY A O   1 
ATOM 306  N N   . GLN A 1 74  ? -5.22610  19.02355 59.42199  1.000 55.55083  ?  44  GLN A N   1 
ATOM 307  C CA  . GLN A 1 74  ? -5.42177  20.15837 60.31079  1.000 52.31130  ?  44  GLN A CA  1 
ATOM 308  C C   . GLN A 1 74  ? -4.11544  20.49064 61.02047  1.000 47.78331  ?  44  GLN A C   1 
ATOM 309  O O   . GLN A 1 74  ? -3.10506  19.79455 60.88275  1.000 59.47598  ?  44  GLN A O   1 
ATOM 310  C CB  . GLN A 1 74  ? -6.52771  19.88036 61.33832  1.000 49.90636  ?  44  GLN A CB  1 
ATOM 311  C CG  . GLN A 1 74  ? -7.87299  19.51736 60.72515  1.000 65.57051  ?  44  GLN A CG  1 
ATOM 312  C CD  . GLN A 1 74  ? -8.95137  19.28977 61.76763  1.000 71.92678  ?  44  GLN A CD  1 
ATOM 313  O OE1 . GLN A 1 74  ? -8.75832  19.57390 62.94957  1.000 70.43648  ?  44  GLN A OE1 1 
ATOM 314  N NE2 . GLN A 1 74  ? -10.09461 18.77181 61.33334  1.000 79.51847  ?  44  GLN A NE2 1 
ATOM 315  N N   . ALA A 1 75  ? -4.14862  21.57359 61.78177  1.000 47.10183  ?  45  ALA A N   1 
ATOM 316  C CA  . ALA A 1 75  ? -3.02614  22.00956 62.59326  1.000 41.67076  ?  45  ALA A CA  1 
ATOM 317  C C   . ALA A 1 75  ? -3.04717  21.31014 63.94510  1.000 39.92443  ?  45  ALA A C   1 
ATOM 318  O O   . ALA A 1 75  ? -4.09118  20.81864 64.38558  1.000 59.16055  ?  45  ALA A O   1 
ATOM 319  C CB  . ALA A 1 75  ? -3.07647  23.52414 62.78130  1.000 41.93381  ?  45  ALA A CB  1 
ATOM 320  N N   . PRO A 1 76  ? -1.90173  21.22816 64.62349  1.000 38.13876  ?  46  PRO A N   1 
ATOM 321  C CA  . PRO A 1 76  ? -1.88300  20.61538 65.95765  1.000 37.61264  ?  46  PRO A CA  1 
ATOM 322  C C   . PRO A 1 76  ? -2.79162  21.35544 66.92929  1.000 42.20983  ?  46  PRO A C   1 
ATOM 323  O O   . PRO A 1 76  ? -2.91177  22.58174 66.89004  1.000 45.30483  ?  46  PRO A O   1 
ATOM 324  C CB  . PRO A 1 76  ? -0.41140  20.71708 66.37235  1.000 36.18104  ?  46  PRO A CB  1 
ATOM 325  C CG  . PRO A 1 76  ? 0.33329   20.75117 65.08184  1.000 36.23076  ?  46  PRO A CG  1 
ATOM 326  C CD  . PRO A 1 76  ? -0.54267  21.51405 64.12985  1.000 39.88649  ?  46  PRO A CD  1 
ATOM 327  N N   . ARG A 1 77  ? -3.43848  20.58856 67.80399  1.000 44.73225  ?  47  ARG A N   1 
ATOM 328  C CA  . ARG A 1 77  ? -4.36560  21.11236 68.79989  1.000 52.66394  ?  47  ARG A CA  1 
ATOM 329  C C   . ARG A 1 77  ? -3.78851  20.84698 70.18206  1.000 39.45639  ?  47  ARG A C   1 
ATOM 330  O O   . ARG A 1 77  ? -3.50812  19.69455 70.52794  1.000 49.38774  ?  47  ARG A O   1 
ATOM 331  C CB  . ARG A 1 77  ? -5.74492  20.46422 68.65392  1.000 51.79424  ?  47  ARG A CB  1 
ATOM 332  C CG  . ARG A 1 77  ? -6.76952  20.89282 69.69411  1.000 44.38665  ?  47  ARG A CG  1 
ATOM 333  C CD  . ARG A 1 77  ? -7.99223  19.98386 69.64936  1.000 79.76736  ?  47  ARG A CD  1 
ATOM 334  N NE  . ARG A 1 77  ? -9.01564  20.37098 70.61672  1.000 111.11106 ?  47  ARG A NE  1 
ATOM 335  C CZ  . ARG A 1 77  ? -10.09903 19.64873 70.88725  1.000 110.49676 ?  47  ARG A CZ  1 
ATOM 336  N NH1 . ARG A 1 77  ? -10.30247 18.49343 70.26743  1.000 55.83769  ?  47  ARG A NH1 1 
ATOM 337  N NH2 . ARG A 1 77  ? -10.97857 20.07895 71.78162  1.000 117.53226 ?  47  ARG A NH2 1 
ATOM 338  N N   . LEU A 1 78  ? -3.61130  21.90743 70.96665  1.000 43.47996  ?  48  LEU A N   1 
ATOM 339  C CA  . LEU A 1 78  ? -3.03479  21.76887 72.29855  1.000 41.58792  ?  48  LEU A CA  1 
ATOM 340  C C   . LEU A 1 78  ? -4.00050  21.02365 73.21244  1.000 37.05953  ?  48  LEU A C   1 
ATOM 341  O O   . LEU A 1 78  ? -5.12156  21.48404 73.45266  1.000 49.35849  ?  48  LEU A O   1 
ATOM 342  C CB  . LEU A 1 78  ? -2.69937  23.14005 72.88002  1.000 39.49560  ?  48  LEU A CB  1 
ATOM 343  C CG  . LEU A 1 78  ? -2.11723  23.12009 74.29663  1.000 35.44933  ?  48  LEU A CG  1 
ATOM 344  C CD1 . LEU A 1 78  ? -0.77879  22.39786 74.31878  1.000 48.98184  ?  48  LEU A CD1 1 
ATOM 345  C CD2 . LEU A 1 78  ? -1.98004  24.52543 74.86002  1.000 36.08490  ?  48  LEU A CD2 1 
ATOM 346  N N   . LEU A 1 79  ? -3.56500  19.86993 73.71948  1.000 39.98302  ?  49  LEU A N   1 
ATOM 347  C CA  . LEU A 1 79  ? -4.34835  19.08055 74.66449  1.000 43.07788  ?  49  LEU A CA  1 
ATOM 348  C C   . LEU A 1 79  ? -3.93214  19.35691 76.10500  1.000 44.20392  ?  49  LEU A C   1 
ATOM 349  O O   . LEU A 1 79  ? -4.75932  19.74205 76.93653  1.000 51.44607  ?  49  LEU A O   1 
ATOM 350  C CB  . LEU A 1 79  ? -4.20290  17.58384 74.35594  1.000 46.11829  ?  49  LEU A CB  1 
ATOM 351  C CG  . LEU A 1 79  ? -4.58876  17.07447 72.96766  1.000 43.72239  ?  49  LEU A CG  1 
ATOM 352  C CD1 . LEU A 1 79  ? -4.27585  15.59214 72.86460  1.000 49.50995  ?  49  LEU A CD1 1 
ATOM 353  C CD2 . LEU A 1 79  ? -6.05807  17.33461 72.67914  1.000 40.84664  ?  49  LEU A CD2 1 
ATOM 354  N N   . ILE A 1 80  ? -2.65285  19.16143 76.41225  1.000 44.88423  ?  50  ILE A N   1 
ATOM 355  C CA  . ILE A 1 80  ? -2.11807  19.31925 77.75756  1.000 50.52046  ?  50  ILE A CA  1 
ATOM 356  C C   . ILE A 1 80  ? -0.92558  20.26214 77.69335  1.000 44.83456  ?  50  ILE A C   1 
ATOM 357  O O   . ILE A 1 80  ? -0.11775  20.19138 76.76076  1.000 53.05670  ?  50  ILE A O   1 
ATOM 358  C CB  . ILE A 1 80  ? -1.70449  17.95966 78.36424  1.000 67.96762  ?  50  ILE A CB  1 
ATOM 359  C CG1 . ILE A 1 80  ? -2.88433  16.98445 78.36408  1.000 53.28959  ?  50  ILE A CG1 1 
ATOM 360  C CG2 . ILE A 1 80  ? -1.16112  18.13598 79.77315  1.000 56.90971  ?  50  ILE A CG2 1 
ATOM 361  C CD1 . ILE A 1 80  ? -4.03474  17.41397 79.24384  1.000 66.54527  ?  50  ILE A CD1 1 
ATOM 362  N N   . TYR A 1 81  ? -0.82331  21.15426 78.67639  1.000 45.09819  ?  51  TYR A N   1 
ATOM 363  C CA  . TYR A 1 81  ? 0.33919   22.01476 78.83177  1.000 53.65875  ?  51  TYR A CA  1 
ATOM 364  C C   . TYR A 1 81  ? 0.87138   21.87844 80.24958  1.000 59.41198  ?  51  TYR A C   1 
ATOM 365  O O   . TYR A 1 81  ? 0.12577   21.55646 81.17857  1.000 56.59604  ?  51  TYR A O   1 
ATOM 366  C CB  . TYR A 1 81  ? 0.01136   23.49220 78.53467  1.000 41.04932  ?  51  TYR A CB  1 
ATOM 367  C CG  . TYR A 1 81  ? -0.66061  24.22852 79.67685  1.000 47.06489  ?  51  TYR A CG  1 
ATOM 368  C CD1 . TYR A 1 81  ? -2.04344  24.25182 79.79619  1.000 57.12834  ?  51  TYR A CD1 1 
ATOM 369  C CD2 . TYR A 1 81  ? 0.08942   24.91015 80.62964  1.000 42.61860  ?  51  TYR A CD2 1 
ATOM 370  C CE1 . TYR A 1 81  ? -2.66032  24.92620 80.83564  1.000 42.58963  ?  51  TYR A CE1 1 
ATOM 371  C CE2 . TYR A 1 81  ? -0.51737  25.58312 81.67170  1.000 51.46987  ?  51  TYR A CE2 1 
ATOM 372  C CZ  . TYR A 1 81  ? -1.89219  25.58917 81.76995  1.000 43.31093  ?  51  TYR A CZ  1 
ATOM 373  O OH  . TYR A 1 81  ? -2.50112  26.26031 82.80591  1.000 46.17844  ?  51  TYR A OH  1 
ATOM 374  N N   . GLY A 1 82  ? 2.16747   22.13823 80.40690  1.000 54.06896  ?  52  GLY A N   1 
ATOM 375  C CA  . GLY A 1 82  ? 2.79897   22.09254 81.71115  1.000 50.37701  ?  52  GLY A CA  1 
ATOM 376  C C   . GLY A 1 82  ? 2.58658   20.78212 82.43974  1.000 50.20180  ?  52  GLY A C   1 
ATOM 377  O O   . GLY A 1 82  ? 1.88323   20.73770 83.45425  1.000 65.39638  ?  52  GLY A O   1 
ATOM 378  N N   . ALA A 1 83  ? 3.17743   19.70870 81.91078  1.000 51.05235  ?  53  ALA A N   1 
ATOM 379  C CA  . ALA A 1 83  ? 3.10918   18.36983 82.48960  1.000 55.62488  ?  53  ALA A CA  1 
ATOM 380  C C   . ALA A 1 83  ? 1.69414   17.79895 82.47875  1.000 62.11883  ?  53  ALA A C   1 
ATOM 381  O O   . ALA A 1 83  ? 1.44203   16.78543 81.81887  1.000 52.92984  ?  53  ALA A O   1 
ATOM 382  C CB  . ALA A 1 83  ? 3.67095   18.36504 83.91552  1.000 67.19877  ?  53  ALA A CB  1 
ATOM 383  N N   . SER A 1 84  ? 0.76223   18.42981 83.19864  1.000 65.93949  ?  54  SER A N   1 
ATOM 384  C CA  . SER A 1 84  ? -0.55908  17.83463 83.37632  1.000 47.28103  ?  54  SER A CA  1 
ATOM 385  C C   . SER A 1 84  ? -1.73593  18.78816 83.22185  1.000 66.31513  ?  54  SER A C   1 
ATOM 386  O O   . SER A 1 84  ? -2.87201  18.30716 83.17492  1.000 79.31468  ?  54  SER A O   1 
ATOM 387  C CB  . SER A 1 84  ? -0.65242  17.16884 84.75690  1.000 47.26157  ?  54  SER A CB  1 
ATOM 388  O OG  . SER A 1 84  ? 0.32810   16.15650 84.89964  1.000 78.34501  ?  54  SER A OG  1 
ATOM 389  N N   . TYR A 1 85  ? -1.52687  20.09992 83.14248  1.000 79.60310  ?  55  TYR A N   1 
ATOM 390  C CA  . TYR A 1 85  ? -2.64791  21.02937 83.06748  1.000 59.35027  ?  55  TYR A CA  1 
ATOM 391  C C   . TYR A 1 85  ? -3.34474  20.92676 81.71420  1.000 61.82922  ?  55  TYR A C   1 
ATOM 392  O O   . TYR A 1 85  ? -2.69788  20.97875 80.66366  1.000 50.55351  ?  55  TYR A O   1 
ATOM 393  C CB  . TYR A 1 85  ? -2.16704  22.45838 83.31287  1.000 57.42604  ?  55  TYR A CB  1 
ATOM 394  C CG  . TYR A 1 85  ? -1.80422  22.74467 84.75274  1.000 59.26388  ?  55  TYR A CG  1 
ATOM 395  C CD1 . TYR A 1 85  ? -2.71804  23.33938 85.61350  1.000 79.14483  ?  55  TYR A CD1 1 
ATOM 396  C CD2 . TYR A 1 85  ? -0.55037  22.41819 85.25237  1.000 46.70252  ?  55  TYR A CD2 1 
ATOM 397  C CE1 . TYR A 1 85  ? -2.39253  23.60303 86.93057  1.000 84.76338  ?  55  TYR A CE1 1 
ATOM 398  C CE2 . TYR A 1 85  ? -0.21565  22.67754 86.56803  1.000 49.13767  ?  55  TYR A CE2 1 
ATOM 399  C CZ  . TYR A 1 85  ? -1.13998  23.26984 87.40253  1.000 74.58098  ?  55  TYR A CZ  1 
ATOM 400  O OH  . TYR A 1 85  ? -0.81025  23.52952 88.71341  1.000 73.30855  ?  55  TYR A OH  1 
ATOM 401  N N   . MET A 1 86  ? -4.66830  20.78425 81.74300  1.000 68.63448  ?  56  MET A N   1 
ATOM 402  C CA  . MET A 1 86  ? -5.44980  20.64793 80.52238  1.000 59.61501  ?  56  MET A CA  1 
ATOM 403  C C   . MET A 1 86  ? -5.65547  22.00191 79.85250  1.000 53.38517  ?  56  MET A C   1 
ATOM 404  O O   . MET A 1 86  ? -5.63072  23.05212 80.50035  1.000 49.77179  ?  56  MET A O   1 
ATOM 405  C CB  . MET A 1 86  ? -6.80608  20.00605 80.81948  1.000 63.43968  ?  56  MET A CB  1 
ATOM 406  C CG  . MET A 1 86  ? -6.72651  18.63314 81.46935  1.000 51.80815  ?  56  MET A CG  1 
ATOM 407  S SD  . MET A 1 86  ? -8.35573  17.89585 81.70507  1.000 144.85688 ?  56  MET A SD  1 
ATOM 408  C CE  . MET A 1 86  ? -7.93249  16.42088 82.62754  1.000 118.99784 ?  56  MET A CE  1 
ATOM 409  N N   . ALA A 1 87  ? -5.87149  21.96493 78.54060  1.000 50.67339  ?  57  ALA A N   1 
ATOM 410  C CA  . ALA A 1 87  ? -6.04127  23.16154 77.73548  1.000 54.12277  ?  57  ALA A CA  1 
ATOM 411  C C   . ALA A 1 87  ? -7.52723  23.47464 77.56000  1.000 70.71064  ?  57  ALA A C   1 
ATOM 412  O O   . ALA A 1 87  ? -8.39876  22.84285 78.16589  1.000 89.60735  ?  57  ALA A O   1 
ATOM 413  C CB  . ALA A 1 87  ? -5.33485  22.99044 76.38986  1.000 44.45678  ?  57  ALA A CB  1 
ATOM 414  N N   . THR A 1 88  ? -7.82330  24.45834 76.71299  1.000 68.09720  ?  58  THR A N   1 
ATOM 415  C CA  . THR A 1 88  ? -9.19209  24.91849 76.51905  1.000 70.32116  ?  58  THR A CA  1 
ATOM 416  C C   . THR A 1 88  ? -9.95727  23.96345 75.61116  1.000 72.62031  ?  58  THR A C   1 
ATOM 417  O O   . THR A 1 88  ? -9.48798  23.61401 74.52344  1.000 75.98066  ?  58  THR A O   1 
ATOM 418  C CB  . THR A 1 88  ? -9.20183  26.32834 75.92675  1.000 69.89179  ?  58  THR A CB  1 
ATOM 419  O OG1 . THR A 1 88  ? -8.57642  27.23791 76.84097  1.000 81.13400  ?  58  THR A OG1 1 
ATOM 420  C CG2 . THR A 1 88  ? -10.62911 26.78771 75.66123  1.000 80.93497  ?  58  THR A CG2 1 
ATOM 421  N N   . GLY A 1 89  ? -11.13972 23.54723 76.06058  1.000 62.90985  ?  59  GLY A N   1 
ATOM 422  C CA  . GLY A 1 89  ? -11.98533 22.68669 75.25858  1.000 63.29408  ?  59  GLY A CA  1 
ATOM 423  C C   . GLY A 1 89  ? -11.53651 21.24784 75.17227  1.000 72.39818  ?  59  GLY A C   1 
ATOM 424  O O   . GLY A 1 89  ? -11.93334 20.54095 74.24238  1.000 79.40574  ?  59  GLY A O   1 
ATOM 425  N N   . ILE A 1 90  ? -10.72292 20.78954 76.11443  1.000 70.47572  ?  60  ILE A N   1 
ATOM 426  C CA  . ILE A 1 90  ? -10.20905 19.42305 76.12338  1.000 57.87457  ?  60  ILE A CA  1 
ATOM 427  C C   . ILE A 1 90  ? -11.07440 18.60101 77.07204  1.000 61.61462  ?  60  ILE A C   1 
ATOM 428  O O   . ILE A 1 90  ? -11.22221 18.98478 78.24264  1.000 68.27111  ?  60  ILE A O   1 
ATOM 429  C CB  . ILE A 1 90  ? -8.73348  19.37685 76.54379  1.000 54.63805  ?  60  ILE A CB  1 
ATOM 430  C CG1 . ILE A 1 90  ? -7.90188  20.29865 75.65005  1.000 55.71782  ?  60  ILE A CG1 1 
ATOM 431  C CG2 . ILE A 1 90  ? -8.20793  17.95073 76.48407  1.000 46.65499  ?  60  ILE A CG2 1 
ATOM 432  C CD1 . ILE A 1 90  ? -8.07468  20.03204 74.17063  1.000 44.29590  ?  60  ILE A CD1 1 
ATOM 433  N N   . PRO A 1 91  ? -11.65726 17.49176 76.62444  1.000 55.23008  ?  61  PRO A N   1 
ATOM 434  C CA  . PRO A 1 91  ? -12.51081 16.68997 77.50855  1.000 61.81297  ?  61  PRO A CA  1 
ATOM 435  C C   . PRO A 1 91  ? -11.71382 16.07732 78.65117  1.000 67.39639  ?  61  PRO A C   1 
ATOM 436  O O   . PRO A 1 91  ? -10.48200 16.03731 78.65047  1.000 75.90939  ?  61  PRO A O   1 
ATOM 437  C CB  . PRO A 1 91  ? -13.07481 15.60875 76.58013  1.000 62.24128  ?  61  PRO A CB  1 
ATOM 438  C CG  . PRO A 1 91  ? -12.90413 16.15813 75.19510  1.000 57.77377  ?  61  PRO A CG  1 
ATOM 439  C CD  . PRO A 1 91  ? -11.65477 16.98035 75.24432  1.000 54.03970  ?  61  PRO A CD  1 
ATOM 440  N N   . ASP A 1 92  ? -12.45434 15.58624 79.64695  1.000 95.70252  ?  62  ASP A N   1 
ATOM 441  C CA  . ASP A 1 92  ? -11.84210 14.95370 80.80870  1.000 89.24090  ?  62  ASP A CA  1 
ATOM 442  C C   . ASP A 1 92  ? -11.18827 13.61840 80.48048  1.000 85.45649  ?  62  ASP A C   1 
ATOM 443  O O   . ASP A 1 92  ? -10.46305 13.08192 81.32504  1.000 96.19230  ?  62  ASP A O   1 
ATOM 444  C CB  . ASP A 1 92  ? -12.88675 14.75948 81.91027  1.000 93.99830  ?  62  ASP A CB  1 
ATOM 445  C CG  . ASP A 1 92  ? -14.10728 13.99474 81.43079  1.000 106.19566 ?  62  ASP A CG  1 
ATOM 446  O OD1 . ASP A 1 92  ? -14.20959 13.72981 80.21428  1.000 99.25776  ?  62  ASP A OD1 1 
ATOM 447  O OD2 . ASP A 1 92  ? -14.96593 13.65727 82.27270  1.000 132.98543 -1 62  ASP A OD2 1 
ATOM 448  N N   . ARG A 1 93  ? -11.42719 13.07186 79.28641  1.000 80.55807  ?  63  ARG A N   1 
ATOM 449  C CA  . ARG A 1 93  ? -10.81951 11.79818 78.91605  1.000 67.98502  ?  63  ARG A CA  1 
ATOM 450  C C   . ARG A 1 93  ? -9.30532  11.92612 78.80967  1.000 76.03272  ?  63  ARG A C   1 
ATOM 451  O O   . ARG A 1 93  ? -8.56206  11.07271 79.30810  1.000 86.66187  ?  63  ARG A O   1 
ATOM 452  C CB  . ARG A 1 93  ? -11.41174 11.30060 77.59752  1.000 60.79161  ?  63  ARG A CB  1 
ATOM 453  C CG  . ARG A 1 93  ? -12.90658 11.53461 77.46157  1.000 67.75990  ?  63  ARG A CG  1 
ATOM 454  C CD  . ARG A 1 93  ? -13.45865 10.84094 76.22944  1.000 81.67726  ?  63  ARG A CD  1 
ATOM 455  N NE  . ARG A 1 93  ? -12.69839 11.16708 75.02613  1.000 61.82592  ?  63  ARG A NE  1 
ATOM 456  C CZ  . ARG A 1 93  ? -13.05585 12.09409 74.14378  1.000 67.77950  ?  63  ARG A CZ  1 
ATOM 457  N NH1 . ARG A 1 93  ? -14.16919 12.79148 74.32515  1.000 69.03540  ?  63  ARG A NH1 1 
ATOM 458  N NH2 . ARG A 1 93  ? -12.30156 12.32183 73.07727  1.000 64.26488  ?  63  ARG A NH2 1 
ATOM 459  N N   . PHE A 1 94  ? -8.83181  12.98733 78.16206  1.000 61.74348  ?  64  PHE A N   1 
ATOM 460  C CA  . PHE A 1 94  ? -7.39959  13.21835 78.04011  1.000 54.00382  ?  64  PHE A CA  1 
ATOM 461  C C   . PHE A 1 94  ? -6.82062  13.62020 79.39052  1.000 65.62298  ?  64  PHE A C   1 
ATOM 462  O O   . PHE A 1 94  ? -7.33035  14.53110 80.04998  1.000 80.91357  ?  64  PHE A O   1 
ATOM 463  C CB  . PHE A 1 94  ? -7.12421  14.30490 77.00147  1.000 54.45117  ?  64  PHE A CB  1 
ATOM 464  C CG  . PHE A 1 94  ? -7.67972  14.00009 75.63778  1.000 53.14726  ?  64  PHE A CG  1 
ATOM 465  C CD1 . PHE A 1 94  ? -8.99043  14.31895 75.31983  1.000 49.71567  ?  64  PHE A CD1 1 
ATOM 466  C CD2 . PHE A 1 94  ? -6.88782  13.40463 74.67051  1.000 51.04250  ?  64  PHE A CD2 1 
ATOM 467  C CE1 . PHE A 1 94  ? -9.50215  14.04256 74.06609  1.000 50.25608  ?  64  PHE A CE1 1 
ATOM 468  C CE2 . PHE A 1 94  ? -7.39376  13.12697 73.41437  1.000 46.71467  ?  64  PHE A CE2 1 
ATOM 469  C CZ  . PHE A 1 94  ? -8.70246  13.44634 73.11228  1.000 48.72778  ?  64  PHE A CZ  1 
ATOM 470  N N   . SER A 1 95  ? -5.75476  12.93836 79.80387  1.000 57.88575  ?  65  SER A N   1 
ATOM 471  C CA  . SER A 1 95  ? -5.11158  13.21502 81.08109  1.000 82.89026  ?  65  SER A CA  1 
ATOM 472  C C   . SER A 1 95  ? -3.60306  13.14067 80.91237  1.000 77.36456  ?  65  SER A C   1 
ATOM 473  O O   . SER A 1 95  ? -3.08713  12.18446 80.32627  1.000 65.07047  ?  65  SER A O   1 
ATOM 474  C CB  . SER A 1 95  ? -5.57217  12.22913 82.16128  1.000 53.86369  ?  65  SER A CB  1 
ATOM 475  O OG  . SER A 1 95  ? -5.20412  10.90194 81.82970  1.000 73.32013  ?  65  SER A OG  1 
ATOM 476  N N   . GLY A 1 96  ? -2.90459  14.14805 81.42409  1.000 67.12221  ?  66  GLY A N   1 
ATOM 477  C CA  . GLY A 1 96  ? -1.45732  14.18599 81.38800  1.000 66.55813  ?  66  GLY A CA  1 
ATOM 478  C C   . GLY A 1 96  ? -0.85713  13.74855 82.71114  1.000 62.09110  ?  66  GLY A C   1 
ATOM 479  O O   . GLY A 1 96  ? -1.42997  13.97265 83.77501  1.000 49.00885  ?  66  GLY A O   1 
ATOM 480  N N   . SER A 1 97  ? 0.31040   13.11565 82.63125  1.000 68.19866  ?  67  SER A N   1 
ATOM 481  C CA  . SER A 1 97  ? 0.99405   12.62750 83.81998  1.000 62.47168  ?  67  SER A CA  1 
ATOM 482  C C   . SER A 1 97  ? 2.46453   12.42079 83.49259  1.000 62.89429  ?  67  SER A C   1 
ATOM 483  O O   . SER A 1 97  ? 2.84937   12.29280 82.32725  1.000 59.93939  ?  67  SER A O   1 
ATOM 484  C CB  . SER A 1 97  ? 0.36589   11.32812 84.33664  1.000 51.94419  ?  67  SER A CB  1 
ATOM 485  O OG  . SER A 1 97  ? 0.33927   10.33664 83.32487  1.000 62.78740  ?  67  SER A OG  1 
ATOM 486  N N   . GLY A 1 98  ? 3.27751   12.39264 84.53678  1.000 59.85294  ?  68  GLY A N   1 
ATOM 487  C CA  . GLY A 1 98  ? 4.70061   12.17730 84.40074  1.000 62.81571  ?  68  GLY A CA  1 
ATOM 488  C C   . GLY A 1 98  ? 5.50190   13.42410 84.74554  1.000 72.27353  ?  68  GLY A C   1 
ATOM 489  O O   . GLY A 1 98  ? 5.00413   14.55373 84.72425  1.000 62.08188  ?  68  GLY A O   1 
ATOM 490  N N   . SER A 1 99  ? 6.77364   13.19951 85.06784  1.000 78.82924  ?  69  SER A N   1 
ATOM 491  C CA  . SER A 1 99  ? 7.68051   14.28162 85.42145  1.000 53.58096  ?  69  SER A CA  1 
ATOM 492  C C   . SER A 1 99  ? 9.11247   13.79321 85.26477  1.000 78.58554  ?  69  SER A C   1 
ATOM 493  O O   . SER A 1 99  ? 9.39276   12.59887 85.39756  1.000 89.61773  ?  69  SER A O   1 
ATOM 494  C CB  . SER A 1 99  ? 7.43549   14.77786 86.85116  1.000 50.97108  ?  69  SER A CB  1 
ATOM 495  O OG  . SER A 1 99  ? 7.57079   13.72365 87.78812  1.000 60.44689  ?  69  SER A OG  1 
ATOM 496  N N   . GLY A 1 100 ? 10.01239  14.73102 84.97974  1.000 70.41366  ?  70  GLY A N   1 
ATOM 497  C CA  . GLY A 1 100 ? 11.41400  14.40329 84.81034  1.000 66.36389  ?  70  GLY A CA  1 
ATOM 498  C C   . GLY A 1 100 ? 11.74529  13.90061 83.42093  1.000 61.19417  ?  70  GLY A C   1 
ATOM 499  O O   . GLY A 1 100 ? 11.98768  14.69506 82.50764  1.000 50.48398  ?  70  GLY A O   1 
ATOM 500  N N   . THR A 1 101 ? 11.75952  12.58108 83.24801  1.000 66.53210  ?  71  THR A N   1 
ATOM 501  C CA  . THR A 1 101 ? 12.05791  11.96770 81.96150  1.000 60.62712  ?  71  THR A CA  1 
ATOM 502  C C   . THR A 1 101 ? 10.92751  11.11383 81.41037  1.000 59.20183  ?  71  THR A C   1 
ATOM 503  O O   . THR A 1 101 ? 10.84436  10.94488 80.19249  1.000 48.26697  ?  71  THR A O   1 
ATOM 504  C CB  . THR A 1 101 ? 13.32469  11.10162 82.05758  1.000 66.40033  ?  71  THR A CB  1 
ATOM 505  O OG1 . THR A 1 101 ? 13.16403  10.12683 83.09578  1.000 80.95434  ?  71  THR A OG1 1 
ATOM 506  C CG2 . THR A 1 101 ? 14.53930  11.96482 82.36025  1.000 54.08799  ?  71  THR A CG2 1 
ATOM 507  N N   . ASP A 1 102 ? 10.06157  10.57419 82.26340  1.000 75.56315  ?  72  ASP A N   1 
ATOM 508  C CA  . ASP A 1 102 ? 8.94132   9.74851  81.83295  1.000 68.47985  ?  72  ASP A CA  1 
ATOM 509  C C   . ASP A 1 102 ? 7.65649   10.56477 81.87401  1.000 66.73384  ?  72  ASP A C   1 
ATOM 510  O O   . ASP A 1 102 ? 7.31837   11.14733 82.90955  1.000 59.76333  ?  72  ASP A O   1 
ATOM 511  C CB  . ASP A 1 102 ? 8.80533   8.50683  82.71631  1.000 68.36144  ?  72  ASP A CB  1 
ATOM 512  C CG  . ASP A 1 102 ? 9.95005   7.53027  82.53120  1.000 89.06652  ?  72  ASP A CG  1 
ATOM 513  O OD1 . ASP A 1 102 ? 10.42180  7.37516  81.38526  1.000 88.32925  ?  72  ASP A OD1 1 
ATOM 514  O OD2 . ASP A 1 102 ? 10.37716  6.91655  83.53169  1.000 108.16671 -1 72  ASP A OD2 1 
ATOM 515  N N   . PHE A 1 103 ? 6.94844   10.60527 80.74698  1.000 66.99111  ?  73  PHE A N   1 
ATOM 516  C CA  . PHE A 1 103 ? 5.67094   11.29429 80.63428  1.000 61.22504  ?  73  PHE A CA  1 
ATOM 517  C C   . PHE A 1 103 ? 4.68749   10.39800 79.89821  1.000 63.16148  ?  73  PHE A C   1 
ATOM 518  O O   . PHE A 1 103 ? 5.04678   9.75340  78.90871  1.000 71.49687  ?  73  PHE A O   1 
ATOM 519  C CB  . PHE A 1 103 ? 5.81292   12.63175 79.89455  1.000 54.51435  ?  73  PHE A CB  1 
ATOM 520  C CG  . PHE A 1 103 ? 6.65000   13.64548 80.62233  1.000 61.60338  ?  73  PHE A CG  1 
ATOM 521  C CD1 . PHE A 1 103 ? 6.06625   14.54035 81.50355  1.000 63.23650  ?  73  PHE A CD1 1 
ATOM 522  C CD2 . PHE A 1 103 ? 8.01901   13.70888 80.42000  1.000 64.89348  ?  73  PHE A CD2 1 
ATOM 523  C CE1 . PHE A 1 103 ? 6.83179   15.47736 82.17125  1.000 53.04399  ?  73  PHE A CE1 1 
ATOM 524  C CE2 . PHE A 1 103 ? 8.79054   14.64301 81.08622  1.000 55.61653  ?  73  PHE A CE2 1 
ATOM 525  C CZ  . PHE A 1 103 ? 8.19581   15.52790 81.96301  1.000 55.40759  ?  73  PHE A CZ  1 
ATOM 526  N N   . THR A 1 104 ? 3.44721   10.35856 80.38215  1.000 65.78009  ?  74  THR A N   1 
ATOM 527  C CA  . THR A 1 104 ? 2.41418   9.50991  79.80543  1.000 68.38603  ?  74  THR A CA  1 
ATOM 528  C C   . THR A 1 104 ? 1.16311   10.32625 79.51776  1.000 64.33582  ?  74  THR A C   1 
ATOM 529  O O   . THR A 1 104 ? 0.79279   11.20990 80.29656  1.000 65.70834  ?  74  THR A O   1 
ATOM 530  C CB  . THR A 1 104 ? 2.05780   8.33875  80.73573  1.000 69.61982  ?  74  THR A CB  1 
ATOM 531  O OG1 . THR A 1 104 ? 1.63031   8.84550  82.00603  1.000 83.31108  ?  74  THR A OG1 1 
ATOM 532  C CG2 . THR A 1 104 ? 3.25772   7.42343  80.93463  1.000 69.48244  ?  74  THR A CG2 1 
ATOM 533  N N   . LEU A 1 105 ? 0.51726   10.02279 78.39345  1.000 61.19477  ?  75  LEU A N   1 
ATOM 534  C CA  . LEU A 1 105 ? -0.76530  10.61001 78.02423  1.000 55.27230  ?  75  LEU A CA  1 
ATOM 535  C C   . LEU A 1 105 ? -1.80723  9.50242  78.00400  1.000 55.30364  ?  75  LEU A C   1 
ATOM 536  O O   . LEU A 1 105 ? -1.71646  8.57645  77.19073  1.000 52.14503  ?  75  LEU A O   1 
ATOM 537  C CB  . LEU A 1 105 ? -0.69186  11.30290 76.66231  1.000 44.97049  ?  75  LEU A CB  1 
ATOM 538  C CG  . LEU A 1 105 ? -2.01790  11.87405 76.15447  1.000 42.46055  ?  75  LEU A CG  1 
ATOM 539  C CD1 . LEU A 1 105 ? -2.52390  12.96418 77.08781  1.000 48.87564  ?  75  LEU A CD1 1 
ATOM 540  C CD2 . LEU A 1 105 ? -1.88228  12.39683 74.73246  1.000 40.77302  ?  75  LEU A CD2 1 
ATOM 541  N N   . THR A 1 106 ? -2.79228  9.59864  78.89168  1.000 60.33756  ?  76  THR A N   1 
ATOM 542  C CA  . THR A 1 106 ? -3.80247  8.56113  79.06760  1.000 58.60040  ?  76  THR A CA  1 
ATOM 543  C C   . THR A 1 106 ? -5.14122  9.08075  78.55707  1.000 62.74287  ?  76  THR A C   1 
ATOM 544  O O   . THR A 1 106 ? -5.70457  10.02412 79.12244  1.000 72.71719  ?  76  THR A O   1 
ATOM 545  C CB  . THR A 1 106 ? -3.90216  8.14461  80.53329  1.000 63.43982  ?  76  THR A CB  1 
ATOM 546  O OG1 . THR A 1 106 ? -2.58873  7.89619  81.04990  1.000 65.71440  ?  76  THR A OG1 1 
ATOM 547  C CG2 . THR A 1 106 ? -4.74039  6.88212  80.67027  1.000 73.62311  ?  76  THR A CG2 1 
ATOM 548  N N   . ILE A 1 107 ? -5.64487  8.46589  77.49229  1.000 64.07155  ?  77  ILE A N   1 
ATOM 549  C CA  . ILE A 1 107 ? -6.96738  8.76260  76.95523  1.000 59.95549  ?  77  ILE A CA  1 
ATOM 550  C C   . ILE A 1 107 ? -7.89897  7.65381  77.42670  1.000 60.32524  ?  77  ILE A C   1 
ATOM 551  O O   . ILE A 1 107 ? -7.77463  6.50184  76.99719  1.000 60.44642  ?  77  ILE A O   1 
ATOM 552  C CB  . ILE A 1 107 ? -6.94866  8.87046  75.42522  1.000 62.91574  ?  77  ILE A CB  1 
ATOM 553  C CG1 . ILE A 1 107 ? -5.78530  9.75312  74.96810  1.000 50.81485  ?  77  ILE A CG1 1 
ATOM 554  C CG2 . ILE A 1 107 ? -8.26755  9.43277  74.91799  1.000 63.61489  ?  77  ILE A CG2 1 
ATOM 555  C CD1 . ILE A 1 107 ? -5.63778  9.83961  73.46407  1.000 48.32782  ?  77  ILE A CD1 1 
ATOM 556  N N   . SER A 1 108 ? -8.83389  7.99904  78.31225  1.000 56.63308  ?  78  SER A N   1 
ATOM 557  C CA  . SER A 1 108 ? -9.66867  7.00839  78.98290  1.000 58.51901  ?  78  SER A CA  1 
ATOM 558  C C   . SER A 1 108 ? -10.56350 6.25018  78.00922  1.000 88.08846  ?  78  SER A C   1 
ATOM 559  O O   . SER A 1 108 ? -10.35953 5.05502  77.77556  1.000 116.92145 ?  78  SER A O   1 
ATOM 560  C CB  . SER A 1 108 ? -10.52163 7.67870  80.06238  1.000 78.24550  ?  78  SER A CB  1 
ATOM 561  O OG  . SER A 1 108 ? -11.41859 8.61700  79.49473  1.000 109.38763 ?  78  SER A OG  1 
ATOM 562  N N   . ARG A 1 109 ? -11.55843 6.92751  77.44434  1.000 87.42771  ?  79  ARG A N   1 
ATOM 563  C CA  . ARG A 1 109 ? -12.53744 6.30744  76.55954  1.000 64.14903  ?  79  ARG A CA  1 
ATOM 564  C C   . ARG A 1 109 ? -12.37061 6.87789  75.15805  1.000 68.13252  ?  79  ARG A C   1 
ATOM 565  O O   . ARG A 1 109 ? -12.58338 8.07525  74.94241  1.000 97.41140  ?  79  ARG A O   1 
ATOM 566  C CB  . ARG A 1 109 ? -13.95623 6.53808  77.07840  1.000 60.67127  ?  79  ARG A CB  1 
ATOM 567  C CG  . ARG A 1 109 ? -14.23224 5.86362  78.41268  1.000 85.43463  ?  79  ARG A CG  1 
ATOM 568  C CD  . ARG A 1 109 ? -15.38275 6.52948  79.14655  1.000 93.75408  ?  79  ARG A CD  1 
ATOM 569  N NE  . ARG A 1 109 ? -15.06850 7.91023  79.50263  1.000 85.65580  ?  79  ARG A NE  1 
ATOM 570  C CZ  . ARG A 1 109 ? -15.85694 8.69250  80.23237  1.000 121.12901 ?  79  ARG A CZ  1 
ATOM 571  N NH1 . ARG A 1 109 ? -17.01280 8.23082  80.69031  1.000 137.70657 ?  79  ARG A NH1 1 
ATOM 572  N NH2 . ARG A 1 109 ? -15.48907 9.93686  80.50641  1.000 105.29466 ?  79  ARG A NH2 1 
ATOM 573  N N   . LEU A 1 110 ? -11.99473 6.02287  74.21229  1.000 63.55957  ?  80  LEU A N   1 
ATOM 574  C CA  . LEU A 1 110 ? -11.73051 6.46803  72.85327  1.000 70.60224  ?  80  LEU A CA  1 
ATOM 575  C C   . LEU A 1 110 ? -13.02608 6.65832  72.07388  1.000 59.08074  ?  80  LEU A C   1 
ATOM 576  O O   . LEU A 1 110 ? -14.00329 5.92652  72.25460  1.000 59.68458  ?  80  LEU A O   1 
ATOM 577  C CB  . LEU A 1 110 ? -10.83320 5.46813  72.12315  1.000 57.11692  ?  80  LEU A CB  1 
ATOM 578  C CG  . LEU A 1 110 ? -9.38925  5.34731  72.61138  1.000 56.19515  ?  80  LEU A CG  1 
ATOM 579  C CD1 . LEU A 1 110 ? -8.64077  4.31127  71.79345  1.000 66.11690  ?  80  LEU A CD1 1 
ATOM 580  C CD2 . LEU A 1 110 ? -8.68658  6.69138  72.54346  1.000 61.14336  ?  80  LEU A CD2 1 
ATOM 581  N N   . GLU A 1 111 ? -13.02116 7.65983  71.20380  1.000 67.32960  ?  81  GLU A N   1 
ATOM 582  C CA  . GLU A 1 111 ? -14.09002 7.94592  70.26353  1.000 61.30026  ?  81  GLU A CA  1 
ATOM 583  C C   . GLU A 1 111 ? -13.53295 7.93592  68.84610  1.000 69.70938  ?  81  GLU A C   1 
ATOM 584  O O   . GLU A 1 111 ? -12.32807 8.12954  68.64397  1.000 63.78634  ?  81  GLU A O   1 
ATOM 585  C CB  . GLU A 1 111 ? -14.73689 9.30945  70.55336  1.000 79.91194  ?  81  GLU A CB  1 
ATOM 586  C CG  . GLU A 1 111 ? -16.01896 9.25250  71.37274  1.000 97.39454  ?  81  GLU A CG  1 
ATOM 587  C CD  . GLU A 1 111 ? -15.77723 9.40352  72.86168  1.000 98.98278  ?  81  GLU A CD  1 
ATOM 588  O OE1 . GLU A 1 111 ? -14.88706 8.71214  73.39826  1.000 89.03253  ?  81  GLU A OE1 1 
ATOM 589  O OE2 . GLU A 1 111 ? -16.47585 10.22306 73.49485  1.000 80.91435  -1 81  GLU A OE2 1 
ATOM 590  N N   . PRO A 1 112 ? -14.37846 7.70410  67.83742  1.000 77.90161  ?  82  PRO A N   1 
ATOM 591  C CA  . PRO A 1 112 ? -13.89427 7.78005  66.44814  1.000 78.39792  ?  82  PRO A CA  1 
ATOM 592  C C   . PRO A 1 112 ? -13.33399 9.14183  66.07413  1.000 81.91036  ?  82  PRO A C   1 
ATOM 593  O O   . PRO A 1 112 ? -12.58992 9.24058  65.09036  1.000 72.25731  ?  82  PRO A O   1 
ATOM 594  C CB  . PRO A 1 112 ? -15.14263 7.44168  65.62183  1.000 65.97337  ?  82  PRO A CB  1 
ATOM 595  C CG  . PRO A 1 112 ? -16.00074 6.64706  66.54699  1.000 65.92760  ?  82  PRO A CG  1 
ATOM 596  C CD  . PRO A 1 112 ? -15.77035 7.22705  67.91116  1.000 64.07785  ?  82  PRO A CD  1 
ATOM 597  N N   . GLU A 1 113 ? -13.66773 10.19419 66.82488  1.000 81.42040  ?  83  GLU A N   1 
ATOM 598  C CA  . GLU A 1 113 ? -13.10931 11.51454 66.56379  1.000 80.27979  ?  83  GLU A CA  1 
ATOM 599  C C   . GLU A 1 113 ? -11.65402 11.62441 66.99937  1.000 70.37736  ?  83  GLU A C   1 
ATOM 600  O O   . GLU A 1 113 ? -10.96094 12.55359 66.57133  1.000 67.70735  ?  83  GLU A O   1 
ATOM 601  C CB  . GLU A 1 113 ? -13.94347 12.58301 67.27223  1.000 80.71950  ?  83  GLU A CB  1 
ATOM 602  C CG  . GLU A 1 113 ? -13.99755 12.41421 68.78330  1.000 91.90703  ?  83  GLU A CG  1 
ATOM 603  C CD  . GLU A 1 113 ? -14.86179 13.45860 69.46214  1.000 110.41075 ?  83  GLU A CD  1 
ATOM 604  O OE1 . GLU A 1 113 ? -15.41504 14.32734 68.75559  1.000 105.49933 ?  83  GLU A OE1 1 
ATOM 605  O OE2 . GLU A 1 113 ? -14.98784 13.40982 70.70413  1.000 120.06103 -1 83  GLU A OE2 1 
ATOM 606  N N   . ASP A 1 114 ? -11.17697 10.70238 67.83415  1.000 74.93575  ?  84  ASP A N   1 
ATOM 607  C CA  . ASP A 1 114 ? -9.81392  10.74291 68.34892  1.000 73.16640  ?  84  ASP A CA  1 
ATOM 608  C C   . ASP A 1 114 ? -8.79224  10.14801 67.38605  1.000 65.32589  ?  84  ASP A C   1 
ATOM 609  O O   . ASP A 1 114 ? -7.63458  9.96194  67.77599  1.000 59.90261  ?  84  ASP A O   1 
ATOM 610  C CB  . ASP A 1 114 ? -9.73968  10.01800 69.69597  1.000 60.06939  ?  84  ASP A CB  1 
ATOM 611  C CG  . ASP A 1 114 ? -10.65371 10.63207 70.73965  1.000 77.24007  ?  84  ASP A CG  1 
ATOM 612  O OD1 . ASP A 1 114 ? -10.95961 11.83861 70.62978  1.000 62.38743  ?  84  ASP A OD1 1 
ATOM 613  O OD2 . ASP A 1 114 ? -11.06504 9.90866  71.67128  1.000 64.03233  -1 84  ASP A OD2 1 
ATOM 614  N N   . PHE A 1 115 ? -9.18669  9.84424  66.15216  1.000 86.77556  ?  85  PHE A N   1 
ATOM 615  C CA  . PHE A 1 115 ? -8.25748  9.34381  65.14106  1.000 92.01663  ?  85  PHE A CA  1 
ATOM 616  C C   . PHE A 1 115 ? -7.33257  10.48002 64.72545  1.000 92.85536  ?  85  PHE A C   1 
ATOM 617  O O   . PHE A 1 115 ? -7.70564  11.34182 63.92631  1.000 80.48019  ?  85  PHE A O   1 
ATOM 618  C CB  . PHE A 1 115 ? -9.02201  8.78447  63.94604  1.000 101.77886 ?  85  PHE A CB  1 
ATOM 619  C CG  . PHE A 1 115 ? -8.14601  8.41959  62.77947  1.000 110.69512 ?  85  PHE A CG  1 
ATOM 620  C CD1 . PHE A 1 115 ? -7.41760  7.24291  62.78509  1.000 83.45887  ?  85  PHE A CD1 1 
ATOM 621  C CD2 . PHE A 1 115 ? -8.05889  9.24953  61.67301  1.000 124.82549 ?  85  PHE A CD2 1 
ATOM 622  C CE1 . PHE A 1 115 ? -6.61206  6.90315  61.71436  1.000 88.71579  ?  85  PHE A CE1 1 
ATOM 623  C CE2 . PHE A 1 115 ? -7.25514  8.91580  60.59908  1.000 121.76247 ?  85  PHE A CE2 1 
ATOM 624  C CZ  . PHE A 1 115 ? -6.53132  7.74053  60.61985  1.000 110.82696 ?  85  PHE A CZ  1 
ATOM 625  N N   . ALA A 1 116 ? -6.11897  10.48770 65.26961  1.000 73.99295  ?  86  ALA A N   1 
ATOM 626  C CA  . ALA A 1 116 ? -5.16408  11.55497 65.00060  1.000 55.86841  ?  86  ALA A CA  1 
ATOM 627  C C   . ALA A 1 116 ? -3.78403  11.10101 65.45344  1.000 54.45805  ?  86  ALA A C   1 
ATOM 628  O O   . ALA A 1 116 ? -3.62836  10.05770 66.09340  1.000 54.08367  ?  86  ALA A O   1 
ATOM 629  C CB  . ALA A 1 116 ? -5.56252  12.85546 65.70246  1.000 54.93201  ?  86  ALA A CB  1 
ATOM 630  N N   . VAL A 1 117 ? -2.78201  11.90635 65.11003  1.000 54.00974  ?  87  VAL A N   1 
ATOM 631  C CA  . VAL A 1 117 ? -1.40461  11.69461 65.53827  1.000 52.83196  ?  87  VAL A CA  1 
ATOM 632  C C   . VAL A 1 117 ? -1.12100  12.63362 66.70122  1.000 50.71875  ?  87  VAL A C   1 
ATOM 633  O O   . VAL A 1 117 ? -1.42095  13.83204 66.62833  1.000 50.47646  ?  87  VAL A O   1 
ATOM 634  C CB  . VAL A 1 117 ? -0.41801  11.93260 64.38246  1.000 54.01806  ?  87  VAL A CB  1 
ATOM 635  C CG1 . VAL A 1 117 ? 1.00285   11.61771 64.82178  1.000 53.16879  ?  87  VAL A CG1 1 
ATOM 636  C CG2 . VAL A 1 117 ? -0.80752  11.09853 63.17224  1.000 56.73932  ?  87  VAL A CG2 1 
ATOM 637  N N   . TYR A 1 118 ? -0.54715  12.09565 67.77285  1.000 49.63561  ?  88  TYR A N   1 
ATOM 638  C CA  . TYR A 1 118 ? -0.29186  12.84885 68.99327  1.000 58.63885  ?  88  TYR A CA  1 
ATOM 639  C C   . TYR A 1 118 ? 1.20252   13.10046 69.13916  1.000 58.90260  ?  88  TYR A C   1 
ATOM 640  O O   . TYR A 1 118 ? 2.01158   12.18504 68.95419  1.000 58.22017  ?  88  TYR A O   1 
ATOM 641  C CB  . TYR A 1 118 ? -0.83564  12.10299 70.21366  1.000 48.80702  ?  88  TYR A CB  1 
ATOM 642  C CG  . TYR A 1 118 ? -2.33685  11.91930 70.18376  1.000 48.67910  ?  88  TYR A CG  1 
ATOM 643  C CD1 . TYR A 1 118 ? -2.91213  10.84204 69.52193  1.000 49.96087  ?  88  TYR A CD1 1 
ATOM 644  C CD2 . TYR A 1 118 ? -3.17920  12.82801 70.81051  1.000 52.21339  ?  88  TYR A CD2 1 
ATOM 645  C CE1 . TYR A 1 118 ? -4.28378  10.67363 69.48818  1.000 59.55878  ?  88  TYR A CE1 1 
ATOM 646  C CE2 . TYR A 1 118 ? -4.55206  12.66742 70.78288  1.000 49.46530  ?  88  TYR A CE2 1 
ATOM 647  C CZ  . TYR A 1 118 ? -5.09868  11.58902 70.12058  1.000 59.28227  ?  88  TYR A CZ  1 
ATOM 648  O OH  . TYR A 1 118 ? -6.46482  11.42574 70.09063  1.000 60.59205  ?  88  TYR A OH  1 
ATOM 649  N N   . TYR A 1 119 ? 1.56221   14.33702 69.47317  1.000 52.46109  ?  89  TYR A N   1 
ATOM 650  C CA  . TYR A 1 119 ? 2.95121   14.76079 69.56190  1.000 53.79779  ?  89  TYR A CA  1 
ATOM 651  C C   . TYR A 1 119 ? 3.29999   15.16614 70.98923  1.000 47.51938  ?  89  TYR A C   1 
ATOM 652  O O   . TYR A 1 119 ? 2.43672   15.29001 71.86185  1.000 44.36662  ?  89  TYR A O   1 
ATOM 653  C CB  . TYR A 1 119 ? 3.23623   15.91949 68.59780  1.000 45.57221  ?  89  TYR A CB  1 
ATOM 654  C CG  . TYR A 1 119 ? 3.26905   15.50905 67.14370  1.000 47.15653  ?  89  TYR A CG  1 
ATOM 655  C CD1 . TYR A 1 119 ? 4.43691   15.03056 66.56460  1.000 51.68755  ?  89  TYR A CD1 1 
ATOM 656  C CD2 . TYR A 1 119 ? 2.13416   15.60030 66.34975  1.000 48.44431  ?  89  TYR A CD2 1 
ATOM 657  C CE1 . TYR A 1 119 ? 4.47382   14.65404 65.23590  1.000 49.80454  ?  89  TYR A CE1 1 
ATOM 658  C CE2 . TYR A 1 119 ? 2.16127   15.22616 65.01938  1.000 50.39830  ?  89  TYR A CE2 1 
ATOM 659  C CZ  . TYR A 1 119 ? 3.33381   14.75399 64.46816  1.000 51.10365  ?  89  TYR A CZ  1 
ATOM 660  O OH  . TYR A 1 119 ? 3.36696   14.38020 63.14449  1.000 63.05406  ?  89  TYR A OH  1 
ATOM 661  N N   . CYS A 1 120 ? 4.59573   15.38061 71.20857  1.000 56.41367  ?  90  CYS A N   1 
ATOM 662  C CA  . CYS A 1 120 ? 5.14510   15.69391 72.52051  1.000 53.64586  ?  90  CYS A CA  1 
ATOM 663  C C   . CYS A 1 120 ? 6.14579   16.82878 72.36533  1.000 60.59615  ?  90  CYS A C   1 
ATOM 664  O O   . CYS A 1 120 ? 7.02469   16.76450 71.50122  1.000 67.18143  ?  90  CYS A O   1 
ATOM 665  C CB  . CYS A 1 120 ? 5.81735   14.45896 73.13363  1.000 44.56111  ?  90  CYS A CB  1 
ATOM 666  S SG  . CYS A 1 120 ? 6.39658   14.64093 74.82999  1.000 91.39759  ?  90  CYS A SG  1 
ATOM 667  N N   . GLN A 1 121 ? 6.01463   17.86256 73.19567  1.000 42.05212  ?  91  GLN A N   1 
ATOM 668  C CA  . GLN A 1 121 ? 6.83345   19.06010 73.06767  1.000 41.38236  ?  91  GLN A CA  1 
ATOM 669  C C   . GLN A 1 121 ? 7.28668   19.52902 74.44192  1.000 47.37443  ?  91  GLN A C   1 
ATOM 670  O O   . GLN A 1 121 ? 6.54455   19.41782 75.42171  1.000 46.07718  ?  91  GLN A O   1 
ATOM 671  C CB  . GLN A 1 121 ? 6.06165   20.17875 72.34918  1.000 50.89875  ?  91  GLN A CB  1 
ATOM 672  C CG  . GLN A 1 121 ? 6.83633   21.47489 72.14672  1.000 42.59849  ?  91  GLN A CG  1 
ATOM 673  C CD  . GLN A 1 121 ? 6.57760   22.49053 73.24423  1.000 48.36916  ?  91  GLN A CD  1 
ATOM 674  O OE1 . GLN A 1 121 ? 5.66694   22.32651 74.05664  1.000 42.34120  ?  91  GLN A OE1 1 
ATOM 675  N NE2 . GLN A 1 121 ? 7.37943   23.54873 73.27183  1.000 51.02508  ?  91  GLN A NE2 1 
ATOM 676  N N   . GLN A 1 122 ? 8.50958   20.05295 74.50441  1.000 51.57921  ?  92  GLN A N   1 
ATOM 677  C CA  . GLN A 1 122 ? 9.08008   20.58160 75.73312  1.000 48.67985  ?  92  GLN A CA  1 
ATOM 678  C C   . GLN A 1 122 ? 9.73652   21.92636 75.45225  1.000 59.55442  ?  92  GLN A C   1 
ATOM 679  O O   . GLN A 1 122 ? 10.13893  22.22296 74.32427  1.000 52.92613  ?  92  GLN A O   1 
ATOM 680  C CB  . GLN A 1 122 ? 10.10154  19.60798 76.34472  1.000 50.94586  ?  92  GLN A CB  1 
ATOM 681  C CG  . GLN A 1 122 ? 11.27553  19.26610 75.43460  1.000 41.66380  ?  92  GLN A CG  1 
ATOM 682  C CD  . GLN A 1 122 ? 12.43886  20.22905 75.58234  1.000 41.26930  ?  92  GLN A CD  1 
ATOM 683  O OE1 . GLN A 1 122 ? 12.55070  20.93735 76.58277  1.000 52.20322  ?  92  GLN A OE1 1 
ATOM 684  N NE2 . GLN A 1 122 ? 13.31147  20.26033 74.58216  1.000 41.10539  ?  92  GLN A NE2 1 
ATOM 685  N N   . TYR A 1 123 ? 9.83983   22.74154 76.49997  1.000 65.26395  ?  93  TYR A N   1 
ATOM 686  C CA  . TYR A 1 123 ? 10.48659  24.04192 76.41388  1.000 40.26457  ?  93  TYR A CA  1 
ATOM 687  C C   . TYR A 1 123 ? 11.36907  24.24380 77.63605  1.000 40.84949  ?  93  TYR A C   1 
ATOM 688  O O   . TYR A 1 123 ? 11.05860  23.76987 78.73196  1.000 50.83048  ?  93  TYR A O   1 
ATOM 689  C CB  . TYR A 1 123 ? 9.46329   25.18347 76.30726  1.000 55.74622  ?  93  TYR A CB  1 
ATOM 690  C CG  . TYR A 1 123 ? 10.08023  26.56667 76.31329  1.000 58.24423  ?  93  TYR A CG  1 
ATOM 691  C CD1 . TYR A 1 123 ? 10.57632  27.13299 75.14608  1.000 47.13707  ?  93  TYR A CD1 1 
ATOM 692  C CD2 . TYR A 1 123 ? 10.16567  27.30603 77.48723  1.000 50.23026  ?  93  TYR A CD2 1 
ATOM 693  C CE1 . TYR A 1 123 ? 11.14142  28.39570 75.14834  1.000 41.38570  ?  93  TYR A CE1 1 
ATOM 694  C CE2 . TYR A 1 123 ? 10.72912  28.56815 77.49901  1.000 55.72620  ?  93  TYR A CE2 1 
ATOM 695  C CZ  . TYR A 1 123 ? 11.21467  29.10839 76.32743  1.000 49.14716  ?  93  TYR A CZ  1 
ATOM 696  O OH  . TYR A 1 123 ? 11.77492  30.36545 76.33647  1.000 41.47129  ?  93  TYR A OH  1 
ATOM 697  N N   . GLY A 1 124 ? 12.47378  24.95586 77.43485  1.000 40.42184  ?  94  GLY A N   1 
ATOM 698  C CA  . GLY A 1 124 ? 13.40427  25.23791 78.50893  1.000 45.92360  ?  94  GLY A CA  1 
ATOM 699  C C   . GLY A 1 124 ? 14.78862  25.56594 77.99306  1.000 53.24128  ?  94  GLY A C   1 
ATOM 700  O O   . GLY A 1 124 ? 15.04062  26.68568 77.53767  1.000 40.03952  ?  94  GLY A O   1 
ATOM 701  N N   . SER A 1 125 ? 15.69950  24.59314 78.06135  1.000 56.31170  ?  95  SER A N   1 
ATOM 702  C CA  . SER A 1 125 ? 17.01492  24.76927 77.46074  1.000 40.78488  ?  95  SER A CA  1 
ATOM 703  C C   . SER A 1 125 ? 16.95049  24.76436 75.94019  1.000 45.69673  ?  95  SER A C   1 
ATOM 704  O O   . SER A 1 125 ? 17.86933  25.27365 75.29007  1.000 39.53512  ?  95  SER A O   1 
ATOM 705  C CB  . SER A 1 125 ? 17.96614  23.67543 77.94663  1.000 48.05030  ?  95  SER A CB  1 
ATOM 706  O OG  . SER A 1 125 ? 18.04086  23.65848 79.36128  1.000 73.30353  ?  95  SER A OG  1 
ATOM 707  N N   . SER A 1 126 ? 15.88971  24.20699 75.36630  1.000 54.23069  ?  96  SER A N   1 
ATOM 708  C CA  . SER A 1 126 ? 15.70548  24.15003 73.92199  1.000 39.19269  ?  96  SER A CA  1 
ATOM 709  C C   . SER A 1 126 ? 14.21478  23.98499 73.64472  1.000 44.57152  ?  96  SER A C   1 
ATOM 710  O O   . SER A 1 126 ? 13.38719  24.03348 74.56117  1.000 50.28775  ?  96  SER A O   1 
ATOM 711  C CB  . SER A 1 126 ? 16.53770  23.01827 73.31010  1.000 47.04318  ?  96  SER A CB  1 
ATOM 712  O OG  . SER A 1 126 ? 16.23992  21.77721 73.92679  1.000 41.40548  ?  96  SER A OG  1 
ATOM 713  N N   . LEU A 1 127 ? 13.87018  23.78882 72.37348  1.000 48.01438  ?  97  LEU A N   1 
ATOM 714  C CA  . LEU A 1 127 ? 12.48571  23.59038 71.94573  1.000 44.60881  ?  97  LEU A CA  1 
ATOM 715  C C   . LEU A 1 127 ? 12.47222  22.38939 71.00482  1.000 40.00821  ?  97  LEU A C   1 
ATOM 716  O O   . LEU A 1 127 ? 12.78372  22.51997 69.81727  1.000 40.57674  ?  97  LEU A O   1 
ATOM 717  C CB  . LEU A 1 127 ? 11.93097  24.84448 71.27321  1.000 46.33810  ?  97  LEU A CB  1 
ATOM 718  C CG  . LEU A 1 127 ? 10.41736  25.08346 71.29905  1.000 43.62452  ?  97  LEU A CG  1 
ATOM 719  C CD1 . LEU A 1 127 ? 10.10866  26.53138 70.95060  1.000 40.57102  ?  97  LEU A CD1 1 
ATOM 720  C CD2 . LEU A 1 127 ? 9.68105   24.14425 70.35379  1.000 54.30878  ?  97  LEU A CD2 1 
ATOM 721  N N   . THR A 1 128 ? 12.11084  21.22391 71.53590  1.000 48.42988  ?  98  THR A N   1 
ATOM 722  C CA  . THR A 1 128 ? 12.14535  19.97198 70.79423  1.000 41.32618  ?  98  THR A CA  1 
ATOM 723  C C   . THR A 1 128 ? 10.75878  19.34468 70.76116  1.000 47.85904  ?  98  THR A C   1 
ATOM 724  O O   . THR A 1 128 ? 10.04263  19.34310 71.76769  1.000 47.30439  ?  98  THR A O   1 
ATOM 725  C CB  . THR A 1 128 ? 13.14366  18.98804 71.41977  1.000 42.12652  ?  98  THR A CB  1 
ATOM 726  O OG1 . THR A 1 128 ? 14.42150  19.62163 71.55459  1.000 71.13597  ?  98  THR A OG1 1 
ATOM 727  C CG2 . THR A 1 128 ? 13.29145  17.74545 70.55197  1.000 61.92583  ?  98  THR A CG2 1 
ATOM 728  N N   . PHE A 1 129 ? 10.38566  18.81790 69.59938  1.000 42.47319  ?  99  PHE A N   1 
ATOM 729  C CA  . PHE A 1 129 ? 9.15261   18.06522 69.43013  1.000 46.54794  ?  99  PHE A CA  1 
ATOM 730  C C   . PHE A 1 129 ? 9.44185   16.56782 69.40631  1.000 56.62981  ?  99  PHE A C   1 
ATOM 731  O O   . PHE A 1 129 ? 10.54623  16.12581 69.07914  1.000 46.18873  ?  99  PHE A O   1 
ATOM 732  C CB  . PHE A 1 129 ? 8.43051   18.47754 68.14395  1.000 46.48347  ?  99  PHE A CB  1 
ATOM 733  C CG  . PHE A 1 129 ? 7.50207   19.64645 68.31464  1.000 46.82019  ?  99  PHE A CG  1 
ATOM 734  C CD1 . PHE A 1 129 ? 6.20304   19.45488 68.75533  1.000 49.67558  ?  99  PHE A CD1 1 
ATOM 735  C CD2 . PHE A 1 129 ? 7.92351   20.93409 68.02722  1.000 43.09770  ?  99  PHE A CD2 1 
ATOM 736  C CE1 . PHE A 1 129 ? 5.34252   20.52550 68.91027  1.000 49.45058  ?  99  PHE A CE1 1 
ATOM 737  C CE2 . PHE A 1 129 ? 7.06799   22.00916 68.18104  1.000 43.20569  ?  99  PHE A CE2 1 
ATOM 738  C CZ  . PHE A 1 129 ? 5.77585   21.80406 68.62350  1.000 53.46904  ?  99  PHE A CZ  1 
ATOM 739  N N   . GLY A 1 130 ? 8.42440   15.78615 69.76107  1.000 54.25107  ?  100 GLY A N   1 
ATOM 740  C CA  . GLY A 1 130 ? 8.54229   14.34572 69.76510  1.000 45.90202  ?  100 GLY A CA  1 
ATOM 741  C C   . GLY A 1 130 ? 8.41750   13.74924 68.37666  1.000 47.49390  ?  100 GLY A C   1 
ATOM 742  O O   . GLY A 1 130 ? 8.19405   14.43547 67.37949  1.000 47.60114  ?  100 GLY A O   1 
ATOM 743  N N   . GLY A 1 131 ? 8.57167   12.42486 68.32091  1.000 50.35699  ?  101 GLY A N   1 
ATOM 744  C CA  . GLY A 1 131 ? 8.45229   11.72851 67.05228  1.000 51.29257  ?  101 GLY A CA  1 
ATOM 745  C C   . GLY A 1 131 ? 7.02324   11.61941 66.56236  1.000 67.51247  ?  101 GLY A C   1 
ATOM 746  O O   . GLY A 1 131 ? 6.77185   11.67949 65.35508  1.000 58.67097  ?  101 GLY A O   1 
ATOM 747  N N   . GLY A 1 132 ? 6.07861   11.46039 67.47369  1.000 62.54442  ?  102 GLY A N   1 
ATOM 748  C CA  . GLY A 1 132 ? 4.67403   11.36525 67.11665  1.000 50.44532  ?  102 GLY A CA  1 
ATOM 749  C C   . GLY A 1 132 ? 4.16185   9.94437  67.26818  1.000 52.60366  ?  102 GLY A C   1 
ATOM 750  O O   . GLY A 1 132 ? 4.87500   8.96997  66.99775  1.000 64.44406  ?  102 GLY A O   1 
ATOM 751  N N   . THR A 1 133 ? 2.91068   9.82372  67.70903  1.000 71.13077  ?  103 THR A N   1 
ATOM 752  C CA  . THR A 1 133 ? 2.24131   8.53595  67.86994  1.000 52.73177  ?  103 THR A CA  1 
ATOM 753  C C   . THR A 1 133 ? 0.93904   8.58044  67.08413  1.000 53.28543  ?  103 THR A C   1 
ATOM 754  O O   . THR A 1 133 ? 0.02088   9.32478  67.44305  1.000 65.49845  ?  103 THR A O   1 
ATOM 755  C CB  . THR A 1 133 ? 1.97272   8.22578  69.34340  1.000 51.96979  ?  103 THR A CB  1 
ATOM 756  O OG1 . THR A 1 133 ? 3.21564   8.05611  70.03606  1.000 52.14165  ?  103 THR A OG1 1 
ATOM 757  C CG2 . THR A 1 133 ? 1.13971   6.95829  69.47831  1.000 53.47677  ?  103 THR A CG2 1 
ATOM 758  N N   . LYS A 1 134 ? 0.85685   7.78967  66.01675  1.000 55.46937  ?  104 LYS A N   1 
ATOM 759  C CA  . LYS A 1 134 ? -0.33876  7.75778  65.18096  1.000 64.46131  ?  104 LYS A CA  1 
ATOM 760  C C   . LYS A 1 134 ? -1.34992  6.79893  65.79706  1.000 60.36753  ?  104 LYS A C   1 
ATOM 761  O O   . LYS A 1 134 ? -1.18214  5.57704  65.72725  1.000 65.72874  ?  104 LYS A O   1 
ATOM 762  C CB  . LYS A 1 134 ? 0.01028   7.34708  63.75347  1.000 60.27297  ?  104 LYS A CB  1 
ATOM 763  C CG  . LYS A 1 134 ? -1.18139  7.36742  62.80740  1.000 97.55273  ?  104 LYS A CG  1 
ATOM 764  C CD  . LYS A 1 134 ? -0.77119  7.07293  61.37408  1.000 114.34683 ?  104 LYS A CD  1 
ATOM 765  C CE  . LYS A 1 134 ? -1.97029  7.13472  60.43961  1.000 105.14400 ?  104 LYS A CE  1 
ATOM 766  N NZ  . LYS A 1 134 ? -1.59132  6.87689  59.02304  1.000 93.79932  ?  104 LYS A NZ  1 
ATOM 767  N N   . LEU A 1 135 ? -2.39842  7.35053  66.40210  1.000 62.69004  ?  105 LEU A N   1 
ATOM 768  C CA  . LEU A 1 135 ? -3.45936  6.55383  67.00393  1.000 60.85909  ?  105 LEU A CA  1 
ATOM 769  C C   . LEU A 1 135 ? -4.56860  6.34874  65.97992  1.000 57.95752  ?  105 LEU A C   1 
ATOM 770  O O   . LEU A 1 135 ? -5.16894  7.31892  65.50458  1.000 70.58099  ?  105 LEU A O   1 
ATOM 771  C CB  . LEU A 1 135 ? -4.00188  7.23396  68.25992  1.000 54.17434  ?  105 LEU A CB  1 
ATOM 772  C CG  . LEU A 1 135 ? -5.11141  6.49042  69.00571  1.000 64.09047  ?  105 LEU A CG  1 
ATOM 773  C CD1 . LEU A 1 135 ? -4.62800  5.12348  69.46518  1.000 55.73178  ?  105 LEU A CD1 1 
ATOM 774  C CD2 . LEU A 1 135 ? -5.60878  7.31133  70.18517  1.000 65.94932  ?  105 LEU A CD2 1 
ATOM 775  N N   . GLU A 1 136 ? -4.83680  5.09160  65.64181  1.000 59.48472  ?  106 GLU A N   1 
ATOM 776  C CA  . GLU A 1 136 ? -5.84331  4.74031  64.65196  1.000 70.29372  ?  106 GLU A CA  1 
ATOM 777  C C   . GLU A 1 136 ? -7.03654  4.08660  65.33500  1.000 66.81228  ?  106 GLU A C   1 
ATOM 778  O O   . GLU A 1 136 ? -6.87453  3.30267  66.27562  1.000 69.54715  ?  106 GLU A O   1 
ATOM 779  C CB  . GLU A 1 136 ? -5.26260  3.80454  63.58878  1.000 81.68540  ?  106 GLU A CB  1 
ATOM 780  C CG  . GLU A 1 136 ? -3.96537  4.30950  62.97580  1.000 86.91477  ?  106 GLU A CG  1 
ATOM 781  C CD  . GLU A 1 136 ? -3.51487  3.48010  61.79068  1.000 109.48603 ?  106 GLU A CD  1 
ATOM 782  O OE1 . GLU A 1 136 ? -4.37252  3.11057  60.96130  1.000 118.62156 ?  106 GLU A OE1 1 
ATOM 783  O OE2 . GLU A 1 136 ? -2.30318  3.19413  61.69080  1.000 116.78635 -1 106 GLU A OE2 1 
ATOM 784  N N   . ILE A 1 137 ? -8.23282  4.41421  64.85732  1.000 66.03716  ?  107 ILE A N   1 
ATOM 785  C CA  . ILE A 1 137 ? -9.48093  3.93282  65.43690  1.000 76.42446  ?  107 ILE A CA  1 
ATOM 786  C C   . ILE A 1 137 ? -10.14945 3.02674  64.41196  1.000 78.76599  ?  107 ILE A C   1 
ATOM 787  O O   . ILE A 1 137 ? -10.66591 3.50080  63.39237  1.000 97.88849  ?  107 ILE A O   1 
ATOM 788  C CB  . ILE A 1 137 ? -10.40358 5.09000  65.84224  1.000 90.18779  ?  107 ILE A CB  1 
ATOM 789  C CG1 . ILE A 1 137 ? -9.67243  6.05250  66.78112  1.000 64.62409  ?  107 ILE A CG1 1 
ATOM 790  C CG2 . ILE A 1 137 ? -11.66598 4.55856  66.49940  1.000 88.70534  ?  107 ILE A CG2 1 
ATOM 791  C CD1 . ILE A 1 137 ? -9.19458  5.41135  68.06498  1.000 58.24265  ?  107 ILE A CD1 1 
ATOM 792  N N   . LYS A 1 138 ? -10.14409 1.72449  64.67896  1.000 93.19077  ?  108 LYS A N   1 
ATOM 793  C CA  . LYS A 1 138 ? -10.77733 0.75846  63.78809  1.000 102.23789 ?  108 LYS A CA  1 
ATOM 794  C C   . LYS A 1 138 ? -12.29629 0.82895  63.89892  1.000 80.75293  ?  108 LYS A C   1 
ATOM 795  O O   . LYS A 1 138 ? -12.88281 0.30976  64.84818  1.000 99.02467  ?  108 LYS A O   1 
ATOM 796  C CB  . LYS A 1 138 ? -10.29283 -0.66031 64.09694  1.000 84.32271  ?  108 LYS A CB  1 
ATOM 797  C CG  . LYS A 1 138 ? -8.81741  -0.88964 63.81407  1.000 103.62177 ?  108 LYS A CG  1 
ATOM 798  C CD  . LYS A 1 138 ? -8.42049  -2.33228 64.08393  1.000 94.83325  ?  108 LYS A CD  1 
ATOM 799  C CE  . LYS A 1 138 ? -6.96451  -2.57972 63.72404  1.000 105.40361 ?  108 LYS A CE  1 
ATOM 800  N NZ  . LYS A 1 138 ? -6.55887  -3.98940 63.97813  1.000 99.10727  ?  108 LYS A NZ  1 
ATOM 801  N N   . SER A 1 153 ? -9.38589  30.43193 70.87853  1.000 99.75007  ?  123 SER A N   1 
ATOM 802  C CA  . SER A 1 153 ? -10.63203 30.38558 70.12257  1.000 87.29053  ?  123 SER A CA  1 
ATOM 803  C C   . SER A 1 153 ? -11.02950 31.77553 69.63422  1.000 66.88094  ?  123 SER A C   1 
ATOM 804  O O   . SER A 1 153 ? -11.41475 31.94841 68.47782  1.000 61.32317  ?  123 SER A O   1 
ATOM 805  C CB  . SER A 1 153 ? -11.75179 29.78214 70.97221  1.000 94.02443  ?  123 SER A CB  1 
ATOM 806  O OG  . SER A 1 153 ? -11.92167 30.50490 72.17892  1.000 93.74219  ?  123 SER A OG  1 
ATOM 807  N N   . GLN A 1 154 ? -10.93713 32.76675 70.52406  1.000 68.67053  ?  124 GLN A N   1 
ATOM 808  C CA  . GLN A 1 154 ? -11.22852 34.14134 70.13255  1.000 57.13639  ?  124 GLN A CA  1 
ATOM 809  C C   . GLN A 1 154 ? -10.05282 34.79054 69.41512  1.000 53.87916  ?  124 GLN A C   1 
ATOM 810  O O   . GLN A 1 154 ? -10.25211 35.71852 68.62309  1.000 35.17840  ?  124 GLN A O   1 
ATOM 811  C CB  . GLN A 1 154 ? -11.61901 34.97236 71.35528  1.000 44.56002  ?  124 GLN A CB  1 
ATOM 812  C CG  . GLN A 1 154 ? -12.92253 34.54347 72.00528  1.000 63.92165  ?  124 GLN A CG  1 
ATOM 813  C CD  . GLN A 1 154 ? -13.42537 35.55361 73.01641  1.000 59.12578  ?  124 GLN A CD  1 
ATOM 814  O OE1 . GLN A 1 154 ? -12.91812 36.67268 73.09732  1.000 49.27996  ?  124 GLN A OE1 1 
ATOM 815  N NE2 . GLN A 1 154 ? -14.42889 35.16387 73.79438  1.000 46.36385  ?  124 GLN A NE2 1 
ATOM 816  N N   . VAL A 1 155 ? -8.83478  34.33041 69.68075  1.000 53.22241  ?  125 VAL A N   1 
ATOM 817  C CA  . VAL A 1 155 ? -7.65492  34.78328 68.95509  1.000 33.08565  ?  125 VAL A CA  1 
ATOM 818  C C   . VAL A 1 155 ? -7.47180  33.88808 67.73859  1.000 32.25978  ?  125 VAL A C   1 
ATOM 819  O O   . VAL A 1 155 ? -7.48204  32.65669 67.85454  1.000 40.32119  ?  125 VAL A O   1 
ATOM 820  C CB  . VAL A 1 155 ? -6.40882  34.75962 69.85494  1.000 32.85848  ?  125 VAL A CB  1 
ATOM 821  C CG1 . VAL A 1 155 ? -5.19595  35.27990 69.09810  1.000 42.71408  ?  125 VAL A CG1 1 
ATOM 822  C CG2 . VAL A 1 155 ? -6.65013  35.57087 71.11807  1.000 45.10232  ?  125 VAL A CG2 1 
ATOM 823  N N   . GLN A 1 156 ? -7.31047  34.50240 66.56962  1.000 31.39862  ?  126 GLN A N   1 
ATOM 824  C CA  . GLN A 1 156 ? -7.23948  33.77450 65.31067  1.000 30.92163  ?  126 GLN A CA  1 
ATOM 825  C C   . GLN A 1 156 ? -5.98083  34.17335 64.55658  1.000 37.63452  ?  126 GLN A C   1 
ATOM 826  O O   . GLN A 1 156 ? -5.73745  35.36331 64.33198  1.000 33.86704  ?  126 GLN A O   1 
ATOM 827  C CB  . GLN A 1 156 ? -8.47879  34.04411 64.45121  1.000 31.71477  ?  126 GLN A CB  1 
ATOM 828  C CG  . GLN A 1 156 ? -8.50958  33.27523 63.14249  1.000 31.61969  ?  126 GLN A CG  1 
ATOM 829  C CD  . GLN A 1 156 ? -9.69803  33.64756 62.27876  1.000 49.75512  ?  126 GLN A CD  1 
ATOM 830  O OE1 . GLN A 1 156 ? -10.36655 34.65258 62.52248  1.000 63.65021  ?  126 GLN A OE1 1 
ATOM 831  N NE2 . GLN A 1 156 ? -9.96851  32.83668 61.26254  1.000 38.88506  ?  126 GLN A NE2 1 
ATOM 832  N N   . LEU A 1 157 ? -5.18773  33.17838 64.16907  1.000 29.47446  ?  127 LEU A N   1 
ATOM 833  C CA  . LEU A 1 157 ? -4.00492  33.37702 63.34160  1.000 28.54425  ?  127 LEU A CA  1 
ATOM 834  C C   . LEU A 1 157 ? -4.31334  32.87409 61.93805  1.000 31.60980  ?  127 LEU A C   1 
ATOM 835  O O   . LEU A 1 157 ? -4.63851  31.69555 61.75633  1.000 41.93614  ?  127 LEU A O   1 
ATOM 836  C CB  . LEU A 1 157 ? -2.79480  32.64667 63.92433  1.000 28.17102  ?  127 LEU A CB  1 
ATOM 837  C CG  . LEU A 1 157 ? -2.41011  32.98986 65.36453  1.000 28.43099  ?  127 LEU A CG  1 
ATOM 838  C CD1 . LEU A 1 157 ? -1.17880  32.20880 65.78835  1.000 28.34868  ?  127 LEU A CD1 1 
ATOM 839  C CD2 . LEU A 1 157 ? -2.17572  34.48098 65.51694  1.000 45.79220  ?  127 LEU A CD2 1 
ATOM 840  N N   . GLN A 1 158 ? -4.21849  33.76468 60.95327  1.000 28.78852  ?  128 GLN A N   1 
ATOM 841  C CA  . GLN A 1 158 ? -4.52309  33.44167 59.56448  1.000 29.28383  ?  128 GLN A CA  1 
ATOM 842  C C   . GLN A 1 158 ? -3.26723  33.62984 58.72697  1.000 31.83904  ?  128 GLN A C   1 
ATOM 843  O O   . GLN A 1 158 ? -2.68749  34.72097 58.70853  1.000 37.87004  ?  128 GLN A O   1 
ATOM 844  C CB  . GLN A 1 158 ? -5.66308  34.31351 59.03494  1.000 30.18703  ?  128 GLN A CB  1 
ATOM 845  C CG  . GLN A 1 158 ? -6.92550  34.25510 59.87777  1.000 30.66641  ?  128 GLN A CG  1 
ATOM 846  C CD  . GLN A 1 158 ? -8.08394  34.99583 59.24278  1.000 41.25007  ?  128 GLN A CD  1 
ATOM 847  O OE1 . GLN A 1 158 ? -8.32113  34.88626 58.03986  1.000 64.09126  ?  128 GLN A OE1 1 
ATOM 848  N NE2 . GLN A 1 158 ? -8.81082  35.76038 60.04934  1.000 72.01879  ?  128 GLN A NE2 1 
ATOM 849  N N   . GLN A 1 159 ? -2.85664  32.57346 58.03299  1.000 45.30315  ?  129 GLN A N   1 
ATOM 850  C CA  . GLN A 1 159 ? -1.63426  32.59061 57.24559  1.000 39.68818  ?  129 GLN A CA  1 
ATOM 851  C C   . GLN A 1 159 ? -1.92304  32.96709 55.79536  1.000 38.85633  ?  129 GLN A C   1 
ATOM 852  O O   . GLN A 1 159 ? -3.03585  32.80149 55.29011  1.000 46.66876  ?  129 GLN A O   1 
ATOM 853  C CB  . GLN A 1 159 ? -0.93959  31.22981 57.30342  1.000 39.07531  ?  129 GLN A CB  1 
ATOM 854  C CG  . GLN A 1 159 ? -0.65018  30.74825 58.71292  1.000 49.11377  ?  129 GLN A CG  1 
ATOM 855  C CD  . GLN A 1 159 ? 0.04229   29.40144 58.74170  1.000 45.53333  ?  129 GLN A CD  1 
ATOM 856  O OE1 . GLN A 1 159 ? 0.21705   28.80369 59.80304  1.000 44.08915  ?  129 GLN A OE1 1 
ATOM 857  N NE2 . GLN A 1 159 ? 0.44040   28.91582 57.57311  1.000 33.98595  ?  129 GLN A NE2 1 
ATOM 858  N N   . SER A 1 160 ? -0.89164  33.47801 55.12688  1.000 31.23238  ?  130 SER A N   1 
ATOM 859  C CA  . SER A 1 160 ? -0.99190  33.87048 53.72882  1.000 32.77851  ?  130 SER A CA  1 
ATOM 860  C C   . SER A 1 160 ? 0.39820   33.83649 53.11112  1.000 38.28884  ?  130 SER A C   1 
ATOM 861  O O   . SER A 1 160 ? 1.40329   34.00459 53.80650  1.000 33.04561  ?  130 SER A O   1 
ATOM 862  C CB  . SER A 1 160 ? -1.61420  35.26355 53.57917  1.000 33.54325  ?  130 SER A CB  1 
ATOM 863  O OG  . SER A 1 160 ? -0.88163  36.23248 54.30921  1.000 33.18332  ?  130 SER A OG  1 
ATOM 864  N N   . GLY A 1 161 ? 0.44254   33.61394 51.79923  1.000 41.07477  ?  131 GLY A N   1 
ATOM 865  C CA  . GLY A 1 161 ? 1.69191   33.55519 51.07912  1.000 37.22482  ?  131 GLY A CA  1 
ATOM 866  C C   . GLY A 1 161 ? 1.68980   32.49878 49.99369  1.000 48.89892  ?  131 GLY A C   1 
ATOM 867  O O   . GLY A 1 161 ? 0.81056   31.63213 49.93687  1.000 68.90427  ?  131 GLY A O   1 
ATOM 868  N N   . PRO A 1 162 ? 2.68227   32.55261 49.10752  1.000 40.28918  ?  132 PRO A N   1 
ATOM 869  C CA  . PRO A 1 162 ? 2.74236   31.58277 48.01014  1.000 44.97032  ?  132 PRO A CA  1 
ATOM 870  C C   . PRO A 1 162 ? 3.16424   30.20726 48.49930  1.000 57.39748  ?  132 PRO A C   1 
ATOM 871  O O   . PRO A 1 162 ? 3.87060   30.06173 49.50068  1.000 57.45021  ?  132 PRO A O   1 
ATOM 872  C CB  . PRO A 1 162 ? 3.78913   32.18221 47.06551  1.000 42.98229  ?  132 PRO A CB  1 
ATOM 873  C CG  . PRO A 1 162 ? 4.67787   32.97762 47.96940  1.000 59.04778  ?  132 PRO A CG  1 
ATOM 874  C CD  . PRO A 1 162 ? 3.78030   33.53231 49.04470  1.000 54.40862  ?  132 PRO A CD  1 
ATOM 875  N N   . GLY A 1 163 ? 2.71654   29.18821 47.77146  1.000 59.88082  ?  133 GLY A N   1 
ATOM 876  C CA  . GLY A 1 163 ? 3.00184   27.81790 48.14295  1.000 69.83922  ?  133 GLY A CA  1 
ATOM 877  C C   . GLY A 1 163 ? 3.96805   27.11705 47.21020  1.000 64.93010  ?  133 GLY A C   1 
ATOM 878  O O   . GLY A 1 163 ? 4.22448   25.91838 47.36098  1.000 56.58204  ?  133 GLY A O   1 
ATOM 879  N N   . LEU A 1 164 ? 4.51209   27.85178 46.24117  1.000 63.10452  ?  134 LEU A N   1 
ATOM 880  C CA  . LEU A 1 164 ? 5.46873   27.30008 45.28417  1.000 54.67963  ?  134 LEU A CA  1 
ATOM 881  C C   . LEU A 1 164 ? 6.61693   28.28964 45.14670  1.000 52.29671  ?  134 LEU A C   1 
ATOM 882  O O   . LEU A 1 164 ? 6.42341   29.40360 44.65020  1.000 48.34612  ?  134 LEU A O   1 
ATOM 883  C CB  . LEU A 1 164 ? 4.81114   27.02753 43.92959  1.000 50.47676  ?  134 LEU A CB  1 
ATOM 884  C CG  . LEU A 1 164 ? 5.70803   26.41378 42.84959  1.000 60.15296  ?  134 LEU A CG  1 
ATOM 885  C CD1 . LEU A 1 164 ? 6.25466   25.06440 43.29477  1.000 58.69061  ?  134 LEU A CD1 1 
ATOM 886  C CD2 . LEU A 1 164 ? 4.95098   26.28670 41.53780  1.000 52.93571  ?  134 LEU A CD2 1 
ATOM 887  N N   . VAL A 1 165 ? 7.80379   27.89012 45.59559  1.000 53.19190  ?  135 VAL A N   1 
ATOM 888  C CA  . VAL A 1 165 ? 8.99142   28.73541 45.57409  1.000 47.61486  ?  135 VAL A CA  1 
ATOM 889  C C   . VAL A 1 165 ? 10.06844  28.03107 44.76268  1.000 52.42310  ?  135 VAL A C   1 
ATOM 890  O O   . VAL A 1 165 ? 10.32510  26.83892 44.96613  1.000 59.72137  ?  135 VAL A O   1 
ATOM 891  C CB  . VAL A 1 165 ? 9.49567   29.04309 46.99615  1.000 45.64459  ?  135 VAL A CB  1 
ATOM 892  C CG1 . VAL A 1 165 ? 10.68719  29.98113 46.94498  1.000 47.78169  ?  135 VAL A CG1 1 
ATOM 893  C CG2 . VAL A 1 165 ? 8.37541   29.63579 47.83725  1.000 53.27628  ?  135 VAL A CG2 1 
ATOM 894  N N   . LYS A 1 166 ? 10.69091  28.76492 43.84406  1.000 61.00440  ?  136 LYS A N   1 
ATOM 895  C CA  . LYS A 1 166 ? 11.79468  28.21304 43.07892  1.000 61.70342  ?  136 LYS A CA  1 
ATOM 896  C C   . LYS A 1 166 ? 13.03123  28.07017 43.96662  1.000 64.43968  ?  136 LYS A C   1 
ATOM 897  O O   . LYS A 1 166 ? 13.18336  28.79508 44.95389  1.000 72.30879  ?  136 LYS A O   1 
ATOM 898  C CB  . LYS A 1 166 ? 12.11368  29.10206 41.87937  1.000 59.88791  ?  136 LYS A CB  1 
ATOM 899  C CG  . LYS A 1 166 ? 11.05718  29.08304 40.78543  1.000 61.19405  ?  136 LYS A CG  1 
ATOM 900  C CD  . LYS A 1 166 ? 11.51338  29.87334 39.56834  1.000 65.76932  ?  136 LYS A CD  1 
ATOM 901  C CE  . LYS A 1 166 ? 10.49696  29.79434 38.44064  1.000 84.01310  ?  136 LYS A CE  1 
ATOM 902  N NZ  . LYS A 1 166 ? 10.94563  30.54736 37.23607  1.000 79.65659  ?  136 LYS A NZ  1 
ATOM 903  N N   . PRO A 1 167 ? 13.92209  27.13175 43.64567  1.000 69.68901  ?  137 PRO A N   1 
ATOM 904  C CA  . PRO A 1 167 ? 15.14638  26.97777 44.43847  1.000 65.24932  ?  137 PRO A CA  1 
ATOM 905  C C   . PRO A 1 167 ? 16.01569  28.22574 44.37956  1.000 79.33035  ?  137 PRO A C   1 
ATOM 906  O O   . PRO A 1 167 ? 15.95301  29.02077 43.43853  1.000 73.72363  ?  137 PRO A O   1 
ATOM 907  C CB  . PRO A 1 167 ? 15.84672  25.77971 43.78519  1.000 69.72604  ?  137 PRO A CB  1 
ATOM 908  C CG  . PRO A 1 167 ? 14.75300  25.02884 43.10225  1.000 60.79199  ?  137 PRO A CG  1 
ATOM 909  C CD  . PRO A 1 167 ? 13.78548  26.07286 42.63098  1.000 76.12933  ?  137 PRO A CD  1 
ATOM 910  N N   . SER A 1 168 ? 16.83498  28.38915 45.41960  1.000 73.32543  ?  138 SER A N   1 
ATOM 911  C CA  . SER A 1 168 ? 17.74288  29.52521 45.57389  1.000 69.99732  ?  138 SER A CA  1 
ATOM 912  C C   . SER A 1 168 ? 17.00653  30.86123 45.60435  1.000 72.23293  ?  138 SER A C   1 
ATOM 913  O O   . SER A 1 168 ? 17.58887  31.90134 45.28031  1.000 75.22857  ?  138 SER A O   1 
ATOM 914  C CB  . SER A 1 168 ? 18.81404  29.53736 44.47620  1.000 80.72328  ?  138 SER A CB  1 
ATOM 915  O OG  . SER A 1 168 ? 19.60860  28.36483 44.52673  1.000 111.45102 ?  138 SER A OG  1 
ATOM 916  N N   . GLN A 1 169 ? 15.73393  30.85372 45.98901  1.000 63.14575  ?  139 GLN A N   1 
ATOM 917  C CA  . GLN A 1 169 ? 14.93714  32.06218 46.13256  1.000 57.63185  ?  139 GLN A CA  1 
ATOM 918  C C   . GLN A 1 169 ? 14.38464  32.14363 47.55001  1.000 65.42333  ?  139 GLN A C   1 
ATOM 919  O O   . GLN A 1 169 ? 14.51473  31.21274 48.34828  1.000 76.81648  ?  139 GLN A O   1 
ATOM 920  C CB  . GLN A 1 169 ? 13.79837  32.10441 45.10505  1.000 61.68864  ?  139 GLN A CB  1 
ATOM 921  C CG  . GLN A 1 169 ? 14.26399  32.34463 43.67693  1.000 75.41846  ?  139 GLN A CG  1 
ATOM 922  C CD  . GLN A 1 169 ? 13.11138  32.54913 42.71313  1.000 93.49016  ?  139 GLN A CD  1 
ATOM 923  O OE1 . GLN A 1 169 ? 11.95584  32.28036 43.04243  1.000 97.28327  ?  139 GLN A OE1 1 
ATOM 924  N NE2 . GLN A 1 169 ? 13.42073  33.03203 41.51502  1.000 78.94060  ?  139 GLN A NE2 1 
ATOM 925  N N   . THR A 1 170 ? 13.75599  33.27526 47.85734  1.000 60.79452  ?  140 THR A N   1 
ATOM 926  C CA  . THR A 1 170 ? 13.30100  33.56271 49.21109  1.000 50.49479  ?  140 THR A CA  1 
ATOM 927  C C   . THR A 1 170 ? 11.85512  33.11880 49.39739  1.000 47.54583  ?  140 THR A C   1 
ATOM 928  O O   . THR A 1 170 ? 10.99543  33.40576 48.55806  1.000 69.98377  ?  140 THR A O   1 
ATOM 929  C CB  . THR A 1 170 ? 13.43566  35.05497 49.51888  1.000 59.86103  ?  140 THR A CB  1 
ATOM 930  O OG1 . THR A 1 170 ? 14.78204  35.47732 49.26783  1.000 58.05765  ?  140 THR A OG1 1 
ATOM 931  C CG2 . THR A 1 170 ? 13.09024  35.33187 50.97539  1.000 48.94708  ?  140 THR A CG2 1 
ATOM 932  N N   . LEU A 1 171 ? 11.59577  32.41987 50.49938  1.000 49.78997  ?  141 LEU A N   1 
ATOM 933  C CA  . LEU A 1 171 ? 10.25134  32.01368 50.88630  1.000 40.42467  ?  141 LEU A CA  1 
ATOM 934  C C   . LEU A 1 171 ? 9.69920   33.00425 51.90221  1.000 44.55284  ?  141 LEU A C   1 
ATOM 935  O O   . LEU A 1 171 ? 10.33083  33.25947 52.93253  1.000 53.08012  ?  141 LEU A O   1 
ATOM 936  C CB  . LEU A 1 171 ? 10.25516  30.60147 51.47409  1.000 37.56237  ?  141 LEU A CB  1 
ATOM 937  C CG  . LEU A 1 171 ? 9.02857   30.19507 52.29593  1.000 36.43315  ?  141 LEU A CG  1 
ATOM 938  C CD1 . LEU A 1 171 ? 7.76452   30.21309 51.44762  1.000 60.20516  ?  141 LEU A CD1 1 
ATOM 939  C CD2 . LEU A 1 171 ? 9.23547   28.82721 52.92814  1.000 37.86260  ?  141 LEU A CD2 1 
ATOM 940  N N   . SER A 1 172 ? 8.52135   33.55356 51.61388  1.000 49.44530  ?  142 SER A N   1 
ATOM 941  C CA  . SER A 1 172 ? 7.89463   34.55221 52.46935  1.000 38.63899  ?  142 SER A CA  1 
ATOM 942  C C   . SER A 1 172 ? 6.48747   34.10231 52.83162  1.000 34.79233  ?  142 SER A C   1 
ATOM 943  O O   . SER A 1 172 ? 5.70880   33.71921 51.95263  1.000 36.17715  ?  142 SER A O   1 
ATOM 944  C CB  . SER A 1 172 ? 7.85556   35.92100 51.78099  1.000 56.79673  ?  142 SER A CB  1 
ATOM 945  O OG  . SER A 1 172 ? 9.16184   36.36191 51.45141  1.000 41.39780  ?  142 SER A OG  1 
ATOM 946  N N   . LEU A 1 173 ? 6.16852   34.14913 54.12491  1.000 33.63805  ?  143 LEU A N   1 
ATOM 947  C CA  . LEU A 1 173 ? 4.85215   33.78873 54.63304  1.000 38.15627  ?  143 LEU A CA  1 
ATOM 948  C C   . LEU A 1 173 ? 4.46714   34.75686 55.74137  1.000 35.87202  ?  143 LEU A C   1 
ATOM 949  O O   . LEU A 1 173 ? 5.29093   35.08508 56.59904  1.000 40.39797  ?  143 LEU A O   1 
ATOM 950  C CB  . LEU A 1 173 ? 4.82659   32.34804 55.16250  1.000 32.34601  ?  143 LEU A CB  1 
ATOM 951  C CG  . LEU A 1 173 ? 5.09799   31.23198 54.15217  1.000 33.80957  ?  143 LEU A CG  1 
ATOM 952  C CD1 . LEU A 1 173 ? 5.28809   29.90202 54.86243  1.000 33.64961  ?  143 LEU A CD1 1 
ATOM 953  C CD2 . LEU A 1 173 ? 3.97148   31.14556 53.13413  1.000 35.53657  ?  143 LEU A CD2 1 
ATOM 954  N N   . THR A 1 174 ? 3.21415   35.20622 55.72318  1.000 38.74495  ?  144 THR A N   1 
ATOM 955  C CA  . THR A 1 174 ? 2.71275   36.19180 56.67136  1.000 42.59718  ?  144 THR A CA  1 
ATOM 956  C C   . THR A 1 174 ? 1.63240   35.56810 57.54542  1.000 37.53684  ?  144 THR A C   1 
ATOM 957  O O   . THR A 1 174 ? 0.82529   34.76217 57.07184  1.000 34.77840  ?  144 THR A O   1 
ATOM 958  C CB  . THR A 1 174 ? 2.15560   37.42309 55.94304  1.000 43.87814  ?  144 THR A CB  1 
ATOM 959  O OG1 . THR A 1 174 ? 3.11466   37.88587 54.98394  1.000 44.48708  ?  144 THR A OG1 1 
ATOM 960  C CG2 . THR A 1 174 ? 1.85998   38.54416 56.92804  1.000 44.09002  ?  144 THR A CG2 1 
ATOM 961  N N   . CYS A 1 175 ? 1.62155   35.94788 58.82202  1.000 41.56620  ?  145 CYS A N   1 
ATOM 962  C CA  . CYS A 1 175 ? 0.69269   35.41228 59.81658  1.000 37.32113  ?  145 CYS A CA  1 
ATOM 963  C C   . CYS A 1 175 ? -0.05544  36.58592 60.44467  1.000 46.63010  ?  145 CYS A C   1 
ATOM 964  O O   . CYS A 1 175 ? 0.50319   37.31762 61.26863  1.000 43.96563  ?  145 CYS A O   1 
ATOM 965  C CB  . CYS A 1 175 ? 1.44330   34.59611 60.86716  1.000 43.78845  ?  145 CYS A CB  1 
ATOM 966  S SG  . CYS A 1 175 ? 0.42568   33.76828 62.11796  1.000 70.93912  ?  145 CYS A SG  1 
ATOM 967  N N   . SER A 1 176 ? -1.31649  36.76641 60.05484  1.000 57.98064  ?  146 SER A N   1 
ATOM 968  C CA  . SER A 1 176 ? -2.13090  37.85384 60.58315  1.000 32.94289  ?  146 SER A CA  1 
ATOM 969  C C   . SER A 1 176 ? -2.70578  37.46921 61.94142  1.000 32.37697  ?  146 SER A C   1 
ATOM 970  O O   . SER A 1 176 ? -3.21554  36.35815 62.11773  1.000 40.10258  ?  146 SER A O   1 
ATOM 971  C CB  . SER A 1 176 ? -3.25670  38.19929 59.60807  1.000 34.94300  ?  146 SER A CB  1 
ATOM 972  O OG  . SER A 1 176 ? -2.73968  38.62063 58.35754  1.000 62.24299  ?  146 SER A OG  1 
ATOM 973  N N   . ILE A 1 177 ? -2.62943  38.39114 62.89832  1.000 36.43383  ?  147 ILE A N   1 
ATOM 974  C CA  . ILE A 1 177 ? -3.07520  38.15426 64.26639  1.000 32.26133  ?  147 ILE A CA  1 
ATOM 975  C C   . ILE A 1 177 ? -4.30169  39.01281 64.53483  1.000 34.14760  ?  147 ILE A C   1 
ATOM 976  O O   . ILE A 1 177 ? -4.29736  40.21826 64.25748  1.000 37.43478  ?  147 ILE A O   1 
ATOM 977  C CB  . ILE A 1 177 ? -1.96462  38.46167 65.28511  1.000 31.29609  ?  147 ILE A CB  1 
ATOM 978  C CG1 . ILE A 1 177 ? -0.65652  37.78549 64.87767  1.000 33.66720  ?  147 ILE A CG1 1 
ATOM 979  C CG2 . ILE A 1 177 ? -2.38350  38.01342 66.67832  1.000 31.09218  ?  147 ILE A CG2 1 
ATOM 980  C CD1 . ILE A 1 177 ? 0.50040   38.11409 65.79102  1.000 33.65035  ?  147 ILE A CD1 1 
ATOM 981  N N   . SER A 1 178 ? -5.34755  38.39273 65.07635  1.000 42.87673  ?  148 SER A N   1 
ATOM 982  C CA  . SER A 1 178 ? -6.55091  39.10158 65.48903  1.000 36.54845  ?  148 SER A CA  1 
ATOM 983  C C   . SER A 1 178 ? -7.03406  38.50596 66.80077  1.000 36.38486  ?  148 SER A C   1 
ATOM 984  O O   . SER A 1 178 ? -7.15854  37.28400 66.92033  1.000 48.16171  ?  148 SER A O   1 
ATOM 985  C CB  . SER A 1 178 ? -7.64896  39.01437 64.42269  1.000 38.15481  ?  148 SER A CB  1 
ATOM 986  O OG  . SER A 1 178 ? -8.03125  37.67125 64.18857  1.000 37.57865  ?  148 SER A OG  1 
ATOM 987  N N   . GLY A 1 179 ? -7.30167  39.37007 67.78226  1.000 37.53193  ?  149 GLY A N   1 
ATOM 988  C CA  . GLY A 1 179 ? -7.68116  38.96513 69.11877  1.000 37.69657  ?  149 GLY A CA  1 
ATOM 989  C C   . GLY A 1 179 ? -6.60081  39.21036 70.15358  1.000 36.80036  ?  149 GLY A C   1 
ATOM 990  O O   . GLY A 1 179 ? -6.91567  39.37978 71.33822  1.000 45.81439  ?  149 GLY A O   1 
ATOM 991  N N   . ASP A 1 180 ? -5.33811  39.22813 69.73211  1.000 36.33859  ?  150 ASP A N   1 
ATOM 992  C CA  . ASP A 1 180 ? -4.22348  39.54843 70.60981  1.000 37.27901  ?  150 ASP A CA  1 
ATOM 993  C C   . ASP A 1 180 ? -3.27684  40.48192 69.86841  1.000 37.05684  ?  150 ASP A C   1 
ATOM 994  O O   . ASP A 1 180 ? -3.26597  40.53722 68.63616  1.000 34.49224  ?  150 ASP A O   1 
ATOM 995  C CB  . ASP A 1 180 ? -3.48518  38.28424 71.07685  1.000 32.92495  ?  150 ASP A CB  1 
ATOM 996  C CG  . ASP A 1 180 ? -2.56835  38.54452 72.25960  1.000 49.60941  ?  150 ASP A CG  1 
ATOM 997  O OD1 . ASP A 1 180 ? -2.57866  39.67792 72.78554  1.000 48.93233  ?  150 ASP A OD1 1 
ATOM 998  O OD2 . ASP A 1 180 ? -1.83759  37.61495 72.66393  1.000 31.70906  -1 150 ASP A OD2 1 
ATOM 999  N N   . SER A 1 181 ? -2.48448  41.22541 70.63511  1.000 35.16555  ?  151 SER A N   1 
ATOM 1000 C CA  . SER A 1 181 ? -1.54159  42.18074 70.07139  1.000 35.56357  ?  151 SER A CA  1 
ATOM 1001 C C   . SER A 1 181 ? -0.21778  41.49777 69.75365  1.000 39.14391  ?  151 SER A C   1 
ATOM 1002 O O   . SER A 1 181 ? 0.28410   40.69154 70.54198  1.000 35.36669  ?  151 SER A O   1 
ATOM 1003 C CB  . SER A 1 181 ? -1.31120  43.34334 71.03815  1.000 37.54684  ?  151 SER A CB  1 
ATOM 1004 O OG  . SER A 1 181 ? -0.40633  44.28737 70.49337  1.000 48.04968  ?  151 SER A OG  1 
ATOM 1005 N N   . VAL A 1 182 ? 0.34610   41.82866 68.58854  1.000 34.64058  ?  152 VAL A N   1 
ATOM 1006 C CA  . VAL A 1 182 ? 1.63132   41.25428 68.20161  1.000 31.87254  ?  152 VAL A CA  1 
ATOM 1007 C C   . VAL A 1 182 ? 2.73738   41.73957 69.13122  1.000 43.36905  ?  152 VAL A C   1 
ATOM 1008 O O   . VAL A 1 182 ? 3.74317   41.04574 69.32905  1.000 39.24073  ?  152 VAL A O   1 
ATOM 1009 C CB  . VAL A 1 182 ? 1.93927   41.57715 66.72545  1.000 32.02922  ?  152 VAL A CB  1 
ATOM 1010 C CG1 . VAL A 1 182 ? 2.14273   43.07257 66.52830  1.000 36.90385  ?  152 VAL A CG1 1 
ATOM 1011 C CG2 . VAL A 1 182 ? 3.15417   40.79528 66.24126  1.000 30.52994  ?  152 VAL A CG2 1 
ATOM 1012 N N   . SER A 1 183 ? 2.57032   42.92125 69.72717  1.000 35.23519  ?  153 SER A N   1 
ATOM 1013 C CA  . SER A 1 183 ? 3.52196   43.46613 70.68652  1.000 45.24432  ?  153 SER A CA  1 
ATOM 1014 C C   . SER A 1 183 ? 3.10659   43.18962 72.12771  1.000 45.42962  ?  153 SER A C   1 
ATOM 1015 O O   . SER A 1 183 ? 3.40756   43.98467 73.02501  1.000 37.21807  ?  153 SER A O   1 
ATOM 1016 C CB  . SER A 1 183 ? 3.69985   44.96739 70.46041  1.000 37.52179  ?  153 SER A CB  1 
ATOM 1017 O OG  . SER A 1 183 ? 2.46154   45.64889 70.55793  1.000 52.87264  ?  153 SER A OG  1 
ATOM 1018 N N   . SER A 1 184 ? 2.41679   42.07580 72.36389  1.000 44.81115  ?  154 SER A N   1 
ATOM 1019 C CA  . SER A 1 184 ? 1.98008   41.73123 73.70940  1.000 35.90684  ?  154 SER A CA  1 
ATOM 1020 C C   . SER A 1 184 ? 3.17735   41.42715 74.60013  1.000 46.89868  ?  154 SER A C   1 
ATOM 1021 O O   . SER A 1 184 ? 4.16460   40.82956 74.16225  1.000 49.06621  ?  154 SER A O   1 
ATOM 1022 C CB  . SER A 1 184 ? 1.03652   40.52977 73.67141  1.000 33.48281  ?  154 SER A CB  1 
ATOM 1023 O OG  . SER A 1 184 ? 0.69220   40.10893 74.97979  1.000 35.79796  ?  154 SER A OG  1 
ATOM 1024 N N   . ASN A 1 185 ? 3.08356   41.84550 75.86314  1.000 52.48574  ?  155 ASN A N   1 
ATOM 1025 C CA  . ASN A 1 185 ? 4.17996   41.63211 76.79922  1.000 47.79534  ?  155 ASN A CA  1 
ATOM 1026 C C   . ASN A 1 185 ? 4.26051   40.18574 77.26824  1.000 53.03102  ?  155 ASN A C   1 
ATOM 1027 O O   . ASN A 1 185 ? 5.35220   39.70498 77.58991  1.000 66.38106  ?  155 ASN A O   1 
ATOM 1028 C CB  . ASN A 1 185 ? 4.03360   42.56540 78.00174  1.000 49.70013  ?  155 ASN A CB  1 
ATOM 1029 C CG  . ASN A 1 185 ? 5.21300   42.48243 78.94955  1.000 61.82986  ?  155 ASN A CG  1 
ATOM 1030 O OD1 . ASN A 1 185 ? 5.23079   41.66158 79.86667  1.000 70.97456  ?  155 ASN A OD1 1 
ATOM 1031 N ND2 . ASN A 1 185 ? 6.20806   43.33473 78.73176  1.000 65.27782  ?  155 ASN A ND2 1 
ATOM 1032 N N   . SER A 1 186 ? 3.13114   39.48093 77.31458  1.000 51.40146  ?  156 SER A N   1 
ATOM 1033 C CA  . SER A 1 186 ? 3.12228   38.09350 77.76065  1.000 48.94404  ?  156 SER A CA  1 
ATOM 1034 C C   . SER A 1 186 ? 2.76931   37.15605 76.61330  1.000 45.10168  ?  156 SER A C   1 
ATOM 1035 O O   . SER A 1 186 ? 1.85061   36.33899 76.73265  1.000 56.62073  ?  156 SER A O   1 
ATOM 1036 C CB  . SER A 1 186 ? 2.13964   37.90967 78.91937  1.000 53.41292  ?  156 SER A CB  1 
ATOM 1037 O OG  . SER A 1 186 ? 0.82422   38.26875 78.53396  1.000 35.50570  ?  156 SER A OG  1 
ATOM 1038 N N   . ALA A 1 187 ? 3.49285   37.26343 75.50117  1.000 49.95433  ?  157 ALA A N   1 
ATOM 1039 C CA  . ALA A 1 187 ? 3.23355   36.41821 74.34460  1.000 40.39459  ?  157 ALA A CA  1 
ATOM 1040 C C   . ALA A 1 187 ? 4.50335   36.29618 73.51546  1.000 40.30177  ?  157 ALA A C   1 
ATOM 1041 O O   . ALA A 1 187 ? 5.42856   37.10381 73.63489  1.000 45.13068  ?  157 ALA A O   1 
ATOM 1042 C CB  . ALA A 1 187 ? 2.08477   36.96751 73.49176  1.000 29.52621  ?  157 ALA A CB  1 
ATOM 1043 N N   . ALA A 1 188 ? 4.53080   35.26520 72.67340  1.000 38.13037  ?  158 ALA A N   1 
ATOM 1044 C CA  . ALA A 1 188 ? 5.63106   35.02957 71.75043  1.000 26.77647  ?  158 ALA A CA  1 
ATOM 1045 C C   . ALA A 1 188 ? 5.06002   34.44171 70.46941  1.000 39.50427  ?  158 ALA A C   1 
ATOM 1046 O O   . ALA A 1 188 ? 4.13131   33.63044 70.51434  1.000 48.53345  ?  158 ALA A O   1 
ATOM 1047 C CB  . ALA A 1 188 ? 6.68387   34.09055 72.35006  1.000 32.95804  ?  158 ALA A CB  1 
ATOM 1048 N N   . TRP A 1 189 ? 5.61790   34.85210 69.33235  1.000 28.18891  ?  159 TRP A N   1 
ATOM 1049 C CA  . TRP A 1 189 ? 5.09470   34.48593 68.01897  1.000 36.29118  ?  159 TRP A CA  1 
ATOM 1050 C C   . TRP A 1 189 ? 6.13606   33.64708 67.29038  1.000 30.96893  ?  159 TRP A C   1 
ATOM 1051 O O   . TRP A 1 189 ? 7.17362   34.16695 66.86666  1.000 25.31711  ?  159 TRP A O   1 
ATOM 1052 C CB  . TRP A 1 189 ? 4.72282   35.73603 67.22579  1.000 37.53562  ?  159 TRP A CB  1 
ATOM 1053 C CG  . TRP A 1 189 ? 3.86081   36.66480 68.01956  1.000 34.08050  ?  159 TRP A CG  1 
ATOM 1054 C CD1 . TRP A 1 189 ? 4.24476   37.82622 68.62281  1.000 33.36588  ?  159 TRP A CD1 1 
ATOM 1055 C CD2 . TRP A 1 189 ? 2.47233   36.49251 68.32688  1.000 32.54705  ?  159 TRP A CD2 1 
ATOM 1056 N NE1 . TRP A 1 189 ? 3.17781   38.39589 69.27432  1.000 38.23798  ?  159 TRP A NE1 1 
ATOM 1057 C CE2 . TRP A 1 189 ? 2.07783   37.59591 69.10824  1.000 37.05429  ?  159 TRP A CE2 1 
ATOM 1058 C CE3 . TRP A 1 189 ? 1.52294   35.51555 68.01115  1.000 37.57185  ?  159 TRP A CE3 1 
ATOM 1059 C CZ2 . TRP A 1 189 ? 0.77503   37.75011 69.57788  1.000 42.57888  ?  159 TRP A CZ2 1 
ATOM 1060 C CZ3 . TRP A 1 189 ? 0.23009   35.67142 68.47700  1.000 38.92019  ?  159 TRP A CZ3 1 
ATOM 1061 C CH2 . TRP A 1 189 ? -0.13163  36.77925 69.25271  1.000 40.30973  ?  159 TRP A CH2 1 
ATOM 1062 N N   . ASN A 1 190 ? 5.84814   32.35871 67.13299  1.000 36.57031  ?  160 ASN A N   1 
ATOM 1063 C CA  . ASN A 1 190 ? 6.79689   31.37581 66.63220  1.000 33.59479  ?  160 ASN A CA  1 
ATOM 1064 C C   . ASN A 1 190 ? 6.44092   30.95341 65.21148  1.000 33.99639  ?  160 ASN A C   1 
ATOM 1065 O O   . ASN A 1 190 ? 5.35920   31.24657 64.69553  1.000 35.94323  ?  160 ASN A O   1 
ATOM 1066 C CB  . ASN A 1 190 ? 6.83331   30.14605 67.54892  1.000 34.87681  ?  160 ASN A CB  1 
ATOM 1067 C CG  . ASN A 1 190 ? 6.99280   30.50945 69.01406  1.000 33.41793  ?  160 ASN A CG  1 
ATOM 1068 O OD1 . ASN A 1 190 ? 8.08100   30.40140 69.57755  1.000 34.32092  ?  160 ASN A OD1 1 
ATOM 1069 N ND2 . ASN A 1 190 ? 5.90237   30.93506 69.64063  1.000 32.11414  ?  160 ASN A ND2 1 
ATOM 1070 N N   . TRP A 1 191 ? 7.38004   30.24748 64.58288  1.000 30.27771  ?  161 TRP A N   1 
ATOM 1071 C CA  . TRP A 1 191 ? 7.18527   29.64816 63.26890  1.000 26.83208  ?  161 TRP A CA  1 
ATOM 1072 C C   . TRP A 1 191 ? 7.67129   28.20814 63.31079  1.000 27.79293  ?  161 TRP A C   1 
ATOM 1073 O O   . TRP A 1 191 ? 8.80768   27.94614 63.71683  1.000 33.52106  ?  161 TRP A O   1 
ATOM 1074 C CB  . TRP A 1 191 ? 7.92700   30.42680 62.17728  1.000 26.93563  ?  161 TRP A CB  1 
ATOM 1075 C CG  . TRP A 1 191 ? 7.13554   31.56219 61.60741  1.000 35.45621  ?  161 TRP A CG  1 
ATOM 1076 C CD1 . TRP A 1 191 ? 7.24975   32.88381 61.92540  1.000 34.47584  ?  161 TRP A CD1 1 
ATOM 1077 C CD2 . TRP A 1 191 ? 6.10188   31.47513 60.61854  1.000 42.25853  ?  161 TRP A CD2 1 
ATOM 1078 N NE1 . TRP A 1 191 ? 6.35401   33.62569 61.19333  1.000 40.79573  ?  161 TRP A NE1 1 
ATOM 1079 C CE2 . TRP A 1 191 ? 5.63586   32.78401 60.38522  1.000 43.26833  ?  161 TRP A CE2 1 
ATOM 1080 C CE3 . TRP A 1 191 ? 5.52603   30.41746 59.90772  1.000 40.01223  ?  161 TRP A CE3 1 
ATOM 1081 C CZ2 . TRP A 1 191 ? 4.62199   33.06370 59.47080  1.000 37.32795  ?  161 TRP A CZ2 1 
ATOM 1082 C CZ3 . TRP A 1 191 ? 4.51913   30.69700 59.00081  1.000 35.80929  ?  161 TRP A CZ3 1 
ATOM 1083 C CH2 . TRP A 1 191 ? 4.07775   32.00902 58.79046  1.000 37.87926  ?  161 TRP A CH2 1 
ATOM 1084 N N   . ILE A 1 192 ? 6.80996   27.27947 62.89931  1.000 28.70924  ?  162 ILE A N   1 
ATOM 1085 C CA  . ILE A 1 192 ? 7.10320   25.85179 62.93487  1.000 31.41444  ?  162 ILE A CA  1 
ATOM 1086 C C   . ILE A 1 192 ? 6.75659   25.24726 61.58184  1.000 37.98645  ?  162 ILE A C   1 
ATOM 1087 O O   . ILE A 1 192 ? 5.74011   25.60376 60.97579  1.000 31.54271  ?  162 ILE A O   1 
ATOM 1088 C CB  . ILE A 1 192 ? 6.32177   25.13600 64.05833  1.000 30.56213  ?  162 ILE A CB  1 
ATOM 1089 C CG1 . ILE A 1 192 ? 6.44806   25.89853 65.37831  1.000 29.31625  ?  162 ILE A CG1 1 
ATOM 1090 C CG2 . ILE A 1 192 ? 6.81500   23.70633 64.22695  1.000 32.42043  ?  162 ILE A CG2 1 
ATOM 1091 C CD1 . ILE A 1 192 ? 5.62704   25.31091 66.49913  1.000 29.83753  ?  162 ILE A CD1 1 
ATOM 1092 N N   . ARG A 1 193 ? 7.59969   24.33162 61.10910  1.000 33.05497  ?  163 ARG A N   1 
ATOM 1093 C CA  . ARG A 1 193 ? 7.33823   23.58691 59.88760  1.000 37.42667  ?  163 ARG A CA  1 
ATOM 1094 C C   . ARG A 1 193 ? 7.25486   22.09784 60.19828  1.000 45.90570  ?  163 ARG A C   1 
ATOM 1095 O O   . ARG A 1 193 ? 7.81100   21.61465 61.18841  1.000 42.18167  ?  163 ARG A O   1 
ATOM 1096 C CB  . ARG A 1 193 ? 8.41367   23.84556 58.82297  1.000 35.49414  ?  163 ARG A CB  1 
ATOM 1097 C CG  . ARG A 1 193 ? 9.81281   23.39018 59.19698  1.000 38.56100  ?  163 ARG A CG  1 
ATOM 1098 C CD  . ARG A 1 193 ? 10.77519  23.62702 58.04175  1.000 44.06269  ?  163 ARG A CD  1 
ATOM 1099 N NE  . ARG A 1 193 ? 12.14439  23.23824 58.36632  1.000 55.46010  ?  163 ARG A NE  1 
ATOM 1100 C CZ  . ARG A 1 193 ? 13.16817  23.34294 57.52485  1.000 55.68964  ?  163 ARG A CZ  1 
ATOM 1101 N NH1 . ARG A 1 193 ? 12.97859  23.82469 56.30377  1.000 39.32535  ?  163 ARG A NH1 1 
ATOM 1102 N NH2 . ARG A 1 193 ? 14.38225  22.96593 57.90291  1.000 66.82695  ?  163 ARG A NH2 1 
ATOM 1103 N N   . GLN A 1 194 ? 6.54550   21.37087 59.33651  1.000 49.79901  ?  164 GLN A N   1 
ATOM 1104 C CA  . GLN A 1 194 ? 6.30327   19.94556 59.52569  1.000 41.69860  ?  164 GLN A CA  1 
ATOM 1105 C C   . GLN A 1 194 ? 6.57682   19.21248 58.22252  1.000 44.40101  ?  164 GLN A C   1 
ATOM 1106 O O   . GLN A 1 194 ? 5.98450   19.53732 57.18840  1.000 44.75903  ?  164 GLN A O   1 
ATOM 1107 C CB  . GLN A 1 194 ? 4.86822   19.68670 59.99018  1.000 52.21528  ?  164 GLN A CB  1 
ATOM 1108 C CG  . GLN A 1 194 ? 4.56330   18.22400 60.25878  1.000 45.03396  ?  164 GLN A CG  1 
ATOM 1109 C CD  . GLN A 1 194 ? 3.12084   17.99535 60.65807  1.000 45.58801  ?  164 GLN A CD  1 
ATOM 1110 O OE1 . GLN A 1 194 ? 2.82228   17.12251 61.47198  1.000 53.25401  ?  164 GLN A OE1 1 
ATOM 1111 N NE2 . GLN A 1 194 ? 2.21512   18.77778 60.08186  1.000 44.57424  ?  164 GLN A NE2 1 
ATOM 1112 N N   . SER A 1 195 ? 7.46307   18.22438 58.27742  1.000 53.23258  ?  165 SER A N   1 
ATOM 1113 C CA  . SER A 1 195 ? 7.79903   17.37839 57.14455  1.000 49.78676  ?  165 SER A CA  1 
ATOM 1114 C C   . SER A 1 195 ? 8.01843   15.96117 57.64765  1.000 65.14114  ?  165 SER A C   1 
ATOM 1115 O O   . SER A 1 195 ? 8.49878   15.76837 58.77062  1.000 81.39141  ?  165 SER A O   1 
ATOM 1116 C CB  . SER A 1 195 ? 9.06011   17.87137 56.41725  1.000 57.17212  ?  165 SER A CB  1 
ATOM 1117 O OG  . SER A 1 195 ? 10.18719  17.84218 57.27561  1.000 66.59940  ?  165 SER A OG  1 
ATOM 1118 N N   . PRO A 1 196 ? 7.67708   14.95009 56.84340  1.000 82.35829  ?  166 PRO A N   1 
ATOM 1119 C CA  . PRO A 1 196 ? 7.85390   13.55980 57.29637  1.000 61.21482  ?  166 PRO A CA  1 
ATOM 1120 C C   . PRO A 1 196 ? 9.30563   13.16276 57.51699  1.000 61.44558  ?  166 PRO A C   1 
ATOM 1121 O O   . PRO A 1 196 ? 9.55284   12.13325 58.15753  1.000 64.15603  ?  166 PRO A O   1 
ATOM 1122 C CB  . PRO A 1 196 ? 7.21700   12.73751 56.16760  1.000 69.32718  ?  166 PRO A CB  1 
ATOM 1123 C CG  . PRO A 1 196 ? 7.27838   13.62811 54.97023  1.000 62.68244  ?  166 PRO A CG  1 
ATOM 1124 C CD  . PRO A 1 196 ? 7.09424   15.02278 55.49268  1.000 67.94255  ?  166 PRO A CD  1 
ATOM 1125 N N   . SER A 1 197 ? 10.26823  13.94040 57.01842  1.000 67.12897  ?  167 SER A N   1 
ATOM 1126 C CA  . SER A 1 197 ? 11.67306  13.59783 57.20567  1.000 67.46346  ?  167 SER A CA  1 
ATOM 1127 C C   . SER A 1 197 ? 12.21286  14.08037 58.54725  1.000 87.85211  ?  167 SER A C   1 
ATOM 1128 O O   . SER A 1 197 ? 13.08640  13.42560 59.12716  1.000 102.36414 ?  167 SER A O   1 
ATOM 1129 C CB  . SER A 1 197 ? 12.50971  14.17438 56.06188  1.000 72.46689  ?  167 SER A CB  1 
ATOM 1130 O OG  . SER A 1 197 ? 12.26807  15.56095 55.89941  1.000 80.50055  ?  167 SER A OG  1 
ATOM 1131 N N   . ARG A 1 198 ? 11.71518  15.21029 59.05555  1.000 69.38993  ?  168 ARG A N   1 
ATOM 1132 C CA  . ARG A 1 198 ? 12.16167  15.74465 60.33404  1.000 68.88820  ?  168 ARG A CA  1 
ATOM 1133 C C   . ARG A 1 198 ? 11.05471  15.87937 61.36945  1.000 64.97547  ?  168 ARG A C   1 
ATOM 1134 O O   . ARG A 1 198 ? 11.36326  16.06287 62.55260  1.000 77.67622  ?  168 ARG A O   1 
ATOM 1135 C CB  . ARG A 1 198 ? 12.82590  17.12007 60.14841  1.000 92.40796  ?  168 ARG A CB  1 
ATOM 1136 C CG  . ARG A 1 198 ? 14.22696  17.08450 59.55040  1.000 87.83092  ?  168 ARG A CG  1 
ATOM 1137 C CD  . ARG A 1 198 ? 14.18916  17.02862 58.03331  1.000 94.17786  ?  168 ARG A CD  1 
ATOM 1138 N NE  . ARG A 1 198 ? 13.33056  18.06991 57.47695  1.000 80.01520  ?  168 ARG A NE  1 
ATOM 1139 C CZ  . ARG A 1 198 ? 13.73707  19.30297 57.19517  1.000 69.53380  ?  168 ARG A CZ  1 
ATOM 1140 N NH1 . ARG A 1 198 ? 14.99603  19.65517 57.41642  1.000 82.75119  ?  168 ARG A NH1 1 
ATOM 1141 N NH2 . ARG A 1 198 ? 12.88384  20.18474 56.69214  1.000 72.43158  ?  168 ARG A NH2 1 
ATOM 1142 N N   . GLY A 1 199 ? 9.78728   15.79593 60.97137  1.000 65.75048  ?  169 GLY A N   1 
ATOM 1143 C CA  . GLY A 1 199 ? 8.70450   15.98367 61.91823  1.000 49.55945  ?  169 GLY A CA  1 
ATOM 1144 C C   . GLY A 1 199 ? 8.41199   17.45648 62.15554  1.000 51.71219  ?  169 GLY A C   1 
ATOM 1145 O O   . GLY A 1 199 ? 8.63491   18.30936 61.29468  1.000 58.44907  ?  169 GLY A O   1 
ATOM 1146 N N   . LEU A 1 200 ? 7.90194   17.75149 63.34804  1.000 46.62430  ?  170 LEU A N   1 
ATOM 1147 C CA  . LEU A 1 200 ? 7.61937   19.12792 63.74896  1.000 48.43977  ?  170 LEU A CA  1 
ATOM 1148 C C   . LEU A 1 200 ? 8.93638   19.79657 64.12061  1.000 58.22719  ?  170 LEU A C   1 
ATOM 1149 O O   . LEU A 1 200 ? 9.48437   19.56571 65.20118  1.000 43.87122  ?  170 LEU A O   1 
ATOM 1150 C CB  . LEU A 1 200 ? 6.62778   19.15851 64.90623  1.000 45.77144  ?  170 LEU A CB  1 
ATOM 1151 C CG  . LEU A 1 200 ? 5.18299   18.79666 64.55703  1.000 41.25078  ?  170 LEU A CG  1 
ATOM 1152 C CD1 . LEU A 1 200 ? 4.33918   18.66604 65.81267  1.000 45.86615  ?  170 LEU A CD1 1 
ATOM 1153 C CD2 . LEU A 1 200 ? 4.59015   19.83835 63.62432  1.000 39.49193  ?  170 LEU A CD2 1 
ATOM 1154 N N   . GLU A 1 201 ? 9.45159   20.62704 63.21900  1.000 62.63120  ?  171 GLU A N   1 
ATOM 1155 C CA  . GLU A 1 201 ? 10.73210  21.30177 63.39889  1.000 37.49740  ?  171 GLU A CA  1 
ATOM 1156 C C   . GLU A 1 201 ? 10.46383  22.77727 63.66979  1.000 37.07040  ?  171 GLU A C   1 
ATOM 1157 O O   . GLU A 1 201 ? 9.94521   23.48903 62.80288  1.000 37.00523  ?  171 GLU A O   1 
ATOM 1158 C CB  . GLU A 1 201 ? 11.61819  21.11937 62.16820  1.000 42.87629  ?  171 GLU A CB  1 
ATOM 1159 C CG  . GLU A 1 201 ? 13.07770  21.48555 62.38552  1.000 77.20456  ?  171 GLU A CG  1 
ATOM 1160 C CD  . GLU A 1 201 ? 13.88110  21.46933 61.09809  1.000 79.83904  ?  171 GLU A CD  1 
ATOM 1161 O OE1 . GLU A 1 201 ? 14.09515  22.55289 60.51472  1.000 91.64173  ?  171 GLU A OE1 1 
ATOM 1162 O OE2 . GLU A 1 201 ? 14.28946  20.37218 60.66351  1.000 82.50297  -1 171 GLU A OE2 1 
ATOM 1163 N N   . TRP A 1 202 ? 10.81463  23.23133 64.86980  1.000 44.99737  ?  172 TRP A N   1 
ATOM 1164 C CA  . TRP A 1 202 ? 10.65432  24.63215 65.23235  1.000 39.62674  ?  172 TRP A CA  1 
ATOM 1165 C C   . TRP A 1 202 ? 11.73107  25.47524 64.56158  1.000 41.08684  ?  172 TRP A C   1 
ATOM 1166 O O   . TRP A 1 202 ? 12.90734  25.10128 64.53509  1.000 53.62946  ?  172 TRP A O   1 
ATOM 1167 C CB  . TRP A 1 202 ? 10.71830  24.79852 66.75140  1.000 33.52135  ?  172 TRP A CB  1 
ATOM 1168 C CG  . TRP A 1 202 ? 10.63020  26.22019 67.21622  1.000 35.09373  ?  172 TRP A CG  1 
ATOM 1169 C CD1 . TRP A 1 202 ? 9.51070   26.99879 67.26594  1.000 46.49641  ?  172 TRP A CD1 1 
ATOM 1170 C CD2 . TRP A 1 202 ? 11.70361  27.02918 67.71322  1.000 40.41867  ?  172 TRP A CD2 1 
ATOM 1171 N NE1 . TRP A 1 202 ? 9.82148   28.24451 67.75563  1.000 36.56212  ?  172 TRP A NE1 1 
ATOM 1172 C CE2 . TRP A 1 202 ? 11.16146  28.28859 68.03811  1.000 38.77210  ?  172 TRP A CE2 1 
ATOM 1173 C CE3 . TRP A 1 202 ? 13.07077  26.81196 67.91144  1.000 39.11497  ?  172 TRP A CE3 1 
ATOM 1174 C CZ2 . TRP A 1 202 ? 11.93794  29.32575 68.55045  1.000 31.74979  ?  172 TRP A CZ2 1 
ATOM 1175 C CZ3 . TRP A 1 202 ? 13.83972  27.84320 68.41972  1.000 30.74216  ?  172 TRP A CZ3 1 
ATOM 1176 C CH2 . TRP A 1 202 ? 13.27149  29.08387 68.73302  1.000 33.55983  ?  172 TRP A CH2 1 
ATOM 1177 N N   . LEU A 1 203 ? 11.32108  26.62001 64.01447  1.000 29.88174  ?  173 LEU A N   1 
ATOM 1178 C CA  . LEU A 1 203 ? 12.21817  27.48007 63.24890  1.000 37.05326  ?  173 LEU A CA  1 
ATOM 1179 C C   . LEU A 1 203 ? 12.71444  28.66891 64.06554  1.000 36.33831  ?  173 LEU A C   1 
ATOM 1180 O O   . LEU A 1 203 ? 13.91975  28.81201 64.29020  1.000 50.68376  ?  173 LEU A O   1 
ATOM 1181 C CB  . LEU A 1 203 ? 11.51669  27.96048 61.97169  1.000 29.47522  ?  173 LEU A CB  1 
ATOM 1182 C CG  . LEU A 1 203 ? 11.06421  26.85332 61.01806  1.000 31.12950  ?  173 LEU A CG  1 
ATOM 1183 C CD1 . LEU A 1 203 ? 10.41415  27.44047 59.77541  1.000 30.84063  ?  173 LEU A CD1 1 
ATOM 1184 C CD2 . LEU A 1 203 ? 12.23596  25.95705 60.64482  1.000 40.08109  ?  173 LEU A CD2 1 
ATOM 1185 N N   . GLY A 1 204 ? 11.80762  29.52815 64.50909  1.000 27.61373  ?  174 GLY A N   1 
ATOM 1186 C CA  . GLY A 1 204 ? 12.21599  30.69564 65.26061  1.000 38.18663  ?  174 GLY A CA  1 
ATOM 1187 C C   . GLY A 1 204 ? 11.02901  31.37322 65.90482  1.000 33.50031  ?  174 GLY A C   1 
ATOM 1188 O O   . GLY A 1 204 ? 9.90994   30.85798 65.88776  1.000 31.22493  ?  174 GLY A O   1 
ATOM 1189 N N   . ARG A 1 205 ? 11.28973  32.54853 66.47340  1.000 26.14042  ?  175 ARG A N   1 
ATOM 1190 C CA  . ARG A 1 205 ? 10.24432  33.30120 67.15062  1.000 25.85823  ?  175 ARG A CA  1 
ATOM 1191 C C   . ARG A 1 205 ? 10.67437  34.75122 67.30503  1.000 30.29728  ?  175 ARG A C   1 
ATOM 1192 O O   . ARG A 1 205 ? 11.85313  35.09099 67.17322  1.000 37.38315  ?  175 ARG A O   1 
ATOM 1193 C CB  . ARG A 1 205 ? 9.91712   32.70347 68.52206  1.000 25.84741  ?  175 ARG A CB  1 
ATOM 1194 C CG  . ARG A 1 205 ? 11.05697  32.77789 69.52247  1.000 26.48333  ?  175 ARG A CG  1 
ATOM 1195 C CD  . ARG A 1 205 ? 10.60405  32.31422 70.89604  1.000 43.06616  ?  175 ARG A CD  1 
ATOM 1196 N NE  . ARG A 1 205 ? 11.70002  32.28419 71.85971  1.000 27.77001  ?  175 ARG A NE  1 
ATOM 1197 C CZ  . ARG A 1 205 ? 11.55509  31.96925 73.14263  1.000 28.49279  ?  175 ARG A CZ  1 
ATOM 1198 N NH1 . ARG A 1 205 ? 10.35718  31.65957 73.61931  1.000 53.53924  ?  175 ARG A NH1 1 
ATOM 1199 N NH2 . ARG A 1 205 ? 12.60627  31.96565 73.95032  1.000 37.11946  ?  175 ARG A NH2 1 
ATOM 1200 N N   . THR A 1 206 ? 9.68962   35.60047 67.58972  1.000 39.23540  ?  176 THR A N   1 
ATOM 1201 C CA  . THR A 1 206 ? 9.91935   36.99687 67.92307  1.000 42.25242  ?  176 THR A CA  1 
ATOM 1202 C C   . THR A 1 206 ? 8.90239   37.41658 68.97441  1.000 39.85637  ?  176 THR A C   1 
ATOM 1203 O O   . THR A 1 206 ? 7.76266   36.94284 68.98264  1.000 39.92324  ?  176 THR A O   1 
ATOM 1204 C CB  . THR A 1 206 ? 9.82401   37.91021 66.68873  1.000 38.81163  ?  176 THR A CB  1 
ATOM 1205 O OG1 . THR A 1 206 ? 10.09332  39.26482 67.07090  1.000 46.24181  ?  176 THR A OG1 1 
ATOM 1206 C CG2 . THR A 1 206 ? 8.43965   37.83119 66.05889  1.000 39.31129  ?  176 THR A CG2 1 
ATOM 1207 N N   . TYR A 1 207 ? 9.33043   38.29678 69.87484  1.000 31.71101  ?  177 TYR A N   1 
ATOM 1208 C CA  . TYR A 1 207 ? 8.46097   38.75670 70.94788  1.000 37.15501  ?  177 TYR A CA  1 
ATOM 1209 C C   . TYR A 1 207 ? 8.93360   40.12554 71.41153  1.000 32.66151  ?  177 TYR A C   1 
ATOM 1210 O O   . TYR A 1 207 ? 10.05661  40.54662 71.12260  1.000 44.13458  ?  177 TYR A O   1 
ATOM 1211 C CB  . TYR A 1 207 ? 8.42417   37.75931 72.11322  1.000 50.96739  ?  177 TYR A CB  1 
ATOM 1212 C CG  . TYR A 1 207 ? 9.78196   37.36442 72.65248  1.000 37.65112  ?  177 TYR A CG  1 
ATOM 1213 C CD1 . TYR A 1 207 ? 10.51310  36.33758 72.06763  1.000 37.56042  ?  177 TYR A CD1 1 
ATOM 1214 C CD2 . TYR A 1 207 ? 10.32515  38.00760 73.75625  1.000 37.12835  ?  177 TYR A CD2 1 
ATOM 1215 C CE1 . TYR A 1 207 ? 11.75142  35.97134 72.56073  1.000 44.52992  ?  177 TYR A CE1 1 
ATOM 1216 C CE2 . TYR A 1 207 ? 11.56130  37.64765 74.25719  1.000 37.35893  ?  177 TYR A CE2 1 
ATOM 1217 C CZ  . TYR A 1 207 ? 12.27001  36.62951 73.65596  1.000 44.67910  ?  177 TYR A CZ  1 
ATOM 1218 O OH  . TYR A 1 207 ? 13.50187  36.26880 74.15162  1.000 45.89752  ?  177 TYR A OH  1 
ATOM 1219 N N   . TYR A 1 208 ? 8.05505   40.81584 72.13588  1.000 41.24855  ?  178 TYR A N   1 
ATOM 1220 C CA  . TYR A 1 208 ? 8.28476   42.19619 72.54385  1.000 33.64693  ?  178 TYR A CA  1 
ATOM 1221 C C   . TYR A 1 208 ? 8.14030   42.30621 74.05347  1.000 45.65380  ?  178 TYR A C   1 
ATOM 1222 O O   . TYR A 1 208 ? 7.08959   41.96444 74.60583  1.000 59.78616  ?  178 TYR A O   1 
ATOM 1223 C CB  . TYR A 1 208 ? 7.30747   43.14295 71.83922  1.000 37.26005  ?  178 TYR A CB  1 
ATOM 1224 C CG  . TYR A 1 208 ? 7.51615   44.60597 72.16211  1.000 49.95671  ?  178 TYR A CG  1 
ATOM 1225 C CD1 . TYR A 1 208 ? 8.43068   45.37014 71.44924  1.000 46.51161  ?  178 TYR A CD1 1 
ATOM 1226 C CD2 . TYR A 1 208 ? 6.79329   45.22499 73.17451  1.000 39.02724  ?  178 TYR A CD2 1 
ATOM 1227 C CE1 . TYR A 1 208 ? 8.62392   46.70774 71.73851  1.000 47.36242  ?  178 TYR A CE1 1 
ATOM 1228 C CE2 . TYR A 1 208 ? 6.98045   46.56207 73.47134  1.000 41.92221  ?  178 TYR A CE2 1 
ATOM 1229 C CZ  . TYR A 1 208 ? 7.89644   47.29849 72.75001  1.000 43.01804  ?  178 TYR A CZ  1 
ATOM 1230 O OH  . TYR A 1 208 ? 8.08632   48.63027 73.04024  1.000 46.31532  ?  178 TYR A OH  1 
ATOM 1231 N N   . ARG A 1 209 ? 9.19841   42.78194 74.71699  1.000 54.27253  ?  179 ARG A N   1 
ATOM 1232 C CA  . ARG A 1 209 ? 9.13917   43.09428 76.13486  1.000 65.74288  ?  179 ARG A CA  1 
ATOM 1233 C C   . ARG A 1 209 ? 9.30742   44.59617 76.25809  1.000 80.27201  ?  179 ARG A C   1 
ATOM 1234 O O   . ARG A 1 209 ? 8.30358   45.33619 76.23241  1.000 92.79542  ?  179 ARG A O   1 
ATOM 1235 C CB  . ARG A 1 209 ? 10.19451  42.29274 76.90996  1.000 47.44657  ?  179 ARG A CB  1 
ATOM 1236 C CG  . ARG A 1 209 ? 10.19562  40.80763 76.59128  1.000 43.48330  ?  179 ARG A CG  1 
ATOM 1237 C CD  . ARG A 1 209 ? 8.93537   40.12504 77.09721  1.000 45.08599  ?  179 ARG A CD  1 
ATOM 1238 N NE  . ARG A 1 209 ? 8.58342   38.96627 76.28172  1.000 49.00266  ?  179 ARG A NE  1 
ATOM 1239 C CZ  . ARG A 1 209 ? 7.69883   38.04076 76.63692  1.000 35.23880  ?  179 ARG A CZ  1 
ATOM 1240 N NH1 . ARG A 1 209 ? 7.07721   38.12854 77.80442  1.000 38.62052  ?  179 ARG A NH1 1 
ATOM 1241 N NH2 . ARG A 1 209 ? 7.43998   37.02315 75.82749  1.000 41.44896  ?  179 ARG A NH2 1 
ATOM 1242 N N   . SER A 1 210 ? 10.52858  45.10992 76.39567  1.000 61.50725  ?  180 SER A N   1 
ATOM 1243 C CA  . SER A 1 210 ? 10.78039  46.53494 76.22991  1.000 63.08259  ?  180 SER A CA  1 
ATOM 1244 C C   . SER A 1 210 ? 11.11179  46.87089 74.78178  1.000 72.98214  ?  180 SER A C   1 
ATOM 1245 O O   . SER A 1 210 ? 10.65833  47.89576 74.26073  1.000 69.91997  ?  180 SER A O   1 
ATOM 1246 C CB  . SER A 1 210 ? 11.91815  46.98434 77.15034  1.000 120.09047 ?  180 SER A CB  1 
ATOM 1247 O OG  . SER A 1 210 ? 13.11068  46.26959 76.87484  1.000 117.27683 ?  180 SER A OG  1 
ATOM 1248 N N   . LYS A 1 211 ? 11.89749  46.01671 74.12619  1.000 74.38581  ?  181 LYS A N   1 
ATOM 1249 C CA  . LYS A 1 211 ? 12.14932  46.11589 72.69456  1.000 49.19481  ?  181 LYS A CA  1 
ATOM 1250 C C   . LYS A 1 211 ? 11.85882  44.77095 72.04073  1.000 42.13571  ?  181 LYS A C   1 
ATOM 1251 O O   . LYS A 1 211 ? 11.23330  43.90230 72.65720  1.000 49.39420  ?  181 LYS A O   1 
ATOM 1252 C CB  . LYS A 1 211 ? 13.58971  46.55621 72.42213  1.000 56.23268  ?  181 LYS A CB  1 
ATOM 1253 C CG  . LYS A 1 211 ? 14.64867  45.63473 73.00637  1.000 42.27863  ?  181 LYS A CG  1 
ATOM 1254 C CD  . LYS A 1 211 ? 16.04966  46.13176 72.68393  1.000 44.09393  ?  181 LYS A CD  1 
ATOM 1255 C CE  . LYS A 1 211 ? 17.11183  45.20049 73.24754  1.000 67.90282  ?  181 LYS A CE  1 
ATOM 1256 N NZ  . LYS A 1 211 ? 18.48949  45.66686 72.92475  1.000 55.20527  ?  181 LYS A NZ  1 
ATOM 1257 N N   . TRP A 1 212 ? 12.30579  44.58255 70.80356  1.000 37.92561  ?  182 TRP A N   1 
ATOM 1258 C CA  . TRP A 1 212 ? 12.07572  43.34203 70.07727  1.000 35.09213  ?  182 TRP A CA  1 
ATOM 1259 C C   . TRP A 1 212 ? 13.27960  42.41856 70.20833  1.000 41.38922  ?  182 TRP A C   1 
ATOM 1260 O O   . TRP A 1 212 ? 14.42823  42.85354 70.08252  1.000 65.55212  ?  182 TRP A O   1 
ATOM 1261 C CB  . TRP A 1 212 ? 11.78224  43.61847 68.60174  1.000 34.85864  ?  182 TRP A CB  1 
ATOM 1262 C CG  . TRP A 1 212 ? 10.42923  44.21624 68.37321  1.000 41.49069  ?  182 TRP A CG  1 
ATOM 1263 C CD1 . TRP A 1 212 ? 10.13965  45.52977 68.14610  1.000 48.91512  ?  182 TRP A CD1 1 
ATOM 1264 C CD2 . TRP A 1 212 ? 9.17644   43.52109 68.36143  1.000 42.86173  ?  182 TRP A CD2 1 
ATOM 1265 N NE1 . TRP A 1 212 ? 8.78463   45.69510 67.98788  1.000 45.16236  ?  182 TRP A NE1 1 
ATOM 1266 C CE2 . TRP A 1 212 ? 8.17101   44.47669 68.11594  1.000 46.13547  ?  182 TRP A CE2 1 
ATOM 1267 C CE3 . TRP A 1 212 ? 8.80802   42.18296 68.53235  1.000 39.50601  ?  182 TRP A CE3 1 
ATOM 1268 C CZ2 . TRP A 1 212 ? 6.82180   44.13701 68.03673  1.000 56.31218  ?  182 TRP A CZ2 1 
ATOM 1269 C CZ3 . TRP A 1 212 ? 7.46800   41.84789 68.45336  1.000 39.54315  ?  182 TRP A CZ3 1 
ATOM 1270 C CH2 . TRP A 1 212 ? 6.49169   42.82054 68.20768  1.000 32.68023  ?  182 TRP A CH2 1 
ATOM 1271 N N   . TYR A 1 213 ? 13.00696  41.14109 70.46174  1.000 32.73316  ?  183 TYR A N   1 
ATOM 1272 C CA  . TYR A 1 213 ? 14.03768  40.13031 70.63142  1.000 48.00052  ?  183 TYR A CA  1 
ATOM 1273 C C   . TYR A 1 213 ? 13.82177  38.99255 69.64149  1.000 56.08259  ?  183 TYR A C   1 
ATOM 1274 O O   . TYR A 1 213 ? 12.70770  38.75517 69.16622  1.000 29.51833  ?  183 TYR A O   1 
ATOM 1275 C CB  . TYR A 1 213 ? 14.04917  39.58441 72.06507  1.000 40.55060  ?  183 TYR A CB  1 
ATOM 1276 C CG  . TYR A 1 213 ? 14.31861  40.63610 73.11716  1.000 34.46033  ?  183 TYR A CG  1 
ATOM 1277 C CD1 . TYR A 1 213 ? 15.61798  40.99889 73.44663  1.000 36.09536  ?  183 TYR A CD1 1 
ATOM 1278 C CD2 . TYR A 1 213 ? 13.27438  41.26465 73.78185  1.000 35.07142  ?  183 TYR A CD2 1 
ATOM 1279 C CE1 . TYR A 1 213 ? 15.87047  41.95897 74.40787  1.000 38.33500  ?  183 TYR A CE1 1 
ATOM 1280 C CE2 . TYR A 1 213 ? 13.51682  42.22602 74.74512  1.000 60.00464  ?  183 TYR A CE2 1 
ATOM 1281 C CZ  . TYR A 1 213 ? 14.81681  42.56886 75.05395  1.000 53.93272  ?  183 TYR A CZ  1 
ATOM 1282 O OH  . TYR A 1 213 ? 15.06398  43.52554 76.01154  1.000 51.38181  ?  183 TYR A OH  1 
ATOM 1283 N N   . ASN A 1 214 ? 14.90875  38.28624 69.33752  1.000 75.69124  ?  184 ASN A N   1 
ATOM 1284 C CA  . ASN A 1 214 ? 14.89895  37.19235 68.37875  1.000 44.97251  ?  184 ASN A CA  1 
ATOM 1285 C C   . ASN A 1 214 ? 15.42521  35.91554 69.01942  1.000 59.76598  ?  184 ASN A C   1 
ATOM 1286 O O   . ASN A 1 214 ? 16.27277  35.95150 69.91681  1.000 81.74962  ?  184 ASN A O   1 
ATOM 1287 C CB  . ASN A 1 214 ? 15.74537  37.52419 67.14117  1.000 40.87604  ?  184 ASN A CB  1 
ATOM 1288 C CG  . ASN A 1 214 ? 15.00907  38.39584 66.14514  1.000 64.51249  ?  184 ASN A CG  1 
ATOM 1289 O OD1 . ASN A 1 214 ? 13.96287  38.96622 66.45391  1.000 92.08971  ?  184 ASN A OD1 1 
ATOM 1290 N ND2 . ASN A 1 214 ? 15.55433  38.50299 64.93855  1.000 40.46002  ?  184 ASN A ND2 1 
ATOM 1291 N N   . ASP A 1 215 ? 14.90994  34.78446 68.54141  1.000 53.76867  ?  185 ASP A N   1 
ATOM 1292 C CA  . ASP A 1 215 ? 15.40929  33.46774 68.93178  1.000 40.00988  ?  185 ASP A CA  1 
ATOM 1293 C C   . ASP A 1 215 ? 15.22766  32.54352 67.73713  1.000 32.75347  ?  185 ASP A C   1 
ATOM 1294 O O   . ASP A 1 215 ? 14.09366  32.23348 67.36163  1.000 42.03759  ?  185 ASP A O   1 
ATOM 1295 C CB  . ASP A 1 215 ? 14.67888  32.93199 70.16043  1.000 35.78817  ?  185 ASP A CB  1 
ATOM 1296 C CG  . ASP A 1 215 ? 15.27084  33.44112 71.45938  1.000 56.14016  ?  185 ASP A CG  1 
ATOM 1297 O OD1 . ASP A 1 215 ? 16.50924  33.58656 71.53331  1.000 79.81104  ?  185 ASP A OD1 1 
ATOM 1298 O OD2 . ASP A 1 215 ? 14.49861  33.69422 72.40739  1.000 70.20892  -1 185 ASP A OD2 1 
ATOM 1299 N N   . TYR A 1 216 ? 16.33554  32.11193 67.14167  1.000 39.27530  ?  186 TYR A N   1 
ATOM 1300 C CA  . TYR A 1 216 ? 16.31276  31.29051 65.94208  1.000 40.79059  ?  186 TYR A CA  1 
ATOM 1301 C C   . TYR A 1 216 ? 16.98243  29.94889 66.20508  1.000 47.76440  ?  186 TYR A C   1 
ATOM 1302 O O   . TYR A 1 216 ? 17.88551  29.83797 67.03980  1.000 42.44131  ?  186 TYR A O   1 
ATOM 1303 C CB  . TYR A 1 216 ? 17.01394  31.99643 64.77509  1.000 39.05343  ?  186 TYR A CB  1 
ATOM 1304 C CG  . TYR A 1 216 ? 16.29937  33.23516 64.28448  1.000 52.31177  ?  186 TYR A CG  1 
ATOM 1305 C CD1 . TYR A 1 216 ? 14.91341  33.31353 64.30121  1.000 46.94297  ?  186 TYR A CD1 1 
ATOM 1306 C CD2 . TYR A 1 216 ? 17.01160  34.32637 63.80326  1.000 46.89340  ?  186 TYR A CD2 1 
ATOM 1307 C CE1 . TYR A 1 216 ? 14.25633  34.44349 63.85111  1.000 46.14035  ?  186 TYR A CE1 1 
ATOM 1308 C CE2 . TYR A 1 216 ? 16.36344  35.46052 63.35172  1.000 36.81786  ?  186 TYR A CE2 1 
ATOM 1309 C CZ  . TYR A 1 216 ? 14.98603  35.51350 63.37804  1.000 34.95726  ?  186 TYR A CZ  1 
ATOM 1310 O OH  . TYR A 1 216 ? 14.33536  36.63998 62.92981  1.000 38.26395  ?  186 TYR A OH  1 
ATOM 1311 N N   . ALA A 1 217 ? 16.52729  28.92881 65.48236  1.000 54.34482  ?  187 ALA A N   1 
ATOM 1312 C CA  . ALA A 1 217 ? 17.14255  27.61262 65.55472  1.000 42.19002  ?  187 ALA A CA  1 
ATOM 1313 C C   . ALA A 1 217 ? 18.37366  27.56237 64.66040  1.000 53.52988  ?  187 ALA A C   1 
ATOM 1314 O O   . ALA A 1 217 ? 18.34593  28.02365 63.51575  1.000 57.46685  ?  187 ALA A O   1 
ATOM 1315 C CB  . ALA A 1 217 ? 16.14614  26.52992 65.14132  1.000 33.70857  ?  187 ALA A CB  1 
ATOM 1316 N N   . GLY A 1 218 ? 19.45831  26.99208 65.19069  1.000 46.73178  ?  188 GLY A N   1 
ATOM 1317 C CA  . GLY A 1 218 ? 20.71902  26.95502 64.46814  1.000 37.22718  ?  188 GLY A CA  1 
ATOM 1318 C C   . GLY A 1 218 ? 20.66114  26.21691 63.14691  1.000 38.25099  ?  188 GLY A C   1 
ATOM 1319 O O   . GLY A 1 218 ? 21.55284  26.39286 62.30994  1.000 61.75771  ?  188 GLY A O   1 
ATOM 1320 N N   . THR A 1 219 ? 19.63101  25.39433 62.93749  1.000 52.68671  ?  189 THR A N   1 
ATOM 1321 C CA  . THR A 1 219 ? 19.51164  24.65846 61.68304  1.000 43.03103  ?  189 THR A CA  1 
ATOM 1322 C C   . THR A 1 219 ? 19.25315  25.59765 60.51051  1.000 56.72120  ?  189 THR A C   1 
ATOM 1323 O O   . THR A 1 219 ? 19.76391  25.37655 59.40594  1.000 46.64690  ?  189 THR A O   1 
ATOM 1324 C CB  . THR A 1 219 ? 18.39477  23.61965 61.79185  1.000 39.69756  ?  189 THR A CB  1 
ATOM 1325 O OG1 . THR A 1 219 ? 18.61994  22.79298 62.94037  1.000 40.79940  ?  189 THR A OG1 1 
ATOM 1326 C CG2 . THR A 1 219 ? 18.34973  22.74584 60.54590  1.000 54.34757  ?  189 THR A CG2 1 
ATOM 1327 N N   . VAL A 1 220 ? 18.47056  26.65308 60.73054  1.000 51.54344  ?  190 VAL A N   1 
ATOM 1328 C CA  . VAL A 1 220 ? 18.09331  27.56694 59.65823  1.000 49.68565  ?  190 VAL A CA  1 
ATOM 1329 C C   . VAL A 1 220 ? 18.44282  28.99876 60.04158  1.000 42.94106  ?  190 VAL A C   1 
ATOM 1330 O O   . VAL A 1 220 ? 18.00373  29.94974 59.38570  1.000 33.83627  ?  190 VAL A O   1 
ATOM 1331 C CB  . VAL A 1 220 ? 16.59501  27.44018 59.32657  1.000 42.80760  ?  190 VAL A CB  1 
ATOM 1332 C CG1 . VAL A 1 220 ? 16.30003  26.08263 58.70855  1.000 37.20060  ?  190 VAL A CG1 1 
ATOM 1333 C CG2 . VAL A 1 220 ? 15.75692  27.65350 60.57850  1.000 32.94987  ?  190 VAL A CG2 1 
ATOM 1334 N N   . LYS A 1 221 ? 19.24056  29.16195 61.10136  1.000 53.79747  ?  191 LYS A N   1 
ATOM 1335 C CA  . LYS A 1 221 ? 19.59464  30.50135 61.56439  1.000 44.15247  ?  191 LYS A CA  1 
ATOM 1336 C C   . LYS A 1 221 ? 20.33671  31.29355 60.49543  1.000 34.95926  ?  191 LYS A C   1 
ATOM 1337 O O   . LYS A 1 221 ? 20.16206  32.51307 60.39355  1.000 34.43618  ?  191 LYS A O   1 
ATOM 1338 C CB  . LYS A 1 221 ? 20.43900  30.41227 62.83737  1.000 43.34429  ?  191 LYS A CB  1 
ATOM 1339 C CG  . LYS A 1 221 ? 20.87707  31.75961 63.39263  1.000 34.38780  ?  191 LYS A CG  1 
ATOM 1340 C CD  . LYS A 1 221 ? 21.82594  31.59518 64.56864  1.000 35.46205  ?  191 LYS A CD  1 
ATOM 1341 C CE  . LYS A 1 221 ? 22.29722  32.94398 65.09140  1.000 40.79443  ?  191 LYS A CE  1 
ATOM 1342 N NZ  . LYS A 1 221 ? 23.30187  32.80775 66.18367  1.000 37.23079  ?  191 LYS A NZ  1 
ATOM 1343 N N   . SER A 1 222 ? 21.14639  30.62297 59.67719  1.000 47.28840  ?  192 SER A N   1 
ATOM 1344 C CA  . SER A 1 222 ? 21.96491  31.31191 58.68631  1.000 37.98518  ?  192 SER A CA  1 
ATOM 1345 C C   . SER A 1 222 ? 21.15842  31.90018 57.53355  1.000 37.60236  ?  192 SER A C   1 
ATOM 1346 O O   . SER A 1 222 ? 21.76549  32.45180 56.60890  1.000 38.93091  ?  192 SER A O   1 
ATOM 1347 C CB  . SER A 1 222 ? 23.02613  30.35705 58.13401  1.000 40.24906  ?  192 SER A CB  1 
ATOM 1348 O OG  . SER A 1 222 ? 22.43215  29.23894 57.49598  1.000 42.18495  ?  192 SER A OG  1 
ATOM 1349 N N   . ARG A 1 223 ? 19.82812  31.80992 57.54991  1.000 36.49168  ?  193 ARG A N   1 
ATOM 1350 C CA  . ARG A 1 223 ? 19.04825  32.31229 56.42419  1.000 55.12404  ?  193 ARG A CA  1 
ATOM 1351 C C   . ARG A 1 223 ? 17.59718  32.59604 56.79306  1.000 39.83141  ?  193 ARG A C   1 
ATOM 1352 O O   . ARG A 1 223 ? 16.75825  32.79154 55.90715  1.000 34.46194  ?  193 ARG A O   1 
ATOM 1353 C CB  . ARG A 1 223 ? 19.10266  31.31851 55.26027  1.000 54.53803  ?  193 ARG A CB  1 
ATOM 1354 C CG  . ARG A 1 223 ? 18.72498  29.89399 55.63297  1.000 45.49004  ?  193 ARG A CG  1 
ATOM 1355 C CD  . ARG A 1 223 ? 19.03624  28.92866 54.49993  1.000 39.86221  ?  193 ARG A CD  1 
ATOM 1356 N NE  . ARG A 1 223 ? 18.82095  27.53869 54.89064  1.000 54.65435  ?  193 ARG A NE  1 
ATOM 1357 C CZ  . ARG A 1 223 ? 17.69897  26.86370 54.66459  1.000 50.06187  ?  193 ARG A CZ  1 
ATOM 1358 N NH1 . ARG A 1 223 ? 16.68434  27.44984 54.04503  1.000 48.61854  ?  193 ARG A NH1 1 
ATOM 1359 N NH2 . ARG A 1 223 ? 17.59251  25.60078 55.05482  1.000 49.63165  ?  193 ARG A NH2 1 
ATOM 1360 N N   . ILE A 1 224 ? 17.28919  32.63010 58.08598  1.000 36.56684  ?  194 ILE A N   1 
ATOM 1361 C CA  . ILE A 1 224 ? 15.93262  32.87122 58.54700  1.000 32.92417  ?  194 ILE A CA  1 
ATOM 1362 C C   . ILE A 1 224 ? 15.81149  34.31845 59.00926  1.000 35.50523  ?  194 ILE A C   1 
ATOM 1363 O O   . ILE A 1 224 ? 16.79060  34.96899 59.38668  1.000 48.88254  ?  194 ILE A O   1 
ATOM 1364 C CB  . ILE A 1 224 ? 15.51637  31.89159 59.67336  1.000 40.54583  ?  194 ILE A CB  1 
ATOM 1365 C CG1 . ILE A 1 224 ? 13.99296  31.86056 59.82591  1.000 36.79771  ?  194 ILE A CG1 1 
ATOM 1366 C CG2 . ILE A 1 224 ? 16.18770  32.26940 60.98542  1.000 30.40961  ?  194 ILE A CG2 1 
ATOM 1367 C CD1 . ILE A 1 224 ? 13.50673  30.96024 60.93109  1.000 37.61365  ?  194 ILE A CD1 1 
ATOM 1368 N N   . ALA A 1 225 ? 14.58297  34.83508 58.96774  1.000 47.61013  ?  195 ALA A N   1 
ATOM 1369 C CA  . ALA A 1 225 ? 14.28105  36.18060 59.44226  1.000 31.64697  ?  195 ALA A CA  1 
ATOM 1370 C C   . ALA A 1 225 ? 12.79755  36.25140 59.76846  1.000 37.07923  ?  195 ALA A C   1 
ATOM 1371 O O   . ALA A 1 225 ? 11.96601  35.84436 58.95185  1.000 40.70572  ?  195 ALA A O   1 
ATOM 1372 C CB  . ALA A 1 225 ? 14.65143  37.24082 58.39804  1.000 50.40189  ?  195 ALA A CB  1 
ATOM 1373 N N   . ILE A 1 226 ? 12.47076  36.75224 60.95839  1.000 32.71502  ?  196 ILE A N   1 
ATOM 1374 C CA  . ILE A 1 226 ? 11.08954  36.87638 61.41907  1.000 41.24958  ?  196 ILE A CA  1 
ATOM 1375 C C   . ILE A 1 226 ? 10.88128  38.31453 61.87592  1.000 41.39013  ?  196 ILE A C   1 
ATOM 1376 O O   . ILE A 1 226 ? 11.39876  38.71769 62.92531  1.000 46.51874  ?  196 ILE A O   1 
ATOM 1377 C CB  . ILE A 1 226 ? 10.76125  35.89085 62.54866  1.000 28.21634  ?  196 ILE A CB  1 
ATOM 1378 C CG1 . ILE A 1 226 ? 11.00291  34.45353 62.08359  1.000 36.14979  ?  196 ILE A CG1 1 
ATOM 1379 C CG2 . ILE A 1 226 ? 9.32339   36.06445 63.00047  1.000 29.50486  ?  196 ILE A CG2 1 
ATOM 1380 C CD1 . ILE A 1 226 ? 10.70155  33.41151 63.13615  1.000 26.42235  ?  196 ILE A CD1 1 
ATOM 1381 N N   . ASN A 1 227 ? 10.11672  39.08344 61.10011  1.000 29.50627  ?  197 ASN A N   1 
ATOM 1382 C CA  . ASN A 1 227 ? 9.92205   40.50309 61.35760  1.000 36.56471  ?  197 ASN A CA  1 
ATOM 1383 C C   . ASN A 1 227 ? 8.47112   40.77870 61.71978  1.000 39.04426  ?  197 ASN A C   1 
ATOM 1384 O O   . ASN A 1 227 ? 7.56813   40.41530 60.95151  1.000 37.87417  ?  197 ASN A O   1 
ATOM 1385 C CB  . ASN A 1 227 ? 10.32866  41.32576 60.13515  1.000 46.09782  ?  197 ASN A CB  1 
ATOM 1386 C CG  . ASN A 1 227 ? 11.77867  41.11163 59.74215  1.000 67.43913  ?  197 ASN A CG  1 
ATOM 1387 O OD1 . ASN A 1 227 ? 12.65645  41.00813 60.59829  1.000 63.70524  ?  197 ASN A OD1 1 
ATOM 1388 N ND2 . ASN A 1 227 ? 12.03606  41.03916 58.44012  1.000 75.18469  ?  197 ASN A ND2 1 
ATOM 1389 N N   . PRO A 1 228 ? 8.19645   41.40303 62.86051  1.000 37.21030  ?  198 PRO A N   1 
ATOM 1390 C CA  . PRO A 1 228 ? 6.81881   41.77193 63.19215  1.000 39.09157  ?  198 PRO A CA  1 
ATOM 1391 C C   . PRO A 1 228 ? 6.42103   43.09904 62.56086  1.000 41.19563  ?  198 PRO A C   1 
ATOM 1392 O O   . PRO A 1 228 ? 7.25520   43.94281 62.22804  1.000 46.47509  ?  198 PRO A O   1 
ATOM 1393 C CB  . PRO A 1 228 ? 6.84785   41.88042 64.71995  1.000 38.51575  ?  198 PRO A CB  1 
ATOM 1394 C CG  . PRO A 1 228 ? 8.23494   42.33962 65.00989  1.000 31.78995  ?  198 PRO A CG  1 
ATOM 1395 C CD  . PRO A 1 228 ? 9.12248   41.68427 63.97253  1.000 53.19769  ?  198 PRO A CD  1 
ATOM 1396 N N   . ASP A 1 229 ? 5.10994   43.26876 62.40097  1.000 38.78194  ?  199 ASP A N   1 
ATOM 1397 C CA  . ASP A 1 229 ? 4.52710   44.49407 61.86192  1.000 36.42401  ?  199 ASP A CA  1 
ATOM 1398 C C   . ASP A 1 229 ? 3.43307   44.94701 62.81876  1.000 42.75853  ?  199 ASP A C   1 
ATOM 1399 O O   . ASP A 1 229 ? 2.38102   44.30675 62.91057  1.000 48.52365  ?  199 ASP A O   1 
ATOM 1400 C CB  . ASP A 1 229 ? 3.97240   44.27109 60.45295  1.000 50.17957  ?  199 ASP A CB  1 
ATOM 1401 C CG  . ASP A 1 229 ? 3.65643   45.57255 59.73000  1.000 48.57296  ?  199 ASP A CG  1 
ATOM 1402 O OD1 . ASP A 1 229 ? 3.18567   46.52961 60.37945  1.000 41.47185  ?  199 ASP A OD1 1 
ATOM 1403 O OD2 . ASP A 1 229 ? 3.88111   45.63724 58.50287  1.000 56.25748  -1 199 ASP A OD2 1 
ATOM 1404 N N   . THR A 1 230 ? 3.67877   46.05019 63.52784  1.000 50.75053  ?  200 THR A N   1 
ATOM 1405 C CA  . THR A 1 230 ? 2.71599   46.52994 64.51262  1.000 40.20615  ?  200 THR A CA  1 
ATOM 1406 C C   . THR A 1 230 ? 1.53758   47.24953 63.86873  1.000 44.61811  ?  200 THR A C   1 
ATOM 1407 O O   . THR A 1 230 ? 0.42587   47.20758 64.40766  1.000 54.40589  ?  200 THR A O   1 
ATOM 1408 C CB  . THR A 1 230 ? 3.40423   47.45635 65.51717  1.000 41.77751  ?  200 THR A CB  1 
ATOM 1409 O OG1 . THR A 1 230 ? 4.10507   48.49036 64.81514  1.000 49.55088  ?  200 THR A OG1 1 
ATOM 1410 C CG2 . THR A 1 230 ? 4.38739   46.67585 66.37617  1.000 39.75642  ?  200 THR A CG2 1 
ATOM 1411 N N   . SER A 1 231 ? 1.75347   47.90918 62.72791  1.000 46.54841  ?  201 SER A N   1 
ATOM 1412 C CA  . SER A 1 231 ? 0.66679   48.64172 62.08446  1.000 46.73464  ?  201 SER A CA  1 
ATOM 1413 C C   . SER A 1 231 ? -0.39164  47.69389 61.53306  1.000 48.82384  ?  201 SER A C   1 
ATOM 1414 O O   . SER A 1 231 ? -1.59167  47.98201 61.61133  1.000 54.62477  ?  201 SER A O   1 
ATOM 1415 C CB  . SER A 1 231 ? 1.21986   49.53622 60.97486  1.000 49.04122  ?  201 SER A CB  1 
ATOM 1416 O OG  . SER A 1 231 ? 1.88540   48.77217 59.98462  1.000 61.26394  ?  201 SER A OG  1 
ATOM 1417 N N   . LYS A 1 232 ? 0.02998   46.56136 60.97414  1.000 51.53113  ?  202 LYS A N   1 
ATOM 1418 C CA  . LYS A 1 232 ? -0.88608  45.56201 60.44264  1.000 42.13273  ?  202 LYS A CA  1 
ATOM 1419 C C   . LYS A 1 232 ? -1.15940  44.42987 61.42288  1.000 42.94708  ?  202 LYS A C   1 
ATOM 1420 O O   . LYS A 1 232 ? -1.95901  43.54104 61.11126  1.000 43.60776  ?  202 LYS A O   1 
ATOM 1421 C CB  . LYS A 1 232 ? -0.33749  44.98531 59.13297  1.000 41.49537  ?  202 LYS A CB  1 
ATOM 1422 C CG  . LYS A 1 232 ? -0.12964  46.01490 58.03530  1.000 44.62207  ?  202 LYS A CG  1 
ATOM 1423 C CD  . LYS A 1 232 ? 0.48785   45.38242 56.79834  1.000 49.14448  ?  202 LYS A CD  1 
ATOM 1424 C CE  . LYS A 1 232 ? 0.76151   46.42089 55.72256  1.000 69.59267  ?  202 LYS A CE  1 
ATOM 1425 N NZ  . LYS A 1 232 ? 1.41266   45.82107 54.52479  1.000 72.32060  ?  202 LYS A NZ  1 
ATOM 1426 N N   . ASN A 1 233 ? -0.51763  44.44453 62.59380  1.000 45.56827  ?  203 ASN A N   1 
ATOM 1427 C CA  . ASN A 1 233 ? -0.66641  43.39400 63.60272  1.000 46.82896  ?  203 ASN A CA  1 
ATOM 1428 C C   . ASN A 1 233 ? -0.31261  42.02534 63.01979  1.000 47.36292  ?  203 ASN A C   1 
ATOM 1429 O O   . ASN A 1 233 ? -1.09019  41.07131 63.08979  1.000 48.07140  ?  203 ASN A O   1 
ATOM 1430 C CB  . ASN A 1 233 ? -2.07797  43.39515 64.19675  1.000 38.04833  ?  203 ASN A CB  1 
ATOM 1431 C CG  . ASN A 1 233 ? -2.11457  42.86003 65.61461  1.000 36.64580  ?  203 ASN A CG  1 
ATOM 1432 O OD1 . ASN A 1 233 ? -1.18335  43.06709 66.39203  1.000 44.15389  ?  203 ASN A OD1 1 
ATOM 1433 N ND2 . ASN A 1 233 ? -3.19301  42.16629 65.95837  1.000 36.54575  ?  203 ASN A ND2 1 
ATOM 1434 N N   . GLN A 1 234 ? 0.88183   41.93706 62.43566  1.000 46.55159  ?  204 GLN A N   1 
ATOM 1435 C CA  . GLN A 1 234 ? 1.33484   40.72826 61.76399  1.000 40.77988  ?  204 GLN A CA  1 
ATOM 1436 C C   . GLN A 1 234 ? 2.77753   40.43458 62.15065  1.000 44.39847  ?  204 GLN A C   1 
ATOM 1437 O O   . GLN A 1 234 ? 3.44127   41.22413 62.82800  1.000 39.13401  ?  204 GLN A O   1 
ATOM 1438 C CB  . GLN A 1 234 ? 1.22867   40.85538 60.23806  1.000 35.77500  ?  204 GLN A CB  1 
ATOM 1439 C CG  . GLN A 1 234 ? -0.17131  41.10222 59.70854  1.000 54.26084  ?  204 GLN A CG  1 
ATOM 1440 C CD  . GLN A 1 234 ? -0.17724  41.40037 58.22178  1.000 61.41657  ?  204 GLN A CD  1 
ATOM 1441 O OE1 . GLN A 1 234 ? 0.87377   41.62086 57.61882  1.000 36.68778  ?  204 GLN A OE1 1 
ATOM 1442 N NE2 . GLN A 1 234 ? -1.36289  41.40824 57.62218  1.000 44.96409  ?  204 GLN A NE2 1 
ATOM 1443 N N   . PHE A 1 235 ? 3.25426   39.27229 61.70793  1.000 40.39362  ?  205 PHE A N   1 
ATOM 1444 C CA  . PHE A 1 235 ? 4.66956   38.92858 61.76778  1.000 38.97275  ?  205 PHE A CA  1 
ATOM 1445 C C   . PHE A 1 235 ? 4.93250   37.89463 60.68379  1.000 37.87509  ?  205 PHE A C   1 
ATOM 1446 O O   . PHE A 1 235 ? 4.19411   36.91126 60.57286  1.000 42.04374  ?  205 PHE A O   1 
ATOM 1447 C CB  . PHE A 1 235 ? 5.07450   38.40309 63.15526  1.000 41.38441  ?  205 PHE A CB  1 
ATOM 1448 C CG  . PHE A 1 235 ? 4.51196   37.04959 63.49188  1.000 42.19737  ?  205 PHE A CG  1 
ATOM 1449 C CD1 . PHE A 1 235 ? 3.18891   36.90756 63.87292  1.000 56.30753  ?  205 PHE A CD1 1 
ATOM 1450 C CD2 . PHE A 1 235 ? 5.31356   35.92105 63.44466  1.000 40.50081  ?  205 PHE A CD2 1 
ATOM 1451 C CE1 . PHE A 1 235 ? 2.67193   35.66453 64.18824  1.000 41.95442  ?  205 PHE A CE1 1 
ATOM 1452 C CE2 . PHE A 1 235 ? 4.80201   34.67590 63.76019  1.000 37.13402  ?  205 PHE A CE2 1 
ATOM 1453 C CZ  . PHE A 1 235 ? 3.47979   34.54801 64.13112  1.000 26.71202  ?  205 PHE A CZ  1 
ATOM 1454 N N   . SER A 1 236 ? 5.96076   38.12888 59.87579  1.000 39.72974  ?  206 SER A N   1 
ATOM 1455 C CA  . SER A 1 236 ? 6.21122   37.32906 58.68769  1.000 41.76709  ?  206 SER A CA  1 
ATOM 1456 C C   . SER A 1 236 ? 7.48276   36.50305 58.83916  1.000 42.90263  ?  206 SER A C   1 
ATOM 1457 O O   . SER A 1 236 ? 8.33880   36.77871 59.68385  1.000 33.77728  ?  206 SER A O   1 
ATOM 1458 C CB  . SER A 1 236 ? 6.30888   38.21955 57.44320  1.000 33.75873  ?  206 SER A CB  1 
ATOM 1459 O OG  . SER A 1 236 ? 7.28674   39.23068 57.61373  1.000 82.57310  ?  206 SER A OG  1 
ATOM 1460 N N   . LEU A 1 237 ? 7.58907   35.47642 57.99787  1.000 48.09532  ?  207 LEU A N   1 
ATOM 1461 C CA  . LEU A 1 237 ? 8.72875   34.57130 57.96848  1.000 35.23550  ?  207 LEU A CA  1 
ATOM 1462 C C   . LEU A 1 237 ? 9.45022   34.70579 56.63533  1.000 42.51072  ?  207 LEU A C   1 
ATOM 1463 O O   . LEU A 1 237 ? 8.81271   34.82161 55.58407  1.000 40.67789  ?  207 LEU A O   1 
ATOM 1464 C CB  . LEU A 1 237 ? 8.28339   33.11829 58.17788  1.000 29.45703  ?  207 LEU A CB  1 
ATOM 1465 C CG  . LEU A 1 237 ? 9.33401   32.01942 57.99895  1.000 32.46909  ?  207 LEU A CG  1 
ATOM 1466 C CD1 . LEU A 1 237 ? 10.43435  32.15065 59.03834  1.000 45.45142  ?  207 LEU A CD1 1 
ATOM 1467 C CD2 . LEU A 1 237 ? 8.69146   30.64255 58.06291  1.000 29.62202  ?  207 LEU A CD2 1 
ATOM 1468 N N   . HIS A 1 238 ? 10.78085  34.68855 56.68106  1.000 49.51001  ?  208 HIS A N   1 
ATOM 1469 C CA  . HIS A 1 238 ? 11.60523  34.80063 55.48533  1.000 45.75178  ?  208 HIS A CA  1 
ATOM 1470 C C   . HIS A 1 238 ? 12.70682  33.75302 55.52799  1.000 49.03397  ?  208 HIS A C   1 
ATOM 1471 O O   . HIS A 1 238 ? 13.45946  33.67749 56.50435  1.000 66.30539  ?  208 HIS A O   1 
ATOM 1472 C CB  . HIS A 1 238 ? 12.20896  36.20258 55.35783  1.000 45.57677  ?  208 HIS A CB  1 
ATOM 1473 C CG  . HIS A 1 238 ? 11.18847  37.28679 55.20270  1.000 50.40658  ?  208 HIS A CG  1 
ATOM 1474 N ND1 . HIS A 1 238 ? 10.63208  37.61634 53.98550  1.000 44.84975  ?  208 HIS A ND1 1 
ATOM 1475 C CD2 . HIS A 1 238 ? 10.62406  38.11708 56.11137  1.000 42.50431  ?  208 HIS A CD2 1 
ATOM 1476 C CE1 . HIS A 1 238 ? 9.76915   38.60283 54.15087  1.000 40.71652  ?  208 HIS A CE1 1 
ATOM 1477 N NE2 . HIS A 1 238 ? 9.74560   38.92535 55.43158  1.000 41.40846  ?  208 HIS A NE2 1 
ATOM 1478 N N   . LEU A 1 239 ? 12.79667  32.94973 54.46955  1.000 35.65110  ?  209 LEU A N   1 
ATOM 1479 C CA  . LEU A 1 239 ? 13.81999  31.91810 54.32862  1.000 37.11465  ?  209 LEU A CA  1 
ATOM 1480 C C   . LEU A 1 239 ? 14.64318  32.25354 53.09132  1.000 53.16732  ?  209 LEU A C   1 
ATOM 1481 O O   . LEU A 1 239 ? 14.15534  32.12121 51.96378  1.000 52.84795  ?  209 LEU A O   1 
ATOM 1482 C CB  . LEU A 1 239 ? 13.18611  30.53210 54.22029  1.000 42.51702  ?  209 LEU A CB  1 
ATOM 1483 C CG  . LEU A 1 239 ? 14.00221  29.35072 54.74475  1.000 46.04919  ?  209 LEU A CG  1 
ATOM 1484 C CD1 . LEU A 1 239 ? 14.32593  29.53868 56.21868  1.000 37.02485  ?  209 LEU A CD1 1 
ATOM 1485 C CD2 . LEU A 1 239 ? 13.25218  28.04759 54.52254  1.000 39.83016  ?  209 LEU A CD2 1 
ATOM 1486 N N   . ASN A 1 240 ? 15.88899  32.68204 53.30404  1.000 79.87412  ?  210 ASN A N   1 
ATOM 1487 C CA  . ASN A 1 240 ? 16.70614  33.26861 52.24590  1.000 87.80912  ?  210 ASN A CA  1 
ATOM 1488 C C   . ASN A 1 240 ? 16.95810  32.30276 51.09398  1.000 84.48703  ?  210 ASN A C   1 
ATOM 1489 O O   . ASN A 1 240 ? 16.37044  32.44918 50.01804  1.000 97.81670  ?  210 ASN A O   1 
ATOM 1490 C CB  . ASN A 1 240 ? 18.03950  33.75693 52.81593  1.000 88.49502  ?  210 ASN A CB  1 
ATOM 1491 C CG  . ASN A 1 240 ? 18.83127  34.57987 51.81908  1.000 133.43322 ?  210 ASN A CG  1 
ATOM 1492 O OD1 . ASN A 1 240 ? 18.27051  35.14613 50.88060  1.000 157.14046 ?  210 ASN A OD1 1 
ATOM 1493 N ND2 . ASN A 1 240 ? 20.14222  34.65144 52.01832  1.000 141.11489 ?  210 ASN A ND2 1 
ATOM 1494 N N   . SER A 1 241 ? 17.83740  31.32632 51.29826  1.000 67.88530  ?  211 SER A N   1 
ATOM 1495 C CA  . SER A 1 241 ? 18.18821  30.35646 50.26615  1.000 70.05408  ?  211 SER A CA  1 
ATOM 1496 C C   . SER A 1 241 ? 17.46731  29.04786 50.56737  1.000 70.41106  ?  211 SER A C   1 
ATOM 1497 O O   . SER A 1 241 ? 17.78575  28.36876 51.54849  1.000 78.80346  ?  211 SER A O   1 
ATOM 1498 C CB  . SER A 1 241 ? 19.69982  30.15065 50.20375  1.000 89.29766  ?  211 SER A CB  1 
ATOM 1499 O OG  . SER A 1 241 ? 20.04329  29.22755 49.18528  1.000 112.95215 ?  211 SER A OG  1 
ATOM 1500 N N   . VAL A 1 242 ? 16.50050  28.69335 49.72438  1.000 70.51447  ?  212 VAL A N   1 
ATOM 1501 C CA  . VAL A 1 242 ? 15.69846  27.49342 49.92718  1.000 77.27492  ?  212 VAL A CA  1 
ATOM 1502 C C   . VAL A 1 242 ? 16.24362  26.36966 49.05933  1.000 72.67711  ?  212 VAL A C   1 
ATOM 1503 O O   . VAL A 1 242 ? 16.83861  26.59638 47.99854  1.000 65.77053  ?  212 VAL A O   1 
ATOM 1504 C CB  . VAL A 1 242 ? 14.20356  27.74555 49.63112  1.000 52.41059  ?  212 VAL A CB  1 
ATOM 1505 C CG1 . VAL A 1 242 ? 13.67218  28.87653 50.49848  1.000 51.87009  ?  212 VAL A CG1 1 
ATOM 1506 C CG2 . VAL A 1 242 ? 13.98661  28.04117 48.15299  1.000 59.34968  ?  212 VAL A CG2 1 
ATOM 1507 N N   . THR A 1 243 ? 16.04238  25.14566 49.52615  1.000 71.49685  ?  213 THR A N   1 
ATOM 1508 C CA  . THR A 1 243 ? 16.40143  23.91765 48.83350  1.000 58.04814  ?  213 THR A CA  1 
ATOM 1509 C C   . THR A 1 243 ? 15.20045  22.98875 48.85702  1.000 66.43184  ?  213 THR A C   1 
ATOM 1510 O O   . THR A 1 243 ? 14.23490  23.22579 49.58990  1.000 60.11268  ?  213 THR A O   1 
ATOM 1511 C CB  . THR A 1 243 ? 17.61687  23.24817 49.50130  1.000 43.05006  ?  213 THR A CB  1 
ATOM 1512 O OG1 . THR A 1 243 ? 17.35387  23.04802 50.89573  1.000 55.03314  ?  213 THR A OG1 1 
ATOM 1513 C CG2 . THR A 1 243 ? 18.86279  24.11008 49.34150  1.000 57.34948  ?  213 THR A CG2 1 
ATOM 1514 N N   . PRO A 1 244 ? 15.21154  21.91829 48.03864  1.000 61.46061  ?  214 PRO A N   1 
ATOM 1515 C CA  . PRO A 1 244 ? 14.11002  20.94390 48.08777  1.000 46.49066  ?  214 PRO A CA  1 
ATOM 1516 C C   . PRO A 1 244 ? 13.88562  20.34742 49.47013  1.000 49.55719  ?  214 PRO A C   1 
ATOM 1517 O O   . PRO A 1 244 ? 12.81937  19.78938 49.75070  1.000 63.87976  ?  214 PRO A O   1 
ATOM 1518 C CB  . PRO A 1 244 ? 14.55816  19.87431 47.08691  1.000 54.25820  ?  214 PRO A CB  1 
ATOM 1519 C CG  . PRO A 1 244 ? 15.33956  20.64097 46.08168  1.000 48.12176  ?  214 PRO A CG  1 
ATOM 1520 C CD  . PRO A 1 244 ? 16.07306  21.70170 46.86105  1.000 56.79742  ?  214 PRO A CD  1 
ATOM 1521 N N   . GLU A 1 245 ? 14.89702  20.44439 50.33579  1.000 56.27446  ?  215 GLU A N   1 
ATOM 1522 C CA  . GLU A 1 245 ? 14.76011  19.98245 51.71137  1.000 56.99044  ?  215 GLU A CA  1 
ATOM 1523 C C   . GLU A 1 245 ? 13.79573  20.84050 52.52220  1.000 46.01363  ?  215 GLU A C   1 
ATOM 1524 O O   . GLU A 1 245 ? 13.24587  20.35926 53.51936  1.000 51.88835  ?  215 GLU A O   1 
ATOM 1525 C CB  . GLU A 1 245 ? 16.13001  19.96155 52.38873  1.000 58.47109  ?  215 GLU A CB  1 
ATOM 1526 C CG  . GLU A 1 245 ? 17.11039  18.96825 51.79047  1.000 75.76304  ?  215 GLU A CG  1 
ATOM 1527 C CD  . GLU A 1 245 ? 18.52698  19.20760 52.26896  1.000 110.22196 ?  215 GLU A CD  1 
ATOM 1528 O OE1 . GLU A 1 245 ? 18.90942  20.38628 52.42050  1.000 105.95461 ?  215 GLU A OE1 1 
ATOM 1529 O OE2 . GLU A 1 245 ? 19.25500  18.22201 52.50632  1.000 122.04459 -1 215 GLU A OE2 1 
ATOM 1530 N N   . ASP A 1 246 ? 13.57995  22.09344 52.12184  1.000 48.69143  ?  216 ASP A N   1 
ATOM 1531 C CA  . ASP A 1 246 ? 12.69895  22.99905 52.84902  1.000 51.97528  ?  216 ASP A CA  1 
ATOM 1532 C C   . ASP A 1 246 ? 11.22935  22.81351 52.49847  1.000 48.11752  ?  216 ASP A C   1 
ATOM 1533 O O   . ASP A 1 246 ? 10.39030  23.55446 53.02143  1.000 40.21687  ?  216 ASP A O   1 
ATOM 1534 C CB  . ASP A 1 246 ? 13.10725  24.45236 52.59120  1.000 42.98375  ?  216 ASP A CB  1 
ATOM 1535 C CG  . ASP A 1 246 ? 14.48364  24.77520 53.13633  1.000 46.67060  ?  216 ASP A CG  1 
ATOM 1536 O OD1 . ASP A 1 246 ? 14.83705  24.24609 54.21153  1.000 47.46958  ?  216 ASP A OD1 1 
ATOM 1537 O OD2 . ASP A 1 246 ? 15.21314  25.55459 52.48800  1.000 52.62249  -1 216 ASP A OD2 1 
ATOM 1538 N N   . THR A 1 247 ? 10.89800  21.85588 51.63509  1.000 55.88071  ?  217 THR A N   1 
ATOM 1539 C CA  . THR A 1 247 ? 9.50652   21.58251 51.28969  1.000 37.37710  ?  217 THR A CA  1 
ATOM 1540 C C   . THR A 1 247 ? 8.80038   20.97374 52.49483  1.000 43.68758  ?  217 THR A C   1 
ATOM 1541 O O   . THR A 1 247 ? 9.07857   19.83191 52.87559  1.000 49.14215  ?  217 THR A O   1 
ATOM 1542 C CB  . THR A 1 247 ? 9.43345   20.64906 50.08498  1.000 34.29796  ?  217 THR A CB  1 
ATOM 1543 O OG1 . THR A 1 247 ? 10.01720  21.29065 48.94430  1.000 42.83861  ?  217 THR A OG1 1 
ATOM 1544 C CG2 . THR A 1 247 ? 7.98946   20.28889 49.77443  1.000 34.38513  ?  217 THR A CG2 1 
ATOM 1545 N N   . ALA A 1 248 ? 7.89036   21.73328 53.09785  1.000 40.41199  ?  218 ALA A N   1 
ATOM 1546 C CA  . ALA A 1 248 ? 7.17427   21.28999 54.28676  1.000 39.72449  ?  218 ALA A CA  1 
ATOM 1547 C C   . ALA A 1 248 ? 5.93322   22.15810 54.45338  1.000 40.63094  ?  218 ALA A C   1 
ATOM 1548 O O   . ALA A 1 248 ? 5.66793   23.05893 53.65254  1.000 41.18212  ?  218 ALA A O   1 
ATOM 1549 C CB  . ALA A 1 248 ? 8.07184   21.34937 55.52649  1.000 35.40417  ?  218 ALA A CB  1 
ATOM 1550 N N   . VAL A 1 249 ? 5.17032   21.87629 55.50547  1.000 31.71777  ?  219 VAL A N   1 
ATOM 1551 C CA  . VAL A 1 249 ? 3.99016   22.65610 55.86024  1.000 42.48429  ?  219 VAL A CA  1 
ATOM 1552 C C   . VAL A 1 249 ? 4.34946   23.53363 57.05066  1.000 46.69995  ?  219 VAL A C   1 
ATOM 1553 O O   . VAL A 1 249 ? 4.67804   23.02585 58.12960  1.000 50.82716  ?  219 VAL A O   1 
ATOM 1554 C CB  . VAL A 1 249 ? 2.79017   21.75178 56.18068  1.000 37.17212  ?  219 VAL A CB  1 
ATOM 1555 C CG1 . VAL A 1 249 ? 1.57323   22.59405 56.52397  1.000 32.12516  ?  219 VAL A CG1 1 
ATOM 1556 C CG2 . VAL A 1 249 ? 2.49108   20.83240 55.00849  1.000 35.88085  ?  219 VAL A CG2 1 
ATOM 1557 N N   . TYR A 1 250 ? 4.28295   24.84743 56.85909  1.000 43.77574  ?  220 TYR A N   1 
ATOM 1558 C CA  . TYR A 1 250 ? 4.70362   25.81216 57.86481  1.000 39.06620  ?  220 TYR A CA  1 
ATOM 1559 C C   . TYR A 1 250 ? 3.50967   26.28632 58.68371  1.000 39.82703  ?  220 TYR A C   1 
ATOM 1560 O O   . TYR A 1 250 ? 2.40093   26.43194 58.16044  1.000 41.35590  ?  220 TYR A O   1 
ATOM 1561 C CB  . TYR A 1 250 ? 5.40114   27.00558 57.20718  1.000 46.37120  ?  220 TYR A CB  1 
ATOM 1562 C CG  . TYR A 1 250 ? 6.70309   26.64348 56.52481  1.000 53.03908  ?  220 TYR A CG  1 
ATOM 1563 C CD1 . TYR A 1 250 ? 6.71203   26.06660 55.26053  1.000 42.14283  ?  220 TYR A CD1 1 
ATOM 1564 C CD2 . TYR A 1 250 ? 7.92314   26.87669 57.14616  1.000 45.08720  ?  220 TYR A CD2 1 
ATOM 1565 C CE1 . TYR A 1 250 ? 7.89899   25.73006 54.63618  1.000 44.42028  ?  220 TYR A CE1 1 
ATOM 1566 C CE2 . TYR A 1 250 ? 9.11521   26.54380 56.52917  1.000 41.36200  ?  220 TYR A CE2 1 
ATOM 1567 C CZ  . TYR A 1 250 ? 9.09716   25.97150 55.27484  1.000 43.89937  ?  220 TYR A CZ  1 
ATOM 1568 O OH  . TYR A 1 250 ? 10.28150  25.63978 54.65764  1.000 37.70274  ?  220 TYR A OH  1 
ATOM 1569 N N   . PHE A 1 251 ? 3.74586   26.52400 59.97347  1.000 38.34686  ?  221 PHE A N   1 
ATOM 1570 C CA  . PHE A 1 251 ? 2.71495   26.97421 60.89627  1.000 38.23412  ?  221 PHE A CA  1 
ATOM 1571 C C   . PHE A 1 251 ? 3.22571   28.15379 61.71109  1.000 37.42985  ?  221 PHE A C   1 
ATOM 1572 O O   . PHE A 1 251 ? 4.42734   28.28478 61.95876  1.000 49.66465  ?  221 PHE A O   1 
ATOM 1573 C CB  . PHE A 1 251 ? 2.28014   25.85666 61.85933  1.000 41.45943  ?  221 PHE A CB  1 
ATOM 1574 C CG  . PHE A 1 251 ? 1.73715   24.63399 61.17717  1.000 39.66944  ?  221 PHE A CG  1 
ATOM 1575 C CD1 . PHE A 1 251 ? 0.40946   24.57283 60.78900  1.000 42.11622  ?  221 PHE A CD1 1 
ATOM 1576 C CD2 . PHE A 1 251 ? 2.54987   23.53710 60.94345  1.000 46.34506  ?  221 PHE A CD2 1 
ATOM 1577 C CE1 . PHE A 1 251 ? -0.09414  23.44585 60.16905  1.000 50.38116  ?  221 PHE A CE1 1 
ATOM 1578 C CE2 . PHE A 1 251 ? 2.05220   22.40710 60.32398  1.000 42.35824  ?  221 PHE A CE2 1 
ATOM 1579 C CZ  . PHE A 1 251 ? 0.72819   22.36147 59.93715  1.000 52.48516  ?  221 PHE A CZ  1 
ATOM 1580 N N   . CYS A 1 252 ? 2.29763   29.01079 62.13014  1.000 31.48115  ?  222 CYS A N   1 
ATOM 1581 C CA  . CYS A 1 252 ? 2.57203   30.05969 63.10305  1.000 31.03977  ?  222 CYS A CA  1 
ATOM 1582 C C   . CYS A 1 252 ? 1.66919   29.84684 64.30794  1.000 42.11321  ?  222 CYS A C   1 
ATOM 1583 O O   . CYS A 1 252 ? 0.47366   29.57757 64.15145  1.000 53.04243  ?  222 CYS A O   1 
ATOM 1584 C CB  . CYS A 1 252 ? 2.35918   31.45943 62.51368  1.000 40.96870  ?  222 CYS A CB  1 
ATOM 1585 S SG  . CYS A 1 252 ? 0.72985   31.78339 61.78778  1.000 69.35181  ?  222 CYS A SG  1 
ATOM 1586 N N   . ALA A 1 253 ? 2.24129   29.95863 65.50435  1.000 27.74589  ?  223 ALA A N   1 
ATOM 1587 C CA  . ALA A 1 253 ? 1.50288   29.70635 66.73135  1.000 27.26886  ?  223 ALA A CA  1 
ATOM 1588 C C   . ALA A 1 253 ? 1.87349   30.74660 67.77789  1.000 33.22162  ?  223 ALA A C   1 
ATOM 1589 O O   . ALA A 1 253 ? 2.90311   31.41930 67.68217  1.000 36.16302  ?  223 ALA A O   1 
ATOM 1590 C CB  . ALA A 1 253 ? 1.76955   28.29452 67.27009  1.000 27.70954  ?  223 ALA A CB  1 
ATOM 1591 N N   . ARG A 1 254 ? 1.01316   30.86847 68.78415  1.000 27.62806  ?  224 ARG A N   1 
ATOM 1592 C CA  . ARG A 1 254 ? 1.22294   31.78383 69.89548  1.000 36.65657  ?  224 ARG A CA  1 
ATOM 1593 C C   . ARG A 1 254 ? 1.67012   31.00823 71.12686  1.000 40.86037  ?  224 ARG A C   1 
ATOM 1594 O O   . ARG A 1 254 ? 1.18364   29.90445 71.38959  1.000 35.21213  ?  224 ARG A O   1 
ATOM 1595 C CB  . ARG A 1 254 ? -0.05415  32.56707 70.21081  1.000 34.59089  ?  224 ARG A CB  1 
ATOM 1596 C CG  . ARG A 1 254 ? 0.11142   33.60514 71.31212  1.000 38.46668  ?  224 ARG A CG  1 
ATOM 1597 C CD  . ARG A 1 254 ? -1.21540  34.24045 71.69496  1.000 39.97189  ?  224 ARG A CD  1 
ATOM 1598 N NE  . ARG A 1 254 ? -2.09959  33.29801 72.37419  1.000 36.52733  ?  224 ARG A NE  1 
ATOM 1599 C CZ  . ARG A 1 254 ? -3.28753  33.61814 72.87716  1.000 40.85244  ?  224 ARG A CZ  1 
ATOM 1600 N NH1 . ARG A 1 254 ? -3.73825  34.86109 72.77986  1.000 34.91004  ?  224 ARG A NH1 1 
ATOM 1601 N NH2 . ARG A 1 254 ? -4.02504  32.69588 73.47993  1.000 59.52834  ?  224 ARG A NH2 1 
ATOM 1602 N N   . VAL A 1 255 ? 2.60100   31.59041 71.87707  1.000 36.93788  ?  225 VAL A N   1 
ATOM 1603 C CA  . VAL A 1 255 ? 3.08867   31.01645 73.12537  1.000 38.46265  ?  225 VAL A CA  1 
ATOM 1604 C C   . VAL A 1 255 ? 2.86223   32.03595 74.23102  1.000 43.21099  ?  225 VAL A C   1 
ATOM 1605 O O   . VAL A 1 255 ? 3.38464   33.15601 74.16744  1.000 45.19681  ?  225 VAL A O   1 
ATOM 1606 C CB  . VAL A 1 255 ? 4.57136   30.62228 73.03753  1.000 31.72925  ?  225 VAL A CB  1 
ATOM 1607 C CG1 . VAL A 1 255 ? 5.16004   30.46113 74.42852  1.000 41.40089  ?  225 VAL A CG1 1 
ATOM 1608 C CG2 . VAL A 1 255 ? 4.72536   29.33465 72.25350  1.000 33.92098  ?  225 VAL A CG2 1 
ATOM 1609 N N   . ILE A 1 256 ? 2.07811   31.65369 75.23429  1.000 44.28164  ?  226 ILE A N   1 
ATOM 1610 C CA  . ILE A 1 256 ? 1.86330   32.46645 76.42471  1.000 51.38234  ?  226 ILE A CA  1 
ATOM 1611 C C   . ILE A 1 256 ? 2.76967   31.93593 77.52543  1.000 53.07466  ?  226 ILE A C   1 
ATOM 1612 O O   . ILE A 1 256 ? 2.81641   30.72368 77.77083  1.000 49.38031  ?  226 ILE A O   1 
ATOM 1613 C CB  . ILE A 1 256 ? 0.38739   32.44778 76.85685  1.000 42.79154  ?  226 ILE A CB  1 
ATOM 1614 C CG1 . ILE A 1 256 ? -0.49472  33.03679 75.75408  1.000 35.31113  ?  226 ILE A CG1 1 
ATOM 1615 C CG2 . ILE A 1 256 ? 0.20009   33.21961 78.15083  1.000 39.24087  ?  226 ILE A CG2 1 
ATOM 1616 C CD1 . ILE A 1 256 ? -1.95929  33.10928 76.11902  1.000 66.20973  ?  226 ILE A CD1 1 
ATOM 1617 N N   . SER A 1 257 ? 3.49754   32.84198 78.18319  1.000 58.39229  ?  227 SER A N   1 
ATOM 1618 C CA  . SER A 1 257 ? 4.50336   32.42224 79.15440  1.000 53.30247  ?  227 SER A CA  1 
ATOM 1619 C C   . SER A 1 257 ? 3.87316   31.70112 80.34035  1.000 51.29010  ?  227 SER A C   1 
ATOM 1620 O O   . SER A 1 257 ? 4.40962   30.69493 80.81913  1.000 51.82422  ?  227 SER A O   1 
ATOM 1621 C CB  . SER A 1 257 ? 5.31052   33.63203 79.62544  1.000 56.16234  ?  227 SER A CB  1 
ATOM 1622 O OG  . SER A 1 257 ? 4.46114   34.64137 80.14212  1.000 84.76184  ?  227 SER A OG  1 
ATOM 1623 N N   . VAL A 1 258 ? 2.73177   32.19590 80.82872  1.000 44.91703  ?  228 VAL A N   1 
ATOM 1624 C CA  . VAL A 1 258 ? 2.08770   31.57790 81.98700  1.000 47.08399  ?  228 VAL A CA  1 
ATOM 1625 C C   . VAL A 1 258 ? 1.32110   30.31436 81.63474  1.000 55.72183  ?  228 VAL A C   1 
ATOM 1626 O O   . VAL A 1 258 ? 0.84742   29.61793 82.54142  1.000 45.26249  ?  228 VAL A O   1 
ATOM 1627 C CB  . VAL A 1 258 ? 1.13505   32.56559 82.68687  1.000 36.43396  ?  228 VAL A CB  1 
ATOM 1628 C CG1 . VAL A 1 258 ? 1.89217   33.80834 83.12750  1.000 44.19958  ?  228 VAL A CG1 1 
ATOM 1629 C CG2 . VAL A 1 258 ? -0.02023  32.93212 81.77131  1.000 35.40586  ?  228 VAL A CG2 1 
ATOM 1630 N N   . ALA A 1 259 ? 1.18711   29.99293 80.34939  1.000 59.80855  ?  229 ALA A N   1 
ATOM 1631 C CA  . ALA A 1 259 ? 0.50465   28.77944 79.90367  1.000 40.43784  ?  229 ALA A CA  1 
ATOM 1632 C C   . ALA A 1 259 ? 1.48807   27.67023 79.55489  1.000 47.58256  ?  229 ALA A C   1 
ATOM 1633 O O   . ALA A 1 259 ? 1.33232   26.98875 78.53797  1.000 46.72805  ?  229 ALA A O   1 
ATOM 1634 C CB  . ALA A 1 259 ? -0.40178  29.08485 78.71535  1.000 40.37964  ?  229 ALA A CB  1 
ATOM 1635 N N   . GLY A 1 260 ? 2.51096   27.46775 80.38341  1.000 47.17565  ?  230 GLY A N   1 
ATOM 1636 C CA  . GLY A 1 260 ? 3.46160   26.39954 80.14780  1.000 40.05588  ?  230 GLY A CA  1 
ATOM 1637 C C   . GLY A 1 260 ? 4.35602   26.59628 78.94735  1.000 40.02287  ?  230 GLY A C   1 
ATOM 1638 O O   . GLY A 1 260 ? 5.00026   25.63986 78.50734  1.000 60.32721  ?  230 GLY A O   1 
ATOM 1639 N N   . TYR A 1 261 ? 4.41513   27.81538 78.40472  1.000 36.05265  ?  231 TYR A N   1 
ATOM 1640 C CA  . TYR A 1 261 ? 5.21631   28.11928 77.21663  1.000 34.65118  ?  231 TYR A CA  1 
ATOM 1641 C C   . TYR A 1 261 ? 4.86032   27.20109 76.04998  1.000 34.21611  ?  231 TYR A C   1 
ATOM 1642 O O   . TYR A 1 261 ? 5.71627   26.84292 75.23632  1.000 34.13609  ?  231 TYR A O   1 
ATOM 1643 C CB  . TYR A 1 261 ? 6.71547   28.04473 77.52064  1.000 43.83918  ?  231 TYR A CB  1 
ATOM 1644 C CG  . TYR A 1 261 ? 7.27196   29.26204 78.22489  1.000 48.82821  ?  231 TYR A CG  1 
ATOM 1645 C CD1 . TYR A 1 261 ? 7.74085   30.35038 77.50091  1.000 49.00783  ?  231 TYR A CD1 1 
ATOM 1646 C CD2 . TYR A 1 261 ? 7.33660   29.32069 79.61079  1.000 37.95732  ?  231 TYR A CD2 1 
ATOM 1647 C CE1 . TYR A 1 261 ? 8.25492   31.46509 78.13649  1.000 52.77045  ?  231 TYR A CE1 1 
ATOM 1648 C CE2 . TYR A 1 261 ? 7.84994   30.43231 80.25688  1.000 42.77328  ?  231 TYR A CE2 1 
ATOM 1649 C CZ  . TYR A 1 261 ? 8.30727   31.50172 79.51453  1.000 59.11636  ?  231 TYR A CZ  1 
ATOM 1650 O OH  . TYR A 1 261 ? 8.81823   32.61035 80.15184  1.000 55.79836  ?  231 TYR A OH  1 
ATOM 1651 N N   . ALA A 1 262 ? 3.59245   26.81237 75.96258  1.000 34.26965  ?  232 ALA A N   1 
ATOM 1652 C CA  . ALA A 1 262 ? 3.12732   25.88598 74.94313  1.000 34.38592  ?  232 ALA A CA  1 
ATOM 1653 C C   . ALA A 1 262 ? 2.36928   26.62683 73.84954  1.000 32.46614  ?  232 ALA A C   1 
ATOM 1654 O O   . ALA A 1 262 ? 1.76165   27.67411 74.08593  1.000 34.42546  ?  232 ALA A O   1 
ATOM 1655 C CB  . ALA A 1 262 ? 2.23400   24.80374 75.55383  1.000 36.74170  ?  232 ALA A CB  1 
ATOM 1656 N N   . PHE A 1 263 ? 2.41627   26.06811 72.64361  1.000 32.10739  ?  233 PHE A N   1 
ATOM 1657 C CA  . PHE A 1 263 ? 1.71308   26.62895 71.49235  1.000 33.89283  ?  233 PHE A CA  1 
ATOM 1658 C C   . PHE A 1 263 ? 0.22394   26.35060 71.65117  1.000 44.08554  ?  233 PHE A C   1 
ATOM 1659 O O   . PHE A 1 263 ? -0.24391  25.23816 71.39939  1.000 40.65304  ?  233 PHE A O   1 
ATOM 1660 C CB  . PHE A 1 263 ? 2.25397   26.03032 70.19878  1.000 36.12512  ?  233 PHE A CB  1 
ATOM 1661 C CG  . PHE A 1 263 ? 3.75388   26.05753 70.09676  1.000 36.40137  ?  233 PHE A CG  1 
ATOM 1662 C CD1 . PHE A 1 263 ? 4.40555   27.15632 69.56364  1.000 35.12493  ?  233 PHE A CD1 1 
ATOM 1663 C CD2 . PHE A 1 263 ? 4.51193   24.98146 70.53037  1.000 42.28296  ?  233 PHE A CD2 1 
ATOM 1664 C CE1 . PHE A 1 263 ? 5.78502   27.18505 69.47047  1.000 37.48300  ?  233 PHE A CE1 1 
ATOM 1665 C CE2 . PHE A 1 263 ? 5.89111   25.00381 70.43796  1.000 45.95055  ?  233 PHE A CE2 1 
ATOM 1666 C CZ  . PHE A 1 263 ? 6.52799   26.10665 69.90662  1.000 31.66281  ?  233 PHE A CZ  1 
ATOM 1667 N N   . ASP A 1 264 ? -0.53182  27.36535 72.07094  1.000 44.00321  ?  234 ASP A N   1 
ATOM 1668 C CA  . ASP A 1 264 ? -1.94120  27.17638 72.39162  1.000 47.43658  ?  234 ASP A CA  1 
ATOM 1669 C C   . ASP A 1 264 ? -2.87279  27.48440 71.22758  1.000 51.45670  ?  234 ASP A C   1 
ATOM 1670 O O   . ASP A 1 264 ? -3.95422  26.89059 71.14070  1.000 53.90328  ?  234 ASP A O   1 
ATOM 1671 C CB  . ASP A 1 264 ? -2.32652  28.03877 73.59812  1.000 49.14199  ?  234 ASP A CB  1 
ATOM 1672 C CG  . ASP A 1 264 ? -1.90999  29.48769 73.43857  1.000 57.53093  ?  234 ASP A CG  1 
ATOM 1673 O OD1 . ASP A 1 264 ? -2.53823  30.20588 72.63356  1.000 45.57753  ?  234 ASP A OD1 1 
ATOM 1674 O OD2 . ASP A 1 264 ? -0.95403  29.90973 74.12250  1.000 76.64378  -1 234 ASP A OD2 1 
ATOM 1675 N N   . ILE A 1 265 ? -2.49020  28.39315 70.33403  1.000 38.41526  ?  235 ILE A N   1 
ATOM 1676 C CA  . ILE A 1 265 ? -3.32477  28.78888 69.20345  1.000 37.56000  ?  235 ILE A CA  1 
ATOM 1677 C C   . ILE A 1 265 ? -2.45810  28.76723 67.95231  1.000 31.10071  ?  235 ILE A C   1 
ATOM 1678 O O   . ILE A 1 265 ? -1.51916  29.56299 67.82804  1.000 29.71326  ?  235 ILE A O   1 
ATOM 1679 C CB  . ILE A 1 265 ? -3.96291  30.16958 69.40776  1.000 32.71659  ?  235 ILE A CB  1 
ATOM 1680 C CG1 . ILE A 1 265 ? -4.99044  30.10599 70.53970  1.000 35.86959  ?  235 ILE A CG1 1 
ATOM 1681 C CG2 . ILE A 1 265 ? -4.60931  30.65873 68.11940  1.000 33.53204  ?  235 ILE A CG2 1 
ATOM 1682 C CD1 . ILE A 1 265 ? -5.65663  31.41955 70.83956  1.000 54.82766  ?  235 ILE A CD1 1 
ATOM 1683 N N   . TRP A 1 266 ? -2.77328  27.86515 67.02690  1.000 36.59754  ?  236 TRP A N   1 
ATOM 1684 C CA  . TRP A 1 266 ? -2.00367  27.67306 65.80960  1.000 40.91805  ?  236 TRP A CA  1 
ATOM 1685 C C   . TRP A 1 266 ? -2.67820  28.38506 64.63872  1.000 31.54391  ?  236 TRP A C   1 
ATOM 1686 O O   . TRP A 1 266 ? -3.76421  28.95635 64.76098  1.000 34.49363  ?  236 TRP A O   1 
ATOM 1687 C CB  . TRP A 1 266 ? -1.83129  26.17989 65.52193  1.000 34.72855  ?  236 TRP A CB  1 
ATOM 1688 C CG  . TRP A 1 266 ? -0.97339  25.46705 66.52370  1.000 31.59706  ?  236 TRP A CG  1 
ATOM 1689 C CD1 . TRP A 1 266 ? -1.22554  25.30862 67.85584  1.000 32.43860  ?  236 TRP A CD1 1 
ATOM 1690 C CD2 . TRP A 1 266 ? 0.27016   24.80268 66.26971  1.000 35.03806  ?  236 TRP A CD2 1 
ATOM 1691 N NE1 . TRP A 1 266 ? -0.21262  24.59456 68.44820  1.000 32.58660  ?  236 TRP A NE1 1 
ATOM 1692 C CE2 . TRP A 1 266 ? 0.71743   24.27078 67.49579  1.000 31.83014  ?  236 TRP A CE2 1 
ATOM 1693 C CE3 . TRP A 1 266 ? 1.04993   24.60829 65.12531  1.000 30.36717  ?  236 TRP A CE3 1 
ATOM 1694 C CZ2 . TRP A 1 266 ? 1.90838   23.55810 67.60974  1.000 32.12617  ?  236 TRP A CZ2 1 
ATOM 1695 C CZ3 . TRP A 1 266 ? 2.23138   23.90094 65.24057  1.000 30.48521  ?  236 TRP A CZ3 1 
ATOM 1696 C CH2 . TRP A 1 266 ? 2.64911   23.38393 66.47365  1.000 45.77269  ?  236 TRP A CH2 1 
ATOM 1697 N N   . GLY A 1 267 ? -2.01935  28.34082 63.48044  1.000 30.87378  ?  237 GLY A N   1 
ATOM 1698 C CA  . GLY A 1 267 ? -2.49788  29.00633 62.29085  1.000 31.71137  ?  237 GLY A CA  1 
ATOM 1699 C C   . GLY A 1 267 ? -3.14849  28.05245 61.30445  1.000 36.65912  ?  237 GLY A C   1 
ATOM 1700 O O   . GLY A 1 267 ? -3.46413  26.90108 61.61097  1.000 33.97295  ?  237 GLY A O   1 
ATOM 1701 N N   . GLN A 1 268 ? -3.34712  28.56019 60.08625  1.000 53.37671  ?  238 GLN A N   1 
ATOM 1702 C CA  . GLN A 1 268 ? -3.99276  27.77417 59.03935  1.000 55.47540  ?  238 GLN A CA  1 
ATOM 1703 C C   . GLN A 1 268 ? -3.11942  26.59765 58.61963  1.000 52.41366  ?  238 GLN A C   1 
ATOM 1704 O O   . GLN A 1 268 ? -3.53604  25.43605 58.69833  1.000 35.94330  ?  238 GLN A O   1 
ATOM 1705 C CB  . GLN A 1 268 ? -4.30785  28.66810 57.83724  1.000 37.08160  ?  238 GLN A CB  1 
ATOM 1706 C CG  . GLN A 1 268 ? -5.09662  29.92207 58.18007  1.000 49.91089  ?  238 GLN A CG  1 
ATOM 1707 C CD  . GLN A 1 268 ? -6.53134  29.62477 58.57518  1.000 104.93581 ?  238 GLN A CD  1 
ATOM 1708 O OE1 . GLN A 1 268 ? -7.16981  28.73239 58.01645  1.000 97.83759  ?  238 GLN A OE1 1 
ATOM 1709 N NE2 . GLN A 1 268 ? -7.04530  30.37326 59.54496  1.000 65.87591  ?  238 GLN A NE2 1 
ATOM 1710 N N   . GLY A 1 269 ? -1.90005  26.88167 58.17133  1.000 34.60255  ?  239 GLY A N   1 
ATOM 1711 C CA  . GLY A 1 269 ? -1.01087  25.84681 57.68614  1.000 34.18189  ?  239 GLY A CA  1 
ATOM 1712 C C   . GLY A 1 269 ? -0.88592  25.85502 56.17728  1.000 45.25025  ?  239 GLY A C   1 
ATOM 1713 O O   . GLY A 1 269 ? -1.74836  25.32087 55.47315  1.000 54.94635  ?  239 GLY A O   1 
ATOM 1714 N N   . THR A 1 270 ? 0.18167   26.46236 55.66873  1.000 36.42897  ?  240 THR A N   1 
ATOM 1715 C CA  . THR A 1 270 ? 0.41935   26.55992 54.23616  1.000 56.18494  ?  240 THR A CA  1 
ATOM 1716 C C   . THR A 1 270 ? 1.47199   25.54608 53.80617  1.000 44.82591  ?  240 THR A C   1 
ATOM 1717 O O   . THR A 1 270 ? 2.44783   25.30264 54.52236  1.000 40.95985  ?  240 THR A O   1 
ATOM 1718 C CB  . THR A 1 270 ? 0.86276   27.97353 53.84841  1.000 54.08689  ?  240 THR A CB  1 
ATOM 1719 O OG1 . THR A 1 270 ? 1.30442   27.98423 52.48484  1.000 70.91790  ?  240 THR A OG1 1 
ATOM 1720 C CG2 . THR A 1 270 ? 1.99084   28.44694 54.74775  1.000 42.37985  ?  240 THR A CG2 1 
ATOM 1721 N N   . MET A 1 271 ? 1.26227   24.95393 52.63382  1.000 50.82883  ?  241 MET A N   1 
ATOM 1722 C CA  . MET A 1 271 ? 2.16901   23.96053 52.07313  1.000 45.91868  ?  241 MET A CA  1 
ATOM 1723 C C   . MET A 1 271 ? 3.07876   24.63602 51.05461  1.000 47.99663  ?  241 MET A C   1 
ATOM 1724 O O   . MET A 1 271 ? 2.60178   25.16118 50.04269  1.000 58.40259  ?  241 MET A O   1 
ATOM 1725 C CB  . MET A 1 271 ? 1.38722   22.81769 51.42474  1.000 49.21880  ?  241 MET A CB  1 
ATOM 1726 C CG  . MET A 1 271 ? 2.23137   21.87896 50.57520  1.000 51.58924  ?  241 MET A CG  1 
ATOM 1727 S SD  . MET A 1 271 ? 3.47288   20.97699 51.52185  1.000 70.48811  ?  241 MET A SD  1 
ATOM 1728 C CE  . MET A 1 271 ? 4.27052   20.03720 50.22269  1.000 35.28193  ?  241 MET A CE  1 
ATOM 1729 N N   . VAL A 1 272 ? 4.38185   24.62093 51.32266  1.000 48.22952  ?  242 VAL A N   1 
ATOM 1730 C CA  . VAL A 1 272 ? 5.38245   25.22260 50.44889  1.000 57.23151  ?  242 VAL A CA  1 
ATOM 1731 C C   . VAL A 1 272 ? 6.17223   24.10605 49.78190  1.000 43.30699  ?  242 VAL A C   1 
ATOM 1732 O O   . VAL A 1 272 ? 6.65908   23.19153 50.45788  1.000 38.21000  ?  242 VAL A O   1 
ATOM 1733 C CB  . VAL A 1 272 ? 6.31527   26.16826 51.22463  1.000 52.25053  ?  242 VAL A CB  1 
ATOM 1734 C CG1 . VAL A 1 272 ? 7.34169   26.78406 50.28687  1.000 48.16053  ?  242 VAL A CG1 1 
ATOM 1735 C CG2 . VAL A 1 272 ? 5.50881   27.24917 51.92802  1.000 59.05720  ?  242 VAL A CG2 1 
ATOM 1736 N N   . THR A 1 273 ? 6.29927   24.18200 48.45937  1.000 45.65242  ?  243 THR A N   1 
ATOM 1737 C CA  . THR A 1 273 ? 7.02204   23.19288 47.67183  1.000 36.03086  ?  243 THR A CA  1 
ATOM 1738 C C   . THR A 1 273 ? 8.13975   23.88205 46.90338  1.000 49.68858  ?  243 THR A C   1 
ATOM 1739 O O   . THR A 1 273 ? 7.89483   24.85623 46.18398  1.000 57.41650  ?  243 THR A O   1 
ATOM 1740 C CB  . THR A 1 273 ? 6.08562   22.46451 46.70225  1.000 44.60038  ?  243 THR A CB  1 
ATOM 1741 O OG1 . THR A 1 273 ? 5.08865   21.74865 47.44245  1.000 45.57608  ?  243 THR A OG1 1 
ATOM 1742 C CG2 . THR A 1 273 ? 6.86720   21.48756 45.83648  1.000 60.19873  ?  243 THR A CG2 1 
ATOM 1743 N N   . VAL A 1 274 ? 9.35964   23.37763 47.05811  1.000 58.02130  ?  244 VAL A N   1 
ATOM 1744 C CA  . VAL A 1 274 ? 10.53052  23.90917 46.37071  1.000 44.73878  ?  244 VAL A CA  1 
ATOM 1745 C C   . VAL A 1 274 ? 10.78144  23.01390 45.16266  1.000 62.87882  ?  244 VAL A C   1 
ATOM 1746 O O   . VAL A 1 274 ? 11.33882  21.91987 45.28751  1.000 75.43140  ?  244 VAL A O   1 
ATOM 1747 C CB  . VAL A 1 274 ? 11.74994  23.97584 47.29311  1.000 42.18865  ?  244 VAL A CB  1 
ATOM 1748 C CG1 . VAL A 1 274 ? 12.94367  24.55793 46.55074  1.000 60.75447  ?  244 VAL A CG1 1 
ATOM 1749 C CG2 . VAL A 1 274 ? 11.43128  24.79910 48.53155  1.000 42.10089  ?  244 VAL A CG2 1 
ATOM 1750 N N   . SER A 1 275 ? 10.36742  23.47778 43.98547  1.000 85.27475  ?  245 SER A N   1 
ATOM 1751 C CA  . SER A 1 275 ? 10.52307  22.71706 42.75537  1.000 89.47465  ?  245 SER A CA  1 
ATOM 1752 C C   . SER A 1 275 ? 10.94659  23.65283 41.63283  1.000 105.48702 ?  245 SER A C   1 
ATOM 1753 O O   . SER A 1 275 ? 10.77280  24.87161 41.71107  1.000 97.10870  ?  245 SER A O   1 
ATOM 1754 C CB  . SER A 1 275 ? 9.22863   21.98434 42.37541  1.000 94.91360  ?  245 SER A CB  1 
ATOM 1755 O OG  . SER A 1 275 ? 9.38566   21.26598 41.16387  1.000 103.14922 ?  245 SER A OG  1 
ATOM 1756 N N   . SER A 1 276 ? 11.50630  23.06308 40.58133  1.000 103.21660 ?  246 SER A N   1 
ATOM 1757 C CA  . SER A 1 276 ? 11.96308  23.82573 39.42576  1.000 92.88371  ?  246 SER A CA  1 
ATOM 1758 C C   . SER A 1 276 ? 11.14924  23.47809 38.18349  1.000 89.59671  ?  246 SER A C   1 
ATOM 1759 O O   . SER A 1 276 ? 10.16274  22.74537 38.26044  1.000 85.67849  ?  246 SER A O   1 
ATOM 1760 C CB  . SER A 1 276 ? 13.45058  23.57223 39.17031  1.000 88.24856  ?  246 SER A CB  1 
ATOM 1761 O OG  . SER A 1 276 ? 13.70546  22.19420 38.95956  1.000 91.96509  ?  246 SER A OG  1 
ATOM 1762 N N   . PHE B 2 17  ? -16.51786 38.47199 109.05214 1.000 84.71001  ?  338 PHE C N   1 
ATOM 1763 C CA  . PHE B 2 17  ? -16.35976 37.11500 108.54100 1.000 110.78835 ?  338 PHE C CA  1 
ATOM 1764 C C   . PHE B 2 17  ? -16.90600 36.98173 107.12350 1.000 118.97583 ?  338 PHE C C   1 
ATOM 1765 O O   . PHE B 2 17  ? -16.25483 36.40653 106.25147 1.000 119.25317 ?  338 PHE C O   1 
ATOM 1766 C CB  . PHE B 2 17  ? -17.05133 36.11115 109.46550 1.000 116.42658 ?  338 PHE C CB  1 
ATOM 1767 C CG  . PHE B 2 17  ? -16.13943 35.50723 110.49450 1.000 124.15948 ?  338 PHE C CG  1 
ATOM 1768 C CD1 . PHE B 2 17  ? -15.79321 36.21248 111.63527 1.000 133.62863 ?  338 PHE C CD1 1 
ATOM 1769 C CD2 . PHE B 2 17  ? -15.63051 34.23065 110.32119 1.000 121.25126 ?  338 PHE C CD2 1 
ATOM 1770 C CE1 . PHE B 2 17  ? -14.95365 35.65631 112.58293 1.000 124.61896 ?  338 PHE C CE1 1 
ATOM 1771 C CE2 . PHE B 2 17  ? -14.79172 33.66885 111.26472 1.000 130.23630 ?  338 PHE C CE2 1 
ATOM 1772 C CZ  . PHE B 2 17  ? -14.45282 34.38266 112.39716 1.000 132.07442 ?  338 PHE C CZ  1 
ATOM 1773 N N   . GLY B 2 18  ? -18.10808 37.51738 106.89973 1.000 120.63305 ?  339 GLY C N   1 
ATOM 1774 C CA  . GLY B 2 18  ? -18.71479 37.43045 105.58286 1.000 120.05852 ?  339 GLY C CA  1 
ATOM 1775 C C   . GLY B 2 18  ? -17.95292 38.19154 104.51745 1.000 124.24304 ?  339 GLY C C   1 
ATOM 1776 O O   . GLY B 2 18  ? -18.02005 37.84373 103.33492 1.000 128.21912 ?  339 GLY C O   1 
ATOM 1777 N N   . GLU B 2 19  ? -17.21836 39.23252 104.91322 1.000 116.97346 ?  340 GLU C N   1 
ATOM 1778 C CA  . GLU B 2 19  ? -16.44060 40.01371 103.96004 1.000 110.38882 ?  340 GLU C CA  1 
ATOM 1779 C C   . GLU B 2 19  ? -15.20034 39.28077 103.46700 1.000 112.83272 ?  340 GLU C C   1 
ATOM 1780 O O   . GLU B 2 19  ? -14.57514 39.73848 102.50436 1.000 112.32551 ?  340 GLU C O   1 
ATOM 1781 C CB  . GLU B 2 19  ? -16.03814 41.34950 104.58664 1.000 108.81064 ?  340 GLU C CB  1 
ATOM 1782 C CG  . GLU B 2 19  ? -17.21672 42.21605 104.99768 1.000 129.46988 ?  340 GLU C CG  1 
ATOM 1783 C CD  . GLU B 2 19  ? -16.78724 43.49838 105.68119 1.000 153.05736 ?  340 GLU C CD  1 
ATOM 1784 O OE1 . GLU B 2 19  ? -15.58277 43.63978 105.97974 1.000 141.82818 ?  340 GLU C OE1 1 
ATOM 1785 O OE2 . GLU B 2 19  ? -17.65413 44.36552 105.91914 1.000 166.39439 -1 340 GLU C OE2 1 
ATOM 1786 N N   . VAL B 2 20  ? -14.83116 38.16851 104.09466 1.000 106.38159 ?  341 VAL C N   1 
ATOM 1787 C CA  . VAL B 2 20  ? -13.68413 37.36815 103.68684 1.000 99.55920  ?  341 VAL C CA  1 
ATOM 1788 C C   . VAL B 2 20  ? -14.12430 36.09015 102.98142 1.000 103.80380 ?  341 VAL C C   1 
ATOM 1789 O O   . VAL B 2 20  ? -13.59345 35.73770 101.92755 1.000 113.43039 ?  341 VAL C O   1 
ATOM 1790 C CB  . VAL B 2 20  ? -12.77494 37.04902 104.89513 1.000 103.12993 ?  341 VAL C CB  1 
ATOM 1791 C CG1 . VAL B 2 20  ? -11.55952 36.24869 104.45059 1.000 111.54617 ?  341 VAL C CG1 1 
ATOM 1792 C CG2 . VAL B 2 20  ? -12.35114 38.33160 105.59322 1.000 88.94584  ?  341 VAL C CG2 1 
ATOM 1793 N N   . PHE B 2 21  ? -15.10264 35.38409 103.55126 1.000 97.34467  ?  342 PHE C N   1 
ATOM 1794 C CA  . PHE B 2 21  ? -15.58621 34.14971 102.94197 1.000 101.77634 ?  342 PHE C CA  1 
ATOM 1795 C C   . PHE B 2 21  ? -16.46891 34.43469 101.73262 1.000 103.11873 ?  342 PHE C C   1 
ATOM 1796 O O   . PHE B 2 21  ? -16.21716 33.92198 100.63661 1.000 103.58017 ?  342 PHE C O   1 
ATOM 1797 C CB  . PHE B 2 21  ? -16.34648 33.31530 103.97504 1.000 94.82145  ?  342 PHE C CB  1 
ATOM 1798 C CG  . PHE B 2 21  ? -15.47118 32.73068 105.04617 1.000 94.17192  ?  342 PHE C CG  1 
ATOM 1799 C CD1 . PHE B 2 21  ? -14.99486 31.43478 104.93824 1.000 109.25222 ?  342 PHE C CD1 1 
ATOM 1800 C CD2 . PHE B 2 21  ? -15.12406 33.47618 106.16023 1.000 94.57072  ?  342 PHE C CD2 1 
ATOM 1801 C CE1 . PHE B 2 21  ? -14.18941 30.89364 105.92151 1.000 107.26785 ?  342 PHE C CE1 1 
ATOM 1802 C CE2 . PHE B 2 21  ? -14.31863 32.94109 107.14625 1.000 116.13406 ?  342 PHE C CE2 1 
ATOM 1803 C CZ  . PHE B 2 21  ? -13.85168 31.64857 107.02685 1.000 114.66885 ?  342 PHE C CZ  1 
ATOM 1804 N N   . ASN B 2 22  ? -17.50587 35.25110 101.91235 1.000 101.02634 ?  343 ASN C N   1 
ATOM 1805 C CA  . ASN B 2 22  ? -18.44277 35.57164 100.83596 1.000 105.05228 ?  343 ASN C CA  1 
ATOM 1806 C C   . ASN B 2 22  ? -17.94749 36.69311 99.92985  1.000 101.03072 ?  343 ASN C C   1 
ATOM 1807 O O   . ASN B 2 22  ? -18.73300 37.54137 99.50024  1.000 121.09641 ?  343 ASN C O   1 
ATOM 1808 C CB  . ASN B 2 22  ? -19.80228 35.92211 101.43717 1.000 108.96665 ?  343 ASN C CB  1 
ATOM 1809 C CG  . ASN B 2 22  ? -20.38916 34.78729 102.25476 1.000 115.98711 ?  343 ASN C CG  1 
ATOM 1810 O OD1 . ASN B 2 22  ? -20.12286 33.61451 101.99171 1.000 112.06737 ?  343 ASN C OD1 1 
ATOM 1811 N ND2 . ASN B 2 22  ? -21.19472 35.13205 103.25291 1.000 112.27344 ?  343 ASN C ND2 1 
ATOM 1812 N N   . ALA B 2 23  ? -16.65338 36.72001 99.62554  1.000 91.35168  ?  344 ALA C N   1 
ATOM 1813 C CA  . ALA B 2 23  ? -16.10760 37.73015 98.73349  1.000 94.72164  ?  344 ALA C CA  1 
ATOM 1814 C C   . ALA B 2 23  ? -16.45167 37.40504 97.28494  1.000 102.77073 ?  344 ALA C C   1 
ATOM 1815 O O   . ALA B 2 23  ? -16.54193 36.23893 96.89053  1.000 113.17921 ?  344 ALA C O   1 
ATOM 1816 C CB  . ALA B 2 23  ? -14.59159 37.83669 98.90183  1.000 94.73434  ?  344 ALA C CB  1 
ATOM 1817 N N   . THR B 2 24  ? -16.64867 38.45851 96.48985  1.000 87.04121  ?  345 THR C N   1 
ATOM 1818 C CA  . THR B 2 24  ? -17.00980 38.27268 95.08769  1.000 95.84245  ?  345 THR C CA  1 
ATOM 1819 C C   . THR B 2 24  ? -15.85599 37.66478 94.29881  1.000 106.73973 ?  345 THR C C   1 
ATOM 1820 O O   . THR B 2 24  ? -16.05130 36.73059 93.51230  1.000 95.53190  ?  345 THR C O   1 
ATOM 1821 C CB  . THR B 2 24  ? -17.43768 39.60711 94.47476  1.000 108.08263 ?  345 THR C CB  1 
ATOM 1822 O OG1 . THR B 2 24  ? -18.53168 40.14897 95.22501  1.000 113.23515 ?  345 THR C OG1 1 
ATOM 1823 C CG2 . THR B 2 24  ? -17.86923 39.41638 93.02562  1.000 94.57309  ?  345 THR C CG2 1 
ATOM 1824 N N   . ARG B 2 25  ? -14.64544 38.18143 94.49717  1.000 115.00157 ?  346 ARG C N   1 
ATOM 1825 C CA  . ARG B 2 25  ? -13.46275 37.68305 93.81299  1.000 92.43527  ?  346 ARG C CA  1 
ATOM 1826 C C   . ARG B 2 25  ? -12.31551 37.58431 94.80578  1.000 80.52228  ?  346 ARG C C   1 
ATOM 1827 O O   . ARG B 2 25  ? -12.10647 38.48811 95.62016  1.000 72.83775  ?  346 ARG C O   1 
ATOM 1828 C CB  . ARG B 2 25  ? -13.07221 38.58788 92.63571  1.000 87.82024  ?  346 ARG C CB  1 
ATOM 1829 C CG  . ARG B 2 25  ? -12.87790 40.04757 93.01239  1.000 91.38849  ?  346 ARG C CG  1 
ATOM 1830 C CD  . ARG B 2 25  ? -12.45412 40.88582 91.82048  1.000 88.47914  ?  346 ARG C CD  1 
ATOM 1831 N NE  . ARG B 2 25  ? -12.14632 42.25817 92.21237  1.000 108.45399 ?  346 ARG C NE  1 
ATOM 1832 C CZ  . ARG B 2 25  ? -11.78532 43.21666 91.36553  1.000 106.76707 ?  346 ARG C CZ  1 
ATOM 1833 N NH1 . ARG B 2 25  ? -11.52428 44.43638 91.81595  1.000 99.62547  ?  346 ARG C NH1 1 
ATOM 1834 N NH2 . ARG B 2 25  ? -11.68665 42.95775 90.06859  1.000 78.06450  ?  346 ARG C NH2 1 
ATOM 1835 N N   . PHE B 2 26  ? -11.58163 36.47947 94.73679  1.000 83.46509  ?  347 PHE C N   1 
ATOM 1836 C CA  . PHE B 2 26  ? -10.43700 36.24243 95.59844  1.000 83.36015  ?  347 PHE C CA  1 
ATOM 1837 C C   . PHE B 2 26  ? -9.15058  36.65308 94.88695  1.000 86.44953  ?  347 PHE C C   1 
ATOM 1838 O O   . PHE B 2 26  ? -9.14487  37.02324 93.71065  1.000 87.17888  ?  347 PHE C O   1 
ATOM 1839 C CB  . PHE B 2 26  ? -10.38383 34.77453 96.02537  1.000 72.82227  ?  347 PHE C CB  1 
ATOM 1840 C CG  . PHE B 2 26  ? -11.18520 34.46949 97.25812  1.000 78.69640  ?  347 PHE C CG  1 
ATOM 1841 C CD1 . PHE B 2 26  ? -12.54861 34.70976 97.29529  1.000 93.97195  ?  347 PHE C CD1 1 
ATOM 1842 C CD2 . PHE B 2 26  ? -10.57411 33.92930 98.37705  1.000 74.14646  ?  347 PHE C CD2 1 
ATOM 1843 C CE1 . PHE B 2 26  ? -13.28527 34.42642 98.43108  1.000 102.51018 ?  347 PHE C CE1 1 
ATOM 1844 C CE2 . PHE B 2 26  ? -11.30475 33.64151 99.51354  1.000 85.04122  ?  347 PHE C CE2 1 
ATOM 1845 C CZ  . PHE B 2 26  ? -12.66209 33.89014 99.54075  1.000 108.85969 ?  347 PHE C CZ  1 
ATOM 1846 N N   . ALA B 2 27  ? -8.04488  36.58348 95.61802  1.000 85.54713  ?  348 ALA C N   1 
ATOM 1847 C CA  . ALA B 2 27  ? -6.73096  36.91112 95.09038  1.000 68.62504  ?  348 ALA C CA  1 
ATOM 1848 C C   . ALA B 2 27  ? -5.96444  35.63662 94.75427  1.000 82.07104  ?  348 ALA C C   1 
ATOM 1849 O O   . ALA B 2 27  ? -6.38255  34.52179 95.07543  1.000 70.67123  ?  348 ALA C O   1 
ATOM 1850 C CB  . ALA B 2 27  ? -5.94798  37.76430 96.09197  1.000 73.86804  ?  348 ALA C CB  1 
ATOM 1851 N N   . SER B 2 28  ? -4.82186  35.81746 94.09749  1.000 95.53651  ?  349 SER C N   1 
ATOM 1852 C CA  . SER B 2 28  ? -4.00120  34.69024 93.68538  1.000 95.18683  ?  349 SER C CA  1 
ATOM 1853 C C   . SER B 2 28  ? -3.27881  34.09201 94.89329  1.000 103.08506 ?  349 SER C C   1 
ATOM 1854 O O   . SER B 2 28  ? -3.40813  34.55717 96.02962  1.000 105.98434 ?  349 SER C O   1 
ATOM 1855 C CB  . SER B 2 28  ? -3.01031  35.12607 92.60931  1.000 92.62753  ?  349 SER C CB  1 
ATOM 1856 O OG  . SER B 2 28  ? -2.26341  34.02313 92.12797  1.000 109.96781 ?  349 SER C OG  1 
ATOM 1857 N N   . VAL B 2 29  ? -2.50075  33.03854 94.63758  1.000 100.36140 ?  350 VAL C N   1 
ATOM 1858 C CA  . VAL B 2 29  ? -1.79785  32.35458 95.71943  1.000 86.75797  ?  350 VAL C CA  1 
ATOM 1859 C C   . VAL B 2 29  ? -0.64635  33.21040 96.23208  1.000 88.96824  ?  350 VAL C C   1 
ATOM 1860 O O   . VAL B 2 29  ? -0.51254  33.44184 97.43939  1.000 88.48914  ?  350 VAL C O   1 
ATOM 1861 C CB  . VAL B 2 29  ? -1.30389  30.97347 95.25346  1.000 97.80481  ?  350 VAL C CB  1 
ATOM 1862 C CG1 . VAL B 2 29  ? -0.96379  30.10296 96.45260  1.000 87.54006  ?  350 VAL C CG1 1 
ATOM 1863 C CG2 . VAL B 2 29  ? -2.34125  30.30327 94.37149  1.000 91.57758  ?  350 VAL C CG2 1 
ATOM 1864 N N   . TYR B 2 30  ? 0.20596   33.68914 95.32192  1.000 91.09794  ?  351 TYR C N   1 
ATOM 1865 C CA  . TYR B 2 30  ? 1.35334   34.49060 95.73411  1.000 77.98751  ?  351 TYR C CA  1 
ATOM 1866 C C   . TYR B 2 30  ? 0.92726   35.85399 96.26234  1.000 86.53109  ?  351 TYR C C   1 
ATOM 1867 O O   . TYR B 2 30  ? 1.61493   36.42930 97.11354  1.000 91.93549  ?  351 TYR C O   1 
ATOM 1868 C CB  . TYR B 2 30  ? 2.32863   34.65350 94.56719  1.000 69.53913  ?  351 TYR C CB  1 
ATOM 1869 C CG  . TYR B 2 30  ? 1.82997   35.56494 93.46741  1.000 75.32445  ?  351 TYR C CG  1 
ATOM 1870 C CD1 . TYR B 2 30  ? 0.93565   35.10646 92.50895  1.000 76.65416  ?  351 TYR C CD1 1 
ATOM 1871 C CD2 . TYR B 2 30  ? 2.25919   36.88375 93.38456  1.000 90.53505  ?  351 TYR C CD2 1 
ATOM 1872 C CE1 . TYR B 2 30  ? 0.47852   35.93731 91.50214  1.000 88.55202  ?  351 TYR C CE1 1 
ATOM 1873 C CE2 . TYR B 2 30  ? 1.80819   37.72119 92.38217  1.000 85.99082  ?  351 TYR C CE2 1 
ATOM 1874 C CZ  . TYR B 2 30  ? 0.91850   37.24353 91.44402  1.000 93.40715  ?  351 TYR C CZ  1 
ATOM 1875 O OH  . TYR B 2 30  ? 0.46889   38.07559 90.44427  1.000 90.11734  ?  351 TYR C OH  1 
ATOM 1876 N N   . ALA B 2 31  ? -0.19015  36.38202 95.77706  1.000 84.20337  ?  352 ALA C N   1 
ATOM 1877 C CA  . ALA B 2 31  ? -0.70855  37.67827 96.21666  1.000 80.27616  ?  352 ALA C CA  1 
ATOM 1878 C C   . ALA B 2 31  ? -1.85930  37.50695 97.19975  1.000 85.29475  ?  352 ALA C C   1 
ATOM 1879 O O   . ALA B 2 31  ? -2.91019  38.13376 97.07259  1.000 89.84680  ?  352 ALA C O   1 
ATOM 1880 C CB  . ALA B 2 31  ? -1.13646  38.50766 95.01239  1.000 77.69898  ?  352 ALA C CB  1 
ATOM 1881 N N   . TRP B 2 32  ? -1.66355  36.64896 98.19814  1.000 87.31769  ?  353 TRP C N   1 
ATOM 1882 C CA  . TRP B 2 32  ? -2.70983  36.37335 99.17354  1.000 93.21349  ?  353 TRP C CA  1 
ATOM 1883 C C   . TRP B 2 32  ? -2.98366  37.60472 100.02910 1.000 97.75157  ?  353 TRP C C   1 
ATOM 1884 O O   . TRP B 2 32  ? -2.05850  38.22122 100.56666 1.000 100.42960 ?  353 TRP C O   1 
ATOM 1885 C CB  . TRP B 2 32  ? -2.31094  35.18888 100.05386 1.000 92.96255  ?  353 TRP C CB  1 
ATOM 1886 C CG  . TRP B 2 32  ? -0.93129  35.30018 100.63800 1.000 99.45085  ?  353 TRP C CG  1 
ATOM 1887 C CD1 . TRP B 2 32  ? 0.24330   34.94305 100.04060 1.000 90.69285  ?  353 TRP C CD1 1 
ATOM 1888 C CD2 . TRP B 2 32  ? -0.58485  35.79485 101.93781 1.000 100.26081 ?  353 TRP C CD2 1 
ATOM 1889 N NE1 . TRP B 2 32  ? 1.29861   35.18862 100.88511 1.000 83.84602  ?  353 TRP C NE1 1 
ATOM 1890 C CE2 . TRP B 2 32  ? 0.81713   35.71124 102.05649 1.000 93.14859  ?  353 TRP C CE2 1 
ATOM 1891 C CE3 . TRP B 2 32  ? -1.32344  36.30172 103.01150 1.000 103.30576 ?  353 TRP C CE3 1 
ATOM 1892 C CZ2 . TRP B 2 32  ? 1.49462   36.11547 103.20507 1.000 99.83748  ?  353 TRP C CZ2 1 
ATOM 1893 C CZ3 . TRP B 2 32  ? -0.64867  36.70266 104.15083 1.000 112.52589 ?  353 TRP C CZ3 1 
ATOM 1894 C CH2 . TRP B 2 32  ? 0.74579   36.60710 104.23855 1.000 110.94091 ?  353 TRP C CH2 1 
ATOM 1895 N N   . ASN B 2 33  ? -4.25911  37.96287 100.15012 1.000 104.08045 ?  354 ASN C N   1 
ATOM 1896 C CA  . ASN B 2 33  ? -4.65421  39.11128 100.94837 1.000 106.99784 ?  354 ASN C CA  1 
ATOM 1897 C C   . ASN B 2 33  ? -4.60125  38.77623 102.43620 1.000 106.81512 ?  354 ASN C C   1 
ATOM 1898 O O   . ASN B 2 33  ? -4.58631  37.61044 102.84049 1.000 106.31343 ?  354 ASN C O   1 
ATOM 1899 C CB  . ASN B 2 33  ? -6.06009  39.57715 100.56662 1.000 98.42371  ?  354 ASN C CB  1 
ATOM 1900 C CG  . ASN B 2 33  ? -6.13750  40.09189 99.14271  1.000 114.65332 ?  354 ASN C CG  1 
ATOM 1901 O OD1 . ASN B 2 33  ? -5.18040  40.66823 98.62582  1.000 114.68123 ?  354 ASN C OD1 1 
ATOM 1902 N ND2 . ASN B 2 33  ? -7.28160  39.88624 98.50031  1.000 99.05033  ?  354 ASN C ND2 1 
ATOM 1903 N N   . ARG B 2 34  ? -4.57454  39.82593 103.25514 1.000 105.68492 ?  355 ARG C N   1 
ATOM 1904 C CA  . ARG B 2 34  ? -4.51642  39.68445 104.70569 1.000 108.96528 ?  355 ARG C CA  1 
ATOM 1905 C C   . ARG B 2 34  ? -5.43641  40.72263 105.32703 1.000 113.73879 ?  355 ARG C C   1 
ATOM 1906 O O   . ARG B 2 34  ? -5.20967  41.92613 105.17026 1.000 123.34233 ?  355 ARG C O   1 
ATOM 1907 C CB  . ARG B 2 34  ? -3.08296  39.85135 105.22014 1.000 96.99338  ?  355 ARG C CB  1 
ATOM 1908 C CG  . ARG B 2 34  ? -2.88074  39.41940 106.66297 1.000 100.26993 ?  355 ARG C CG  1 
ATOM 1909 C CD  . ARG B 2 34  ? -1.43173  39.59699 107.08810 1.000 116.82317 ?  355 ARG C CD  1 
ATOM 1910 N NE  . ARG B 2 34  ? -1.16870  39.02077 108.40358 1.000 121.15787 ?  355 ARG C NE  1 
ATOM 1911 C CZ  . ARG B 2 34  ? -0.73022  37.78166 108.60145 1.000 116.14340 ?  355 ARG C CZ  1 
ATOM 1912 N NH1 . ARG B 2 34  ? -0.50342  36.98337 107.56721 1.000 118.74324 ?  355 ARG C NH1 1 
ATOM 1913 N NH2 . ARG B 2 34  ? -0.51702  37.33984 109.83345 1.000 115.73519 ?  355 ARG C NH2 1 
ATOM 1914 N N   . LYS B 2 35  ? -6.46854  40.25965 106.02686 1.000 106.16235 ?  356 LYS C N   1 
ATOM 1915 C CA  . LYS B 2 35  ? -7.47207  41.12729 106.63068 1.000 109.94061 ?  356 LYS C CA  1 
ATOM 1916 C C   . LYS B 2 35  ? -7.26502  41.15512 108.13888 1.000 112.52528 ?  356 LYS C C   1 
ATOM 1917 O O   . LYS B 2 35  ? -7.40525  40.12575 108.80786 1.000 116.64095 ?  356 LYS C O   1 
ATOM 1918 C CB  . LYS B 2 35  ? -8.88301  40.64806 106.28910 1.000 115.70555 ?  356 LYS C CB  1 
ATOM 1919 C CG  . LYS B 2 35  ? -9.99137  41.54018 106.82516 1.000 129.02943 ?  356 LYS C CG  1 
ATOM 1920 C CD  . LYS B 2 35  ? -9.92214  42.93255 106.21861 1.000 128.50212 ?  356 LYS C CD  1 
ATOM 1921 C CE  . LYS B 2 35  ? -11.05534 43.81180 106.72237 1.000 101.22651 ?  356 LYS C CE  1 
ATOM 1922 N NZ  . LYS B 2 35  ? -11.01464 43.97791 108.20152 1.000 97.02095  ?  356 LYS C NZ  1 
ATOM 1923 N N   . ARG B 2 36  ? -6.93276  42.32982 108.66810 1.000 108.14000 ?  357 ARG C N   1 
ATOM 1924 C CA  . ARG B 2 36  ? -6.72784  42.51343 110.10390 1.000 109.38819 ?  357 ARG C CA  1 
ATOM 1925 C C   . ARG B 2 36  ? -8.08158  42.79776 110.74175 1.000 108.40354 ?  357 ARG C C   1 
ATOM 1926 O O   . ARG B 2 36  ? -8.62238  43.89875 110.61657 1.000 120.12697 ?  357 ARG C O   1 
ATOM 1927 C CB  . ARG B 2 36  ? -5.73608  43.64044 110.36891 1.000 116.17199 ?  357 ARG C CB  1 
ATOM 1928 C CG  . ARG B 2 36  ? -5.45698  43.89786 111.84093 1.000 107.14310 ?  357 ARG C CG  1 
ATOM 1929 C CD  . ARG B 2 36  ? -4.48050  45.05177 112.02260 1.000 123.56093 ?  357 ARG C CD  1 
ATOM 1930 N NE  . ARG B 2 36  ? -3.19803  44.79424 111.37250 1.000 150.68023 ?  357 ARG C NE  1 
ATOM 1931 C CZ  . ARG B 2 36  ? -2.14810  44.24746 111.97754 1.000 148.18429 ?  357 ARG C CZ  1 
ATOM 1932 N NH1 . ARG B 2 36  ? -1.02274  44.04751 111.30461 1.000 122.25300 ?  357 ARG C NH1 1 
ATOM 1933 N NH2 . ARG B 2 36  ? -2.22285  43.89625 113.25442 1.000 153.94352 ?  357 ARG C NH2 1 
ATOM 1934 N N   . ILE B 2 37  ? -8.62880  41.80381 111.43250 1.000 104.66048 ?  358 ILE C N   1 
ATOM 1935 C CA  . ILE B 2 37  ? -9.94072  41.90214 112.06181 1.000 108.58861 ?  358 ILE C CA  1 
ATOM 1936 C C   . ILE B 2 37  ? -9.72537  42.25409 113.52771 1.000 124.76895 ?  358 ILE C C   1 
ATOM 1937 O O   . ILE B 2 37  ? -9.23135  41.43304 114.30821 1.000 135.58509 ?  358 ILE C O   1 
ATOM 1938 C CB  . ILE B 2 37  ? -10.73902 40.60055 111.91220 1.000 92.56074  ?  358 ILE C CB  1 
ATOM 1939 C CG1 . ILE B 2 37  ? -10.67304 40.09881 110.46824 1.000 91.36528  ?  358 ILE C CG1 1 
ATOM 1940 C CG2 . ILE B 2 37  ? -12.18329 40.81184 112.33428 1.000 91.49189  ?  358 ILE C CG2 1 
ATOM 1941 C CD1 . ILE B 2 37  ? -11.35420 38.76473 110.25548 1.000 87.76490  ?  358 ILE C CD1 1 
ATOM 1942 N N   . SER B 2 38  ? -10.09401 43.47599 113.90601 1.000 120.57388 ?  359 SER C N   1 
ATOM 1943 C CA  . SER B 2 38  ? -9.94017  43.95330 115.27116 1.000 124.50938 ?  359 SER C CA  1 
ATOM 1944 C C   . SER B 2 38  ? -11.24075 44.58685 115.74169 1.000 134.50121 ?  359 SER C C   1 
ATOM 1945 O O   . SER B 2 38  ? -12.03151 45.08861 114.93726 1.000 131.89423 ?  359 SER C O   1 
ATOM 1946 C CB  . SER B 2 38  ? -8.79322  44.96767 115.38791 1.000 120.62617 ?  359 SER C CB  1 
ATOM 1947 O OG  . SER B 2 38  ? -7.55990  44.39306 114.99205 1.000 110.31783 ?  359 SER C OG  1 
ATOM 1948 N N   . ASN B 2 39  ? -11.44694 44.55892 117.05776 1.000 148.03011 ?  360 ASN C N   1 
ATOM 1949 C CA  . ASN B 2 39  ? -12.63442 45.11942 117.70194 1.000 141.71556 ?  360 ASN C CA  1 
ATOM 1950 C C   . ASN B 2 39  ? -13.90917 44.54352 117.08454 1.000 137.41146 ?  360 ASN C C   1 
ATOM 1951 O O   . ASN B 2 39  ? -14.73455 45.25249 116.50637 1.000 131.78770 ?  360 ASN C O   1 
ATOM 1952 C CB  . ASN B 2 39  ? -12.62801 46.64910 117.62605 1.000 134.86274 ?  360 ASN C CB  1 
ATOM 1953 C CG  . ASN B 2 39  ? -11.23587 47.23501 117.76034 1.000 137.21118 ?  360 ASN C CG  1 
ATOM 1954 O OD1 . ASN B 2 39  ? -10.63968 47.21143 118.83678 1.000 135.91999 ?  360 ASN C OD1 1 
ATOM 1955 N ND2 . ASN B 2 39  ? -10.71322 47.77291 116.66387 1.000 133.00480 ?  360 ASN C ND2 1 
ATOM 1956 N N   . CYS B 2 40  ? -14.05736 43.22799 117.21935 1.000 135.69780 ?  361 CYS C N   1 
ATOM 1957 C CA  . CYS B 2 40  ? -15.13507 42.49947 116.56968 1.000 143.21927 ?  361 CYS C CA  1 
ATOM 1958 C C   . CYS B 2 40  ? -15.79706 41.54295 117.55041 1.000 140.25859 ?  361 CYS C C   1 
ATOM 1959 O O   . CYS B 2 40  ? -15.18322 41.09757 118.52416 1.000 131.69453 ?  361 CYS C O   1 
ATOM 1960 C CB  . CYS B 2 40  ? -14.61857 41.71750 115.35133 1.000 125.13014 ?  361 CYS C CB  1 
ATOM 1961 S SG  . CYS B 2 40  ? -15.86583 40.71544 114.50879 1.000 118.95947 ?  361 CYS C SG  1 
ATOM 1962 N N   . VAL B 2 41  ? -17.06490 41.23857 117.28168 1.000 121.02224 ?  362 VAL C N   1 
ATOM 1963 C CA  . VAL B 2 41  ? -17.79844 40.20704 118.00712 1.000 117.58182 ?  362 VAL C CA  1 
ATOM 1964 C C   . VAL B 2 41  ? -17.62144 38.91222 117.22052 1.000 134.39552 ?  362 VAL C C   1 
ATOM 1965 O O   . VAL B 2 41  ? -18.34180 38.65024 116.25575 1.000 136.58204 ?  362 VAL C O   1 
ATOM 1966 C CB  . VAL B 2 41  ? -19.27297 40.57230 118.18430 1.000 122.53216 ?  362 VAL C CB  1 
ATOM 1967 C CG1 . VAL B 2 41  ? -19.49738 41.21892 119.54126 1.000 116.58302 ?  362 VAL C CG1 1 
ATOM 1968 C CG2 . VAL B 2 41  ? -19.72545 41.50505 117.06831 1.000 110.81336 ?  362 VAL C CG2 1 
ATOM 1969 N N   . ALA B 2 42  ? -16.65171 38.10076 117.63448 1.000 152.09281 ?  363 ALA C N   1 
ATOM 1970 C CA  . ALA B 2 42  ? -16.28281 36.90321 116.89102 1.000 159.11156 ?  363 ALA C CA  1 
ATOM 1971 C C   . ALA B 2 42  ? -17.20913 35.75121 117.25916 1.000 170.63375 ?  363 ALA C C   1 
ATOM 1972 O O   . ALA B 2 42  ? -17.27966 35.34886 118.42571 1.000 160.89812 ?  363 ALA C O   1 
ATOM 1973 C CB  . ALA B 2 42  ? -14.82755 36.53348 117.16767 1.000 150.21577 ?  363 ALA C CB  1 
ATOM 1974 N N   . ASP B 2 43  ? -17.91711 35.22403 116.26407 1.000 174.31381 ?  364 ASP C N   1 
ATOM 1975 C CA  . ASP B 2 43  ? -18.75553 34.03803 116.41487 1.000 168.26398 ?  364 ASP C CA  1 
ATOM 1976 C C   . ASP B 2 43  ? -18.07295 32.90115 115.65842 1.000 182.37207 ?  364 ASP C C   1 
ATOM 1977 O O   . ASP B 2 43  ? -18.39658 32.60565 114.50771 1.000 190.51166 ?  364 ASP C O   1 
ATOM 1978 C CB  . ASP B 2 43  ? -20.18272 34.30138 115.90338 1.000 153.59340 ?  364 ASP C CB  1 
ATOM 1979 C CG  . ASP B 2 43  ? -20.20177 35.00178 114.55729 1.000 166.56882 ?  364 ASP C CG  1 
ATOM 1980 O OD1 . ASP B 2 43  ? -19.11465 35.34526 114.04673 1.000 172.05484 ?  364 ASP C OD1 1 
ATOM 1981 O OD2 . ASP B 2 43  ? -21.30518 35.20781 114.00971 1.000 165.44161 -1 364 ASP C OD2 1 
ATOM 1982 N N   . TYR B 2 44  ? -17.11039 32.25836 116.32565 1.000 186.17593 ?  365 TYR C N   1 
ATOM 1983 C CA  . TYR B 2 44  ? -16.30463 31.22987 115.67705 1.000 175.03311 ?  365 TYR C CA  1 
ATOM 1984 C C   . TYR B 2 44  ? -17.13533 30.03826 115.22107 1.000 170.30630 ?  365 TYR C C   1 
ATOM 1985 O O   . TYR B 2 44  ? -16.69850 29.29749 114.33383 1.000 162.66238 ?  365 TYR C O   1 
ATOM 1986 C CB  . TYR B 2 44  ? -15.19687 30.75760 116.62100 1.000 164.46147 ?  365 TYR C CB  1 
ATOM 1987 C CG  . TYR B 2 44  ? -14.35505 31.87696 117.19194 1.000 167.27836 ?  365 TYR C CG  1 
ATOM 1988 C CD1 . TYR B 2 44  ? -13.35542 32.47535 116.43644 1.000 139.83533 ?  365 TYR C CD1 1 
ATOM 1989 C CD2 . TYR B 2 44  ? -14.55590 32.33050 118.48947 1.000 174.54346 ?  365 TYR C CD2 1 
ATOM 1990 C CE1 . TYR B 2 44  ? -12.58255 33.49800 116.95539 1.000 154.79711 ?  365 TYR C CE1 1 
ATOM 1991 C CE2 . TYR B 2 44  ? -13.78703 33.35177 119.01735 1.000 177.62645 ?  365 TYR C CE2 1 
ATOM 1992 C CZ  . TYR B 2 44  ? -12.80134 33.93089 118.24616 1.000 171.55304 ?  365 TYR C CZ  1 
ATOM 1993 O OH  . TYR B 2 44  ? -12.03393 34.94804 118.76633 1.000 163.11450 ?  365 TYR C OH  1 
ATOM 1994 N N   . SER B 2 45  ? -18.31951 29.83806 115.79942 1.000 162.04327 ?  366 SER C N   1 
ATOM 1995 C CA  . SER B 2 45  ? -19.18111 28.71589 115.45597 1.000 161.90033 ?  366 SER C CA  1 
ATOM 1996 C C   . SER B 2 45  ? -20.27782 29.09968 114.46801 1.000 172.85499 ?  366 SER C C   1 
ATOM 1997 O O   . SER B 2 45  ? -21.23949 28.34337 114.29661 1.000 161.40945 ?  366 SER C O   1 
ATOM 1998 C CB  . SER B 2 45  ? -19.79696 28.11814 116.72204 1.000 138.85794 ?  366 SER C CB  1 
ATOM 1999 O OG  . SER B 2 45  ? -20.52915 29.09351 117.44297 1.000 133.55411 ?  366 SER C OG  1 
ATOM 2000 N N   . VAL B 2 46  ? -20.15649 30.25858 113.81659 1.000 186.91534 ?  367 VAL C N   1 
ATOM 2001 C CA  . VAL B 2 46  ? -21.16545 30.67018 112.84523 1.000 186.65135 ?  367 VAL C CA  1 
ATOM 2002 C C   . VAL B 2 46  ? -21.00366 29.94770 111.51302 1.000 182.30799 ?  367 VAL C C   1 
ATOM 2003 O O   . VAL B 2 46  ? -21.95559 29.89599 110.72359 1.000 181.13756 ?  367 VAL C O   1 
ATOM 2004 C CB  . VAL B 2 46  ? -21.12791 32.19454 112.63365 1.000 187.46152 ?  367 VAL C CB  1 
ATOM 2005 C CG1 . VAL B 2 46  ? -19.99233 32.58516 111.69380 1.000 179.15705 ?  367 VAL C CG1 1 
ATOM 2006 C CG2 . VAL B 2 46  ? -22.46738 32.69982 112.11310 1.000 186.18771 ?  367 VAL C CG2 1 
ATOM 2007 N N   . LEU B 2 47  ? -19.82870 29.37809 111.24290 1.000 154.70137 ?  368 LEU C N   1 
ATOM 2008 C CA  . LEU B 2 47  ? -19.58383 28.66363 110.00115 1.000 141.43442 ?  368 LEU C CA  1 
ATOM 2009 C C   . LEU B 2 47  ? -19.28950 27.18363 110.19188 1.000 148.39270 ?  368 LEU C C   1 
ATOM 2010 O O   . LEU B 2 47  ? -19.19621 26.46029 109.19361 1.000 151.70855 ?  368 LEU C O   1 
ATOM 2011 C CB  . LEU B 2 47  ? -18.42187 29.30998 109.23086 1.000 130.29724 ?  368 LEU C CB  1 
ATOM 2012 C CG  . LEU B 2 47  ? -18.67427 30.72449 108.70618 1.000 136.14603 ?  368 LEU C CG  1 
ATOM 2013 C CD1 . LEU B 2 47  ? -17.42397 31.27816 108.04275 1.000 121.09114 ?  368 LEU C CD1 1 
ATOM 2014 C CD2 . LEU B 2 47  ? -19.84900 30.73857 107.73877 1.000 130.55296 ?  368 LEU C CD2 1 
ATOM 2015 N N   . TYR B 2 48  ? -19.13571 26.71146 111.43179 1.000 186.54496 ?  369 TYR C N   1 
ATOM 2016 C CA  . TYR B 2 48  ? -18.95897 25.28039 111.65385 1.000 185.88176 ?  369 TYR C CA  1 
ATOM 2017 C C   . TYR B 2 48  ? -20.22082 24.50151 111.31060 1.000 192.03838 ?  369 TYR C C   1 
ATOM 2018 O O   . TYR B 2 48  ? -20.13611 23.34808 110.87365 1.000 189.00228 ?  369 TYR C O   1 
ATOM 2019 C CB  . TYR B 2 48  ? -18.54851 25.01336 113.10155 1.000 191.44734 ?  369 TYR C CB  1 
ATOM 2020 C CG  . TYR B 2 48  ? -17.05769 25.08340 113.33481 1.000 199.24561 ?  369 TYR C CG  1 
ATOM 2021 C CD1 . TYR B 2 48  ? -16.45868 26.25237 113.78229 1.000 204.25762 ?  369 TYR C CD1 1 
ATOM 2022 C CD2 . TYR B 2 48  ? -16.24834 23.97891 113.10400 1.000 193.55050 ?  369 TYR C CD2 1 
ATOM 2023 C CE1 . TYR B 2 48  ? -15.09518 26.31998 113.99577 1.000 212.54577 ?  369 TYR C CE1 1 
ATOM 2024 C CE2 . TYR B 2 48  ? -14.88420 24.03622 113.31431 1.000 196.52649 ?  369 TYR C CE2 1 
ATOM 2025 C CZ  . TYR B 2 48  ? -14.31318 25.20898 113.76135 1.000 207.52712 ?  369 TYR C CZ  1 
ATOM 2026 O OH  . TYR B 2 48  ? -12.95489 25.27351 113.97035 1.000 219.59461 ?  369 TYR C OH  1 
ATOM 2027 N N   . ASN B 2 49  ? -21.39360 25.10828 111.50078 1.000 185.61608 ?  370 ASN C N   1 
ATOM 2028 C CA  . ASN B 2 49  ? -22.64225 24.46938 111.10804 1.000 188.27654 ?  370 ASN C CA  1 
ATOM 2029 C C   . ASN B 2 49  ? -22.85102 24.47233 109.60047 1.000 189.33758 ?  370 ASN C C   1 
ATOM 2030 O O   . ASN B 2 49  ? -23.72815 23.75141 109.11305 1.000 188.26236 ?  370 ASN C O   1 
ATOM 2031 C CB  . ASN B 2 49  ? -23.82294 25.15647 111.79623 1.000 194.41359 ?  370 ASN C CB  1 
ATOM 2032 C CG  . ASN B 2 49  ? -23.74142 25.07792 113.30763 1.000 207.16635 ?  370 ASN C CG  1 
ATOM 2033 O OD1 . ASN B 2 49  ? -22.66738 24.87236 113.87285 1.000 201.63827 ?  370 ASN C OD1 1 
ATOM 2034 N ND2 . ASN B 2 49  ? -24.88024 25.24049 113.97113 1.000 213.64531 ?  370 ASN C ND2 1 
ATOM 2035 N N   . SER B 2 50  ? -22.07518 25.25821 108.85743 1.000 182.31677 ?  371 SER C N   1 
ATOM 2036 C CA  . SER B 2 50  ? -22.16954 25.28775 107.40213 1.000 174.35412 ?  371 SER C CA  1 
ATOM 2037 C C   . SER B 2 50  ? -21.47262 24.05433 106.84133 1.000 169.20483 ?  371 SER C C   1 
ATOM 2038 O O   . SER B 2 50  ? -20.24386 23.94338 106.90476 1.000 157.16206 ?  371 SER C O   1 
ATOM 2039 C CB  . SER B 2 50  ? -21.54880 26.56893 106.85278 1.000 145.49705 ?  371 SER C CB  1 
ATOM 2040 O OG  . SER B 2 50  ? -22.18767 27.71612 107.38525 1.000 140.33207 ?  371 SER C OG  1 
ATOM 2041 N N   . ALA B 2 51  ? -22.25340 23.12567 106.29163 1.000 167.91097 ?  372 ALA C N   1 
ATOM 2042 C CA  . ALA B 2 51  ? -21.70745 21.89906 105.72492 1.000 155.42538 ?  372 ALA C CA  1 
ATOM 2043 C C   . ALA B 2 51  ? -21.06536 22.10664 104.35946 1.000 150.85629 ?  372 ALA C C   1 
ATOM 2044 O O   . ALA B 2 51  ? -20.65320 21.12466 103.73230 1.000 137.38288 ?  372 ALA C O   1 
ATOM 2045 C CB  . ALA B 2 51  ? -22.80196 20.83365 105.62269 1.000 132.30453 ?  372 ALA C CB  1 
ATOM 2046 N N   . SER B 2 52  ? -20.96604 23.34821 103.88760 1.000 155.80201 ?  373 SER C N   1 
ATOM 2047 C CA  . SER B 2 52  ? -20.36247 23.64086 102.59441 1.000 149.15685 ?  373 SER C CA  1 
ATOM 2048 C C   . SER B 2 52  ? -18.84174 23.56709 102.61560 1.000 150.22778 ?  373 SER C C   1 
ATOM 2049 O O   . SER B 2 52  ? -18.21788 23.71448 101.55918 1.000 153.19986 ?  373 SER C O   1 
ATOM 2050 C CB  . SER B 2 52  ? -20.80214 25.02635 102.11390 1.000 136.98440 ?  373 SER C CB  1 
ATOM 2051 O OG  . SER B 2 52  ? -20.46061 26.02452 103.06000 1.000 125.26221 ?  373 SER C OG  1 
ATOM 2052 N N   . PHE B 2 53  ? -18.23390 23.34576 103.77785 1.000 145.54726 ?  374 PHE C N   1 
ATOM 2053 C CA  . PHE B 2 53  ? -16.78374 23.26964 103.89626 1.000 134.96877 ?  374 PHE C CA  1 
ATOM 2054 C C   . PHE B 2 53  ? -16.33622 21.82323 103.72333 1.000 142.25215 ?  374 PHE C C   1 
ATOM 2055 O O   . PHE B 2 53  ? -16.80090 20.93311 104.44426 1.000 148.17987 ?  374 PHE C O   1 
ATOM 2056 C CB  . PHE B 2 53  ? -16.32267 23.81802 105.24586 1.000 126.82850 ?  374 PHE C CB  1 
ATOM 2057 C CG  . PHE B 2 53  ? -16.55673 25.29176 105.41394 1.000 130.50736 ?  374 PHE C CG  1 
ATOM 2058 C CD1 . PHE B 2 53  ? -16.58756 26.13258 104.31355 1.000 136.36852 ?  374 PHE C CD1 1 
ATOM 2059 C CD2 . PHE B 2 53  ? -16.74635 25.83654 106.67265 1.000 135.63255 ?  374 PHE C CD2 1 
ATOM 2060 C CE1 . PHE B 2 53  ? -16.80227 27.48947 104.46581 1.000 130.80342 ?  374 PHE C CE1 1 
ATOM 2061 C CE2 . PHE B 2 53  ? -16.96143 27.19179 106.83120 1.000 134.03212 ?  374 PHE C CE2 1 
ATOM 2062 C CZ  . PHE B 2 53  ? -16.98965 28.01943 105.72653 1.000 133.44413 ?  374 PHE C CZ  1 
ATOM 2063 N N   . SER B 2 54  ? -15.43674 21.59214 102.76756 1.000 129.64023 ?  375 SER C N   1 
ATOM 2064 C CA  . SER B 2 54  ? -14.89213 20.26023 102.53842 1.000 117.26819 ?  375 SER C CA  1 
ATOM 2065 C C   . SER B 2 54  ? -13.62958 19.99810 103.34606 1.000 114.46789 ?  375 SER C C   1 
ATOM 2066 O O   . SER B 2 54  ? -13.36103 18.84573 103.70536 1.000 122.78161 ?  375 SER C O   1 
ATOM 2067 C CB  . SER B 2 54  ? -14.59737 20.05827 101.04932 1.000 105.57979 ?  375 SER C CB  1 
ATOM 2068 O OG  . SER B 2 54  ? -13.64700 21.00122 100.58539 1.000 112.83988 ?  375 SER C OG  1 
ATOM 2069 N N   . THR B 2 55  ? -12.85090 21.03757 103.63840 1.000 122.32279 ?  376 THR C N   1 
ATOM 2070 C CA  . THR B 2 55  ? -11.63730 20.91762 104.43461 1.000 127.39189 ?  376 THR C CA  1 
ATOM 2071 C C   . THR B 2 55  ? -11.70642 21.90800 105.58639 1.000 125.87616 ?  376 THR C C   1 
ATOM 2072 O O   . THR B 2 55  ? -11.90908 23.10664 105.36712 1.000 112.69140 ?  376 THR C O   1 
ATOM 2073 C CB  . THR B 2 55  ? -10.38425 21.17353 103.58910 1.000 119.08484 ?  376 THR C CB  1 
ATOM 2074 O OG1 . THR B 2 55  ? -10.35281 20.25719 102.48759 1.000 120.40705 ?  376 THR C OG1 1 
ATOM 2075 C CG2 . THR B 2 55  ? -9.12876  20.98976 104.42898 1.000 104.32521 ?  376 THR C CG2 1 
ATOM 2076 N N   . PHE B 2 56  ? -11.53939 21.40527 106.81008 1.000 130.90815 ?  377 PHE C N   1 
ATOM 2077 C CA  . PHE B 2 56  ? -11.62944 22.24272 108.00555 1.000 120.74620 ?  377 PHE C CA  1 
ATOM 2078 C C   . PHE B 2 56  ? -10.77910 21.57767 109.08469 1.000 128.08326 ?  377 PHE C C   1 
ATOM 2079 O O   . PHE B 2 56  ? -11.22874 20.62808 109.73300 1.000 135.39800 ?  377 PHE C O   1 
ATOM 2080 C CB  . PHE B 2 56  ? -13.07789 22.40624 108.44797 1.000 115.58237 ?  377 PHE C CB  1 
ATOM 2081 C CG  . PHE B 2 56  ? -13.34805 23.67808 109.20393 1.000 129.00079 ?  377 PHE C CG  1 
ATOM 2082 C CD1 . PHE B 2 56  ? -12.35750 24.28097 109.96182 1.000 131.09067 ?  377 PHE C CD1 1 
ATOM 2083 C CD2 . PHE B 2 56  ? -14.59808 24.27277 109.15096 1.000 142.16567 ?  377 PHE C CD2 1 
ATOM 2084 C CE1 . PHE B 2 56  ? -12.61021 25.44925 110.65500 1.000 148.63639 ?  377 PHE C CE1 1 
ATOM 2085 C CE2 . PHE B 2 56  ? -14.85635 25.44147 109.84055 1.000 149.76100 ?  377 PHE C CE2 1 
ATOM 2086 C CZ  . PHE B 2 56  ? -13.86128 26.03054 110.59258 1.000 146.53569 ?  377 PHE C CZ  1 
ATOM 2087 N N   . LYS B 2 57  ? -9.55878  22.07936 109.26987 1.000 124.13490 ?  378 LYS C N   1 
ATOM 2088 C CA  . LYS B 2 57  ? -8.60649  21.50564 110.21656 1.000 126.50010 ?  378 LYS C CA  1 
ATOM 2089 C C   . LYS B 2 57  ? -8.00760  22.62161 111.06169 1.000 116.40224 ?  378 LYS C C   1 
ATOM 2090 O O   . LYS B 2 57  ? -7.29847  23.48820 110.53981 1.000 104.76867 ?  378 LYS C O   1 
ATOM 2091 C CB  . LYS B 2 57  ? -7.50636  20.72960 109.49005 1.000 113.91386 ?  378 LYS C CB  1 
ATOM 2092 C CG  . LYS B 2 57  ? -7.99766  19.51284 108.72329 1.000 111.41284 ?  378 LYS C CG  1 
ATOM 2093 C CD  . LYS B 2 57  ? -6.84096  18.76386 108.08120 1.000 111.88686 ?  378 LYS C CD  1 
ATOM 2094 C CE  . LYS B 2 57  ? -7.32358  17.51931 107.35428 1.000 111.83025 ?  378 LYS C CE  1 
ATOM 2095 N NZ  . LYS B 2 57  ? -6.19724  16.76100 106.74321 1.000 106.83274 ?  378 LYS C NZ  1 
ATOM 2096 N N   . CYS B 2 58  ? -8.29083  22.59870 112.36048 1.000 129.07813 ?  379 CYS C N   1 
ATOM 2097 C CA  . CYS B 2 58  ? -7.65278  23.49816 113.30887 1.000 129.29119 ?  379 CYS C CA  1 
ATOM 2098 C C   . CYS B 2 58  ? -6.43001  22.82236 113.91634 1.000 128.25052 ?  379 CYS C C   1 
ATOM 2099 O O   . CYS B 2 58  ? -6.39675  21.60216 114.09727 1.000 132.85181 ?  379 CYS C O   1 
ATOM 2100 C CB  . CYS B 2 58  ? -8.62701  23.91018 114.41328 1.000 141.43633 ?  379 CYS C CB  1 
ATOM 2101 S SG  . CYS B 2 58  ? -10.07435 24.83105 113.84142 1.000 179.38939 ?  379 CYS C SG  1 
ATOM 2102 N N   . TYR B 2 59  ? -5.42028  23.62943 114.23377 1.000 123.84734 ?  380 TYR C N   1 
ATOM 2103 C CA  . TYR B 2 59  ? -4.13765  23.10796 114.68970 1.000 125.33444 ?  380 TYR C CA  1 
ATOM 2104 C C   . TYR B 2 59  ? -3.77888  23.54951 116.09909 1.000 137.82628 ?  380 TYR C C   1 
ATOM 2105 O O   . TYR B 2 59  ? -3.48182  22.70248 116.94998 1.000 153.73220 ?  380 TYR C O   1 
ATOM 2106 C CB  . TYR B 2 59  ? -3.02719  23.52459 113.71025 1.000 114.56124 ?  380 TYR C CB  1 
ATOM 2107 C CG  . TYR B 2 59  ? -3.12171  22.85277 112.35793 1.000 115.71333 ?  380 TYR C CG  1 
ATOM 2108 C CD1 . TYR B 2 59  ? -3.93860  23.36716 111.35918 1.000 113.16202 ?  380 TYR C CD1 1 
ATOM 2109 C CD2 . TYR B 2 59  ? -2.39333  21.70329 112.08043 1.000 120.75935 ?  380 TYR C CD2 1 
ATOM 2110 C CE1 . TYR B 2 59  ? -4.02823  22.75471 110.12263 1.000 116.37413 ?  380 TYR C CE1 1 
ATOM 2111 C CE2 . TYR B 2 59  ? -2.47597  21.08442 110.84714 1.000 113.18549 ?  380 TYR C CE2 1 
ATOM 2112 C CZ  . TYR B 2 59  ? -3.29465  21.61409 109.87233 1.000 114.68666 ?  380 TYR C CZ  1 
ATOM 2113 O OH  . TYR B 2 59  ? -3.37983  21.00090 108.64325 1.000 105.43669 ?  380 TYR C OH  1 
ATOM 2114 N N   . GLY B 2 60  ? -3.79773  24.84948 116.37623 1.000 132.08504 ?  381 GLY C N   1 
ATOM 2115 C CA  . GLY B 2 60  ? -3.30695  25.36090 117.63703 1.000 132.30944 ?  381 GLY C CA  1 
ATOM 2116 C C   . GLY B 2 60  ? -4.31097  25.49598 118.75759 1.000 133.42552 ?  381 GLY C C   1 
ATOM 2117 O O   . GLY B 2 60  ? -3.92603  25.88105 119.86616 1.000 121.63723 ?  381 GLY C O   1 
ATOM 2118 N N   . VAL B 2 61  ? -5.58641  25.19101 118.52049 1.000 132.88619 ?  382 VAL C N   1 
ATOM 2119 C CA  . VAL B 2 61  ? -6.61180  25.35421 119.54424 1.000 138.36404 ?  382 VAL C CA  1 
ATOM 2120 C C   . VAL B 2 61  ? -7.78478  24.45363 119.18990 1.000 136.99856 ?  382 VAL C C   1 
ATOM 2121 O O   . VAL B 2 61  ? -8.01572  24.14242 118.01826 1.000 128.01822 ?  382 VAL C O   1 
ATOM 2122 C CB  . VAL B 2 61  ? -7.03762  26.84031 119.67255 1.000 137.42250 ?  382 VAL C CB  1 
ATOM 2123 C CG1 . VAL B 2 61  ? -7.78472  27.29573 118.42673 1.000 121.54364 ?  382 VAL C CG1 1 
ATOM 2124 C CG2 . VAL B 2 61  ? -7.86873  27.06510 120.93099 1.000 122.92420 ?  382 VAL C CG2 1 
ATOM 2125 N N   . SER B 2 62  ? -8.51883  24.02203 120.21204 1.000 152.90927 ?  383 SER C N   1 
ATOM 2126 C CA  . SER B 2 62  ? -9.70447  23.21164 119.98361 1.000 147.47460 ?  383 SER C CA  1 
ATOM 2127 C C   . SER B 2 62  ? -10.79887 24.05936 119.33770 1.000 141.66442 ?  383 SER C C   1 
ATOM 2128 O O   . SER B 2 62  ? -10.95958 25.23515 119.68051 1.000 140.13638 ?  383 SER C O   1 
ATOM 2129 C CB  . SER B 2 62  ? -10.20844 22.61317 121.29634 1.000 140.65202 ?  383 SER C CB  1 
ATOM 2130 O OG  . SER B 2 62  ? -10.49863 23.62757 122.24152 1.000 136.58397 ?  383 SER C OG  1 
ATOM 2131 N N   . PRO B 2 63  ? -11.56527 23.49522 118.40342 1.000 142.74093 ?  384 PRO C N   1 
ATOM 2132 C CA  . PRO B 2 63  ? -12.56314 24.29777 117.68205 1.000 141.70164 ?  384 PRO C CA  1 
ATOM 2133 C C   . PRO B 2 63  ? -13.76493 24.68226 118.53191 1.000 138.80531 ?  384 PRO C C   1 
ATOM 2134 O O   . PRO B 2 63  ? -14.19726 25.83926 118.51625 1.000 131.74206 ?  384 PRO C O   1 
ATOM 2135 C CB  . PRO B 2 63  ? -12.97171 23.38031 116.52260 1.000 138.49114 ?  384 PRO C CB  1 
ATOM 2136 C CG  . PRO B 2 63  ? -12.70924 22.00082 117.02484 1.000 131.97328 ?  384 PRO C CG  1 
ATOM 2137 C CD  . PRO B 2 63  ? -11.50179 22.10765 117.91180 1.000 130.76408 ?  384 PRO C CD  1 
ATOM 2138 N N   . THR B 2 64  ? -14.31178 23.72082 119.27911 1.000 142.28070 ?  385 THR C N   1 
ATOM 2139 C CA  . THR B 2 64  ? -15.54870 23.95932 120.01379 1.000 141.20170 ?  385 THR C CA  1 
ATOM 2140 C C   . THR B 2 64  ? -15.35487 24.87112 121.21897 1.000 145.25856 ?  385 THR C C   1 
ATOM 2141 O O   . THR B 2 64  ? -16.33306 25.45328 121.69953 1.000 141.05078 ?  385 THR C O   1 
ATOM 2142 C CB  . THR B 2 64  ? -16.15740 22.63000 120.46528 1.000 139.83498 ?  385 THR C CB  1 
ATOM 2143 O OG1 . THR B 2 64  ? -17.33614 22.88021 121.24097 1.000 163.83005 ?  385 THR C OG1 1 
ATOM 2144 C CG2 . THR B 2 64  ? -15.16017 21.84191 121.30273 1.000 126.42670 ?  385 THR C CG2 1 
ATOM 2145 N N   . LYS B 2 65  ? -14.12575 25.01302 121.71679 1.000 143.55667 ?  386 LYS C N   1 
ATOM 2146 C CA  . LYS B 2 65  ? -13.84607 25.83323 122.88923 1.000 139.18735 ?  386 LYS C CA  1 
ATOM 2147 C C   . LYS B 2 65  ? -13.24720 27.18871 122.52555 1.000 140.74041 ?  386 LYS C C   1 
ATOM 2148 O O   . LYS B 2 65  ? -12.51348 27.77860 123.32613 1.000 136.34321 ?  386 LYS C O   1 
ATOM 2149 C CB  . LYS B 2 65  ? -12.92817 25.08257 123.85396 1.000 130.59509 ?  386 LYS C CB  1 
ATOM 2150 C CG  . LYS B 2 65  ? -13.66934 24.17534 124.82543 1.000 132.33020 ?  386 LYS C CG  1 
ATOM 2151 C CD  . LYS B 2 65  ? -12.71077 23.32693 125.64493 1.000 122.12775 ?  386 LYS C CD  1 
ATOM 2152 C CE  . LYS B 2 65  ? -12.14910 22.18089 124.82093 1.000 110.18005 ?  386 LYS C CE  1 
ATOM 2153 N NZ  . LYS B 2 65  ? -13.22432 21.25465 124.36792 1.000 112.67321 ?  386 LYS C NZ  1 
ATOM 2154 N N   . LEU B 2 66  ? -13.54863 27.69724 121.32945 1.000 141.97973 ?  387 LEU C N   1 
ATOM 2155 C CA  . LEU B 2 66  ? -13.11201 29.03447 120.94844 1.000 147.86019 ?  387 LEU C CA  1 
ATOM 2156 C C   . LEU B 2 66  ? -14.06248 30.12068 121.43139 1.000 152.75098 ?  387 LEU C C   1 
ATOM 2157 O O   . LEU B 2 66  ? -13.64180 31.27362 121.57742 1.000 157.74939 ?  387 LEU C O   1 
ATOM 2158 C CB  . LEU B 2 66  ? -12.95933 29.13046 119.42867 1.000 143.73003 ?  387 LEU C CB  1 
ATOM 2159 C CG  . LEU B 2 66  ? -11.61900 28.68266 118.84631 1.000 137.58397 ?  387 LEU C CG  1 
ATOM 2160 C CD1 . LEU B 2 66  ? -11.65029 28.73904 117.32789 1.000 126.28168 ?  387 LEU C CD1 1 
ATOM 2161 C CD2 . LEU B 2 66  ? -10.49670 29.54959 119.39305 1.000 135.84533 ?  387 LEU C CD2 1 
ATOM 2162 N N   . ASN B 2 67  ? -15.32231 29.78147 121.68309 1.000 148.56516 ?  388 ASN C N   1 
ATOM 2163 C CA  . ASN B 2 67  ? -16.31461 30.75924 122.11089 1.000 138.77521 ?  388 ASN C CA  1 
ATOM 2164 C C   . ASN B 2 67  ? -16.05101 31.22454 123.53950 1.000 121.06266 ?  388 ASN C C   1 
ATOM 2165 O O   . ASN B 2 67  ? -16.13881 32.41481 123.84129 1.000 114.16114 ?  388 ASN C O   1 
ATOM 2166 C CB  . ASN B 2 67  ? -17.72203 30.17050 121.99942 1.000 123.31211 ?  388 ASN C CB  1 
ATOM 2167 C CG  . ASN B 2 67  ? -17.95245 29.45924 120.67949 1.000 124.18031 ?  388 ASN C CG  1 
ATOM 2168 O OD1 . ASN B 2 67  ? -18.28220 30.08517 119.67223 1.000 120.27118 ?  388 ASN C OD1 1 
ATOM 2169 N ND2 . ASN B 2 67  ? -17.77992 28.14213 120.67946 1.000 113.39674 ?  388 ASN C ND2 1 
ATOM 2170 N N   . ASN B 2 73  ? -5.33413  40.20581 118.12946 1.000 148.14654 ?  394 ASN C N   1 
ATOM 2171 C CA  . ASN B 2 73  ? -5.85744  40.36465 116.77746 1.000 143.07986 ?  394 ASN C CA  1 
ATOM 2172 C C   . ASN B 2 73  ? -6.07044  39.01509 116.10177 1.000 132.16116 ?  394 ASN C C   1 
ATOM 2173 O O   . ASN B 2 73  ? -5.47050  38.01273 116.48988 1.000 135.23723 ?  394 ASN C O   1 
ATOM 2174 C CB  . ASN B 2 73  ? -4.91547  41.22620 115.93364 1.000 144.40126 ?  394 ASN C CB  1 
ATOM 2175 C CG  . ASN B 2 73  ? -4.84439  42.65927 116.41922 1.000 151.27349 ?  394 ASN C CG  1 
ATOM 2176 O OD1 . ASN B 2 73  ? -5.80965  43.18882 116.96973 1.000 154.97389 ?  394 ASN C OD1 1 
ATOM 2177 N ND2 . ASN B 2 73  ? -3.69757  43.29690 116.21512 1.000 143.23044 ?  394 ASN C ND2 1 
ATOM 2178 N N   . VAL B 2 74  ? -6.93374  38.99929 115.08880 1.000 130.18204 ?  395 VAL C N   1 
ATOM 2179 C CA  . VAL B 2 74  ? -7.22227  37.80420 114.30407 1.000 132.73795 ?  395 VAL C CA  1 
ATOM 2180 C C   . VAL B 2 74  ? -7.11637  38.17702 112.83251 1.000 121.50645 ?  395 VAL C C   1 
ATOM 2181 O O   . VAL B 2 74  ? -7.80961  39.09105 112.36980 1.000 116.64964 ?  395 VAL C O   1 
ATOM 2182 C CB  . VAL B 2 74  ? -8.61264  37.22473 114.61663 1.000 123.85411 ?  395 VAL C CB  1 
ATOM 2183 C CG1 . VAL B 2 74  ? -8.90683  36.03660 113.71336 1.000 106.34903 ?  395 VAL C CG1 1 
ATOM 2184 C CG2 . VAL B 2 74  ? -8.70710  36.82097 116.08119 1.000 131.00582 ?  395 VAL C CG2 1 
ATOM 2185 N N   . TYR B 2 75  ? -6.25369  37.47722 112.10176 1.000 125.16584 ?  396 TYR C N   1 
ATOM 2186 C CA  . TYR B 2 75  ? -6.03874  37.72746 110.68539 1.000 108.02389 ?  396 TYR C CA  1 
ATOM 2187 C C   . TYR B 2 75  ? -6.70081  36.63854 109.85170 1.000 102.19989 ?  396 TYR C C   1 
ATOM 2188 O O   . TYR B 2 75  ? -6.85444  35.49746 110.29667 1.000 113.48535 ?  396 TYR C O   1 
ATOM 2189 C CB  . TYR B 2 75  ? -4.54464  37.79622 110.35658 1.000 104.51326 ?  396 TYR C CB  1 
ATOM 2190 C CG  . TYR B 2 75  ? -3.78511  38.80162 111.18934 1.000 113.91474 ?  396 TYR C CG  1 
ATOM 2191 C CD1 . TYR B 2 75  ? -3.87722  40.16162 110.92606 1.000 115.83302 ?  396 TYR C CD1 1 
ATOM 2192 C CD2 . TYR B 2 75  ? -2.97393  38.39061 112.23834 1.000 115.50636 ?  396 TYR C CD2 1 
ATOM 2193 C CE1 . TYR B 2 75  ? -3.18449  41.08427 111.68601 1.000 126.22601 ?  396 TYR C CE1 1 
ATOM 2194 C CE2 . TYR B 2 75  ? -2.27665  39.30540 113.00327 1.000 116.57898 ?  396 TYR C CE2 1 
ATOM 2195 C CZ  . TYR B 2 75  ? -2.38518  40.65084 112.72307 1.000 125.10020 ?  396 TYR C CZ  1 
ATOM 2196 O OH  . TYR B 2 75  ? -1.69216  41.56489 113.48320 1.000 132.89741 ?  396 TYR C OH  1 
ATOM 2197 N N   . ALA B 2 76  ? -7.08982  37.00380 108.63156 1.000 107.55811 ?  397 ALA C N   1 
ATOM 2198 C CA  . ALA B 2 76  ? -7.76027  36.09221 107.70945 1.000 110.97551 ?  397 ALA C CA  1 
ATOM 2199 C C   . ALA B 2 76  ? -7.08153  36.18695 106.35012 1.000 118.87387 ?  397 ALA C C   1 
ATOM 2200 O O   . ALA B 2 76  ? -7.23194  37.19089 105.64596 1.000 108.31892 ?  397 ALA C O   1 
ATOM 2201 C CB  . ALA B 2 76  ? -9.25036  36.41603 107.59888 1.000 95.29710  ?  397 ALA C CB  1 
ATOM 2202 N N   . ASP B 2 77  ? -6.33903  35.14544 105.98349 1.000 116.46003 ?  398 ASP C N   1 
ATOM 2203 C CA  . ASP B 2 77  ? -5.67104  35.08232 104.69084 1.000 109.54932 ?  398 ASP C CA  1 
ATOM 2204 C C   . ASP B 2 77  ? -6.57858  34.38702 103.68432 1.000 107.76775 ?  398 ASP C C   1 
ATOM 2205 O O   . ASP B 2 77  ? -7.10761  33.30617 103.96125 1.000 107.06813 ?  398 ASP C O   1 
ATOM 2206 C CB  . ASP B 2 77  ? -4.33844  34.34173 104.80805 1.000 110.73228 ?  398 ASP C CB  1 
ATOM 2207 C CG  . ASP B 2 77  ? -3.42433  34.94932 105.85481 1.000 118.70994 ?  398 ASP C CG  1 
ATOM 2208 O OD1 . ASP B 2 77  ? -3.49337  36.17853 106.06518 1.000 110.02596 ?  398 ASP C OD1 1 
ATOM 2209 O OD2 . ASP B 2 77  ? -2.63772  34.19758 106.46853 1.000 122.30605 -1 398 ASP C OD2 1 
ATOM 2210 N N   . SER B 2 78  ? -6.75479  35.00661 102.51875 1.000 106.78712 ?  399 SER C N   1 
ATOM 2211 C CA  . SER B 2 78  ? -7.66853  34.50756 101.49942 1.000 100.36464 ?  399 SER C CA  1 
ATOM 2212 C C   . SER B 2 78  ? -6.93487  34.35998 100.17498 1.000 101.85442 ?  399 SER C C   1 
ATOM 2213 O O   . SER B 2 78  ? -6.25876  35.29233 99.72814  1.000 104.69248 ?  399 SER C O   1 
ATOM 2214 C CB  . SER B 2 78  ? -8.87309  35.44146 101.33665 1.000 98.70604  ?  399 SER C CB  1 
ATOM 2215 O OG  . SER B 2 78  ? -8.46179  36.74860 100.97676 1.000 103.33808 ?  399 SER C OG  1 
ATOM 2216 N N   . PHE B 2 79  ? -7.07576  33.19135 99.55259  1.000 93.38885  ?  400 PHE C N   1 
ATOM 2217 C CA  . PHE B 2 79  ? -6.48329  32.91954 98.24923  1.000 83.25565  ?  400 PHE C CA  1 
ATOM 2218 C C   . PHE B 2 79  ? -7.17635  31.70284 97.65040  1.000 78.57020  ?  400 PHE C C   1 
ATOM 2219 O O   . PHE B 2 79  ? -7.97737  31.03338 98.30712  1.000 84.92366  ?  400 PHE C O   1 
ATOM 2220 C CB  . PHE B 2 79  ? -4.96809  32.70511 98.35090  1.000 90.58849  ?  400 PHE C CB  1 
ATOM 2221 C CG  . PHE B 2 79  ? -4.56103  31.71866 99.40945  1.000 81.44801  ?  400 PHE C CG  1 
ATOM 2222 C CD1 . PHE B 2 79  ? -4.49007  30.36517 99.12508  1.000 83.05114  ?  400 PHE C CD1 1 
ATOM 2223 C CD2 . PHE B 2 79  ? -4.24063  32.14694 100.68717 1.000 82.73892  ?  400 PHE C CD2 1 
ATOM 2224 C CE1 . PHE B 2 79  ? -4.11378  29.45643 100.09622 1.000 78.07801  ?  400 PHE C CE1 1 
ATOM 2225 C CE2 . PHE B 2 79  ? -3.86350  31.24330 101.66276 1.000 91.44995  ?  400 PHE C CE2 1 
ATOM 2226 C CZ  . PHE B 2 79  ? -3.79986  29.89634 101.36649 1.000 91.41450  ?  400 PHE C CZ  1 
ATOM 2227 N N   . VAL B 2 80  ? -6.85796  31.42566 96.38753  1.000 77.86368  ?  401 VAL C N   1 
ATOM 2228 C CA  . VAL B 2 80  ? -7.45395  30.31973 95.64431  1.000 82.02310  ?  401 VAL C CA  1 
ATOM 2229 C C   . VAL B 2 80  ? -6.33342  29.44019 95.11210  1.000 80.44442  ?  401 VAL C C   1 
ATOM 2230 O O   . VAL B 2 80  ? -5.46033  29.91812 94.37841  1.000 80.99262  ?  401 VAL C O   1 
ATOM 2231 C CB  . VAL B 2 80  ? -8.34528  30.80889 94.49075  1.000 71.86698  ?  401 VAL C CB  1 
ATOM 2232 C CG1 . VAL B 2 80  ? -8.70545  29.65137 93.57128  1.000 77.61933  ?  401 VAL C CG1 1 
ATOM 2233 C CG2 . VAL B 2 80  ? -9.59894  31.45830 95.03610  1.000 77.37255  ?  401 VAL C CG2 1 
ATOM 2234 N N   . ILE B 2 81  ? -6.36489  28.15801 95.46918  1.000 79.12372  ?  402 ILE C N   1 
ATOM 2235 C CA  . ILE B 2 81  ? -5.36371  27.20158 95.01291  1.000 72.58143  ?  402 ILE C CA  1 
ATOM 2236 C C   . ILE B 2 81  ? -6.04496  26.08948 94.22758  1.000 79.03211  ?  402 ILE C C   1 
ATOM 2237 O O   . ILE B 2 81  ? -7.24933  26.15001 93.95617  1.000 76.94830  ?  402 ILE C O   1 
ATOM 2238 C CB  . ILE B 2 81  ? -4.56834  26.62223 96.19508  1.000 64.05575  ?  402 ILE C CB  1 
ATOM 2239 C CG1 . ILE B 2 81  ? -5.52237  25.96436 97.19237  1.000 71.67637  ?  402 ILE C CG1 1 
ATOM 2240 C CG2 . ILE B 2 81  ? -3.74580  27.70680 96.86794  1.000 72.51082  ?  402 ILE C CG2 1 
ATOM 2241 C CD1 . ILE B 2 81  ? -4.83213  25.27887 98.33553  1.000 82.62374  ?  402 ILE C CD1 1 
ATOM 2242 N N   . ARG B 2 82  ? -5.27803  25.06438 93.86720  1.000 75.19378  ?  403 ARG C N   1 
ATOM 2243 C CA  . ARG B 2 82  ? -5.80308  23.90530 93.16592  1.000 74.21251  ?  403 ARG C CA  1 
ATOM 2244 C C   . ARG B 2 82  ? -6.39152  22.91589 94.17194  1.000 81.72594  ?  403 ARG C C   1 
ATOM 2245 O O   . ARG B 2 82  ? -6.38254  23.14000 95.38675  1.000 85.99610  ?  403 ARG C O   1 
ATOM 2246 C CB  . ARG B 2 82  ? -4.69934  23.26836 92.32291  1.000 77.11189  ?  403 ARG C CB  1 
ATOM 2247 C CG  . ARG B 2 82  ? -5.16888  22.44221 91.14103  1.000 85.07819  ?  403 ARG C CG  1 
ATOM 2248 C CD  . ARG B 2 82  ? -3.98483  21.85510 90.39039  1.000 87.61914  ?  403 ARG C CD  1 
ATOM 2249 N NE  . ARG B 2 82  ? -3.07308  21.13015 91.27264  1.000 92.31341  ?  403 ARG C NE  1 
ATOM 2250 C CZ  . ARG B 2 82  ? -1.88078  20.67473 90.89975  1.000 84.52173  ?  403 ARG C CZ  1 
ATOM 2251 N NH1 . ARG B 2 82  ? -1.11186  20.02618 91.76467  1.000 88.85422  ?  403 ARG C NH1 1 
ATOM 2252 N NH2 . ARG B 2 82  ? -1.45262  20.87474 89.66088  1.000 92.80660  ?  403 ARG C NH2 1 
ATOM 2253 N N   . GLY B 2 83  ? -6.90978  21.80192 93.66068  1.000 82.48992  ?  404 GLY C N   1 
ATOM 2254 C CA  . GLY B 2 83  ? -7.48248  20.77920 94.51243  1.000 73.25153  ?  404 GLY C CA  1 
ATOM 2255 C C   . GLY B 2 83  ? -6.44435  19.99308 95.28679  1.000 82.41856  ?  404 GLY C C   1 
ATOM 2256 O O   . GLY B 2 83  ? -6.64730  19.68523 96.46325  1.000 76.29177  ?  404 GLY C O   1 
ATOM 2257 N N   . ASP B 2 84  ? -5.32438  19.66320 94.64287  1.000 93.18582  ?  405 ASP C N   1 
ATOM 2258 C CA  . ASP B 2 84  ? -4.26332  18.90390 95.29286  1.000 83.62220  ?  405 ASP C CA  1 
ATOM 2259 C C   . ASP B 2 84  ? -3.36862  19.76046 96.17978  1.000 89.06613  ?  405 ASP C C   1 
ATOM 2260 O O   . ASP B 2 84  ? -2.61143  19.20556 96.98224  1.000 84.11753  ?  405 ASP C O   1 
ATOM 2261 C CB  . ASP B 2 84  ? -3.40974  18.19563 94.23823  1.000 81.14843  ?  405 ASP C CB  1 
ATOM 2262 C CG  . ASP B 2 84  ? -4.21219  17.22237 93.39710  1.000 90.82392  ?  405 ASP C CG  1 
ATOM 2263 O OD1 . ASP B 2 84  ? -5.19442  16.64821 93.91440  1.000 88.40113  ?  405 ASP C OD1 1 
ATOM 2264 O OD2 . ASP B 2 84  ? -3.85579  17.03029 92.21649  1.000 101.72323 -1 405 ASP C OD2 1 
ATOM 2265 N N   . GLU B 2 85  ? -3.43143  21.08526 96.05748  1.000 97.38599  ?  406 GLU C N   1 
ATOM 2266 C CA  . GLU B 2 85  ? -2.60203  21.97388 96.86072  1.000 78.37109  ?  406 GLU C CA  1 
ATOM 2267 C C   . GLU B 2 85  ? -3.17280  22.22563 98.24997  1.000 87.54400  ?  406 GLU C C   1 
ATOM 2268 O O   . GLU B 2 85  ? -2.52755  22.91299 99.04826  1.000 89.49021  ?  406 GLU C O   1 
ATOM 2269 C CB  . GLU B 2 85  ? -2.41300  23.31255 96.13949  1.000 81.53650  ?  406 GLU C CB  1 
ATOM 2270 C CG  . GLU B 2 85  ? -2.07481  23.20285 94.65798  1.000 85.21872  ?  406 GLU C CG  1 
ATOM 2271 C CD  . GLU B 2 85  ? -0.62971  22.82304 94.39379  1.000 109.55322 ?  406 GLU C CD  1 
ATOM 2272 O OE1 . GLU B 2 85  ? 0.11879   22.57708 95.36288  1.000 133.94935 ?  406 GLU C OE1 1 
ATOM 2273 O OE2 . GLU B 2 85  ? -0.24039  22.77633 93.20770  1.000 94.41919  -1 406 GLU C OE2 1 
ATOM 2274 N N   . VAL B 2 86  ? -4.36075  21.69765 98.55583  1.000 96.97401  ?  407 VAL C N   1 
ATOM 2275 C CA  . VAL B 2 86  ? -4.96647  21.94117 99.86138  1.000 80.82983  ?  407 VAL C CA  1 
ATOM 2276 C C   . VAL B 2 86  ? -4.15324  21.28130 100.96714 1.000 93.42974  ?  407 VAL C C   1 
ATOM 2277 O O   . VAL B 2 86  ? -4.07969  21.79926 102.08849 1.000 97.96936  ?  407 VAL C O   1 
ATOM 2278 C CB  . VAL B 2 86  ? -6.42850  21.45663 99.86458  1.000 77.22148  ?  407 VAL C CB  1 
ATOM 2279 C CG1 . VAL B 2 86  ? -7.11240  21.81831 101.17453 1.000 80.39840  ?  407 VAL C CG1 1 
ATOM 2280 C CG2 . VAL B 2 86  ? -7.18341  22.04829 98.68390  1.000 73.22660  ?  407 VAL C CG2 1 
ATOM 2281 N N   . ARG B 2 87  ? -3.51939  20.14467 100.67462 1.000 96.99741  ?  408 ARG C N   1 
ATOM 2282 C CA  . ARG B 2 87  ? -2.72455  19.43671 101.67109 1.000 101.13240 ?  408 ARG C CA  1 
ATOM 2283 C C   . ARG B 2 87  ? -1.43324  20.16119 102.03242 1.000 107.55504 ?  408 ARG C C   1 
ATOM 2284 O O   . ARG B 2 87  ? -0.81713  19.81664 103.04707 1.000 118.18581 ?  408 ARG C O   1 
ATOM 2285 C CB  . ARG B 2 87  ? -2.40432  18.02709 101.16984 1.000 99.91967  ?  408 ARG C CB  1 
ATOM 2286 C CG  . ARG B 2 87  ? -1.60884  18.00321 99.87690  1.000 100.08870 ?  408 ARG C CG  1 
ATOM 2287 C CD  . ARG B 2 87  ? -1.35745  16.58404 99.40069  1.000 114.66611 ?  408 ARG C CD  1 
ATOM 2288 N NE  . ARG B 2 87  ? -0.54313  15.82504 100.34444 1.000 132.12180 ?  408 ARG C NE  1 
ATOM 2289 C CZ  . ARG B 2 87  ? -0.14928  14.57134 100.14809 1.000 137.17485 ?  408 ARG C CZ  1 
ATOM 2290 N NH1 . ARG B 2 87  ? -0.49458  13.93314 99.03847  1.000 146.23833 ?  408 ARG C NH1 1 
ATOM 2291 N NH2 . ARG B 2 87  ? 0.59039   13.95520 101.05973 1.000 117.72070 ?  408 ARG C NH2 1 
ATOM 2292 N N   . GLN B 2 88  ? -1.01498  21.14998 101.24011 1.000 107.37945 ?  409 GLN C N   1 
ATOM 2293 C CA  . GLN B 2 88  ? 0.23303   21.86176 101.48638 1.000 90.05475  ?  409 GLN C CA  1 
ATOM 2294 C C   . GLN B 2 88  ? 0.09384   23.00063 102.48648 1.000 88.59680  ?  409 GLN C C   1 
ATOM 2295 O O   . GLN B 2 88  ? 1.08667   23.36424 103.12687 1.000 102.10402 ?  409 GLN C O   1 
ATOM 2296 C CB  . GLN B 2 88  ? 0.80131   22.40685 100.17235 1.000 78.56806  ?  409 GLN C CB  1 
ATOM 2297 C CG  . GLN B 2 88  ? 1.15306   21.32371 99.16941  1.000 86.73775  ?  409 GLN C CG  1 
ATOM 2298 C CD  . GLN B 2 88  ? 1.95422   21.84476 97.99060  1.000 83.45884  ?  409 GLN C CD  1 
ATOM 2299 O OE1 . GLN B 2 88  ? 2.46361   22.96510 98.01233  1.000 81.76570  ?  409 GLN C OE1 1 
ATOM 2300 N NE2 . GLN B 2 88  ? 2.07112   21.02737 96.95300  1.000 81.08889  ?  409 GLN C NE2 1 
ATOM 2301 N N   . ILE B 2 89  ? -1.09928  23.57219 102.63905 1.000 87.05661  ?  410 ILE C N   1 
ATOM 2302 C CA  . ILE B 2 89  ? -1.31336  24.60624 103.64615 1.000 97.69631  ?  410 ILE C CA  1 
ATOM 2303 C C   . ILE B 2 89  ? -1.45074  23.90608 104.99234 1.000 100.73579 ?  410 ILE C C   1 
ATOM 2304 O O   . ILE B 2 89  ? -2.55045  23.51062 105.39816 1.000 84.87328  ?  410 ILE C O   1 
ATOM 2305 C CB  . ILE B 2 89  ? -2.53406  25.49605 103.32624 1.000 92.82568  ?  410 ILE C CB  1 
ATOM 2306 C CG1 . ILE B 2 89  ? -2.23955  26.42516 102.14280 1.000 77.26533  ?  410 ILE C CG1 1 
ATOM 2307 C CG2 . ILE B 2 89  ? -2.91227  26.36435 104.52329 1.000 81.96893  ?  410 ILE C CG2 1 
ATOM 2308 C CD1 . ILE B 2 89  ? -2.30203  25.77353 100.78342 1.000 73.87234  ?  410 ILE C CD1 1 
ATOM 2309 N N   . ALA B 2 90  ? -0.31891  23.72772 105.67630 1.000 112.97763 ?  411 ALA C N   1 
ATOM 2310 C CA  . ALA B 2 90  ? -0.21109  23.03405 106.95358 1.000 106.85069 ?  411 ALA C CA  1 
ATOM 2311 C C   . ALA B 2 90  ? 1.22700   23.14061 107.44621 1.000 120.12962 ?  411 ALA C C   1 
ATOM 2312 O O   . ALA B 2 90  ? 2.14743   23.29544 106.63283 1.000 115.18095 ?  411 ALA C O   1 
ATOM 2313 C CB  . ALA B 2 90  ? -0.62720  21.56690 106.82258 1.000 96.90676  ?  411 ALA C CB  1 
ATOM 2314 N N   . PRO B 2 91  ? 1.46444   23.07625 108.75571 1.000 124.63999 ?  412 PRO C N   1 
ATOM 2315 C CA  . PRO B 2 91  ? 2.84241   23.16343 109.25432 1.000 125.32772 ?  412 PRO C CA  1 
ATOM 2316 C C   . PRO B 2 91  ? 3.68284   21.97974 108.79580 1.000 115.62386 ?  412 PRO C C   1 
ATOM 2317 O O   . PRO B 2 91  ? 3.24817   20.82708 108.84276 1.000 109.90307 ?  412 PRO C O   1 
ATOM 2318 C CB  . PRO B 2 91  ? 2.66848   23.17210 110.77763 1.000 125.50633 ?  412 PRO C CB  1 
ATOM 2319 C CG  . PRO B 2 91  ? 1.26666   23.63811 111.00033 1.000 115.97607 ?  412 PRO C CG  1 
ATOM 2320 C CD  . PRO B 2 91  ? 0.47938   23.08954 109.85048 1.000 109.41206 ?  412 PRO C CD  1 
ATOM 2321 N N   . GLY B 2 92  ? 4.89859   22.27956 108.34531 1.000 109.03707 ?  413 GLY C N   1 
ATOM 2322 C CA  . GLY B 2 92  ? 5.83424   21.23947 107.96117 1.000 102.06432 ?  413 GLY C CA  1 
ATOM 2323 C C   . GLY B 2 92  ? 5.51348   20.53514 106.66250 1.000 96.42249  ?  413 GLY C C   1 
ATOM 2324 O O   . GLY B 2 92  ? 5.81140   19.34468 106.52331 1.000 101.23861 ?  413 GLY C O   1 
ATOM 2325 N N   . GLN B 2 93  ? 4.91689   21.23566 105.70405 1.000 91.45841  ?  414 GLN C N   1 
ATOM 2326 C CA  . GLN B 2 93  ? 4.59122   20.66198 104.40769 1.000 92.56887  ?  414 GLN C CA  1 
ATOM 2327 C C   . GLN B 2 93  ? 5.57061   21.14940 103.34748 1.000 84.37719  ?  414 GLN C C   1 
ATOM 2328 O O   . GLN B 2 93  ? 6.09233   22.26496 103.42047 1.000 82.19953  ?  414 GLN C O   1 
ATOM 2329 C CB  . GLN B 2 93  ? 3.16054   21.01456 103.99569 1.000 96.81827  ?  414 GLN C CB  1 
ATOM 2330 C CG  . GLN B 2 93  ? 2.08788   20.28831 104.79007 1.000 90.91443  ?  414 GLN C CG  1 
ATOM 2331 C CD  . GLN B 2 93  ? 2.01955   18.80806 104.46581 1.000 84.46841  ?  414 GLN C CD  1 
ATOM 2332 O OE1 . GLN B 2 93  ? 2.52073   18.36180 103.43329 1.000 91.21655  ?  414 GLN C OE1 1 
ATOM 2333 N NE2 . GLN B 2 93  ? 1.39569   18.03782 105.34950 1.000 76.14417  ?  414 GLN C NE2 1 
ATOM 2334 N N   . THR B 2 94  ? 5.81435   20.29566 102.35666 1.000 87.12140  ?  415 THR C N   1 
ATOM 2335 C CA  . THR B 2 94  ? 6.73239   20.58822 101.26498 1.000 85.84391  ?  415 THR C CA  1 
ATOM 2336 C C   . THR B 2 94  ? 5.98711   20.48189 99.94313  1.000 86.20521  ?  415 THR C C   1 
ATOM 2337 O O   . THR B 2 94  ? 5.26652   19.50594 99.70838  1.000 87.51742  ?  415 THR C O   1 
ATOM 2338 C CB  . THR B 2 94  ? 7.92985   19.63272 101.27672 1.000 92.39973  ?  415 THR C CB  1 
ATOM 2339 O OG1 . THR B 2 94  ? 8.59801   19.71762 102.54162 1.000 101.98058 ?  415 THR C OG1 1 
ATOM 2340 C CG2 . THR B 2 94  ? 8.91029   19.98964 100.16841 1.000 89.13822  ?  415 THR C CG2 1 
ATOM 2341 N N   . GLY B 2 95  ? 6.15984   21.48341 99.08952  1.000 85.38382  ?  416 GLY C N   1 
ATOM 2342 C CA  . GLY B 2 95  ? 5.50877   21.48303 97.79725  1.000 80.65715  ?  416 GLY C CA  1 
ATOM 2343 C C   . GLY B 2 95  ? 5.77106   22.78649 97.07112  1.000 83.40952  ?  416 GLY C C   1 
ATOM 2344 O O   . GLY B 2 95  ? 6.56416   23.61903 97.51578  1.000 87.58883  ?  416 GLY C O   1 
ATOM 2345 N N   . LYS B 2 96  ? 5.08493   22.94401 95.93773  1.000 79.80935  ?  417 LYS C N   1 
ATOM 2346 C CA  . LYS B 2 96  ? 5.22854   24.16947 95.15909  1.000 65.76278  ?  417 LYS C CA  1 
ATOM 2347 C C   . LYS B 2 96  ? 4.56680   25.34882 95.86093  1.000 72.13105  ?  417 LYS C C   1 
ATOM 2348 O O   . LYS B 2 96  ? 5.12659   26.45075 95.89770  1.000 72.10157  ?  417 LYS C O   1 
ATOM 2349 C CB  . LYS B 2 96  ? 4.64151   23.97454 93.76147  1.000 66.50781  ?  417 LYS C CB  1 
ATOM 2350 C CG  . LYS B 2 96  ? 5.62605   24.23760 92.63440  1.000 63.00225  ?  417 LYS C CG  1 
ATOM 2351 C CD  . LYS B 2 96  ? 6.84528   23.33470 92.74415  1.000 93.03324  ?  417 LYS C CD  1 
ATOM 2352 C CE  . LYS B 2 96  ? 7.84694   23.62033 91.63586  1.000 101.07983 ?  417 LYS C CE  1 
ATOM 2353 N NZ  . LYS B 2 96  ? 9.06228   22.76549 91.74525  1.000 54.42936  ?  417 LYS C NZ  1 
ATOM 2354 N N   . ILE B 2 97  ? 3.37812   25.13620 96.42639  1.000 80.29309  ?  418 ILE C N   1 
ATOM 2355 C CA  . ILE B 2 97  ? 2.67987   26.20928 97.12619  1.000 73.09866  ?  418 ILE C CA  1 
ATOM 2356 C C   . ILE B 2 97  ? 3.26571   26.41900 98.51725  1.000 75.07748  ?  418 ILE C C   1 
ATOM 2357 O O   . ILE B 2 97  ? 3.37530   27.55479 98.99275  1.000 78.31250  ?  418 ILE C O   1 
ATOM 2358 C CB  . ILE B 2 97  ? 1.17093   25.90499 97.18374  1.000 65.00244  ?  418 ILE C CB  1 
ATOM 2359 C CG1 . ILE B 2 97  ? 0.59350   25.79077 95.77168  1.000 66.18101  ?  418 ILE C CG1 1 
ATOM 2360 C CG2 . ILE B 2 97  ? 0.43187   26.97422 97.97463  1.000 70.64404  ?  418 ILE C CG2 1 
ATOM 2361 C CD1 . ILE B 2 97  ? 0.69174   27.06563 94.96538  1.000 81.11180  ?  418 ILE C CD1 1 
ATOM 2362 N N   . ALA B 2 98  ? 3.66304   25.33438 99.18599  1.000 86.60534  ?  419 ALA C N   1 
ATOM 2363 C CA  . ALA B 2 98  ? 4.14623   25.43640 100.55761 1.000 89.68779  ?  419 ALA C CA  1 
ATOM 2364 C C   . ALA B 2 98  ? 5.53442   26.05631 100.65136 1.000 91.57032  ?  419 ALA C C   1 
ATOM 2365 O O   . ALA B 2 98  ? 5.89958   26.56076 101.71785 1.000 95.04642  ?  419 ALA C O   1 
ATOM 2366 C CB  . ALA B 2 98  ? 4.15175   24.05616 101.21617 1.000 100.18681 ?  419 ALA C CB  1 
ATOM 2367 N N   . ASP B 2 99  ? 6.31498   26.03361 99.57204  1.000 88.95186  ?  420 ASP C N   1 
ATOM 2368 C CA  . ASP B 2 99  ? 7.67754   26.54887 99.60158  1.000 89.18794  ?  420 ASP C CA  1 
ATOM 2369 C C   . ASP B 2 99  ? 7.85978   27.86165 98.85734  1.000 88.16089  ?  420 ASP C C   1 
ATOM 2370 O O   . ASP B 2 99  ? 8.74136   28.64161 99.22284  1.000 88.51888  ?  420 ASP C O   1 
ATOM 2371 C CB  . ASP B 2 99  ? 8.65183   25.51567 99.01978  1.000 91.83233  ?  420 ASP C CB  1 
ATOM 2372 C CG  . ASP B 2 99  ? 8.68493   24.22794 99.82080  1.000 94.32370  ?  420 ASP C CG  1 
ATOM 2373 O OD1 . ASP B 2 99  ? 8.45246   24.28176 101.04678 1.000 95.26257  ?  420 ASP C OD1 1 
ATOM 2374 O OD2 . ASP B 2 99  ? 8.94549   23.16157 99.22424  1.000 89.62408  -1 420 ASP C OD2 1 
ATOM 2375 N N   . TYR B 2 100 ? 7.05393   28.12957 97.82840  1.000 79.29109  ?  421 TYR C N   1 
ATOM 2376 C CA  . TYR B 2 100 ? 7.23891   29.30687 96.99334  1.000 68.75928  ?  421 TYR C CA  1 
ATOM 2377 C C   . TYR B 2 100 ? 6.07542   30.28815 97.02101  1.000 71.48047  ?  421 TYR C C   1 
ATOM 2378 O O   . TYR B 2 100 ? 6.20524   31.38084 96.45715  1.000 73.34236  ?  421 TYR C O   1 
ATOM 2379 C CB  . TYR B 2 100 ? 7.49303   28.89374 95.53387  1.000 67.54412  ?  421 TYR C CB  1 
ATOM 2380 C CG  . TYR B 2 100 ? 8.78877   28.14485 95.30924  1.000 66.45195  ?  421 TYR C CG  1 
ATOM 2381 C CD1 . TYR B 2 100 ? 9.85305   28.27298 96.19216  1.000 77.44303  ?  421 TYR C CD1 1 
ATOM 2382 C CD2 . TYR B 2 100 ? 8.94780   27.31213 94.20898  1.000 67.81739  ?  421 TYR C CD2 1 
ATOM 2383 C CE1 . TYR B 2 100 ? 11.03824  27.59029 95.98711  1.000 82.82516  ?  421 TYR C CE1 1 
ATOM 2384 C CE2 . TYR B 2 100 ? 10.12848  26.62612 93.99547  1.000 69.09412  ?  421 TYR C CE2 1 
ATOM 2385 C CZ  . TYR B 2 100 ? 11.17000  26.76874 94.88721  1.000 72.14878  ?  421 TYR C CZ  1 
ATOM 2386 O OH  . TYR B 2 100 ? 12.34695  26.08744 94.67797  1.000 73.25776  ?  421 TYR C OH  1 
ATOM 2387 N N   . ASN B 2 101 ? 4.95255   29.94607 97.65297  1.000 75.97803  ?  422 ASN C N   1 
ATOM 2388 C CA  . ASN B 2 101 ? 3.76818   30.79899 97.62422  1.000 68.38057  ?  422 ASN C CA  1 
ATOM 2389 C C   . ASN B 2 101 ? 3.29444   31.18419 99.01895  1.000 70.67252  ?  422 ASN C C   1 
ATOM 2390 O O   . ASN B 2 101 ? 3.28793   32.37330 99.35371  1.000 75.61283  ?  422 ASN C O   1 
ATOM 2391 C CB  . ASN B 2 101 ? 2.64297   30.10280 96.84737  1.000 65.64397  ?  422 ASN C CB  1 
ATOM 2392 C CG  . ASN B 2 101 ? 2.97553   29.91723 95.38020  1.000 69.94483  ?  422 ASN C CG  1 
ATOM 2393 O OD1 . ASN B 2 101 ? 2.65591   30.76559 94.54730  1.000 71.03791  ?  422 ASN C OD1 1 
ATOM 2394 N ND2 . ASN B 2 101 ? 3.62076   28.80299 95.05591  1.000 69.37187  ?  422 ASN C ND2 1 
ATOM 2395 N N   . TYR B 2 102 ? 2.88943   30.21923 99.84189  1.000 78.59013  ?  423 TYR C N   1 
ATOM 2396 C CA  . TYR B 2 102 ? 2.32995   30.51818 101.15814 1.000 78.64015  ?  423 TYR C CA  1 
ATOM 2397 C C   . TYR B 2 102 ? 2.73955   29.40398 102.11015 1.000 83.96770  ?  423 TYR C C   1 
ATOM 2398 O O   . TYR B 2 102 ? 2.24931   28.27702 101.99198 1.000 94.48919  ?  423 TYR C O   1 
ATOM 2399 C CB  . TYR B 2 102 ? 0.81007   30.65264 101.08504 1.000 79.77955  ?  423 TYR C CB  1 
ATOM 2400 C CG  . TYR B 2 102 ? 0.14714   30.99670 102.40020 1.000 89.88998  ?  423 TYR C CG  1 
ATOM 2401 C CD1 . TYR B 2 102 ? 0.05090   32.31435 102.82747 1.000 99.26701  ?  423 TYR C CD1 1 
ATOM 2402 C CD2 . TYR B 2 102 ? -0.39292  30.00477 103.20909 1.000 99.74423  ?  423 TYR C CD2 1 
ATOM 2403 C CE1 . TYR B 2 102 ? -0.55744  32.63430 104.02684 1.000 99.46554  ?  423 TYR C CE1 1 
ATOM 2404 C CE2 . TYR B 2 102 ? -1.00305  30.31496 104.41005 1.000 89.75266  ?  423 TYR C CE2 1 
ATOM 2405 C CZ  . TYR B 2 102 ? -1.08256  31.63084 104.81359 1.000 90.23245  ?  423 TYR C CZ  1 
ATOM 2406 O OH  . TYR B 2 102 ? -1.68923  31.94434 106.00803 1.000 93.07450  ?  423 TYR C OH  1 
ATOM 2407 N N   . LYS B 2 103 ? 3.63026   29.71578 103.04743 1.000 83.35344  ?  424 LYS C N   1 
ATOM 2408 C CA  . LYS B 2 103 ? 4.12116   28.74841 104.01740 1.000 90.97137  ?  424 LYS C CA  1 
ATOM 2409 C C   . LYS B 2 103 ? 3.56658   29.07082 105.39791 1.000 92.57643  ?  424 LYS C C   1 
ATOM 2410 O O   . LYS B 2 103 ? 3.39772   30.24165 105.75351 1.000 90.72345  ?  424 LYS C O   1 
ATOM 2411 C CB  . LYS B 2 103 ? 5.65227   28.73257 104.05698 1.000 85.26672  ?  424 LYS C CB  1 
ATOM 2412 C CG  . LYS B 2 103 ? 6.23636   27.52575 104.77666 1.000 88.40608  ?  424 LYS C CG  1 
ATOM 2413 C CD  . LYS B 2 103 ? 7.71904   27.36746 104.48566 1.000 97.86317  ?  424 LYS C CD  1 
ATOM 2414 C CE  . LYS B 2 103 ? 8.24658   26.04510 105.01864 1.000 100.17155 ?  424 LYS C CE  1 
ATOM 2415 N NZ  . LYS B 2 103 ? 7.55039   24.88235 104.39986 1.000 71.86002  ?  424 LYS C NZ  1 
ATOM 2416 N N   . LEU B 2 104 ? 3.28414   28.02296 106.17173 1.000 99.70380  ?  425 LEU C N   1 
ATOM 2417 C CA  . LEU B 2 104 ? 2.72609   28.14936 107.50546 1.000 98.50208  ?  425 LEU C CA  1 
ATOM 2418 C C   . LEU B 2 104 ? 3.75443   27.73995 108.55380 1.000 108.26169 ?  425 LEU C C   1 
ATOM 2419 O O   . LEU B 2 104 ? 4.47443   26.75370 108.36007 1.000 104.15252 ?  425 LEU C O   1 
ATOM 2420 C CB  . LEU B 2 104 ? 1.47209   27.27895 107.65422 1.000 98.50919  ?  425 LEU C CB  1 
ATOM 2421 C CG  . LEU B 2 104 ? 0.34028   27.82258 108.52709 1.000 97.14283  ?  425 LEU C CG  1 
ATOM 2422 C CD1 . LEU B 2 104 ? -0.17382  29.13934 107.96874 1.000 86.66622  ?  425 LEU C CD1 1 
ATOM 2423 C CD2 . LEU B 2 104 ? -0.78653  26.80795 108.63548 1.000 102.98750 ?  425 LEU C CD2 1 
ATOM 2424 N N   . PRO B 2 105 ? 3.85340   28.47108 109.66164 1.000 114.96511 ?  426 PRO C N   1 
ATOM 2425 C CA  . PRO B 2 105 ? 4.83518   28.11869 110.69235 1.000 119.38704 ?  426 PRO C CA  1 
ATOM 2426 C C   . PRO B 2 105 ? 4.48260   26.80964 111.38245 1.000 123.37432 ?  426 PRO C C   1 
ATOM 2427 O O   . PRO B 2 105 ? 3.33878   26.34955 111.36969 1.000 130.33132 ?  426 PRO C O   1 
ATOM 2428 C CB  . PRO B 2 105 ? 4.76506   29.29737 111.66922 1.000 113.63288 ?  426 PRO C CB  1 
ATOM 2429 C CG  . PRO B 2 105 ? 3.39704   29.86146 111.47443 1.000 115.47153 ?  426 PRO C CG  1 
ATOM 2430 C CD  . PRO B 2 105 ? 3.08832   29.67921 110.01530 1.000 105.84270 ?  426 PRO C CD  1 
ATOM 2431 N N   . ASP B 2 106 ? 5.50348   26.20665 111.99688 1.000 122.63614 ?  427 ASP C N   1 
ATOM 2432 C CA  . ASP B 2 106 ? 5.30563   24.93142 112.67895 1.000 129.85273 ?  427 ASP C CA  1 
ATOM 2433 C C   . ASP B 2 106 ? 4.48476   25.10406 113.95121 1.000 133.20167 ?  427 ASP C C   1 
ATOM 2434 O O   . ASP B 2 106 ? 3.64034   24.25908 114.27088 1.000 126.28056 ?  427 ASP C O   1 
ATOM 2435 C CB  . ASP B 2 106 ? 6.65656   24.28839 112.99104 1.000 131.56217 ?  427 ASP C CB  1 
ATOM 2436 C CG  . ASP B 2 106 ? 7.46904   24.00590 111.74231 1.000 124.40808 ?  427 ASP C CG  1 
ATOM 2437 O OD1 . ASP B 2 106 ? 7.00763   24.36315 110.63783 1.000 118.91180 ?  427 ASP C OD1 1 
ATOM 2438 O OD2 . ASP B 2 106 ? 8.56803   23.42523 111.86477 1.000 115.74550 -1 427 ASP C OD2 1 
ATOM 2439 N N   . ASP B 2 107 ? 4.71714   26.18585 114.68860 1.000 139.67948 ?  428 ASP C N   1 
ATOM 2440 C CA  . ASP B 2 107 ? 3.94675   26.48727 115.89545 1.000 126.84893 ?  428 ASP C CA  1 
ATOM 2441 C C   . ASP B 2 107 ? 2.71465   27.32730 115.56988 1.000 126.51400 ?  428 ASP C C   1 
ATOM 2442 O O   . ASP B 2 107 ? 2.45420   28.36208 116.18239 1.000 112.37756 ?  428 ASP C O   1 
ATOM 2443 C CB  . ASP B 2 107 ? 4.83549   27.18440 116.91867 1.000 119.21757 ?  428 ASP C CB  1 
ATOM 2444 C CG  . ASP B 2 107 ? 5.52486   28.41069 116.35338 1.000 124.78669 ?  428 ASP C CG  1 
ATOM 2445 O OD1 . ASP B 2 107 ? 5.81473   28.42465 115.13861 1.000 131.69502 ?  428 ASP C OD1 1 
ATOM 2446 O OD2 . ASP B 2 107 ? 5.77714   29.36054 117.12406 1.000 126.06263 -1 428 ASP C OD2 1 
ATOM 2447 N N   . PHE B 2 108 ? 1.94295   26.87061 114.58747 1.000 129.93109 ?  429 PHE C N   1 
ATOM 2448 C CA  . PHE B 2 108 ? 0.76818   27.60007 114.13451 1.000 124.75604 ?  429 PHE C CA  1 
ATOM 2449 C C   . PHE B 2 108 ? -0.38063  27.44002 115.12162 1.000 125.50993 ?  429 PHE C C   1 
ATOM 2450 O O   . PHE B 2 108 ? -0.60667  26.35578 115.66682 1.000 115.54691 ?  429 PHE C O   1 
ATOM 2451 C CB  . PHE B 2 108 ? 0.34588   27.11121 112.74860 1.000 104.62805 ?  429 PHE C CB  1 
ATOM 2452 C CG  . PHE B 2 108 ? -0.91304  27.74823 112.23614 1.000 104.47503 ?  429 PHE C CG  1 
ATOM 2453 C CD1 . PHE B 2 108 ? -0.92615  29.07934 111.85464 1.000 112.86462 ?  429 PHE C CD1 1 
ATOM 2454 C CD2 . PHE B 2 108 ? -2.08066  27.01211 112.12390 1.000 108.47075 ?  429 PHE C CD2 1 
ATOM 2455 C CE1 . PHE B 2 108 ? -2.08299  29.66722 111.37945 1.000 116.34752 ?  429 PHE C CE1 1 
ATOM 2456 C CE2 . PHE B 2 108 ? -3.23967  27.59339 111.64774 1.000 108.80917 ?  429 PHE C CE2 1 
ATOM 2457 C CZ  . PHE B 2 108 ? -3.24118  28.92298 111.27570 1.000 110.24097 ?  429 PHE C CZ  1 
ATOM 2458 N N   . THR B 2 109 ? -1.10791  28.53412 115.34913 1.000 130.19744 ?  430 THR C N   1 
ATOM 2459 C CA  . THR B 2 109 ? -2.25003  28.56371 116.26411 1.000 139.15166 ?  430 THR C CA  1 
ATOM 2460 C C   . THR B 2 109 ? -3.43472  29.15596 115.50521 1.000 132.62365 ?  430 THR C C   1 
ATOM 2461 O O   . THR B 2 109 ? -3.59982  30.37750 115.44768 1.000 126.98843 ?  430 THR C O   1 
ATOM 2462 C CB  . THR B 2 109 ? -1.92900  29.36338 117.52576 1.000 143.17252 ?  430 THR C CB  1 
ATOM 2463 O OG1 . THR B 2 109 ? -0.75858  28.82249 118.15152 1.000 137.57871 ?  430 THR C OG1 1 
ATOM 2464 C CG2 . THR B 2 109 ? -3.09252  29.30282 118.50562 1.000 133.29216 ?  430 THR C CG2 1 
ATOM 2465 N N   . GLY B 2 110 ? -4.25587  28.28740 114.92268 1.000 131.27120 ?  431 GLY C N   1 
ATOM 2466 C CA  . GLY B 2 110 ? -5.41282  28.75382 114.17389 1.000 135.53097 ?  431 GLY C CA  1 
ATOM 2467 C C   . GLY B 2 110 ? -6.12465  27.61164 113.48112 1.000 131.82271 ?  431 GLY C C   1 
ATOM 2468 O O   . GLY B 2 110 ? -6.05091  26.45660 113.91612 1.000 128.24032 ?  431 GLY C O   1 
ATOM 2469 N N   . CYS B 2 111 ? -6.81590  27.95187 112.39484 1.000 124.08876 ?  432 CYS C N   1 
ATOM 2470 C CA  . CYS B 2 111 ? -7.57900  26.98307 111.62277 1.000 118.36914 ?  432 CYS C CA  1 
ATOM 2471 C C   . CYS B 2 111 ? -7.39253  27.26200 110.13815 1.000 111.91414 ?  432 CYS C C   1 
ATOM 2472 O O   . CYS B 2 111 ? -7.04683  28.37405 109.73144 1.000 110.33559 ?  432 CYS C O   1 
ATOM 2473 C CB  . CYS B 2 111 ? -9.07134  27.02258 111.98170 1.000 126.30069 ?  432 CYS C CB  1 
ATOM 2474 S SG  . CYS B 2 111 ? -9.44527  26.76025 113.73366 1.000 157.43133 ?  432 CYS C SG  1 
ATOM 2475 N N   . VAL B 2 112 ? -7.62817  26.23180 109.32952 1.000 122.46205 ?  433 VAL C N   1 
ATOM 2476 C CA  . VAL B 2 112 ? -7.54602  26.32221 107.87539 1.000 113.34942 ?  433 VAL C CA  1 
ATOM 2477 C C   . VAL B 2 112 ? -8.87850  25.85954 107.30385 1.000 108.41954 ?  433 VAL C C   1 
ATOM 2478 O O   . VAL B 2 112 ? -9.28642  24.71085 107.51771 1.000 122.85093 ?  433 VAL C O   1 
ATOM 2479 C CB  . VAL B 2 112 ? -6.38696  25.48550 107.31097 1.000 99.82253  ?  433 VAL C CB  1 
ATOM 2480 C CG1 . VAL B 2 112 ? -6.38675  25.53958 105.79112 1.000 78.64088  ?  433 VAL C CG1 1 
ATOM 2481 C CG2 . VAL B 2 112 ? -5.05737  25.97534 107.86560 1.000 96.20370  ?  433 VAL C CG2 1 
ATOM 2482 N N   . ILE B 2 113 ? -9.55299  26.74891 106.57958 1.000 99.38138  ?  434 ILE C N   1 
ATOM 2483 C CA  . ILE B 2 113 ? -10.86638 26.47933 106.00694 1.000 98.79447  ?  434 ILE C CA  1 
ATOM 2484 C C   . ILE B 2 113 ? -10.74418 26.51447 104.49077 1.000 106.13845 ?  434 ILE C C   1 
ATOM 2485 O O   . ILE B 2 113 ? -10.12446 27.42870 103.93525 1.000 101.00845 ?  434 ILE C O   1 
ATOM 2486 C CB  . ILE B 2 113 ? -11.91519 27.49523 106.49451 1.000 94.60506  ?  434 ILE C CB  1 
ATOM 2487 C CG1 . ILE B 2 113 ? -11.82594 27.66057 108.01223 1.000 108.85752 ?  434 ILE C CG1 1 
ATOM 2488 C CG2 . ILE B 2 113 ? -13.31287 27.05624 106.08660 1.000 103.98386 ?  434 ILE C CG2 1 
ATOM 2489 C CD1 . ILE B 2 113 ? -12.76263 28.70577 108.57026 1.000 102.13697 ?  434 ILE C CD1 1 
ATOM 2490 N N   . ALA B 2 114 ? -11.33546 25.52386 103.82549 1.000 110.34624 ?  435 ALA C N   1 
ATOM 2491 C CA  . ALA B 2 114 ? -11.28132 25.43913 102.37403 1.000 103.53480 ?  435 ALA C CA  1 
ATOM 2492 C C   . ALA B 2 114 ? -12.55580 24.78797 101.85856 1.000 109.54596 ?  435 ALA C C   1 
ATOM 2493 O O   . ALA B 2 114 ? -13.15544 23.94429 102.53042 1.000 119.19395 ?  435 ALA C O   1 
ATOM 2494 C CB  . ALA B 2 114 ? -10.05395 24.65198 101.89958 1.000 104.56991 ?  435 ALA C CB  1 
ATOM 2495 N N   . TRP B 2 115 ? -12.96209 25.19016 100.65569 1.000 101.61772 ?  436 TRP C N   1 
ATOM 2496 C CA  . TRP B 2 115 ? -14.14806 24.63626 100.01972 1.000 98.54390  ?  436 TRP C CA  1 
ATOM 2497 C C   . TRP B 2 115 ? -13.99548 24.74160 98.50941  1.000 101.29962 ?  436 TRP C C   1 
ATOM 2498 O O   . TRP B 2 115 ? -13.22759 25.56079 97.99810  1.000 101.03648 ?  436 TRP C O   1 
ATOM 2499 C CB  . TRP B 2 115 ? -15.42572 25.34810 100.48453 1.000 112.27056 ?  436 TRP C CB  1 
ATOM 2500 C CG  . TRP B 2 115 ? -15.51719 26.78245 100.05320 1.000 105.06405 ?  436 TRP C CG  1 
ATOM 2501 C CD1 . TRP B 2 115 ? -16.11303 27.26197 98.92255  1.000 103.81009 ?  436 TRP C CD1 1 
ATOM 2502 C CD2 . TRP B 2 115 ? -15.00120 27.92414 100.74900 1.000 100.44097 ?  436 TRP C CD2 1 
ATOM 2503 N NE1 . TRP B 2 115 ? -15.99796 28.62997 98.86996  1.000 89.60449  ?  436 TRP C NE1 1 
ATOM 2504 C CE2 . TRP B 2 115 ? -15.31953 29.06117 99.97941  1.000 97.75740  ?  436 TRP C CE2 1 
ATOM 2505 C CE3 . TRP B 2 115 ? -14.30013 28.09515 101.94668 1.000 106.52438 ?  436 TRP C CE3 1 
ATOM 2506 C CZ2 . TRP B 2 115 ? -14.96123 30.35035 100.36841 1.000 96.71485  ?  436 TRP C CZ2 1 
ATOM 2507 C CZ3 . TRP B 2 115 ? -13.94509 29.37604 102.33074 1.000 102.80901 ?  436 TRP C CZ3 1 
ATOM 2508 C CH2 . TRP B 2 115 ? -14.27617 30.48644 101.54412 1.000 97.55385  ?  436 TRP C CH2 1 
ATOM 2509 N N   . ASN B 2 116 ? -14.74120 23.89836 97.79900  1.000 103.74637 ?  437 ASN C N   1 
ATOM 2510 C CA  . ASN B 2 116 ? -14.68246 23.86892 96.34382  1.000 83.34154  ?  437 ASN C CA  1 
ATOM 2511 C C   . ASN B 2 116 ? -15.47613 25.03195 95.76147  1.000 95.19056  ?  437 ASN C C   1 
ATOM 2512 O O   . ASN B 2 116 ? -16.60547 25.29923 96.18441  1.000 95.89327  ?  437 ASN C O   1 
ATOM 2513 C CB  . ASN B 2 116 ? -15.22363 22.54042 95.81559  1.000 79.74895  ?  437 ASN C CB  1 
ATOM 2514 C CG  . ASN B 2 116 ? -15.08920 22.41209 94.30982  1.000 73.71430  ?  437 ASN C CG  1 
ATOM 2515 O OD1 . ASN B 2 116 ? -15.94115 22.88230 93.55566  1.000 85.36965  ?  437 ASN C OD1 1 
ATOM 2516 N ND2 . ASN B 2 116 ? -14.01683 21.76781 93.86477  1.000 72.07540  ?  437 ASN C ND2 1 
ATOM 2517 N N   . SER B 2 117 ? -14.88390 25.72018 94.78858  1.000 86.47795  ?  438 SER C N   1 
ATOM 2518 C CA  . SER B 2 117 ? -15.50802 26.85794 94.12345  1.000 84.78639  ?  438 SER C CA  1 
ATOM 2519 C C   . SER B 2 117 ? -15.38692 26.72727 92.61277  1.000 82.62961  ?  438 SER C C   1 
ATOM 2520 O O   . SER B 2 117 ? -15.05696 27.68735 91.91013  1.000 78.55602  ?  438 SER C O   1 
ATOM 2521 C CB  . SER B 2 117 ? -14.89730 28.17336 94.60040  1.000 77.88882  ?  438 SER C CB  1 
ATOM 2522 O OG  . SER B 2 117 ? -13.52079 28.24404 94.27239  1.000 66.13960  ?  438 SER C OG  1 
ATOM 2523 N N   . ASN B 2 118 ? -15.65349 25.52846 92.08863  1.000 86.12608  ?  439 ASN C N   1 
ATOM 2524 C CA  . ASN B 2 118 ? -15.56153 25.31705 90.64813  1.000 78.69568  ?  439 ASN C CA  1 
ATOM 2525 C C   . ASN B 2 118 ? -16.68245 26.03035 89.90311  1.000 88.73580  ?  439 ASN C C   1 
ATOM 2526 O O   . ASN B 2 118 ? -16.51913 26.38264 88.72968  1.000 85.13737  ?  439 ASN C O   1 
ATOM 2527 C CB  . ASN B 2 118 ? -15.58111 23.82016 90.33546  1.000 67.67433  ?  439 ASN C CB  1 
ATOM 2528 C CG  . ASN B 2 118 ? -15.30840 23.52469 88.87254  1.000 74.43587  ?  439 ASN C CG  1 
ATOM 2529 O OD1 . ASN B 2 118 ? -14.66153 24.30883 88.17806  1.000 80.86890  ?  439 ASN C OD1 1 
ATOM 2530 N ND2 . ASN B 2 118 ? -15.80216 22.38721 88.39703  1.000 76.82038  ?  439 ASN C ND2 1 
ATOM 2531 N N   . ASN B 2 119 ? -17.81728 26.25674 90.56123  1.000 87.47153  ?  440 ASN C N   1 
ATOM 2532 C CA  . ASN B 2 119 ? -18.94738 26.93219 89.93739  1.000 90.57152  ?  440 ASN C CA  1 
ATOM 2533 C C   . ASN B 2 119 ? -18.78070 28.44526 89.87967  1.000 90.94579  ?  440 ASN C C   1 
ATOM 2534 O O   . ASN B 2 119 ? -19.64591 29.12444 89.31648  1.000 93.90178  ?  440 ASN C O   1 
ATOM 2535 C CB  . ASN B 2 119 ? -20.23907 26.58399 90.68199  1.000 95.82595  ?  440 ASN C CB  1 
ATOM 2536 C CG  . ASN B 2 119 ? -20.19262 26.98001 92.14452  1.000 108.83494 ?  440 ASN C CG  1 
ATOM 2537 O OD1 . ASN B 2 119 ? -19.62454 26.26967 92.97416  1.000 108.60152 ?  440 ASN C OD1 1 
ATOM 2538 N ND2 . ASN B 2 119 ? -20.79475 28.11821 92.46887  1.000 100.57178 ?  440 ASN C ND2 1 
ATOM 2539 N N   . LEU B 2 120 ? -17.69931 28.98800 90.43966  1.000 87.29739  ?  441 LEU C N   1 
ATOM 2540 C CA  . LEU B 2 120 ? -17.46930 30.42894 90.44903  1.000 78.15640  ?  441 LEU C CA  1 
ATOM 2541 C C   . LEU B 2 120 ? -16.20487 30.81033 89.69211  1.000 85.90700  ?  441 LEU C C   1 
ATOM 2542 O O   . LEU B 2 120 ? -16.27976 31.56913 88.72018  1.000 84.58644  ?  441 LEU C O   1 
ATOM 2543 C CB  . LEU B 2 120 ? -17.40324 30.94083 91.89417  1.000 62.74139  ?  441 LEU C CB  1 
ATOM 2544 C CG  . LEU B 2 120 ? -18.65459 30.74855 92.75169  1.000 88.42368  ?  441 LEU C CG  1 
ATOM 2545 C CD1 . LEU B 2 120 ? -18.41799 31.25916 94.16456  1.000 78.81245  ?  441 LEU C CD1 1 
ATOM 2546 C CD2 . LEU B 2 120 ? -19.85001 31.44400 92.11940  1.000 90.60396  ?  441 LEU C CD2 1 
ATOM 2547 N N   . ASP B 2 121 ? -15.04391 30.30717 90.10651  1.000 81.88709  ?  442 ASP C N   1 
ATOM 2548 C CA  . ASP B 2 121 ? -13.76854 30.68712 89.49888  1.000 75.75997  ?  442 ASP C CA  1 
ATOM 2549 C C   . ASP B 2 121 ? -13.37294 29.69181 88.40627  1.000 79.35568  ?  442 ASP C C   1 
ATOM 2550 O O   . ASP B 2 121 ? -12.35726 29.00101 88.48328  1.000 75.04529  ?  442 ASP C O   1 
ATOM 2551 C CB  . ASP B 2 121 ? -12.68956 30.79215 90.56991  1.000 70.99950  ?  442 ASP C CB  1 
ATOM 2552 C CG  . ASP B 2 121 ? -13.08714 31.70992 91.70801  1.000 84.08028  ?  442 ASP C CG  1 
ATOM 2553 O OD1 . ASP B 2 121 ? -13.79309 32.70766 91.45029  1.000 92.14704  ?  442 ASP C OD1 1 
ATOM 2554 O OD2 . ASP B 2 121 ? -12.69583 31.43184 92.86111  1.000 79.29525  -1 442 ASP C OD2 1 
ATOM 2555 N N   . SER B 2 122 ? -14.20652 29.63473 87.36456  1.000 80.82150  ?  443 SER C N   1 
ATOM 2556 C CA  . SER B 2 122 ? -13.95966 28.72558 86.24617  1.000 68.19224  ?  443 SER C CA  1 
ATOM 2557 C C   . SER B 2 122 ? -14.78684 29.21193 85.05601  1.000 82.37285  ?  443 SER C C   1 
ATOM 2558 O O   . SER B 2 122 ? -15.99009 28.94698 84.98940  1.000 98.99463  ?  443 SER C O   1 
ATOM 2559 C CB  . SER B 2 122 ? -14.30583 27.29279 86.61742  1.000 57.41167  ?  443 SER C CB  1 
ATOM 2560 O OG  . SER B 2 122 ? -14.10084 26.41841 85.52290  1.000 81.81339  ?  443 SER C OG  1 
ATOM 2561 N N   . LYS B 2 123 ? -14.13514 29.91501 84.13356  1.000 86.34062  ?  444 LYS C N   1 
ATOM 2562 C CA  . LYS B 2 123 ? -14.80692 30.35733 82.92276  1.000 69.59941  ?  444 LYS C CA  1 
ATOM 2563 C C   . LYS B 2 123 ? -15.01841 29.18285 81.97098  1.000 76.03858  ?  444 LYS C C   1 
ATOM 2564 O O   . LYS B 2 123 ? -14.40143 28.12167 82.09951  1.000 82.47901  ?  444 LYS C O   1 
ATOM 2565 C CB  . LYS B 2 123 ? -14.00243 31.45637 82.22728  1.000 83.07746  ?  444 LYS C CB  1 
ATOM 2566 C CG  . LYS B 2 123 ? -13.92246 32.76395 83.00003  1.000 93.52078  ?  444 LYS C CG  1 
ATOM 2567 C CD  . LYS B 2 123 ? -13.17490 33.82439 82.20466  1.000 103.99128 ?  444 LYS C CD  1 
ATOM 2568 C CE  . LYS B 2 123 ? -13.13572 35.15208 82.94411  1.000 100.08480 ?  444 LYS C CE  1 
ATOM 2569 N NZ  . LYS B 2 123 ? -12.40973 36.19586 82.16818  1.000 99.57782  ?  444 LYS C NZ  1 
ATOM 2570 N N   . VAL B 2 124 ? -15.91070 29.38747 80.99938  1.000 94.04684  ?  445 VAL C N   1 
ATOM 2571 C CA  . VAL B 2 124 ? -16.19726 28.33408 80.03125  1.000 94.48713  ?  445 VAL C CA  1 
ATOM 2572 C C   . VAL B 2 124 ? -15.01729 28.13286 79.08698  1.000 95.17529  ?  445 VAL C C   1 
ATOM 2573 O O   . VAL B 2 124 ? -14.78510 27.01924 78.59973  1.000 114.68002 ?  445 VAL C O   1 
ATOM 2574 C CB  . VAL B 2 124 ? -17.49847 28.65432 79.26865  1.000 92.99195  ?  445 VAL C CB  1 
ATOM 2575 C CG1 . VAL B 2 124 ? -17.36673 29.96065 78.49614  1.000 111.14189 ?  445 VAL C CG1 1 
ATOM 2576 C CG2 . VAL B 2 124 ? -17.88047 27.50671 78.34232  1.000 99.42813  ?  445 VAL C CG2 1 
ATOM 2577 N N   . GLY B 2 125 ? -14.24575 29.18447 78.82752  1.000 70.23338  ?  446 GLY C N   1 
ATOM 2578 C CA  . GLY B 2 125 ? -13.08962 29.11402 77.96066  1.000 80.52400  ?  446 GLY C CA  1 
ATOM 2579 C C   . GLY B 2 125 ? -11.75238 29.05974 78.66574  1.000 80.90581  ?  446 GLY C C   1 
ATOM 2580 O O   . GLY B 2 125 ? -10.71548 29.14592 77.99711  1.000 86.10424  ?  446 GLY C O   1 
ATOM 2581 N N   . GLY B 2 126 ? -11.73510 28.92138 79.98891  1.000 73.92505  ?  447 GLY C N   1 
ATOM 2582 C CA  . GLY B 2 126 ? -10.48831 28.86173 80.72513  1.000 86.70518  ?  447 GLY C CA  1 
ATOM 2583 C C   . GLY B 2 126 ? -10.22811 30.09544 81.56349  1.000 88.38118  ?  447 GLY C C   1 
ATOM 2584 O O   . GLY B 2 126 ? -10.02907 31.18940 81.02656  1.000 91.83093  ?  447 GLY C O   1 
ATOM 2585 N N   . ASN B 2 127 ? -10.22561 29.93134 82.88553  1.000 85.49675  ?  448 ASN C N   1 
ATOM 2586 C CA  . ASN B 2 127 ? -9.98610  31.03928 83.80981  1.000 93.40890  ?  448 ASN C CA  1 
ATOM 2587 C C   . ASN B 2 127 ? -8.49847  31.07366 84.13511  1.000 93.91883  ?  448 ASN C C   1 
ATOM 2588 O O   . ASN B 2 127 ? -8.02788  30.43332 85.07648  1.000 78.19113  ?  448 ASN C O   1 
ATOM 2589 C CB  . ASN B 2 127 ? -10.83703 30.88924 85.06462  1.000 86.97665  ?  448 ASN C CB  1 
ATOM 2590 C CG  . ASN B 2 127 ? -10.67562 32.05454 86.02195  1.000 93.54500  ?  448 ASN C CG  1 
ATOM 2591 O OD1 . ASN B 2 127 ? -10.22198 33.13254 85.63703  1.000 92.33679  ?  448 ASN C OD1 1 
ATOM 2592 N ND2 . ASN B 2 127 ? -11.05001 31.84323 87.27821  1.000 95.42428  ?  448 ASN C ND2 1 
ATOM 2593 N N   . TYR B 2 128 ? -7.74790  31.83431 83.34222  1.000 93.55993  ?  449 TYR C N   1 
ATOM 2594 C CA  . TYR B 2 128 ? -6.31270  31.98733 83.53141  1.000 77.43123  ?  449 TYR C CA  1 
ATOM 2595 C C   . TYR B 2 128 ? -5.95815  33.17463 84.41875  1.000 79.17250  ?  449 TYR C C   1 
ATOM 2596 O O   . TYR B 2 128 ? -4.79147  33.57880 84.45429  1.000 76.27105  ?  449 TYR C O   1 
ATOM 2597 C CB  . TYR B 2 128 ? -5.61486  32.12711 82.17518  1.000 77.40170  ?  449 TYR C CB  1 
ATOM 2598 C CG  . TYR B 2 128 ? -5.76381  30.91936 81.27593  1.000 85.77956  ?  449 TYR C CG  1 
ATOM 2599 C CD1 . TYR B 2 128 ? -6.84202  30.80347 80.40789  1.000 89.83752  ?  449 TYR C CD1 1 
ATOM 2600 C CD2 . TYR B 2 128 ? -4.82351  29.89726 81.29213  1.000 86.78396  ?  449 TYR C CD2 1 
ATOM 2601 C CE1 . TYR B 2 128 ? -6.98118  29.70217 79.58352  1.000 87.13368  ?  449 TYR C CE1 1 
ATOM 2602 C CE2 . TYR B 2 128 ? -4.95400  28.79243 80.47128  1.000 78.99011  ?  449 TYR C CE2 1 
ATOM 2603 C CZ  . TYR B 2 128 ? -6.03439  28.70020 79.61933  1.000 85.77999  ?  449 TYR C CZ  1 
ATOM 2604 O OH  . TYR B 2 128 ? -6.16839  27.60236 78.80060  1.000 76.79458  ?  449 TYR C OH  1 
ATOM 2605 N N   . ASN B 2 129 ? -6.93319  33.73919 85.13436  1.000 85.10868  ?  450 ASN C N   1 
ATOM 2606 C CA  . ASN B 2 129 ? -6.67661  34.89726 85.98129  1.000 60.73061  ?  450 ASN C CA  1 
ATOM 2607 C C   . ASN B 2 129 ? -5.97253  34.53583 87.28229  1.000 62.90581  ?  450 ASN C C   1 
ATOM 2608 O O   . ASN B 2 129 ? -5.33383  35.40485 87.88547  1.000 73.40815  ?  450 ASN C O   1 
ATOM 2609 C CB  . ASN B 2 129 ? -7.98763  35.62323 86.29348  1.000 81.24117  ?  450 ASN C CB  1 
ATOM 2610 C CG  . ASN B 2 129 ? -8.66949  36.15698 85.04850  1.000 101.48791 ?  450 ASN C CG  1 
ATOM 2611 O OD1 . ASN B 2 129 ? -8.39503  37.27262 84.60625  1.000 99.28391  ?  450 ASN C OD1 1 
ATOM 2612 N ND2 . ASN B 2 129 ? -9.56592  35.36098 84.47708  1.000 106.85176 ?  450 ASN C ND2 1 
ATOM 2613 N N   . TYR B 2 130 ? -6.07365  33.28677 87.72875  1.000 74.50529  ?  451 TYR C N   1 
ATOM 2614 C CA  . TYR B 2 130 ? -5.41909  32.84912 88.95403  1.000 73.39215  ?  451 TYR C CA  1 
ATOM 2615 C C   . TYR B 2 130 ? -4.04451  32.27997 88.62974  1.000 63.88719  ?  451 TYR C C   1 
ATOM 2616 O O   . TYR B 2 130 ? -3.91419  31.40464 87.76795  1.000 53.71284  ?  451 TYR C O   1 
ATOM 2617 C CB  . TYR B 2 130 ? -6.27135  31.80929 89.68181  1.000 81.38045  ?  451 TYR C CB  1 
ATOM 2618 C CG  . TYR B 2 130 ? -7.53025  32.38336 90.28891  1.000 75.98717  ?  451 TYR C CG  1 
ATOM 2619 C CD1 . TYR B 2 130 ? -7.52163  32.92458 91.56753  1.000 82.07094  ?  451 TYR C CD1 1 
ATOM 2620 C CD2 . TYR B 2 130 ? -8.72499  32.39156 89.58218  1.000 71.41630  ?  451 TYR C CD2 1 
ATOM 2621 C CE1 . TYR B 2 130 ? -8.66803  33.45505 92.12666  1.000 78.21231  ?  451 TYR C CE1 1 
ATOM 2622 C CE2 . TYR B 2 130 ? -9.87689  32.91976 90.13351  1.000 82.94201  ?  451 TYR C CE2 1 
ATOM 2623 C CZ  . TYR B 2 130 ? -9.84258  33.44925 91.40616  1.000 76.64381  ?  451 TYR C CZ  1 
ATOM 2624 O OH  . TYR B 2 130 ? -10.98603 33.97655 91.96052  1.000 70.99284  ?  451 TYR C OH  1 
ATOM 2625 N N   . LEU B 2 131 ? -3.02591  32.77915 89.32201  1.000 77.35080  ?  452 LEU C N   1 
ATOM 2626 C CA  . LEU B 2 131 ? -1.64258  32.40144 89.08212  1.000 71.24844  ?  452 LEU C CA  1 
ATOM 2627 C C   . LEU B 2 131 ? -1.04917  31.76017 90.33019  1.000 66.73328  ?  452 LEU C C   1 
ATOM 2628 O O   . LEU B 2 131 ? -1.67018  31.71476 91.39544  1.000 80.89415  ?  452 LEU C O   1 
ATOM 2629 C CB  . LEU B 2 131 ? -0.80396  33.61795 88.66642  1.000 56.14857  ?  452 LEU C CB  1 
ATOM 2630 C CG  . LEU B 2 131 ? -1.31094  34.44662 87.48445  1.000 46.89726  ?  452 LEU C CG  1 
ATOM 2631 C CD1 . LEU B 2 131 ? -0.42190  35.65970 87.26406  1.000 60.75686  ?  452 LEU C CD1 1 
ATOM 2632 C CD2 . LEU B 2 131 ? -1.38668  33.60272 86.22403  1.000 45.53895  ?  452 LEU C CD2 1 
ATOM 2633 N N   . TYR B 2 132 ? 0.17446   31.25956 90.17895  1.000 56.25207  ?  453 TYR C N   1 
ATOM 2634 C CA  . TYR B 2 132 ? 0.93038   30.70107 91.29055  1.000 53.65000  ?  453 TYR C CA  1 
ATOM 2635 C C   . TYR B 2 132 ? 2.40463   30.71846 90.91888  1.000 61.51675  ?  453 TYR C C   1 
ATOM 2636 O O   . TYR B 2 132 ? 2.76533   30.76986 89.74014  1.000 69.75075  ?  453 TYR C O   1 
ATOM 2637 C CB  . TYR B 2 132 ? 0.46937   29.28053 91.63895  1.000 59.97708  ?  453 TYR C CB  1 
ATOM 2638 C CG  . TYR B 2 132 ? 0.76059   28.25118 90.57012  1.000 57.69866  ?  453 TYR C CG  1 
ATOM 2639 C CD1 . TYR B 2 132 ? -0.08566  28.09391 89.48082  1.000 61.35969  ?  453 TYR C CD1 1 
ATOM 2640 C CD2 . TYR B 2 132 ? 1.87677   27.42959 90.65596  1.000 53.34681  ?  453 TYR C CD2 1 
ATOM 2641 C CE1 . TYR B 2 132 ? 0.17510   27.15269 88.50291  1.000 61.94933  ?  453 TYR C CE1 1 
ATOM 2642 C CE2 . TYR B 2 132 ? 2.14487   26.48575 89.68455  1.000 55.77692  ?  453 TYR C CE2 1 
ATOM 2643 C CZ  . TYR B 2 132 ? 1.29184   26.35145 88.60985  1.000 61.62301  ?  453 TYR C CZ  1 
ATOM 2644 O OH  . TYR B 2 132 ? 1.55625   25.41215 87.63953  1.000 59.48941  ?  453 TYR C OH  1 
ATOM 2645 N N   . ARG B 2 133 ? 3.25210   30.67522 91.94175  1.000 67.40811  ?  454 ARG C N   1 
ATOM 2646 C CA  . ARG B 2 133 ? 4.69581   30.75527 91.76728  1.000 59.37204  ?  454 ARG C CA  1 
ATOM 2647 C C   . ARG B 2 133 ? 5.31626   29.37513 91.93650  1.000 57.89652  ?  454 ARG C C   1 
ATOM 2648 O O   . ARG B 2 133 ? 5.06954   28.69623 92.93900  1.000 76.18849  ?  454 ARG C O   1 
ATOM 2649 C CB  . ARG B 2 133 ? 5.30864   31.73640 92.76758  1.000 56.10375  ?  454 ARG C CB  1 
ATOM 2650 C CG  . ARG B 2 133 ? 6.80933   31.91701 92.62373  1.000 62.52776  ?  454 ARG C CG  1 
ATOM 2651 C CD  . ARG B 2 133 ? 7.34744   32.85520 93.68925  1.000 67.41669  ?  454 ARG C CD  1 
ATOM 2652 N NE  . ARG B 2 133 ? 6.64661   34.13557 93.69094  1.000 71.22197  ?  454 ARG C NE  1 
ATOM 2653 C CZ  . ARG B 2 133 ? 7.00257   35.18259 92.95433  1.000 74.65890  ?  454 ARG C CZ  1 
ATOM 2654 N NH1 . ARG B 2 133 ? 8.05612   35.10425 92.15257  1.000 77.20655  ?  454 ARG C NH1 1 
ATOM 2655 N NH2 . ARG B 2 133 ? 6.30566   36.30870 93.01946  1.000 74.36748  ?  454 ARG C NH2 1 
ATOM 2656 N N   . LEU B 2 134 ? 6.11758   28.96397 90.95358  1.000 44.21468  ?  455 LEU C N   1 
ATOM 2657 C CA  . LEU B 2 134 ? 6.84176   27.70342 91.02055  1.000 70.36780  ?  455 LEU C CA  1 
ATOM 2658 C C   . LEU B 2 134 ? 8.34158   27.86595 90.81831  1.000 66.15595  ?  455 LEU C C   1 
ATOM 2659 O O   . LEU B 2 134 ? 9.05991   26.85940 90.79438  1.000 68.04252  ?  455 LEU C O   1 
ATOM 2660 C CB  . LEU B 2 134 ? 6.28101   26.70550 89.99246  1.000 77.97357  ?  455 LEU C CB  1 
ATOM 2661 C CG  . LEU B 2 134 ? 6.20110   27.06455 88.50349  1.000 57.56503  ?  455 LEU C CG  1 
ATOM 2662 C CD1 . LEU B 2 134 ? 7.51833   26.82454 87.79202  1.000 48.37819  ?  455 LEU C CD1 1 
ATOM 2663 C CD2 . LEU B 2 134 ? 5.09538   26.27148 87.82819  1.000 66.35917  ?  455 LEU C CD2 1 
ATOM 2664 N N   . PHE B 2 135 ? 8.83430   29.09496 90.67300  1.000 68.85000  ?  456 PHE C N   1 
ATOM 2665 C CA  . PHE B 2 135 ? 10.25460  29.36321 90.46682  1.000 67.34913  ?  456 PHE C CA  1 
ATOM 2666 C C   . PHE B 2 135 ? 10.71140  30.39706 91.48765  1.000 71.60141  ?  456 PHE C C   1 
ATOM 2667 O O   . PHE B 2 135 ? 10.31817  31.56597 91.41171  1.000 73.58873  ?  456 PHE C O   1 
ATOM 2668 C CB  . PHE B 2 135 ? 10.52334  29.85002 89.04168  1.000 67.04199  ?  456 PHE C CB  1 
ATOM 2669 C CG  . PHE B 2 135 ? 10.56541  28.74909 88.01929  1.000 57.65753  ?  456 PHE C CG  1 
ATOM 2670 C CD1 . PHE B 2 135 ? 11.01344  27.48332 88.36046  1.000 64.70769  ?  456 PHE C CD1 1 
ATOM 2671 C CD2 . PHE B 2 135 ? 10.16028  28.98196 86.71515  1.000 54.58553  ?  456 PHE C CD2 1 
ATOM 2672 C CE1 . PHE B 2 135 ? 11.05534  26.46927 87.42017  1.000 53.39380  ?  456 PHE C CE1 1 
ATOM 2673 C CE2 . PHE B 2 135 ? 10.19884  27.97264 85.77039  1.000 61.69153  ?  456 PHE C CE2 1 
ATOM 2674 C CZ  . PHE B 2 135 ? 10.64729  26.71447 86.12359  1.000 50.66398  ?  456 PHE C CZ  1 
ATOM 2675 N N   . ARG B 2 136 ? 11.53685  29.96641 92.43961  1.000 67.41703  ?  457 ARG C N   1 
ATOM 2676 C CA  . ARG B 2 136 ? 12.13575  30.86467 93.41605  1.000 66.29563  ?  457 ARG C CA  1 
ATOM 2677 C C   . ARG B 2 136 ? 13.42884  30.24131 93.91763  1.000 71.40335  ?  457 ARG C C   1 
ATOM 2678 O O   . ARG B 2 136 ? 13.48096  29.03869 94.18893  1.000 86.31218  ?  457 ARG C O   1 
ATOM 2679 C CB  . ARG B 2 136 ? 11.19144  31.14701 94.59098  1.000 73.63857  ?  457 ARG C CB  1 
ATOM 2680 C CG  . ARG B 2 136 ? 10.90410  32.62594 94.80908  1.000 76.64318  ?  457 ARG C CG  1 
ATOM 2681 C CD  . ARG B 2 136 ? 10.08625  32.86161 96.07050  1.000 80.26484  ?  457 ARG C CD  1 
ATOM 2682 N NE  . ARG B 2 136 ? 10.91594  32.90294 97.27111  1.000 88.29907  ?  457 ARG C NE  1 
ATOM 2683 C CZ  . ARG B 2 136 ? 11.41534  34.01906 97.79228  1.000 93.43051  ?  457 ARG C CZ  1 
ATOM 2684 N NH1 . ARG B 2 136 ? 12.15936  33.96796 98.88888  1.000 104.94770 ?  457 ARG C NH1 1 
ATOM 2685 N NH2 . ARG B 2 136 ? 11.16769  35.18845 97.21777  1.000 79.25484  ?  457 ARG C NH2 1 
ATOM 2686 N N   . LYS B 2 137 ? 14.46681  31.06580 94.03877  1.000 73.09502  ?  458 LYS C N   1 
ATOM 2687 C CA  . LYS B 2 137 ? 15.78616  30.60187 94.44866  1.000 80.16182  ?  458 LYS C CA  1 
ATOM 2688 C C   . LYS B 2 137 ? 15.91950  30.42928 95.95782  1.000 82.15928  ?  458 LYS C C   1 
ATOM 2689 O O   . LYS B 2 137 ? 17.02530  30.15479 96.43680  1.000 81.74655  ?  458 LYS C O   1 
ATOM 2690 C CB  . LYS B 2 137 ? 16.86114  31.56566 93.93840  1.000 75.87991  ?  458 LYS C CB  1 
ATOM 2691 C CG  . LYS B 2 137 ? 16.65866  33.00988 94.36648  1.000 68.50903  ?  458 LYS C CG  1 
ATOM 2692 C CD  . LYS B 2 137 ? 17.73866  33.90907 93.78668  1.000 83.56413  ?  458 LYS C CD  1 
ATOM 2693 C CE  . LYS B 2 137 ? 17.54337  35.35579 94.20937  1.000 84.08788  ?  458 LYS C CE  1 
ATOM 2694 N NZ  . LYS B 2 137 ? 18.59263  36.24570 93.63882  1.000 76.15397  ?  458 LYS C NZ  1 
ATOM 2695 N N   . SER B 2 138 ? 14.83213  30.57878 96.71124  1.000 84.00574  ?  459 SER C N   1 
ATOM 2696 C CA  . SER B 2 138 ? 14.87046  30.40064 98.15537  1.000 91.65101  ?  459 SER C CA  1 
ATOM 2697 C C   . SER B 2 138 ? 13.45907  30.13244 98.65543  1.000 90.26132  ?  459 SER C C   1 
ATOM 2698 O O   . SER B 2 138 ? 12.49657  30.72132 98.15614  1.000 86.54123  ?  459 SER C O   1 
ATOM 2699 C CB  . SER B 2 138 ? 15.46105  31.62923 98.85784  1.000 87.33444  ?  459 SER C CB  1 
ATOM 2700 O OG  . SER B 2 138 ? 14.70457  32.79277 98.57359  1.000 111.49061 ?  459 SER C OG  1 
ATOM 2701 N N   . ASN B 2 139 ? 13.34653  29.24165 99.63727  1.000 88.57692  ?  460 ASN C N   1 
ATOM 2702 C CA  . ASN B 2 139 ? 12.04767  28.92177 100.20941 1.000 85.91802  ?  460 ASN C CA  1 
ATOM 2703 C C   . ASN B 2 139 ? 11.51908  30.09806 101.02180 1.000 95.26088  ?  460 ASN C C   1 
ATOM 2704 O O   . ASN B 2 139 ? 12.27606  30.82690 101.66839 1.000 103.96552 ?  460 ASN C O   1 
ATOM 2705 C CB  . ASN B 2 139 ? 12.14119  27.67601 101.09022 1.000 78.32265  ?  460 ASN C CB  1 
ATOM 2706 C CG  . ASN B 2 139 ? 12.62759  26.45972 100.32911 1.000 87.47283  ?  460 ASN C CG  1 
ATOM 2707 O OD1 . ASN B 2 139 ? 11.83291  25.70599 99.76859  1.000 76.32093  ?  460 ASN C OD1 1 
ATOM 2708 N ND2 . ASN B 2 139 ? 13.94065  26.26157 100.30613 1.000 92.53383  ?  460 ASN C ND2 1 
ATOM 2709 N N   . LEU B 2 140 ? 10.20216  30.27962 100.98039 1.000 96.65604  ?  461 LEU C N   1 
ATOM 2710 C CA  . LEU B 2 140 ? 9.57862   31.39059 101.68300 1.000 92.70799  ?  461 LEU C CA  1 
ATOM 2711 C C   . LEU B 2 140 ? 9.53555   31.13586 103.18500 1.000 92.58522  ?  461 LEU C C   1 
ATOM 2712 O O   . LEU B 2 140 ? 9.39858   29.99973 103.64630 1.000 95.58548  ?  461 LEU C O   1 
ATOM 2713 C CB  . LEU B 2 140 ? 8.16097   31.63197 101.16147 1.000 89.55290  ?  461 LEU C CB  1 
ATOM 2714 C CG  . LEU B 2 140 ? 8.02096   32.43180 99.86632  1.000 95.75122  ?  461 LEU C CG  1 
ATOM 2715 C CD1 . LEU B 2 140 ? 6.55504   32.64126 99.53219  1.000 76.50695  ?  461 LEU C CD1 1 
ATOM 2716 C CD2 . LEU B 2 140 ? 8.73781   33.76564 99.98524  1.000 92.09385  ?  461 LEU C CD2 1 
ATOM 2717 N N   . LYS B 2 141 ? 9.66126   32.21563 103.94682 1.000 98.87201  ?  462 LYS C N   1 
ATOM 2718 C CA  . LYS B 2 141 ? 9.49797   32.16877 105.38756 1.000 98.11034  ?  462 LYS C CA  1 
ATOM 2719 C C   . LYS B 2 141 ? 8.01275   32.12469 105.73733 1.000 94.93948  ?  462 LYS C C   1 
ATOM 2720 O O   . LYS B 2 141 ? 7.16224   32.44086 104.90187 1.000 96.48064  ?  462 LYS C O   1 
ATOM 2721 C CB  . LYS B 2 141 ? 10.17033  33.38291 106.02347 1.000 89.96099  ?  462 LYS C CB  1 
ATOM 2722 C CG  . LYS B 2 141 ? 11.65634  33.49160 105.71405 1.000 85.10580  ?  462 LYS C CG  1 
ATOM 2723 C CD  . LYS B 2 141 ? 12.26938  34.73433 106.33846 1.000 99.53988  ?  462 LYS C CD  1 
ATOM 2724 C CE  . LYS B 2 141 ? 13.75023  34.84149 106.00843 1.000 98.60450  ?  462 LYS C CE  1 
ATOM 2725 N NZ  . LYS B 2 141 ? 14.37186  36.05315 106.61076 1.000 97.14706  ?  462 LYS C NZ  1 
ATOM 2726 N N   . PRO B 2 142 ? 7.66777   31.71139 106.95726 1.000 100.03009 ?  463 PRO C N   1 
ATOM 2727 C CA  . PRO B 2 142 ? 6.25045   31.69028 107.34527 1.000 100.74562 ?  463 PRO C CA  1 
ATOM 2728 C C   . PRO B 2 142 ? 5.63859   33.08357 107.29405 1.000 96.46844  ?  463 PRO C C   1 
ATOM 2729 O O   . PRO B 2 142 ? 6.22866   34.05824 107.76646 1.000 104.13375 ?  463 PRO C O   1 
ATOM 2730 C CB  . PRO B 2 142 ? 6.27950   31.13168 108.77420 1.000 96.61228  ?  463 PRO C CB  1 
ATOM 2731 C CG  . PRO B 2 142 ? 7.69215   31.30947 109.23731 1.000 93.60033  ?  463 PRO C CG  1 
ATOM 2732 C CD  . PRO B 2 142 ? 8.52792   31.14665 108.01070 1.000 94.61274  ?  463 PRO C CD  1 
ATOM 2733 N N   . PHE B 2 143 ? 4.44533   33.16593 106.69944 1.000 93.26472  ?  464 PHE C N   1 
ATOM 2734 C CA  . PHE B 2 143 ? 3.70482   34.42216 106.55745 1.000 99.70665  ?  464 PHE C CA  1 
ATOM 2735 C C   . PHE B 2 143 ? 4.49392   35.45108 105.74974 1.000 97.66926  ?  464 PHE C C   1 
ATOM 2736 O O   . PHE B 2 143 ? 4.50506   36.64180 106.06836 1.000 102.86063 ?  464 PHE C O   1 
ATOM 2737 C CB  . PHE B 2 143 ? 3.30648   34.99131 107.92194 1.000 109.90548 ?  464 PHE C CB  1 
ATOM 2738 C CG  . PHE B 2 143 ? 2.30373   34.15164 108.66040 1.000 118.15397 ?  464 PHE C CG  1 
ATOM 2739 C CD1 . PHE B 2 143 ? 1.38657   33.37677 107.97016 1.000 115.94682 ?  464 PHE C CD1 1 
ATOM 2740 C CD2 . PHE B 2 143 ? 2.27933   34.13623 110.04518 1.000 120.28584 ?  464 PHE C CD2 1 
ATOM 2741 C CE1 . PHE B 2 143 ? 0.46255   32.60365 108.64720 1.000 114.31165 ?  464 PHE C CE1 1 
ATOM 2742 C CE2 . PHE B 2 143 ? 1.35822   33.36449 110.72802 1.000 115.37387 ?  464 PHE C CE2 1 
ATOM 2743 C CZ  . PHE B 2 143 ? 0.44881   32.59712 110.02781 1.000 111.82558 ?  464 PHE C CZ  1 
ATOM 2744 N N   . GLU B 2 144 ? 5.15607   34.99113 104.69196 1.000 92.49597  ?  465 GLU C N   1 
ATOM 2745 C CA  . GLU B 2 144 ? 5.89852   35.85945 103.79002 1.000 97.09093  ?  465 GLU C CA  1 
ATOM 2746 C C   . GLU B 2 144 ? 5.15525   35.97293 102.46594 1.000 88.90793  ?  465 GLU C C   1 
ATOM 2747 O O   . GLU B 2 144 ? 4.57406   34.99596 101.98277 1.000 87.26095  ?  465 GLU C O   1 
ATOM 2748 C CB  . GLU B 2 144 ? 7.31844   35.33400 103.55617 1.000 110.10537 ?  465 GLU C CB  1 
ATOM 2749 C CG  . GLU B 2 144 ? 8.23710   36.31762 102.84555 1.000 111.50603 ?  465 GLU C CG  1 
ATOM 2750 C CD  . GLU B 2 144 ? 9.66401   35.81407 102.73826 1.000 107.16626 ?  465 GLU C CD  1 
ATOM 2751 O OE1 . GLU B 2 144 ? 9.89628   34.61685 103.00701 1.000 113.79973 ?  465 GLU C OE1 1 
ATOM 2752 O OE2 . GLU B 2 144 ? 10.55458  36.61686 102.38777 1.000 92.59730  -1 465 GLU C OE2 1 
ATOM 2753 N N   . ARG B 2 145 ? 5.17652   37.16957 101.88439 1.000 86.28528  ?  466 ARG C N   1 
ATOM 2754 C CA  . ARG B 2 145 ? 4.43879   37.47432 100.66470 1.000 89.49265  ?  466 ARG C CA  1 
ATOM 2755 C C   . ARG B 2 145 ? 5.41576   37.99645 99.62113  1.000 87.11039  ?  466 ARG C C   1 
ATOM 2756 O O   . ARG B 2 145 ? 6.11738   38.98443 99.86361  1.000 86.51379  ?  466 ARG C O   1 
ATOM 2757 C CB  . ARG B 2 145 ? 3.33485   38.49655 100.94572 1.000 100.02770 ?  466 ARG C CB  1 
ATOM 2758 C CG  . ARG B 2 145 ? 2.29666   38.63868 99.84768  1.000 88.14709  ?  466 ARG C CG  1 
ATOM 2759 C CD  . ARG B 2 145 ? 1.08077   39.39785 100.35923 1.000 80.88877  ?  466 ARG C CD  1 
ATOM 2760 N NE  . ARG B 2 145 ? 0.08171   39.61845 99.31811  1.000 83.55600  ?  466 ARG C NE  1 
ATOM 2761 C CZ  . ARG B 2 145 ? -0.04735  40.75172 98.63616  1.000 91.18905  ?  466 ARG C CZ  1 
ATOM 2762 N NH1 . ARG B 2 145 ? 0.75993   41.77341 98.88635  1.000 91.10804  ?  466 ARG C NH1 1 
ATOM 2763 N NH2 . ARG B 2 145 ? -0.98544  40.86548 97.70588  1.000 93.80118  ?  466 ARG C NH2 1 
ATOM 2764 N N   . ASP B 2 146 ? 5.46114   37.33423 98.46587  1.000 78.53156  ?  467 ASP C N   1 
ATOM 2765 C CA  . ASP B 2 146 ? 6.39732   37.66533 97.39494  1.000 72.76407  ?  467 ASP C CA  1 
ATOM 2766 C C   . ASP B 2 146 ? 5.60555   37.95479 96.12575  1.000 75.91695  ?  467 ASP C C   1 
ATOM 2767 O O   . ASP B 2 146 ? 4.99636   37.04792 95.54780  1.000 72.93291  ?  467 ASP C O   1 
ATOM 2768 C CB  . ASP B 2 146 ? 7.39646   36.52874 97.17532  1.000 90.77383  ?  467 ASP C CB  1 
ATOM 2769 C CG  . ASP B 2 146 ? 8.48026   36.88642 96.17544  1.000 80.55019  ?  467 ASP C CG  1 
ATOM 2770 O OD1 . ASP B 2 146 ? 9.23928   37.84344 96.43536  1.000 99.24413  ?  467 ASP C OD1 1 
ATOM 2771 O OD2 . ASP B 2 146 ? 8.57968   36.20508 95.13367  1.000 75.41016  -1 467 ASP C OD2 1 
ATOM 2772 N N   . ILE B 2 147 ? 5.61634   39.21594 95.69456  1.000 87.93567  ?  468 ILE C N   1 
ATOM 2773 C CA  . ILE B 2 147 ? 4.91875   39.63237 94.48234  1.000 73.84180  ?  468 ILE C CA  1 
ATOM 2774 C C   . ILE B 2 147 ? 5.95843   39.96953 93.42137  1.000 75.71920  ?  468 ILE C C   1 
ATOM 2775 O O   . ILE B 2 147 ? 5.71731   40.79407 92.53220  1.000 82.47135  ?  468 ILE C O   1 
ATOM 2776 C CB  . ILE B 2 147 ? 3.98812   40.83000 94.75291  1.000 63.98065  ?  468 ILE C CB  1 
ATOM 2777 C CG1 . ILE B 2 147 ? 3.38651   40.73463 96.15522  1.000 73.53307  ?  468 ILE C CG1 1 
ATOM 2778 C CG2 . ILE B 2 147 ? 2.86607   40.88507 93.72387  1.000 86.81209  ?  468 ILE C CG2 1 
ATOM 2779 C CD1 . ILE B 2 147 ? 2.41800   39.58695 96.32641  1.000 90.17879  ?  468 ILE C CD1 1 
ATOM 2780 N N   . SER B 2 148 ? 7.12317   39.33383 93.51002  1.000 72.09678  ?  469 SER C N   1 
ATOM 2781 C CA  . SER B 2 148 ? 8.21399   39.63699 92.59450  1.000 70.49246  ?  469 SER C CA  1 
ATOM 2782 C C   . SER B 2 148 ? 7.93062   39.06274 91.21209  1.000 72.12904  ?  469 SER C C   1 
ATOM 2783 O O   . SER B 2 148 ? 7.60963   37.87875 91.07113  1.000 91.28799  ?  469 SER C O   1 
ATOM 2784 C CB  . SER B 2 148 ? 9.52939   39.08142 93.13811  1.000 77.08442  ?  469 SER C CB  1 
ATOM 2785 O OG  . SER B 2 148 ? 10.59840  39.33141 92.24206  1.000 80.61475  ?  469 SER C OG  1 
ATOM 2786 N N   . THR B 2 149 ? 8.04724   39.90954 90.18951  1.000 67.15272  ?  470 THR C N   1 
ATOM 2787 C CA  . THR B 2 149 ? 7.93655   39.48878 88.80023  1.000 59.67583  ?  470 THR C CA  1 
ATOM 2788 C C   . THR B 2 149 ? 9.30083   39.32861 88.13871  1.000 76.76710  ?  470 THR C C   1 
ATOM 2789 O O   . THR B 2 149 ? 9.38804   39.30724 86.90641  1.000 67.59670  ?  470 THR C O   1 
ATOM 2790 C CB  . THR B 2 149 ? 7.07961   40.47992 88.01028  1.000 65.00097  ?  470 THR C CB  1 
ATOM 2791 O OG1 . THR B 2 149 ? 7.66348   41.78683 88.08588  1.000 99.95339  ?  470 THR C OG1 1 
ATOM 2792 C CG2 . THR B 2 149 ? 5.66657   40.52733 88.57172  1.000 70.33048  ?  470 THR C CG2 1 
ATOM 2793 N N   . GLU B 2 150 ? 10.36334  39.22005 88.93442  1.000 75.11056  ?  471 GLU C N   1 
ATOM 2794 C CA  . GLU B 2 150 ? 11.70422  39.07470 88.38593  1.000 69.43419  ?  471 GLU C CA  1 
ATOM 2795 C C   . GLU B 2 150 ? 11.83244  37.75581 87.63439  1.000 73.69601  ?  471 GLU C C   1 
ATOM 2796 O O   . GLU B 2 150 ? 11.39230  36.70487 88.10703  1.000 73.46014  ?  471 GLU C O   1 
ATOM 2797 C CB  . GLU B 2 150 ? 12.74375  39.14795 89.50512  1.000 80.25644  ?  471 GLU C CB  1 
ATOM 2798 C CG  . GLU B 2 150 ? 14.18206  39.01103 89.03166  1.000 98.81444  ?  471 GLU C CG  1 
ATOM 2799 C CD  . GLU B 2 150 ? 15.16797  38.92503 90.17989  1.000 107.09185 ?  471 GLU C CD  1 
ATOM 2800 O OE1 . GLU B 2 150 ? 14.72178  38.80691 91.34060  1.000 103.78267 ?  471 GLU C OE1 1 
ATOM 2801 O OE2 . GLU B 2 150 ? 16.38915  38.97508 89.92157  1.000 109.61144 -1 471 GLU C OE2 1 
ATOM 2802 N N   . ILE B 2 151 ? 12.44458  37.81711 86.45433  1.000 66.44846  ?  472 ILE C N   1 
ATOM 2803 C CA  . ILE B 2 151 ? 12.58246  36.63728 85.60797  1.000 65.76406  ?  472 ILE C CA  1 
ATOM 2804 C C   . ILE B 2 151 ? 13.54130  35.65392 86.26735  1.000 62.62595  ?  472 ILE C C   1 
ATOM 2805 O O   . ILE B 2 151 ? 14.68268  35.99835 86.59485  1.000 59.56649  ?  472 ILE C O   1 
ATOM 2806 C CB  . ILE B 2 151 ? 13.05457  37.02940 84.20332  1.000 50.04215  ?  472 ILE C CB  1 
ATOM 2807 C CG1 . ILE B 2 151 ? 11.98571  37.88162 83.51736  1.000 55.87038  ?  472 ILE C CG1 1 
ATOM 2808 C CG2 . ILE B 2 151 ? 13.37518  35.79264 83.38003  1.000 63.82239  ?  472 ILE C CG2 1 
ATOM 2809 C CD1 . ILE B 2 151 ? 12.37131  38.35784 82.14315  1.000 68.95257  ?  472 ILE C CD1 1 
ATOM 2810 N N   . TYR B 2 152 ? 13.07738  34.42244 86.46368  1.000 79.18458  ?  473 TYR C N   1 
ATOM 2811 C CA  . TYR B 2 152 ? 13.87632  33.41030 87.14037  1.000 82.25809  ?  473 TYR C CA  1 
ATOM 2812 C C   . TYR B 2 152 ? 14.97871  32.89974 86.22076  1.000 72.52580  ?  473 TYR C C   1 
ATOM 2813 O O   . TYR B 2 152 ? 14.72761  32.55547 85.06154  1.000 58.55253  ?  473 TYR C O   1 
ATOM 2814 C CB  . TYR B 2 152 ? 12.98307  32.25568 87.59460  1.000 64.69294  ?  473 TYR C CB  1 
ATOM 2815 C CG  . TYR B 2 152 ? 13.70231  31.18098 88.37859  1.000 66.07781  ?  473 TYR C CG  1 
ATOM 2816 C CD1 . TYR B 2 152 ? 13.92427  31.32072 89.74234  1.000 65.15114  ?  473 TYR C CD1 1 
ATOM 2817 C CD2 . TYR B 2 152 ? 14.14775  30.02111 87.75788  1.000 63.56399  ?  473 TYR C CD2 1 
ATOM 2818 C CE1 . TYR B 2 152 ? 14.57712  30.33907 90.46481  1.000 64.22462  ?  473 TYR C CE1 1 
ATOM 2819 C CE2 . TYR B 2 152 ? 14.80148  29.03396 88.47179  1.000 54.17154  ?  473 TYR C CE2 1 
ATOM 2820 C CZ  . TYR B 2 152 ? 15.01311  29.19819 89.82480  1.000 66.23140  ?  473 TYR C CZ  1 
ATOM 2821 O OH  . TYR B 2 152 ? 15.66288  28.21864 90.54043  1.000 85.27123  ?  473 TYR C OH  1 
ATOM 2822 N N   . GLN B 2 153 ? 16.20273  32.85230 86.74228  1.000 68.25806  ?  474 GLN C N   1 
ATOM 2823 C CA  . GLN B 2 153 ? 17.35959  32.35455 86.00648  1.000 61.66212  ?  474 GLN C CA  1 
ATOM 2824 C C   . GLN B 2 153 ? 17.59161  30.89984 86.39804  1.000 61.95270  ?  474 GLN C C   1 
ATOM 2825 O O   . GLN B 2 153 ? 17.94579  30.60722 87.54495  1.000 66.59023  ?  474 GLN C O   1 
ATOM 2826 C CB  . GLN B 2 153 ? 18.59567  33.20376 86.29356  1.000 64.69774  ?  474 GLN C CB  1 
ATOM 2827 C CG  . GLN B 2 153 ? 19.87337  32.66450 85.67090  1.000 60.27379  ?  474 GLN C CG  1 
ATOM 2828 C CD  . GLN B 2 153 ? 21.09528  33.48175 86.04333  1.000 65.13033  ?  474 GLN C CD  1 
ATOM 2829 O OE1 . GLN B 2 153 ? 20.98023  34.59057 86.56569  1.000 70.47991  ?  474 GLN C OE1 1 
ATOM 2830 N NE2 . GLN B 2 153 ? 22.27571  32.93414 85.77878  1.000 66.14763  ?  474 GLN C NE2 1 
ATOM 2831 N N   . ALA B 2 154 ? 17.39220  29.99120 85.44468  1.000 60.07854  ?  475 ALA C N   1 
ATOM 2832 C CA  . ALA B 2 154 ? 17.58645  28.56705 85.68224  1.000 62.98417  ?  475 ALA C CA  1 
ATOM 2833 C C   . ALA B 2 154 ? 18.91014  28.04308 85.14738  1.000 66.55990  ?  475 ALA C C   1 
ATOM 2834 O O   . ALA B 2 154 ? 19.45924  27.09222 85.71238  1.000 57.58336  ?  475 ALA C O   1 
ATOM 2835 C CB  . ALA B 2 154 ? 16.44032  27.76363 85.05864  1.000 55.52230  ?  475 ALA C CB  1 
ATOM 2836 N N   . GLY B 2 155 ? 19.43573  28.63640 84.08158  1.000 79.80141  ?  476 GLY C N   1 
ATOM 2837 C CA  . GLY B 2 155 ? 20.69172  28.21692 83.49758  1.000 83.55117  ?  476 GLY C CA  1 
ATOM 2838 C C   . GLY B 2 155 ? 21.88955  28.84274 84.17884  1.000 77.58814  ?  476 GLY C C   1 
ATOM 2839 O O   . GLY B 2 155 ? 21.83772  29.25687 85.33958  1.000 69.93177  ?  476 GLY C O   1 
ATOM 2840 N N   . SER B 2 156 ? 22.99087  28.91100 83.43332  1.000 71.09062  ?  477 SER C N   1 
ATOM 2841 C CA  . SER B 2 156 ? 24.23576  29.48661 83.92737  1.000 71.24587  ?  477 SER C CA  1 
ATOM 2842 C C   . SER B 2 156 ? 24.42198  30.94108 83.51943  1.000 69.09882  ?  477 SER C C   1 
ATOM 2843 O O   . SER B 2 156 ? 24.87967  31.75148 84.33036  1.000 84.67997  ?  477 SER C O   1 
ATOM 2844 C CB  . SER B 2 156 ? 25.43145  28.66453 83.43514  1.000 71.20600  ?  477 SER C CB  1 
ATOM 2845 O OG  . SER B 2 156 ? 25.47712  28.62336 82.01931  1.000 89.40335  ?  477 SER C OG  1 
ATOM 2846 N N   . THR B 2 157 ? 24.08168  31.29089 82.28154  1.000 65.35565  ?  478 THR C N   1 
ATOM 2847 C CA  . THR B 2 157 ? 24.21285  32.66908 81.83111  1.000 61.07531  ?  478 THR C CA  1 
ATOM 2848 C C   . THR B 2 157 ? 23.10036  33.52776 82.43114  1.000 77.73252  ?  478 THR C C   1 
ATOM 2849 O O   . THR B 2 157 ? 21.96286  33.06771 82.56265  1.000 83.83190  ?  478 THR C O   1 
ATOM 2850 C CB  . THR B 2 157 ? 24.15928  32.74696 80.30667  1.000 59.57493  ?  478 THR C CB  1 
ATOM 2851 O OG1 . THR B 2 157 ? 22.91550  32.20702 79.84270  1.000 71.63039  ?  478 THR C OG1 1 
ATOM 2852 C CG2 . THR B 2 157 ? 25.30986  31.96375 79.69276  1.000 66.07792  ?  478 THR C CG2 1 
ATOM 2853 N N   . PRO B 2 158 ? 23.39964  34.77031 82.80068  1.000 80.37931  ?  479 PRO C N   1 
ATOM 2854 C CA  . PRO B 2 158 ? 22.37042  35.63428 83.38646  1.000 62.43432  ?  479 PRO C CA  1 
ATOM 2855 C C   . PRO B 2 158 ? 21.31149  36.01831 82.36433  1.000 65.96640  ?  479 PRO C C   1 
ATOM 2856 O O   . PRO B 2 158 ? 21.50774  35.92743 81.15044  1.000 56.60465  ?  479 PRO C O   1 
ATOM 2857 C CB  . PRO B 2 158 ? 23.16039  36.85973 83.85621  1.000 64.26675  ?  479 PRO C CB  1 
ATOM 2858 C CG  . PRO B 2 158 ? 24.37139  36.87841 82.98139  1.000 72.99449  ?  479 PRO C CG  1 
ATOM 2859 C CD  . PRO B 2 158 ? 24.70934  35.44019 82.71982  1.000 65.39944  ?  479 PRO C CD  1 
ATOM 2860 N N   . CYS B 2 159 ? 20.16648  36.45685 82.88366  1.000 78.25134  ?  480 CYS C N   1 
ATOM 2861 C CA  . CYS B 2 159 ? 19.02031  36.82347 82.06073  1.000 73.00942  ?  480 CYS C CA  1 
ATOM 2862 C C   . CYS B 2 159 ? 18.89743  38.32491 81.84421  1.000 68.45708  ?  480 CYS C C   1 
ATOM 2863 O O   . CYS B 2 159 ? 18.48961  38.75501 80.76044  1.000 67.70492  ?  480 CYS C O   1 
ATOM 2864 C CB  . CYS B 2 159 ? 17.73098  36.29000 82.69221  1.000 67.19080  ?  480 CYS C CB  1 
ATOM 2865 S SG  . CYS B 2 159 ? 17.73734  34.50221 82.95285  1.000 94.12080  ?  480 CYS C SG  1 
ATOM 2866 N N   . ASN B 2 160 ? 19.23723  39.12691 82.85581  1.000 77.48003  ?  481 ASN C N   1 
ATOM 2867 C CA  . ASN B 2 160 ? 19.22887  40.58809 82.75560  1.000 65.92626  ?  481 ASN C CA  1 
ATOM 2868 C C   . ASN B 2 160 ? 17.83756  41.12039 82.41659  1.000 73.17333  ?  481 ASN C C   1 
ATOM 2869 O O   . ASN B 2 160 ? 17.68002  42.01204 81.58022  1.000 87.53699  ?  481 ASN C O   1 
ATOM 2870 C CB  . ASN B 2 160 ? 20.26235  41.07861 81.73849  1.000 62.13256  ?  481 ASN C CB  1 
ATOM 2871 C CG  . ASN B 2 160 ? 21.64806  40.52327 82.00260  1.000 84.56909  ?  481 ASN C CG  1 
ATOM 2872 O OD1 . ASN B 2 160 ? 22.24548  39.87939 81.14023  1.000 90.85560  ?  481 ASN C OD1 1 
ATOM 2873 N ND2 . ASN B 2 160 ? 22.16590  40.76785 83.20090  1.000 96.97990  ?  481 ASN C ND2 1 
ATOM 2874 N N   . GLY B 2 161 ? 16.81829  40.56776 83.07153  1.000 66.16105  ?  482 GLY C N   1 
ATOM 2875 C CA  . GLY B 2 161 ? 15.46179  41.04798 82.89846  1.000 55.88953  ?  482 GLY C CA  1 
ATOM 2876 C C   . GLY B 2 161 ? 14.81375  40.72089 81.57351  1.000 65.43997  ?  482 GLY C C   1 
ATOM 2877 O O   . GLY B 2 161 ? 13.73719  41.25079 81.28277  1.000 74.10367  ?  482 GLY C O   1 
ATOM 2878 N N   . VAL B 2 162 ? 15.42808  39.86635 80.75956  1.000 73.10116  ?  483 VAL C N   1 
ATOM 2879 C CA  . VAL B 2 162 ? 14.88023  39.45898 79.47115  1.000 59.17715  ?  483 VAL C CA  1 
ATOM 2880 C C   . VAL B 2 162 ? 14.68578  37.95010 79.49459  1.000 62.70443  ?  483 VAL C C   1 
ATOM 2881 O O   . VAL B 2 162 ? 15.62808  37.20336 79.78420  1.000 63.55748  ?  483 VAL C O   1 
ATOM 2882 C CB  . VAL B 2 162 ? 15.79548  39.87520 78.30500  1.000 51.00729  ?  483 VAL C CB  1 
ATOM 2883 C CG1 . VAL B 2 162 ? 15.17319  39.48053 76.97546  1.000 49.50872  ?  483 VAL C CG1 1 
ATOM 2884 C CG2 . VAL B 2 162 ? 16.06559  41.37015 78.34991  1.000 55.23455  ?  483 VAL C CG2 1 
ATOM 2885 N N   . GLU B 2 163 ? 13.47019  37.50438 79.19077  1.000 48.29654  ?  484 GLU C N   1 
ATOM 2886 C CA  . GLU B 2 163 ? 13.14899  36.08658 79.23340  1.000 48.90522  ?  484 GLU C CA  1 
ATOM 2887 C C   . GLU B 2 163 ? 13.47926  35.41743 77.90594  1.000 48.37420  ?  484 GLU C C   1 
ATOM 2888 O O   . GLU B 2 163 ? 13.49109  36.05303 76.84817  1.000 44.80517  ?  484 GLU C O   1 
ATOM 2889 C CB  . GLU B 2 163 ? 11.67340  35.86325 79.57097  1.000 42.20047  ?  484 GLU C CB  1 
ATOM 2890 C CG  . GLU B 2 163 ? 10.69884  36.38033 78.52851  1.000 54.69793  ?  484 GLU C CG  1 
ATOM 2891 C CD  . GLU B 2 163 ? 9.44911   35.52527 78.43283  1.000 51.21724  ?  484 GLU C CD  1 
ATOM 2892 O OE1 . GLU B 2 163 ? 9.46375   34.53492 77.67224  1.000 57.33533  ?  484 GLU C OE1 1 
ATOM 2893 O OE2 . GLU B 2 163 ? 8.45741   35.83354 79.12642  1.000 57.59570  -1 484 GLU C OE2 1 
ATOM 2894 N N   . GLY B 2 164 ? 13.74770  34.11722 77.97761  1.000 41.76152  ?  485 GLY C N   1 
ATOM 2895 C CA  . GLY B 2 164 ? 14.08537  33.33015 76.80968  1.000 41.39550  ?  485 GLY C CA  1 
ATOM 2896 C C   . GLY B 2 164 ? 14.45172  31.91211 77.18992  1.000 40.97703  ?  485 GLY C C   1 
ATOM 2897 O O   . GLY B 2 164 ? 13.83499  31.32858 78.08623  1.000 63.04911  ?  485 GLY C O   1 
ATOM 2898 N N   . PHE B 2 165 ? 15.45134  31.34491 76.52116  1.000 41.73768  ?  486 PHE C N   1 
ATOM 2899 C CA  . PHE B 2 165 ? 15.92818  30.01856 76.88583  1.000 41.99245  ?  486 PHE C CA  1 
ATOM 2900 C C   . PHE B 2 165 ? 16.64254  30.07716 78.23058  1.000 45.16277  ?  486 PHE C C   1 
ATOM 2901 O O   . PHE B 2 165 ? 17.50362  30.93494 78.45057  1.000 57.13684  ?  486 PHE C O   1 
ATOM 2902 C CB  . PHE B 2 165 ? 16.85798  29.47122 75.80458  1.000 43.04975  ?  486 PHE C CB  1 
ATOM 2903 C CG  . PHE B 2 165 ? 16.15621  29.12022 74.52277  1.000 42.36007  ?  486 PHE C CG  1 
ATOM 2904 C CD1 . PHE B 2 165 ? 14.81790  28.76440 74.52525  1.000 46.16595  ?  486 PHE C CD1 1 
ATOM 2905 C CD2 . PHE B 2 165 ? 16.83434  29.14591 73.31579  1.000 63.81621  ?  486 PHE C CD2 1 
ATOM 2906 C CE1 . PHE B 2 165 ? 14.16921  28.44007 73.34793  1.000 40.93488  ?  486 PHE C CE1 1 
ATOM 2907 C CE2 . PHE B 2 165 ? 16.19082  28.82293 72.13507  1.000 59.89602  ?  486 PHE C CE2 1 
ATOM 2908 C CZ  . PHE B 2 165 ? 14.85658  28.46977 72.15180  1.000 42.02628  ?  486 PHE C CZ  1 
ATOM 2909 N N   . ASN B 2 166 ? 16.26900  29.16898 79.13404  1.000 48.77858  ?  487 ASN C N   1 
ATOM 2910 C CA  . ASN B 2 166 ? 16.78864  29.11045 80.50073  1.000 49.57086  ?  487 ASN C CA  1 
ATOM 2911 C C   . ASN B 2 166 ? 16.49175  30.38209 81.29067  1.000 48.87872  ?  487 ASN C C   1 
ATOM 2912 O O   . ASN B 2 166 ? 17.14429  30.65458 82.30351  1.000 60.69439  ?  487 ASN C O   1 
ATOM 2913 C CB  . ASN B 2 166 ? 18.29417  28.81647 80.51677  1.000 46.47338  ?  487 ASN C CB  1 
ATOM 2914 C CG  . ASN B 2 166 ? 18.63756  27.50222 79.84442  1.000 55.56896  ?  487 ASN C CG  1 
ATOM 2915 O OD1 . ASN B 2 166 ? 18.97111  27.46621 78.65986  1.000 53.37849  ?  487 ASN C OD1 1 
ATOM 2916 N ND2 . ASN B 2 166 ? 18.55370  26.41195 80.59848  1.000 58.53983  ?  487 ASN C ND2 1 
ATOM 2917 N N   . CYS B 2 167 ? 15.50845  31.16711 80.84503  1.000 51.50543  ?  488 CYS C N   1 
ATOM 2918 C CA  . CYS B 2 167 ? 15.08905  32.39665 81.52534  1.000 51.87742  ?  488 CYS C CA  1 
ATOM 2919 C C   . CYS B 2 167 ? 13.56286  32.43183 81.47218  1.000 50.95990  ?  488 CYS C C   1 
ATOM 2920 O O   . CYS B 2 167 ? 12.97395  32.99862 80.54771  1.000 40.98968  ?  488 CYS C O   1 
ATOM 2921 C CB  . CYS B 2 167 ? 15.71286  33.62869 80.88402  1.000 60.91899  ?  488 CYS C CB  1 
ATOM 2922 S SG  . CYS B 2 167 ? 17.50509  33.73220 81.08820  1.000 62.21626  ?  488 CYS C SG  1 
ATOM 2923 N N   . TYR B 2 168 ? 12.93247  31.82493 82.47113  1.000 60.42086  ?  489 TYR C N   1 
ATOM 2924 C CA  . TYR B 2 168 ? 11.49443  31.60926 82.48397  1.000 60.97355  ?  489 TYR C CA  1 
ATOM 2925 C C   . TYR B 2 168 ? 10.79540  32.64417 83.35799  1.000 55.38772  ?  489 TYR C C   1 
ATOM 2926 O O   . TYR B 2 168 ? 11.40950  33.30395 84.19983  1.000 47.96152  ?  489 TYR C O   1 
ATOM 2927 C CB  . TYR B 2 168 ? 11.16906  30.20058 82.98929  1.000 49.93613  ?  489 TYR C CB  1 
ATOM 2928 C CG  . TYR B 2 168 ? 12.13038  29.13520 82.51078  1.000 39.89843  ?  489 TYR C CG  1 
ATOM 2929 C CD1 . TYR B 2 168 ? 12.44588  29.00547 81.16379  1.000 39.51303  ?  489 TYR C CD1 1 
ATOM 2930 C CD2 . TYR B 2 168 ? 12.73211  28.26560 83.41065  1.000 40.99889  ?  489 TYR C CD2 1 
ATOM 2931 C CE1 . TYR B 2 168 ? 13.32789  28.03372 80.72774  1.000 40.18293  ?  489 TYR C CE1 1 
ATOM 2932 C CE2 . TYR B 2 168 ? 13.61349  27.29248 82.98459  1.000 41.78204  ?  489 TYR C CE2 1 
ATOM 2933 C CZ  . TYR B 2 168 ? 13.90879  27.18050 81.64351  1.000 47.23327  ?  489 TYR C CZ  1 
ATOM 2934 O OH  . TYR B 2 168 ? 14.78847  26.21068 81.22048  1.000 45.86357  ?  489 TYR C OH  1 
ATOM 2935 N N   . PHE B 2 169 ? 9.48765   32.77373 83.14538  1.000 51.81049  ?  490 PHE C N   1 
ATOM 2936 C CA  . PHE B 2 169 ? 8.66820   33.64471 83.97541  1.000 56.77694  ?  490 PHE C CA  1 
ATOM 2937 C C   . PHE B 2 169 ? 8.38270   32.96352 85.31374  1.000 54.86380  ?  490 PHE C C   1 
ATOM 2938 O O   . PHE B 2 169 ? 8.06497   31.77177 85.34752  1.000 57.23461  ?  490 PHE C O   1 
ATOM 2939 C CB  . PHE B 2 169 ? 7.35771   33.98139 83.26503  1.000 55.17026  ?  490 PHE C CB  1 
ATOM 2940 C CG  . PHE B 2 169 ? 6.63049   35.15865 83.85116  1.000 61.88851  ?  490 PHE C CG  1 
ATOM 2941 C CD1 . PHE B 2 169 ? 5.51198   34.97474 84.64723  1.000 66.33354  ?  490 PHE C CD1 1 
ATOM 2942 C CD2 . PHE B 2 169 ? 7.06528   36.45056 83.60363  1.000 46.35100  ?  490 PHE C CD2 1 
ATOM 2943 C CE1 . PHE B 2 169 ? 4.84029   36.05783 85.18495  1.000 59.10560  ?  490 PHE C CE1 1 
ATOM 2944 C CE2 . PHE B 2 169 ? 6.39858   37.53687 84.13932  1.000 47.50804  ?  490 PHE C CE2 1 
ATOM 2945 C CZ  . PHE B 2 169 ? 5.28480   37.33989 84.93121  1.000 46.44399  ?  490 PHE C CZ  1 
ATOM 2946 N N   . PRO B 2 170 ? 8.49190   33.69138 86.42872  1.000 56.96605  ?  491 PRO C N   1 
ATOM 2947 C CA  . PRO B 2 170 ? 8.35901   33.03350 87.73843  1.000 58.41137  ?  491 PRO C CA  1 
ATOM 2948 C C   . PRO B 2 170 ? 6.95365   32.54262 88.03793  1.000 59.97733  ?  491 PRO C C   1 
ATOM 2949 O O   . PRO B 2 170 ? 6.79833   31.59668 88.82038  1.000 52.44748  ?  491 PRO C O   1 
ATOM 2950 C CB  . PRO B 2 170 ? 8.79461   34.12794 88.72169  1.000 68.14225  ?  491 PRO C CB  1 
ATOM 2951 C CG  . PRO B 2 170 ? 8.47595   35.40187 88.01251  1.000 75.86739  ?  491 PRO C CG  1 
ATOM 2952 C CD  . PRO B 2 170 ? 8.75372   35.13512 86.55786  1.000 59.34876  ?  491 PRO C CD  1 
ATOM 2953 N N   . LEU B 2 171 ? 5.92880   33.14774 87.44702  1.000 60.90793  ?  492 LEU C N   1 
ATOM 2954 C CA  . LEU B 2 171 ? 4.54778   32.78351 87.72307  1.000 56.81403  ?  492 LEU C CA  1 
ATOM 2955 C C   . LEU B 2 171 ? 4.00308   31.86305 86.63794  1.000 51.73155  ?  492 LEU C C   1 
ATOM 2956 O O   . LEU B 2 171 ? 4.44302   31.89698 85.48579  1.000 55.85843  ?  492 LEU C O   1 
ATOM 2957 C CB  . LEU B 2 171 ? 3.66667   34.02946 87.83501  1.000 49.79409  ?  492 LEU C CB  1 
ATOM 2958 C CG  . LEU B 2 171 ? 4.03329   35.01925 88.94174  1.000 54.95043  ?  492 LEU C CG  1 
ATOM 2959 C CD1 . LEU B 2 171 ? 3.11136   36.22675 88.90407  1.000 54.89871  ?  492 LEU C CD1 1 
ATOM 2960 C CD2 . LEU B 2 171 ? 3.98494   34.34452 90.30418  1.000 52.04400  ?  492 LEU C CD2 1 
ATOM 2961 N N   . GLN B 2 172 ? 3.03470   31.03525 87.02426  1.000 49.70084  ?  493 GLN C N   1 
ATOM 2962 C CA  . GLN B 2 172 ? 2.37137   30.12492 86.10497  1.000 41.19525  ?  493 GLN C CA  1 
ATOM 2963 C C   . GLN B 2 172 ? 0.87232   30.17763 86.35866  1.000 50.10438  ?  493 GLN C C   1 
ATOM 2964 O O   . GLN B 2 172 ? 0.42620   30.46185 87.47278  1.000 48.70281  ?  493 GLN C O   1 
ATOM 2965 C CB  . GLN B 2 172 ? 2.89134   28.68955 86.25698  1.000 48.45671  ?  493 GLN C CB  1 
ATOM 2966 C CG  . GLN B 2 172 ? 2.85908   27.87876 84.97108  1.000 74.04432  ?  493 GLN C CG  1 
ATOM 2967 C CD  . GLN B 2 172 ? 3.83579   28.39655 83.93026  1.000 55.50927  ?  493 GLN C CD  1 
ATOM 2968 O OE1 . GLN B 2 172 ? 3.61020   28.25864 82.72884  1.000 64.85774  ?  493 GLN C OE1 1 
ATOM 2969 N NE2 . GLN B 2 172 ? 4.93162   28.99050 84.38877  1.000 38.54849  ?  493 GLN C NE2 1 
ATOM 2970 N N   . SER B 2 173 ? 0.09798   29.89666 85.31599  1.000 48.48953  ?  494 SER C N   1 
ATOM 2971 C CA  . SER B 2 173 ? -1.35069  30.04579 85.35507  1.000 46.96644  ?  494 SER C CA  1 
ATOM 2972 C C   . SER B 2 173 ? -2.02203  28.71722 85.67755  1.000 51.64579  ?  494 SER C C   1 
ATOM 2973 O O   . SER B 2 173 ? -1.70298  27.68850 85.07164  1.000 63.94416  ?  494 SER C O   1 
ATOM 2974 C CB  . SER B 2 173 ? -1.87405  30.58408 84.02195  1.000 51.40020  ?  494 SER C CB  1 
ATOM 2975 O OG  . SER B 2 173 ? -3.28622  30.68376 84.03067  1.000 49.30510  ?  494 SER C OG  1 
ATOM 2976 N N   . TYR B 2 174 ? -2.94726  28.74597 86.63278  1.000 59.15774  ?  495 TYR C N   1 
ATOM 2977 C CA  . TYR B 2 174 ? -3.82893  27.61151 86.85578  1.000 53.39807  ?  495 TYR C CA  1 
ATOM 2978 C C   . TYR B 2 174 ? -4.77476  27.44868 85.67064  1.000 52.21333  ?  495 TYR C C   1 
ATOM 2979 O O   . TYR B 2 174 ? -5.19915  28.42553 85.04763  1.000 87.04152  ?  495 TYR C O   1 
ATOM 2980 C CB  . TYR B 2 174 ? -4.63305  27.80060 88.14365  1.000 48.22002  ?  495 TYR C CB  1 
ATOM 2981 C CG  . TYR B 2 174 ? -3.91007  27.40217 89.41363  1.000 50.96662  ?  495 TYR C CG  1 
ATOM 2982 C CD1 . TYR B 2 174 ? -3.13246  26.25268 89.46484  1.000 66.81869  ?  495 TYR C CD1 1 
ATOM 2983 C CD2 . TYR B 2 174 ? -4.01359  28.17394 90.56506  1.000 55.37393  ?  495 TYR C CD2 1 
ATOM 2984 C CE1 . TYR B 2 174 ? -2.47610  25.88320 90.62707  1.000 72.38329  ?  495 TYR C CE1 1 
ATOM 2985 C CE2 . TYR B 2 174 ? -3.36023  27.81361 91.73073  1.000 63.20151  ?  495 TYR C CE2 1 
ATOM 2986 C CZ  . TYR B 2 174 ? -2.59291  26.66798 91.75604  1.000 72.87370  ?  495 TYR C CZ  1 
ATOM 2987 O OH  . TYR B 2 174 ? -1.94140  26.30560 92.91343  1.000 77.94594  ?  495 TYR C OH  1 
ATOM 2988 N N   . GLY B 2 175 ? -5.09827  26.19796 85.35416  1.000 50.15171  ?  496 GLY C N   1 
ATOM 2989 C CA  . GLY B 2 175 ? -6.01039  25.92078 84.26130  1.000 60.41663  ?  496 GLY C CA  1 
ATOM 2990 C C   . GLY B 2 175 ? -7.41841  26.40335 84.54304  1.000 64.32268  ?  496 GLY C C   1 
ATOM 2991 O O   . GLY B 2 175 ? -7.87516  27.38750 83.95323  1.000 77.22003  ?  496 GLY C O   1 
ATOM 2992 N N   . PHE B 2 176 ? -8.11203  25.70696 85.44537  1.000 74.59198  ?  497 PHE C N   1 
ATOM 2993 C CA  . PHE B 2 176 ? -9.44444  26.08459 85.90924  1.000 63.38199  ?  497 PHE C CA  1 
ATOM 2994 C C   . PHE B 2 176 ? -10.46619 26.13426 84.77953  1.000 76.37806  ?  497 PHE C C   1 
ATOM 2995 O O   . PHE B 2 176 ? -10.79082 27.21028 84.26636  1.000 75.32570  ?  497 PHE C O   1 
ATOM 2996 C CB  . PHE B 2 176 ? -9.39833  27.42941 86.64051  1.000 59.17287  ?  497 PHE C CB  1 
ATOM 2997 C CG  . PHE B 2 176 ? -8.71296  27.36636 87.97497  1.000 66.05440  ?  497 PHE C CG  1 
ATOM 2998 C CD1 . PHE B 2 176 ? -8.40018  26.14396 88.54801  1.000 67.62291  ?  497 PHE C CD1 1 
ATOM 2999 C CD2 . PHE B 2 176 ? -8.38563  28.52483 88.65922  1.000 75.79122  ?  497 PHE C CD2 1 
ATOM 3000 C CE1 . PHE B 2 176 ? -7.76911  26.07716 89.77239  1.000 61.94876  ?  497 PHE C CE1 1 
ATOM 3001 C CE2 . PHE B 2 176 ? -7.75570  28.46408 89.88655  1.000 79.61256  ?  497 PHE C CE2 1 
ATOM 3002 C CZ  . PHE B 2 176 ? -7.44744  27.23925 90.44343  1.000 71.16701  ?  497 PHE C CZ  1 
ATOM 3003 N N   . GLN B 2 177 ? -10.97985 24.96987 84.39939  1.000 87.83164  ?  498 GLN C N   1 
ATOM 3004 C CA  . GLN B 2 177 ? -12.08158 24.81184 83.46611  1.000 78.39157  ?  498 GLN C CA  1 
ATOM 3005 C C   . GLN B 2 177 ? -13.10226 23.85803 84.06730  1.000 74.34054  ?  498 GLN C C   1 
ATOM 3006 O O   . GLN B 2 177 ? -12.74335 22.99030 84.86932  1.000 82.31082  ?  498 GLN C O   1 
ATOM 3007 C CB  . GLN B 2 177 ? -11.59175 24.27492 82.11306  1.000 75.39630  ?  498 GLN C CB  1 
ATOM 3008 C CG  . GLN B 2 177 ? -10.86952 25.31441 81.27646  1.000 77.96910  ?  498 GLN C CG  1 
ATOM 3009 C CD  . GLN B 2 177 ? -10.02647 24.70440 80.17677  1.000 85.89135  ?  498 GLN C CD  1 
ATOM 3010 O OE1 . GLN B 2 177 ? -9.11082  25.34348 79.66031  1.000 93.71004  ?  498 GLN C OE1 1 
ATOM 3011 N NE2 . GLN B 2 177 ? -10.32779 23.46239 79.81411  1.000 73.55838  ?  498 GLN C NE2 1 
ATOM 3012 N N   . PRO B 2 178 ? -14.38288 23.99683 83.70956  1.000 73.87992  ?  499 PRO C N   1 
ATOM 3013 C CA  . PRO B 2 178 ? -15.41453 23.15581 84.34081  1.000 78.72804  ?  499 PRO C CA  1 
ATOM 3014 C C   . PRO B 2 178 ? -15.27146 21.67123 84.04486  1.000 94.18064  ?  499 PRO C C   1 
ATOM 3015 O O   . PRO B 2 178 ? -15.90523 20.86191 84.73434  1.000 101.07128 ?  499 PRO C O   1 
ATOM 3016 C CB  . PRO B 2 178 ? -16.72448 23.71364 83.76692  1.000 91.56134  ?  499 PRO C CB  1 
ATOM 3017 C CG  . PRO B 2 178 ? -16.32979 24.36337 82.48581  1.000 81.47733  ?  499 PRO C CG  1 
ATOM 3018 C CD  . PRO B 2 178 ? -14.96183 24.93261 82.73062  1.000 75.47053  ?  499 PRO C CD  1 
ATOM 3019 N N   . THR B 2 179 ? -14.46542 21.28702 83.05707  1.000 97.63083  ?  500 THR C N   1 
ATOM 3020 C CA  . THR B 2 179 ? -14.27141 19.88811 82.70327  1.000 100.57430 ?  500 THR C CA  1 
ATOM 3021 C C   . THR B 2 179 ? -13.01752 19.28935 83.32944  1.000 101.98151 ?  500 THR C C   1 
ATOM 3022 O O   . THR B 2 179 ? -12.65733 18.15380 83.00353  1.000 125.29043 ?  500 THR C O   1 
ATOM 3023 C CB  . THR B 2 179 ? -14.21718 19.73040 81.18199  1.000 109.61437 ?  500 THR C CB  1 
ATOM 3024 O OG1 . THR B 2 179 ? -13.12728 20.49994 80.65871  1.000 122.45019 ?  500 THR C OG1 1 
ATOM 3025 C CG2 . THR B 2 179 ? -15.51725 20.20819 80.55190  1.000 88.35120  ?  500 THR C CG2 1 
ATOM 3026 N N   . ASN B 2 180 ? -12.34720 20.02024 84.21560  1.000 80.26774  ?  501 ASN C N   1 
ATOM 3027 C CA  . ASN B 2 180 ? -11.14860 19.50548 84.85725  1.000 90.56054  ?  501 ASN C CA  1 
ATOM 3028 C C   . ASN B 2 180 ? -11.50852 18.53756 85.98092  1.000 90.18656  ?  501 ASN C C   1 
ATOM 3029 O O   . ASN B 2 180 ? -12.62900 18.52720 86.49788  1.000 71.55274  ?  501 ASN C O   1 
ATOM 3030 C CB  . ASN B 2 180 ? -10.29372 20.64669 85.41076  1.000 64.25217  ?  501 ASN C CB  1 
ATOM 3031 C CG  . ASN B 2 180 ? -9.65093  21.47679 84.31929  1.000 67.05689  ?  501 ASN C CG  1 
ATOM 3032 O OD1 . ASN B 2 180 ? -9.76815  22.70141 84.30580  1.000 71.10761  ?  501 ASN C OD1 1 
ATOM 3033 N ND2 . ASN B 2 180 ? -8.96459  20.81286 83.39668  1.000 103.89789 ?  501 ASN C ND2 1 
ATOM 3034 N N   . GLY B 2 181 ? -10.53077 17.71498 86.35520  1.000 82.00275  ?  502 GLY C N   1 
ATOM 3035 C CA  . GLY B 2 181 ? -10.72215 16.79454 87.45401  1.000 69.51457  ?  502 GLY C CA  1 
ATOM 3036 C C   . GLY B 2 181 ? -10.81413 17.50632 88.78936  1.000 72.35162  ?  502 GLY C C   1 
ATOM 3037 O O   . GLY B 2 181 ? -10.46256 18.67779 88.93252  1.000 81.97366  ?  502 GLY C O   1 
ATOM 3038 N N   . VAL B 2 182 ? -11.29831 16.76742 89.79101  1.000 84.97088  ?  503 VAL C N   1 
ATOM 3039 C CA  . VAL B 2 182 ? -11.49511 17.34387 91.11954  1.000 83.65871  ?  503 VAL C CA  1 
ATOM 3040 C C   . VAL B 2 182 ? -10.17023 17.82603 91.69721  1.000 87.78342  ?  503 VAL C C   1 
ATOM 3041 O O   . VAL B 2 182 ? -10.11435 18.84681 92.39414  1.000 86.82613  ?  503 VAL C O   1 
ATOM 3042 C CB  . VAL B 2 182 ? -12.18158 16.32428 92.04750  1.000 84.31701  ?  503 VAL C CB  1 
ATOM 3043 C CG1 . VAL B 2 182 ? -12.51274 16.96233 93.39026  1.000 78.89073  ?  503 VAL C CG1 1 
ATOM 3044 C CG2 . VAL B 2 182 ? -13.43587 15.76998 91.38872  1.000 83.84516  ?  503 VAL C CG2 1 
ATOM 3045 N N   . GLY B 2 183 ? -9.08375  17.10762 91.41393  1.000 88.65568  ?  504 GLY C N   1 
ATOM 3046 C CA  . GLY B 2 183 ? -7.77114  17.53019 91.86883  1.000 87.20045  ?  504 GLY C CA  1 
ATOM 3047 C C   . GLY B 2 183 ? -7.23897  18.77292 91.18644  1.000 84.36949  ?  504 GLY C C   1 
ATOM 3048 O O   . GLY B 2 183 ? -6.26993  19.36043 91.67958  1.000 69.26498  ?  504 GLY C O   1 
ATOM 3049 N N   . TYR B 2 184 ? -7.84520  19.18554 90.07307  1.000 84.43780  ?  505 TYR C N   1 
ATOM 3050 C CA  . TYR B 2 184 ? -7.41864  20.36488 89.33000  1.000 81.72043  ?  505 TYR C CA  1 
ATOM 3051 C C   . TYR B 2 184 ? -8.52409  21.41489 89.26460  1.000 83.72689  ?  505 TYR C C   1 
ATOM 3052 O O   . TYR B 2 184 ? -8.62097  22.16687 88.29271  1.000 91.52404  ?  505 TYR C O   1 
ATOM 3053 C CB  . TYR B 2 184 ? -6.95331  19.97890 87.92594  1.000 81.49635  ?  505 TYR C CB  1 
ATOM 3054 C CG  . TYR B 2 184 ? -5.60565  19.29002 87.89859  1.000 91.78028  ?  505 TYR C CG  1 
ATOM 3055 C CD1 . TYR B 2 184 ? -4.47086  19.95847 87.45725  1.000 97.73051  ?  505 TYR C CD1 1 
ATOM 3056 C CD2 . TYR B 2 184 ? -5.46649  17.97440 88.32239  1.000 101.26203 ?  505 TYR C CD2 1 
ATOM 3057 C CE1 . TYR B 2 184 ? -3.23665  19.33442 87.43308  1.000 83.54448  ?  505 TYR C CE1 1 
ATOM 3058 C CE2 . TYR B 2 184 ? -4.23634  17.34277 88.30313  1.000 100.50948 ?  505 TYR C CE2 1 
ATOM 3059 C CZ  . TYR B 2 184 ? -3.12533  18.02749 87.85757  1.000 87.63716  ?  505 TYR C CZ  1 
ATOM 3060 O OH  . TYR B 2 184 ? -1.89898  17.40362 87.83566  1.000 88.28271  ?  505 TYR C OH  1 
ATOM 3061 N N   . GLN B 2 185 ? -9.37410  21.47629 90.31092  1.000 78.52156  ?  506 GLN C N   1 
ATOM 3062 C CA  . GLN B 2 185 ? -10.45516 22.43712 90.45687  1.000 75.60704  ?  506 GLN C CA  1 
ATOM 3063 C C   . GLN B 2 185 ? -10.08494 23.51034 91.47477  1.000 73.40346  ?  506 GLN C C   1 
ATOM 3064 O O   . GLN B 2 185 ? -9.28816  23.26316 92.38520  1.000 79.29994  ?  506 GLN C O   1 
ATOM 3065 C CB  . GLN B 2 185 ? -11.74689 21.74016 90.89811  1.000 79.82247  ?  506 GLN C CB  1 
ATOM 3066 C CG  . GLN B 2 185 ? -12.44552 20.96918 89.79041  1.000 74.93078  ?  506 GLN C CG  1 
ATOM 3067 C CD  . GLN B 2 185 ? -13.72243 20.29964 90.25848  1.000 81.36137  ?  506 GLN C CD  1 
ATOM 3068 O OE1 . GLN B 2 185 ? -14.15664 20.48901 91.39477  1.000 90.04058  ?  506 GLN C OE1 1 
ATOM 3069 N NE2 . GLN B 2 185 ? -14.33136 19.50972 89.38168  1.000 75.12905  ?  506 GLN C NE2 1 
ATOM 3070 N N   . PRO B 2 186 ? -10.64037 24.71512 91.34506  1.000 75.89123  ?  507 PRO C N   1 
ATOM 3071 C CA  . PRO B 2 186 ? -10.29755 25.78405 92.29069  1.000 79.72187  ?  507 PRO C CA  1 
ATOM 3072 C C   . PRO B 2 186 ? -10.88716 25.52920 93.66926  1.000 72.79444  ?  507 PRO C C   1 
ATOM 3073 O O   . PRO B 2 186 ? -12.00283 25.02211 93.80743  1.000 73.80902  ?  507 PRO C O   1 
ATOM 3074 C CB  . PRO B 2 186 ? -10.90372 27.03557 91.64559  1.000 80.18591  ?  507 PRO C CB  1 
ATOM 3075 C CG  . PRO B 2 186 ? -12.01734 26.51510 90.80150  1.000 80.03564  ?  507 PRO C CG  1 
ATOM 3076 C CD  . PRO B 2 186 ? -11.54457 25.18751 90.28169  1.000 67.50399  ?  507 PRO C CD  1 
ATOM 3077 N N   . TYR B 2 187 ? -10.11813 25.89037 94.69484  1.000 70.75633  ?  508 TYR C N   1 
ATOM 3078 C CA  . TYR B 2 187 ? -10.53347 25.75944 96.08657  1.000 79.97737  ?  508 TYR C CA  1 
ATOM 3079 C C   . TYR B 2 187 ? -10.18674 27.04534 96.81979  1.000 83.54336  ?  508 TYR C C   1 
ATOM 3080 O O   . TYR B 2 187 ? -9.00898  27.40346 96.92375  1.000 90.22976  ?  508 TYR C O   1 
ATOM 3081 C CB  . TYR B 2 187 ? -9.85755  24.56029 96.75969  1.000 79.21980  ?  508 TYR C CB  1 
ATOM 3082 C CG  . TYR B 2 187 ? -10.55242 23.23829 96.52134  1.000 81.26597  ?  508 TYR C CG  1 
ATOM 3083 C CD1 . TYR B 2 187 ? -10.38435 22.54683 95.32965  1.000 76.39576  ?  508 TYR C CD1 1 
ATOM 3084 C CD2 . TYR B 2 187 ? -11.36996 22.67732 97.49405  1.000 90.68259  ?  508 TYR C CD2 1 
ATOM 3085 C CE1 . TYR B 2 187 ? -11.01536 21.33606 95.11028  1.000 85.11132  ?  508 TYR C CE1 1 
ATOM 3086 C CE2 . TYR B 2 187 ? -12.00519 21.46753 97.28411  1.000 81.12877  ?  508 TYR C CE2 1 
ATOM 3087 C CZ  . TYR B 2 187 ? -11.82450 20.80149 96.09070  1.000 80.44979  ?  508 TYR C CZ  1 
ATOM 3088 O OH  . TYR B 2 187 ? -12.45470 19.59688 95.87706  1.000 80.12268  ?  508 TYR C OH  1 
ATOM 3089 N N   . ARG B 2 188 ? -11.20634 27.73622 97.32381  1.000 85.48553  ?  509 ARG C N   1 
ATOM 3090 C CA  . ARG B 2 188 ? -10.99599 28.96299 98.08230  1.000 97.56733  ?  509 ARG C CA  1 
ATOM 3091 C C   . ARG B 2 188 ? -10.61176 28.61228 99.51471  1.000 96.27579  ?  509 ARG C C   1 
ATOM 3092 O O   . ARG B 2 188 ? -11.35878 27.91743 100.21198 1.000 100.47628 ?  509 ARG C O   1 
ATOM 3093 C CB  . ARG B 2 188 ? -12.25052 29.83311 98.05295  1.000 90.09173  ?  509 ARG C CB  1 
ATOM 3094 C CG  . ARG B 2 188 ? -12.63112 30.31985 96.66447  1.000 79.80059  ?  509 ARG C CG  1 
ATOM 3095 C CD  . ARG B 2 188 ? -13.74856 31.34778 96.72002  1.000 88.15105  ?  509 ARG C CD  1 
ATOM 3096 N NE  . ARG B 2 188 ? -14.01052 31.93850 95.41054  1.000 83.40416  ?  509 ARG C NE  1 
ATOM 3097 C CZ  . ARG B 2 188 ? -14.85312 32.94437 95.19900  1.000 82.09873  ?  509 ARG C CZ  1 
ATOM 3098 N NH1 . ARG B 2 188 ? -15.51950 33.47837 96.21342  1.000 86.72401  ?  509 ARG C NH1 1 
ATOM 3099 N NH2 . ARG B 2 188 ? -15.02845 33.41873 93.97313  1.000 72.25135  ?  509 ARG C NH2 1 
ATOM 3100 N N   . VAL B 2 189 ? -9.45027  29.09168 99.95203  1.000 93.82512  ?  510 VAL C N   1 
ATOM 3101 C CA  . VAL B 2 189 ? -8.90733  28.78693 101.27067 1.000 98.63437  ?  510 VAL C CA  1 
ATOM 3102 C C   . VAL B 2 189 ? -8.90887  30.06057 102.10321 1.000 87.73434  ?  510 VAL C C   1 
ATOM 3103 O O   . VAL B 2 189 ? -8.49065  31.12281 101.62650 1.000 96.77289  ?  510 VAL C O   1 
ATOM 3104 C CB  . VAL B 2 189 ? -7.48993  28.19608 101.17230 1.000 98.63220  ?  510 VAL C CB  1 
ATOM 3105 C CG1 . VAL B 2 189 ? -6.96185  27.83919 102.55486 1.000 85.58597  ?  510 VAL C CG1 1 
ATOM 3106 C CG2 . VAL B 2 189 ? -7.48683  26.97822 100.26242 1.000 84.49299  ?  510 VAL C CG2 1 
ATOM 3107 N N   . VAL B 2 190 ? -9.38144  29.95439 103.34238 1.000 86.89876  ?  511 VAL C N   1 
ATOM 3108 C CA  . VAL B 2 190 ? -9.37906  31.05931 104.29486 1.000 103.90137 ?  511 VAL C CA  1 
ATOM 3109 C C   . VAL B 2 190 ? -8.64816  30.58096 105.54138 1.000 102.46482 ?  511 VAL C C   1 
ATOM 3110 O O   . VAL B 2 190 ? -9.17825  29.76387 106.30571 1.000 100.91556 ?  511 VAL C O   1 
ATOM 3111 C CB  . VAL B 2 190 ? -10.79665 31.53741 104.63529 1.000 106.30275 ?  511 VAL C CB  1 
ATOM 3112 C CG1 . VAL B 2 190 ? -10.74092 32.67828 105.64042 1.000 86.78097  ?  511 VAL C CG1 1 
ATOM 3113 C CG2 . VAL B 2 190 ? -11.52937 31.96895 103.37406 1.000 88.02718  ?  511 VAL C CG2 1 
ATOM 3114 N N   . VAL B 2 191 ? -7.43492  31.08410 105.74788 1.000 102.12185 ?  512 VAL C N   1 
ATOM 3115 C CA  . VAL B 2 191 ? -6.60026  30.69970 106.88021 1.000 101.11742 ?  512 VAL C CA  1 
ATOM 3116 C C   . VAL B 2 191 ? -6.78862  31.72922 107.98565 1.000 103.78576 ?  512 VAL C C   1 
ATOM 3117 O O   . VAL B 2 191 ? -6.49340  32.91585 107.79808 1.000 96.40759  ?  512 VAL C O   1 
ATOM 3118 C CB  . VAL B 2 191 ? -5.12209  30.58694 106.47576 1.000 95.90230  ?  512 VAL C CB  1 
ATOM 3119 C CG1 . VAL B 2 191 ? -4.27377  30.18641 107.67323 1.000 93.38995  ?  512 VAL C CG1 1 
ATOM 3120 C CG2 . VAL B 2 191 ? -4.95735  29.58824 105.33991 1.000 88.92873  ?  512 VAL C CG2 1 
ATOM 3121 N N   . LEU B 2 192 ? -7.27869  31.27761 109.13706 1.000 117.26437 ?  513 LEU C N   1 
ATOM 3122 C CA  . LEU B 2 192 ? -7.49383  32.13550 110.29525 1.000 123.66731 ?  513 LEU C CA  1 
ATOM 3123 C C   . LEU B 2 192 ? -6.33352  31.95832 111.26672 1.000 124.56197 ?  513 LEU C C   1 
ATOM 3124 O O   . LEU B 2 192 ? -6.03460  30.83429 111.68452 1.000 127.98912 ?  513 LEU C O   1 
ATOM 3125 C CB  . LEU B 2 192 ? -8.82218  31.80935 110.97770 1.000 113.05323 ?  513 LEU C CB  1 
ATOM 3126 C CG  . LEU B 2 192 ? -10.08844 32.04455 110.15219 1.000 108.57669 ?  513 LEU C CG  1 
ATOM 3127 C CD1 . LEU B 2 192 ? -11.32472 31.63484 110.93656 1.000 99.38451  ?  513 LEU C CD1 1 
ATOM 3128 C CD2 . LEU B 2 192 ? -10.18273 33.49905 109.72084 1.000 105.41716 ?  513 LEU C CD2 1 
ATOM 3129 N N   . SER B 2 193 ? -5.68536  33.06514 111.62313 1.000 116.74804 ?  514 SER C N   1 
ATOM 3130 C CA  . SER B 2 193 ? -4.54323  33.06043 112.53206 1.000 116.78286 ?  514 SER C CA  1 
ATOM 3131 C C   . SER B 2 193 ? -4.92668  33.82428 113.79238 1.000 119.76808 ?  514 SER C C   1 
ATOM 3132 O O   . SER B 2 193 ? -5.13879  35.04092 113.74597 1.000 117.84088 ?  514 SER C O   1 
ATOM 3133 C CB  . SER B 2 193 ? -3.31209  33.67809 111.86971 1.000 126.20940 ?  514 SER C CB  1 
ATOM 3134 O OG  . SER B 2 193 ? -2.95382  32.97029 110.69566 1.000 142.06048 ?  514 SER C OG  1 
ATOM 3135 N N   . PHE B 2 194 ? -5.01559  33.11277 114.91396 1.000 130.36269 ?  515 PHE C N   1 
ATOM 3136 C CA  . PHE B 2 194 ? -5.33742  33.72265 116.20272 1.000 116.61498 ?  515 PHE C CA  1 
ATOM 3137 C C   . PHE B 2 194 ? -4.02825  34.10559 116.88147 1.000 123.79662 ?  515 PHE C C   1 
ATOM 3138 O O   . PHE B 2 194 ? -3.37044  33.27116 117.50785 1.000 130.48067 ?  515 PHE C O   1 
ATOM 3139 C CB  . PHE B 2 194 ? -6.16162  32.77044 117.06160 1.000 118.42606 ?  515 PHE C CB  1 
ATOM 3140 C CG  . PHE B 2 194 ? -7.40346  32.26551 116.38403 1.000 122.22051 ?  515 PHE C CG  1 
ATOM 3141 C CD1 . PHE B 2 194 ? -8.46495  33.11773 116.12959 1.000 119.43504 ?  515 PHE C CD1 1 
ATOM 3142 C CD2 . PHE B 2 194 ? -7.51153  30.93755 116.00648 1.000 127.92432 ?  515 PHE C CD2 1 
ATOM 3143 C CE1 . PHE B 2 194 ? -9.60833  32.65616 115.50571 1.000 124.38459 ?  515 PHE C CE1 1 
ATOM 3144 C CE2 . PHE B 2 194 ? -8.65333  30.46945 115.38347 1.000 127.06971 ?  515 PHE C CE2 1 
ATOM 3145 C CZ  . PHE B 2 194 ? -9.70316  31.33010 115.13337 1.000 123.69139 ?  515 PHE C CZ  1 
ATOM 3146 N N   . GLU B 2 195 ? -3.64932  35.37324 116.75625 1.000 129.58980 ?  516 GLU C N   1 
ATOM 3147 C CA  . GLU B 2 195 ? -2.38132  35.85539 117.29083 1.000 121.75073 ?  516 GLU C CA  1 
ATOM 3148 C C   . GLU B 2 195 ? -2.44733  36.03104 118.80492 1.000 114.61335 ?  516 GLU C C   1 
ATOM 3149 O O   . GLU B 2 195 ? -3.31040  36.74096 119.32124 1.000 110.16551 ?  516 GLU C O   1 
ATOM 3150 C CB  . GLU B 2 195 ? -1.99282  37.17582 116.62226 1.000 126.29470 ?  516 GLU C CB  1 
ATOM 3151 C CG  . GLU B 2 195 ? -0.53017  37.55315 116.78382 1.000 132.57062 ?  516 GLU C CG  1 
ATOM 3152 C CD  . GLU B 2 195 ? -0.17856  38.83505 116.05438 1.000 140.90550 ?  516 GLU C CD  1 
ATOM 3153 O OE1 . GLU B 2 195 ? -1.04010  39.73701 115.98670 1.000 134.31592 ?  516 GLU C OE1 1 
ATOM 3154 O OE2 . GLU B 2 195 ? 0.95601   38.93783 115.54188 1.000 136.04490 -1 516 GLU C OE2 1 
ATOM 3155 N N   . ALA B 2 201 ? -7.65227  42.00784 125.01243 1.000 131.79591 ?  522 ALA C N   1 
ATOM 3156 C CA  . ALA B 2 201 ? -8.73401  41.14453 124.55358 1.000 140.39325 ?  522 ALA C CA  1 
ATOM 3157 C C   . ALA B 2 201 ? -9.68575  41.90444 123.63645 1.000 140.16693 ?  522 ALA C C   1 
ATOM 3158 O O   . ALA B 2 201 ? -10.85606 42.09572 123.96429 1.000 150.24370 ?  522 ALA C O   1 
ATOM 3159 C CB  . ALA B 2 201 ? -9.49031  40.56371 125.74077 1.000 142.74641 ?  522 ALA C CB  1 
ATOM 3160 N N   . THR B 2 202 ? -9.17606  42.33464 122.48217 1.000 139.13869 ?  523 THR C N   1 
ATOM 3161 C CA  . THR B 2 202 ? -9.97773  43.09194 121.53003 1.000 143.21022 ?  523 THR C CA  1 
ATOM 3162 C C   . THR B 2 202 ? -10.89861 42.21513 120.69083 1.000 142.61371 ?  523 THR C C   1 
ATOM 3163 O O   . THR B 2 202 ? -11.79484 42.74864 120.02741 1.000 138.90928 ?  523 THR C O   1 
ATOM 3164 C CB  . THR B 2 202 ? -9.06867  43.90410 120.60372 1.000 138.59782 ?  523 THR C CB  1 
ATOM 3165 O OG1 . THR B 2 202 ? -9.87056  44.67609 119.70121 1.000 142.27232 ?  523 THR C OG1 1 
ATOM 3166 C CG2 . THR B 2 202 ? -8.15888  42.98007 119.80543 1.000 122.07740 ?  523 THR C CG2 1 
ATOM 3167 N N   . VAL B 2 203 ? -10.70041 40.89765 120.69566 1.000 134.07043 ?  524 VAL C N   1 
ATOM 3168 C CA  . VAL B 2 203 ? -11.53076 39.96582 119.93800 1.000 130.00358 ?  524 VAL C CA  1 
ATOM 3169 C C   . VAL B 2 203 ? -11.79141 38.73808 120.79941 1.000 132.97269 ?  524 VAL C C   1 
ATOM 3170 O O   . VAL B 2 203 ? -10.85044 38.12177 121.31046 1.000 127.21192 ?  524 VAL C O   1 
ATOM 3171 C CB  . VAL B 2 203 ? -10.87255 39.54939 118.60710 1.000 140.02039 ?  524 VAL C CB  1 
ATOM 3172 C CG1 . VAL B 2 203 ? -11.68750 38.45563 117.93487 1.000 126.30318 ?  524 VAL C CG1 1 
ATOM 3173 C CG2 . VAL B 2 203 ? -10.71608 40.74727 117.68227 1.000 134.25666 ?  524 VAL C CG2 1 
ATOM 3174 N N   . CYS B 2 204 ? -13.06280 38.37954 120.95436 1.000 133.83911 ?  525 CYS C N   1 
ATOM 3175 C CA  . CYS B 2 204 ? -13.44197 37.18812 121.70885 1.000 125.60596 ?  525 CYS C CA  1 
ATOM 3176 C C   . CYS B 2 204 ? -14.55856 36.42651 121.00216 1.000 123.26212 ?  525 CYS C C   1 
ATOM 3177 O O   . CYS B 2 204 ? -15.66652 36.93917 120.84139 1.000 112.31564 ?  525 CYS C O   1 
ATOM 3178 C CB  . CYS B 2 204 ? -13.87925 37.56013 123.12740 1.000 115.25112 ?  525 CYS C CB  1 
ATOM 3179 S SG  . CYS B 2 204 ? -12.55427 38.19018 124.18386 1.000 127.36110 ?  525 CYS C SG  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 33  ? 0.55796 0.69940 0.76014 0.08165  -0.13421 -0.04451 3   ILE A N   
2    C CA  . ILE A 33  ? 0.58639 0.70439 0.82926 0.09025  -0.13601 -0.01180 3   ILE A CA  
3    C C   . ILE A 33  ? 0.58925 0.69377 0.89128 0.09489  -0.12570 -0.03999 3   ILE A C   
4    O O   . ILE A 33  ? 0.50839 0.60846 0.78193 0.08553  -0.11144 -0.07287 3   ILE A O   
5    C CB  . ILE A 33  ? 0.41681 0.51349 0.58725 0.08091  -0.12468 0.01961  3   ILE A CB  
6    C CG1 . ILE A 33  ? 0.72404 0.83134 0.82237 0.06992  -0.13125 0.04211  3   ILE A CG1 
7    C CG2 . ILE A 33  ? 0.43672 0.51004 0.64811 0.08750  -0.12701 0.05552  3   ILE A CG2 
8    C CD1 . ILE A 33  ? 0.92064 1.00458 0.94512 0.05727  -0.11512 0.07032  3   ILE A CD1 
9    N N   . VAL A 34  ? 0.67730 0.77326 1.05986 0.10729  -0.13402 -0.02591 4   VAL A N   
10   C CA  . VAL A 34  ? 0.48822 0.56908 0.93125 0.10969  -0.12431 -0.05073 4   VAL A CA  
11   C C   . VAL A 34  ? 0.60137 0.65512 1.05649 0.11259  -0.12153 -0.01614 4   VAL A C   
12   O O   . VAL A 34  ? 0.55685 0.60320 1.03915 0.12141  -0.13409 0.02308  4   VAL A O   
13   C CB  . VAL A 34  ? 0.37409 0.46508 0.90935 0.12072  -0.13149 -0.06989 4   VAL A CB  
14   C CG1 . VAL A 34  ? 0.36721 0.43813 0.95815 0.11872  -0.11796 -0.09745 4   VAL A CG1 
15   C CG2 . VAL A 34  ? 0.39225 0.51256 0.91775 0.11626  -0.13200 -0.10543 4   VAL A CG2 
16   N N   . LEU A 35  ? 0.53711 0.57597 0.97281 0.10363  -0.10643 -0.02960 5   LEU A N   
17   C CA  . LEU A 35  ? 0.38764 0.40288 0.83595 0.10403  -0.10064 -0.00170 5   LEU A CA  
18   C C   . LEU A 35  ? 0.45713 0.45867 0.98347 0.10690  -0.09848 -0.01840 5   LEU A C   
19   O O   . LEU A 35  ? 0.58042 0.58260 1.11584 0.09768  -0.09077 -0.05782 5   LEU A O   
20   C CB  . LEU A 35  ? 0.47069 0.47998 0.85840 0.09247  -0.08599 -0.00366 5   LEU A CB  
21   C CG  . LEU A 35  ? 0.44414 0.46090 0.75111 0.08738  -0.08199 0.01178  5   LEU A CG  
22   C CD1 . LEU A 35  ? 0.52158 0.53012 0.78599 0.07822  -0.06536 0.00780  5   LEU A CD1 
23   C CD2 . LEU A 35  ? 0.41737 0.42712 0.71355 0.09070  -0.08807 0.05717  5   LEU A CD2 
24   N N   . THR A 36  ? 0.61090 0.59710 1.18925 0.11684  -0.10510 0.01174  6   THR A N   
25   C CA  . THR A 36  ? 0.57149 0.54019 1.22594 0.11958  -0.10163 -0.00024 6   THR A CA  
26   C C   . THR A 36  ? 0.47959 0.42504 1.13354 0.11524  -0.09505 0.02954  6   THR A C   
27   O O   . THR A 36  ? 0.53310 0.46815 1.18177 0.12019  -0.10153 0.07133  6   THR A O   
28   C CB  . THR A 36  ? 0.43865 0.40907 1.13969 0.12634  -0.11065 0.00636  6   THR A CB  
29   O OG1 . THR A 36  ? 0.42485 0.41976 1.12814 0.12964  -0.11544 -0.02089 6   THR A OG1 
30   C CG2 . THR A 36  ? 0.45310 0.40666 1.20806 0.11863  -0.10016 -0.01083 6   THR A CG2 
31   N N   . GLN A 37  ? 0.41470 0.35197 1.07356 0.10370  -0.08301 0.00833  7   GLN A N   
32   C CA  . GLN A 37  ? 0.42644 0.34574 1.08913 0.09771  -0.07518 0.03222  7   GLN A CA  
33   C C   . GLN A 37  ? 0.58504 0.48991 1.29991 0.09229  -0.07211 0.03082  7   GLN A C   
34   O O   . GLN A 37  ? 0.61654 0.52413 1.36568 0.08913  -0.07150 0.00165  7   GLN A O   
35   C CB  . GLN A 37  ? 0.47867 0.40193 1.11385 0.08430  -0.06559 0.01370  7   GLN A CB  
36   C CG  . GLN A 37  ? 0.48529 0.42645 1.04854 0.08149  -0.06370 0.01328  7   GLN A CG  
37   C CD  . GLN A 37  ? 0.51456 0.45878 1.05589 0.06829  -0.05603 0.00104  7   GLN A CD  
38   O OE1 . GLN A 37  ? 0.59300 0.54997 1.09200 0.06206  -0.05680 -0.02005 7   GLN A OE1 
39   N NE2 . GLN A 37  ? 0.52536 0.45782 1.09774 0.06341  -0.04985 0.01553  7   GLN A NE2 
40   N N   . SER A 38  ? 0.64140 0.53046 1.36276 0.09008  -0.06806 0.06200  8   SER A N   
41   C CA  . SER A 38  ? 0.57418 0.44866 1.34265 0.08509  -0.06449 0.06471  8   SER A CA  
42   C C   . SER A 38  ? 0.70863 0.57051 1.47351 0.07714  -0.05526 0.08729  8   SER A C   
43   O O   . SER A 38  ? 0.72474 0.58302 1.45508 0.07977  -0.05386 0.11728  8   SER A O   
44   C CB  . SER A 38  ? 0.63273 0.50023 1.42343 0.09562  -0.07503 0.08754  8   SER A CB  
45   O OG  . SER A 38  ? 0.86809 0.72931 1.62379 0.10143  -0.08249 0.12944  8   SER A OG  
46   N N   . PRO A 39  ? 0.52538 0.38050 1.32593 0.06589  -0.04739 0.07354  9   PRO A N   
47   C CA  . PRO A 39  ? 0.50456 0.36106 1.34469 0.05936  -0.04550 0.03788  9   PRO A CA  
48   C C   . PRO A 39  ? 0.55115 0.42086 1.37783 0.04942  -0.04418 -0.00066 9   PRO A C   
49   O O   . PRO A 39  ? 0.62675 0.50449 1.41571 0.04931  -0.04620 0.00121  9   PRO A O   
50   C CB  . PRO A 39  ? 0.52433 0.36726 1.39823 0.04937  -0.03700 0.04417  9   PRO A CB  
51   C CG  . PRO A 39  ? 0.51776 0.36026 1.36627 0.04509  -0.03280 0.06750  9   PRO A CG  
52   C CD  . PRO A 39  ? 0.51781 0.36277 1.32387 0.05736  -0.03808 0.09377  9   PRO A CD  
53   N N   . GLY A 40  ? 0.64423 0.51512 1.49983 0.04009  -0.03991 -0.03543 10  GLY A N   
54   C CA  . GLY A 40  ? 0.70192 0.58302 1.53907 0.02602  -0.03861 -0.07353 10  GLY A CA  
55   C C   . GLY A 40  ? 0.72407 0.60250 1.55807 0.00819  -0.03555 -0.07861 10  GLY A C   
56   O O   . GLY A 40  ? 0.65120 0.53740 1.45052 -0.00168 -0.04047 -0.08833 10  GLY A O   
57   N N   . THR A 41  ? 0.60488 0.47266 1.47319 0.00332  -0.02865 -0.07091 11  THR A N   
58   C CA  . THR A 41  ? 0.56650 0.43223 1.43383 -0.01346 -0.02656 -0.07214 11  THR A CA  
59   C C   . THR A 41  ? 0.51886 0.37341 1.41478 -0.00842 -0.02248 -0.03787 11  THR A C   
60   O O   . THR A 41  ? 0.52017 0.36284 1.44554 -0.00032 -0.01742 -0.02833 11  THR A O   
61   C CB  . THR A 41  ? 0.66900 0.53137 1.53691 -0.03058 -0.01896 -0.10633 11  THR A CB  
62   O OG1 . THR A 41  ? 0.56672 0.43941 1.39675 -0.03690 -0.02015 -0.13711 11  THR A OG1 
63   C CG2 . THR A 41  ? 0.89132 0.75142 1.74652 -0.04981 -0.02032 -0.10499 11  THR A CG2 
64   N N   . LEU A 42  ? 0.60017 0.45918 1.48730 -0.01393 -0.02421 -0.01917 12  LEU A N   
65   C CA  . LEU A 42  ? 0.52236 0.37303 1.42996 -0.01138 -0.01791 0.01314  12  LEU A CA  
66   C C   . LEU A 42  ? 0.50405 0.36064 1.41966 -0.02881 -0.01706 0.01042  12  LEU A C   
67   O O   . LEU A 42  ? 0.75146 0.62326 1.64920 -0.03544 -0.02345 0.00841  12  LEU A O   
68   C CB  . LEU A 42  ? 0.49559 0.34803 1.38132 0.00215  -0.01744 0.04606  12  LEU A CB  
69   C CG  . LEU A 42  ? 0.52062 0.36209 1.41694 0.00453  -0.00841 0.08070  12  LEU A CG  
70   C CD1 . LEU A 42  ? 0.55487 0.37747 1.47326 0.00989  -0.00720 0.08688  12  LEU A CD1 
71   C CD2 . LEU A 42  ? 0.51774 0.36066 1.37939 0.01453  -0.00522 0.10928  12  LEU A CD2 
72   N N   . SER A 43  ? 0.53192 0.37667 1.47373 -0.03641 -0.01024 0.01113  13  SER A N   
73   C CA  . SER A 43  ? 0.54036 0.38975 1.48958 -0.05382 -0.01004 0.01009  13  SER A CA  
74   C C   . SER A 43  ? 0.55442 0.39848 1.52688 -0.05052 -0.00082 0.04231  13  SER A C   
75   O O   . SER A 43  ? 0.58115 0.40626 1.57006 -0.04456 0.00705  0.05330  13  SER A O   
76   C CB  . SER A 43  ? 0.66058 0.49802 1.61198 -0.06970 -0.00754 -0.01758 13  SER A CB  
77   O OG  . SER A 43  ? 1.12135 0.96297 2.04134 -0.07636 -0.01310 -0.04841 13  SER A OG  
78   N N   . LEU A 44  ? 0.54013 0.40069 1.51346 -0.05493 -0.00116 0.05726  14  LEU A N   
79   C CA  . LEU A 44  ? 0.67687 0.53482 1.66860 -0.05396 0.01088  0.08602  14  LEU A CA  
80   C C   . LEU A 44  ? 0.55170 0.42801 1.55959 -0.06881 0.00911  0.08600  14  LEU A C   
81   O O   . LEU A 44  ? 0.53844 0.42959 1.53715 -0.07875 -0.00432 0.06785  14  LEU A O   
82   C CB  . LEU A 44  ? 0.57081 0.43040 1.54530 -0.03967 0.01814  0.11150  14  LEU A CB  
83   C CG  . LEU A 44  ? 0.56084 0.39989 1.51672 -0.02531 0.01925  0.12204  14  LEU A CG  
84   C CD1 . LEU A 44  ? 0.55318 0.39452 1.47641 -0.01454 0.02422  0.14404  14  LEU A CD1 
85   C CD2 . LEU A 44  ? 0.60226 0.41802 1.57433 -0.02687 0.02697  0.13673  14  LEU A CD2 
86   N N   . SER A 45  ? 0.56909 0.44379 1.59778 -0.07130 0.02195  0.10724  15  SER A N   
87   C CA  . SER A 45  ? 0.57675 0.47038 1.62812 -0.08395 0.02218  0.11098  15  SER A CA  
88   C C   . SER A 45  ? 0.74160 0.65408 1.80039 -0.07626 0.03251  0.13147  15  SER A C   
89   O O   . SER A 45  ? 0.72336 0.62684 1.76586 -0.06433 0.04485  0.14705  15  SER A O   
90   C CB  . SER A 45  ? 0.60777 0.48605 1.68033 -0.09486 0.03240  0.11707  15  SER A CB  
91   O OG  . SER A 45  ? 0.73578 0.59607 1.80276 -0.10417 0.02576  0.09613  15  SER A OG  
92   N N   . PRO A 46  ? 0.54285 0.48058 1.62351 -0.08345 0.02818  0.13199  16  PRO A N   
93   C CA  . PRO A 46  ? 0.53009 0.48567 1.62474 -0.07577 0.04263  0.14967  16  PRO A CA  
94   C C   . PRO A 46  ? 0.55760 0.49951 1.65984 -0.07512 0.06951  0.17003  16  PRO A C   
95   O O   . PRO A 46  ? 0.58575 0.51804 1.70439 -0.08551 0.07456  0.17224  16  PRO A O   
96   C CB  . PRO A 46  ? 0.52474 0.50739 1.64932 -0.08505 0.02991  0.14532  16  PRO A CB  
97   C CG  . PRO A 46  ? 0.52568 0.50581 1.63138 -0.09657 0.00345  0.12363  16  PRO A CG  
98   C CD  . PRO A 46  ? 0.54605 0.49690 1.63457 -0.09920 0.00848  0.11576  16  PRO A CD  
99   N N   . GLY A 47  ? 0.55485 0.49311 1.63800 -0.06519 0.08755  0.18451  17  GLY A N   
100  C CA  . GLY A 47  ? 0.58832 0.50955 1.66300 -0.06716 0.11431  0.20409  17  GLY A CA  
101  C C   . GLY A 47  ? 0.61052 0.49840 1.63851 -0.06173 0.11752  0.21501  17  GLY A C   
102  O O   . GLY A 47  ? 0.68887 0.55947 1.69226 -0.06378 0.13863  0.23348  17  GLY A O   
103  N N   . GLU A 48  ? 0.60082 0.47799 1.61372 -0.05594 0.09673  0.20391  18  GLU A N   
104  C CA  . GLU A 48  ? 0.62419 0.47106 1.59809 -0.04865 0.09478  0.21470  18  GLU A CA  
105  C C   . GLU A 48  ? 0.64512 0.49339 1.57918 -0.03752 0.09538  0.22017  18  GLU A C   
106  O O   . GLU A 48  ? 0.65782 0.52846 1.59505 -0.03564 0.10001  0.21515  18  GLU A O   
107  C CB  . GLU A 48  ? 0.62534 0.46079 1.60721 -0.04673 0.07502  0.19824  18  GLU A CB  
108  C CG  . GLU A 48  ? 0.80191 0.64076 1.82174 -0.05956 0.07229  0.18532  18  GLU A CG  
109  C CD  . GLU A 48  ? 0.88623 0.70403 1.90944 -0.05916 0.06118  0.17226  18  GLU A CD  
110  O OE1 . GLU A 48  ? 0.91879 0.70867 1.93315 -0.05633 0.06590  0.18711  18  GLU A OE1 
111  O OE2 . GLU A 48  ? 0.85300 0.68033 1.88574 -0.06262 0.04830  0.14698  18  GLU A OE2 
112  N N   . ARG A 49  ? 0.88451 0.70796 1.78074 -0.03005 0.08961  0.23129  19  ARG A N   
113  C CA  . ARG A 49  ? 0.62172 0.44223 1.47275 -0.02042 0.08861  0.23849  19  ARG A CA  
114  C C   . ARG A 49  ? 0.64080 0.46038 1.48461 -0.00873 0.06465  0.22273  19  ARG A C   
115  O O   . ARG A 49  ? 0.68513 0.48962 1.53917 -0.00653 0.05335  0.22091  19  ARG A O   
116  C CB  . ARG A 49  ? 0.67048 0.46276 1.47590 -0.02393 0.10109  0.26796  19  ARG A CB  
117  C CG  . ARG A 49  ? 0.67074 0.45672 1.42284 -0.01624 0.09813  0.27773  19  ARG A CG  
118  C CD  . ARG A 49  ? 0.72822 0.48389 1.42842 -0.02566 0.10874  0.30833  19  ARG A CD  
119  N NE  . ARG A 49  ? 0.78282 0.53775 1.47512 -0.04175 0.14012  0.31642  19  ARG A NE  
120  C CZ  . ARG A 49  ? 1.00498 0.73351 1.64578 -0.05707 0.15600  0.33941  19  ARG A CZ  
121  N NH1 . ARG A 49  ? 0.98905 0.68943 1.58159 -0.05831 0.13936  0.36052  19  ARG A NH1 
122  N NH2 . ARG A 49  ? 1.17100 0.90152 1.80816 -0.07275 0.18780  0.34038  19  ARG A NH2 
123  N N   . ALA A 50  ? 0.71555 0.55076 1.54301 -0.00160 0.05860  0.21016  20  ALA A N   
124  C CA  . ALA A 50  ? 0.55111 0.38777 1.36743 0.00873  0.03847  0.19220  20  ALA A CA  
125  C C   . ALA A 50  ? 0.67427 0.50068 1.43988 0.01889  0.03721  0.20889  20  ALA A C   
126  O O   . ALA A 50  ? 0.56441 0.39576 1.30148 0.01907  0.04899  0.21709  20  ALA A O   
127  C CB  . ALA A 50  ? 0.50887 0.36857 1.33920 0.00693  0.02968  0.16343  20  ALA A CB  
128  N N   . THR A 51  ? 0.82692 0.63921 1.58338 0.02652  0.02329  0.21446  21  THR A N   
129  C CA  . THR A 51  ? 0.59814 0.40114 1.30871 0.03500  0.01668  0.23269  21  THR A CA  
130  C C   . THR A 51  ? 0.57007 0.38667 1.28140 0.04690  -0.00168 0.20774  21  THR A C   
131  O O   . THR A 51  ? 0.57703 0.39091 1.31463 0.05147  -0.01440 0.19698  21  THR A O   
132  C CB  . THR A 51  ? 0.65049 0.42753 1.35082 0.03328  0.01206  0.26260  21  THR A CB  
133  O OG1 . THR A 51  ? 0.67994 0.44319 1.37476 0.01918  0.03164  0.28259  21  THR A OG1 
134  C CG2 . THR A 51  ? 0.67066 0.43936 1.32168 0.03883  0.00134  0.28436  21  THR A CG2 
135  N N   . LEU A 52  ? 0.54869 0.37928 1.23215 0.05113  -0.00076 0.19741  22  LEU A N   
136  C CA  . LEU A 52  ? 0.59488 0.43951 1.27195 0.06088  -0.01588 0.17202  22  LEU A CA  
137  C C   . LEU A 52  ? 0.58958 0.42953 1.22657 0.07035  -0.02505 0.19261  22  LEU A C   
138  O O   . LEU A 52  ? 0.63080 0.45999 1.22866 0.06554  -0.01701 0.22345  22  LEU A O   
139  C CB  . LEU A 52  ? 0.58540 0.44956 1.25270 0.05856  -0.01201 0.14596  22  LEU A CB  
140  C CG  . LEU A 52  ? 0.56925 0.44121 1.27753 0.04858  -0.01334 0.11788  22  LEU A CG  
141  C CD1 . LEU A 52  ? 0.50416 0.37085 1.24308 0.03736  -0.00100 0.13262  22  LEU A CD1 
142  C CD2 . LEU A 52  ? 0.71119 0.60532 1.39374 0.04493  -0.01564 0.09349  22  LEU A CD2 
143  N N   . SER A 53  ? 0.51822 0.36967 1.15987 0.07975  -0.04099 0.17298  23  SER A N   
144  C CA  . SER A 53  ? 0.62432 0.47634 1.23591 0.08859  -0.05453 0.19126  23  SER A CA  
145  C C   . SER A 53  ? 0.61817 0.49703 1.20949 0.09357  -0.06121 0.15775  23  SER A C   
146  O O   . SER A 53  ? 0.66797 0.55648 1.28626 0.09305  -0.06040 0.12156  23  SER A O   
147  C CB  . SER A 53  ? 0.56756 0.40994 1.20722 0.09251  -0.06956 0.20534  23  SER A CB  
148  O OG  . SER A 53  ? 0.72277 0.54233 1.36566 0.08422  -0.06361 0.23538  23  SER A OG  
149  N N   . CYS A 54  ? 0.59047 0.47962 1.12944 0.09504  -0.06764 0.17016  24  CYS A N   
150  C CA  . CYS A 54  ? 0.53638 0.45068 1.04918 0.09837  -0.07381 0.14096  24  CYS A CA  
151  C C   . CYS A 54  ? 0.68750 0.60692 1.17696 0.10333  -0.09094 0.16395  24  CYS A C   
152  O O   . CYS A 54  ? 0.86540 0.78237 1.29309 0.09497  -0.08768 0.18976  24  CYS A O   
153  C CB  . CYS A 54  ? 0.52512 0.45164 0.98009 0.08913  -0.05785 0.12616  24  CYS A CB  
154  S SG  . CYS A 54  ? 0.51310 0.46637 0.91936 0.08982  -0.06393 0.09484  24  CYS A SG  
155  N N   . ARG A 55  ? 0.50268 0.42893 1.04346 0.11506  -0.10847 0.15428  25  ARG A N   
156  C CA  . ARG A 55  ? 0.52491 0.46017 1.05856 0.12085  -0.12989 0.17623  25  ARG A CA  
157  C C   . ARG A 55  ? 0.59852 0.56457 1.10467 0.12168  -0.13295 0.14424  25  ARG A C   
158  O O   . ARG A 55  ? 0.69329 0.67094 1.22965 0.12471  -0.12708 0.10190  25  ARG A O   
159  C CB  . ARG A 55  ? 0.54636 0.47226 1.15777 0.13249  -0.14635 0.18621  25  ARG A CB  
160  C CG  . ARG A 55  ? 0.71379 0.65510 1.32817 0.13821  -0.17098 0.20403  25  ARG A CG  
161  C CD  . ARG A 55  ? 0.97956 0.91148 1.65378 0.14246  -0.18065 0.21182  25  ARG A CD  
162  N NE  . ARG A 55  ? 1.33944 1.24180 2.00603 0.13533  -0.18253 0.25125  25  ARG A NE  
163  C CZ  . ARG A 55  ? 1.24943 1.13877 1.95909 0.13748  -0.19381 0.26901  25  ARG A CZ  
164  N NH1 . ARG A 55  ? 1.11217 1.01513 1.87988 0.14732  -0.20296 0.25196  25  ARG A NH1 
165  N NH2 . ARG A 55  ? 1.05025 0.91200 1.74588 0.12898  -0.19484 0.30355  25  ARG A NH2 
166  N N   . ALA A 56  ? 0.51318 0.49045 0.95801 0.11567  -0.14132 0.16395  26  ALA A N   
167  C CA  . ALA A 56  ? 0.49226 0.49848 0.90398 0.11435  -0.14491 0.13764  26  ALA A CA  
168  C C   . ALA A 56  ? 0.60369 0.62721 1.06066 0.12478  -0.17170 0.14762  26  ALA A C   
169  O O   . ALA A 56  ? 0.65563 0.66766 1.13919 0.12879  -0.19094 0.18840  26  ALA A O   
170  C CB  . ALA A 56  ? 0.57196 0.58042 0.88428 0.09860  -0.13494 0.14973  26  ALA A CB  
171  N N   . SER A 57  ? 0.60889 0.66013 1.07664 0.12813  -0.17352 0.11042  27  SER A N   
172  C CA  . SER A 57  ? 0.52768 0.60130 1.04839 0.13875  -0.19777 0.11553  27  SER A CA  
173  C C   . SER A 57  ? 0.57554 0.65858 1.04008 0.13021  -0.21879 0.15740  27  SER A C   
174  O O   . SER A 57  ? 0.66937 0.76077 1.18272 0.13835  -0.24678 0.18601  27  SER A O   
175  C CB  . SER A 57  ? 0.45222 0.55384 0.99235 0.14054  -0.19034 0.06217  27  SER A CB  
176  O OG  . SER A 57  ? 0.45923 0.57392 0.90796 0.12561  -0.17978 0.04532  27  SER A OG  
177  N N   . GLN A 58  ? 0.63521 0.71584 0.99904 0.11240  -0.20620 0.16216  28  GLN A N   
178  C CA  . GLN A 58  ? 0.64323 0.72713 0.93827 0.09746  -0.22184 0.20130  28  GLN A CA  
179  C C   . GLN A 58  ? 0.61475 0.67074 0.82158 0.07900  -0.19894 0.21844  28  GLN A C   
180  O O   . GLN A 58  ? 0.67380 0.71381 0.87886 0.08027  -0.17316 0.19868  28  GLN A O   
181  C CB  . GLN A 58  ? 0.55330 0.67242 0.81369 0.09145  -0.22890 0.18008  28  GLN A CB  
182  C CG  . GLN A 58  ? 1.06113 1.18761 1.27227 0.08549  -0.20033 0.13114  28  GLN A CG  
183  C CD  . GLN A 58  ? 1.01211 1.17301 1.19633 0.07954  -0.20744 0.10773  28  GLN A CD  
184  O OE1 . GLN A 58  ? 1.01221 1.19614 1.25619 0.09001  -0.21040 0.07262  28  GLN A OE1 
185  N NE2 . GLN A 58  ? 1.02505 1.18846 1.11771 0.06021  -0.20791 0.12541  28  GLN A NE2 
186  N N   . SER A 59  ? 0.64682 0.69697 0.78166 0.05977  -0.20798 0.25528  29  SER A N   
187  C CA  . SER A 59  ? 0.70631 0.72662 0.76048 0.03943  -0.18384 0.27429  29  SER A CA  
188  C C   . SER A 59  ? 0.78209 0.80651 0.77214 0.03163  -0.15116 0.23729  29  SER A C   
189  O O   . SER A 59  ? 1.08165 1.12984 1.03901 0.02825  -0.15312 0.21466  29  SER A O   
190  C CB  . SER A 59  ? 0.72580 0.73612 0.71324 0.01536  -0.20145 0.32197  29  SER A CB  
191  O OG  . SER A 59  ? 0.81456 0.79272 0.72446 -0.00742 -0.17322 0.33802  29  SER A OG  
192  N N   . VAL A 60  ? 0.87404 0.87483 0.84948 0.02860  -0.12140 0.23198  30  VAL A N   
193  C CA  . VAL A 60  ? 0.88358 0.88264 0.80136 0.02101  -0.08962 0.20304  30  VAL A CA  
194  C C   . VAL A 60  ? 0.88952 0.87053 0.71138 -0.00580 -0.07432 0.22903  30  VAL A C   
195  O O   . VAL A 60  ? 0.87440 0.82792 0.67323 -0.01715 -0.05163 0.24662  30  VAL A O   
196  C CB  . VAL A 60  ? 0.66920 0.65466 0.62698 0.03068  -0.06688 0.18524  30  VAL A CB  
197  C CG1 . VAL A 60  ? 0.62731 0.61378 0.53712 0.02572  -0.03953 0.15501  30  VAL A CG1 
198  C CG2 . VAL A 60  ? 0.68589 0.68325 0.73673 0.05167  -0.08323 0.16495  30  VAL A CG2 
199  N N   . SER A 61  ? 1.07172 1.06802 0.83610 -0.01865 -0.08509 0.22992  31  SER A N   
200  C CA  . SER A 61  ? 1.11277 1.09078 0.77968 -0.04926 -0.07242 0.25498  31  SER A CA  
201  C C   . SER A 61  ? 1.25212 1.21060 0.86053 -0.06025 -0.02719 0.23510  31  SER A C   
202  O O   . SER A 61  ? 1.22770 1.15810 0.79170 -0.07596 -0.00131 0.24277  31  SER A O   
203  C CB  . SER A 61  ? 1.15537 1.15711 0.77667 -0.06163 -0.09593 0.25810  31  SER A CB  
204  O OG  . SER A 61  ? 1.33276 1.35636 0.94329 -0.05376 -0.08646 0.21542  31  SER A OG  
205  N N   . SER A 62  ? 0.97847 0.94881 0.60905 -0.04386 -0.01349 0.19532  32  SER A N   
206  C CA  . SER A 62  ? 0.73466 0.68744 0.32097 -0.05110 0.02710  0.17659  32  SER A CA  
207  C C   . SER A 62  ? 0.90979 0.83877 0.53146 -0.04792 0.05171  0.18607  32  SER A C   
208  O O   . SER A 62  ? 1.11774 1.02884 0.70590 -0.05649 0.08842  0.17731  32  SER A O   
209  C CB  . SER A 62  ? 0.66195 0.63309 0.26339 -0.03563 0.02894  0.13444  32  SER A CB  
210  O OG  . SER A 62  ? 0.65505 0.63951 0.34526 -0.01207 0.01161  0.12010  32  SER A OG  
211  N N   . THR A 63  ? 0.94107 0.86937 0.63267 -0.03608 0.03365  0.20297  33  THR A N   
212  C CA  . THR A 63  ? 0.93289 0.84044 0.66330 -0.03423 0.05466  0.21343  33  THR A CA  
213  C C   . THR A 63  ? 0.68442 0.59521 0.44748 -0.02065 0.07756  0.18210  33  THR A C   
214  O O   . THR A 63  ? 1.02315 0.91613 0.77649 -0.02811 0.11167  0.18313  33  THR A O   
215  C CB  . THR A 63  ? 0.99325 0.87012 0.65853 -0.06290 0.08101  0.24221  33  THR A CB  
216  O OG1 . THR A 63  ? 1.23722 1.11268 0.84561 -0.08197 0.05858  0.26792  33  THR A OG1 
217  C CG2 . THR A 63  ? 1.15632 1.01391 0.87077 -0.06269 0.08890  0.26316  33  THR A CG2 
218  N N   . PHE A 64  ? 0.58753 0.52100 0.39137 -0.00218 0.05816  0.15415  34  PHE A N   
219  C CA  . PHE A 64  ? 0.85022 0.78744 0.68644 0.00914  0.07147  0.12650  34  PHE A CA  
220  C C   . PHE A 64  ? 0.86379 0.81111 0.78708 0.02611  0.05119  0.11797  34  PHE A C   
221  O O   . PHE A 64  ? 0.70801 0.66925 0.65618 0.03546  0.03992  0.08963  34  PHE A O   
222  C CB  . PHE A 64  ? 0.79103 0.74039 0.58370 0.00925  0.07045  0.09723  34  PHE A CB  
223  C CG  . PHE A 64  ? 0.85204 0.78830 0.55786 -0.00880 0.09556  0.10125  34  PHE A CG  
224  C CD1 . PHE A 64  ? 0.69751 0.60958 0.37784 -0.02219 0.12894  0.11964  34  PHE A CD1 
225  C CD2 . PHE A 64  ? 0.84067 0.78741 0.48927 -0.01489 0.08848  0.08477  34  PHE A CD2 
226  C CE1 . PHE A 64  ? 0.62671 0.54272 0.25752 -0.03990 0.14327  0.11477  34  PHE A CE1 
227  C CE2 . PHE A 64  ? 0.70119 0.66148 0.32013 -0.02790 0.09999  0.08199  34  PHE A CE2 
228  C CZ  . PHE A 64  ? 0.60146 0.55172 0.22255 -0.03776 0.12267  0.09518  34  PHE A CZ  
229  N N   . LEU A 65  ? 0.68547 0.62298 0.65086 0.02707  0.04721  0.14201  35  LEU A N   
230  C CA  . LEU A 65  ? 0.72017 0.66291 0.76707 0.04033  0.03152  0.13532  35  LEU A CA  
231  C C   . LEU A 65  ? 0.68760 0.62501 0.76977 0.04200  0.05156  0.12790  35  LEU A C   
232  O O   . LEU A 65  ? 0.69832 0.62068 0.77102 0.03377  0.07698  0.14566  35  LEU A O   
233  C CB  . LEU A 65  ? 0.77902 0.71089 0.85665 0.04019  0.01835  0.16534  35  LEU A CB  
234  C CG  . LEU A 65  ? 0.66068 0.59937 0.81535 0.05406  -0.00612 0.15746  35  LEU A CG  
235  C CD1 . LEU A 65  ? 0.79629 0.73000 1.00988 0.05798  0.00327  0.14832  35  LEU A CD1 
236  C CD2 . LEU A 65  ? 0.47937 0.44022 0.63903 0.06221  -0.02523 0.12668  35  LEU A CD2 
237  N N   . ALA A 66  ? 0.65597 0.60571 0.77944 0.05038  0.04013  0.10159  36  ALA A N   
238  C CA  . ALA A 66  ? 0.48758 0.43666 0.64882 0.05146  0.05249  0.09409  36  ALA A CA  
239  C C   . ALA A 66  ? 0.58038 0.53361 0.81485 0.05640  0.03494  0.08713  36  ALA A C   
240  O O   . ALA A 66  ? 0.57035 0.52988 0.82191 0.06009  0.01316  0.07375  36  ALA A O   
241  C CB  . ALA A 66  ? 0.40739 0.36426 0.53997 0.05140  0.05506  0.06949  36  ALA A CB  
242  N N   . TRP A 67  ? 0.56847 0.51797 0.84811 0.05498  0.04659  0.09511  37  TRP A N   
243  C CA  . TRP A 67  ? 0.41847 0.37057 0.76609 0.05580  0.03289  0.08913  37  TRP A CA  
244  C C   . TRP A 67  ? 0.47555 0.43770 0.84789 0.05322  0.03078  0.07283  37  TRP A C   
245  O O   . TRP A 67  ? 0.41624 0.37954 0.77762 0.05281  0.04844  0.07803  37  TRP A O   
246  C CB  . TRP A 67  ? 0.41224 0.35176 0.79811 0.05351  0.04485  0.11554  37  TRP A CB  
247  C CG  . TRP A 67  ? 0.43896 0.36560 0.81046 0.05458  0.03944  0.13461  37  TRP A CG  
248  C CD1 . TRP A 67  ? 0.53156 0.44622 0.85352 0.04973  0.05240  0.15807  37  TRP A CD1 
249  C CD2 . TRP A 67  ? 0.43893 0.36142 0.84751 0.05920  0.01852  0.13321  37  TRP A CD2 
250  N NE1 . TRP A 67  ? 0.49437 0.39882 0.82091 0.05141  0.03645  0.17452  37  TRP A NE1 
251  C CE2 . TRP A 67  ? 0.47258 0.38176 0.85630 0.05921  0.01656  0.15930  37  TRP A CE2 
252  C CE3 . TRP A 67  ? 0.41813 0.34480 0.87842 0.06142  0.00206  0.11218  37  TRP A CE3 
253  C CZ2 . TRP A 67  ? 0.56906 0.47021 0.98607 0.06510  -0.00266 0.16657  37  TRP A CZ2 
254  C CZ3 . TRP A 67  ? 0.42926 0.34658 0.92064 0.06639  -0.01207 0.11577  37  TRP A CZ3 
255  C CH2 . TRP A 67  ? 0.46040 0.36569 0.93413 0.07005  -0.01501 0.14355  37  TRP A CH2 
256  N N   . TYR A 68  ? 0.40865 0.37653 0.81548 0.04982  0.00912  0.05353  38  TYR A N   
257  C CA  . TYR A 68  ? 0.36650 0.34310 0.79388 0.04335  -0.00069 0.03904  38  TYR A CA  
258  C C   . TYR A 68  ? 0.45548 0.43280 0.94691 0.03542  -0.01277 0.03734  38  TYR A C   
259  O O   . TYR A 68  ? 0.42343 0.39350 0.93583 0.03478  -0.01810 0.03613  38  TYR A O   
260  C CB  . TYR A 68  ? 0.34658 0.32750 0.73106 0.03883  -0.01808 0.01082  38  TYR A CB  
261  C CG  . TYR A 68  ? 0.35441 0.33481 0.67281 0.04423  -0.00697 0.00987  38  TYR A CG  
262  C CD1 . TYR A 68  ? 0.47362 0.45200 0.75355 0.04889  -0.00413 0.01047  38  TYR A CD1 
263  C CD2 . TYR A 68  ? 0.49542 0.47688 0.79216 0.04384  -0.00012 0.00914  38  TYR A CD2 
264  C CE1 . TYR A 68  ? 0.51535 0.49338 0.73159 0.05059  0.00580  0.00940  38  TYR A CE1 
265  C CE2 . TYR A 68  ? 0.48694 0.46495 0.72051 0.04689  0.01234  0.00688  38  TYR A CE2 
266  C CZ  . TYR A 68  ? 0.50467 0.48126 0.69537 0.04904  0.01553  0.00647  38  TYR A CZ  
267  O OH  . TYR A 68  ? 0.47341 0.44676 0.59801 0.04896  0.02765  0.00404  38  TYR A OH  
268  N N   . GLN A 69  ? 0.40569 0.39134 0.93032 0.02868  -0.01755 0.03803  39  GLN A N   
269  C CA  . GLN A 69  ? 0.31885 0.30732 0.90060 0.01644  -0.03195 0.03508  39  GLN A CA  
270  C C   . GLN A 69  ? 0.36419 0.35891 0.93844 0.00208  -0.05720 0.01430  39  GLN A C   
271  O O   . GLN A 69  ? 0.53765 0.53885 1.09455 0.00364  -0.05944 0.01579  39  GLN A O   
272  C CB  . GLN A 69  ? 0.32363 0.31833 0.96078 0.01741  -0.01712 0.05926  39  GLN A CB  
273  C CG  . GLN A 69  ? 0.38452 0.38424 1.08193 0.00246  -0.03259 0.05783  39  GLN A CG  
274  C CD  . GLN A 69  ? 0.49489 0.50597 1.25136 0.00260  -0.01859 0.08022  39  GLN A CD  
275  O OE1 . GLN A 69  ? 0.46180 0.48732 1.23666 0.00360  -0.01968 0.08563  39  GLN A OE1 
276  N NE2 . GLN A 69  ? 0.53785 0.54195 1.32787 0.00140  -0.00484 0.09339  39  GLN A NE2 
277  N N   . GLN A 70  ? 0.31319 0.30296 0.89872 -0.01398 -0.07552 -0.00497 40  GLN A N   
278  C CA  . GLN A 70  ? 0.44434 0.43528 1.01429 -0.03476 -0.10117 -0.02623 40  GLN A CA  
279  C C   . GLN A 70  ? 0.32342 0.31445 0.94405 -0.05596 -0.11604 -0.02772 40  GLN A C   
280  O O   . GLN A 70  ? 0.33602 0.31593 0.95316 -0.06400 -0.11617 -0.04358 40  GLN A O   
281  C CB  . GLN A 70  ? 0.31625 0.29749 0.83181 -0.04096 -0.10732 -0.05665 40  GLN A CB  
282  C CG  . GLN A 70  ? 0.32524 0.30353 0.80729 -0.06539 -0.13111 -0.07906 40  GLN A CG  
283  C CD  . GLN A 70  ? 0.44827 0.41844 0.86334 -0.06878 -0.12734 -0.10750 40  GLN A CD  
284  O OE1 . GLN A 70  ? 0.33010 0.30048 0.69659 -0.06650 -0.12846 -0.11631 40  GLN A OE1 
285  N NE2 . GLN A 70  ? 0.54505 0.50892 0.95818 -0.07446 -0.12011 -0.12103 40  GLN A NE2 
286  N N   . LYS A 71  ? 0.57333 0.41188 0.79203 -0.07251 -0.15223 -0.04812 41  LYS A N   
287  C CA  . LYS A 71  ? 0.56459 0.40173 0.80633 -0.08249 -0.18541 -0.05601 41  LYS A CA  
288  C C   . LYS A 71  ? 0.59966 0.43142 0.78195 -0.08548 -0.20928 -0.07152 41  LYS A C   
289  O O   . LYS A 71  ? 0.61457 0.44981 0.75280 -0.08221 -0.20253 -0.06662 41  LYS A O   
290  C CB  . LYS A 71  ? 0.55713 0.41486 0.86669 -0.08622 -0.19636 -0.03665 41  LYS A CB  
291  C CG  . LYS A 71  ? 0.61247 0.47902 0.98540 -0.08936 -0.17498 -0.02459 41  LYS A CG  
292  C CD  . LYS A 71  ? 0.55835 0.45659 1.00809 -0.09253 -0.18350 -0.00797 41  LYS A CD  
293  C CE  . LYS A 71  ? 1.11019 1.02346 1.56372 -0.07639 -0.16848 0.00581  41  LYS A CE  
294  N NZ  . LYS A 71  ? 0.76798 0.71811 1.30691 -0.07427 -0.17294 0.02011  41  LYS A NZ  
295  N N   . PRO A 72  ? 0.71339 0.53379 0.88848 -0.09377 -0.23687 -0.09064 42  PRO A N   
296  C CA  . PRO A 72  ? 0.74470 0.55853 0.85134 -0.09737 -0.25596 -0.10927 42  PRO A CA  
297  C C   . PRO A 72  ? 0.69514 0.51890 0.78600 -0.10186 -0.27589 -0.09129 42  PRO A C   
298  O O   . PRO A 72  ? 0.79397 0.62653 0.93508 -0.10589 -0.29965 -0.07591 42  PRO A O   
299  C CB  . PRO A 72  ? 0.82399 0.61966 0.93762 -0.10627 -0.28505 -0.13259 42  PRO A CB  
300  C CG  . PRO A 72  ? 0.72724 0.52652 0.92417 -0.11282 -0.29069 -0.11671 42  PRO A CG  
301  C CD  . PRO A 72  ? 0.75565 0.56520 0.97985 -0.10253 -0.25147 -0.09726 42  PRO A CD  
302  N N   . GLY A 73  ? 0.81992 0.64301 0.84249 -0.10163 -0.26690 -0.09215 43  GLY A N   
303  C CA  . GLY A 73  ? 0.98814 0.81127 0.98204 -0.10671 -0.28641 -0.07269 43  GLY A CA  
304  C C   . GLY A 73  ? 0.82850 0.65574 0.84905 -0.09854 -0.26974 -0.04427 43  GLY A C   
305  O O   . GLY A 73  ? 0.92130 0.74232 0.92583 -0.10035 -0.28957 -0.02486 43  GLY A O   
306  N N   . GLN A 74  ? 0.74050 0.57347 0.79671 -0.08919 -0.23579 -0.04157 44  GLN A N   
307  C CA  . GLN A 74  ? 0.69101 0.52423 0.77234 -0.08018 -0.21778 -0.01926 44  GLN A CA  
308  C C   . GLN A 74  ? 0.64704 0.47713 0.69138 -0.07859 -0.18148 -0.02328 44  GLN A C   
309  O O   . GLN A 74  ? 0.80521 0.63916 0.81545 -0.08215 -0.16969 -0.04250 44  GLN A O   
310  C CB  . GLN A 74  ? 0.62730 0.47389 0.79502 -0.07130 -0.21188 -0.01025 44  GLN A CB  
311  C CG  . GLN A 74  ? 0.80417 0.66317 1.02404 -0.07443 -0.24833 -0.00596 44  GLN A CG  
312  C CD  . GLN A 74  ? 0.84682 0.72836 1.15772 -0.06802 -0.23704 0.00368  44  GLN A CD  
313  O OE1 . GLN A 74  ? 0.82111 0.70535 1.14981 -0.05947 -0.20150 0.00914  44  GLN A OE1 
314  N NE2 . GLN A 74  ? 0.91769 0.81791 1.28574 -0.07404 -0.26697 0.00535  44  GLN A NE2 
315  N N   . ALA A 75  ? 0.63741 0.46098 0.69126 -0.07225 -0.16531 -0.00647 45  ALA A N   
316  C CA  . ALA A 75  ? 0.57912 0.39934 0.60484 -0.07219 -0.13366 -0.00813 45  ALA A CA  
317  C C   . ALA A 75  ? 0.54010 0.36823 0.60862 -0.06329 -0.10927 -0.01313 45  ALA A C   
318  O O   . ALA A 75  ? 0.76287 0.59716 0.88780 -0.05732 -0.11252 -0.00911 45  ALA A O   
319  C CB  . ALA A 75  ? 0.59405 0.39470 0.60454 -0.07106 -0.13055 0.01090  45  ALA A CB  
320  N N   . PRO A 76  ? 0.52543 0.35544 0.56823 -0.06404 -0.08551 -0.02076 46  PRO A N   
321  C CA  . PRO A 76  ? 0.50763 0.34006 0.58142 -0.05658 -0.06438 -0.02216 46  PRO A CA  
322  C C   . PRO A 76  ? 0.55633 0.38196 0.66549 -0.04899 -0.05166 -0.00685 46  PRO A C   
323  O O   . PRO A 76  ? 0.60364 0.41747 0.70027 -0.04732 -0.05081 0.00242  46  PRO A O   
324  C CB  . PRO A 76  ? 0.50198 0.33818 0.53456 -0.05930 -0.04690 -0.03077 46  PRO A CB  
325  C CG  . PRO A 76  ? 0.51335 0.35904 0.50421 -0.06825 -0.05872 -0.04159 46  PRO A CG  
326  C CD  . PRO A 76  ? 0.56505 0.39997 0.55049 -0.07345 -0.07900 -0.02964 46  PRO A CD  
327  N N   . ARG A 77  ? 0.57186 0.40323 0.72453 -0.04459 -0.04090 -0.00471 47  ARG A N   
328  C CA  . ARG A 77  ? 0.65916 0.49145 0.85038 -0.03674 -0.02305 0.00664  47  ARG A CA  
329  C C   . ARG A 77  ? 0.49874 0.32501 0.67541 -0.03588 0.00530  0.00609  47  ARG A C   
330  O O   . ARG A 77  ? 0.62306 0.45086 0.80259 -0.03993 0.00746  0.00301  47  ARG A O   
331  C CB  . ARG A 77  ? 0.61997 0.47033 0.87764 -0.03637 -0.03275 0.01218  47  ARG A CB  
332  C CG  . ARG A 77  ? 0.50583 0.36795 0.81271 -0.02783 -0.00939 0.02190  47  ARG A CG  
333  C CD  . ARG A 77  ? 0.92161 0.81003 1.29917 -0.03323 -0.01578 0.02704  47  ARG A CD  
334  N NE  . ARG A 77  ? 1.29348 1.20339 1.72485 -0.02546 0.01080  0.03518  47  ARG A NE  
335  C CZ  . ARG A 77  ? 1.25295 1.19310 1.75232 -0.03262 0.01576  0.04170  47  ARG A CZ  
336  N NH1 . ARG A 77  ? 0.55226 0.49744 1.07188 -0.04884 -0.00775 0.04133  47  ARG A NH1 
337  N NH2 . ARG A 77  ? 1.31744 1.28325 1.86500 -0.02462 0.04532  0.04728  47  ARG A NH2 
338  N N   . LEU A 78  ? 0.55998 0.37455 0.71751 -0.03070 0.02438  0.00904  48  LEU A N   
339  C CA  . LEU A 78  ? 0.54679 0.35290 0.68046 -0.03106 0.04896  0.00837  48  LEU A CA  
340  C C   . LEU A 78  ? 0.47268 0.28819 0.64722 -0.02984 0.06684  0.01588  48  LEU A C   
341  O O   . LEU A 78  ? 0.61170 0.43707 0.82662 -0.02317 0.07822  0.02090  48  LEU A O   
342  C CB  . LEU A 78  ? 0.53772 0.32460 0.63833 -0.02721 0.06313  0.00716  48  LEU A CB  
343  C CG  . LEU A 78  ? 0.50126 0.27662 0.56903 -0.02865 0.08645  0.00530  48  LEU A CG  
344  C CD1 . LEU A 78  ? 0.68345 0.46155 0.71609 -0.03727 0.07719  0.00066  48  LEU A CD1 
345  C CD2 . LEU A 78  ? 0.52747 0.27853 0.56507 -0.02484 0.09930  0.00123  48  LEU A CD2 
346  N N   . LEU A 79  ? 0.51342 0.32657 0.67918 -0.03637 0.06943  0.01732  49  LEU A N   
347  C CA  . LEU A 79  ? 0.54168 0.35907 0.73601 -0.04082 0.08779  0.02801  49  LEU A CA  
348  C C   . LEU A 79  ? 0.57424 0.37730 0.72801 -0.04073 0.11512  0.03181  49  LEU A C   
349  O O   . LEU A 79  ? 0.65911 0.46807 0.82754 -0.03905 0.14200  0.03711  49  LEU A O   
350  C CB  . LEU A 79  ? 0.57744 0.39096 0.78389 -0.04963 0.07070  0.03012  49  LEU A CB  
351  C CG  . LEU A 79  ? 0.53287 0.35572 0.77266 -0.05236 0.04137  0.02359  49  LEU A CG  
352  C CD1 . LEU A 79  ? 0.61090 0.41824 0.85201 -0.05959 0.02648  0.02242  49  LEU A CD1 
353  C CD2 . LEU A 79  ? 0.46784 0.31434 0.76981 -0.05447 0.04228  0.03050  49  LEU A CD2 
354  N N   . ILE A 80  ? 0.60526 0.39207 0.70807 -0.04222 0.10833  0.02796  50  ILE A N   
355  C CA  . ILE A 80  ? 0.69781 0.46819 0.75355 -0.04402 0.12710  0.03164  50  ILE A CA  
356  C C   . ILE A 80  ? 0.64431 0.40616 0.65304 -0.04149 0.11921  0.01989  50  ILE A C   
357  O O   . ILE A 80  ? 0.74727 0.51615 0.75249 -0.04137 0.09703  0.01201  50  ILE A O   
358  C CB  . ILE A 80  ? 0.92750 0.68542 0.96955 -0.05067 0.12172  0.04252  50  ILE A CB  
359  C CG1 . ILE A 80  ? 0.72372 0.48715 0.81389 -0.05880 0.12775  0.05591  50  ILE A CG1 
360  C CG2 . ILE A 80  ? 0.81235 0.55148 0.79848 -0.05360 0.13756  0.04843  50  ILE A CG2 
361  C CD1 . ILE A 80  ? 0.88302 0.65661 0.98879 -0.06314 0.16257  0.06496  50  ILE A CD1 
362  N N   . TYR A 81  ? 0.66460 0.41218 0.63675 -0.04117 0.13838  0.01752  51  TYR A N   
363  C CA  . TYR A 81  ? 0.79289 0.52893 0.71696 -0.04366 0.13094  0.00740  51  TYR A CA  
364  C C   . TYR A 81  ? 0.88850 0.60738 0.76150 -0.04841 0.14154  0.01034  51  TYR A C   
365  O O   . TYR A 81  ? 0.85709 0.56831 0.72499 -0.04886 0.16349  0.01870  51  TYR A O   
366  C CB  . TYR A 81  ? 0.63786 0.36308 0.55875 -0.03997 0.13776  -0.00178 51  TYR A CB  
367  C CG  . TYR A 81  ? 0.72682 0.43264 0.62878 -0.03504 0.16653  -0.00518 51  TYR A CG  
368  C CD1 . TYR A 81  ? 0.83687 0.55189 0.78186 -0.02515 0.18770  -0.00211 51  TYR A CD1 
369  C CD2 . TYR A 81  ? 0.69873 0.37961 0.54097 -0.04030 0.17272  -0.01368 51  TYR A CD2 
370  C CE1 . TYR A 81  ? 0.66265 0.36407 0.59150 -0.01817 0.21833  -0.00893 51  TYR A CE1 
371  C CE2 . TYR A 81  ? 0.82572 0.48590 0.64400 -0.03479 0.20061  -0.02097 51  TYR A CE2 
372  C CZ  . TYR A 81  ? 0.70426 0.37549 0.56586 -0.02248 0.22539  -0.01936 51  TYR A CZ  
373  O OH  . TYR A 81  ? 0.75364 0.40830 0.59263 -0.01461 0.25741  -0.03013 51  TYR A OH  
374  N N   . GLY A 82  ? 0.83484 0.55026 0.66928 -0.05369 0.12556  0.00388  52  GLY A N   
375  C CA  . GLY A 82  ? 0.81180 0.51027 0.59202 -0.05924 0.12848  0.00595  52  GLY A CA  
376  C C   . GLY A 82  ? 0.81256 0.50630 0.58858 -0.05931 0.13027  0.02267  52  GLY A C   
377  O O   . GLY A 82  ? 1.01841 0.69584 0.77051 -0.06224 0.15383  0.03048  52  GLY A O   
378  N N   . ALA A 83  ? 0.81189 0.51788 0.60999 -0.05619 0.10632  0.02805  53  ALA A N   
379  C CA  . ALA A 83  ? 0.87499 0.56873 0.66978 -0.05610 0.10047  0.04580  53  ALA A CA  
380  C C   . ALA A 83  ? 0.94769 0.63687 0.77567 -0.05904 0.12130  0.05863  53  ALA A C   
381  O O   . ALA A 83  ? 0.81688 0.50924 0.68497 -0.05704 0.10875  0.06469  53  ALA A O   
382  C CB  . ALA A 83  ? 1.05085 0.72193 0.78046 -0.06210 0.10042  0.05464  53  ALA A CB  
383  N N   . SER A 84  ? 1.00261 0.68594 0.81685 -0.06418 0.15334  0.06117  54  SER A N   
384  C CA  . SER A 84  ? 0.75437 0.44042 0.60167 -0.07017 0.17627  0.07549  54  SER A CA  
385  C C   . SER A 84  ? 0.97869 0.68272 0.85827 -0.06705 0.20641  0.06655  54  SER A C   
386  O O   . SER A 84  ? 1.12379 0.84201 1.04780 -0.07203 0.22372  0.07679  54  SER A O   
387  C CB  . SER A 84  ? 0.77886 0.44064 0.57623 -0.08204 0.19054  0.09617  54  SER A CB  
388  O OG  . SER A 84  ? 1.18681 0.82856 0.96138 -0.08252 0.15894  0.10802  54  SER A OG  
389  N N   . TYR A 85  ? 1.15257 0.85631 1.01568 -0.05909 0.21205  0.04824  55  TYR A N   
390  C CA  . TYR A 85  ? 0.88126 0.59776 0.77602 -0.05137 0.23950  0.03891  55  TYR A CA  
391  C C   . TYR A 85  ? 0.87851 0.62106 0.84966 -0.04516 0.22640  0.03803  55  TYR A C   
392  O O   . TYR A 85  ? 0.73184 0.47614 0.71282 -0.04247 0.19659  0.03229  55  TYR A O   
393  C CB  . TYR A 85  ? 0.87698 0.57506 0.72989 -0.04406 0.24380  0.01916  55  TYR A CB  
394  C CG  . TYR A 85  ? 0.93397 0.60637 0.71141 -0.04987 0.26309  0.01618  55  TYR A CG  
395  C CD1 . TYR A 85  ? 1.19109 0.85993 0.95613 -0.04505 0.30269  0.00841  55  TYR A CD1 
396  C CD2 . TYR A 85  ? 0.80078 0.45450 0.51921 -0.05936 0.24116  0.01974  55  TYR A CD2 
397  C CE1 . TYR A 85  ? 1.29718 0.93982 0.98362 -0.05143 0.32081  0.00356  55  TYR A CE1 
398  C CE2 . TYR A 85  ? 0.86521 0.49344 0.50836 -0.06622 0.25455  0.01731  55  TYR A CE2 
399  C CZ  . TYR A 85  ? 1.19690 0.81729 0.81954 -0.06319 0.29483  0.00888  55  TYR A CZ  
400  O OH  . TYR A 85  ? 1.21823 0.81058 0.75658 -0.07104 0.30867  0.00439  55  TYR A OH  
401  N N   . MET A 86  ? 0.93903 0.70491 0.96385 -0.04403 0.24885  0.04350  56  MET A N   
402  C CA  . MET A 86  ? 0.79076 0.58369 0.89065 -0.03949 0.23416  0.04389  56  MET A CA  
403  C C   . MET A 86  ? 0.70561 0.50065 0.82213 -0.02275 0.22976  0.02845  56  MET A C   
404  O O   . MET A 86  ? 0.67496 0.45506 0.76107 -0.01341 0.24940  0.01715  56  MET A O   
405  C CB  . MET A 86  ? 0.80927 0.63263 0.96853 -0.04641 0.25805  0.05619  56  MET A CB  
406  C CG  . MET A 86  ? 0.66970 0.48490 0.81387 -0.06668 0.26210  0.07588  56  MET A CG  
407  S SD  . MET A 86  ? 1.80853 1.66463 2.03074 -0.08158 0.28995  0.09222  56  MET A SD  
408  C CE  . MET A 86  ? 1.50723 1.33224 1.68190 -0.10791 0.29207  0.11803  56  MET A CE  
409  N N   . ALA A 87  ? 0.65172 0.46052 0.81312 -0.01934 0.20197  0.02807  57  ALA A N   
410  C CA  . ALA A 87  ? 0.69167 0.49723 0.86751 -0.00509 0.18982  0.01824  57  ALA A CA  
411  C C   . ALA A 87  ? 0.86640 0.70264 1.11764 0.00753  0.20217  0.01935  57  ALA A C   
412  O O   . ALA A 87  ? 1.08325 0.94725 1.37417 0.00343  0.22590  0.02619  57  ALA A O   
413  C CB  . ALA A 87  ? 0.57234 0.37380 0.74301 -0.00981 0.15092  0.01794  57  ALA A CB  
414  N N   . THR A 88  ? 0.82693 0.65982 1.10063 0.02230  0.18494  0.01392  58  THR A N   
415  C CA  . THR A 88  ? 0.81972 0.68255 1.16962 0.03970  0.19237  0.01347  58  THR A CA  
416  C C   . THR A 88  ? 0.81275 0.71462 1.23187 0.03142  0.16967  0.02466  58  THR A C   
417  O O   . THR A 88  ? 0.86163 0.75536 1.26992 0.02267  0.13337  0.02826  58  THR A O   
418  C CB  . THR A 88  ? 0.82431 0.66122 1.17004 0.05980  0.17616  0.00582  58  THR A CB  
419  O OG1 . THR A 88  ? 1.00056 0.79773 1.28443 0.06623  0.19791  -0.00691 58  THR A OG1 
420  C CG2 . THR A 88  ? 0.92375 0.79432 1.35708 0.08238  0.17841  0.00552  58  THR A CG2 
421  N N   . GLY A 89  ? 0.65161 0.59742 1.14126 0.03263  0.19189  0.02893  59  GLY A N   
422  C CA  . GLY A 89  ? 0.61853 0.60429 1.18206 0.02267  0.16984  0.03881  59  GLY A CA  
423  C C   . GLY A 89  ? 0.74116 0.72282 1.28682 -0.00487 0.15917  0.04789  59  GLY A C   
424  O O   . GLY A 89  ? 0.81024 0.80904 1.39778 -0.01553 0.12870  0.05300  59  GLY A O   
425  N N   . ILE A 90  ? 0.74619 0.70204 1.22953 -0.01605 0.18062  0.04955  60  ILE A N   
426  C CA  . ILE A 90  ? 0.59834 0.54088 1.05975 -0.03895 0.16948  0.05838  60  ILE A CA  
427  C C   . ILE A 90  ? 0.62377 0.59278 1.12453 -0.05547 0.20105  0.07170  60  ILE A C   
428  O O   . ILE A 90  ? 0.71318 0.68562 1.19519 -0.05248 0.24131  0.07257  60  ILE A O   
429  C CB  . ILE A 90  ? 0.60259 0.50024 0.97316 -0.04077 0.16805  0.05452  60  ILE A CB  
430  C CG1 . ILE A 90  ? 0.63515 0.51252 0.96935 -0.02798 0.14232  0.04230  60  ILE A CG1 
431  C CG2 . ILE A 90  ? 0.51266 0.39367 0.86635 -0.05923 0.15218  0.06261  60  ILE A CG2 
432  C CD1 . ILE A 90  ? 0.47728 0.36361 0.84215 -0.02962 0.10331  0.04041  60  ILE A CD1 
433  N N   . PRO A 91  ? 0.52029 0.50663 1.07157 -0.07511 0.18521  0.08191  61  PRO A N   
434  C CA  . PRO A 91  ? 0.58181 0.59411 1.17270 -0.09658 0.21596  0.09786  61  PRO A CA  
435  C C   . PRO A 91  ? 0.69077 0.66389 1.20609 -0.11005 0.23750  0.10857  61  PRO A C   
436  O O   . PRO A 91  ? 0.83832 0.76607 1.27982 -0.10446 0.22130  0.10384  61  PRO A O   
437  C CB  . PRO A 91  ? 0.56297 0.58846 1.21345 -0.11732 0.18232  0.10488  61  PRO A CB  
438  C CG  . PRO A 91  ? 0.50324 0.52770 1.16420 -0.10047 0.13975  0.09008  61  PRO A CG  
439  C CD  . PRO A 91  ? 0.49735 0.48177 1.07414 -0.08023 0.13835  0.07851  61  PRO A CD  
440  N N   . ASP A 92  ? 1.03517 1.02954 1.57155 -0.12918 0.27445  0.12454  62  ASP A N   
441  C CA  . ASP A 92  ? 0.99004 0.94695 1.45375 -0.14526 0.29527  0.13977  62  ASP A CA  
442  C C   . ASP A 92  ? 0.96590 0.87721 1.40385 -0.16413 0.26017  0.15245  62  ASP A C   
443  O O   . ASP A 92  ? 1.13877 1.00817 1.50793 -0.17334 0.26615  0.16538  62  ASP A O   
444  C CB  . ASP A 92  ? 1.02841 1.02227 1.52083 -0.16449 0.34613  0.15565  62  ASP A CB  
445  C CG  . ASP A 92  ? 1.13445 1.17427 1.72623 -0.18834 0.34341  0.16817  62  ASP A CG  
446  O OD1 . ASP A 92  ? 1.02966 1.07298 1.66870 -0.18681 0.30046  0.16163  62  ASP A OD1 
447  O OD2 . ASP A 92  ? 1.45779 1.53006 2.06499 -0.20611 0.37576  0.18024  62  ASP A OD2 
448  N N   . ARG A 93  ? 0.88539 0.80089 1.37456 -0.16890 0.22208  0.14818  63  ARG A N   
449  C CA  . ARG A 93  ? 0.74970 0.61718 1.21624 -0.18352 0.18751  0.15548  63  ARG A CA  
450  C C   . ARG A 93  ? 0.89405 0.71425 1.28060 -0.16326 0.16569  0.14362  63  ARG A C   
451  O O   . ARG A 93  ? 1.06052 0.83454 1.39770 -0.17052 0.15692  0.15483  63  ARG A O   
452  C CB  . ARG A 93  ? 0.63092 0.51314 1.16574 -0.19112 0.15071  0.14761  63  ARG A CB  
453  C CG  . ARG A 93  ? 0.66652 0.61277 1.29527 -0.20377 0.16665  0.15273  63  ARG A CG  
454  C CD  . ARG A 93  ? 0.82052 0.77442 1.50843 -0.21673 0.12403  0.14684  63  ARG A CD  
455  N NE  . ARG A 93  ? 0.58487 0.51722 1.24702 -0.19496 0.08365  0.12409  63  ARG A NE  
456  C CZ  . ARG A 93  ? 0.63740 0.60497 1.33294 -0.17710 0.06866  0.10951  63  ARG A CZ  
457  N NH1 . ARG A 93  ? 0.61003 0.63717 1.37583 -0.17505 0.08889  0.11398  63  ARG A NH1 
458  N NH2 . ARG A 93  ? 0.61306 0.55690 1.27181 -0.16087 0.03354  0.09088  63  ARG A NH2 
459  N N   . PHE A 94  ? 0.71288 0.54479 1.08830 -0.13834 0.15563  0.12211  64  PHE A N   
460  C CA  . PHE A 94  ? 0.64878 0.44715 0.95597 -0.12087 0.13777  0.10985  64  PHE A CA  
461  C C   . PHE A 94  ? 0.82276 0.60479 1.06582 -0.11817 0.16588  0.11798  64  PHE A C   
462  O O   . PHE A 94  ? 1.00888 0.81370 1.25177 -0.11476 0.19892  0.11784  64  PHE A O   
463  C CB  . PHE A 94  ? 0.64665 0.46326 0.95899 -0.10054 0.12227  0.08784  64  PHE A CB  
464  C CG  . PHE A 94  ? 0.60723 0.43916 0.97296 -0.10297 0.09202  0.07913  64  PHE A CG  
465  C CD1 . PHE A 94  ? 0.52739 0.39899 0.96259 -0.10785 0.09769  0.08224  64  PHE A CD1 
466  C CD2 . PHE A 94  ? 0.59466 0.40359 0.94113 -0.09950 0.05728  0.06617  64  PHE A CD2 
467  C CE1 . PHE A 94  ? 0.51463 0.39957 0.99531 -0.11144 0.06512  0.07456  64  PHE A CE1 
468  C CE2 . PHE A 94  ? 0.52312 0.34279 0.90903 -0.10299 0.02840  0.05628  64  PHE A CE2 
469  C CZ  . PHE A 94  ? 0.51471 0.37089 0.96583 -0.11005 0.03023  0.06142  64  PHE A CZ  
470  N N   . SER A 95  ? 0.75658 0.49817 0.94464 -0.11834 0.15115  0.12366  65  SER A N   
471  C CA  . SER A 95  ? 1.10271 0.82419 1.22255 -0.11742 0.17026  0.13250  65  SER A CA  
472  C C   . SER A 95  ? 1.05832 0.75313 1.12805 -0.10232 0.14083  0.12223  65  SER A C   
473  O O   . SER A 95  ? 0.90711 0.58112 0.98415 -0.10005 0.11012  0.12112  65  SER A O   
474  C CB  . SER A 95  ? 0.74756 0.44701 0.85200 -0.14061 0.18728  0.16144  65  SER A CB  
475  O OG  . SER A 95  ? 1.00529 0.66778 1.11277 -0.14798 0.15523  0.17184  65  SER A OG  
476  N N   . GLY A 96  ? 0.94382 0.64058 0.96594 -0.09191 0.15011  0.11304  66  GLY A N   
477  C CA  . GLY A 96  ? 0.95652 0.63751 0.93488 -0.07953 0.12489  0.10371  66  GLY A CA  
478  C C   . GLY A 96  ? 0.93101 0.58074 0.84743 -0.08505 0.12661  0.12151  66  GLY A C   
479  O O   . GLY A 96  ? 0.77695 0.42083 0.66433 -0.09675 0.15575  0.13516  66  GLY A O   
480  N N   . SER A 97  ? 1.02153 0.65245 0.91726 -0.07559 0.09459  0.12078  67  SER A N   
481  C CA  . SER A 97  ? 0.97954 0.57798 0.81611 -0.07849 0.08654  0.13929  67  SER A CA  
482  C C   . SER A 97  ? 0.98880 0.58610 0.81480 -0.06001 0.04970  0.12718  67  SER A C   
483  O O   . SER A 97  ? 0.93126 0.54708 0.79908 -0.04706 0.03165  0.10789  67  SER A O   
484  C CB  . SER A 97  ? 0.85838 0.42056 0.69470 -0.09351 0.08627  0.16863  67  SER A CB  
485  O OG  . SER A 97  ? 0.98216 0.53460 0.86887 -0.08803 0.06061  0.16490  67  SER A OG  
486  N N   . GLY A 98  ? 0.97530 0.55388 0.74496 -0.05916 0.03903  0.13809  68  GLY A N   
487  C CA  . GLY A 98  ? 1.01364 0.59661 0.77646 -0.04136 0.00326  0.12875  68  GLY A CA  
488  C C   . GLY A 98  ? 1.13603 0.74469 0.86534 -0.04049 0.00486  0.11341  68  GLY A C   
489  O O   . GLY A 98  ? 1.00393 0.62886 0.72604 -0.04939 0.03168  0.10241  68  GLY A O   
490  N N   . SER A 99  ? 1.22420 0.83522 0.93573 -0.02922 -0.02692 0.11237  69  SER A N   
491  C CA  . SER A 99  ? 0.90614 0.54174 0.58795 -0.03101 -0.03247 0.09838  69  SER A CA  
492  C C   . SER A 99  ? 1.21057 0.86605 0.90927 -0.01301 -0.07300 0.09206  69  SER A C   
493  O O   . SER A 99  ? 1.35428 0.98803 1.06276 0.00070  -0.09792 0.10583  69  SER A O   
494  C CB  . SER A 99  ? 0.90818 0.51511 0.51338 -0.04759 -0.01918 0.11339  69  SER A CB  
495  O OG  . SER A 99  ? 1.05390 0.62180 0.62101 -0.04752 -0.03792 0.14146  69  SER A OG  
496  N N   . GLY A 100 ? 1.09096 0.78813 0.79632 -0.01324 -0.07977 0.07115  70  GLY A N   
497  C CA  . GLY A 100 ? 1.01991 0.75074 0.75087 0.00311  -0.11552 0.06201  70  GLY A CA  
498  C C   . GLY A 100 ? 0.91871 0.68539 0.72100 0.02191  -0.12109 0.04237  70  GLY A C   
499  O O   . GLY A 100 ? 0.75948 0.56903 0.58965 0.01732  -0.10890 0.02044  70  GLY A O   
500  N N   . THR A 101 ? 0.98486 0.73036 0.81269 0.04236  -0.13956 0.04981  71  THR A N   
501  C CA  . THR A 101 ? 0.88008 0.65293 0.77055 0.06314  -0.14535 0.02823  71  THR A CA  
502  C C   . THR A 101 ? 0.87050 0.60224 0.77666 0.06535  -0.13448 0.03352  71  THR A C   
503  O O   . THR A 101 ? 0.71089 0.46418 0.65885 0.07396  -0.12844 0.01167  71  THR A O   
504  C CB  . THR A 101 ? 0.93703 0.72798 0.85789 0.09242  -0.18334 0.02312  71  THR A CB  
505  O OG1 . THR A 101 ? 1.15144 0.88276 1.04170 0.09977  -0.20669 0.05216  71  THR A OG1 
506  C CG2 . THR A 101 ? 0.76114 0.60984 0.68411 0.08968  -0.19573 0.01240  71  THR A CG2 
507  N N   . ASP A 102 ? 1.10825 0.78251 0.98030 0.05529  -0.13190 0.06179  72  ASP A N   
508  C CA  . ASP A 102 ? 1.02639 0.66070 0.91483 0.05187  -0.12286 0.06971  72  ASP A CA  
509  C C   . ASP A 102 ? 1.01050 0.64191 0.88317 0.02502  -0.08586 0.07638  72  ASP A C   
510  O O   . ASP A 102 ? 0.94183 0.56078 0.76812 0.00810  -0.07079 0.09369  72  ASP A O   
511  C CB  . ASP A 102 ? 1.05312 0.62464 0.91966 0.05606  -0.14481 0.09934  72  ASP A CB  
512  C CG  . ASP A 102 ? 1.30773 0.87482 1.20156 0.08882  -0.18472 0.09132  72  ASP A CG  
513  O OD1 . ASP A 102 ? 1.27033 0.87129 1.21449 0.10880  -0.18981 0.06024  72  ASP A OD1 
514  O OD2 . ASP A 102 ? 1.57215 1.10170 1.43599 0.09567  -0.21121 0.11580  72  ASP A OD2 
515  N N   . PHE A 103 ? 0.99684 0.64057 0.90795 0.02260  -0.07228 0.06121  73  PHE A N   
516  C CA  . PHE A 103 ? 0.92343 0.56857 0.83427 0.00157  -0.04077 0.06589  73  PHE A CA  
517  C C   . PHE A 103 ? 0.94253 0.56613 0.89119 -0.00156 -0.04092 0.06733  73  PHE A C   
518  O O   . PHE A 103 ? 1.03620 0.66301 1.01735 0.01333  -0.05936 0.04896  73  PHE A O   
519  C CB  . PHE A 103 ? 0.82012 0.51165 0.73953 -0.00144 -0.02562 0.04365  73  PHE A CB  
520  C CG  . PHE A 103 ? 0.91627 0.62620 0.79817 -0.00466 -0.02373 0.04171  73  PHE A CG  
521  C CD1 . PHE A 103 ? 0.95310 0.65251 0.79709 -0.02071 -0.00066 0.05220  73  PHE A CD1 
522  C CD2 . PHE A 103 ? 0.94643 0.68607 0.83317 0.00799  -0.04487 0.02725  73  PHE A CD2 
523  C CE1 . PHE A 103 ? 0.83322 0.54355 0.63866 -0.02558 -0.00146 0.04793  73  PHE A CE1 
524  C CE2 . PHE A 103 ? 0.83368 0.59105 0.68844 0.00120  -0.04624 0.02525  73  PHE A CE2 
525  C CZ  . PHE A 103 ? 0.85182 0.59061 0.66280 -0.01637 -0.02588 0.03540  73  PHE A CZ  
526  N N   . THR A 104 ? 0.98349 0.58719 0.92867 -0.02176 -0.01983 0.08748  74  THR A N   
527  C CA  . THR A 104 ? 1.01062 0.59412 0.99361 -0.03080 -0.02050 0.09218  74  THR A CA  
528  C C   . THR A 104 ? 0.94313 0.55253 0.94880 -0.04781 0.00853  0.09195  74  THR A C   
529  O O   . THR A 104 ? 0.96421 0.58585 0.94656 -0.05742 0.03466  0.10123  74  THR A O   
530  C CB  . THR A 104 ? 1.04971 0.57932 1.01620 -0.04179 -0.02743 0.12291  74  THR A CB  
531  O OG1 . THR A 104 ? 1.23869 0.76363 1.16312 -0.05936 -0.00156 0.14728  74  THR A OG1 
532  C CG2 . THR A 104 ? 1.06366 0.56158 1.01477 -0.02049 -0.06262 0.12348  74  THR A CG2 
533  N N   . LEU A 105 ? 0.88552 0.50264 0.93696 -0.04994 0.00213  0.07972  75  LEU A N   
534  C CA  . LEU A 105 ? 0.79099 0.43271 0.87640 -0.06463 0.02279  0.08079  75  LEU A CA  
535  C C   . LEU A 105 ? 0.78817 0.40520 0.90792 -0.08271 0.01928  0.09652  75  LEU A C   
536  O O   . LEU A 105 ? 0.74766 0.34432 0.88930 -0.07962 -0.00682 0.08635  75  LEU A O   
537  C CB  . LEU A 105 ? 0.64141 0.31653 0.75073 -0.05521 0.01472  0.05428  75  LEU A CB  
538  C CG  . LEU A 105 ? 0.58730 0.28795 0.73806 -0.06696 0.02814  0.05510  75  LEU A CG  
539  C CD1 . LEU A 105 ? 0.66633 0.38470 0.80602 -0.07195 0.06062  0.06663  75  LEU A CD1 
540  C CD2 . LEU A 105 ? 0.55289 0.27731 0.71899 -0.05843 0.01270  0.03160  75  LEU A CD2 
541  N N   . THR A 106 ? 0.84967 0.46889 0.97400 -0.10280 0.04643  0.11982  76  THR A N   
542  C CA  . THR A 106 ? 0.82423 0.42205 0.98027 -0.12673 0.04734  0.14019  76  THR A CA  
543  C C   . THR A 106 ? 0.84225 0.48407 1.05762 -0.14034 0.06481  0.13757  76  THR A C   
544  O O   . THR A 106 ? 0.95625 0.63215 1.17452 -0.14361 0.09746  0.14285  76  THR A O   
545  C CB  . THR A 106 ? 0.90863 0.47734 1.02445 -0.14317 0.06636  0.17253  76  THR A CB  
546  O OG1 . THR A 106 ? 0.96788 0.50257 1.02640 -0.12633 0.04792  0.17427  76  THR A OG1 
547  C CG2 . THR A 106 ? 1.03945 0.57510 1.18279 -0.17072 0.06118  0.19600  76  THR A CG2 
548  N N   . ILE A 107 ? 0.84342 0.48427 1.10673 -0.14687 0.04143  0.12781  77  ILE A N   
549  C CA  . ILE A 107 ? 0.75573 0.43787 1.08443 -0.16177 0.04981  0.12725  77  ILE A CA  
550  C C   . ILE A 107 ? 0.75580 0.42105 1.11523 -0.19343 0.05356  0.15151  77  ILE A C   
551  O O   . ILE A 107 ? 0.77133 0.40026 1.12510 -0.19882 0.02385  0.14765  77  ILE A O   
552  C CB  . ILE A 107 ? 0.77949 0.47451 1.13652 -0.15106 0.01822  0.09991  77  ILE A CB  
553  C CG1 . ILE A 107 ? 0.63866 0.34054 0.95153 -0.12261 0.01173  0.07775  77  ILE A CG1 
554  C CG2 . ILE A 107 ? 0.74947 0.49482 1.17279 -0.16197 0.02510  0.09968  77  ILE A CG2 
555  C CD1 . ILE A 107 ? 0.59978 0.31074 0.92572 -0.11308 -0.01792 0.05146  77  ILE A CD1 
556  N N   . SER A 108 ? 0.35794 0.48586 1.30800 0.05076  -0.00577 0.15731  78  SER A N   
557  C CA  . SER A 108 ? 0.36151 0.50720 1.35474 0.04183  0.00557  0.16644  78  SER A CA  
558  C C   . SER A 108 ? 0.74418 0.85379 1.74899 0.04598  -0.00095 0.14938  78  SER A C   
559  O O   . SER A 108 ? 1.10996 1.20651 2.12601 0.04461  0.00193  0.16667  78  SER A O   
560  C CB  . SER A 108 ? 0.58730 0.77792 1.60776 0.02662  0.02043  0.14869  78  SER A CB  
561  O OG  . SER A 108 ? 0.98652 1.15719 2.01252 0.03427  0.01370  0.10803  78  SER A OG  
562  N N   . ARG A 109 ? 0.73887 0.83581 1.74718 0.04833  -0.00996 0.11635  79  ARG A N   
563  C CA  . ARG A 109 ? 0.44628 0.52040 1.47069 0.04791  -0.01818 0.09994  79  ARG A CA  
564  C C   . ARG A 109 ? 0.51549 0.56468 1.50855 0.05187  -0.04032 0.08519  79  ARG A C   
565  O O   . ARG A 109 ? 0.88995 0.93737 1.87387 0.05394  -0.05320 0.07079  79  ARG A O   
566  C CB  . ARG A 109 ? 0.38382 0.47107 1.45034 0.04358  -0.01302 0.07746  79  ARG A CB  
567  C CG  . ARG A 109 ? 0.67454 0.79615 1.77544 0.03408  0.01059  0.09007  79  ARG A CG  
568  C CD  . ARG A 109 ? 0.76045 0.90774 1.89405 0.02511  0.02252  0.05907  79  ARG A CD  
569  N NE  . ARG A 109 ? 0.65637 0.81890 1.77926 0.02411  0.02457  0.04307  79  ARG A NE  
570  C CZ  . ARG A 109 ? 1.08840 1.27569 2.23826 0.01291  0.04033  0.01082  79  ARG A CZ  
571  N NH1 . ARG A 109 ? 1.28253 1.48309 2.46660 0.00154  0.05486  -0.00871 79  ARG A NH1 
572  N NH2 . ARG A 109 ? 0.88651 1.08437 2.02983 0.01140  0.04400  -0.00504 79  ARG A NH2 
573  N N   . LEU A 110 ? 0.46564 0.49858 1.45075 0.05129  -0.04416 0.08897  80  LEU A N   
574  C CA  . LEU A 110 ? 0.56827 0.58364 1.53066 0.05274  -0.06467 0.07798  80  LEU A CA  
575  C C   . LEU A 110 ? 0.41566 0.42412 1.40502 0.04951  -0.08521 0.05954  80  LEU A C   
576  O O   . LEU A 110 ? 0.40981 0.42190 1.43603 0.04589  -0.07969 0.05330  80  LEU A O   
577  C CB  . LEU A 110 ? 0.40250 0.40655 1.36113 0.05187  -0.05754 0.08390  80  LEU A CB  
578  C CG  . LEU A 110 ? 0.39739 0.40542 1.33234 0.05456  -0.04289 0.10248  80  LEU A CG  
579  C CD1 . LEU A 110 ? 0.52238 0.51817 1.47159 0.05248  -0.03328 0.10110  80  LEU A CD1 
580  C CD2 . LEU A 110 ? 0.47413 0.48197 1.36708 0.05914  -0.05428 0.10223  80  LEU A CD2 
581  N N   . GLU A 111 ? 0.52835 0.52673 1.50314 0.04987  -0.11143 0.05349  81  GLU A N   
582  C CA  . GLU A 111 ? 0.44534 0.43546 1.44833 0.04529  -0.14085 0.04282  81  GLU A CA  
583  C C   . GLU A 111 ? 0.56161 0.53384 1.55318 0.04225  -0.16602 0.04570  81  GLU A C   
584  O O   . GLU A 111 ? 0.50090 0.46572 1.45697 0.04479  -0.16170 0.05273  81  GLU A O   
585  C CB  . GLU A 111 ? 0.67724 0.66981 1.68924 0.04536  -0.15676 0.03704  81  GLU A CB  
586  C CG  . GLU A 111 ? 0.87941 0.88334 1.93780 0.04374  -0.14679 0.02368  81  GLU A CG  
587  C CD  . GLU A 111 ? 0.89419 0.91479 1.95191 0.04694  -0.11491 0.02152  81  GLU A CD  
588  O OE1 . GLU A 111 ? 0.77409 0.80121 1.80753 0.04908  -0.09345 0.03435  81  GLU A OE1 
589  O OE2 . GLU A 111 ? 0.65243 0.68005 1.74189 0.04616  -0.11214 0.00710  81  GLU A OE2 
590  N N   . PRO A 112 ? 0.65666 0.62047 1.68278 0.03553  -0.19462 0.04056  82  PRO A N   
591  C CA  . PRO A 112 ? 0.67177 0.61352 1.69348 0.02925  -0.22710 0.04512  82  PRO A CA  
592  C C   . PRO A 112 ? 0.73237 0.66312 1.71673 0.02700  -0.25628 0.05830  82  PRO A C   
593  O O   . PRO A 112 ? 0.63307 0.54548 1.56689 0.00859  -0.26979 0.06074  82  PRO A O   
594  C CB  . PRO A 112 ? 0.50122 0.44312 1.56235 0.01576  -0.25799 0.03985  82  PRO A CB  
595  C CG  . PRO A 112 ? 0.48034 0.43975 1.58486 0.02412  -0.22870 0.02891  82  PRO A CG  
596  C CD  . PRO A 112 ? 0.46287 0.43415 1.53765 0.03174  -0.19936 0.03095  82  PRO A CD  
597  N N   . GLU A 113 ? 0.72537 0.66679 1.70144 0.03024  -0.25498 0.05989  83  GLU A N   
598  C CA  . GLU A 113 ? 0.72530 0.65594 1.66902 0.02787  -0.27710 0.07110  83  GLU A CA  
599  C C   . GLU A 113 ? 0.61612 0.54633 1.51156 0.03551  -0.24997 0.07339  83  GLU A C   
600  O O   . GLU A 113 ? 0.59750 0.51426 1.46081 0.03226  -0.26915 0.08333  83  GLU A O   
601  C CB  . GLU A 113 ? 0.72075 0.65946 1.68677 0.02948  -0.27819 0.06666  83  GLU A CB  
602  C CG  . GLU A 113 ? 0.85325 0.81331 1.82548 0.03980  -0.23251 0.05283  83  GLU A CG  
603  C CD  . GLU A 113 ? 1.07279 1.03877 2.08355 0.04013  -0.23314 0.04298  83  GLU A CD  
604  O OE1 . GLU A 113 ? 1.00693 0.95990 2.04166 0.03351  -0.26763 0.04819  83  GLU A OE1 
605  O OE2 . GLU A 113 ? 1.18516 1.16763 2.20898 0.04531  -0.20036 0.03075  83  GLU A OE2 
606  N N   . ASP A 114 ? 0.67092 0.61457 1.56173 0.04360  -0.20827 0.06725  84  ASP A N   
607  C CA  . ASP A 114 ? 0.66077 0.60689 1.51233 0.05008  -0.18249 0.07190  84  ASP A CA  
608  C C   . ASP A 114 ? 0.57330 0.49748 1.41131 0.04691  -0.18421 0.07343  84  ASP A C   
609  O O   . ASP A 114 ? 0.51135 0.43810 1.32657 0.05190  -0.15940 0.07611  84  ASP A O   
610  C CB  . ASP A 114 ? 0.48554 0.45369 1.34313 0.05621  -0.14328 0.07144  84  ASP A CB  
611  C CG  . ASP A 114 ? 0.69157 0.67551 1.56769 0.05761  -0.13809 0.06654  84  ASP A CG  
612  O OD1 . ASP A 114 ? 0.50452 0.48490 1.38101 0.05686  -0.15628 0.06307  84  ASP A OD1 
613  O OD2 . ASP A 114 ? 0.51236 0.51081 1.40977 0.05826  -0.11568 0.06588  84  ASP A OD2 
614  N N   . PHE A 115 ? 0.85137 0.75393 1.69178 0.03051  -0.20915 0.06845  85  PHE A N   
615  C CA  . PHE A 115 ? 0.94055 0.82796 1.72770 0.00467  -0.19847 0.05582  85  PHE A CA  
616  C C   . PHE A 115 ? 0.97521 0.85072 1.70216 -0.00512 -0.21439 0.06330  85  PHE A C   
617  O O   . PHE A 115 ? 0.83214 0.69686 1.52888 -0.02458 -0.25373 0.07149  85  PHE A O   
618  C CB  . PHE A 115 ? 1.07010 0.95020 1.84682 -0.02762 -0.21559 0.04227  85  PHE A CB  
619  C CG  . PHE A 115 ? 1.20769 1.07460 1.92362 -0.06522 -0.20517 0.02270  85  PHE A CG  
620  C CD1 . PHE A 115 ? 0.85835 0.72485 1.58785 -0.06856 -0.15951 -0.00033 85  PHE A CD1 
621  C CD2 . PHE A 115 ? 1.41212 1.26804 2.06264 -0.10095 -0.24048 0.02664  85  PHE A CD2 
622  C CE1 . PHE A 115 ? 0.94400 0.80083 1.62596 -0.10686 -0.14341 -0.02682 85  PHE A CE1 
623  C CE2 . PHE A 115 ? 1.39658 1.24388 1.98596 -0.14351 -0.22687 0.00362  85  PHE A CE2 
624  C CZ  . PHE A 115 ? 1.25194 1.10043 1.85855 -0.14658 -0.17538 -0.02710 85  PHE A CZ  
625  N N   . ALA A 116 ? 0.74037 0.61851 1.45252 0.00673  -0.18618 0.06348  86  ALA A N   
626  C CA  . ALA A 116 ? 0.53249 0.40092 1.18934 -0.00059 -0.19655 0.06946  86  ALA A CA  
627  C C   . ALA A 116 ? 0.51524 0.38934 1.16458 0.00776  -0.15790 0.06344  86  ALA A C   
628  O O   . ALA A 116 ? 0.49121 0.37740 1.18632 0.02229  -0.12775 0.06091  86  ALA A O   
629  C CB  . ALA A 116 ? 0.51440 0.38730 1.18546 0.01893  -0.22056 0.08842  86  ALA A CB  
630  N N   . VAL A 117 ? 0.53020 0.39569 1.12624 -0.00268 -0.16134 0.06368  87  VAL A N   
631  C CA  . VAL A 117 ? 0.51471 0.38743 1.10523 0.00527  -0.12948 0.06005  87  VAL A CA  
632  C C   . VAL A 117 ? 0.48138 0.36862 1.07707 0.03098  -0.13255 0.08096  87  VAL A C   
633  O O   . VAL A 117 ? 0.48932 0.36932 1.05924 0.02947  -0.15952 0.08967  87  VAL A O   
634  C CB  . VAL A 117 ? 0.55629 0.41287 1.08329 -0.02787 -0.12621 0.04113  87  VAL A CB  
635  C CG1 . VAL A 117 ? 0.53904 0.40553 1.07561 -0.01848 -0.09124 0.03471  87  VAL A CG1 
636  C CG2 . VAL A 117 ? 0.59861 0.44403 1.11319 -0.06339 -0.12316 0.01552  87  VAL A CG2 
637  N N   . TYR A 118 ? 0.44815 0.35704 1.08073 0.05135  -0.10574 0.08989  88  TYR A N   
638  C CA  . TYR A 118 ? 0.55328 0.48352 1.19121 0.06988  -0.10402 0.10805  88  TYR A CA  
639  C C   . TYR A 118 ? 0.56353 0.50026 1.17424 0.06890  -0.08826 0.11015  88  TYR A C   
640  O O   . TYR A 118 ? 0.54805 0.48708 1.17696 0.06657  -0.06678 0.10511  88  TYR A O   
641  C CB  . TYR A 118 ? 0.40837 0.37022 1.07585 0.07675  -0.08519 0.11614  88  TYR A CB  
642  C CG  . TYR A 118 ? 0.40067 0.36176 1.08715 0.07402  -0.09623 0.10988  88  TYR A CG  
643  C CD1 . TYR A 118 ? 0.41004 0.36005 1.12820 0.07002  -0.09540 0.10197  88  TYR A CD1 
644  C CD2 . TYR A 118 ? 0.44359 0.41482 1.12546 0.07491  -0.10550 0.10916  88  TYR A CD2 
645  C CE1 . TYR A 118 ? 0.52427 0.47549 1.26320 0.06734  -0.10645 0.09662  88  TYR A CE1 
646  C CE2 . TYR A 118 ? 0.39999 0.37147 1.10800 0.07222  -0.11457 0.10187  88  TYR A CE2 
647  C CZ  . TYR A 118 ? 0.51885 0.48130 1.25230 0.06857  -0.11643 0.09711  88  TYR A CZ  
648  O OH  . TYR A 118 ? 0.52520 0.48953 1.28749 0.06561  -0.12631 0.09022  88  TYR A OH  
649  N N   . TYR A 119 ? 0.49242 0.43266 1.06820 0.07045  -0.09785 0.11596  89  TYR A N   
650  C CA  . TYR A 119 ? 0.51799 0.46433 1.06175 0.06753  -0.08605 0.11679  89  TYR A CA  
651  C C   . TYR A 119 ? 0.42265 0.40289 0.97998 0.08113  -0.07656 0.13535  89  TYR A C   
652  O O   . TYR A 119 ? 0.36993 0.36763 0.94817 0.08703  -0.07793 0.14221  89  TYR A O   
653  C CB  . TYR A 119 ? 0.44370 0.36389 0.92395 0.05005  -0.10490 0.10618  89  TYR A CB  
654  C CG  . TYR A 119 ? 0.48290 0.37571 0.93312 0.02455  -0.11024 0.08722  89  TYR A CG  
655  C CD1 . TYR A 119 ? 0.54697 0.43729 0.97963 0.00973  -0.08808 0.07029  89  TYR A CD1 
656  C CD2 . TYR A 119 ? 0.50864 0.38136 0.95066 0.01093  -0.13658 0.08446  89  TYR A CD2 
657  C CE1 . TYR A 119 ? 0.54054 0.40979 0.94202 -0.02201 -0.08765 0.04645  89  TYR A CE1 
658  C CE2 . TYR A 119 ? 0.55207 0.40462 0.95822 -0.02133 -0.14149 0.06672  89  TYR A CE2 
659  C CZ  . TYR A 119 ? 0.56923 0.42047 0.95200 -0.03973 -0.11477 0.04542  89  TYR A CZ  
660  O OH  . TYR A 119 ? 0.73908 0.57400 1.08269 -0.07984 -0.11448 0.02141  89  TYR A OH  
661  N N   . CYS A 120 ? 0.53766 0.53021 1.07559 0.07947  -0.06447 0.13938  90  CYS A N   
662  C CA  . CYS A 120 ? 0.48799 0.51797 1.03234 0.08539  -0.05480 0.15832  90  CYS A CA  
663  C C   . CYS A 120 ? 0.59395 0.62186 1.08657 0.07813  -0.05545 0.15198  90  CYS A C   
664  O O   . CYS A 120 ? 0.69038 0.70173 1.16048 0.07075  -0.05158 0.14073  90  CYS A O   
665  C CB  . CYS A 120 ? 0.34776 0.40439 0.94097 0.09087  -0.03894 0.17882  90  CYS A CB  
666  S SG  . CYS A 120 ? 0.92234 1.03196 1.51839 0.08736  -0.03160 0.20946  90  CYS A SG  
667  N N   . GLN A 121 ? 0.35881 0.40438 0.83460 0.07726  -0.05724 0.15542  91  GLN A N   
668  C CA  . GLN A 121 ? 0.36785 0.40923 0.79526 0.06962  -0.05829 0.14764  91  GLN A CA  
669  C C   . GLN A 121 ? 0.42926 0.51495 0.85580 0.06671  -0.04543 0.15917  91  GLN A C   
670  O O   . GLN A 121 ? 0.39513 0.50732 0.84827 0.06622  -0.04052 0.16580  91  GLN A O   
671  C CB  . GLN A 121 ? 0.50825 0.51410 0.91157 0.06525  -0.07816 0.13256  91  GLN A CB  
672  C CG  . GLN A 121 ? 0.42243 0.41815 0.77797 0.05601  -0.08110 0.12521  91  GLN A CG  
673  C CD  . GLN A 121 ? 0.48466 0.50343 0.84972 0.05648  -0.07426 0.12261  91  GLN A CD  
674  O OE1 . GLN A 121 ? 0.38786 0.42689 0.79402 0.06118  -0.06899 0.12270  91  GLN A OE1 
675  N NE2 . GLN A 121 ? 0.53121 0.54813 0.85939 0.04828  -0.07121 0.11646  91  GLN A NE2 
676  N N   . GLN A 122 ? 0.49006 0.58624 0.88348 0.06022  -0.03881 0.15965  92  GLN A N   
677  C CA  . GLN A 122 ? 0.44189 0.58270 0.82502 0.05127  -0.02712 0.16935  92  GLN A CA  
678  C C   . GLN A 122 ? 0.59996 0.72867 0.93417 0.04303  -0.02653 0.15276  92  GLN A C   
679  O O   . GLN A 122 ? 0.53778 0.62930 0.84387 0.04298  -0.03426 0.14098  92  GLN A O   
680  C CB  . GLN A 122 ? 0.45017 0.63000 0.85554 0.04993  -0.01942 0.19647  92  GLN A CB  
681  C CG  . GLN A 122 ? 0.33928 0.50274 0.74101 0.05367  -0.01794 0.19338  92  GLN A CG  
682  C CD  . GLN A 122 ? 0.34356 0.52136 0.70313 0.04353  -0.01233 0.18832  92  GLN A CD  
683  O OE1 . GLN A 122 ? 0.47725 0.68877 0.81746 0.03268  -0.00824 0.19461  92  GLN A OE1 
684  N NE2 . GLN A 122 ? 0.35451 0.50858 0.69873 0.04313  -0.00957 0.17358  92  GLN A NE2 
685  N N   . TYR A 123 ? 0.66504 0.82705 0.98765 0.03151  -0.01571 0.15058  93  TYR A N   
686  C CA  . TYR A 123 ? 0.36430 0.52007 0.64550 0.02193  -0.01165 0.13472  93  TYR A CA  
687  C C   . TYR A 123 ? 0.35745 0.57019 0.62445 0.00544  0.00493  0.14451  93  TYR A C   
688  O O   . TYR A 123 ? 0.46227 0.71937 0.74968 -0.00442 0.01299  0.15811  93  TYR A O   
689  C CB  . TYR A 123 ? 0.56700 0.69657 0.85453 0.02078  -0.01547 0.11186  93  TYR A CB  
690  C CG  . TYR A 123 ? 0.61204 0.73508 0.86590 0.00977  -0.00956 0.09542  93  TYR A CG  
691  C CD1 . TYR A 123 ? 0.49783 0.57597 0.71719 0.01065  -0.02394 0.09076  93  TYR A CD1 
692  C CD2 . TYR A 123 ? 0.49688 0.65988 0.75176 -0.00623 0.01193  0.08312  93  TYR A CD2 
693  C CE1 . TYR A 123 ? 0.43734 0.50739 0.62774 -0.00021 -0.01887 0.07727  93  TYR A CE1 
694  C CE2 . TYR A 123 ? 0.57741 0.73389 0.80604 -0.01714 0.01985  0.06559  93  TYR A CE2 
695  C CZ  . TYR A 123 ? 0.52024 0.62856 0.71857 -0.01208 0.00348  0.06420  93  TYR A CZ  
696  O OH  . TYR A 123 ? 0.43401 0.53376 0.60795 -0.02367 0.01100  0.04826  93  TYR A OH  
697  N N   . GLY A 124 ? 0.36471 0.57789 0.59324 -0.00182 0.00902  0.13843  94  GLY A N   
698  C CA  . GLY A 124 ? 0.42226 0.69040 0.63223 -0.02080 0.02262  0.14740  94  GLY A CA  
699  C C   . GLY A 124 ? 0.52723 0.79149 0.70420 -0.02283 0.02319  0.14651  94  GLY A C   
700  O O   . GLY A 124 ? 0.38042 0.61880 0.52210 -0.02762 0.02623  0.12411  94  GLY A O   
701  N N   . SER A 125 ? 0.55140 0.84135 0.74683 -0.01994 0.02027  0.17097  95  SER A N   
702  C CA  . SER A 125 ? 0.36291 0.64804 0.53868 -0.02061 0.02226  0.16686  95  SER A CA  
703  C C   . SER A 125 ? 0.44981 0.67265 0.61381 -0.00919 0.01707  0.14546  95  SER A C   
704  O O   . SER A 125 ? 0.38743 0.59542 0.51930 -0.01534 0.02143  0.13069  95  SER A O   
705  C CB  . SER A 125 ? 0.42535 0.75616 0.64418 -0.02001 0.01970  0.19915  95  SER A CB  
706  O OG  . SER A 125 ? 0.72312 1.11609 0.94599 -0.03845 0.01987  0.22519  95  SER A OG  
707  N N   . SER A 126 ? 0.56198 0.75084 0.74770 0.00255  0.00811  0.14306  96  SER A N   
708  C CA  . SER A 126 ? 0.39534 0.52875 0.56505 0.00552  0.00116  0.12423  96  SER A CA  
709  C C   . SER A 126 ? 0.46810 0.57166 0.65375 0.01356  -0.01181 0.12260  96  SER A C   
710  O O   . SER A 126 ? 0.52601 0.65023 0.73447 0.01728  -0.01216 0.13119  96  SER A O   
711  C CB  . SER A 126 ? 0.48391 0.61918 0.68433 0.00896  0.00781  0.12511  96  SER A CB  
712  O OG  . SER A 126 ? 0.38163 0.54433 0.64725 0.02130  0.00770  0.14832  96  SER A OG  
713  N N   . LEU A 127 ? 0.53110 0.58877 0.70445 0.01209  -0.02187 0.11011  97  LEU A N   
714  C CA  . LEU A 127 ? 0.49243 0.52044 0.68206 0.01776  -0.03788 0.10944  97  LEU A CA  
715  C C   . LEU A 127 ? 0.43418 0.44469 0.64126 0.01757  -0.03768 0.10489  97  LEU A C   
716  O O   . LEU A 127 ? 0.46447 0.44268 0.63458 0.00170  -0.04151 0.08887  97  LEU A O   
717  C CB  . LEU A 127 ? 0.54068 0.52740 0.69255 0.00818  -0.05629 0.09940  97  LEU A CB  
718  C CG  . LEU A 127 ? 0.50247 0.47034 0.68473 0.01563  -0.07476 0.10239  97  LEU A CG  
719  C CD1 . LEU A 127 ? 0.48140 0.41783 0.64228 0.00697  -0.09173 0.09739  97  LEU A CD1 
720  C CD2 . LEU A 127 ? 0.64193 0.58436 0.83720 0.01576  -0.08924 0.10375  97  LEU A CD2 
721  N N   . THR A 128 ? 0.51474 0.54750 0.77788 0.03086  -0.03174 0.11759  98  THR A N   
722  C CA  . THR A 128 ? 0.41776 0.43936 0.71309 0.03130  -0.02564 0.11113  98  THR A CA  
723  C C   . THR A 128 ? 0.49354 0.50342 0.82146 0.03984  -0.03643 0.11638  98  THR A C   
724  O O   . THR A 128 ? 0.47054 0.50171 0.82510 0.05124  -0.03994 0.13283  98  THR A O   
725  C CB  . THR A 128 ? 0.39708 0.45640 0.74713 0.03962  -0.00756 0.12370  98  THR A CB  
726  O OG1 . THR A 128 ? 0.76768 0.84324 1.09193 0.03205  0.00137  0.12009  98  THR A OG1 
727  C CG2 . THR A 128 ? 0.63807 0.68276 1.03207 0.03805  0.00424  0.10912  98  THR A CG2 
728  N N   . PHE A 129 ? 0.43721 0.41568 0.76090 0.02995  -0.04001 0.09989  99  PHE A N   
729  C CA  . PHE A 129 ? 0.48114 0.44875 0.83872 0.03577  -0.04852 0.10213  99  PHE A CA  
730  C C   . PHE A 129 ? 0.58449 0.56406 1.00313 0.04151  -0.02897 0.10055  99  PHE A C   
731  O O   . PHE A 129 ? 0.44605 0.43112 0.87779 0.03543  -0.01015 0.08899  99  PHE A O   
732  C CB  . PHE A 129 ? 0.50858 0.43539 0.82219 0.01592  -0.06883 0.08678  99  PHE A CB  
733  C CG  . PHE A 129 ? 0.52402 0.43760 0.81733 0.01801  -0.09557 0.09684  99  PHE A CG  
734  C CD1 . PHE A 129 ? 0.54555 0.46170 0.88019 0.03147  -0.10771 0.10622  99  PHE A CD1 
735  C CD2 . PHE A 129 ? 0.49918 0.39734 0.74100 0.00590  -0.10760 0.09563  99  PHE A CD2 
736  C CE1 . PHE A 129 ? 0.54656 0.45135 0.88099 0.03398  -0.13036 0.11213  99  PHE A CE1 
737  C CE2 . PHE A 129 ? 0.50536 0.38976 0.74650 0.00874  -0.13181 0.10456  99  PHE A CE2 
738  C CZ  . PHE A 129 ? 0.61701 0.50528 0.90929 0.02336  -0.14272 0.11177  99  PHE A CZ  
739  N N   . GLY A 130 ? 0.53781 0.52125 1.00223 0.05294  -0.03247 0.11094  100 GLY A N   
740  C CA  . GLY A 130 ? 0.40667 0.39819 0.93921 0.05911  -0.01548 0.11154  100 GLY A CA  
741  C C   . GLY A 130 ? 0.43839 0.39953 0.96663 0.04019  -0.00758 0.07908  100 GLY A C   
742  O O   . GLY A 130 ? 0.46965 0.40443 0.93455 0.01863  -0.01905 0.05969  100 GLY A O   
743  N N   . GLY A 131 ? 0.44891 0.41541 1.04902 0.04455  0.01249  0.07382  101 GLY A N   
744  C CA  . GLY A 131 ? 0.46734 0.40965 1.07189 0.02208  0.02699  0.03698  101 GLY A CA  
745  C C   . GLY A 131 ? 0.68610 0.60878 1.27028 0.01388  0.00943  0.03225  101 GLY A C   
746  O O   . GLY A 131 ? 0.59629 0.49632 1.13661 -0.01627 0.00804  0.00329  101 GLY A O   
747  N N   . GLY A 132 ? 0.60947 0.54313 1.22380 0.03599  -0.00437 0.06002  102 GLY A N   
748  C CA  . GLY A 132 ? 0.46424 0.38304 1.06941 0.03107  -0.02237 0.05757  102 GLY A CA  
749  C C   . GLY A 132 ? 0.46513 0.38771 1.14586 0.03874  -0.00617 0.05596  102 GLY A C   
750  O O   . GLY A 132 ? 0.59777 0.52129 1.32952 0.03493  0.02133  0.04033  102 GLY A O   
751  N N   . THR A 133 ? 0.69401 0.61870 1.38994 0.04912  -0.02183 0.07052  103 THR A N   
752  C CA  . THR A 133 ? 0.43783 0.36435 1.20139 0.05532  -0.00956 0.07067  103 THR A CA  
753  C C   . THR A 133 ? 0.45899 0.36786 1.19775 0.04032  -0.02738 0.05520  103 THR A C   
754  O O   . THR A 133 ? 0.61970 0.53107 1.33787 0.04729  -0.05272 0.06945  103 THR A O   
755  C CB  . THR A 133 ? 0.40828 0.36664 1.19970 0.07244  -0.00923 0.10407  103 THR A CB  
756  O OG1 . THR A 133 ? 0.40004 0.37921 1.20190 0.07518  0.00453  0.11972  103 THR A OG1 
757  C CG2 . THR A 133 ? 0.41163 0.37421 1.24603 0.06855  0.00057  0.10294  103 THR A CG2 
758  N N   . LYS A 134 ? 0.48932 0.38269 1.23557 0.01728  -0.01339 0.02438  104 LYS A N   
759  C CA  . LYS A 134 ? 0.61600 0.49580 1.33744 -0.00322 -0.03173 0.00994  104 LYS A CA  
760  C C   . LYS A 134 ? 0.53944 0.42688 1.32738 0.01358  -0.02704 0.01965  104 LYS A C   
761  O O   . LYS A 134 ? 0.58805 0.47479 1.43456 0.01240  0.00130  0.00635  104 LYS A O   
762  C CB  . LYS A 134 ? 0.57804 0.44231 1.26976 -0.04441 -0.01684 -0.03074 104 LYS A CB  
763  C CG  . LYS A 134 ? 1.06543 0.91946 1.72167 -0.07400 -0.04044 -0.04307 104 LYS A CG  
764  C CD  . LYS A 134 ? 1.29677 1.14023 1.90766 -0.12606 -0.02552 -0.08498 104 LYS A CD  
765  C CE  . LYS A 134 ? 1.19580 1.03384 1.76535 -0.16147 -0.05498 -0.09151 104 LYS A CE  
766  N NZ  . LYS A 134 ? 1.07271 0.90518 1.58606 -0.22326 -0.04055 -0.13354 104 LYS A NZ  
767  N N   . LEU A 135 ? 0.56725 0.46192 1.35277 0.02797  -0.05293 0.04082  105 LEU A N   
768  C CA  . LEU A 135 ? 0.52225 0.42555 1.36458 0.04101  -0.05032 0.04936  105 LEU A CA  
769  C C   . LEU A 135 ? 0.49389 0.38465 1.32358 0.01833  -0.06602 0.02901  105 LEU A C   
770  O O   . LEU A 135 ? 0.66991 0.55545 1.45640 0.00785  -0.09900 0.03110  105 LEU A O   
771  C CB  . LEU A 135 ? 0.43138 0.36142 1.26558 0.05791  -0.06288 0.07504  105 LEU A CB  
772  C CG  . LEU A 135 ? 0.54162 0.49116 1.40237 0.05832  -0.05652 0.08038  105 LEU A CG  
773  C CD1 . LEU A 135 ? 0.42001 0.37928 1.31827 0.05692  -0.02736 0.08591  105 LEU A CD1 
774  C CD2 . LEU A 135 ? 0.56669 0.53728 1.40180 0.06274  -0.06331 0.09480  105 LEU A CD2 
775  N N   . GLU A 136 ? 0.50027 0.38706 1.37282 0.00918  -0.04392 0.01103  106 GLU A N   
776  C CA  . GLU A 136 ? 0.64329 0.52181 1.50573 -0.01732 -0.05508 -0.01078 106 GLU A CA  
777  C C   . GLU A 136 ? 0.57674 0.46481 1.49701 -0.00085 -0.05590 -0.00089 106 GLU A C   
778  O O   . GLU A 136 ? 0.58926 0.48519 1.56803 0.02050  -0.03223 0.01145  106 GLU A O   
779  C CB  . GLU A 136 ? 0.79086 0.65816 1.65465 -0.04941 -0.02460 -0.04899 106 GLU A CB  
780  C CG  . GLU A 136 ? 0.87582 0.73607 1.69048 -0.06818 -0.01468 -0.06416 106 GLU A CG  
781  C CD  . GLU A 136 ? 1.16559 1.01736 1.97702 -0.11027 0.01725  -0.11170 106 GLU A CD  
782  O OE1 . GLU A 136 ? 1.28753 1.13716 2.08239 -0.14238 0.01108  -0.13290 106 GLU A OE1 
783  O OE2 . GLU A 136 ? 1.25282 1.10243 2.08210 -0.11391 0.05010  -0.13035 106 GLU A OE2 
784  N N   . ILE A 137 ? 0.57152 0.46003 1.47756 -0.01322 -0.08526 -0.00397 107 ILE A N   
785  C CA  . ILE A 137 ? 0.68225 0.58138 1.64015 -0.00034 -0.08929 0.00249  107 ILE A CA  
786  C C   . ILE A 137 ? 0.71167 0.60445 1.67663 -0.03000 -0.08495 -0.02504 107 ILE A C   
787  O O   . ILE A 137 ? 0.96906 0.85884 1.89141 -0.05852 -0.11429 -0.03430 107 ILE A O   
788  C CB  . ILE A 137 ? 0.85465 0.76400 1.80807 0.01184  -0.12669 0.02068  107 ILE A CB  
789  C CG1 . ILE A 137 ? 0.53259 0.44915 1.47369 0.03477  -0.12734 0.04156  107 ILE A CG1 
790  C CG2 . ILE A 137 ? 0.81139 0.73458 1.82442 0.02386  -0.12567 0.02287  107 ILE A CG2 
791  C CD1 . ILE A 137 ? 0.44062 0.38309 1.38925 0.04549  -0.09150 0.05221  107 ILE A CD1 
792  N N   . LYS A 138 ? 1.74623 0.89959 0.89501 -0.30092 0.27536  -0.12834 108 LYS A N   
793  C CA  . LYS A 138 ? 1.83613 1.00968 1.03876 -0.33147 0.27277  -0.14230 108 LYS A CA  
794  C C   . LYS A 138 ? 1.52293 0.72946 0.81585 -0.36430 0.31261  -0.14571 108 LYS A C   
795  O O   . LYS A 138 ? 1.78297 0.92549 1.05403 -0.37994 0.36311  -0.13939 108 LYS A O   
796  C CB  . LYS A 138 ? 1.65370 0.75826 0.79191 -0.32822 0.27664  -0.13549 108 LYS A CB  
797  C CG  . LYS A 138 ? 1.90694 1.02122 1.00899 -0.29045 0.22803  -0.12089 108 LYS A CG  
798  C CD  . LYS A 138 ? 1.83321 0.88628 0.88374 -0.28891 0.23035  -0.11378 108 LYS A CD  
799  C CE  . LYS A 138 ? 1.96235 1.03580 1.00671 -0.25264 0.18073  -0.10128 108 LYS A CE  
800  N NZ  . LYS A 138 ? 1.91865 0.93333 0.91365 -0.25067 0.18069  -0.09552 108 LYS A NZ  
801  N N   . SER A 153 ? 1.37261 1.25647 1.16097 0.11320  0.04123  -0.05831 123 SER A N   
802  C CA  . SER A 153 ? 1.17483 1.11974 1.02208 0.08307  0.05926  -0.05536 123 SER A CA  
803  C C   . SER A 153 ? 0.86661 0.87951 0.79504 0.08749  0.03819  -0.05244 123 SER A C   
804  O O   . SER A 153 ? 0.75802 0.82854 0.74343 0.06921  0.02713  -0.04746 123 SER A O   
805  C CB  . SER A 153 ? 1.27820 1.19626 1.09804 0.07189  0.10487  -0.06134 123 SER A CB  
806  O OG  . SER A 153 ? 1.29212 1.18072 1.08894 0.09736  0.11430  -0.06635 123 SER A OG  
807  N N   . GLN A 154 ? 0.89273 0.89439 0.82205 0.11384  0.03090  -0.05624 124 GLN A N   
808  C CA  . GLN A 154 ? 0.70235 0.76271 0.70587 0.12109  0.00833  -0.05361 124 GLN A CA  
809  C C   . GLN A 154 ? 0.64790 0.72260 0.67666 0.13306  -0.03068 -0.04571 124 GLN A C   
810  O O   . GLN A 154 ? 0.37181 0.50023 0.46458 0.13051  -0.04986 -0.03902 124 GLN A O   
811  C CB  . GLN A 154 ? 0.55066 0.59410 0.54831 0.14513  0.01565  -0.06183 124 GLN A CB  
812  C CG  . GLN A 154 ? 0.80043 0.83912 0.78918 0.13260  0.05942  -0.06922 124 GLN A CG  
813  C CD  . GLN A 154 ? 0.73766 0.77367 0.73517 0.15581  0.06558  -0.07703 124 GLN A CD  
814  O OE1 . GLN A 154 ? 0.60000 0.64915 0.62327 0.17901  0.03269  -0.07692 124 GLN A OE1 
815  N NE2 . GLN A 154 ? 0.58875 0.60635 0.56652 0.14972  0.10968  -0.08428 124 GLN A NE2 
816  N N   . VAL A 155 ? 0.67181 0.69725 0.65315 0.14668  -0.04191 -0.04702 125 VAL A N   
817  C CA  . VAL A 155 ? 0.40375 0.44030 0.41305 0.15492  -0.07294 -0.04066 125 VAL A CA  
818  C C   . VAL A 155 ? 0.38822 0.44120 0.39631 0.12967  -0.06904 -0.03238 125 VAL A C   
819  O O   . VAL A 155 ? 0.51859 0.53861 0.47482 0.11804  -0.05131 -0.03607 125 VAL A O   
820  C CB  . VAL A 155 ? 0.43439 0.41106 0.40302 0.18428  -0.08994 -0.05039 125 VAL A CB  
821  C CG1 . VAL A 155 ? 0.53927 0.53156 0.55211 0.19145  -0.11871 -0.04553 125 VAL A CG1 
822  C CG2 . VAL A 155 ? 0.60068 0.55355 0.55945 0.21206  -0.09431 -0.06069 125 VAL A CG2 
823  N N   . GLN A 156 ? 0.34417 0.44383 0.40500 0.12236  -0.08508 -0.02100 126 GLN A N   
824  C CA  . GLN A 156 ? 0.33236 0.45038 0.39214 0.10036  -0.08240 -0.01272 126 GLN A CA  
825  C C   . GLN A 156 ? 0.41009 0.53022 0.48963 0.10862  -0.10123 -0.00395 126 GLN A C   
826  O O   . GLN A 156 ? 0.33860 0.48208 0.46611 0.11999  -0.11700 0.00303  126 GLN A O   
827  C CB  . GLN A 156 ? 0.31139 0.48276 0.41086 0.08159  -0.07958 -0.00726 126 GLN A CB  
828  C CG  . GLN A 156 ? 0.30739 0.49420 0.39982 0.06132  -0.07933 -0.00075 126 GLN A CG  
829  C CD  . GLN A 156 ? 0.50681 0.74334 0.64032 0.04803  -0.08454 0.00185  126 GLN A CD  
830  O OE1 . GLN A 156 ? 0.65944 0.92401 0.83496 0.05501  -0.09153 0.00114  126 GLN A OE1 
831  N NE2 . GLN A 156 ? 0.36991 0.61597 0.49158 0.03064  -0.08401 0.00291  126 GLN A NE2 
832  N N   . LEU A 157 ? 0.32672 0.42140 0.37177 0.10265  -0.09759 -0.00467 127 LEU A N   
833  C CA  . LEU A 157 ? 0.30799 0.40449 0.37207 0.10700  -0.10850 0.00297  127 LEU A CA  
834  C C   . LEU A 157 ? 0.33964 0.46175 0.39964 0.08580  -0.10170 0.01416  127 LEU A C   
835  O O   . LEU A 157 ? 0.48815 0.59801 0.50722 0.07070  -0.09014 0.00940  127 LEU A O   
836  C CB  . LEU A 157 ? 0.33079 0.37803 0.36155 0.11918  -0.11148 -0.00883 127 LEU A CB  
837  C CG  . LEU A 157 ? 0.35003 0.35925 0.37097 0.14468  -0.12257 -0.02362 127 LEU A CG  
838  C CD1 . LEU A 157 ? 0.37649 0.33568 0.36495 0.15787  -0.13051 -0.03722 127 LEU A CD1 
839  C CD2 . LEU A 157 ? 0.54191 0.57367 0.62432 0.15924  -0.13798 -0.02011 127 LEU A CD2 
840  N N   . GLN A 158 ? 0.28067 0.43375 0.37942 0.08607  -0.10933 0.02872  128 GLN A N   
841  C CA  . GLN A 158 ? 0.28330 0.45639 0.37296 0.07091  -0.10610 0.03998  128 GLN A CA  
842  C C   . GLN A 158 ? 0.31615 0.48037 0.41321 0.07651  -0.10516 0.05083  128 GLN A C   
843  O O   . GLN A 158 ? 0.37663 0.54659 0.51567 0.08913  -0.11095 0.05898  128 GLN A O   
844  C CB  . GLN A 158 ? 0.27172 0.48378 0.39147 0.06740  -0.11457 0.04834  128 GLN A CB  
845  C CG  . GLN A 158 ? 0.27101 0.49668 0.39750 0.06230  -0.11286 0.03615  128 GLN A CG  
846  C CD  . GLN A 158 ? 0.38063 0.64654 0.54014 0.05834  -0.12394 0.04090  128 GLN A CD  
847  O OE1 . GLN A 158 ? 0.66798 0.94672 0.82048 0.05149  -0.13062 0.04872  128 GLN A OE1 
848  N NE2 . GLN A 158 ? 0.75327 1.03648 0.94663 0.06487  -0.12760 0.03483  128 GLN A NE2 
849  N N   . GLN A 159 ? 0.50411 0.65377 0.56344 0.06695  -0.09608 0.05044  129 GLN A N   
850  C CA  . GLN A 159 ? 0.43551 0.57362 0.49884 0.07137  -0.08936 0.05879  129 GLN A CA  
851  C C   . GLN A 159 ? 0.42102 0.57647 0.47888 0.06619  -0.08611 0.07752  129 GLN A C   
852  O O   . GLN A 159 ? 0.52113 0.69301 0.55906 0.05719  -0.09179 0.07975  129 GLN A O   
853  C CB  . GLN A 159 ? 0.45116 0.55975 0.47378 0.06664  -0.08113 0.04672  129 GLN A CB  
854  C CG  . GLN A 159 ? 0.59077 0.67130 0.60403 0.07425  -0.08587 0.02774  129 GLN A CG  
855  C CD  . GLN A 159 ? 0.57058 0.61828 0.54120 0.07085  -0.08011 0.01554  129 GLN A CD  
856  O OE1 . GLN A 159 ? 0.57075 0.58697 0.51747 0.07678  -0.08401 -0.00005 129 GLN A OE1 
857  N NE2 . GLN A 159 ? 0.42823 0.47890 0.38418 0.06303  -0.07102 0.02240  129 GLN A NE2 
858  N N   . SER A 160 ? 0.32087 0.46898 0.39683 0.07330  -0.07662 0.08996  130 SER A N   
859  C CA  . SER A 160 ? 0.34407 0.49666 0.40471 0.07211  -0.06970 0.10995  130 SER A CA  
860  C C   . SER A 160 ? 0.41859 0.55085 0.48536 0.07671  -0.04880 0.11774  130 SER A C   
861  O O   . SER A 160 ? 0.34119 0.46474 0.44965 0.08357  -0.04439 0.10970  130 SER A O   
862  C CB  . SER A 160 ? 0.33623 0.50819 0.43007 0.07902  -0.07995 0.12442  130 SER A CB  
863  O OG  . SER A 160 ? 0.31207 0.48400 0.46474 0.08987  -0.07979 0.12556  130 SER A OG  
864  N N   . GLY A 161 ? 0.47069 0.59360 0.49636 0.07428  -0.03621 0.13179  131 GLY A N   
865  C CA  . GLY A 161 ? 0.42821 0.53064 0.45552 0.07795  -0.01028 0.14050  131 GLY A CA  
866  C C   . GLY A 161 ? 0.60462 0.69037 0.56295 0.07284  0.00074  0.14224  131 GLY A C   
867  O O   . GLY A 161 ? 0.87173 0.96133 0.78499 0.06536  -0.01434 0.13217  131 GLY A O   
868  N N   . PRO A 162 ? 0.50467 0.57029 0.45585 0.07715  0.02865  0.15422  132 PRO A N   
869  C CA  . PRO A 162 ? 0.59421 0.63983 0.47463 0.07518  0.04072  0.15619  132 PRO A CA  
870  C C   . PRO A 162 ? 0.75756 0.79816 0.62512 0.06844  0.03889  0.13236  132 PRO A C   
871  O O   . PRO A 162 ? 0.74125 0.78455 0.65704 0.06849  0.03832  0.11709  132 PRO A O   
872  C CB  . PRO A 162 ? 0.57460 0.59799 0.46054 0.08300  0.07715  0.17639  132 PRO A CB  
873  C CG  . PRO A 162 ? 0.74447 0.77790 0.72118 0.08534  0.08554  0.17330  132 PRO A CG  
874  C CD  . PRO A 162 ? 0.66613 0.72500 0.67616 0.08436  0.05254  0.16631  132 PRO A CD  
875  N N   . GLY A 163 ? 0.81534 0.84510 0.61476 0.06438  0.03524  0.12809  133 GLY A N   
876  C CA  . GLY A 163 ? 0.95101 0.97279 0.72977 0.05761  0.03177  0.10611  133 GLY A CA  
877  C C   . GLY A 163 ? 0.90827 0.90601 0.65277 0.06122  0.05695  0.10648  133 GLY A C   
878  O O   . GLY A 163 ? 0.81387 0.80177 0.53423 0.05662  0.05406  0.08845  133 GLY A O   
879  N N   . LEU A 164 ? 0.89072 0.87589 0.63107 0.06993  0.08373  0.12712  134 LEU A N   
880  C CA  . LEU A 164 ? 0.80312 0.76317 0.51129 0.07499  0.11460  0.12952  134 LEU A CA  
881  C C   . LEU A 164 ? 0.75485 0.70962 0.52257 0.08153  0.15017  0.14327  134 LEU A C   
882  O O   . LEU A 164 ? 0.70521 0.65559 0.47614 0.08698  0.16194  0.16687  134 LEU A O   
883  C CB  . LEU A 164 ? 0.78720 0.72593 0.40475 0.08067  0.11565  0.14221  134 LEU A CB  
884  C CG  . LEU A 164 ? 0.93603 0.84381 0.50570 0.08812  0.14896  0.14514  134 LEU A CG  
885  C CD1 . LEU A 164 ? 0.91671 0.82491 0.48836 0.08174  0.14529  0.11832  134 LEU A CD1 
886  C CD2 . LEU A 164 ? 0.88579 0.76705 0.35848 0.09809  0.14472  0.15821  134 LEU A CD2 
887  N N   . VAL A 165 ? 0.74958 0.70338 0.56808 0.08132  0.16648  0.12737  135 VAL A N   
888  C CA  . VAL A 165 ? 0.65459 0.60627 0.54829 0.08613  0.20054  0.13444  135 VAL A CA  
889  C C   . VAL A 165 ? 0.72717 0.65785 0.60682 0.08943  0.23795  0.13001  135 VAL A C   
890  O O   . VAL A 165 ? 0.82702 0.75491 0.68721 0.08747  0.22822  0.10735  135 VAL A O   
891  C CB  . VAL A 165 ? 0.59110 0.56334 0.57985 0.08540  0.18248  0.11448  135 VAL A CB  
892  C CG1 . VAL A 165 ? 0.58844 0.56037 0.66667 0.09021  0.21580  0.12002  135 VAL A CG1 
893  C CG2 . VAL A 165 ? 0.67936 0.67073 0.67417 0.08302  0.14581  0.11686  135 VAL A CG2 
894  N N   . LYS A 166 ? 0.83874 0.75213 0.72701 0.09475  0.28250  0.15176  136 LYS A N   
895  C CA  . LYS A 166 ? 0.85543 0.74875 0.74027 0.09846  0.32566  0.14808  136 LYS A CA  
896  C C   . LYS A 166 ? 0.84809 0.75793 0.84240 0.09701  0.33238  0.12164  136 LYS A C   
897  O O   . LYS A 166 ? 0.91263 0.84300 0.99178 0.09569  0.31560  0.11482  136 LYS A O   
898  C CB  . LYS A 166 ? 0.84892 0.71384 0.71271 0.10491  0.37703  0.18033  136 LYS A CB  
899  C CG  . LYS A 166 ? 0.91630 0.75256 0.65624 0.11183  0.37318  0.20387  136 LYS A CG  
900  C CD  . LYS A 166 ? 0.99832 0.79452 0.70610 0.12117  0.42961  0.23569  136 LYS A CD  
901  C CE  . LYS A 166 ? 1.28052 1.04485 0.86675 0.13048  0.40977  0.24893  136 LYS A CE  
902  N NZ  . LYS A 166 ? 1.24651 0.97122 0.80886 0.13868  0.44561  0.26796  136 LYS A NZ  
903  N N   . PRO A 167 ? 0.91760 0.81772 0.91254 0.09908  0.35362  0.10401  137 PRO A N   
904  C CA  . PRO A 167 ? 0.82057 0.73463 0.92397 0.10013  0.35796  0.07536  137 PRO A CA  
905  C C   . PRO A 167 ? 0.96270 0.88157 1.16993 0.10123  0.39657  0.08616  137 PRO A C   
906  O O   . PRO A 167 ? 0.90425 0.80669 1.09021 0.10153  0.43704  0.11730  137 PRO A O   
907  C CB  . PRO A 167 ? 0.89390 0.79220 0.96317 0.10319  0.38073  0.05952  137 PRO A CB  
908  C CG  . PRO A 167 ? 0.82988 0.71157 0.76836 0.10253  0.36462  0.07066  137 PRO A CG  
909  C CD  . PRO A 167 ? 1.04037 0.91670 0.93550 0.10204  0.36652  0.10473  137 PRO A CD  
910  N N   . SER A 168 ? 0.84241 0.78048 1.16314 0.10299  0.38216  0.05885  138 SER A N   
911  C CA  . SER A 168 ? 0.75639 0.70339 1.19979 0.10380  0.41164  0.06089  138 SER A CA  
912  C C   . SER A 168 ? 0.78217 0.73224 1.23011 0.10121  0.40921  0.09109  138 SER A C   
913  O O   . SER A 168 ? 0.79639 0.74400 1.31796 0.10014  0.44824  0.10606  138 SER A O   
914  C CB  . SER A 168 ? 0.88746 0.81891 1.36075 0.10379  0.48041  0.06794  138 SER A CB  
915  O OG  . SER A 168 ? 1.27172 1.20363 1.75928 0.10730  0.48198  0.03584  138 SER A OG  
916  N N   . GLN A 169 ? 0.69010 0.64486 1.06429 0.09998  0.36512  0.09963  139 GLN A N   
917  C CA  . GLN A 169 ? 0.61766 0.57762 0.99447 0.09878  0.35417  0.12441  139 GLN A CA  
918  C C   . GLN A 169 ? 0.69881 0.68142 1.10556 0.10065  0.29487  0.10413  139 GLN A C   
919  O O   . GLN A 169 ? 0.84091 0.82927 1.24849 0.10309  0.26277  0.07410  139 GLN A O   
920  C CB  . GLN A 169 ? 0.71692 0.65756 0.96940 0.09743  0.36054  0.15706  139 GLN A CB  
921  C CG  . GLN A 169 ? 0.91388 0.82251 1.12916 0.09917  0.42216  0.18405  139 GLN A CG  
922  C CD  . GLN A 169 ? 1.19192 1.07564 1.28464 0.10238  0.42170  0.21569  139 GLN A CD  
923  O OE1 . GLN A 169 ? 1.25627 1.15041 1.28964 0.10186  0.37458  0.21337  139 GLN A OE1 
924  N NE2 . GLN A 169 ? 1.03244 0.87998 1.08696 0.10692  0.47466  0.24450  139 GLN A NE2 
925  N N   . THR A 170 ? 0.63068 0.62195 1.05729 0.10082  0.28130  0.12119  140 THR A N   
926  C CA  . THR A 170 ? 0.48140 0.49181 0.94537 0.10467  0.23063  0.10360  140 THR A CA  
927  C C   . THR A 170 ? 0.47646 0.49009 0.83998 0.10158  0.19485  0.10957  140 THR A C   
928  O O   . THR A 170 ? 0.78585 0.79327 1.07994 0.09790  0.20410  0.13678  140 THR A O   
929  C CB  . THR A 170 ? 0.56834 0.58787 1.11824 0.10743  0.23385  0.11565  140 THR A CB  
930  O OG1 . THR A 170 ? 0.51262 0.52896 1.16434 0.10857  0.27186  0.11022  140 THR A OG1 
931  C CG2 . THR A 170 ? 0.41052 0.44684 1.00240 0.11465  0.18158  0.09356  140 THR A CG2 
932  N N   . LEU A 171 ? 0.73446 0.57472 0.58261 -0.02354 -0.02536 -0.02645 141 LEU A N   
933  C CA  . LEU A 171 ? 0.62118 0.44167 0.47310 -0.02612 -0.03865 -0.03039 141 LEU A CA  
934  C C   . LEU A 171 ? 0.66928 0.47709 0.54644 -0.02665 -0.04534 -0.01007 141 LEU A C   
935  O O   . LEU A 171 ? 0.77371 0.57109 0.67201 -0.02224 -0.03984 -0.00778 141 LEU A O   
936  C CB  . LEU A 171 ? 0.59172 0.38749 0.44799 -0.02000 -0.03690 -0.05506 141 LEU A CB  
937  C CG  . LEU A 171 ? 0.58050 0.35377 0.45002 -0.02371 -0.04887 -0.05602 141 LEU A CG  
938  C CD1 . LEU A 171 ? 0.88303 0.66906 0.73543 -0.03569 -0.06147 -0.05566 141 LEU A CD1 
939  C CD2 . LEU A 171 ? 0.60587 0.35088 0.48186 -0.01766 -0.04470 -0.07584 141 LEU A CD2 
940  N N   . SER A 172 ? 0.73042 0.54281 0.60547 -0.03126 -0.05692 0.00355  142 SER A N   
941  C CA  . SER A 172 ? 0.58968 0.39070 0.48772 -0.02914 -0.06252 0.02169  142 SER A CA  
942  C C   . SER A 172 ? 0.54000 0.33810 0.44385 -0.02969 -0.07523 0.01854  142 SER A C   
943  O O   . SER A 172 ? 0.55749 0.37302 0.44406 -0.03525 -0.08349 0.01666  142 SER A O   
944  C CB  . SER A 172 ? 0.81711 0.62891 0.71200 -0.03091 -0.06276 0.04836  142 SER A CB  
945  O OG  . SER A 172 ? 0.62164 0.43910 0.51218 -0.03400 -0.05067 0.05306  142 SER A OG  
946  N N   . LEU A 173 ? 0.52271 0.30479 0.45059 -0.02542 -0.07675 0.01768  143 LEU A N   
947  C CA  . LEU A 173 ? 0.57609 0.35990 0.51378 -0.02633 -0.08772 0.01668  143 LEU A CA  
948  C C   . LEU A 173 ? 0.54077 0.31783 0.50437 -0.01880 -0.08834 0.02838  143 LEU A C   
949  O O   . LEU A 173 ? 0.59810 0.36201 0.57483 -0.01541 -0.08005 0.02580  143 LEU A O   
950  C CB  . LEU A 173 ? 0.50628 0.27825 0.44448 -0.03032 -0.08781 -0.00349 143 LEU A CB  
951  C CG  . LEU A 173 ? 0.53330 0.30471 0.44660 -0.03744 -0.08649 -0.02154 143 LEU A CG  
952  C CD1 . LEU A 173 ? 0.53742 0.28476 0.45635 -0.03830 -0.08332 -0.03903 143 LEU A CD1 
953  C CD2 . LEU A 173 ? 0.55312 0.34735 0.44976 -0.04781 -0.09821 -0.02068 143 LEU A CD2 
954  N N   . THR A 174 ? 0.57037 0.36035 0.54142 -0.01594 -0.09790 0.03981  144 THR A N   
955  C CA  . THR A 174 ? 0.61275 0.39797 0.60777 -0.00600 -0.09793 0.04948  144 THR A CA  
956  C C   . THR A 174 ? 0.53985 0.33725 0.54914 -0.00593 -0.10512 0.04342  144 THR A C   
957  O O   . THR A 174 ? 0.50156 0.31726 0.50260 -0.01355 -0.11411 0.04098  144 THR A O   
958  C CB  . THR A 174 ? 0.62639 0.41850 0.62229 0.00225  -0.10126 0.07214  144 THR A CB  
959  O OG1 . THR A 174 ? 0.64163 0.42734 0.62134 -0.00125 -0.09517 0.08083  144 THR A OG1 
960  C CG2 . THR A 174 ? 0.62565 0.40292 0.64665 0.01488  -0.09759 0.07870  144 THR A CG2 
961  N N   . CYS A 175 ? 0.58614 0.37680 0.61639 0.00064  -0.10093 0.04036  145 CYS A N   
962  C CA  . CYS A 175 ? 0.52198 0.32842 0.56763 0.00062  -0.10576 0.03577  145 CYS A CA  
963  C C   . CYS A 175 ? 0.63038 0.44479 0.69656 0.01494  -0.10549 0.04381  145 CYS A C   
964  O O   . CYS A 175 ? 0.59783 0.39728 0.67538 0.02135  -0.09704 0.03890  145 CYS A O   
965  C CB  . CYS A 175 ? 0.60539 0.40243 0.65594 -0.00431 -0.09974 0.02282  145 CYS A CB  
966  S SG  . CYS A 175 ? 0.93623 0.75528 1.00386 -0.00783 -0.10460 0.02021  145 CYS A SG  
967  N N   . SER A 176 ? 0.76386 0.60395 0.83519 0.02021  -0.11437 0.05479  146 SER A N   
968  C CA  . SER A 176 ? 0.43647 0.28638 0.52883 0.03813  -0.11360 0.06274  146 SER A CA  
969  C C   . SER A 176 ? 0.41656 0.28660 0.52702 0.03924  -0.11281 0.05257  146 SER A C   
970  O O   . SER A 176 ? 0.50715 0.40034 0.61622 0.02682  -0.11918 0.04965  146 SER A O   
971  C CB  . SER A 176 ? 0.45229 0.33050 0.54489 0.04612  -0.12349 0.08149  146 SER A CB  
972  O OG  . SER A 176 ? 0.80826 0.67325 0.88344 0.04557  -0.12402 0.09403  146 SER A OG  
973  N N   . ILE A 177 ? 0.46523 0.32689 0.59221 0.05275  -0.10449 0.04677  147 ILE A N   
974  C CA  . ILE A 177 ? 0.39918 0.28420 0.54241 0.05483  -0.10180 0.03596  147 ILE A CA  
975  C C   . ILE A 177 ? 0.40802 0.31808 0.57136 0.07543  -0.10238 0.04172  147 ILE A C   
976  O O   . ILE A 177 ? 0.45472 0.34314 0.62450 0.09282  -0.09751 0.04602  147 ILE A O   
977  C CB  . ILE A 177 ? 0.39344 0.25688 0.53879 0.05307  -0.09080 0.01956  147 ILE A CB  
978  C CG1 . ILE A 177 ? 0.43746 0.27704 0.56471 0.03738  -0.08919 0.01656  147 ILE A CG1 
979  C CG2 . ILE A 177 ? 0.37554 0.27201 0.53380 0.05213  -0.08886 0.00964  147 ILE A CG2 
980  C CD1 . ILE A 177 ? 0.44105 0.26697 0.57054 0.03438  -0.07935 0.00222  147 ILE A CD1 
981  N N   . SER A 178 ? 0.49967 0.45527 0.67418 0.07397  -0.10760 0.04285  148 SER A N   
982  C CA  . SER A 178 ? 0.40066 0.39088 0.59713 0.09511  -0.10709 0.04671  148 SER A CA  
983  C C   . SER A 178 ? 0.38099 0.41176 0.58971 0.09014  -0.10491 0.03674  148 SER A C   
984  O O   . SER A 178 ? 0.52516 0.57686 0.72791 0.06888  -0.11118 0.03942  148 SER A O   
985  C CB  . SER A 178 ? 0.40910 0.43266 0.60795 0.09950  -0.11878 0.06685  148 SER A CB  
986  O OG  . SER A 178 ? 0.39444 0.44845 0.58493 0.07497  -0.12908 0.06996  148 SER A OG  
987  N N   . GLY A 179 ? 0.38652 0.42750 0.61202 0.10933  -0.09529 0.02512  149 GLY A N   
988  C CA  . GLY A 179 ? 0.37081 0.45426 0.60723 0.10651  -0.09105 0.01440  149 GLY A CA  
989  C C   . GLY A 179 ? 0.36842 0.42965 0.60017 0.10301  -0.08021 -0.00641 149 GLY A C   
990  O O   . GLY A 179 ? 0.46752 0.56291 0.71031 0.10923  -0.07321 -0.01947 149 GLY A O   
991  N N   . ASP A 180 ? 0.38453 0.39612 0.60005 0.09251  -0.07867 -0.01000 150 ASP A N   
992  C CA  . ASP A 180 ? 0.40424 0.39697 0.61522 0.08786  -0.06911 -0.02953 150 ASP A CA  
993  C C   . ASP A 180 ? 0.42357 0.35777 0.62665 0.09100  -0.06461 -0.03367 150 ASP A C   
994  O O   . ASP A 180 ? 0.40192 0.31075 0.59788 0.09141  -0.07014 -0.01801 150 ASP A O   
995  C CB  . ASP A 180 ? 0.34878 0.35363 0.54860 0.06546  -0.07196 -0.02730 150 ASP A CB  
996  C CG  . ASP A 180 ? 0.55865 0.56878 0.75750 0.06157  -0.06295 -0.04654 150 ASP A CG  
997  O OD1 . ASP A 180 ? 0.54905 0.55474 0.75541 0.07391  -0.05423 -0.06565 150 ASP A OD1 
998  O OD2 . ASP A 180 ? 0.33148 0.35101 0.52231 0.04642  -0.06445 -0.04285 150 ASP A OD2 
999  N N   . SER A 181 ? 0.40521 0.32168 0.60924 0.09124  -0.05441 -0.05491 151 SER A N   
1000 C CA  . SER A 181 ? 0.43051 0.29185 0.62889 0.09058  -0.04865 -0.06030 151 SER A CA  
1001 C C   . SER A 181 ? 0.48637 0.33285 0.66807 0.06874  -0.05072 -0.05728 151 SER A C   
1002 O O   . SER A 181 ? 0.43067 0.30469 0.60840 0.05638  -0.05102 -0.06351 151 SER A O   
1003 C CB  . SER A 181 ? 0.45700 0.30487 0.66474 0.09813  -0.03619 -0.08792 151 SER A CB  
1004 O OG  . SER A 181 ? 0.61032 0.40156 0.81379 0.09392  -0.03026 -0.09235 151 SER A OG  
1005 N N   . VAL A 182 ? 0.44573 0.25209 0.61837 0.06550  -0.05170 -0.04580 152 VAL A N   
1006 C CA  . VAL A 182 ? 0.41961 0.21400 0.57741 0.04724  -0.05226 -0.04328 152 VAL A CA  
1007 C C   . VAL A 182 ? 0.56619 0.35641 0.72522 0.03667  -0.04336 -0.06472 152 VAL A C   
1008 O O   . VAL A 182 ? 0.51244 0.31503 0.66350 0.02266  -0.04356 -0.06626 152 VAL A O   
1009 C CB  . VAL A 182 ? 0.43678 0.19585 0.58434 0.04631  -0.05436 -0.02590 152 VAL A CB  
1010 C CG1 . VAL A 182 ? 0.51006 0.22781 0.66431 0.05256  -0.04613 -0.02941 152 VAL A CG1 
1011 C CG2 . VAL A 182 ? 0.42399 0.18001 0.55600 0.02965  -0.05512 -0.02241 152 VAL A CG2 
1012 N N   . SER A 183 ? 0.46476 0.23970 0.63431 0.04335  -0.03523 -0.08252 153 SER A N   
1013 C CA  . SER A 183 ? 0.59105 0.36605 0.76199 0.03086  -0.02681 -0.10769 153 SER A CA  
1014 C C   . SER A 183 ? 0.57512 0.39835 0.75265 0.03322  -0.02494 -0.12675 153 SER A C   
1015 O O   . SER A 183 ? 0.46935 0.29336 0.65141 0.02933  -0.01665 -0.15364 153 SER A O   
1016 C CB  . SER A 183 ? 0.50861 0.23137 0.68568 0.03297  -0.01761 -0.11943 153 SER A CB  
1017 O OG  . SER A 183 ? 0.70263 0.41396 0.89233 0.05599  -0.01498 -0.12200 153 SER A OG  
1018 N N   . SER A 184 ? 0.55341 0.41826 0.73096 0.03776  -0.03219 -0.11367 154 SER A N   
1019 C CA  . SER A 184 ? 0.42107 0.33899 0.60424 0.03927  -0.03063 -0.12677 154 SER A CA  
1020 C C   . SER A 184 ? 0.55299 0.49894 0.73000 0.02175  -0.02820 -0.13933 154 SER A C   
1021 O O   . SER A 184 ? 0.58501 0.52554 0.75373 0.00994  -0.03149 -0.12755 154 SER A O   
1022 C CB  . SER A 184 ? 0.37777 0.33203 0.56240 0.04388  -0.03928 -0.10499 154 SER A CB  
1023 O OG  . SER A 184 ? 0.38671 0.39754 0.57591 0.04287  -0.03769 -0.11321 154 SER A OG  
1024 N N   . ASN A 185 ? 0.61050 0.59196 0.79177 0.02106  -0.02211 -0.16386 155 ASN A N   
1025 C CA  . ASN A 185 ? 0.54043 0.55944 0.71614 0.00416  -0.02023 -0.17682 155 ASN A CA  
1026 C C   . ASN A 185 ? 0.59018 0.66205 0.76271 0.00050  -0.02746 -0.15417 155 ASN A C   
1027 O O   . ASN A 185 ? 0.75317 0.84851 0.92050 -0.01186 -0.02885 -0.15069 155 ASN A O   
1028 C CB  . ASN A 185 ? 0.55498 0.59913 0.73427 0.00337  -0.01121 -0.21313 155 ASN A CB  
1029 C CG  . ASN A 185 ? 0.69620 0.78410 0.86895 -0.01661 -0.00963 -0.22926 155 ASN A CG  
1030 O OD1 . ASN A 185 ? 0.79104 0.94417 0.96149 -0.01959 -0.01277 -0.22305 155 ASN A OD1 
1031 N ND2 . ASN A 185 ? 0.75142 0.80718 0.92166 -0.03157 -0.00496 -0.24814 155 ASN A ND2 
1032 N N   . SER A 186 ? 0.56139 0.65337 0.73827 0.01082  -0.03188 -0.13708 156 SER A N   
1033 C CA  . SER A 186 ? 0.51629 0.65185 0.69152 0.00654  -0.03809 -0.11284 156 SER A CA  
1034 C C   . SER A 186 ? 0.47900 0.58206 0.65260 0.00899  -0.04582 -0.08402 156 SER A C   
1035 O O   . SER A 186 ? 0.61650 0.74083 0.79400 0.01130  -0.05037 -0.06657 156 SER A O   
1036 C CB  . SER A 186 ? 0.55085 0.74646 0.73214 0.01105  -0.03648 -0.11600 156 SER A CB  
1037 O OG  . SER A 186 ? 0.32519 0.50925 0.51461 0.02418  -0.03615 -0.11643 156 SER A OG  
1038 N N   . ALA A 187 ? 0.55882 0.61303 0.72619 0.00655  -0.04701 -0.07990 157 ALA A N   
1039 C CA  . ALA A 187 ? 0.44959 0.47254 0.61268 0.00767  -0.05369 -0.05742 157 ALA A CA  
1040 C C   . ALA A 187 ? 0.46223 0.45266 0.61639 0.00208  -0.05316 -0.05406 157 ALA A C   
1041 O O   . ALA A 187 ? 0.52576 0.51042 0.67858 -0.00267 -0.04784 -0.06903 157 ALA A O   
1042 C CB  . ALA A 187 ? 0.31975 0.31601 0.48611 0.01694  -0.05587 -0.05652 157 ALA A CB  
1043 N N   . ALA A 188 ? 0.44315 0.41425 0.59138 0.00156  -0.05821 -0.03554 158 ALA A N   
1044 C CA  . ALA A 188 ? 0.31193 0.25428 0.45118 -0.00127 -0.05721 -0.03145 158 ALA A CA  
1045 C C   . ALA A 188 ? 0.48686 0.39575 0.61837 0.00052  -0.06250 -0.01949 158 ALA A C   
1046 O O   . ALA A 188 ? 0.59849 0.51380 0.73176 0.00046  -0.06783 -0.00920 158 ALA A O   
1047 C CB  . ALA A 188 ? 0.38189 0.34905 0.52131 -0.00345 -0.05595 -0.02322 158 ALA A CB  
1048 N N   . TRP A 189 ? 0.35718 0.23420 0.47966 -0.00009 -0.06096 -0.02109 159 TRP A N   
1049 C CA  . TRP A 189 ? 0.47236 0.32173 0.58481 0.00057  -0.06580 -0.01296 159 TRP A CA  
1050 C C   . TRP A 189 ? 0.41361 0.24807 0.51500 -0.00130 -0.06384 -0.00900 159 TRP A C   
1051 O O   . TRP A 189 ? 0.34616 0.17282 0.44296 -0.00245 -0.05843 -0.01319 159 TRP A O   
1052 C CB  . TRP A 189 ? 0.49565 0.32443 0.60610 0.00336  -0.06541 -0.01597 159 TRP A CB  
1053 C CG  . TRP A 189 ? 0.44335 0.28473 0.56683 0.00919  -0.06463 -0.02282 159 TRP A CG  
1054 C CD1 . TRP A 189 ? 0.43262 0.27187 0.56326 0.01019  -0.05780 -0.03616 159 TRP A CD1 
1055 C CD2 . TRP A 189 ? 0.41495 0.27512 0.54657 0.01476  -0.06995 -0.01873 159 TRP A CD2 
1056 N NE1 . TRP A 189 ? 0.48606 0.33856 0.62825 0.01882  -0.05771 -0.04222 159 TRP A NE1 
1057 C CE2 . TRP A 189 ? 0.46498 0.33424 0.60867 0.02247  -0.06516 -0.03040 159 TRP A CE2 
1058 C CE3 . TRP A 189 ? 0.47518 0.34681 0.60557 0.01270  -0.07789 -0.00748 159 TRP A CE3 
1059 C CZ2 . TRP A 189 ? 0.52293 0.41671 0.67816 0.03138  -0.06752 -0.03004 159 TRP A CZ2 
1060 C CZ3 . TRP A 189 ? 0.47943 0.37767 0.62168 0.01817  -0.08122 -0.00551 159 TRP A CZ3 
1061 C CH2 . TRP A 189 ? 0.48847 0.39975 0.64336 0.02900  -0.07580 -0.01616 159 TRP A CH2 
1062 N N   . ASN A 190 ? 0.48721 0.31730 0.58499 -0.00191 -0.06747 -0.00152 160 ASN A N   
1063 C CA  . ASN A 190 ? 0.45686 0.27310 0.54649 -0.00018 -0.06421 0.00074  160 ASN A CA  
1064 C C   . ASN A 190 ? 0.47654 0.26474 0.55043 -0.00275 -0.06728 -0.00056 160 ASN A C   
1065 O O   . ASN A 190 ? 0.50371 0.28793 0.57404 -0.00700 -0.07370 0.00001  160 ASN A O   
1066 C CB  . ASN A 190 ? 0.46709 0.29346 0.56461 0.00175  -0.06446 0.00987  160 ASN A CB  
1067 C CG  . ASN A 190 ? 0.43119 0.29563 0.54291 0.00293  -0.06287 0.01251  160 ASN A CG  
1068 O OD1 . ASN A 190 ? 0.43483 0.31810 0.55111 0.00737  -0.05798 0.01432  160 ASN A OD1 
1069 N ND2 . ASN A 190 ? 0.40646 0.28848 0.52525 -0.00075 -0.06690 0.01231  160 ASN A ND2 
1070 N N   . TRP A 191 ? 0.43741 0.21108 0.50193 0.00068  -0.06234 -0.00296 161 TRP A N   
1071 C CA  . TRP A 191 ? 0.40760 0.15711 0.45478 -0.00199 -0.06385 -0.00804 161 TRP A CA  
1072 C C   . TRP A 191 ? 0.42628 0.15802 0.47171 0.00274  -0.05997 -0.00923 161 TRP A C   
1073 O O   . TRP A 191 ? 0.49485 0.23273 0.54607 0.01296  -0.05230 -0.00751 161 TRP A O   
1074 C CB  . TRP A 191 ? 0.41386 0.16159 0.44798 -0.00098 -0.05924 -0.01288 161 TRP A CB  
1075 C CG  . TRP A 191 ? 0.52213 0.27303 0.55201 -0.00628 -0.06463 -0.00990 161 TRP A CG  
1076 C CD1 . TRP A 191 ? 0.50402 0.26375 0.54216 -0.00595 -0.06297 -0.00611 161 TRP A CD1 
1077 C CD2 . TRP A 191 ? 0.61427 0.35984 0.63152 -0.01202 -0.07239 -0.00953 161 TRP A CD2 
1078 N NE1 . TRP A 191 ? 0.58683 0.34368 0.61955 -0.00799 -0.06864 -0.00074 161 TRP A NE1 
1079 C CE2 . TRP A 191 ? 0.62361 0.37693 0.64346 -0.01168 -0.07512 -0.00180 161 TRP A CE2 
1080 C CE3 . TRP A 191 ? 0.59346 0.32919 0.59764 -0.01822 -0.07729 -0.01557 161 TRP A CE3 
1081 C CZ2 . TRP A 191 ? 0.54985 0.30787 0.56057 -0.01484 -0.08317 0.00366  161 TRP A CZ2 
1082 C CZ3 . TRP A 191 ? 0.54129 0.28444 0.53486 -0.02510 -0.08582 -0.01354 161 TRP A CZ3 
1083 C CH2 . TRP A 191 ? 0.56153 0.31888 0.55883 -0.02218 -0.08900 -0.00224 161 TRP A CH2 
1084 N N   . ILE A 192 ? 0.44734 0.15750 0.48598 -0.00471 -0.06502 -0.01197 162 ILE A N   
1085 C CA  . ILE A 192 ? 0.49117 0.17349 0.52895 -0.00132 -0.06113 -0.01364 162 ILE A CA  
1086 C C   . ILE A 192 ? 0.59068 0.24487 0.60776 -0.00911 -0.06245 -0.02944 162 ILE A C   
1087 O O   . ILE A 192 ? 0.51017 0.16993 0.51838 -0.02266 -0.07097 -0.03335 162 ILE A O   
1088 C CB  . ILE A 192 ? 0.47565 0.15684 0.52873 -0.00718 -0.06563 -0.00056 162 ILE A CB  
1089 C CG1 . ILE A 192 ? 0.44116 0.16078 0.51195 -0.00245 -0.06582 0.01268  162 ILE A CG1 
1090 C CG2 . ILE A 192 ? 0.50958 0.15702 0.56523 -0.00052 -0.05958 0.00210  162 ILE A CG2 
1091 C CD1 . ILE A 192 ? 0.43985 0.16896 0.52488 -0.00917 -0.07014 0.02761  162 ILE A CD1 
1092 N N   . ARG A 193 ? 0.53963 0.16716 0.54915 0.00027  -0.05376 -0.03934 163 ARG A N   
1093 C CA  . ARG A 193 ? 0.61174 0.20990 0.60040 -0.00721 -0.05337 -0.05914 163 ARG A CA  
1094 C C   . ARG A 193 ? 0.73168 0.28771 0.72482 -0.00702 -0.04914 -0.06225 163 ARG A C   
1095 O O   . ARG A 193 ? 0.67966 0.23341 0.68964 0.00610  -0.04178 -0.04754 163 ARG A O   
1096 C CB  . ARG A 193 ? 0.59124 0.19413 0.56325 0.00403  -0.04413 -0.07328 163 ARG A CB  
1097 C CG  . ARG A 193 ? 0.62858 0.22674 0.60983 0.02689  -0.03090 -0.07181 163 ARG A CG  
1098 C CD  . ARG A 193 ? 0.70052 0.30947 0.66419 0.03600  -0.02147 -0.08713 163 ARG A CD  
1099 N NE  . ARG A 193 ? 0.83975 0.45329 0.81419 0.05973  -0.00833 -0.08516 163 ARG A NE  
1100 C CZ  . ARG A 193 ? 0.84107 0.47014 0.80474 0.07162  0.00248  -0.09665 163 ARG A CZ  
1101 N NH1 . ARG A 193 ? 0.63799 0.27821 0.57798 0.06083  0.00165  -0.11025 163 ARG A NH1 
1102 N NH2 . ARG A 193 ? 0.97422 0.61366 0.95124 0.09480  0.01423  -0.09285 163 ARG A NH2 
1103 N N   . GLN A 194 ? 0.79378 0.32686 0.77149 -0.02281 -0.05041 -0.07964 164 GLN A N   
1104 C CA  . GLN A 194 ? 0.70113 0.20028 0.68295 -0.02776 -0.04154 -0.08294 164 GLN A CA  
1105 C C   . GLN A 194 ? 0.75204 0.22091 0.71409 -0.02964 -0.03418 -0.11335 164 GLN A C   
1106 O O   . GLN A 194 ? 0.76114 0.23664 0.70287 -0.04594 -0.04342 -0.13200 164 GLN A O   
1107 C CB  . GLN A 194 ? 0.83038 0.33431 0.81925 -0.05251 -0.05133 -0.07419 164 GLN A CB  
1108 C CG  . GLN A 194 ? 0.75069 0.21585 0.74454 -0.06080 -0.04191 -0.07529 164 GLN A CG  
1109 C CD  . GLN A 194 ? 0.75248 0.22613 0.75353 -0.08810 -0.05266 -0.06741 164 GLN A CD  
1110 O OE1 . GLN A 194 ? 0.85219 0.30659 0.86463 -0.09348 -0.04775 -0.05354 164 GLN A OE1 
1111 N NE2 . GLN A 194 ? 0.73232 0.23554 0.72576 -0.10560 -0.06799 -0.07457 164 GLN A NE2 
1112 N N   . SER A 195 ? 0.87273 0.30995 0.83992 -0.01246 -0.01783 -0.11859 165 SER A N   
1113 C CA  . SER A 195 ? 0.84287 0.25028 0.79852 -0.01121 -0.00822 -0.15029 165 SER A CA  
1114 C C   . SER A 195 ? 1.04397 0.41325 1.01785 -0.00387 0.00585  -0.14635 165 SER A C   
1115 O O   . SER A 195 ? 1.25025 0.61227 1.22999 0.01258  0.01283  -0.11786 165 SER A O   
1116 C CB  . SER A 195 ? 0.93754 0.35502 0.87972 0.01279  -0.00259 -0.16455 165 SER A CB  
1117 O OG  . SER A 195 ? 1.04933 0.46998 1.01116 0.04139  0.00730  -0.14513 165 SER A OG  
1118 N N   . PRO A 196 ? 1.26730 0.61355 1.24840 -0.01386 0.00350  -0.17397 166 PRO A N   
1119 C CA  . PRO A 196 ? 1.00512 0.31196 1.00880 -0.00081 -0.01284 -0.17000 166 PRO A CA  
1120 C C   . PRO A 196 ? 1.03024 0.30199 1.00243 0.03949  -0.01384 -0.16278 166 PRO A C   
1121 O O   . PRO A 196 ? 1.08158 0.30760 1.04845 0.05140  -0.01285 -0.14905 166 PRO A O   
1122 C CB  . PRO A 196 ? 1.12956 0.39860 1.10595 -0.01840 -0.02342 -0.20416 166 PRO A CB  
1123 C CG  . PRO A 196 ? 1.04284 0.34337 0.99543 -0.02482 -0.01822 -0.23191 166 PRO A CG  
1124 C CD  . PRO A 196 ? 1.09193 0.44043 1.04914 -0.03243 -0.00890 -0.20912 166 PRO A CD  
1125 N N   . SER A 197 ? 1.09063 0.39496 1.06501 0.05822  -0.00218 -0.17349 167 SER A N   
1126 C CA  . SER A 197 ? 1.09711 0.39212 1.07407 0.09572  0.00978  -0.17034 167 SER A CA  
1127 C C   . SER A 197 ? 1.34194 0.66122 1.33482 0.11232  0.01033  -0.13194 167 SER A C   
1128 O O   . SER A 197 ? 1.52569 0.83158 1.53211 0.13992  0.01645  -0.11920 167 SER A O   
1129 C CB  . SER A 197 ? 1.15556 0.47573 1.12212 0.10893  0.02377  -0.19906 167 SER A CB  
1130 O OG  . SER A 197 ? 1.24387 0.60888 1.20590 0.09427  0.02490  -0.19520 167 SER A OG  
1131 N N   . ARG A 198 ? 1.09674 0.45236 1.08740 0.09700  0.00456  -0.11380 168 ARG A N   
1132 C CA  . ARG A 198 ? 1.07890 0.45956 1.07898 0.11036  0.00736  -0.07967 168 ARG A CA  
1133 C C   . ARG A 198 ? 1.03163 0.41089 1.02625 0.08742  0.00658  -0.05348 168 ARG A C   
1134 O O   . ARG A 198 ? 1.17846 0.57929 1.19360 0.09873  0.00423  -0.02608 168 ARG A O   
1135 C CB  . ARG A 198 ? 1.35690 0.78841 1.36577 0.11812  0.01233  -0.08059 168 ARG A CB  
1136 C CG  . ARG A 198 ? 1.29032 0.73652 1.31034 0.14780  0.02761  -0.09465 168 ARG A CG  
1137 C CD  . ARG A 198 ? 1.38225 0.81580 1.38027 0.14134  0.03505  -0.13177 168 ARG A CD  
1138 N NE  . ARG A 198 ? 1.20608 0.65300 1.18113 0.11357  0.02900  -0.13980 168 ARG A NE  
1139 C CZ  . ARG A 198 ? 1.06206 0.55487 1.02504 0.11345  0.02797  -0.13649 168 ARG A CZ  
1140 N NH1 . ARG A 198 ? 1.21260 0.74405 1.18752 0.13676  0.03776  -0.12690 168 ARG A NH1 
1141 N NH2 . ARG A 198 ? 1.09692 0.61101 1.04413 0.08722  0.01621  -0.13975 168 ARG A NH2 
1142 N N   . GLY A 199 ? 1.04924 0.41544 1.03354 0.05521  0.00929  -0.06288 169 GLY A N   
1143 C CA  . GLY A 199 ? 0.83538 0.21406 0.83359 0.03395  0.00264  -0.04226 169 GLY A CA  
1144 C C   . GLY A 199 ? 0.83759 0.27596 0.85128 0.02593  -0.00894 -0.03588 169 GLY A C   
1145 O O   . GLY A 199 ? 0.91806 0.37684 0.92590 0.02547  -0.01171 -0.05285 169 GLY A O   
1146 N N   . LEU A 200 ? 0.75900 0.22326 0.78925 0.01994  -0.01768 -0.01099 170 LEU A N   
1147 C CA  . LEU A 200 ? 0.76112 0.27667 0.80270 0.01432  -0.02980 -0.00339 170 LEU A CA  
1148 C C   . LEU A 200 ? 0.87256 0.41458 0.92523 0.03924  -0.02689 0.00409  170 LEU A C   
1149 O O   . LEU A 200 ? 0.68061 0.23539 0.75091 0.05368  -0.02513 0.02584  170 LEU A O   
1150 C CB  . LEU A 200 ? 0.71572 0.25056 0.77282 -0.00019 -0.03904 0.01853  170 LEU A CB  
1151 C CG  . LEU A 200 ? 0.66423 0.18769 0.71542 -0.02871 -0.04566 0.01170  170 LEU A CG  
1152 C CD1 . LEU A 200 ? 0.71027 0.25260 0.77983 -0.04048 -0.05325 0.03673  170 LEU A CD1 
1153 C CD2 . LEU A 200 ? 0.63791 0.18358 0.67903 -0.04135 -0.05558 -0.00590 170 LEU A CD2 
1154 N N   . GLU A 201 ? 0.92725 0.48093 0.97152 0.04351  -0.02704 -0.01303 171 GLU A N   
1155 C CA  . GLU A 201 ? 0.59564 0.17885 0.65023 0.06428  -0.02283 -0.00939 171 GLU A CA  
1156 C C   . GLU A 201 ? 0.57370 0.20567 0.62914 0.05283  -0.03026 -0.00567 171 GLU A C   
1157 O O   . GLU A 201 ? 0.57694 0.21193 0.61716 0.03963  -0.03495 -0.01887 171 GLU A O   
1158 C CB  . GLU A 201 ? 0.67350 0.24308 0.71252 0.07711  -0.01267 -0.03103 171 GLU A CB  
1159 C CG  . GLU A 201 ? 1.09254 0.69961 1.14127 0.10011  -0.00292 -0.02492 171 GLU A CG  
1160 C CD  . GLU A 201 ? 1.13235 0.73679 1.16438 0.11042  0.00721  -0.04698 171 GLU A CD  
1161 O OE1 . GLU A 201 ? 1.27406 0.91211 1.29580 0.10205  0.00611  -0.05334 171 GLU A OE1 
1162 O OE2 . GLU A 201 ? 1.17916 0.74726 1.20832 0.12703  0.01699  -0.05784 171 GLU A OE2 
1163 N N   . TRP A 202 ? 0.65551 0.32559 0.72860 0.05822  -0.03104 0.01223  172 TRP A N   
1164 C CA  . TRP A 202 ? 0.57263 0.28484 0.64817 0.04870  -0.03622 0.01329  172 TRP A CA  
1165 C C   . TRP A 202 ? 0.58627 0.31953 0.65532 0.05477  -0.02987 0.00336  172 TRP A C   
1166 O O   . TRP A 202 ? 0.74046 0.48318 0.81404 0.07113  -0.02102 0.00477  172 TRP A O   
1167 C CB  . TRP A 202 ? 0.47657 0.22569 0.57139 0.05094  -0.03837 0.03195  172 TRP A CB  
1168 C CG  . TRP A 202 ? 0.48193 0.27150 0.57997 0.04196  -0.04198 0.02910  172 TRP A CG  
1169 C CD1 . TRP A 202 ? 0.62594 0.41926 0.72145 0.02756  -0.04936 0.02473  172 TRP A CD1 
1170 C CD2 . TRP A 202 ? 0.53301 0.36419 0.63852 0.04675  -0.03774 0.02922  172 TRP A CD2 
1171 N NE1 . TRP A 202 ? 0.48710 0.31447 0.58762 0.02448  -0.04902 0.02075  172 TRP A NE1 
1172 C CE2 . TRP A 202 ? 0.50539 0.35633 0.61145 0.03362  -0.04231 0.02256  172 TRP A CE2 
1173 C CE3 . TRP A 202 ? 0.50589 0.36166 0.61864 0.06066  -0.03031 0.03385  172 TRP A CE3 
1174 C CZ2 . TRP A 202 ? 0.40190 0.29035 0.51409 0.03072  -0.03962 0.01798  172 TRP A CZ2 
1175 C CZ3 . TRP A 202 ? 0.38238 0.28394 0.50174 0.05667  -0.02869 0.03102  172 TRP A CZ3 
1176 C CH2 . TRP A 202 ? 0.41405 0.32870 0.53238 0.04021  -0.03329 0.02197  172 TRP A CH2 
1177 N N   . LEU A 203 ? 0.44443 0.18683 0.50411 0.04187  -0.03403 -0.00469 173 LEU A N   
1178 C CA  . LEU A 203 ? 0.53229 0.29139 0.58418 0.04291  -0.02830 -0.01234 173 LEU A CA  
1179 C C   . LEU A 203 ? 0.50620 0.30401 0.57048 0.03843  -0.02810 -0.00703 173 LEU A C   
1180 O O   . LEU A 203 ? 0.67624 0.50178 0.74773 0.04552  -0.02106 -0.00531 173 LEU A O   
1181 C CB  . LEU A 203 ? 0.44874 0.19031 0.48088 0.03153  -0.03210 -0.02250 173 LEU A CB  
1182 C CG  . LEU A 203 ? 0.48655 0.19358 0.50264 0.03203  -0.03220 -0.03347 173 LEU A CG  
1183 C CD1 . LEU A 203 ? 0.49091 0.19413 0.48677 0.01985  -0.03691 -0.04176 173 LEU A CD1 
1184 C CD2 . LEU A 203 ? 0.60317 0.30301 0.61672 0.04907  -0.02051 -0.04054 173 LEU A CD2 
1185 N N   . GLY A 204 ? 0.39333 0.19514 0.46072 0.02651  -0.03528 -0.00592 174 GLY A N   
1186 C CA  . GLY A 204 ? 0.51363 0.34587 0.59141 0.02026  -0.03444 -0.00575 174 GLY A CA  
1187 C C   . GLY A 204 ? 0.45261 0.28470 0.53556 0.01163  -0.04175 -0.00583 174 GLY A C   
1188 O O   . GLY A 204 ? 0.42988 0.24574 0.51079 0.01080  -0.04791 -0.00303 174 GLY A O   
1189 N N   . ARG A 205 ? 0.35042 0.20208 0.44071 0.00458  -0.04037 -0.01044 175 ARG A N   
1190 C CA  . ARG A 205 ? 0.34399 0.19790 0.44060 -0.00081 -0.04519 -0.01361 175 ARG A CA  
1191 C C   . ARG A 205 ? 0.39704 0.25675 0.49736 -0.00964 -0.04133 -0.02311 175 ARG A C   
1192 O O   . ARG A 205 ? 0.48263 0.35439 0.58337 -0.01436 -0.03550 -0.02600 175 ARG A O   
1193 C CB  . ARG A 205 ? 0.33080 0.21216 0.43912 0.00201  -0.04775 -0.00921 175 ARG A CB  
1194 C CG  . ARG A 205 ? 0.32227 0.24386 0.44011 0.00180  -0.04333 -0.01015 175 ARG A CG  
1195 C CD  . ARG A 205 ? 0.51786 0.47263 0.64583 0.00360  -0.04640 -0.00400 175 ARG A CD  
1196 N NE  . ARG A 205 ? 0.30554 0.30767 0.44192 0.00379  -0.04326 -0.00257 175 ARG A NE  
1197 C CZ  . ARG A 205 ? 0.29791 0.34208 0.44260 0.00456  -0.04521 0.00382  175 ARG A CZ  
1198 N NH1 . ARG A 205 ? 0.61503 0.65799 0.76124 0.00476  -0.04948 0.00932  175 ARG A NH1 
1199 N NH2 . ARG A 205 ? 0.38828 0.48223 0.53987 0.00436  -0.04301 0.00587  175 ARG A NH2 
1200 N N   . THR A 206 ? 0.51191 0.36279 0.61606 -0.01200 -0.04410 -0.02817 176 THR A N   
1201 C CA  . THR A 206 ? 0.54881 0.39796 0.65863 -0.02016 -0.03990 -0.03969 176 THR A CA  
1202 C C   . THR A 206 ? 0.51182 0.37128 0.63126 -0.01764 -0.04213 -0.04801 176 THR A C   
1203 O O   . THR A 206 ? 0.51314 0.37060 0.63316 -0.00995 -0.04759 -0.04177 176 THR A O   
1204 C CB  . THR A 206 ? 0.51979 0.33281 0.62207 -0.02320 -0.03821 -0.03659 176 THR A CB  
1205 O OG1 . THR A 206 ? 0.61453 0.41849 0.72396 -0.03230 -0.03295 -0.04782 176 THR A OG1 
1206 C CG2 . THR A 206 ? 0.53442 0.32663 0.63259 -0.01427 -0.04472 -0.02837 176 THR A CG2 
1207 N N   . TYR A 207 ? 0.40113 0.27560 0.52815 -0.02536 -0.03743 -0.06374 177 TYR A N   
1208 C CA  . TYR A 207 ? 0.46225 0.35165 0.59783 -0.02251 -0.03759 -0.07621 177 TYR A CA  
1209 C C   . TYR A 207 ? 0.40603 0.28846 0.54650 -0.03317 -0.03055 -0.09803 177 TYR A C   
1210 O O   . TYR A 207 ? 0.55370 0.43098 0.69223 -0.04602 -0.02634 -0.10208 177 TYR A O   
1211 C CB  . TYR A 207 ? 0.61949 0.55785 0.75919 -0.02044 -0.04034 -0.07350 177 TYR A CB  
1212 C CG  . TYR A 207 ? 0.43871 0.41281 0.57906 -0.02828 -0.03808 -0.07395 177 TYR A CG  
1213 C CD1 . TYR A 207 ? 0.43851 0.41383 0.57478 -0.02471 -0.03934 -0.05701 177 TYR A CD1 
1214 C CD2 . TYR A 207 ? 0.41825 0.42875 0.56370 -0.03847 -0.03447 -0.09227 177 TYR A CD2 
1215 C CE1 . TYR A 207 ? 0.51287 0.52678 0.65228 -0.02846 -0.03711 -0.05502 177 TYR A CE1 
1216 C CE2 . TYR A 207 ? 0.40643 0.45941 0.55363 -0.04572 -0.03337 -0.09097 177 TYR A CE2 
1217 C CZ  . TYR A 207 ? 0.49888 0.55460 0.64413 -0.03934 -0.03475 -0.07062 177 TYR A CZ  
1218 O OH  . TYR A 207 ? 0.49700 0.60047 0.64642 -0.04327 -0.03347 -0.06705 177 TYR A OH  
1219 N N   . TYR A 208 ? 0.51236 0.39520 0.65970 -0.02839 -0.02866 -0.11324 178 TYR A N   
1220 C CA  . TYR A 208 ? 0.42057 0.28498 0.57288 -0.03705 -0.02094 -0.13786 178 TYR A CA  
1221 C C   . TYR A 208 ? 0.55573 0.46577 0.71313 -0.03982 -0.01853 -0.16090 178 TYR A C   
1222 O O   . TYR A 208 ? 0.72633 0.65798 0.88729 -0.02673 -0.02074 -0.16053 178 TYR A O   
1223 C CB  . TYR A 208 ? 0.48251 0.29457 0.63863 -0.02507 -0.01864 -0.13698 178 TYR A CB  
1224 C CG  . TYR A 208 ? 0.65243 0.43101 0.81469 -0.03271 -0.00921 -0.16191 178 TYR A CG  
1225 C CD1 . TYR A 208 ? 0.62264 0.36175 0.78284 -0.04817 -0.00440 -0.16122 178 TYR A CD1 
1226 C CD2 . TYR A 208 ? 0.50906 0.29445 0.67934 -0.02518 -0.00420 -0.18690 178 TYR A CD2 
1227 C CE1 . TYR A 208 ? 0.64411 0.34796 0.80748 -0.05713 0.00468  -0.18183 178 TYR A CE1 
1228 C CE2 . TYR A 208 ? 0.55649 0.30398 0.73238 -0.03219 0.00566  -0.21329 178 TYR A CE2 
1229 C CZ  . TYR A 208 ? 0.58613 0.29311 0.75525 -0.04841 0.00963  -0.20701 178 TYR A CZ  
1230 O OH  . TYR A 208 ? 0.64060 0.31482 0.80435 -0.05536 0.01823  -0.22245 178 TYR A OH  
1231 N N   . ARG A 209 ? 0.65805 0.58861 0.81545 -0.05844 -0.01399 -0.18107 179 ARG A N   
1232 C CA  . ARG A 209 ? 0.78755 0.76267 0.94771 -0.06435 -0.01068 -0.20847 179 ARG A CA  
1233 C C   . ARG A 209 ? 0.98384 0.91899 1.14714 -0.07602 -0.00143 -0.24030 179 ARG A C   
1234 O O   . ARG A 209 ? 1.15299 1.05149 1.32132 -0.06255 0.00321  -0.25187 179 ARG A O   
1235 C CB  . ARG A 209 ? 0.53417 0.57708 0.69151 -0.07705 -0.01404 -0.20572 179 ARG A CB  
1236 C CG  . ARG A 209 ? 0.47671 0.54342 0.63203 -0.06528 -0.02186 -0.17093 179 ARG A CG  
1237 C CD  . ARG A 209 ? 0.48950 0.57695 0.64661 -0.04881 -0.02556 -0.16097 179 ARG A CD  
1238 N NE  . ARG A 209 ? 0.54474 0.61692 0.70022 -0.03680 -0.03190 -0.12866 179 ARG A NE  
1239 C CZ  . ARG A 209 ? 0.36229 0.45711 0.51951 -0.02648 -0.03646 -0.11212 179 ARG A CZ  
1240 N NH1 . ARG A 209 ? 0.38899 0.52880 0.54961 -0.02520 -0.03527 -0.12248 179 ARG A NH1 
1241 N NH2 . ARG A 209 ? 0.44859 0.52251 0.60377 -0.01910 -0.04171 -0.08617 179 ARG A NH2 
1242 N N   . SER A 210 ? 0.74519 0.68472 0.90708 -0.10075 0.00208  -0.25558 180 SER A N   
1243 C CA  . SER A 210 ? 0.78235 0.66701 0.94749 -0.11555 0.01120  -0.28137 180 SER A CA  
1244 C C   . SER A 210 ? 0.92855 0.75064 1.09380 -0.11811 0.01204  -0.25814 180 SER A C   
1245 O O   . SER A 210 ? 0.91063 0.67394 1.07206 -0.11029 0.01706  -0.25296 180 SER A O   
1246 C CB  . SER A 210 ? 1.49162 1.41633 1.65494 -0.14574 0.01471  -0.31117 180 SER A CB  
1247 O OG  . SER A 210 ? 1.44315 1.40847 1.60437 -0.16069 0.00943  -0.29304 180 SER A OG  
1248 N N   . LYS A 211 ? 0.94043 0.78478 1.10111 -0.12285 0.00641  -0.23159 181 LYS A N   
1249 C CA  . LYS A 211 ? 0.63778 0.43535 0.79605 -0.12250 0.00639  -0.20530 181 LYS A CA  
1250 C C   . LYS A 211 ? 0.54338 0.36180 0.69578 -0.10323 -0.00203 -0.17326 181 LYS A C   
1251 O O   . LYS A 211 ? 0.62335 0.47791 0.77550 -0.08843 -0.00730 -0.17039 181 LYS A O   
1252 C CB  . LYS A 211 ? 0.72558 0.52725 0.88376 -0.15236 0.01046  -0.20901 181 LYS A CB  
1253 C CG  . LYS A 211 ? 0.52356 0.40245 0.68038 -0.16318 0.00630  -0.20809 181 LYS A CG  
1254 C CD  . LYS A 211 ? 0.54281 0.43097 0.70160 -0.19347 0.01064  -0.21111 181 LYS A CD  
1255 C CE  . LYS A 211 ? 0.81597 0.78822 0.97580 -0.20059 0.00641  -0.20746 181 LYS A CE  
1256 N NZ  . LYS A 211 ? 0.64754 0.63886 0.81115 -0.23072 0.01058  -0.20951 181 LYS A NZ  
1257 N N   . TRP A 212 ? 0.49910 0.29557 0.64633 -0.10456 -0.00279 -0.14986 182 TRP A N   
1258 C CA  . TRP A 212 ? 0.46111 0.27102 0.60122 -0.08810 -0.00964 -0.12337 182 TRP A CA  
1259 C C   . TRP A 212 ? 0.52471 0.38526 0.66263 -0.09592 -0.01093 -0.11718 182 TRP A C   
1260 O O   . TRP A 212 ? 0.82678 0.69775 0.96615 -0.11527 -0.00631 -0.12163 182 TRP A O   
1261 C CB  . TRP A 212 ? 0.47631 0.23798 0.61018 -0.08231 -0.00955 -0.10200 182 TRP A CB  
1262 C CG  . TRP A 212 ? 0.57299 0.29365 0.70983 -0.06623 -0.01046 -0.09972 182 TRP A CG  
1263 C CD1 . TRP A 212 ? 0.68168 0.35417 0.82271 -0.06837 -0.00451 -0.10413 182 TRP A CD1 
1264 C CD2 . TRP A 212 ? 0.58821 0.31590 0.72444 -0.04456 -0.01744 -0.09059 182 TRP A CD2 
1265 N NE1 . TRP A 212 ? 0.64000 0.29572 0.78025 -0.04555 -0.00719 -0.09610 182 TRP A NE1 
1266 C CE2 . TRP A 212 ? 0.64097 0.32866 0.78330 -0.03278 -0.01558 -0.09014 182 TRP A CE2 
1267 C CE3 . TRP A 212 ? 0.53516 0.29847 0.66742 -0.03470 -0.02475 -0.08184 182 TRP A CE3 
1268 C CZ2 . TRP A 212 ? 0.76781 0.45899 0.91280 -0.01175 -0.02137 -0.08149 182 TRP A CZ2 
1269 C CZ3 . TRP A 212 ? 0.53551 0.29747 0.66949 -0.01761 -0.03044 -0.07415 182 TRP A CZ3 
1270 C CH2 . TRP A 212 ? 0.45691 0.18741 0.59737 -0.00642 -0.02902 -0.07415 182 TRP A CH2 
1271 N N   . TYR A 213 ? 0.40513 0.29758 0.54100 -0.08060 -0.01682 -0.10571 183 TYR A N   
1272 C CA  . TYR A 213 ? 0.58265 0.52266 0.71849 -0.08105 -0.01791 -0.09677 183 TYR A CA  
1273 C C   . TYR A 213 ? 0.69173 0.61937 0.81978 -0.06415 -0.02131 -0.07441 183 TYR A C   
1274 O O   . TYR A 213 ? 0.36725 0.26385 0.49046 -0.05212 -0.02524 -0.06703 183 TYR A O   
1275 C CB  . TYR A 213 ? 0.46794 0.46276 0.61003 -0.07893 -0.02080 -0.10411 183 TYR A CB  
1276 C CG  . TYR A 213 ? 0.38189 0.39780 0.52964 -0.09735 -0.01735 -0.13093 183 TYR A CG  
1277 C CD1 . TYR A 213 ? 0.38878 0.44227 0.54040 -0.11756 -0.01413 -0.14083 183 TYR A CD1 
1278 C CD2 . TYR A 213 ? 0.39387 0.39541 0.54327 -0.09512 -0.01688 -0.14834 183 TYR A CD2 
1279 C CE1 . TYR A 213 ? 0.40922 0.48263 0.56470 -0.13799 -0.01106 -0.16930 183 TYR A CE1 
1280 C CE2 . TYR A 213 ? 0.70266 0.72147 0.85577 -0.11232 -0.01265 -0.17777 183 TYR A CE2 
1281 C CZ  . TYR A 213 ? 0.61349 0.66684 0.76887 -0.13519 -0.01002 -0.18913 183 TYR A CZ  
1282 O OH  . TYR A 213 ? 0.57444 0.64558 0.73225 -0.15581 -0.00591 -0.22218 183 TYR A OH  
1283 N N   . ASN A 214 ? 0.93116 0.88627 1.05849 -0.06347 -0.01940 -0.06519 184 ASN A N   
1284 C CA  . ASN A 214 ? 0.54860 0.49226 0.66790 -0.04823 -0.02059 -0.04850 184 ASN A CA  
1285 C C   . ASN A 214 ? 0.72041 0.70528 0.84515 -0.03581 -0.02174 -0.03990 184 ASN A C   
1286 O O   . ASN A 214 ? 0.97970 1.01248 1.11393 -0.04125 -0.02024 -0.04334 184 ASN A O   
1287 C CB  . ASN A 214 ? 0.50277 0.43510 0.61523 -0.05490 -0.01485 -0.04363 184 ASN A CB  
1288 C CG  . ASN A 214 ? 0.82154 0.70452 0.92512 -0.05962 -0.01485 -0.04166 184 ASN A CG  
1289 O OD1 . ASN A 214 ? 1.17872 1.03625 1.28403 -0.05904 -0.01826 -0.04643 184 ASN A OD1 
1290 N ND2 . ASN A 214 ? 0.52312 0.39658 0.61760 -0.06286 -0.01061 -0.03307 184 ASN A ND2 
1291 N N   . ASP A 215 ? 0.65268 0.61861 0.77167 -0.01944 -0.02442 -0.02810 185 ASP A N   
1292 C CA  . ASP A 215 ? 0.46804 0.46003 0.59212 -0.00414 -0.02418 -0.01617 185 ASP A CA  
1293 C C   . ASP A 215 ? 0.39187 0.34750 0.50511 0.00875  -0.02299 -0.00900 185 ASP A C   
1294 O O   . ASP A 215 ? 0.52404 0.44352 0.62967 0.01109  -0.02773 -0.00786 185 ASP A O   
1295 C CB  . ASP A 215 ? 0.40633 0.41562 0.53783 0.00093  -0.02969 -0.01082 185 ASP A CB  
1296 C CG  . ASP A 215 ? 0.64174 0.70711 0.78422 -0.00774 -0.02955 -0.01629 185 ASP A CG  
1297 O OD1 . ASP A 215 ? 0.92744 1.02965 1.07537 -0.01090 -0.02547 -0.01686 185 ASP A OD1 
1298 O OD2 . ASP A 215 ? 0.81471 0.89271 0.96019 -0.01207 -0.03339 -0.02086 185 ASP A OD2 
1299 N N   . TYR A 216 ? 0.47024 0.43922 0.58282 0.01647  -0.01639 -0.00587 186 TYR A N   
1300 C CA  . TYR A 216 ? 0.50394 0.44143 0.60448 0.02835  -0.01324 -0.00413 186 TYR A CA  
1301 C C   . TYR A 216 ? 0.58512 0.53651 0.69320 0.04974  -0.00904 0.00511  186 TYR A C   
1302 O O   . TYR A 216 ? 0.49751 0.49493 0.62013 0.05544  -0.00652 0.01199  186 TYR A O   
1303 C CB  . TYR A 216 ? 0.48502 0.42283 0.57600 0.02080  -0.00685 -0.00974 186 TYR A CB  
1304 C CG  . TYR A 216 ? 0.66401 0.57724 0.74636 0.00285  -0.01019 -0.01467 186 TYR A CG  
1305 C CD1 . TYR A 216 ? 0.60903 0.48854 0.68605 0.00105  -0.01803 -0.01524 186 TYR A CD1 
1306 C CD2 . TYR A 216 ? 0.59188 0.51687 0.67299 -0.01191 -0.00512 -0.01661 186 TYR A CD2 
1307 C CE1 . TYR A 216 ? 0.60794 0.46590 0.67928 -0.01104 -0.02064 -0.01698 186 TYR A CE1 
1308 C CE2 . TYR A 216 ? 0.47559 0.37299 0.55033 -0.02618 -0.00744 -0.01758 186 TYR A CE2 
1309 C CZ  . TYR A 216 ? 0.46472 0.32855 0.53495 -0.02371 -0.01516 -0.01744 186 TYR A CZ  
1310 O OH  . TYR A 216 ? 0.51681 0.35419 0.58286 -0.03375 -0.01707 -0.01579 186 TYR A OH  
1311 N N   . ALA A 217 ? 0.68496 0.59647 0.78342 0.06168  -0.00819 0.00514  187 ALA A N   
1312 C CA  . ALA A 217 ? 0.52887 0.44032 0.63383 0.08482  -0.00230 0.01277  187 ALA A CA  
1313 C C   . ALA A 217 ? 0.66724 0.59723 0.76942 0.09550  0.00846  0.00728  187 ALA A C   
1314 O O   . ALA A 217 ? 0.72718 0.64277 0.81353 0.08746  0.01120  -0.00419 187 ALA A O   
1315 C CB  . ALA A 217 ? 0.44310 0.29889 0.53878 0.09081  -0.00479 0.01157  187 ALA A CB  
1316 N N   . GLY A 218 ? 0.56319 0.53098 0.68142 0.11466  0.01480  0.01735  188 GLY A N   
1317 C CA  . GLY A 218 ? 0.43210 0.43070 0.55166 0.12677  0.02597  0.01353  188 GLY A CA  
1318 C C   . GLY A 218 ? 0.46446 0.42150 0.56741 0.13994  0.03375  0.00076  188 GLY A C   
1319 O O   . GLY A 218 ? 0.75537 0.73709 0.85405 0.14527  0.04333  -0.00640 188 GLY A O   
1320 N N   . THR A 219 ? 0.67035 0.56814 0.76337 0.14352  0.03017  -0.00353 189 THR A N   
1321 C CA  . THR A 219 ? 0.56782 0.42444 0.64272 0.15348  0.03734  -0.02038 189 THR A CA  
1322 C C   . THR A 219 ? 0.74869 0.60513 0.80133 0.13287  0.03657  -0.03474 189 THR A C   
1323 O O   . THR A 219 ? 0.62506 0.48309 0.66422 0.14093  0.04616  -0.04820 189 THR A O   
1324 C CB  . THR A 219 ? 0.54834 0.34192 0.61807 0.15568  0.03240  -0.02256 189 THR A CB  
1325 O OG1 . THR A 219 ? 0.55473 0.34920 0.64626 0.17391  0.03295  -0.00360 189 THR A OG1 
1326 C CG2 . THR A 219 ? 0.75443 0.50498 0.80555 0.16627  0.04090  -0.04413 189 THR A CG2 
1327 N N   . VAL A 220 ? 0.68436 0.54095 0.73311 0.10767  0.02591  -0.03114 190 VAL A N   
1328 C CA  . VAL A 220 ? 0.66874 0.52170 0.69740 0.08864  0.02396  -0.03940 190 VAL A CA  
1329 C C   . VAL A 220 ? 0.56836 0.45802 0.60518 0.07026  0.02149  -0.03028 190 VAL A C   
1330 O O   . VAL A 220 ? 0.45912 0.34316 0.48335 0.05238  0.01811  -0.03108 190 VAL A O   
1331 C CB  . VAL A 220 ? 0.60196 0.40889 0.61565 0.07609  0.01341  -0.04492 190 VAL A CB  
1332 C CG1 . VAL A 220 ? 0.54787 0.31606 0.54953 0.08882  0.01701  -0.05896 190 VAL A CG1 
1333 C CG2 . VAL A 220 ? 0.47457 0.27424 0.50314 0.06799  0.00269  -0.03356 190 VAL A CG2 
1334 N N   . LYS A 221 ? 0.68608 0.61375 0.74423 0.07405  0.02329  -0.02122 191 LYS A N   
1335 C CA  . LYS A 221 ? 0.55014 0.51048 0.61698 0.05358  0.02124  -0.01606 191 LYS A CA  
1336 C C   . LYS A 221 ? 0.42963 0.41175 0.48691 0.04249  0.02886  -0.01811 191 LYS A C   
1337 O O   . LYS A 221 ? 0.42364 0.40601 0.47877 0.02005  0.02599  -0.01550 191 LYS A O   
1338 C CB  . LYS A 221 ? 0.51653 0.52356 0.60679 0.05929  0.02232  -0.00813 191 LYS A CB  
1339 C CG  . LYS A 221 ? 0.38810 0.43067 0.48781 0.03519  0.02067  -0.00708 191 LYS A CG  
1340 C CD  . LYS A 221 ? 0.37500 0.47589 0.49651 0.04030  0.02185  -0.00060 191 LYS A CD  
1341 C CE  . LYS A 221 ? 0.42792 0.56441 0.55768 0.01201  0.02058  -0.00417 191 LYS A CE  
1342 N NZ  . LYS A 221 ? 0.35304 0.55837 0.50319 0.01431  0.02128  0.00104  191 LYS A NZ  
1343 N N   . SER A 222 ? 0.58195 0.58127 0.63352 0.05818  0.03937  -0.02229 192 SER A N   
1344 C CA  . SER A 222 ? 0.45628 0.48720 0.49978 0.04797  0.04811  -0.02218 192 SER A CA  
1345 C C   . SER A 222 ? 0.46987 0.46969 0.48915 0.03286  0.04520  -0.02395 192 SER A C   
1346 O O   . SER A 222 ? 0.48130 0.50670 0.49120 0.02362  0.05262  -0.02131 192 SER A O   
1347 C CB  . SER A 222 ? 0.47413 0.53688 0.51827 0.07250  0.06139  -0.02764 192 SER A CB  
1348 O OG  . SER A 222 ? 0.51778 0.53908 0.54598 0.09157  0.06292  -0.03992 192 SER A OG  
1349 N N   . ARG A 223 ? 0.47502 0.42696 0.48454 0.02977  0.03472  -0.02613 193 ARG A N   
1350 C CA  . ARG A 223 ? 0.72594 0.65571 0.71281 0.01779  0.03123  -0.02551 193 ARG A CA  
1351 C C   . ARG A 223 ? 0.54669 0.43513 0.53160 0.00995  0.01782  -0.02286 193 ARG A C   
1352 O O   . ARG A 223 ? 0.49108 0.36072 0.45760 0.00395  0.01293  -0.02208 193 ARG A O   
1353 C CB  . ARG A 223 ? 0.72665 0.65354 0.69200 0.03175  0.03754  -0.03853 193 ARG A CB  
1354 C CG  . ARG A 223 ? 0.62110 0.51941 0.58790 0.05203  0.03649  -0.05199 193 ARG A CG  
1355 C CD  . ARG A 223 ? 0.55652 0.45468 0.50337 0.06654  0.04613  -0.06973 193 ARG A CD  
1356 N NE  . ARG A 223 ? 0.75350 0.61868 0.70443 0.08658  0.04743  -0.08287 193 ARG A NE  
1357 C CZ  . ARG A 223 ? 0.71463 0.53491 0.65259 0.08404  0.04000  -0.09409 193 ARG A CZ  
1358 N NH1 . ARG A 223 ? 0.70563 0.51578 0.62587 0.06423  0.03008  -0.09352 193 ARG A NH1 
1359 N NH2 . ARG A 223 ? 0.71847 0.50508 0.66222 0.10086  0.04256  -0.10447 193 ARG A NH2 
1360 N N   . ILE A 224 ? 0.50161 0.38240 0.50536 0.01023  0.01188  -0.02083 194 ILE A N   
1361 C CA  . ILE A 224 ? 0.46584 0.31450 0.47063 0.00470  0.00022  -0.01872 194 ILE A CA  
1362 C C   . ILE A 224 ? 0.49478 0.34477 0.50949 -0.01190 -0.00248 -0.01026 194 ILE A C   
1363 O O   . ILE A 224 ? 0.65220 0.52710 0.67801 -0.02021 0.00347  -0.00792 194 ILE A O   
1364 C CB  . ILE A 224 ? 0.56149 0.39991 0.57915 0.01616  -0.00434 -0.02222 194 ILE A CB  
1365 C CG1 . ILE A 224 ? 0.52553 0.33307 0.53954 0.01181  -0.01568 -0.02163 194 ILE A CG1 
1366 C CG2 . ILE A 224 ? 0.41662 0.28243 0.45638 0.01465  -0.00289 -0.01814 194 ILE A CG2 
1367 C CD1 . ILE A 224 ? 0.53442 0.33374 0.56099 0.01957  -0.02019 -0.02177 194 ILE A CD1 
1368 N N   . ALA A 225 ? 0.65822 0.48115 0.66960 -0.01705 -0.01120 -0.00639 195 ALA A N   
1369 C CA  . ALA A 225 ? 0.45567 0.26947 0.47729 -0.02939 -0.01348 -0.00026 195 ALA A CA  
1370 C C   . ALA A 225 ? 0.53228 0.32108 0.55548 -0.02578 -0.02366 0.00069  195 ALA A C   
1371 O O   . ALA A 225 ? 0.58668 0.36390 0.59606 -0.02160 -0.02909 0.00347  195 ALA A O   
1372 C CB  . ALA A 225 ? 0.69679 0.50906 0.70919 -0.04157 -0.00886 0.01100  195 ALA A CB  
1373 N N   . ILE A 226 ? 0.47233 0.25853 0.51216 -0.02788 -0.02604 -0.00281 196 ILE A N   
1374 C CA  . ILE A 226 ? 0.58413 0.35424 0.62893 -0.02330 -0.03445 -0.00251 196 ILE A CA  
1375 C C   . ILE A 226 ? 0.58657 0.34345 0.64262 -0.03011 -0.03299 -0.00182 196 ILE A C   
1376 O O   . ILE A 226 ? 0.64383 0.41066 0.71301 -0.03579 -0.02926 -0.01124 196 ILE A O   
1377 C CB  . ILE A 226 ? 0.41187 0.19394 0.46629 -0.01629 -0.03806 -0.00950 196 ILE A CB  
1378 C CG1 . ILE A 226 ? 0.51458 0.29989 0.55906 -0.00905 -0.03808 -0.01036 196 ILE A CG1 
1379 C CG2 . ILE A 226 ? 0.42934 0.20204 0.48967 -0.01275 -0.04597 -0.00851 196 ILE A CG2 
1380 C CD1 . ILE A 226 ? 0.38561 0.17849 0.43983 -0.00251 -0.04111 -0.01233 196 ILE A CD1 
1381 N N   . ASN A 227 ? 0.44499 0.18000 0.49611 -0.02912 -0.03574 0.00895  197 ASN A N   
1382 C CA  . ASN A 227 ? 0.53841 0.25084 0.60004 -0.03344 -0.03280 0.01136  197 ASN A CA  
1383 C C   . ASN A 227 ? 0.57119 0.27156 0.64076 -0.02117 -0.03945 0.01258  197 ASN A C   
1384 O O   . ASN A 227 ? 0.55893 0.25998 0.62014 -0.01279 -0.04655 0.02376  197 ASN A O   
1385 C CB  . ASN A 227 ? 0.66766 0.36407 0.71978 -0.04072 -0.02871 0.02815  197 ASN A CB  
1386 C CG  . ASN A 227 ? 0.93392 0.64922 0.97924 -0.05348 -0.02103 0.02767  197 ASN A CG  
1387 O OD1 . ASN A 227 ? 0.87800 0.60977 0.93274 -0.06115 -0.01629 0.01456  197 ASN A OD1 
1388 N ND2 . ASN A 227 ? 1.03592 0.75587 1.06488 -0.05557 -0.01972 0.04237  197 ASN A ND2 
1389 N N   . PRO A 228 ? 0.54464 0.23910 0.63008 -0.01986 -0.03727 0.00031  198 PRO A N   
1390 C CA  . PRO A 228 ? 0.56799 0.25441 0.66290 -0.00579 -0.04191 0.00133  198 PRO A CA  
1391 C C   . PRO A 228 ? 0.60502 0.25626 0.70397 -0.00076 -0.03916 0.01406  198 PRO A C   
1392 O O   . PRO A 228 ? 0.67995 0.30840 0.77749 -0.01154 -0.03166 0.01750  198 PRO A O   
1393 C CB  . PRO A 228 ? 0.55179 0.25077 0.66087 -0.00671 -0.03867 -0.02009 198 PRO A CB  
1394 C CG  . PRO A 228 ? 0.46744 0.16328 0.57715 -0.02355 -0.03048 -0.03015 198 PRO A CG  
1395 C CD  . PRO A 228 ? 0.74075 0.44447 0.83604 -0.03089 -0.03061 -0.01754 198 PRO A CD  
1396 N N   . ASP A 229 ? 0.57307 0.22292 0.67754 0.01606  -0.04492 0.02303  199 ASP A N   
1397 C CA  . ASP A 229 ? 0.55109 0.17399 0.65887 0.02707  -0.04144 0.03800  199 ASP A CA  
1398 C C   . ASP A 229 ? 0.62535 0.24986 0.74941 0.04430  -0.04047 0.02722  199 ASP A C   
1399 O O   . ASP A 229 ? 0.68785 0.33500 0.82083 0.05717  -0.05044 0.03088  199 ASP A O   
1400 C CB  . ASP A 229 ? 0.72709 0.35344 0.82607 0.03405  -0.05080 0.06624  199 ASP A CB  
1401 C CG  . ASP A 229 ? 0.71570 0.31490 0.81495 0.04372  -0.04561 0.08761  199 ASP A CG  
1402 O OD1 . ASP A 229 ? 0.62869 0.20950 0.73755 0.05516  -0.03826 0.08056  199 ASP A OD1 
1403 O OD2 . ASP A 229 ? 0.81764 0.41410 0.90578 0.04026  -0.04895 0.11218  199 ASP A OD2 
1404 N N   . THR A 230 ? 0.73316 0.33356 0.86156 0.04397  -0.02920 0.01325  200 THR A N   
1405 C CA  . THR A 230 ? 0.59404 0.19506 0.73855 0.06113  -0.02663 -0.00108 200 THR A CA  
1406 C C   . THR A 230 ? 0.65222 0.24042 0.80265 0.08550  -0.02781 0.01914  200 THR A C   
1407 O O   . THR A 230 ? 0.76482 0.37030 0.93206 0.10538  -0.03050 0.01466  200 THR A O   
1408 C CB  . THR A 230 ? 0.62121 0.19967 0.76648 0.05142  -0.01480 -0.02643 200 THR A CB  
1409 O OG1 . THR A 230 ? 0.73753 0.27539 0.86979 0.04218  -0.00807 -0.01603 200 THR A OG1 
1410 C CG2 . THR A 230 ? 0.58702 0.19108 0.73246 0.03115  -0.01512 -0.04785 200 THR A CG2 
1411 N N   . SER A 231 ? 0.68931 0.25137 0.82794 0.08559  -0.02615 0.04267  201 SER A N   
1412 C CA  . SER A 231 ? 0.69332 0.24510 0.83728 0.11053  -0.02779 0.06510  201 SER A CA  
1413 C C   . SER A 231 ? 0.70236 0.29781 0.85491 0.12422  -0.04208 0.08358  201 SER A C   
1414 O O   . SER A 231 ? 0.76643 0.37545 0.93361 0.14910  -0.04504 0.09165  201 SER A O   
1415 C CB  . SER A 231 ? 0.73959 0.25529 0.86846 0.10553  -0.02412 0.08834  201 SER A CB  
1416 O OG  . SER A 231 ? 0.89300 0.42529 1.00946 0.08896  -0.03011 0.10481  201 SER A OG  
1417 N N   . LYS A 232 ? 0.73167 0.35099 0.87530 0.10830  -0.05198 0.09004  202 LYS A N   
1418 C CA  . LYS A 232 ? 0.59728 0.25904 0.74453 0.11517  -0.06829 0.10516  202 LYS A CA  
1419 C C   . LYS A 232 ? 0.59435 0.29451 0.74293 0.10775  -0.07216 0.08149  202 LYS A C   
1420 O O   . LYS A 232 ? 0.58977 0.33272 0.73440 0.10789  -0.08289 0.08821  202 LYS A O   
1421 C CB  . LYS A 232 ? 0.59369 0.26647 0.71647 0.09937  -0.07479 0.12329  202 LYS A CB  
1422 C CG  . LYS A 232 ? 0.64383 0.28887 0.76273 0.10534  -0.07215 0.15325  202 LYS A CG  
1423 C CD  . LYS A 232 ? 0.70369 0.36740 0.79618 0.08790  -0.07761 0.16762  202 LYS A CD  
1424 C CE  . LYS A 232 ? 0.97215 0.61190 1.06016 0.09186  -0.07442 0.20101  202 LYS A CE  
1425 N NZ  . LYS A 232 ? 1.00773 0.67223 1.06789 0.07418  -0.07832 0.21308  202 LYS A NZ  
1426 N N   . ASN A 233 ? 0.62978 0.31784 0.78376 0.09963  -0.06384 0.05514  203 ASN A N   
1427 C CA  . ASN A 233 ? 0.63322 0.35758 0.78848 0.09174  -0.06644 0.03567  203 ASN A CA  
1428 C C   . ASN A 233 ? 0.63868 0.38613 0.77476 0.07362  -0.07489 0.04029  203 ASN A C   
1429 O O   . ASN A 233 ? 0.63573 0.41931 0.77145 0.07217  -0.08327 0.04190  203 ASN A O   
1430 C CB  . ASN A 233 ? 0.50459 0.26344 0.67764 0.11064  -0.06975 0.03474  203 ASN A CB  
1431 C CG  . ASN A 233 ? 0.47546 0.26110 0.65582 0.10556  -0.06651 0.01113  203 ASN A CG  
1432 O OD1 . ASN A 233 ? 0.57655 0.34541 0.75568 0.09602  -0.05830 -0.00816 203 ASN A OD1 
1433 N ND2 . ASN A 233 ? 0.45591 0.28874 0.64392 0.11035  -0.07318 0.01382  203 ASN A ND2 
1434 N N   . GLN A 234 ? 0.64083 0.36647 0.76145 0.05916  -0.07181 0.04160  204 GLN A N   
1435 C CA  . GLN A 234 ? 0.56914 0.30971 0.67060 0.04445  -0.07754 0.04414  204 GLN A CA  
1436 C C   . GLN A 234 ? 0.62139 0.34965 0.71590 0.02991  -0.06998 0.03060  204 GLN A C   
1437 O O   . GLN A 234 ? 0.55790 0.26809 0.66093 0.02812  -0.06133 0.02056  204 GLN A O   
1438 C CB  . GLN A 234 ? 0.51154 0.25000 0.59775 0.04440  -0.08272 0.06519  204 GLN A CB  
1439 C CG  . GLN A 234 ? 0.73644 0.49657 0.82865 0.05872  -0.09174 0.08243  204 GLN A CG  
1440 C CD  . GLN A 234 ? 0.83179 0.59333 0.90843 0.05895  -0.09620 0.10557  204 GLN A CD  
1441 O OE1 . GLN A 234 ? 0.52988 0.27120 0.59288 0.04967  -0.09074 0.10953  204 GLN A OE1 
1442 N NE2 . GLN A 234 ? 0.61248 0.40477 0.69118 0.06901  -0.10625 0.12215  204 GLN A NE2 
1443 N N   . PHE A 235 ? 0.57177 0.31182 0.65118 0.01951  -0.07314 0.02938  205 PHE A N   
1444 C CA  . PHE A 235 ? 0.55859 0.29228 0.62992 0.00835  -0.06630 0.02119  205 PHE A CA  
1445 C C   . PHE A 235 ? 0.54897 0.28967 0.60044 0.00245  -0.07006 0.02550  205 PHE A C   
1446 O O   . PHE A 235 ? 0.59865 0.35294 0.64588 0.00225  -0.07744 0.02441  205 PHE A O   
1447 C CB  . PHE A 235 ? 0.58115 0.32837 0.66290 0.00547  -0.06306 0.00547  205 PHE A CB  
1448 C CG  . PHE A 235 ? 0.58509 0.35259 0.66563 0.00520  -0.06949 0.00375  205 PHE A CG  
1449 C CD1 . PHE A 235 ? 0.75583 0.53831 0.84529 0.01080  -0.07608 0.00629  205 PHE A CD1 
1450 C CD2 . PHE A 235 ? 0.56514 0.33654 0.63717 -0.00050 -0.06816 0.00042  205 PHE A CD2 
1451 C CE1 . PHE A 235 ? 0.56846 0.36797 0.65764 0.00672  -0.08165 0.00634  205 PHE A CE1 
1452 C CE2 . PHE A 235 ? 0.51899 0.30099 0.59095 -0.00183 -0.07322 0.00027  205 PHE A CE2 
1453 C CZ  . PHE A 235 ? 0.37981 0.17512 0.46001 -0.00023 -0.08016 0.00359  205 PHE A CZ  
1454 N N   . SER A 236 ? 0.57929 0.31169 0.61858 -0.00352 -0.06447 0.02927  206 SER A N   
1455 C CA  . SER A 236 ? 0.60962 0.34955 0.62779 -0.00778 -0.06652 0.03198  206 SER A CA  
1456 C C   . SER A 236 ? 0.62452 0.36852 0.63706 -0.01253 -0.05924 0.02021  206 SER A C   
1457 O O   . SER A 236 ? 0.50513 0.24916 0.52909 -0.01432 -0.05233 0.01435  206 SER A O   
1458 C CB  . SER A 236 ? 0.51352 0.24935 0.51981 -0.00908 -0.06566 0.04902  206 SER A CB  
1459 O OG  . SER A 236 ? 1.13441 0.85586 1.14713 -0.01358 -0.05617 0.05299  206 SER A OG  
1460 N N   . LEU A 237 ? 0.69413 0.44419 0.68908 -0.01404 -0.06069 0.01584  207 LEU A N   
1461 C CA  . LEU A 237 ? 0.53201 0.28601 0.52076 -0.01413 -0.05319 0.00486  207 LEU A CA  
1462 C C   . LEU A 237 ? 0.62825 0.38996 0.59701 -0.01737 -0.04786 0.00770  207 LEU A C   
1463 O O   . LEU A 237 ? 0.60899 0.37478 0.56181 -0.01993 -0.05311 0.01380  207 LEU A O   
1464 C CB  . LEU A 237 ? 0.46116 0.21130 0.44677 -0.01180 -0.05721 -0.00632 207 LEU A CB  
1465 C CG  . LEU A 237 ? 0.50213 0.25107 0.48048 -0.00747 -0.04915 -0.01788 207 LEU A CG  
1466 C CD1 . LEU A 237 ? 0.65785 0.41581 0.65328 -0.00230 -0.04115 -0.01758 207 LEU A CD1 
1467 C CD2 . LEU A 237 ? 0.47224 0.20677 0.44649 -0.00696 -0.05360 -0.02778 207 LEU A CD2 
1468 N N   . HIS A 238 ? 0.71357 0.48430 0.68328 -0.01748 -0.03745 0.00410  208 HIS A N   
1469 C CA  . HIS A 238 ? 0.66700 0.45250 0.61886 -0.02062 -0.03029 0.00654  208 HIS A CA  
1470 C C   . HIS A 238 ? 0.70538 0.50277 0.65492 -0.01360 -0.02105 -0.00779 208 HIS A C   
1471 O O   . HIS A 238 ? 0.91626 0.71981 0.88323 -0.01020 -0.01600 -0.01049 208 HIS A O   
1472 C CB  . HIS A 238 ? 0.66131 0.45148 0.61892 -0.02952 -0.02493 0.02213  208 HIS A CB  
1473 C CG  . HIS A 238 ? 0.72680 0.50120 0.68722 -0.03278 -0.03219 0.03859  208 HIS A CG  
1474 N ND1 . HIS A 238 ? 0.66051 0.44031 0.60326 -0.03451 -0.03628 0.05281  208 HIS A ND1 
1475 C CD2 . HIS A 238 ? 0.62669 0.38225 0.60603 -0.03256 -0.03553 0.04335  208 HIS A CD2 
1476 C CE1 . HIS A 238 ? 0.61030 0.37391 0.56282 -0.03339 -0.04198 0.06835  208 HIS A CE1 
1477 N NE2 . HIS A 238 ? 0.61738 0.36381 0.59214 -0.03176 -0.04102 0.06127  208 HIS A NE2 
1478 N N   . LEU A 239 ? 0.54099 0.34440 0.46919 -0.01044 -0.01859 -0.01750 209 LEU A N   
1479 C CA  . LEU A 239 ? 0.55756 0.37068 0.48195 0.00016  -0.00814 -0.03259 209 LEU A CA  
1480 C C   . LEU A 239 ? 0.75752 0.59918 0.66341 -0.00282 0.00102  -0.03113 209 LEU A C   
1481 O O   . LEU A 239 ? 0.75983 0.60616 0.64199 -0.00675 -0.00142 -0.03453 209 LEU A O   
1482 C CB  . LEU A 239 ? 0.63643 0.42719 0.55183 0.00738  -0.01153 -0.05052 209 LEU A CB  
1483 C CG  . LEU A 239 ? 0.68042 0.46451 0.60473 0.02354  -0.00251 -0.06380 209 LEU A CG  
1484 C CD1 . LEU A 239 ? 0.55616 0.34191 0.50871 0.02814  -0.00297 -0.05317 209 LEU A CD1 
1485 C CD2 . LEU A 239 ? 0.61579 0.36793 0.52964 0.02693  -0.00589 -0.08137 209 LEU A CD2 
1486 N N   . ASN A 240 ? 1.00287 0.90509 1.12689 -0.18719 0.21192  -0.10017 210 ASN A N   
1487 C CA  . ASN A 240 ? 1.11674 1.00810 1.21151 -0.22678 0.24986  -0.11737 210 ASN A CA  
1488 C C   . ASN A 240 ? 1.06353 0.98392 1.16268 -0.21403 0.24269  -0.11965 210 ASN A C   
1489 O O   . ASN A 240 ? 1.27004 1.12804 1.31850 -0.21001 0.25005  -0.09464 210 ASN A O   
1490 C CB  . ASN A 240 ? 1.09159 1.05097 1.21984 -0.26903 0.27536  -0.16541 210 ASN A CB  
1491 C CG  . ASN A 240 ? 1.68365 1.61892 1.76728 -0.31539 0.31855  -0.18407 210 ASN A CG  
1492 O OD1 . ASN A 240 ? 2.03940 1.88005 2.05117 -0.31698 0.33361  -0.15482 210 ASN A OD1 
1493 N ND2 . ASN A 240 ? 1.74236 1.76251 1.85685 -0.34005 0.32948  -0.23309 210 ASN A ND2 
1494 N N   . SER A 241 ? 0.80316 0.81805 0.95812 -0.20379 0.22793  -0.15103 211 SER A N   
1495 C CA  . SER A 241 ? 0.81680 0.86577 0.97917 -0.19015 0.22102  -0.15893 211 SER A CA  
1496 C C   . SER A 241 ? 0.81274 0.86751 0.99505 -0.13885 0.17828  -0.14062 211 SER A C   
1497 O O   . SER A 241 ? 0.88905 0.99472 1.11040 -0.11470 0.15563  -0.15536 211 SER A O   
1498 C CB  . SER A 241 ? 1.01266 1.16328 1.21697 -0.21075 0.23580  -0.21113 211 SER A CB  
1499 O OG  . SER A 241 ? 1.29977 1.48273 1.50917 -0.19545 0.22963  -0.22013 211 SER A OG  
1500 N N   . VAL A 242 ? 0.84301 0.84349 0.99274 -0.12271 0.16897  -0.11052 212 VAL A N   
1501 C CA  . VAL A 242 ? 0.92726 0.92152 1.08731 -0.08373 0.13479  -0.09434 212 VAL A CA  
1502 C C   . VAL A 242 ? 0.85364 0.88385 1.02391 -0.06915 0.12749  -0.11138 212 VAL A C   
1503 O O   . VAL A 242 ? 0.76559 0.80954 0.92385 -0.08777 0.14793  -0.12431 212 VAL A O   
1504 C CB  . VAL A 242 ? 0.64757 0.57316 0.77064 -0.07462 0.12701  -0.05726 212 VAL A CB  
1505 C CG1 . VAL A 242 ? 0.65714 0.54653 0.76716 -0.08402 0.13387  -0.04221 212 VAL A CG1 
1506 C CG2 . VAL A 242 ? 0.75973 0.65476 0.84053 -0.08302 0.14217  -0.04794 212 VAL A CG2 
1507 N N   . THR A 243 ? 0.83040 0.86943 1.01672 -0.03590 0.10021  -0.11189 213 THR A N   
1508 C CA  . THR A 243 ? 0.65255 0.71096 0.84205 -0.01405 0.08912  -0.12598 213 THR A CA  
1509 C C   . THR A 243 ? 0.78254 0.78796 0.95361 0.00641  0.06833  -0.10271 213 THR A C   
1510 O O   . THR A 243 ? 0.71678 0.68622 0.88100 0.00597  0.06085  -0.08066 213 THR A O   
1511 C CB  . THR A 243 ? 0.43071 0.55377 0.65123 0.00992  0.07918  -0.15980 213 THR A CB  
1512 O OG1 . THR A 243 ? 0.58377 0.69618 0.81106 0.03060  0.06143  -0.15223 213 THR A OG1 
1513 C CG2 . THR A 243 ? 0.57971 0.77500 0.82430 -0.01691 0.10300  -0.19337 213 THR A CG2 
1514 N N   . PRO A 244 ? 0.72416 0.72523 0.88583 0.02127  0.06091  -0.11025 214 PRO A N   
1515 C CA  . PRO A 244 ? 0.55769 0.50854 0.70020 0.03403  0.04509  -0.09495 214 PRO A CA  
1516 C C   . PRO A 244 ? 0.60532 0.53043 0.74719 0.05321  0.03024  -0.08952 214 PRO A C   
1517 O O   . PRO A 244 ? 0.80854 0.68650 0.93210 0.05274  0.02287  -0.07467 214 PRO A O   
1518 C CB  . PRO A 244 ? 0.65688 0.61387 0.79082 0.04785  0.04252  -0.11354 214 PRO A CB  
1519 C CG  . PRO A 244 ? 0.56174 0.56361 0.70307 0.03091  0.06065  -0.12645 214 PRO A CG  
1520 C CD  . PRO A 244 ? 0.65254 0.69006 0.81544 0.01859  0.07168  -0.13260 214 PRO A CD  
1521 N N   . GLU A 245 ? 0.67338 0.63251 0.83228 0.06948  0.02708  -0.10444 215 GLU A N   
1522 C CA  . GLU A 245 ? 0.69351 0.62750 0.84436 0.09157  0.01344  -0.09830 215 GLU A CA  
1523 C C   . GLU A 245 ? 0.56069 0.47349 0.71413 0.07106  0.01565  -0.07458 215 GLU A C   
1524 O O   . GLU A 245 ? 0.65360 0.52748 0.79045 0.08219  0.00646  -0.06260 215 GLU A O   
1525 C CB  . GLU A 245 ? 0.68691 0.67853 0.85620 0.11885  0.00758  -0.12483 215 GLU A CB  
1526 C CG  . GLU A 245 ? 0.89963 0.91579 1.06323 0.15164  0.00105  -0.15204 215 GLU A CG  
1527 C CD  . GLU A 245 ? 1.29678 1.40159 1.48956 0.17474  -0.00271 -0.18705 215 GLU A CD  
1528 O OE1 . GLU A 245 ? 1.21175 1.37510 1.43894 0.14475  0.01064  -0.19710 215 GLU A OE1 
1529 O OE2 . GLU A 245 ? 1.44761 1.56397 1.62556 0.22383  -0.01832 -0.20724 215 GLU A OE2 
1530 N N   . ASP A 246 ? 0.58392 0.51538 0.75075 0.04286  0.02913  -0.06787 216 ASP A N   
1531 C CA  . ASP A 246 ? 0.63152 0.54458 0.79873 0.02764  0.03140  -0.04772 216 ASP A CA  
1532 C C   . ASP A 246 ? 0.60224 0.47529 0.75072 0.01882  0.02827  -0.02738 216 ASP A C   
1533 O O   . ASP A 246 ? 0.50596 0.36831 0.65379 0.00951  0.02917  -0.01229 216 ASP A O   
1534 C CB  . ASP A 246 ? 0.50618 0.44347 0.68354 0.00425  0.04948  -0.05041 216 ASP A CB  
1535 C CG  . ASP A 246 ? 0.52671 0.51749 0.72907 0.00456  0.05529  -0.07694 216 ASP A CG  
1536 O OD1 . ASP A 246 ? 0.52794 0.53485 0.74084 0.02684  0.04116  -0.08522 216 ASP A OD1 
1537 O OD2 . ASP A 246 ? 0.59099 0.60948 0.79895 -0.01789 0.07522  -0.09185 216 ASP A OD2 
1538 N N   . THR A 247 ? 0.71047 0.56794 0.84481 0.02169  0.02482  -0.03068 217 THR A N   
1539 C CA  . THR A 247 ? 0.48830 0.32308 0.60878 0.01097  0.02198  -0.01991 217 THR A CA  
1540 C C   . THR A 247 ? 0.58114 0.38503 0.69376 0.01141  0.01574  -0.01305 217 THR A C   
1541 O O   . THR A 247 ? 0.66681 0.43836 0.76201 0.02206  0.01224  -0.01925 217 THR A O   
1542 C CB  . THR A 247 ? 0.45532 0.28493 0.56292 0.01082  0.02157  -0.03119 217 THR A CB  
1543 O OG1 . THR A 247 ? 0.55346 0.41088 0.66333 0.00853  0.02951  -0.03607 217 THR A OG1 
1544 C CG2 . THR A 247 ? 0.46342 0.28270 0.56037 -0.00332 0.01896  -0.02804 217 THR A CG2 
1545 N N   . ALA A 248 ? 0.53633 0.34446 0.65468 0.00136  0.01591  -0.00061 218 ALA A N   
1546 C CA  . ALA A 248 ? 0.53871 0.32173 0.64891 -0.00295 0.01341  0.00557  218 ALA A CA  
1547 C C   . ALA A 248 ? 0.54022 0.34411 0.65946 -0.01580 0.01398  0.01399  218 ALA A C   
1548 O O   . ALA A 248 ? 0.53670 0.36641 0.66162 -0.01514 0.01471  0.01634  218 ALA A O   
1549 C CB  . ALA A 248 ? 0.48668 0.26073 0.59779 0.01324  0.01040  0.00776  218 ALA A CB  
1550 N N   . VAL A 249 ? 0.43350 0.22376 0.54787 -0.02457 0.01425  0.01775  219 VAL A N   
1551 C CA  . VAL A 249 ? 0.55713 0.37502 0.68206 -0.03332 0.01392  0.02196  219 VAL A CA  
1552 C C   . VAL A 249 ? 0.60796 0.42504 0.74138 -0.02438 0.01315  0.03267  219 VAL A C   
1553 O O   . VAL A 249 ? 0.67171 0.46320 0.79630 -0.02304 0.01365  0.03534  219 VAL A O   
1554 C CB  . VAL A 249 ? 0.49428 0.30818 0.60991 -0.05646 0.01848  0.01293  219 VAL A CB  
1555 C CG1 . VAL A 249 ? 0.40967 0.26966 0.54128 -0.06190 0.01686  0.01173  219 VAL A CG1 
1556 C CG2 . VAL A 249 ? 0.48050 0.29557 0.58724 -0.06929 0.02101  -0.00277 219 VAL A CG2 
1557 N N   . TYR A 250 ? 0.56031 0.39937 0.70360 -0.01670 0.01283  0.03830  220 TYR A N   
1558 C CA  . TYR A 250 ? 0.49864 0.33643 0.64927 -0.01042 0.01426  0.04514  220 TYR A CA  
1559 C C   . TYR A 250 ? 0.50237 0.35429 0.65659 -0.01297 0.01258  0.04888  220 TYR A C   
1560 O O   . TYR A 250 ? 0.51402 0.38975 0.66756 -0.01355 0.01016  0.04565  220 TYR A O   
1561 C CB  . TYR A 250 ? 0.59146 0.43008 0.74035 -0.00426 0.02037  0.04725  220 TYR A CB  
1562 C CG  . TYR A 250 ? 0.67652 0.51238 0.82635 -0.00478 0.02479  0.03913  220 TYR A CG  
1563 C CD1 . TYR A 250 ? 0.54095 0.37791 0.68238 -0.00511 0.02472  0.03499  220 TYR A CD1 
1564 C CD2 . TYR A 250 ? 0.57002 0.41200 0.73108 -0.00452 0.02886  0.03127  220 TYR A CD2 
1565 C CE1 . TYR A 250 ? 0.56792 0.40851 0.71133 -0.00483 0.02928  0.02486  220 TYR A CE1 
1566 C CE2 . TYR A 250 ? 0.51709 0.37148 0.68300 -0.00412 0.03298  0.01793  220 TYR A CE2 
1567 C CZ  . TYR A 250 ? 0.55316 0.40499 0.70983 -0.00411 0.03353  0.01559  220 TYR A CZ  
1568 O OH  . TYR A 250 ? 0.46674 0.33656 0.62923 -0.00298 0.03818  -0.00016 220 TYR A OH  
1569 N N   . PHE A 251 ? 0.48441 0.32967 0.64293 -0.01221 0.01310  0.05250  221 PHE A N   
1570 C CA  . PHE A 251 ? 0.47650 0.33707 0.63915 -0.01455 0.01256  0.05449  221 PHE A CA  
1571 C C   . PHE A 251 ? 0.46541 0.32338 0.63338 -0.00556 0.01421  0.05869  221 PHE A C   
1572 O O   . PHE A 251 ? 0.62317 0.47013 0.79373 -0.00314 0.01619  0.05710  221 PHE A O   
1573 C CB  . PHE A 251 ? 0.52390 0.37310 0.67828 -0.02861 0.01469  0.05292  221 PHE A CB  
1574 C CG  . PHE A 251 ? 0.50734 0.34961 0.65031 -0.04534 0.01818  0.04504  221 PHE A CG  
1575 C CD1 . PHE A 251 ? 0.52333 0.40333 0.67356 -0.05971 0.02018  0.03387  221 PHE A CD1 
1576 C CD2 . PHE A 251 ? 0.61211 0.41333 0.73546 -0.04598 0.01996  0.04479  221 PHE A CD2 
1577 C CE1 . PHE A 251 ? 0.63217 0.50952 0.77256 -0.08165 0.02628  0.02099  221 PHE A CE1 
1578 C CE2 . PHE A 251 ? 0.57240 0.35751 0.67951 -0.06443 0.02611  0.03552  221 PHE A CE2 
1579 C CZ  . PHE A 251 ? 0.68473 0.50803 0.80144 -0.08601 0.03051  0.02281  221 PHE A CZ  
1580 N N   . CYS A 252 ? 0.38424 0.25788 0.55402 -0.00045 0.01375  0.05996  222 CYS A N   
1581 C CA  . CYS A 252 ? 0.37963 0.24804 0.55170 0.00538  0.01653  0.06172  222 CYS A CA  
1582 C C   . CYS A 252 ? 0.51160 0.39908 0.68942 0.00138  0.01443  0.06046  222 CYS A C   
1583 O O   . CYS A 252 ? 0.64042 0.55468 0.82027 -0.00134 0.01252  0.05622  222 CYS A O   
1584 C CB  . CYS A 252 ? 0.51406 0.37069 0.67187 0.01957  0.02056  0.06421  222 CYS A CB  
1585 S SG  . CYS A 252 ? 0.86825 0.75196 1.01483 0.03933  0.01304  0.06318  222 CYS A SG  
1586 N N   . ALA A 253 ? 0.33107 0.21173 0.51141 0.00003  0.01558  0.06081  223 ALA A N   
1587 C CA  . ALA A 253 ? 0.32066 0.21458 0.50084 -0.00531 0.01577  0.06031  223 ALA A CA  
1588 C C   . ALA A 253 ? 0.39400 0.28963 0.57864 0.00234  0.01669  0.05850  223 ALA A C   
1589 O O   . ALA A 253 ? 0.43422 0.31821 0.62159 0.00653  0.01858  0.05544  223 ALA A O   
1590 C CB  . ALA A 253 ? 0.33798 0.21222 0.50263 -0.01582 0.01691  0.06310  223 ALA A CB  
1591 N N   . ARG A 254 ? 0.31694 0.23064 0.50216 0.00047  0.01753  0.05691  224 ARG A N   
1592 C CA  . ARG A 254 ? 0.42872 0.34698 0.61708 0.00686  0.01850  0.05324  224 ARG A CA  
1593 C C   . ARG A 254 ? 0.48639 0.40101 0.66511 0.00234  0.01769  0.05481  224 ARG A C   
1594 O O   . ARG A 254 ? 0.42232 0.33028 0.58530 -0.00759 0.01998  0.05975  224 ARG A O   
1595 C CB  . ARG A 254 ? 0.39258 0.33678 0.58493 0.01369  0.01943  0.04844  224 ARG A CB  
1596 C CG  . ARG A 254 ? 0.44095 0.38625 0.63436 0.02130  0.02132  0.04289  224 ARG A CG  
1597 C CD  . ARG A 254 ? 0.44898 0.42493 0.64484 0.03192  0.02126  0.03601  224 ARG A CD  
1598 N NE  . ARG A 254 ? 0.39221 0.40354 0.59212 0.01707  0.02309  0.03329  224 ARG A NE  
1599 C CZ  . ARG A 254 ? 0.43027 0.48507 0.63686 0.02090  0.02446  0.02241  224 ARG A CZ  
1600 N NH1 . ARG A 254 ? 0.35125 0.41627 0.55890 0.04703  0.02090  0.01472  224 ARG A NH1 
1601 N NH2 . ARG A 254 ? 0.65671 0.74152 0.86358 -0.00136 0.03140  0.01753  224 ARG A NH2 
1602 N N   . VAL A 255 ? 0.43517 0.35109 0.61721 0.00937  0.01605  0.04886  225 VAL A N   
1603 C CA  . VAL A 255 ? 0.45907 0.37571 0.62662 0.01396  0.01268  0.04869  225 VAL A CA  
1604 C C   . VAL A 255 ? 0.50995 0.44722 0.68465 0.01667  0.01421  0.04040  225 VAL A C   
1605 O O   . VAL A 255 ? 0.52750 0.47212 0.71764 0.01825  0.01609  0.02873  225 VAL A O   
1606 C CB  . VAL A 255 ? 0.37515 0.28976 0.54066 0.02497  0.00603  0.04252  225 VAL A CB  
1607 C CG1 . VAL A 255 ? 0.49814 0.42554 0.64936 0.03906  -0.00017 0.03675  225 VAL A CG1 
1608 C CG2 . VAL A 255 ? 0.41798 0.30565 0.56522 0.02678  0.00386  0.05175  225 VAL A CG2 
1609 N N   . ILE A 256 ? 0.52692 0.46934 0.68624 0.01409  0.01632  0.04480  226 ILE A N   
1610 C CA  . ILE A 256 ? 0.60875 0.57246 0.77109 0.01783  0.01737  0.03647  226 ILE A CA  
1611 C C   . ILE A 256 ? 0.63740 0.60067 0.77852 0.02878  0.01141  0.03515  226 ILE A C   
1612 O O   . ILE A 256 ? 0.61032 0.54839 0.71752 0.03184  0.01071  0.04703  226 ILE A O   
1613 C CB  . ILE A 256 ? 0.49604 0.47532 0.65452 0.00868  0.02458  0.03853  226 ILE A CB  
1614 C CG1 . ILE A 256 ? 0.39048 0.38241 0.56878 0.00795  0.02648  0.03525  226 ILE A CG1 
1615 C CG2 . ILE A 256 ? 0.44342 0.44508 0.60247 0.01397  0.02569  0.02925  226 ILE A CG2 
1616 C CD1 . ILE A 256 ? 0.76858 0.79660 0.95049 0.00213  0.03223  0.02906  226 ILE A CD1 
1617 N N   . SER A 257 ? 0.69197 0.67984 0.84683 0.03631  0.00783  0.01895  227 SER A N   
1618 C CA  . SER A 257 ? 0.62874 0.63042 0.76609 0.05334  -0.00147 0.01191  227 SER A CA  
1619 C C   . SER A 257 ? 0.62094 0.61031 0.71753 0.05956  -0.00047 0.02421  227 SER A C   
1620 O O   . SER A 257 ? 0.64760 0.61786 0.70362 0.07815  -0.00703 0.03181  227 SER A O   
1621 C CB  . SER A 257 ? 0.64286 0.68380 0.80725 0.05399  -0.00301 -0.01466 227 SER A CB  
1622 O OG  . SER A 257 ? 1.00004 1.04673 1.17380 0.04459  0.00504  -0.01966 227 SER A OG  
1623 N N   . VAL A 258 ? 0.53652 0.53347 0.63666 0.04642  0.00879  0.02560  228 VAL A N   
1624 C CA  . VAL A 258 ? 0.58132 0.56751 0.64015 0.04633  0.01441  0.03529  228 VAL A CA  
1625 C C   . VAL A 258 ? 0.71830 0.65934 0.73953 0.03132  0.02580  0.05485  228 VAL A C   
1626 O O   . VAL A 258 ? 0.61038 0.52637 0.58302 0.02672  0.03545  0.06470  228 VAL A O   
1627 C CB  . VAL A 258 ? 0.42924 0.44857 0.50652 0.03652  0.02184  0.02509  228 VAL A CB  
1628 C CG1 . VAL A 258 ? 0.50648 0.56033 0.61258 0.04764  0.01418  0.00325  228 VAL A CG1 
1629 C CG2 . VAL A 258 ? 0.40415 0.43184 0.50927 0.01918  0.03063  0.02488  228 VAL A CG2 
1630 N N   . ALA A 259 ? 0.76957 0.69601 0.80688 0.02074  0.02751  0.05921  229 ALA A N   
1631 C CA  . ALA A 259 ? 0.55012 0.43334 0.55300 0.00124  0.04047  0.07281  229 ALA A CA  
1632 C C   . ALA A 259 ? 0.67243 0.50116 0.63433 0.01790  0.03468  0.08438  229 ALA A C   
1633 O O   . ALA A 259 ? 0.67237 0.47290 0.63018 0.00599  0.03946  0.08966  229 ALA A O   
1634 C CB  . ALA A 259 ? 0.52745 0.43538 0.57141 -0.02008 0.04611  0.06672  229 ALA A CB  
1635 N N   . GLY A 260 ? 0.68217 0.49892 0.61137 0.04932  0.02326  0.08596  230 GLY A N   
1636 C CA  . GLY A 260 ? 0.62447 0.39083 0.50664 0.07570  0.01548  0.09492  230 GLY A CA  
1637 C C   . GLY A 260 ? 0.60156 0.39165 0.52748 0.08655  0.00243  0.08499  230 GLY A C   
1638 O O   . GLY A 260 ? 0.88429 0.63279 0.77508 0.10595  -0.00253 0.09117  230 GLY A O   
1639 N N   . TYR A 261 ? 0.50830 0.35818 0.50336 0.07511  -0.00137 0.06927  231 TYR A N   
1640 C CA  . TYR A 261 ? 0.46970 0.34172 0.50517 0.07844  -0.00892 0.05854  231 TYR A CA  
1641 C C   . TYR A 261 ? 0.48289 0.31170 0.50546 0.06666  -0.00262 0.07053  231 TYR A C   
1642 O O   . TYR A 261 ? 0.48110 0.30719 0.50872 0.07956  -0.00991 0.06624  231 TYR A O   
1643 C CB  . TYR A 261 ? 0.57775 0.47732 0.61062 0.11239  -0.02528 0.04322  231 TYR A CB  
1644 C CG  . TYR A 261 ? 0.60712 0.57122 0.67691 0.11524  -0.03076 0.01958  231 TYR A CG  
1645 C CD1 . TYR A 261 ? 0.57747 0.58318 0.70143 0.09835  -0.02787 -0.00074 231 TYR A CD1 
1646 C CD2 . TYR A 261 ? 0.47331 0.45137 0.51753 0.13258  -0.03624 0.01616  231 TYR A CD2 
1647 C CE1 . TYR A 261 ? 0.59825 0.65564 0.75115 0.09439  -0.02832 -0.02614 231 TYR A CE1 
1648 C CE2 . TYR A 261 ? 0.50222 0.54216 0.58081 0.13235  -0.04026 -0.00972 231 TYR A CE2 
1649 C CZ  . TYR A 261 ? 0.67806 0.75649 0.81161 0.11111  -0.03532 -0.03198 231 TYR A CZ  
1650 O OH  . TYR A 261 ? 0.60811 0.74084 0.77114 0.10447  -0.03486 -0.06127 231 TYR A OH  
1651 N N   . ALA A 262 ? 0.49774 0.29933 0.50502 0.04031  0.01191  0.08161  232 ALA A N   
1652 C CA  . ALA A 262 ? 0.51743 0.27978 0.50930 0.02354  0.02060  0.08918  232 ALA A CA  
1653 C C   . ALA A 262 ? 0.46266 0.26413 0.50677 0.00098  0.02420  0.08192  232 ALA A C   
1654 O O   . ALA A 262 ? 0.46274 0.30627 0.53899 -0.00610 0.02536  0.07518  232 ALA A O   
1655 C CB  . ALA A 262 ? 0.58692 0.29112 0.51797 0.00455  0.03837  0.10119  232 ALA A CB  
1656 N N   . PHE A 263 ? 0.46273 0.24776 0.50944 -0.00557 0.02517  0.08266  233 PHE A N   
1657 C CA  . PHE A 263 ? 0.46111 0.27954 0.54713 -0.02108 0.02709  0.07612  233 PHE A CA  
1658 C C   . PHE A 263 ? 0.58804 0.41787 0.66914 -0.04934 0.04070  0.07299  233 PHE A C   
1659 O O   . PHE A 263 ? 0.56485 0.36272 0.61706 -0.07046 0.05237  0.07380  233 PHE A O   
1660 C CB  . PHE A 263 ? 0.49555 0.29519 0.58185 -0.01883 0.02402  0.07616  233 PHE A CB  
1661 C CG  . PHE A 263 ? 0.50089 0.29445 0.58774 0.00698  0.01290  0.07456  233 PHE A CG  
1662 C CD1 . PHE A 263 ? 0.46024 0.28982 0.58452 0.01404  0.00738  0.06583  233 PHE A CD1 
1663 C CD2 . PHE A 263 ? 0.60358 0.35485 0.64813 0.02485  0.00963  0.07907  233 PHE A CD2 
1664 C CE1 . PHE A 263 ? 0.48522 0.32407 0.61490 0.03207  -0.00011 0.05716  233 PHE A CE1 
1665 C CE2 . PHE A 263 ? 0.64443 0.40789 0.69359 0.05279  -0.00246 0.07122  233 PHE A CE2 
1666 C CZ  . PHE A 263 ? 0.43037 0.24539 0.52728 0.05318  -0.00679 0.05799  233 PHE A CZ  
1667 N N   . ASP A 264 ? 0.56215 0.43972 0.67005 -0.05116 0.04096  0.06569  234 ASP A N   
1668 C CA  . ASP A 264 ? 0.59592 0.50279 0.70366 -0.07684 0.05403  0.05640  234 ASP A CA  
1669 C C   . ASP A 264 ? 0.61905 0.57692 0.75916 -0.08408 0.05291  0.04213  234 ASP A C   
1670 O O   . ASP A 264 ? 0.64194 0.62599 0.78015 -0.11242 0.06562  0.02875  234 ASP A O   
1671 C CB  . ASP A 264 ? 0.60447 0.54252 0.72018 -0.07099 0.05465  0.05267  234 ASP A CB  
1672 C CG  . ASP A 264 ? 0.69048 0.65611 0.83933 -0.04309 0.04079  0.04959  234 ASP A CG  
1673 O OD1 . ASP A 264 ? 0.51860 0.52023 0.69290 -0.03614 0.03687  0.04063  234 ASP A OD1 
1674 O OD2 . ASP A 264 ? 0.93974 0.88866 1.08372 -0.02743 0.03490  0.05427  234 ASP A OD2 
1675 N N   . ILE A 265 ? 0.44026 0.41388 0.60546 -0.05978 0.03957  0.04223  235 ILE A N   
1676 C CA  . ILE A 265 ? 0.40622 0.42698 0.59390 -0.05536 0.03516  0.02965  235 ILE A CA  
1677 C C   . ILE A 265 ? 0.33392 0.32648 0.52129 -0.04266 0.02737  0.03726  235 ILE A C   
1678 O O   . ILE A 265 ? 0.32393 0.29275 0.51229 -0.02220 0.02106  0.04604  235 ILE A O   
1679 C CB  . ILE A 265 ? 0.32352 0.38974 0.52982 -0.03066 0.02816  0.02137  235 ILE A CB  
1680 C CG1 . ILE A 265 ? 0.34744 0.45722 0.55821 -0.04572 0.03693  0.00837  235 ILE A CG1 
1681 C CG2 . ILE A 265 ? 0.31707 0.42201 0.53498 -0.01153 0.01941  0.01100  235 ILE A CG2 
1682 C CD1 . ILE A 265 ? 0.56727 0.72270 0.79323 -0.01719 0.02971  -0.00229 235 ILE A CD1 
1683 N N   . TRP A 266 ? 0.40295 0.39974 0.58785 -0.05845 0.03026  0.03091  236 TRP A N   
1684 C CA  . TRP A 266 ? 0.46676 0.43883 0.64911 -0.04971 0.02452  0.03643  236 TRP A CA  
1685 C C   . TRP A 266 ? 0.32873 0.34507 0.52473 -0.03241 0.01634  0.02705  236 TRP A C   
1686 O O   . TRP A 266 ? 0.34429 0.41448 0.55183 -0.02406 0.01354  0.01421  236 TRP A O   
1687 C CB  . TRP A 266 ? 0.40581 0.34478 0.56894 -0.07507 0.03304  0.03511  236 TRP A CB  
1688 C CG  . TRP A 266 ? 0.39569 0.27510 0.52975 -0.07913 0.03862  0.04749  236 TRP A CG  
1689 C CD1 . TRP A 266 ? 0.41624 0.28324 0.53304 -0.08813 0.04654  0.05059  236 TRP A CD1 
1690 C CD2 . TRP A 266 ? 0.46395 0.29025 0.57709 -0.06869 0.03570  0.05693  236 TRP A CD2 
1691 N NE1 . TRP A 266 ? 0.45064 0.25568 0.53181 -0.08018 0.04754  0.06302  236 TRP A NE1 
1692 C CE2 . TRP A 266 ? 0.44894 0.23152 0.52894 -0.06642 0.04007  0.06572  236 TRP A CE2 
1693 C CE3 . TRP A 266 ? 0.40745 0.22213 0.52424 -0.05807 0.02952  0.05722  236 TRP A CE3 
1694 C CZ2 . TRP A 266 ? 0.47992 0.21103 0.52970 -0.04804 0.03601  0.07342  236 TRP A CZ2 
1695 C CZ3 . TRP A 266 ? 0.43247 0.20052 0.52530 -0.04463 0.02705  0.06333  236 TRP A CZ3 
1696 C CH2 . TRP A 266 ? 0.65052 0.37879 0.70984 -0.03691 0.02911  0.07071  236 TRP A CH2 
1697 N N   . GLY A 267 ? 0.32907 0.32434 0.51965 -0.02304 0.01194  0.03223  237 GLY A N   
1698 C CA  . GLY A 267 ? 0.32997 0.35421 0.52071 -0.00063 0.00376  0.02677  237 GLY A CA  
1699 C C   . GLY A 267 ? 0.37916 0.43908 0.57464 -0.01518 0.00304  0.01085  237 GLY A C   
1700 O O   . GLY A 267 ? 0.34217 0.40756 0.54109 -0.04801 0.01191  0.00051  237 GLY A O   
1701 N N   . GLN A 268 ? 0.58675 0.66580 0.77552 0.00947  -0.00595 0.00790  238 GLN A N   
1702 C CA  . GLN A 268 ? 0.59644 0.72065 0.79072 -0.00031 -0.00878 -0.01131 238 GLN A CA  
1703 C C   . GLN A 268 ? 0.57497 0.65301 0.76350 -0.02726 -0.00103 -0.00714 238 GLN A C   
1704 O O   . GLN A 268 ? 0.36085 0.45048 0.55436 -0.06098 0.00753  -0.02295 238 GLN A O   
1705 C CB  . GLN A 268 ? 0.36047 0.50938 0.53908 0.04092  -0.02189 -0.01285 238 GLN A CB  
1706 C CG  . GLN A 268 ? 0.51473 0.69580 0.68585 0.07999  -0.03109 -0.01546 238 GLN A CG  
1707 C CD  . GLN A 268 ? 1.16928 1.44950 1.36830 0.07376  -0.03534 -0.04731 238 GLN A CD  
1708 O OE1 . GLN A 268 ? 1.05291 1.39494 1.26953 0.05271  -0.03566 -0.07291 238 GLN A OE1 
1709 N NE2 . GLN A 268 ? 0.66613 0.96677 0.87008 0.08936  -0.03695 -0.04984 238 GLN A NE2 
1710 N N   . GLY A 269 ? 0.37235 0.39579 0.54659 -0.01385 -0.00173 0.01154  239 GLY A N   
1711 C CA  . GLY A 269 ? 0.38236 0.36661 0.54979 -0.03057 0.00338  0.01362  239 GLY A CA  
1712 C C   . GLY A 269 ? 0.52182 0.51676 0.68073 -0.01843 -0.00183 0.00948  239 GLY A C   
1713 O O   . GLY A 269 ? 0.62803 0.66806 0.79162 -0.02638 -0.00468 -0.00974 239 GLY A O   
1714 N N   . THR A 270 ? 0.42701 0.38484 0.57228 -0.00169 -0.00143 0.02439  240 THR A N   
1715 C CA  . THR A 270 ? 0.68185 0.64155 0.81137 0.01086  -0.00406 0.02328  240 THR A CA  
1716 C C   . THR A 270 ? 0.54812 0.47737 0.67768 -0.00489 0.00147  0.02175  240 THR A C   
1717 O O   . THR A 270 ? 0.50923 0.40412 0.64294 -0.01176 0.00680  0.02837  240 THR A O   
1718 C CB  . THR A 270 ? 0.67310 0.60564 0.77632 0.03768  -0.00235 0.03910  240 THR A CB  
1719 O OG1 . THR A 270 ? 0.89750 0.81924 0.97782 0.04625  -0.00092 0.04029  240 THR A OG1 
1720 C CG2 . THR A 270 ? 0.53887 0.42681 0.64456 0.03023  0.00767  0.05116  240 THR A CG2 
1721 N N   . MET A 271 ? 0.62013 0.56732 0.74382 -0.00678 -0.00108 0.01026  241 MET A N   
1722 C CA  . MET A 271 ? 0.56750 0.48904 0.68816 -0.01792 0.00338  0.00545  241 MET A CA  
1723 C C   . MET A 271 ? 0.60384 0.51176 0.70805 -0.00189 0.00600  0.01380  241 MET A C   
1724 O O   . MET A 271 ? 0.73479 0.66267 0.82157 0.01279  0.00233  0.01316  241 MET A O   
1725 C CB  . MET A 271 ? 0.60019 0.54734 0.72256 -0.03538 0.00204  -0.01626 241 MET A CB  
1726 C CG  . MET A 271 ? 0.64179 0.56358 0.75478 -0.04103 0.00567  -0.02340 241 MET A CG  
1727 S SD  . MET A 271 ? 0.90457 0.76165 1.01201 -0.04671 0.01285  -0.01755 241 MET A SD  
1728 C CE  . MET A 271 ? 0.46778 0.31036 0.56241 -0.04485 0.01459  -0.03079 241 MET A CE  
1729 N N   . VAL A 272 ? 0.61643 0.49351 0.72257 -0.00399 0.01322  0.01928  242 VAL A N   
1730 C CA  . VAL A 272 ? 0.73949 0.60437 0.83068 0.00242  0.02151  0.02318  242 VAL A CA  
1731 C C   . VAL A 272 ? 0.56221 0.42609 0.65717 -0.00341 0.02287  0.01021  242 VAL A C   
1732 O O   . VAL A 272 ? 0.49711 0.35004 0.60466 -0.00771 0.02122  0.00346  242 VAL A O   
1733 C CB  . VAL A 272 ? 0.68221 0.52730 0.77577 0.00119  0.03155  0.03132  242 VAL A CB  
1734 C CG1 . VAL A 272 ? 0.64074 0.47376 0.71538 -0.00136 0.04628  0.03076  242 VAL A CG1 
1735 C CG2 . VAL A 272 ? 0.77307 0.61191 0.85892 0.00865  0.03059  0.04313  242 VAL A CG2 
1736 N N   . THR A 273 ? 0.59528 0.46656 0.67274 0.00051  0.02578  0.00670  243 THR A N   
1737 C CA  . THR A 273 ? 0.47232 0.34588 0.55080 -0.00278 0.02747  -0.00752 243 THR A CA  
1738 C C   . THR A 273 ? 0.65049 0.52161 0.71584 -0.00188 0.04100  -0.00676 243 THR A C   
1739 O O   . THR A 273 ? 0.75996 0.62487 0.79673 0.00241  0.04787  0.00326  243 THR A O   
1740 C CB  . THR A 273 ? 0.57750 0.46999 0.64713 -0.00382 0.02000  -0.01879 243 THR A CB  
1741 O OG1 . THR A 273 ? 0.58444 0.48110 0.66614 -0.01410 0.01290  -0.02550 243 THR A OG1 
1742 C CG2 . THR A 273 ? 0.77655 0.66718 0.84355 -0.00601 0.02281  -0.03443 243 THR A CG2 
1743 N N   . VAL A 274 ? 0.74960 0.62473 0.83021 -0.00462 0.04609  -0.01909 244 VAL A N   
1744 C CA  . VAL A 274 ? 0.58053 0.46504 0.65430 -0.01048 0.06246  -0.02616 244 VAL A CA  
1745 C C   . VAL A 274 ? 0.80826 0.70602 0.87483 -0.00724 0.06150  -0.04055 244 VAL A C   
1746 O O   . VAL A 274 ? 0.95868 0.86579 1.04159 -0.00062 0.05529  -0.05716 244 VAL A O   
1747 C CB  . VAL A 274 ? 0.53401 0.43497 0.63400 -0.01381 0.06826  -0.03841 244 VAL A CB  
1748 C CG1 . VAL A 274 ? 0.76360 0.68576 0.85903 -0.02773 0.08961  -0.05246 244 VAL A CG1 
1749 C CG2 . VAL A 274 ? 0.53457 0.42323 0.64184 -0.01731 0.06806  -0.02593 244 VAL A CG2 
1750 N N   . SER A 275 ? 1.10320 0.99795 1.13891 -0.00788 0.06738  -0.03451 245 SER A N   
1751 C CA  . SER A 275 ? 1.15491 1.06444 1.18028 -0.00512 0.06689  -0.04834 245 SER A CA  
1752 C C   . SER A 275 ? 1.37184 1.27660 1.35959 -0.01058 0.08603  -0.04328 245 SER A C   
1753 O O   . SER A 275 ? 1.28455 1.16229 1.24285 -0.01374 0.09782  -0.02551 245 SER A O   
1754 C CB  . SER A 275 ? 1.22424 1.13796 1.24408 0.00179  0.05008  -0.05012 245 SER A CB  
1755 O OG  . SER A 275 ? 1.32713 1.25620 1.33587 0.00347  0.05010  -0.06591 245 SER A OG  
1756 N N   . SER A 276 ? 1.33890 1.26241 1.32045 -0.01144 0.09105  -0.05925 246 SER A N   
1757 C CA  . SER A 276 ? 1.22478 1.14086 1.16351 -0.01890 0.11235  -0.05619 246 SER A CA  
1758 C C   . SER A 276 ? 1.19278 1.11293 1.09856 -0.00487 0.10327  -0.05528 246 SER A C   
1759 O O   . SER A 276 ? 1.13421 1.06750 1.05368 0.00701  0.08135  -0.05883 246 SER A O   
1760 C CB  . SER A 276 ? 1.15017 1.09586 1.10701 -0.03403 0.13036  -0.07995 246 SER A CB  
1761 O OG  . SER A 276 ? 1.17660 1.15427 1.16338 -0.02251 0.11556  -0.10282 246 SER A OG  
1762 N N   . PHE B 17  ? 0.97869 1.40698 0.83292 0.41665  0.18208  -0.12443 338 PHE C N   
1763 C CA  . PHE B 17  ? 1.30481 1.74409 1.16055 0.41470  0.14562  -0.06618 338 PHE C CA  
1764 C C   . PHE B 17  ? 1.40502 1.77688 1.33865 0.39748  0.11140  -0.02536 338 PHE C C   
1765 O O   . PHE B 17  ? 1.42172 1.77158 1.33778 0.37881  0.07003  -0.01282 338 PHE C O   
1766 C CB  . PHE B 17  ? 1.35804 1.85117 1.21448 0.44287  0.17236  -0.01598 338 PHE C CB  
1767 C CG  . PHE B 17  ? 1.46623 2.02656 1.22470 0.45265  0.17358  -0.02832 338 PHE C CG  
1768 C CD1 . PHE B 17  ? 1.59942 2.19498 1.28287 0.46089  0.20584  -0.08261 338 PHE C CD1 
1769 C CD2 . PHE B 17  ? 1.42657 2.01206 1.16836 0.45303  0.13989  0.01460  338 PHE C CD2 
1770 C CE1 . PHE B 17  ? 1.49656 2.15301 1.08538 0.46805  0.19892  -0.09036 338 PHE C CE1 
1771 C CE2 . PHE B 17  ? 1.54708 2.19483 1.20648 0.46244  0.13562  0.00914  338 PHE C CE2 
1772 C CZ  . PHE B 17  ? 1.58451 2.26874 1.16498 0.46934  0.16243  -0.04157 338 PHE C CZ  
1773 N N   . GLY B 18  ? 1.40865 1.74630 1.42855 0.40349  0.12872  -0.00499 339 GLY C N   
1774 C CA  . GLY B 18  ? 1.39899 1.67062 1.49207 0.38601  0.09013  0.03704  339 GLY C CA  
1775 C C   . GLY B 18  ? 1.48042 1.69102 1.54924 0.35420  0.05671  0.00326  339 GLY C C   
1776 O O   . GLY B 18  ? 1.54347 1.70040 1.62787 0.33308  0.01355  0.03509  339 GLY C O   
1777 N N   . GLU B 19  ? 1.40080 1.61574 1.42792 0.34862  0.07646  -0.06146 340 GLU C N   
1778 C CA  . GLU B 19  ? 1.34306 1.50206 1.34915 0.31744  0.05072  -0.09419 340 GLU C CA  
1779 C C   . GLU B 19  ? 1.39634 1.56166 1.32913 0.29866  0.02034  -0.10099 340 GLU C C   
1780 O O   . GLU B 19  ? 1.41290 1.52668 1.32828 0.27022  -0.00155 -0.11737 340 GLU C O   
1781 C CB  . GLU B 19  ? 1.32585 1.48844 1.32002 0.31675  0.08254  -0.16279 340 GLU C CB  
1782 C CG  . GLU B 19  ? 1.56573 1.71254 1.64100 0.33450  0.11792  -0.16378 340 GLU C CG  
1783 C CD  . GLU B 19  ? 1.86931 2.01735 1.92883 0.33426  0.15201  -0.23810 340 GLU C CD  
1784 O OE1 . GLU B 19  ? 1.74505 1.91670 1.72707 0.32172  0.14715  -0.28799 340 GLU C OE1 
1785 O OE2 . GLU B 19  ? 2.02200 2.14657 2.15366 0.34633  0.18312  -0.24752 340 GLU C OE2 
1786 N N   . VAL B 20  ? 1.30750 1.53305 1.20146 0.31396  0.02105  -0.08717 341 VAL C N   
1787 C CA  . VAL B 20  ? 1.23559 1.47217 1.07504 0.30047  -0.00460 -0.09048 341 VAL C CA  
1788 C C   . VAL B 20  ? 1.29003 1.50632 1.14772 0.30023  -0.03211 -0.02930 341 VAL C C   
1789 O O   . VAL B 20  ? 1.43358 1.60543 1.27083 0.27752  -0.05939 -0.02403 341 VAL C O   
1790 C CB  . VAL B 20  ? 1.27203 1.59066 1.05578 0.31602  0.00983  -0.12199 341 VAL C CB  
1791 C CG1 . VAL B 20  ? 1.38686 1.71825 1.13314 0.30325  -0.01616 -0.12489 341 VAL C CG1 
1792 C CG2 . VAL B 20  ? 1.09469 1.42822 0.85663 0.31334  0.03321  -0.18766 341 VAL C CG2 
1793 N N   . PHE B 21  ? 1.18549 1.43124 1.08193 0.32441  -0.02276 0.01626  342 PHE C N   
1794 C CA  . PHE B 21  ? 1.23934 1.46561 1.16209 0.32403  -0.05005 0.07441  342 PHE C CA  
1795 C C   . PHE B 21  ? 1.26706 1.41121 1.23977 0.30406  -0.07831 0.10392  342 PHE C C   
1796 O O   . PHE B 21  ? 1.29726 1.38798 1.25033 0.28169  -0.11338 0.11846  342 PHE C O   
1797 C CB  . PHE B 21  ? 1.12056 1.40636 1.07586 0.35504  -0.02937 0.11652  342 PHE C CB  
1798 C CG  . PHE B 21  ? 1.10616 1.46790 1.00404 0.37265  -0.01395 0.10272  342 PHE C CG  
1799 C CD1 . PHE B 21  ? 1.29555 1.67548 1.18005 0.37576  -0.03481 0.13274  342 PHE C CD1 
1800 C CD2 . PHE B 21  ? 1.10796 1.51996 0.96534 0.38541  0.01867  0.05981  342 PHE C CD2 
1801 C CE1 . PHE B 21  ? 1.26261 1.71256 1.10053 0.39219  -0.02614 0.12590  342 PHE C CE1 
1802 C CE2 . PHE B 21  ? 1.37765 1.85824 1.17668 0.39965  0.02500  0.05037  342 PHE C CE2 
1803 C CZ  . PHE B 21  ? 1.35447 1.85561 1.14681 0.40351  0.00119  0.08633  342 PHE C CZ  
1804 N N   . ASN B 22  ? 1.22346 1.35456 1.26052 0.31146  -0.06412 0.11290  343 ASN C N   
1805 C CA  . ASN B 22  ? 1.27936 1.33596 1.37619 0.29391  -0.09635 0.14700  343 ASN C CA  
1806 C C   . ASN B 22  ? 1.26018 1.25102 1.32750 0.26476  -0.11196 0.11325  343 ASN C C   
1807 O O   . ASN B 22  ? 1.51004 1.45504 1.63603 0.25786  -0.12108 0.12570  343 ASN C O   
1808 C CB  . ASN B 22  ? 1.28918 1.36376 1.48730 0.31666  -0.07337 0.17659  343 ASN C CB  
1809 C CG  . ASN B 22  ? 1.34622 1.48026 1.58050 0.34307  -0.05621 0.21877  343 ASN C CG  
1810 O OD1 . ASN B 22  ? 1.30360 1.44173 1.51272 0.33916  -0.08058 0.24536  343 ASN C OD1 
1811 N ND2 . ASN B 22  ? 1.26408 1.44206 1.55975 0.37005  -0.01046 0.22522  343 ASN C ND2 
1812 N N   . ALA B 23  ? 1.16705 1.15234 1.15157 0.24731  -0.11446 0.07349  344 ALA C N   
1813 C CA  . ALA B 23  ? 1.24152 1.16322 1.19425 0.21717  -0.12594 0.04439  344 ALA C CA  
1814 C C   . ALA B 23  ? 1.37648 1.21129 1.31704 0.18788  -0.17371 0.08343  344 ALA C C   
1815 O O   . ALA B 23  ? 1.51710 1.34325 1.43994 0.18515  -0.19742 0.11406  344 ALA C O   
1816 C CB  . ALA B 23  ? 1.25792 1.20617 1.13539 0.20750  -0.10936 -0.00973 344 ALA C CB  
1817 N N   . THR B 24  ? 1.19788 0.96407 1.14522 0.16476  -0.18921 0.08223  345 THR C N   
1818 C CA  . THR B 24  ? 1.34752 1.02312 1.27094 0.13350  -0.23883 0.12022  345 THR C CA  
1819 C C   . THR B 24  ? 1.53113 1.17522 1.34927 0.10796  -0.24606 0.10127  345 THR C C   
1820 O O   . THR B 24  ? 1.41515 1.01596 1.19866 0.09378  -0.27959 0.13119  345 THR C O   
1821 C CB  . THR B 24  ? 1.51437 1.12469 1.46759 0.11490  -0.25324 0.12580  345 THR C CB  
1822 O OG1 . THR B 24  ? 1.53247 1.17286 1.59709 0.14137  -0.24155 0.14220  345 THR C OG1 
1823 C CG2 . THR B 24  ? 1.38726 0.90020 1.30589 0.08070  -0.31128 0.17034  345 THR C CG2 
1824 N N   . ARG B 25  ? 1.64489 1.30893 1.41571 0.10128  -0.21345 0.04983  346 ARG C N   
1825 C CA  . ARG B 25  ? 1.39615 1.03666 1.07931 0.07880  -0.20963 0.02713  346 ARG C CA  
1826 C C   . ARG B 25  ? 1.21936 0.94494 0.89518 0.09615  -0.16882 -0.02200 346 ARG C C   
1827 O O   . ARG B 25  ? 1.09714 0.86597 0.80439 0.10713  -0.14371 -0.05441 346 ARG C O   
1828 C CB  . ARG B 25  ? 1.38545 0.93763 1.01369 0.03956  -0.21846 0.01993  346 ARG C CB  
1829 C CG  . ARG B 25  ? 1.41671 0.97549 1.08015 0.03739  -0.19555 -0.00965 346 ARG C CG  
1830 C CD  . ARG B 25  ? 1.42834 0.89748 1.03598 -0.00303 -0.20301 -0.01085 346 ARG C CD  
1831 N NE  . ARG B 25  ? 1.66567 1.14255 1.31253 -0.00581 -0.17809 -0.04298 346 ARG C NE  
1832 C CZ  . ARG B 25  ? 1.67787 1.08422 1.29457 -0.03854 -0.17818 -0.04534 346 ARG C CZ  
1833 N NH1 . ARG B 25  ? 1.56795 0.98493 1.23243 -0.03904 -0.15478 -0.07639 346 ARG C NH1 
1834 N NH2 . ARG B 25  ? 1.36982 0.69137 0.90491 -0.07195 -0.20088 -0.01684 346 ARG C NH2 
1835 N N   . PHE B 26  ? 1.26213 1.00958 0.89958 0.09819  -0.16481 -0.02767 347 PHE C N   
1836 C CA  . PHE B 26  ? 1.23529 1.06298 0.86903 0.11325  -0.13444 -0.06830 347 PHE C CA  
1837 C C   . PHE B 26  ? 1.30071 1.09900 0.88497 0.08442  -0.11704 -0.10679 347 PHE C C   
1838 O O   . PHE B 26  ? 1.35282 1.06590 0.89369 0.05290  -0.12535 -0.09991 347 PHE C O   
1839 C CB  . PHE B 26  ? 1.08421 0.95935 0.72335 0.13584  -0.13902 -0.04824 347 PHE C CB  
1840 C CG  . PHE B 26  ? 1.11685 1.06267 0.81058 0.17129  -0.13681 -0.02690 347 PHE C CG  
1841 C CD1 . PHE B 26  ? 1.30304 1.22636 1.04110 0.17844  -0.15122 0.00998  347 PHE C CD1 
1842 C CD2 . PHE B 26  ? 1.02677 1.06129 0.72917 0.19702  -0.11984 -0.04094 347 PHE C CD2 
1843 C CE1 . PHE B 26  ? 1.37261 1.36057 1.16174 0.21081  -0.14065 0.03016  347 PHE C CE1 
1844 C CE2 . PHE B 26  ? 1.13158 1.22776 0.87184 0.22820  -0.11350 -0.01902 347 PHE C CE2 
1845 C CZ  . PHE B 26  ? 1.42678 1.49948 1.20991 0.23520  -0.11993 0.01558  347 PHE C CZ  
1846 N N   . ALA B 27  ? 1.26273 1.13294 0.85473 0.09453  -0.09288 -0.14565 348 ALA C N   
1847 C CA  . ALA B 27  ? 1.06152 0.92001 0.62590 0.07024  -0.07099 -0.18379 348 ALA C CA  
1848 C C   . ALA B 27  ? 1.23502 1.10414 0.77916 0.07218  -0.06496 -0.18241 348 ALA C C   
1849 O O   . ALA B 27  ? 1.07861 0.97286 0.63371 0.09447  -0.07873 -0.15500 348 ALA C O   
1850 C CB  . ALA B 27  ? 1.09233 1.02269 0.69163 0.07698  -0.05128 -0.23095 348 ALA C CB  
1851 N N   . SER B 28  ? 1.41998 1.26849 0.94148 0.04847  -0.04075 -0.21221 349 SER C N   
1852 C CA  . SER B 28  ? 1.41852 1.27052 0.92763 0.04864  -0.02703 -0.21639 349 SER C CA  
1853 C C   . SER B 28  ? 1.46210 1.42397 1.03070 0.07960  -0.02260 -0.23192 349 SER C C   
1854 O O   . SER B 28  ? 1.46349 1.49507 1.06836 0.09846  -0.03069 -0.24095 349 SER C O   
1855 C CB  . SER B 28  ? 1.41732 1.21291 0.88919 0.01336  0.00489  -0.24334 349 SER C CB  
1856 O OG  . SER B 28  ? 1.64223 1.43237 1.10368 0.01354  0.02426  -0.24884 349 SER C OG  
1857 N N   . VAL B 29  ? 1.42066 1.39518 0.99744 0.08450  -0.00991 -0.23502 350 VAL C N   
1858 C CA  . VAL B 29  ? 1.19441 1.27028 0.83171 0.11402  -0.01146 -0.24221 350 VAL C CA  
1859 C C   . VAL B 29  ? 1.18865 1.32542 0.86632 0.10690  0.00422  -0.28630 350 VAL C C   
1860 O O   . VAL B 29  ? 1.14297 1.36269 0.85652 0.12650  -0.01081 -0.29551 350 VAL C O   
1861 C CB  . VAL B 29  ? 1.33370 1.40108 0.98136 0.12207  -0.00208 -0.23154 350 VAL C CB  
1862 C CG1 . VAL B 29  ? 1.14917 1.31657 0.86039 0.15840  -0.01666 -0.21981 350 VAL C CG1 
1863 C CG2 . VAL B 29  ? 1.30213 1.28063 0.89678 0.11546  -0.01455 -0.19758 350 VAL C CG2 
1864 N N   . TYR B 30  ? 1.23195 1.32684 0.90252 0.07707  0.03470  -0.31423 351 TYR C N   
1865 C CA  . TYR B 30  ? 1.03020 1.18119 0.75178 0.06682  0.04984  -0.35622 351 TYR C CA  
1866 C C   . TYR B 30  ? 1.13810 1.29497 0.85472 0.05806  0.03839  -0.37329 351 TYR C C   
1867 O O   . TYR B 30  ? 1.16717 1.39452 0.93144 0.06036  0.03401  -0.40532 351 TYR C O   
1868 C CB  . TYR B 30  ? 0.94111 1.04078 0.66028 0.03557  0.09234  -0.37846 351 TYR C CB  
1869 C CG  . TYR B 30  ? 1.07275 1.06794 0.72130 0.00061  0.10789  -0.37621 351 TYR C CG  
1870 C CD1 . TYR B 30  ? 1.14704 1.04892 0.71655 -0.00812 0.10411  -0.34463 351 TYR C CD1 
1871 C CD2 . TYR B 30  ? 1.26334 1.25110 0.92547 -0.02515 0.12276  -0.40386 351 TYR C CD2 
1872 C CE1 . TYR B 30  ? 1.35313 1.15792 0.85352 -0.04120 0.11192  -0.33742 351 TYR C CE1 
1873 C CE2 . TYR B 30  ? 1.25924 1.14971 0.85831 -0.05727 0.13500  -0.39593 351 TYR C CE2 
1874 C CZ  . TYR B 30  ? 1.41129 1.21088 0.92687 -0.06502 0.12823  -0.36108 351 TYR C CZ  
1875 O OH  . TYR B 30  ? 1.42483 1.12605 0.87317 -0.09810 0.13428  -0.34832 351 TYR C OH  
1876 N N   . ALA B 31  ? 1.15068 1.23351 0.81516 0.04769  0.03142  -0.35333 352 ALA C N   
1877 C CA  . ALA B 31  ? 1.10220 1.18028 0.76765 0.04081  0.02327  -0.36773 352 ALA C CA  
1878 C C   . ALA B 31  ? 1.15518 1.26642 0.81921 0.07153  -0.00389 -0.34507 352 ALA C C   
1879 O O   . ALA B 31  ? 1.23463 1.29869 0.88045 0.06873  -0.01176 -0.32987 352 ALA C O   
1880 C CB  . ALA B 31  ? 1.11951 1.09229 0.74041 0.00750  0.03514  -0.35939 352 ALA C CB  
1881 N N   . TRP B 32  ? 1.14549 1.33894 0.83324 0.10142  -0.01689 -0.34016 353 TRP C N   
1882 C CA  . TRP B 32  ? 1.20967 1.43863 0.89339 0.13153  -0.03618 -0.31555 353 TRP C CA  
1883 C C   . TRP B 32  ? 1.25701 1.50989 0.94722 0.13254  -0.03625 -0.34663 353 TRP C C   
1884 O O   . TRP B 32  ? 1.26846 1.56455 0.98286 0.12374  -0.03309 -0.38599 353 TRP C O   
1885 C CB  . TRP B 32  ? 1.17232 1.48385 0.87598 0.16104  -0.04895 -0.30160 353 TRP C CB  
1886 C CG  . TRP B 32  ? 1.21810 1.60316 0.95742 0.15947  -0.04937 -0.33998 353 TRP C CG  
1887 C CD1 . TRP B 32  ? 1.09487 1.48480 0.86624 0.14613  -0.03772 -0.35476 353 TRP C CD1 
1888 C CD2 . TRP B 32  ? 1.19849 1.66249 0.94848 0.17083  -0.06349 -0.36861 353 TRP C CD2 
1889 N NE1 . TRP B 32  ? 0.96698 1.43806 0.78073 0.14861  -0.04749 -0.38788 353 TRP C NE1 
1890 C CE2 . TRP B 32  ? 1.07614 1.59215 0.87094 0.16255  -0.06663 -0.39763 353 TRP C CE2 
1891 C CE3 . TRP B 32  ? 1.23450 1.71998 0.97068 0.18292  -0.07125 -0.36441 353 TRP C CE3 
1892 C CZ2 . TRP B 32  ? 1.12825 1.72339 0.94173 0.16722  -0.08684 -0.42926 353 TRP C CZ2 
1893 C CZ3 . TRP B 32  ? 1.32404 1.87493 1.07650 0.18480  -0.08408 -0.38997 353 TRP C CZ3 
1894 C CH2 . TRP B 32  ? 1.27385 1.87833 1.06307 0.17653  -0.09546 -0.42060 353 TRP C CH2 
1895 N N   . ASN B 33  ? 1.07175 1.77949 1.10334 0.03031  0.14202  -0.45625 354 ASN C N   
1896 C CA  . ASN B 33  ? 1.12701 1.82758 1.11085 0.01540  0.11684  -0.45793 354 ASN C CA  
1897 C C   . ASN B 33  ? 1.12347 1.84706 1.08795 0.00297  0.14281  -0.43814 354 ASN C C   
1898 O O   . ASN B 33  ? 1.10092 1.82884 1.10967 0.00433  0.17798  -0.41655 354 ASN C O   
1899 C CB  . ASN B 33  ? 1.02379 1.68429 1.03157 0.01492  0.10065  -0.48616 354 ASN C CB  
1900 C CG  . ASN B 33  ? 1.23168 1.87117 1.25345 0.02632  0.07261  -0.49287 354 ASN C CG  
1901 O OD1 . ASN B 33  ? 1.23919 1.88384 1.23434 0.03193  0.05382  -0.47589 354 ASN C OD1 
1902 N ND2 . ASN B 33  ? 1.02657 1.64680 1.09010 0.02974  0.07078  -0.51471 354 ASN C ND2 
1903 N N   . ARG B 34  ? 1.13141 1.85142 1.03272 -0.01027 0.11913  -0.43162 355 ARG C N   
1904 C CA  . ARG B 34  ? 1.18100 1.90460 1.05459 -0.02308 0.13196  -0.39980 355 ARG C CA  
1905 C C   . ARG B 34  ? 1.26622 1.96148 1.09386 -0.02925 0.11619  -0.42536 355 ARG C C   
1906 O O   . ARG B 34  ? 1.41074 2.07628 1.19942 -0.03422 0.07677  -0.41842 355 ARG C O   
1907 C CB  . ARG B 34  ? 1.03624 1.77603 0.87303 -0.03451 0.11217  -0.33854 355 ARG C CB  
1908 C CG  . ARG B 34  ? 1.08186 1.82971 0.89823 -0.04468 0.12903  -0.29727 355 ARG C CG  
1909 C CD  . ARG B 34  ? 1.29492 2.06466 1.07917 -0.05691 0.10434  -0.23596 355 ARG C CD  
1910 N NE  . ARG B 34  ? 1.35032 2.13265 1.12047 -0.06354 0.12242  -0.19187 355 ARG C NE  
1911 C CZ  . ARG B 34  ? 1.26257 2.06620 1.08416 -0.05530 0.15640  -0.15003 355 ARG C CZ  
1912 N NH1 . ARG B 34  ? 1.27110 2.08134 1.15925 -0.04053 0.17627  -0.14844 355 ARG C NH1 
1913 N NH2 . ARG B 34  ? 1.25958 2.07530 1.06254 -0.06003 0.17152  -0.10938 355 ARG C NH2 
1914 N N   . LYS B 35  ? 1.16598 1.85387 1.01383 -0.02711 0.14669  -0.43878 356 LYS C N   
1915 C CA  . LYS B 35  ? 1.23637 1.88492 1.05595 -0.02803 0.13617  -0.45044 356 LYS C CA  
1916 C C   . LYS B 35  ? 1.28758 1.94301 1.04486 -0.03621 0.15033  -0.42810 356 LYS C C   
1917 O O   . LYS B 35  ? 1.32276 2.00731 1.10175 -0.03428 0.19335  -0.41897 356 LYS C O   
1918 C CB  . LYS B 35  ? 1.29117 1.92779 1.17732 -0.01850 0.15813  -0.47977 356 LYS C CB  
1919 C CG  . LYS B 35  ? 1.47956 2.08185 1.34112 -0.01549 0.15166  -0.48950 356 LYS C CG  
1920 C CD  . LYS B 35  ? 1.49568 2.06137 1.32544 -0.01386 0.10945  -0.48608 356 LYS C CD  
1921 C CE  . LYS B 35  ? 1.17021 1.69970 0.97624 -0.00748 0.10874  -0.49300 356 LYS C CE  
1922 N NZ  . LYS B 35  ? 1.14336 1.65949 0.88350 -0.01045 0.12315  -0.48122 356 LYS C NZ  
1923 N N   . ARG B 36  ? 1.26724 1.89004 0.95154 -0.04436 0.11571  -0.41389 357 ARG C N   
1924 C CA  . ARG B 36  ? 1.30902 1.92622 0.92101 -0.05227 0.12009  -0.39102 357 ARG C CA  
1925 C C   . ARG B 36  ? 1.31121 1.89155 0.91608 -0.04087 0.13988  -0.41078 357 ARG C C   
1926 O O   . ARG B 36  ? 1.48477 2.01304 1.06647 -0.03642 0.11688  -0.42143 357 ARG C O   
1927 C CB  . ARG B 36  ? 1.42837 2.01543 0.97021 -0.06662 0.07185  -0.36509 357 ARG C CB  
1928 C CG  . ARG B 36  ? 1.34616 1.91769 0.80710 -0.07570 0.06806  -0.33947 357 ARG C CG  
1929 C CD  . ARG B 36  ? 1.58726 2.11702 0.99047 -0.09091 0.01720  -0.31521 357 ARG C CD  
1930 N NE  . ARG B 36  ? 1.90829 2.48261 1.33426 -0.10421 -0.00462 -0.28815 357 ARG C NE  
1931 C CZ  . ARG B 36  ? 1.86867 2.48993 1.27173 -0.11903 -0.01090 -0.24618 357 ARG C CZ  
1932 N NH1 . ARG B 36  ? 1.51725 2.18087 0.94694 -0.12903 -0.03043 -0.21754 357 ARG C NH1 
1933 N NH2 . ARG B 36  ? 1.95598 2.58275 1.31043 -0.12198 0.00315  -0.22726 357 ARG C NH2 
1934 N N   . ILE B 37  ? 1.24725 1.85430 0.87507 -0.03427 0.18710  -0.41020 358 ILE C N   
1935 C CA  . ILE B 37  ? 1.30494 1.88614 0.93480 -0.02121 0.21368  -0.42525 358 ILE C CA  
1936 C C   . ILE B 37  ? 1.54697 2.10931 1.08437 -0.02237 0.21789  -0.40082 358 ILE C C   
1937 O O   . ILE B 37  ? 1.67637 2.27430 1.20095 -0.02514 0.24494  -0.37303 358 ILE C O   
1938 C CB  . ILE B 37  ? 1.05970 1.67437 0.78282 -0.01208 0.26486  -0.43471 358 ILE C CB  
1939 C CG1 . ILE B 37  ? 1.01077 1.64256 0.81814 -0.01357 0.25645  -0.45361 358 ILE C CG1 
1940 C CG2 . ILE B 37  ? 1.04993 1.63936 0.78699 0.00176  0.28699  -0.45120 358 ILE C CG2 
1941 C CD1 . ILE B 37  ? 0.92493 1.57880 0.83093 -0.00810 0.30122  -0.45889 358 ILE C CD1 
1942 N N   . SER B 38  ? 1.53548 2.03789 1.00789 -0.01874 0.19238  -0.40678 359 SER C N   
1943 C CA  . SER B 38  ? 1.62935 2.09699 1.00445 -0.01795 0.19089  -0.38683 359 SER C CA  
1944 C C   . SER B 38  ? 1.78086 2.19759 1.13198 0.00127  0.20775  -0.40449 359 SER C C   
1945 O O   . SER B 38  ? 1.74101 2.13780 1.13257 0.00908  0.20136  -0.42778 359 SER C O   
1946 C CB  . SER B 38  ? 1.61766 2.04698 0.91860 -0.03468 0.13613  -0.36867 359 SER C CB  
1947 O OG  . SER B 38  ? 1.46271 1.94415 0.78472 -0.05206 0.12058  -0.34660 359 SER C OG  
1948 N N   . ASN B 39  ? 1.98175 2.37875 1.26398 0.01013  0.23019  -0.38931 360 ASN C N   
1949 C CA  . ASN B 39  ? 1.93055 2.27788 1.17612 0.03143  0.25265  -0.40059 360 ASN C CA  
1950 C C   . ASN B 39  ? 1.83202 2.21078 1.17820 0.04670  0.29129  -0.42204 360 ASN C C   
1951 O O   . ASN B 39  ? 1.76403 2.11428 1.12902 0.05537  0.28243  -0.44239 360 ASN C O   
1952 C CB  . ASN B 39  ? 1.89506 2.16060 1.06851 0.03072  0.21025  -0.40893 360 ASN C CB  
1953 C CG  . ASN B 39  ? 1.95542 2.19404 1.06393 0.00954  0.15991  -0.39050 360 ASN C CG  
1954 O OD1 . ASN B 39  ? 1.97024 2.19282 1.00128 0.00536  0.15522  -0.36943 360 ASN C OD1 
1955 N ND2 . ASN B 39  ? 1.89292 2.12578 1.03488 -0.00309 0.12180  -0.39564 360 ASN C ND2 
1956 N N   . CYS B 40  ? 1.76773 2.20531 1.18285 0.04930  0.33487  -0.41307 361 CYS C N   
1957 C CA  . CYS B 40  ? 1.81414 2.28561 1.34194 0.05871  0.36870  -0.42984 361 CYS C CA  
1958 C C   . CYS B 40  ? 1.75990 2.25375 1.31554 0.07460  0.43047  -0.40997 361 CYS C C   
1959 O O   . CYS B 40  ? 1.66439 2.16687 1.17253 0.07474  0.44955  -0.38005 361 CYS C O   
1960 C CB  . CYS B 40  ? 1.53849 2.05676 1.15913 0.04251  0.35745  -0.43865 361 CYS C CB  
1961 S SG  . CYS B 40  ? 1.40079 1.95434 1.16479 0.04880  0.39173  -0.45784 361 CYS C SG  
1962 N N   . VAL B 41  ? 1.48609 1.99030 1.12190 0.08818  0.46064  -0.42240 362 VAL C N   
1963 C CA  . VAL B 41  ? 1.41435 1.94463 1.10859 0.10288  0.52134  -0.40059 362 VAL C CA  
1964 C C   . VAL B 41  ? 1.57054 2.14934 1.38654 0.08851  0.53479  -0.39771 362 VAL C C   
1965 O O   . VAL B 41  ? 1.56263 2.15586 1.47101 0.08481  0.53038  -0.41979 362 VAL C O   
1966 C CB  . VAL B 41  ? 1.47359 1.98971 1.19237 0.12545  0.54618  -0.41003 362 VAL C CB  
1967 C CG1 . VAL B 41  ? 1.44976 1.92209 1.05778 0.14800  0.56815  -0.39185 362 VAL C CG1 
1968 C CG2 . VAL B 41  ? 1.32624 1.82612 1.05805 0.12110  0.50347  -0.44531 362 VAL C CG2 
1969 N N   . ALA B 42  ? 1.78833 2.38903 1.60148 0.08010  0.54974  -0.36833 363 ALA C N   
1970 C CA  . ALA B 42  ? 1.83112 2.46635 1.74804 0.06624  0.55953  -0.36165 363 ALA C CA  
1971 C C   . ALA B 42  ? 1.93844 2.59046 1.95440 0.07665  0.61308  -0.33973 363 ALA C C   
1972 O O   . ALA B 42  ? 1.82164 2.47642 1.81534 0.09045  0.65375  -0.30282 363 ALA C O   
1973 C CB  . ALA B 42  ? 1.72695 2.37966 1.60091 0.05418  0.55315  -0.33307 363 ALA C CB  
1974 N N   . ASP B 43  ? 1.94609 2.60857 2.06847 0.06971  0.61013  -0.36064 364 ASP C N   
1975 C CA  . ASP B 43  ? 1.82823 2.50779 2.05725 0.07337  0.65101  -0.34117 364 ASP C CA  
1976 C C   . ASP B 43  ? 1.97877 2.66866 2.28188 0.05594  0.64850  -0.33436 364 ASP C C   
1977 O O   . ASP B 43  ? 2.05844 2.74842 2.43172 0.04256  0.62794  -0.36432 364 ASP C O   
1978 C CB  . ASP B 43  ? 1.62117 2.30308 1.91161 0.07656  0.64783  -0.37011 364 ASP C CB  
1979 C CG  . ASP B 43  ? 1.78640 2.46124 2.08122 0.06285  0.59673  -0.41793 364 ASP C CG  
1980 O OD1 . ASP B 43  ? 1.87482 2.54143 2.12105 0.05262  0.56317  -0.42847 364 ASP C OD1 
1981 O OD2 . ASP B 43  ? 1.75247 2.43346 2.10010 0.06282  0.58988  -0.44266 364 ASP C OD2 
1982 N N   . TYR B 44  ? 2.03158 2.72833 2.31393 0.05727  0.67006  -0.29319 365 TYR C N   
1983 C CA  . TYR B 44  ? 1.87001 2.57181 2.20864 0.04427  0.66867  -0.28106 365 TYR C CA  
1984 C C   . TYR B 44  ? 1.77141 2.47287 2.22658 0.03811  0.68789  -0.28148 365 TYR C C   
1985 O O   . TYR B 44  ? 1.65941 2.35438 2.16664 0.02550  0.67832  -0.28853 365 TYR C O   
1986 C CB  . TYR B 44  ? 1.74728 2.45982 2.04168 0.04957  0.69237  -0.22906 365 TYR C CB  
1987 C CG  . TYR B 44  ? 1.82349 2.53708 1.99525 0.05072  0.67369  -0.22671 365 TYR C CG  
1988 C CD1 . TYR B 44  ? 1.48934 2.20718 1.61658 0.03651  0.63064  -0.24670 365 TYR C CD1 
1989 C CD2 . TYR B 44  ? 1.94196 2.65315 2.03674 0.06525  0.69545  -0.20425 365 TYR C CD2 
1990 C CE1 . TYR B 44  ? 1.71656 2.43808 1.72694 0.03397  0.60240  -0.24277 365 TYR C CE1 
1991 C CE2 . TYR B 44  ? 2.02306 2.73231 1.99362 0.06273  0.66966  -0.20412 365 TYR C CE2 
1992 C CZ  . TYR B 44  ? 1.95901 2.67047 1.88875 0.04657  0.61702  -0.22043 365 TYR C CZ  
1993 O OH  . TYR B 44  ? 1.89832 2.59440 1.70489 0.04411  0.57535  -0.21143 365 TYR C OH  
1994 N N   . SER B 45  ? 1.65189 2.35848 2.14653 0.04596  0.71453  -0.27489 366 SER C N   
1995 C CA  . SER B 45  ? 1.61370 2.31949 2.21829 0.03617  0.73330  -0.27565 366 SER C CA  
1996 C C   . SER B 45  ? 1.73507 2.43929 2.39334 0.02548  0.71060  -0.32559 366 SER C C   
1997 O O   . SER B 45  ? 1.55938 2.26588 2.30756 0.01678  0.72763  -0.32962 366 SER C O   
1998 C CB  . SER B 45  ? 1.31140 2.02833 1.93624 0.04888  0.77839  -0.23306 366 SER C CB  
1999 O OG  . SER B 45  ? 1.25723 1.98421 1.83301 0.06617  0.78524  -0.23540 366 SER C OG  
2000 N N   . VAL B 46  ? 1.93176 2.63297 2.53720 0.02473  0.67145  -0.36338 367 VAL C N   
2001 C CA  . VAL B 46  ? 1.91179 2.61585 2.56426 0.01519  0.64624  -0.41031 367 VAL C CA  
2002 C C   . VAL B 46  ? 1.83691 2.53238 2.55758 -0.00659 0.62444  -0.44186 367 VAL C C   
2003 O O   . VAL B 46  ? 1.79842 2.49971 2.58428 -0.01828 0.61142  -0.47778 367 VAL C O   
2004 C CB  . VAL B 46  ? 1.95121 2.65274 2.51873 0.02363  0.61056  -0.43804 367 VAL C CB  
2005 C CG1 . VAL B 46  ? 1.86512 2.55528 2.38676 0.01403  0.56799  -0.46055 367 VAL C CG1 
2006 C CG2 . VAL B 46  ? 1.91668 2.62907 2.52853 0.02249  0.59831  -0.47154 367 VAL C CG2 
2007 N N   . LEU B 47  ? 1.82025 1.91237 2.14533 0.00392  0.98304  0.31330  368 LEU C N   
2008 C CA  . LEU B 47  ? 1.64731 1.71355 2.01300 -0.03080 0.91360  0.34778  368 LEU C CA  
2009 C C   . LEU B 47  ? 1.77159 1.81101 2.05565 -0.06209 0.88215  0.38899  368 LEU C C   
2010 O O   . LEU B 47  ? 1.80585 1.82992 2.12847 -0.08997 0.82239  0.41932  368 LEU C O   
2011 C CB  . LEU B 47  ? 1.52816 1.54317 1.87937 -0.01996 0.85878  0.29948  368 LEU C CB  
2012 C CG  . LEU B 47  ? 1.55758 1.59530 2.02005 0.00575  0.87514  0.26980  368 LEU C CG  
2013 C CD1 . LEU B 47  ? 1.38995 1.37604 1.83492 0.01668  0.82395  0.22975  368 LEU C CD1 
2014 C CD2 . LEU B 47  ? 1.42050 1.51164 2.02828 -0.00761 0.87710  0.32027  368 LEU C CD2 
2015 N N   . TYR B 48  ? 2.29285 2.32818 2.46683 -0.05475 0.91852  0.39063  369 TYR C N   
2016 C CA  . TYR B 48  ? 2.31291 2.32682 2.42293 -0.08515 0.89353  0.43865  369 TYR C CA  
2017 C C   . TYR B 48  ? 2.33411 2.39825 2.56422 -0.11542 0.89744  0.51095  369 TYR C C   
2018 O O   . TYR B 48  ? 2.29991 2.34366 2.53766 -0.14859 0.84564  0.54983  369 TYR C O   
2019 C CB  . TYR B 48  ? 2.43477 2.43958 2.39977 -0.06375 0.93580  0.42705  369 TYR C CB  
2020 C CG  . TYR B 48  ? 2.60410 2.53800 2.42832 -0.04945 0.89167  0.36549  369 TYR C CG  
2021 C CD1 . TYR B 48  ? 2.68805 2.60889 2.46391 -0.00791 0.90716  0.28856  369 TYR C CD1 
2022 C CD2 . TYR B 48  ? 2.57521 2.45516 2.32367 -0.07679 0.83145  0.38194  369 TYR C CD2 
2023 C CE1 . TYR B 48  ? 2.85351 2.70986 2.51240 0.00531  0.86467  0.23057  369 TYR C CE1 
2024 C CE2 . TYR B 48  ? 2.67588 2.49193 2.29930 -0.06375 0.79064  0.32534  369 TYR C CE2 
2025 C CZ  . TYR B 48  ? 2.83328 2.63798 2.41382 -0.02304 0.80789  0.25022  369 TYR C CZ  
2026 O OH  . TYR B 48  ? 3.04487 2.78631 2.51241 -0.00983 0.76526  0.19209  369 TYR C OH  
2027 N N   . ASN B 49  ? 2.20029 2.32770 2.52457 -0.10203 0.93779  0.51712  370 ASN C N   
2028 C CA  . ASN B 49  ? 2.17825 2.35101 2.62439 -0.12669 0.92257  0.56925  370 ASN C CA  
2029 C C   . ASN B 49  ? 2.15415 2.32332 2.71649 -0.14420 0.86180  0.57438  370 ASN C C   
2030 O O   . ASN B 49  ? 2.09945 2.29420 2.75947 -0.16637 0.83346  0.61382  370 ASN C O   
2031 C CB  . ASN B 49  ? 2.21497 2.45360 2.71826 -0.10397 0.98506  0.57186  370 ASN C CB  
2032 C CG  . ASN B 49  ? 2.40802 2.66358 2.79977 -0.08084 1.04412  0.57173  370 ASN C CG  
2033 O OD1 . ASN B 49  ? 2.39586 2.61007 2.65540 -0.07101 1.04517  0.55112  370 ASN C OD1 
2034 N ND2 . ASN B 49  ? 2.45301 2.77085 2.89370 -0.06853 1.09228  0.59395  370 ASN C ND2 
2035 N N   . SER B 50  ? 2.07661 2.21698 2.63362 -0.13119 0.84118  0.53535  371 SER C N   
2036 C CA  . SER B 50  ? 1.94289 2.08364 2.59814 -0.14002 0.78161  0.54027  371 SER C CA  
2037 C C   . SER B 50  ? 1.90379 2.00212 2.52309 -0.16851 0.71370  0.56316  371 SER C C   
2038 O O   . SER B 50  ? 1.80619 1.84968 2.31557 -0.16699 0.69014  0.53892  371 SER C O   
2039 C CB  . SER B 50  ? 1.57897 1.70726 2.24199 -0.11285 0.78571  0.49557  371 SER C CB  
2040 O OG  . SER B 50  ? 1.48855 1.65332 2.19010 -0.08552 0.84347  0.47073  371 SER C OG  
2041 N N   . ALA B 51  ? 1.84992 1.97074 2.55920 -0.19101 0.67236  0.60126  372 ALA C N   
2042 C CA  . ALA B 51  ? 1.70892 1.79380 2.40274 -0.21703 0.60066  0.62218  372 ALA C CA  
2043 C C   . ALA B 51  ? 1.64895 1.71657 2.36634 -0.20818 0.53388  0.60338  372 ALA C C   
2044 O O   . ALA B 51  ? 1.48987 1.53220 2.19785 -0.22222 0.45808  0.60967  372 ALA C O   
2045 C CB  . ALA B 51  ? 1.37100 1.48767 2.16830 -0.24052 0.57706  0.66486  372 ALA C CB  
2046 N N   . SER B 52  ? 1.70008 1.78197 2.43772 -0.17852 0.54919  0.57117  373 SER C N   
2047 C CA  . SER B 52  ? 1.61587 1.68860 2.36281 -0.15879 0.48251  0.54782  373 SER C CA  
2048 C C   . SER B 52  ? 1.69761 1.70800 2.30236 -0.15148 0.44442  0.51158  373 SER C C   
2049 O O   . SER B 52  ? 1.73917 1.74197 2.33976 -0.13334 0.38767  0.49608  373 SER C O   
2050 C CB  . SER B 52  ? 1.42158 1.53365 2.24956 -0.12855 0.51761  0.53390  373 SER C CB  
2051 O OG  . SER B 52  ? 1.29718 1.39561 2.06660 -0.11450 0.58407  0.50419  373 SER C OG  
2052 N N   . PHE B 53  ? 1.69040 1.66004 2.17970 -0.16163 0.47428  0.49878  374 PHE C N   
2053 C CA  . PHE B 53  ? 1.62165 1.53043 1.97612 -0.15528 0.43997  0.46171  374 PHE C CA  
2054 C C   . PHE B 53  ? 1.74287 1.61812 2.04394 -0.18023 0.37249  0.47810  374 PHE C C   
2055 O O   . PHE B 53  ? 1.81982 1.69404 2.11630 -0.20590 0.38671  0.50950  374 PHE C O   
2056 C CB  . PHE B 53  ? 1.56053 1.44286 1.81552 -0.14718 0.50239  0.43189  374 PHE C CB  
2057 C CG  . PHE B 53  ? 1.58343 1.49047 1.88479 -0.11831 0.55915  0.40346  374 PHE C CG  
2058 C CD1 . PHE B 53  ? 1.62190 1.55008 2.00941 -0.09860 0.54084  0.39612  374 PHE C CD1 
2059 C CD2 . PHE B 53  ? 1.66025 1.57218 1.92099 -0.10692 0.62967  0.38421  374 PHE C CD2 
2060 C CE1 . PHE B 53  ? 1.52644 1.47545 1.96804 -0.07266 0.59107  0.37153  374 PHE C CE1 
2061 C CE2 . PHE B 53  ? 1.61571 1.54984 1.92706 -0.07841 0.67685  0.35274  374 PHE C CE2 
2062 C CZ  . PHE B 53  ? 1.57109 1.52142 1.97775 -0.06358 0.65716  0.34710  374 PHE C CZ  
2063 N N   . SER B 54  ? 1.60312 1.45381 1.86881 -0.17061 0.29990  0.45922  375 SER C N   
2064 C CA  . SER B 54  ? 1.47608 1.29220 1.68737 -0.18993 0.22784  0.46635  375 SER C CA  
2065 C C   . SER B 54  ? 1.51362 1.26511 1.57053 -0.19479 0.22320  0.43771  375 SER C C   
2066 O O   . SER B 54  ? 1.64766 1.36732 1.65016 -0.21822 0.18990  0.45062  375 SER C O   
2067 C CB  . SER B 54  ? 1.31017 1.14019 1.56119 -0.17152 0.14646  0.45964  375 SER C CB  
2068 O OG  . SER B 54  ? 1.42241 1.24100 1.62399 -0.14082 0.14279  0.42704  375 SER C OG  
2069 N N   . THR B 55  ? 1.64125 1.37229 1.63417 -0.17244 0.25341  0.39851  376 THR C N   
2070 C CA  . THR B 55  ? 1.77297 1.44372 1.62362 -0.17244 0.25047  0.36408  376 THR C CA  
2071 C C   . THR B 55  ? 1.76491 1.43472 1.58309 -0.15861 0.33029  0.33977  376 THR C C   
2072 O O   . THR B 55  ? 1.56886 1.26411 1.44879 -0.13581 0.36487  0.32219  376 THR C O   
2073 C CB  . THR B 55  ? 1.69356 1.33522 1.49591 -0.15345 0.19406  0.33023  376 THR C CB  
2074 O OG1 . THR B 55  ? 1.69787 1.34822 1.52883 -0.15880 0.11740  0.34918  376 THR C OG1 
2075 C CG2 . THR B 55  ? 1.57545 1.15318 1.23524 -0.15470 0.18701  0.29259  376 THR C CG2 
2076 N N   . PHE B 56  ? 1.86939 1.51221 1.59232 -0.16865 0.35772  0.33828  377 PHE C N   
2077 C CA  . PHE B 56  ? 1.75360 1.40015 1.43405 -0.14907 0.43119  0.31158  377 PHE C CA  
2078 C C   . PHE B 56  ? 1.91367 1.50943 1.44348 -0.15169 0.42749  0.29383  377 PHE C C   
2079 O O   . PHE B 56  ? 2.01495 1.61486 1.51469 -0.16989 0.44151  0.33408  377 PHE C O   
2080 C CB  . PHE B 56  ? 1.63807 1.34502 1.40851 -0.15223 0.49767  0.35116  377 PHE C CB  
2081 C CG  . PHE B 56  ? 1.79762 1.52829 1.57553 -0.12107 0.56898  0.31666  377 PHE C CG  
2082 C CD1 . PHE B 56  ? 1.87164 1.56387 1.54533 -0.09510 0.57961  0.25667  377 PHE C CD1 
2083 C CD2 . PHE B 56  ? 1.90467 1.69706 1.79992 -0.11553 0.62173  0.34023  377 PHE C CD2 
2084 C CE1 . PHE B 56  ? 2.08144 1.79661 1.76946 -0.06235 0.63887  0.21802  377 PHE C CE1 
2085 C CE2 . PHE B 56  ? 1.98947 1.80540 1.89536 -0.08416 0.68407  0.30465  377 PHE C CE2 
2086 C CZ  . PHE B 56  ? 1.99572 1.77313 1.79884 -0.05659 0.69128  0.24199  377 PHE C CZ  
2087 N N   . LYS B 57  ? 1.90812 1.45769 1.35075 -0.13226 0.40870  0.23612  378 LYS C N   
2088 C CA  . LYS B 57  ? 2.00517 1.50221 1.29904 -0.13014 0.39649  0.21050  378 LYS C CA  
2089 C C   . LYS B 57  ? 1.90191 1.38332 1.13753 -0.09319 0.43266  0.14375  378 LYS C C   
2090 O O   . LYS B 57  ? 1.75170 1.21564 1.01340 -0.07707 0.41185  0.09904  378 LYS C O   
2091 C CB  . LYS B 57  ? 1.88128 1.32734 1.11960 -0.14566 0.31413  0.20202  378 LYS C CB  
2092 C CG  . LYS B 57  ? 1.82978 1.28625 1.11715 -0.17845 0.26727  0.25886  378 LYS C CG  
2093 C CD  . LYS B 57  ? 1.87440 1.28104 1.09575 -0.18788 0.18471  0.24267  378 LYS C CD  
2094 C CE  . LYS B 57  ? 1.85286 1.26948 1.12670 -0.21667 0.13129  0.29192  378 LYS C CE  
2095 N NZ  . LYS B 57  ? 1.82725 1.19810 1.03380 -0.22230 0.04843  0.27279  378 LYS C NZ  
2096 N N   . CYS B 58  ? 2.08374 1.57444 1.24620 -0.07652 0.48559  0.13760  379 CYS C N   
2097 C CA  . CYS B 58  ? 2.11705 1.59003 1.20540 -0.03595 0.51174  0.06626  379 CYS C CA  
2098 C C   . CYS B 58  ? 2.17514 1.58627 1.11153 -0.03197 0.47194  0.03413  379 CYS C C   
2099 O O   . CYS B 58  ? 2.26085 1.65622 1.13069 -0.05545 0.45242  0.07730  379 CYS C O   
2100 C CB  . CYS B 58  ? 2.25460 1.77970 1.33964 -0.00892 0.59148  0.07080  379 CYS C CB  
2101 S SG  . CYS B 58  ? 2.65133 2.25106 1.91359 -0.00795 0.64415  0.09986  379 CYS C SG  
2102 N N   . TYR B 59  ? 1.68253 2.03033 0.99278 -0.18339 -0.06171 0.11158  380 TYR C N   
2103 C CA  . TYR B 59  ? 1.67712 2.11808 0.96694 -0.14405 -0.05288 0.11787  380 TYR C CA  
2104 C C   . TYR B 59  ? 1.79929 2.35092 1.08657 -0.10664 -0.06579 0.09135  380 TYR C C   
2105 O O   . TYR B 59  ? 1.99260 2.60254 1.24598 -0.04447 -0.04208 0.11381  380 TYR C O   
2106 C CB  . TYR B 59  ? 1.52787 1.98860 0.83634 -0.18306 -0.07052 0.10327  380 TYR C CB  
2107 C CG  . TYR B 59  ? 1.57368 1.94533 0.87757 -0.20870 -0.05294 0.13467  380 TYR C CG  
2108 C CD1 . TYR B 59  ? 1.56397 1.84432 0.89136 -0.26068 -0.06405 0.12996  380 TYR C CD1 
2109 C CD2 . TYR B 59  ? 1.64369 2.02660 0.91802 -0.17836 -0.02331 0.16915  380 TYR C CD2 
2110 C CE1 . TYR B 59  ? 1.62932 1.83874 0.95363 -0.28465 -0.04829 0.15555  380 TYR C CE1 
2111 C CE2 . TYR B 59  ? 1.57568 1.87835 0.84650 -0.20438 -0.00527 0.19507  380 TYR C CE2 
2112 C CZ  . TYR B 59  ? 1.61361 1.83307 0.91089 -0.25902 -0.01895 0.18651  380 TYR C CZ  
2113 O OH  . TYR B 59  ? 1.52050 1.67022 0.81539 -0.28548 -0.00136 0.20929  380 TYR C OH  
2114 N N   . GLY B 60  ? 1.70521 2.28812 1.02531 -0.14104 -0.09919 0.04399  381 GLY C N   
2115 C CA  . GLY B 60  ? 1.66733 2.36980 0.99003 -0.11412 -0.11314 0.00963  381 GLY C CA  
2116 C C   . GLY B 60  ? 1.68287 2.38699 0.99970 -0.08575 -0.11178 0.00550  381 GLY C C   
2117 O O   . GLY B 60  ? 1.49763 2.30858 0.81545 -0.06017 -0.12229 -0.02351 381 GLY C O   
2118 N N   . VAL B 61  ? 1.71366 2.31038 1.02503 -0.08972 -0.09880 0.03102  382 VAL C N   
2119 C CA  . VAL B 61  ? 1.78603 2.37780 1.09337 -0.06618 -0.09776 0.02632  382 VAL C CA  
2120 C C   . VAL B 61  ? 1.81077 2.29540 1.09915 -0.05668 -0.06847 0.06795  382 VAL C C   
2121 O O   . VAL B 61  ? 1.72285 2.12617 1.01509 -0.08889 -0.05972 0.08639  382 VAL C O   
2122 C CB  . VAL B 61  ? 1.76421 2.34837 1.10885 -0.11299 -0.13047 -0.02197 382 VAL C CB  
2123 C CG1 . VAL B 61  ? 1.59568 2.06215 0.96028 -0.16736 -0.13701 -0.01774 382 VAL C CG1 
2124 C CG2 . VAL B 61  ? 1.57428 2.18171 0.91457 -0.08296 -0.13202 -0.03270 382 VAL C CG2 
2125 N N   . SER B 62  ? 2.01758 2.50684 1.28544 -0.01329 -0.05110 0.08024  383 SER C N   
2126 C CA  . SER B 62  ? 1.98659 2.37876 1.23801 -0.00769 -0.01963 0.11221  383 SER C CA  
2127 C C   . SER B 62  ? 1.92770 2.24318 1.21172 -0.06259 -0.04157 0.09322  383 SER C C   
2128 O O   . SER B 62  ? 1.89177 2.23122 1.20156 -0.08292 -0.07450 0.05813  383 SER C O   
2129 C CB  . SER B 62  ? 1.90185 2.31935 1.12293 0.05250  0.00590  0.12726  383 SER C CB  
2130 O OG  . SER B 62  ? 1.82623 2.29695 1.06640 0.05393  -0.02508 0.09194  383 SER C OG  
2131 N N   . PRO B 63  ? 1.97144 2.19832 1.25375 -0.08614 -0.02142 0.11453  384 PRO C N   
2132 C CA  . PRO B 63  ? 1.96898 2.13453 1.28051 -0.13439 -0.04259 0.09824  384 PRO C CA  
2133 C C   . PRO B 63  ? 1.93445 2.08947 1.25005 -0.12343 -0.04701 0.08649  384 PRO C C   
2134 O O   . PRO B 63  ? 1.83831 1.98829 1.17900 -0.14843 -0.07794 0.06014  384 PRO C O   
2135 C CB  . PRO B 63  ? 1.95463 2.04833 1.25907 -0.15590 -0.01399 0.12432  384 PRO C CB  
2136 C CG  . PRO B 63  ? 1.88384 1.98050 1.15004 -0.11122 0.03307  0.15525  384 PRO C CG  
2137 C CD  . PRO B 63  ? 1.84408 2.02745 1.09691 -0.07047 0.02432  0.15267  384 PRO C CD  
2138 N N   . THR B 64  ? 1.98986 2.13741 1.27874 -0.08487 -0.01264 0.10658  385 THR C N   
2139 C CA  . THR B 64  ? 1.98090 2.11157 1.27255 -0.07590 -0.01251 0.09768  385 THR C CA  
2140 C C   . THR B 64  ? 2.00775 2.20476 1.30666 -0.05376 -0.04051 0.07190  385 THR C C   
2141 O O   . THR B 64  ? 1.95498 2.13905 1.26525 -0.05698 -0.05271 0.05663  385 THR C O   
2142 C CB  . THR B 64  ? 1.98519 2.08388 1.24402 -0.04230 0.03889  0.12557  385 THR C CB  
2143 O OG1 . THR B 64  ? 2.29176 2.37934 1.55370 -0.03302 0.03858  0.11489  385 THR C OG1 
2144 C CG2 . THR B 64  ? 1.81046 1.95945 1.03373 0.01404  0.06531  0.14671  385 THR C CG2 
2145 N N   . LYS B 65  ? 1.96257 2.23621 1.25573 -0.03208 -0.05018 0.06428  386 LYS C N   
2146 C CA  . LYS B 65  ? 1.87885 2.23041 1.17923 -0.01219 -0.07400 0.03472  386 LYS C CA  
2147 C C   . LYS B 65  ? 1.87847 2.25682 1.21221 -0.05557 -0.11261 -0.00485 386 LYS C C   
2148 O O   . LYS B 65  ? 1.79231 2.25592 1.13219 -0.04464 -0.12897 -0.03401 386 LYS C O   
2149 C CB  . LYS B 65  ? 1.75153 2.18939 1.02110 0.04687  -0.05531 0.04795  386 LYS C CB  
2150 C CG  . LYS B 65  ? 1.78755 2.21612 1.02427 0.10038  -0.02071 0.07403  386 LYS C CG  
2151 C CD  . LYS B 65  ? 1.64391 2.15380 0.84259 0.16674  0.00450  0.09568  386 LYS C CD  
2152 C CE  . LYS B 65  ? 1.51416 1.98639 0.68579 0.17742  0.04160  0.13470  386 LYS C CE  
2153 N NZ  . LYS B 65  ? 1.58919 1.94831 0.74357 0.17183  0.08467  0.16500  386 LYS C NZ  
2154 N N   . LEU B 66  ? 1.91049 2.21931 1.26478 -0.10465 -0.12396 -0.00807 387 LEU C N   
2155 C CA  . LEU B 66  ? 1.97358 2.28808 1.35635 -0.14684 -0.15291 -0.04437 387 LEU C CA  
2156 C C   . LEU B 66  ? 2.03804 2.32876 1.43704 -0.15894 -0.16904 -0.07000 387 LEU C C   
2157 O O   . LEU B 66  ? 2.08819 2.39949 1.50608 -0.18369 -0.18674 -0.10693 387 LEU C O   
2158 C CB  . LEU B 66  ? 1.93927 2.18901 1.33280 -0.18910 -0.15495 -0.03364 387 LEU C CB  
2159 C CG  . LEU B 66  ? 1.85119 2.13590 1.24048 -0.19501 -0.15083 -0.02733 387 LEU C CG  
2160 C CD1 . LEU B 66  ? 1.72889 1.94135 1.12788 -0.23556 -0.15153 -0.01386 387 LEU C CD1 
2161 C CD2 . LEU B 66  ? 1.79726 2.16403 1.20022 -0.20364 -0.16860 -0.06824 387 LEU C CD2 
2162 N N   . ASN B 67  ? 2.00202 2.24940 1.39338 -0.14318 -0.15991 -0.05307 388 ASN C N   
2163 C CA  . ASN B 67  ? 1.88234 2.10375 1.28673 -0.15105 -0.17362 -0.07339 388 ASN C CA  
2164 C C   . ASN B 67  ? 1.63327 1.92834 1.03822 -0.12718 -0.18187 -0.10252 388 ASN C C   
2165 O O   . ASN B 67  ? 1.53964 1.83635 0.96161 -0.14675 -0.19752 -0.13627 388 ASN C O   
2166 C CB  . ASN B 67  ? 1.70775 1.87398 1.10357 -0.13961 -0.16016 -0.04847 388 ASN C CB  
2167 C CG  . ASN B 67  ? 1.73783 1.84972 1.13073 -0.15921 -0.14662 -0.02077 388 ASN C CG  
2168 O OD1 . ASN B 67  ? 1.69892 1.76511 1.10573 -0.19081 -0.15755 -0.02294 388 ASN C OD1 
2169 N ND2 . ASN B 67  ? 1.60633 1.72324 0.97899 -0.13877 -0.11930 0.00550  388 ASN C ND2 
2170 N N   . ASN B 73  ? 1.89912 2.25597 1.47380 -0.60648 -0.15700 -0.49233 394 ASN C N   
2171 C CA  . ASN B 73  ? 1.88470 2.10311 1.44856 -0.61696 -0.14858 -0.44882 394 ASN C CA  
2172 C C   . ASN B 73  ? 1.75243 1.96702 1.30207 -0.57996 -0.16718 -0.38328 394 ASN C C   
2173 O O   . ASN B 73  ? 1.75848 2.07325 1.30667 -0.55542 -0.18063 -0.37560 394 ASN C O   
2174 C CB  . ASN B 73  ? 1.91151 2.08944 1.48564 -0.67404 -0.12487 -0.48392 394 ASN C CB  
2175 C CG  . ASN B 73  ? 2.00518 2.15273 1.58980 -0.71675 -0.09498 -0.54705 394 ASN C CG  
2176 O OD1 . ASN B 73  ? 2.07001 2.16962 1.64868 -0.70390 -0.08871 -0.54808 394 ASN C OD1 
2177 N ND2 . ASN B 73  ? 1.88939 2.06338 1.48933 -0.76964 -0.07292 -0.60215 394 ASN C ND2 
2178 N N   . VAL B 74  ? 1.93215 2.18166 0.83252 -0.07015 -0.09354 -0.34480 395 VAL C N   
2179 C CA  . VAL B 74  ? 1.94724 2.20668 0.88952 -0.05535 -0.07395 -0.28138 395 VAL C CA  
2180 C C   . VAL B 74  ? 1.78868 2.00453 0.82349 -0.05309 -0.08706 -0.26971 395 VAL C C   
2181 O O   . VAL B 74  ? 1.72910 1.89945 0.80360 -0.04542 -0.08001 -0.30858 395 VAL C O   
2182 C CB  . VAL B 74  ? 1.83562 2.10451 0.76576 -0.03767 -0.02055 -0.28397 395 VAL C CB  
2183 C CG1 . VAL B 74  ? 1.59622 1.86804 0.57652 -0.02731 -0.00175 -0.22361 395 VAL C CG1 
2184 C CG2 . VAL B 74  ? 1.94652 2.25777 0.77333 -0.04366 -0.00363 -0.29062 395 VAL C CG2 
2185 N N   . TYR B 75  ? 1.81978 2.04914 0.88680 -0.05803 -0.10589 -0.21632 396 TYR C N   
2186 C CA  . TYR B 75  ? 1.58856 1.78288 0.73297 -0.05984 -0.11738 -0.19954 396 TYR C CA  
2187 C C   . TYR B 75  ? 1.50076 1.69733 0.68504 -0.04234 -0.08893 -0.15654 396 TYR C C   
2188 O O   . TYR B 75  ? 1.64218 1.87095 0.79880 -0.03441 -0.06912 -0.12434 396 TYR C O   
2189 C CB  . TYR B 75  ? 1.53288 1.74525 0.69290 -0.08151 -0.15648 -0.17741 396 TYR C CB  
2190 C CG  . TYR B 75  ? 1.66233 1.88048 0.78542 -0.10548 -0.18803 -0.22027 396 TYR C CG  
2191 C CD1 . TYR B 75  ? 1.69934 1.86081 0.84098 -0.12018 -0.19931 -0.26763 396 TYR C CD1 
2192 C CD2 . TYR B 75  ? 1.68089 1.95855 0.74928 -0.11384 -0.20857 -0.21350 396 TYR C CD2 
2193 C CE1 . TYR B 75  ? 1.84173 2.00384 0.95044 -0.14680 -0.22732 -0.31197 396 TYR C CE1 
2194 C CE2 . TYR B 75  ? 1.70208 1.99118 0.73620 -0.13944 -0.24008 -0.25734 396 TYR C CE2 
2195 C CZ  . TYR B 75  ? 1.82247 2.05280 0.87797 -0.15802 -0.24792 -0.30895 396 TYR C CZ  
2196 O OH  . TYR B 75  ? 1.93005 2.16719 0.95225 -0.18803 -0.27843 -0.35753 396 TYR C OH  
2197 N N   . ALA B 76  ? 1.56074 1.71911 0.80687 -0.03805 -0.08805 -0.15589 397 ALA C N   
2198 C CA  . ALA B 76  ? 1.58976 1.74842 0.87838 -0.02479 -0.06431 -0.12319 397 ALA C CA  
2199 C C   . ALA B 76  ? 1.67991 1.81780 1.01896 -0.03392 -0.08439 -0.09756 397 ALA C C   
2200 O O   . ALA B 76  ? 1.55099 1.64645 0.91818 -0.03700 -0.09823 -0.11627 397 ALA C O   
2201 C CB  . ALA B 76  ? 1.38915 1.53143 0.70028 -0.00667 -0.03784 -0.15401 397 ALA C CB  
2202 N N   . ASP B 77  ? 1.63725 1.80230 0.98540 -0.03740 -0.08459 -0.05447 398 ASP C N   
2203 C CA  . ASP B 77  ? 1.53814 1.69302 0.93121 -0.04699 -0.09682 -0.02988 398 ASP C CA  
2204 C C   . ASP B 77  ? 1.50790 1.65112 0.93566 -0.03507 -0.07301 -0.01378 398 ASP C C   
2205 O O   . ASP B 77  ? 1.49479 1.65679 0.91652 -0.02398 -0.04738 0.00150  398 ASP C O   
2206 C CB  . ASP B 77  ? 1.53959 1.73597 0.93176 -0.05435 -0.10920 0.00237  398 ASP C CB  
2207 C CG  . ASP B 77  ? 1.64329 1.86489 1.00226 -0.06754 -0.13684 -0.01429 398 ASP C CG  
2208 O OD1 . ASP B 77  ? 1.54549 1.73980 0.89519 -0.08125 -0.15194 -0.05128 398 ASP C OD1 
2209 O OD2 . ASP B 77  ? 1.67905 1.94655 1.02147 -0.06355 -0.14526 0.00878  398 ASP C OD2 
2210 N N   . SER B 78  ? 1.49537 1.60601 0.95605 -0.03983 -0.08227 -0.01663 399 SER C N   
2211 C CA  . SER B 78  ? 1.40651 1.50827 0.89862 -0.03027 -0.06603 -0.00732 399 SER C CA  
2212 C C   . SER B 78  ? 1.41994 1.51421 0.93585 -0.04396 -0.07518 0.01791  399 SER C C   
2213 O O   . SER B 78  ? 1.46327 1.53417 0.98039 -0.05971 -0.09704 0.01655  399 SER C O   
2214 C CB  . SER B 78  ? 1.39115 1.46273 0.89649 -0.01698 -0.06874 -0.03788 399 SER C CB  
2215 O OG  . SER B 78  ? 1.46457 1.49208 0.96972 -0.02548 -0.09655 -0.04958 399 SER C OG  
2216 N N   . PHE B 79  ? 1.30122 1.41320 0.83393 -0.04066 -0.05575 0.03899  400 PHE C N   
2217 C CA  . PHE B 79  ? 1.16710 1.27676 0.71948 -0.05282 -0.05783 0.05891  400 PHE C CA  
2218 C C   . PHE B 79  ? 1.09852 1.21883 0.66796 -0.04533 -0.03280 0.06783  400 PHE C C   
2219 O O   . PHE B 79  ? 1.17614 1.30650 0.74407 -0.03394 -0.01339 0.06256  400 PHE C O   
2220 C CB  . PHE B 79  ? 1.25140 1.38606 0.80449 -0.06559 -0.06460 0.07632  400 PHE C CB  
2221 C CG  . PHE B 79  ? 1.12750 1.29584 0.67132 -0.05330 -0.05390 0.08763  400 PHE C CG  
2222 C CD1 . PHE B 79  ? 1.13847 1.32096 0.69613 -0.04326 -0.03141 0.10778  400 PHE C CD1 
2223 C CD2 . PHE B 79  ? 1.14836 1.32988 0.66546 -0.05165 -0.06758 0.07845  400 PHE C CD2 
2224 C CE1 . PHE B 79  ? 1.07259 1.27613 0.61789 -0.02901 -0.02368 0.12436  400 PHE C CE1 
2225 C CE2 . PHE B 79  ? 1.25457 1.46570 0.75441 -0.03892 -0.06154 0.09439  400 PHE C CE2 
2226 C CZ  . PHE B 79  ? 1.24660 1.46601 0.76073 -0.02622 -0.04008 0.12035  400 PHE C CZ  
2227 N N   . VAL B 80  ? 1.08578 1.20346 0.66923 -0.05554 -0.03144 0.07956  401 VAL C N   
2228 C CA  . VAL B 80  ? 1.13094 1.25534 0.73022 -0.05347 -0.00964 0.08279  401 VAL C CA  
2229 C C   . VAL B 80  ? 1.10319 1.24232 0.71101 -0.06026 0.00312  0.10046  401 VAL C C   
2230 O O   . VAL B 80  ? 1.10939 1.25041 0.71754 -0.07398 -0.00716 0.10714  401 VAL C O   
2231 C CB  . VAL B 80  ? 1.00516 1.11445 0.61100 -0.05736 -0.02033 0.07320  401 VAL C CB  
2232 C CG1 . VAL B 80  ? 1.06968 1.19021 0.68928 -0.06239 -0.00022 0.07400  401 VAL C CG1 
2233 C CG2 . VAL B 80  ? 1.07504 1.17836 0.68641 -0.04290 -0.02868 0.05266  401 VAL C CG2 
2234 N N   . ILE B 81  ? 1.08086 1.22852 0.69696 -0.05088 0.02768  0.10764  402 ILE C N   
2235 C CA  . ILE B 81  ? 0.98916 1.14831 0.62030 -0.05005 0.04285  0.12137  402 ILE C CA  
2236 C C   . ILE B 81  ? 1.07072 1.21752 0.71462 -0.05172 0.06869  0.11462  402 ILE C C   
2237 O O   . ILE B 81  ? 1.04779 1.18491 0.69099 -0.05707 0.07091  0.09962  402 ILE C O   
2238 C CB  . ILE B 81  ? 0.87686 1.05025 0.50672 -0.03358 0.04598  0.13924  402 ILE C CB  
2239 C CG1 . ILE B 81  ? 0.98379 1.14142 0.59817 -0.02254 0.06179  0.14201  402 ILE C CG1 
2240 C CG2 . ILE B 81  ? 0.98052 1.17442 0.60014 -0.03689 0.01781  0.14125  402 ILE C CG2 
2241 C CD1 . ILE B 81  ? 1.12405 1.28884 0.72644 -0.00469 0.06446  0.16594  402 ILE C CD1 
2242 N N   . ARG B 82  ? 1.01588 1.16538 0.67576 -0.04671 0.08801  0.12248  403 ARG C N   
2243 C CA  . ARG B 82  ? 1.00537 1.13694 0.67743 -0.04968 0.11524  0.11240  403 ARG C CA  
2244 C C   . ARG B 82  ? 1.10806 1.21678 0.78037 -0.03844 0.13552  0.12082  403 ARG C C   
2245 O O   . ARG B 82  ? 1.16645 1.27706 0.82395 -0.02757 0.12831  0.13575  403 ARG C O   
2246 C CB  . ARG B 82  ? 1.03329 1.17311 0.72350 -0.04763 0.13002  0.11282  403 ARG C CB  
2247 C CG  . ARG B 82  ? 1.13731 1.26159 0.83369 -0.05975 0.15306  0.09102  403 ARG C CG  
2248 C CD  . ARG B 82  ? 1.15927 1.29536 0.87449 -0.05464 0.17114  0.08746  403 ARG C CD  
2249 N NE  . ARG B 82  ? 1.21068 1.34612 0.95069 -0.02609 0.18067  0.10707  403 ARG C NE  
2250 C CZ  . ARG B 82  ? 1.09553 1.25159 0.86433 -0.01210 0.19369  0.10709  403 ARG C CZ  
2251 N NH1 . ARG B 82  ? 1.14150 1.29873 0.93583 0.01944  0.19674  0.12772  403 ARG C NH1 
2252 N NH2 . ARG B 82  ? 1.19185 1.37090 0.96348 -0.02851 0.20353  0.08682  403 ARG C NH2 
2253 N N   . GLY B 83  ? 1.12169 1.20603 0.80653 -0.04425 0.16255  0.11062  404 GLY C N   
2254 C CA  . GLY B 83  ? 1.01549 1.06843 0.69931 -0.03961 0.18688  0.12065  404 GLY C CA  
2255 C C   . GLY B 83  ? 1.13790 1.17236 0.82126 -0.01445 0.19567  0.15098  404 GLY C C   
2256 O O   . GLY B 83  ? 1.07221 1.09029 0.73624 -0.00515 0.20087  0.17345  404 GLY C O   
2257 N N   . ASP B 84  ? 1.26556 1.30557 0.96951 -0.00187 0.19728  0.15250  405 ASP C N   
2258 C CA  . ASP B 84  ? 1.14493 1.17369 0.85864 0.02889  0.20170  0.18097  405 ASP C CA  
2259 C C   . ASP B 84  ? 1.20252 1.27484 0.90674 0.04493  0.16968  0.20268  405 ASP C C   
2260 O O   . ASP B 84  ? 1.14015 1.20940 0.84654 0.07299  0.16589  0.23135  405 ASP C O   
2261 C CB  . ASP B 84  ? 1.10272 1.12844 0.85212 0.03912  0.21846  0.16828  405 ASP C CB  
2262 C CG  . ASP B 84  ? 1.23867 1.21648 0.99575 0.02293  0.25110  0.14295  405 ASP C CG  
2263 O OD1 . ASP B 84  ? 1.22714 1.16135 0.97035 0.01329  0.26645  0.14776  405 ASP C OD1 
2264 O OD2 . ASP B 84  ? 1.36774 1.35367 1.14362 0.01670  0.26293  0.11603  405 ASP C OD2 
2265 N N   . GLU B 85  ? 1.29874 1.40912 0.99237 0.02807  0.14487  0.18971  406 GLU C N   
2266 C CA  . GLU B 85  ? 1.04698 1.19861 0.73216 0.03645  0.11370  0.20332  406 GLU C CA  
2267 C C   . GLU B 85  ? 1.17936 1.32311 0.82380 0.04018  0.10342  0.21774  406 GLU C C   
2268 O O   . GLU B 85  ? 1.19756 1.37428 0.82838 0.04629  0.07642  0.22683  406 GLU C O   
2269 C CB  . GLU B 85  ? 1.07513 1.25937 0.76352 0.01348  0.09338  0.18272  406 GLU C CB  
2270 C CG  . GLU B 85  ? 1.11075 1.30213 0.82504 0.00116  0.10677  0.16550  406 GLU C CG  
2271 C CD  . GLU B 85  ? 1.39397 1.62237 1.14619 0.01620  0.10961  0.17274  406 GLU C CD  
2272 O OE1 . GLU B 85  ? 1.69228 1.94171 1.45548 0.03976  0.09758  0.19333  406 GLU C OE1 
2273 O OE2 . GLU B 85  ? 1.19146 1.43325 0.96278 0.00484  0.12364  0.15689  406 GLU C OE2 
2274 N N   . VAL B 86  ? 1.31833 1.42362 0.94263 0.03348  0.12562  0.21717  407 VAL C N   
2275 C CA  . VAL B 86  ? 1.12945 1.23099 0.71073 0.03378  0.12213  0.22800  407 VAL C CA  
2276 C C   . VAL B 86  ? 1.29752 1.39627 0.85612 0.05971  0.11562  0.26610  407 VAL C C   
2277 O O   . VAL B 86  ? 1.36214 1.47985 0.88039 0.06328  0.09770  0.27613  407 VAL C O   
2278 C CB  . VAL B 86  ? 1.09776 1.16593 0.67037 0.01682  0.15300  0.21733  407 VAL C CB  
2279 C CG1 . VAL B 86  ? 1.15148 1.22416 0.67914 0.01363  0.15431  0.22293  407 VAL C CG1 
2280 C CG2 . VAL B 86  ? 1.03491 1.11261 0.63476 -0.00431 0.15338  0.18116  407 VAL C CG2 
2281 N N   . ARG B 87  ? 1.34270 1.41779 0.92498 0.08011  0.12820  0.28703  408 ARG C N   
2282 C CA  . ARG B 87  ? 1.40342 1.47217 0.96698 0.11131  0.11851  0.32856  408 ARG C CA  
2283 C C   . ARG B 87  ? 1.45974 1.59352 1.03334 0.12781  0.07743  0.33466  408 ARG C C   
2284 O O   . ARG B 87  ? 1.59940 1.74259 1.14853 0.15309  0.05878  0.36854  408 ARG C O   
2285 C CB  . ARG B 87  ? 1.39416 1.41340 0.98894 0.13290  0.14337  0.34638  408 ARG C CB  
2286 C CG  . ARG B 87  ? 1.36726 1.41062 1.02503 0.13889  0.14419  0.32269  408 ARG C CG  
2287 C CD  . ARG B 87  ? 1.56018 1.54770 1.24891 0.16190  0.17257  0.33375  408 ARG C CD  
2288 N NE  . ARG B 87  ? 1.78796 1.76107 1.47100 0.20463  0.16015  0.37948  408 ARG C NE  
2289 C CZ  . ARG B 87  ? 1.86095 1.78007 1.57099 0.23588  0.17924  0.39726  408 ARG C CZ  
2290 N NH1 . ARG B 87  ? 1.97924 1.85460 1.72255 0.22515  0.21427  0.36779  408 ARG C NH1 
2291 N NH2 . ARG B 87  ? 1.62117 1.52816 1.32353 0.27913  0.16175  0.44369  408 ARG C NH2 
2292 N N   . GLN B 88  ? 1.43117 1.61049 1.03828 0.11212  0.06205  0.30412  409 GLN C N   
2293 C CA  . GLN B 88  ? 1.18308 1.42922 0.80938 0.12016  0.02545  0.30502  409 GLN C CA  
2294 C C   . GLN B 88  ? 1.17032 1.44553 0.75042 0.10498  -0.00364 0.29744  409 GLN C C   
2295 O O   . GLN B 88  ? 1.32345 1.65104 0.90500 0.11494  -0.03703 0.30609  409 GLN C O   
2296 C CB  . GLN B 88  ? 1.00837 1.28752 0.68934 0.10460  0.02607  0.27699  409 GLN C CB  
2297 C CG  . GLN B 88  ? 1.10143 1.36365 0.83056 0.12118  0.05388  0.27814  409 GLN C CG  
2298 C CD  . GLN B 88  ? 1.02749 1.33665 0.80691 0.10738  0.05422  0.25377  409 GLN C CD  
2299 O OE1 . GLN B 88  ? 0.98799 1.34640 0.77233 0.08789  0.03006  0.24267  409 GLN C OE1 
2300 N NE2 . GLN B 88  ? 0.99156 1.28339 0.80605 0.11454  0.08418  0.24386  409 GLN C NE2 
2301 N N   . ILE B 89  ? 1.20253 1.36137 0.74385 0.05037  0.09881  0.21496  410 ILE C N   
2302 C CA  . ILE B 89  ? 1.34932 1.51677 0.84592 0.05674  0.09617  0.20123  410 ILE C CA  
2303 C C   . ILE B 89  ? 1.41484 1.56435 0.84831 0.05612  0.10387  0.22291  410 ILE C C   
2304 O O   . ILE B 89  ? 1.22022 1.36984 0.63474 0.04762  0.13369  0.22829  410 ILE C O   
2305 C CB  . ILE B 89  ? 1.27388 1.46564 0.78744 0.05248  0.11715  0.17770  410 ILE C CB  
2306 C CG1 . ILE B 89  ? 1.05518 1.26134 0.61921 0.05594  0.10342  0.15622  410 ILE C CG1 
2307 C CG2 . ILE B 89  ? 1.15089 1.34884 0.61472 0.05631  0.12246  0.16531  410 ILE C CG2 
2308 C CD1 . ILE B 89  ? 0.99502 1.20060 0.61120 0.04833  0.10700  0.16077  410 ILE C CD1 
2309 N N   . ALA B 90  ? 1.58623 1.71880 0.98760 0.06492  0.07668  0.23584  411 ALA C N   
2310 C CA  . ALA B 90  ? 1.53811 1.64825 0.87348 0.06607  0.07627  0.26030  411 ALA C CA  
2311 C C   . ALA B 90  ? 1.71676 1.81487 1.03275 0.07853  0.03560  0.26722  411 ALA C C   
2312 O O   . ALA B 90  ? 1.63589 1.73801 1.00245 0.08397  0.01323  0.26034  411 ALA C O   
2313 C CB  . ALA B 90  ? 1.41631 1.50778 0.75792 0.05754  0.09752  0.28931  411 ALA C CB  
2314 N N   . PRO B 91  ? 1.80286 1.88582 1.04707 0.08287  0.02477  0.27966  412 PRO C N   
2315 C CA  . PRO B 91  ? 1.82052 1.89344 1.04793 0.09535  -0.01792 0.28598  412 PRO C CA  
2316 C C   . PRO B 91  ? 1.69155 1.74573 0.95590 0.09883  -0.03384 0.31316  412 PRO C C   
2317 O O   . PRO B 91  ? 1.62727 1.66311 0.88543 0.09282  -0.01485 0.34023  412 PRO C O   
2318 C CB  . PRO B 91  ? 1.85920 1.91671 0.99275 0.09636  -0.02046 0.29735  412 PRO C CB  
2319 C CG  . PRO B 91  ? 1.74303 1.81137 0.85216 0.08523  0.02015  0.28208  412 PRO C CG  
2320 C CD  . PRO B 91  ? 1.63576 1.71181 0.80959 0.07625  0.05036  0.28376  412 PRO C CD  
2321 N N   . GLY B 92  ? 1.59243 1.65091 0.89957 0.10821  -0.06725 0.30446  413 GLY C N   
2322 C CA  . GLY B 92  ? 1.49650 1.53758 0.84390 0.11264  -0.08541 0.32740  413 GLY C CA  
2323 C C   . GLY B 92  ? 1.40184 1.44333 0.81845 0.10318  -0.06095 0.33031  413 GLY C C   
2324 O O   . GLY B 92  ? 1.46287 1.48469 0.89905 0.10233  -0.06039 0.35675  413 GLY C O   
2325 N N   . GLN B 93  ? 1.31945 1.38203 0.77353 0.09587  -0.04128 0.30381  414 GLN C N   
2326 C CA  . GLN B 93  ? 1.31193 1.37643 0.82884 0.08561  -0.01930 0.30283  414 GLN C CA  
2327 C C   . GLN B 93  ? 1.18461 1.25613 0.76521 0.08843  -0.03696 0.28295  414 GLN C C   
2328 O O   . GLN B 93  ? 1.15314 1.23655 0.73352 0.09577  -0.05618 0.26064  414 GLN C O   
2329 C CB  . GLN B 93  ? 1.36061 1.44211 0.87594 0.07428  0.01569  0.28873  414 GLN C CB  
2330 C CG  . GLN B 93  ? 1.30462 1.37678 0.77294 0.06745  0.04279  0.30867  414 GLN C CG  
2331 C CD  . GLN B 93  ? 1.22153 1.27418 0.71370 0.06032  0.05778  0.33573  414 GLN C CD  
2332 O OE1 . GLN B 93  ? 1.28782 1.33873 0.83926 0.05729  0.05489  0.33483  414 GLN C OE1 
2333 N NE2 . GLN B 93  ? 1.13709 1.17319 0.58285 0.05672  0.07608  0.35931  414 GLN C NE2 
2334 N N   . THR B 94  ? 1.20396 1.26660 0.83965 0.08145  -0.02795 0.29019  415 THR C N   
2335 C CA  . THR B 94  ? 1.16641 1.23073 0.86454 0.08126  -0.03902 0.27281  415 THR C CA  
2336 C C   . THR B 94  ? 1.15549 1.22699 0.89292 0.06670  -0.01036 0.26094  415 THR C C   
2337 O O   . THR B 94  ? 1.17232 1.23802 0.91493 0.05664  0.01307  0.27592  415 THR C O   
2338 C CB  . THR B 94  ? 1.24468 1.28864 0.97745 0.08615  -0.05783 0.29097  415 THR C CB  
2339 O OG1 . THR B 94  ? 1.38143 1.41889 1.07448 0.10037  -0.08840 0.30340  415 THR C OG1 
2340 C CG2 . THR B 94  ? 1.18125 1.22576 0.97985 0.08486  -0.06651 0.26994  415 THR C CG2 
2341 N N   . GLY B 95  ? 1.13243 1.21553 0.89624 0.06533  -0.01257 0.23411  416 GLY C N   
2342 C CA  . GLY B 95  ? 1.05963 1.14865 0.85633 0.05188  0.01032  0.22182  416 GLY C CA  
2343 C C   . GLY B 95  ? 1.08562 1.18476 0.89881 0.05346  0.00337  0.19355  416 GLY C C   
2344 O O   . GLY B 95  ? 1.13992 1.24072 0.94734 0.06444  -0.01811 0.18258  416 GLY C O   
2345 N N   . LYS B 96  ? 1.03124 1.13625 0.86490 0.04204  0.02168  0.18198  417 LYS C N   
2346 C CA  . LYS B 96  ? 0.84680 0.95823 0.69366 0.04265  0.01758  0.15729  417 LYS C CA  
2347 C C   . LYS B 96  ? 0.93304 1.06318 0.74444 0.05162  0.01368  0.14600  417 LYS C C   
2348 O O   . LYS B 96  ? 0.93134 1.06425 0.74394 0.05965  0.00002  0.12879  417 LYS C O   
2349 C CB  . LYS B 96  ? 0.84785 0.95844 0.72070 0.02772  0.03627  0.15012  417 LYS C CB  
2350 C CG  . LYS B 96  ? 0.79656 0.89159 0.70564 0.02254  0.03285  0.13604  417 LYS C CG  
2351 C CD  . LYS B 96  ? 1.17371 1.24967 1.11146 0.02250  0.02602  0.14546  417 LYS C CD  
2352 C CE  . LYS B 96  ? 1.26844 1.32743 1.24470 0.01610  0.02614  0.12889  417 LYS C CE  
2353 N NZ  . LYS B 96  ? 0.67128 0.71253 0.68426 0.01642  0.01980  0.13600  417 LYS C NZ  
2354 N N   . ILE B 97  ? 1.04180 1.18435 0.82462 0.04973  0.02757  0.15409  418 ILE C N   
2355 C CA  . ILE B 97  ? 0.95512 1.11535 0.70695 0.05703  0.02750  0.14239  418 ILE C CA  
2356 C C   . ILE B 97  ? 0.99317 1.15157 0.70786 0.06869  0.01093  0.14677  418 ILE C C   
2357 O O   . ILE B 97  ? 1.03627 1.20432 0.73493 0.07707  0.00127  0.13023  418 ILE C O   
2358 C CB  . ILE B 97  ? 0.85175 1.02588 0.59216 0.04948  0.05091  0.14697  418 ILE C CB  
2359 C CG1 . ILE B 97  ? 0.85331 1.03124 0.63003 0.03822  0.06292  0.14027  418 ILE C CG1 
2360 C CG2 . ILE B 97  ? 0.92684 1.11871 0.63859 0.05646  0.05358  0.13413  418 ILE C CG2 
2361 C CD1 . ILE B 97  ? 1.03514 1.21880 0.82794 0.04147  0.05485  0.11896  418 ILE C CD1 
2362 N N   . ALA B 98  ? 1.14850 1.29356 0.84855 0.06928  0.00665  0.16898  419 ALA C N   
2363 C CA  . ALA B 98  ? 1.20310 1.34478 0.85985 0.07972  -0.01068 0.17606  419 ALA C CA  
2364 C C   . ALA B 98  ? 1.22362 1.36088 0.89475 0.08990  -0.03996 0.16425  419 ALA C C   
2365 O O   . ALA B 98  ? 1.27862 1.41876 0.91395 0.09925  -0.05737 0.16081  419 ALA C O   
2366 C CB  . ALA B 98  ? 1.34838 1.47396 0.98430 0.07776  -0.00760 0.20625  419 ALA C CB  
2367 N N   . ASP B 99  ? 1.17575 1.30571 0.89831 0.08742  -0.04496 0.15651  420 ASP C N   
2368 C CA  . ASP B 99  ? 1.17285 1.29766 0.91823 0.09607  -0.07071 0.14415  420 ASP C CA  
2369 C C   . ASP B 99  ? 1.14907 1.28184 0.91880 0.09691  -0.07061 0.11524  420 ASP C C   
2370 O O   . ASP B 99  ? 1.15125 1.28591 0.92615 0.10578  -0.09065 0.09974  420 ASP C O   
2371 C CB  . ASP B 99  ? 1.19742 1.30378 0.98801 0.09309  -0.07696 0.15618  420 ASP C CB  
2372 C CG  . ASP B 99  ? 1.23935 1.33435 1.01016 0.09463  -0.08136 0.18632  420 ASP C CG  
2373 O OD1 . ASP B 99  ? 1.26736 1.36573 0.98645 0.10203  -0.09150 0.19609  420 ASP C OD1 
2374 O OD2 . ASP B 99  ? 1.17286 1.25378 0.97867 0.08794  -0.07372 0.20029  420 ASP C OD2 
2375 N N   . TYR B 100 ? 1.03033 1.16707 0.81530 0.08799  -0.04935 0.10770  421 TYR C N   
2376 C CA  . TYR B 100 ? 0.88811 1.02727 0.69716 0.08816  -0.04805 0.08345  421 TYR C CA  
2377 C C   . TYR B 100 ? 0.92391 1.08012 0.71190 0.08886  -0.03574 0.07169  421 TYR C C   
2378 O O   . TYR B 100 ? 0.94158 1.09934 0.74575 0.09091  -0.03587 0.05214  421 TYR C O   
2379 C CB  . TYR B 100 ? 0.86362 0.98787 0.71488 0.07686  -0.03643 0.08245  421 TYR C CB  
2380 C CG  . TYR B 100 ? 0.84424 0.95031 0.73032 0.07574  -0.04675 0.08721  421 TYR C CG  
2381 C CD1 . TYR B 100 ? 0.98293 1.08768 0.87187 0.08687  -0.07042 0.08481  421 TYR C CD1 
2382 C CD2 . TYR B 100 ? 0.85580 0.94642 0.77454 0.06315  -0.03304 0.09268  421 TYR C CD2 
2383 C CE1 . TYR B 100 ? 1.04306 1.13226 0.97166 0.08657  -0.08077 0.08841  421 TYR C CE1 
2384 C CE2 . TYR B 100 ? 0.86488 0.93863 0.82175 0.06165  -0.04021 0.09548  421 TYR C CE2 
2385 C CZ  . TYR B 100 ? 0.90120 0.97464 0.86548 0.07394  -0.06437 0.09365  421 TYR C CZ  
2386 O OH  . TYR B 100 ? 0.90536 0.96307 0.91503 0.07318  -0.07247 0.09576  421 TYR C OH  
2387 N N   . ASN B 101 ? 0.98782 1.15562 0.74337 0.08719  -0.02400 0.08260  422 ASN C N   
2388 C CA  . ASN B 101 ? 0.88979 1.07453 0.63383 0.08711  -0.01022 0.07134  422 ASN C CA  
2389 C C   . ASN B 101 ? 0.92889 1.12670 0.62964 0.09372  -0.01068 0.06907  422 ASN C C   
2390 O O   . ASN B 101 ? 0.99013 1.19770 0.68511 0.10050  -0.01470 0.04940  422 ASN C O   
2391 C CB  . ASN B 101 ? 0.85053 1.03866 0.60499 0.07596  0.01028  0.08193  422 ASN C CB  
2392 C CG  . ASN B 101 ? 0.89650 1.07230 0.68878 0.06784  0.01255  0.07988  422 ASN C CG  
2393 O OD1 . ASN B 101 ? 0.90433 1.08297 0.71182 0.06700  0.01557  0.06656  422 ASN C OD1 
2394 N ND2 . ASN B 101 ? 0.88963 1.04989 0.69629 0.06143  0.01166  0.09328  422 ASN C ND2 
2395 N N   . TYR B 102 ? 1.04017 1.23669 0.70921 0.09110  -0.00477 0.08811  423 TYR C N   
2396 C CA  . TYR B 102 ? 1.05357 1.25958 0.67482 0.09479  -0.00069 0.08653  423 TYR C CA  
2397 C C   . TYR B 102 ? 1.13761 1.33019 0.72259 0.09515  -0.00820 0.10996  423 TYR C C   
2398 O O   . TYR B 102 ? 1.27390 1.45927 0.85698 0.08776  0.00564  0.13078  423 TYR C O   
2399 C CB  . TYR B 102 ? 1.06428 1.28500 0.68198 0.08855  0.02597  0.08380  423 TYR C CB  
2400 C CG  . TYR B 102 ? 1.20532 1.43471 0.77538 0.09023  0.03588  0.07942  423 TYR C CG  
2401 C CD1 . TYR B 102 ? 1.32234 1.56430 0.88505 0.09629  0.03410  0.05512  423 TYR C CD1 
2402 C CD2 . TYR B 102 ? 1.34487 1.56796 0.87700 0.08472  0.04956  0.09889  423 TYR C CD2 
2403 C CE1 . TYR B 102 ? 1.33745 1.58617 0.85561 0.09607  0.04582  0.04881  423 TYR C CE1 
2404 C CE2 . TYR B 102 ? 1.23273 1.46057 0.71690 0.08445  0.06169  0.09410  423 TYR C CE2 
2405 C CZ  . TYR B 102 ? 1.23676 1.47782 0.71384 0.08973  0.05992  0.06826  423 TYR C CZ  
2406 O OH  . TYR B 102 ? 1.28777 1.53247 0.71616 0.08781  0.07446  0.06129  423 TYR C OH  
2407 N N   . LYS B 103 ? 1.14055 1.32919 0.69731 0.10370  -0.03066 0.10672  424 LYS C N   
2408 C CA  . LYS B 103 ? 1.25481 1.42879 0.77289 0.10600  -0.04342 0.12982  424 LYS C CA  
2409 C C   . LYS B 103 ? 1.29591 1.47393 0.74765 0.10743  -0.03900 0.12844  424 LYS C C   
2410 O O   . LYS B 103 ? 1.27187 1.46364 0.71157 0.11057  -0.03918 0.10407  424 LYS C O   
2411 C CB  . LYS B 103 ? 1.17974 1.34422 0.71579 0.11466  -0.07676 0.12911  424 LYS C CB  
2412 C CG  . LYS B 103 ? 1.23395 1.38019 0.74489 0.11736  -0.09250 0.15801  424 LYS C CG  
2413 C CD  . LYS B 103 ? 1.34324 1.48075 0.89436 0.12478  -0.12314 0.15752  424 LYS C CD  
2414 C CE  . LYS B 103 ? 1.38338 1.50131 0.92138 0.12750  -0.13765 0.18945  424 LYS C CE  
2415 N NZ  . LYS B 103 ? 1.02299 1.13030 0.57706 0.11749  -0.11119 0.21195  424 LYS C NZ  
2416 N N   . LEU B 104 ? 1.40542 1.56941 0.81346 0.10434  -0.03324 0.15448  425 LEU C N   
2417 C CA  . LEU B 104 ? 1.41459 1.57666 0.75137 0.10332  -0.02544 0.15687  425 LEU C CA  
2418 C C   . LEU B 104 ? 1.55975 1.70510 0.84860 0.11091  -0.05658 0.17247  425 LEU C C   
2419 O O   . LEU B 104 ? 1.50802 1.63740 0.81190 0.11376  -0.07253 0.19590  425 LEU C O   
2420 C CB  . LEU B 104 ? 1.42353 1.57952 0.73985 0.09256  0.00941  0.17520  425 LEU C CB  
2421 C CG  . LEU B 104 ? 1.41981 1.58338 0.68779 0.08678  0.03599  0.16346  425 LEU C CG  
2422 C CD1 . LEU B 104 ? 1.26610 1.45499 0.57183 0.08702  0.04604  0.12983  425 LEU C CD1 
2423 C CD2 . LEU B 104 ? 1.50139 1.65597 0.75569 0.07568  0.07054  0.18340  425 LEU C CD2 
2424 N N   . PRO B 105 ? 1.66245 1.81082 0.89487 0.11420  -0.06673 0.15967  426 PRO C N   
2425 C CA  . PRO B 105 ? 1.74035 1.87318 0.92264 0.12175  -0.10063 0.17412  426 PRO C CA  
2426 C C   . PRO B 105 ? 1.81710 1.92456 0.94601 0.11774  -0.09214 0.21153  426 PRO C C   
2427 O O   . PRO B 105 ? 1.91155 2.01467 1.02577 0.10772  -0.05574 0.22143  426 PRO C O   
2428 C CB  . PRO B 105 ? 1.68086 1.82485 0.81182 0.12297  -0.10597 0.14726  426 PRO C CB  
2429 C CG  . PRO B 105 ? 1.69902 1.85656 0.83182 0.11329  -0.06409 0.13033  426 PRO C CG  
2430 C CD  . PRO B 105 ? 1.54720 1.71350 0.76084 0.11103  -0.04860 0.12998  426 PRO C CD  
2431 N N   . ASP B 106 ? 1.82259 1.91238 0.92464 0.12605  -0.12708 0.23258  427 ASP C N   
2432 C CA  . ASP B 106 ? 1.94088 2.00207 0.99087 0.12389  -0.12308 0.27169  427 ASP C CA  
2433 C C   . ASP B 106 ? 2.01552 2.06063 0.98491 0.11084  -0.10466 0.26925  427 ASP C C   
2434 O O   . ASP B 106 ? 1.94448 1.96801 0.88559 0.09921  -0.07578 0.28983  427 ASP C O   
2435 C CB  . ASP B 106 ? 1.96782 2.01261 1.01833 0.13609  -0.16886 0.29383  427 ASP C CB  
2436 C CG  . ASP B 106 ? 1.84264 1.89395 0.99035 0.14118  -0.18234 0.29219  427 ASP C CG  
2437 O OD1 . ASP B 106 ? 1.74747 1.81527 0.95537 0.13500  -0.15769 0.27341  427 ASP C OD1 
2438 O OD2 . ASP B 106 ? 1.73166 1.77062 0.89553 0.15105  -0.21756 0.30950  427 ASP C OD2 
2439 N N   . ASP B 107 ? 2.10595 2.15935 1.04189 0.11010  -0.11917 0.24233  428 ASP C N   
2440 C CA  . ASP B 107 ? 1.97292 2.01151 0.83525 0.09468  -0.09987 0.23474  428 ASP C CA  
2441 C C   . ASP B 107 ? 1.95769 2.01670 0.83256 0.08658  -0.05661 0.20643  428 ASP C C   
2442 O O   . ASP B 107 ? 1.78562 1.85268 0.63153 0.08123  -0.05090 0.17814  428 ASP C O   
2443 C CB  . ASP B 107 ? 1.89154 1.92808 0.71011 0.09596  -0.13732 0.22073  428 ASP C CB  
2444 C CG  . ASP B 107 ? 1.93498 2.00411 0.80223 0.10812  -0.15832 0.18585  428 ASP C CG  
2445 O OD1 . ASP B 107 ? 1.99256 2.08094 0.93031 0.11980  -0.16107 0.18308  428 ASP C OD1 
2446 O OD2 . ASP B 107 ? 1.95998 2.03504 0.79479 0.10488  -0.17102 0.16068  428 ASP C OD2 
2447 N N   . PHE B 108 ? 1.98224 2.05037 0.90418 0.08524  -0.02580 0.21385  429 PHE C N   
2448 C CA  . PHE B 108 ? 1.90074 1.99170 0.84772 0.07871  0.01342  0.18882  429 PHE C CA  
2449 C C   . PHE B 108 ? 1.93589 2.00697 0.82595 0.06100  0.04995  0.18864  429 PHE C C   
2450 O O   . PHE B 108 ? 1.83233 1.87345 0.68447 0.05197  0.05882  0.21647  429 PHE C O   
2451 C CB  . PHE B 108 ? 1.61664 1.72469 0.63405 0.08165  0.03167  0.19776  429 PHE C CB  
2452 C CG  . PHE B 108 ? 1.59623 1.72841 0.64494 0.07471  0.07064  0.17505  429 PHE C CG  
2453 C CD1 . PHE B 108 ? 1.68189 1.83984 0.76661 0.07820  0.06737  0.13988  429 PHE C CD1 
2454 C CD2 . PHE B 108 ? 1.64745 1.77242 0.70152 0.06262  0.10936  0.18664  429 PHE C CD2 
2455 C CE1 . PHE B 108 ? 1.70696 1.88458 0.82914 0.07161  0.10040  0.11898  429 PHE C CE1 
2456 C CE2 . PHE B 108 ? 1.63180 1.78014 0.72231 0.05646  0.14281  0.16480  429 PHE C CE2 
2457 C CZ  . PHE B 108 ? 1.62957 1.80332 0.75576 0.06096  0.13700  0.13119  429 PHE C CZ  
2458 N N   . THR B 109 ? 1.99103 2.07856 0.87732 0.05549  0.07243  0.15638  430 THR C N   
2459 C CA  . THR B 109 ? 2.12626 2.19754 0.96333 0.03785  0.11109  0.14957  430 THR C CA  
2460 C C   . THR B 109 ? 2.01544 2.11534 0.90831 0.03537  0.14998  0.12654  430 THR C C   
2461 O O   . THR B 109 ? 1.93052 2.05362 0.84084 0.03845  0.15385  0.09425  430 THR C O   
2462 C CB  . THR B 109 ? 2.20413 2.26285 0.97292 0.03186  0.09946  0.13094  430 THR C CB  
2463 O OG1 . THR B 109 ? 2.15528 2.19235 0.87974 0.03498  0.05762  0.15289  430 THR C OG1 
2464 C CG2 . THR B 109 ? 2.10445 2.14242 0.81762 0.01099  0.14182  0.12531  430 THR C CG2 
2465 N N   . GLY B 110 ? 1.98803 2.08719 0.91248 0.02959  0.17808  0.14276  431 GLY C N   
2466 C CA  . GLY B 110 ? 2.01307 2.14086 0.99563 0.02683  0.21323  0.12284  431 GLY C CA  
2467 C C   . GLY B 110 ? 1.95446 2.07992 0.97428 0.02085  0.23714  0.14461  431 GLY C C   
2468 O O   . GLY B 110 ? 1.93040 2.02555 0.91659 0.01328  0.23984  0.17253  431 GLY C O   
2469 N N   . CYS B 111 ? 1.82148 1.98024 0.91308 0.02361  0.25370  0.13102  432 CYS C N   
2470 C CA  . CYS B 111 ? 1.73262 1.89490 0.86997 0.01736  0.27750  0.14632  432 CYS C CA  
2471 C C   . CYS B 111 ? 1.61345 1.80451 0.83426 0.02589  0.26117  0.13903  432 CYS C C   
2472 O O   . CYS B 111 ? 1.57725 1.78751 0.82749 0.03399  0.24231  0.11591  432 CYS C O   
2473 C CB  . CYS B 111 ? 1.82960 1.99486 0.97439 0.00256  0.32488  0.13164  432 CYS C CB  
2474 S SG  . CYS B 111 ? 2.26768 2.39310 1.32089 -0.01580 0.34781  0.13341  432 CYS C SG  
2475 N N   . VAL B 112 ? 1.73433 1.92248 0.99619 0.02156  0.26799  0.15722  433 VAL C N   
2476 C CA  . VAL B 112 ? 1.58580 1.79337 0.92759 0.02496  0.25413  0.15079  433 VAL C CA  
2477 C C   . VAL B 112 ? 1.50255 1.72355 0.89335 0.01390  0.28799  0.14708  433 VAL C C   
2478 O O   . VAL B 112 ? 1.69434 1.89985 1.07358 0.00479  0.30956  0.16717  433 VAL C O   
2479 C CB  . VAL B 112 ? 1.41686 1.60843 0.76752 0.03003  0.22504  0.17464  433 VAL C CB  
2480 C CG1 . VAL B 112 ? 1.11681 1.32589 0.54530 0.03068  0.21552  0.16691  433 VAL C CG1 
2481 C CG2 . VAL B 112 ? 1.38820 1.56901 0.69809 0.04153  0.18941  0.17601  433 VAL C CG2 
2482 N N   . ILE B 113 ? 1.35972 1.60909 0.80723 0.01491  0.29204  0.12148  434 ILE C N   
2483 C CA  . ILE B 113 ? 1.32812 1.59554 0.83009 0.00548  0.32063  0.11304  434 ILE C CA  
2484 C C   . ILE B 113 ? 1.39247 1.67649 0.96382 0.00842  0.30024  0.10937  434 ILE C C   
2485 O O   . ILE B 113 ? 1.31860 1.61165 0.90761 0.01829  0.27310  0.09763  434 ILE C O   
2486 C CB  . ILE B 113 ? 1.26511 1.55219 0.77726 0.00354  0.34468  0.08521  434 ILE C CB  
2487 C CG1 . ILE B 113 ? 1.47813 1.74637 0.91159 0.00102  0.36062  0.08557  434 ILE C CG1 
2488 C CG2 . ILE B 113 ? 1.36035 1.66403 0.92653 -0.00733 0.37709  0.07804  434 ILE C CG2 
2489 C CD1 . ILE B 113 ? 1.38485 1.67022 0.82567 -0.00162 0.38593  0.05592  434 ILE C CD1 
2490 N N   . ALA B 114 ? 1.43243 1.71901 1.04122 -0.00099 0.31434  0.11872  435 ALA C N   
2491 C CA  . ALA B 114 ? 1.32135 1.62165 0.99086 -0.00080 0.29691  0.11566  435 ALA C CA  
2492 C C   . ALA B 114 ? 1.37567 1.69168 1.09489 -0.01276 0.32290  0.11153  435 ALA C C   
2493 O O   . ALA B 114 ? 1.50602 1.81299 1.20981 -0.02249 0.35297  0.12069  435 ALA C O   
2494 C CB  . ALA B 114 ? 1.34496 1.62414 1.00408 0.00082  0.27388  0.13708  435 ALA C CB  
2495 N N   . TRP B 115 ? 1.24788 1.58658 1.02655 -0.01222 0.31072  0.09750  436 TRP C N   
2496 C CA  . TRP B 115 ? 1.18428 1.54190 1.01804 -0.02305 0.32943  0.09068  436 TRP C CA  
2497 C C   . TRP B 115 ? 1.19899 1.56918 1.08075 -0.02239 0.30329  0.08577  436 TRP C C   
2498 O O   . TRP B 115 ? 1.19715 1.56615 1.07562 -0.01251 0.27476  0.08185  436 TRP C O   
2499 C CB  . TRP B 115 ? 1.34160 1.72264 1.20153 -0.02403 0.35237  0.06871  436 TRP C CB  
2500 C CG  . TRP B 115 ? 1.23455 1.63592 1.12149 -0.01243 0.33166  0.04811  436 TRP C CG  
2501 C CD1 . TRP B 115 ? 1.18980 1.61592 1.13859 -0.01048 0.31719  0.03417  436 TRP C CD1 
2502 C CD2 . TRP B 115 ? 1.18856 1.58604 1.04170 -0.00121 0.32288  0.03942  436 TRP C CD2 
2503 N NE1 . TRP B 115 ? 1.00402 1.44019 0.96035 0.00198  0.30068  0.01915  436 TRP C NE1 
2504 C CE2 . TRP B 115 ? 1.13150 1.55114 1.03170 0.00745  0.30501  0.02086  436 TRP C CE2 
2505 C CE3 . TRP B 115 ? 1.29446 1.67145 1.08153 0.00215  0.32752  0.04528  436 TRP C CE3 
2506 C CZ2 . TRP B 115 ? 1.12193 1.54370 1.00909 0.01904  0.29447  0.00742  436 TRP C CZ2 
2507 C CZ3 . TRP B 115 ? 1.25081 1.63180 1.02366 0.01292  0.31585  0.03009  436 TRP C CZ3 
2508 C CH2 . TRP B 115 ? 1.15962 1.56279 0.98419 0.02113  0.30086  0.01105  436 TRP C CH2 
2509 N N   . ASN B 116 ? 1.21189 1.59296 1.13704 -0.03396 0.31434  0.08528  437 ASN C N   
2510 C CA  . ASN B 116 ? 0.93601 1.32773 0.90286 -0.03622 0.29145  0.08055  437 ASN C CA  
2511 C C   . ASN B 116 ? 1.06228 1.48254 1.07199 -0.02976 0.27888  0.05867  437 ASN C C   
2512 O O   . ASN B 116 ? 1.05495 1.49566 1.09290 -0.03117 0.29795  0.04503  437 ASN C O   
2513 C CB  . ASN B 116 ? 0.87923 1.27338 0.87749 -0.05193 0.30775  0.08584  437 ASN C CB  
2514 C CG  . ASN B 116 ? 0.78847 1.19039 0.82195 -0.05649 0.28422  0.08118  437 ASN C CG  
2515 O OD1 . ASN B 116 ? 0.91281 1.34029 0.99056 -0.05736 0.27566  0.06464  437 ASN C OD1 
2516 N ND2 . ASN B 116 ? 0.78188 1.16086 0.79580 -0.05979 0.27349  0.09550  437 ASN C ND2 
2517 N N   . SER B 117 ? 0.94985 1.36994 0.96597 -0.02275 0.24758  0.05556  438 SER C N   
2518 C CA  . SER B 117 ? 0.90805 1.35094 0.96250 -0.01503 0.23051  0.03817  438 SER C CA  
2519 C C   . SER B 117 ? 0.87149 1.31690 0.95115 -0.01915 0.20544  0.03795  438 SER C C   
2520 O O   . SER B 117 ? 0.81901 1.26411 0.90165 -0.01026 0.17991  0.03313  438 SER C O   
2521 C CB  . SER B 117 ? 0.83118 1.26821 0.86003 0.00033  0.21751  0.03295  438 SER C CB  
2522 O OG  . SER B 117 ? 0.70254 1.11493 0.69553 0.00443  0.19702  0.04392  438 SER C OG  
2523 N N   . ASN B 118 ? 0.90999 1.35613 1.00628 -0.03359 0.21357  0.04290  439 ASN C N   
2524 C CA  . ASN B 118 ? 0.80893 1.25631 0.92484 -0.04020 0.19145  0.04143  439 ASN C CA  
2525 C C   . ASN B 118 ? 0.91015 1.38679 1.07462 -0.03742 0.17657  0.02513  439 ASN C C   
2526 O O   . ASN B 118 ? 0.86272 1.33845 1.03366 -0.03731 0.14994  0.02295  439 ASN C O   
2527 C CB  . ASN B 118 ? 0.66898 1.11018 0.79215 -0.05756 0.20640  0.04885  439 ASN C CB  
2528 C CG  . ASN B 118 ? 0.75238 1.18970 0.88615 -0.06660 0.18512  0.04726  439 ASN C CG  
2529 O OD1 . ASN B 118 ? 0.84270 1.26959 0.96036 -0.05995 0.16008  0.04693  439 ASN C OD1 
2530 N ND2 . ASN B 118 ? 0.77163 1.21584 0.93135 -0.08287 0.19665  0.04543  439 ASN C ND2 
2531 N N   . ASN B 119 ? 0.87440 1.37579 1.07332 -0.03528 0.19316  0.01364  440 ASN C N   
2532 C CA  . ASN B 119 ? 0.88541 1.41701 1.13889 -0.03140 0.17871  -0.00237 440 ASN C CA  
2533 C C   . ASN B 119 ? 0.89039 1.42329 1.14185 -0.01369 0.15716  -0.00740 440 ASN C C   
2534 O O   . ASN B 119 ? 0.90501 1.46084 1.20199 -0.00800 0.14073  -0.01890 440 ASN C O   
2535 C CB  . ASN B 119 ? 0.92796 1.48583 1.22717 -0.03644 0.20757  -0.01482 440 ASN C CB  
2536 C CG  . ASN B 119 ? 1.10228 1.65424 1.37871 -0.02960 0.23462  -0.01542 440 ASN C CG  
2537 O OD1 . ASN B 119 ? 1.12045 1.65142 1.35450 -0.03505 0.25713  -0.00354 440 ASN C OD1 
2538 N ND2 . ASN B 119 ? 0.98262 1.55206 1.28659 -0.01787 0.23237  -0.02932 440 ASN C ND2 
2539 N N   . LEU B 120 ? 0.86821 1.37733 1.07136 -0.00469 0.15611  0.00056  441 LEU C N   
2540 C CA  . LEU B 120 ? 0.75359 1.26159 0.95441 0.01180  0.13872  -0.00479 441 LEU C CA  
2541 C C   . LEU B 120 ? 0.87409 1.35432 1.03567 0.01590  0.11398  0.00537  441 LEU C C   
2542 O O   . LEU B 120 ? 0.85246 1.33360 1.02784 0.02202  0.08824  0.00303  441 LEU C O   
2543 C CB  . LEU B 120 ? 0.56437 1.07143 0.74809 0.01954  0.16166  -0.00959 441 LEU C CB  
2544 C CG  . LEU B 120 ? 0.86883 1.40074 1.09013 0.01593  0.19063  -0.02222 441 LEU C CG  
2545 C CD1 . LEU B 120 ? 0.75958 1.28435 0.95058 0.02193  0.21335  -0.02651 441 LEU C CD1 
2546 C CD2 . LEU B 120 ? 0.86371 1.42589 1.15295 0.02142  0.17812  -0.03755 441 LEU C CD2 
2547 N N   . ASP B 121 ? 0.84764 1.30195 0.96175 0.01266  0.12118  0.01673  442 ASP C N   
2548 C CA  . ASP B 121 ? 0.79082 1.21744 0.87027 0.01630  0.10158  0.02440  442 ASP C CA  
2549 C C   . ASP B 121 ? 0.84314 1.25634 0.91568 0.00206  0.09353  0.03272  442 ASP C C   
2550 O O   . ASP B 121 ? 0.80632 1.19674 0.84832 -0.00413 0.09852  0.04257  442 ASP C O   
2551 C CB  . ASP B 121 ? 0.75112 1.15821 0.78833 0.02185  0.11153  0.02984  442 ASP C CB  
2552 C CG  . ASP B 121 ? 0.91162 1.33138 0.95167 0.03352  0.12239  0.01959  442 ASP C CG  
2553 O OD1 . ASP B 121 ? 0.99789 1.43375 1.06953 0.04217  0.11414  0.00838  442 ASP C OD1 
2554 O OD2 . ASP B 121 ? 0.86326 1.27599 0.87361 0.03379  0.13907  0.02266  442 ASP C OD2 
2555 N N   . SER B 122 ? 0.84641 1.27443 0.95001 -0.00336 0.08018  0.02761  443 SER C N   
2556 C CA  . SER B 122 ? 0.69175 1.10899 0.79025 -0.01869 0.07251  0.03227  443 SER C CA  
2557 C C   . SER B 122 ? 0.85768 1.28906 0.98306 -0.01902 0.04791  0.02525  443 SER C C   
2558 O O   . SER B 122 ? 1.04478 1.50508 1.21149 -0.02249 0.04927  0.01707  443 SER C O   
2559 C CB  . SER B 122 ? 0.54907 0.97392 0.65839 -0.03354 0.09592  0.03466  443 SER C CB  
2560 O OG  . SER B 122 ? 0.86178 1.27725 0.96951 -0.04945 0.08990  0.03667  443 SER C OG  
2561 N N   . LYS B 123 ? 0.92289 1.33283 1.02483 -0.01556 0.02554  0.02850  444 LYS C N   
2562 C CA  . LYS B 123 ? 0.70319 1.12055 0.82072 -0.01629 -0.00115 0.02486  444 LYS C CA  
2563 C C   . LYS B 123 ? 0.78425 1.20210 0.90277 -0.03662 -0.00371 0.02400  444 LYS C C   
2564 O O   . LYS B 123 ? 0.87568 1.28053 0.97762 -0.04985 0.01431  0.02762  444 LYS C O   
2565 C CB  . LYS B 123 ? 0.89399 1.28282 0.97975 -0.00740 -0.02188 0.03005  444 LYS C CB  
2566 C CG  . LYS B 123 ? 1.02387 1.41416 1.11533 0.01303  -0.02291 0.02844  444 LYS C CG  
2567 C CD  . LYS B 123 ? 1.17605 1.53629 1.23886 0.02066  -0.04259 0.03363  444 LYS C CD  
2568 C CE  . LYS B 123 ? 1.12226 1.48464 1.19586 0.04073  -0.04294 0.03041  444 LYS C CE  
2569 N NZ  . LYS B 123 ? 1.13506 1.46590 1.18255 0.04804  -0.05988 0.03574  444 LYS C NZ  
2570 N N   . VAL B 124 ? 1.00011 1.43327 1.13997 -0.03901 -0.02740 0.01866  445 VAL C N   
2571 C CA  . VAL B 124 ? 1.00416 1.44008 1.14584 -0.05915 -0.03240 0.01495  445 VAL C CA  
2572 C C   . VAL B 124 ? 1.04363 1.43992 1.13268 -0.07050 -0.03808 0.02160  445 VAL C C   
2573 O O   . VAL B 124 ? 1.29603 1.68496 1.37633 -0.08989 -0.02879 0.01945  445 VAL C O   
2574 C CB  . VAL B 124 ? 0.96305 1.42775 1.14248 -0.05794 -0.05984 0.00651  445 VAL C CB  
2575 C CG1 . VAL B 124 ? 1.20494 1.65401 1.36393 -0.04493 -0.09203 0.01229  445 VAL C CG1 
2576 C CG2 . VAL B 124 ? 1.04038 1.51223 1.22520 -0.08009 -0.06426 -0.00048 445 VAL C CG2 
2577 N N   . GLY B 125 ? 0.74793 1.11708 0.80354 -0.05963 -0.05050 0.02851  446 GLY C N   
2578 C CA  . GLY B 125 ? 0.90822 1.23680 0.91453 -0.06991 -0.05318 0.03371  446 GLY C CA  
2579 C C   . GLY B 125 ? 0.93022 1.23200 0.91183 -0.06736 -0.03159 0.03939  446 GLY C C   
2580 O O   . GLY B 125 ? 1.02037 1.28656 0.96464 -0.07425 -0.03224 0.04259  446 GLY C O   
2581 N N   . GLY B 126 ? 0.83041 1.14717 0.83124 -0.05818 -0.01263 0.04018  447 GLY C N   
2582 C CA  . GLY B 126 ? 1.00705 1.30085 0.98650 -0.05470 0.00447  0.04553  447 GLY C CA  
2583 C C   . GLY B 126 ? 1.02907 1.32244 1.00657 -0.03355 0.00161  0.04672  447 GLY C C   
2584 O O   . GLY B 126 ? 1.08187 1.36108 1.04621 -0.02479 -0.01493 0.04703  447 GLY C O   
2585 N N   . ASN B 127 ? 0.98419 1.29136 0.97293 -0.02582 0.01844  0.04724  448 ASN C N   
2586 C CA  . ASN B 127 ? 1.08447 1.39317 1.07147 -0.00706 0.01838  0.04592  448 ASN C CA  
2587 C C   . ASN B 127 ? 1.11077 1.38955 1.06817 -0.00569 0.02500  0.04998  448 ASN C C   
2588 O O   . ASN B 127 ? 0.91335 1.19177 0.86578 -0.00648 0.04035  0.05335  448 ASN C O   
2589 C CB  . ASN B 127 ? 0.98465 1.32373 0.99633 -0.00054 0.03311  0.04259  448 ASN C CB  
2590 C CG  . ASN B 127 ? 1.06728 1.40951 1.07749 0.01746  0.03405  0.03847  448 ASN C CG  
2591 O OD1 . ASN B 127 ? 1.05981 1.38766 1.06091 0.02698  0.02032  0.03683  448 ASN C OD1 
2592 N ND2 . ASN B 127 ? 1.08274 1.44227 1.10067 0.02133  0.05186  0.03617  448 ASN C ND2 
2593 N N   . TYR B 128 ? 1.12142 1.37373 1.05970 -0.00357 0.01290  0.04979  449 TYR C N   
2594 C CA  . TYR B 128 ? 0.93420 1.15745 0.85038 -0.00215 0.01780  0.05104  449 TYR C CA  
2595 C C   . TYR B 128 ? 0.95619 1.18037 0.87163 0.01623  0.01590  0.04657  449 TYR C C   
2596 O O   . TYR B 128 ? 0.93244 1.13238 0.83314 0.01928  0.01622  0.04505  449 TYR C O   
2597 C CB  . TYR B 128 ? 0.95172 1.14190 0.84729 -0.01214 0.01013  0.05152  449 TYR C CB  
2598 C CG  . TYR B 128 ? 1.06080 1.24550 0.95293 -0.03274 0.01404  0.05360  449 TYR C CG  
2599 C CD1 . TYR B 128 ? 1.10622 1.30362 1.00358 -0.03991 0.00262  0.05276  449 TYR C CD1 
2600 C CD2 . TYR B 128 ? 1.08125 1.24846 0.96768 -0.04517 0.02854  0.05537  449 TYR C CD2 
2601 C CE1 . TYR B 128 ? 1.07457 1.26764 0.96847 -0.06002 0.00645  0.05223  449 TYR C CE1 
2602 C CE2 . TYR B 128 ? 0.98457 1.14635 0.87034 -0.06503 0.03440  0.05537  449 TYR C CE2 
2603 C CZ  . TYR B 128 ? 1.06549 1.24034 0.95342 -0.07295 0.02378  0.05310  449 TYR C CZ  
2604 O OH  . TYR B 128 ? 0.95360 1.12373 0.84052 -0.09393 0.02984  0.05078  449 TYR C OH  
2605 N N   . ASN B 129 ? 1.01598 1.26772 0.95004 0.02774  0.01521  0.04256  450 ASN C N   
2606 C CA  . ASN B 129 ? 0.70607 0.96016 0.64126 0.04427  0.01476  0.03587  450 ASN C CA  
2607 C C   . ASN B 129 ? 0.73692 0.99237 0.66085 0.04730  0.02742  0.03514  450 ASN C C   
2608 O O   . ASN B 129 ? 0.87422 1.12327 0.79168 0.05831  0.02632  0.02860  450 ASN C O   
2609 C CB  . ASN B 129 ? 0.94711 1.22994 0.90974 0.05463  0.01157  0.03012  450 ASN C CB  
2610 C CG  . ASN B 129 ? 1.20003 1.48119 1.17485 0.05492  -0.00601 0.03160  450 ASN C CG  
2611 O OD1 . ASN B 129 ? 1.17816 1.44392 1.15026 0.06421  -0.01686 0.03009  450 ASN C OD1 
2612 N ND2 . ASN B 129 ? 1.25847 1.55472 1.24669 0.04469  -0.00952 0.03472  450 ASN C ND2 
2613 N N   . TYR B 130 ? 0.88235 1.14513 0.80339 0.03784  0.03872  0.04173  451 TYR C N   
2614 C CA  . TYR B 130 ? 0.87362 1.13539 0.77956 0.04042  0.04853  0.04408  451 TYR C CA  
2615 C C   . TYR B 130 ? 0.76730 1.00121 0.65891 0.03395  0.04657  0.04948  451 TYR C C   
2616 O O   . TYR B 130 ? 0.64124 0.86417 0.53544 0.02077  0.04823  0.05554  451 TYR C O   
2617 C CB  . TYR B 130 ? 0.96671 1.24850 0.87688 0.03431  0.06343  0.04997  451 TYR C CB  
2618 C CG  . TYR B 130 ? 0.88369 1.19325 0.81022 0.04136  0.06963  0.04218  451 TYR C CG  
2619 C CD1 . TYR B 130 ? 0.96176 1.27958 0.87698 0.05123  0.07717  0.03633  451 TYR C CD1 
2620 C CD2 . TYR B 130 ? 0.81031 1.13788 0.76530 0.03764  0.06788  0.03921  451 TYR C CD2 
2621 C CE1 . TYR B 130 ? 0.89881 1.24092 0.83198 0.05649  0.08614  0.02710  451 TYR C CE1 
2622 C CE2 . TYR B 130 ? 0.94000 1.29358 0.91783 0.04412  0.07451  0.03051  451 TYR C CE2 
2623 C CZ  . TYR B 130 ? 0.86148 1.22165 0.82899 0.05319  0.08531  0.02416  451 TYR C CZ  
2624 O OH  . TYR B 130 ? 0.77314 1.15815 0.76611 0.05846  0.09516  0.01351  451 TYR C OH  
2625 N N   . LEU B 131 ? 0.94813 0.90791 1.08293 0.19418  -0.05144 0.05339  452 LEU C N   
2626 C CA  . LEU B 131 ? 0.88330 0.82540 0.99842 0.17382  -0.06679 0.04667  452 LEU C CA  
2627 C C   . LEU B 131 ? 0.83798 0.77204 0.92554 0.17340  -0.05900 0.04376  452 LEU C C   
2628 O O   . LEU B 131 ? 1.02080 0.95555 1.09725 0.18770  -0.04154 0.04525  452 LEU C O   
2629 C CB  . LEU B 131 ? 0.71368 0.61819 0.80151 0.17135  -0.08011 0.03671  452 LEU C CB  
2630 C CG  . LEU B 131 ? 0.59152 0.49436 0.69600 0.17676  -0.08681 0.04265  452 LEU C CG  
2631 C CD1 . LEU B 131 ? 0.79533 0.64857 0.86458 0.17292  -0.09400 0.03250  452 LEU C CD1 
2632 C CD2 . LEU B 131 ? 0.55089 0.48980 0.68958 0.15983  -0.09900 0.05120  452 LEU C CD2 
2633 N N   . TYR B 132 ? 0.71053 0.64007 0.78672 0.15860  -0.07150 0.04135  453 TYR C N   
2634 C CA  . TYR B 132 ? 0.68795 0.61490 0.73560 0.16039  -0.06871 0.04162  453 TYR C CA  
2635 C C   . TYR B 132 ? 0.79225 0.71651 0.82860 0.14643  -0.08788 0.03621  453 TYR C C   
2636 O O   . TYR B 132 ? 0.88934 0.81522 0.94566 0.13363  -0.09863 0.03510  453 TYR C O   
2637 C CB  . TYR B 132 ? 0.75661 0.70165 0.82059 0.16247  -0.05243 0.05644  453 TYR C CB  
2638 C CG  . TYR B 132 ? 0.71437 0.66974 0.80817 0.14706  -0.05556 0.06315  453 TYR C CG  
2639 C CD1 . TYR B 132 ? 0.74421 0.71337 0.87380 0.13634  -0.05424 0.06385  453 TYR C CD1 
2640 C CD2 . TYR B 132 ? 0.66308 0.61619 0.74767 0.14404  -0.05881 0.06879  453 TYR C CD2 
2641 C CE1 . TYR B 132 ? 0.74336 0.71710 0.89333 0.11899  -0.05511 0.06622  453 TYR C CE1 
2642 C CE2 . TYR B 132 ? 0.68567 0.64019 0.79342 0.13137  -0.05682 0.07330  453 TYR C CE2 
2643 C CZ  . TYR B 132 ? 0.74742 0.70886 0.88511 0.11686  -0.05442 0.07013  453 TYR C CZ  
2644 O OH  . TYR B 132 ? 0.71600 0.67421 0.87012 0.10100  -0.05064 0.07095  453 TYR C OH  
2645 N N   . ARG B 133 ? 0.87725 0.80271 0.88124 0.14888  -0.09193 0.03340  454 ARG C N   
2646 C CA  . ARG B 133 ? 0.77550 0.71019 0.77017 0.13645  -0.11046 0.02826  454 ARG C CA  
2647 C C   . ARG B 133 ? 0.74518 0.70432 0.75031 0.14170  -0.10851 0.04509  454 ARG C C   
2648 O O   . ARG B 133 ? 0.97992 0.94497 0.96993 0.15628  -0.09715 0.05650  454 ARG C O   
2649 C CB  . ARG B 133 ? 0.75124 0.67857 0.70188 0.13298  -0.11925 0.01225  454 ARG C CB  
2650 C CG  . ARG B 133 ? 0.82779 0.77567 0.77230 0.11607  -0.13983 0.00517  454 ARG C CG  
2651 C CD  . ARG B 133 ? 0.90646 0.85096 0.80411 0.10701  -0.14849 -0.01382 454 ARG C CD  
2652 N NE  . ARG B 133 ? 0.97817 0.87467 0.85326 0.10235  -0.13997 -0.03247 454 ARG C NE  
2653 C CZ  . ARG B 133 ? 1.03156 0.90077 0.90436 0.08324  -0.14568 -0.04779 454 ARG C CZ  
2654 N NH1 . ARG B 133 ? 1.04981 0.94036 0.94332 0.06423  -0.16084 -0.04796 454 ARG C NH1 
2655 N NH2 . ARG B 133 ? 1.05293 0.87087 0.90182 0.08458  -0.13323 -0.06170 454 ARG C NH2 
2656 N N   . LEU B 134 ? 0.56049 0.53033 0.58914 0.13181  -0.11671 0.04799  455 LEU C N   
2657 C CA  . LEU B 134 ? 0.88217 0.87059 0.92090 0.14002  -0.11258 0.06457  455 LEU C CA  
2658 C C   . LEU B 134 ? 0.81932 0.83474 0.85956 0.13369  -0.13031 0.06217  455 LEU C C   
2659 O O   . LEU B 134 ? 0.83316 0.86714 0.88500 0.14442  -0.12647 0.07768  455 LEU C O   
2660 C CB  . LEU B 134 ? 0.97211 0.94819 1.04233 0.13675  -0.09708 0.07303  455 LEU C CB  
2661 C CG  . LEU B 134 ? 0.70828 0.67684 0.80209 0.11782  -0.10304 0.06271  455 LEU C CG  
2662 C CD1 . LEU B 134 ? 0.58435 0.56536 0.68844 0.11142  -0.11110 0.06287  455 LEU C CD1 
2663 C CD2 . LEU B 134 ? 0.81656 0.77319 0.93160 0.11220  -0.08638 0.06675  455 LEU C CD2 
2664 N N   . PHE B 135 ? 0.85612 0.87398 0.88589 0.11681  -0.14714 0.04390  456 PHE C N   
2665 C CA  . PHE B 135 ? 0.82454 0.87509 0.85934 0.10519  -0.16406 0.03918  456 PHE C CA  
2666 C C   . PHE B 135 ? 0.88572 0.94907 0.88573 0.09511  -0.17932 0.02337  456 PHE C C   
2667 O O   . PHE B 135 ? 0.92745 0.95943 0.90916 0.07953  -0.18140 0.00406  456 PHE C O   
2668 C CB  . PHE B 135 ? 0.81710 0.85567 0.87452 0.08501  -0.16743 0.02967  456 PHE C CB  
2669 C CG  . PHE B 135 ? 0.68784 0.72648 0.77640 0.09037  -0.15565 0.04269  456 PHE C CG  
2670 C CD1 . PHE B 135 ? 0.76666 0.82622 0.86572 0.10990  -0.14665 0.06113  456 PHE C CD1 
2671 C CD2 . PHE B 135 ? 0.65213 0.66677 0.75510 0.07651  -0.15194 0.03675  456 PHE C CD2 
2672 C CE1 . PHE B 135 ? 0.61891 0.66847 0.74134 0.11370  -0.13130 0.07030  456 PHE C CE1 
2673 C CE2 . PHE B 135 ? 0.73579 0.74734 0.86087 0.07785  -0.13982 0.04490  456 PHE C CE2 
2674 C CZ  . PHE B 135 ? 0.58836 0.61392 0.72272 0.09554  -0.12806 0.06011  456 PHE C CZ  
2675 N N   . ARG B 136 ? 0.82165 0.92997 0.80992 0.10421  -0.18899 0.03177  457 ARG C N   
2676 C CA  . ARG B 136 ? 0.81146 0.94290 0.76457 0.08961  -0.20644 0.01477  457 ARG C CA  
2677 C C   . ARG B 136 ? 0.84943 1.05303 0.81054 0.09670  -0.22245 0.02846  457 ARG C C   
2678 O O   . ARG B 136 ? 1.02766 1.25192 0.99989 0.12601  -0.21485 0.05567  457 ARG C O   
2679 C CB  . ARG B 136 ? 0.92815 1.03307 0.83671 0.09931  -0.19860 0.00953  457 ARG C CB  
2680 C CG  . ARG B 136 ? 0.99050 1.05738 0.86421 0.07525  -0.20107 -0.02142 457 ARG C CG  
2681 C CD  . ARG B 136 ? 1.05974 1.10462 0.88534 0.08660  -0.19125 -0.02731 457 ARG C CD  
2682 N NE  . ARG B 136 ? 1.15937 1.24935 0.94624 0.08106  -0.20805 -0.03266 457 ARG C NE  
2683 C CZ  . ARG B 136 ? 1.23836 1.32632 0.98526 0.05237  -0.22014 -0.06247 457 ARG C CZ  
2684 N NH1 . ARG B 136 ? 1.37920 1.51806 1.09028 0.04614  -0.23779 -0.06662 457 ARG C NH1 
2685 N NH2 . ARG B 136 ? 1.07923 1.11304 0.81905 0.02923  -0.21377 -0.08792 457 ARG C NH2 
2686 N N   . LYS B 137 ? 0.85963 1.10223 0.81542 0.06984  -0.24330 0.01042  458 LYS C N   
2687 C CA  . LYS B 137 ? 0.91624 1.24322 0.88633 0.07386  -0.26215 0.02252  458 LYS C CA  
2688 C C   . LYS B 137 ? 0.94185 1.30922 0.87061 0.08651  -0.27450 0.02863  458 LYS C C   
2689 O O   . LYS B 137 ? 0.90706 1.35569 0.84325 0.08947  -0.29449 0.03855  458 LYS C O   
2690 C CB  . LYS B 137 ? 0.84554 1.20706 0.83049 0.03450  -0.27963 -0.00050 458 LYS C CB  
2691 C CG  . LYS B 137 ? 0.77825 1.10580 0.71898 -0.00366 -0.28677 -0.03680 458 LYS C CG  
2692 C CD  . LYS B 137 ? 0.95355 1.31066 0.91084 -0.04661 -0.30007 -0.05895 458 LYS C CD  
2693 C CE  . LYS B 137 ? 0.99223 1.30270 0.90003 -0.08712 -0.30245 -0.09683 458 LYS C CE  
2694 N NZ  . LYS B 137 ? 0.87919 1.21290 0.80141 -0.13415 -0.31210 -0.11935 458 LYS C NZ  
2695 N N   . SER B 138 ? 0.99599 1.31410 0.88174 0.09493  -0.26299 0.02417  459 SER C N   
2696 C CA  . SER B 138 ? 1.09768 1.44834 0.93630 0.10765  -0.27205 0.03045  459 SER C CA  
2697 C C   . SER B 138 ? 1.11198 1.39762 0.91992 0.12861  -0.24706 0.03675  459 SER C C   
2698 O O   . SER B 138 ? 1.08740 1.30639 0.89439 0.11835  -0.23060 0.01985  459 SER C O   
2699 C CB  . SER B 138 ? 1.04786 1.42529 0.84516 0.06928  -0.29510 -0.00386 459 SER C CB  
2700 O OG  . SER B 138 ? 1.38707 1.68789 1.16118 0.04216  -0.28327 -0.03708 459 SER C OG  
2701 N N   . ASN B 139 ? 1.09094 1.39961 0.87496 0.15924  -0.24335 0.06320  460 ASN C N   
2702 C CA  . ASN B 139 ? 1.08538 1.33931 0.83980 0.17861  -0.21754 0.07123  460 ASN C CA  
2703 C C   . ASN B 139 ? 1.23242 1.45716 0.92990 0.15761  -0.21834 0.03860  460 ASN C C   
2704 O O   . ASN B 139 ? 1.34221 1.60384 1.00416 0.13582  -0.24127 0.01819  460 ASN C O   
2705 C CB  . ASN B 139 ? 0.98478 1.26860 0.72253 0.21630  -0.21142 0.10998  460 ASN C CB  
2706 C CG  . ASN B 139 ? 1.07778 1.37880 0.86699 0.24118  -0.20414 0.14332  460 ASN C CG  
2707 O OD1 . ASN B 139 ? 0.94531 1.19644 0.75810 0.25542  -0.17642 0.15806  460 ASN C OD1 
2708 N ND2 . ASN B 139 ? 1.11189 1.48514 0.91883 0.24565  -0.22757 0.15447  460 ASN C ND2 
2709 N N   . LEU B 140 ? 1.27476 1.43394 0.96379 0.16344  -0.19155 0.03278  461 LEU C N   
2710 C CA  . LEU B 140 ? 1.25533 1.37549 0.89166 0.14831  -0.18480 0.00218  461 LEU C CA  
2711 C C   . LEU B 140 ? 1.26782 1.40928 0.84071 0.16154  -0.18464 0.00886  461 LEU C C   
2712 O O   . LEU B 140 ? 1.29958 1.46079 0.87144 0.19111  -0.17614 0.04286  461 LEU C O   
2713 C CB  . LEU B 140 ? 1.23248 1.28479 0.88533 0.15562  -0.15462 -0.00240 461 LEU C CB  
2714 C CG  . LEU B 140 ? 1.30964 1.32733 1.00115 0.13660  -0.15442 -0.02055 461 LEU C CG  
2715 C CD1 . LEU B 140 ? 1.07973 1.04325 0.78394 0.14934  -0.12568 -0.02111 461 LEU C CD1 
2716 C CD2 . LEU B 140 ? 1.27692 1.28670 0.93553 0.10349  -0.17093 -0.05603 461 LEU C CD2 
2717 N N   . LYS B 141 ? 1.36962 1.50250 0.88457 0.13826  -0.19229 -0.02440 462 LYS C N   
2718 C CA  . LYS B 141 ? 1.38014 1.52422 0.82339 0.14651  -0.18977 -0.02492 462 LYS C CA  
2719 C C   . LYS B 141 ? 1.36738 1.44756 0.79233 0.16690  -0.15120 -0.02229 462 LYS C C   
2720 O O   . LYS B 141 ? 1.39140 1.42033 0.85409 0.16780  -0.13061 -0.02899 462 LYS C O   
2721 C CB  . LYS B 141 ? 1.29327 1.44713 0.67771 0.10856  -0.21013 -0.06689 462 LYS C CB  
2722 C CG  . LYS B 141 ? 1.20014 1.42800 0.60550 0.08313  -0.24883 -0.07193 462 LYS C CG  
2723 C CD  . LYS B 141 ? 1.40085 1.63528 0.74593 0.03752  -0.26701 -0.11828 462 LYS C CD  
2724 C CE  . LYS B 141 ? 1.35162 1.67028 0.72463 0.00840  -0.30543 -0.12353 462 LYS C CE  
2725 N NZ  . LYS B 141 ? 1.35011 1.67726 0.66378 -0.04389 -0.32311 -0.17213 462 LYS C NZ  
2726 N N   . PRO B 142 ? 1.44820 1.53550 0.81699 0.18467  -0.14030 -0.01036 463 PRO C N   
2727 C CA  . PRO B 142 ? 1.48150 1.51304 0.83334 0.20308  -0.10071 -0.00838 463 PRO C CA  
2728 C C   . PRO B 142 ? 1.45544 1.42692 0.78300 0.18385  -0.08575 -0.05092 463 PRO C C   
2729 O O   . PRO B 142 ? 1.57109 1.53940 0.84612 0.15708  -0.10066 -0.08525 463 PRO C O   
2730 C CB  . PRO B 142 ? 1.44378 1.50116 0.72589 0.21993  -0.09699 0.00845  463 PRO C CB  
2731 C CG  . PRO B 142 ? 1.39563 1.51755 0.64320 0.20215  -0.13832 0.00110  463 PRO C CG  
2732 C CD  . PRO B 142 ? 1.37374 1.52581 0.69530 0.19237  -0.16217 0.00712  463 PRO C CD  
2733 N N   . PHE B 143 ? 1.41757 1.34173 0.78433 0.19759  -0.05492 -0.04810 464 PHE C N   
2734 C CA  . PHE B 143 ? 1.52470 1.38683 0.87687 0.18937  -0.03403 -0.08150 464 PHE C CA  
2735 C C   . PHE B 143 ? 1.50025 1.34724 0.86350 0.15854  -0.05621 -0.11062 464 PHE C C   
2736 O O   . PHE B 143 ? 1.59714 1.39916 0.91193 0.14015  -0.04989 -0.14700 464 PHE C O   
2737 C CB  . PHE B 143 ? 1.69179 1.52657 0.95755 0.19062  -0.01434 -0.10327 464 PHE C CB  
2738 C CG  . PHE B 143 ? 1.79921 1.63581 1.05429 0.22127  0.01696  -0.07690 464 PHE C CG  
2739 C CD1 . PHE B 143 ? 1.74760 1.58489 1.07295 0.24335  0.03774  -0.04730 464 PHE C CD1 
2740 C CD2 . PHE B 143 ? 1.85298 1.69193 1.02540 0.22498  0.02641  -0.08250 464 PHE C CD2 
2741 C CE1 . PHE B 143 ? 1.72900 1.56819 1.04613 0.26719  0.06920  -0.02362 464 PHE C CE1 
2742 C CE2 . PHE B 143 ? 1.79474 1.63344 0.95549 0.25213  0.05833  -0.05695 464 PHE C CE2 
2743 C CZ  . PHE B 143 ? 1.72515 1.56345 0.96026 0.27258  0.08066  -0.02736 464 PHE C CZ  
2744 N N   . GLU B 144 ? 1.40334 1.28297 0.82812 0.15195  -0.07899 -0.09507 465 GLU C N   
2745 C CA  . GLU B 144 ? 1.45921 1.32688 0.90292 0.12288  -0.09786 -0.11765 465 GLU C CA  
2746 C C   . GLU B 144 ? 1.34464 1.17926 0.85419 0.13303  -0.08381 -0.10848 465 GLU C C   
2747 O O   . GLU B 144 ? 1.30096 1.15340 0.86116 0.15543  -0.07526 -0.07834 465 GLU C O   
2748 C CB  . GLU B 144 ? 1.59508 1.53091 1.05752 0.10579  -0.13498 -0.10840 465 GLU C CB  
2749 C CG  . GLU B 144 ? 1.61259 1.54183 1.08230 0.06844  -0.15467 -0.13623 465 GLU C CG  
2750 C CD  . GLU B 144 ? 1.52494 1.53349 1.01339 0.05190  -0.19036 -0.12752 465 GLU C CD  
2751 O OE1 . GLU B 144 ? 1.58447 1.64868 1.09073 0.07582  -0.19855 -0.09446 465 GLU C OE1 
2752 O OE2 . GLU B 144 ? 1.33901 1.35423 0.82503 0.01562  -0.20813 -0.15271 465 GLU C OE2 
2753 N N   . ARG B 145 ? 1.32918 1.11466 0.83460 0.11521  -0.08077 -0.13451 466 ARG C N   
2754 C CA  . ARG B 145 ? 1.36367 1.11476 0.92188 0.12581  -0.06741 -0.12709 466 ARG C CA  
2755 C C   . ARG B 145 ? 1.32654 1.07577 0.90749 0.09742  -0.08921 -0.13727 466 ARG C C   
2756 O O   . ARG B 145 ? 1.34202 1.06472 0.88040 0.06829  -0.09593 -0.16726 466 ARG C O   
2757 C CB  . ARG B 145 ? 1.52964 1.21217 1.05879 0.14002  -0.03440 -0.14398 466 ARG C CB  
2758 C CG  . ARG B 145 ? 1.36759 1.02799 0.95361 0.16258  -0.01748 -0.12772 466 ARG C CG  
2759 C CD  . ARG B 145 ? 1.30162 0.90956 0.86223 0.18776  0.01928  -0.13677 466 ARG C CD  
2760 N NE  . ARG B 145 ? 1.32118 0.91643 0.93714 0.21176  0.03388  -0.11969 466 ARG C NE  
2761 C CZ  . ARG B 145 ? 1.43713 0.97704 1.05059 0.21312  0.04255  -0.13005 466 ARG C CZ  
2762 N NH1 . ARG B 145 ? 1.47329 0.95776 1.03064 0.18785  0.04090  -0.16034 466 ARG C NH1 
2763 N NH2 . ARG B 145 ? 1.45263 0.99324 1.11815 0.23889  0.05345  -0.10955 466 ARG C NH2 
2764 N N   . ASP B 146 ? 1.18768 0.96333 0.83283 0.10313  -0.09823 -0.11380 467 ASP C N   
2765 C CA  . ASP B 146 ? 1.10400 0.88480 0.77591 0.07804  -0.11752 -0.11871 467 ASP C CA  
2766 C C   . ASP B 146 ? 1.14091 0.88787 0.85571 0.09005  -0.10527 -0.10802 467 ASP C C   
2767 O O   . ASP B 146 ? 1.07895 0.85127 0.84090 0.10993  -0.10200 -0.08267 467 ASP C O   
2768 C CB  . ASP B 146 ? 1.29725 1.14945 1.00229 0.07268  -0.14186 -0.09992 467 ASP C CB  
2769 C CG  . ASP B 146 ? 1.15556 1.01975 0.88523 0.04453  -0.16062 -0.10694 467 ASP C CG  
2770 O OD1 . ASP B 146 ? 1.40793 1.25939 1.10351 0.01380  -0.16928 -0.13383 467 ASP C OD1 
2771 O OD2 . ASP B 146 ? 1.06610 0.95184 0.84731 0.05069  -0.16501 -0.08688 467 ASP C OD2 
2772 N N   . ILE B 147 ? 1.31882 1.00791 1.01442 0.07697  -0.09788 -0.12709 468 ILE C N   
2773 C CA  . ILE B 147 ? 1.13997 0.79606 0.86962 0.08962  -0.08746 -0.11552 468 ILE C CA  
2774 C C   . ILE B 147 ? 1.15873 0.81418 0.90408 0.06081  -0.10456 -0.11928 468 ILE C C   
2775 O O   . ILE B 147 ? 1.25850 0.86719 1.00784 0.06030  -0.09608 -0.11931 468 ILE C O   
2776 C CB  . ILE B 147 ? 1.05119 0.63331 0.74648 0.10546  -0.05931 -0.12828 468 ILE C CB  
2777 C CG1 . ILE B 147 ? 1.18666 0.76396 0.84330 0.12160  -0.04217 -0.13715 468 ILE C CG1 
2778 C CG2 . ILE B 147 ? 1.32892 0.90092 1.06862 0.13531  -0.04680 -0.10464 468 ILE C CG2 
2779 C CD1 . ILE B 147 ? 1.36817 0.99421 1.06400 0.15231  -0.03535 -0.11034 468 ILE C CD1 
2780 N N   . SER B 148 ? 1.09194 0.80107 0.84633 0.03866  -0.12719 -0.12035 469 SER C N   
2781 C CA  . SER B 148 ? 1.06431 0.78033 0.83375 0.00859  -0.14201 -0.12543 469 SER C CA  
2782 C C   . SER B 148 ? 1.06234 0.79309 0.88515 0.02066  -0.14402 -0.10052 469 SER C C   
2783 O O   . SER B 148 ? 1.27853 1.05377 1.13623 0.03945  -0.14752 -0.07967 469 SER C O   
2784 C CB  . SER B 148 ? 1.12636 0.90750 0.89499 -0.01479 -0.16500 -0.13174 469 SER C CB  
2785 O OG  . SER B 148 ? 1.15926 0.95533 0.94840 -0.04409 -0.17750 -0.13584 469 SER C OG  
2786 N N   . THR B 149 ? 1.01253 0.70189 0.83707 0.00830  -0.14010 -0.10322 470 THR C N   
2787 C CA  . THR B 149 ? 0.89927 0.60198 0.76616 0.01344  -0.14382 -0.08264 470 THR C CA  
2788 C C   . THR B 149 ? 1.10003 0.83379 0.98298 -0.01743 -0.15893 -0.08593 470 THR C C   
2789 O O   . THR B 149 ? 0.97741 0.70779 0.88317 -0.02104 -0.15958 -0.07448 470 THR C O   
2790 C CB  . THR B 149 ? 0.99029 0.63043 0.84901 0.02582  -0.12834 -0.07718 470 THR C CB  
2791 O OG1 . THR B 149 ? 1.46679 1.04659 1.28439 0.00135  -0.12074 -0.09796 470 THR C OG1 
2792 C CG2 . THR B 149 ? 1.06504 0.68784 0.91936 0.06156  -0.11221 -0.06967 470 THR C CG2 
2793 N N   . GLU B 150 ? 1.07115 0.84014 0.94257 -0.03943 -0.17089 -0.10076 471 GLU C N   
2794 C CA  . GLU B 150 ? 0.97900 0.78858 0.87061 -0.06835 -0.18435 -0.10384 471 GLU C CA  
2795 C C   . GLU B 150 ? 0.99919 0.86164 0.93928 -0.05235 -0.19032 -0.08000 471 GLU C C   
2796 O O   . GLU B 150 ? 0.98111 0.87478 0.93526 -0.02720 -0.19114 -0.06632 471 GLU C O   
2797 C CB  . GLU B 150 ? 1.10810 0.96032 0.98096 -0.09206 -0.19822 -0.12271 471 GLU C CB  
2798 C CG  . GLU B 150 ? 1.31562 1.22392 1.21497 -0.12228 -0.21240 -0.12591 471 GLU C CG  
2799 C CD  . GLU B 150 ? 1.40344 1.37472 1.29084 -0.14194 -0.23022 -0.14060 471 GLU C CD  
2800 O OE1 . GLU B 150 ? 1.37105 1.34404 1.22818 -0.12879 -0.23229 -0.14560 471 GLU C OE1 
2801 O OE2 . GLU B 150 ? 1.41075 1.43489 1.31910 -0.17070 -0.24224 -0.14653 471 GLU C OE2 
2802 N N   . ILE B 151 ? 0.89852 0.76563 0.86059 -0.06821 -0.19139 -0.07570 472 ILE C N   
2803 C CA  . ILE B 151 ? 0.86306 0.76978 0.86590 -0.05554 -0.19289 -0.05614 472 ILE C CA  
2804 C C   . ILE B 151 ? 0.79284 0.77037 0.81629 -0.05334 -0.20357 -0.05226 472 ILE C C   
2805 O O   . ILE B 151 ? 0.74246 0.75501 0.76579 -0.07683 -0.21353 -0.06372 472 ILE C O   
2806 C CB  . ILE B 151 ? 0.66490 0.55695 0.67952 -0.07450 -0.18928 -0.05410 472 ILE C CB  
2807 C CG1 . ILE B 151 ? 0.76785 0.59290 0.76207 -0.06801 -0.17872 -0.05069 472 ILE C CG1 
2808 C CG2 . ILE B 151 ? 0.81291 0.74695 0.86510 -0.06506 -0.18896 -0.03821 472 ILE C CG2 
2809 C CD1 . ILE B 151 ? 0.93979 0.74354 0.93656 -0.08536 -0.17395 -0.04636 472 ILE C CD1 
2810 N N   . TYR B 152 ? 0.98889 0.98930 1.03046 -0.02502 -0.20056 -0.03494 473 TYR C N   
2811 C CA  . TYR B 152 ? 1.00144 1.06394 1.06005 -0.01395 -0.20761 -0.02536 473 TYR C CA  
2812 C C   . TYR B 152 ? 0.85293 0.95556 0.94716 -0.02174 -0.20830 -0.01836 473 TYR C C   
2813 O O   . TYR B 152 ? 0.67698 0.75962 0.78812 -0.01974 -0.19782 -0.01137 473 TYR C O   
2814 C CB  . TYR B 152 ? 0.77786 0.83933 0.84085 0.01881  -0.19843 -0.00756 473 TYR C CB  
2815 C CG  . TYR B 152 ? 0.77305 0.88997 0.84764 0.03725  -0.20243 0.00739  473 TYR C CG  
2816 C CD1 . TYR B 152 ? 0.76077 0.90451 0.81017 0.04195  -0.21288 0.00491  473 TYR C CD1 
2817 C CD2 . TYR B 152 ? 0.72267 0.86283 0.82965 0.05198  -0.19408 0.02505  473 TYR C CD2 
2818 C CE1 . TYR B 152 ? 0.72822 0.92595 0.78607 0.06311  -0.21726 0.02321  473 TYR C CE1 
2819 C CE2 . TYR B 152 ? 0.58466 0.77205 0.70156 0.07485  -0.19497 0.04303  473 TYR C CE2 
2820 C CZ  . TYR B 152 ? 0.73491 0.95359 0.82799 0.08156  -0.20771 0.04387  473 TYR C CZ  
2821 O OH  . TYR B 152 ? 0.95665 1.22573 1.05754 0.10830  -0.20942 0.06616  473 TYR C OH  
2822 N N   . GLN B 153 ? 0.77478 0.93866 0.88006 -0.03075 -0.22036 -0.02044 474 GLN C N   
2823 C CA  . GLN B 153 ? 0.66172 0.87597 0.80518 -0.03514 -0.21972 -0.01273 474 GLN C CA  
2824 C C   . GLN B 153 ? 0.64340 0.90069 0.80984 0.00099  -0.21544 0.01098  474 GLN C C   
2825 O O   . GLN B 153 ? 0.68862 0.99156 0.84994 0.01408  -0.22663 0.01746  474 GLN C O   
2826 C CB  . GLN B 153 ? 0.68183 0.94673 0.82967 -0.06789 -0.23467 -0.02824 474 GLN C CB  
2827 C CG  . GLN B 153 ? 0.58787 0.92093 0.78133 -0.06994 -0.23372 -0.01867 474 GLN C CG  
2828 C CD  . GLN B 153 ? 0.62509 1.02189 0.82768 -0.10571 -0.24982 -0.03448 474 GLN C CD  
2829 O OE1 . GLN B 153 ? 0.71141 1.08551 0.88100 -0.13664 -0.25912 -0.05698 474 GLN C OE1 
2830 N NE2 . GLN B 153 ? 0.59588 1.07373 0.84369 -0.10259 -0.25140 -0.02357 474 GLN C NE2 
2831 N N   . ALA B 154 ? 0.61855 0.85809 0.80607 0.01708  -0.19784 0.02413  475 ALA C N   
2832 C CA  . ALA B 154 ? 0.64063 0.90505 0.84743 0.05244  -0.18667 0.04731  475 ALA C CA  
2833 C C   . ALA B 154 ? 0.65391 0.97560 0.89946 0.05821  -0.18189 0.05723  475 ALA C C   
2834 O O   . ALA B 154 ? 0.52002 0.88561 0.78228 0.08895  -0.17860 0.07781  475 ALA C O   
2835 C CB  . ALA B 154 ? 0.56863 0.77095 0.77001 0.06688  -0.16563 0.05420  475 ALA C CB  
2836 N N   . GLY B 155 ? 0.81647 1.13927 1.07634 0.03189  -0.17940 0.04523  476 GLY C N   
2837 C CA  . GLY B 155 ? 0.83207 1.21120 1.13129 0.03565  -0.17181 0.05327  476 GLY C CA  
2838 C C   . GLY B 155 ? 0.72142 1.18660 1.03998 0.02053  -0.19281 0.04947  476 GLY C C   
2839 O O   . GLY B 155 ? 0.62194 1.11234 0.92281 0.01708  -0.21326 0.04567  476 GLY C O   
2840 N N   . SER B 156 ? 0.61064 1.12495 0.96553 0.00909  -0.18693 0.04933  477 SER C N   
2841 C CA  . SER B 156 ? 0.57180 1.18106 0.95415 -0.01066 -0.20567 0.04481  477 SER C CA  
2842 C C   . SER B 156 ? 0.55361 1.14850 0.92333 -0.06577 -0.21425 0.01707  477 SER C C   
2843 O O   . SER B 156 ? 0.73756 1.37796 1.10193 -0.09341 -0.23609 0.00320  477 SER C O   
2844 C CB  . SER B 156 ? 0.52766 1.21317 0.96467 0.01148  -0.19200 0.06352  477 SER C CB  
2845 O OG  . SER B 156 ? 0.76892 1.41268 1.21532 0.00116  -0.16691 0.05861  477 SER C OG  
2846 N N   . THR B 157 ? 0.53065 1.06094 0.89162 -0.08357 -0.19641 0.00864  478 THR C N   
2847 C CA  . THR B 157 ? 0.49110 0.99446 0.83502 -0.13370 -0.19971 -0.01438 478 THR C CA  
2848 C C   . THR B 157 ? 0.74440 1.17363 1.03545 -0.14716 -0.21061 -0.02954 478 THR C C   
2849 O O   . THR B 157 ? 0.84872 1.22090 1.11560 -0.11996 -0.20669 -0.02217 478 THR C O   
2850 C CB  . THR B 157 ? 0.48761 0.94285 0.83312 -0.14437 -0.17609 -0.01467 478 THR C CB  
2851 O OG1 . THR B 157 ? 0.67628 1.05161 0.99374 -0.11944 -0.16485 -0.00757 478 THR C OG1 
2852 C CG2 . THR B 157 ? 0.52884 1.05606 0.92576 -0.13212 -0.16100 -0.00178 478 THR C CG2 
2853 N N   . PRO B 158 ? 0.78463 1.21232 1.05710 -0.18949 -0.22170 -0.05136 479 PRO C N   
2854 C CA  . PRO B 158 ? 0.60011 0.95210 0.82001 -0.20029 -0.22771 -0.06662 479 PRO C CA  
2855 C C   . PRO B 158 ? 0.68771 0.93959 0.87912 -0.19859 -0.21063 -0.06575 479 PRO C C   
2856 O O   . PRO B 158 ? 0.56934 0.80706 0.77432 -0.20322 -0.19574 -0.05933 479 PRO C O   
2857 C CB  . PRO B 158 ? 0.61936 0.99402 0.82846 -0.25160 -0.23834 -0.09211 479 PRO C CB  
2858 C CG  . PRO B 158 ? 0.69604 1.12867 0.94875 -0.27531 -0.23075 -0.09069 479 PRO C CG  
2859 C CD  . PRO B 158 ? 0.56352 1.05896 0.86240 -0.23116 -0.22676 -0.06422 479 PRO C CD  
2860 N N   . CYS B 159 ? 0.87904 1.06474 1.02941 -0.19046 -0.21274 -0.07140 480 CYS C N   
2861 C CA  . CYS B 159 ? 0.85092 0.94906 0.97404 -0.18275 -0.19958 -0.06761 480 CYS C CA  
2862 C C   . CYS B 159 ? 0.82763 0.85970 0.91373 -0.21682 -0.19377 -0.08453 480 CYS C C   
2863 O O   . CYS B 159 ? 0.84097 0.81734 0.91417 -0.22041 -0.18064 -0.07877 480 CYS C O   
2864 C CB  . CYS B 159 ? 0.79287 0.86106 0.89901 -0.14661 -0.20157 -0.05927 480 CYS C CB  
2865 S SG  . CYS B 159 ? 1.10290 1.22882 1.24444 -0.10582 -0.20224 -0.03780 480 CYS C SG  
2866 N N   . ASN B 160 ? 0.94833 0.98250 1.01306 -0.24196 -0.20200 -0.10506 481 ASN C N   
2867 C CA  . ASN B 160 ? 0.83842 0.80285 0.86363 -0.27840 -0.19255 -0.12424 481 ASN C CA  
2868 C C   . ASN B 160 ? 0.97561 0.84205 0.96259 -0.25626 -0.17948 -0.11749 481 ASN C C   
2869 O O   . ASN B 160 ? 1.18725 0.98703 1.15172 -0.27109 -0.16419 -0.11712 481 ASN C O   
2870 C CB  . ASN B 160 ? 0.78219 0.75557 0.82299 -0.31635 -0.18246 -0.12748 481 ASN C CB  
2871 C CG  . ASN B 160 ? 1.01439 1.09701 1.10184 -0.33536 -0.19432 -0.13145 481 ASN C CG  
2872 O OD1 . ASN B 160 ? 1.06585 1.19405 1.19220 -0.33071 -0.18891 -0.11745 481 ASN C OD1 
2873 N ND2 . ASN B 160 ? 1.15760 1.28640 1.24080 -0.35594 -0.21014 -0.15033 481 ASN C ND2 
2874 N N   . GLY B 161 ? 0.89096 0.75143 0.87142 -0.21901 -0.18441 -0.10992 482 GLY C N   
2875 C CA  . GLY B 161 ? 0.79741 0.57893 0.74720 -0.19462 -0.17314 -0.10288 482 GLY C CA  
2876 C C   . GLY B 161 ? 0.92157 0.68147 0.88338 -0.17352 -0.16539 -0.07976 482 GLY C C   
2877 O O   . GLY B 161 ? 1.05958 0.75828 0.99775 -0.15464 -0.15622 -0.07150 482 GLY C O   
2878 N N   . VAL B 162 ? 0.99018 0.80059 0.98674 -0.17520 -0.16818 -0.06892 483 VAL C N   
2879 C CA  . VAL B 162 ? 0.81576 0.61231 0.82039 -0.15907 -0.16189 -0.04943 483 VAL C CA  
2880 C C   . VAL B 162 ? 0.83036 0.68327 0.86886 -0.13367 -0.16837 -0.03839 483 VAL C C   
2881 O O   . VAL B 162 ? 0.81209 0.72419 0.87861 -0.13874 -0.17285 -0.04091 483 VAL C O   
2882 C CB  . VAL B 162 ? 0.71341 0.50480 0.71983 -0.18781 -0.15268 -0.04803 483 VAL C CB  
2883 C CG1 . VAL B 162 ? 0.69972 0.47552 0.70586 -0.17161 -0.14695 -0.02862 483 VAL C CG1 
2884 C CG2 . VAL B 162 ? 0.79977 0.52884 0.77006 -0.21721 -0.14251 -0.05988 483 VAL C CG2 
2885 N N   . GLU B 163 ? 0.65447 0.48978 0.69080 -0.10653 -0.16740 -0.02561 484 GLU C N   
2886 C CA  . GLU B 163 ? 0.63966 0.51587 0.70265 -0.08505 -0.16968 -0.01673 484 GLU C CA  
2887 C C   . GLU B 163 ? 0.62346 0.51361 0.70092 -0.09000 -0.16336 -0.00866 484 GLU C C   
2888 O O   . GLU B 163 ? 0.59290 0.45458 0.65492 -0.10260 -0.15853 -0.00524 484 GLU C O   
2889 C CB  . GLU B 163 ? 0.56324 0.42058 0.61960 -0.05852 -0.17047 -0.00921 484 GLU C CB  
2890 C CG  . GLU B 163 ? 0.73861 0.55932 0.78035 -0.05268 -0.16753 0.00125  484 GLU C CG  
2891 C CD  . GLU B 163 ? 0.68566 0.52030 0.74007 -0.03039 -0.16867 0.01135  484 GLU C CD  
2892 O OE1 . GLU B 163 ? 0.75016 0.60845 0.81987 -0.03260 -0.16735 0.01564  484 GLU C OE1 
2893 O OE2 . GLU B 163 ? 0.77244 0.59468 0.82126 -0.01243 -0.16899 0.01364  484 GLU C OE2 
2894 N N   . GLY B 164 ? 0.51784 0.44790 0.62101 -0.07897 -0.16104 -0.00514 485 GLY C N   
2895 C CA  . GLY B 164 ? 0.50549 0.44717 0.62019 -0.08241 -0.15133 -0.00034 485 GLY C CA  
2896 C C   . GLY B 164 ? 0.47888 0.45793 0.62013 -0.06655 -0.14506 0.00275  485 GLY C C   
2897 O O   . GLY B 164 ? 0.75549 0.73917 0.90093 -0.04773 -0.14758 0.00588  485 GLY C O   
2898 N N   . PHE B 165 ? 0.47496 0.47788 0.63300 -0.07217 -0.13381 0.00328  486 PHE C N   
2899 C CA  . PHE B 165 ? 0.45930 0.49390 0.64232 -0.05299 -0.12363 0.00858  486 PHE C CA  
2900 C C   . PHE B 165 ? 0.47937 0.55684 0.67977 -0.04379 -0.13339 0.01040  486 PHE C C   
2901 O O   . PHE B 165 ? 0.62073 0.72367 0.82654 -0.06112 -0.14165 0.00457  486 PHE C O   
2902 C CB  . PHE B 165 ? 0.46367 0.51219 0.65983 -0.05886 -0.10573 0.00883  486 PHE C CB  
2903 C CG  . PHE B 165 ? 0.47471 0.48499 0.64979 -0.06606 -0.09452 0.00640  486 PHE C CG  
2904 C CD1 . PHE B 165 ? 0.53852 0.51879 0.69679 -0.05995 -0.09796 0.00657  486 PHE C CD1 
2905 C CD2 . PHE B 165 ? 0.74803 0.75733 0.91936 -0.08089 -0.08046 0.00336  486 PHE C CD2 
2906 C CE1 . PHE B 165 ? 0.48788 0.44192 0.62553 -0.07030 -0.09054 0.00281  486 PHE C CE1 
2907 C CE2 . PHE B 165 ? 0.71783 0.69449 0.86346 -0.08962 -0.07146 -0.00020 486 PHE C CE2 
2908 C CZ  . PHE B 165 ? 0.50575 0.45679 0.63427 -0.08523 -0.07800 -0.00095 486 PHE C CZ  
2909 N N   . ASN B 166 ? 0.52024 0.60631 0.72681 -0.01863 -0.13219 0.01844  487 ASN C N   
2910 C CA  . ASN B 166 ? 0.51287 0.64100 0.72960 -0.00550 -0.14296 0.02309  487 ASN C CA  
2911 C C   . ASN B 166 ? 0.51376 0.63450 0.70891 -0.02091 -0.16183 0.01228  487 ASN C C   
2912 O O   . ASN B 166 ? 0.64860 0.81004 0.84746 -0.02144 -0.17411 0.01060  487 ASN C O   
2913 C CB  . ASN B 166 ? 0.44232 0.63270 0.69076 -0.00307 -0.14042 0.02825  487 ASN C CB  
2914 C CG  . ASN B 166 ? 0.54978 0.74345 0.81814 0.01808  -0.11679 0.03978  487 ASN C CG  
2915 O OD1 . ASN B 166 ? 0.52391 0.70699 0.79724 0.00612  -0.10303 0.03539  487 ASN C OD1 
2916 N ND2 . ASN B 166 ? 0.58189 0.78483 0.85752 0.05019  -0.10912 0.05485  487 ASN C ND2 
2917 N N   . CYS B 167 ? 0.57227 0.64186 0.74285 -0.03274 -0.16349 0.00499  488 CYS C N   
2918 C CA  . CYS B 167 ? 0.59322 0.63994 0.73794 -0.04445 -0.17542 -0.00569 488 CYS C CA  
2919 C C   . CYS B 167 ? 0.60331 0.60329 0.72964 -0.03163 -0.17237 -0.00271 488 CYS C C   
2920 O O   . CYS B 167 ? 0.49293 0.45698 0.60751 -0.03992 -0.16966 -0.00354 488 CYS C O   
2921 C CB  . CYS B 167 ? 0.71532 0.74867 0.85065 -0.07557 -0.17755 -0.01698 488 CYS C CB  
2922 S SG  . CYS B 167 ? 0.70022 0.80168 0.86203 -0.09649 -0.18243 -0.02287 488 CYS C SG  
2923 N N   . TYR B 168 ? 0.72192 0.72727 0.84652 -0.01062 -0.17244 0.00256  489 TYR C N   
2924 C CA  . TYR B 168 ? 0.74167 0.71689 0.85816 0.00330  -0.16722 0.00731  489 TYR C CA  
2925 C C   . TYR B 168 ? 0.68739 0.63817 0.77893 0.00572  -0.17252 0.00018  489 TYR C C   
2926 O O   . TYR B 168 ? 0.59604 0.55343 0.67285 -0.00187 -0.17974 -0.00940 489 TYR C O   
2927 C CB  . TYR B 168 ? 0.59207 0.58328 0.72199 0.02422  -0.15800 0.01861  489 TYR C CB  
2928 C CG  . TYR B 168 ? 0.44956 0.46547 0.60092 0.02728  -0.14944 0.02557  489 TYR C CG  
2929 C CD1 . TYR B 168 ? 0.44415 0.45298 0.60419 0.01418  -0.14302 0.02333  489 TYR C CD1 
2930 C CD2 . TYR B 168 ? 0.45061 0.49613 0.61103 0.04592  -0.14591 0.03583  489 TYR C CD2 
2931 C CE1 . TYR B 168 ? 0.44026 0.46786 0.61865 0.01950  -0.13078 0.02894  489 TYR C CE1 
2932 C CE2 . TYR B 168 ? 0.44692 0.51277 0.62784 0.05446  -0.13449 0.04461  489 TYR C CE2 
2933 C CZ  . TYR B 168 ? 0.51627 0.57163 0.70675 0.04114  -0.12573 0.04001  489 TYR C CZ  
2934 O OH  . TYR B 168 ? 0.48697 0.55894 0.69669 0.05204  -0.11014 0.04802  489 TYR C OH  
2935 N N   . PHE B 169 ? 0.65241 0.57707 0.73909 0.01591  -0.16781 0.00418  490 PHE C N   
2936 C CA  . PHE B 169 ? 0.73104 0.63033 0.79590 0.02480  -0.16750 -0.00059 490 PHE C CA  
2937 C C   . PHE B 169 ? 0.70177 0.61887 0.76394 0.04162  -0.16425 0.00193  490 PHE C C   
2938 O O   . PHE B 169 ? 0.71956 0.65536 0.79973 0.05262  -0.15770 0.01269  490 PHE C O   
2939 C CB  . PHE B 169 ? 0.71775 0.59404 0.78443 0.03403  -0.16293 0.00634  490 PHE C CB  
2940 C CG  . PHE B 169 ? 0.82217 0.66394 0.86536 0.04413  -0.15944 0.00189  490 PHE C CG  
2941 C CD1 . PHE B 169 ? 0.87746 0.72108 0.92183 0.06525  -0.15176 0.00595  490 PHE C CD1 
2942 C CD2 . PHE B 169 ? 0.64638 0.44973 0.66502 0.03254  -0.16008 -0.00635 490 PHE C CD2 
2943 C CE1 . PHE B 169 ? 0.80477 0.61401 0.82697 0.07803  -0.14445 0.00183  490 PHE C CE1 
2944 C CE2 . PHE B 169 ? 0.68355 0.44490 0.67664 0.04406  -0.15198 -0.01083 490 PHE C CE2 
2945 C CZ  . PHE B 169 ? 0.66814 0.43316 0.66336 0.06856  -0.14398 -0.00675 490 PHE C CZ  
2946 N N   . PRO B 170 ? 0.74043 0.64809 0.77593 0.04245  -0.16664 -0.00826 491 PRO C N   
2947 C CA  . PRO B 170 ? 0.75494 0.68261 0.78181 0.05773  -0.16401 -0.00483 491 PRO C CA  
2948 C C   . PRO B 170 ? 0.77598 0.69463 0.80825 0.07840  -0.15055 0.00501  491 PRO C C   
2949 O O   . PRO B 170 ? 0.67391 0.61125 0.70761 0.09164  -0.14431 0.01432  491 PRO C O   
2950 C CB  . PRO B 170 ? 0.89484 0.80963 0.88462 0.04796  -0.16990 -0.02258 491 PRO C CB  
2951 C CG  . PRO B 170 ? 1.01236 0.88032 0.98994 0.03678  -0.16698 -0.03296 491 PRO C CG  
2952 C CD  . PRO B 170 ? 0.79158 0.66519 0.79821 0.02790  -0.16956 -0.02419 491 PRO C CD  
2953 N N   . LEU B 171 ? 0.79473 0.68852 0.83097 0.08229  -0.14494 0.00512  492 LEU C N   
2954 C CA  . LEU B 171 ? 0.73915 0.63370 0.78582 0.10036  -0.13201 0.01391  492 LEU C CA  
2955 C C   . LEU B 171 ? 0.65711 0.56983 0.73862 0.09772  -0.12940 0.02537  492 LEU C C   
2956 O O   . LEU B 171 ? 0.70573 0.61878 0.79786 0.08427  -0.13714 0.02520  492 LEU C O   
2957 C CB  . LEU B 171 ? 0.66550 0.52921 0.69724 0.11064  -0.12597 0.00865  492 LEU C CB  
2958 C CG  . LEU B 171 ? 0.75456 0.58905 0.74425 0.11133  -0.12363 -0.00705 492 LEU C CG  
2959 C CD1 . LEU B 171 ? 0.77192 0.56644 0.74754 0.12527  -0.11211 -0.01062 492 LEU C CD1 
2960 C CD2 . LEU B 171 ? 0.71689 0.56897 0.69158 0.12085  -0.11728 -0.00685 492 LEU C CD2 
2961 N N   . GLN B 172 ? 0.62147 0.54892 0.71802 0.10790  -0.11692 0.03400  493 GLN C N   
2962 C CA  . GLN B 172 ? 0.49751 0.44301 0.62470 0.10079  -0.11232 0.04158  493 GLN C CA  
2963 C C   . GLN B 172 ? 0.60049 0.55960 0.74365 0.11188  -0.10153 0.04703  493 GLN C C   
2964 O O   . GLN B 172 ? 0.58820 0.54302 0.71926 0.12743  -0.09160 0.04744  493 GLN C O   
2965 C CB  . GLN B 172 ? 0.58447 0.53795 0.71871 0.09555  -0.10375 0.04704  493 GLN C CB  
2966 C CG  . GLN B 172 ? 0.89944 0.85914 1.05477 0.07823  -0.10252 0.04763  493 GLN C CG  
2967 C CD  . GLN B 172 ? 0.66821 0.62180 0.81908 0.06628  -0.11660 0.04149  493 GLN C CD  
2968 O OE1 . GLN B 172 ? 0.78180 0.73930 0.94321 0.05206  -0.11972 0.03946  493 GLN C OE1 
2969 N NE2 . GLN B 172 ? 0.46128 0.40827 0.59512 0.06964  -0.12477 0.03795  493 GLN C NE2 
2970 N N   . SER B 173 ? 0.56386 0.54429 0.73423 0.10296  -0.10323 0.05089  494 SER C N   
2971 C CA  . SER B 173 ? 0.52764 0.53523 0.72165 0.11217  -0.09603 0.05710  494 SER C CA  
2972 C C   . SER B 173 ? 0.57188 0.60278 0.78764 0.10275  -0.07980 0.06099  494 SER C C   
2973 O O   . SER B 173 ? 0.72462 0.75712 0.94785 0.08211  -0.07830 0.05908  494 SER C O   
2974 C CB  . SER B 173 ? 0.57114 0.59911 0.78273 0.10740  -0.10972 0.06052  494 SER C CB  
2975 O OG  . SER B 173 ? 0.52139 0.58946 0.76252 0.11753  -0.10424 0.06869  494 SER C OG  
2976 N N   . TYR B 174 ? 0.65991 0.70432 0.88350 0.11705  -0.06438 0.06580  495 TYR C N   
2977 C CA  . TYR B 174 ? 0.56958 0.64052 0.81878 0.10553  -0.04639 0.07029  495 TYR C CA  
2978 C C   . TYR B 174 ? 0.52645 0.64350 0.81392 0.08808  -0.05376 0.07067  495 TYR C C   
2979 O O   . TYR B 174 ? 0.95651 1.09548 1.25519 0.09821  -0.06831 0.07332  495 TYR C O   
2980 C CB  . TYR B 174 ? 0.50155 0.58005 0.75054 0.12555  -0.02659 0.07586  495 TYR C CB  
2981 C CG  . TYR B 174 ? 0.56015 0.60361 0.77274 0.13491  -0.01354 0.07737  495 TYR C CG  
2982 C CD1 . TYR B 174 ? 0.77140 0.79489 0.97251 0.12168  -0.00806 0.07988  495 TYR C CD1 
2983 C CD2 . TYR B 174 ? 0.62898 0.65925 0.81572 0.15864  -0.00553 0.07715  495 TYR C CD2 
2984 C CE1 . TYR B 174 ? 0.86166 0.85979 1.02879 0.13413  0.00232  0.08563  495 TYR C CE1 
2985 C CE2 . TYR B 174 ? 0.74919 0.75391 0.89827 0.16665  0.00399  0.07932  495 TYR C CE2 
2986 C CZ  . TYR B 174 ? 0.87871 0.87090 1.01926 0.15546  0.00649  0.08531  495 TYR C CZ  
2987 O OH  . TYR B 174 ? 0.96205 0.93506 1.06448 0.16718  0.01438  0.09166  495 TYR C OH  
2988 N N   . GLY B 175 ? 0.48985 0.62090 0.79479 0.06106  -0.04300 0.06834  496 GLY C N   
2989 C CA  . GLY B 175 ? 0.59141 0.77319 0.93096 0.03749  -0.05049 0.06577  496 GLY C CA  
2990 C C   . GLY B 175 ? 0.60860 0.84995 0.98542 0.04922  -0.04646 0.07384  496 GLY C C   
2991 O O   . GLY B 175 ? 0.75550 1.03135 1.14716 0.06387  -0.06386 0.07950  496 GLY C O   
2992 N N   . PHE B 176 ? 0.72912 0.98345 1.12159 0.04468  -0.02141 0.07647  497 PHE C N   
2993 C CA  . PHE B 176 ? 0.55458 0.86816 0.98549 0.05776  -0.01122 0.08499  497 PHE C CA  
2994 C C   . PHE B 176 ? 0.67664 1.07079 1.15459 0.03977  -0.02695 0.08570  497 PHE C C   
2995 O O   . PHE B 176 ? 0.64786 1.07551 1.13866 0.06318  -0.04589 0.09393  497 PHE C O   
2996 C CB  . PHE B 176 ? 0.51155 0.80979 0.92695 0.10285  -0.01211 0.09292  497 PHE C CB  
2997 C CG  . PHE B 176 ? 0.63251 0.87093 1.00633 0.11915  0.00638  0.09225  497 PHE C CG  
2998 C CD1 . PHE B 176 ? 0.66553 0.87787 1.02596 0.09974  0.02535  0.09072  497 PHE C CD1 
2999 C CD2 . PHE B 176 ? 0.77622 0.98287 1.12063 0.15345  0.00585  0.09342  497 PHE C CD2 
3000 C CE1 . PHE B 176 ? 0.62337 0.78752 0.94288 0.11663  0.04011  0.09312  497 PHE C CE1 
3001 C CE2 . PHE B 176 ? 0.85479 1.01312 1.15700 0.16539  0.02035  0.09134  497 PHE C CE2 
3002 C CZ  . PHE B 176 ? 0.75743 0.89885 1.04774 0.14820  0.03587  0.09260  497 PHE C CZ  
3003 N N   . GLN B 177 ? 0.80339 1.22872 1.30510 -0.00220 -0.01830 0.07760  498 GLN C N   
3004 C CA  . GLN B 177 ? 0.63762 1.15319 1.18772 -0.02782 -0.03073 0.07614  498 GLN C CA  
3005 C C   . GLN B 177 ? 0.55994 1.11767 1.14699 -0.05524 -0.00276 0.07385  498 GLN C C   
3006 O O   . GLN B 177 ? 0.68737 1.18775 1.25231 -0.06742 0.02518  0.06966  498 GLN C O   
3007 C CB  . GLN B 177 ? 0.60590 1.11691 1.14190 -0.06606 -0.05096 0.06175  498 GLN C CB  
3008 C CG  . GLN B 177 ? 0.65224 1.14716 1.16307 -0.04276 -0.08111 0.06639  498 GLN C CG  
3009 C CD  . GLN B 177 ? 0.77424 1.23505 1.25419 -0.07680 -0.09316 0.05069  498 GLN C CD  
3010 O OE1 . GLN B 177 ? 0.89689 1.31902 1.34465 -0.06128 -0.10978 0.05230  498 GLN C OE1 
3011 N NE2 . GLN B 177 ? 0.61188 1.08346 1.09954 -0.12501 -0.08181 0.03431  498 GLN C NE2 
3012 N N   . PRO B 178 ? 0.50086 1.16124 1.14500 -0.06491 -0.00847 0.07829  499 PRO C N   
3013 C CA  . PRO B 178 ? 0.53293 1.24080 1.21758 -0.09239 0.02086  0.07655  499 PRO C CA  
3014 C C   . PRO B 178 ? 0.74213 1.42028 1.41603 -0.15362 0.03732  0.05688  499 PRO C C   
3015 O O   . PRO B 178 ? 0.81916 1.50784 1.51325 -0.17827 0.06940  0.05491  499 PRO C O   
3016 C CB  . PRO B 178 ? 0.62978 1.46767 1.38147 -0.09040 0.00339  0.08547  499 PRO C CB  
3017 C CG  . PRO B 178 ? 0.50053 1.35481 1.24043 -0.08439 -0.03711 0.08573  499 PRO C CG  
3018 C CD  . PRO B 178 ? 0.48286 1.22587 1.15881 -0.04996 -0.04106 0.08751  499 PRO C CD  
3019 N N   . THR B 179 ? 0.81087 1.44735 1.45131 -0.17893 0.02024  0.04221  500 THR C N   
3020 C CA  . THR B 179 ? 0.86740 1.46314 1.49083 -0.23624 0.03895  0.02143  500 THR C CA  
3021 C C   . THR B 179 ? 0.94631 1.41774 1.51079 -0.22612 0.06256  0.02044  500 THR C C   
3022 O O   . THR B 179 ? 1.26739 1.68504 1.80804 -0.26649 0.08071  0.00458  500 THR C O   
3023 C CB  . THR B 179 ? 0.97172 1.60033 1.59280 -0.27404 0.00951  0.00365  500 THR C CB  
3024 O OG1 . THR B 179 ? 1.16318 1.74508 1.74429 -0.24086 -0.01629 0.00786  500 THR C OG1 
3025 C CG2 . THR B 179 ? 0.63692 1.40131 1.31871 -0.28711 -0.01485 0.00637  500 THR C CG2 
3026 N N   . ASN B 180 ? 0.69484 1.12066 1.23431 -0.17328 0.06356  0.03693  501 ASN C N   
3027 C CA  . ASN B 180 ? 0.87758 1.19916 1.36414 -0.15932 0.08270  0.03947  501 ASN C CA  
3028 C C   . ASN B 180 ? 0.88457 1.17373 1.36838 -0.17030 0.12580  0.04531  501 ASN C C   
3029 O O   . ASN B 180 ? 0.61693 0.96287 1.13888 -0.17774 0.14100  0.05023  501 ASN C O   
3030 C CB  . ASN B 180 ? 0.56377 0.85484 1.02268 -0.10368 0.06646  0.05313  501 ASN C CB  
3031 C CG  . ASN B 180 ? 0.60093 0.89766 1.04927 -0.09408 0.02970  0.04820  501 ASN C CG  
3032 O OD1 . ASN B 180 ? 0.63922 0.96676 1.09579 -0.06152 0.00866  0.05679  501 ASN C OD1 
3033 N ND2 . ASN B 180 ? 1.08630 1.34803 1.51332 -0.12199 0.02513  0.03464  501 ASN C ND2 
3034 N N   . GLY B 181 ? 0.82675 1.02421 1.26477 -0.16940 0.14724  0.04680  502 GLY C N   
3035 C CA  . GLY B 181 ? 0.68793 0.84057 1.11274 -0.17415 0.18998  0.05686  502 GLY C CA  
3036 C C   . GLY B 181 ? 0.72425 0.88225 1.14253 -0.12782 0.19679  0.07732  502 GLY C C   
3037 O O   . GLY B 181 ? 0.84191 1.01773 1.25499 -0.08865 0.16998  0.08281  502 GLY C O   
3038 N N   . VAL B 182 ? 1.06345 1.32506 0.84000 -0.04101 0.05920  -0.04775 503 VAL C N   
3039 C CA  . VAL B 182 ? 1.08481 1.29459 0.79926 -0.04078 0.06306  -0.03898 503 VAL C CA  
3040 C C   . VAL B 182 ? 1.15497 1.33293 0.84747 -0.02935 0.03197  -0.03769 503 VAL C C   
3041 O O   . VAL B 182 ? 1.15880 1.31912 0.82108 -0.02566 0.03233  -0.03537 503 VAL C O   
3042 C CB  . VAL B 182 ? 1.12662 1.28504 0.79200 -0.05292 0.07588  -0.03136 503 VAL C CB  
3043 C CG1 . VAL B 182 ? 1.09397 1.20699 0.69653 -0.05319 0.08289  -0.02290 503 VAL C CG1 
3044 C CG2 . VAL B 182 ? 1.09971 1.29509 0.79094 -0.06690 0.10583  -0.03485 503 VAL C CG2 
3045 N N   . GLY B 183 ? 1.16300 1.33515 0.87036 -0.02358 0.00492  -0.04032 504 GLY C N   
3046 C CA  . GLY B 183 ? 1.15676 1.30854 0.84792 -0.01286 -0.02582 -0.04046 504 GLY C CA  
3047 C C   . GLY B 183 ? 1.09342 1.29056 0.82168 -0.00657 -0.03365 -0.04729 504 GLY C C   
3048 O O   . GLY B 183 ? 0.91387 1.09447 0.62341 -0.00059 -0.05528 -0.04817 504 GLY C O   
3049 N N   . TYR B 184 ? 1.05799 1.31278 0.83749 -0.00830 -0.01623 -0.05185 505 TYR C N   
3050 C CA  . TYR B 184 ? 0.99590 1.29564 0.81346 -0.00265 -0.02079 -0.05639 505 TYR C CA  
3051 C C   . TYR B 184 ? 1.01539 1.33251 0.83334 -0.00448 0.00927  -0.05374 505 TYR C C   
3052 O O   . TYR B 184 ? 1.08177 1.45080 0.94494 -0.00073 0.01637  -0.05598 505 TYR C O   
3053 C CB  . TYR B 184 ? 0.95032 1.31155 0.83462 0.00065  -0.03080 -0.06354 505 TYR C CB  
3054 C CG  . TYR B 184 ? 1.08201 1.43408 0.97115 0.00677  -0.06488 -0.06763 505 TYR C CG  
3055 C CD1 . TYR B 184 ? 1.13964 1.51952 1.05415 0.01319  -0.08818 -0.07225 505 TYR C CD1 
3056 C CD2 . TYR B 184 ? 1.22157 1.53709 1.08884 0.00652  -0.07330 -0.06646 505 TYR C CD2 
3057 C CE1 . TYR B 184 ? 0.95953 1.33631 0.87847 0.02004  -0.11951 -0.07647 505 TYR C CE1 
3058 C CE2 . TYR B 184 ? 1.21342 1.52132 1.08415 0.01520  -0.10428 -0.06974 505 TYR C CE2 
3059 C CZ  . TYR B 184 ? 1.03057 1.37171 0.92753 0.02238  -0.12760 -0.07517 505 TYR C CZ  
3060 O OH  . TYR B 184 ? 1.03830 1.37714 0.93890 0.03218  -0.15860 -0.07893 505 TYR C OH  
3061 N N   . GLN B 185 ? 0.98082 1.25539 0.74726 -0.00916 0.02755  -0.04825 506 GLN C N   
3062 C CA  . GLN B 185 ? 0.94434 1.22736 0.70102 -0.00905 0.05641  -0.04555 506 GLN C CA  
3063 C C   . GLN B 185 ? 0.94620 1.18537 0.65743 -0.00559 0.05093  -0.04484 506 GLN C C   
3064 O O   . GLN B 185 ? 1.04946 1.24233 0.72125 -0.00657 0.02979  -0.04488 506 GLN C O   
3065 C CB  . GLN B 185 ? 1.01000 1.28148 0.74142 -0.01760 0.08282  -0.04132 506 GLN C CB  
3066 C CG  . GLN B 185 ? 0.91364 1.23967 0.69373 -0.02284 0.09805  -0.04399 506 GLN C CG  
3067 C CD  . GLN B 185 ? 1.00744 1.32304 0.76088 -0.03411 0.12486  -0.04064 506 GLN C CD  
3068 O OE1 . GLN B 185 ? 1.15051 1.42100 0.84963 -0.03686 0.13379  -0.03532 506 GLN C OE1 
3069 N NE2 . GLN B 185 ? 0.90102 1.26088 0.69266 -0.04185 0.13814  -0.04461 506 GLN C NE2 
3070 N N   . PRO B 186 ? 0.97170 1.22485 0.68697 -0.00092 0.06985  -0.04462 507 PRO C N   
3071 C CA  . PRO B 186 ? 1.04880 1.25879 0.72148 0.00157  0.06599  -0.04626 507 PRO C CA  
3072 C C   . PRO B 186 ? 1.00039 1.15754 0.60793 -0.00298 0.07566  -0.04352 507 PRO C C   
3073 O O   . PRO B 186 ? 1.01514 1.17680 0.61247 -0.00644 0.09840  -0.03916 507 PRO C O   
3074 C CB  . PRO B 186 ? 1.03537 1.27704 0.73428 0.00915  0.08814  -0.04585 507 PRO C CB  
3075 C CG  . PRO B 186 ? 1.00498 1.29705 0.73895 0.00987  0.11200  -0.04189 507 PRO C CG  
3076 C CD  . PRO B 186 ? 0.83107 1.14204 0.59173 0.00354  0.09490  -0.04327 507 PRO C CD  
3077 N N   . TYR B 187 ? 1.00501 1.11517 0.56825 -0.00381 0.05818  -0.04655 508 TYR C N   
3078 C CA  . TYR B 187 ? 1.16039 1.22000 0.65838 -0.00761 0.06450  -0.04445 508 TYR C CA  
3079 C C   . TYR B 187 ? 1.22620 1.25611 0.69196 -0.00510 0.06249  -0.05145 508 TYR C C   
3080 O O   . TYR B 187 ? 1.31452 1.33402 0.77978 -0.00544 0.03761  -0.05748 508 TYR C O   
3081 C CB  . TYR B 187 ? 1.17105 1.19910 0.63984 -0.01223 0.04157  -0.04067 508 TYR C CB  
3082 C CG  . TYR B 187 ? 1.19204 1.22769 0.66801 -0.01745 0.05183  -0.03298 508 TYR C CG  
3083 C CD1 . TYR B 187 ? 1.09863 1.17454 0.62952 -0.01732 0.04698  -0.03333 508 TYR C CD1 
3084 C CD2 . TYR B 187 ? 1.33859 1.34114 0.76580 -0.02375 0.06675  -0.02606 508 TYR C CD2 
3085 C CE1 . TYR B 187 ? 1.20547 1.28582 0.74255 -0.02404 0.05726  -0.02825 508 TYR C CE1 
3086 C CE2 . TYR B 187 ? 1.21447 1.22099 0.64706 -0.03115 0.07724  -0.01937 508 TYR C CE2 
3087 C CZ  . TYR B 187 ? 1.17504 1.21909 0.66259 -0.03164 0.07265  -0.02111 508 TYR C CZ  
3088 O OH  . TYR B 187 ? 1.16861 1.21436 0.66132 -0.04084 0.08400  -0.01635 508 TYR C OH  
3089 N N   . ARG B 188 ? 1.26382 1.28149 0.70274 -0.00293 0.08891  -0.05177 509 ARG C N   
3090 C CA  . ARG B 188 ? 1.43912 1.42426 0.84373 -0.00075 0.09041  -0.06006 509 ARG C CA  
3091 C C   . ARG B 188 ? 1.46009 1.39655 0.80140 -0.00665 0.07680  -0.06201 509 ARG C C   
3092 O O   . ARG B 188 ? 1.52983 1.45104 0.83677 -0.00960 0.08819  -0.05567 509 ARG C O   
3093 C CB  . ARG B 188 ? 1.34356 1.33549 0.74402 0.00639  0.12454  -0.06013 509 ARG C CB  
3094 C CG  . ARG B 188 ? 1.17641 1.21833 0.63732 0.01462  0.13901  -0.05730 509 ARG C CG  
3095 C CD  . ARG B 188 ? 1.28419 1.32865 0.73650 0.02510  0.17120  -0.05773 509 ARG C CD  
3096 N NE  . ARG B 188 ? 1.18970 1.28109 0.69819 0.03517  0.18384  -0.05393 509 ARG C NE  
3097 C CZ  . ARG B 188 ? 1.16909 1.26935 0.68094 0.04814  0.21059  -0.05290 509 ARG C CZ  
3098 N NH1 . ARG B 188 ? 1.25584 1.32085 0.71843 0.05239  0.22757  -0.05706 509 ARG C NH1 
3099 N NH2 . ARG B 188 ? 1.01184 1.15751 0.57587 0.05813  0.22055  -0.04742 509 ARG C NH2 
3100 N N   . VAL B 189 ? 1.44142 1.35642 0.76709 -0.00903 0.05278  -0.07061 510 VAL C N   
3101 C CA  . VAL B 189 ? 1.53489 1.40988 0.80289 -0.01392 0.03600  -0.07313 510 VAL C CA  
3102 C C   . VAL B 189 ? 1.41935 1.26461 0.64955 -0.01469 0.04308  -0.08582 510 VAL C C   
3103 O O   . VAL B 189 ? 1.52456 1.37509 0.77728 -0.01396 0.04225  -0.09532 510 VAL C O   
3104 C CB  . VAL B 189 ? 1.53054 1.40886 0.80817 -0.01625 0.00016  -0.07403 510 VAL C CB  
3105 C CG1 . VAL B 189 ? 1.39805 1.23931 0.61452 -0.01955 -0.01672 -0.07506 510 VAL C CG1 
3106 C CG2 . VAL B 189 ? 1.32823 1.23543 0.64669 -0.01427 -0.00582 -0.06328 510 VAL C CG2 
3107 N N   . VAL B 190 ? 1.43859 1.25211 0.61106 -0.01670 0.05065  -0.08622 511 VAL C N   
3108 C CA  . VAL B 190 ? 1.67868 1.46103 0.80807 -0.01806 0.05659  -0.10007 511 VAL C CA  
3109 C C   . VAL B 190 ? 1.68727 1.44257 0.76336 -0.02405 0.03429  -0.10244 511 VAL C C   
3110 O O   . VAL B 190 ? 1.68410 1.42695 0.72328 -0.02472 0.03914  -0.09293 511 VAL C O   
3111 C CB  . VAL B 190 ? 1.71858 1.49341 0.82703 -0.01284 0.09127  -0.09989 511 VAL C CB  
3112 C CG1 . VAL B 190 ? 1.49795 1.23842 0.56091 -0.01376 0.09663  -0.11635 511 VAL C CG1 
3113 C CG2 . VAL B 190 ? 1.45850 1.26575 0.62037 -0.00470 0.11330  -0.09594 511 VAL C CG2 
3114 N N   . VAL B 191 ? 1.68669 1.43524 0.75824 -0.02880 0.01023  -0.11465 512 VAL C N   
3115 C CA  . VAL B 191 ? 1.69613 1.42606 0.71980 -0.03365 -0.01361 -0.11808 512 VAL C CA  
3116 C C   . VAL B 191 ? 1.75633 1.45713 0.72993 -0.03770 -0.00382 -0.13445 512 VAL C C   
3117 O O   . VAL B 191 ? 1.66160 1.35661 0.64484 -0.04111 -0.00067 -0.15092 512 VAL C O   
3118 C CB  . VAL B 191 ? 1.61656 1.36312 0.66418 -0.03693 -0.04699 -0.12299 512 VAL C CB  
3119 C CG1 . VAL B 191 ? 1.60651 1.33882 0.60306 -0.04017 -0.07144 -0.12608 512 VAL C CG1 
3120 C CG2 . VAL B 191 ? 1.50113 1.27769 0.60007 -0.03176 -0.05577 -0.10841 512 VAL C CG2 
3121 N N   . LEU B 192 ? 1.94749 1.63319 0.87483 -0.03731 0.00149  -0.12957 513 LEU C N   
3122 C CA  . LEU B 192 ? 2.04417 1.71467 0.93995 -0.03950 0.01017  -0.14349 513 LEU C CA  
3123 C C   . LEU B 192 ? 2.06309 1.73455 0.93515 -0.04466 -0.01829 -0.14974 513 LEU C C   
3124 O O   . LEU B 192 ? 2.10716 1.78667 0.96917 -0.04247 -0.03345 -0.13488 513 LEU C O   
3125 C CB  . LEU B 192 ? 1.91592 1.58479 0.79479 -0.03469 0.03492  -0.13330 513 LEU C CB  
3126 C CG  . LEU B 192 ? 1.84806 1.52456 0.75280 -0.02837 0.06577  -0.12778 513 LEU C CG  
3127 C CD1 . LEU B 192 ? 1.73473 1.41680 0.62462 -0.02516 0.08628  -0.11775 513 LEU C CD1 
3128 C CD2 . LEU B 192 ? 1.80831 1.47415 0.72291 -0.02634 0.08005  -0.14605 513 LEU C CD2 
3129 N N   . SER B 193 ? 1.96941 1.63350 0.83299 -0.05130 -0.02451 -0.17164 514 SER C N   
3130 C CA  . SER B 193 ? 1.97328 1.64562 0.81832 -0.05690 -0.05031 -0.18102 514 SER C CA  
3131 C C   . SER B 193 ? 2.02720 1.68683 0.83662 -0.05947 -0.03822 -0.19584 514 SER C C   
3132 O O   . SER B 193 ? 2.00893 1.65163 0.81685 -0.06367 -0.02402 -0.21506 514 SER C O   
3133 C CB  . SER B 193 ? 2.08145 1.76306 0.95087 -0.06510 -0.07070 -0.19615 514 SER C CB  
3134 O OG  . SER B 193 ? 2.26529 1.96279 1.16958 -0.06202 -0.08281 -0.18302 514 SER C OG  
3135 N N   . PHE B 194 ? 2.16866 1.83572 0.94881 -0.05659 -0.04346 -0.18693 515 PHE C N   
3136 C CA  . PHE B 194 ? 2.00832 1.66937 0.75315 -0.05853 -0.03441 -0.20045 515 PHE C CA  
3137 C C   . PHE B 194 ? 2.09856 1.77330 0.83185 -0.06592 -0.05909 -0.21799 515 PHE C C   
3138 O O   . PHE B 194 ? 2.18059 1.87600 0.90109 -0.06381 -0.07915 -0.20857 515 PHE C O   
3139 C CB  . PHE B 194 ? 2.03832 1.70377 0.75756 -0.05211 -0.02591 -0.18126 515 PHE C CB  
3140 C CG  . PHE B 194 ? 2.08337 1.74258 0.81787 -0.04605 -0.00299 -0.16309 515 PHE C CG  
3141 C CD1 . PHE B 194 ? 2.04954 1.69778 0.79067 -0.04380 0.02482  -0.17148 515 PHE C CD1 
3142 C CD2 . PHE B 194 ? 2.15047 1.81646 0.89362 -0.04223 -0.00874 -0.13807 515 PHE C CD2 
3143 C CE1 . PHE B 194 ? 2.10532 1.75632 0.86441 -0.03805 0.04609  -0.15531 515 PHE C CE1 
3144 C CE2 . PHE B 194 ? 2.13484 1.79915 0.89408 -0.03841 0.01290  -0.12292 515 PHE C CE2 
3145 C CZ  . PHE B 194 ? 2.09022 1.75054 0.85895 -0.03645 0.04018  -0.13160 515 PHE C CZ  
3146 N N   . GLU B 195 ? 2.17383 1.83795 0.91204 -0.07447 -0.05681 -0.24353 516 GLU C N   
3147 C CA  . GLU B 195 ? 2.07106 1.75107 0.80384 -0.08354 -0.07910 -0.26335 516 GLU C CA  
3148 C C   . GLU B 195 ? 1.99167 1.67863 0.68449 -0.08379 -0.07863 -0.27392 516 GLU C C   
3149 O O   . GLU B 195 ? 1.94844 1.61561 0.62174 -0.08372 -0.05691 -0.28506 516 GLU C O   
3150 C CB  . GLU B 195 ? 2.12813 1.79079 0.87971 -0.09474 -0.07493 -0.28748 516 GLU C CB  
3151 C CG  . GLU B 195 ? 2.19736 1.88226 0.95746 -0.10574 -0.10094 -0.30536 516 GLU C CG  
3152 C CD  . GLU B 195 ? 2.30319 1.96746 1.08312 -0.11903 -0.09537 -0.32750 516 GLU C CD  
3153 O OE1 . GLU B 195 ? 2.23469 1.86307 1.00563 -0.12050 -0.06958 -0.33794 516 GLU C OE1 
3154 O OE2 . GLU B 195 ? 2.22649 1.91089 1.03170 -0.12751 -0.11612 -0.33387 516 GLU C OE2 
3155 N N   . ALA B 201 ? 2.30258 1.89436 0.81071 -0.07565 0.05633  -0.40425 522 ALA C N   
3156 C CA  . ALA B 201 ? 2.40592 2.00373 0.92466 -0.06410 0.07042  -0.37429 522 ALA C CA  
3157 C C   . ALA B 201 ? 2.40630 1.97309 0.94631 -0.05718 0.09750  -0.37654 522 ALA C C   
3158 O O   . ALA B 201 ? 2.53673 2.10319 1.06866 -0.04674 0.11943  -0.37514 522 ALA C O   
3159 C CB  . ALA B 201 ? 2.43700 2.06099 0.92573 -0.05654 0.07589  -0.36559 522 ALA C CB  
3160 N N   . THR B 202 ? 2.39165 1.93544 0.95955 -0.06215 0.09580  -0.37950 523 THR C N   
3161 C CA  . THR B 202 ? 2.44604 1.96008 1.03521 -0.05430 0.12103  -0.38094 523 THR C CA  
3162 C C   . THR B 202 ? 2.42638 1.95339 1.03891 -0.04256 0.13270  -0.35016 523 THR C C   
3163 O O   . THR B 202 ? 2.37916 1.89068 1.00808 -0.03196 0.15650  -0.34841 523 THR C O   
3164 C CB  . THR B 202 ? 2.39052 1.87542 1.00015 -0.06460 0.11548  -0.39536 523 THR C CB  
3165 O OG1 . THR B 202 ? 2.44089 1.89561 1.06920 -0.05483 0.14172  -0.39589 523 THR C OG1 
3166 C CG2 . THR B 202 ? 2.16782 1.67055 0.80001 -0.07170 0.09201  -0.37723 523 THR C CG2 
3167 N N   . VAL B 203 ? 2.30766 1.86329 0.92312 -0.04366 0.11703  -0.32611 524 VAL C N   
3168 C CA  . VAL B 203 ? 2.24354 1.81413 0.88187 -0.03469 0.12669  -0.29718 524 VAL C CA  
3169 C C   . VAL B 203 ? 2.27721 1.87820 0.89695 -0.03395 0.11843  -0.27800 524 VAL C C   
3170 O O   . VAL B 203 ? 2.20510 1.81799 0.81038 -0.04136 0.09463  -0.27517 524 VAL C O   
3171 C CB  . VAL B 203 ? 2.36043 1.92798 1.03173 -0.03815 0.11530  -0.28454 524 VAL C CB  
3172 C CG1 . VAL B 203 ? 2.17254 1.76030 0.86610 -0.03018 0.12337  -0.25511 524 VAL C CG1 
3173 C CG2 . VAL B 203 ? 2.29112 1.82837 0.98165 -0.03824 0.12636  -0.30070 524 VAL C CG2 
3174 N N   . CYS B 204 ? 2.28299 1.89831 0.90397 -0.02482 0.13812  -0.26428 525 CYS C N   
3175 C CA  . CYS B 204 ? 2.17515 1.81751 0.77979 -0.02462 0.13354  -0.24375 525 CYS C CA  
3176 C C   . CYS B 204 ? 2.13171 1.78949 0.76220 -0.01801 0.14997  -0.21907 525 CYS C C   
3177 O O   . CYS B 204 ? 1.98777 1.65050 0.62921 -0.00971 0.17331  -0.22172 525 CYS C O   
3178 C CB  . CYS B 204 ? 2.05254 1.70533 0.62115 -0.02299 0.13974  -0.25693 525 CYS C CB  
3179 S SG  . CYS B 204 ? 2.21920 1.86577 0.75417 -0.03208 0.11769  -0.28414 525 CYS C SG  
# 
