data_9GWA
# 
_entry.id   9GWA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9GWA         pdb_00009gwa 10.2210/pdb9gwa/pdb 
WWPDB D_1292142050 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-14 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.journal_volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GWA 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9GVM 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              patrik.johansson@astrazeneca.com 
_pdbx_contact_author.name_first         Patrik 
_pdbx_contact_author.name_last          Johansson 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7850-1169 
# 
_audit_author.name               'Johansson, P.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-7850-1169 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            301 
_citation.language                  ? 
_citation.page_first                108492 
_citation.page_last                 108492 
_citation.title                     
'Mechanism and kinetics of turnover inhibitors of nicotinamide N-methyl transferase in vitro and in vivo.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2025.108492 
_citation.pdbx_database_id_PubMed   40209950 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Akerud, T.'     1  ? 
primary 'De Fusco, C.'   2  ? 
primary 'Brandt, P.'     3  ? 
primary 'Bergstrom, F.'  4  ? 
primary 'Johansson, P.'  5  ? 
primary 'Ek, M.'         6  ? 
primary 'Borjesson, U.'  7  ? 
primary 'Johansson, A.'  8  ? 
primary 'Danielsson, J.' 9  ? 
primary 'Bauer, M.'      10 ? 
primary 'Arnaud, B.'     11 ? 
primary 'Castaldo, M.'   12 ? 
primary 'Stromstedt, M.' 13 ? 
primary 'Rosengren, B.'  14 ? 
primary 'Jansen, F.'     15 ? 
primary 'Fredlund, L.'   16 ? 
# 
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 'Nicotinamide N-methyltransferase' 31326.623 2  2.1.1.1 K100A,E101A,E103A ? ? 
2 non-polymer syn S-ADENOSYL-L-HOMOCYSTEINE          384.411   2  ?       ?                 ? ? 
3 non-polymer syn 3,4-dihydroisoquinolin-1-amine     146.189   2  ?       ?                 ? ? 
4 water       nat water                              18.015    65 ?       ?                 ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;HNHNHNHNHNHNAAAENLYFQSGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLID
IGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKAAPAAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKC
DVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAV
EAAVKEAGYTIEWFEVISQSYSSTMANNEGLFSLVARKLS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HNHNHNHNHNHNAAAENLYFQSGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLID
IGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKAAPAAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKC
DVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAV
EAAVKEAGYTIEWFEVISQSYSSTMANNEGLFSLVARKLS
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 S-ADENOSYL-L-HOMOCYSTEINE      SAH   
3 3,4-dihydroisoquinolin-1-amine A1IQR 
4 water                          HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   ASN n 
1 3   HIS n 
1 4   ASN n 
1 5   HIS n 
1 6   ASN n 
1 7   HIS n 
1 8   ASN n 
1 9   HIS n 
1 10  ASN n 
1 11  HIS n 
1 12  ASN n 
1 13  ALA n 
1 14  ALA n 
1 15  ALA n 
1 16  GLU n 
1 17  ASN n 
1 18  LEU n 
1 19  TYR n 
1 20  PHE n 
1 21  GLN n 
1 22  SER n 
1 23  GLY n 
1 24  PHE n 
1 25  THR n 
1 26  SER n 
1 27  LYS n 
1 28  ASP n 
1 29  THR n 
1 30  TYR n 
1 31  LEU n 
1 32  SER n 
1 33  HIS n 
1 34  PHE n 
1 35  ASN n 
1 36  PRO n 
1 37  ARG n 
1 38  ASP n 
1 39  TYR n 
1 40  LEU n 
1 41  GLU n 
1 42  LYS n 
1 43  TYR n 
1 44  TYR n 
1 45  LYS n 
1 46  PHE n 
1 47  GLY n 
1 48  SER n 
1 49  ARG n 
1 50  HIS n 
1 51  SER n 
1 52  ALA n 
1 53  GLU n 
1 54  SER n 
1 55  GLN n 
1 56  ILE n 
1 57  LEU n 
1 58  LYS n 
1 59  HIS n 
1 60  LEU n 
1 61  LEU n 
1 62  LYS n 
1 63  ASN n 
1 64  LEU n 
1 65  PHE n 
1 66  LYS n 
1 67  ILE n 
1 68  PHE n 
1 69  CYS n 
1 70  LEU n 
1 71  ASP n 
1 72  GLY n 
1 73  VAL n 
1 74  LYS n 
1 75  GLY n 
1 76  ASP n 
1 77  LEU n 
1 78  LEU n 
1 79  ILE n 
1 80  ASP n 
1 81  ILE n 
1 82  GLY n 
1 83  SER n 
1 84  GLY n 
1 85  PRO n 
1 86  THR n 
1 87  ILE n 
1 88  TYR n 
1 89  GLN n 
1 90  LEU n 
1 91  LEU n 
1 92  SER n 
1 93  ALA n 
1 94  CYS n 
1 95  GLU n 
1 96  SER n 
1 97  PHE n 
1 98  LYS n 
1 99  GLU n 
1 100 ILE n 
1 101 VAL n 
1 102 VAL n 
1 103 THR n 
1 104 ASP n 
1 105 TYR n 
1 106 SER n 
1 107 ASP n 
1 108 GLN n 
1 109 ASN n 
1 110 LEU n 
1 111 GLN n 
1 112 GLU n 
1 113 LEU n 
1 114 GLU n 
1 115 LYS n 
1 116 TRP n 
1 117 LEU n 
1 118 LYS n 
1 119 ALA n 
1 120 ALA n 
1 121 PRO n 
1 122 ALA n 
1 123 ALA n 
1 124 PHE n 
1 125 ASP n 
1 126 TRP n 
1 127 SER n 
1 128 PRO n 
1 129 VAL n 
1 130 VAL n 
1 131 THR n 
1 132 TYR n 
1 133 VAL n 
1 134 CYS n 
1 135 ASP n 
1 136 LEU n 
1 137 GLU n 
1 138 GLY n 
1 139 ASN n 
1 140 ARG n 
1 141 VAL n 
1 142 LYS n 
1 143 GLY n 
1 144 PRO n 
1 145 GLU n 
1 146 LYS n 
1 147 GLU n 
1 148 GLU n 
1 149 LYS n 
1 150 LEU n 
1 151 ARG n 
1 152 GLN n 
1 153 ALA n 
1 154 VAL n 
1 155 LYS n 
1 156 GLN n 
1 157 VAL n 
1 158 LEU n 
1 159 LYS n 
1 160 CYS n 
1 161 ASP n 
1 162 VAL n 
1 163 THR n 
1 164 GLN n 
1 165 SER n 
1 166 GLN n 
1 167 PRO n 
1 168 LEU n 
1 169 GLY n 
1 170 ALA n 
1 171 VAL n 
1 172 PRO n 
1 173 LEU n 
1 174 PRO n 
1 175 PRO n 
1 176 ALA n 
1 177 ASP n 
1 178 CYS n 
1 179 VAL n 
1 180 LEU n 
1 181 SER n 
1 182 THR n 
1 183 LEU n 
1 184 CYS n 
1 185 LEU n 
1 186 ASP n 
1 187 ALA n 
1 188 ALA n 
1 189 CYS n 
1 190 PRO n 
1 191 ASP n 
1 192 LEU n 
1 193 PRO n 
1 194 THR n 
1 195 TYR n 
1 196 CYS n 
1 197 ARG n 
1 198 ALA n 
1 199 LEU n 
1 200 ARG n 
1 201 ASN n 
1 202 LEU n 
1 203 GLY n 
1 204 SER n 
1 205 LEU n 
1 206 LEU n 
1 207 LYS n 
1 208 PRO n 
1 209 GLY n 
1 210 GLY n 
1 211 PHE n 
1 212 LEU n 
1 213 VAL n 
1 214 ILE n 
1 215 MET n 
1 216 ASP n 
1 217 ALA n 
1 218 LEU n 
1 219 LYS n 
1 220 SER n 
1 221 SER n 
1 222 TYR n 
1 223 TYR n 
1 224 MET n 
1 225 ILE n 
1 226 GLY n 
1 227 GLU n 
1 228 GLN n 
1 229 LYS n 
1 230 PHE n 
1 231 SER n 
1 232 SER n 
1 233 LEU n 
1 234 PRO n 
1 235 LEU n 
1 236 GLY n 
1 237 ARG n 
1 238 GLU n 
1 239 ALA n 
1 240 VAL n 
1 241 GLU n 
1 242 ALA n 
1 243 ALA n 
1 244 VAL n 
1 245 LYS n 
1 246 GLU n 
1 247 ALA n 
1 248 GLY n 
1 249 TYR n 
1 250 THR n 
1 251 ILE n 
1 252 GLU n 
1 253 TRP n 
1 254 PHE n 
1 255 GLU n 
1 256 VAL n 
1 257 ILE n 
1 258 SER n 
1 259 GLN n 
1 260 SER n 
1 261 TYR n 
1 262 SER n 
1 263 SER n 
1 264 THR n 
1 265 MET n 
1 266 ALA n 
1 267 ASN n 
1 268 ASN n 
1 269 GLU n 
1 270 GLY n 
1 271 LEU n 
1 272 PHE n 
1 273 SER n 
1 274 LEU n 
1 275 VAL n 
1 276 ALA n 
1 277 ARG n 
1 278 LYS n 
1 279 LEU n 
1 280 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   280 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 NNMT 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli-Pichia pastoris shuttle vector pPpARG4' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     1182032 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1IQR non-polymer         . 3,4-dihydroisoquinolin-1-amine ? 'C9 H10 N2'       146.189 
ALA   'L-peptide linking' y ALANINE                        ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                       ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                     ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                       ? 'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE                      ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                        ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                      ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                          ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                     ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                        ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                         ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                     ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                  ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                        ? 'C5 H9 N O2'      115.130 
SAH   non-polymer         . S-ADENOSYL-L-HOMOCYSTEINE      ? 'C14 H20 N6 O5 S' 384.411 
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   HIS 1   -18 ?   ?   ?   A . n 
A 1 2   ASN 2   -17 ?   ?   ?   A . n 
A 1 3   HIS 3   -16 ?   ?   ?   A . n 
A 1 4   ASN 4   -15 ?   ?   ?   A . n 
A 1 5   HIS 5   -14 ?   ?   ?   A . n 
A 1 6   ASN 6   -13 ?   ?   ?   A . n 
A 1 7   HIS 7   -12 ?   ?   ?   A . n 
A 1 8   ASN 8   -11 ?   ?   ?   A . n 
A 1 9   HIS 9   -10 ?   ?   ?   A . n 
A 1 10  ASN 10  -9  ?   ?   ?   A . n 
A 1 11  HIS 11  -8  ?   ?   ?   A . n 
A 1 12  ASN 12  -7  ?   ?   ?   A . n 
A 1 13  ALA 13  -6  ?   ?   ?   A . n 
A 1 14  ALA 14  -5  ?   ?   ?   A . n 
A 1 15  ALA 15  -4  ?   ?   ?   A . n 
A 1 16  GLU 16  -3  ?   ?   ?   A . n 
A 1 17  ASN 17  -2  ?   ?   ?   A . n 
A 1 18  LEU 18  -1  ?   ?   ?   A . n 
A 1 19  TYR 19  0   ?   ?   ?   A . n 
A 1 20  PHE 20  1   ?   ?   ?   A . n 
A 1 21  GLN 21  2   ?   ?   ?   A . n 
A 1 22  SER 22  3   ?   ?   ?   A . n 
A 1 23  GLY 23  4   4   GLY GLY A . n 
A 1 24  PHE 24  5   5   PHE PHE A . n 
A 1 25  THR 25  6   6   THR THR A . n 
A 1 26  SER 26  7   7   SER SER A . n 
A 1 27  LYS 27  8   8   LYS LYS A . n 
A 1 28  ASP 28  9   9   ASP ASP A . n 
A 1 29  THR 29  10  10  THR THR A . n 
A 1 30  TYR 30  11  11  TYR TYR A . n 
A 1 31  LEU 31  12  12  LEU LEU A . n 
A 1 32  SER 32  13  13  SER SER A . n 
A 1 33  HIS 33  14  14  HIS HIS A . n 
A 1 34  PHE 34  15  15  PHE PHE A . n 
A 1 35  ASN 35  16  16  ASN ASN A . n 
A 1 36  PRO 36  17  17  PRO PRO A . n 
A 1 37  ARG 37  18  18  ARG ARG A . n 
A 1 38  ASP 38  19  19  ASP ASP A . n 
A 1 39  TYR 39  20  20  TYR TYR A . n 
A 1 40  LEU 40  21  21  LEU LEU A . n 
A 1 41  GLU 41  22  22  GLU GLU A . n 
A 1 42  LYS 42  23  23  LYS LYS A . n 
A 1 43  TYR 43  24  24  TYR TYR A . n 
A 1 44  TYR 44  25  25  TYR TYR A . n 
A 1 45  LYS 45  26  26  LYS LYS A . n 
A 1 46  PHE 46  27  27  PHE PHE A . n 
A 1 47  GLY 47  28  28  GLY GLY A . n 
A 1 48  SER 48  29  29  SER SER A . n 
A 1 49  ARG 49  30  30  ARG ARG A . n 
A 1 50  HIS 50  31  31  HIS HIS A . n 
A 1 51  SER 51  32  32  SER SER A . n 
A 1 52  ALA 52  33  33  ALA ALA A . n 
A 1 53  GLU 53  34  34  GLU GLU A . n 
A 1 54  SER 54  35  35  SER SER A . n 
A 1 55  GLN 55  36  36  GLN GLN A . n 
A 1 56  ILE 56  37  37  ILE ILE A . n 
A 1 57  LEU 57  38  38  LEU LEU A . n 
A 1 58  LYS 58  39  39  LYS LYS A . n 
A 1 59  HIS 59  40  40  HIS HIS A . n 
A 1 60  LEU 60  41  41  LEU LEU A . n 
A 1 61  LEU 61  42  42  LEU LEU A . n 
A 1 62  LYS 62  43  43  LYS LYS A . n 
A 1 63  ASN 63  44  44  ASN ASN A . n 
A 1 64  LEU 64  45  45  LEU LEU A . n 
A 1 65  PHE 65  46  46  PHE PHE A . n 
A 1 66  LYS 66  47  47  LYS LYS A . n 
A 1 67  ILE 67  48  48  ILE ILE A . n 
A 1 68  PHE 68  49  49  PHE PHE A . n 
A 1 69  CYS 69  50  50  CYS CYS A . n 
A 1 70  LEU 70  51  51  LEU LEU A . n 
A 1 71  ASP 71  52  52  ASP ASP A . n 
A 1 72  GLY 72  53  53  GLY GLY A . n 
A 1 73  VAL 73  54  54  VAL VAL A . n 
A 1 74  LYS 74  55  55  LYS LYS A . n 
A 1 75  GLY 75  56  56  GLY GLY A . n 
A 1 76  ASP 76  57  57  ASP ASP A . n 
A 1 77  LEU 77  58  58  LEU LEU A . n 
A 1 78  LEU 78  59  59  LEU LEU A . n 
A 1 79  ILE 79  60  60  ILE ILE A . n 
A 1 80  ASP 80  61  61  ASP ASP A . n 
A 1 81  ILE 81  62  62  ILE ILE A . n 
A 1 82  GLY 82  63  63  GLY GLY A . n 
A 1 83  SER 83  64  64  SER SER A . n 
A 1 84  GLY 84  65  65  GLY GLY A . n 
A 1 85  PRO 85  66  66  PRO PRO A . n 
A 1 86  THR 86  67  67  THR THR A . n 
A 1 87  ILE 87  68  68  ILE ILE A . n 
A 1 88  TYR 88  69  69  TYR TYR A . n 
A 1 89  GLN 89  70  70  GLN GLN A . n 
A 1 90  LEU 90  71  71  LEU LEU A . n 
A 1 91  LEU 91  72  72  LEU LEU A . n 
A 1 92  SER 92  73  73  SER SER A . n 
A 1 93  ALA 93  74  74  ALA ALA A . n 
A 1 94  CYS 94  75  75  CYS CYS A . n 
A 1 95  GLU 95  76  76  GLU GLU A . n 
A 1 96  SER 96  77  77  SER SER A . n 
A 1 97  PHE 97  78  78  PHE PHE A . n 
A 1 98  LYS 98  79  79  LYS LYS A . n 
A 1 99  GLU 99  80  80  GLU GLU A . n 
A 1 100 ILE 100 81  81  ILE ILE A . n 
A 1 101 VAL 101 82  82  VAL VAL A . n 
A 1 102 VAL 102 83  83  VAL VAL A . n 
A 1 103 THR 103 84  84  THR THR A . n 
A 1 104 ASP 104 85  85  ASP ASP A . n 
A 1 105 TYR 105 86  86  TYR TYR A . n 
A 1 106 SER 106 87  87  SER SER A . n 
A 1 107 ASP 107 88  88  ASP ASP A . n 
A 1 108 GLN 108 89  89  GLN GLN A . n 
A 1 109 ASN 109 90  90  ASN ASN A . n 
A 1 110 LEU 110 91  91  LEU LEU A . n 
A 1 111 GLN 111 92  92  GLN GLN A . n 
A 1 112 GLU 112 93  93  GLU GLU A . n 
A 1 113 LEU 113 94  94  LEU LEU A . n 
A 1 114 GLU 114 95  95  GLU GLU A . n 
A 1 115 LYS 115 96  96  LYS LYS A . n 
A 1 116 TRP 116 97  97  TRP TRP A . n 
A 1 117 LEU 117 98  98  LEU LEU A . n 
A 1 118 LYS 118 99  99  LYS LYS A . n 
A 1 119 ALA 119 100 100 ALA ALA A . n 
A 1 120 ALA 120 101 101 ALA ALA A . n 
A 1 121 PRO 121 102 102 PRO PRO A . n 
A 1 122 ALA 122 103 103 ALA ALA A . n 
A 1 123 ALA 123 104 104 ALA ALA A . n 
A 1 124 PHE 124 105 105 PHE PHE A . n 
A 1 125 ASP 125 106 106 ASP ASP A . n 
A 1 126 TRP 126 107 107 TRP TRP A . n 
A 1 127 SER 127 108 108 SER SER A . n 
A 1 128 PRO 128 109 109 PRO PRO A . n 
A 1 129 VAL 129 110 110 VAL VAL A . n 
A 1 130 VAL 130 111 111 VAL VAL A . n 
A 1 131 THR 131 112 112 THR THR A . n 
A 1 132 TYR 132 113 113 TYR TYR A . n 
A 1 133 VAL 133 114 114 VAL VAL A . n 
A 1 134 CYS 134 115 115 CYS CYS A . n 
A 1 135 ASP 135 116 116 ASP ASP A . n 
A 1 136 LEU 136 117 117 LEU LEU A . n 
A 1 137 GLU 137 118 118 GLU GLU A . n 
A 1 138 GLY 138 119 119 GLY GLY A . n 
A 1 139 ASN 139 120 120 ASN ASN A . n 
A 1 140 ARG 140 121 121 ARG ARG A . n 
A 1 141 VAL 141 122 122 VAL VAL A . n 
A 1 142 LYS 142 123 123 LYS LYS A . n 
A 1 143 GLY 143 124 124 GLY GLY A . n 
A 1 144 PRO 144 125 125 PRO PRO A . n 
A 1 145 GLU 145 126 126 GLU GLU A . n 
A 1 146 LYS 146 127 127 LYS LYS A . n 
A 1 147 GLU 147 128 128 GLU GLU A . n 
A 1 148 GLU 148 129 129 GLU GLU A . n 
A 1 149 LYS 149 130 130 LYS LYS A . n 
A 1 150 LEU 150 131 131 LEU LEU A . n 
A 1 151 ARG 151 132 132 ARG ARG A . n 
A 1 152 GLN 152 133 133 GLN GLN A . n 
A 1 153 ALA 153 134 134 ALA ALA A . n 
A 1 154 VAL 154 135 135 VAL VAL A . n 
A 1 155 LYS 155 136 136 LYS LYS A . n 
A 1 156 GLN 156 137 137 GLN GLN A . n 
A 1 157 VAL 157 138 138 VAL VAL A . n 
A 1 158 LEU 158 139 139 LEU LEU A . n 
A 1 159 LYS 159 140 140 LYS LYS A . n 
A 1 160 CYS 160 141 141 CYS CYS A . n 
A 1 161 ASP 161 142 142 ASP ASP A . n 
A 1 162 VAL 162 143 143 VAL VAL A . n 
A 1 163 THR 163 144 144 THR THR A . n 
A 1 164 GLN 164 145 145 GLN GLN A . n 
A 1 165 SER 165 146 146 SER SER A . n 
A 1 166 GLN 166 147 147 GLN GLN A . n 
A 1 167 PRO 167 148 148 PRO PRO A . n 
A 1 168 LEU 168 149 149 LEU LEU A . n 
A 1 169 GLY 169 150 150 GLY GLY A . n 
A 1 170 ALA 170 151 151 ALA ALA A . n 
A 1 171 VAL 171 152 152 VAL VAL A . n 
A 1 172 PRO 172 153 153 PRO PRO A . n 
A 1 173 LEU 173 154 154 LEU LEU A . n 
A 1 174 PRO 174 155 155 PRO PRO A . n 
A 1 175 PRO 175 156 156 PRO PRO A . n 
A 1 176 ALA 176 157 157 ALA ALA A . n 
A 1 177 ASP 177 158 158 ASP ASP A . n 
A 1 178 CYS 178 159 159 CYS CYS A . n 
A 1 179 VAL 179 160 160 VAL VAL A . n 
A 1 180 LEU 180 161 161 LEU LEU A . n 
A 1 181 SER 181 162 162 SER SER A . n 
A 1 182 THR 182 163 163 THR THR A . n 
A 1 183 LEU 183 164 164 LEU LEU A . n 
A 1 184 CYS 184 165 165 CYS CYS A . n 
A 1 185 LEU 185 166 166 LEU LEU A . n 
A 1 186 ASP 186 167 167 ASP ASP A . n 
A 1 187 ALA 187 168 168 ALA ALA A . n 
A 1 188 ALA 188 169 169 ALA ALA A . n 
A 1 189 CYS 189 170 170 CYS CYS A . n 
A 1 190 PRO 190 171 171 PRO PRO A . n 
A 1 191 ASP 191 172 172 ASP ASP A . n 
A 1 192 LEU 192 173 173 LEU LEU A . n 
A 1 193 PRO 193 174 174 PRO PRO A . n 
A 1 194 THR 194 175 175 THR THR A . n 
A 1 195 TYR 195 176 176 TYR TYR A . n 
A 1 196 CYS 196 177 177 CYS CYS A . n 
A 1 197 ARG 197 178 178 ARG ARG A . n 
A 1 198 ALA 198 179 179 ALA ALA A . n 
A 1 199 LEU 199 180 180 LEU LEU A . n 
A 1 200 ARG 200 181 181 ARG ARG A . n 
A 1 201 ASN 201 182 182 ASN ASN A . n 
A 1 202 LEU 202 183 183 LEU LEU A . n 
A 1 203 GLY 203 184 184 GLY GLY A . n 
A 1 204 SER 204 185 185 SER SER A . n 
A 1 205 LEU 205 186 186 LEU LEU A . n 
A 1 206 LEU 206 187 187 LEU LEU A . n 
A 1 207 LYS 207 188 188 LYS LYS A . n 
A 1 208 PRO 208 189 189 PRO PRO A . n 
A 1 209 GLY 209 190 190 GLY GLY A . n 
A 1 210 GLY 210 191 191 GLY GLY A . n 
A 1 211 PHE 211 192 192 PHE PHE A . n 
A 1 212 LEU 212 193 193 LEU LEU A . n 
A 1 213 VAL 213 194 194 VAL VAL A . n 
A 1 214 ILE 214 195 195 ILE ILE A . n 
A 1 215 MET 215 196 196 MET MET A . n 
A 1 216 ASP 216 197 197 ASP ASP A . n 
A 1 217 ALA 217 198 198 ALA ALA A . n 
A 1 218 LEU 218 199 199 LEU LEU A . n 
A 1 219 LYS 219 200 200 LYS LYS A . n 
A 1 220 SER 220 201 201 SER SER A . n 
A 1 221 SER 221 202 202 SER SER A . n 
A 1 222 TYR 222 203 203 TYR TYR A . n 
A 1 223 TYR 223 204 204 TYR TYR A . n 
A 1 224 MET 224 205 205 MET MET A . n 
A 1 225 ILE 225 206 206 ILE ILE A . n 
A 1 226 GLY 226 207 207 GLY GLY A . n 
A 1 227 GLU 227 208 208 GLU GLU A . n 
A 1 228 GLN 228 209 209 GLN GLN A . n 
A 1 229 LYS 229 210 210 LYS LYS A . n 
A 1 230 PHE 230 211 211 PHE PHE A . n 
A 1 231 SER 231 212 212 SER SER A . n 
A 1 232 SER 232 213 213 SER SER A . n 
A 1 233 LEU 233 214 214 LEU LEU A . n 
A 1 234 PRO 234 215 215 PRO PRO A . n 
A 1 235 LEU 235 216 216 LEU LEU A . n 
A 1 236 GLY 236 217 217 GLY GLY A . n 
A 1 237 ARG 237 218 218 ARG ARG A . n 
A 1 238 GLU 238 219 219 GLU GLU A . n 
A 1 239 ALA 239 220 220 ALA ALA A . n 
A 1 240 VAL 240 221 221 VAL VAL A . n 
A 1 241 GLU 241 222 222 GLU GLU A . n 
A 1 242 ALA 242 223 223 ALA ALA A . n 
A 1 243 ALA 243 224 224 ALA ALA A . n 
A 1 244 VAL 244 225 225 VAL VAL A . n 
A 1 245 LYS 245 226 226 LYS LYS A . n 
A 1 246 GLU 246 227 227 GLU GLU A . n 
A 1 247 ALA 247 228 228 ALA ALA A . n 
A 1 248 GLY 248 229 229 GLY GLY A . n 
A 1 249 TYR 249 230 230 TYR TYR A . n 
A 1 250 THR 250 231 231 THR THR A . n 
A 1 251 ILE 251 232 232 ILE ILE A . n 
A 1 252 GLU 252 233 233 GLU GLU A . n 
A 1 253 TRP 253 234 234 TRP TRP A . n 
A 1 254 PHE 254 235 235 PHE PHE A . n 
A 1 255 GLU 255 236 236 GLU GLU A . n 
A 1 256 VAL 256 237 237 VAL VAL A . n 
A 1 257 ILE 257 238 238 ILE ILE A . n 
A 1 258 SER 258 239 239 SER SER A . n 
A 1 259 GLN 259 240 240 GLN GLN A . n 
A 1 260 SER 260 241 241 SER SER A . n 
A 1 261 TYR 261 242 242 TYR TYR A . n 
A 1 262 SER 262 243 243 SER SER A . n 
A 1 263 SER 263 244 244 SER SER A . n 
A 1 264 THR 264 245 245 THR THR A . n 
A 1 265 MET 265 246 246 MET MET A . n 
A 1 266 ALA 266 247 247 ALA ALA A . n 
A 1 267 ASN 267 248 248 ASN ASN A . n 
A 1 268 ASN 268 249 249 ASN ASN A . n 
A 1 269 GLU 269 250 250 GLU GLU A . n 
A 1 270 GLY 270 251 251 GLY GLY A . n 
A 1 271 LEU 271 252 252 LEU LEU A . n 
A 1 272 PHE 272 253 253 PHE PHE A . n 
A 1 273 SER 273 254 254 SER SER A . n 
A 1 274 LEU 274 255 255 LEU LEU A . n 
A 1 275 VAL 275 256 256 VAL VAL A . n 
A 1 276 ALA 276 257 257 ALA ALA A . n 
A 1 277 ARG 277 258 258 ARG ARG A . n 
A 1 278 LYS 278 259 259 LYS LYS A . n 
A 1 279 LEU 279 260 260 LEU LEU A . n 
A 1 280 SER 280 261 261 SER SER A . n 
B 1 1   HIS 1   -18 ?   ?   ?   B . n 
B 1 2   ASN 2   -17 ?   ?   ?   B . n 
B 1 3   HIS 3   -16 ?   ?   ?   B . n 
B 1 4   ASN 4   -15 ?   ?   ?   B . n 
B 1 5   HIS 5   -14 ?   ?   ?   B . n 
B 1 6   ASN 6   -13 ?   ?   ?   B . n 
B 1 7   HIS 7   -12 ?   ?   ?   B . n 
B 1 8   ASN 8   -11 ?   ?   ?   B . n 
B 1 9   HIS 9   -10 ?   ?   ?   B . n 
B 1 10  ASN 10  -9  ?   ?   ?   B . n 
B 1 11  HIS 11  -8  ?   ?   ?   B . n 
B 1 12  ASN 12  -7  ?   ?   ?   B . n 
B 1 13  ALA 13  -6  ?   ?   ?   B . n 
B 1 14  ALA 14  -5  ?   ?   ?   B . n 
B 1 15  ALA 15  -4  ?   ?   ?   B . n 
B 1 16  GLU 16  -3  ?   ?   ?   B . n 
B 1 17  ASN 17  -2  ?   ?   ?   B . n 
B 1 18  LEU 18  -1  ?   ?   ?   B . n 
B 1 19  TYR 19  0   ?   ?   ?   B . n 
B 1 20  PHE 20  1   ?   ?   ?   B . n 
B 1 21  GLN 21  2   ?   ?   ?   B . n 
B 1 22  SER 22  3   ?   ?   ?   B . n 
B 1 23  GLY 23  4   ?   ?   ?   B . n 
B 1 24  PHE 24  5   5   PHE PHE B . n 
B 1 25  THR 25  6   6   THR THR B . n 
B 1 26  SER 26  7   7   SER SER B . n 
B 1 27  LYS 27  8   8   LYS LYS B . n 
B 1 28  ASP 28  9   9   ASP ASP B . n 
B 1 29  THR 29  10  10  THR THR B . n 
B 1 30  TYR 30  11  11  TYR TYR B . n 
B 1 31  LEU 31  12  12  LEU LEU B . n 
B 1 32  SER 32  13  13  SER SER B . n 
B 1 33  HIS 33  14  14  HIS HIS B . n 
B 1 34  PHE 34  15  15  PHE PHE B . n 
B 1 35  ASN 35  16  16  ASN ASN B . n 
B 1 36  PRO 36  17  17  PRO PRO B . n 
B 1 37  ARG 37  18  18  ARG ARG B . n 
B 1 38  ASP 38  19  19  ASP ASP B . n 
B 1 39  TYR 39  20  20  TYR TYR B . n 
B 1 40  LEU 40  21  21  LEU LEU B . n 
B 1 41  GLU 41  22  22  GLU GLU B . n 
B 1 42  LYS 42  23  23  LYS LYS B . n 
B 1 43  TYR 43  24  24  TYR TYR B . n 
B 1 44  TYR 44  25  25  TYR TYR B . n 
B 1 45  LYS 45  26  26  LYS LYS B . n 
B 1 46  PHE 46  27  27  PHE PHE B . n 
B 1 47  GLY 47  28  28  GLY GLY B . n 
B 1 48  SER 48  29  29  SER SER B . n 
B 1 49  ARG 49  30  30  ARG ARG B . n 
B 1 50  HIS 50  31  31  HIS HIS B . n 
B 1 51  SER 51  32  32  SER SER B . n 
B 1 52  ALA 52  33  33  ALA ALA B . n 
B 1 53  GLU 53  34  34  GLU GLU B . n 
B 1 54  SER 54  35  35  SER SER B . n 
B 1 55  GLN 55  36  36  GLN GLN B . n 
B 1 56  ILE 56  37  37  ILE ILE B . n 
B 1 57  LEU 57  38  38  LEU LEU B . n 
B 1 58  LYS 58  39  39  LYS LYS B . n 
B 1 59  HIS 59  40  40  HIS HIS B . n 
B 1 60  LEU 60  41  41  LEU LEU B . n 
B 1 61  LEU 61  42  42  LEU LEU B . n 
B 1 62  LYS 62  43  43  LYS LYS B . n 
B 1 63  ASN 63  44  44  ASN ASN B . n 
B 1 64  LEU 64  45  45  LEU LEU B . n 
B 1 65  PHE 65  46  46  PHE PHE B . n 
B 1 66  LYS 66  47  47  LYS LYS B . n 
B 1 67  ILE 67  48  48  ILE ILE B . n 
B 1 68  PHE 68  49  49  PHE PHE B . n 
B 1 69  CYS 69  50  50  CYS CYS B . n 
B 1 70  LEU 70  51  51  LEU LEU B . n 
B 1 71  ASP 71  52  52  ASP ASP B . n 
B 1 72  GLY 72  53  53  GLY GLY B . n 
B 1 73  VAL 73  54  54  VAL VAL B . n 
B 1 74  LYS 74  55  55  LYS LYS B . n 
B 1 75  GLY 75  56  56  GLY GLY B . n 
B 1 76  ASP 76  57  57  ASP ASP B . n 
B 1 77  LEU 77  58  58  LEU LEU B . n 
B 1 78  LEU 78  59  59  LEU LEU B . n 
B 1 79  ILE 79  60  60  ILE ILE B . n 
B 1 80  ASP 80  61  61  ASP ASP B . n 
B 1 81  ILE 81  62  62  ILE ILE B . n 
B 1 82  GLY 82  63  63  GLY GLY B . n 
B 1 83  SER 83  64  64  SER SER B . n 
B 1 84  GLY 84  65  65  GLY GLY B . n 
B 1 85  PRO 85  66  66  PRO PRO B . n 
B 1 86  THR 86  67  67  THR THR B . n 
B 1 87  ILE 87  68  68  ILE ILE B . n 
B 1 88  TYR 88  69  69  TYR TYR B . n 
B 1 89  GLN 89  70  70  GLN GLN B . n 
B 1 90  LEU 90  71  71  LEU LEU B . n 
B 1 91  LEU 91  72  72  LEU LEU B . n 
B 1 92  SER 92  73  73  SER SER B . n 
B 1 93  ALA 93  74  74  ALA ALA B . n 
B 1 94  CYS 94  75  75  CYS CYS B . n 
B 1 95  GLU 95  76  76  GLU GLU B . n 
B 1 96  SER 96  77  77  SER SER B . n 
B 1 97  PHE 97  78  78  PHE PHE B . n 
B 1 98  LYS 98  79  79  LYS LYS B . n 
B 1 99  GLU 99  80  80  GLU GLU B . n 
B 1 100 ILE 100 81  81  ILE ILE B . n 
B 1 101 VAL 101 82  82  VAL VAL B . n 
B 1 102 VAL 102 83  83  VAL VAL B . n 
B 1 103 THR 103 84  84  THR THR B . n 
B 1 104 ASP 104 85  85  ASP ASP B . n 
B 1 105 TYR 105 86  86  TYR TYR B . n 
B 1 106 SER 106 87  87  SER SER B . n 
B 1 107 ASP 107 88  88  ASP ASP B . n 
B 1 108 GLN 108 89  89  GLN GLN B . n 
B 1 109 ASN 109 90  90  ASN ASN B . n 
B 1 110 LEU 110 91  91  LEU LEU B . n 
B 1 111 GLN 111 92  92  GLN GLN B . n 
B 1 112 GLU 112 93  93  GLU GLU B . n 
B 1 113 LEU 113 94  94  LEU LEU B . n 
B 1 114 GLU 114 95  95  GLU GLU B . n 
B 1 115 LYS 115 96  96  LYS LYS B . n 
B 1 116 TRP 116 97  97  TRP TRP B . n 
B 1 117 LEU 117 98  98  LEU LEU B . n 
B 1 118 LYS 118 99  99  LYS LYS B . n 
B 1 119 ALA 119 100 100 ALA ALA B . n 
B 1 120 ALA 120 101 101 ALA ALA B . n 
B 1 121 PRO 121 102 102 PRO PRO B . n 
B 1 122 ALA 122 103 103 ALA ALA B . n 
B 1 123 ALA 123 104 104 ALA ALA B . n 
B 1 124 PHE 124 105 105 PHE PHE B . n 
B 1 125 ASP 125 106 106 ASP ASP B . n 
B 1 126 TRP 126 107 107 TRP TRP B . n 
B 1 127 SER 127 108 108 SER SER B . n 
B 1 128 PRO 128 109 109 PRO PRO B . n 
B 1 129 VAL 129 110 110 VAL VAL B . n 
B 1 130 VAL 130 111 111 VAL VAL B . n 
B 1 131 THR 131 112 112 THR THR B . n 
B 1 132 TYR 132 113 113 TYR TYR B . n 
B 1 133 VAL 133 114 114 VAL VAL B . n 
B 1 134 CYS 134 115 115 CYS CYS B . n 
B 1 135 ASP 135 116 116 ASP ASP B . n 
B 1 136 LEU 136 117 117 LEU LEU B . n 
B 1 137 GLU 137 118 118 GLU GLU B . n 
B 1 138 GLY 138 119 119 GLY GLY B . n 
B 1 139 ASN 139 120 120 ASN ASN B . n 
B 1 140 ARG 140 121 121 ARG ARG B . n 
B 1 141 VAL 141 122 122 VAL VAL B . n 
B 1 142 LYS 142 123 123 LYS LYS B . n 
B 1 143 GLY 143 124 124 GLY GLY B . n 
B 1 144 PRO 144 125 125 PRO PRO B . n 
B 1 145 GLU 145 126 126 GLU GLU B . n 
B 1 146 LYS 146 127 127 LYS LYS B . n 
B 1 147 GLU 147 128 128 GLU GLU B . n 
B 1 148 GLU 148 129 129 GLU GLU B . n 
B 1 149 LYS 149 130 130 LYS LYS B . n 
B 1 150 LEU 150 131 131 LEU LEU B . n 
B 1 151 ARG 151 132 132 ARG ARG B . n 
B 1 152 GLN 152 133 133 GLN GLN B . n 
B 1 153 ALA 153 134 134 ALA ALA B . n 
B 1 154 VAL 154 135 135 VAL VAL B . n 
B 1 155 LYS 155 136 136 LYS LYS B . n 
B 1 156 GLN 156 137 137 GLN GLN B . n 
B 1 157 VAL 157 138 138 VAL VAL B . n 
B 1 158 LEU 158 139 139 LEU LEU B . n 
B 1 159 LYS 159 140 140 LYS LYS B . n 
B 1 160 CYS 160 141 141 CYS CYS B . n 
B 1 161 ASP 161 142 142 ASP ASP B . n 
B 1 162 VAL 162 143 143 VAL VAL B . n 
B 1 163 THR 163 144 144 THR THR B . n 
B 1 164 GLN 164 145 145 GLN GLN B . n 
B 1 165 SER 165 146 146 SER SER B . n 
B 1 166 GLN 166 147 147 GLN GLN B . n 
B 1 167 PRO 167 148 148 PRO PRO B . n 
B 1 168 LEU 168 149 149 LEU LEU B . n 
B 1 169 GLY 169 150 150 GLY GLY B . n 
B 1 170 ALA 170 151 151 ALA ALA B . n 
B 1 171 VAL 171 152 152 VAL VAL B . n 
B 1 172 PRO 172 153 153 PRO PRO B . n 
B 1 173 LEU 173 154 154 LEU LEU B . n 
B 1 174 PRO 174 155 155 PRO PRO B . n 
B 1 175 PRO 175 156 156 PRO PRO B . n 
B 1 176 ALA 176 157 157 ALA ALA B . n 
B 1 177 ASP 177 158 158 ASP ASP B . n 
B 1 178 CYS 178 159 159 CYS CYS B . n 
B 1 179 VAL 179 160 160 VAL VAL B . n 
B 1 180 LEU 180 161 161 LEU LEU B . n 
B 1 181 SER 181 162 162 SER SER B . n 
B 1 182 THR 182 163 163 THR THR B . n 
B 1 183 LEU 183 164 164 LEU LEU B . n 
B 1 184 CYS 184 165 165 CYS CYS B . n 
B 1 185 LEU 185 166 166 LEU LEU B . n 
B 1 186 ASP 186 167 167 ASP ASP B . n 
B 1 187 ALA 187 168 168 ALA ALA B . n 
B 1 188 ALA 188 169 169 ALA ALA B . n 
B 1 189 CYS 189 170 170 CYS CYS B . n 
B 1 190 PRO 190 171 171 PRO PRO B . n 
B 1 191 ASP 191 172 172 ASP ASP B . n 
B 1 192 LEU 192 173 173 LEU LEU B . n 
B 1 193 PRO 193 174 174 PRO PRO B . n 
B 1 194 THR 194 175 175 THR THR B . n 
B 1 195 TYR 195 176 176 TYR TYR B . n 
B 1 196 CYS 196 177 177 CYS CYS B . n 
B 1 197 ARG 197 178 178 ARG ARG B . n 
B 1 198 ALA 198 179 179 ALA ALA B . n 
B 1 199 LEU 199 180 180 LEU LEU B . n 
B 1 200 ARG 200 181 181 ARG ARG B . n 
B 1 201 ASN 201 182 182 ASN ASN B . n 
B 1 202 LEU 202 183 183 LEU LEU B . n 
B 1 203 GLY 203 184 184 GLY GLY B . n 
B 1 204 SER 204 185 185 SER SER B . n 
B 1 205 LEU 205 186 186 LEU LEU B . n 
B 1 206 LEU 206 187 187 LEU LEU B . n 
B 1 207 LYS 207 188 188 LYS LYS B . n 
B 1 208 PRO 208 189 189 PRO PRO B . n 
B 1 209 GLY 209 190 190 GLY GLY B . n 
B 1 210 GLY 210 191 191 GLY GLY B . n 
B 1 211 PHE 211 192 192 PHE PHE B . n 
B 1 212 LEU 212 193 193 LEU LEU B . n 
B 1 213 VAL 213 194 194 VAL VAL B . n 
B 1 214 ILE 214 195 195 ILE ILE B . n 
B 1 215 MET 215 196 196 MET MET B . n 
B 1 216 ASP 216 197 197 ASP ASP B . n 
B 1 217 ALA 217 198 198 ALA ALA B . n 
B 1 218 LEU 218 199 199 LEU LEU B . n 
B 1 219 LYS 219 200 200 LYS LYS B . n 
B 1 220 SER 220 201 201 SER SER B . n 
B 1 221 SER 221 202 202 SER SER B . n 
B 1 222 TYR 222 203 203 TYR TYR B . n 
B 1 223 TYR 223 204 204 TYR TYR B . n 
B 1 224 MET 224 205 205 MET MET B . n 
B 1 225 ILE 225 206 206 ILE ILE B . n 
B 1 226 GLY 226 207 207 GLY GLY B . n 
B 1 227 GLU 227 208 208 GLU GLU B . n 
B 1 228 GLN 228 209 209 GLN GLN B . n 
B 1 229 LYS 229 210 210 LYS LYS B . n 
B 1 230 PHE 230 211 211 PHE PHE B . n 
B 1 231 SER 231 212 212 SER SER B . n 
B 1 232 SER 232 213 213 SER SER B . n 
B 1 233 LEU 233 214 214 LEU LEU B . n 
B 1 234 PRO 234 215 215 PRO PRO B . n 
B 1 235 LEU 235 216 216 LEU LEU B . n 
B 1 236 GLY 236 217 217 GLY GLY B . n 
B 1 237 ARG 237 218 218 ARG ARG B . n 
B 1 238 GLU 238 219 219 GLU GLU B . n 
B 1 239 ALA 239 220 220 ALA ALA B . n 
B 1 240 VAL 240 221 221 VAL VAL B . n 
B 1 241 GLU 241 222 222 GLU GLU B . n 
B 1 242 ALA 242 223 223 ALA ALA B . n 
B 1 243 ALA 243 224 224 ALA ALA B . n 
B 1 244 VAL 244 225 225 VAL VAL B . n 
B 1 245 LYS 245 226 226 LYS LYS B . n 
B 1 246 GLU 246 227 227 GLU GLU B . n 
B 1 247 ALA 247 228 228 ALA ALA B . n 
B 1 248 GLY 248 229 229 GLY GLY B . n 
B 1 249 TYR 249 230 230 TYR TYR B . n 
B 1 250 THR 250 231 231 THR THR B . n 
B 1 251 ILE 251 232 232 ILE ILE B . n 
B 1 252 GLU 252 233 233 GLU GLU B . n 
B 1 253 TRP 253 234 234 TRP TRP B . n 
B 1 254 PHE 254 235 235 PHE PHE B . n 
B 1 255 GLU 255 236 236 GLU GLU B . n 
B 1 256 VAL 256 237 237 VAL VAL B . n 
B 1 257 ILE 257 238 238 ILE ILE B . n 
B 1 258 SER 258 239 239 SER SER B . n 
B 1 259 GLN 259 240 240 GLN GLN B . n 
B 1 260 SER 260 241 241 SER SER B . n 
B 1 261 TYR 261 242 242 TYR TYR B . n 
B 1 262 SER 262 243 243 SER SER B . n 
B 1 263 SER 263 244 244 SER SER B . n 
B 1 264 THR 264 245 245 THR THR B . n 
B 1 265 MET 265 246 246 MET MET B . n 
B 1 266 ALA 266 247 247 ALA ALA B . n 
B 1 267 ASN 267 248 248 ASN ASN B . n 
B 1 268 ASN 268 249 249 ASN ASN B . n 
B 1 269 GLU 269 250 250 GLU GLU B . n 
B 1 270 GLY 270 251 251 GLY GLY B . n 
B 1 271 LEU 271 252 252 LEU LEU B . n 
B 1 272 PHE 272 253 253 PHE PHE B . n 
B 1 273 SER 273 254 254 SER SER B . n 
B 1 274 LEU 274 255 255 LEU LEU B . n 
B 1 275 VAL 275 256 256 VAL VAL B . n 
B 1 276 ALA 276 257 257 ALA ALA B . n 
B 1 277 ARG 277 258 258 ARG ARG B . n 
B 1 278 LYS 278 259 259 LYS LYS B . n 
B 1 279 LEU 279 260 260 LEU LEU B . n 
B 1 280 SER 280 261 261 SER SER B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IQR 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IQR 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SAH   1  301 301 SAH   SAH A . 
D 3 A1IQR 1  302 1   A1IQR INH A . 
E 2 SAH   1  301 302 SAH   SAH B . 
F 3 A1IQR 1  302 2   A1IQR INH B . 
G 4 HOH   1  401 4   HOH   HOH A . 
G 4 HOH   2  402 51  HOH   HOH A . 
G 4 HOH   3  403 28  HOH   HOH A . 
G 4 HOH   4  404 10  HOH   HOH A . 
G 4 HOH   5  405 14  HOH   HOH A . 
G 4 HOH   6  406 19  HOH   HOH A . 
G 4 HOH   7  407 54  HOH   HOH A . 
G 4 HOH   8  408 26  HOH   HOH A . 
G 4 HOH   9  409 24  HOH   HOH A . 
G 4 HOH   10 410 13  HOH   HOH A . 
G 4 HOH   11 411 21  HOH   HOH A . 
G 4 HOH   12 412 11  HOH   HOH A . 
G 4 HOH   13 413 33  HOH   HOH A . 
G 4 HOH   14 414 38  HOH   HOH A . 
G 4 HOH   15 415 48  HOH   HOH A . 
G 4 HOH   16 416 37  HOH   HOH A . 
G 4 HOH   17 417 55  HOH   HOH A . 
G 4 HOH   18 418 61  HOH   HOH A . 
G 4 HOH   19 419 64  HOH   HOH A . 
G 4 HOH   20 420 31  HOH   HOH A . 
G 4 HOH   21 421 1   HOH   HOH A . 
G 4 HOH   22 422 8   HOH   HOH A . 
G 4 HOH   23 423 50  HOH   HOH A . 
G 4 HOH   24 424 43  HOH   HOH A . 
G 4 HOH   25 425 39  HOH   HOH A . 
G 4 HOH   26 426 41  HOH   HOH A . 
G 4 HOH   27 427 15  HOH   HOH A . 
G 4 HOH   28 428 25  HOH   HOH A . 
G 4 HOH   29 429 30  HOH   HOH A . 
H 4 HOH   1  401 17  HOH   HOH B . 
H 4 HOH   2  402 2   HOH   HOH B . 
H 4 HOH   3  403 49  HOH   HOH B . 
H 4 HOH   4  404 12  HOH   HOH B . 
H 4 HOH   5  405 59  HOH   HOH B . 
H 4 HOH   6  406 47  HOH   HOH B . 
H 4 HOH   7  407 22  HOH   HOH B . 
H 4 HOH   8  408 6   HOH   HOH B . 
H 4 HOH   9  409 35  HOH   HOH B . 
H 4 HOH   10 410 52  HOH   HOH B . 
H 4 HOH   11 411 9   HOH   HOH B . 
H 4 HOH   12 412 63  HOH   HOH B . 
H 4 HOH   13 413 65  HOH   HOH B . 
H 4 HOH   14 414 58  HOH   HOH B . 
H 4 HOH   15 415 57  HOH   HOH B . 
H 4 HOH   16 416 36  HOH   HOH B . 
H 4 HOH   17 417 44  HOH   HOH B . 
H 4 HOH   18 418 18  HOH   HOH B . 
H 4 HOH   19 419 16  HOH   HOH B . 
H 4 HOH   20 420 5   HOH   HOH B . 
H 4 HOH   21 421 7   HOH   HOH B . 
H 4 HOH   22 422 20  HOH   HOH B . 
H 4 HOH   23 423 60  HOH   HOH B . 
H 4 HOH   24 424 46  HOH   HOH B . 
H 4 HOH   25 425 32  HOH   HOH B . 
H 4 HOH   26 426 53  HOH   HOH B . 
H 4 HOH   27 427 27  HOH   HOH B . 
H 4 HOH   28 428 23  HOH   HOH B . 
H 4 HOH   29 429 56  HOH   HOH B . 
H 4 HOH   30 430 3   HOH   HOH B . 
H 4 HOH   31 431 40  HOH   HOH B . 
H 4 HOH   32 432 45  HOH   HOH B . 
H 4 HOH   33 433 29  HOH   HOH B . 
H 4 HOH   34 434 62  HOH   HOH B . 
H 4 HOH   35 435 42  HOH   HOH B . 
H 4 HOH   36 436 34  HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER ? ? ? 2.11.7 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM ? ? ? .      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? BUSTER ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GWA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.07 
_cell.length_a_esd                 ? 
_cell.length_b                     69.8 
_cell.length_b_esd                 ? 
_cell.length_c                     114.88 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GWA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9GWA 
_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             1.99 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.07 
_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    '32% PEG3350, 0.2 M NaAc, and 0.1 M Hepes pH 6.8-7.5' 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 210' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-07-12 
_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   1.54178 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU FR-E' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54178 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GWA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.0 
_reflns.d_resolution_low                               30 
_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                                     34070 
_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 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.7 
_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                                   1 
_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                                    2.0 
_reflns_shell.d_res_low                                     2.05 
_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                             2369 
_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                                  0.907 
_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]                            5.5837 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            5.662 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -11.2457 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               24.67 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.908 
_refine.correlation_coeff_Fo_to_Fc_free          0.877 
_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                                 9GWA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2 
_refine.ls_d_res_low                             29.96 
_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                     34070 
_refine.ls_number_reflns_R_free                  1759 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.9 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.216 
_refine.ls_R_factor_R_free                       0.25 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.214 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.175 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.172 
_refine.pdbx_overall_SU_R_Blow_DPI               0.207 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.21 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        9GWA 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.28 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2 
_refine_hist.d_res_low                        29.96 
_refine_hist.number_atoms_solvent             65 
_refine_hist.number_atoms_total               4169 
_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        4030 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         74 
_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' ? 0.009 ? 4198 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 1.08  ? 5689 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1449 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 96   ? t_trig_c_planes           2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 629  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 4198 ? t_it                      20 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 532  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 4872 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 3.49  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 18.13 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2 
_refine_ls_shell.d_res_low                        2.06 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                2787 
_refine_ls_shell.number_reflns_R_free             166 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               94.34 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     0.2552 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2508 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.3227 
# 
_struct.entry_id                     9GWA 
_struct.title                        'NNMT-SAH IN COMPLEX WITH 5' 
_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        9GWA 
_struct_keywords.text            'NNMT, SAM, SAH, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NNMT_HUMAN 
_struct_ref.pdbx_db_accession          P40261 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLIDIGSGPTIYQLLSACESFKEIV
VTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLS
TLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQSY
SSTMANNEGLFSLVARKLS
;
_struct_ref.pdbx_align_begin           3 
# 
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 9GWA A 22 ? 280 ? P40261 3 ? 261 ? 3 261 
2 1 9GWA B 22 ? 280 ? P40261 3 ? 261 ? 3 261 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GWA HIS A 1   ? UNP P40261 ?   ?   'expression tag'      -18 1  
1 9GWA ASN A 2   ? UNP P40261 ?   ?   'expression tag'      -17 2  
1 9GWA HIS A 3   ? UNP P40261 ?   ?   'expression tag'      -16 3  
1 9GWA ASN A 4   ? UNP P40261 ?   ?   'expression tag'      -15 4  
1 9GWA HIS A 5   ? UNP P40261 ?   ?   'expression tag'      -14 5  
1 9GWA ASN A 6   ? UNP P40261 ?   ?   'expression tag'      -13 6  
1 9GWA HIS A 7   ? UNP P40261 ?   ?   'expression tag'      -12 7  
1 9GWA ASN A 8   ? UNP P40261 ?   ?   'expression tag'      -11 8  
1 9GWA HIS A 9   ? UNP P40261 ?   ?   'expression tag'      -10 9  
1 9GWA ASN A 10  ? UNP P40261 ?   ?   'expression tag'      -9  10 
1 9GWA HIS A 11  ? UNP P40261 ?   ?   'expression tag'      -8  11 
1 9GWA ASN A 12  ? UNP P40261 ?   ?   'expression tag'      -7  12 
1 9GWA ALA A 13  ? UNP P40261 ?   ?   'expression tag'      -6  13 
1 9GWA ALA A 14  ? UNP P40261 ?   ?   'expression tag'      -5  14 
1 9GWA ALA A 15  ? UNP P40261 ?   ?   'expression tag'      -4  15 
1 9GWA GLU A 16  ? UNP P40261 ?   ?   'expression tag'      -3  16 
1 9GWA ASN A 17  ? UNP P40261 ?   ?   'expression tag'      -2  17 
1 9GWA LEU A 18  ? UNP P40261 ?   ?   'expression tag'      -1  18 
1 9GWA TYR A 19  ? UNP P40261 ?   ?   'expression tag'      0   19 
1 9GWA PHE A 20  ? UNP P40261 ?   ?   'expression tag'      1   20 
1 9GWA GLN A 21  ? UNP P40261 ?   ?   'expression tag'      2   21 
1 9GWA ALA A 119 ? UNP P40261 LYS 100 'engineered mutation' 100 22 
1 9GWA ALA A 120 ? UNP P40261 GLU 101 'engineered mutation' 101 23 
1 9GWA ALA A 122 ? UNP P40261 GLU 103 'engineered mutation' 103 24 
2 9GWA HIS B 1   ? UNP P40261 ?   ?   'expression tag'      -18 25 
2 9GWA ASN B 2   ? UNP P40261 ?   ?   'expression tag'      -17 26 
2 9GWA HIS B 3   ? UNP P40261 ?   ?   'expression tag'      -16 27 
2 9GWA ASN B 4   ? UNP P40261 ?   ?   'expression tag'      -15 28 
2 9GWA HIS B 5   ? UNP P40261 ?   ?   'expression tag'      -14 29 
2 9GWA ASN B 6   ? UNP P40261 ?   ?   'expression tag'      -13 30 
2 9GWA HIS B 7   ? UNP P40261 ?   ?   'expression tag'      -12 31 
2 9GWA ASN B 8   ? UNP P40261 ?   ?   'expression tag'      -11 32 
2 9GWA HIS B 9   ? UNP P40261 ?   ?   'expression tag'      -10 33 
2 9GWA ASN B 10  ? UNP P40261 ?   ?   'expression tag'      -9  34 
2 9GWA HIS B 11  ? UNP P40261 ?   ?   'expression tag'      -8  35 
2 9GWA ASN B 12  ? UNP P40261 ?   ?   'expression tag'      -7  36 
2 9GWA ALA B 13  ? UNP P40261 ?   ?   'expression tag'      -6  37 
2 9GWA ALA B 14  ? UNP P40261 ?   ?   'expression tag'      -5  38 
2 9GWA ALA B 15  ? UNP P40261 ?   ?   'expression tag'      -4  39 
2 9GWA GLU B 16  ? UNP P40261 ?   ?   'expression tag'      -3  40 
2 9GWA ASN B 17  ? UNP P40261 ?   ?   'expression tag'      -2  41 
2 9GWA LEU B 18  ? UNP P40261 ?   ?   'expression tag'      -1  42 
2 9GWA TYR B 19  ? UNP P40261 ?   ?   'expression tag'      0   43 
2 9GWA PHE B 20  ? UNP P40261 ?   ?   'expression tag'      1   44 
2 9GWA GLN B 21  ? UNP P40261 ?   ?   'expression tag'      2   45 
2 9GWA ALA B 119 ? UNP P40261 LYS 100 'engineered mutation' 100 46 
2 9GWA ALA B 120 ? UNP P40261 GLU 101 'engineered mutation' 101 47 
2 9GWA ALA B 122 ? UNP P40261 GLU 103 'engineered mutation' 103 48 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 ASP A 28  ? HIS A 33  ? ASP A 9   HIS A 14  1 ? 6  
HELX_P HELX_P2  AA2 ASN A 35  ? LYS A 45  ? ASN A 16  LYS A 26  1 ? 11 
HELX_P HELX_P3  AA3 SER A 51  ? CYS A 69  ? SER A 32  CYS A 50  1 ? 19 
HELX_P HELX_P4  AA4 ILE A 87  ? LEU A 91  ? ILE A 68  LEU A 72  5 ? 5  
HELX_P HELX_P5  AA5 SER A 92  ? GLU A 95  ? SER A 73  GLU A 76  5 ? 4  
HELX_P HELX_P6  AA6 SER A 106 ? LYS A 118 ? SER A 87  LYS A 99  1 ? 13 
HELX_P HELX_P7  AA7 TRP A 126 ? GLU A 137 ? TRP A 107 GLU A 118 1 ? 12 
HELX_P HELX_P8  AA8 LYS A 142 ? ALA A 153 ? LYS A 123 ALA A 134 1 ? 12 
HELX_P HELX_P9  AA9 CYS A 184 ? CYS A 189 ? CYS A 165 CYS A 170 1 ? 6  
HELX_P HELX_P10 AB1 ASP A 191 ? SER A 204 ? ASP A 172 SER A 185 1 ? 14 
HELX_P HELX_P11 AB2 GLY A 236 ? ALA A 247 ? GLY A 217 ALA A 228 1 ? 12 
HELX_P HELX_P12 AB3 SER B 26  ? PHE B 34  ? SER B 7   PHE B 15  1 ? 9  
HELX_P HELX_P13 AB4 ASN B 35  ? TYR B 44  ? ASN B 16  TYR B 25  1 ? 10 
HELX_P HELX_P14 AB5 SER B 51  ? CYS B 69  ? SER B 32  CYS B 50  1 ? 19 
HELX_P HELX_P15 AB6 ILE B 87  ? LEU B 91  ? ILE B 68  LEU B 72  5 ? 5  
HELX_P HELX_P16 AB7 SER B 92  ? GLU B 95  ? SER B 73  GLU B 76  5 ? 4  
HELX_P HELX_P17 AB8 SER B 106 ? LYS B 118 ? SER B 87  LYS B 99  1 ? 13 
HELX_P HELX_P18 AB9 TRP B 126 ? GLU B 137 ? TRP B 107 GLU B 118 1 ? 12 
HELX_P HELX_P19 AC1 LYS B 142 ? ALA B 153 ? LYS B 123 ALA B 134 1 ? 12 
HELX_P HELX_P20 AC2 CYS B 184 ? CYS B 189 ? CYS B 165 CYS B 170 1 ? 6  
HELX_P HELX_P21 AC3 ASP B 191 ? SER B 204 ? ASP B 172 SER B 185 1 ? 14 
HELX_P HELX_P22 AC4 GLY B 236 ? ALA B 247 ? GLY B 217 ALA B 228 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 14 ? 
AA2 ? 2  ? 
AA3 ? 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  ? parallel      
AA1 2  3  ? parallel      
AA1 3  4  ? parallel      
AA1 4  5  ? parallel      
AA1 5  6  ? anti-parallel 
AA1 6  7  ? anti-parallel 
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? parallel      
AA1 11 12 ? parallel      
AA1 12 13 ? parallel      
AA1 13 14 ? parallel      
AA2 1  2  ? anti-parallel 
AA3 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  VAL A 154 ? LYS A 159 ? VAL A 135 LYS A 140 
AA1 2  PHE A 97  ? ASP A 104 ? PHE A 78  ASP A 85  
AA1 3  GLY A 75  ? ASP A 80  ? GLY A 56  ASP A 61  
AA1 4  ALA A 176 ? THR A 182 ? ALA A 157 THR A 163 
AA1 5  LEU A 206 ? ALA A 217 ? LEU A 187 ALA A 198 
AA1 6  LEU A 271 ? LYS A 278 ? LEU A 252 LYS A 259 
AA1 7  TYR A 249 ? ILE A 257 ? TYR A 230 ILE A 238 
AA1 8  TYR B 249 ? ILE B 257 ? TYR B 230 ILE B 238 
AA1 9  LEU B 271 ? LYS B 278 ? LEU B 252 LYS B 259 
AA1 10 LEU B 206 ? ALA B 217 ? LEU B 187 ALA B 198 
AA1 11 ALA B 176 ? THR B 182 ? ALA B 157 THR B 163 
AA1 12 GLY B 75  ? ASP B 80  ? GLY B 56  ASP B 61  
AA1 13 PHE B 97  ? ASP B 104 ? PHE B 78  ASP B 85  
AA1 14 VAL B 154 ? LYS B 159 ? VAL B 135 LYS B 140 
AA2 1  TYR A 222 ? ILE A 225 ? TYR A 203 ILE A 206 
AA2 2  GLN A 228 ? SER A 231 ? GLN A 209 SER A 212 
AA3 1  TYR B 222 ? ILE B 225 ? TYR B 203 ILE B 206 
AA3 2  GLN B 228 ? SER B 231 ? GLN B 209 SER B 212 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  O LEU A 158 ? O LEU A 139 N VAL A 102 ? N VAL A 83  
AA1 2  3  O VAL A 101 ? O VAL A 82  N ASP A 80  ? N ASP A 61  
AA1 3  4  N ILE A 79  ? N ILE A 60  O CYS A 178 ? O CYS A 159 
AA1 4  5  N VAL A 179 ? N VAL A 160 O PHE A 211 ? O PHE A 192 
AA1 5  6  N LEU A 212 ? N LEU A 193 O ALA A 276 ? O ALA A 257 
AA1 6  7  O VAL A 275 ? O VAL A 256 N GLU A 252 ? N GLU A 233 
AA1 7  8  N PHE A 254 ? N PHE A 235 O VAL B 256 ? O VAL B 237 
AA1 8  9  N ILE B 257 ? N ILE B 238 O LEU B 271 ? O LEU B 252 
AA1 9  10 O ALA B 276 ? O ALA B 257 N LEU B 212 ? N LEU B 193 
AA1 10 11 O VAL B 213 ? O VAL B 194 N VAL B 179 ? N VAL B 160 
AA1 11 12 O LEU B 180 ? O LEU B 161 N ILE B 79  ? N ILE B 60  
AA1 12 13 N ASP B 80  ? N ASP B 61  O VAL B 101 ? O VAL B 82  
AA1 13 14 N VAL B 102 ? N VAL B 83  O LEU B 158 ? O LEU B 139 
AA2 1  2  N ILE A 225 ? N ILE A 206 O GLN A 228 ? O GLN A 209 
AA3 1  2  N ILE B 225 ? N ILE B 206 O GLN B 228 ? O GLN B 209 
# 
_pdbx_entry_details.entry_id                   9GWA 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 31  ? ? -69.81  69.02   
2 1 GLU A 250 ? ? -119.87 77.48   
3 1 HIS B 31  ? ? -64.54  70.35   
4 1 LEU B 51  ? ? -29.78  -54.32  
5 1 ASP B 52  ? ? -161.12 -109.79 
# 
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 HIS -18 ? A HIS 1  
2  1 Y 1 A ASN -17 ? A ASN 2  
3  1 Y 1 A HIS -16 ? A HIS 3  
4  1 Y 1 A ASN -15 ? A ASN 4  
5  1 Y 1 A HIS -14 ? A HIS 5  
6  1 Y 1 A ASN -13 ? A ASN 6  
7  1 Y 1 A HIS -12 ? A HIS 7  
8  1 Y 1 A ASN -11 ? A ASN 8  
9  1 Y 1 A HIS -10 ? A HIS 9  
10 1 Y 1 A ASN -9  ? A ASN 10 
11 1 Y 1 A HIS -8  ? A HIS 11 
12 1 Y 1 A ASN -7  ? A ASN 12 
13 1 Y 1 A ALA -6  ? A ALA 13 
14 1 Y 1 A ALA -5  ? A ALA 14 
15 1 Y 1 A ALA -4  ? A ALA 15 
16 1 Y 1 A GLU -3  ? A GLU 16 
17 1 Y 1 A ASN -2  ? A ASN 17 
18 1 Y 1 A LEU -1  ? A LEU 18 
19 1 Y 1 A TYR 0   ? A TYR 19 
20 1 Y 1 A PHE 1   ? A PHE 20 
21 1 Y 1 A GLN 2   ? A GLN 21 
22 1 Y 1 A SER 3   ? A SER 22 
23 1 Y 1 B HIS -18 ? B HIS 1  
24 1 Y 1 B ASN -17 ? B ASN 2  
25 1 Y 1 B HIS -16 ? B HIS 3  
26 1 Y 1 B ASN -15 ? B ASN 4  
27 1 Y 1 B HIS -14 ? B HIS 5  
28 1 Y 1 B ASN -13 ? B ASN 6  
29 1 Y 1 B HIS -12 ? B HIS 7  
30 1 Y 1 B ASN -11 ? B ASN 8  
31 1 Y 1 B HIS -10 ? B HIS 9  
32 1 Y 1 B ASN -9  ? B ASN 10 
33 1 Y 1 B HIS -8  ? B HIS 11 
34 1 Y 1 B ASN -7  ? B ASN 12 
35 1 Y 1 B ALA -6  ? B ALA 13 
36 1 Y 1 B ALA -5  ? B ALA 14 
37 1 Y 1 B ALA -4  ? B ALA 15 
38 1 Y 1 B GLU -3  ? B GLU 16 
39 1 Y 1 B ASN -2  ? B ASN 17 
40 1 Y 1 B LEU -1  ? B LEU 18 
41 1 Y 1 B TYR 0   ? B TYR 19 
42 1 Y 1 B PHE 1   ? B PHE 20 
43 1 Y 1 B GLN 2   ? B GLN 21 
44 1 Y 1 B SER 3   ? B SER 22 
45 1 Y 1 B GLY 4   ? B GLY 23 
# 
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 
A1IQR C2     C N N 1   
A1IQR C7     C Y N 2   
A1IQR C8     C Y N 3   
A1IQR C9     C Y N 4   
A1IQR C10    C Y N 5   
A1IQR C11    C Y N 6   
A1IQR N1     N N N 7   
A1IQR N3     N N N 8   
A1IQR C4     C N N 9   
A1IQR C5     C N N 10  
A1IQR C6     C Y N 11  
A1IQR H1     H N N 12  
A1IQR H2     H N N 13  
A1IQR H3     H N N 14  
A1IQR H4     H N N 15  
A1IQR H5     H N N 16  
A1IQR H6     H N N 17  
A1IQR H7     H N N 18  
A1IQR H8     H N N 19  
A1IQR H9     H N N 20  
A1IQR H10    H N N 21  
ALA   N      N N N 22  
ALA   CA     C N S 23  
ALA   C      C N N 24  
ALA   O      O N N 25  
ALA   CB     C N N 26  
ALA   OXT    O N N 27  
ALA   H      H N N 28  
ALA   H2     H N N 29  
ALA   HA     H N N 30  
ALA   HB1    H N N 31  
ALA   HB2    H N N 32  
ALA   HB3    H N N 33  
ALA   HXT    H N N 34  
ARG   N      N N N 35  
ARG   CA     C N S 36  
ARG   C      C N N 37  
ARG   O      O N N 38  
ARG   CB     C N N 39  
ARG   CG     C N N 40  
ARG   CD     C N N 41  
ARG   NE     N N N 42  
ARG   CZ     C N N 43  
ARG   NH1    N N N 44  
ARG   NH2    N N N 45  
ARG   OXT    O N N 46  
ARG   H      H N N 47  
ARG   H2     H N N 48  
ARG   HA     H N N 49  
ARG   HB2    H N N 50  
ARG   HB3    H N N 51  
ARG   HG2    H N N 52  
ARG   HG3    H N N 53  
ARG   HD2    H N N 54  
ARG   HD3    H N N 55  
ARG   HE     H N N 56  
ARG   HH11   H N N 57  
ARG   HH12   H N N 58  
ARG   HH21   H N N 59  
ARG   HH22   H N N 60  
ARG   HXT    H N N 61  
ASN   N      N N N 62  
ASN   CA     C N S 63  
ASN   C      C N N 64  
ASN   O      O N N 65  
ASN   CB     C N N 66  
ASN   CG     C N N 67  
ASN   OD1    O N N 68  
ASN   ND2    N N N 69  
ASN   OXT    O N N 70  
ASN   H      H N N 71  
ASN   H2     H N N 72  
ASN   HA     H N N 73  
ASN   HB2    H N N 74  
ASN   HB3    H N N 75  
ASN   HD21   H N N 76  
ASN   HD22   H N N 77  
ASN   HXT    H N N 78  
ASP   N      N N N 79  
ASP   CA     C N S 80  
ASP   C      C N N 81  
ASP   O      O N N 82  
ASP   CB     C N N 83  
ASP   CG     C N N 84  
ASP   OD1    O N N 85  
ASP   OD2    O N N 86  
ASP   OXT    O N N 87  
ASP   H      H N N 88  
ASP   H2     H N N 89  
ASP   HA     H N N 90  
ASP   HB2    H N N 91  
ASP   HB3    H N N 92  
ASP   HD2    H N N 93  
ASP   HXT    H N N 94  
CYS   N      N N N 95  
CYS   CA     C N R 96  
CYS   C      C N N 97  
CYS   O      O N N 98  
CYS   CB     C N N 99  
CYS   SG     S N N 100 
CYS   OXT    O N N 101 
CYS   H      H N N 102 
CYS   H2     H N N 103 
CYS   HA     H N N 104 
CYS   HB2    H N N 105 
CYS   HB3    H N N 106 
CYS   HG     H N N 107 
CYS   HXT    H N N 108 
GLN   N      N N N 109 
GLN   CA     C N S 110 
GLN   C      C N N 111 
GLN   O      O N N 112 
GLN   CB     C N N 113 
GLN   CG     C N N 114 
GLN   CD     C N N 115 
GLN   OE1    O N N 116 
GLN   NE2    N N N 117 
GLN   OXT    O N N 118 
GLN   H      H N N 119 
GLN   H2     H N N 120 
GLN   HA     H N N 121 
GLN   HB2    H N N 122 
GLN   HB3    H N N 123 
GLN   HG2    H N N 124 
GLN   HG3    H N N 125 
GLN   HE21   H N N 126 
GLN   HE22   H N N 127 
GLN   HXT    H N N 128 
GLU   N      N N N 129 
GLU   CA     C N S 130 
GLU   C      C N N 131 
GLU   O      O N N 132 
GLU   CB     C N N 133 
GLU   CG     C N N 134 
GLU   CD     C N N 135 
GLU   OE1    O N N 136 
GLU   OE2    O N N 137 
GLU   OXT    O N N 138 
GLU   H      H N N 139 
GLU   H2     H N N 140 
GLU   HA     H N N 141 
GLU   HB2    H N N 142 
GLU   HB3    H N N 143 
GLU   HG2    H N N 144 
GLU   HG3    H N N 145 
GLU   HE2    H N N 146 
GLU   HXT    H N N 147 
GLY   N      N N N 148 
GLY   CA     C N N 149 
GLY   C      C N N 150 
GLY   O      O N N 151 
GLY   OXT    O N N 152 
GLY   H      H N N 153 
GLY   H2     H N N 154 
GLY   HA2    H N N 155 
GLY   HA3    H N N 156 
GLY   HXT    H N N 157 
HIS   N      N N N 158 
HIS   CA     C N S 159 
HIS   C      C N N 160 
HIS   O      O N N 161 
HIS   CB     C N N 162 
HIS   CG     C Y N 163 
HIS   ND1    N Y N 164 
HIS   CD2    C Y N 165 
HIS   CE1    C Y N 166 
HIS   NE2    N Y N 167 
HIS   OXT    O N N 168 
HIS   H      H N N 169 
HIS   H2     H N N 170 
HIS   HA     H N N 171 
HIS   HB2    H N N 172 
HIS   HB3    H N N 173 
HIS   HD1    H N N 174 
HIS   HD2    H N N 175 
HIS   HE1    H N N 176 
HIS   HE2    H N N 177 
HIS   HXT    H N N 178 
HOH   O      O N N 179 
HOH   H1     H N N 180 
HOH   H2     H N N 181 
ILE   N      N N N 182 
ILE   CA     C N S 183 
ILE   C      C N N 184 
ILE   O      O N N 185 
ILE   CB     C N S 186 
ILE   CG1    C N N 187 
ILE   CG2    C N N 188 
ILE   CD1    C N N 189 
ILE   OXT    O N N 190 
ILE   H      H N N 191 
ILE   H2     H N N 192 
ILE   HA     H N N 193 
ILE   HB     H N N 194 
ILE   HG12   H N N 195 
ILE   HG13   H N N 196 
ILE   HG21   H N N 197 
ILE   HG22   H N N 198 
ILE   HG23   H N N 199 
ILE   HD11   H N N 200 
ILE   HD12   H N N 201 
ILE   HD13   H N N 202 
ILE   HXT    H N N 203 
LEU   N      N N N 204 
LEU   CA     C N S 205 
LEU   C      C N N 206 
LEU   O      O N N 207 
LEU   CB     C N N 208 
LEU   CG     C N N 209 
LEU   CD1    C N N 210 
LEU   CD2    C N N 211 
LEU   OXT    O N N 212 
LEU   H      H N N 213 
LEU   H2     H N N 214 
LEU   HA     H N N 215 
LEU   HB2    H N N 216 
LEU   HB3    H N N 217 
LEU   HG     H N N 218 
LEU   HD11   H N N 219 
LEU   HD12   H N N 220 
LEU   HD13   H N N 221 
LEU   HD21   H N N 222 
LEU   HD22   H N N 223 
LEU   HD23   H N N 224 
LEU   HXT    H N N 225 
LYS   N      N N N 226 
LYS   CA     C N S 227 
LYS   C      C N N 228 
LYS   O      O N N 229 
LYS   CB     C N N 230 
LYS   CG     C N N 231 
LYS   CD     C N N 232 
LYS   CE     C N N 233 
LYS   NZ     N N N 234 
LYS   OXT    O N N 235 
LYS   H      H N N 236 
LYS   H2     H N N 237 
LYS   HA     H N N 238 
LYS   HB2    H N N 239 
LYS   HB3    H N N 240 
LYS   HG2    H N N 241 
LYS   HG3    H N N 242 
LYS   HD2    H N N 243 
LYS   HD3    H N N 244 
LYS   HE2    H N N 245 
LYS   HE3    H N N 246 
LYS   HZ1    H N N 247 
LYS   HZ2    H N N 248 
LYS   HZ3    H N N 249 
LYS   HXT    H N N 250 
MET   N      N N N 251 
MET   CA     C N S 252 
MET   C      C N N 253 
MET   O      O N N 254 
MET   CB     C N N 255 
MET   CG     C N N 256 
MET   SD     S N N 257 
MET   CE     C N N 258 
MET   OXT    O N N 259 
MET   H      H N N 260 
MET   H2     H N N 261 
MET   HA     H N N 262 
MET   HB2    H N N 263 
MET   HB3    H N N 264 
MET   HG2    H N N 265 
MET   HG3    H N N 266 
MET   HE1    H N N 267 
MET   HE2    H N N 268 
MET   HE3    H N N 269 
MET   HXT    H N N 270 
PHE   N      N N N 271 
PHE   CA     C N S 272 
PHE   C      C N N 273 
PHE   O      O N N 274 
PHE   CB     C N N 275 
PHE   CG     C Y N 276 
PHE   CD1    C Y N 277 
PHE   CD2    C Y N 278 
PHE   CE1    C Y N 279 
PHE   CE2    C Y N 280 
PHE   CZ     C Y N 281 
PHE   OXT    O N N 282 
PHE   H      H N N 283 
PHE   H2     H N N 284 
PHE   HA     H N N 285 
PHE   HB2    H N N 286 
PHE   HB3    H N N 287 
PHE   HD1    H N N 288 
PHE   HD2    H N N 289 
PHE   HE1    H N N 290 
PHE   HE2    H N N 291 
PHE   HZ     H N N 292 
PHE   HXT    H N N 293 
PRO   N      N N N 294 
PRO   CA     C N S 295 
PRO   C      C N N 296 
PRO   O      O N N 297 
PRO   CB     C N N 298 
PRO   CG     C N N 299 
PRO   CD     C N N 300 
PRO   OXT    O N N 301 
PRO   H      H N N 302 
PRO   HA     H N N 303 
PRO   HB2    H N N 304 
PRO   HB3    H N N 305 
PRO   HG2    H N N 306 
PRO   HG3    H N N 307 
PRO   HD2    H N N 308 
PRO   HD3    H N N 309 
PRO   HXT    H N N 310 
SAH   N      N N N 311 
SAH   CA     C N S 312 
SAH   CB     C N N 313 
SAH   CG     C N N 314 
SAH   SD     S N N 315 
SAH   C      C N N 316 
SAH   O      O N N 317 
SAH   OXT    O N N 318 
SAH   "C5'"  C N N 319 
SAH   "C4'"  C N S 320 
SAH   "O4'"  O N N 321 
SAH   "C3'"  C N S 322 
SAH   "O3'"  O N N 323 
SAH   "C2'"  C N R 324 
SAH   "O2'"  O N N 325 
SAH   "C1'"  C N R 326 
SAH   N9     N Y N 327 
SAH   C8     C Y N 328 
SAH   N7     N Y N 329 
SAH   C5     C Y N 330 
SAH   C6     C Y N 331 
SAH   N6     N N N 332 
SAH   N1     N Y N 333 
SAH   C2     C Y N 334 
SAH   N3     N Y N 335 
SAH   C4     C Y N 336 
SAH   HN1    H N N 337 
SAH   HN2    H N N 338 
SAH   HA     H N N 339 
SAH   HB1    H N N 340 
SAH   HB2    H N N 341 
SAH   HG1    H N N 342 
SAH   HG2    H N N 343 
SAH   HXT    H N N 344 
SAH   "H5'1" H N N 345 
SAH   "H5'2" H N N 346 
SAH   "H4'"  H N N 347 
SAH   "H3'"  H N N 348 
SAH   "HO3'" H N N 349 
SAH   "H2'"  H N N 350 
SAH   "HO2'" H N N 351 
SAH   "H1'"  H N N 352 
SAH   H8     H N N 353 
SAH   HN61   H N N 354 
SAH   HN62   H N N 355 
SAH   H2     H N N 356 
SER   N      N N N 357 
SER   CA     C N S 358 
SER   C      C N N 359 
SER   O      O N N 360 
SER   CB     C N N 361 
SER   OG     O N N 362 
SER   OXT    O N N 363 
SER   H      H N N 364 
SER   H2     H N N 365 
SER   HA     H N N 366 
SER   HB2    H N N 367 
SER   HB3    H N N 368 
SER   HG     H N N 369 
SER   HXT    H N N 370 
THR   N      N N N 371 
THR   CA     C N S 372 
THR   C      C N N 373 
THR   O      O N N 374 
THR   CB     C N R 375 
THR   OG1    O N N 376 
THR   CG2    C N N 377 
THR   OXT    O N N 378 
THR   H      H N N 379 
THR   H2     H N N 380 
THR   HA     H N N 381 
THR   HB     H N N 382 
THR   HG1    H N N 383 
THR   HG21   H N N 384 
THR   HG22   H N N 385 
THR   HG23   H N N 386 
THR   HXT    H N N 387 
TRP   N      N N N 388 
TRP   CA     C N S 389 
TRP   C      C N N 390 
TRP   O      O N N 391 
TRP   CB     C N N 392 
TRP   CG     C Y N 393 
TRP   CD1    C Y N 394 
TRP   CD2    C Y N 395 
TRP   NE1    N Y N 396 
TRP   CE2    C Y N 397 
TRP   CE3    C Y N 398 
TRP   CZ2    C Y N 399 
TRP   CZ3    C Y N 400 
TRP   CH2    C Y N 401 
TRP   OXT    O N N 402 
TRP   H      H N N 403 
TRP   H2     H N N 404 
TRP   HA     H N N 405 
TRP   HB2    H N N 406 
TRP   HB3    H N N 407 
TRP   HD1    H N N 408 
TRP   HE1    H N N 409 
TRP   HE3    H N N 410 
TRP   HZ2    H N N 411 
TRP   HZ3    H N N 412 
TRP   HH2    H N N 413 
TRP   HXT    H N N 414 
TYR   N      N N N 415 
TYR   CA     C N S 416 
TYR   C      C N N 417 
TYR   O      O N N 418 
TYR   CB     C N N 419 
TYR   CG     C Y N 420 
TYR   CD1    C Y N 421 
TYR   CD2    C Y N 422 
TYR   CE1    C Y N 423 
TYR   CE2    C Y N 424 
TYR   CZ     C Y N 425 
TYR   OH     O N N 426 
TYR   OXT    O N N 427 
TYR   H      H N N 428 
TYR   H2     H N N 429 
TYR   HA     H N N 430 
TYR   HB2    H N N 431 
TYR   HB3    H N N 432 
TYR   HD1    H N N 433 
TYR   HD2    H N N 434 
TYR   HE1    H N N 435 
TYR   HE2    H N N 436 
TYR   HH     H N N 437 
TYR   HXT    H N N 438 
VAL   N      N N N 439 
VAL   CA     C N S 440 
VAL   C      C N N 441 
VAL   O      O N N 442 
VAL   CB     C N N 443 
VAL   CG1    C N N 444 
VAL   CG2    C N N 445 
VAL   OXT    O N N 446 
VAL   H      H N N 447 
VAL   H2     H N N 448 
VAL   HA     H N N 449 
VAL   HB     H N N 450 
VAL   HG11   H N N 451 
VAL   HG12   H N N 452 
VAL   HG13   H N N 453 
VAL   HG21   H N N 454 
VAL   HG22   H N N 455 
VAL   HG23   H N N 456 
VAL   HXT    H N N 457 
# 
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 
A1IQR C9    C8     doub Y N 1   
A1IQR C9    C10    sing Y N 2   
A1IQR C8    C7     sing Y N 3   
A1IQR C10   C11    doub Y N 4   
A1IQR C7    C6     doub Y N 5   
A1IQR C11   C6     sing Y N 6   
A1IQR C11   C2     sing N N 7   
A1IQR C6    C5     sing N N 8   
A1IQR N1    C2     sing N N 9   
A1IQR C2    N3     doub N N 10  
A1IQR C5    C4     sing N N 11  
A1IQR N3    C4     sing N N 12  
A1IQR C7    H1     sing N N 13  
A1IQR C8    H2     sing N N 14  
A1IQR C9    H3     sing N N 15  
A1IQR C10   H4     sing N N 16  
A1IQR N1    H5     sing N N 17  
A1IQR N1    H6     sing N N 18  
A1IQR C4    H7     sing N N 19  
A1IQR C4    H8     sing N N 20  
A1IQR C5    H9     sing N N 21  
A1IQR C5    H10    sing N N 22  
ALA   N     CA     sing N N 23  
ALA   N     H      sing N N 24  
ALA   N     H2     sing N N 25  
ALA   CA    C      sing N N 26  
ALA   CA    CB     sing N N 27  
ALA   CA    HA     sing N N 28  
ALA   C     O      doub N N 29  
ALA   C     OXT    sing N N 30  
ALA   CB    HB1    sing N N 31  
ALA   CB    HB2    sing N N 32  
ALA   CB    HB3    sing N N 33  
ALA   OXT   HXT    sing N N 34  
ARG   N     CA     sing N N 35  
ARG   N     H      sing N N 36  
ARG   N     H2     sing N N 37  
ARG   CA    C      sing N N 38  
ARG   CA    CB     sing N N 39  
ARG   CA    HA     sing N N 40  
ARG   C     O      doub N N 41  
ARG   C     OXT    sing N N 42  
ARG   CB    CG     sing N N 43  
ARG   CB    HB2    sing N N 44  
ARG   CB    HB3    sing N N 45  
ARG   CG    CD     sing N N 46  
ARG   CG    HG2    sing N N 47  
ARG   CG    HG3    sing N N 48  
ARG   CD    NE     sing N N 49  
ARG   CD    HD2    sing N N 50  
ARG   CD    HD3    sing N N 51  
ARG   NE    CZ     sing N N 52  
ARG   NE    HE     sing N N 53  
ARG   CZ    NH1    sing N N 54  
ARG   CZ    NH2    doub N N 55  
ARG   NH1   HH11   sing N N 56  
ARG   NH1   HH12   sing N N 57  
ARG   NH2   HH21   sing N N 58  
ARG   NH2   HH22   sing N N 59  
ARG   OXT   HXT    sing N N 60  
ASN   N     CA     sing N N 61  
ASN   N     H      sing N N 62  
ASN   N     H2     sing N N 63  
ASN   CA    C      sing N N 64  
ASN   CA    CB     sing N N 65  
ASN   CA    HA     sing N N 66  
ASN   C     O      doub N N 67  
ASN   C     OXT    sing N N 68  
ASN   CB    CG     sing N N 69  
ASN   CB    HB2    sing N N 70  
ASN   CB    HB3    sing N N 71  
ASN   CG    OD1    doub N N 72  
ASN   CG    ND2    sing N N 73  
ASN   ND2   HD21   sing N N 74  
ASN   ND2   HD22   sing N N 75  
ASN   OXT   HXT    sing N N 76  
ASP   N     CA     sing N N 77  
ASP   N     H      sing N N 78  
ASP   N     H2     sing N N 79  
ASP   CA    C      sing N N 80  
ASP   CA    CB     sing N N 81  
ASP   CA    HA     sing N N 82  
ASP   C     O      doub N N 83  
ASP   C     OXT    sing N N 84  
ASP   CB    CG     sing N N 85  
ASP   CB    HB2    sing N N 86  
ASP   CB    HB3    sing N N 87  
ASP   CG    OD1    doub N N 88  
ASP   CG    OD2    sing N N 89  
ASP   OD2   HD2    sing N N 90  
ASP   OXT   HXT    sing N N 91  
CYS   N     CA     sing N N 92  
CYS   N     H      sing N N 93  
CYS   N     H2     sing N N 94  
CYS   CA    C      sing N N 95  
CYS   CA    CB     sing N N 96  
CYS   CA    HA     sing N N 97  
CYS   C     O      doub N N 98  
CYS   C     OXT    sing N N 99  
CYS   CB    SG     sing N N 100 
CYS   CB    HB2    sing N N 101 
CYS   CB    HB3    sing N N 102 
CYS   SG    HG     sing N N 103 
CYS   OXT   HXT    sing N N 104 
GLN   N     CA     sing N N 105 
GLN   N     H      sing N N 106 
GLN   N     H2     sing N N 107 
GLN   CA    C      sing N N 108 
GLN   CA    CB     sing N N 109 
GLN   CA    HA     sing N N 110 
GLN   C     O      doub N N 111 
GLN   C     OXT    sing N N 112 
GLN   CB    CG     sing N N 113 
GLN   CB    HB2    sing N N 114 
GLN   CB    HB3    sing N N 115 
GLN   CG    CD     sing N N 116 
GLN   CG    HG2    sing N N 117 
GLN   CG    HG3    sing N N 118 
GLN   CD    OE1    doub N N 119 
GLN   CD    NE2    sing N N 120 
GLN   NE2   HE21   sing N N 121 
GLN   NE2   HE22   sing N N 122 
GLN   OXT   HXT    sing N N 123 
GLU   N     CA     sing N N 124 
GLU   N     H      sing N N 125 
GLU   N     H2     sing N N 126 
GLU   CA    C      sing N N 127 
GLU   CA    CB     sing N N 128 
GLU   CA    HA     sing N N 129 
GLU   C     O      doub N N 130 
GLU   C     OXT    sing N N 131 
GLU   CB    CG     sing N N 132 
GLU   CB    HB2    sing N N 133 
GLU   CB    HB3    sing N N 134 
GLU   CG    CD     sing N N 135 
GLU   CG    HG2    sing N N 136 
GLU   CG    HG3    sing N N 137 
GLU   CD    OE1    doub N N 138 
GLU   CD    OE2    sing N N 139 
GLU   OE2   HE2    sing N N 140 
GLU   OXT   HXT    sing N N 141 
GLY   N     CA     sing N N 142 
GLY   N     H      sing N N 143 
GLY   N     H2     sing N N 144 
GLY   CA    C      sing N N 145 
GLY   CA    HA2    sing N N 146 
GLY   CA    HA3    sing N N 147 
GLY   C     O      doub N N 148 
GLY   C     OXT    sing N N 149 
GLY   OXT   HXT    sing N N 150 
HIS   N     CA     sing N N 151 
HIS   N     H      sing N N 152 
HIS   N     H2     sing N N 153 
HIS   CA    C      sing N N 154 
HIS   CA    CB     sing N N 155 
HIS   CA    HA     sing N N 156 
HIS   C     O      doub N N 157 
HIS   C     OXT    sing N N 158 
HIS   CB    CG     sing N N 159 
HIS   CB    HB2    sing N N 160 
HIS   CB    HB3    sing N N 161 
HIS   CG    ND1    sing Y N 162 
HIS   CG    CD2    doub Y N 163 
HIS   ND1   CE1    doub Y N 164 
HIS   ND1   HD1    sing N N 165 
HIS   CD2   NE2    sing Y N 166 
HIS   CD2   HD2    sing N N 167 
HIS   CE1   NE2    sing Y N 168 
HIS   CE1   HE1    sing N N 169 
HIS   NE2   HE2    sing N N 170 
HIS   OXT   HXT    sing N N 171 
HOH   O     H1     sing N N 172 
HOH   O     H2     sing N N 173 
ILE   N     CA     sing N N 174 
ILE   N     H      sing N N 175 
ILE   N     H2     sing N N 176 
ILE   CA    C      sing N N 177 
ILE   CA    CB     sing N N 178 
ILE   CA    HA     sing N N 179 
ILE   C     O      doub N N 180 
ILE   C     OXT    sing N N 181 
ILE   CB    CG1    sing N N 182 
ILE   CB    CG2    sing N N 183 
ILE   CB    HB     sing N N 184 
ILE   CG1   CD1    sing N N 185 
ILE   CG1   HG12   sing N N 186 
ILE   CG1   HG13   sing N N 187 
ILE   CG2   HG21   sing N N 188 
ILE   CG2   HG22   sing N N 189 
ILE   CG2   HG23   sing N N 190 
ILE   CD1   HD11   sing N N 191 
ILE   CD1   HD12   sing N N 192 
ILE   CD1   HD13   sing N N 193 
ILE   OXT   HXT    sing N N 194 
LEU   N     CA     sing N N 195 
LEU   N     H      sing N N 196 
LEU   N     H2     sing N N 197 
LEU   CA    C      sing N N 198 
LEU   CA    CB     sing N N 199 
LEU   CA    HA     sing N N 200 
LEU   C     O      doub N N 201 
LEU   C     OXT    sing N N 202 
LEU   CB    CG     sing N N 203 
LEU   CB    HB2    sing N N 204 
LEU   CB    HB3    sing N N 205 
LEU   CG    CD1    sing N N 206 
LEU   CG    CD2    sing N N 207 
LEU   CG    HG     sing N N 208 
LEU   CD1   HD11   sing N N 209 
LEU   CD1   HD12   sing N N 210 
LEU   CD1   HD13   sing N N 211 
LEU   CD2   HD21   sing N N 212 
LEU   CD2   HD22   sing N N 213 
LEU   CD2   HD23   sing N N 214 
LEU   OXT   HXT    sing N N 215 
LYS   N     CA     sing N N 216 
LYS   N     H      sing N N 217 
LYS   N     H2     sing N N 218 
LYS   CA    C      sing N N 219 
LYS   CA    CB     sing N N 220 
LYS   CA    HA     sing N N 221 
LYS   C     O      doub N N 222 
LYS   C     OXT    sing N N 223 
LYS   CB    CG     sing N N 224 
LYS   CB    HB2    sing N N 225 
LYS   CB    HB3    sing N N 226 
LYS   CG    CD     sing N N 227 
LYS   CG    HG2    sing N N 228 
LYS   CG    HG3    sing N N 229 
LYS   CD    CE     sing N N 230 
LYS   CD    HD2    sing N N 231 
LYS   CD    HD3    sing N N 232 
LYS   CE    NZ     sing N N 233 
LYS   CE    HE2    sing N N 234 
LYS   CE    HE3    sing N N 235 
LYS   NZ    HZ1    sing N N 236 
LYS   NZ    HZ2    sing N N 237 
LYS   NZ    HZ3    sing N N 238 
LYS   OXT   HXT    sing N N 239 
MET   N     CA     sing N N 240 
MET   N     H      sing N N 241 
MET   N     H2     sing N N 242 
MET   CA    C      sing N N 243 
MET   CA    CB     sing N N 244 
MET   CA    HA     sing N N 245 
MET   C     O      doub N N 246 
MET   C     OXT    sing N N 247 
MET   CB    CG     sing N N 248 
MET   CB    HB2    sing N N 249 
MET   CB    HB3    sing N N 250 
MET   CG    SD     sing N N 251 
MET   CG    HG2    sing N N 252 
MET   CG    HG3    sing N N 253 
MET   SD    CE     sing N N 254 
MET   CE    HE1    sing N N 255 
MET   CE    HE2    sing N N 256 
MET   CE    HE3    sing N N 257 
MET   OXT   HXT    sing N N 258 
PHE   N     CA     sing N N 259 
PHE   N     H      sing N N 260 
PHE   N     H2     sing N N 261 
PHE   CA    C      sing N N 262 
PHE   CA    CB     sing N N 263 
PHE   CA    HA     sing N N 264 
PHE   C     O      doub N N 265 
PHE   C     OXT    sing N N 266 
PHE   CB    CG     sing N N 267 
PHE   CB    HB2    sing N N 268 
PHE   CB    HB3    sing N N 269 
PHE   CG    CD1    doub Y N 270 
PHE   CG    CD2    sing Y N 271 
PHE   CD1   CE1    sing Y N 272 
PHE   CD1   HD1    sing N N 273 
PHE   CD2   CE2    doub Y N 274 
PHE   CD2   HD2    sing N N 275 
PHE   CE1   CZ     doub Y N 276 
PHE   CE1   HE1    sing N N 277 
PHE   CE2   CZ     sing Y N 278 
PHE   CE2   HE2    sing N N 279 
PHE   CZ    HZ     sing N N 280 
PHE   OXT   HXT    sing N N 281 
PRO   N     CA     sing N N 282 
PRO   N     CD     sing N N 283 
PRO   N     H      sing N N 284 
PRO   CA    C      sing N N 285 
PRO   CA    CB     sing N N 286 
PRO   CA    HA     sing N N 287 
PRO   C     O      doub N N 288 
PRO   C     OXT    sing N N 289 
PRO   CB    CG     sing N N 290 
PRO   CB    HB2    sing N N 291 
PRO   CB    HB3    sing N N 292 
PRO   CG    CD     sing N N 293 
PRO   CG    HG2    sing N N 294 
PRO   CG    HG3    sing N N 295 
PRO   CD    HD2    sing N N 296 
PRO   CD    HD3    sing N N 297 
PRO   OXT   HXT    sing N N 298 
SAH   N     CA     sing N N 299 
SAH   N     HN1    sing N N 300 
SAH   N     HN2    sing N N 301 
SAH   CA    CB     sing N N 302 
SAH   CA    C      sing N N 303 
SAH   CA    HA     sing N N 304 
SAH   CB    CG     sing N N 305 
SAH   CB    HB1    sing N N 306 
SAH   CB    HB2    sing N N 307 
SAH   CG    SD     sing N N 308 
SAH   CG    HG1    sing N N 309 
SAH   CG    HG2    sing N N 310 
SAH   SD    "C5'"  sing N N 311 
SAH   C     O      doub N N 312 
SAH   C     OXT    sing N N 313 
SAH   OXT   HXT    sing N N 314 
SAH   "C5'" "C4'"  sing N N 315 
SAH   "C5'" "H5'1" sing N N 316 
SAH   "C5'" "H5'2" sing N N 317 
SAH   "C4'" "O4'"  sing N N 318 
SAH   "C4'" "C3'"  sing N N 319 
SAH   "C4'" "H4'"  sing N N 320 
SAH   "O4'" "C1'"  sing N N 321 
SAH   "C3'" "O3'"  sing N N 322 
SAH   "C3'" "C2'"  sing N N 323 
SAH   "C3'" "H3'"  sing N N 324 
SAH   "O3'" "HO3'" sing N N 325 
SAH   "C2'" "O2'"  sing N N 326 
SAH   "C2'" "C1'"  sing N N 327 
SAH   "C2'" "H2'"  sing N N 328 
SAH   "O2'" "HO2'" sing N N 329 
SAH   "C1'" N9     sing N N 330 
SAH   "C1'" "H1'"  sing N N 331 
SAH   N9    C8     sing Y N 332 
SAH   N9    C4     sing Y N 333 
SAH   C8    N7     doub Y N 334 
SAH   C8    H8     sing N N 335 
SAH   N7    C5     sing Y N 336 
SAH   C5    C6     sing Y N 337 
SAH   C5    C4     doub Y N 338 
SAH   C6    N6     sing N N 339 
SAH   C6    N1     doub Y N 340 
SAH   N6    HN61   sing N N 341 
SAH   N6    HN62   sing N N 342 
SAH   N1    C2     sing Y N 343 
SAH   C2    N3     doub Y N 344 
SAH   C2    H2     sing N N 345 
SAH   N3    C4     sing Y N 346 
SER   N     CA     sing N N 347 
SER   N     H      sing N N 348 
SER   N     H2     sing N N 349 
SER   CA    C      sing N N 350 
SER   CA    CB     sing N N 351 
SER   CA    HA     sing N N 352 
SER   C     O      doub N N 353 
SER   C     OXT    sing N N 354 
SER   CB    OG     sing N N 355 
SER   CB    HB2    sing N N 356 
SER   CB    HB3    sing N N 357 
SER   OG    HG     sing N N 358 
SER   OXT   HXT    sing N N 359 
THR   N     CA     sing N N 360 
THR   N     H      sing N N 361 
THR   N     H2     sing N N 362 
THR   CA    C      sing N N 363 
THR   CA    CB     sing N N 364 
THR   CA    HA     sing N N 365 
THR   C     O      doub N N 366 
THR   C     OXT    sing N N 367 
THR   CB    OG1    sing N N 368 
THR   CB    CG2    sing N N 369 
THR   CB    HB     sing N N 370 
THR   OG1   HG1    sing N N 371 
THR   CG2   HG21   sing N N 372 
THR   CG2   HG22   sing N N 373 
THR   CG2   HG23   sing N N 374 
THR   OXT   HXT    sing N N 375 
TRP   N     CA     sing N N 376 
TRP   N     H      sing N N 377 
TRP   N     H2     sing N N 378 
TRP   CA    C      sing N N 379 
TRP   CA    CB     sing N N 380 
TRP   CA    HA     sing N N 381 
TRP   C     O      doub N N 382 
TRP   C     OXT    sing N N 383 
TRP   CB    CG     sing N N 384 
TRP   CB    HB2    sing N N 385 
TRP   CB    HB3    sing N N 386 
TRP   CG    CD1    doub Y N 387 
TRP   CG    CD2    sing Y N 388 
TRP   CD1   NE1    sing Y N 389 
TRP   CD1   HD1    sing N N 390 
TRP   CD2   CE2    doub Y N 391 
TRP   CD2   CE3    sing Y N 392 
TRP   NE1   CE2    sing Y N 393 
TRP   NE1   HE1    sing N N 394 
TRP   CE2   CZ2    sing Y N 395 
TRP   CE3   CZ3    doub Y N 396 
TRP   CE3   HE3    sing N N 397 
TRP   CZ2   CH2    doub Y N 398 
TRP   CZ2   HZ2    sing N N 399 
TRP   CZ3   CH2    sing Y N 400 
TRP   CZ3   HZ3    sing N N 401 
TRP   CH2   HH2    sing N N 402 
TRP   OXT   HXT    sing N N 403 
TYR   N     CA     sing N N 404 
TYR   N     H      sing N N 405 
TYR   N     H2     sing N N 406 
TYR   CA    C      sing N N 407 
TYR   CA    CB     sing N N 408 
TYR   CA    HA     sing N N 409 
TYR   C     O      doub N N 410 
TYR   C     OXT    sing N N 411 
TYR   CB    CG     sing N N 412 
TYR   CB    HB2    sing N N 413 
TYR   CB    HB3    sing N N 414 
TYR   CG    CD1    doub Y N 415 
TYR   CG    CD2    sing Y N 416 
TYR   CD1   CE1    sing Y N 417 
TYR   CD1   HD1    sing N N 418 
TYR   CD2   CE2    doub Y N 419 
TYR   CD2   HD2    sing N N 420 
TYR   CE1   CZ     doub Y N 421 
TYR   CE1   HE1    sing N N 422 
TYR   CE2   CZ     sing Y N 423 
TYR   CE2   HE2    sing N N 424 
TYR   CZ    OH     sing N N 425 
TYR   OH    HH     sing N N 426 
TYR   OXT   HXT    sing N N 427 
VAL   N     CA     sing N N 428 
VAL   N     H      sing N N 429 
VAL   N     H2     sing N N 430 
VAL   CA    C      sing N N 431 
VAL   CA    CB     sing N N 432 
VAL   CA    HA     sing N N 433 
VAL   C     O      doub N N 434 
VAL   C     OXT    sing N N 435 
VAL   CB    CG1    sing N N 436 
VAL   CB    CG2    sing N N 437 
VAL   CB    HB     sing N N 438 
VAL   CG1   HG11   sing N N 439 
VAL   CG1   HG12   sing N N 440 
VAL   CG1   HG13   sing N N 441 
VAL   CG2   HG21   sing N N 442 
VAL   CG2   HG22   sing N N 443 
VAL   CG2   HG23   sing N N 444 
VAL   OXT   HXT    sing N N 445 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                Sweden 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5XVK 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GWA 
_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]   0.016111 
_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]   0.014327 
_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]   0.008705 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . GLY   A 1 23  ? -0.405  11.819 21.087 1 29.63  ? 4   GLY   A N     1 
ATOM   2    C CA    . GLY   A 1 23  ? 1.004   11.713 21.454 1 28.8   ? 4   GLY   A CA    1 
ATOM   3    C C     . GLY   A 1 23  ? 1.343   12.275 22.825 1 30.38  ? 4   GLY   A C     1 
ATOM   4    O O     . GLY   A 1 23  ? 2.523   12.362 23.174 1 31.89  ? 4   GLY   A O     1 
ATOM   5    N N     . PHE   A 1 24  ? 0.318   12.622 23.635 1 21.51  ? 5   PHE   A N     1 
ATOM   6    C CA    . PHE   A 1 24  ? 0.505   13.201 24.966 1 19.46  ? 5   PHE   A CA    1 
ATOM   7    C C     . PHE   A 1 24  ? -0.333  12.452 25.983 1 23.07  ? 5   PHE   A C     1 
ATOM   8    O O     . PHE   A 1 24  ? -1.473  12.095 25.677 1 22.18  ? 5   PHE   A O     1 
ATOM   9    C CB    . PHE   A 1 24  ? 0.049   14.676 24.95  1 19.68  ? 5   PHE   A CB    1 
ATOM   10   C CG    . PHE   A 1 24  ? 0.695   15.59  25.963 1 19.12  ? 5   PHE   A CG    1 
ATOM   11   C CD1   . PHE   A 1 24  ? 1.907   16.22  25.682 1 20.34  ? 5   PHE   A CD1   1 
ATOM   12   C CD2   . PHE   A 1 24  ? 0.045   15.907 27.151 1 18.08  ? 5   PHE   A CD2   1 
ATOM   13   C CE1   . PHE   A 1 24  ? 2.482   17.103 26.6   1 19.92  ? 5   PHE   A CE1   1 
ATOM   14   C CE2   . PHE   A 1 24  ? 0.613   16.803 28.061 1 19.71  ? 5   PHE   A CE2   1 
ATOM   15   C CZ    . PHE   A 1 24  ? 1.823   17.396 27.781 1 17.84  ? 5   PHE   A CZ    1 
ATOM   16   N N     . THR   A 1 25  ? 0.209   12.266 27.208 1 18.45  ? 6   THR   A N     1 
ATOM   17   C CA    . THR   A 1 25  ? -0.462  11.637 28.349 1 17.99  ? 6   THR   A CA    1 
ATOM   18   C C     . THR   A 1 25  ? -1.92   12.098 28.394 1 21.83  ? 6   THR   A C     1 
ATOM   19   O O     . THR   A 1 25  ? -2.171  13.3   28.334 1 20.9   ? 6   THR   A O     1 
ATOM   20   C CB    . THR   A 1 25  ? 0.278   12.021 29.662 1 20.97  ? 6   THR   A CB    1 
ATOM   21   O OG1   . THR   A 1 25  ? 1.548   11.385 29.674 1 16.55  ? 6   THR   A OG1   1 
ATOM   22   C CG2   . THR   A 1 25  ? -0.493  11.621 30.942 1 18.45  ? 6   THR   A CG2   1 
ATOM   23   N N     . SER   A 1 26  ? -2.874  11.146 28.477 1 19.38  ? 7   SER   A N     1 
ATOM   24   C CA    . SER   A 1 26  ? -4.293  11.474 28.582 1 18.93  ? 7   SER   A CA    1 
ATOM   25   C C     . SER   A 1 26  ? -4.571  11.959 30.007 1 23.08  ? 7   SER   A C     1 
ATOM   26   O O     . SER   A 1 26  ? -3.899  11.531 30.947 1 21.36  ? 7   SER   A O     1 
ATOM   27   C CB    . SER   A 1 26  ? -5.168  10.277 28.216 1 21.1   ? 7   SER   A CB    1 
ATOM   28   O OG    . SER   A 1 26  ? -5.041  9.184  29.111 1 20.85  ? 7   SER   A OG    1 
ATOM   29   N N     . LYS   A 1 27  ? -5.541  12.874 30.153 1 21.17  ? 8   LYS   A N     1 
ATOM   30   C CA    . LYS   A 1 27  ? -5.97   13.485 31.417 1 21.8   ? 8   LYS   A CA    1 
ATOM   31   C C     . LYS   A 1 27  ? -6.284  12.415 32.446 1 24.36  ? 8   LYS   A C     1 
ATOM   32   O O     . LYS   A 1 27  ? -5.85   12.519 33.587 1 24.87  ? 8   LYS   A O     1 
ATOM   33   C CB    . LYS   A 1 27  ? -7.249  14.29  31.155 1 26.39  ? 8   LYS   A CB    1 
ATOM   34   C CG    . LYS   A 1 27  ? -7.334  15.642 31.831 1 35.27  ? 8   LYS   A CG    1 
ATOM   35   C CD    . LYS   A 1 27  ? -8.67   16.307 31.477 1 32.52  ? 8   LYS   A CD    1 
ATOM   36   C CE    . LYS   A 1 27  ? -8.63   17.041 30.158 1 33.79  ? 8   LYS   A CE    1 
ATOM   37   N NZ    . LYS   A 1 27  ? -9.833  17.887 29.959 1 32.14  ? 8   LYS   A NZ    1 
ATOM   38   N N     . ASP   A 1 28  ? -7.057  11.392 32.046 1 19.53  ? 9   ASP   A N     1 
ATOM   39   C CA    . ASP   A 1 28  ? -7.464  10.269 32.904 1 18.97  ? 9   ASP   A CA    1 
ATOM   40   C C     . ASP   A 1 28  ? -6.28   9.448  33.484 1 21.01  ? 9   ASP   A C     1 
ATOM   41   O O     . ASP   A 1 28  ? -6.474  8.742  34.464 1 21.94  ? 9   ASP   A O     1 
ATOM   42   C CB    . ASP   A 1 28  ? -8.437  9.356  32.145 1 20.98  ? 9   ASP   A CB    1 
ATOM   43   C CG    . ASP   A 1 28  ? -7.817  8.705  30.932 1 25.63  ? 9   ASP   A CG    1 
ATOM   44   O OD1   . ASP   A 1 28  ? -7.148  7.678  31.092 1 31.06  ? 9   ASP   A OD1   1 
ATOM   45   O OD2   . ASP   A 1 28  ? -7.97   9.24   29.843 1 29.96  ? 9   ASP   A OD2   1 
ATOM   46   N N     . THR   A 1 29  ? -5.072  9.542  32.889 1 16.24  ? 10  THR   A N     1 
ATOM   47   C CA    . THR   A 1 29  ? -3.876  8.845  33.398 1 15.62  ? 10  THR   A CA    1 
ATOM   48   C C     . THR   A 1 29  ? -3.497  9.445  34.762 1 19.31  ? 10  THR   A C     1 
ATOM   49   O O     . THR   A 1 29  ? -3.023  8.727  35.629 1 19.39  ? 10  THR   A O     1 
ATOM   50   C CB    . THR   A 1 29  ? -2.744  8.852  32.345 1 23.62  ? 10  THR   A CB    1 
ATOM   51   O OG1   . THR   A 1 29  ? -3.277  8.392  31.101 1 23.13  ? 10  THR   A OG1   1 
ATOM   52   C CG2   . THR   A 1 29  ? -1.534  7.986  32.744 1 20.55  ? 10  THR   A CG2   1 
ATOM   53   N N     . TYR   A 1 30  ? -3.773  10.748 34.964 1 16.08  ? 11  TYR   A N     1 
ATOM   54   C CA    . TYR   A 1 30  ? -3.506  11.431 36.216 1 16.27  ? 11  TYR   A CA    1 
ATOM   55   C C     . TYR   A 1 30  ? -4.352  10.915 37.359 1 23.98  ? 11  TYR   A C     1 
ATOM   56   O O     . TYR   A 1 30  ? -3.876  10.888 38.497 1 23.97  ? 11  TYR   A O     1 
ATOM   57   C CB    . TYR   A 1 30  ? -3.617  12.948 36.043 1 16.49  ? 11  TYR   A CB    1 
ATOM   58   C CG    . TYR   A 1 30  ? -2.327  13.476 35.468 1 16.88  ? 11  TYR   A CG    1 
ATOM   59   C CD1   . TYR   A 1 30  ? -1.187  13.584 36.259 1 18.62  ? 11  TYR   A CD1   1 
ATOM   60   C CD2   . TYR   A 1 30  ? -2.192  13.701 34.101 1 17.69  ? 11  TYR   A CD2   1 
ATOM   61   C CE1   . TYR   A 1 30  ? 0.029   13.999 35.725 1 20.38  ? 11  TYR   A CE1   1 
ATOM   62   C CE2   . TYR   A 1 30  ? -0.982  14.131 33.557 1 18.49  ? 11  TYR   A CE2   1 
ATOM   63   C CZ    . TYR   A 1 30  ? 0.127   14.276 34.376 1 23.08  ? 11  TYR   A CZ    1 
ATOM   64   O OH    . TYR   A 1 30  ? 1.338   14.671 33.877 1 26.19  ? 11  TYR   A OH    1 
ATOM   65   N N     . LEU   A 1 31  ? -5.579  10.447 37.057 1 22.36  ? 12  LEU   A N     1 
ATOM   66   C CA    . LEU   A 1 31  ? -6.47   9.901  38.074 1 23.05  ? 12  LEU   A CA    1 
ATOM   67   C C     . LEU   A 1 31  ? -5.994  8.547  38.587 1 23.33  ? 12  LEU   A C     1 
ATOM   68   O O     . LEU   A 1 31  ? -6.029  8.288  39.786 1 21.51  ? 12  LEU   A O     1 
ATOM   69   C CB    . LEU   A 1 31  ? -7.897  9.75   37.511 1 24.16  ? 12  LEU   A CB    1 
ATOM   70   C CG    . LEU   A 1 31  ? -8.583  11.005 36.959 1 29.56  ? 12  LEU   A CG    1 
ATOM   71   C CD1   . LEU   A 1 31  ? -9.934  10.647 36.336 1 29.74  ? 12  LEU   A CD1   1 
ATOM   72   C CD2   . LEU   A 1 31  ? -8.774  12.047 38.044 1 32.16  ? 12  LEU   A CD2   1 
ATOM   73   N N     . SER   A 1 32  ? -5.548  7.69   37.67  1 19.3   ? 13  SER   A N     1 
ATOM   74   C CA    . SER   A 1 32  ? -5.184  6.308  37.957 1 18.81  ? 13  SER   A CA    1 
ATOM   75   C C     . SER   A 1 32  ? -3.72   6.001  38.185 1 23.3   ? 13  SER   A C     1 
ATOM   76   O O     . SER   A 1 32  ? -3.421  5.192  39.071 1 23.93  ? 13  SER   A O     1 
ATOM   77   C CB    . SER   A 1 32  ? -5.686  5.414  36.83  1 20.5   ? 13  SER   A CB    1 
ATOM   78   O OG    . SER   A 1 32  ? -5.235  5.938  35.589 1 24.48  ? 13  SER   A OG    1 
ATOM   79   N N     . HIS   A 1 33  ? -2.811  6.566  37.354 1 19.18  ? 14  HIS   A N     1 
ATOM   80   C CA    . HIS   A 1 33  ? -1.406  6.17   37.326 1 18.76  ? 14  HIS   A CA    1 
ATOM   81   C C     . HIS   A 1 33  ? -0.398  7.148  37.941 1 20.84  ? 14  HIS   A C     1 
ATOM   82   O O     . HIS   A 1 33  ? 0.787   6.82   37.973 1 18.57  ? 14  HIS   A O     1 
ATOM   83   C CB    . HIS   A 1 33  ? -1.005  5.828  35.881 1 19.81  ? 14  HIS   A CB    1 
ATOM   84   C CG    . HIS   A 1 33  ? -1.634  4.563  35.383 1 23.23  ? 14  HIS   A CG    1 
ATOM   85   N ND1   . HIS   A 1 33  ? -2.943  4.535  34.941 1 24.95  ? 14  HIS   A ND1   1 
ATOM   86   C CD2   . HIS   A 1 33  ? -1.131  3.308  35.333 1 25.37  ? 14  HIS   A CD2   1 
ATOM   87   C CE1   . HIS   A 1 33  ? -3.192  3.273  34.622 1 24.62  ? 14  HIS   A CE1   1 
ATOM   88   N NE2   . HIS   A 1 33  ? -2.132  2.499  34.825 1 25.04  ? 14  HIS   A NE2   1 
ATOM   89   N N     . PHE   A 1 34  ? -0.845  8.322  38.436 1 16.84  ? 15  PHE   A N     1 
ATOM   90   C CA    . PHE   A 1 34  ? 0.049   9.264  39.11  1 15.04  ? 15  PHE   A CA    1 
ATOM   91   C C     . PHE   A 1 34  ? 0.017   8.845  40.57  1 19.64  ? 15  PHE   A C     1 
ATOM   92   O O     . PHE   A 1 34  ? -0.985  9.101  41.234 1 19.91  ? 15  PHE   A O     1 
ATOM   93   C CB    . PHE   A 1 34  ? -0.433  10.725 38.942 1 15.8   ? 15  PHE   A CB    1 
ATOM   94   C CG    . PHE   A 1 34  ? 0.529   11.774 39.475 1 16.24  ? 15  PHE   A CG    1 
ATOM   95   C CD1   . PHE   A 1 34  ? 0.607   12.047 40.841 1 18.35  ? 15  PHE   A CD1   1 
ATOM   96   C CD2   . PHE   A 1 34  ? 1.336   12.507 38.609 1 16.97  ? 15  PHE   A CD2   1 
ATOM   97   C CE1   . PHE   A 1 34  ? 1.503   13.008 41.333 1 18.45  ? 15  PHE   A CE1   1 
ATOM   98   C CE2   . PHE   A 1 34  ? 2.214   13.48  39.098 1 19     ? 15  PHE   A CE2   1 
ATOM   99   C CZ    . PHE   A 1 34  ? 2.291   13.725 40.457 1 17.21  ? 15  PHE   A CZ    1 
ATOM   100  N N     . ASN   A 1 35  ? 1.062   8.143  41.057 1 15.7   ? 16  ASN   A N     1 
ATOM   101  C CA    . ASN   A 1 35  ? 1.134   7.676  42.453 1 15.38  ? 16  ASN   A CA    1 
ATOM   102  C C     . ASN   A 1 35  ? 1.6     8.834  43.379 1 19.11  ? 16  ASN   A C     1 
ATOM   103  O O     . ASN   A 1 35  ? 2.766   9.22   43.312 1 18.12  ? 16  ASN   A O     1 
ATOM   104  C CB    . ASN   A 1 35  ? 2.042   6.429  42.562 1 14.95  ? 16  ASN   A CB    1 
ATOM   105  C CG    . ASN   A 1 35  ? 2.043   5.763  43.915 1 37.11  ? 16  ASN   A CG    1 
ATOM   106  O OD1   . ASN   A 1 35  ? 2.249   6.389  44.96  1 27.03  ? 16  ASN   A OD1   1 
ATOM   107  N ND2   . ASN   A 1 35  ? 1.89    4.453  43.92  1 34.44  ? 16  ASN   A ND2   1 
ATOM   108  N N     . PRO   A 1 36  ? 0.715   9.411  44.233 1 16.84  ? 17  PRO   A N     1 
ATOM   109  C CA    . PRO   A 1 36  ? 1.127   10.572 45.041 1 18.08  ? 17  PRO   A CA    1 
ATOM   110  C C     . PRO   A 1 36  ? 2.323   10.344 45.952 1 22.62  ? 17  PRO   A C     1 
ATOM   111  O O     . PRO   A 1 36  ? 3.247   11.151 45.936 1 20.98  ? 17  PRO   A O     1 
ATOM   112  C CB    . PRO   A 1 36  ? -0.135  10.945 45.834 1 19.53  ? 17  PRO   A CB    1 
ATOM   113  C CG    . PRO   A 1 36  ? -1.231  10.244 45.199 1 22.24  ? 17  PRO   A CG    1 
ATOM   114  C CD    . PRO   A 1 36  ? -0.707  9.082  44.453 1 17.78  ? 17  PRO   A CD    1 
ATOM   115  N N     . ARG   A 1 37  ? 2.322   9.238  46.717 1 20.64  ? 18  ARG   A N     1 
ATOM   116  C CA    . ARG   A 1 37  ? 3.424   8.933  47.625 1 20.84  ? 18  ARG   A CA    1 
ATOM   117  C C     . ARG   A 1 37  ? 4.751   8.732  46.89  1 22.25  ? 18  ARG   A C     1 
ATOM   118  O O     . ARG   A 1 37  ? 5.77    9.261  47.34  1 20.61  ? 18  ARG   A O     1 
ATOM   119  C CB    . ARG   A 1 37  ? 3.077   7.747  48.537 1 23.35  ? 18  ARG   A CB    1 
ATOM   120  C CG    . ARG   A 1 37  ? 4.202   7.299  49.499 1 40.75  ? 18  ARG   A CG    1 
ATOM   121  C CD    . ARG   A 1 37  ? 4.781   8.408  50.373 1 47.77  ? 18  ARG   A CD    1 
ATOM   122  N NE    . ARG   A 1 37  ? 3.769   8.994  51.243 1 55.11  ? 18  ARG   A NE    1 
ATOM   123  C CZ    . ARG   A 1 37  ? 3.908   9.144  52.553 1 69.42  ? 18  ARG   A CZ    1 
ATOM   124  N NH1   . ARG   A 1 37  ? 2.933   9.676  53.27  1 58.42  ? 18  ARG   A NH1   1 
ATOM   125  N NH2   . ARG   A 1 37  ? 5.027   8.765  53.158 1 54.77  ? 18  ARG   A NH2   1 
ATOM   126  N N     . ASP   A 1 38  ? 4.725   8.022  45.743 1 17.97  ? 19  ASP   A N     1 
ATOM   127  C CA    . ASP   A 1 38  ? 5.909   7.764  44.926 1 17.79  ? 19  ASP   A CA    1 
ATOM   128  C C     . ASP   A 1 38  ? 6.485   9.072  44.352 1 21.61  ? 19  ASP   A C     1 
ATOM   129  O O     . ASP   A 1 38  ? 7.704   9.265  44.354 1 22.22  ? 19  ASP   A O     1 
ATOM   130  C CB    . ASP   A 1 38  ? 5.577   6.746  43.819 1 19.57  ? 19  ASP   A CB    1 
ATOM   131  C CG    . ASP   A 1 38  ? 6.765   5.988  43.253 1 31.29  ? 19  ASP   A CG    1 
ATOM   132  O OD1   . ASP   A 1 38  ? 7.762   5.792  43.993 1 34.34  ? 19  ASP   A OD1   1 
ATOM   133  O OD2   . ASP   A 1 38  ? 6.684   5.547  42.097 1 34.38  ? 19  ASP   A OD2   1 
ATOM   134  N N     . TYR   A 1 39  ? 5.608   9.997  43.933 1 16.05  ? 20  TYR   A N     1 
ATOM   135  C CA    . TYR   A 1 39  ? 6.015   11.322 43.444 1 14.58  ? 20  TYR   A CA    1 
ATOM   136  C C     . TYR   A 1 39  ? 6.787   12.054 44.553 1 20.29  ? 20  TYR   A C     1 
ATOM   137  O O     . TYR   A 1 39  ? 7.873   12.556 44.306 1 20.54  ? 20  TYR   A O     1 
ATOM   138  C CB    . TYR   A 1 39  ? 4.762   12.126 43.055 1 14.13  ? 20  TYR   A CB    1 
ATOM   139  C CG    . TYR   A 1 39  ? 5.064   13.501 42.505 1 15.03  ? 20  TYR   A CG    1 
ATOM   140  C CD1   . TYR   A 1 39  ? 5.59    13.661 41.223 1 16.2   ? 20  TYR   A CD1   1 
ATOM   141  C CD2   . TYR   A 1 39  ? 4.778   14.647 43.243 1 14.56  ? 20  TYR   A CD2   1 
ATOM   142  C CE1   . TYR   A 1 39  ? 5.838   14.924 40.699 1 17.27  ? 20  TYR   A CE1   1 
ATOM   143  C CE2   . TYR   A 1 39  ? 5.023   15.919 42.726 1 14.17  ? 20  TYR   A CE2   1 
ATOM   144  C CZ    . TYR   A 1 39  ? 5.562   16.049 41.455 1 19.82  ? 20  TYR   A CZ    1 
ATOM   145  O OH    . TYR   A 1 39  ? 5.823   17.284 40.918 1 20.26  ? 20  TYR   A OH    1 
ATOM   146  N N     . LEU   A 1 40  ? 6.249   12.042 45.789 1 17.96  ? 21  LEU   A N     1 
ATOM   147  C CA    . LEU   A 1 40  ? 6.834   12.693 46.96  1 17.93  ? 21  LEU   A CA    1 
ATOM   148  C C     . LEU   A 1 40  ? 8.17    12.09  47.337 1 24.12  ? 21  LEU   A C     1 
ATOM   149  O O     . LEU   A 1 40  ? 9.111   12.829 47.634 1 23.88  ? 21  LEU   A O     1 
ATOM   150  C CB    . LEU   A 1 40  ? 5.852   12.67  48.155 1 17.48  ? 21  LEU   A CB    1 
ATOM   151  C CG    . LEU   A 1 40  ? 4.509   13.398 47.962 1 20.51  ? 21  LEU   A CG    1 
ATOM   152  C CD1   . LEU   A 1 40  ? 3.562   13.1   49.095 1 20.26  ? 21  LEU   A CD1   1 
ATOM   153  C CD2   . LEU   A 1 40  ? 4.697   14.883 47.811 1 22.86  ? 21  LEU   A CD2   1 
ATOM   154  N N     . GLU   A 1 41  ? 8.274   10.754 47.266 1 22.57  ? 22  GLU   A N     1 
ATOM   155  C CA    . GLU   A 1 41  ? 9.505   10.036 47.561 1 23.13  ? 22  GLU   A CA    1 
ATOM   156  C C     . GLU   A 1 41  ? 10.596  10.391 46.542 1 25.91  ? 22  GLU   A C     1 
ATOM   157  O O     . GLU   A 1 41  ? 11.733  10.656 46.932 1 25.24  ? 22  GLU   A O     1 
ATOM   158  C CB    . GLU   A 1 41  ? 9.229   8.522  47.566 1 25.49  ? 22  GLU   A CB    1 
ATOM   159  C CG    . GLU   A 1 41  ? 10.279  7.688  48.291 1 41.42  ? 22  GLU   A CG    1 
ATOM   160  C CD    . GLU   A 1 41  ? 10.384  7.861  49.797 1 67.99  ? 22  GLU   A CD    1 
ATOM   161  O OE1   . GLU   A 1 41  ? 9.399   8.305  50.432 1 61.85  ? 22  GLU   A OE1   1 
ATOM   162  O OE2   . GLU   A 1 41  ? 11.461  7.534  50.345 1 68.98  ? 22  GLU   A OE2   1 
ATOM   163  N N     . LYS   A 1 42  ? 10.234  10.442 45.242 1 21.46  ? 23  LYS   A N     1 
ATOM   164  C CA    . LYS   A 1 42  ? 11.159  10.7   44.136 1 20.61  ? 23  LYS   A CA    1 
ATOM   165  C C     . LYS   A 1 42  ? 11.653  12.119 44.012 1 24.04  ? 23  LYS   A C     1 
ATOM   166  O O     . LYS   A 1 42  ? 12.791  12.322 43.596 1 24.27  ? 23  LYS   A O     1 
ATOM   167  C CB    . LYS   A 1 42  ? 10.532  10.26  42.79  1 21.74  ? 23  LYS   A CB    1 
ATOM   168  C CG    . LYS   A 1 42  ? 11.019  8.909  42.273 1 23.48  ? 23  LYS   A CG    1 
ATOM   169  C CD    . LYS   A 1 42  ? 10.384  7.733  42.996 1 33.79  ? 23  LYS   A CD    1 
ATOM   170  C CE    . LYS   A 1 42  ? 10.891  6.412  42.473 1 33.99  ? 23  LYS   A CE    1 
ATOM   171  N NZ    . LYS   A 1 42  ? 10.429  5.287  43.315 1 32.11  ? 23  LYS   A NZ    1 
ATOM   172  N N     . TYR   A 1 43  ? 10.806  13.105 44.324 1 19.42  ? 24  TYR   A N     1 
ATOM   173  C CA    . TYR   A 1 43  ? 11.15   14.498 44.073 1 17.92  ? 24  TYR   A CA    1 
ATOM   174  C C     . TYR   A 1 43  ? 11.293  15.392 45.283 1 21.43  ? 24  TYR   A C     1 
ATOM   175  O O     . TYR   A 1 43  ? 11.935  16.44  45.175 1 20.92  ? 24  TYR   A O     1 
ATOM   176  C CB    . TYR   A 1 43  ? 10.096  15.103 43.125 1 18     ? 24  TYR   A CB    1 
ATOM   177  C CG    . TYR   A 1 43  ? 10.185  14.596 41.697 1 18.77  ? 24  TYR   A CG    1 
ATOM   178  C CD1   . TYR   A 1 43  ? 11.032  15.202 40.774 1 20.36  ? 24  TYR   A CD1   1 
ATOM   179  C CD2   . TYR   A 1 43  ? 9.381   13.544 41.253 1 18.62  ? 24  TYR   A CD2   1 
ATOM   180  C CE1   . TYR   A 1 43  ? 11.112  14.75  39.454 1 19.64  ? 24  TYR   A CE1   1 
ATOM   181  C CE2   . TYR   A 1 43  ? 9.426   13.105 39.924 1 18.56  ? 24  TYR   A CE2   1 
ATOM   182  C CZ    . TYR   A 1 43  ? 10.297  13.712 39.029 1 22.29  ? 24  TYR   A CZ    1 
ATOM   183  O OH    . TYR   A 1 43  ? 10.401  13.277 37.726 1 17.28  ? 24  TYR   A OH    1 
ATOM   184  N N     . TYR   A 1 44  ? 10.646  15.035 46.398 1 18.74  ? 25  TYR   A N     1 
ATOM   185  C CA    . TYR   A 1 44  ? 10.568  15.914 47.55  1 19.81  ? 25  TYR   A CA    1 
ATOM   186  C C     . TYR   A 1 44  ? 11.034  15.311 48.886 1 29.48  ? 25  TYR   A C     1 
ATOM   187  O O     . TYR   A 1 44  ? 10.761  15.914 49.926 1 28.53  ? 25  TYR   A O     1 
ATOM   188  C CB    . TYR   A 1 44  ? 9.119   16.451 47.655 1 19.07  ? 25  TYR   A CB    1 
ATOM   189  C CG    . TYR   A 1 44  ? 8.751   17.338 46.487 1 18.06  ? 25  TYR   A CG    1 
ATOM   190  C CD1   . TYR   A 1 44  ? 9.244   18.635 46.391 1 18.95  ? 25  TYR   A CD1   1 
ATOM   191  C CD2   . TYR   A 1 44  ? 7.944   16.868 45.452 1 17.87  ? 25  TYR   A CD2   1 
ATOM   192  C CE1   . TYR   A 1 44  ? 8.988   19.429 45.273 1 16.51  ? 25  TYR   A CE1   1 
ATOM   193  C CE2   . TYR   A 1 44  ? 7.671   17.659 44.331 1 17.92  ? 25  TYR   A CE2   1 
ATOM   194  C CZ    . TYR   A 1 44  ? 8.188   18.943 44.254 1 20.29  ? 25  TYR   A CZ    1 
ATOM   195  O OH    . TYR   A 1 44  ? 7.89    19.762 43.194 1 17.17  ? 25  TYR   A OH    1 
ATOM   196  N N     . LYS   A 1 45  ? 11.758  14.172 48.872 1 31.99  ? 26  LYS   A N     1 
ATOM   197  C CA    . LYS   A 1 45  ? 12.248  13.555 50.121 1 35.26  ? 26  LYS   A CA    1 
ATOM   198  C C     . LYS   A 1 45  ? 13.301  14.43  50.847 1 44.58  ? 26  LYS   A C     1 
ATOM   199  O O     . LYS   A 1 45  ? 13.386  14.366 52.082 1 45.08  ? 26  LYS   A O     1 
ATOM   200  C CB    . LYS   A 1 45  ? 12.736  12.105 49.929 1 38.65  ? 26  LYS   A CB    1 
ATOM   201  C CG    . LYS   A 1 45  ? 13.957  11.924 49.032 1 64.14  ? 26  LYS   A CG    1 
ATOM   202  C CD    . LYS   A 1 45  ? 14.391  10.452 49.006 1 79.19  ? 26  LYS   A CD    1 
ATOM   203  C CE    . LYS   A 1 45  ? 15.008  10.028 47.692 1 92.12  ? 26  LYS   A CE    1 
ATOM   204  N NZ    . LYS   A 1 45  ? 16.399  10.534 47.536 1 102.29 ? 26  LYS   A NZ    1 
ATOM   205  N N     . PHE   A 1 46  ? 14.055  15.274 50.081 1 43.72  ? 27  PHE   A N     1 
ATOM   206  C CA    . PHE   A 1 46  ? 15.047  16.242 50.574 1 44.97  ? 27  PHE   A CA    1 
ATOM   207  C C     . PHE   A 1 46  ? 16.122  15.548 51.426 1 53.79  ? 27  PHE   A C     1 
ATOM   208  O O     . PHE   A 1 46  ? 16.413  15.972 52.55  1 53.72  ? 27  PHE   A O     1 
ATOM   209  C CB    . PHE   A 1 46  ? 14.315  17.377 51.339 1 46.7   ? 27  PHE   A CB    1 
ATOM   210  C CG    . PHE   A 1 46  ? 14.932  18.758 51.384 1 48.41  ? 27  PHE   A CG    1 
ATOM   211  C CD1   . PHE   A 1 46  ? 15.345  19.394 50.217 1 52.27  ? 27  PHE   A CD1   1 
ATOM   212  C CD2   . PHE   A 1 46  ? 14.996  19.467 52.578 1 50.2   ? 27  PHE   A CD2   1 
ATOM   213  C CE1   . PHE   A 1 46  ? 15.864  20.693 50.255 1 53.4   ? 27  PHE   A CE1   1 
ATOM   214  C CE2   . PHE   A 1 46  ? 15.521  20.761 52.617 1 53.25  ? 27  PHE   A CE2   1 
ATOM   215  C CZ    . PHE   A 1 46  ? 15.95   21.368 51.455 1 51.91  ? 27  PHE   A CZ    1 
ATOM   216  N N     . GLY   A 1 47  ? 16.672  14.465 50.875 1 53.69  ? 28  GLY   A N     1 
ATOM   217  C CA    . GLY   A 1 47  ? 17.69   13.633 51.511 1 54.9   ? 28  GLY   A CA    1 
ATOM   218  C C     . GLY   A 1 47  ? 19.023  14.319 51.729 1 61.48  ? 28  GLY   A C     1 
ATOM   219  O O     . GLY   A 1 47  ? 19.289  15.371 51.136 1 61.48  ? 28  GLY   A O     1 
ATOM   220  N N     . SER   A 1 48  ? 19.869  13.707 52.59  1 59.64  ? 29  SER   A N     1 
ATOM   221  C CA    . SER   A 1 48  ? 21.21   14.179 52.973 1 60.32  ? 29  SER   A CA    1 
ATOM   222  C C     . SER   A 1 48  ? 22.134  14.473 51.782 1 64.32  ? 29  SER   A C     1 
ATOM   223  O O     . SER   A 1 48  ? 22.883  15.455 51.821 1 64.45  ? 29  SER   A O     1 
ATOM   224  C CB    . SER   A 1 48  ? 21.873  13.196 53.935 1 65.23  ? 29  SER   A CB    1 
ATOM   225  O OG    . SER   A 1 48  ? 22.121  11.938 53.326 1 76.46  ? 29  SER   A OG    1 
ATOM   226  N N     . ARG   A 1 49  ? 22.061  13.639 50.721 1 60.09  ? 30  ARG   A N     1 
ATOM   227  C CA    . ARG   A 1 49  ? 22.851  13.812 49.496 1 59.24  ? 30  ARG   A CA    1 
ATOM   228  C C     . ARG   A 1 49  ? 22.319  14.998 48.685 1 59.3   ? 30  ARG   A C     1 
ATOM   229  O O     . ARG   A 1 49  ? 21.102  15.13  48.514 1 59.37  ? 30  ARG   A O     1 
ATOM   230  C CB    . ARG   A 1 49  ? 22.861  12.526 48.638 1 60.86  ? 30  ARG   A CB    1 
ATOM   231  C CG    . ARG   A 1 49  ? 23.21   11.228 49.386 1 75.91  ? 30  ARG   A CG    1 
ATOM   232  C CD    . ARG   A 1 49  ? 24.599  11.222 50.011 1 91.27  ? 30  ARG   A CD    1 
ATOM   233  N NE    . ARG   A 1 49  ? 24.534  11.286 51.475 1 104.2  ? 30  ARG   A NE    1 
ATOM   234  C CZ    . ARG   A 1 49  ? 25.204  12.155 52.229 1 118.63 ? 30  ARG   A CZ    1 
ATOM   235  N NH1   . ARG   A 1 49  ? 26.007  13.052 51.668 1 105.49 ? 30  ARG   A NH1   1 
ATOM   236  N NH2   . ARG   A 1 49  ? 25.082  12.129 53.549 1 104.4  ? 30  ARG   A NH2   1 
ATOM   237  N N     . HIS   A 1 50  ? 23.238  15.858 48.202 1 51.98  ? 31  HIS   A N     1 
ATOM   238  C CA    . HIS   A 1 50  ? 22.952  17.063 47.409 1 49.42  ? 31  HIS   A CA    1 
ATOM   239  C C     . HIS   A 1 50  ? 22.438  16.722 45.991 1 44.29  ? 31  HIS   A C     1 
ATOM   240  O O     . HIS   A 1 50  ? 23.136  16.977 44.998 1 44.38  ? 31  HIS   A O     1 
ATOM   241  C CB    . HIS   A 1 50  ? 24.208  17.961 47.331 1 50.88  ? 31  HIS   A CB    1 
ATOM   242  C CG    . HIS   A 1 50  ? 24.633  18.567 48.634 1 54.91  ? 31  HIS   A CG    1 
ATOM   243  N ND1   . HIS   A 1 50  ? 25.228  17.804 49.629 1 56.91  ? 31  HIS   A ND1   1 
ATOM   244  C CD2   . HIS   A 1 50  ? 24.594  19.859 49.038 1 57.11  ? 31  HIS   A CD2   1 
ATOM   245  C CE1   . HIS   A 1 50  ? 25.501  18.648 50.614 1 56.54  ? 31  HIS   A CE1   1 
ATOM   246  N NE2   . HIS   A 1 50  ? 25.144  19.897 50.303 1 57     ? 31  HIS   A NE2   1 
ATOM   247  N N     . SER   A 1 51  ? 21.209  16.167 45.898 1 32.5   ? 32  SER   A N     1 
ATOM   248  C CA    . SER   A 1 51  ? 20.58   15.802 44.62  1 28.87  ? 32  SER   A CA    1 
ATOM   249  C C     . SER   A 1 51  ? 20.165  17.021 43.786 1 26.54  ? 32  SER   A C     1 
ATOM   250  O O     . SER   A 1 51  ? 20.03   18.122 44.321 1 23.51  ? 32  SER   A O     1 
ATOM   251  C CB    . SER   A 1 51  ? 19.366  14.902 44.853 1 29.87  ? 32  SER   A CB    1 
ATOM   252  O OG    . SER   A 1 51  ? 18.304  15.58  45.507 1 30.93  ? 32  SER   A OG    1 
ATOM   253  N N     . ALA   A 1 52  ? 19.919  16.803 42.478 1 21.97  ? 33  ALA   A N     1 
ATOM   254  C CA    . ALA   A 1 52  ? 19.437  17.838 41.564 1 20.57  ? 33  ALA   A CA    1 
ATOM   255  C C     . ALA   A 1 52  ? 18.025  18.253 42.027 1 22.45  ? 33  ALA   A C     1 
ATOM   256  O O     . ALA   A 1 52  ? 17.704  19.436 42.005 1 20.76  ? 33  ALA   A O     1 
ATOM   257  C CB    . ALA   A 1 52  ? 19.379  17.293 40.143 1 21.07  ? 33  ALA   A CB    1 
ATOM   258  N N     . GLU   A 1 53  ? 17.221  17.274 42.519 1 17.56  ? 34  GLU   A N     1 
ATOM   259  C CA    . GLU   A 1 53  ? 15.849  17.492 42.99  1 17.24  ? 34  GLU   A CA    1 
ATOM   260  C C     . GLU   A 1 53  ? 15.831  18.412 44.207 1 21.78  ? 34  GLU   A C     1 
ATOM   261  O O     . GLU   A 1 53  ? 14.975  19.297 44.284 1 20.83  ? 34  GLU   A O     1 
ATOM   262  C CB    . GLU   A 1 53  ? 15.143  16.159 43.291 1 18.76  ? 34  GLU   A CB    1 
ATOM   263  C CG    . GLU   A 1 53  ? 14.735  15.343 42.065 1 26.36  ? 34  GLU   A CG    1 
ATOM   264  C CD    . GLU   A 1 53  ? 15.848  14.922 41.123 1 36.98  ? 34  GLU   A CD    1 
ATOM   265  O OE1   . GLU   A 1 53  ? 16.831  14.312 41.6   1 23.42  ? 34  GLU   A OE1   1 
ATOM   266  O OE2   . GLU   A 1 53  ? 15.773  15.275 39.924 1 24.67  ? 34  GLU   A OE2   1 
ATOM   267  N N     . SER   A 1 54  ? 16.799  18.237 45.132 1 18.74  ? 35  SER   A N     1 
ATOM   268  C CA    . SER   A 1 54  ? 16.892  19.088 46.317 1 19.1   ? 35  SER   A CA    1 
ATOM   269  C C     . SER   A 1 54  ? 17.396  20.494 45.98  1 22.37  ? 35  SER   A C     1 
ATOM   270  O O     . SER   A 1 54  ? 16.918  21.45  46.579 1 23.36  ? 35  SER   A O     1 
ATOM   271  C CB    . SER   A 1 54  ? 17.736  18.422 47.4   1 24.39  ? 35  SER   A CB    1 
ATOM   272  O OG    . SER   A 1 54  ? 17.023  17.311 47.92  1 34.35  ? 35  SER   A OG    1 
ATOM   273  N N     . GLN   A 1 55  ? 18.31   20.632 44.988 1 19.31  ? 36  GLN   A N     1 
ATOM   274  C CA    . GLN   A 1 55  ? 18.828  21.936 44.536 1 18.33  ? 36  GLN   A CA    1 
ATOM   275  C C     . GLN   A 1 55  ? 17.692  22.746 43.91  1 20.3   ? 36  GLN   A C     1 
ATOM   276  O O     . GLN   A 1 55  ? 17.623  23.964 44.1   1 19.36  ? 36  GLN   A O     1 
ATOM   277  C CB    . GLN   A 1 55  ? 19.962  21.769 43.496 1 19.7   ? 36  GLN   A CB    1 
ATOM   278  C CG    . GLN   A 1 55  ? 21.265  21.144 44.027 1 32.01  ? 36  GLN   A CG    1 
ATOM   279  C CD    . GLN   A 1 55  ? 21.923  21.973 45.099 1 54.88  ? 36  GLN   A CD    1 
ATOM   280  O OE1   . GLN   A 1 55  ? 21.751  21.721 46.293 1 50.84  ? 36  GLN   A OE1   1 
ATOM   281  N NE2   . GLN   A 1 55  ? 22.675  22.99  44.699 1 49.42  ? 36  GLN   A NE2   1 
ATOM   282  N N     . ILE   A 1 56  ? 16.792  22.06  43.166 1 16.42  ? 37  ILE   A N     1 
ATOM   283  C CA    . ILE   A 1 56  ? 15.628  22.692 42.529 1 15.14  ? 37  ILE   A CA    1 
ATOM   284  C C     . ILE   A 1 56  ? 14.648  23.142 43.603 1 19.82  ? 37  ILE   A C     1 
ATOM   285  O O     . ILE   A 1 56  ? 14.28   24.314 43.617 1 19.91  ? 37  ILE   A O     1 
ATOM   286  C CB    . ILE   A 1 56  ? 15.014  21.776 41.429 1 16.76  ? 37  ILE   A CB    1 
ATOM   287  C CG1   . ILE   A 1 56  ? 15.984  21.694 40.234 1 15.71  ? 37  ILE   A CG1   1 
ATOM   288  C CG2   . ILE   A 1 56  ? 13.612  22.259 40.972 1 15.64  ? 37  ILE   A CG2   1 
ATOM   289  C CD1   . ILE   A 1 56  ? 15.775  20.511 39.3   1 17.01  ? 37  ILE   A CD1   1 
ATOM   290  N N     . LEU   A 1 57  ? 14.326  22.247 44.558 1 16.27  ? 38  LEU   A N     1 
ATOM   291  C CA    . LEU   A 1 57  ? 13.399  22.525 45.663 1 16.88  ? 38  LEU   A CA    1 
ATOM   292  C C     . LEU   A 1 57  ? 13.838  23.72  46.521 1 19.07  ? 38  LEU   A C     1 
ATOM   293  O O     . LEU   A 1 57  ? 13.011  24.569 46.853 1 17.5   ? 38  LEU   A O     1 
ATOM   294  C CB    . LEU   A 1 57  ? 13.18   21.26  46.511 1 17.27  ? 38  LEU   A CB    1 
ATOM   295  C CG    . LEU   A 1 57  ? 12.258  21.358 47.742 1 23.01  ? 38  LEU   A CG    1 
ATOM   296  C CD1   . LEU   A 1 57  ? 10.84   21.738 47.351 1 23.75  ? 38  LEU   A CD1   1 
ATOM   297  C CD2   . LEU   A 1 57  ? 12.25   20.047 48.51  1 24.44  ? 38  LEU   A CD2   1 
ATOM   298  N N     . LYS   A 1 58  ? 15.144  23.81  46.813 1 15.18  ? 39  LYS   A N     1 
ATOM   299  C CA    . LYS   A 1 58  ? 15.736  24.923 47.564 1 14.76  ? 39  LYS   A CA    1 
ATOM   300  C C     . LYS   A 1 58  ? 15.564  26.239 46.799 1 19.97  ? 39  LYS   A C     1 
ATOM   301  O O     . LYS   A 1 58  ? 15.246  27.267 47.407 1 18.91  ? 39  LYS   A O     1 
ATOM   302  C CB    . LYS   A 1 58  ? 17.224  24.671 47.844 1 16.48  ? 39  LYS   A CB    1 
ATOM   303  C CG    . LYS   A 1 58  ? 17.474  23.67  48.962 1 27.55  ? 39  LYS   A CG    1 
ATOM   304  C CD    . LYS   A 1 58  ? 18.959  23.523 49.261 1 35.97  ? 39  LYS   A CD    1 
ATOM   305  C CE    . LYS   A 1 58  ? 19.522  22.239 48.701 1 55.59  ? 39  LYS   A CE    1 
ATOM   306  N NZ    . LYS   A 1 58  ? 20.985  22.131 48.947 1 67.58  ? 39  LYS   A NZ    1 
ATOM   307  N N     . HIS   A 1 59  ? 15.751  26.206 45.468 1 16.88  ? 40  HIS   A N     1 
ATOM   308  C CA    . HIS   A 1 59  ? 15.594  27.417 44.663 1 16.85  ? 40  HIS   A CA    1 
ATOM   309  C C     . HIS   A 1 59  ? 14.149  27.863 44.576 1 21.28  ? 40  HIS   A C     1 
ATOM   310  O O     . HIS   A 1 59  ? 13.883  29.055 44.75  1 20.16  ? 40  HIS   A O     1 
ATOM   311  C CB    . HIS   A 1 59  ? 16.236  27.314 43.277 1 17.38  ? 40  HIS   A CB    1 
ATOM   312  C CG    . HIS   A 1 59  ? 16.323  28.66  42.628 1 20.68  ? 40  HIS   A CG    1 
ATOM   313  N ND1   . HIS   A 1 59  ? 17.367  29.518 42.896 1 22.52  ? 40  HIS   A ND1   1 
ATOM   314  C CD2   . HIS   A 1 59  ? 15.429  29.295 41.836 1 22.31  ? 40  HIS   A CD2   1 
ATOM   315  C CE1   . HIS   A 1 59  ? 17.115  30.618 42.207 1 21.94  ? 40  HIS   A CE1   1 
ATOM   316  N NE2   . HIS   A 1 59  ? 15.955  30.531 41.561 1 22.27  ? 40  HIS   A NE2   1 
ATOM   317  N N     . LEU   A 1 60  ? 13.209  26.911 44.354 1 19.26  ? 41  LEU   A N     1 
ATOM   318  C CA    . LEU   A 1 60  ? 11.776  27.234 44.321 1 18.36  ? 41  LEU   A CA    1 
ATOM   319  C C     . LEU   A 1 60  ? 11.354  27.886 45.639 1 20.76  ? 41  LEU   A C     1 
ATOM   320  O O     . LEU   A 1 60  ? 10.713  28.937 45.603 1 19.74  ? 41  LEU   A O     1 
ATOM   321  C CB    . LEU   A 1 60  ? 10.913  25.994 44     1 18.07  ? 41  LEU   A CB    1 
ATOM   322  C CG    . LEU   A 1 60  ? 11.156  25.342 42.622 1 21.44  ? 41  LEU   A CG    1 
ATOM   323  C CD1   . LEU   A 1 60  ? 10.318  24.084 42.463 1 20.36  ? 41  LEU   A CD1   1 
ATOM   324  C CD2   . LEU   A 1 60  ? 10.912  26.332 41.46  1 23.83  ? 41  LEU   A CD2   1 
ATOM   325  N N     . LEU   A 1 61  ? 11.816  27.335 46.79  1 17.15  ? 42  LEU   A N     1 
ATOM   326  C CA    . LEU   A 1 61  ? 11.519  27.884 48.122 1 17.45  ? 42  LEU   A CA    1 
ATOM   327  C C     . LEU   A 1 61  ? 12.03   29.306 48.32  1 21.4   ? 42  LEU   A C     1 
ATOM   328  O O     . LEU   A 1 61  ? 11.35   30.117 48.955 1 19.17  ? 42  LEU   A O     1 
ATOM   329  C CB    . LEU   A 1 61  ? 12.01   26.965 49.256 1 17.67  ? 42  LEU   A CB    1 
ATOM   330  C CG    . LEU   A 1 61  ? 11.316  25.595 49.394 1 22.21  ? 42  LEU   A CG    1 
ATOM   331  C CD1   . LEU   A 1 61  ? 12.02   24.725 50.445 1 22.72  ? 42  LEU   A CD1   1 
ATOM   332  C CD2   . LEU   A 1 61  ? 9.825   25.732 49.723 1 24.04  ? 42  LEU   A CD2   1 
ATOM   333  N N     . LYS   A 1 62  ? 13.209  29.623 47.746 1 20.52  ? 43  LYS   A N     1 
ATOM   334  C CA    . LYS   A 1 62  ? 13.812  30.959 47.832 1 19.99  ? 43  LYS   A CA    1 
ATOM   335  C C     . LYS   A 1 62  ? 12.946  31.976 47.112 1 22.43  ? 43  LYS   A C     1 
ATOM   336  O O     . LYS   A 1 62  ? 12.718  33.07  47.638 1 21.06  ? 43  LYS   A O     1 
ATOM   337  C CB    . LYS   A 1 62  ? 15.232  30.968 47.231 1 22.61  ? 43  LYS   A CB    1 
ATOM   338  C CG    . LYS   A 1 62  ? 16.283  30.266 48.083 1 31.93  ? 43  LYS   A CG    1 
ATOM   339  C CD    . LYS   A 1 62  ? 17.63   30.243 47.363 1 38.58  ? 43  LYS   A CD    1 
ATOM   340  C CE    . LYS   A 1 62  ? 18.61   29.278 47.986 1 38.91  ? 43  LYS   A CE    1 
ATOM   341  N NZ    . LYS   A 1 62  ? 19.922  29.27  47.265 1 43.04  ? 43  LYS   A NZ    1 
ATOM   342  N N     . ASN   A 1 63  ? 12.455  31.61  45.911 1 18.6   ? 44  ASN   A N     1 
ATOM   343  C CA    . ASN   A 1 63  ? 11.608  32.478 45.081 1 17.88  ? 44  ASN   A CA    1 
ATOM   344  C C     . ASN   A 1 63  ? 10.257  32.713 45.73  1 21.29  ? 44  ASN   A C     1 
ATOM   345  O O     . ASN   A 1 63  ? 9.814   33.866 45.832 1 20.55  ? 44  ASN   A O     1 
ATOM   346  C CB    . ASN   A 1 63  ? 11.452  31.893 43.68  1 17.14  ? 44  ASN   A CB    1 
ATOM   347  C CG    . ASN   A 1 63  ? 12.638  32.132 42.773 1 24.47  ? 44  ASN   A CG    1 
ATOM   348  O OD1   . ASN   A 1 63  ? 13.51   32.96  43.034 1 20.1   ? 44  ASN   A OD1   1 
ATOM   349  N ND2   . ASN   A 1 63  ? 12.657  31.451 41.653 1 16.61  ? 44  ASN   A ND2   1 
ATOM   350  N N     . LEU   A 1 64  ? 9.643   31.634 46.248 1 16.19  ? 45  LEU   A N     1 
ATOM   351  C CA    . LEU   A 1 64  ? 8.358   31.704 46.952 1 15.5   ? 45  LEU   A CA    1 
ATOM   352  C C     . LEU   A 1 64  ? 8.463   32.591 48.19  1 22.61  ? 45  LEU   A C     1 
ATOM   353  O O     . LEU   A 1 64  ? 7.569   33.404 48.422 1 22.14  ? 45  LEU   A O     1 
ATOM   354  C CB    . LEU   A 1 64  ? 7.878   30.31  47.33  1 14.63  ? 45  LEU   A CB    1 
ATOM   355  C CG    . LEU   A 1 64  ? 7.498   29.415 46.159 1 17.33  ? 45  LEU   A CG    1 
ATOM   356  C CD1   . LEU   A 1 64  ? 7.568   27.963 46.564 1 16.15  ? 45  LEU   A CD1   1 
ATOM   357  C CD2   . LEU   A 1 64  ? 6.126   29.817 45.554 1 18.42  ? 45  LEU   A CD2   1 
ATOM   358  N N     . PHE   A 1 65  ? 9.58    32.464 48.956 1 21.64  ? 46  PHE   A N     1 
ATOM   359  C CA    . PHE   A 1 65  ? 9.858   33.314 50.122 1 21.7   ? 46  PHE   A CA    1 
ATOM   360  C C     . PHE   A 1 65  ? 9.929   34.763 49.678 1 24.26  ? 46  PHE   A C     1 
ATOM   361  O O     . PHE   A 1 65  ? 9.271   35.603 50.286 1 25.35  ? 46  PHE   A O     1 
ATOM   362  C CB    . PHE   A 1 65  ? 11.161  32.912 50.836 1 24.05  ? 46  PHE   A CB    1 
ATOM   363  C CG    . PHE   A 1 65  ? 11.631  33.959 51.819 1 26.63  ? 46  PHE   A CG    1 
ATOM   364  C CD1   . PHE   A 1 65  ? 10.907  34.228 52.976 1 30.6   ? 46  PHE   A CD1   1 
ATOM   365  C CD2   . PHE   A 1 65  ? 12.754  34.728 51.553 1 29.99  ? 46  PHE   A CD2   1 
ATOM   366  C CE1   . PHE   A 1 65  ? 11.321  35.227 53.868 1 31.38  ? 46  PHE   A CE1   1 
ATOM   367  C CE2   . PHE   A 1 65  ? 13.179  35.709 52.462 1 32.82  ? 46  PHE   A CE2   1 
ATOM   368  C CZ    . PHE   A 1 65  ? 12.455  35.955 53.609 1 30.22  ? 46  PHE   A CZ    1 
ATOM   369  N N     . LYS   A 1 66  ? 10.709  35.052 48.613 1 18.54  ? 47  LYS   A N     1 
ATOM   370  C CA    . LYS   A 1 66  ? 10.847  36.399 48.061 1 17.98  ? 47  LYS   A CA    1 
ATOM   371  C C     . LYS   A 1 66  ? 9.509   36.985 47.596 1 21.68  ? 47  LYS   A C     1 
ATOM   372  O O     . LYS   A 1 66  ? 9.251   38.152 47.86  1 21     ? 47  LYS   A O     1 
ATOM   373  C CB    . LYS   A 1 66  ? 11.886  36.437 46.92  1 20.44  ? 47  LYS   A CB    1 
ATOM   374  C CG    . LYS   A 1 66  ? 12.132  37.856 46.39  1 29.53  ? 47  LYS   A CG    1 
ATOM   375  C CD    . LYS   A 1 66  ? 12.846  37.892 45.066 1 36.09  ? 47  LYS   A CD    1 
ATOM   376  C CE    . LYS   A 1 66  ? 12.832  39.294 44.477 1 43.22  ? 47  LYS   A CE    1 
ATOM   377  N NZ    . LYS   A 1 66  ? 11.582  39.582 43.708 1 43.97  ? 47  LYS   A NZ    1 
ATOM   378  N N     . ILE   A 1 67  ? 8.686   36.199 46.875 1 18.48  ? 48  ILE   A N     1 
ATOM   379  C CA    . ILE   A 1 67  ? 7.392   36.641 46.341 1 18.76  ? 48  ILE   A CA    1 
ATOM   380  C C     . ILE   A 1 67  ? 6.398   37.026 47.444 1 23.77  ? 48  ILE   A C     1 
ATOM   381  O O     . ILE   A 1 67  ? 5.82    38.118 47.414 1 23.65  ? 48  ILE   A O     1 
ATOM   382  C CB    . ILE   A 1 67  ? 6.794   35.562 45.371 1 21.56  ? 48  ILE   A CB    1 
ATOM   383  C CG1   . ILE   A 1 67  ? 7.616   35.475 44.078 1 21.81  ? 48  ILE   A CG1   1 
ATOM   384  C CG2   . ILE   A 1 67  ? 5.306   35.83  45.036 1 21.24  ? 48  ILE   A CG2   1 
ATOM   385  C CD1   . ILE   A 1 67  ? 7.521   34.103 43.295 1 24.29  ? 48  ILE   A CD1   1 
ATOM   386  N N     . PHE   A 1 68  ? 6.177   36.109 48.386 1 21.23  ? 49  PHE   A N     1 
ATOM   387  C CA    . PHE   A 1 68  ? 5.152   36.275 49.389 1 22.27  ? 49  PHE   A CA    1 
ATOM   388  C C     . PHE   A 1 68  ? 5.607   37.062 50.611 1 26.19  ? 49  PHE   A C     1 
ATOM   389  O O     . PHE   A 1 68  ? 4.808   37.816 51.155 1 25.46  ? 49  PHE   A O     1 
ATOM   390  C CB    . PHE   A 1 68  ? 4.551   34.904 49.759 1 24.36  ? 49  PHE   A CB    1 
ATOM   391  C CG    . PHE   A 1 68  ? 3.904   34.193 48.581 1 25.89  ? 49  PHE   A CG    1 
ATOM   392  C CD1   . PHE   A 1 68  ? 2.921   34.822 47.818 1 27.49  ? 49  PHE   A CD1   1 
ATOM   393  C CD2   . PHE   A 1 68  ? 4.291   32.903 48.224 1 27.79  ? 49  PHE   A CD2   1 
ATOM   394  C CE1   . PHE   A 1 68  ? 2.346   34.174 46.716 1 28     ? 49  PHE   A CE1   1 
ATOM   395  C CE2   . PHE   A 1 68  ? 3.693   32.249 47.138 1 29.65  ? 49  PHE   A CE2   1 
ATOM   396  C CZ    . PHE   A 1 68  ? 2.736   32.89  46.386 1 26.79  ? 49  PHE   A CZ    1 
ATOM   397  N N     . CYS   A 1 69  ? 6.863   36.928 51.025 1 24.85  ? 50  CYS   A N     1 
ATOM   398  C CA    . CYS   A 1 69  ? 7.335   37.646 52.214 1 26.59  ? 50  CYS   A CA    1 
ATOM   399  C C     . CYS   A 1 69  ? 8.079   38.951 51.892 1 30.09  ? 50  CYS   A C     1 
ATOM   400  O O     . CYS   A 1 69  ? 7.802   39.963 52.534 1 30.1   ? 50  CYS   A O     1 
ATOM   401  C CB    . CYS   A 1 69  ? 8.154   36.731 53.12  1 28.06  ? 50  CYS   A CB    1 
ATOM   402  S SG    . CYS   A 1 69  ? 7.277   35.229 53.636 1 32.55  ? 50  CYS   A SG    1 
ATOM   403  N N     . LEU   A 1 70  ? 8.984   38.948 50.899 1 26.07  ? 51  LEU   A N     1 
ATOM   404  C CA    . LEU   A 1 70  ? 9.75    40.146 50.531 1 26.39  ? 51  LEU   A CA    1 
ATOM   405  C C     . LEU   A 1 70  ? 8.961   41.121 49.656 1 30.08  ? 51  LEU   A C     1 
ATOM   406  O O     . LEU   A 1 70  ? 8.967   42.327 49.922 1 28.48  ? 51  LEU   A O     1 
ATOM   407  C CB    . LEU   A 1 70  ? 11.094  39.765 49.886 1 26.99  ? 51  LEU   A CB    1 
ATOM   408  C CG    . LEU   A 1 70  ? 12.322  39.53  50.776 1 32.69  ? 51  LEU   A CG    1 
ATOM   409  C CD1   . LEU   A 1 70  ? 11.971  39.229 52.227 1 33.51  ? 51  LEU   A CD1   1 
ATOM   410  C CD2   . LEU   A 1 70  ? 13.23   38.475 50.178 1 34.39  ? 51  LEU   A CD2   1 
ATOM   411  N N     . ASP   A 1 71  ? 8.28    40.605 48.607 1 27.81  ? 52  ASP   A N     1 
ATOM   412  C CA    . ASP   A 1 71  ? 7.441   41.424 47.733 1 27.29  ? 52  ASP   A CA    1 
ATOM   413  C C     . ASP   A 1 71  ? 6.07    41.551 48.422 1 33.5   ? 52  ASP   A C     1 
ATOM   414  O O     . ASP   A 1 71  ? 5.836   40.937 49.476 1 33.08  ? 52  ASP   A O     1 
ATOM   415  C CB    . ASP   A 1 71  ? 7.324   40.82  46.312 1 28.19  ? 52  ASP   A CB    1 
ATOM   416  C CG    . ASP   A 1 71  ? 8.631   40.52  45.588 1 37.12  ? 52  ASP   A CG    1 
ATOM   417  O OD1   . ASP   A 1 71  ? 9.607   41.275 45.779 1 37.29  ? 52  ASP   A OD1   1 
ATOM   418  O OD2   . ASP   A 1 71  ? 8.659   39.564 44.786 1 42.82  ? 52  ASP   A OD2   1 
ATOM   419  N N     . GLY   A 1 72  ? 5.199   42.372 47.854 1 32.57  ? 53  GLY   A N     1 
ATOM   420  C CA    . GLY   A 1 72  ? 3.868   42.613 48.406 1 32.78  ? 53  GLY   A CA    1 
ATOM   421  C C     . GLY   A 1 72  ? 2.766   41.686 47.932 1 36.66  ? 53  GLY   A C     1 
ATOM   422  O O     . GLY   A 1 72  ? 1.602   42.105 47.897 1 38.41  ? 53  GLY   A O     1 
ATOM   423  N N     . VAL   A 1 73  ? 3.099   40.421 47.569 1 30.42  ? 54  VAL   A N     1 
ATOM   424  C CA    . VAL   A 1 73  ? 2.081   39.467 47.114 1 28.68  ? 54  VAL   A CA    1 
ATOM   425  C C     . VAL   A 1 73  ? 1.349   38.928 48.34  1 30.55  ? 54  VAL   A C     1 
ATOM   426  O O     . VAL   A 1 73  ? 1.88    38.118 49.117 1 29.9   ? 54  VAL   A O     1 
ATOM   427  C CB    . VAL   A 1 73  ? 2.579   38.383 46.128 1 32.51  ? 54  VAL   A CB    1 
ATOM   428  C CG1   . VAL   A 1 73  ? 1.404   37.574 45.577 1 32.05  ? 54  VAL   A CG1   1 
ATOM   429  C CG2   . VAL   A 1 73  ? 3.358   39.019 44.973 1 32.16  ? 54  VAL   A CG2   1 
ATOM   430  N N     . LYS   A 1 74  ? 0.158   39.487 48.551 1 24.95  ? 55  LYS   A N     1 
ATOM   431  C CA    . LYS   A 1 74  ? -0.707  39.251 49.708 1 24.28  ? 55  LYS   A CA    1 
ATOM   432  C C     . LYS   A 1 74  ? -2.17   39.435 49.326 1 26.74  ? 55  LYS   A C     1 
ATOM   433  O O     . LYS   A 1 74  ? -2.478  39.946 48.245 1 26.65  ? 55  LYS   A O     1 
ATOM   434  C CB    . LYS   A 1 74  ? -0.333  40.227 50.853 1 26.12  ? 55  LYS   A CB    1 
ATOM   435  C CG    . LYS   A 1 74  ? -0.503  41.706 50.505 1 33.36  ? 55  LYS   A CG    1 
ATOM   436  C CD    . LYS   A 1 74  ? -0.32   42.614 51.712 1 42.03  ? 55  LYS   A CD    1 
ATOM   437  C CE    . LYS   A 1 74  ? -0.726  44.042 51.414 1 49.05  ? 55  LYS   A CE    1 
ATOM   438  N NZ    . LYS   A 1 74  ? 0.396   44.849 50.869 1 51.46  ? 55  LYS   A NZ    1 
ATOM   439  N N     . GLY   A 1 75  ? -3.054  39.057 50.232 1 22.49  ? 56  GLY   A N     1 
ATOM   440  C CA    . GLY   A 1 75  ? -4.484  39.227 50.033 1 21.6   ? 56  GLY   A CA    1 
ATOM   441  C C     . GLY   A 1 75  ? -5.315  38.33  50.908 1 24.87  ? 56  GLY   A C     1 
ATOM   442  O O     . GLY   A 1 75  ? -4.806  37.674 51.825 1 24.12  ? 56  GLY   A O     1 
ATOM   443  N N     . ASP   A 1 76  ? -6.61   38.305 50.626 1 22.78  ? 57  ASP   A N     1 
ATOM   444  C CA    . ASP   A 1 76  ? -7.536  37.466 51.365 1 22.5   ? 57  ASP   A CA    1 
ATOM   445  C C     . ASP   A 1 76  ? -7.49   36.048 50.824 1 25.96  ? 57  ASP   A C     1 
ATOM   446  O O     . ASP   A 1 76  ? -7.554  35.103 51.602 1 26.39  ? 57  ASP   A O     1 
ATOM   447  C CB    . ASP   A 1 76  ? -8.953  38.039 51.267 1 24.89  ? 57  ASP   A CB    1 
ATOM   448  C CG    . ASP   A 1 76  ? -9.209  39.204 52.202 1 34.75  ? 57  ASP   A CG    1 
ATOM   449  O OD1   . ASP   A 1 76  ? -8.469  39.339 53.201 1 34.98  ? 57  ASP   A OD1   1 
ATOM   450  O OD2   . ASP   A 1 76  ? -10.171 39.958 51.953 1 45.03  ? 57  ASP   A OD2   1 
ATOM   451  N N     . LEU   A 1 77  ? -7.335  35.899 49.491 1 22.08  ? 58  LEU   A N     1 
ATOM   452  C CA    . LEU   A 1 77  ? -7.344  34.587 48.851 1 20.37  ? 58  LEU   A CA    1 
ATOM   453  C C     . LEU   A 1 77  ? -6.23   34.324 47.845 1 22.57  ? 58  LEU   A C     1 
ATOM   454  O O     . LEU   A 1 77  ? -6.016  35.118 46.927 1 21.11  ? 58  LEU   A O     1 
ATOM   455  C CB    . LEU   A 1 77  ? -8.727  34.382 48.172 1 20.25  ? 58  LEU   A CB    1 
ATOM   456  C CG    . LEU   A 1 77  ? -8.998  33.04  47.465 1 24.66  ? 58  LEU   A CG    1 
ATOM   457  C CD1   . LEU   A 1 77  ? -8.989  31.877 48.445 1 24.64  ? 58  LEU   A CD1   1 
ATOM   458  C CD2   . LEU   A 1 77  ? -10.31  33.077 46.709 1 26.81  ? 58  LEU   A CD2   1 
ATOM   459  N N     . LEU   A 1 78  ? -5.602  33.137 47.974 1 20.26  ? 59  LEU   A N     1 
ATOM   460  C CA    . LEU   A 1 78  ? -4.63   32.562 47.036 1 19.89  ? 59  LEU   A CA    1 
ATOM   461  C C     . LEU   A 1 78  ? -5.191  31.201 46.564 1 22.98  ? 59  LEU   A C     1 
ATOM   462  O O     . LEU   A 1 78  ? -5.569  30.37  47.394 1 22.6   ? 59  LEU   A O     1 
ATOM   463  C CB    . LEU   A 1 78  ? -3.235  32.347 47.681 1 19.83  ? 59  LEU   A CB    1 
ATOM   464  C CG    . LEU   A 1 78  ? -2.203  31.605 46.803 1 24.58  ? 59  LEU   A CG    1 
ATOM   465  C CD1   . LEU   A 1 78  ? -0.962  32.407 46.61  1 25.42  ? 59  LEU   A CD1   1 
ATOM   466  C CD2   . LEU   A 1 78  ? -1.835  30.274 47.391 1 26.34  ? 59  LEU   A CD2   1 
ATOM   467  N N     . ILE   A 1 79  ? -5.228  30.973 45.251 1 18.07  ? 60  ILE   A N     1 
ATOM   468  C CA    . ILE   A 1 79  ? -5.647  29.684 44.708 1 17.66  ? 60  ILE   A CA    1 
ATOM   469  C C     . ILE   A 1 79  ? -4.386  28.997 44.159 1 22.31  ? 60  ILE   A C     1 
ATOM   470  O O     . ILE   A 1 79  ? -3.713  29.556 43.288 1 22.05  ? 60  ILE   A O     1 
ATOM   471  C CB    . ILE   A 1 79  ? -6.777  29.784 43.631 1 19.99  ? 60  ILE   A CB    1 
ATOM   472  C CG1   . ILE   A 1 79  ? -8.088  30.368 44.217 1 20.43  ? 60  ILE   A CG1   1 
ATOM   473  C CG2   . ILE   A 1 79  ? -7.054  28.394 42.993 1 19.73  ? 60  ILE   A CG2   1 
ATOM   474  C CD1   . ILE   A 1 79  ? -9.119  30.879 43.12  1 20.97  ? 60  ILE   A CD1   1 
ATOM   475  N N     . ASP   A 1 80  ? -4.07   27.795 44.674 1 18.08  ? 61  ASP   A N     1 
ATOM   476  C CA    . ASP   A 1 80  ? -2.954  27.005 44.16  1 17.48  ? 61  ASP   A CA    1 
ATOM   477  C C     . ASP   A 1 80  ? -3.518  26.021 43.138 1 21.66  ? 61  ASP   A C     1 
ATOM   478  O O     . ASP   A 1 80  ? -4.381  25.203 43.472 1 22.29  ? 61  ASP   A O     1 
ATOM   479  C CB    . ASP   A 1 80  ? -2.195  26.271 45.27  1 18.44  ? 61  ASP   A CB    1 
ATOM   480  C CG    . ASP   A 1 80  ? -0.961  25.527 44.772 1 21.48  ? 61  ASP   A CG    1 
ATOM   481  O OD1   . ASP   A 1 80  ? -0.308  26.02  43.821 1 16.84  ? 61  ASP   A OD1   1 
ATOM   482  O OD2   . ASP   A 1 80  ? -0.637  24.476 45.346 1 26.66  ? 61  ASP   A OD2   1 
ATOM   483  N N     . ILE   A 1 81  ? -3.1    26.178 41.87  1 16.76  ? 62  ILE   A N     1 
ATOM   484  C CA    . ILE   A 1 81  ? -3.539  25.364 40.729 1 14.64  ? 62  ILE   A CA    1 
ATOM   485  C C     . ILE   A 1 81  ? -2.616  24.153 40.492 1 18.99  ? 62  ILE   A C     1 
ATOM   486  O O     . ILE   A 1 81  ? -1.404  24.326 40.284 1 17.59  ? 62  ILE   A O     1 
ATOM   487  C CB    . ILE   A 1 81  ? -3.639  26.292 39.491 1 17.36  ? 62  ILE   A CB    1 
ATOM   488  C CG1   . ILE   A 1 81  ? -4.734  27.388 39.678 1 17.04  ? 62  ILE   A CG1   1 
ATOM   489  C CG2   . ILE   A 1 81  ? -3.806  25.517 38.164 1 17.13  ? 62  ILE   A CG2   1 
ATOM   490  C CD1   . ILE   A 1 81  ? -6.194  26.933 39.716 1 19.15  ? 62  ILE   A CD1   1 
ATOM   491  N N     . GLY   A 1 82  ? -3.187  22.946 40.496 1 16.48  ? 63  GLY   A N     1 
ATOM   492  C CA    . GLY   A 1 82  ? -2.411  21.723 40.256 1 15.67  ? 63  GLY   A CA    1 
ATOM   493  C C     . GLY   A 1 82  ? -1.387  21.423 41.338 1 17.57  ? 63  GLY   A C     1 
ATOM   494  O O     . GLY   A 1 82  ? -0.233  21.074 41.048 1 14.61  ? 63  GLY   A O     1 
ATOM   495  N N     . SER   A 1 83  ? -1.828  21.581 42.605 1 14.47  ? 64  SER   A N     1 
ATOM   496  C CA    . SER   A 1 83  ? -1.1    21.361 43.862 1 13.54  ? 64  SER   A CA    1 
ATOM   497  C C     . SER   A 1 83  ? -0.403  20.006 43.928 1 18.28  ? 64  SER   A C     1 
ATOM   498  O O     . SER   A 1 83  ? 0.611   19.874 44.624 1 17.11  ? 64  SER   A O     1 
ATOM   499  C CB    . SER   A 1 83  ? -2.077  21.439 45.039 1 15.09  ? 64  SER   A CB    1 
ATOM   500  O OG    . SER   A 1 83  ? -2.808  22.657 45.052 1 18.68  ? 64  SER   A OG    1 
ATOM   501  N N     . GLY   A 1 84  ? -0.989  19.004 43.267 1 15.46  ? 65  GLY   A N     1 
ATOM   502  C CA    . GLY   A 1 84  ? -0.542  17.623 43.351 1 16     ? 65  GLY   A CA    1 
ATOM   503  C C     . GLY   A 1 84  ? -0.643  17.201 44.799 1 18.34  ? 65  GLY   A C     1 
ATOM   504  O O     . GLY   A 1 84  ? -1.531  17.695 45.503 1 16.6   ? 65  GLY   A O     1 
ATOM   505  N N     . PRO   A 1 85  ? 0.292   16.377 45.322 1 16.16  ? 66  PRO   A N     1 
ATOM   506  C CA    . PRO   A 1 85  ? 0.234   16.037 46.748 1 15.35  ? 66  PRO   A CA    1 
ATOM   507  C C     . PRO   A 1 85  ? 1.184   16.923 47.59  1 18.34  ? 66  PRO   A C     1 
ATOM   508  O O     . PRO   A 1 85  ? 1.452   16.61  48.749 1 16.99  ? 66  PRO   A O     1 
ATOM   509  C CB    . PRO   A 1 85  ? 0.684   14.569 46.734 1 17.16  ? 66  PRO   A CB    1 
ATOM   510  C CG    . PRO   A 1 85  ? 1.68    14.501 45.574 1 21.06  ? 66  PRO   A CG    1 
ATOM   511  C CD    . PRO   A 1 85  ? 1.416   15.672 44.66  1 17.58  ? 66  PRO   A CD    1 
ATOM   512  N N     . THR   A 1 86  ? 1.709   18.022 47.017 1 15.21  ? 67  THR   A N     1 
ATOM   513  C CA    . THR   A 1 86  ? 2.719   18.826 47.717 1 15.83  ? 67  THR   A CA    1 
ATOM   514  C C     . THR   A 1 86  ? 2.188   20.035 48.469 1 20.74  ? 67  THR   A C     1 
ATOM   515  O O     . THR   A 1 86  ? 1.192   20.651 48.066 1 21.47  ? 67  THR   A O     1 
ATOM   516  C CB    . THR   A 1 86  ? 3.855   19.251 46.752 1 19.76  ? 67  THR   A CB    1 
ATOM   517  O OG1   . THR   A 1 86  ? 3.37    20.236 45.854 1 18.74  ? 67  THR   A OG1   1 
ATOM   518  C CG2   . THR   A 1 86  ? 4.428   18.088 45.958 1 16.48  ? 67  THR   A CG2   1 
ATOM   519  N N     . ILE   A 1 87  ? 2.926   20.43  49.524 1 19.14  ? 68  ILE   A N     1 
ATOM   520  C CA    . ILE   A 1 87  ? 2.612   21.629 50.313 1 19.15  ? 68  ILE   A CA    1 
ATOM   521  C C     . ILE   A 1 87  ? 3.786   22.636 50.351 1 23.19  ? 68  ILE   A C     1 
ATOM   522  O O     . ILE   A 1 87  ? 3.597   23.741 50.868 1 22.52  ? 68  ILE   A O     1 
ATOM   523  C CB    . ILE   A 1 87  ? 2.064   21.324 51.742 1 21.64  ? 68  ILE   A CB    1 
ATOM   524  C CG1   . ILE   A 1 87  ? 3.067   20.542 52.61  1 21.55  ? 68  ILE   A CG1   1 
ATOM   525  C CG2   . ILE   A 1 87  ? 0.713   20.64  51.687 1 21.93  ? 68  ILE   A CG2   1 
ATOM   526  C CD1   . ILE   A 1 87  ? 3.966   21.388 53.505 1 26.96  ? 68  ILE   A CD1   1 
ATOM   527  N N     . TYR   A 1 88  ? 4.98    22.261 49.825 1 19.57  ? 69  TYR   A N     1 
ATOM   528  C CA    . TYR   A 1 88  ? 6.171   23.132 49.822 1 18.39  ? 69  TYR   A CA    1 
ATOM   529  C C     . TYR   A 1 88  ? 5.896   24.534 49.239 1 20.64  ? 69  TYR   A C     1 
ATOM   530  O O     . TYR   A 1 88  ? 6.475   25.5   49.707 1 19.45  ? 69  TYR   A O     1 
ATOM   531  C CB    . TYR   A 1 88  ? 7.37    22.469 49.098 1 18.61  ? 69  TYR   A CB    1 
ATOM   532  C CG    . TYR   A 1 88  ? 7.308   22.585 47.585 1 18.65  ? 69  TYR   A CG    1 
ATOM   533  C CD1   . TYR   A 1 88  ? 6.614   21.651 46.823 1 20.47  ? 69  TYR   A CD1   1 
ATOM   534  C CD2   . TYR   A 1 88  ? 7.894   23.663 46.923 1 18.71  ? 69  TYR   A CD2   1 
ATOM   535  C CE1   . TYR   A 1 88  ? 6.504   21.786 45.439 1 20.87  ? 69  TYR   A CE1   1 
ATOM   536  C CE2   . TYR   A 1 88  ? 7.79    23.808 45.542 1 19.06  ? 69  TYR   A CE2   1 
ATOM   537  C CZ    . TYR   A 1 88  ? 7.109   22.855 44.802 1 21.12  ? 69  TYR   A CZ    1 
ATOM   538  O OH    . TYR   A 1 88  ? 7.031   22.977 43.44  1 18.45  ? 69  TYR   A OH    1 
ATOM   539  N N     . GLN   A 1 89  ? 5.042   24.621 48.194 1 16.85  ? 70  GLN   A N     1 
ATOM   540  C CA    . GLN   A 1 89  ? 4.719   25.865 47.492 1 15.57  ? 70  GLN   A CA    1 
ATOM   541  C C     . GLN   A 1 89  ? 3.793   26.794 48.288 1 19.09  ? 70  GLN   A C     1 
ATOM   542  O O     . GLN   A 1 89  ? 3.497   27.896 47.827 1 18.84  ? 70  GLN   A O     1 
ATOM   543  C CB    . GLN   A 1 89  ? 4.161   25.582 46.078 1 16.22  ? 70  GLN   A CB    1 
ATOM   544  C CG    . GLN   A 1 89  ? 2.744   24.969 46.015 1 15.92  ? 70  GLN   A CG    1 
ATOM   545  C CD    . GLN   A 1 89  ? 2.674   23.461 46.179 1 20.74  ? 70  GLN   A CD    1 
ATOM   546  O OE1   . GLN   A 1 89  ? 3.589   22.8   46.678 1 17.08  ? 70  GLN   A OE1   1 
ATOM   547  N NE2   . GLN   A 1 89  ? 1.541   22.887 45.831 1 15.69  ? 70  GLN   A NE2   1 
ATOM   548  N N     . LEU   A 1 90  ? 3.354   26.363 49.476 1 15.87  ? 71  LEU   A N     1 
ATOM   549  C CA    . LEU   A 1 90  ? 2.425   27.13  50.303 1 16.19  ? 71  LEU   A CA    1 
ATOM   550  C C     . LEU   A 1 90  ? 2.999   27.635 51.622 1 22.42  ? 71  LEU   A C     1 
ATOM   551  O O     . LEU   A 1 90  ? 2.377   28.49  52.264 1 22.45  ? 71  LEU   A O     1 
ATOM   552  C CB    . LEU   A 1 90  ? 1.163   26.296 50.571 1 16.02  ? 71  LEU   A CB    1 
ATOM   553  C CG    . LEU   A 1 90  ? 0.631   25.433 49.424 1 19.93  ? 71  LEU   A CG    1 
ATOM   554  C CD1   . LEU   A 1 90  ? -0.33   24.364 49.954 1 19.37  ? 71  LEU   A CD1   1 
ATOM   555  C CD2   . LEU   A 1 90  ? 0.007   26.289 48.327 1 19.07  ? 71  LEU   A CD2   1 
ATOM   556  N N     . LEU   A 1 91  ? 4.168   27.118 52.023 1 20.14  ? 72  LEU   A N     1 
ATOM   557  C CA    . LEU   A 1 91  ? 4.797   27.44  53.299 1 20.4   ? 72  LEU   A CA    1 
ATOM   558  C C     . LEU   A 1 91  ? 5.052   28.943 53.495 1 25.29  ? 72  LEU   A C     1 
ATOM   559  O O     . LEU   A 1 91  ? 4.671   29.45  54.544 1 25.24  ? 72  LEU   A O     1 
ATOM   560  C CB    . LEU   A 1 91  ? 6.048   26.587 53.544 1 20.18  ? 72  LEU   A CB    1 
ATOM   561  C CG    . LEU   A 1 91  ? 5.728   25.074 53.719 1 24.45  ? 72  LEU   A CG    1 
ATOM   562  C CD1   . LEU   A 1 91  ? 6.928   24.205 53.422 1 24.14  ? 72  LEU   A CD1   1 
ATOM   563  C CD2   . LEU   A 1 91  ? 5.164   24.767 55.111 1 26.43  ? 72  LEU   A CD2   1 
ATOM   564  N N     . SER   A 1 92  ? 5.563   29.673 52.481 1 21.7   ? 73  SER   A N     1 
ATOM   565  C CA    . SER   A 1 92  ? 5.732   31.134 52.598 1 20.66  ? 73  SER   A CA    1 
ATOM   566  C C     . SER   A 1 92  ? 4.415   31.9   52.356 1 23.86  ? 73  SER   A C     1 
ATOM   567  O O     . SER   A 1 92  ? 4.176   32.942 52.984 1 22.65  ? 73  SER   A O     1 
ATOM   568  C CB    . SER   A 1 92  ? 6.814   31.64  51.653 1 23.14  ? 73  SER   A CB    1 
ATOM   569  O OG    . SER   A 1 92  ? 8.091   31.254 52.131 1 30.56  ? 73  SER   A OG    1 
ATOM   570  N N     . ALA   A 1 93  ? 3.561   31.373 51.457 1 20.87  ? 74  ALA   A N     1 
ATOM   571  C CA    . ALA   A 1 93  ? 2.263   31.946 51.102 1 21.1   ? 74  ALA   A CA    1 
ATOM   572  C C     . ALA   A 1 93  ? 1.293   32.108 52.283 1 25.36  ? 74  ALA   A C     1 
ATOM   573  O O     . ALA   A 1 93  ? 0.501   33.056 52.286 1 25.03  ? 74  ALA   A O     1 
ATOM   574  C CB    . ALA   A 1 93  ? 1.609   31.11  50.012 1 21.96  ? 74  ALA   A CB    1 
ATOM   575  N N     . CYS   A 1 94  ? 1.349   31.197 53.281 1 22.17  ? 75  CYS   A N     1 
ATOM   576  C CA    . CYS   A 1 94  ? 0.423   31.231 54.419 1 22.67  ? 75  CYS   A CA    1 
ATOM   577  C C     . CYS   A 1 94  ? 0.689   32.408 55.382 1 27.89  ? 75  CYS   A C     1 
ATOM   578  O O     . CYS   A 1 94  ? -0.141  32.702 56.247 1 27.57  ? 75  CYS   A O     1 
ATOM   579  C CB    . CYS   A 1 94  ? 0.364   29.887 55.145 1 22.74  ? 75  CYS   A CB    1 
ATOM   580  S SG    . CYS   A 1 94  ? 1.818   29.503 56.147 1 26.55  ? 75  CYS   A SG    1 
ATOM   581  N N     . GLU   A 1 95  ? 1.816   33.105 55.177 1 24.97  ? 76  GLU   A N     1 
ATOM   582  C CA    . GLU   A 1 95  ? 2.212   34.287 55.935 1 25.1   ? 76  GLU   A CA    1 
ATOM   583  C C     . GLU   A 1 95  ? 1.552   35.516 55.357 1 28.92  ? 76  GLU   A C     1 
ATOM   584  O O     . GLU   A 1 95  ? 1.477   36.546 56.035 1 29.32  ? 76  GLU   A O     1 
ATOM   585  C CB    . GLU   A 1 95  ? 3.747   34.471 55.887 1 26.24  ? 76  GLU   A CB    1 
ATOM   586  C CG    . GLU   A 1 95  ? 4.549   33.345 56.518 1 32.82  ? 76  GLU   A CG    1 
ATOM   587  C CD    . GLU   A 1 95  ? 4.23    33.077 57.977 1 49.88  ? 76  GLU   A CD    1 
ATOM   588  O OE1   . GLU   A 1 95  ? 4.146   34.048 58.762 1 50.07  ? 76  GLU   A OE1   1 
ATOM   589  O OE2   . GLU   A 1 95  ? 4.023   31.895 58.326 1 37.95  ? 76  GLU   A OE2   1 
ATOM   590  N N     . SER   A 1 96  ? 1.079   35.422 54.102 1 24.36  ? 77  SER   A N     1 
ATOM   591  C CA    . SER   A 1 96  ? 0.527   36.567 53.379 1 23     ? 77  SER   A CA    1 
ATOM   592  C C     . SER   A 1 96  ? -0.922  36.443 52.923 1 25.5   ? 77  SER   A C     1 
ATOM   593  O O     . SER   A 1 96  ? -1.502  37.452 52.504 1 24.84  ? 77  SER   A O     1 
ATOM   594  C CB    . SER   A 1 96  ? 1.418   36.894 52.187 1 23.88  ? 77  SER   A CB    1 
ATOM   595  O OG    . SER   A 1 96  ? 2.758   36.983 52.638 1 28.92  ? 77  SER   A OG    1 
ATOM   596  N N     . PHE   A 1 97  ? -1.518  35.244 52.999 1 21.77  ? 78  PHE   A N     1 
ATOM   597  C CA    . PHE   A 1 97  ? -2.911  35.088 52.583 1 21.33  ? 78  PHE   A CA    1 
ATOM   598  C C     . PHE   A 1 97  ? -3.773  34.547 53.702 1 26.53  ? 78  PHE   A C     1 
ATOM   599  O O     . PHE   A 1 97  ? -3.366  33.602 54.372 1 25.5   ? 78  PHE   A O     1 
ATOM   600  C CB    . PHE   A 1 97  ? -3.043  34.248 51.297 1 22.68  ? 78  PHE   A CB    1 
ATOM   601  C CG    . PHE   A 1 97  ? -2.464  34.919 50.075 1 22.95  ? 78  PHE   A CG    1 
ATOM   602  C CD1   . PHE   A 1 97  ? -1.112  34.793 49.765 1 24.9   ? 78  PHE   A CD1   1 
ATOM   603  C CD2   . PHE   A 1 97  ? -3.264  35.698 49.245 1 23.82  ? 78  PHE   A CD2   1 
ATOM   604  C CE1   . PHE   A 1 97  ? -0.567  35.446 48.659 1 24.69  ? 78  PHE   A CE1   1 
ATOM   605  C CE2   . PHE   A 1 97  ? -2.723  36.324 48.118 1 25.71  ? 78  PHE   A CE2   1 
ATOM   606  C CZ    . PHE   A 1 97  ? -1.377  36.2   47.84  1 23.68  ? 78  PHE   A CZ    1 
ATOM   607  N N     . LYS   A 1 98  ? -4.961  35.157 53.914 1 24.57  ? 79  LYS   A N     1 
ATOM   608  C CA    . LYS   A 1 98  ? -5.907  34.724 54.951 1 25.31  ? 79  LYS   A CA    1 
ATOM   609  C C     . LYS   A 1 98  ? -6.367  33.299 54.655 1 29.67  ? 79  LYS   A C     1 
ATOM   610  O O     . LYS   A 1 98  ? -6.504  32.495 55.574 1 30.11  ? 79  LYS   A O     1 
ATOM   611  C CB    . LYS   A 1 98  ? -7.136  35.66  55.015 1 28.11  ? 79  LYS   A CB    1 
ATOM   612  C CG    . LYS   A 1 98  ? -6.864  37.037 55.628 1 49.31  ? 79  LYS   A CG    1 
ATOM   613  C CD    . LYS   A 1 98  ? -6.878  37.037 57.169 1 62.13  ? 79  LYS   A CD    1 
ATOM   614  C CE    . LYS   A 1 98  ? -8.256  37.204 57.775 1 74.04  ? 79  LYS   A CE    1 
ATOM   615  N NZ    . LYS   A 1 98  ? -8.758  38.598 57.648 1 82.4   ? 79  LYS   A NZ    1 
ATOM   616  N N     . GLU   A 1 99  ? -6.605  32.995 53.364 1 26.27  ? 80  GLU   A N     1 
ATOM   617  C CA    . GLU   A 1 99  ? -7.057  31.687 52.916 1 26.07  ? 80  GLU   A CA    1 
ATOM   618  C C     . GLU   A 1 99  ? -6.312  31.229 51.667 1 28.38  ? 80  GLU   A C     1 
ATOM   619  O O     . GLU   A 1 99  ? -6.042  32.027 50.765 1 26.38  ? 80  GLU   A O     1 
ATOM   620  C CB    . GLU   A 1 99  ? -8.576  31.689 52.666 1 27.98  ? 80  GLU   A CB    1 
ATOM   621  C CG    . GLU   A 1 99  ? -9.402  31.678 53.95  1 44.05  ? 80  GLU   A CG    1 
ATOM   622  C CD    . GLU   A 1 99  ? -10.586 32.627 54.048 1 72.03  ? 80  GLU   A CD    1 
ATOM   623  O OE1   . GLU   A 1 99  ? -11.343 32.512 55.039 1 64.14  ? 80  GLU   A OE1   1 
ATOM   624  O OE2   . GLU   A 1 99  ? -10.749 33.495 53.158 1 72.68  ? 80  GLU   A OE2   1 
ATOM   625  N N     . ILE   A 1 100 ? -5.991  29.928 51.636 1 24.72  ? 81  ILE   A N     1 
ATOM   626  C CA    . ILE   A 1 100 ? -5.331  29.233 50.533 1 24.55  ? 81  ILE   A CA    1 
ATOM   627  C C     . ILE   A 1 100 ? -6.25   28.105 50.103 1 27.94  ? 81  ILE   A C     1 
ATOM   628  O O     . ILE   A 1 100 ? -6.597  27.254 50.92  1 27.93  ? 81  ILE   A O     1 
ATOM   629  C CB    . ILE   A 1 100 ? -3.919  28.695 50.945 1 27.21  ? 81  ILE   A CB    1 
ATOM   630  C CG1   . ILE   A 1 100 ? -2.929  29.851 51.18  1 26.94  ? 81  ILE   A CG1   1 
ATOM   631  C CG2   . ILE   A 1 100 ? -3.355  27.686 49.905 1 26.96  ? 81  ILE   A CG2   1 
ATOM   632  C CD1   . ILE   A 1 100 ? -1.743  29.476 51.974 1 32.82  ? 81  ILE   A CD1   1 
ATOM   633  N N     . VAL   A 1 101 ? -6.607  28.077 48.816 1 24.12  ? 82  VAL   A N     1 
ATOM   634  C CA    . VAL   A 1 101 ? -7.414  27.009 48.233 1 23.89  ? 82  VAL   A CA    1 
ATOM   635  C C     . VAL   A 1 101 ? -6.466  26.124 47.391 1 27.44  ? 82  VAL   A C     1 
ATOM   636  O O     . VAL   A 1 101 ? -5.792  26.631 46.49  1 26.5   ? 82  VAL   A O     1 
ATOM   637  C CB    . VAL   A 1 101 ? -8.631  27.567 47.44  1 27.64  ? 82  VAL   A CB    1 
ATOM   638  C CG1   . VAL   A 1 101 ? -9.228  26.521 46.501 1 27.44  ? 82  VAL   A CG1   1 
ATOM   639  C CG2   . VAL   A 1 101 ? -9.699  28.102 48.395 1 27.58  ? 82  VAL   A CG2   1 
ATOM   640  N N     . VAL   A 1 102 ? -6.375  24.826 47.739 1 23.28  ? 83  VAL   A N     1 
ATOM   641  C CA    . VAL   A 1 102 ? -5.541  23.841 47.031 1 23.13  ? 83  VAL   A CA    1 
ATOM   642  C C     . VAL   A 1 102 ? -6.384  23.07  46.009 1 26.46  ? 83  VAL   A C     1 
ATOM   643  O O     . VAL   A 1 102 ? -7.523  22.712 46.299 1 26.04  ? 83  VAL   A O     1 
ATOM   644  C CB    . VAL   A 1 102 ? -4.701  22.91  47.949 1 26.53  ? 83  VAL   A CB    1 
ATOM   645  C CG1   . VAL   A 1 102 ? -3.715  23.716 48.781 1 26.09  ? 83  VAL   A CG1   1 
ATOM   646  C CG2   . VAL   A 1 102 ? -5.583  22.035 48.844 1 26.48  ? 83  VAL   A CG2   1 
ATOM   647  N N     . THR   A 1 103 ? -5.855  22.886 44.799 1 21.51  ? 84  THR   A N     1 
ATOM   648  C CA    . THR   A 1 103 ? -6.596  22.251 43.712 1 20.81  ? 84  THR   A CA    1 
ATOM   649  C C     . THR   A 1 103 ? -5.749  21.256 42.918 1 22.37  ? 84  THR   A C     1 
ATOM   650  O O     . THR   A 1 103 ? -4.552  21.455 42.775 1 22     ? 84  THR   A O     1 
ATOM   651  C CB    . THR   A 1 103 ? -7.191  23.329 42.753 1 28.82  ? 84  THR   A CB    1 
ATOM   652  O OG1   . THR   A 1 103 ? -6.179  23.798 41.852 1 26.28  ? 84  THR   A OG1   1 
ATOM   653  C CG2   . THR   A 1 103 ? -7.853  24.512 43.474 1 26.26  ? 84  THR   A CG2   1 
ATOM   654  N N     . ASP   A 1 104 ? -6.378  20.225 42.349 1 19.02  ? 85  ASP   A N     1 
ATOM   655  C CA    . ASP   A 1 104 ? -5.702  19.252 41.483 1 18.01  ? 85  ASP   A CA    1 
ATOM   656  C C     . ASP   A 1 104 ? -6.692  18.452 40.641 1 21.42  ? 85  ASP   A C     1 
ATOM   657  O O     . ASP   A 1 104 ? -7.841  18.273 41.05  1 19.37  ? 85  ASP   A O     1 
ATOM   658  C CB    . ASP   A 1 104 ? -4.793  18.293 42.265 1 19.02  ? 85  ASP   A CB    1 
ATOM   659  C CG    . ASP   A 1 104 ? -3.655  17.779 41.414 1 23.04  ? 85  ASP   A CG    1 
ATOM   660  O OD1   . ASP   A 1 104 ? -2.807  18.591 41.016 1 24.42  ? 85  ASP   A OD1   1 
ATOM   661  O OD2   . ASP   A 1 104 ? -3.64   16.569 41.105 1 25.93  ? 85  ASP   A OD2   1 
ATOM   662  N N     . TYR   A 1 105 ? -6.24   17.955 39.472 1 18.24  ? 86  TYR   A N     1 
ATOM   663  C CA    . TYR   A 1 105 ? -7.075  17.109 38.638 1 18.1   ? 86  TYR   A CA    1 
ATOM   664  C C     . TYR   A 1 105 ? -7.269  15.734 39.307 1 24.2   ? 86  TYR   A C     1 
ATOM   665  O O     . TYR   A 1 105 ? -8.358  15.169 39.214 1 23.58  ? 86  TYR   A O     1 
ATOM   666  C CB    . TYR   A 1 105 ? -6.508  16.954 37.223 1 18.71  ? 86  TYR   A CB    1 
ATOM   667  C CG    . TYR   A 1 105 ? -7.487  16.252 36.304 1 21.36  ? 86  TYR   A CG    1 
ATOM   668  C CD1   . TYR   A 1 105 ? -8.649  16.892 35.872 1 23.6   ? 86  TYR   A CD1   1 
ATOM   669  C CD2   . TYR   A 1 105 ? -7.296  14.923 35.931 1 21.28  ? 86  TYR   A CD2   1 
ATOM   670  C CE1   . TYR   A 1 105 ? -9.583  16.236 35.073 1 25.49  ? 86  TYR   A CE1   1 
ATOM   671  C CE2   . TYR   A 1 105 ? -8.229  14.253 35.138 1 22.15  ? 86  TYR   A CE2   1 
ATOM   672  C CZ    . TYR   A 1 105 ? -9.371  14.915 34.713 1 28.87  ? 86  TYR   A CZ    1 
ATOM   673  O OH    . TYR   A 1 105 ? -10.277 14.291 33.896 1 27.79  ? 86  TYR   A OH    1 
ATOM   674  N N     . SER   A 1 106 ? -6.223  15.223 39.998 1 21.2   ? 87  SER   A N     1 
ATOM   675  C CA    . SER   A 1 106 ? -6.239  13.922 40.674 1 21.12  ? 87  SER   A CA    1 
ATOM   676  C C     . SER   A 1 106 ? -6.834  13.965 42.078 1 24.03  ? 87  SER   A C     1 
ATOM   677  O O     . SER   A 1 106 ? -6.33   14.688 42.942 1 21.31  ? 87  SER   A O     1 
ATOM   678  C CB    . SER   A 1 106 ? -4.839  13.321 40.72  1 24.72  ? 87  SER   A CB    1 
ATOM   679  O OG    . SER   A 1 106 ? -4.812  12.213 41.607 1 29.68  ? 87  SER   A OG    1 
ATOM   680  N N     . ASP   A 1 107 ? -7.884  13.138 42.309 1 23.11  ? 88  ASP   A N     1 
ATOM   681  C CA    . ASP   A 1 107 ? -8.574  12.979 43.604 1 23.59  ? 88  ASP   A CA    1 
ATOM   682  C C     . ASP   A 1 107 ? -7.639  12.273 44.573 1 27.13  ? 88  ASP   A C     1 
ATOM   683  O O     . ASP   A 1 107 ? -7.64   12.6   45.757 1 27.45  ? 88  ASP   A O     1 
ATOM   684  C CB    . ASP   A 1 107 ? -9.879  12.172 43.463 1 25.9   ? 88  ASP   A CB    1 
ATOM   685  C CG    . ASP   A 1 107 ? -10.782 12.647 42.341 1 39.44  ? 88  ASP   A CG    1 
ATOM   686  O OD1   . ASP   A 1 107 ? -11.524 13.635 42.552 1 39.65  ? 88  ASP   A OD1   1 
ATOM   687  O OD2   . ASP   A 1 107 ? -10.724 12.049 41.241 1 45.59  ? 88  ASP   A OD2   1 
ATOM   688  N N     . GLN   A 1 108 ? -6.823  11.323 44.051 1 21.95  ? 89  GLN   A N     1 
ATOM   689  C CA    . GLN   A 1 108 ? -5.807  10.572 44.788 1 21.44  ? 89  GLN   A CA    1 
ATOM   690  C C     . GLN   A 1 108 ? -4.773  11.566 45.362 1 23.76  ? 89  GLN   A C     1 
ATOM   691  O O     . GLN   A 1 108 ? -4.391  11.431 46.519 1 22.17  ? 89  GLN   A O     1 
ATOM   692  C CB    . GLN   A 1 108 ? -5.144  9.536  43.852 1 23.42  ? 89  GLN   A CB    1 
ATOM   693  C CG    . GLN   A 1 108 ? -4.477  8.363  44.578 1 43.37  ? 89  GLN   A CG    1 
ATOM   694  C CD    . GLN   A 1 108 ? -3.935  7.257  43.688 1 53.33  ? 89  GLN   A CD    1 
ATOM   695  O OE1   . GLN   A 1 108 ? -3.823  7.37   42.456 1 39.84  ? 89  GLN   A OE1   1 
ATOM   696  N NE2   . GLN   A 1 108 ? -3.561  6.153  44.317 1 51.7   ? 89  GLN   A NE2   1 
ATOM   697  N N     . ASN   A 1 109 ? -4.388  12.606 44.573 1 20.7   ? 90  ASN   A N     1 
ATOM   698  C CA    . ASN   A 1 109 ? -3.468  13.67  45.011 1 21.08  ? 90  ASN   A CA    1 
ATOM   699  C C     . ASN   A 1 109 ? -4.071  14.508 46.115 1 25.06  ? 90  ASN   A C     1 
ATOM   700  O O     . ASN   A 1 109 ? -3.397  14.79  47.1   1 24.43  ? 90  ASN   A O     1 
ATOM   701  C CB    . ASN   A 1 109 ? -3.012  14.566 43.837 1 21.1   ? 90  ASN   A CB    1 
ATOM   702  C CG    . ASN   A 1 109 ? -1.892  13.951 43.045 1 25.32  ? 90  ASN   A CG    1 
ATOM   703  O OD1   . ASN   A 1 109 ? -1.215  13.039 43.511 1 17     ? 90  ASN   A OD1   1 
ATOM   704  N ND2   . ASN   A 1 109 ? -1.676  14.417 41.821 1 20.35  ? 90  ASN   A ND2   1 
ATOM   705  N N     . LEU   A 1 110 ? -5.35   14.874 45.973 1 22.97  ? 91  LEU   A N     1 
ATOM   706  C CA    . LEU   A 1 110 ? -6.058  15.665 46.979 1 22.91  ? 91  LEU   A CA    1 
ATOM   707  C C     . LEU   A 1 110 ? -6.225  14.899 48.312 1 26.57  ? 91  LEU   A C     1 
ATOM   708  O O     . LEU   A 1 110 ? -6.175  15.512 49.38  1 25.61  ? 91  LEU   A O     1 
ATOM   709  C CB    . LEU   A 1 110 ? -7.387  16.171 46.437 1 23.05  ? 91  LEU   A CB    1 
ATOM   710  C CG    . LEU   A 1 110 ? -7.294  17.094 45.205 1 28.34  ? 91  LEU   A CG    1 
ATOM   711  C CD1   . LEU   A 1 110 ? -8.666  17.361 44.622 1 28.99  ? 91  LEU   A CD1   1 
ATOM   712  C CD2   . LEU   A 1 110 ? -6.589  18.397 45.522 1 29     ? 91  LEU   A CD2   1 
ATOM   713  N N     . GLN   A 1 111 ? -6.333  13.561 48.246 1 23.76  ? 92  GLN   A N     1 
ATOM   714  C CA    . GLN   A 1 111 ? -6.436  12.686 49.424 1 23.75  ? 92  GLN   A CA    1 
ATOM   715  C C     . GLN   A 1 111 ? -5.12   12.681 50.201 1 27.94  ? 92  GLN   A C     1 
ATOM   716  O O     . GLN   A 1 111 ? -5.138  12.758 51.433 1 27.66  ? 92  GLN   A O     1 
ATOM   717  C CB    . GLN   A 1 111 ? -6.84   11.26  49.016 1 25.37  ? 92  GLN   A CB    1 
ATOM   718  C CG    . GLN   A 1 111 ? -8.253  11.166 48.443 1 51.35  ? 92  GLN   A CG    1 
ATOM   719  C CD    . GLN   A 1 111 ? -9.23   10.522 49.388 1 81.68  ? 92  GLN   A CD    1 
ATOM   720  O OE1   . GLN   A 1 111 ? -9.603  9.354  49.223 1 79.23  ? 92  GLN   A OE1   1 
ATOM   721  N NE2   . GLN   A 1 111 ? -9.691  11.28  50.383 1 74.39  ? 92  GLN   A NE2   1 
ATOM   722  N N     . GLU   A 1 112 ? -3.977  12.64  49.48  1 25.62  ? 93  GLU   A N     1 
ATOM   723  C CA    . GLU   A 1 112 ? -2.633  12.698 50.073 1 26.45  ? 93  GLU   A CA    1 
ATOM   724  C C     . GLU   A 1 112 ? -2.397  14.083 50.725 1 31.89  ? 93  GLU   A C     1 
ATOM   725  O O     . GLU   A 1 112 ? -1.791  14.153 51.793 1 30.87  ? 93  GLU   A O     1 
ATOM   726  C CB    . GLU   A 1 112 ? -1.552  12.391 49.019 1 27.53  ? 93  GLU   A CB    1 
ATOM   727  C CG    . GLU   A 1 112 ? -0.142  12.26  49.583 1 33.98  ? 93  GLU   A CG    1 
ATOM   728  C CD    . GLU   A 1 112 ? 0.142   11.054 50.46  1 45.45  ? 93  GLU   A CD    1 
ATOM   729  O OE1   . GLU   A 1 112 ? -0.424  9.967  50.198 1 34.26  ? 93  GLU   A OE1   1 
ATOM   730  O OE2   . GLU   A 1 112 ? 0.98    11.186 51.38  1 33.43  ? 93  GLU   A OE2   1 
ATOM   731  N N     . LEU   A 1 113 ? -2.901  15.165 50.087 1 29.89  ? 94  LEU   A N     1 
ATOM   732  C CA    . LEU   A 1 113 ? -2.827  16.533 50.615 1 29.9   ? 94  LEU   A CA    1 
ATOM   733  C C     . LEU   A 1 113 ? -3.58   16.571 51.94  1 32.7   ? 94  LEU   A C     1 
ATOM   734  O O     . LEU   A 1 113 ? -3.01   16.973 52.951 1 31.6   ? 94  LEU   A O     1 
ATOM   735  C CB    . LEU   A 1 113 ? -3.486  17.544 49.649 1 30.13  ? 94  LEU   A CB    1 
ATOM   736  C CG    . LEU   A 1 113 ? -2.632  18.248 48.609 1 34.79  ? 94  LEU   A CG    1 
ATOM   737  C CD1   . LEU   A 1 113 ? -3.515  19.014 47.647 1 35.2   ? 94  LEU   A CD1   1 
ATOM   738  C CD2   . LEU   A 1 113 ? -1.683  19.222 49.244 1 36.93  ? 94  LEU   A CD2   1 
ATOM   739  N N     . GLU   A 1 114 ? -4.853  16.113 51.918 1 29.94  ? 95  GLU   A N     1 
ATOM   740  C CA    . GLU   A 1 114 ? -5.786  16.015 53.044 1 30.29  ? 95  GLU   A CA    1 
ATOM   741  C C     . GLU   A 1 114 ? -5.191  15.221 54.205 1 33.42  ? 95  GLU   A C     1 
ATOM   742  O O     . GLU   A 1 114 ? -5.438  15.575 55.363 1 33.21  ? 95  GLU   A O     1 
ATOM   743  C CB    . GLU   A 1 114 ? -7.091  15.347 52.587 1 32.1   ? 95  GLU   A CB    1 
ATOM   744  C CG    . GLU   A 1 114 ? -8.34   16.025 53.115 1 47.06  ? 95  GLU   A CG    1 
ATOM   745  C CD    . GLU   A 1 114 ? -9.229  16.659 52.063 1 69.37  ? 95  GLU   A CD    1 
ATOM   746  O OE1   . GLU   A 1 114 ? -9.227  16.184 50.904 1 60.94  ? 95  GLU   A OE1   1 
ATOM   747  O OE2   . GLU   A 1 114 ? -9.957  17.618 52.409 1 67.8   ? 95  GLU   A OE2   1 
ATOM   748  N N     . LYS   A 1 115 ? -4.406  14.154 53.9   1 29.23  ? 96  LYS   A N     1 
ATOM   749  C CA    . LYS   A 1 115 ? -3.728  13.333 54.915 1 29.03  ? 96  LYS   A CA    1 
ATOM   750  C C     . LYS   A 1 115 ? -2.725  14.177 55.703 1 32.52  ? 96  LYS   A C     1 
ATOM   751  O O     . LYS   A 1 115 ? -2.609  14.003 56.918 1 31.84  ? 96  LYS   A O     1 
ATOM   752  C CB    . LYS   A 1 115 ? -3.023  12.129 54.277 1 32.12  ? 96  LYS   A CB    1 
ATOM   753  C CG    . LYS   A 1 115 ? -3.914  10.916 54.043 1 40.18  ? 96  LYS   A CG    1 
ATOM   754  C CD    . LYS   A 1 115 ? -3.078  9.741  53.535 1 48.9   ? 96  LYS   A CD    1 
ATOM   755  C CE    . LYS   A 1 115 ? -3.937  8.582  53.092 1 63.68  ? 96  LYS   A CE    1 
ATOM   756  N NZ    . LYS   A 1 115 ? -3.139  7.522  52.42  1 72.41  ? 96  LYS   A NZ    1 
ATOM   757  N N     . TRP   A 1 116 ? -2.017  15.112 55.014 1 28.39  ? 97  TRP   A N     1 
ATOM   758  C CA    . TRP   A 1 116 ? -1.069  16.001 55.675 1 27.98  ? 97  TRP   A CA    1 
ATOM   759  C C     . TRP   A 1 116 ? -1.793  17.097 56.428 1 32.84  ? 97  TRP   A C     1 
ATOM   760  O O     . TRP   A 1 116 ? -1.431  17.388 57.564 1 33.19  ? 97  TRP   A O     1 
ATOM   761  C CB    . TRP   A 1 116 ? -0.022  16.59  54.712 1 26.22  ? 97  TRP   A CB    1 
ATOM   762  C CG    . TRP   A 1 116 ? 1.05    17.321 55.457 1 26.28  ? 97  TRP   A CG    1 
ATOM   763  C CD1   . TRP   A 1 116 ? 2.153   16.775 56.043 1 28.95  ? 97  TRP   A CD1   1 
ATOM   764  C CD2   . TRP   A 1 116 ? 1.047   18.707 55.817 1 25.89  ? 97  TRP   A CD2   1 
ATOM   765  N NE1   . TRP   A 1 116 ? 2.846   17.736 56.736 1 28.48  ? 97  TRP   A NE1   1 
ATOM   766  C CE2   . TRP   A 1 116 ? 2.178   18.929 56.633 1 29.98  ? 97  TRP   A CE2   1 
ATOM   767  C CE3   . TRP   A 1 116 ? 0.181   19.783 55.552 1 27.07  ? 97  TRP   A CE3   1 
ATOM   768  C CZ2   . TRP   A 1 116 ? 2.506   20.197 57.124 1 29.15  ? 97  TRP   A CZ2   1 
ATOM   769  C CZ3   . TRP   A 1 116 ? 0.494   21.034 56.058 1 28.42  ? 97  TRP   A CZ3   1 
ATOM   770  C CH2   . TRP   A 1 116 ? 1.645   21.233 56.829 1 29.24  ? 97  TRP   A CH2   1 
ATOM   771  N N     . LEU   A 1 117 ? -2.802  17.707 55.791 1 30.17  ? 98  LEU   A N     1 
ATOM   772  C CA    . LEU   A 1 117 ? -3.626  18.784 56.336 1 31.15  ? 98  LEU   A CA    1 
ATOM   773  C C     . LEU   A 1 117 ? -4.239  18.424 57.686 1 38     ? 98  LEU   A C     1 
ATOM   774  O O     . LEU   A 1 117 ? -4.248  19.263 58.584 1 37.79  ? 98  LEU   A O     1 
ATOM   775  C CB    . LEU   A 1 117 ? -4.721  19.132 55.322 1 31.31  ? 98  LEU   A CB    1 
ATOM   776  C CG    . LEU   A 1 117 ? -4.585  20.428 54.501 1 35.75  ? 98  LEU   A CG    1 
ATOM   777  C CD1   . LEU   A 1 117 ? -3.17   20.666 54.002 1 35.5   ? 98  LEU   A CD1   1 
ATOM   778  C CD2   . LEU   A 1 117 ? -5.543  20.413 53.336 1 38.41  ? 98  LEU   A CD2   1 
ATOM   779  N N     . LYS   A 1 118 ? -4.7    17.16  57.842 1 36.31  ? 99  LYS   A N     1 
ATOM   780  C CA    . LYS   A 1 118 ? -5.311  16.613 59.065 1 36.19  ? 99  LYS   A CA    1 
ATOM   781  C C     . LYS   A 1 118 ? -4.263  16.11  60.072 1 40.98  ? 99  LYS   A C     1 
ATOM   782  O O     . LYS   A 1 118 ? -4.64   15.644 61.147 1 41.84  ? 99  LYS   A O     1 
ATOM   783  C CB    . LYS   A 1 118 ? -6.293  15.474 58.71  1 38.01  ? 99  LYS   A CB    1 
ATOM   784  C CG    . LYS   A 1 118 ? -7.555  15.937 57.997 1 47.25  ? 99  LYS   A CG    1 
ATOM   785  C CD    . LYS   A 1 118 ? -8.214  14.799 57.224 1 56.73  ? 99  LYS   A CD    1 
ATOM   786  C CE    . LYS   A 1 118 ? -9.531  15.224 56.624 1 66.87  ? 99  LYS   A CE    1 
ATOM   787  N NZ    . LYS   A 1 118 ? -10.103 14.167 55.751 1 76.64  ? 99  LYS   A NZ    1 
ATOM   788  N N     . ALA   A 1 119 ? -2.958  16.219 59.73  1 37.73  ? 100 ALA   A N     1 
ATOM   789  C CA    . ALA   A 1 119 ? -1.802  15.78  60.532 1 37.57  ? 100 ALA   A CA    1 
ATOM   790  C C     . ALA   A 1 119 ? -1.843  14.281 60.894 1 41.98  ? 100 ALA   A C     1 
ATOM   791  O O     . ALA   A 1 119 ? -1.504  13.899 62.023 1 41.34  ? 100 ALA   A O     1 
ATOM   792  C CB    . ALA   A 1 119 ? -1.627  16.657 61.779 1 38.3   ? 100 ALA   A CB    1 
ATOM   793  N N     . ALA   A 1 120 ? -2.256  13.435 59.92  1 38.69  ? 101 ALA   A N     1 
ATOM   794  C CA    . ALA   A 1 120 ? -2.338  11.977 60.073 1 38.77  ? 101 ALA   A CA    1 
ATOM   795  C C     . ALA   A 1 120 ? -0.923  11.355 60.199 1 44.29  ? 101 ALA   A C     1 
ATOM   796  O O     . ALA   A 1 120 ? 0.032   11.95  59.695 1 43.62  ? 101 ALA   A O     1 
ATOM   797  C CB    . ALA   A 1 120 ? -3.091  11.366 58.898 1 39.06  ? 101 ALA   A CB    1 
ATOM   798  N N     . PRO   A 1 121 ? -0.746  10.189 60.876 1 43.01  ? 102 PRO   A N     1 
ATOM   799  C CA    . PRO   A 1 121 ? 0.612   9.607  60.997 1 42.81  ? 102 PRO   A CA    1 
ATOM   800  C C     . PRO   A 1 121 ? 1.206   9.074  59.689 1 45.17  ? 102 PRO   A C     1 
ATOM   801  O O     . PRO   A 1 121 ? 2.429   9.016  59.555 1 44.83  ? 102 PRO   A O     1 
ATOM   802  C CB    . PRO   A 1 121 ? 0.415   8.47   62.004 1 44.86  ? 102 PRO   A CB    1 
ATOM   803  C CG    . PRO   A 1 121 ? -1.016  8.061  61.83  1 49.48  ? 102 PRO   A CG    1 
ATOM   804  C CD    . PRO   A 1 121 ? -1.751  9.349  61.568 1 45.02  ? 102 PRO   A CD    1 
ATOM   805  N N     . ALA   A 1 122 ? 0.332   8.669  58.738 1 40.12  ? 103 ALA   A N     1 
ATOM   806  C CA    . ALA   A 1 122 ? 0.683   8.124  57.427 1 39.14  ? 103 ALA   A CA    1 
ATOM   807  C C     . ALA   A 1 122 ? 0.929   9.227  56.375 1 41.12  ? 103 ALA   A C     1 
ATOM   808  O O     . ALA   A 1 122 ? 1.101   8.926  55.193 1 40.99  ? 103 ALA   A O     1 
ATOM   809  C CB    . ALA   A 1 122 ? -0.419  7.185  56.952 1 40.03  ? 103 ALA   A CB    1 
ATOM   810  N N     . ALA   A 1 123 ? 0.931   10.498 56.804 1 35.1   ? 104 ALA   A N     1 
ATOM   811  C CA    . ALA   A 1 123 ? 1.156   11.642 55.928 1 33.6   ? 104 ALA   A CA    1 
ATOM   812  C C     . ALA   A 1 123 ? 2.647   11.757 55.621 1 35.61  ? 104 ALA   A C     1 
ATOM   813  O O     . ALA   A 1 123 ? 3.476   11.155 56.316 1 35.03  ? 104 ALA   A O     1 
ATOM   814  C CB    . ALA   A 1 123 ? 0.656   12.909 56.6   1 34.14  ? 104 ALA   A CB    1 
ATOM   815  N N     . PHE   A 1 124 ? 2.991   12.506 54.563 1 30.65  ? 105 PHE   A N     1 
ATOM   816  C CA    . PHE   A 1 124 ? 4.389   12.692 54.178 1 29.25  ? 105 PHE   A CA    1 
ATOM   817  C C     . PHE   A 1 124 ? 5.103   13.58  55.186 1 32.85  ? 105 PHE   A C     1 
ATOM   818  O O     . PHE   A 1 124 ? 4.517   14.542 55.696 1 32.39  ? 105 PHE   A O     1 
ATOM   819  C CB    . PHE   A 1 124 ? 4.493   13.27  52.758 1 30.11  ? 105 PHE   A CB    1 
ATOM   820  C CG    . PHE   A 1 124 ? 5.893   13.366 52.207 1 30.48  ? 105 PHE   A CG    1 
ATOM   821  C CD1   . PHE   A 1 124 ? 6.603   12.223 51.866 1 32.88  ? 105 PHE   A CD1   1 
ATOM   822  C CD2   . PHE   A 1 124 ? 6.486   14.601 51.989 1 32.49  ? 105 PHE   A CD2   1 
ATOM   823  C CE1   . PHE   A 1 124 ? 7.898   12.312 51.356 1 33.64  ? 105 PHE   A CE1   1 
ATOM   824  C CE2   . PHE   A 1 124 ? 7.776   14.691 51.456 1 34.91  ? 105 PHE   A CE2   1 
ATOM   825  C CZ    . PHE   A 1 124 ? 8.466   13.547 51.131 1 32.58  ? 105 PHE   A CZ    1 
ATOM   826  N N     . ASP   A 1 125 ? 6.359   13.234 55.491 1 30.01  ? 106 ASP   A N     1 
ATOM   827  C CA    . ASP   A 1 125 ? 7.184   13.998 56.424 1 29.78  ? 106 ASP   A CA    1 
ATOM   828  C C     . ASP   A 1 125 ? 7.788   15.222 55.712 1 31.06  ? 106 ASP   A C     1 
ATOM   829  O O     . ASP   A 1 125 ? 8.782   15.096 54.992 1 30.35  ? 106 ASP   A O     1 
ATOM   830  C CB    . ASP   A 1 125 ? 8.278   13.107 57.058 1 31.76  ? 106 ASP   A CB    1 
ATOM   831  C CG    . ASP   A 1 125 ? 9.184   13.838 58.034 1 42.68  ? 106 ASP   A CG    1 
ATOM   832  O OD1   . ASP   A 1 125 ? 8.729   14.838 58.633 1 41.44  ? 106 ASP   A OD1   1 
ATOM   833  O OD2   . ASP   A 1 125 ? 10.358  13.426 58.177 1 52.73  ? 106 ASP   A OD2   1 
ATOM   834  N N     . TRP   A 1 126 ? 7.175   16.398 55.922 1 25.95  ? 107 TRP   A N     1 
ATOM   835  C CA    . TRP   A 1 126 ? 7.636   17.658 55.322 1 24.78  ? 107 TRP   A CA    1 
ATOM   836  C C     . TRP   A 1 126 ? 8.638   18.427 56.209 1 29.54  ? 107 TRP   A C     1 
ATOM   837  O O     . TRP   A 1 126 ? 9.137   19.472 55.778 1 28.33  ? 107 TRP   A O     1 
ATOM   838  C CB    . TRP   A 1 126 ? 6.435   18.552 54.959 1 22.25  ? 107 TRP   A CB    1 
ATOM   839  C CG    . TRP   A 1 126 ? 5.722   18.141 53.706 1 22.61  ? 107 TRP   A CG    1 
ATOM   840  C CD1   . TRP   A 1 126 ? 4.526   17.488 53.616 1 25.33  ? 107 TRP   A CD1   1 
ATOM   841  C CD2   . TRP   A 1 126 ? 6.182   18.324 52.361 1 22.25  ? 107 TRP   A CD2   1 
ATOM   842  N NE1   . TRP   A 1 126 ? 4.212   17.25  52.299 1 24.57  ? 107 TRP   A NE1   1 
ATOM   843  C CE2   . TRP   A 1 126 ? 5.205   17.766 51.504 1 25.93  ? 107 TRP   A CE2   1 
ATOM   844  C CE3   . TRP   A 1 126 ? 7.331   18.903 51.791 1 22.98  ? 107 TRP   A CE3   1 
ATOM   845  C CZ2   . TRP   A 1 126 ? 5.332   17.787 50.108 1 24.53  ? 107 TRP   A CZ2   1 
ATOM   846  C CZ3   . TRP   A 1 126 ? 7.456   18.914 50.406 1 23.78  ? 107 TRP   A CZ3   1 
ATOM   847  C CH2   . TRP   A 1 126 ? 6.458   18.379 49.583 1 23.98  ? 107 TRP   A CH2   1 
ATOM   848  N N     . SER   A 1 127 ? 8.952   17.899 57.426 1 27.85  ? 108 SER   A N     1 
ATOM   849  C CA    . SER   A 1 127 ? 9.837   18.542 58.424 1 28.31  ? 108 SER   A CA    1 
ATOM   850  C C     . SER   A 1 127 ? 11.195  19.075 57.869 1 32     ? 108 SER   A C     1 
ATOM   851  O O     . SER   A 1 127 ? 11.503  20.213 58.22  1 30.76  ? 108 SER   A O     1 
ATOM   852  C CB    . SER   A 1 127 ? 10.059  17.665 59.659 1 32.95  ? 108 SER   A CB    1 
ATOM   853  O OG    . SER   A 1 127 ? 10.784  16.473 59.401 1 46.82  ? 108 SER   A OG    1 
ATOM   854  N N     . PRO   A 1 128 ? 11.981  18.408 56.976 1 29.87  ? 109 PRO   A N     1 
ATOM   855  C CA    . PRO   A 1 128 ? 13.208  19.064 56.481 1 29.9   ? 109 PRO   A CA    1 
ATOM   856  C C     . PRO   A 1 128 ? 12.946  20.279 55.575 1 32.63  ? 109 PRO   A C     1 
ATOM   857  O O     . PRO   A 1 128 ? 13.806  21.143 55.466 1 32.83  ? 109 PRO   A O     1 
ATOM   858  C CB    . PRO   A 1 128 ? 13.954  17.943 55.743 1 31.99  ? 109 PRO   A CB    1 
ATOM   859  C CG    . PRO   A 1 128 ? 13.225  16.674 56.07  1 36.51  ? 109 PRO   A CG    1 
ATOM   860  C CD    . PRO   A 1 128 ? 11.825  17.07  56.373 1 31.96  ? 109 PRO   A CD    1 
ATOM   861  N N     . VAL   A 1 129 ? 11.754  20.357 54.95  1 27.85  ? 110 VAL   A N     1 
ATOM   862  C CA    . VAL   A 1 129 ? 11.365  21.46  54.058 1 26.94  ? 110 VAL   A CA    1 
ATOM   863  C C     . VAL   A 1 129 ? 10.819  22.618 54.906 1 29.14  ? 110 VAL   A C     1 
ATOM   864  O O     . VAL   A 1 129 ? 11.195  23.771 54.687 1 28.57  ? 110 VAL   A O     1 
ATOM   865  C CB    . VAL   A 1 129 ? 10.353  20.97  52.972 1 29.9   ? 110 VAL   A CB    1 
ATOM   866  C CG1   . VAL   A 1 129 ? 9.807   22.121 52.132 1 29.45  ? 110 VAL   A CG1   1 
ATOM   867  C CG2   . VAL   A 1 129 ? 10.979  19.902 52.082 1 29.33  ? 110 VAL   A CG2   1 
ATOM   868  N N     . VAL   A 1 130 ? 9.956   22.296 55.889 1 24.85  ? 111 VAL   A N     1 
ATOM   869  C CA    . VAL   A 1 130 ? 9.357   23.244 56.833 1 25.26  ? 111 VAL   A CA    1 
ATOM   870  C C     . VAL   A 1 130 ? 10.471  24.033 57.572 1 30.66  ? 111 VAL   A C     1 
ATOM   871  O O     . VAL   A 1 130 ? 10.38   25.263 57.687 1 30.17  ? 111 VAL   A O     1 
ATOM   872  C CB    . VAL   A 1 130 ? 8.382   22.532 57.82  1 28.62  ? 111 VAL   A CB    1 
ATOM   873  C CG1   . VAL   A 1 130 ? 7.821   23.508 58.852 1 28.2   ? 111 VAL   A CG1   1 
ATOM   874  C CG2   . VAL   A 1 130 ? 7.243   21.85  57.071 1 28.24  ? 111 VAL   A CG2   1 
ATOM   875  N N     . THR   A 1 131 ? 11.524  23.315 58.023 1 27.84  ? 112 THR   A N     1 
ATOM   876  C CA    . THR   A 1 131 ? 12.69   23.852 58.736 1 28.04  ? 112 THR   A CA    1 
ATOM   877  C C     . THR   A 1 131 ? 13.456  24.831 57.834 1 32.53  ? 112 THR   A C     1 
ATOM   878  O O     . THR   A 1 131 ? 13.846  25.917 58.287 1 32.22  ? 112 THR   A O     1 
ATOM   879  C CB    . THR   A 1 131 ? 13.58   22.677 59.202 1 35.71  ? 112 THR   A CB    1 
ATOM   880  O OG1   . THR   A 1 131 ? 12.826  21.842 60.089 1 34.7   ? 112 THR   A OG1   1 
ATOM   881  C CG2   . THR   A 1 131 ? 14.888  23.133 59.866 1 33.76  ? 112 THR   A CG2   1 
ATOM   882  N N     . TYR   A 1 132 ? 13.674  24.429 56.564 1 28.83  ? 113 TYR   A N     1 
ATOM   883  C CA    . TYR   A 1 132 ? 14.385  25.213 55.562 1 28.52  ? 113 TYR   A CA    1 
ATOM   884  C C     . TYR   A 1 132 ? 13.683  26.567 55.364 1 32.2   ? 113 TYR   A C     1 
ATOM   885  O O     . TYR   A 1 132 ? 14.358  27.593 55.364 1 32.46  ? 113 TYR   A O     1 
ATOM   886  C CB    . TYR   A 1 132 ? 14.511  24.422 54.234 1 29.59  ? 113 TYR   A CB    1 
ATOM   887  C CG    . TYR   A 1 132 ? 15.463  25.05  53.234 1 30.41  ? 113 TYR   A CG    1 
ATOM   888  C CD1   . TYR   A 1 132 ? 15.021  26.009 52.326 1 32.06  ? 113 TYR   A CD1   1 
ATOM   889  C CD2   . TYR   A 1 132 ? 16.807  24.69  53.2   1 31.18  ? 113 TYR   A CD2   1 
ATOM   890  C CE1   . TYR   A 1 132 ? 15.894  26.601 51.415 1 31.39  ? 113 TYR   A CE1   1 
ATOM   891  C CE2   . TYR   A 1 132 ? 17.69   25.276 52.293 1 32.19  ? 113 TYR   A CE2   1 
ATOM   892  C CZ    . TYR   A 1 132 ? 17.228  26.236 51.406 1 37.92  ? 113 TYR   A CZ    1 
ATOM   893  O OH    . TYR   A 1 132 ? 18.086  26.819 50.506 1 39.19  ? 113 TYR   A OH    1 
ATOM   894  N N     . VAL   A 1 133 ? 12.335  26.563 55.253 1 27.74  ? 114 VAL   A N     1 
ATOM   895  C CA    . VAL   A 1 133 ? 11.495  27.757 55.089 1 27.43  ? 114 VAL   A CA    1 
ATOM   896  C C     . VAL   A 1 133 ? 11.623  28.671 56.328 1 32.31  ? 114 VAL   A C     1 
ATOM   897  O O     . VAL   A 1 133 ? 11.807  29.881 56.172 1 31.49  ? 114 VAL   A O     1 
ATOM   898  C CB    . VAL   A 1 133 ? 10.018  27.386 54.758 1 30.82  ? 114 VAL   A CB    1 
ATOM   899  C CG1   . VAL   A 1 133 ? 9.097   28.613 54.77  1 30.54  ? 114 VAL   A CG1   1 
ATOM   900  C CG2   . VAL   A 1 133 ? 9.918   26.644 53.424 1 30.36  ? 114 VAL   A CG2   1 
ATOM   901  N N     . CYS   A 1 134 ? 11.54   28.089 57.548 1 29.07  ? 115 CYS   A N     1 
ATOM   902  C CA    . CYS   A 1 134 ? 11.691  28.833 58.813 1 28.88  ? 115 CYS   A CA    1 
ATOM   903  C C     . CYS   A 1 134 ? 13.049  29.52  58.883 1 32.21  ? 115 CYS   A C     1 
ATOM   904  O O     . CYS   A 1 134 ? 13.113  30.686 59.293 1 31.79  ? 115 CYS   A O     1 
ATOM   905  C CB    . CYS   A 1 134 ? 11.459  27.926 60.014 1 28.95  ? 115 CYS   A CB    1 
ATOM   906  S SG    . CYS   A 1 134 ? 9.739   27.419 60.221 1 32.4   ? 115 CYS   A SG    1 
ATOM   907  N N     . ASP   A 1 135 ? 14.109  28.822 58.401 1 28.7   ? 116 ASP   A N     1 
ATOM   908  C CA    . ASP   A 1 135 ? 15.476  29.331 58.283 1 29.19  ? 116 ASP   A CA    1 
ATOM   909  C C     . ASP   A 1 135 ? 15.49   30.55  57.355 1 34.02  ? 116 ASP   A C     1 
ATOM   910  O O     . ASP   A 1 135 ? 15.892  31.628 57.794 1 33.55  ? 116 ASP   A O     1 
ATOM   911  C CB    . ASP   A 1 135 ? 16.429  28.235 57.762 1 30.85  ? 116 ASP   A CB    1 
ATOM   912  C CG    . ASP   A 1 135 ? 16.851  27.201 58.787 1 41.91  ? 116 ASP   A CG    1 
ATOM   913  O OD1   . ASP   A 1 135 ? 16.611  27.426 59.997 1 43.74  ? 116 ASP   A OD1   1 
ATOM   914  O OD2   . ASP   A 1 135 ? 17.468  26.188 58.387 1 45.46  ? 116 ASP   A OD2   1 
ATOM   915  N N     . LEU   A 1 136 ? 14.986  30.392 56.095 1 30.85  ? 117 LEU   A N     1 
ATOM   916  C CA    . LEU   A 1 136 ? 14.883  31.468 55.095 1 29.99  ? 117 LEU   A CA    1 
ATOM   917  C C     . LEU   A 1 136 ? 14.186  32.723 55.653 1 32.76  ? 117 LEU   A C     1 
ATOM   918  O O     . LEU   A 1 136 ? 14.682  33.832 55.447 1 31.85  ? 117 LEU   A O     1 
ATOM   919  C CB    . LEU   A 1 136 ? 14.122  31.012 53.82  1 29.81  ? 117 LEU   A CB    1 
ATOM   920  C CG    . LEU   A 1 136 ? 14.65   29.821 52.986 1 34.37  ? 117 LEU   A CG    1 
ATOM   921  C CD1   . LEU   A 1 136 ? 13.783  29.601 51.744 1 33.2   ? 117 LEU   A CD1   1 
ATOM   922  C CD2   . LEU   A 1 136 ? 16.124  29.984 52.596 1 38.2   ? 117 LEU   A CD2   1 
ATOM   923  N N     . GLU   A 1 137 ? 13.055  32.535 56.369 1 28.93  ? 118 GLU   A N     1 
ATOM   924  C CA    . GLU   A 1 137 ? 12.207  33.599 56.916 1 29.56  ? 118 GLU   A CA    1 
ATOM   925  C C     . GLU   A 1 137 ? 12.792  34.382 58.127 1 35.64  ? 118 GLU   A C     1 
ATOM   926  O O     . GLU   A 1 137 ? 12.152  35.322 58.61  1 36.05  ? 118 GLU   A O     1 
ATOM   927  C CB    . GLU   A 1 137 ? 10.81   33.048 57.244 1 30.85  ? 118 GLU   A CB    1 
ATOM   928  C CG    . GLU   A 1 137 ? 10.03   32.704 55.982 1 39.36  ? 118 GLU   A CG    1 
ATOM   929  C CD    . GLU   A 1 137 ? 8.549   32.396 56.085 1 52.74  ? 118 GLU   A CD    1 
ATOM   930  O OE1   . GLU   A 1 137 ? 7.935   32.709 57.131 1 45.21  ? 118 GLU   A OE1   1 
ATOM   931  O OE2   . GLU   A 1 137 ? 7.99    31.891 55.083 1 37.73  ? 118 GLU   A OE2   1 
ATOM   932  N N     . GLY   A 1 138 ? 13.998  34.028 58.563 1 33.36  ? 119 GLY   A N     1 
ATOM   933  C CA    . GLY   A 1 138 ? 14.682  34.708 59.661 1 33.43  ? 119 GLY   A CA    1 
ATOM   934  C C     . GLY   A 1 138 ? 14.503  34.075 61.023 1 38.66  ? 119 GLY   A C     1 
ATOM   935  O O     . GLY   A 1 138 ? 14.695  34.746 62.043 1 39.39  ? 119 GLY   A O     1 
ATOM   936  N N     . ASN   A 1 139 ? 14.136  32.771 61.048 1 34.89  ? 120 ASN   A N     1 
ATOM   937  C CA    . ASN   A 1 139 ? 13.914  31.96  62.252 1 34.56  ? 120 ASN   A CA    1 
ATOM   938  C C     . ASN   A 1 139 ? 12.979  32.644 63.272 1 38.1   ? 120 ASN   A C     1 
ATOM   939  O O     . ASN   A 1 139 ? 13.181  32.528 64.488 1 37.45  ? 120 ASN   A O     1 
ATOM   940  C CB    . ASN   A 1 139 ? 15.248  31.53  62.874 1 35.18  ? 120 ASN   A CB    1 
ATOM   941  C CG    . ASN   A 1 139 ? 15.965  30.474 62.08  1 45     ? 120 ASN   A CG    1 
ATOM   942  O OD1   . ASN   A 1 139 ? 15.667  29.283 62.168 1 40.51  ? 120 ASN   A OD1   1 
ATOM   943  N ND2   . ASN   A 1 139 ? 16.929  30.885 61.288 1 34.99  ? 120 ASN   A ND2   1 
ATOM   944  N N     . ARG   A 1 140 ? 11.947  33.357 62.753 1 34.04  ? 121 ARG   A N     1 
ATOM   945  C CA    . ARG   A 1 140 ? 10.923  34.057 63.53  1 33.89  ? 121 ARG   A CA    1 
ATOM   946  C C     . ARG   A 1 140 ? 10.033  33.05  64.267 1 39.05  ? 121 ARG   A C     1 
ATOM   947  O O     . ARG   A 1 140 ? 9.471   33.381 65.311 1 38.87  ? 121 ARG   A O     1 
ATOM   948  C CB    . ARG   A 1 140 ? 10.03   34.918 62.614 1 34.15  ? 121 ARG   A CB    1 
ATOM   949  C CG    . ARG   A 1 140 ? 10.741  36.03  61.841 1 43.79  ? 121 ARG   A CG    1 
ATOM   950  C CD    . ARG   A 1 140 ? 9.737   36.779 60.986 1 52.58  ? 121 ARG   A CD    1 
ATOM   951  N NE    . ARG   A 1 140 ? 10.347  37.768 60.093 1 61.34  ? 121 ARG   A NE    1 
ATOM   952  C CZ    . ARG   A 1 140 ? 10.615  39.029 60.426 1 70.29  ? 121 ARG   A CZ    1 
ATOM   953  N NH1   . ARG   A 1 140 ? 10.377  39.464 61.658 1 56.01  ? 121 ARG   A NH1   1 
ATOM   954  N NH2   . ARG   A 1 140 ? 11.145  39.857 59.536 1 51.19  ? 121 ARG   A NH2   1 
ATOM   955  N N     . VAL   A 1 141 ? 9.863   31.84  63.68  1 35.81  ? 122 VAL   A N     1 
ATOM   956  C CA    . VAL   A 1 141 ? 9.027   30.738 64.178 1 35.1   ? 122 VAL   A CA    1 
ATOM   957  C C     . VAL   A 1 141 ? 9.768   29.389 64.033 1 38.36  ? 122 VAL   A C     1 
ATOM   958  O O     . VAL   A 1 141 ? 10.821  29.317 63.388 1 37.1   ? 122 VAL   A O     1 
ATOM   959  C CB    . VAL   A 1 141 ? 7.614   30.7   63.494 1 38.89  ? 122 VAL   A CB    1 
ATOM   960  C CG1   . VAL   A 1 141 ? 6.805   31.965 63.783 1 38.6   ? 122 VAL   A CG1   1 
ATOM   961  C CG2   . VAL   A 1 141 ? 7.711   30.449 61.986 1 38.32  ? 122 VAL   A CG2   1 
ATOM   962  N N     . LYS   A 1 142 ? 9.208   28.328 64.635 1 35.17  ? 123 LYS   A N     1 
ATOM   963  C CA    . LYS   A 1 142 ? 9.749   26.973 64.554 1 35.5   ? 123 LYS   A CA    1 
ATOM   964  C C     . LYS   A 1 142 ? 8.771   26.096 63.753 1 38.84  ? 123 LYS   A C     1 
ATOM   965  O O     . LYS   A 1 142 ? 7.635   26.51  63.532 1 37.93  ? 123 LYS   A O     1 
ATOM   966  C CB    . LYS   A 1 142 ? 9.993   26.401 65.959 1 38.68  ? 123 LYS   A CB    1 
ATOM   967  C CG    . LYS   A 1 142 ? 11.364  26.73  66.53  1 53.97  ? 123 LYS   A CG    1 
ATOM   968  C CD    . LYS   A 1 142 ? 11.527  26.154 67.941 1 63.28  ? 123 LYS   A CD    1 
ATOM   969  C CE    . LYS   A 1 142 ? 12.867  26.472 68.568 1 72.88  ? 123 LYS   A CE    1 
ATOM   970  N NZ    . LYS   A 1 142 ? 13.963  25.625 68.022 1 79.29  ? 123 LYS   A NZ    1 
ATOM   971  N N     . GLY   A 1 143 ? 9.233   24.92  63.318 1 36.73  ? 124 GLY   A N     1 
ATOM   972  C CA    . GLY   A 1 143 ? 8.474   23.941 62.534 1 36.96  ? 124 GLY   A CA    1 
ATOM   973  C C     . GLY   A 1 143 ? 7.008   23.747 62.901 1 40.82  ? 124 GLY   A C     1 
ATOM   974  O O     . GLY   A 1 143 ? 6.146   23.952 62.04  1 40.13  ? 124 GLY   A O     1 
ATOM   975  N N     . PRO   A 1 144 ? 6.676   23.386 64.178 1 36.95  ? 125 PRO   A N     1 
ATOM   976  C CA    . PRO   A 1 144 ? 5.257   23.194 64.552 1 36.18  ? 125 PRO   A CA    1 
ATOM   977  C C     . PRO   A 1 144 ? 4.352   24.414 64.379 1 37.93  ? 125 PRO   A C     1 
ATOM   978  O O     . PRO   A 1 144 ? 3.193   24.256 63.988 1 37.54  ? 125 PRO   A O     1 
ATOM   979  C CB    . PRO   A 1 144 ? 5.331   22.75  66.02  1 38.32  ? 125 PRO   A CB    1 
ATOM   980  C CG    . PRO   A 1 144 ? 6.722   22.21  66.19  1 42.93  ? 125 PRO   A CG    1 
ATOM   981  C CD    . PRO   A 1 144 ? 7.568   23.082 65.319 1 38.41  ? 125 PRO   A CD    1 
ATOM   982  N N     . GLU   A 1 145 ? 4.865   25.623 64.673 1 32.79  ? 126 GLU   A N     1 
ATOM   983  C CA    . GLU   A 1 145 ? 4.102   26.867 64.526 1 31.97  ? 126 GLU   A CA    1 
ATOM   984  C C     . GLU   A 1 145 ? 3.833   27.175 63.041 1 34.7   ? 126 GLU   A C     1 
ATOM   985  O O     . GLU   A 1 145 ? 2.741   27.633 62.69  1 33.8   ? 126 GLU   A O     1 
ATOM   986  C CB    . GLU   A 1 145 ? 4.853   28.03  65.183 1 33.4   ? 126 GLU   A CB    1 
ATOM   987  C CG    . GLU   A 1 145 ? 3.953   29.19  65.569 1 43.27  ? 126 GLU   A CG    1 
ATOM   988  C CD    . GLU   A 1 145 ? 4.663   30.424 66.093 1 57.55  ? 126 GLU   A CD    1 
ATOM   989  O OE1   . GLU   A 1 145 ? 5.759   30.281 66.684 1 46.32  ? 126 GLU   A OE1   1 
ATOM   990  O OE2   . GLU   A 1 145 ? 4.125   31.539 65.9   1 44.91  ? 126 GLU   A OE2   1 
ATOM   991  N N     . LYS   A 1 146 ? 4.838   26.904 62.18  1 30.79  ? 127 LYS   A N     1 
ATOM   992  C CA    . LYS   A 1 146 ? 4.8     27.11  60.732 1 29.91  ? 127 LYS   A CA    1 
ATOM   993  C C     . LYS   A 1 146 ? 3.734   26.221 60.101 1 32.18  ? 127 LYS   A C     1 
ATOM   994  O O     . LYS   A 1 146 ? 2.91    26.72  59.337 1 30.88  ? 127 LYS   A O     1 
ATOM   995  C CB    . LYS   A 1 146 ? 6.189   26.837 60.119 1 31.45  ? 127 LYS   A CB    1 
ATOM   996  C CG    . LYS   A 1 146 ? 6.255   26.917 58.586 1 37.79  ? 127 LYS   A CG    1 
ATOM   997  C CD    . LYS   A 1 146 ? 6.791   28.24  58.087 1 42.67  ? 127 LYS   A CD    1 
ATOM   998  C CE    . LYS   A 1 146 ? 5.676   29.102 57.591 1 41.19  ? 127 LYS   A CE    1 
ATOM   999  N NZ    . LYS   A 1 146 ? 6.182   30.36  57.003 1 39.34  ? 127 LYS   A NZ    1 
ATOM   1000 N N     . GLU   A 1 147 ? 3.747   24.915 60.448 1 29.26  ? 128 GLU   A N     1 
ATOM   1001 C CA    . GLU   A 1 147 ? 2.805   23.902 59.971 1 29.18  ? 128 GLU   A CA    1 
ATOM   1002 C C     . GLU   A 1 147 ? 1.368   24.269 60.332 1 34.16  ? 128 GLU   A C     1 
ATOM   1003 O O     . GLU   A 1 147 ? 0.471   24.121 59.495 1 33.23  ? 128 GLU   A O     1 
ATOM   1004 C CB    . GLU   A 1 147 ? 3.149   22.52  60.546 1 30.17  ? 128 GLU   A CB    1 
ATOM   1005 C CG    . GLU   A 1 147 ? 4.416   21.888 59.995 1 34.68  ? 128 GLU   A CG    1 
ATOM   1006 C CD    . GLU   A 1 147 ? 4.496   20.38  60.143 1 49.33  ? 128 GLU   A CD    1 
ATOM   1007 O OE1   . GLU   A 1 147 ? 3.544   19.778 60.689 1 47.69  ? 128 GLU   A OE1   1 
ATOM   1008 O OE2   . GLU   A 1 147 ? 5.498   19.793 59.676 1 40.3   ? 128 GLU   A OE2   1 
ATOM   1009 N N     . GLU   A 1 148 ? 1.16    24.779 61.565 1 32.26  ? 129 GLU   A N     1 
ATOM   1010 C CA    . GLU   A 1 148 ? -0.153  25.183 62.064 1 32.42  ? 129 GLU   A CA    1 
ATOM   1011 C C     . GLU   A 1 148 ? -0.764  26.371 61.299 1 36.89  ? 129 GLU   A C     1 
ATOM   1012 O O     . GLU   A 1 148 ? -1.974  26.367 61.049 1 37.53  ? 129 GLU   A O     1 
ATOM   1013 C CB    . GLU   A 1 148 ? -0.122  25.445 63.582 1 33.95  ? 129 GLU   A CB    1 
ATOM   1014 C CG    . GLU   A 1 148 ? -1.5    25.48  64.233 1 44.56  ? 129 GLU   A CG    1 
ATOM   1015 C CD    . GLU   A 1 148 ? -2.543  24.522 63.675 1 65.79  ? 129 GLU   A CD    1 
ATOM   1016 O OE1   . GLU   A 1 148 ? -2.35   23.287 63.776 1 60.42  ? 129 GLU   A OE1   1 
ATOM   1017 O OE2   . GLU   A 1 148 ? -3.552  25.012 63.118 1 58.99  ? 129 GLU   A OE2   1 
ATOM   1018 N N     . LYS   A 1 149 ? 0.059   27.372 60.923 1 32.34  ? 130 LYS   A N     1 
ATOM   1019 C CA    . LYS   A 1 149 ? -0.426  28.537 60.179 1 31.35  ? 130 LYS   A CA    1 
ATOM   1020 C C     . LYS   A 1 149 ? -0.966  28.115 58.805 1 34.17  ? 130 LYS   A C     1 
ATOM   1021 O O     . LYS   A 1 149 ? -2.011  28.616 58.378 1 33.85  ? 130 LYS   A O     1 
ATOM   1022 C CB    . LYS   A 1 149 ? 0.666   29.618 60.053 1 33.34  ? 130 LYS   A CB    1 
ATOM   1023 C CG    . LYS   A 1 149 ? 0.09    31.021 59.868 1 40.63  ? 130 LYS   A CG    1 
ATOM   1024 C CD    . LYS   A 1 149 ? 1.135   32.098 60.056 1 50.3   ? 130 LYS   A CD    1 
ATOM   1025 C CE    . LYS   A 1 149 ? 0.551   33.484 59.932 1 60.77  ? 130 LYS   A CE    1 
ATOM   1026 N NZ    . LYS   A 1 149 ? 1.611   34.531 59.947 1 69.04  ? 130 LYS   A NZ    1 
ATOM   1027 N N     . LEU   A 1 150 ? -0.276  27.162 58.143 1 30.02  ? 131 LEU   A N     1 
ATOM   1028 C CA    . LEU   A 1 150 ? -0.666  26.639 56.826 1 28.61  ? 131 LEU   A CA    1 
ATOM   1029 C C     . LEU   A 1 150 ? -1.964  25.819 56.897 1 32.41  ? 131 LEU   A C     1 
ATOM   1030 O O     . LEU   A 1 150 ? -2.864  26.025 56.079 1 32.36  ? 131 LEU   A O     1 
ATOM   1031 C CB    . LEU   A 1 150 ? 0.485   25.812 56.202 1 28     ? 131 LEU   A CB    1 
ATOM   1032 C CG    . LEU   A 1 150 ? 0.182   25.138 54.851 1 30.94  ? 131 LEU   A CG    1 
ATOM   1033 C CD1   . LEU   A 1 150 ? -0.256  26.165 53.799 1 30.55  ? 131 LEU   A CD1   1 
ATOM   1034 C CD2   . LEU   A 1 150 ? 1.34    24.29  54.383 1 30.08  ? 131 LEU   A CD2   1 
ATOM   1035 N N     . ARG   A 1 151 ? -2.046  24.886 57.861 1 29.38  ? 132 ARG   A N     1 
ATOM   1036 C CA    . ARG   A 1 151 ? -3.226  24.041 58.099 1 29.09  ? 132 ARG   A CA    1 
ATOM   1037 C C     . ARG   A 1 151 ? -4.454  24.906 58.369 1 33.48  ? 132 ARG   A C     1 
ATOM   1038 O O     . ARG   A 1 151 ? -5.542  24.593 57.878 1 34.24  ? 132 ARG   A O     1 
ATOM   1039 C CB    . ARG   A 1 151 ? -2.987  23.062 59.263 1 27.72  ? 132 ARG   A CB    1 
ATOM   1040 C CG    . ARG   A 1 151 ? -2.005  21.962 58.919 1 32.9   ? 132 ARG   A CG    1 
ATOM   1041 C CD    . ARG   A 1 151 ? -1.831  20.993 60.059 1 36.43  ? 132 ARG   A CD    1 
ATOM   1042 N NE    . ARG   A 1 151 ? -1.217  19.745 59.598 1 36.92  ? 132 ARG   A NE    1 
ATOM   1043 C CZ    . ARG   A 1 151 ? -0.004  19.327 59.944 1 46.83  ? 132 ARG   A CZ    1 
ATOM   1044 N NH1   . ARG   A 1 151 ? 0.748   20.054 60.762 1 35.05  ? 132 ARG   A NH1   1 
ATOM   1045 N NH2   . ARG   A 1 151 ? 0.462   18.175 59.484 1 30.17  ? 132 ARG   A NH2   1 
ATOM   1046 N N     . GLN   A 1 152 ? -4.267  26.029 59.082 1 29.77  ? 133 GLN   A N     1 
ATOM   1047 C CA    . GLN   A 1 152 ? -5.354  26.96  59.368 1 29.61  ? 133 GLN   A CA    1 
ATOM   1048 C C     . GLN   A 1 152 ? -5.733  27.775 58.128 1 33.14  ? 133 GLN   A C     1 
ATOM   1049 O O     . GLN   A 1 152 ? -6.89   28.196 57.998 1 32.39  ? 133 GLN   A O     1 
ATOM   1050 C CB    . GLN   A 1 152 ? -4.987  27.874 60.549 1 31.31  ? 133 GLN   A CB    1 
ATOM   1051 C CG    . GLN   A 1 152 ? -6.193  28.266 61.414 1 49.37  ? 133 GLN   A CG    1 
ATOM   1052 C CD    . GLN   A 1 152 ? -6.58   27.189 62.404 1 63.12  ? 133 GLN   A CD    1 
ATOM   1053 O OE1   . GLN   A 1 152 ? -6.123  27.173 63.555 1 61.87  ? 133 GLN   A OE1   1 
ATOM   1054 N NE2   . GLN   A 1 152 ? -7.443  26.273 61.985 1 43.68  ? 133 GLN   A NE2   1 
ATOM   1055 N N     . ALA   A 1 153 ? -4.758  27.992 57.215 1 28.44  ? 134 ALA   A N     1 
ATOM   1056 C CA    . ALA   A 1 153 ? -4.975  28.75  55.984 1 28.34  ? 134 ALA   A CA    1 
ATOM   1057 C C     . ALA   A 1 153 ? -5.755  27.954 54.945 1 31.78  ? 134 ALA   A C     1 
ATOM   1058 O O     . ALA   A 1 153 ? -6.528  28.555 54.197 1 30.65  ? 134 ALA   A O     1 
ATOM   1059 C CB    . ALA   A 1 153 ? -3.647  29.214 55.4   1 29.03  ? 134 ALA   A CB    1 
ATOM   1060 N N     . VAL   A 1 154 ? -5.562  26.611 54.892 1 28.15  ? 135 VAL   A N     1 
ATOM   1061 C CA    . VAL   A 1 154 ? -6.25   25.783 53.893 1 28.38  ? 135 VAL   A CA    1 
ATOM   1062 C C     . VAL   A 1 154 ? -7.624  25.358 54.396 1 34.13  ? 135 VAL   A C     1 
ATOM   1063 O O     . VAL   A 1 154 ? -7.726  24.663 55.41  1 33.15  ? 135 VAL   A O     1 
ATOM   1064 C CB    . VAL   A 1 154 ? -5.411  24.593 53.347 1 31.96  ? 135 VAL   A CB    1 
ATOM   1065 C CG1   . VAL   A 1 154 ? -6.129  23.917 52.179 1 31.84  ? 135 VAL   A CG1   1 
ATOM   1066 C CG2   . VAL   A 1 154 ? -4.015  25.05  52.913 1 31.72  ? 135 VAL   A CG2   1 
ATOM   1067 N N     . LYS   A 1 155 ? -8.676  25.794 53.668 1 32.37  ? 136 LYS   A N     1 
ATOM   1068 C CA    . LYS   A 1 155 ? -10.086 25.522 53.989 1 32.61  ? 136 LYS   A CA    1 
ATOM   1069 C C     . LYS   A 1 155 ? -10.752 24.639 52.939 1 36.12  ? 136 LYS   A C     1 
ATOM   1070 O O     . LYS   A 1 155 ? -11.635 23.847 53.281 1 37.43  ? 136 LYS   A O     1 
ATOM   1071 C CB    . LYS   A 1 155 ? -10.89  26.841 54.12  1 36.02  ? 136 LYS   A CB    1 
ATOM   1072 C CG    . LYS   A 1 155 ? -10.206 27.988 54.883 1 49.85  ? 136 LYS   A CG    1 
ATOM   1073 C CD    . LYS   A 1 155 ? -10.304 27.863 56.412 1 59.19  ? 136 LYS   A CD    1 
ATOM   1074 C CE    . LYS   A 1 155 ? -10.252 29.205 57.116 1 64.35  ? 136 LYS   A CE    1 
ATOM   1075 N NZ    . LYS   A 1 155 ? -8.957  29.914 56.916 1 68.29  ? 136 LYS   A NZ    1 
ATOM   1076 N N     . GLN   A 1 156 ? -10.37  24.808 51.655 1 29.57  ? 137 GLN   A N     1 
ATOM   1077 C CA    . GLN   A 1 156 ? -10.955 24.077 50.539 1 28.06  ? 137 GLN   A CA    1 
ATOM   1078 C C     . GLN   A 1 156 ? -9.895  23.309 49.754 1 30.01  ? 137 GLN   A C     1 
ATOM   1079 O O     . GLN   A 1 156 ? -8.801  23.818 49.53  1 28.05  ? 137 GLN   A O     1 
ATOM   1080 C CB    . GLN   A 1 156 ? -11.778 25.003 49.613 1 29.06  ? 137 GLN   A CB    1 
ATOM   1081 C CG    . GLN   A 1 156 ? -12.878 25.818 50.318 1 34.82  ? 137 GLN   A CG    1 
ATOM   1082 C CD    . GLN   A 1 156 ? -14.112 25.98  49.463 1 51.49  ? 137 GLN   A CD    1 
ATOM   1083 O OE1   . GLN   A 1 156 ? -14.834 25.015 49.162 1 49.08  ? 137 GLN   A OE1   1 
ATOM   1084 N NE2   . GLN   A 1 156 ? -14.403 27.211 49.085 1 37.28  ? 137 GLN   A NE2   1 
ATOM   1085 N N     . VAL   A 1 157 ? -10.237 22.06  49.381 1 26.29  ? 138 VAL   A N     1 
ATOM   1086 C CA    . VAL   A 1 157 ? -9.432  21.081 48.642 1 25.53  ? 138 VAL   A CA    1 
ATOM   1087 C C     . VAL   A 1 157 ? -10.318 20.72  47.448 1 29.25  ? 138 VAL   A C     1 
ATOM   1088 O O     . VAL   A 1 157 ? -11.287 19.966 47.592 1 29.26  ? 138 VAL   A O     1 
ATOM   1089 C CB    . VAL   A 1 157 ? -9.128  19.855 49.549 1 29.28  ? 138 VAL   A CB    1 
ATOM   1090 C CG1   . VAL   A 1 157 ? -8.384  18.762 48.79  1 29.17  ? 138 VAL   A CG1   1 
ATOM   1091 C CG2   . VAL   A 1 157 ? -8.356  20.267 50.795 1 29.04  ? 138 VAL   A CG2   1 
ATOM   1092 N N     . LEU   A 1 158 ? -10.03  21.323 46.289 1 24.29  ? 139 LEU   A N     1 
ATOM   1093 C CA    . LEU   A 1 158 ? -10.887 21.216 45.122 1 23.09  ? 139 LEU   A CA    1 
ATOM   1094 C C     . LEU   A 1 158 ? -10.31  20.545 43.913 1 26.8   ? 139 LEU   A C     1 
ATOM   1095 O O     . LEU   A 1 158 ? -9.116  20.632 43.651 1 27.48  ? 139 LEU   A O     1 
ATOM   1096 C CB    . LEU   A 1 158 ? -11.386 22.623 44.696 1 22.74  ? 139 LEU   A CB    1 
ATOM   1097 C CG    . LEU   A 1 158 ? -11.996 23.545 45.757 1 26.87  ? 139 LEU   A CG    1 
ATOM   1098 C CD1   . LEU   A 1 158 ? -12.418 24.861 45.139 1 25.62  ? 139 LEU   A CD1   1 
ATOM   1099 C CD2   . LEU   A 1 158 ? -13.166 22.891 46.476 1 29.89  ? 139 LEU   A CD2   1 
ATOM   1100 N N     . LYS   A 1 159 ? -11.203 19.967 43.115 1 21.74  ? 140 LYS   A N     1 
ATOM   1101 C CA    . LYS   A 1 159 ? -10.914 19.391 41.819 1 21.71  ? 140 LYS   A CA    1 
ATOM   1102 C C     . LYS   A 1 159 ? -10.76  20.577 40.838 1 26.45  ? 140 LYS   A C     1 
ATOM   1103 O O     . LYS   A 1 159 ? -11.506 21.563 40.92  1 24.55  ? 140 LYS   A O     1 
ATOM   1104 C CB    . LYS   A 1 159 ? -12.096 18.507 41.379 1 23.4   ? 140 LYS   A CB    1 
ATOM   1105 C CG    . LYS   A 1 159 ? -11.935 17.87  39.998 1 33.07  ? 140 LYS   A CG    1 
ATOM   1106 C CD    . LYS   A 1 159 ? -11.474 16.432 40.11  1 44.17  ? 140 LYS   A CD    1 
ATOM   1107 C CE    . LYS   A 1 159 ? -11.624 15.728 38.792 1 57.36  ? 140 LYS   A CE    1 
ATOM   1108 N NZ    . LYS   A 1 159 ? -11.021 14.377 38.841 1 68.09  ? 140 LYS   A NZ    1 
ATOM   1109 N N     . CYS   A 1 160 ? -9.796  20.475 39.922 1 23.77  ? 141 CYS   A N     1 
ATOM   1110 C CA    . CYS   A 1 160 ? -9.579  21.503 38.909 1 24.07  ? 141 CYS   A CA    1 
ATOM   1111 C C     . CYS   A 1 160 ? -9.116  20.918 37.592 1 23.32  ? 141 CYS   A C     1 
ATOM   1112 O O     . CYS   A 1 160 ? -8.478  19.879 37.576 1 23     ? 141 CYS   A O     1 
ATOM   1113 C CB    . CYS   A 1 160 ? -8.61   22.567 39.409 1 26.12  ? 141 CYS   A CB    1 
ATOM   1114 S SG    . CYS   A 1 160 ? -6.879  22.036 39.458 1 30.87  ? 141 CYS   A SG    1 
ATOM   1115 N N     . ASP   A 1 161 ? -9.423  21.595 36.492 1 18.52  ? 142 ASP   A N     1 
ATOM   1116 C CA    . ASP   A 1 161 ? -8.961  21.22  35.175 1 18.03  ? 142 ASP   A CA    1 
ATOM   1117 C C     . ASP   A 1 161 ? -8.641  22.519 34.453 1 21.48  ? 142 ASP   A C     1 
ATOM   1118 O O     . ASP   A 1 161 ? -9.546  23.226 34.014 1 21.96  ? 142 ASP   A O     1 
ATOM   1119 C CB    . ASP   A 1 161 ? -9.985  20.351 34.417 1 19.64  ? 142 ASP   A CB    1 
ATOM   1120 C CG    . ASP   A 1 161 ? -9.522  19.845 33.057 1 22     ? 142 ASP   A CG    1 
ATOM   1121 O OD1   . ASP   A 1 161 ? -8.402  20.212 32.627 1 21.51  ? 142 ASP   A OD1   1 
ATOM   1122 O OD2   . ASP   A 1 161 ? -10.272 19.092 32.426 1 21.17  ? 142 ASP   A OD2   1 
ATOM   1123 N N     . VAL   A 1 162 ? -7.34   22.806 34.314 1 17.05  ? 143 VAL   A N     1 
ATOM   1124 C CA    . VAL   A 1 162 ? -6.789  24.02  33.698 1 16.24  ? 143 VAL   A CA    1 
ATOM   1125 C C     . VAL   A 1 162 ? -7.206  24.189 32.225 1 17.85  ? 143 VAL   A C     1 
ATOM   1126 O O     . VAL   A 1 162 ? -7.206  25.313 31.718 1 16.24  ? 143 VAL   A O     1 
ATOM   1127 C CB    . VAL   A 1 162 ? -5.241  24.134 33.887 1 18.86  ? 143 VAL   A CB    1 
ATOM   1128 C CG1   . VAL   A 1 162 ? -4.864  23.899 35.332 1 18.34  ? 143 VAL   A CG1   1 
ATOM   1129 C CG2   . VAL   A 1 162 ? -4.467  23.181 32.973 1 18.35  ? 143 VAL   A CG2   1 
ATOM   1130 N N     . THR   A 1 163 ? -7.56   23.076 31.552 1 15.74  ? 144 THR   A N     1 
ATOM   1131 C CA    . THR   A 1 163 ? -7.927  23.069 30.126 1 16.36  ? 144 THR   A CA    1 
ATOM   1132 C C     . THR   A 1 163 ? -9.34   23.584 29.87  1 20.03  ? 144 THR   A C     1 
ATOM   1133 O O     . THR   A 1 163 ? -9.663  23.936 28.73  1 19.76  ? 144 THR   A O     1 
ATOM   1134 C CB    . THR   A 1 163 ? -7.701  21.688 29.493 1 22.17  ? 144 THR   A CB    1 
ATOM   1135 O OG1   . THR   A 1 163 ? -8.657  20.769 30.015 1 21.23  ? 144 THR   A OG1   1 
ATOM   1136 C CG2   . THR   A 1 163 ? -6.301  21.172 29.704 1 18.76  ? 144 THR   A CG2   1 
ATOM   1137 N N     . GLN   A 1 164 ? -10.156 23.673 30.935 1 17.05  ? 145 GLN   A N     1 
ATOM   1138 C CA    . GLN   A 1 164 ? -11.548 24.116 30.875 1 17.05  ? 145 GLN   A CA    1 
ATOM   1139 C C     . GLN   A 1 164 ? -11.65  25.61  31.135 1 22.7   ? 145 GLN   A C     1 
ATOM   1140 O O     . GLN   A 1 164 ? -10.883 26.124 31.946 1 22.24  ? 145 GLN   A O     1 
ATOM   1141 C CB    . GLN   A 1 164 ? -12.402 23.346 31.906 1 18.07  ? 145 GLN   A CB    1 
ATOM   1142 C CG    . GLN   A 1 164 ? -12.356 21.805 31.79  1 20.98  ? 145 GLN   A CG    1 
ATOM   1143 C CD    . GLN   A 1 164 ? -12.644 21.252 30.408 1 27.32  ? 145 GLN   A CD    1 
ATOM   1144 O OE1   . GLN   A 1 164 ? -13.373 21.826 29.61  1 23.3   ? 145 GLN   A OE1   1 
ATOM   1145 N NE2   . GLN   A 1 164 ? -12.077 20.108 30.093 1 29.26  ? 145 GLN   A NE2   1 
ATOM   1146 N N     . SER   A 1 165 ? -12.629 26.296 30.49  1 19.97  ? 146 SER   A N     1 
ATOM   1147 C CA    . SER   A 1 165 ? -12.881 27.739 30.664 1 20.4   ? 146 SER   A CA    1 
ATOM   1148 C C     . SER   A 1 165 ? -13.243 28.077 32.129 1 24.14  ? 146 SER   A C     1 
ATOM   1149 O O     . SER   A 1 165 ? -12.955 29.174 32.601 1 23.92  ? 146 SER   A O     1 
ATOM   1150 C CB    . SER   A 1 165 ? -13.941 28.226 29.684 1 25.45  ? 146 SER   A CB    1 
ATOM   1151 O OG    . SER   A 1 165 ? -15.192 27.61  29.947 1 38.62  ? 146 SER   A OG    1 
ATOM   1152 N N     . GLN   A 1 166 ? -13.833 27.108 32.846 1 20.98  ? 147 GLN   A N     1 
ATOM   1153 C CA    . GLN   A 1 166 ? -14.126 27.17  34.276 1 21.08  ? 147 GLN   A CA    1 
ATOM   1154 C C     . GLN   A 1 166 ? -13.289 26.041 34.914 1 25.16  ? 147 GLN   A C     1 
ATOM   1155 O O     . GLN   A 1 166 ? -13.75  24.89  34.985 1 23.37  ? 147 GLN   A O     1 
ATOM   1156 C CB    . GLN   A 1 166 ? -15.623 26.981 34.583 1 22.34  ? 147 GLN   A CB    1 
ATOM   1157 C CG    . GLN   A 1 166 ? -16.506 28.119 34.102 1 34.85  ? 147 GLN   A CG    1 
ATOM   1158 C CD    . GLN   A 1 166 ? -17.434 27.623 33.031 1 64.71  ? 147 GLN   A CD    1 
ATOM   1159 O OE1   . GLN   A 1 166 ? -17.153 27.743 31.838 1 59.84  ? 147 GLN   A OE1   1 
ATOM   1160 N NE2   . GLN   A 1 166 ? -18.546 27.012 33.435 1 63.91  ? 147 GLN   A NE2   1 
ATOM   1161 N N     . PRO   A 1 167 ? -12.04  26.34  35.348 1 22.74  ? 148 PRO   A N     1 
ATOM   1162 C CA    . PRO   A 1 167 ? -11.185 25.278 35.913 1 21.7   ? 148 PRO   A CA    1 
ATOM   1163 C C     . PRO   A 1 167 ? -11.757 24.573 37.129 1 23.77  ? 148 PRO   A C     1 
ATOM   1164 O O     . PRO   A 1 167 ? -11.555 23.373 37.256 1 22.44  ? 148 PRO   A O     1 
ATOM   1165 C CB    . PRO   A 1 167 ? -9.859  25.996 36.217 1 23.37  ? 148 PRO   A CB    1 
ATOM   1166 C CG    . PRO   A 1 167 ? -9.873  27.2   35.361 1 28.37  ? 148 PRO   A CG    1 
ATOM   1167 C CD    . PRO   A 1 167 ? -11.316 27.627 35.311 1 24.15  ? 148 PRO   A CD    1 
ATOM   1168 N N     . LEU   A 1 168 ? -12.485 25.289 37.993 1 20.29  ? 149 LEU   A N     1 
ATOM   1169 C CA    . LEU   A 1 168 ? -13.077 24.707 39.205 1 20.83  ? 149 LEU   A CA    1 
ATOM   1170 C C     . LEU   A 1 168 ? -14.503 24.157 38.983 1 27.17  ? 149 LEU   A C     1 
ATOM   1171 O O     . LEU   A 1 168 ? -15.179 23.766 39.933 1 27.22  ? 149 LEU   A O     1 
ATOM   1172 C CB    . LEU   A 1 168 ? -13.015 25.71  40.379 1 20.99  ? 149 LEU   A CB    1 
ATOM   1173 C CG    . LEU   A 1 168 ? -11.613 26.225 40.727 1 25.87  ? 149 LEU   A CG    1 
ATOM   1174 C CD1   . LEU   A 1 168 ? -11.665 27.232 41.824 1 26.34  ? 149 LEU   A CD1   1 
ATOM   1175 C CD2   . LEU   A 1 168 ? -10.678 25.104 41.098 1 28.84  ? 149 LEU   A CD2   1 
ATOM   1176 N N     . GLY   A 1 169 ? -14.902 24.079 37.717 1 26.78  ? 150 GLY   A N     1 
ATOM   1177 C CA    . GLY   A 1 169 ? -16.191 23.547 37.289 1 27.83  ? 150 GLY   A CA    1 
ATOM   1178 C C     . GLY   A 1 169 ? -17.377 24.356 37.768 1 32.98  ? 150 GLY   A C     1 
ATOM   1179 O O     . GLY   A 1 169 ? -17.451 25.563 37.522 1 33.14  ? 150 GLY   A O     1 
ATOM   1180 N N     . ALA   A 1 170 ? -18.302 23.684 38.462 1 29.7   ? 151 ALA   A N     1 
ATOM   1181 C CA    . ALA   A 1 170 ? -19.521 24.284 38.998 1 29.36  ? 151 ALA   A CA    1 
ATOM   1182 C C     . ALA   A 1 170 ? -19.301 24.923 40.375 1 33.39  ? 151 ALA   A C     1 
ATOM   1183 O O     . ALA   A 1 170 ? -20.198 25.606 40.881 1 33.14  ? 151 ALA   A O     1 
ATOM   1184 C CB    . ALA   A 1 170 ? -20.627 23.24  39.064 1 29.73  ? 151 ALA   A CB    1 
ATOM   1185 N N     . VAL   A 1 171 ? -18.094 24.747 40.954 1 29.72  ? 152 VAL   A N     1 
ATOM   1186 C CA    . VAL   A 1 171 ? -17.746 25.275 42.276 1 28.59  ? 152 VAL   A CA    1 
ATOM   1187 C C     . VAL   A 1 171 ? -17.429 26.79  42.215 1 30.77  ? 152 VAL   A C     1 
ATOM   1188 O O     . VAL   A 1 171 ? -16.536 27.211 41.47  1 28.37  ? 152 VAL   A O     1 
ATOM   1189 C CB    . VAL   A 1 171 ? -16.636 24.446 42.985 1 32.63  ? 152 VAL   A CB    1 
ATOM   1190 C CG1   . VAL   A 1 171 ? -16.237 25.06  44.327 1 32.53  ? 152 VAL   A CG1   1 
ATOM   1191 C CG2   . VAL   A 1 171 ? -17.07  22.998 43.176 1 32.4   ? 152 VAL   A CG2   1 
ATOM   1192 N N     . PRO   A 1 172 ? -18.138 27.619 43.018 1 28.42  ? 153 PRO   A N     1 
ATOM   1193 C CA    . PRO   A 1 172 ? -17.849 29.058 43.009 1 28.44  ? 153 PRO   A CA    1 
ATOM   1194 C C     . PRO   A 1 172 ? -16.788 29.46  44.028 1 30.89  ? 153 PRO   A C     1 
ATOM   1195 O O     . PRO   A 1 172 ? -16.675 28.857 45.102 1 30.63  ? 153 PRO   A O     1 
ATOM   1196 C CB    . PRO   A 1 172 ? -19.202 29.691 43.359 1 30.42  ? 153 PRO   A CB    1 
ATOM   1197 C CG    . PRO   A 1 172 ? -19.95  28.624 44.13  1 34.48  ? 153 PRO   A CG    1 
ATOM   1198 C CD    . PRO   A 1 172 ? -19.241 27.302 43.954 1 30.19  ? 153 PRO   A CD    1 
ATOM   1199 N N     . LEU   A 1 173 ? -16.026 30.505 43.683 1 25.26  ? 154 LEU   A N     1 
ATOM   1200 C CA    . LEU   A 1 173 ? -15.028 31.112 44.549 1 24.02  ? 154 LEU   A CA    1 
ATOM   1201 C C     . LEU   A 1 173 ? -14.988 32.611 44.307 1 26.26  ? 154 LEU   A C     1 
ATOM   1202 O O     . LEU   A 1 173 ? -15.2   33.043 43.167 1 24.01  ? 154 LEU   A O     1 
ATOM   1203 C CB    . LEU   A 1 173 ? -13.622 30.521 44.33  1 24.17  ? 154 LEU   A CB    1 
ATOM   1204 C CG    . LEU   A 1 173 ? -13.232 29.273 45.139 1 29.05  ? 154 LEU   A CG    1 
ATOM   1205 C CD1   . LEU   A 1 173 ? -11.764 28.995 44.984 1 30.05  ? 154 LEU   A CD1   1 
ATOM   1206 C CD2   . LEU   A 1 173 ? -13.503 29.446 46.63  1 30.37  ? 154 LEU   A CD2   1 
ATOM   1207 N N     . PRO   A 1 174 ? -14.679 33.435 45.342 1 22.82  ? 155 PRO   A N     1 
ATOM   1208 C CA    . PRO   A 1 174 ? -14.516 34.871 45.088 1 23.04  ? 155 PRO   A CA    1 
ATOM   1209 C C     . PRO   A 1 174 ? -13.31  35.064 44.164 1 29.44  ? 155 PRO   A C     1 
ATOM   1210 O O     . PRO   A 1 174 ? -12.437 34.186 44.181 1 28.6   ? 155 PRO   A O     1 
ATOM   1211 C CB    . PRO   A 1 174 ? -14.192 35.446 46.472 1 24.31  ? 155 PRO   A CB    1 
ATOM   1212 C CG    . PRO   A 1 174 ? -14.552 34.39  47.446 1 28.15  ? 155 PRO   A CG    1 
ATOM   1213 C CD    . PRO   A 1 174 ? -14.356 33.102 46.745 1 23.73  ? 155 PRO   A CD    1 
ATOM   1214 N N     . PRO   A 1 175 ? -13.211 36.166 43.367 1 27.48  ? 156 PRO   A N     1 
ATOM   1215 C CA    . PRO   A 1 175 ? -12.014 36.356 42.543 1 27.11  ? 156 PRO   A CA    1 
ATOM   1216 C C     . PRO   A 1 175 ? -10.782 36.404 43.446 1 29.15  ? 156 PRO   A C     1 
ATOM   1217 O O     . PRO   A 1 175 ? -10.81  37.06  44.49  1 28.74  ? 156 PRO   A O     1 
ATOM   1218 C CB    . PRO   A 1 175 ? -12.281 37.683 41.825 1 28.44  ? 156 PRO   A CB    1 
ATOM   1219 C CG    . PRO   A 1 175 ? -13.739 37.877 41.894 1 33.26  ? 156 PRO   A CG    1 
ATOM   1220 C CD    . PRO   A 1 175 ? -14.137 37.305 43.208 1 29.33  ? 156 PRO   A CD    1 
ATOM   1221 N N     . ALA   A 1 176 ? -9.746  35.616 43.091 1 24.13  ? 157 ALA   A N     1 
ATOM   1222 C CA    . ALA   A 1 176 ? -8.518  35.506 43.881 1 22.1   ? 157 ALA   A CA    1 
ATOM   1223 C C     . ALA   A 1 176 ? -7.653  36.756 43.801 1 20.14  ? 157 ALA   A C     1 
ATOM   1224 O O     . ALA   A 1 176 ? -7.729  37.502 42.828 1 18.64  ? 157 ALA   A O     1 
ATOM   1225 C CB    . ALA   A 1 176 ? -7.715  34.291 43.434 1 22.68  ? 157 ALA   A CB    1 
ATOM   1226 N N     . ASP   A 1 177 ? -6.836  36.98  44.83  1 16.29  ? 158 ASP   A N     1 
ATOM   1227 C CA    . ASP   A 1 177 ? -5.859  38.069 44.851 1 16.82  ? 158 ASP   A CA    1 
ATOM   1228 C C     . ASP   A 1 177 ? -4.599  37.554 44.131 1 21.04  ? 158 ASP   A C     1 
ATOM   1229 O O     . ASP   A 1 177 ? -3.868  38.327 43.506 1 20.4   ? 158 ASP   A O     1 
ATOM   1230 C CB    . ASP   A 1 177 ? -5.527  38.467 46.299 1 18.42  ? 158 ASP   A CB    1 
ATOM   1231 C CG    . ASP   A 1 177 ? -6.75   39.01  47.02  1 27.59  ? 158 ASP   A CG    1 
ATOM   1232 O OD1   . ASP   A 1 177 ? -7.143  40.164 46.735 1 29.83  ? 158 ASP   A OD1   1 
ATOM   1233 O OD2   . ASP   A 1 177 ? -7.357  38.253 47.808 1 25.81  ? 158 ASP   A OD2   1 
ATOM   1234 N N     . CYS   A 1 178 ? -4.375  36.222 44.212 1 18.22  ? 159 CYS   A N     1 
ATOM   1235 C CA    . CYS   A 1 178 ? -3.249  35.545 43.586 1 18.33  ? 159 CYS   A CA    1 
ATOM   1236 C C     . CYS   A 1 178 ? -3.588  34.129 43.122 1 20.41  ? 159 CYS   A C     1 
ATOM   1237 O O     . CYS   A 1 178 ? -4.274  33.381 43.819 1 19.81  ? 159 CYS   A O     1 
ATOM   1238 C CB    . CYS   A 1 178 ? -2.027  35.556 44.508 1 18.94  ? 159 CYS   A CB    1 
ATOM   1239 S SG    . CYS   A 1 178 ? -0.57   34.696 43.845 1 23.03  ? 159 CYS   A SG    1 
ATOM   1240 N N     . VAL   A 1 179 ? -3.06   33.758 41.959 1 15.48  ? 160 VAL   A N     1 
ATOM   1241 C CA    . VAL   A 1 179 ? -3.18   32.395 41.445 1 15.05  ? 160 VAL   A CA    1 
ATOM   1242 C C     . VAL   A 1 179 ? -1.752  31.895 41.266 1 18.72  ? 160 VAL   A C     1 
ATOM   1243 O O     . VAL   A 1 179 ? -0.975  32.481 40.499 1 18.95  ? 160 VAL   A O     1 
ATOM   1244 C CB    . VAL   A 1 179 ? -4.067  32.244 40.174 1 17.83  ? 160 VAL   A CB    1 
ATOM   1245 C CG1   . VAL   A 1 179 ? -3.757  30.939 39.43  1 17.56  ? 160 VAL   A CG1   1 
ATOM   1246 C CG2   . VAL   A 1 179 ? -5.549  32.318 40.529 1 16.95  ? 160 VAL   A CG2   1 
ATOM   1247 N N     . LEU   A 1 180 ? -1.404  30.85  42.019 1 15.56  ? 161 LEU   A N     1 
ATOM   1248 C CA    . LEU   A 1 180 ? -0.088  30.221 41.993 1 15.29  ? 161 LEU   A CA    1 
ATOM   1249 C C     . LEU   A 1 180 ? -0.173  28.856 41.306 1 18.26  ? 161 LEU   A C     1 
ATOM   1250 O O     . LEU   A 1 180 ? -1.118  28.111 41.558 1 17.55  ? 161 LEU   A O     1 
ATOM   1251 C CB    . LEU   A 1 180 ? 0.416   30.069 43.448 1 15.19  ? 161 LEU   A CB    1 
ATOM   1252 C CG    . LEU   A 1 180 ? 1.611   29.142 43.745 1 17.94  ? 161 LEU   A CG    1 
ATOM   1253 C CD1   . LEU   A 1 180 ? 2.945   29.773 43.337 1 16.24  ? 161 LEU   A CD1   1 
ATOM   1254 C CD2   . LEU   A 1 180 ? 1.643   28.771 45.193 1 18.96  ? 161 LEU   A CD2   1 
ATOM   1255 N N     . SER   A 1 181 ? 0.818   28.515 40.459 1 13.8   ? 162 SER   A N     1 
ATOM   1256 C CA    . SER   A 1 181 ? 0.875   27.189 39.833 1 12.62  ? 162 SER   A CA    1 
ATOM   1257 C C     . SER   A 1 181 ? 2.326   26.717 39.649 1 16.69  ? 162 SER   A C     1 
ATOM   1258 O O     . SER   A 1 181 ? 3.026   27.217 38.763 1 15.34  ? 162 SER   A O     1 
ATOM   1259 C CB    . SER   A 1 181 ? 0.111   27.157 38.51  1 15.32  ? 162 SER   A CB    1 
ATOM   1260 O OG    . SER   A 1 181 ? 0.02    25.823 38.018 1 22.64  ? 162 SER   A OG    1 
ATOM   1261 N N     . THR   A 1 182 ? 2.756   25.721 40.456 1 13.63  ? 163 THR   A N     1 
ATOM   1262 C CA    . THR   A 1 182 ? 4.116   25.161 40.37  1 12.62  ? 163 THR   A CA    1 
ATOM   1263 C C     . THR   A 1 182 ? 4.14    23.79  39.681 1 14.83  ? 163 THR   A C     1 
ATOM   1264 O O     . THR   A 1 182 ? 3.481   22.867 40.152 1 15.42  ? 163 THR   A O     1 
ATOM   1265 C CB    . THR   A 1 182 ? 4.766   25.108 41.765 1 16.38  ? 163 THR   A CB    1 
ATOM   1266 O OG1   . THR   A 1 182 ? 4.055   24.171 42.594 1 13.91  ? 163 THR   A OG1   1 
ATOM   1267 C CG2   . THR   A 1 182 ? 4.787   26.482 42.45  1 12.36  ? 163 THR   A CG2   1 
ATOM   1268 N N     . LEU   A 1 183 ? 4.901   23.659 38.584 1 9.24   ? 164 LEU   A N     1 
ATOM   1269 C CA    . LEU   A 1 183 ? 5.11    22.4   37.847 1 9.95   ? 164 LEU   A CA    1 
ATOM   1270 C C     . LEU   A 1 183 ? 3.809   21.701 37.371 1 16.25  ? 164 LEU   A C     1 
ATOM   1271 O O     . LEU   A 1 183 ? 3.781   20.474 37.219 1 14.43  ? 164 LEU   A O     1 
ATOM   1272 C CB    . LEU   A 1 183 ? 6.004   21.422 38.657 1 9.48   ? 164 LEU   A CB    1 
ATOM   1273 C CG    . LEU   A 1 183 ? 7.434   21.92  38.873 1 12.86  ? 164 LEU   A CG    1 
ATOM   1274 C CD1   . LEU   A 1 183 ? 8.033   21.353 40.142 1 13.2   ? 164 LEU   A CD1   1 
ATOM   1275 C CD2   . LEU   A 1 183 ? 8.296   21.712 37.64  1 11.64  ? 164 LEU   A CD2   1 
ATOM   1276 N N     . CYS   A 1 184 ? 2.788   22.501 37.001 1 12.62  ? 165 CYS   A N     1 
ATOM   1277 C CA    . CYS   A 1 184 ? 1.527   21.949 36.559 1 12.33  ? 165 CYS   A CA    1 
ATOM   1278 C C     . CYS   A 1 184 ? 1.255   22.111 35.064 1 18     ? 165 CYS   A C     1 
ATOM   1279 O O     . CYS   A 1 184 ? 0.942   21.114 34.408 1 17.54  ? 165 CYS   A O     1 
ATOM   1280 C CB    . CYS   A 1 184 ? 0.386   22.522 37.402 1 12.77  ? 165 CYS   A CB    1 
ATOM   1281 S SG    . CYS   A 1 184 ? -1.267  22.203 36.726 1 15.93  ? 165 CYS   A SG    1 
ATOM   1282 N N     . LEU   A 1 185 ? 1.327   23.358 34.53  1 13.12  ? 166 LEU   A N     1 
ATOM   1283 C CA    . LEU   A 1 185 ? 0.947   23.676 33.15  1 13.08  ? 166 LEU   A CA    1 
ATOM   1284 C C     . LEU   A 1 185 ? 1.707   22.894 32.064 1 18.56  ? 166 LEU   A C     1 
ATOM   1285 O O     . LEU   A 1 185 ? 1.105   22.553 31.049 1 17.63  ? 166 LEU   A O     1 
ATOM   1286 C CB    . LEU   A 1 185 ? 1.027   25.195 32.885 1 12.93  ? 166 LEU   A CB    1 
ATOM   1287 C CG    . LEU   A 1 185 ? 0.246   26.122 33.851 1 16.98  ? 166 LEU   A CG    1 
ATOM   1288 C CD1   . LEU   A 1 185 ? 0.357   27.579 33.415 1 16.66  ? 166 LEU   A CD1   1 
ATOM   1289 C CD2   . LEU   A 1 185 ? -1.224  25.728 33.989 1 17.24  ? 166 LEU   A CD2   1 
ATOM   1290 N N     . ASP   A 1 186 ? 2.996   22.583 32.275 1 16.7   ? 167 ASP   A N     1 
ATOM   1291 C CA    . ASP   A 1 186 ? 3.777   21.8   31.301 1 17.31  ? 167 ASP   A CA    1 
ATOM   1292 C C     . ASP   A 1 186 ? 3.229   20.379 31.184 1 19.65  ? 167 ASP   A C     1 
ATOM   1293 O O     . ASP   A 1 186 ? 3.284   19.798 30.105 1 19.71  ? 167 ASP   A O     1 
ATOM   1294 C CB    . ASP   A 1 186 ? 5.252   21.712 31.716 1 19.52  ? 167 ASP   A CB    1 
ATOM   1295 C CG    . ASP   A 1 186 ? 6.112   22.927 31.45  1 32.97  ? 167 ASP   A CG    1 
ATOM   1296 O OD1   . ASP   A 1 186 ? 5.655   23.844 30.726 1 34.68  ? 167 ASP   A OD1   1 
ATOM   1297 O OD2   . ASP   A 1 186 ? 7.252   22.944 31.924 1 38.25  ? 167 ASP   A OD2   1 
ATOM   1298 N N     . ALA   A 1 187 ? 2.72    19.828 32.3   1 15.14  ? 168 ALA   A N     1 
ATOM   1299 C CA    . ALA   A 1 187 ? 2.159   18.478 32.403 1 14.76  ? 168 ALA   A CA    1 
ATOM   1300 C C     . ALA   A 1 187 ? 0.708   18.419 31.916 1 19.73  ? 168 ALA   A C     1 
ATOM   1301 O O     . ALA   A 1 187 ? 0.266   17.391 31.396 1 18.21  ? 168 ALA   A O     1 
ATOM   1302 C CB    . ALA   A 1 187 ? 2.226   18.007 33.851 1 15.09  ? 168 ALA   A CB    1 
ATOM   1303 N N     . ALA   A 1 188 ? -0.028  19.527 32.069 1 15.92  ? 169 ALA   A N     1 
ATOM   1304 C CA    . ALA   A 1 188 ? -1.442  19.586 31.747 1 15.36  ? 169 ALA   A CA    1 
ATOM   1305 C C     . ALA   A 1 188 ? -1.774  20.015 30.332 1 17.49  ? 169 ALA   A C     1 
ATOM   1306 O O     . ALA   A 1 188 ? -2.877  19.751 29.883 1 17.62  ? 169 ALA   A O     1 
ATOM   1307 C CB    . ALA   A 1 188 ? -2.141  20.495 32.751 1 16.26  ? 169 ALA   A CB    1 
ATOM   1308 N N     . CYS   A 1 189 ? -0.856  20.704 29.639 1 14.33  ? 170 CYS   A N     1 
ATOM   1309 C CA    . CYS   A 1 189 ? -1.101  21.248 28.311 1 13.25  ? 170 CYS   A CA    1 
ATOM   1310 C C     . CYS   A 1 189 ? -0.397  20.489 27.176 1 17.69  ? 170 CYS   A C     1 
ATOM   1311 O O     . CYS   A 1 189 ? 0.837   20.533 27.059 1 15.03  ? 170 CYS   A O     1 
ATOM   1312 C CB    . CYS   A 1 189 ? -0.783  22.74  28.284 1 12.92  ? 170 CYS   A CB    1 
ATOM   1313 S SG    . CYS   A 1 189 ? -1.601  23.676 29.604 1 16.25  ? 170 CYS   A SG    1 
ATOM   1314 N N     . PRO   A 1 190 ? -1.2    19.818 26.295 1 16.79  ? 171 PRO   A N     1 
ATOM   1315 C CA    . PRO   A 1 190 ? -0.606  19.036 25.194 1 16.48  ? 171 PRO   A CA    1 
ATOM   1316 C C     . PRO   A 1 190 ? 0.083   19.872 24.125 1 20.76  ? 171 PRO   A C     1 
ATOM   1317 O O     . PRO   A 1 190 ? 0.941   19.347 23.428 1 19.7   ? 171 PRO   A O     1 
ATOM   1318 C CB    . PRO   A 1 190 ? -1.797  18.263 24.607 1 18.34  ? 171 PRO   A CB    1 
ATOM   1319 C CG    . PRO   A 1 190 ? -2.883  18.348 25.639 1 23.5   ? 171 PRO   A CG    1 
ATOM   1320 C CD    . PRO   A 1 190 ? -2.669  19.658 26.324 1 18.85  ? 171 PRO   A CD    1 
ATOM   1321 N N     . ASP   A 1 191 ? -0.309  21.152 23.97  1 17.55  ? 172 ASP   A N     1 
ATOM   1322 C CA    . ASP   A 1 191 ? 0.276   22.032 22.953 1 19.2   ? 172 ASP   A CA    1 
ATOM   1323 C C     . ASP   A 1 191 ? 0.257   23.494 23.399 1 22.23  ? 172 ASP   A C     1 
ATOM   1324 O O     . ASP   A 1 191 ? -0.386  23.808 24.4   1 19.81  ? 172 ASP   A O     1 
ATOM   1325 C CB    . ASP   A 1 191 ? -0.436  21.842 21.584 1 21.18  ? 172 ASP   A CB    1 
ATOM   1326 C CG    . ASP   A 1 191 ? -1.959  21.911 21.632 1 29.75  ? 172 ASP   A CG    1 
ATOM   1327 O OD1   . ASP   A 1 191 ? -2.494  22.862 22.244 1 28.83  ? 172 ASP   A OD1   1 
ATOM   1328 O OD2   . ASP   A 1 191 ? -2.617  21.033 21.018 1 36.18  ? 172 ASP   A OD2   1 
ATOM   1329 N N     . LEU   A 1 192 ? 0.953   24.379 22.644 1 21.17  ? 173 LEU   A N     1 
ATOM   1330 C CA    . LEU   A 1 192 ? 1.032   25.819 22.91  1 22.1   ? 173 LEU   A CA    1 
ATOM   1331 C C     . LEU   A 1 192 ? -0.361  26.502 22.888 1 24.86  ? 173 LEU   A C     1 
ATOM   1332 O O     . LEU   A 1 192 ? -0.651  27.204 23.855 1 23.75  ? 173 LEU   A O     1 
ATOM   1333 C CB    . LEU   A 1 192 ? 2.053   26.516 21.985 1 22.61  ? 173 LEU   A CB    1 
ATOM   1334 C CG    . LEU   A 1 192 ? 2.489   27.954 22.331 1 28.06  ? 173 LEU   A CG    1 
ATOM   1335 C CD1   . LEU   A 1 192 ? 2.847   28.117 23.822 1 28.21  ? 173 LEU   A CD1   1 
ATOM   1336 C CD2   . LEU   A 1 192 ? 3.673   28.376 21.473 1 30.71  ? 173 LEU   A CD2   1 
ATOM   1337 N N     . PRO   A 1 193 ? -1.276  26.268 21.897 1 21.28  ? 174 PRO   A N     1 
ATOM   1338 C CA    . PRO   A 1 193 ? -2.616  26.866 21.999 1 20.76  ? 174 PRO   A CA    1 
ATOM   1339 C C     . PRO   A 1 193 ? -3.332  26.514 23.316 1 21.48  ? 174 PRO   A C     1 
ATOM   1340 O O     . PRO   A 1 193 ? -3.893  27.414 23.939 1 20.51  ? 174 PRO   A O     1 
ATOM   1341 C CB    . PRO   A 1 193 ? -3.35   26.302 20.771 1 22.92  ? 174 PRO   A CB    1 
ATOM   1342 C CG    . PRO   A 1 193 ? -2.261  25.997 19.8   1 27.44  ? 174 PRO   A CG    1 
ATOM   1343 C CD    . PRO   A 1 193 ? -1.155  25.47  20.656 1 23.01  ? 174 PRO   A CD    1 
ATOM   1344 N N     . THR   A 1 194 ? -3.267  25.236 23.776 1 15.35  ? 175 THR   A N     1 
ATOM   1345 C CA    . THR   A 1 194 ? -3.868  24.83  25.069 1 14.37  ? 175 THR   A CA    1 
ATOM   1346 C C     . THR   A 1 194 ? -3.192  25.568 26.234 1 16.01  ? 175 THR   A C     1 
ATOM   1347 O O     . THR   A 1 194 ? -3.868  25.958 27.186 1 13.64  ? 175 THR   A O     1 
ATOM   1348 C CB    . THR   A 1 194 ? -3.81   23.297 25.293 1 20.16  ? 175 THR   A CB    1 
ATOM   1349 O OG1   . THR   A 1 194 ? -4.381  22.624 24.17  1 22.52  ? 175 THR   A OG1   1 
ATOM   1350 C CG2   . THR   A 1 194 ? -4.558  22.862 26.542 1 17.81  ? 175 THR   A CG2   1 
ATOM   1351 N N     . TYR   A 1 195 ? -1.861  25.734 26.154 1 13.43  ? 176 TYR   A N     1 
ATOM   1352 C CA    . TYR   A 1 195 ? -1.066  26.42  27.177 1 13.48  ? 176 TYR   A CA    1 
ATOM   1353 C C     . TYR   A 1 195 ? -1.544  27.868 27.362 1 19.03  ? 176 TYR   A C     1 
ATOM   1354 O O     . TYR   A 1 195 ? -1.828  28.264 28.492 1 16.58  ? 176 TYR   A O     1 
ATOM   1355 C CB    . TYR   A 1 195 ? 0.425   26.358 26.817 1 14.33  ? 176 TYR   A CB    1 
ATOM   1356 C CG    . TYR   A 1 195 ? 1.336   26.864 27.91  1 15.47  ? 176 TYR   A CG    1 
ATOM   1357 C CD1   . TYR   A 1 195 ? 1.693   26.051 28.978 1 17.16  ? 176 TYR   A CD1   1 
ATOM   1358 C CD2   . TYR   A 1 195 ? 1.836   28.165 27.883 1 16.26  ? 176 TYR   A CD2   1 
ATOM   1359 C CE1   . TYR   A 1 195 ? 2.521   26.519 29.997 1 18.21  ? 176 TYR   A CE1   1 
ATOM   1360 C CE2   . TYR   A 1 195 ? 2.656   28.647 28.903 1 16.33  ? 176 TYR   A CE2   1 
ATOM   1361 C CZ    . TYR   A 1 195 ? 2.997   27.82  29.957 1 18.96  ? 176 TYR   A CZ    1 
ATOM   1362 O OH    . TYR   A 1 195 ? 3.786   28.292 30.97  1 18.22  ? 176 TYR   A OH    1 
ATOM   1363 N N     . CYS   A 1 196 ? -1.661  28.641 26.244 1 17.65  ? 177 CYS   A N     1 
ATOM   1364 C CA    . CYS   A 1 196 ? -2.145  30.024 26.283 1 18.06  ? 177 CYS   A CA    1 
ATOM   1365 C C     . CYS   A 1 196 ? -3.589  30.036 26.752 1 20.37  ? 177 CYS   A C     1 
ATOM   1366 O O     . CYS   A 1 196 ? -3.939  30.857 27.598 1 19.44  ? 177 CYS   A O     1 
ATOM   1367 C CB    . CYS   A 1 196 ? -1.972  30.721 24.933 1 18.93  ? 177 CYS   A CB    1 
ATOM   1368 S SG    . CYS   A 1 196 ? -2.6    32.427 24.895 1 23.14  ? 177 CYS   A SG    1 
ATOM   1369 N N     . ARG   A 1 197 ? -4.402  29.065 26.289 1 17.89  ? 178 ARG   A N     1 
ATOM   1370 C CA    . ARG   A 1 197 ? -5.798  28.939 26.73  1 17.85  ? 178 ARG   A CA    1 
ATOM   1371 C C     . ARG   A 1 197 ? -5.878  28.703 28.226 1 17.23  ? 178 ARG   A C     1 
ATOM   1372 O O     . ARG   A 1 197 ? -6.717  29.317 28.866 1 16.05  ? 178 ARG   A O     1 
ATOM   1373 C CB    . ARG   A 1 197 ? -6.551  27.807 25.997 1 21.76  ? 178 ARG   A CB    1 
ATOM   1374 C CG    . ARG   A 1 197 ? -7.023  28.152 24.594 1 41.25  ? 178 ARG   A CG    1 
ATOM   1375 C CD    . ARG   A 1 197 ? -8.148  27.252 24.084 1 57.94  ? 178 ARG   A CD    1 
ATOM   1376 N NE    . ARG   A 1 197 ? -8.005  25.841 24.464 1 69.76  ? 178 ARG   A NE    1 
ATOM   1377 C CZ    . ARG   A 1 197 ? -7.284  24.939 23.803 1 84.68  ? 178 ARG   A CZ    1 
ATOM   1378 N NH1   . ARG   A 1 197 ? -7.219  23.687 24.235 1 74.5   ? 178 ARG   A NH1   1 
ATOM   1379 N NH2   . ARG   A 1 197 ? -6.61   25.286 22.711 1 68.32  ? 178 ARG   A NH2   1 
ATOM   1380 N N     . ALA   A 1 198 ? -4.998  27.844 28.795 1 12.97  ? 179 ALA   A N     1 
ATOM   1381 C CA    . ALA   A 1 198 ? -5.002  27.544 30.236 1 12.84  ? 179 ALA   A CA    1 
ATOM   1382 C C     . ALA   A 1 198 ? -4.651  28.776 31.053 1 17.48  ? 179 ALA   A C     1 
ATOM   1383 O O     . ALA   A 1 198 ? -5.193  28.968 32.149 1 16.56  ? 179 ALA   A O     1 
ATOM   1384 C CB    . ALA   A 1 198 ? -4.049  26.407 30.556 1 13.51  ? 179 ALA   A CB    1 
ATOM   1385 N N     . LEU   A 1 199 ? -3.753  29.623 30.52  1 14.3   ? 180 LEU   A N     1 
ATOM   1386 C CA    . LEU   A 1 199 ? -3.376  30.874 31.196 1 14.78  ? 180 LEU   A CA    1 
ATOM   1387 C C     . LEU   A 1 199 ? -4.585  31.808 31.277 1 19.09  ? 180 LEU   A C     1 
ATOM   1388 O O     . LEU   A 1 199 ? -4.743  32.49  32.278 1 18.59  ? 180 LEU   A O     1 
ATOM   1389 C CB    . LEU   A 1 199 ? -2.212  31.571 30.472 1 14.64  ? 180 LEU   A CB    1 
ATOM   1390 C CG    . LEU   A 1 199 ? -0.859  30.843 30.511 1 18.61  ? 180 LEU   A CG    1 
ATOM   1391 C CD1   . LEU   A 1 199 ? 0.166   31.551 29.653 1 18.72  ? 180 LEU   A CD1   1 
ATOM   1392 C CD2   . LEU   A 1 199 ? -0.357  30.715 31.906 1 16.46  ? 180 LEU   A CD2   1 
ATOM   1393 N N     . ARG   A 1 200 ? -5.434  31.825 30.219 1 17.06  ? 181 ARG   A N     1 
ATOM   1394 C CA    . ARG   A 1 200 ? -6.652  32.635 30.161 1 16.81  ? 181 ARG   A CA    1 
ATOM   1395 C C     . ARG   A 1 200 ? -7.65   32.079 31.146 1 20.37  ? 181 ARG   A C     1 
ATOM   1396 O O     . ARG   A 1 200 ? -8.304  32.851 31.816 1 20.75  ? 181 ARG   A O     1 
ATOM   1397 C CB    . ARG   A 1 200 ? -7.263  32.655 28.748 1 17.23  ? 181 ARG   A CB    1 
ATOM   1398 C CG    . ARG   A 1 200 ? -6.44   33.424 27.723 1 18.45  ? 181 ARG   A CG    1 
ATOM   1399 C CD    . ARG   A 1 200 ? -7.323  33.904 26.595 1 20.04  ? 181 ARG   A CD    1 
ATOM   1400 N NE    . ARG   A 1 200 ? -6.616  33.856 25.32  1 24.35  ? 181 ARG   A NE    1 
ATOM   1401 C CZ    . ARG   A 1 200 ? -6.305  34.912 24.579 1 29.7   ? 181 ARG   A CZ    1 
ATOM   1402 N NH1   . ARG   A 1 200 ? -6.638  36.134 24.978 1 17.77  ? 181 ARG   A NH1   1 
ATOM   1403 N NH2   . ARG   A 1 200 ? -5.663  34.754 23.429 1 18.24  ? 181 ARG   A NH2   1 
ATOM   1404 N N     . ASN   A 1 201 ? -7.741  30.744 31.262 1 17.73  ? 182 ASN   A N     1 
ATOM   1405 C CA    . ASN   A 1 201 ? -8.631  30.039 32.193 1 17.34  ? 182 ASN   A CA    1 
ATOM   1406 C C     . ASN   A 1 201 ? -8.248  30.296 33.643 1 21.01  ? 182 ASN   A C     1 
ATOM   1407 O O     . ASN   A 1 201 ? -9.133  30.383 34.497 1 22.18  ? 182 ASN   A O     1 
ATOM   1408 C CB    . ASN   A 1 201 ? -8.675  28.527 31.879 1 16.31  ? 182 ASN   A CB    1 
ATOM   1409 C CG    . ASN   A 1 201 ? -9.144  28.218 30.486 1 25.91  ? 182 ASN   A CG    1 
ATOM   1410 O OD1   . ASN   A 1 201 ? -9.857  29.003 29.86  1 19.13  ? 182 ASN   A OD1   1 
ATOM   1411 N ND2   . ASN   A 1 201 ? -8.715  27.083 29.944 1 15.44  ? 182 ASN   A ND2   1 
ATOM   1412 N N     . LEU   A 1 202 ? -6.942  30.432 33.936 1 15.8   ? 183 LEU   A N     1 
ATOM   1413 C CA    . LEU   A 1 202 ? -6.503  30.76  35.291 1 15.19  ? 183 LEU   A CA    1 
ATOM   1414 C C     . LEU   A 1 202 ? -6.828  32.22  35.634 1 18.51  ? 183 LEU   A C     1 
ATOM   1415 O O     . LEU   A 1 202 ? -7.096  32.524 36.79  1 17.02  ? 183 LEU   A O     1 
ATOM   1416 C CB    . LEU   A 1 202 ? -5.001  30.458 35.527 1 15.55  ? 183 LEU   A CB    1 
ATOM   1417 C CG    . LEU   A 1 202 ? -4.512  28.998 35.353 1 21.24  ? 183 LEU   A CG    1 
ATOM   1418 C CD1   . LEU   A 1 202 ? -3.079  28.832 35.852 1 21.36  ? 183 LEU   A CD1   1 
ATOM   1419 C CD2   . LEU   A 1 202 ? -5.448  27.993 36.002 1 26.27  ? 183 LEU   A CD2   1 
ATOM   1420 N N     . GLY   A 1 203 ? -6.828  33.093 34.624 1 16.7   ? 184 GLY   A N     1 
ATOM   1421 C CA    . GLY   A 1 203 ? -7.158  34.511 34.76  1 16.76  ? 184 GLY   A CA    1 
ATOM   1422 C C     . GLY   A 1 203 ? -8.596  34.756 35.151 1 22.27  ? 184 GLY   A C     1 
ATOM   1423 O O     . GLY   A 1 203 ? -8.89   35.737 35.838 1 21.75  ? 184 GLY   A O     1 
ATOM   1424 N N     . SER   A 1 204 ? -9.511  33.841 34.744 1 20.14  ? 185 SER   A N     1 
ATOM   1425 C CA    . SER   A 1 204 ? -10.939 33.913 35.091 1 18.98  ? 185 SER   A CA    1 
ATOM   1426 C C     . SER   A 1 204 ? -11.153 33.682 36.597 1 22.55  ? 185 SER   A C     1 
ATOM   1427 O O     . SER   A 1 204 ? -12.2   34.049 37.127 1 21.84  ? 185 SER   A O     1 
ATOM   1428 C CB    . SER   A 1 204 ? -11.756 32.935 34.248 1 20.9   ? 185 SER   A CB    1 
ATOM   1429 O OG    . SER   A 1 204 ? -11.515 31.578 34.584 1 22.37  ? 185 SER   A OG    1 
ATOM   1430 N N     . LEU   A 1 205 ? -10.136 33.126 37.298 1 18.54  ? 186 LEU   A N     1 
ATOM   1431 C CA    . LEU   A 1 205 ? -10.188 32.917 38.756 1 17.69  ? 186 LEU   A CA    1 
ATOM   1432 C C     . LEU   A 1 205 ? -9.538  34.113 39.45  1 24.61  ? 186 LEU   A C     1 
ATOM   1433 O O     . LEU   A 1 205 ? -9.514  34.18  40.682 1 23.66  ? 186 LEU   A O     1 
ATOM   1434 C CB    . LEU   A 1 205 ? -9.422  31.644 39.154 1 17.33  ? 186 LEU   A CB    1 
ATOM   1435 C CG    . LEU   A 1 205 ? -9.852  30.327 38.483 1 21.26  ? 186 LEU   A CG    1 
ATOM   1436 C CD1   . LEU   A 1 205 ? -8.808  29.269 38.686 1 21.12  ? 186 LEU   A CD1   1 
ATOM   1437 C CD2   . LEU   A 1 205 ? -11.179 29.845 39.046 1 23.22  ? 186 LEU   A CD2   1 
ATOM   1438 N N     . LEU   A 1 206 ? -8.974  35.044 38.653 1 23.24  ? 187 LEU   A N     1 
ATOM   1439 C CA    . LEU   A 1 206 ? -8.258  36.194 39.193 1 23.24  ? 187 LEU   A CA    1 
ATOM   1440 C C     . LEU   A 1 206 ? -9.057  37.473 39.111 1 25.7   ? 187 LEU   A C     1 
ATOM   1441 O O     . LEU   A 1 206 ? -9.685  37.753 38.082 1 23.19  ? 187 LEU   A O     1 
ATOM   1442 C CB    . LEU   A 1 206 ? -6.925  36.412 38.444 1 22.84  ? 187 LEU   A CB    1 
ATOM   1443 C CG    . LEU   A 1 206 ? -5.642  35.893 39.059 1 26.93  ? 187 LEU   A CG    1 
ATOM   1444 C CD1   . LEU   A 1 206 ? -4.476  36.167 38.13  1 25.8   ? 187 LEU   A CD1   1 
ATOM   1445 C CD2   . LEU   A 1 206 ? -5.39   36.488 40.442 1 26.52  ? 187 LEU   A CD2   1 
ATOM   1446 N N     . LYS   A 1 207 ? -8.919  38.298 40.167 1 23.38  ? 188 LYS   A N     1 
ATOM   1447 C CA    . LYS   A 1 207 ? -9.51   39.625 40.25  1 24.27  ? 188 LYS   A CA    1 
ATOM   1448 C C     . LYS   A 1 207 ? -8.725  40.518 39.283 1 30.97  ? 188 LYS   A C     1 
ATOM   1449 O O     . LYS   A 1 207 ? -7.531  40.247 39.087 1 31.89  ? 188 LYS   A O     1 
ATOM   1450 C CB    . LYS   A 1 207 ? -9.442  40.174 41.7   1 26.45  ? 188 LYS   A CB    1 
ATOM   1451 C CG    . LYS   A 1 207 ? -8.044  40.538 42.211 1 36.28  ? 188 LYS   A CG    1 
ATOM   1452 C CD    . LYS   A 1 207 ? -7.993  41.963 42.727 1 45.39  ? 188 LYS   A CD    1 
ATOM   1453 C CE    . LYS   A 1 207 ? -7.722  42.054 44.206 1 46.16  ? 188 LYS   A CE    1 
ATOM   1454 N NZ    . LYS   A 1 207 ? -6.276  41.92  44.53  1 40     ? 188 LYS   A NZ    1 
ATOM   1455 N N     . PRO   A 1 208 ? -9.327  41.565 38.653 1 27.46  ? 189 PRO   A N     1 
ATOM   1456 C CA    . PRO   A 1 208 ? -8.519  42.433 37.771 1 27     ? 189 PRO   A CA    1 
ATOM   1457 C C     . PRO   A 1 208 ? -7.318  42.979 38.551 1 28.44  ? 189 PRO   A C     1 
ATOM   1458 O O     . PRO   A 1 208 ? -7.445  43.257 39.748 1 25.78  ? 189 PRO   A O     1 
ATOM   1459 C CB    . PRO   A 1 208 ? -9.497  43.536 37.331 1 28.9   ? 189 PRO   A CB    1 
ATOM   1460 C CG    . PRO   A 1 208 ? -10.659 43.427 38.217 1 33.81  ? 189 PRO   A CG    1 
ATOM   1461 C CD    . PRO   A 1 208 ? -10.723 42.039 38.756 1 29.3   ? 189 PRO   A CD    1 
ATOM   1462 N N     . GLY   A 1 209 ? -6.147  42.986 37.917 1 25.1   ? 190 GLY   A N     1 
ATOM   1463 C CA    . GLY   A 1 209 ? -4.908  43.413 38.566 1 24.75  ? 190 GLY   A CA    1 
ATOM   1464 C C     . GLY   A 1 209 ? -4.328  42.399 39.543 1 27.35  ? 190 GLY   A C     1 
ATOM   1465 O O     . GLY   A 1 209 ? -3.332  42.689 40.208 1 25.88  ? 190 GLY   A O     1 
ATOM   1466 N N     . GLY   A 1 210 ? -4.94   41.21  39.626 1 23.33  ? 191 GLY   A N     1 
ATOM   1467 C CA    . GLY   A 1 210 ? -4.481  40.133 40.499 1 22.54  ? 191 GLY   A CA    1 
ATOM   1468 C C     . GLY   A 1 210 ? -3.162  39.54  40.037 1 24.8   ? 191 GLY   A C     1 
ATOM   1469 O O     . GLY   A 1 210 ? -2.779  39.702 38.871 1 24.4   ? 191 GLY   A O     1 
ATOM   1470 N N     . PHE   A 1 211 ? -2.459  38.847 40.951 1 20.2   ? 192 PHE   A N     1 
ATOM   1471 C CA    . PHE   A 1 211 ? -1.157  38.243 40.676 1 19.73  ? 192 PHE   A CA    1 
ATOM   1472 C C     . PHE   A 1 211 ? -1.199  36.813 40.136 1 20.43  ? 192 PHE   A C     1 
ATOM   1473 O O     . PHE   A 1 211 ? -1.932  35.957 40.632 1 18.47  ? 192 PHE   A O     1 
ATOM   1474 C CB    . PHE   A 1 211 ? -0.265  38.271 41.931 1 22.49  ? 192 PHE   A CB    1 
ATOM   1475 C CG    . PHE   A 1 211 ? 0.29    39.619 42.324 1 24.98  ? 192 PHE   A CG    1 
ATOM   1476 C CD1   . PHE   A 1 211 ? 1.356   40.179 41.63  1 29.25  ? 192 PHE   A CD1   1 
ATOM   1477 C CD2   . PHE   A 1 211 ? -0.226  40.31  43.416 1 28.37  ? 192 PHE   A CD2   1 
ATOM   1478 C CE1   . PHE   A 1 211 ? 1.891   41.42  42.012 1 31.16  ? 192 PHE   A CE1   1 
ATOM   1479 C CE2   . PHE   A 1 211 ? 0.314   41.546 43.806 1 31.74  ? 192 PHE   A CE2   1 
ATOM   1480 C CZ    . PHE   A 1 211 ? 1.369   42.091 43.103 1 30.1   ? 192 PHE   A CZ    1 
ATOM   1481 N N     . LEU   A 1 212 ? -0.357  36.556 39.146 1 17.84  ? 193 LEU   A N     1 
ATOM   1482 C CA    . LEU   A 1 212 ? -0.172  35.226 38.566 1 17.76  ? 193 LEU   A CA    1 
ATOM   1483 C C     . LEU   A 1 212 ? 1.269   34.817 38.878 1 19.72  ? 193 LEU   A C     1 
ATOM   1484 O O     . LEU   A 1 212 ? 2.201   35.53  38.51  1 19.51  ? 193 LEU   A O     1 
ATOM   1485 C CB    . LEU   A 1 212 ? -0.429  35.228 37.036 1 17.53  ? 193 LEU   A CB    1 
ATOM   1486 C CG    . LEU   A 1 212 ? -0.237  33.886 36.32  1 21.29  ? 193 LEU   A CG    1 
ATOM   1487 C CD1   . LEU   A 1 212 ? -1.365  32.907 36.645 1 21.67  ? 193 LEU   A CD1   1 
ATOM   1488 C CD2   . LEU   A 1 212 ? -0.047  34.078 34.815 1 21.55  ? 193 LEU   A CD2   1 
ATOM   1489 N N     . VAL   A 1 213 ? 1.443   33.724 39.616 1 14.58  ? 194 VAL   A N     1 
ATOM   1490 C CA    . VAL   A 1 213 ? 2.766   33.221 39.953 1 14.69  ? 194 VAL   A CA    1 
ATOM   1491 C C     . VAL   A 1 213 ? 2.909   31.831 39.294 1 17.41  ? 194 VAL   A C     1 
ATOM   1492 O O     . VAL   A 1 213 ? 2.148   30.93  39.621 1 16.92  ? 194 VAL   A O     1 
ATOM   1493 C CB    . VAL   A 1 213 ? 3.023   33.176 41.495 1 19.18  ? 194 VAL   A CB    1 
ATOM   1494 C CG1   . VAL   A 1 213 ? 4.427   32.648 41.804 1 18.94  ? 194 VAL   A CG1   1 
ATOM   1495 C CG2   . VAL   A 1 213 ? 2.827   34.549 42.133 1 19.2   ? 194 VAL   A CG2   1 
ATOM   1496 N N     . ILE   A 1 214 ? 3.845   31.674 38.347 1 14.02  ? 195 ILE   A N     1 
ATOM   1497 C CA    . ILE   A 1 214 ? 4.076   30.38  37.674 1 12.68  ? 195 ILE   A CA    1 
ATOM   1498 C C     . ILE   A 1 214 ? 5.542   29.97  37.732 1 15.03  ? 195 ILE   A C     1 
ATOM   1499 O O     . ILE   A 1 214 ? 6.439   30.753 37.381 1 13.41  ? 195 ILE   A O     1 
ATOM   1500 C CB    . ILE   A 1 214 ? 3.506   30.352 36.223 1 16.09  ? 195 ILE   A CB    1 
ATOM   1501 C CG1   . ILE   A 1 214 ? 1.966   30.522 36.243 1 17.28  ? 195 ILE   A CG1   1 
ATOM   1502 C CG2   . ILE   A 1 214 ? 3.903   29.047 35.461 1 16.5   ? 195 ILE   A CG2   1 
ATOM   1503 C CD1   . ILE   A 1 214 ? 1.421   30.863 34.983 1 31.2   ? 195 ILE   A CD1   1 
ATOM   1504 N N     . MET   A 1 215 ? 5.786   28.729 38.171 1 12.62  ? 196 MET   A N     1 
ATOM   1505 C CA    . MET   A 1 215 ? 7.125   28.139 38.166 1 12.61  ? 196 MET   A CA    1 
ATOM   1506 C C     . MET   A 1 215 ? 7.011   26.806 37.468 1 16.06  ? 196 MET   A C     1 
ATOM   1507 O O     . MET   A 1 215 ? 6.106   26.046 37.793 1 15.75  ? 196 MET   A O     1 
ATOM   1508 C CB    . MET   A 1 215 ? 7.684   27.965 39.578 1 15.32  ? 196 MET   A CB    1 
ATOM   1509 C CG    . MET   A 1 215 ? 7.643   29.243 40.386 1 19.15  ? 196 MET   A CG    1 
ATOM   1510 S SD    . MET   A 1 215 ? 8.372   29.167 42.024 1 23.39  ? 196 MET   A SD    1 
ATOM   1511 C CE    . MET   A 1 215 ? 7.631   27.85  42.648 1 21.08  ? 196 MET   A CE    1 
ATOM   1512 N N     . ASP   A 1 216 ? 7.896   26.516 36.494 1 11.53  ? 197 ASP   A N     1 
ATOM   1513 C CA    . ASP   A 1 216 ? 7.822   25.236 35.764 1 11.35  ? 197 ASP   A CA    1 
ATOM   1514 C C     . ASP   A 1 216 ? 9.124   24.933 35.056 1 16.3   ? 197 ASP   A C     1 
ATOM   1515 O O     . ASP   A 1 216 ? 10.047  25.744 35.052 1 15.63  ? 197 ASP   A O     1 
ATOM   1516 C CB    . ASP   A 1 216 ? 6.66    25.26  34.73  1 12.48  ? 197 ASP   A CB    1 
ATOM   1517 C CG    . ASP   A 1 216 ? 5.831   23.996 34.619 1 16.24  ? 197 ASP   A CG    1 
ATOM   1518 O OD1   . ASP   A 1 216 ? 6.4     22.886 34.793 1 15.62  ? 197 ASP   A OD1   1 
ATOM   1519 O OD2   . ASP   A 1 216 ? 4.645   24.103 34.25  1 18.72  ? 197 ASP   A OD2   1 
ATOM   1520 N N     . ALA   A 1 217 ? 9.178   23.767 34.427 1 13.65  ? 198 ALA   A N     1 
ATOM   1521 C CA    . ALA   A 1 217 ? 10.342  23.286 33.705 1 12.55  ? 198 ALA   A CA    1 
ATOM   1522 C C     . ALA   A 1 217 ? 10.445  23.891 32.32  1 15.55  ? 198 ALA   A C     1 
ATOM   1523 O O     . ALA   A 1 217 ? 9.446   24.196 31.661 1 15.29  ? 198 ALA   A O     1 
ATOM   1524 C CB    . ALA   A 1 217 ? 10.286  21.767 33.606 1 12.9   ? 198 ALA   A CB    1 
ATOM   1525 N N     . LEU   A 1 218 ? 11.668  24.044 31.863 1 11.54  ? 199 LEU   A N     1 
ATOM   1526 C CA    . LEU   A 1 218 ? 11.899  24.532 30.513 1 10.33  ? 199 LEU   A CA    1 
ATOM   1527 C C     . LEU   A 1 218 ? 12.345  23.381 29.624 1 15.3   ? 199 LEU   A C     1 
ATOM   1528 O O     . LEU   A 1 218 ? 13.155  22.559 30.043 1 15.33  ? 199 LEU   A O     1 
ATOM   1529 C CB    . LEU   A 1 218 ? 12.968  25.637 30.517 1 9.54   ? 199 LEU   A CB    1 
ATOM   1530 C CG    . LEU   A 1 218 ? 12.527  27.016 31.014 1 13.16  ? 199 LEU   A CG    1 
ATOM   1531 C CD1   . LEU   A 1 218 ? 13.727  27.922 31.211 1 12.32  ? 199 LEU   A CD1   1 
ATOM   1532 C CD2   . LEU   A 1 218 ? 11.503  27.663 30.055 1 14.74  ? 199 LEU   A CD2   1 
ATOM   1533 N N     . LYS   A 1 219 ? 11.801  23.315 28.405 1 14.85  ? 200 LYS   A N     1 
ATOM   1534 C CA    . LYS   A 1 219 ? 12.197  22.381 27.346 1 15.31  ? 200 LYS   A CA    1 
ATOM   1535 C C     . LYS   A 1 219 ? 12.21   20.904 27.757 1 19.5   ? 200 LYS   A C     1 
ATOM   1536 O O     . LYS   A 1 219 ? 13.068  20.14  27.317 1 17.87  ? 200 LYS   A O     1 
ATOM   1537 C CB    . LYS   A 1 219 ? 13.563  22.805 26.764 1 17.86  ? 200 LYS   A CB    1 
ATOM   1538 C CG    . LYS   A 1 219 ? 13.508  24.151 26.046 1 20.02  ? 200 LYS   A CG    1 
ATOM   1539 C CD    . LYS   A 1 219 ? 14.884  24.707 25.784 1 28.3   ? 200 LYS   A CD    1 
ATOM   1540 C CE    . LYS   A 1 219 ? 14.868  25.713 24.655 1 38.21  ? 200 LYS   A CE    1 
ATOM   1541 N NZ    . LYS   A 1 219 ? 16.217  26.286 24.402 1 45.23  ? 200 LYS   A NZ    1 
ATOM   1542 N N     . SER   A 1 220 ? 11.224  20.502 28.565 1 17.18  ? 201 SER   A N     1 
ATOM   1543 C CA    . SER   A 1 220 ? 11.057  19.119 29.007 1 16.81  ? 201 SER   A CA    1 
ATOM   1544 C C     . SER   A 1 220 ? 9.939   18.48  28.171 1 19.3   ? 201 SER   A C     1 
ATOM   1545 O O     . SER   A 1 220 ? 8.855   19.052 28.08  1 18.94  ? 201 SER   A O     1 
ATOM   1546 C CB    . SER   A 1 220 ? 10.694  19.097 30.493 1 20.53  ? 201 SER   A CB    1 
ATOM   1547 O OG    . SER   A 1 220 ? 10.907  17.828 31.09  1 26.39  ? 201 SER   A OG    1 
ATOM   1548 N N     . SER   A 1 221 ? 10.204  17.309 27.539 1 15.38  ? 202 SER   A N     1 
ATOM   1549 C CA    . SER   A 1 221 ? 9.2     16.574 26.774 1 13.71  ? 202 SER   A CA    1 
ATOM   1550 C C     . SER   A 1 221 ? 8.571   15.435 27.603 1 18.42  ? 202 SER   A C     1 
ATOM   1551 O O     . SER   A 1 221 ? 7.564   14.861 27.192 1 17.78  ? 202 SER   A O     1 
ATOM   1552 C CB    . SER   A 1 221 ? 9.759   16.089 25.443 1 16.33  ? 202 SER   A CB    1 
ATOM   1553 O OG    . SER   A 1 221 ? 10.855  15.223 25.671 1 23.97  ? 202 SER   A OG    1 
ATOM   1554 N N     . TYR   A 1 222 ? 9.131   15.158 28.807 1 16.37  ? 203 TYR   A N     1 
ATOM   1555 C CA    . TYR   A 1 222 ? 8.609   14.179 29.769 1 15.38  ? 203 TYR   A CA    1 
ATOM   1556 C C     . TYR   A 1 222 ? 9.232   14.35  31.15  1 18.59  ? 203 TYR   A C     1 
ATOM   1557 O O     . TYR   A 1 222 ? 10.259  15.01  31.296 1 18.03  ? 203 TYR   A O     1 
ATOM   1558 C CB    . TYR   A 1 222 ? 8.86    12.704 29.292 1 16.22  ? 203 TYR   A CB    1 
ATOM   1559 C CG    . TYR   A 1 222 ? 10.319  12.303 29.35  1 17.26  ? 203 TYR   A CG    1 
ATOM   1560 C CD1   . TYR   A 1 222 ? 11.17   12.544 28.275 1 18.67  ? 203 TYR   A CD1   1 
ATOM   1561 C CD2   . TYR   A 1 222 ? 10.862  11.736 30.498 1 17.37  ? 203 TYR   A CD2   1 
ATOM   1562 C CE1   . TYR   A 1 222 ? 12.524  12.242 28.344 1 18.82  ? 203 TYR   A CE1   1 
ATOM   1563 C CE2   . TYR   A 1 222 ? 12.224  11.453 30.588 1 18.49  ? 203 TYR   A CE2   1 
ATOM   1564 C CZ    . TYR   A 1 222 ? 13.048  11.698 29.501 1 22.64  ? 203 TYR   A CZ    1 
ATOM   1565 O OH    . TYR   A 1 222 ? 14.385  11.418 29.555 1 19.3   ? 203 TYR   A OH    1 
ATOM   1566 N N     . TYR   A 1 223 ? 8.623   13.67  32.149 1 15.27  ? 204 TYR   A N     1 
ATOM   1567 C CA    . TYR   A 1 223 ? 9.093   13.461 33.515 1 13.68  ? 204 TYR   A CA    1 
ATOM   1568 C C     . TYR   A 1 223 ? 8.651   12.069 33.921 1 17.43  ? 204 TYR   A C     1 
ATOM   1569 O O     . TYR   A 1 223 ? 7.734   11.521 33.301 1 16.73  ? 204 TYR   A O     1 
ATOM   1570 C CB    . TYR   A 1 223 ? 8.683   14.558 34.507 1 14.18  ? 204 TYR   A CB    1 
ATOM   1571 C CG    . TYR   A 1 223 ? 7.217   14.59  34.86  1 15.05  ? 204 TYR   A CG    1 
ATOM   1572 C CD1   . TYR   A 1 223 ? 6.299   15.243 34.042 1 16.45  ? 204 TYR   A CD1   1 
ATOM   1573 C CD2   . TYR   A 1 223 ? 6.755   14.035 36.049 1 15.6   ? 204 TYR   A CD2   1 
ATOM   1574 C CE1   . TYR   A 1 223 ? 4.957   15.343 34.395 1 15.53  ? 204 TYR   A CE1   1 
ATOM   1575 C CE2   . TYR   A 1 223 ? 5.406   14.091 36.393 1 16.42  ? 204 TYR   A CE2   1 
ATOM   1576 C CZ    . TYR   A 1 223 ? 4.51    14.743 35.559 1 19.27  ? 204 TYR   A CZ    1 
ATOM   1577 O OH    . TYR   A 1 223 ? 3.187   14.824 35.887 1 16.87  ? 204 TYR   A OH    1 
ATOM   1578 N N     . MET   A 1 224 ? 9.349   11.464 34.897 1 14.47  ? 205 MET   A N     1 
ATOM   1579 C CA    . MET   A 1 224 ? 9.118   10.084 35.332 1 12.68  ? 205 MET   A CA    1 
ATOM   1580 C C     . MET   A 1 224 ? 8.798   9.999  36.802 1 17.7   ? 205 MET   A C     1 
ATOM   1581 O O     . MET   A 1 224 ? 9.371   10.749 37.598 1 17.63  ? 205 MET   A O     1 
ATOM   1582 C CB    . MET   A 1 224 ? 10.418  9.268  35.167 1 14.54  ? 205 MET   A CB    1 
ATOM   1583 C CG    . MET   A 1 224 ? 10.994  9.201  33.761 1 16.94  ? 205 MET   A CG    1 
ATOM   1584 S SD    . MET   A 1 224 ? 9.965   8.399  32.514 1 18.65  ? 205 MET   A SD    1 
ATOM   1585 C CE    . MET   A 1 224 ? 9.914   6.705  33.089 1 15.19  ? 205 MET   A CE    1 
ATOM   1586 N N     . ILE   A 1 225 ? 7.981   9.002  37.185 1 15.85  ? 206 ILE   A N     1 
ATOM   1587 C CA    . ILE   A 1 225 ? 7.74    8.648  38.587 1 16.16  ? 206 ILE   A CA    1 
ATOM   1588 C C     . ILE   A 1 225 ? 8.088   7.152  38.605 1 23.04  ? 206 ILE   A C     1 
ATOM   1589 O O     . ILE   A 1 225 ? 7.247   6.308  38.286 1 23.66  ? 206 ILE   A O     1 
ATOM   1590 C CB    . ILE   A 1 225 ? 6.332   8.96   39.135 1 18.56  ? 206 ILE   A CB    1 
ATOM   1591 C CG1   . ILE   A 1 225 ? 5.947   10.439 38.894 1 18.26  ? 206 ILE   A CG1   1 
ATOM   1592 C CG2   . ILE   A 1 225 ? 6.282   8.642  40.625 1 21.1   ? 206 ILE   A CG2   1 
ATOM   1593 C CD1   . ILE   A 1 225 ? 4.483   10.745 39.171 1 12.52  ? 206 ILE   A CD1   1 
ATOM   1594 N N     . GLY   A 1 226 ? 9.36    6.861  38.858 1 19.64  ? 207 GLY   A N     1 
ATOM   1595 C CA    . GLY   A 1 226 ? 9.885   5.506  38.753 1 19.67  ? 207 GLY   A CA    1 
ATOM   1596 C C     . GLY   A 1 226 ? 9.874   5.11   37.285 1 21.69  ? 207 GLY   A C     1 
ATOM   1597 O O     . GLY   A 1 226 ? 10.444  5.809  36.449 1 20.32  ? 207 GLY   A O     1 
ATOM   1598 N N     . GLU   A 1 227 ? 9.157   4.024  36.959 1 19.69  ? 208 GLU   A N     1 
ATOM   1599 C CA    . GLU   A 1 227 ? 8.999   3.498  35.591 1 18.72  ? 208 GLU   A CA    1 
ATOM   1600 C C     . GLU   A 1 227 ? 7.83    4.193  34.837 1 18.81  ? 208 GLU   A C     1 
ATOM   1601 O O     . GLU   A 1 227 ? 7.704   4.062  33.62  1 16.62  ? 208 GLU   A O     1 
ATOM   1602 C CB    . GLU   A 1 227 ? 8.713   2.001  35.662 1 20.11  ? 208 GLU   A CB    1 
ATOM   1603 C CG    . GLU   A 1 227 ? 9.925   1.133  35.916 1 28.95  ? 208 GLU   A CG    1 
ATOM   1604 C CD    . GLU   A 1 227 ? 9.584   -0.338 35.813 1 37.48  ? 208 GLU   A CD    1 
ATOM   1605 O OE1   . GLU   A 1 227 ? 9.593   -0.866 34.679 1 30.54  ? 208 GLU   A OE1   1 
ATOM   1606 O OE2   . GLU   A 1 227 ? 9.243   -0.948 36.851 1 34.02  ? 208 GLU   A OE2   1 
ATOM   1607 N N     . GLN   A 1 228 ? 6.967   4.908  35.569 1 14.41  ? 209 GLN   A N     1 
ATOM   1608 C CA    . GLN   A 1 228 ? 5.827   5.568  34.957 1 13.04  ? 209 GLN   A CA    1 
ATOM   1609 C C     . GLN   A 1 228 ? 6.222   6.89   34.279 1 16.98  ? 209 GLN   A C     1 
ATOM   1610 O O     . GLN   A 1 228 ? 6.683   7.82   34.931 1 17.62  ? 209 GLN   A O     1 
ATOM   1611 C CB    . GLN   A 1 228 ? 4.671   5.725  35.958 1 14.52  ? 209 GLN   A CB    1 
ATOM   1612 C CG    . GLN   A 1 228 ? 3.358   6.318  35.344 1 13.85  ? 209 GLN   A CG    1 
ATOM   1613 C CD    . GLN   A 1 228 ? 2.689   5.432  34.325 1 24.37  ? 209 GLN   A CD    1 
ATOM   1614 O OE1   . GLN   A 1 228 ? 2.59    5.753  33.137 1 23.96  ? 209 GLN   A OE1   1 
ATOM   1615 N NE2   . GLN   A 1 228 ? 2.202   4.312  34.767 1 17.92  ? 209 GLN   A NE2   1 
ATOM   1616 N N     . LYS   A 1 229 ? 6.044   6.945  32.964 1 13.45  ? 210 LYS   A N     1 
ATOM   1617 C CA    . LYS   A 1 229 ? 6.354   8.105  32.138 1 14.08  ? 210 LYS   A CA    1 
ATOM   1618 C C     . LYS   A 1 229 ? 5.144   9.038  32.047 1 19.15  ? 210 LYS   A C     1 
ATOM   1619 O O     . LYS   A 1 229 ? 4.009   8.583  31.937 1 19.77  ? 210 LYS   A O     1 
ATOM   1620 C CB    . LYS   A 1 229 ? 6.783   7.646  30.719 1 16.16  ? 210 LYS   A CB    1 
ATOM   1621 C CG    . LYS   A 1 229 ? 7.348   8.756  29.834 1 22.05  ? 210 LYS   A CG    1 
ATOM   1622 C CD    . LYS   A 1 229 ? 7.971   8.182  28.59  1 27.95  ? 210 LYS   A CD    1 
ATOM   1623 C CE    . LYS   A 1 229 ? 8.806   9.222  27.893 1 38.52  ? 210 LYS   A CE    1 
ATOM   1624 N NZ    . LYS   A 1 229 ? 10.028  8.636  27.277 1 39.27  ? 210 LYS   A NZ    1 
ATOM   1625 N N     . PHE   A 1 230 ? 5.403   10.346 32.059 1 15.94  ? 211 PHE   A N     1 
ATOM   1626 C CA    . PHE   A 1 230 ? 4.371   11.361 31.92  1 14.48  ? 211 PHE   A CA    1 
ATOM   1627 C C     . PHE   A 1 230 ? 4.849   12.359 30.902 1 18.1   ? 211 PHE   A C     1 
ATOM   1628 O O     . PHE   A 1 230 ? 6.009   12.746 30.943 1 17.81  ? 211 PHE   A O     1 
ATOM   1629 C CB    . PHE   A 1 230 ? 4.087   12.047 33.264 1 15.4   ? 211 PHE   A CB    1 
ATOM   1630 C CG    . PHE   A 1 230 ? 3.287   11.203 34.224 1 15.99  ? 211 PHE   A CG    1 
ATOM   1631 C CD1   . PHE   A 1 230 ? 1.905   11.126 34.121 1 18.05  ? 211 PHE   A CD1   1 
ATOM   1632 C CD2   . PHE   A 1 230 ? 3.918   10.463 35.218 1 16.37  ? 211 PHE   A CD2   1 
ATOM   1633 C CE1   . PHE   A 1 230 ? 1.169   10.314 34.984 1 18.15  ? 211 PHE   A CE1   1 
ATOM   1634 C CE2   . PHE   A 1 230 ? 3.176   9.657  36.084 1 17.74  ? 211 PHE   A CE2   1 
ATOM   1635 C CZ    . PHE   A 1 230 ? 1.812   9.589  35.959 1 15.73  ? 211 PHE   A CZ    1 
ATOM   1636 N N     . SER   A 1 231 ? 3.988   12.741 29.962 1 13.93  ? 212 SER   A N     1 
ATOM   1637 C CA    . SER   A 1 231 ? 4.345   13.73  28.941 1 14.41  ? 212 SER   A CA    1 
ATOM   1638 C C     . SER   A 1 231 ? 4.504   15.122 29.569 1 17.46  ? 212 SER   A C     1 
ATOM   1639 O O     . SER   A 1 231 ? 3.872   15.43  30.577 1 14.93  ? 212 SER   A O     1 
ATOM   1640 C CB    . SER   A 1 231 ? 3.246   13.806 27.881 1 17.01  ? 212 SER   A CB    1 
ATOM   1641 O OG    . SER   A 1 231 ? 3.255   12.673 27.027 1 25.56  ? 212 SER   A OG    1 
ATOM   1642 N N     . SER   A 1 232 ? 5.338   15.959 28.95  1 15.22  ? 213 SER   A N     1 
ATOM   1643 C CA    . SER   A 1 232 ? 5.518   17.357 29.339 1 14.24  ? 213 SER   A CA    1 
ATOM   1644 C C     . SER   A 1 232 ? 5.594   18.192 28.055 1 17.46  ? 213 SER   A C     1 
ATOM   1645 O O     . SER   A 1 232 ? 6.078   17.704 27.038 1 15.62  ? 213 SER   A O     1 
ATOM   1646 C CB    . SER   A 1 232 ? 6.767   17.53  30.205 1 16.38  ? 213 SER   A CB    1 
ATOM   1647 O OG    . SER   A 1 232 ? 6.994   18.892 30.532 1 20.51  ? 213 SER   A OG    1 
ATOM   1648 N N     . LEU   A 1 233 ? 5.076   19.425 28.081 1 15.62  ? 214 LEU   A N     1 
ATOM   1649 C CA    . LEU   A 1 233 ? 5.117   20.32  26.921 1 15.24  ? 214 LEU   A CA    1 
ATOM   1650 C C     . LEU   A 1 233 ? 6.49    21.022 26.912 1 19.23  ? 214 LEU   A C     1 
ATOM   1651 O O     . LEU   A 1 233 ? 6.787   21.742 27.876 1 17.58  ? 214 LEU   A O     1 
ATOM   1652 C CB    . LEU   A 1 233 ? 3.971   21.353 26.993 1 15     ? 214 LEU   A CB    1 
ATOM   1653 C CG    . LEU   A 1 233 ? 3.867   22.35  25.82  1 19.22  ? 214 LEU   A CG    1 
ATOM   1654 C CD1   . LEU   A 1 233 ? 3.635   21.623 24.463 1 18.73  ? 214 LEU   A CD1   1 
ATOM   1655 C CD2   . LEU   A 1 233 ? 2.833   23.443 26.12  1 18     ? 214 LEU   A CD2   1 
ATOM   1656 N N     . PRO   A 1 234 ? 7.336   20.83  25.86  1 17.62  ? 215 PRO   A N     1 
ATOM   1657 C CA    . PRO   A 1 234 ? 8.674   21.433 25.887 1 18.88  ? 215 PRO   A CA    1 
ATOM   1658 C C     . PRO   A 1 234 ? 8.67    22.865 25.367 1 25.53  ? 215 PRO   A C     1 
ATOM   1659 O O     . PRO   A 1 234 ? 8.683   23.092 24.155 1 27.37  ? 215 PRO   A O     1 
ATOM   1660 C CB    . PRO   A 1 234 ? 9.514   20.463 25.044 1 20.22  ? 215 PRO   A CB    1 
ATOM   1661 C CG    . PRO   A 1 234 ? 8.535   19.848 24.094 1 24.02  ? 215 PRO   A CG    1 
ATOM   1662 C CD    . PRO   A 1 234 ? 7.145   20.023 24.636 1 19.4   ? 215 PRO   A CD    1 
ATOM   1663 N N     . LEU   A 1 235 ? 8.585   23.823 26.297 1 21.87  ? 216 LEU   A N     1 
ATOM   1664 C CA    . LEU   A 1 235 ? 8.567   25.257 25.996 1 21.52  ? 216 LEU   A CA    1 
ATOM   1665 C C     . LEU   A 1 235 ? 9.877   25.911 26.385 1 24.35  ? 216 LEU   A C     1 
ATOM   1666 O O     . LEU   A 1 235 ? 10.464  25.588 27.427 1 23.73  ? 216 LEU   A O     1 
ATOM   1667 C CB    . LEU   A 1 235 ? 7.428   25.981 26.772 1 21.61  ? 216 LEU   A CB    1 
ATOM   1668 C CG    . LEU   A 1 235 ? 5.967   25.685 26.423 1 25.83  ? 216 LEU   A CG    1 
ATOM   1669 C CD1   . LEU   A 1 235 ? 5.063   26.654 27.113 1 25.54  ? 216 LEU   A CD1   1 
ATOM   1670 C CD2   . LEU   A 1 235 ? 5.704   25.746 24.928 1 28.9   ? 216 LEU   A CD2   1 
ATOM   1671 N N     . GLY   A 1 236 ? 10.299  26.855 25.556 1 19.73  ? 217 GLY   A N     1 
ATOM   1672 C CA    . GLY   A 1 236 ? 11.442  27.705 25.827 1 19.22  ? 217 GLY   A CA    1 
ATOM   1673 C C     . GLY   A 1 236 ? 10.908  28.937 26.536 1 21.67  ? 217 GLY   A C     1 
ATOM   1674 O O     . GLY   A 1 236 ? 9.701   29.171 26.511 1 19.27  ? 217 GLY   A O     1 
ATOM   1675 N N     . ARG   A 1 237 ? 11.784  29.745 27.168 1 18.35  ? 218 ARG   A N     1 
ATOM   1676 C CA    . ARG   A 1 237 ? 11.363  30.937 27.911 1 17.58  ? 218 ARG   A CA    1 
ATOM   1677 C C     . ARG   A 1 237 ? 10.596  31.971 27.045 1 19.94  ? 218 ARG   A C     1 
ATOM   1678 O O     . ARG   A 1 237 ? 9.703   32.649 27.552 1 18.63  ? 218 ARG   A O     1 
ATOM   1679 C CB    . ARG   A 1 237 ? 12.546  31.585 28.663 1 18.34  ? 218 ARG   A CB    1 
ATOM   1680 C CG    . ARG   A 1 237 ? 13.655  32.137 27.772 1 34.8   ? 218 ARG   A CG    1 
ATOM   1681 C CD    . ARG   A 1 237 ? 14.446  33.247 28.455 1 45.3   ? 218 ARG   A CD    1 
ATOM   1682 N NE    . ARG   A 1 237 ? 15.349  33.922 27.519 1 45.22  ? 218 ARG   A NE    1 
ATOM   1683 C CZ    . ARG   A 1 237 ? 15.002  34.953 26.754 1 64.68  ? 218 ARG   A CZ    1 
ATOM   1684 N NH1   . ARG   A 1 237 ? 13.768  35.441 26.804 1 57.01  ? 218 ARG   A NH1   1 
ATOM   1685 N NH2   . ARG   A 1 237 ? 15.886  35.505 25.935 1 54.26  ? 218 ARG   A NH2   1 
ATOM   1686 N N     . GLU   A 1 238 ? 10.917  32.047 25.75  1 16.47  ? 219 GLU   A N     1 
ATOM   1687 C CA    . GLU   A 1 238 ? 10.294  32.965 24.793 1 16.94  ? 219 GLU   A CA    1 
ATOM   1688 C C     . GLU   A 1 238 ? 8.829   32.621 24.598 1 21.48  ? 219 GLU   A C     1 
ATOM   1689 O O     . GLU   A 1 238 ? 7.996   33.531 24.62  1 21.16  ? 219 GLU   A O     1 
ATOM   1690 C CB    . GLU   A 1 238 ? 11.032  32.958 23.435 1 18.5   ? 219 GLU   A CB    1 
ATOM   1691 C CG    . GLU   A 1 238 ? 12.476  33.438 23.506 1 30.3   ? 219 GLU   A CG    1 
ATOM   1692 C CD    . GLU   A 1 238 ? 13.538  32.392 23.817 1 53.86  ? 219 GLU   A CD    1 
ATOM   1693 O OE1   . GLU   A 1 238 ? 13.186  31.241 24.172 1 34.9   ? 219 GLU   A OE1   1 
ATOM   1694 O OE2   . GLU   A 1 238 ? 14.737  32.732 23.691 1 55.5   ? 219 GLU   A OE2   1 
ATOM   1695 N N     . ALA   A 1 239 ? 8.511   31.309 24.435 1 17.5   ? 220 ALA   A N     1 
ATOM   1696 C CA    . ALA   A 1 239 ? 7.148   30.802 24.237 1 16.36  ? 220 ALA   A CA    1 
ATOM   1697 C C     . ALA   A 1 239 ? 6.326   31.03  25.48  1 18.52  ? 220 ALA   A C     1 
ATOM   1698 O O     . ALA   A 1 239 ? 5.171   31.444 25.366 1 18.05  ? 220 ALA   A O     1 
ATOM   1699 C CB    . ALA   A 1 239 ? 7.167   29.321 23.867 1 17.44  ? 220 ALA   A CB    1 
ATOM   1700 N N     . VAL   A 1 240 ? 6.917   30.806 26.669 1 14.33  ? 221 VAL   A N     1 
ATOM   1701 C CA    . VAL   A 1 240 ? 6.249   31.071 27.951 1 13.56  ? 221 VAL   A CA    1 
ATOM   1702 C C     . VAL   A 1 240 ? 5.893   32.594 28.04  1 17.28  ? 221 VAL   A C     1 
ATOM   1703 O O     . VAL   A 1 240 ? 4.74    32.927 28.299 1 14.68  ? 221 VAL   A O     1 
ATOM   1704 C CB    . VAL   A 1 240 ? 7.085   30.6   29.173 1 16.34  ? 221 VAL   A CB    1 
ATOM   1705 C CG1   . VAL   A 1 240 ? 6.386   30.97  30.49  1 15.03  ? 221 VAL   A CG1   1 
ATOM   1706 C CG2   . VAL   A 1 240 ? 7.376   29.094 29.11  1 15.83  ? 221 VAL   A CG2   1 
ATOM   1707 N N     . GLU   A 1 241 ? 6.881   33.492 27.824 1 15.69  ? 222 GLU   A N     1 
ATOM   1708 C CA    . GLU   A 1 241 ? 6.679   34.946 27.861 1 16.82  ? 222 GLU   A CA    1 
ATOM   1709 C C     . GLU   A 1 241 ? 5.61    35.38  26.859 1 19.86  ? 222 GLU   A C     1 
ATOM   1710 O O     . GLU   A 1 241 ? 4.746   36.179 27.219 1 18.14  ? 222 GLU   A O     1 
ATOM   1711 C CB    . GLU   A 1 241 ? 7.977   35.72  27.568 1 18.94  ? 222 GLU   A CB    1 
ATOM   1712 C CG    . GLU   A 1 241 ? 8.981   35.737 28.703 1 36.44  ? 222 GLU   A CG    1 
ATOM   1713 C CD    . GLU   A 1 241 ? 10.389  36.096 28.264 1 64.56  ? 222 GLU   A CD    1 
ATOM   1714 O OE1   . GLU   A 1 241 ? 10.589  37.24  27.796 1 69.03  ? 222 GLU   A OE1   1 
ATOM   1715 O OE2   . GLU   A 1 241 ? 11.289  35.231 28.377 1 52.09  ? 222 GLU   A OE2   1 
ATOM   1716 N N     . ALA   A 1 242 ? 5.676   34.86  25.611 1 16.99  ? 223 ALA   A N     1 
ATOM   1717 C CA    . ALA   A 1 242 ? 4.708   35.205 24.565 1 16.96  ? 223 ALA   A CA    1 
ATOM   1718 C C     . ALA   A 1 242 ? 3.271   34.794 24.963 1 20.57  ? 223 ALA   A C     1 
ATOM   1719 O O     . ALA   A 1 242 ? 2.354   35.61  24.838 1 21.26  ? 223 ALA   A O     1 
ATOM   1720 C CB    . ALA   A 1 242 ? 5.112   34.582 23.231 1 17.79  ? 223 ALA   A CB    1 
ATOM   1721 N N     . ALA   A 1 243 ? 3.093   33.577 25.51  1 15.64  ? 224 ALA   A N     1 
ATOM   1722 C CA    . ALA   A 1 243 ? 1.792   33.05  25.939 1 15.23  ? 224 ALA   A CA    1 
ATOM   1723 C C     . ALA   A 1 243 ? 1.176   33.869 27.045 1 18.41  ? 224 ALA   A C     1 
ATOM   1724 O O     . ALA   A 1 243 ? -0.025  34.104 26.993 1 17.29  ? 224 ALA   A O     1 
ATOM   1725 C CB    . ALA   A 1 243 ? 1.917   31.596 26.384 1 15.98  ? 224 ALA   A CB    1 
ATOM   1726 N N     . VAL   A 1 244 ? 1.983   34.279 28.069 1 15.65  ? 225 VAL   A N     1 
ATOM   1727 C CA    . VAL   A 1 244 ? 1.543   35.096 29.223 1 14.19  ? 225 VAL   A CA    1 
ATOM   1728 C C     . VAL   A 1 244 ? 1.045   36.463 28.709 1 18.01  ? 225 VAL   A C     1 
ATOM   1729 O O     . VAL   A 1 244 ? 0.009   36.954 29.171 1 18.74  ? 225 VAL   A O     1 
ATOM   1730 C CB    . VAL   A 1 244 ? 2.668   35.215 30.295 1 18.1   ? 225 VAL   A CB    1 
ATOM   1731 C CG1   . VAL   A 1 244 ? 2.323   36.235 31.377 1 17.7   ? 225 VAL   A CG1   1 
ATOM   1732 C CG2   . VAL   A 1 244 ? 2.979   33.852 30.935 1 17.84  ? 225 VAL   A CG2   1 
ATOM   1733 N N     . LYS   A 1 245 ? 1.759   37.053 27.737 1 13.71  ? 226 LYS   A N     1 
ATOM   1734 C CA    . LYS   A 1 245 ? 1.371   38.336 27.123 1 14.29  ? 226 LYS   A CA    1 
ATOM   1735 C C     . LYS   A 1 245 ? 0.072   38.186 26.298 1 20.67  ? 226 LYS   A C     1 
ATOM   1736 O O     . LYS   A 1 245 ? -0.851  38.992 26.442 1 20.21  ? 226 LYS   A O     1 
ATOM   1737 C CB    . LYS   A 1 245 ? 2.51    38.886 26.256 1 16.01  ? 226 LYS   A CB    1 
ATOM   1738 C CG    . LYS   A 1 245 ? 3.685   39.445 27.07  1 19.62  ? 226 LYS   A CG    1 
ATOM   1739 C CD    . LYS   A 1 245 ? 4.735   40.003 26.142 1 31.16  ? 226 LYS   A CD    1 
ATOM   1740 C CE    . LYS   A 1 245 ? 6.08    39.353 26.284 1 46.24  ? 226 LYS   A CE    1 
ATOM   1741 N NZ    . LYS   A 1 245 ? 7.053   39.933 25.317 1 58.05  ? 226 LYS   A NZ    1 
ATOM   1742 N N     . GLU   A 1 246 ? -0.009  37.121 25.474 1 17.86  ? 227 GLU   A N     1 
ATOM   1743 C CA    . GLU   A 1 246 ? -1.185  36.785 24.666 1 17.55  ? 227 GLU   A CA    1 
ATOM   1744 C C     . GLU   A 1 246 ? -2.413  36.514 25.561 1 20.74  ? 227 GLU   A C     1 
ATOM   1745 O O     . GLU   A 1 246 ? -3.525  36.911 25.214 1 19.57  ? 227 GLU   A O     1 
ATOM   1746 C CB    . GLU   A 1 246 ? -0.88   35.559 23.805 1 18.96  ? 227 GLU   A CB    1 
ATOM   1747 C CG    . GLU   A 1 246 ? -1.9    35.274 22.71  1 29.72  ? 227 GLU   A CG    1 
ATOM   1748 C CD    . GLU   A 1 246 ? -1.584  34.051 21.87  1 36.96  ? 227 GLU   A CD    1 
ATOM   1749 O OE1   . GLU   A 1 246 ? -2.52   33.482 21.266 1 26.94  ? 227 GLU   A OE1   1 
ATOM   1750 O OE2   . GLU   A 1 246 ? -0.398  33.658 21.814 1 25.5   ? 227 GLU   A OE2   1 
ATOM   1751 N N     . ALA   A 1 247 ? -2.197  35.876 26.736 1 16.78  ? 228 ALA   A N     1 
ATOM   1752 C CA    . ALA   A 1 247 ? -3.269  35.56  27.677 1 16.01  ? 228 ALA   A CA    1 
ATOM   1753 C C     . ALA   A 1 247 ? -3.808  36.759 28.452 1 19.32  ? 228 ALA   A C     1 
ATOM   1754 O O     . ALA   A 1 247 ? -4.79   36.613 29.192 1 17.82  ? 228 ALA   A O     1 
ATOM   1755 C CB    . ALA   A 1 247 ? -2.831  34.463 28.631 1 16.79  ? 228 ALA   A CB    1 
ATOM   1756 N N     . GLY   A 1 248 ? -3.183  37.926 28.294 1 16.73  ? 229 GLY   A N     1 
ATOM   1757 C CA    . GLY   A 1 248 ? -3.669  39.138 28.948 1 16.77  ? 229 GLY   A CA    1 
ATOM   1758 C C     . GLY   A 1 248 ? -3.06   39.483 30.29  1 19.46  ? 229 GLY   A C     1 
ATOM   1759 O O     . GLY   A 1 248 ? -3.741  40.062 31.14  1 17.69  ? 229 GLY   A O     1 
ATOM   1760 N N     . TYR   A 1 249 ? -1.758  39.192 30.463 1 15.09  ? 230 TYR   A N     1 
ATOM   1761 C CA    . TYR   A 1 249 ? -1.01   39.554 31.669 1 14     ? 230 TYR   A CA    1 
ATOM   1762 C C     . TYR   A 1 249 ? 0.131   40.5   31.349 1 17.71  ? 230 TYR   A C     1 
ATOM   1763 O O     . TYR   A 1 249 ? 0.533   40.631 30.196 1 17.67  ? 230 TYR   A O     1 
ATOM   1764 C CB    . TYR   A 1 249 ? -0.419  38.312 32.359 1 13.83  ? 230 TYR   A CB    1 
ATOM   1765 C CG    . TYR   A 1 249 ? -1.443  37.291 32.795 1 12.96  ? 230 TYR   A CG    1 
ATOM   1766 C CD1   . TYR   A 1 249 ? -1.765  36.209 31.982 1 14.41  ? 230 TYR   A CD1   1 
ATOM   1767 C CD2   . TYR   A 1 249 ? -2.039  37.366 34.051 1 12     ? 230 TYR   A CD2   1 
ATOM   1768 C CE1   . TYR   A 1 249 ? -2.681  35.247 32.391 1 14.47  ? 230 TYR   A CE1   1 
ATOM   1769 C CE2   . TYR   A 1 249 ? -2.961  36.411 34.47  1 12.76  ? 230 TYR   A CE2   1 
ATOM   1770 C CZ    . TYR   A 1 249 ? -3.291  35.36  33.629 1 17.46  ? 230 TYR   A CZ    1 
ATOM   1771 O OH    . TYR   A 1 249 ? -4.169  34.387 34.037 1 11.75  ? 230 TYR   A OH    1 
ATOM   1772 N N     . THR   A 1 250 ? 0.681   41.139 32.389 1 14.58  ? 231 THR   A N     1 
ATOM   1773 C CA    . THR   A 1 250 ? 1.845   42.004 32.276 1 14.33  ? 231 THR   A CA    1 
ATOM   1774 C C     . THR   A 1 250 ? 2.909   41.434 33.222 1 17.6   ? 231 THR   A C     1 
ATOM   1775 O O     . THR   A 1 250 ? 2.656   41.31  34.414 1 16.2   ? 231 THR   A O     1 
ATOM   1776 C CB    . THR   A 1 250 ? 1.478   43.505 32.452 1 23.09  ? 231 THR   A CB    1 
ATOM   1777 O OG1   . THR   A 1 250 ? 2.596   44.296 32.074 1 22.09  ? 231 THR   A OG1   1 
ATOM   1778 C CG2   . THR   A 1 250 ? 1.021   43.875 33.874 1 24.3   ? 231 THR   A CG2   1 
ATOM   1779 N N     . ILE   A 1 251 ? 4.062   41.04  32.692 1 15.27  ? 232 ILE   A N     1 
ATOM   1780 C CA    . ILE   A 1 251 ? 5.124   40.407 33.492 1 15.38  ? 232 ILE   A CA    1 
ATOM   1781 C C     . ILE   A 1 251 ? 5.907   41.428 34.324 1 17.6   ? 232 ILE   A C     1 
ATOM   1782 O O     . ILE   A 1 251 ? 6.397   42.416 33.783 1 18.07  ? 232 ILE   A O     1 
ATOM   1783 C CB    . ILE   A 1 251 ? 6.038   39.528 32.564 1 18.8   ? 232 ILE   A CB    1 
ATOM   1784 C CG1   . ILE   A 1 251 ? 5.218   38.36  31.938 1 18.47  ? 232 ILE   A CG1   1 
ATOM   1785 C CG2   . ILE   A 1 251 ? 7.289   38.987 33.3   1 18.96  ? 232 ILE   A CG2   1 
ATOM   1786 C CD1   . ILE   A 1 251 ? 5.71    37.864 30.548 1 18.72  ? 232 ILE   A CD1   1 
ATOM   1787 N N     . GLU   A 1 252 ? 6.045   41.172 35.63  1 14.2   ? 233 GLU   A N     1 
ATOM   1788 C CA    . GLU   A 1 252 ? 6.836   42.042 36.512 1 14.9   ? 233 GLU   A CA    1 
ATOM   1789 C C     . GLU   A 1 252 ? 8.287   41.568 36.577 1 19.66  ? 233 GLU   A C     1 
ATOM   1790 O O     . GLU   A 1 252 ? 9.205   42.395 36.583 1 18.51  ? 233 GLU   A O     1 
ATOM   1791 C CB    . GLU   A 1 252 ? 6.224   42.168 37.903 1 16.24  ? 233 GLU   A CB    1 
ATOM   1792 C CG    . GLU   A 1 252 ? 4.915   42.937 37.853 1 25.95  ? 233 GLU   A CG    1 
ATOM   1793 C CD    . GLU   A 1 252 ? 4.349   43.432 39.167 1 42.77  ? 233 GLU   A CD    1 
ATOM   1794 O OE1   . GLU   A 1 252 ? 3.649   44.468 39.145 1 42.95  ? 233 GLU   A OE1   1 
ATOM   1795 O OE2   . GLU   A 1 252 ? 4.581   42.782 40.21  1 38.28  ? 233 GLU   A OE2   1 
ATOM   1796 N N     . TRP   A 1 253 ? 8.492   40.243 36.611 1 15.83  ? 234 TRP   A N     1 
ATOM   1797 C CA    . TRP   A 1 253 ? 9.833   39.663 36.578 1 16.39  ? 234 TRP   A CA    1 
ATOM   1798 C C     . TRP   A 1 253 ? 9.808   38.237 36.048 1 18.12  ? 234 TRP   A C     1 
ATOM   1799 O O     . TRP   A 1 253 ? 8.78    37.548 36.131 1 15.3   ? 234 TRP   A O     1 
ATOM   1800 C CB    . TRP   A 1 253 ? 10.62   39.789 37.909 1 16.28  ? 234 TRP   A CB    1 
ATOM   1801 C CG    . TRP   A 1 253 ? 10.086  39.045 39.09  1 18.01  ? 234 TRP   A CG    1 
ATOM   1802 C CD1   . TRP   A 1 253 ? 9.352   39.566 40.113 1 21.22  ? 234 TRP   A CD1   1 
ATOM   1803 C CD2   . TRP   A 1 253 ? 10.396  37.694 39.466 1 18.31  ? 234 TRP   A CD2   1 
ATOM   1804 N NE1   . TRP   A 1 253 ? 9.127   38.604 41.071 1 21.51  ? 234 TRP   A NE1   1 
ATOM   1805 C CE2   . TRP   A 1 253 ? 9.731   37.436 40.683 1 22.92  ? 234 TRP   A CE2   1 
ATOM   1806 C CE3   . TRP   A 1 253 ? 11.094  36.641 38.844 1 19.78  ? 234 TRP   A CE3   1 
ATOM   1807 C CZ2   . TRP   A 1 253 ? 9.773   36.179 41.311 1 22.39  ? 234 TRP   A CZ2   1 
ATOM   1808 C CZ3   . TRP   A 1 253 ? 11.159  35.409 39.482 1 21.22  ? 234 TRP   A CZ3   1 
ATOM   1809 C CH2   . TRP   A 1 253 ? 10.479  35.177 40.682 1 21.95  ? 234 TRP   A CH2   1 
ATOM   1810 N N     . PHE   A 1 254 ? 10.943  37.822 35.469 1 13.62  ? 235 PHE   A N     1 
ATOM   1811 C CA    . PHE   A 1 254 ? 11.116  36.507 34.877 1 13.07  ? 235 PHE   A CA    1 
ATOM   1812 C C     . PHE   A 1 254 ? 12.54   36.037 35.148 1 16.36  ? 235 PHE   A C     1 
ATOM   1813 O O     . PHE   A 1 254 ? 13.505  36.725 34.791 1 15.46  ? 235 PHE   A O     1 
ATOM   1814 C CB    . PHE   A 1 254 ? 10.82   36.569 33.365 1 14.43  ? 235 PHE   A CB    1 
ATOM   1815 C CG    . PHE   A 1 254 ? 10.52   35.236 32.721 1 16.01  ? 235 PHE   A CG    1 
ATOM   1816 C CD1   . PHE   A 1 254 ? 11.523  34.277 32.56  1 17.9   ? 235 PHE   A CD1   1 
ATOM   1817 C CD2   . PHE   A 1 254 ? 9.245   34.944 32.248 1 18.5   ? 235 PHE   A CD2   1 
ATOM   1818 C CE1   . PHE   A 1 254 ? 11.25   33.052 31.952 1 17.89  ? 235 PHE   A CE1   1 
ATOM   1819 C CE2   . PHE   A 1 254 ? 8.971   33.704 31.653 1 20.73  ? 235 PHE   A CE2   1 
ATOM   1820 C CZ    . PHE   A 1 254 ? 9.977   32.768 31.516 1 17.67  ? 235 PHE   A CZ    1 
ATOM   1821 N N     . GLU   A 1 255 ? 12.663  34.874 35.8   1 11.26  ? 236 GLU   A N     1 
ATOM   1822 C CA    . GLU   A 1 255 ? 13.946  34.263 36.139 1 11.15  ? 236 GLU   A CA    1 
ATOM   1823 C C     . GLU   A 1 255 ? 14.089  32.864 35.538 1 14.18  ? 236 GLU   A C     1 
ATOM   1824 O O     . GLU   A 1 255 ? 13.166  32.052 35.64  1 12.34  ? 236 GLU   A O     1 
ATOM   1825 C CB    . GLU   A 1 255 ? 14.098  34.167 37.656 1 12.67  ? 236 GLU   A CB    1 
ATOM   1826 C CG    . GLU   A 1 255 ? 15.487  33.736 38.103 1 20.57  ? 236 GLU   A CG    1 
ATOM   1827 C CD    . GLU   A 1 255 ? 15.521  33.025 39.436 1 27.21  ? 236 GLU   A CD    1 
ATOM   1828 O OE1   . GLU   A 1 255 ? 16.319  33.436 40.305 1 20.01  ? 236 GLU   A OE1   1 
ATOM   1829 O OE2   . GLU   A 1 255 ? 14.744  32.062 39.619 1 29.29  ? 236 GLU   A OE2   1 
ATOM   1830 N N     . VAL   A 1 256 ? 15.257  32.579 34.941 1 10.53  ? 237 VAL   A N     1 
ATOM   1831 C CA    . VAL   A 1 256 ? 15.576  31.251 34.414 1 11.19  ? 237 VAL   A CA    1 
ATOM   1832 C C     . VAL   A 1 256 ? 16.744  30.741 35.252 1 16.72  ? 237 VAL   A C     1 
ATOM   1833 O O     . VAL   A 1 256 ? 17.665  31.51  35.524 1 16.27  ? 237 VAL   A O     1 
ATOM   1834 C CB    . VAL   A 1 256 ? 15.938  31.261 32.892 1 15.59  ? 237 VAL   A CB    1 
ATOM   1835 C CG1   . VAL   A 1 256 ? 16.501  29.905 32.426 1 15.7   ? 237 VAL   A CG1   1 
ATOM   1836 C CG2   . VAL   A 1 256 ? 14.74   31.658 32.036 1 15.5   ? 237 VAL   A CG2   1 
ATOM   1837 N N     . ILE   A 1 257 ? 16.7    29.463 35.673 1 14.19  ? 238 ILE   A N     1 
ATOM   1838 C CA    . ILE   A 1 257 ? 17.814  28.797 36.359 1 13.92  ? 238 ILE   A CA    1 
ATOM   1839 C C     . ILE   A 1 257 ? 18.267  27.691 35.425 1 15.68  ? 238 ILE   A C     1 
ATOM   1840 O O     . ILE   A 1 257 ? 17.441  27.143 34.688 1 13.16  ? 238 ILE   A O     1 
ATOM   1841 C CB    . ILE   A 1 257 ? 17.551  28.335 37.815 1 17.69  ? 238 ILE   A CB    1 
ATOM   1842 C CG1   . ILE   A 1 257 ? 16.506  27.175 37.893 1 18.13  ? 238 ILE   A CG1   1 
ATOM   1843 C CG2   . ILE   A 1 257 ? 17.142  29.533 38.667 1 17.95  ? 238 ILE   A CG2   1 
ATOM   1844 C CD1   . ILE   A 1 257 ? 16.409  26.455 39.224 1 19.42  ? 238 ILE   A CD1   1 
ATOM   1845 N N     . SER   A 1 258 ? 19.57   27.418 35.393 1 13.45  ? 239 SER   A N     1 
ATOM   1846 C CA    . SER   A 1 258 ? 20.127  26.387 34.507 1 13.88  ? 239 SER   A CA    1 
ATOM   1847 C C     . SER   A 1 258 ? 19.991  24.979 35.066 1 18.08  ? 239 SER   A C     1 
ATOM   1848 O O     . SER   A 1 258 ? 20.03   24.014 34.305 1 18.34  ? 239 SER   A O     1 
ATOM   1849 C CB    . SER   A 1 258 ? 21.592  26.683 34.202 1 16.39  ? 239 SER   A CB    1 
ATOM   1850 O OG    . SER   A 1 258 ? 22.302  26.818 35.421 1 22.94  ? 239 SER   A OG    1 
ATOM   1851 N N     . GLN   A 1 259 ? 19.825  24.858 36.386 1 15.51  ? 240 GLN   A N     1 
ATOM   1852 C CA    . GLN   A 1 259 ? 19.714  23.568 37.057 1 14.67  ? 240 GLN   A CA    1 
ATOM   1853 C C     . GLN   A 1 259 ? 18.55   22.724 36.542 1 19.64  ? 240 GLN   A C     1 
ATOM   1854 O O     . GLN   A 1 259 ? 17.391  23.122 36.624 1 18.23  ? 240 GLN   A O     1 
ATOM   1855 C CB    . GLN   A 1 259 ? 19.663  23.729 38.589 1 15.46  ? 240 GLN   A CB    1 
ATOM   1856 C CG    . GLN   A 1 259 ? 19.51   22.401 39.352 1 17.02  ? 240 GLN   A CG    1 
ATOM   1857 C CD    . GLN   A 1 259 ? 20.766  21.581 39.429 1 31.47  ? 240 GLN   A CD    1 
ATOM   1858 O OE1   . GLN   A 1 259 ? 21.678  21.902 40.183 1 32.37  ? 240 GLN   A OE1   1 
ATOM   1859 N NE2   . GLN   A 1 259 ? 20.82   20.465 38.699 1 23.92  ? 240 GLN   A NE2   1 
ATOM   1860 N N     . SER   A 1 260 ? 18.883  21.531 36.05  1 17.12  ? 241 SER   A N     1 
ATOM   1861 C CA    . SER   A 1 260 ? 17.928  20.577 35.53  1 16.17  ? 241 SER   A CA    1 
ATOM   1862 C C     . SER   A 1 260 ? 17.763  19.444 36.533 1 21.49  ? 241 SER   A C     1 
ATOM   1863 O O     . SER   A 1 260 ? 18.533  19.337 37.501 1 20.99  ? 241 SER   A O     1 
ATOM   1864 C CB    . SER   A 1 260 ? 18.418  20.035 34.192 1 18.49  ? 241 SER   A CB    1 
ATOM   1865 O OG    . SER   A 1 260 ? 18.403  21.076 33.233 1 26.23  ? 241 SER   A OG    1 
ATOM   1866 N N     . TYR   A 1 261 ? 16.726  18.618 36.32  1 18.2   ? 242 TYR   A N     1 
ATOM   1867 C CA    . TYR   A 1 261 ? 16.449  17.446 37.144 1 16.86  ? 242 TYR   A CA    1 
ATOM   1868 C C     . TYR   A 1 261 ? 17.444  16.35  36.78  1 20.26  ? 242 TYR   A C     1 
ATOM   1869 O O     . TYR   A 1 261 ? 18.026  16.39  35.682 1 20.41  ? 242 TYR   A O     1 
ATOM   1870 C CB    . TYR   A 1 261 ? 15.018  16.956 36.874 1 17.12  ? 242 TYR   A CB    1 
ATOM   1871 C CG    . TYR   A 1 261 ? 13.968  17.823 37.529 1 16.68  ? 242 TYR   A CG    1 
ATOM   1872 C CD1   . TYR   A 1 261 ? 13.597  17.62  38.855 1 17.94  ? 242 TYR   A CD1   1 
ATOM   1873 C CD2   . TYR   A 1 261 ? 13.37   18.871 36.836 1 16.75  ? 242 TYR   A CD2   1 
ATOM   1874 C CE1   . TYR   A 1 261 ? 12.653  18.439 39.474 1 17.42  ? 242 TYR   A CE1   1 
ATOM   1875 C CE2   . TYR   A 1 261 ? 12.436  19.703 37.449 1 17.09  ? 242 TYR   A CE2   1 
ATOM   1876 C CZ    . TYR   A 1 261 ? 12.075  19.478 38.764 1 19.23  ? 242 TYR   A CZ    1 
ATOM   1877 O OH    . TYR   A 1 261 ? 11.121  20.269 39.36  1 19.41  ? 242 TYR   A OH    1 
ATOM   1878 N N     . SER   A 1 262 ? 17.606  15.342 37.668 1 17.45  ? 243 SER   A N     1 
ATOM   1879 C CA    . SER   A 1 262 ? 18.486  14.194 37.398 1 18.02  ? 243 SER   A CA    1 
ATOM   1880 C C     . SER   A 1 262 ? 18.05   13.536 36.092 1 23.91  ? 243 SER   A C     1 
ATOM   1881 O O     . SER   A 1 262 ? 16.867  13.624 35.726 1 22.28  ? 243 SER   A O     1 
ATOM   1882 C CB    . SER   A 1 262 ? 18.442  13.184 38.542 1 20.26  ? 243 SER   A CB    1 
ATOM   1883 O OG    . SER   A 1 262 ? 18.673  13.815 39.788 1 20.6   ? 243 SER   A OG    1 
ATOM   1884 N N     . SER   A 1 263 ? 19.01   12.928 35.37  1 23.36  ? 244 SER   A N     1 
ATOM   1885 C CA    . SER   A 1 263 ? 18.82   12.264 34.066 1 24.5   ? 244 SER   A CA    1 
ATOM   1886 C C     . SER   A 1 263 ? 17.688  11.247 34.064 1 29.03  ? 244 SER   A C     1 
ATOM   1887 O O     . SER   A 1 263 ? 16.953  11.137 33.085 1 29.32  ? 244 SER   A O     1 
ATOM   1888 C CB    . SER   A 1 263 ? 20.111  11.59  33.615 1 28.86  ? 244 SER   A CB    1 
ATOM   1889 O OG    . SER   A 1 263 ? 20.529  10.599 34.539 1 37.65  ? 244 SER   A OG    1 
ATOM   1890 N N     . THR   A 1 264 ? 17.551  10.526 35.173 1 26.06  ? 245 THR   A N     1 
ATOM   1891 C CA    . THR   A 1 264 ? 16.533  9.501  35.408 1 26.44  ? 245 THR   A CA    1 
ATOM   1892 C C     . THR   A 1 264 ? 15.114  10.093 35.628 1 29.78  ? 245 THR   A C     1 
ATOM   1893 O O     . THR   A 1 264 ? 14.125  9.352  35.56  1 28.89  ? 245 THR   A O     1 
ATOM   1894 C CB    . THR   A 1 264 ? 16.975  8.634  36.607 1 33.18  ? 245 THR   A CB    1 
ATOM   1895 O OG1   . THR   A 1 264 ? 17.13   9.482  37.744 1 36.73  ? 245 THR   A OG1   1 
ATOM   1896 C CG2   . THR   A 1 264 ? 18.293  7.901  36.349 1 29.12  ? 245 THR   A CG2   1 
ATOM   1897 N N     . MET   A 1 265 ? 15.014  11.415 35.891 1 25.75  ? 246 MET   A N     1 
ATOM   1898 C CA    . MET   A 1 265 ? 13.734  12.065 36.178 1 25.9   ? 246 MET   A CA    1 
ATOM   1899 C C     . MET   A 1 265 ? 13.081  12.751 34.999 1 27.29  ? 246 MET   A C     1 
ATOM   1900 O O     . MET   A 1 265 ? 11.882  12.583 34.807 1 26.48  ? 246 MET   A O     1 
ATOM   1901 C CB    . MET   A 1 265 ? 13.86   13.079 37.339 1 29.21  ? 246 MET   A CB    1 
ATOM   1902 C CG    . MET   A 1 265 ? 14.471  12.515 38.599 1 34.46  ? 246 MET   A CG    1 
ATOM   1903 S SD    . MET   A 1 265 ? 13.559  11.114 39.251 1 40.49  ? 246 MET   A SD    1 
ATOM   1904 C CE    . MET   A 1 265 ? 14.652  10.643 40.558 1 37.57  ? 246 MET   A CE    1 
ATOM   1905 N N     . ALA   A 1 266 ? 13.833  13.602 34.272 1 22.76  ? 247 ALA   A N     1 
ATOM   1906 C CA    . ALA   A 1 266 ? 13.315  14.416 33.164 1 22.23  ? 247 ALA   A CA    1 
ATOM   1907 C C     . ALA   A 1 266 ? 14.444  14.881 32.253 1 24.96  ? 247 ALA   A C     1 
ATOM   1908 O O     . ALA   A 1 266 ? 15.617  14.768 32.63  1 26.47  ? 247 ALA   A O     1 
ATOM   1909 C CB    . ALA   A 1 266 ? 12.576  15.63  33.726 1 22.97  ? 247 ALA   A CB    1 
ATOM   1910 N N     . ASN   A 1 267 ? 14.09   15.397 31.056 1 19.6   ? 248 ASN   A N     1 
ATOM   1911 C CA    . ASN   A 1 267 ? 15.036  15.934 30.071 1 18.92  ? 248 ASN   A CA    1 
ATOM   1912 C C     . ASN   A 1 267 ? 14.915  17.466 29.951 1 22.19  ? 248 ASN   A C     1 
ATOM   1913 O O     . ASN   A 1 267 ? 15.072  18.019 28.857 1 23.23  ? 248 ASN   A O     1 
ATOM   1914 C CB    . ASN   A 1 267 ? 14.845  15.251 28.693 1 19.3   ? 248 ASN   A CB    1 
ATOM   1915 C CG    . ASN   A 1 267 ? 13.501  15.519 28.043 1 29.3   ? 248 ASN   A CG    1 
ATOM   1916 O OD1   . ASN   A 1 267 ? 12.515  15.811 28.707 1 21.41  ? 248 ASN   A OD1   1 
ATOM   1917 N ND2   . ASN   A 1 267 ? 13.432  15.457 26.724 1 21.94  ? 248 ASN   A ND2   1 
ATOM   1918 N N     . ASN   A 1 268 ? 14.654  18.156 31.07  1 18.07  ? 249 ASN   A N     1 
ATOM   1919 C CA    . ASN   A 1 268 ? 14.517  19.617 31.039 1 17.55  ? 249 ASN   A CA    1 
ATOM   1920 C C     . ASN   A 1 268 ? 15.845  20.358 30.9   1 20.91  ? 249 ASN   A C     1 
ATOM   1921 O O     . ASN   A 1 268 ? 16.906  19.813 31.187 1 19.81  ? 249 ASN   A O     1 
ATOM   1922 C CB    . ASN   A 1 268 ? 13.761  20.132 32.27  1 11.83  ? 249 ASN   A CB    1 
ATOM   1923 C CG    . ASN   A 1 268 ? 14.517  20.036 33.564 1 22.3   ? 249 ASN   A CG    1 
ATOM   1924 O OD1   . ASN   A 1 268 ? 14.97   18.972 33.963 1 16.51  ? 249 ASN   A OD1   1 
ATOM   1925 N ND2   . ASN   A 1 268 ? 14.588  21.139 34.296 1 17.23  ? 249 ASN   A ND2   1 
ATOM   1926 N N     . GLU   A 1 269 ? 15.772  21.617 30.479 1 16.39  ? 250 GLU   A N     1 
ATOM   1927 C CA    . GLU   A 1 269 ? 16.942  22.472 30.422 1 15.62  ? 250 GLU   A CA    1 
ATOM   1928 C C     . GLU   A 1 269 ? 16.614  23.632 31.346 1 16.6   ? 250 GLU   A C     1 
ATOM   1929 O O     . GLU   A 1 269 ? 16.188  24.697 30.903 1 14.06  ? 250 GLU   A O     1 
ATOM   1930 C CB    . GLU   A 1 269 ? 17.244  22.918 28.985 1 16.9   ? 250 GLU   A CB    1 
ATOM   1931 C CG    . GLU   A 1 269 ? 17.607  21.748 28.086 1 21.98  ? 250 GLU   A CG    1 
ATOM   1932 C CD    . GLU   A 1 269 ? 17.793  22.116 26.632 1 45.94  ? 250 GLU   A CD    1 
ATOM   1933 O OE1   . GLU   A 1 269 ? 17.118  21.496 25.781 1 46.12  ? 250 GLU   A OE1   1 
ATOM   1934 O OE2   . GLU   A 1 269 ? 18.605  23.026 26.343 1 43.2   ? 250 GLU   A OE2   1 
ATOM   1935 N N     . GLY   A 1 270 ? 16.733  23.366 32.636 1 14.01  ? 251 GLY   A N     1 
ATOM   1936 C CA    . GLY   A 1 270 ? 16.456  24.34  33.686 1 13.95  ? 251 GLY   A CA    1 
ATOM   1937 C C     . GLY   A 1 270 ? 14.988  24.567 33.978 1 16.68  ? 251 GLY   A C     1 
ATOM   1938 O O     . GLY   A 1 270 ? 14.133  23.785 33.559 1 15.91  ? 251 GLY   A O     1 
ATOM   1939 N N     . LEU   A 1 271 ? 14.692  25.618 34.755 1 13.2   ? 252 LEU   A N     1 
ATOM   1940 C CA    . LEU   A 1 271 ? 13.321  25.971 35.129 1 13.29  ? 252 LEU   A CA    1 
ATOM   1941 C C     . LEU   A 1 271 ? 13.163  27.481 35.08  1 17.09  ? 252 LEU   A C     1 
ATOM   1942 O O     . LEU   A 1 271 ? 14.162  28.201 35.152 1 16.54  ? 252 LEU   A O     1 
ATOM   1943 C CB    . LEU   A 1 271 ? 13.005  25.478 36.558 1 13.81  ? 252 LEU   A CB    1 
ATOM   1944 C CG    . LEU   A 1 271 ? 12.83   23.964 36.77  1 18.79  ? 252 LEU   A CG    1 
ATOM   1945 C CD1   . LEU   A 1 271 ? 14.129  23.338 37.27  1 18.92  ? 252 LEU   A CD1   1 
ATOM   1946 C CD2   . LEU   A 1 271 ? 11.714  23.683 37.793 1 20.09  ? 252 LEU   A CD2   1 
ATOM   1947 N N     . PHE   A 1 272 ? 11.917  27.958 34.932 1 13.22  ? 253 PHE   A N     1 
ATOM   1948 C CA    . PHE   A 1 272 ? 11.605  29.383 34.956 1 12.08  ? 253 PHE   A CA    1 
ATOM   1949 C C     . PHE   A 1 272 ? 10.671  29.661 36.143 1 15.75  ? 253 PHE   A C     1 
ATOM   1950 O O     . PHE   A 1 272 ? 9.962   28.762 36.611 1 13.72  ? 253 PHE   A O     1 
ATOM   1951 C CB    . PHE   A 1 272 ? 10.956  29.87  33.624 1 13.07  ? 253 PHE   A CB    1 
ATOM   1952 C CG    . PHE   A 1 272 ? 9.509   29.462 33.436 1 13.5   ? 253 PHE   A CG    1 
ATOM   1953 C CD1   . PHE   A 1 272 ? 8.479   30.202 34.009 1 15.76  ? 253 PHE   A CD1   1 
ATOM   1954 C CD2   . PHE   A 1 272 ? 9.182   28.305 32.736 1 14.94  ? 253 PHE   A CD2   1 
ATOM   1955 C CE1   . PHE   A 1 272 ? 7.153   29.781 33.905 1 16.55  ? 253 PHE   A CE1   1 
ATOM   1956 C CE2   . PHE   A 1 272 ? 7.852   27.91  32.59  1 17.03  ? 253 PHE   A CE2   1 
ATOM   1957 C CZ    . PHE   A 1 272 ? 6.847   28.635 33.203 1 15.46  ? 253 PHE   A CZ    1 
ATOM   1958 N N     . SER   A 1 273 ? 10.657  30.924 36.586 1 12.13  ? 254 SER   A N     1 
ATOM   1959 C CA    . SER   A 1 273 ? 9.77    31.479 37.601 1 11.16  ? 254 SER   A CA    1 
ATOM   1960 C C     . SER   A 1 273 ? 9.37    32.842 37.061 1 15.24  ? 254 SER   A C     1 
ATOM   1961 O O     . SER   A 1 273 ? 10.208  33.583 36.536 1 11.42  ? 254 SER   A O     1 
ATOM   1962 C CB    . SER   A 1 273 ? 10.478  31.67  38.939 1 12.65  ? 254 SER   A CB    1 
ATOM   1963 O OG    . SER   A 1 273 ? 10.809  30.44  39.566 1 22.67  ? 254 SER   A OG    1 
ATOM   1964 N N     . LEU   A 1 274 ? 8.09    33.17  37.178 1 14.53  ? 255 LEU   A N     1 
ATOM   1965 C CA    . LEU   A 1 274 ? 7.605   34.483 36.768 1 14.46  ? 255 LEU   A CA    1 
ATOM   1966 C C     . LEU   A 1 274 ? 6.534   34.978 37.703 1 17.18  ? 255 LEU   A C     1 
ATOM   1967 O O     . LEU   A 1 274 ? 5.826   34.177 38.312 1 15     ? 255 LEU   A O     1 
ATOM   1968 C CB    . LEU   A 1 274 ? 7.11    34.491 35.3   1 15.13  ? 255 LEU   A CB    1 
ATOM   1969 C CG    . LEU   A 1 274 ? 5.842   33.694 34.933 1 19.28  ? 255 LEU   A CG    1 
ATOM   1970 C CD1   . LEU   A 1 274 ? 4.554   34.546 35.119 1 19.93  ? 255 LEU   A CD1   1 
ATOM   1971 C CD2   . LEU   A 1 274 ? 5.888   33.278 33.487 1 20.04  ? 255 LEU   A CD2   1 
ATOM   1972 N N     . VAL   A 1 275 ? 6.391   36.306 37.777 1 15.61  ? 256 VAL   A N     1 
ATOM   1973 C CA    . VAL   A 1 275 ? 5.322   36.998 38.482 1 15.3   ? 256 VAL   A CA    1 
ATOM   1974 C C     . VAL   A 1 275 ? 4.738   37.975 37.465 1 19     ? 256 VAL   A C     1 
ATOM   1975 O O     . VAL   A 1 275 ? 5.473   38.738 36.834 1 17.35  ? 256 VAL   A O     1 
ATOM   1976 C CB    . VAL   A 1 275 ? 5.73    37.666 39.822 1 19.89  ? 256 VAL   A CB    1 
ATOM   1977 C CG1   . VAL   A 1 275 ? 4.541   38.412 40.447 1 20.07  ? 256 VAL   A CG1   1 
ATOM   1978 C CG2   . VAL   A 1 275 ? 6.269   36.623 40.804 1 19.22  ? 256 VAL   A CG2   1 
ATOM   1979 N N     . ALA   A 1 276 ? 3.421   37.887 37.245 1 16.98  ? 257 ALA   A N     1 
ATOM   1980 C CA    . ALA   A 1 276 ? 2.717   38.738 36.293 1 16.92  ? 257 ALA   A CA    1 
ATOM   1981 C C     . ALA   A 1 276 ? 1.46    39.291 36.945 1 21.23  ? 257 ALA   A C     1 
ATOM   1982 O O     . ALA   A 1 276 ? 1.06    38.798 38.003 1 21.41  ? 257 ALA   A O     1 
ATOM   1983 C CB    . ALA   A 1 276 ? 2.345   37.933 35.056 1 17.48  ? 257 ALA   A CB    1 
ATOM   1984 N N     . ARG   A 1 277 ? 0.837   40.299 36.305 1 16.67  ? 258 ARG   A N     1 
ATOM   1985 C CA    . ARG   A 1 277 ? -0.418  40.89  36.766 1 16.74  ? 258 ARG   A CA    1 
ATOM   1986 C C     . ARG   A 1 277 ? -1.457  40.825 35.671 1 18.34  ? 258 ARG   A C     1 
ATOM   1987 O O     . ARG   A 1 277 ? -1.144  41.097 34.51  1 16.96  ? 258 ARG   A O     1 
ATOM   1988 C CB    . ARG   A 1 277 ? -0.234  42.336 37.252 1 18.12  ? 258 ARG   A CB    1 
ATOM   1989 C CG    . ARG   A 1 277 ? 0.269   42.437 38.693 1 26.24  ? 258 ARG   A CG    1 
ATOM   1990 C CD    . ARG   A 1 277 ? 0.428   43.877 39.136 1 41.04  ? 258 ARG   A CD    1 
ATOM   1991 N NE    . ARG   A 1 277 ? -0.844  44.601 39.193 1 54.65  ? 258 ARG   A NE    1 
ATOM   1992 C CZ    . ARG   A 1 277 ? -1.29   45.26  40.259 1 68.61  ? 258 ARG   A CZ    1 
ATOM   1993 N NH1   . ARG   A 1 277 ? -0.575  45.29  41.379 1 58.1   ? 258 ARG   A NH1   1 
ATOM   1994 N NH2   . ARG   A 1 277 ? -2.455  45.893 40.214 1 49.48  ? 258 ARG   A NH2   1 
ATOM   1995 N N     . LYS   A 1 278 ? -2.693  40.461 36.042 1 15.95  ? 259 LYS   A N     1 
ATOM   1996 C CA    . LYS   A 1 278 ? -3.808  40.364 35.099 1 16.6   ? 259 LYS   A CA    1 
ATOM   1997 C C     . LYS   A 1 278 ? -4.221  41.757 34.622 1 22.01  ? 259 LYS   A C     1 
ATOM   1998 O O     . LYS   A 1 278 ? -4.496  42.634 35.439 1 21.48  ? 259 LYS   A O     1 
ATOM   1999 C CB    . LYS   A 1 278 ? -5.003  39.656 35.749 1 17.83  ? 259 LYS   A CB    1 
ATOM   2000 C CG    . LYS   A 1 278 ? -6.01   39.131 34.751 1 20.11  ? 259 LYS   A CG    1 
ATOM   2001 C CD    . LYS   A 1 278 ? -7.273  38.741 35.466 1 27.86  ? 259 LYS   A CD    1 
ATOM   2002 C CE    . LYS   A 1 278 ? -8.479  38.814 34.579 1 25.65  ? 259 LYS   A CE    1 
ATOM   2003 N NZ    . LYS   A 1 278 ? -9.682  38.369 35.316 1 28.61  ? 259 LYS   A NZ    1 
ATOM   2004 N N     . LEU   A 1 279 ? -4.283  41.944 33.31  1 21.01  ? 260 LEU   A N     1 
ATOM   2005 C CA    . LEU   A 1 279 ? -4.699  43.22  32.735 1 22.61  ? 260 LEU   A CA    1 
ATOM   2006 C C     . LEU   A 1 279 ? -6.218  43.346 32.861 1 32.45  ? 260 LEU   A C     1 
ATOM   2007 O O     . LEU   A 1 279 ? -6.964  42.472 32.401 1 30.75  ? 260 LEU   A O     1 
ATOM   2008 C CB    . LEU   A 1 279 ? -4.198  43.359 31.293 1 22.38  ? 260 LEU   A CB    1 
ATOM   2009 C CG    . LEU   A 1 279 ? -2.678  43.464 31.152 1 25.71  ? 260 LEU   A CG    1 
ATOM   2010 C CD1   . LEU   A 1 279 ? -2.29   43.549 29.727 1 25.85  ? 260 LEU   A CD1   1 
ATOM   2011 C CD2   . LEU   A 1 279 ? -2.133  44.673 31.887 1 25.74  ? 260 LEU   A CD2   1 
ATOM   2012 N N     . SER   A 1 280 ? -6.643  44.385 33.618 1 33.24  ? 261 SER   A N     1 
ATOM   2013 C CA    . SER   A 1 280 ? -8.013  44.709 34.052 1 73.43  ? 261 SER   A CA    1 
ATOM   2014 C C     . SER   A 1 280 ? -9.141  44.5   33.046 1 122.75 ? 261 SER   A C     1 
ATOM   2015 O O     . SER   A 1 280 ? -9.974  43.609 33.228 1 87.9   ? 261 SER   A O     1 
ATOM   2016 C CB    . SER   A 1 280 ? -8.074  46.104 34.667 1 76.3   ? 261 SER   A CB    1 
ATOM   2017 O OG    . SER   A 1 280 ? -7.246  46.193 35.815 1 82.44  ? 261 SER   A OG    1 
ATOM   2018 N N     . PHE   B 1 24  ? 31.13   58.056 23.36  1 21.5   ? 5   PHE   B N     1 
ATOM   2019 C CA    . PHE   B 1 24  ? 31.062  57.491 24.712 1 20.38  ? 5   PHE   B CA    1 
ATOM   2020 C C     . PHE   B 1 24  ? 31.879  58.292 25.721 1 22.84  ? 5   PHE   B C     1 
ATOM   2021 O O     . PHE   B 1 24  ? 32.965  58.729 25.384 1 21.24  ? 5   PHE   B O     1 
ATOM   2022 C CB    . PHE   B 1 24  ? 31.509  56.014 24.718 1 21.54  ? 5   PHE   B CB    1 
ATOM   2023 C CG    . PHE   B 1 24  ? 30.785  55.149 25.74  1 22.95  ? 5   PHE   B CG    1 
ATOM   2024 C CD1   . PHE   B 1 24  ? 31.304  54.972 27.021 1 25.01  ? 5   PHE   B CD1   1 
ATOM   2025 C CD2   . PHE   B 1 24  ? 29.59   54.508 25.416 1 24.3   ? 5   PHE   B CD2   1 
ATOM   2026 C CE1   . PHE   B 1 24  ? 30.634  54.175 27.963 1 25.01  ? 5   PHE   B CE1   1 
ATOM   2027 C CE2   . PHE   B 1 24  ? 28.928  53.697 26.359 1 25.97  ? 5   PHE   B CE2   1 
ATOM   2028 C CZ    . PHE   B 1 24  ? 29.449  53.551 27.628 1 23.13  ? 5   PHE   B CZ    1 
ATOM   2029 N N     . THR   B 1 25  ? 31.379  58.452 26.967 1 18.83  ? 6   THR   B N     1 
ATOM   2030 C CA    . THR   B 1 25  ? 32.074  59.155 28.06  1 18.65  ? 6   THR   B CA    1 
ATOM   2031 C C     . THR   B 1 25  ? 33.465  58.502 28.268 1 23.24  ? 6   THR   B C     1 
ATOM   2032 O O     . THR   B 1 25  ? 33.549  57.278 28.401 1 21.52  ? 6   THR   B O     1 
ATOM   2033 C CB    . THR   B 1 25  ? 31.218  59.088 29.36  1 19.88  ? 6   THR   B CB    1 
ATOM   2034 O OG1   . THR   B 1 25  ? 29.922  59.647 29.123 1 11.71  ? 6   THR   B OG1   1 
ATOM   2035 C CG2   . THR   B 1 25  ? 31.879  59.79  30.554 1 14.88  ? 6   THR   B CG2   1 
ATOM   2036 N N     . SER   B 1 26  ? 34.543  59.316 28.268 1 21.21  ? 7   SER   B N     1 
ATOM   2037 C CA    . SER   B 1 26  ? 35.909  58.812 28.476 1 20.47  ? 7   SER   B CA    1 
ATOM   2038 C C     . SER   B 1 26  ? 36.14   58.518 29.956 1 23.7   ? 7   SER   B C     1 
ATOM   2039 O O     . SER   B 1 26  ? 35.516  59.168 30.785 1 22.35  ? 7   SER   B O     1 
ATOM   2040 C CB    . SER   B 1 26  ? 36.931  59.828 27.972 1 23.68  ? 7   SER   B CB    1 
ATOM   2041 O OG    . SER   B 1 26  ? 36.808  61.078 28.628 1 28.44  ? 7   SER   B OG    1 
ATOM   2042 N N     . LYS   B 1 27  ? 37.03   57.542 30.28  1 22.08  ? 8   LYS   B N     1 
ATOM   2043 C CA    . LYS   B 1 27  ? 37.421  57.121 31.636 1 22.64  ? 8   LYS   B CA    1 
ATOM   2044 C C     . LYS   B 1 27  ? 37.7    58.321 32.54  1 24.41  ? 8   LYS   B C     1 
ATOM   2045 O O     . LYS   B 1 27  ? 37.179  58.392 33.645 1 23.18  ? 8   LYS   B O     1 
ATOM   2046 C CB    . LYS   B 1 27  ? 38.738  56.321 31.594 1 27.14  ? 8   LYS   B CB    1 
ATOM   2047 C CG    . LYS   B 1 27  ? 38.683  54.881 31.159 1 42.09  ? 8   LYS   B CG    1 
ATOM   2048 C CD    . LYS   B 1 27  ? 40.063  54.281 31.406 1 41.29  ? 8   LYS   B CD    1 
ATOM   2049 C CE    . LYS   B 1 27  ? 40.546  53.394 30.3   1 47.34  ? 8   LYS   B CE    1 
ATOM   2050 N NZ    . LYS   B 1 27  ? 41.929  52.933 30.566 1 53.23  ? 8   LYS   B NZ    1 
ATOM   2051 N N     . ASP   B 1 28  ? 38.566  59.24  32.072 1 20.34  ? 9   ASP   B N     1 
ATOM   2052 C CA    . ASP   B 1 28  ? 39.008  60.439 32.785 1 19.45  ? 9   ASP   B CA    1 
ATOM   2053 C C     . ASP   B 1 28  ? 37.862  61.351 33.228 1 20.48  ? 9   ASP   B C     1 
ATOM   2054 O O     . ASP   B 1 28  ? 38.024  62.074 34.215 1 19.82  ? 9   ASP   B O     1 
ATOM   2055 C CB    . ASP   B 1 28  ? 40.051  61.211 31.966 1 21.71  ? 9   ASP   B CB    1 
ATOM   2056 C CG    . ASP   B 1 28  ? 39.525  61.613 30.613 1 33.41  ? 9   ASP   B CG    1 
ATOM   2057 O OD1   . ASP   B 1 28  ? 39.503  60.754 29.713 1 36.28  ? 9   ASP   B OD1   1 
ATOM   2058 O OD2   . ASP   B 1 28  ? 39.019  62.739 30.492 1 37.3   ? 9   ASP   B OD2   1 
ATOM   2059 N N     . THR   B 1 29  ? 36.698  61.293 32.537 1 15.4   ? 10  THR   B N     1 
ATOM   2060 C CA    . THR   B 1 29  ? 35.515  62.08  32.905 1 14.78  ? 10  THR   B CA    1 
ATOM   2061 C C     . THR   B 1 29  ? 34.991  61.592 34.265 1 17.25  ? 10  THR   B C     1 
ATOM   2062 O O     . THR   B 1 29  ? 34.467  62.388 35.043 1 15.83  ? 10  THR   B O     1 
ATOM   2063 C CB    . THR   B 1 29  ? 34.459  62.09  31.773 1 24.55  ? 10  THR   B CB    1 
ATOM   2064 O OG1   . THR   B 1 29  ? 35.098  62.42  30.547 1 25.36  ? 10  THR   B OG1   1 
ATOM   2065 C CG2   . THR   B 1 29  ? 33.318  63.077 32.021 1 21.62  ? 10  THR   B CG2   1 
ATOM   2066 N N     . TYR   B 1 30  ? 35.196  60.304 34.579 1 13.76  ? 11  TYR   B N     1 
ATOM   2067 C CA    . TYR   B 1 30  ? 34.773  59.774 35.876 1 13.85  ? 11  TYR   B CA    1 
ATOM   2068 C C     . TYR   B 1 30  ? 35.56   60.329 37.029 1 20.52  ? 11  TYR   B C     1 
ATOM   2069 O O     . TYR   B 1 30  ? 34.999  60.515 38.101 1 20.83  ? 11  TYR   B O     1 
ATOM   2070 C CB    . TYR   B 1 30  ? 34.765  58.244 35.896 1 12.76  ? 11  TYR   B CB    1 
ATOM   2071 C CG    . TYR   B 1 30  ? 33.466  57.726 35.32  1 12.58  ? 11  TYR   B CG    1 
ATOM   2072 C CD1   . TYR   B 1 30  ? 32.319  57.643 36.104 1 13.16  ? 11  TYR   B CD1   1 
ATOM   2073 C CD2   . TYR   B 1 30  ? 33.358  57.405 33.971 1 13.46  ? 11  TYR   B CD2   1 
ATOM   2074 C CE1   . TYR   B 1 30  ? 31.121  57.164 35.585 1 11.86  ? 11  TYR   B CE1   1 
ATOM   2075 C CE2   . TYR   B 1 30  ? 32.147  56.967 33.427 1 14     ? 11  TYR   B CE2   1 
ATOM   2076 C CZ    . TYR   B 1 30  ? 31.031  56.852 34.243 1 16.55  ? 11  TYR   B CZ    1 
ATOM   2077 O OH    . TYR   B 1 30  ? 29.827  56.439 33.745 1 17.07  ? 11  TYR   B OH    1 
ATOM   2078 N N     . LEU   B 1 31  ? 36.842  60.61  36.814 1 18.88  ? 12  LEU   B N     1 
ATOM   2079 C CA    . LEU   B 1 31  ? 37.7    61.17  37.861 1 20.17  ? 12  LEU   B CA    1 
ATOM   2080 C C     . LEU   B 1 31  ? 37.298  62.607 38.239 1 23.52  ? 12  LEU   B C     1 
ATOM   2081 O O     . LEU   B 1 31  ? 37.303  62.955 39.422 1 22.57  ? 12  LEU   B O     1 
ATOM   2082 C CB    . LEU   B 1 31  ? 39.171  61.121 37.412 1 20.89  ? 12  LEU   B CB    1 
ATOM   2083 C CG    . LEU   B 1 31  ? 39.781  59.739 37.187 1 26.28  ? 12  LEU   B CG    1 
ATOM   2084 C CD1   . LEU   B 1 31  ? 41.042  59.838 36.347 1 26.61  ? 12  LEU   B CD1   1 
ATOM   2085 C CD2   . LEU   B 1 31  ? 40.11   59.054 38.505 1 30.15  ? 12  LEU   B CD2   1 
ATOM   2086 N N     . SER   B 1 32  ? 36.876  63.405 37.24  1 20.47  ? 13  SER   B N     1 
ATOM   2087 C CA    . SER   B 1 32  ? 36.54   64.813 37.404 1 19.5   ? 13  SER   B CA    1 
ATOM   2088 C C     . SER   B 1 32  ? 35.068  65.181 37.56  1 23.65  ? 13  SER   B C     1 
ATOM   2089 O O     . SER   B 1 32  ? 34.76   66.132 38.293 1 22.64  ? 13  SER   B O     1 
ATOM   2090 C CB    . SER   B 1 32  ? 37.103  65.605 36.227 1 22.05  ? 13  SER   B CB    1 
ATOM   2091 O OG    . SER   B 1 32  ? 36.746  65.025 34.977 1 23.35  ? 13  SER   B OG    1 
ATOM   2092 N N     . HIS   B 1 33  ? 34.172  64.514 36.807 1 19.21  ? 14  HIS   B N     1 
ATOM   2093 C CA    . HIS   B 1 33  ? 32.784  64.931 36.694 1 18.58  ? 14  HIS   B CA    1 
ATOM   2094 C C     . HIS   B 1 33  ? 31.746  64.097 37.419 1 19.77  ? 14  HIS   B C     1 
ATOM   2095 O O     . HIS   B 1 33  ? 30.611  64.55  37.514 1 17.75  ? 14  HIS   B O     1 
ATOM   2096 C CB    . HIS   B 1 33  ? 32.417  65.057 35.215 1 19.88  ? 14  HIS   B CB    1 
ATOM   2097 C CG    . HIS   B 1 33  ? 33.028  66.276 34.605 1 23.68  ? 14  HIS   B CG    1 
ATOM   2098 N ND1   . HIS   B 1 33  ? 34.361  66.303 34.227 1 25.49  ? 14  HIS   B ND1   1 
ATOM   2099 C CD2   . HIS   B 1 33  ? 32.496  67.504 34.422 1 25.41  ? 14  HIS   B CD2   1 
ATOM   2100 C CE1   . HIS   B 1 33  ? 34.587  67.533 33.802 1 24.91  ? 14  HIS   B CE1   1 
ATOM   2101 N NE2   . HIS   B 1 33  ? 33.496  68.292 33.902 1 25.2   ? 14  HIS   B NE2   1 
ATOM   2102 N N     . PHE   B 1 34  ? 32.12   62.935 37.972 1 14.97  ? 15  PHE   B N     1 
ATOM   2103 C CA    . PHE   B 1 34  ? 31.187  62.085 38.717 1 13.34  ? 15  PHE   B CA    1 
ATOM   2104 C C     . PHE   B 1 34  ? 31.243  62.587 40.152 1 16.78  ? 15  PHE   B C     1 
ATOM   2105 O O     . PHE   B 1 34  ? 32.264  62.387 40.828 1 16.34  ? 15  PHE   B O     1 
ATOM   2106 C CB    . PHE   B 1 34  ? 31.619  60.607 38.647 1 14.37  ? 15  PHE   B CB    1 
ATOM   2107 C CG    . PHE   B 1 34  ? 30.601  59.602 39.156 1 15.05  ? 15  PHE   B CG    1 
ATOM   2108 C CD1   . PHE   B 1 34  ? 30.489  59.325 40.512 1 17.34  ? 15  PHE   B CD1   1 
ATOM   2109 C CD2   . PHE   B 1 34  ? 29.785  58.903 38.268 1 16.01  ? 15  PHE   B CD2   1 
ATOM   2110 C CE1   . PHE   B 1 34  ? 29.555  58.389 40.979 1 18.14  ? 15  PHE   B CE1   1 
ATOM   2111 C CE2   . PHE   B 1 34  ? 28.891  57.925 38.73  1 17.95  ? 15  PHE   B CE2   1 
ATOM   2112 C CZ    . PHE   B 1 34  ? 28.781  57.675 40.082 1 16.08  ? 15  PHE   B CZ    1 
ATOM   2113 N N     . ASN   B 1 35  ? 30.191  63.305 40.585 1 11.76  ? 16  ASN   B N     1 
ATOM   2114 C CA    . ASN   B 1 35  ? 30.118  63.871 41.944 1 11.73  ? 16  ASN   B CA    1 
ATOM   2115 C C     . ASN   B 1 35  ? 29.524  62.795 42.882 1 13.5   ? 16  ASN   B C     1 
ATOM   2116 O O     . ASN   B 1 35  ? 28.364  62.436 42.712 1 12.88  ? 16  ASN   B O     1 
ATOM   2117 C CB    . ASN   B 1 35  ? 29.289  65.18  41.944 1 12.95  ? 16  ASN   B CB    1 
ATOM   2118 C CG    . ASN   B 1 35  ? 29.179  65.872 43.287 1 27.07  ? 16  ASN   B CG    1 
ATOM   2119 O OD1   . ASN   B 1 35  ? 29.07   65.254 44.343 1 22.61  ? 16  ASN   B OD1   1 
ATOM   2120 N ND2   . ASN   B 1 35  ? 29.141  67.179 43.277 1 23.53  ? 16  ASN   B ND2   1 
ATOM   2121 N N     . PRO   B 1 36  ? 30.311  62.258 43.842 1 11.09  ? 17  PRO   B N     1 
ATOM   2122 C CA    . PRO   B 1 36  ? 29.817  61.158 44.693 1 11.6   ? 17  PRO   B CA    1 
ATOM   2123 C C     . PRO   B 1 36  ? 28.597  61.481 45.534 1 17.13  ? 17  PRO   B C     1 
ATOM   2124 O O     . PRO   B 1 36  ? 27.679  60.666 45.596 1 15.69  ? 17  PRO   B O     1 
ATOM   2125 C CB    . PRO   B 1 36  ? 31.03   60.829 45.577 1 13.17  ? 17  PRO   B CB    1 
ATOM   2126 C CG    . PRO   B 1 36  ? 32.175  61.338 44.864 1 16.32  ? 17  PRO   B CG    1 
ATOM   2127 C CD    . PRO   B 1 36  ? 31.721  62.561 44.162 1 12.16  ? 17  PRO   B CD    1 
ATOM   2128 N N     . ARG   B 1 37  ? 28.605  62.65  46.206 1 16.59  ? 18  ARG   B N     1 
ATOM   2129 C CA    . ARG   B 1 37  ? 27.506  63.09  47.058 1 17.24  ? 18  ARG   B CA    1 
ATOM   2130 C C     . ARG   B 1 37  ? 26.253  63.286 46.242 1 18     ? 18  ARG   B C     1 
ATOM   2131 O O     . ARG   B 1 37  ? 25.193  62.847 46.67  1 17.12  ? 18  ARG   B O     1 
ATOM   2132 C CB    . ARG   B 1 37  ? 27.858  64.376 47.821 1 21.31  ? 18  ARG   B CB    1 
ATOM   2133 C CG    . ARG   B 1 37  ? 28.686  64.157 49.081 1 37.32  ? 18  ARG   B CG    1 
ATOM   2134 C CD    . ARG   B 1 37  ? 30.111  64.686 48.967 1 55.59  ? 18  ARG   B CD    1 
ATOM   2135 N NE    . ARG   B 1 37  ? 30.175  66.088 48.543 1 69.25  ? 18  ARG   B NE    1 
ATOM   2136 C CZ    . ARG   B 1 37  ? 30.624  66.496 47.357 1 84.72  ? 18  ARG   B CZ    1 
ATOM   2137 N NH1   . ARG   B 1 37  ? 30.638  67.787 47.055 1 71.25  ? 18  ARG   B NH1   1 
ATOM   2138 N NH2   . ARG   B 1 37  ? 31.06   65.613 46.464 1 71.18  ? 18  ARG   B NH2   1 
ATOM   2139 N N     . ASP   B 1 38  ? 26.375  63.877 45.044 1 15.17  ? 19  ASP   B N     1 
ATOM   2140 C CA    . ASP   B 1 38  ? 25.227  64.119 44.17  1 15.89  ? 19  ASP   B CA    1 
ATOM   2141 C C     . ASP   B 1 38  ? 24.624  62.806 43.653 1 18.79  ? 19  ASP   B C     1 
ATOM   2142 O O     . ASP   B 1 38  ? 23.405  62.659 43.609 1 18.31  ? 19  ASP   B O     1 
ATOM   2143 C CB    . ASP   B 1 38  ? 25.604  65.065 43.02  1 18.41  ? 19  ASP   B CB    1 
ATOM   2144 C CG    . ASP   B 1 38  ? 24.411  65.754 42.398 1 34.28  ? 19  ASP   B CG    1 
ATOM   2145 O OD1   . ASP   B 1 38  ? 23.455  66.079 43.143 1 35.59  ? 19  ASP   B OD1   1 
ATOM   2146 O OD2   . ASP   B 1 38  ? 24.443  66.004 41.174 1 43.08  ? 19  ASP   B OD2   1 
ATOM   2147 N N     . TYR   B 1 39  ? 25.479  61.834 43.324 1 15.77  ? 20  TYR   B N     1 
ATOM   2148 C CA    . TYR   B 1 39  ? 25.028  60.504 42.878 1 14.59  ? 20  TYR   B CA    1 
ATOM   2149 C C     . TYR   B 1 39  ? 24.207  59.802 43.971 1 17.4   ? 20  TYR   B C     1 
ATOM   2150 O O     . TYR   B 1 39  ? 23.141  59.267 43.674 1 16.69  ? 20  TYR   B O     1 
ATOM   2151 C CB    . TYR   B 1 39  ? 26.234  59.654 42.47  1 13.82  ? 20  TYR   B CB    1 
ATOM   2152 C CG    . TYR   B 1 39  ? 25.875  58.274 41.976 1 12.52  ? 20  TYR   B CG    1 
ATOM   2153 C CD1   . TYR   B 1 39  ? 25.269  58.091 40.735 1 14.05  ? 20  TYR   B CD1   1 
ATOM   2154 C CD2   . TYR   B 1 39  ? 26.183  57.142 42.726 1 12.26  ? 20  TYR   B CD2   1 
ATOM   2155 C CE1   . TYR   B 1 39  ? 25.012  56.813 40.237 1 13.6   ? 20  TYR   B CE1   1 
ATOM   2156 C CE2   . TYR   B 1 39  ? 25.898  55.864 42.254 1 12.87  ? 20  TYR   B CE2   1 
ATOM   2157 C CZ    . TYR   B 1 39  ? 25.322  55.705 41.004 1 17.84  ? 20  TYR   B CZ    1 
ATOM   2158 O OH    . TYR   B 1 39  ? 25.041  54.454 40.532 1 17.06  ? 20  TYR   B OH    1 
ATOM   2159 N N     . LEU   B 1 40  ? 24.674  59.866 45.238 1 14.48  ? 21  LEU   B N     1 
ATOM   2160 C CA    . LEU   B 1 40  ? 23.989  59.273 46.394 1 14.91  ? 21  LEU   B CA    1 
ATOM   2161 C C     . LEU   B 1 40  ? 22.641  59.947 46.675 1 21.38  ? 21  LEU   B C     1 
ATOM   2162 O O     . LEU   B 1 40  ? 21.638  59.258 46.912 1 21.18  ? 21  LEU   B O     1 
ATOM   2163 C CB    . LEU   B 1 40  ? 24.887  59.325 47.646 1 14.49  ? 21  LEU   B CB    1 
ATOM   2164 C CG    . LEU   B 1 40  ? 26.158  58.5   47.598 1 17.54  ? 21  LEU   B CG    1 
ATOM   2165 C CD1   . LEU   B 1 40  ? 27.022  58.779 48.794 1 17.44  ? 21  LEU   B CD1   1 
ATOM   2166 C CD2   . LEU   B 1 40  ? 25.853  57.046 47.491 1 18.16  ? 21  LEU   B CD2   1 
ATOM   2167 N N     . GLU   B 1 41  ? 22.611  61.284 46.593 1 18.76  ? 22  GLU   B N     1 
ATOM   2168 C CA    . GLU   B 1 41  ? 21.413  62.099 46.792 1 19.6   ? 22  GLU   B CA    1 
ATOM   2169 C C     . GLU   B 1 41  ? 20.35   61.791 45.709 1 24.29  ? 22  GLU   B C     1 
ATOM   2170 O O     . GLU   B 1 41  ? 19.163  61.698 46.022 1 23.76  ? 22  GLU   B O     1 
ATOM   2171 C CB    . GLU   B 1 41  ? 21.795  63.601 46.771 1 21.48  ? 22  GLU   B CB    1 
ATOM   2172 C CG    . GLU   B 1 41  ? 20.939  64.488 47.668 1 35     ? 22  GLU   B CG    1 
ATOM   2173 C CD    . GLU   B 1 41  ? 20.85   64.095 49.134 1 55.83  ? 22  GLU   B CD    1 
ATOM   2174 O OE1   . GLU   B 1 41  ? 21.868  63.634 49.701 1 48.36  ? 22  GLU   B OE1   1 
ATOM   2175 O OE2   . GLU   B 1 41  ? 19.752  64.249 49.716 1 56.45  ? 22  GLU   B OE2   1 
ATOM   2176 N N     . LYS   B 1 42  ? 20.791  61.586 44.457 1 20.2   ? 23  LYS   B N     1 
ATOM   2177 C CA    . LYS   B 1 42  ? 19.893  61.328 43.332 1 20.13  ? 23  LYS   B CA    1 
ATOM   2178 C C     . LYS   B 1 42  ? 19.353  59.913 43.242 1 22.41  ? 23  LYS   B C     1 
ATOM   2179 O O     . LYS   B 1 42  ? 18.226  59.728 42.786 1 23.33  ? 23  LYS   B O     1 
ATOM   2180 C CB    . LYS   B 1 42  ? 20.558  61.713 42.001 1 22.36  ? 23  LYS   B CB    1 
ATOM   2181 C CG    . LYS   B 1 42  ? 20.077  63.045 41.448 1 31.69  ? 23  LYS   B CG    1 
ATOM   2182 C CD    . LYS   B 1 42  ? 20.772  64.234 42.09  1 38.96  ? 23  LYS   B CD    1 
ATOM   2183 C CE    . LYS   B 1 42  ? 20.201  65.541 41.598 1 40.97  ? 23  LYS   B CE    1 
ATOM   2184 N NZ    . LYS   B 1 42  ? 20.851  66.692 42.272 1 42.9   ? 23  LYS   B NZ    1 
ATOM   2185 N N     . TYR   B 1 43  ? 20.137  58.915 43.637 1 16.61  ? 24  TYR   B N     1 
ATOM   2186 C CA    . TYR   B 1 43  ? 19.688  57.534 43.46  1 15.21  ? 24  TYR   B CA    1 
ATOM   2187 C C     . TYR   B 1 43  ? 19.459  56.738 44.722 1 18.32  ? 24  TYR   B C     1 
ATOM   2188 O O     . TYR   B 1 43  ? 18.746  55.734 44.657 1 17.8   ? 24  TYR   B O     1 
ATOM   2189 C CB    . TYR   B 1 43  ? 20.698  56.785 42.565 1 15.2   ? 24  TYR   B CB    1 
ATOM   2190 C CG    . TYR   B 1 43  ? 20.691  57.221 41.116 1 14.1   ? 24  TYR   B CG    1 
ATOM   2191 C CD1   . TYR   B 1 43  ? 19.767  56.696 40.216 1 14.94  ? 24  TYR   B CD1   1 
ATOM   2192 C CD2   . TYR   B 1 43  ? 21.633  58.132 40.632 1 14.37  ? 24  TYR   B CD2   1 
ATOM   2193 C CE1   . TYR   B 1 43  ? 19.762  57.078 38.875 1 14.03  ? 24  TYR   B CE1   1 
ATOM   2194 C CE2   . TYR   B 1 43  ? 21.63   58.533 39.287 1 14.31  ? 24  TYR   B CE2   1 
ATOM   2195 C CZ    . TYR   B 1 43  ? 20.694  57.995 38.412 1 16.58  ? 24  TYR   B CZ    1 
ATOM   2196 O OH    . TYR   B 1 43  ? 20.665  58.337 37.078 1 12.82  ? 24  TYR   B OH    1 
ATOM   2197 N N     . TYR   B 1 44  ? 20.09   57.135 45.849 1 15.98  ? 25  TYR   B N     1 
ATOM   2198 C CA    . TYR   B 1 44  ? 20.113  56.333 47.07  1 16.44  ? 25  TYR   B CA    1 
ATOM   2199 C C     . TYR   B 1 44  ? 19.663  57.024 48.364 1 25.56  ? 25  TYR   B C     1 
ATOM   2200 O O     . TYR   B 1 44  ? 19.895  56.463 49.446 1 25.04  ? 25  TYR   B O     1 
ATOM   2201 C CB    . TYR   B 1 44  ? 21.525  55.746 47.247 1 16.9   ? 25  TYR   B CB    1 
ATOM   2202 C CG    . TYR   B 1 44  ? 21.905  54.842 46.094 1 17     ? 25  TYR   B CG    1 
ATOM   2203 C CD1   . TYR   B 1 44  ? 21.36   53.568 45.974 1 17.68  ? 25  TYR   B CD1   1 
ATOM   2204 C CD2   . TYR   B 1 44  ? 22.756  55.289 45.081 1 17.19  ? 25  TYR   B CD2   1 
ATOM   2205 C CE1   . TYR   B 1 44  ? 21.626  52.767 44.865 1 17.08  ? 25  TYR   B CE1   1 
ATOM   2206 C CE2   . TYR   B 1 44  ? 23.04   54.49  43.97  1 16.85  ? 25  TYR   B CE2   1 
ATOM   2207 C CZ    . TYR   B 1 44  ? 22.477  53.229 43.87  1 21.95  ? 25  TYR   B CZ    1 
ATOM   2208 O OH    . TYR   B 1 44  ? 22.747  52.429 42.787 1 20.44  ? 25  TYR   B OH    1 
ATOM   2209 N N     . LYS   B 1 45  ? 18.954  58.162 48.279 1 26.59  ? 26  LYS   B N     1 
ATOM   2210 C CA    . LYS   B 1 45  ? 18.474  58.822 49.51  1 29.14  ? 26  LYS   B CA    1 
ATOM   2211 C C     . LYS   B 1 45  ? 17.377  57.988 50.237 1 35.33  ? 26  LYS   B C     1 
ATOM   2212 O O     . LYS   B 1 45  ? 17.248  58.082 51.463 1 36.14  ? 26  LYS   B O     1 
ATOM   2213 C CB    . LYS   B 1 45  ? 18.056  60.286 49.283 1 32.78  ? 26  LYS   B CB    1 
ATOM   2214 C CG    . LYS   B 1 45  ? 16.901  60.498 48.312 1 56.35  ? 26  LYS   B CG    1 
ATOM   2215 C CD    . LYS   B 1 45  ? 16.43   61.953 48.34  1 67.37  ? 26  LYS   B CD    1 
ATOM   2216 C CE    . LYS   B 1 45  ? 14.997  62.108 47.879 1 77.05  ? 26  LYS   B CE    1 
ATOM   2217 N NZ    . LYS   B 1 45  ? 14.021  61.554 48.86  1 83.18  ? 26  LYS   B NZ    1 
ATOM   2218 N N     . PHE   B 1 46  ? 16.658  57.134 49.476 1 32.64  ? 27  PHE   B N     1 
ATOM   2219 C CA    . PHE   B 1 46  ? 15.648  56.158 49.913 1 32.93  ? 27  PHE   B CA    1 
ATOM   2220 C C     . PHE   B 1 46  ? 14.522  56.765 50.779 1 38.71  ? 27  PHE   B C     1 
ATOM   2221 O O     . PHE   B 1 46  ? 14.25   56.282 51.885 1 37.18  ? 27  PHE   B O     1 
ATOM   2222 C CB    . PHE   B 1 46  ? 16.338  54.963 50.621 1 34.24  ? 27  PHE   B CB    1 
ATOM   2223 C CG    . PHE   B 1 46  ? 15.615  53.635 50.588 1 34.85  ? 27  PHE   B CG    1 
ATOM   2224 C CD1   . PHE   B 1 46  ? 15.149  53.106 49.387 1 37.22  ? 27  PHE   B CD1   1 
ATOM   2225 C CD2   . PHE   B 1 46  ? 15.471  52.877 51.741 1 36.79  ? 27  PHE   B CD2   1 
ATOM   2226 C CE1   . PHE   B 1 46  ? 14.524  51.859 49.35  1 38.41  ? 27  PHE   B CE1   1 
ATOM   2227 C CE2   . PHE   B 1 46  ? 14.84   51.631 51.707 1 39.51  ? 27  PHE   B CE2   1 
ATOM   2228 C CZ    . PHE   B 1 46  ? 14.365  51.132 50.514 1 37.84  ? 27  PHE   B CZ    1 
ATOM   2229 N N     . GLY   B 1 47  ? 13.892  57.81  50.246 1 37.6   ? 28  GLY   B N     1 
ATOM   2230 C CA    . GLY   B 1 47  ? 12.788  58.519 50.882 1 38.39  ? 28  GLY   B CA    1 
ATOM   2231 C C     . GLY   B 1 47  ? 11.464  57.783 50.794 1 43.96  ? 28  GLY   B C     1 
ATOM   2232 O O     . GLY   B 1 47  ? 11.292  56.887 49.955 1 43.06  ? 28  GLY   B O     1 
ATOM   2233 N N     . SER   B 1 48  ? 10.511  58.18  51.661 1 42.5   ? 29  SER   B N     1 
ATOM   2234 C CA    . SER   B 1 48  ? 9.161   57.608 51.774 1 42.91  ? 29  SER   B CA    1 
ATOM   2235 C C     . SER   B 1 48  ? 8.294   57.746 50.51  1 48.23  ? 29  SER   B C     1 
ATOM   2236 O O     . SER   B 1 48  ? 7.338   56.976 50.35  1 47.9   ? 29  SER   B O     1 
ATOM   2237 C CB    . SER   B 1 48  ? 8.431   58.176 52.989 1 45.67  ? 29  SER   B CB    1 
ATOM   2238 O OG    . SER   B 1 48  ? 8.311   59.588 52.92  1 52.6   ? 29  SER   B OG    1 
ATOM   2239 N N     . ARG   B 1 49  ? 8.617   58.706 49.613 1 45.82  ? 30  ARG   B N     1 
ATOM   2240 C CA    . ARG   B 1 49  ? 7.869   58.866 48.366 1 46.1   ? 30  ARG   B CA    1 
ATOM   2241 C C     . ARG   B 1 49  ? 8.343   57.825 47.356 1 49.86  ? 30  ARG   B C     1 
ATOM   2242 O O     . ARG   B 1 49  ? 9.539   57.758 47.045 1 50.11  ? 30  ARG   B O     1 
ATOM   2243 C CB    . ARG   B 1 49  ? 7.941   60.309 47.828 1 48.25  ? 30  ARG   B CB    1 
ATOM   2244 C CG    . ARG   B 1 49  ? 6.634   60.798 47.181 1 62.8   ? 30  ARG   B CG    1 
ATOM   2245 C CD    . ARG   B 1 49  ? 5.417   60.711 48.11  1 74.56  ? 30  ARG   B CD    1 
ATOM   2246 N NE    . ARG   B 1 49  ? 4.997   62.008 48.65  1 83.89  ? 30  ARG   B NE    1 
ATOM   2247 C CZ    . ARG   B 1 49  ? 5.5     62.578 49.743 1 97.52  ? 30  ARG   B CZ    1 
ATOM   2248 N NH1   . ARG   B 1 49  ? 6.481   61.989 50.417 1 86.26  ? 30  ARG   B NH1   1 
ATOM   2249 N NH2   . ARG   B 1 49  ? 5.037   63.747 50.161 1 82.96  ? 30  ARG   B NH2   1 
ATOM   2250 N N     . HIS   B 1 50  ? 7.4     56.977 46.902 1 45.38  ? 31  HIS   B N     1 
ATOM   2251 C CA    . HIS   B 1 50  ? 7.597   55.824 46.015 1 44.61  ? 31  HIS   B CA    1 
ATOM   2252 C C     . HIS   B 1 50  ? 8.093   56.17  44.587 1 43.01  ? 31  HIS   B C     1 
ATOM   2253 O O     . HIS   B 1 50  ? 7.363   55.989 43.6   1 43.91  ? 31  HIS   B O     1 
ATOM   2254 C CB    . HIS   B 1 50  ? 6.317   54.969 45.959 1 46.51  ? 31  HIS   B CB    1 
ATOM   2255 C CG    . HIS   B 1 50  ? 5.59    54.875 47.268 1 50.8   ? 31  HIS   B CG    1 
ATOM   2256 N ND1   . HIS   B 1 50  ? 4.621   55.804 47.627 1 52.84  ? 31  HIS   B ND1   1 
ATOM   2257 C CD2   . HIS   B 1 50  ? 5.715   53.965 48.264 1 53.04  ? 31  HIS   B CD2   1 
ATOM   2258 C CE1   . HIS   B 1 50  ? 4.188   55.428 48.819 1 52.5   ? 31  HIS   B CE1   1 
ATOM   2259 N NE2   . HIS   B 1 50  ? 4.821   54.33  49.247 1 52.88  ? 31  HIS   B NE2   1 
ATOM   2260 N N     . SER   B 1 51  ? 9.356   56.609 44.48  1 32.5   ? 32  SER   B N     1 
ATOM   2261 C CA    . SER   B 1 51  ? 9.992   56.919 43.192 1 29.07  ? 32  SER   B CA    1 
ATOM   2262 C C     . SER   B 1 51  ? 10.496  55.634 42.537 1 27.09  ? 32  SER   B C     1 
ATOM   2263 O O     . SER   B 1 51  ? 10.698  54.634 43.223 1 25.19  ? 32  SER   B O     1 
ATOM   2264 C CB    . SER   B 1 51  ? 11.164  57.87  43.402 1 30.05  ? 32  SER   B CB    1 
ATOM   2265 O OG    . SER   B 1 51  ? 12.165  57.245 44.191 1 36.92  ? 32  SER   B OG    1 
ATOM   2266 N N     . ALA   B 1 52  ? 10.743  55.671 41.22  1 21.85  ? 33  ALA   B N     1 
ATOM   2267 C CA    . ALA   B 1 52  ? 11.292  54.536 40.462 1 20.32  ? 33  ALA   B CA    1 
ATOM   2268 C C     . ALA   B 1 52  ? 12.679  54.123 41.004 1 20.9   ? 33  ALA   B C     1 
ATOM   2269 O O     . ALA   B 1 52  ? 12.983  52.934 41.044 1 18.94  ? 33  ALA   B O     1 
ATOM   2270 C CB    . ALA   B 1 52  ? 11.379  54.886 38.982 1 20.33  ? 33  ALA   B CB    1 
ATOM   2271 N N     . GLU   B 1 53  ? 13.473  55.108 41.497 1 19.57  ? 34  GLU   B N     1 
ATOM   2272 C CA    . GLU   B 1 53  ? 14.831  54.94  42.072 1 18.92  ? 34  GLU   B CA    1 
ATOM   2273 C C     . GLU   B 1 53  ? 14.833  54.1   43.351 1 21.72  ? 34  GLU   B C     1 
ATOM   2274 O O     . GLU   B 1 53  ? 15.716  53.256 43.542 1 20.4   ? 34  GLU   B O     1 
ATOM   2275 C CB    . GLU   B 1 53  ? 15.506  56.315 42.3   1 19.92  ? 34  GLU   B CB    1 
ATOM   2276 C CG    . GLU   B 1 53  ? 15.993  56.984 41.013 1 26.4   ? 34  GLU   B CG    1 
ATOM   2277 C CD    . GLU   B 1 53  ? 14.912  57.365 40.017 1 37.7   ? 34  GLU   B CD    1 
ATOM   2278 O OE1   . GLU   B 1 53  ? 13.917  58     40.436 1 21.42  ? 34  GLU   B OE1   1 
ATOM   2279 O OE2   . GLU   B 1 53  ? 15.026  56.974 38.833 1 23.54  ? 34  GLU   B OE2   1 
ATOM   2280 N N     . SER   B 1 54  ? 13.819  54.304 44.206 1 18.9   ? 35  SER   B N     1 
ATOM   2281 C CA    . SER   B 1 54  ? 13.644  53.549 45.446 1 18.46  ? 35  SER   B CA    1 
ATOM   2282 C C     . SER   B 1 54  ? 13.074  52.166 45.156 1 21.45  ? 35  SER   B C     1 
ATOM   2283 O O     . SER   B 1 54  ? 13.407  51.218 45.87  1 21.15  ? 35  SER   B O     1 
ATOM   2284 C CB    . SER   B 1 54  ? 12.752  54.31  46.417 1 21.8   ? 35  SER   B CB    1 
ATOM   2285 O OG    . SER   B 1 54  ? 13.329  55.575 46.702 1 30.19  ? 35  SER   B OG    1 
ATOM   2286 N N     . GLN   B 1 55  ? 12.227  52.035 44.108 1 17     ? 36  GLN   B N     1 
ATOM   2287 C CA    . GLN   B 1 55  ? 11.674  50.734 43.705 1 17.05  ? 36  GLN   B CA    1 
ATOM   2288 C C     . GLN   B 1 55  ? 12.79   49.828 43.158 1 21.24  ? 36  GLN   B C     1 
ATOM   2289 O O     . GLN   B 1 55  ? 12.842  48.633 43.475 1 20.82  ? 36  GLN   B O     1 
ATOM   2290 C CB    . GLN   B 1 55  ? 10.551  50.916 42.668 1 18.74  ? 36  GLN   B CB    1 
ATOM   2291 C CG    . GLN   B 1 55  ? 9.264   51.539 43.258 1 22.52  ? 36  GLN   B CG    1 
ATOM   2292 C CD    . GLN   B 1 55  ? 8.659   50.652 44.313 1 49.6   ? 36  GLN   B CD    1 
ATOM   2293 O OE1   . GLN   B 1 55  ? 8.714   50.956 45.511 1 50.66  ? 36  GLN   B OE1   1 
ATOM   2294 N NE2   . GLN   B 1 55  ? 8.151   49.494 43.901 1 40.93  ? 36  GLN   B NE2   1 
ATOM   2295 N N     . ILE   B 1 56  ? 13.716  50.422 42.378 1 17.57  ? 37  ILE   B N     1 
ATOM   2296 C CA    . ILE   B 1 56  ? 14.871  49.703 41.842 1 16.95  ? 37  ILE   B CA    1 
ATOM   2297 C C     . ILE   B 1 56  ? 15.778  49.32  42.988 1 19.62  ? 37  ILE   B C     1 
ATOM   2298 O O     . ILE   B 1 56  ? 16.13   48.142 43.073 1 20.02  ? 37  ILE   B O     1 
ATOM   2299 C CB    . ILE   B 1 56  ? 15.592  50.443 40.683 1 19.39  ? 37  ILE   B CB    1 
ATOM   2300 C CG1   . ILE   B 1 56  ? 14.69   50.422 39.44  1 19.56  ? 37  ILE   B CG1   1 
ATOM   2301 C CG2   . ILE   B 1 56  ? 16.96   49.791 40.37  1 18.66  ? 37  ILE   B CG2   1 
ATOM   2302 C CD1   . ILE   B 1 56  ? 14.852  51.526 38.57  1 26.67  ? 37  ILE   B CD1   1 
ATOM   2303 N N     . LEU   B 1 57  ? 16.083  50.282 43.911 1 15.26  ? 38  LEU   B N     1 
ATOM   2304 C CA    . LEU   B 1 57  ? 16.91   50.001 45.086 1 15.96  ? 38  LEU   B CA    1 
ATOM   2305 C C     . LEU   B 1 57  ? 16.344  48.806 45.873 1 20.7   ? 38  LEU   B C     1 
ATOM   2306 O O     . LEU   B 1 57  ? 17.083  47.869 46.132 1 20.67  ? 38  LEU   B O     1 
ATOM   2307 C CB    . LEU   B 1 57  ? 17.083  51.235 45.991 1 16.38  ? 38  LEU   B CB    1 
ATOM   2308 C CG    . LEU   B 1 57  ? 18.049  51.105 47.189 1 20.8   ? 38  LEU   B CG    1 
ATOM   2309 C CD1   . LEU   B 1 57  ? 19.387  50.467 46.777 1 20.68  ? 38  LEU   B CD1   1 
ATOM   2310 C CD2   . LEU   B 1 57  ? 18.295  52.447 47.817 1 20.78  ? 38  LEU   B CD2   1 
ATOM   2311 N N     . LYS   B 1 58  ? 15.034  48.817 46.189 1 17.91  ? 39  LYS   B N     1 
ATOM   2312 C CA    . LYS   B 1 58  ? 14.355  47.715 46.884 1 18.36  ? 39  LYS   B CA    1 
ATOM   2313 C C     . LYS   B 1 58  ? 14.527  46.385 46.114 1 24.62  ? 39  LYS   B C     1 
ATOM   2314 O O     . LYS   B 1 58  ? 14.832  45.36  46.722 1 23.12  ? 39  LYS   B O     1 
ATOM   2315 C CB    . LYS   B 1 58  ? 12.864  48.029 47.026 1 19.55  ? 39  LYS   B CB    1 
ATOM   2316 C CG    . LYS   B 1 58  ? 12.507  48.972 48.156 1 30.78  ? 39  LYS   B CG    1 
ATOM   2317 C CD    . LYS   B 1 58  ? 11.009  49.251 48.125 1 35.36  ? 39  LYS   B CD    1 
ATOM   2318 C CE    . LYS   B 1 58  ? 10.593  50.272 49.145 1 51.32  ? 39  LYS   B CE    1 
ATOM   2319 N NZ    . LYS   B 1 58  ? 9.26    50.838 48.814 1 66.98  ? 39  LYS   B NZ    1 
ATOM   2320 N N     . HIS   B 1 59  ? 14.359  46.401 44.781 1 24.91  ? 40  HIS   B N     1 
ATOM   2321 C CA    . HIS   B 1 59  ? 14.531  45.179 43.999 1 26.45  ? 40  HIS   B CA    1 
ATOM   2322 C C     . HIS   B 1 59  ? 15.953  44.633 44.052 1 25.78  ? 40  HIS   B C     1 
ATOM   2323 O O     . HIS   B 1 59  ? 16.128  43.427 44.207 1 24.25  ? 40  HIS   B O     1 
ATOM   2324 C CB    . HIS   B 1 59  ? 14.069  45.341 42.552 1 29.64  ? 40  HIS   B CB    1 
ATOM   2325 C CG    . HIS   B 1 59  ? 13.505  44.069 42.003 1 35.63  ? 40  HIS   B CG    1 
ATOM   2326 N ND1   . HIS   B 1 59  ? 12.144  43.934 41.748 1 38.63  ? 40  HIS   B ND1   1 
ATOM   2327 C CD2   . HIS   B 1 59  ? 14.123  42.894 41.729 1 38.69  ? 40  HIS   B CD2   1 
ATOM   2328 C CE1   . HIS   B 1 59  ? 11.986  42.697 41.297 1 38.88  ? 40  HIS   B CE1   1 
ATOM   2329 N NE2   . HIS   B 1 59  ? 13.144  42.023 41.287 1 39.21  ? 40  HIS   B NE2   1 
ATOM   2330 N N     . LEU   B 1 60  ? 16.965  45.514 43.929 1 21.6   ? 41  LEU   B N     1 
ATOM   2331 C CA    . LEU   B 1 60  ? 18.375  45.115 43.973 1 20.49  ? 41  LEU   B CA    1 
ATOM   2332 C C     . LEU   B 1 60  ? 18.682  44.426 45.305 1 21.28  ? 41  LEU   B C     1 
ATOM   2333 O O     . LEU   B 1 60  ? 19.218  43.31  45.302 1 19.12  ? 41  LEU   B O     1 
ATOM   2334 C CB    . LEU   B 1 60  ? 19.313  46.325 43.736 1 20.75  ? 41  LEU   B CB    1 
ATOM   2335 C CG    . LEU   B 1 60  ? 19.265  46.975 42.327 1 25.46  ? 41  LEU   B CG    1 
ATOM   2336 C CD1   . LEU   B 1 60  ? 20.001  48.304 42.305 1 24.67  ? 41  LEU   B CD1   1 
ATOM   2337 C CD2   . LEU   B 1 60  ? 19.775  46.031 41.234 1 27.68  ? 41  LEU   B CD2   1 
ATOM   2338 N N     . LEU   B 1 61  ? 18.252  45.053 46.425 1 17.52  ? 42  LEU   B N     1 
ATOM   2339 C CA    . LEU   B 1 61  ? 18.449  44.542 47.786 1 17.49  ? 42  LEU   B CA    1 
ATOM   2340 C C     . LEU   B 1 61  ? 17.824  43.172 47.996 1 22.09  ? 42  LEU   B C     1 
ATOM   2341 O O     . LEU   B 1 61  ? 18.495  42.268 48.501 1 21.67  ? 42  LEU   B O     1 
ATOM   2342 C CB    . LEU   B 1 61  ? 17.968  45.556 48.834 1 18.07  ? 42  LEU   B CB    1 
ATOM   2343 C CG    . LEU   B 1 61  ? 18.789  46.855 48.95  1 22.54  ? 42  LEU   B CG    1 
ATOM   2344 C CD1   . LEU   B 1 61  ? 18.057  47.901 49.764 1 22.77  ? 42  LEU   B CD1   1 
ATOM   2345 C CD2   . LEU   B 1 61  ? 20.191  46.602 49.525 1 23.25  ? 42  LEU   B CD2   1 
ATOM   2346 N N     . LYS   B 1 62  ? 16.565  42.993 47.558 1 18.94  ? 43  LYS   B N     1 
ATOM   2347 C CA    . LYS   B 1 62  ? 15.887  41.694 47.647 1 18.56  ? 43  LYS   B CA    1 
ATOM   2348 C C     . LYS   B 1 62  ? 16.654  40.63  46.819 1 20.9   ? 43  LYS   B C     1 
ATOM   2349 O O     . LYS   B 1 62  ? 16.867  39.526 47.309 1 21.42  ? 43  LYS   B O     1 
ATOM   2350 C CB    . LYS   B 1 62  ? 14.418  41.805 47.193 1 20.09  ? 43  LYS   B CB    1 
ATOM   2351 C CG    . LYS   B 1 62  ? 13.525  42.598 48.157 1 26.71  ? 43  LYS   B CG    1 
ATOM   2352 C CD    . LYS   B 1 62  ? 12.068  42.63  47.685 1 28.01  ? 43  LYS   B CD    1 
ATOM   2353 C CE    . LYS   B 1 62  ? 11.703  43.91  46.979 1 34.72  ? 43  LYS   B CE    1 
ATOM   2354 N NZ    . LYS   B 1 62  ? 10.309  43.875 46.469 1 31.74  ? 43  LYS   B NZ    1 
ATOM   2355 N N     . ASN   B 1 63  ? 17.131  40.982 45.605 1 16.3   ? 44  ASN   B N     1 
ATOM   2356 C CA    . ASN   B 1 63  ? 17.908  40.031 44.782 1 16.02  ? 44  ASN   B CA    1 
ATOM   2357 C C     . ASN   B 1 63  ? 19.282  39.7   45.377 1 18.12  ? 44  ASN   B C     1 
ATOM   2358 O O     . ASN   B 1 63  ? 19.728  38.565 45.245 1 18.64  ? 44  ASN   B O     1 
ATOM   2359 C CB    . ASN   B 1 63  ? 18.059  40.531 43.352 1 20.58  ? 44  ASN   B CB    1 
ATOM   2360 C CG    . ASN   B 1 63  ? 16.914  40.156 42.457 1 41.47  ? 44  ASN   B CG    1 
ATOM   2361 O OD1   . ASN   B 1 63  ? 15.732  40.302 42.79  1 35.48  ? 44  ASN   B OD1   1 
ATOM   2362 N ND2   . ASN   B 1 63  ? 17.251  39.675 41.288 1 36.02  ? 44  ASN   B ND2   1 
ATOM   2363 N N     . LEU   B 1 64  ? 19.94   40.681 46.032 1 13.07  ? 45  LEU   B N     1 
ATOM   2364 C CA    . LEU   B 1 64  ? 21.233  40.498 46.701 1 12.71  ? 45  LEU   B CA    1 
ATOM   2365 C C     . LEU   B 1 64  ? 21.063  39.622 47.952 1 19.35  ? 45  LEU   B C     1 
ATOM   2366 O O     . LEU   B 1 64  ? 21.926  38.796 48.251 1 19.16  ? 45  LEU   B O     1 
ATOM   2367 C CB    . LEU   B 1 64  ? 21.861  41.86  47.079 1 12.48  ? 45  LEU   B CB    1 
ATOM   2368 C CG    . LEU   B 1 64  ? 22.399  42.699 45.923 1 16.1   ? 45  LEU   B CG    1 
ATOM   2369 C CD1   . LEU   B 1 64  ? 22.467  44.162 46.305 1 15.53  ? 45  LEU   B CD1   1 
ATOM   2370 C CD2   . LEU   B 1 64  ? 23.745  42.155 45.414 1 17.75  ? 45  LEU   B CD2   1 
ATOM   2371 N N     . PHE   B 1 65  ? 19.95   39.798 48.675 1 17.54  ? 46  PHE   B N     1 
ATOM   2372 C CA    . PHE   B 1 65  ? 19.647  38.964 49.841 1 18.99  ? 46  PHE   B CA    1 
ATOM   2373 C C     . PHE   B 1 65  ? 19.424  37.513 49.373 1 22.96  ? 46  PHE   B C     1 
ATOM   2374 O O     . PHE   B 1 65  ? 19.967  36.594 49.98  1 23.24  ? 46  PHE   B O     1 
ATOM   2375 C CB    . PHE   B 1 65  ? 18.42   39.502 50.6   1 21.88  ? 46  PHE   B CB    1 
ATOM   2376 C CG    . PHE   B 1 65  ? 17.904  38.576 51.686 1 25.21  ? 46  PHE   B CG    1 
ATOM   2377 C CD1   . PHE   B 1 65  ? 18.685  38.263 52.788 1 29.63  ? 46  PHE   B CD1   1 
ATOM   2378 C CD2   . PHE   B 1 65  ? 16.641  38.006 51.593 1 28.47  ? 46  PHE   B CD2   1 
ATOM   2379 C CE1   . PHE   B 1 65  ? 18.208  37.391 53.785 1 30.88  ? 46  PHE   B CE1   1 
ATOM   2380 C CE2   . PHE   B 1 65  ? 16.168  37.146 52.591 1 31.71  ? 46  PHE   B CE2   1 
ATOM   2381 C CZ    . PHE   B 1 65  ? 16.956  36.84  53.675 1 29.54  ? 46  PHE   B CZ    1 
ATOM   2382 N N     . LYS   B 1 66  ? 18.669  37.33  48.26  1 19.94  ? 47  LYS   B N     1 
ATOM   2383 C CA    . LYS   B 1 66  ? 18.366  36.034 47.643 1 19.84  ? 47  LYS   B CA    1 
ATOM   2384 C C     . LYS   B 1 66  ? 19.632  35.278 47.271 1 25.44  ? 47  LYS   B C     1 
ATOM   2385 O O     . LYS   B 1 66  ? 19.741  34.092 47.593 1 26.58  ? 47  LYS   B O     1 
ATOM   2386 C CB    . LYS   B 1 66  ? 17.468  36.211 46.402 1 22     ? 47  LYS   B CB    1 
ATOM   2387 C CG    . LYS   B 1 66  ? 16.692  34.944 46.011 1 29.67  ? 47  LYS   B CG    1 
ATOM   2388 C CD    . LYS   B 1 66  ? 15.772  35.164 44.795 1 34.86  ? 47  LYS   B CD    1 
ATOM   2389 C CE    . LYS   B 1 66  ? 16.346  34.65  43.493 1 50.24  ? 47  LYS   B CE    1 
ATOM   2390 N NZ    . LYS   B 1 66  ? 17.459  35.503 42.982 1 65.49  ? 47  LYS   B NZ    1 
ATOM   2391 N N     . ILE   B 1 67  ? 20.589  35.963 46.607 1 20.85  ? 48  ILE   B N     1 
ATOM   2392 C CA    . ILE   B 1 67  ? 21.866  35.382 46.186 1 19.94  ? 48  ILE   B CA    1 
ATOM   2393 C C     . ILE   B 1 67  ? 22.773  35.012 47.367 1 23.08  ? 48  ILE   B C     1 
ATOM   2394 O O     . ILE   B 1 67  ? 23.343  33.924 47.366 1 21.86  ? 48  ILE   B O     1 
ATOM   2395 C CB    . ILE   B 1 67  ? 22.621  36.323 45.188 1 22.48  ? 48  ILE   B CB    1 
ATOM   2396 C CG1   . ILE   B 1 67  ? 21.815  36.544 43.897 1 22.96  ? 48  ILE   B CG1   1 
ATOM   2397 C CG2   . ILE   B 1 67  ? 24.035  35.798 44.862 1 23.53  ? 48  ILE   B CG2   1 
ATOM   2398 C CD1   . ILE   B 1 67  ? 22.201  37.768 43.098 1 24.59  ? 48  ILE   B CD1   1 
ATOM   2399 N N     . PHE   B 1 68  ? 22.945  35.926 48.336 1 19.78  ? 49  PHE   B N     1 
ATOM   2400 C CA    . PHE   B 1 68  ? 23.923  35.741 49.398 1 21.11  ? 49  PHE   B CA    1 
ATOM   2401 C C     . PHE   B 1 68  ? 23.464  35.108 50.71  1 35.49  ? 49  PHE   B C     1 
ATOM   2402 O O     . PHE   B 1 68  ? 24.197  34.269 51.255 1 35.76  ? 49  PHE   B O     1 
ATOM   2403 C CB    . PHE   B 1 68  ? 24.601  37.081 49.732 1 21.39  ? 49  PHE   B CB    1 
ATOM   2404 C CG    . PHE   B 1 68  ? 25.429  37.664 48.613 1 20.94  ? 49  PHE   B CG    1 
ATOM   2405 C CD1   . PHE   B 1 68  ? 26.525  36.973 48.101 1 22.93  ? 49  PHE   B CD1   1 
ATOM   2406 C CD2   . PHE   B 1 68  ? 25.111  38.901 48.064 1 21.61  ? 49  PHE   B CD2   1 
ATOM   2407 C CE1   . PHE   B 1 68  ? 27.27   37.497 47.039 1 23.54  ? 49  PHE   B CE1   1 
ATOM   2408 C CE2   . PHE   B 1 68  ? 25.855  39.425 47.002 1 24.18  ? 49  PHE   B CE2   1 
ATOM   2409 C CZ    . PHE   B 1 68  ? 26.948  38.732 46.515 1 22.65  ? 49  PHE   B CZ    1 
ATOM   2410 N N     . CYS   B 1 69  ? 22.344  35.555 51.279 1 38.96  ? 50  CYS   B N     1 
ATOM   2411 C CA    . CYS   B 1 69  ? 22.012  35.077 52.616 1 41.82  ? 50  CYS   B CA    1 
ATOM   2412 C C     . CYS   B 1 69  ? 21.174  33.815 52.659 1 52.3   ? 50  CYS   B C     1 
ATOM   2413 O O     . CYS   B 1 69  ? 21.594  32.864 53.33  1 53.15  ? 50  CYS   B O     1 
ATOM   2414 C CB    . CYS   B 1 69  ? 21.393  36.187 53.457 1 41.97  ? 50  CYS   B CB    1 
ATOM   2415 S SG    . CYS   B 1 69  ? 22.489  37.601 53.73  1 45.48  ? 50  CYS   B SG    1 
ATOM   2416 N N     . LEU   B 1 70  ? 19.998  33.795 51.994 1 52.15  ? 51  LEU   B N     1 
ATOM   2417 C CA    . LEU   B 1 70  ? 19.081  32.643 52.004 1 53.34  ? 51  LEU   B CA    1 
ATOM   2418 C C     . LEU   B 1 70  ? 19.82   31.288 52.174 1 59.96  ? 51  LEU   B C     1 
ATOM   2419 O O     . LEU   B 1 70  ? 19.593  30.558 53.146 1 60.29  ? 51  LEU   B O     1 
ATOM   2420 C CB    . LEU   B 1 70  ? 18.165  32.674 50.769 1 53.3   ? 51  LEU   B CB    1 
ATOM   2421 C CG    . LEU   B 1 70  ? 17.067  33.754 50.801 1 58.43  ? 51  LEU   B CG    1 
ATOM   2422 C CD1   . LEU   B 1 70  ? 16.222  33.709 49.568 1 58.74  ? 51  LEU   B CD1   1 
ATOM   2423 C CD2   . LEU   B 1 70  ? 16.159  33.604 52.016 1 61.47  ? 51  LEU   B CD2   1 
ATOM   2424 N N     . ASP   B 1 71  ? 20.795  31.054 51.287 1 57.12  ? 52  ASP   B N     1 
ATOM   2425 C CA    . ASP   B 1 71  ? 21.73   29.935 51.23  1 56.59  ? 52  ASP   B CA    1 
ATOM   2426 C C     . ASP   B 1 71  ? 22.832  30.533 50.322 1 59.09  ? 52  ASP   B C     1 
ATOM   2427 O O     . ASP   B 1 71  ? 23.483  31.501 50.725 1 59.48  ? 52  ASP   B O     1 
ATOM   2428 C CB    . ASP   B 1 71  ? 21.037  28.706 50.599 1 58.31  ? 52  ASP   B CB    1 
ATOM   2429 C CG    . ASP   B 1 71  ? 21.499  27.343 51.075 1 64.61  ? 52  ASP   B CG    1 
ATOM   2430 O OD1   . ASP   B 1 71  ? 22.562  27.267 51.734 1 64.1   ? 52  ASP   B OD1   1 
ATOM   2431 O OD2   . ASP   B 1 71  ? 20.816  26.346 50.758 1 69.46  ? 52  ASP   B OD2   1 
ATOM   2432 N N     . GLY   B 1 72  ? 22.943  30.03  49.096 1 52.48  ? 53  GLY   B N     1 
ATOM   2433 C CA    . GLY   B 1 72  ? 23.798  30.544 48.032 1 50.19  ? 53  GLY   B CA    1 
ATOM   2434 C C     . GLY   B 1 72  ? 25.257  30.857 48.281 1 48.48  ? 53  GLY   B C     1 
ATOM   2435 O O     . GLY   B 1 72  ? 25.926  30.196 49.081 1 48.58  ? 53  GLY   B O     1 
ATOM   2436 N N     . VAL   B 1 73  ? 25.747  31.864 47.521 1 39.85  ? 54  VAL   B N     1 
ATOM   2437 C CA    . VAL   B 1 73  ? 27.129  32.35  47.427 1 36.97  ? 54  VAL   B CA    1 
ATOM   2438 C C     . VAL   B 1 73  ? 27.68   32.832 48.772 1 37.35  ? 54  VAL   B C     1 
ATOM   2439 O O     . VAL   B 1 73  ? 27.153  33.77  49.379 1 36.87  ? 54  VAL   B O     1 
ATOM   2440 C CB    . VAL   B 1 73  ? 27.302  33.412 46.305 1 40.08  ? 54  VAL   B CB    1 
ATOM   2441 C CG1   . VAL   B 1 73  ? 28.779  33.691 46.033 1 39.51  ? 54  VAL   B CG1   1 
ATOM   2442 C CG2   . VAL   B 1 73  ? 26.602  32.977 45.019 1 39.76  ? 54  VAL   B CG2   1 
ATOM   2443 N N     . LYS   B 1 74  ? 28.762  32.166 49.213 1 31.53  ? 55  LYS   B N     1 
ATOM   2444 C CA    . LYS   B 1 74  ? 29.493  32.388 50.47  1 30.55  ? 55  LYS   B CA    1 
ATOM   2445 C C     . LYS   B 1 74  ? 31.007  32.173 50.228 1 31.23  ? 55  LYS   B C     1 
ATOM   2446 O O     . LYS   B 1 74  ? 31.394  31.578 49.215 1 29.31  ? 55  LYS   B O     1 
ATOM   2447 C CB    . LYS   B 1 74  ? 28.988  31.397 51.548 1 33.37  ? 55  LYS   B CB    1 
ATOM   2448 C CG    . LYS   B 1 74  ? 27.582  31.691 52.075 1 51.58  ? 55  LYS   B CG    1 
ATOM   2449 C CD    . LYS   B 1 74  ? 26.854  30.45  52.583 1 61.13  ? 55  LYS   B CD    1 
ATOM   2450 C CE    . LYS   B 1 74  ? 25.501  30.816 53.143 1 69.91  ? 55  LYS   B CE    1 
ATOM   2451 N NZ    . LYS   B 1 74  ? 24.581  29.651 53.202 1 73.61  ? 55  LYS   B NZ    1 
ATOM   2452 N N     . GLY   B 1 75  ? 31.841  32.647 51.155 1 26.75  ? 56  GLY   B N     1 
ATOM   2453 C CA    . GLY   B 1 75  ? 33.283  32.458 51.038 1 25.81  ? 56  GLY   B CA    1 
ATOM   2454 C C     . GLY   B 1 75  ? 34.149  33.356 51.893 1 27.63  ? 56  GLY   B C     1 
ATOM   2455 O O     . GLY   B 1 75  ? 33.655  34.113 52.724 1 27.62  ? 56  GLY   B O     1 
ATOM   2456 N N     . ASP   B 1 76  ? 35.454  33.262 51.692 1 22.96  ? 57  ASP   B N     1 
ATOM   2457 C CA    . ASP   B 1 76  ? 36.442  34.05  52.421 1 23.41  ? 57  ASP   B CA    1 
ATOM   2458 C C     . ASP   B 1 76  ? 36.518  35.461 51.876 1 25.28  ? 57  ASP   B C     1 
ATOM   2459 O O     . ASP   B 1 76  ? 36.662  36.407 52.649 1 25.84  ? 57  ASP   B O     1 
ATOM   2460 C CB    . ASP   B 1 76  ? 37.838  33.399 52.27  1 25.62  ? 57  ASP   B CB    1 
ATOM   2461 C CG    . ASP   B 1 76  ? 38.042  32.119 53.057 1 35.8   ? 57  ASP   B CG    1 
ATOM   2462 O OD1   . ASP   B 1 76  ? 37.338  31.929 54.08  1 35.05  ? 57  ASP   B OD1   1 
ATOM   2463 O OD2   . ASP   B 1 76  ? 38.955  31.346 52.697 1 40.41  ? 57  ASP   B OD2   1 
ATOM   2464 N N     . LEU   B 1 77  ? 36.483  35.598 50.533 1 19.22  ? 58  LEU   B N     1 
ATOM   2465 C CA    . LEU   B 1 77  ? 36.691  36.884 49.897 1 17.5   ? 58  LEU   B CA    1 
ATOM   2466 C C     . LEU   B 1 77  ? 35.732  37.206 48.767 1 17.91  ? 58  LEU   B C     1 
ATOM   2467 O O     . LEU   B 1 77  ? 35.551  36.42  47.841 1 18.2   ? 58  LEU   B O     1 
ATOM   2468 C CB    . LEU   B 1 77  ? 38.166  36.957 49.414 1 17.57  ? 58  LEU   B CB    1 
ATOM   2469 C CG    . LEU   B 1 77  ? 38.634  38.171 48.604 1 21.47  ? 58  LEU   B CG    1 
ATOM   2470 C CD1   . LEU   B 1 77  ? 38.672  39.418 49.443 1 21.87  ? 58  LEU   B CD1   1 
ATOM   2471 C CD2   . LEU   B 1 77  ? 39.997  37.913 47.986 1 23.38  ? 58  LEU   B CD2   1 
ATOM   2472 N N     . LEU   B 1 78  ? 35.177  38.414 48.821 1 12.34  ? 59  LEU   B N     1 
ATOM   2473 C CA    . LEU   B 1 78  ? 34.347  38.956 47.758 1 11.36  ? 59  LEU   B CA    1 
ATOM   2474 C C     . LEU   B 1 78  ? 35.013  40.255 47.298 1 14.15  ? 59  LEU   B C     1 
ATOM   2475 O O     . LEU   B 1 78  ? 35.426  41.066 48.127 1 12.14  ? 59  LEU   B O     1 
ATOM   2476 C CB    . LEU   B 1 78  ? 32.91   39.225 48.261 1 11.15  ? 59  LEU   B CB    1 
ATOM   2477 C CG    . LEU   B 1 78  ? 31.927  39.879 47.262 1 15.31  ? 59  LEU   B CG    1 
ATOM   2478 C CD1   . LEU   B 1 78  ? 30.528  39.323 47.442 1 14.97  ? 59  LEU   B CD1   1 
ATOM   2479 C CD2   . LEU   B 1 78  ? 31.896  41.394 47.431 1 17.57  ? 59  LEU   B CD2   1 
ATOM   2480 N N     . ILE   B 1 79  ? 35.124  40.444 45.992 1 11.14  ? 60  ILE   B N     1 
ATOM   2481 C CA    . ILE   B 1 79  ? 35.636  41.689 45.434 1 11.19  ? 60  ILE   B CA    1 
ATOM   2482 C C     . ILE   B 1 79  ? 34.448  42.387 44.744 1 14.53  ? 60  ILE   B C     1 
ATOM   2483 O O     . ILE   B 1 79  ? 33.834  41.804 43.863 1 13.85  ? 60  ILE   B O     1 
ATOM   2484 C CB    . ILE   B 1 79  ? 36.843  41.488 44.473 1 14.16  ? 60  ILE   B CB    1 
ATOM   2485 C CG1   . ILE   B 1 79  ? 38.064  40.856 45.227 1 14.83  ? 60  ILE   B CG1   1 
ATOM   2486 C CG2   . ILE   B 1 79  ? 37.237  42.833 43.842 1 14.37  ? 60  ILE   B CG2   1 
ATOM   2487 C CD1   . ILE   B 1 79  ? 39.207  40.35  44.301 1 20.89  ? 60  ILE   B CD1   1 
ATOM   2488 N N     . ASP   B 1 80  ? 34.119  43.607 45.171 1 12.17  ? 61  ASP   B N     1 
ATOM   2489 C CA    . ASP   B 1 80  ? 33.061  44.403 44.558 1 12.08  ? 61  ASP   B CA    1 
ATOM   2490 C C     . ASP   B 1 80  ? 33.719  45.373 43.57  1 15.65  ? 61  ASP   B C     1 
ATOM   2491 O O     . ASP   B 1 80  ? 34.585  46.165 43.948 1 16.06  ? 61  ASP   B O     1 
ATOM   2492 C CB    . ASP   B 1 80  ? 32.207  45.129 45.605 1 13.77  ? 61  ASP   B CB    1 
ATOM   2493 C CG    . ASP   B 1 80  ? 31.09   45.977 45.011 1 16.58  ? 61  ASP   B CG    1 
ATOM   2494 O OD1   . ASP   B 1 80  ? 30.482  45.544 44.004 1 11.18  ? 61  ASP   B OD1   1 
ATOM   2495 O OD2   . ASP   B 1 80  ? 30.885  47.101 45.493 1 17.87  ? 61  ASP   B OD2   1 
ATOM   2496 N N     . ILE   B 1 81  ? 33.343  45.253 42.301 1 9.82   ? 62  ILE   B N     1 
ATOM   2497 C CA    . ILE   B 1 81  ? 33.89   46.014 41.182 1 9.35   ? 62  ILE   B CA    1 
ATOM   2498 C C     . ILE   B 1 81  ? 33.026  47.225 40.805 1 14.19  ? 62  ILE   B C     1 
ATOM   2499 O O     . ILE   B 1 81  ? 31.846  47.071 40.467 1 15.7   ? 62  ILE   B O     1 
ATOM   2500 C CB    . ILE   B 1 81  ? 34.1    45.05  39.973 1 11.63  ? 62  ILE   B CB    1 
ATOM   2501 C CG1   . ILE   B 1 81  ? 35.176  43.948 40.275 1 10.77  ? 62  ILE   B CG1   1 
ATOM   2502 C CG2   . ILE   B 1 81  ? 34.4    45.817 38.667 1 10.79  ? 62  ILE   B CG2   1 
ATOM   2503 C CD1   . ILE   B 1 81  ? 36.663  44.411 40.393 1 14.68  ? 62  ILE   B CD1   1 
ATOM   2504 N N     . GLY   B 1 82  ? 33.649  48.4   40.789 1 9.31   ? 63  GLY   B N     1 
ATOM   2505 C CA    . GLY   B 1 82  ? 32.973  49.638 40.429 1 8.57   ? 63  GLY   B CA    1 
ATOM   2506 C C     . GLY   B 1 82  ? 31.949  50.006 41.476 1 11.27  ? 63  GLY   B C     1 
ATOM   2507 O O     . GLY   B 1 82  ? 30.83   50.4   41.138 1 9.5    ? 63  GLY   B O     1 
ATOM   2508 N N     . SER   B 1 83  ? 32.336  49.859 42.759 1 8.48   ? 64  SER   B N     1 
ATOM   2509 C CA    . SER   B 1 83  ? 31.51   50.134 43.944 1 8.76   ? 64  SER   B CA    1 
ATOM   2510 C C     . SER   B 1 83  ? 30.93   51.546 43.972 1 14.26  ? 64  SER   B C     1 
ATOM   2511 O O     . SER   B 1 83  ? 29.906  51.765 44.626 1 13.49  ? 64  SER   B O     1 
ATOM   2512 C CB    . SER   B 1 83  ? 32.328  49.934 45.22  1 11.61  ? 64  SER   B CB    1 
ATOM   2513 O OG    . SER   B 1 83  ? 33.126  48.762 45.196 1 14.08  ? 64  SER   B OG    1 
ATOM   2514 N N     . GLY   B 1 84  ? 31.623  52.497 43.331 1 11.03  ? 65  GLY   B N     1 
ATOM   2515 C CA    . GLY   B 1 84  ? 31.255  53.905 43.36  1 9.72   ? 65  GLY   B CA    1 
ATOM   2516 C C     . GLY   B 1 84  ? 31.308  54.373 44.796 1 13.64  ? 65  GLY   B C     1 
ATOM   2517 O O     . GLY   B 1 84  ? 32.136  53.869 45.551 1 11.35  ? 65  GLY   B O     1 
ATOM   2518 N N     . PRO   B 1 85  ? 30.399  55.273 45.242 1 11.86  ? 66  PRO   B N     1 
ATOM   2519 C CA    . PRO   B 1 85  ? 30.407  55.681 46.656 1 11.96  ? 66  PRO   B CA    1 
ATOM   2520 C C     . PRO   B 1 85  ? 29.342  54.912 47.45  1 17.56  ? 66  PRO   B C     1 
ATOM   2521 O O     . PRO   B 1 85  ? 28.943  55.348 48.534 1 17.2   ? 66  PRO   B O     1 
ATOM   2522 C CB    . PRO   B 1 85  ? 30.054  57.164 46.561 1 13.42  ? 66  PRO   B CB    1 
ATOM   2523 C CG    . PRO   B 1 85  ? 29.161  57.254 45.295 1 17.81  ? 66  PRO   B CG    1 
ATOM   2524 C CD    . PRO   B 1 85  ? 29.363  56.005 44.482 1 13.31  ? 66  PRO   B CD    1 
ATOM   2525 N N     . THR   B 1 86  ? 28.863  53.762 46.908 1 15.22  ? 67  THR   B N     1 
ATOM   2526 C CA    . THR   B 1 86  ? 27.759  53.056 47.55  1 14.38  ? 67  THR   B CA    1 
ATOM   2527 C C     . THR   B 1 86  ? 28.17   51.808 48.337 1 17.92  ? 67  THR   B C     1 
ATOM   2528 O O     . THR   B 1 86  ? 29.138  51.12  47.998 1 17.9   ? 67  THR   B O     1 
ATOM   2529 C CB    . THR   B 1 86  ? 26.633  52.747 46.543 1 17.13  ? 67  THR   B CB    1 
ATOM   2530 O OG1   . THR   B 1 86  ? 26.961  51.597 45.784 1 16.01  ? 67  THR   B OG1   1 
ATOM   2531 C CG2   . THR   B 1 86  ? 26.328  53.906 45.612 1 16.3   ? 67  THR   B CG2   1 
ATOM   2532 N N     . ILE   B 1 87  ? 27.384  51.507 49.386 1 14.17  ? 68  ILE   B N     1 
ATOM   2533 C CA    . ILE   B 1 87  ? 27.61   50.336 50.227 1 13.32  ? 68  ILE   B CA    1 
ATOM   2534 C C     . ILE   B 1 87  ? 26.4    49.386 50.234 1 15.17  ? 68  ILE   B C     1 
ATOM   2535 O O     . ILE   B 1 87  ? 26.515  48.288 50.771 1 13.72  ? 68  ILE   B O     1 
ATOM   2536 C CB    . ILE   B 1 87  ? 28.077  50.724 51.675 1 16.3   ? 68  ILE   B CB    1 
ATOM   2537 C CG1   . ILE   B 1 87  ? 26.993  51.485 52.458 1 17.25  ? 68  ILE   B CG1   1 
ATOM   2538 C CG2   . ILE   B 1 87  ? 29.377  51.51  51.657 1 16.14  ? 68  ILE   B CG2   1 
ATOM   2539 C CD1   . ILE   B 1 87  ? 26.38   50.775 53.556 1 27.65  ? 68  ILE   B CD1   1 
ATOM   2540 N N     . TYR   B 1 88  ? 25.253  49.797 49.649 1 13.08  ? 69  TYR   B N     1 
ATOM   2541 C CA    . TYR   B 1 88  ? 24.005  49.001 49.637 1 13.29  ? 69  TYR   B CA    1 
ATOM   2542 C C     . TYR   B 1 88  ? 24.196  47.547 49.138 1 16.43  ? 69  TYR   B C     1 
ATOM   2543 O O     . TYR   B 1 88  ? 23.586  46.613 49.663 1 14.26  ? 69  TYR   B O     1 
ATOM   2544 C CB    . TYR   B 1 88  ? 22.89   49.724 48.841 1 14.27  ? 69  TYR   B CB    1 
ATOM   2545 C CG    . TYR   B 1 88  ? 22.989  49.543 47.336 1 15.87  ? 69  TYR   B CG    1 
ATOM   2546 C CD1   . TYR   B 1 88  ? 23.738  50.422 46.556 1 17.22  ? 69  TYR   B CD1   1 
ATOM   2547 C CD2   . TYR   B 1 88  ? 22.377  48.462 46.7   1 15.66  ? 69  TYR   B CD2   1 
ATOM   2548 C CE1   . TYR   B 1 88  ? 23.867  50.234 45.177 1 19.15  ? 69  TYR   B CE1   1 
ATOM   2549 C CE2   . TYR   B 1 88  ? 22.499  48.268 45.325 1 15.66  ? 69  TYR   B CE2   1 
ATOM   2550 C CZ    . TYR   B 1 88  ? 23.249  49.152 44.569 1 17.55  ? 69  TYR   B CZ    1 
ATOM   2551 O OH    . TYR   B 1 88  ? 23.396  48.931 43.224 1 15.54  ? 69  TYR   B OH    1 
ATOM   2552 N N     . GLN   B 1 89  ? 25.07   47.373 48.135 1 13.93  ? 70  GLN   B N     1 
ATOM   2553 C CA    . GLN   B 1 89  ? 25.325  46.098 47.464 1 14.13  ? 70  GLN   B CA    1 
ATOM   2554 C C     . GLN   B 1 89  ? 26.126  45.11  48.3   1 17.81  ? 70  GLN   B C     1 
ATOM   2555 O O     . GLN   B 1 89  ? 26.291  43.969 47.872 1 16.12  ? 70  GLN   B O     1 
ATOM   2556 C CB    . GLN   B 1 89  ? 25.981  46.324 46.075 1 15.28  ? 70  GLN   B CB    1 
ATOM   2557 C CG    . GLN   B 1 89  ? 27.437  46.831 46.078 1 12.15  ? 70  GLN   B CG    1 
ATOM   2558 C CD    . GLN   B 1 89  ? 27.61   48.332 46.228 1 18.83  ? 70  GLN   B CD    1 
ATOM   2559 O OE1   . GLN   B 1 89  ? 26.737  49.057 46.7   1 12.27  ? 70  GLN   B OE1   1 
ATOM   2560 N NE2   . GLN   B 1 89  ? 28.791  48.833 45.898 1 14.74  ? 70  GLN   B NE2   1 
ATOM   2561 N N     . LEU   B 1 90  ? 26.615  45.546 49.487 1 14.96  ? 71  LEU   B N     1 
ATOM   2562 C CA    . LEU   B 1 90  ? 27.438  44.734 50.395 1 13.7   ? 71  LEU   B CA    1 
ATOM   2563 C C     . LEU   B 1 90  ? 26.732  44.35  51.706 1 16.76  ? 71  LEU   B C     1 
ATOM   2564 O O     . LEU   B 1 90  ? 27.263  43.546 52.477 1 15.8   ? 71  LEU   B O     1 
ATOM   2565 C CB    . LEU   B 1 90  ? 28.709  45.518 50.737 1 13.58  ? 71  LEU   B CB    1 
ATOM   2566 C CG    . LEU   B 1 90  ? 29.398  46.28  49.588 1 17.22  ? 71  LEU   B CG    1 
ATOM   2567 C CD1   . LEU   B 1 90  ? 30.392  47.283 50.144 1 15.74  ? 71  LEU   B CD1   1 
ATOM   2568 C CD2   . LEU   B 1 90  ? 30.044  45.316 48.589 1 16.46  ? 71  LEU   B CD2   1 
ATOM   2569 N N     . LEU   B 1 91  ? 25.557  44.936 51.959 1 14.3   ? 72  LEU   B N     1 
ATOM   2570 C CA    . LEU   B 1 91  ? 24.825  44.749 53.205 1 13.86  ? 72  LEU   B CA    1 
ATOM   2571 C C     . LEU   B 1 91  ? 24.424  43.308 53.457 1 18.62  ? 72  LEU   B C     1 
ATOM   2572 O O     . LEU   B 1 91  ? 24.645  42.831 54.569 1 18.21  ? 72  LEU   B O     1 
ATOM   2573 C CB    . LEU   B 1 91  ? 23.649  45.714 53.323 1 13.84  ? 72  LEU   B CB    1 
ATOM   2574 C CG    . LEU   B 1 91  ? 24.047  47.198 53.483 1 17.93  ? 72  LEU   B CG    1 
ATOM   2575 C CD1   . LEU   B 1 91  ? 22.865  48.099 53.263 1 18.27  ? 72  LEU   B CD1   1 
ATOM   2576 C CD2   . LEU   B 1 91  ? 24.703  47.475 54.847 1 17.33  ? 72  LEU   B CD2   1 
ATOM   2577 N N     . SER   B 1 92  ? 23.973  42.571 52.428 1 15.95  ? 73  SER   B N     1 
ATOM   2578 C CA    . SER   B 1 92  ? 23.686  41.147 52.624 1 15.3   ? 73  SER   B CA    1 
ATOM   2579 C C     . SER   B 1 92  ? 24.983  40.325 52.517 1 19.12  ? 73  SER   B C     1 
ATOM   2580 O O     . SER   B 1 92  ? 25.199  39.433 53.334 1 17.61  ? 73  SER   B O     1 
ATOM   2581 C CB    . SER   B 1 92  ? 22.625  40.651 51.651 1 16.54  ? 73  SER   B CB    1 
ATOM   2582 O OG    . SER   B 1 92  ? 21.373  41.255 51.934 1 23.63  ? 73  SER   B OG    1 
ATOM   2583 N N     . ALA   B 1 93  ? 25.876  40.678 51.563 1 15.92  ? 74  ALA   B N     1 
ATOM   2584 C CA    . ALA   B 1 93  ? 27.151  39.988 51.332 1 15.74  ? 74  ALA   B CA    1 
ATOM   2585 C C     . ALA   B 1 93  ? 28.034  39.847 52.568 1 19.5   ? 74  ALA   B C     1 
ATOM   2586 O O     . ALA   B 1 93  ? 28.69   38.807 52.7   1 19.31  ? 74  ALA   B O     1 
ATOM   2587 C CB    . ALA   B 1 93  ? 27.926  40.662 50.209 1 16.76  ? 74  ALA   B CB    1 
ATOM   2588 N N     . CYS   B 1 94  ? 28.043  40.872 53.475 1 16.63  ? 75  CYS   B N     1 
ATOM   2589 C CA    . CYS   B 1 94  ? 28.848  40.883 54.708 1 17.21  ? 75  CYS   B CA    1 
ATOM   2590 C C     . CYS   B 1 94  ? 28.419  39.8   55.711 1 23.89  ? 75  CYS   B C     1 
ATOM   2591 O O     . CYS   B 1 94  ? 29.184  39.47  56.625 1 23.98  ? 75  CYS   B O     1 
ATOM   2592 C CB    . CYS   B 1 94  ? 28.908  42.271 55.347 1 17.27  ? 75  CYS   B CB    1 
ATOM   2593 S SG    . CYS   B 1 94  ? 27.477  42.709 56.375 1 20.78  ? 75  CYS   B SG    1 
ATOM   2594 N N     . GLU   B 1 95  ? 27.241  39.189 55.489 1 21.06  ? 76  GLU   B N     1 
ATOM   2595 C CA    . GLU   B 1 95  ? 26.786  38.079 56.323 1 20.52  ? 76  GLU   B CA    1 
ATOM   2596 C C     . GLU   B 1 95  ? 27.425  36.779 55.86  1 23.55  ? 76  GLU   B C     1 
ATOM   2597 O O     . GLU   B 1 95  ? 27.524  35.843 56.643 1 22.8   ? 76  GLU   B O     1 
ATOM   2598 C CB    . GLU   B 1 95  ? 25.244  37.957 56.284 1 21.26  ? 76  GLU   B CB    1 
ATOM   2599 C CG    . GLU   B 1 95  ? 24.495  39.124 56.911 1 27.76  ? 76  GLU   B CG    1 
ATOM   2600 C CD    . GLU   B 1 95  ? 24.777  39.413 58.377 1 38.27  ? 76  GLU   B CD    1 
ATOM   2601 O OE1   . GLU   B 1 95  ? 25.045  38.456 59.137 1 30.21  ? 76  GLU   B OE1   1 
ATOM   2602 O OE2   . GLU   B 1 95  ? 24.75   40.604 58.761 1 23.24  ? 76  GLU   B OE2   1 
ATOM   2603 N N     . SER   B 1 96  ? 27.869  36.724 54.586 1 21.8   ? 77  SER   B N     1 
ATOM   2604 C CA    . SER   B 1 96  ? 28.397  35.516 53.925 1 21.43  ? 77  SER   B CA    1 
ATOM   2605 C C     . SER   B 1 96  ? 29.886  35.524 53.537 1 24.37  ? 77  SER   B C     1 
ATOM   2606 O O     . SER   B 1 96  ? 30.405  34.493 53.072 1 23.09  ? 77  SER   B O     1 
ATOM   2607 C CB    . SER   B 1 96  ? 27.562  35.232 52.677 1 23.63  ? 77  SER   B CB    1 
ATOM   2608 O OG    . SER   B 1 96  ? 26.19   35.131 53.012 1 29.71  ? 77  SER   B OG    1 
ATOM   2609 N N     . PHE   B 1 97  ? 30.56   36.678 53.674 1 20.04  ? 78  PHE   B N     1 
ATOM   2610 C CA    . PHE   B 1 97  ? 31.966  36.812 53.296 1 18.41  ? 78  PHE   B CA    1 
ATOM   2611 C C     . PHE   B 1 97  ? 32.781  37.399 54.414 1 23.17  ? 78  PHE   B C     1 
ATOM   2612 O O     . PHE   B 1 97  ? 32.439  38.464 54.926 1 22.7   ? 78  PHE   B O     1 
ATOM   2613 C CB    . PHE   B 1 97  ? 32.115  37.637 51.997 1 18.98  ? 78  PHE   B CB    1 
ATOM   2614 C CG    . PHE   B 1 97  ? 31.674  36.872 50.773 1 19.16  ? 78  PHE   B CG    1 
ATOM   2615 C CD1   . PHE   B 1 97  ? 30.358  36.923 50.34  1 20.98  ? 78  PHE   B CD1   1 
ATOM   2616 C CD2   . PHE   B 1 97  ? 32.564  36.051 50.089 1 21.12  ? 78  PHE   B CD2   1 
ATOM   2617 C CE1   . PHE   B 1 97  ? 29.938  36.175 49.234 1 22.38  ? 78  PHE   B CE1   1 
ATOM   2618 C CE2   . PHE   B 1 97  ? 32.149  35.323 48.968 1 23.15  ? 78  PHE   B CE2   1 
ATOM   2619 C CZ    . PHE   B 1 97  ? 30.838  35.382 48.558 1 21.07  ? 78  PHE   B CZ    1 
ATOM   2620 N N     . LYS   B 1 98  ? 33.867  36.712 54.794 1 21.35  ? 79  LYS   B N     1 
ATOM   2621 C CA    . LYS   B 1 98  ? 34.765  37.169 55.857 1 21.76  ? 79  LYS   B CA    1 
ATOM   2622 C C     . LYS   B 1 98  ? 35.39   38.527 55.511 1 24.63  ? 79  LYS   B C     1 
ATOM   2623 O O     . LYS   B 1 98  ? 35.494  39.408 56.367 1 24.39  ? 79  LYS   B O     1 
ATOM   2624 C CB    . LYS   B 1 98  ? 35.893  36.154 56.068 1 24.79  ? 79  LYS   B CB    1 
ATOM   2625 C CG    . LYS   B 1 98  ? 35.534  34.949 56.932 1 49.75  ? 79  LYS   B CG    1 
ATOM   2626 C CD    . LYS   B 1 98  ? 36.507  34.746 58.119 1 64.18  ? 79  LYS   B CD    1 
ATOM   2627 C CE    . LYS   B 1 98  ? 37.998  34.761 57.797 1 79.27  ? 79  LYS   B CE    1 
ATOM   2628 N NZ    . LYS   B 1 98  ? 38.397  33.683 56.849 1 90.98  ? 79  LYS   B NZ    1 
ATOM   2629 N N     . GLU   B 1 99  ? 35.813  38.67  54.249 1 19.55  ? 80  GLU   B N     1 
ATOM   2630 C CA    . GLU   B 1 99  ? 36.495  39.836 53.736 1 17.94  ? 80  GLU   B CA    1 
ATOM   2631 C C     . GLU   B 1 99  ? 35.837  40.326 52.452 1 19.14  ? 80  GLU   B C     1 
ATOM   2632 O O     . GLU   B 1 99  ? 35.453  39.539 51.579 1 17.51  ? 80  GLU   B O     1 
ATOM   2633 C CB    . GLU   B 1 99  ? 37.992  39.494 53.528 1 19.78  ? 80  GLU   B CB    1 
ATOM   2634 C CG    . GLU   B 1 99  ? 38.837  40.586 52.868 1 31.97  ? 80  GLU   B CG    1 
ATOM   2635 C CD    . GLU   B 1 99  ? 40.349  40.433 52.922 1 53.65  ? 80  GLU   B CD    1 
ATOM   2636 O OE1   . GLU   B 1 99  ? 40.835  39.481 53.575 1 59.81  ? 80  GLU   B OE1   1 
ATOM   2637 O OE2   . GLU   B 1 99  ? 41.052  41.293 52.341 1 37.95  ? 80  GLU   B OE2   1 
ATOM   2638 N N     . ILE   B 1 100 ? 35.685  41.64  52.364 1 15.46  ? 81  ILE   B N     1 
ATOM   2639 C CA    . ILE   B 1 100 ? 35.135  42.317 51.2   1 14.4   ? 81  ILE   B CA    1 
ATOM   2640 C C     . ILE   B 1 100 ? 36.13   43.391 50.795 1 18.44  ? 81  ILE   B C     1 
ATOM   2641 O O     . ILE   B 1 100 ? 36.598  44.161 51.64  1 18.15  ? 81  ILE   B O     1 
ATOM   2642 C CB    . ILE   B 1 100 ? 33.705  42.889 51.466 1 17.19  ? 81  ILE   B CB    1 
ATOM   2643 C CG1   . ILE   B 1 100 ? 32.692  41.749 51.782 1 17.38  ? 81  ILE   B CG1   1 
ATOM   2644 C CG2   . ILE   B 1 100 ? 33.212  43.794 50.288 1 16.86  ? 81  ILE   B CG2   1 
ATOM   2645 C CD1   . ILE   B 1 100 ? 31.283  42.233 52.218 1 26.46  ? 81  ILE   B CD1   1 
ATOM   2646 N N     . VAL   B 1 101 ? 36.471  43.426 49.505 1 13.81  ? 82  VAL   B N     1 
ATOM   2647 C CA    . VAL   B 1 101 ? 37.349  44.46  48.942 1 12.19  ? 82  VAL   B CA    1 
ATOM   2648 C C     . VAL   B 1 101 ? 36.448  45.32  48.044 1 15.56  ? 82  VAL   B C     1 
ATOM   2649 O O     . VAL   B 1 101 ? 35.736  44.781 47.195 1 14.68  ? 82  VAL   B O     1 
ATOM   2650 C CB    . VAL   B 1 101 ? 38.564  43.848 48.194 1 14.65  ? 82  VAL   B CB    1 
ATOM   2651 C CG1   . VAL   B 1 101 ? 39.328  44.901 47.389 1 14.51  ? 82  VAL   B CG1   1 
ATOM   2652 C CG2   . VAL   B 1 101 ? 39.505  43.129 49.172 1 13.76  ? 82  VAL   B CG2   1 
ATOM   2653 N N     . VAL   B 1 102 ? 36.463  46.647 48.26  1 12.31  ? 83  VAL   B N     1 
ATOM   2654 C CA    . VAL   B 1 102 ? 35.683  47.605 47.483 1 11.52  ? 83  VAL   B CA    1 
ATOM   2655 C C     . VAL   B 1 102 ? 36.618  48.319 46.504 1 15.6   ? 83  VAL   B C     1 
ATOM   2656 O O     . VAL   B 1 102 ? 37.773  48.567 46.831 1 14.97  ? 83  VAL   B O     1 
ATOM   2657 C CB    . VAL   B 1 102 ? 34.824  48.552 48.356 1 14.77  ? 83  VAL   B CB    1 
ATOM   2658 C CG1   . VAL   B 1 102 ? 33.796  47.747 49.15  1 14.1   ? 83  VAL   B CG1   1 
ATOM   2659 C CG2   . VAL   B 1 102 ? 35.7    49.391 49.303 1 14.74  ? 83  VAL   B CG2   1 
ATOM   2660 N N     . THR   B 1 103 ? 36.172  48.525 45.27  1 13.61  ? 84  THR   B N     1 
ATOM   2661 C CA    . THR   B 1 103 ? 37.043  49.097 44.223 1 13.68  ? 84  THR   B CA    1 
ATOM   2662 C C     . THR   B 1 103 ? 36.293  50.045 43.3   1 17.48  ? 84  THR   B C     1 
ATOM   2663 O O     . THR   B 1 103 ? 35.085  49.881 43.116 1 18.88  ? 84  THR   B O     1 
ATOM   2664 C CB    . THR   B 1 103 ? 37.647  47.971 43.327 1 16.99  ? 84  THR   B CB    1 
ATOM   2665 O OG1   . THR   B 1 103 ? 36.622  47.455 42.487 1 18.83  ? 84  THR   B OG1   1 
ATOM   2666 C CG2   . THR   B 1 103 ? 38.297  46.822 44.111 1 13.88  ? 84  THR   B CG2   1 
ATOM   2667 N N     . ASP   B 1 104 ? 37.008  51.003 42.684 1 11.8   ? 85  ASP   B N     1 
ATOM   2668 C CA    . ASP   B 1 104 ? 36.418  51.939 41.729 1 10.73  ? 85  ASP   B CA    1 
ATOM   2669 C C     . ASP   B 1 104 ? 37.479  52.643 40.929 1 14.19  ? 85  ASP   B C     1 
ATOM   2670 O O     . ASP   B 1 104 ? 38.617  52.758 41.372 1 13.3   ? 85  ASP   B O     1 
ATOM   2671 C CB    . ASP   B 1 104 ? 35.529  52.999 42.415 1 11.52  ? 85  ASP   B CB    1 
ATOM   2672 C CG    . ASP   B 1 104 ? 34.475  53.562 41.48  1 13.75  ? 85  ASP   B CG    1 
ATOM   2673 O OD1   . ASP   B 1 104 ? 33.595  52.796 41.053 1 11.71  ? 85  ASP   B OD1   1 
ATOM   2674 O OD2   . ASP   B 1 104 ? 34.572  54.758 41.121 1 18.16  ? 85  ASP   B OD2   1 
ATOM   2675 N N     . TYR   B 1 105 ? 37.1    53.151 39.76  1 12.57  ? 86  TYR   B N     1 
ATOM   2676 C CA    . TYR   B 1 105 ? 38.012  53.943 38.956 1 13.37  ? 86  TYR   B CA    1 
ATOM   2677 C C     . TYR   B 1 105 ? 38.203  55.353 39.551 1 18.49  ? 86  TYR   B C     1 
ATOM   2678 O O     . TYR   B 1 105 ? 39.285  55.908 39.427 1 17.93  ? 86  TYR   B O     1 
ATOM   2679 C CB    . TYR   B 1 105 ? 37.532  54.036 37.494 1 15.46  ? 86  TYR   B CB    1 
ATOM   2680 C CG    . TYR   B 1 105 ? 38.564  54.681 36.592 1 17.76  ? 86  TYR   B CG    1 
ATOM   2681 C CD1   . TYR   B 1 105 ? 39.779  54.053 36.329 1 19.52  ? 86  TYR   B CD1   1 
ATOM   2682 C CD2   . TYR   B 1 105 ? 38.358  55.951 36.063 1 19.29  ? 86  TYR   B CD2   1 
ATOM   2683 C CE1   . TYR   B 1 105 ? 40.74   54.648 35.512 1 19.42  ? 86  TYR   B CE1   1 
ATOM   2684 C CE2   . TYR   B 1 105 ? 39.324  56.569 35.266 1 20.55  ? 86  TYR   B CE2   1 
ATOM   2685 C CZ    . TYR   B 1 105 ? 40.517  55.916 35.002 1 26.22  ? 86  TYR   B CZ    1 
ATOM   2686 O OH    . TYR   B 1 105 ? 41.466  56.519 34.215 1 28.92  ? 86  TYR   B OH    1 
ATOM   2687 N N     . SER   B 1 106 ? 37.152  55.936 40.162 1 15.57  ? 87  SER   B N     1 
ATOM   2688 C CA    . SER   B 1 106 ? 37.195  57.295 40.714 1 15.44  ? 87  SER   B CA    1 
ATOM   2689 C C     . SER   B 1 106 ? 37.744  57.363 42.142 1 18.22  ? 87  SER   B C     1 
ATOM   2690 O O     . SER   B 1 106 ? 37.208  56.718 43.045 1 15.86  ? 87  SER   B O     1 
ATOM   2691 C CB    . SER   B 1 106 ? 35.816  57.946 40.647 1 18.41  ? 87  SER   B CB    1 
ATOM   2692 O OG    . SER   B 1 106 ? 35.712  59.089 41.486 1 25.3   ? 87  SER   B OG    1 
ATOM   2693 N N     . ASP   B 1 107 ? 38.791  58.185 42.338 1 16.51  ? 88  ASP   B N     1 
ATOM   2694 C CA    . ASP   B 1 107 ? 39.404  58.431 43.648 1 17.03  ? 88  ASP   B CA    1 
ATOM   2695 C C     . ASP   B 1 107 ? 38.409  59.145 44.569 1 19.23  ? 88  ASP   B C     1 
ATOM   2696 O O     . ASP   B 1 107 ? 38.359  58.823 45.753 1 19.22  ? 88  ASP   B O     1 
ATOM   2697 C CB    . ASP   B 1 107 ? 40.7    59.246 43.503 1 19.39  ? 88  ASP   B CB    1 
ATOM   2698 C CG    . ASP   B 1 107 ? 41.738  58.59  42.611 1 32.12  ? 88  ASP   B CG    1 
ATOM   2699 O OD1   . ASP   B 1 107 ? 42.168  57.454 42.932 1 31.95  ? 88  ASP   B OD1   1 
ATOM   2700 O OD2   . ASP   B 1 107 ? 42.128  59.214 41.595 1 39.81  ? 88  ASP   B OD2   1 
ATOM   2701 N N     . GLN   B 1 108 ? 37.603  60.083 44.019 1 15.69  ? 89  GLN   B N     1 
ATOM   2702 C CA    . GLN   B 1 108 ? 36.548  60.816 44.742 1 15.88  ? 89  GLN   B CA    1 
ATOM   2703 C C     . GLN   B 1 108 ? 35.534  59.827 45.351 1 18.55  ? 89  GLN   B C     1 
ATOM   2704 O O     . GLN   B 1 108 ? 35.136  59.996 46.495 1 17.66  ? 89  GLN   B O     1 
ATOM   2705 C CB    . GLN   B 1 108 ? 35.81   61.784 43.789 1 17.7   ? 89  GLN   B CB    1 
ATOM   2706 C CG    . GLN   B 1 108 ? 36.49   63.13  43.601 1 31.26  ? 89  GLN   B CG    1 
ATOM   2707 C CD    . GLN   B 1 108 ? 35.593  64.087 42.852 1 50.6   ? 89  GLN   B CD    1 
ATOM   2708 O OE1   . GLN   B 1 108 ? 35.614  64.169 41.616 1 46.43  ? 89  GLN   B OE1   1 
ATOM   2709 N NE2   . GLN   B 1 108 ? 34.763  64.815 43.582 1 42.64  ? 89  GLN   B NE2   1 
ATOM   2710 N N     . ASN   B 1 109 ? 35.138  58.778 44.586 1 15.96  ? 90  ASN   B N     1 
ATOM   2711 C CA    . ASN   B 1 109 ? 34.205  57.744 45.044 1 15.65  ? 90  ASN   B CA    1 
ATOM   2712 C C     . ASN   B 1 109 ? 34.763  56.935 46.199 1 18.33  ? 90  ASN   B C     1 
ATOM   2713 O O     . ASN   B 1 109 ? 34.071  56.752 47.198 1 17.31  ? 90  ASN   B O     1 
ATOM   2714 C CB    . ASN   B 1 109 ? 33.757  56.839 43.881 1 16.88  ? 90  ASN   B CB    1 
ATOM   2715 C CG    . ASN   B 1 109 ? 32.772  57.507 42.957 1 18.54  ? 90  ASN   B CG    1 
ATOM   2716 O OD1   . ASN   B 1 109 ? 32.089  58.469 43.321 1 19.37  ? 90  ASN   B OD1   1 
ATOM   2717 N ND2   . ASN   B 1 109 ? 32.666  57.013 41.743 1 16.86  ? 90  ASN   B ND2   1 
ATOM   2718 N N     . LEU   B 1 110 ? 36.021  56.487 46.077 1 15.1   ? 91  LEU   B N     1 
ATOM   2719 C CA    . LEU   B 1 110 ? 36.747  55.734 47.105 1 15.43  ? 91  LEU   B CA    1 
ATOM   2720 C C     . LEU   B 1 110 ? 36.874  56.548 48.414 1 19.08  ? 91  LEU   B C     1 
ATOM   2721 O O     . LEU   B 1 110 ? 36.759  55.984 49.502 1 17.03  ? 91  LEU   B O     1 
ATOM   2722 C CB    . LEU   B 1 110 ? 38.151  55.342 46.589 1 15.57  ? 91  LEU   B CB    1 
ATOM   2723 C CG    . LEU   B 1 110 ? 38.223  54.434 45.341 1 20.62  ? 91  LEU   B CG    1 
ATOM   2724 C CD1   . LEU   B 1 110 ? 39.659  54.2   44.939 1 20.02  ? 91  LEU   B CD1   1 
ATOM   2725 C CD2   . LEU   B 1 110 ? 37.491  53.114 45.545 1 22.61  ? 91  LEU   B CD2   1 
ATOM   2726 N N     . GLN   B 1 111 ? 37.119  57.868 48.306 1 16.93  ? 92  GLN   B N     1 
ATOM   2727 C CA    . GLN   B 1 111 ? 37.199  58.718 49.498 1 17.54  ? 92  GLN   B CA    1 
ATOM   2728 C C     . GLN   B 1 111 ? 35.811  58.848 50.166 1 21.43  ? 92  GLN   B C     1 
ATOM   2729 O O     . GLN   B 1 111 ? 35.725  58.832 51.398 1 21.66  ? 92  GLN   B O     1 
ATOM   2730 C CB    . GLN   B 1 111 ? 37.832  60.096 49.199 1 18.65  ? 92  GLN   B CB    1 
ATOM   2731 C CG    . GLN   B 1 111 ? 39.294  60.071 48.724 1 37.21  ? 92  GLN   B CG    1 
ATOM   2732 C CD    . GLN   B 1 111 ? 40.215  59.146 49.497 1 75.13  ? 92  GLN   B CD    1 
ATOM   2733 O OE1   . GLN   B 1 111 ? 40.355  59.228 50.728 1 73     ? 92  GLN   B OE1   1 
ATOM   2734 N NE2   . GLN   B 1 111 ? 40.89   58.258 48.774 1 72.86  ? 92  GLN   B NE2   1 
ATOM   2735 N N     . GLU   B 1 112 ? 34.733  58.923 49.36  1 16.44  ? 93  GLU   B N     1 
ATOM   2736 C CA    . GLU   B 1 112 ? 33.356  58.997 49.865 1 16.36  ? 93  GLU   B CA    1 
ATOM   2737 C C     . GLU   B 1 112 ? 32.997  57.709 50.604 1 22     ? 93  GLU   B C     1 
ATOM   2738 O O     . GLU   B 1 112 ? 32.45   57.781 51.707 1 21.56  ? 93  GLU   B O     1 
ATOM   2739 C CB    . GLU   B 1 112 ? 32.351  59.316 48.726 1 17.71  ? 93  GLU   B CB    1 
ATOM   2740 C CG    . GLU   B 1 112 ? 30.904  59.523 49.181 1 25.62  ? 93  GLU   B CG    1 
ATOM   2741 C CD    . GLU   B 1 112 ? 30.626  60.692 50.111 1 34.52  ? 93  GLU   B CD    1 
ATOM   2742 O OE1   . GLU   B 1 112 ? 31.28   61.746 49.959 1 22.38  ? 93  GLU   B OE1   1 
ATOM   2743 O OE2   . GLU   B 1 112 ? 29.738  60.561 50.983 1 24.45  ? 93  GLU   B OE2   1 
ATOM   2744 N N     . LEU   B 1 113 ? 33.38   56.54  50.03  1 18.58  ? 94  LEU   B N     1 
ATOM   2745 C CA    . LEU   B 1 113 ? 33.236  55.214 50.64  1 18.46  ? 94  LEU   B CA    1 
ATOM   2746 C C     . LEU   B 1 113 ? 33.987  55.187 51.985 1 21.51  ? 94  LEU   B C     1 
ATOM   2747 O O     . LEU   B 1 113 ? 33.424  54.763 52.988 1 21.8   ? 94  LEU   B O     1 
ATOM   2748 C CB    . LEU   B 1 113 ? 33.876  54.14  49.727 1 19.04  ? 94  LEU   B CB    1 
ATOM   2749 C CG    . LEU   B 1 113 ? 33.041  53.495 48.633 1 24.85  ? 94  LEU   B CG    1 
ATOM   2750 C CD1   . LEU   B 1 113 ? 33.801  52.345 48.018 1 25.42  ? 94  LEU   B CD1   1 
ATOM   2751 C CD2   . LEU   B 1 113 ? 31.748  52.945 49.161 1 29.79  ? 94  LEU   B CD2   1 
ATOM   2752 N N     . GLU   B 1 114 ? 35.262  55.638 51.989 1 17.82  ? 95  GLU   B N     1 
ATOM   2753 C CA    . GLU   B 1 114 ? 36.119  55.69  53.173 1 18.3   ? 95  GLU   B CA    1 
ATOM   2754 C C     . GLU   B 1 114 ? 35.553  56.6   54.281 1 22.7   ? 95  GLU   B C     1 
ATOM   2755 O O     . GLU   B 1 114 ? 35.758  56.29  55.454 1 22.32  ? 95  GLU   B O     1 
ATOM   2756 C CB    . GLU   B 1 114 ? 37.571  56.041 52.815 1 20     ? 95  GLU   B CB    1 
ATOM   2757 C CG    . GLU   B 1 114 ? 38.31   54.805 52.322 1 33.48  ? 95  GLU   B CG    1 
ATOM   2758 C CD    . GLU   B 1 114 ? 39.782  54.918 51.982 1 62.68  ? 95  GLU   B CD    1 
ATOM   2759 O OE1   . GLU   B 1 114 ? 40.139  55.772 51.139 1 71.18  ? 95  GLU   B OE1   1 
ATOM   2760 O OE2   . GLU   B 1 114 ? 40.562  54.072 52.476 1 58.11  ? 95  GLU   B OE2   1 
ATOM   2761 N N     . LYS   B 1 115 ? 34.794  57.667 53.926 1 18.83  ? 96  LYS   B N     1 
ATOM   2762 C CA    . LYS   B 1 115 ? 34.116  58.521 54.926 1 19.09  ? 96  LYS   B CA    1 
ATOM   2763 C C     . LYS   B 1 115 ? 33.096  57.68  55.715 1 22.69  ? 96  LYS   B C     1 
ATOM   2764 O O     . LYS   B 1 115 ? 33.025  57.795 56.939 1 22.22  ? 96  LYS   B O     1 
ATOM   2765 C CB    . LYS   B 1 115 ? 33.389  59.699 54.262 1 21.27  ? 96  LYS   B CB    1 
ATOM   2766 C CG    . LYS   B 1 115 ? 34.289  60.858 53.857 1 31.53  ? 96  LYS   B CG    1 
ATOM   2767 C CD    . LYS   B 1 115 ? 33.423  62.012 53.354 1 37.45  ? 96  LYS   B CD    1 
ATOM   2768 C CE    . LYS   B 1 115 ? 34.23   63.156 52.802 1 49.62  ? 96  LYS   B CE    1 
ATOM   2769 N NZ    . LYS   B 1 115 ? 33.356  64.174 52.156 1 59.54  ? 96  LYS   B NZ    1 
ATOM   2770 N N     . TRP   B 1 116 ? 32.319  56.814 55.013 1 18.79  ? 97  TRP   B N     1 
ATOM   2771 C CA    . TRP   B 1 116 ? 31.338  55.95  55.669 1 17.72  ? 97  TRP   B CA    1 
ATOM   2772 C C     . TRP   B 1 116 ? 31.999  54.837 56.482 1 21.29  ? 97  TRP   B C     1 
ATOM   2773 O O     . TRP   B 1 116 ? 31.571  54.592 57.615 1 20.15  ? 97  TRP   B O     1 
ATOM   2774 C CB    . TRP   B 1 116 ? 30.287  55.398 54.68  1 16.61  ? 97  TRP   B CB    1 
ATOM   2775 C CG    . TRP   B 1 116 ? 29.185  54.638 55.367 1 17.79  ? 97  TRP   B CG    1 
ATOM   2776 C CD1   . TRP   B 1 116 ? 28.041  55.156 55.893 1 20.53  ? 97  TRP   B CD1   1 
ATOM   2777 C CD2   . TRP   B 1 116 ? 29.162  53.233 55.658 1 17.55  ? 97  TRP   B CD2   1 
ATOM   2778 N NE1   . TRP   B 1 116 ? 27.305  54.161 56.495 1 20.05  ? 97  TRP   B NE1   1 
ATOM   2779 C CE2   . TRP   B 1 116 ? 27.976  52.973 56.377 1 21.75  ? 97  TRP   B CE2   1 
ATOM   2780 C CE3   . TRP   B 1 116 ? 30.049  52.177 55.421 1 18.87  ? 97  TRP   B CE3   1 
ATOM   2781 C CZ2   . TRP   B 1 116 ? 27.642  51.692 56.837 1 21.26  ? 97  TRP   B CZ2   1 
ATOM   2782 C CZ3   . TRP   B 1 116 ? 29.717  50.909 55.872 1 20.86  ? 97  TRP   B CZ3   1 
ATOM   2783 C CH2   . TRP   B 1 116 ? 28.53   50.677 56.581 1 21.47  ? 97  TRP   B CH2   1 
ATOM   2784 N N     . LEU   B 1 117 ? 33.003  54.139 55.893 1 17.54  ? 98  LEU   B N     1 
ATOM   2785 C CA    . LEU   B 1 117 ? 33.738  53.043 56.53  1 18.6   ? 98  LEU   B CA    1 
ATOM   2786 C C     . LEU   B 1 117 ? 34.363  53.479 57.86  1 24.83  ? 98  LEU   B C     1 
ATOM   2787 O O     . LEU   B 1 117 ? 34.278  52.754 58.853 1 25.27  ? 98  LEU   B O     1 
ATOM   2788 C CB    . LEU   B 1 117 ? 34.858  52.553 55.598 1 19.08  ? 98  LEU   B CB    1 
ATOM   2789 C CG    . LEU   B 1 117 ? 34.672  51.265 54.746 1 24.44  ? 98  LEU   B CG    1 
ATOM   2790 C CD1   . LEU   B 1 117 ? 33.243  50.756 54.702 1 24.1   ? 98  LEU   B CD1   1 
ATOM   2791 C CD2   . LEU   B 1 117 ? 35.227  51.452 53.34  1 25.03  ? 98  LEU   B CD2   1 
ATOM   2792 N N     . LYS   B 1 118 ? 34.97   54.663 57.872 1 21.7   ? 99  LYS   B N     1 
ATOM   2793 C CA    . LYS   B 1 118 ? 35.649  55.222 59.043 1 22.84  ? 99  LYS   B CA    1 
ATOM   2794 C C     . LYS   B 1 118 ? 34.707  55.929 60.018 1 28.29  ? 99  LYS   B C     1 
ATOM   2795 O O     . LYS   B 1 118 ? 35.175  56.404 61.058 1 29.5   ? 99  LYS   B O     1 
ATOM   2796 C CB    . LYS   B 1 118 ? 36.772  56.184 58.585 1 25.38  ? 99  LYS   B CB    1 
ATOM   2797 C CG    . LYS   B 1 118 ? 37.92   55.473 57.848 1 33.39  ? 99  LYS   B CG    1 
ATOM   2798 C CD    . LYS   B 1 118 ? 38.893  56.458 57.204 1 33.91  ? 99  LYS   B CD    1 
ATOM   2799 C CE    . LYS   B 1 118 ? 39.964  55.754 56.411 1 39.32  ? 99  LYS   B CE    1 
ATOM   2800 N NZ    . LYS   B 1 118 ? 40.742  56.718 55.583 1 47.66  ? 99  LYS   B NZ    1 
ATOM   2801 N N     . ALA   B 1 119 ? 33.387  55.999 59.691 1 25.01  ? 100 ALA   B N     1 
ATOM   2802 C CA    . ALA   B 1 119 ? 32.333  56.688 60.45  1 25.85  ? 100 ALA   B CA    1 
ATOM   2803 C C     . ALA   B 1 119 ? 32.778  58.138 60.702 1 31.98  ? 100 ALA   B C     1 
ATOM   2804 O O     . ALA   B 1 119 ? 32.708  58.654 61.82  1 31.13  ? 100 ALA   B O     1 
ATOM   2805 C CB    . ALA   B 1 119 ? 32.037  55.955 61.763 1 26.73  ? 100 ALA   B CB    1 
ATOM   2806 N N     . ALA   B 1 120 ? 33.305  58.766 59.638 1 29.65  ? 101 ALA   B N     1 
ATOM   2807 C CA    . ALA   B 1 120 ? 33.84   60.117 59.678 1 29.99  ? 101 ALA   B CA    1 
ATOM   2808 C C     . ALA   B 1 120 ? 32.704  61.125 59.531 1 35.74  ? 101 ALA   B C     1 
ATOM   2809 O O     . ALA   B 1 120 ? 31.666  60.753 58.971 1 35.15  ? 101 ALA   B O     1 
ATOM   2810 C CB    . ALA   B 1 120 ? 34.834  60.292 58.542 1 30.8   ? 101 ALA   B CB    1 
ATOM   2811 N N     . PRO   B 1 121 ? 32.858  62.409 59.967 1 33.55  ? 102 PRO   B N     1 
ATOM   2812 C CA    . PRO   B 1 121 ? 31.778  63.384 59.723 1 33.81  ? 102 PRO   B CA    1 
ATOM   2813 C C     . PRO   B 1 121 ? 31.596  63.567 58.218 1 37.97  ? 102 PRO   B C     1 
ATOM   2814 O O     . PRO   B 1 121 ? 32.538  63.302 57.452 1 39.74  ? 102 PRO   B O     1 
ATOM   2815 C CB    . PRO   B 1 121 ? 32.293  64.668 60.386 1 35.77  ? 102 PRO   B CB    1 
ATOM   2816 C CG    . PRO   B 1 121 ? 33.398  64.23  61.308 1 40.39  ? 102 PRO   B CG    1 
ATOM   2817 C CD    . PRO   B 1 121 ? 34.016  63.051 60.627 1 35.59  ? 102 PRO   B CD    1 
ATOM   2818 N N     . ALA   B 1 122 ? 30.388  63.969 57.786 1 32.56  ? 103 ALA   B N     1 
ATOM   2819 C CA    . ALA   B 1 122 ? 30.016  64.172 56.369 1 31.3   ? 103 ALA   B CA    1 
ATOM   2820 C C     . ALA   B 1 122 ? 29.794  62.863 55.583 1 31.48  ? 103 ALA   B C     1 
ATOM   2821 O O     . ALA   B 1 122 ? 29.491  62.924 54.392 1 31.35  ? 103 ALA   B O     1 
ATOM   2822 C CB    . ALA   B 1 122 ? 31.004  65.084 55.637 1 31.87  ? 103 ALA   B CB    1 
ATOM   2823 N N     . ALA   B 1 123 ? 29.879  61.699 56.262 1 25.32  ? 104 ALA   B N     1 
ATOM   2824 C CA    . ALA   B 1 123 ? 29.607  60.376 55.688 1 23.56  ? 104 ALA   B CA    1 
ATOM   2825 C C     . ALA   B 1 123 ? 28.133  60.339 55.32  1 24.53  ? 104 ALA   B C     1 
ATOM   2826 O O     . ALA   B 1 123 ? 27.306  60.92  56.031 1 23.69  ? 104 ALA   B O     1 
ATOM   2827 C CB    . ALA   B 1 123 ? 29.884  59.291 56.715 1 24.01  ? 104 ALA   B CB    1 
ATOM   2828 N N     . PHE   B 1 124 ? 27.794  59.664 54.219 1 19.13  ? 105 PHE   B N     1 
ATOM   2829 C CA    . PHE   B 1 124 ? 26.397  59.557 53.799 1 17.42  ? 105 PHE   B CA    1 
ATOM   2830 C C     . PHE   B 1 124 ? 25.595  58.764 54.825 1 18.82  ? 105 PHE   B C     1 
ATOM   2831 O O     . PHE   B 1 124 ? 26.116  57.82  55.429 1 17.78  ? 105 PHE   B O     1 
ATOM   2832 C CB    . PHE   B 1 124 ? 26.3    58.904 52.403 1 19.03  ? 105 PHE   B CB    1 
ATOM   2833 C CG    . PHE   B 1 124 ? 24.911  58.837 51.814 1 20.44  ? 105 PHE   B CG    1 
ATOM   2834 C CD1   . PHE   B 1 124 ? 24.248  59.995 51.411 1 23.1   ? 105 PHE   B CD1   1 
ATOM   2835 C CD2   . PHE   B 1 124 ? 24.285  57.615 51.61  1 23.04  ? 105 PHE   B CD2   1 
ATOM   2836 C CE1   . PHE   B 1 124 ? 22.973  59.93  50.846 1 23.83  ? 105 PHE   B CE1   1 
ATOM   2837 C CE2   . PHE   B 1 124 ? 23.006  57.55  51.045 1 25.7   ? 105 PHE   B CE2   1 
ATOM   2838 C CZ    . PHE   B 1 124 ? 22.359  58.708 50.673 1 23.66  ? 105 PHE   B CZ    1 
ATOM   2839 N N     . ASP   B 1 125 ? 24.321  59.137 55.008 1 17.25  ? 106 ASP   B N     1 
ATOM   2840 C CA    . ASP   B 1 125 ? 23.427  58.425 55.908 1 17.27  ? 106 ASP   B CA    1 
ATOM   2841 C C     . ASP   B 1 125 ? 22.741  57.26  55.183 1 19.61  ? 106 ASP   B C     1 
ATOM   2842 O O     . ASP   B 1 125 ? 21.808  57.47  54.407 1 17.77  ? 106 ASP   B O     1 
ATOM   2843 C CB    . ASP   B 1 125 ? 22.398  59.386 56.528 1 20.2   ? 106 ASP   B CB    1 
ATOM   2844 C CG    . ASP   B 1 125 ? 21.48   58.784 57.583 1 33.4   ? 106 ASP   B CG    1 
ATOM   2845 O OD1   . ASP   B 1 125 ? 21.777  57.66  58.07  1 32.01  ? 106 ASP   B OD1   1 
ATOM   2846 O OD2   . ASP   B 1 125 ? 20.485  59.454 57.951 1 43.2   ? 106 ASP   B OD2   1 
ATOM   2847 N N     . TRP   B 1 126 ? 23.218  56.024 55.445 1 17.07  ? 107 TRP   B N     1 
ATOM   2848 C CA    . TRP   B 1 126 ? 22.656  54.802 54.856 1 16.78  ? 107 TRP   B CA    1 
ATOM   2849 C C     . TRP   B 1 126 ? 21.632  54.104 55.782 1 21.55  ? 107 TRP   B C     1 
ATOM   2850 O O     . TRP   B 1 126 ? 21.096  53.074 55.378 1 20.9   ? 107 TRP   B O     1 
ATOM   2851 C CB    . TRP   B 1 126 ? 23.775  53.805 54.499 1 14.9   ? 107 TRP   B CB    1 
ATOM   2852 C CG    . TRP   B 1 126 ? 24.585  54.161 53.292 1 15.24  ? 107 TRP   B CG    1 
ATOM   2853 C CD1   . TRP   B 1 126 ? 25.85   54.667 53.274 1 17.96  ? 107 TRP   B CD1   1 
ATOM   2854 C CD2   . TRP   B 1 126 ? 24.218  53.948 51.922 1 15.18  ? 107 TRP   B CD2   1 
ATOM   2855 N NE1   . TRP   B 1 126 ? 26.268  54.847 51.977 1 17.68  ? 107 TRP   B NE1   1 
ATOM   2856 C CE2   . TRP   B 1 126 ? 25.307  54.365 51.126 1 18.88  ? 107 TRP   B CE2   1 
ATOM   2857 C CE3   . TRP   B 1 126 ? 23.075  53.44  51.286 1 16.36  ? 107 TRP   B CE3   1 
ATOM   2858 C CZ2   . TRP   B 1 126 ? 25.27   54.327 49.725 1 17.46  ? 107 TRP   B CZ2   1 
ATOM   2859 C CZ3   . TRP   B 1 126 ? 23.048  53.389 49.898 1 17.35  ? 107 TRP   B CZ3   1 
ATOM   2860 C CH2   . TRP   B 1 126 ? 24.128  53.854 49.135 1 17.44  ? 107 TRP   B CH2   1 
ATOM   2861 N N     . SER   B 1 127 ? 21.345  54.652 57.005 1 19.21  ? 108 SER   B N     1 
ATOM   2862 C CA    . SER   B 1 127 ? 20.405  54.023 57.978 1 18.82  ? 108 SER   B CA    1 
ATOM   2863 C C     . SER   B 1 127 ? 19.037  53.594 57.378 1 21.81  ? 108 SER   B C     1 
ATOM   2864 O O     . SER   B 1 127 ? 18.67   52.455 57.666 1 23.41  ? 108 SER   B O     1 
ATOM   2865 C CB    . SER   B 1 127 ? 20.215  54.864 59.241 1 21.4   ? 108 SER   B CB    1 
ATOM   2866 O OG    . SER   B 1 127 ? 19.753  56.174 58.974 1 28.85  ? 108 SER   B OG    1 
ATOM   2867 N N     . PRO   B 1 128 ? 18.328  54.343 56.48  1 18.38  ? 109 PRO   B N     1 
ATOM   2868 C CA    . PRO   B 1 128 ? 17.088  53.786 55.881 1 18.67  ? 109 PRO   B CA    1 
ATOM   2869 C C     . PRO   B 1 128 ? 17.295  52.467 55.109 1 22.43  ? 109 PRO   B C     1 
ATOM   2870 O O     . PRO   B 1 128 ? 16.487  51.538 55.227 1 20.52  ? 109 PRO   B O     1 
ATOM   2871 C CB    . PRO   B 1 128 ? 16.629  54.881 54.913 1 20.32  ? 109 PRO   B CB    1 
ATOM   2872 C CG    . PRO   B 1 128 ? 17.318  56.096 55.326 1 24.47  ? 109 PRO   B CG    1 
ATOM   2873 C CD    . PRO   B 1 128 ? 18.587  55.711 55.977 1 19.97  ? 109 PRO   B CD    1 
ATOM   2874 N N     . VAL   B 1 129 ? 18.398  52.384 54.321 1 19.21  ? 110 VAL   B N     1 
ATOM   2875 C CA    . VAL   B 1 129 ? 18.739  51.196 53.524 1 17.88  ? 110 VAL   B CA    1 
ATOM   2876 C C     . VAL   B 1 129 ? 19.137  50.046 54.473 1 19.87  ? 110 VAL   B C     1 
ATOM   2877 O O     . VAL   B 1 129 ? 18.682  48.913 54.295 1 19.54  ? 110 VAL   B O     1 
ATOM   2878 C CB    . VAL   B 1 129 ? 19.834  51.534 52.451 1 21.51  ? 110 VAL   B CB    1 
ATOM   2879 C CG1   . VAL   B 1 129 ? 20.248  50.298 51.653 1 21.32  ? 110 VAL   B CG1   1 
ATOM   2880 C CG2   . VAL   B 1 129 ? 19.356  52.634 51.505 1 20.98  ? 110 VAL   B CG2   1 
ATOM   2881 N N     . VAL   B 1 130 ? 19.967  50.351 55.485 1 15.86  ? 111 VAL   B N     1 
ATOM   2882 C CA    . VAL   B 1 130 ? 20.428  49.396 56.504 1 16.37  ? 111 VAL   B CA    1 
ATOM   2883 C C     . VAL   B 1 130 ? 19.217  48.746 57.198 1 21.05  ? 111 VAL   B C     1 
ATOM   2884 O O     . VAL   B 1 130 ? 19.152  47.523 57.287 1 20.54  ? 111 VAL   B O     1 
ATOM   2885 C CB    . VAL   B 1 130 ? 21.397  50.06  57.527 1 20.75  ? 111 VAL   B CB    1 
ATOM   2886 C CG1   . VAL   B 1 130 ? 21.76   49.098 58.654 1 20.66  ? 111 VAL   B CG1   1 
ATOM   2887 C CG2   . VAL   B 1 130 ? 22.662  50.569 56.842 1 20.05  ? 111 VAL   B CG2   1 
ATOM   2888 N N     . THR   B 1 131 ? 18.259  49.565 57.652 1 19.27  ? 112 THR   B N     1 
ATOM   2889 C CA    . THR   B 1 131 ? 17.017  49.105 58.303 1 20.18  ? 112 THR   B CA    1 
ATOM   2890 C C     . THR   B 1 131 ? 16.23   48.226 57.343 1 23.71  ? 112 THR   B C     1 
ATOM   2891 O O     . THR   B 1 131 ? 15.749  47.186 57.772 1 24.47  ? 112 THR   B O     1 
ATOM   2892 C CB    . THR   B 1 131 ? 16.173  50.301 58.821 1 30.16  ? 112 THR   B CB    1 
ATOM   2893 O OG1   . THR   B 1 131 ? 17.005  51.178 59.577 1 32     ? 112 THR   B OG1   1 
ATOM   2894 C CG2   . THR   B 1 131 ? 14.985  49.861 59.681 1 30.02  ? 112 THR   B CG2   1 
ATOM   2895 N N     . TYR   B 1 132 ? 16.112  48.62  56.048 1 19.84  ? 113 TYR   B N     1 
ATOM   2896 C CA    . TYR   B 1 132 ? 15.377  47.805 55.059 1 19.7   ? 113 TYR   B CA    1 
ATOM   2897 C C     . TYR   B 1 132 ? 15.999  46.399 54.917 1 23.37  ? 113 TYR   B C     1 
ATOM   2898 O O     . TYR   B 1 132 ? 15.26   45.413 54.911 1 23.61  ? 113 TYR   B O     1 
ATOM   2899 C CB    . TYR   B 1 132 ? 15.266  48.509 53.698 1 20.57  ? 113 TYR   B CB    1 
ATOM   2900 C CG    . TYR   B 1 132 ? 14.456  47.731 52.683 1 22.58  ? 113 TYR   B CG    1 
ATOM   2901 C CD1   . TYR   B 1 132 ? 13.065  47.728 52.726 1 24.38  ? 113 TYR   B CD1   1 
ATOM   2902 C CD2   . TYR   B 1 132 ? 15.079  47.023 51.66  1 23.69  ? 113 TYR   B CD2   1 
ATOM   2903 C CE1   . TYR   B 1 132 ? 12.315  47.018 51.789 1 24.98  ? 113 TYR   B CE1   1 
ATOM   2904 C CE2   . TYR   B 1 132 ? 14.339  46.308 50.719 1 24.47  ? 113 TYR   B CE2   1 
ATOM   2905 C CZ    . TYR   B 1 132 ? 12.957  46.322 50.778 1 29.67  ? 113 TYR   B CZ    1 
ATOM   2906 O OH    . TYR   B 1 132 ? 12.228  45.626 49.844 1 31.13  ? 113 TYR   B OH    1 
ATOM   2907 N N     . VAL   B 1 133 ? 17.351  46.315 54.838 1 18.66  ? 114 VAL   B N     1 
ATOM   2908 C CA    . VAL   B 1 133 ? 18.09   45.051 54.747 1 17.88  ? 114 VAL   B CA    1 
ATOM   2909 C C     . VAL   B 1 133 ? 17.887  44.213 56.032 1 24.14  ? 114 VAL   B C     1 
ATOM   2910 O O     . VAL   B 1 133 ? 17.649  43.01  55.941 1 23.4   ? 114 VAL   B O     1 
ATOM   2911 C CB    . VAL   B 1 133 ? 19.579  45.244 54.358 1 19.82  ? 114 VAL   B CB    1 
ATOM   2912 C CG1   . VAL   B 1 133 ? 20.331  43.912 54.346 1 19.69  ? 114 VAL   B CG1   1 
ATOM   2913 C CG2   . VAL   B 1 133 ? 19.689  45.926 52.999 1 19.06  ? 114 VAL   B CG2   1 
ATOM   2914 N N     . CYS   B 1 134 ? 17.946  44.857 57.211 1 22.18  ? 115 CYS   B N     1 
ATOM   2915 C CA    . CYS   B 1 134 ? 17.71   44.181 58.495 1 23.26  ? 115 CYS   B CA    1 
ATOM   2916 C C     . CYS   B 1 134 ? 16.329  43.525 58.526 1 27.54  ? 115 CYS   B C     1 
ATOM   2917 O O     . CYS   B 1 134 ? 16.227  42.4   58.987 1 27.48  ? 115 CYS   B O     1 
ATOM   2918 C CB    . CYS   B 1 134 ? 17.895  45.142 59.662 1 23.99  ? 115 CYS   B CB    1 
ATOM   2919 S SG    . CYS   B 1 134 ? 19.608  45.634 59.94  1 28.03  ? 115 CYS   B SG    1 
ATOM   2920 N N     . ASP   B 1 135 ? 15.29   44.21  57.992 1 24.82  ? 116 ASP   B N     1 
ATOM   2921 C CA    . ASP   B 1 135 ? 13.918  43.695 57.899 1 24.77  ? 116 ASP   B CA    1 
ATOM   2922 C C     . ASP   B 1 135 ? 13.858  42.472 56.973 1 29.26  ? 116 ASP   B C     1 
ATOM   2923 O O     . ASP   B 1 135 ? 13.228  41.473 57.337 1 28.45  ? 116 ASP   B O     1 
ATOM   2924 C CB    . ASP   B 1 135 ? 12.955  44.779 57.375 1 26.89  ? 116 ASP   B CB    1 
ATOM   2925 C CG    . ASP   B 1 135 ? 12.772  46.018 58.235 1 36.73  ? 116 ASP   B CG    1 
ATOM   2926 O OD1   . ASP   B 1 135 ? 13.297  46.042 59.376 1 37.58  ? 116 ASP   B OD1   1 
ATOM   2927 O OD2   . ASP   B 1 135 ? 12.104  46.964 57.768 1 41.57  ? 116 ASP   B OD2   1 
ATOM   2928 N N     . LEU   B 1 136 ? 14.518  42.553 55.776 1 25.28  ? 117 LEU   B N     1 
ATOM   2929 C CA    . LEU   B 1 136 ? 14.588  41.48  54.774 1 24.2   ? 117 LEU   B CA    1 
ATOM   2930 C C     . LEU   B 1 136 ? 15.14   40.198 55.378 1 27.4   ? 117 LEU   B C     1 
ATOM   2931 O O     . LEU   B 1 136 ? 14.619  39.12  55.101 1 26.65  ? 117 LEU   B O     1 
ATOM   2932 C CB    . LEU   B 1 136 ? 15.506  41.862 53.585 1 23.95  ? 117 LEU   B CB    1 
ATOM   2933 C CG    . LEU   B 1 136 ? 15.151  43.058 52.698 1 28.41  ? 117 LEU   B CG    1 
ATOM   2934 C CD1   . LEU   B 1 136 ? 16.225  43.266 51.659 1 27.77  ? 117 LEU   B CD1   1 
ATOM   2935 C CD2   . LEU   B 1 136 ? 13.788  42.881 52.018 1 32.77  ? 117 LEU   B CD2   1 
ATOM   2936 N N     . GLU   B 1 137 ? 16.195  40.334 56.202 1 24.13  ? 118 GLU   B N     1 
ATOM   2937 C CA    . GLU   B 1 137 ? 16.958  39.246 56.812 1 24.54  ? 118 GLU   B CA    1 
ATOM   2938 C C     . GLU   B 1 137 ? 16.307  38.614 58.057 1 30.58  ? 118 GLU   B C     1 
ATOM   2939 O O     . GLU   B 1 137 ? 16.854  37.647 58.607 1 30.25  ? 118 GLU   B O     1 
ATOM   2940 C CB    . GLU   B 1 137 ? 18.391  39.701 57.098 1 25.55  ? 118 GLU   B CB    1 
ATOM   2941 C CG    . GLU   B 1 137 ? 19.151  39.971 55.805 1 33.43  ? 118 GLU   B CG    1 
ATOM   2942 C CD    . GLU   B 1 137 ? 20.579  40.458 55.911 1 43.6   ? 118 GLU   B CD    1 
ATOM   2943 O OE1   . GLU   B 1 137 ? 20.999  40.8   57.036 1 24.19  ? 118 GLU   B OE1   1 
ATOM   2944 O OE2   . GLU   B 1 137 ? 21.269  40.523 54.867 1 29.55  ? 118 GLU   B OE2   1 
ATOM   2945 N N     . GLY   B 1 138 ? 15.122  39.103 58.421 1 27.97  ? 119 GLY   B N     1 
ATOM   2946 C CA    . GLY   B 1 138 ? 14.327  38.563 59.517 1 28.39  ? 119 GLY   B CA    1 
ATOM   2947 C C     . GLY   B 1 138 ? 14.447  39.262 60.855 1 33.87  ? 119 GLY   B C     1 
ATOM   2948 O O     . GLY   B 1 138 ? 14.064  38.681 61.881 1 33.49  ? 119 GLY   B O     1 
ATOM   2949 N N     . ASN   B 1 139 ? 14.951  40.523 60.848 1 30.68  ? 120 ASN   B N     1 
ATOM   2950 C CA    . ASN   B 1 139 ? 15.152  41.387 62.023 1 30.57  ? 120 ASN   B CA    1 
ATOM   2951 C C     . ASN   B 1 139 ? 16.026  40.73  63.121 1 34.78  ? 120 ASN   B C     1 
ATOM   2952 O O     . ASN   B 1 139 ? 15.815  40.97  64.318 1 35.32  ? 120 ASN   B O     1 
ATOM   2953 C CB    . ASN   B 1 139 ? 13.803  41.895 62.585 1 32     ? 120 ASN   B CB    1 
ATOM   2954 C CG    . ASN   B 1 139 ? 13.067  42.873 61.697 1 41.55  ? 120 ASN   B CG    1 
ATOM   2955 O OD1   . ASN   B 1 139 ? 13.45   44.041 61.56  1 34.7   ? 120 ASN   B OD1   1 
ATOM   2956 N ND2   . ASN   B 1 139 ? 11.951  42.436 61.129 1 27.56  ? 120 ASN   B ND2   1 
ATOM   2957 N N     . ARG   B 1 140 ? 17.028  39.929 62.701 1 29.95  ? 121 ARG   B N     1 
ATOM   2958 C CA    . ARG   B 1 140 ? 17.977  39.243 63.599 1 29.73  ? 121 ARG   B CA    1 
ATOM   2959 C C     . ARG   B 1 140 ? 18.872  40.248 64.318 1 33.04  ? 121 ARG   B C     1 
ATOM   2960 O O     . ARG   B 1 140 ? 19.303  39.998 65.447 1 33.42  ? 121 ARG   B O     1 
ATOM   2961 C CB    . ARG   B 1 140 ? 18.882  38.254 62.835 1 29.54  ? 121 ARG   B CB    1 
ATOM   2962 C CG    . ARG   B 1 140 ? 18.288  37.624 61.589 1 41.01  ? 121 ARG   B CG    1 
ATOM   2963 C CD    . ARG   B 1 140 ? 17.739  36.245 61.853 1 51.13  ? 121 ARG   B CD    1 
ATOM   2964 N NE    . ARG   B 1 140 ? 18.039  35.332 60.749 1 57.51  ? 121 ARG   B NE    1 
ATOM   2965 C CZ    . ARG   B 1 140 ? 18.315  34.041 60.902 1 66.77  ? 121 ARG   B CZ    1 
ATOM   2966 N NH1   . ARG   B 1 140 ? 18.341  33.5   62.115 1 44.05  ? 121 ARG   B NH1   1 
ATOM   2967 N NH2   . ARG   B 1 140 ? 18.575  33.282 59.845 1 54.11  ? 121 ARG   B NH2   1 
ATOM   2968 N N     . VAL   B 1 141 ? 19.209  41.353 63.625 1 27.32  ? 122 VAL   B N     1 
ATOM   2969 C CA    . VAL   B 1 141 ? 20.066  42.431 64.125 1 25.92  ? 122 VAL   B CA    1 
ATOM   2970 C C     . VAL   B 1 141 ? 19.4    43.772 63.815 1 28.18  ? 122 VAL   B C     1 
ATOM   2971 O O     . VAL   B 1 141 ? 18.537  43.847 62.925 1 28.13  ? 122 VAL   B O     1 
ATOM   2972 C CB    . VAL   B 1 141 ? 21.523  42.37  63.553 1 30.36  ? 122 VAL   B CB    1 
ATOM   2973 C CG1   . VAL   B 1 141 ? 22.212  41.047 63.879 1 29.89  ? 122 VAL   B CG1   1 
ATOM   2974 C CG2   . VAL   B 1 141 ? 21.559  42.629 62.042 1 30.86  ? 122 VAL   B CG2   1 
ATOM   2975 N N     . LYS   B 1 142 ? 19.814  44.828 64.533 1 22.86  ? 123 LYS   B N     1 
ATOM   2976 C CA    . LYS   B 1 142 ? 19.366  46.198 64.284 1 22.85  ? 123 LYS   B CA    1 
ATOM   2977 C C     . LYS   B 1 142 ? 20.466  46.928 63.477 1 25.78  ? 123 LYS   B C     1 
ATOM   2978 O O     . LYS   B 1 142 ? 21.589  46.424 63.375 1 21.99  ? 123 LYS   B O     1 
ATOM   2979 C CB    . LYS   B 1 142 ? 19.069  46.93  65.605 1 25.76  ? 123 LYS   B CB    1 
ATOM   2980 C CG    . LYS   B 1 142 ? 17.771  46.492 66.284 1 39.31  ? 123 LYS   B CG    1 
ATOM   2981 C CD    . LYS   B 1 142 ? 17.639  47.141 67.663 1 50.38  ? 123 LYS   B CD    1 
ATOM   2982 C CE    . LYS   B 1 142 ? 16.534  46.552 68.508 1 61.18  ? 123 LYS   B CE    1 
ATOM   2983 N NZ    . LYS   B 1 142 ? 15.198  47.089 68.137 1 71.62  ? 123 LYS   B NZ    1 
ATOM   2984 N N     . GLY   B 1 143 ? 20.12   48.092 62.924 1 26.36  ? 124 GLY   B N     1 
ATOM   2985 C CA    . GLY   B 1 143 ? 20.992  48.945 62.114 1 27.71  ? 124 GLY   B CA    1 
ATOM   2986 C C     . GLY   B 1 143 ? 22.454  49.064 62.534 1 33.78  ? 124 GLY   B C     1 
ATOM   2987 O O     . GLY   B 1 143 ? 23.344  48.725 61.741 1 34.23  ? 124 GLY   B O     1 
ATOM   2988 N N     . PRO   B 1 144 ? 22.747  49.531 63.778 1 29.93  ? 125 PRO   B N     1 
ATOM   2989 C CA    . PRO   B 1 144 ? 24.154  49.686 64.201 1 28.47  ? 125 PRO   B CA    1 
ATOM   2990 C C     . PRO   B 1 144 ? 25.02   48.43  64.141 1 28.44  ? 125 PRO   B C     1 
ATOM   2991 O O     . PRO   B 1 144 ? 26.196  48.538 63.802 1 26.52  ? 125 PRO   B O     1 
ATOM   2992 C CB    . PRO   B 1 144 ? 24.028  50.214 65.634 1 30.32  ? 125 PRO   B CB    1 
ATOM   2993 C CG    . PRO   B 1 144 ? 22.728  50.917 65.65  1 34.37  ? 125 PRO   B CG    1 
ATOM   2994 C CD    . PRO   B 1 144 ? 21.833  50.045 64.823 1 30.81  ? 125 PRO   B CD    1 
ATOM   2995 N N     . GLU   B 1 145 ? 24.461  47.253 64.487 1 24.12  ? 126 GLU   B N     1 
ATOM   2996 C CA    . GLU   B 1 145 ? 25.2    45.981 64.463 1 22.86  ? 126 GLU   B CA    1 
ATOM   2997 C C     . GLU   B 1 145 ? 25.498  45.539 63.014 1 22.96  ? 126 GLU   B C     1 
ATOM   2998 O O     . GLU   B 1 145 ? 26.57   45.002 62.743 1 20.65  ? 126 GLU   B O     1 
ATOM   2999 C CB    . GLU   B 1 145 ? 24.43   44.892 65.215 1 24.03  ? 126 GLU   B CB    1 
ATOM   3000 C CG    . GLU   B 1 145 ? 25.259  43.655 65.521 1 31.55  ? 126 GLU   B CG    1 
ATOM   3001 C CD    . GLU   B 1 145 ? 24.501  42.471 66.093 1 41.46  ? 126 GLU   B CD    1 
ATOM   3002 O OE1   . GLU   B 1 145 ? 23.364  42.659 66.586 1 30.21  ? 126 GLU   B OE1   1 
ATOM   3003 O OE2   . GLU   B 1 145 ? 25.037  41.343 66.021 1 30.19  ? 126 GLU   B OE2   1 
ATOM   3004 N N     . LYS   B 1 146 ? 24.545  45.764 62.102 1 20.35  ? 127 LYS   B N     1 
ATOM   3005 C CA    . LYS   B 1 146 ? 24.679  45.441 60.676 1 19.6   ? 127 LYS   B CA    1 
ATOM   3006 C C     . LYS   B 1 146 ? 25.83   46.274 60.055 1 22.8   ? 127 LYS   B C     1 
ATOM   3007 O O     . LYS   B 1 146 ? 26.667  45.732 59.341 1 22.11  ? 127 LYS   B O     1 
ATOM   3008 C CB    . LYS   B 1 146 ? 23.345  45.739 59.946 1 20.77  ? 127 LYS   B CB    1 
ATOM   3009 C CG    . LYS   B 1 146 ? 23.462  45.839 58.412 1 27.66  ? 127 LYS   B CG    1 
ATOM   3010 C CD    . LYS   B 1 146 ? 22.851  44.658 57.684 1 28.74  ? 127 LYS   B CD    1 
ATOM   3011 C CE    . LYS   B 1 146 ? 23.767  43.479 57.684 1 28.59  ? 127 LYS   B CE    1 
ATOM   3012 N NZ    . LYS   B 1 146 ? 23.172  42.319 56.982 1 24.19  ? 127 LYS   B NZ    1 
ATOM   3013 N N     . GLU   B 1 147 ? 25.838  47.587 60.326 1 19.79  ? 128 GLU   B N     1 
ATOM   3014 C CA    . GLU   B 1 147 ? 26.82   48.544 59.826 1 19.96  ? 128 GLU   B CA    1 
ATOM   3015 C C     . GLU   B 1 147 ? 28.217  48.172 60.289 1 24.2   ? 128 GLU   B C     1 
ATOM   3016 O O     . GLU   B 1 147 ? 29.147  48.188 59.485 1 24.15  ? 128 GLU   B O     1 
ATOM   3017 C CB    . GLU   B 1 147 ? 26.465  49.954 60.307 1 21.81  ? 128 GLU   B CB    1 
ATOM   3018 C CG    . GLU   B 1 147 ? 25.381  50.65  59.497 1 26.33  ? 128 GLU   B CG    1 
ATOM   3019 C CD    . GLU   B 1 147 ? 25.288  52.151 59.7   1 40.19  ? 128 GLU   B CD    1 
ATOM   3020 O OE1   . GLU   B 1 147 ? 26.175  52.721 60.376 1 26.03  ? 128 GLU   B OE1   1 
ATOM   3021 O OE2   . GLU   B 1 147 ? 24.342  52.766 59.154 1 30.39  ? 128 GLU   B OE2   1 
ATOM   3022 N N     . GLU   B 1 148 ? 28.359  47.8   61.576 1 20.83  ? 129 GLU   B N     1 
ATOM   3023 C CA    . GLU   B 1 148 ? 29.637  47.397 62.164 1 19.99  ? 129 GLU   B CA    1 
ATOM   3024 C C     . GLU   B 1 148 ? 30.125  46.079 61.546 1 22.52  ? 129 GLU   B C     1 
ATOM   3025 O O     . GLU   B 1 148 ? 31.325  45.945 61.287 1 21.48  ? 129 GLU   B O     1 
ATOM   3026 C CB    . GLU   B 1 148 ? 29.549  47.349 63.718 1 21.22  ? 129 GLU   B CB    1 
ATOM   3027 C CG    . GLU   B 1 148 ? 30.828  46.927 64.438 1 26.15  ? 129 GLU   B CG    1 
ATOM   3028 C CD    . GLU   B 1 148 ? 32.075  47.773 64.237 1 40.35  ? 129 GLU   B CD    1 
ATOM   3029 O OE1   . GLU   B 1 148 ? 31.957  48.951 63.826 1 30.64  ? 129 GLU   B OE1   1 
ATOM   3030 O OE2   . GLU   B 1 148 ? 33.18   47.249 64.507 1 29.48  ? 129 GLU   B OE2   1 
ATOM   3031 N N     . LYS   B 1 149 ? 29.198  45.133 61.253 1 19.17  ? 130 LYS   B N     1 
ATOM   3032 C CA    . LYS   B 1 149 ? 29.572  43.877 60.594 1 18.17  ? 130 LYS   B CA    1 
ATOM   3033 C C     . LYS   B 1 149 ? 30.166  44.197 59.195 1 19.69  ? 130 LYS   B C     1 
ATOM   3034 O O     . LYS   B 1 149 ? 31.154  43.572 58.787 1 18.11  ? 130 LYS   B O     1 
ATOM   3035 C CB    . LYS   B 1 149 ? 28.388  42.895 60.497 1 20.26  ? 130 LYS   B CB    1 
ATOM   3036 C CG    . LYS   B 1 149 ? 28.841  41.488 60.074 1 26.83  ? 130 LYS   B CG    1 
ATOM   3037 C CD    . LYS   B 1 149 ? 27.859  40.375 60.401 1 31.46  ? 130 LYS   B CD    1 
ATOM   3038 C CE    . LYS   B 1 149 ? 28.518  39.037 60.16  1 40.48  ? 130 LYS   B CE    1 
ATOM   3039 N NZ    . LYS   B 1 149 ? 27.564  37.898 60.277 1 48.32  ? 130 LYS   B NZ    1 
ATOM   3040 N N     . LEU   B 1 150 ? 29.59   45.205 58.497 1 14.75  ? 131 LEU   B N     1 
ATOM   3041 C CA    . LEU   B 1 150 ? 30.097  45.631 57.195 1 14.2   ? 131 LEU   B CA    1 
ATOM   3042 C C     . LEU   B 1 150 ? 31.481  46.26  57.29  1 17.95  ? 131 LEU   B C     1 
ATOM   3043 O O     . LEU   B 1 150 ? 32.369  45.851 56.556 1 17.27  ? 131 LEU   B O     1 
ATOM   3044 C CB    . LEU   B 1 150 ? 29.12   46.551 56.44  1 13.45  ? 131 LEU   B CB    1 
ATOM   3045 C CG    . LEU   B 1 150 ? 29.575  46.972 55.015 1 16.87  ? 131 LEU   B CG    1 
ATOM   3046 C CD1   . LEU   B 1 150 ? 29.96   45.747 54.152 1 16.38  ? 131 LEU   B CD1   1 
ATOM   3047 C CD2   . LEU   B 1 150 ? 28.508  47.798 54.326 1 17.99  ? 131 LEU   B CD2   1 
ATOM   3048 N N     . ARG   B 1 151 ? 31.662  47.239 58.196 1 16.36  ? 132 ARG   B N     1 
ATOM   3049 C CA    . ARG   B 1 151 ? 32.922  47.957 58.426 1 16.1   ? 132 ARG   B CA    1 
ATOM   3050 C C     . ARG   B 1 151 ? 34.049  47.004 58.762 1 22.18  ? 132 ARG   B C     1 
ATOM   3051 O O     . ARG   B 1 151 ? 35.172  47.202 58.3   1 22.45  ? 132 ARG   B O     1 
ATOM   3052 C CB    . ARG   B 1 151 ? 32.756  49.025 59.528 1 13.89  ? 132 ARG   B CB    1 
ATOM   3053 C CG    . ARG   B 1 151 ? 31.811  50.149 59.127 1 17.29  ? 132 ARG   B CG    1 
ATOM   3054 C CD    . ARG   B 1 151 ? 31.762  51.271 60.16  1 22.01  ? 132 ARG   B CD    1 
ATOM   3055 N NE    . ARG   B 1 151 ? 31.12   52.46  59.597 1 24.32  ? 132 ARG   B NE    1 
ATOM   3056 C CZ    . ARG   B 1 151 ? 29.898  52.875 59.901 1 29.46  ? 132 ARG   B CZ    1 
ATOM   3057 N NH1   . ARG   B 1 151 ? 29.175  52.228 60.805 1 23.23  ? 132 ARG   B NH1   1 
ATOM   3058 N NH2   . ARG   B 1 151 ? 29.391  53.946 59.31  1 16.09  ? 132 ARG   B NH2   1 
ATOM   3059 N N     . GLN   B 1 152 ? 33.751  45.953 59.536 1 19.33  ? 133 GLN   B N     1 
ATOM   3060 C CA    . GLN   B 1 152 ? 34.758  44.96  59.895 1 19.81  ? 133 GLN   B CA    1 
ATOM   3061 C C     . GLN   B 1 152 ? 35.111  44.048 58.724 1 24.02  ? 133 GLN   B C     1 
ATOM   3062 O O     . GLN   B 1 152 ? 36.235  43.559 58.676 1 25.01  ? 133 GLN   B O     1 
ATOM   3063 C CB    . GLN   B 1 152 ? 34.315  44.117 61.104 1 21     ? 133 GLN   B CB    1 
ATOM   3064 C CG    . GLN   B 1 152 ? 34.298  44.879 62.436 1 26.95  ? 133 GLN   B CG    1 
ATOM   3065 C CD    . GLN   B 1 152 ? 35.665  45.354 62.887 1 43.46  ? 133 GLN   B CD    1 
ATOM   3066 O OE1   . GLN   B 1 152 ? 36.698  44.709 62.657 1 38.53  ? 133 GLN   B OE1   1 
ATOM   3067 N NE2   . GLN   B 1 152 ? 35.703  46.511 63.525 1 37.03  ? 133 GLN   B NE2   1 
ATOM   3068 N N     . ALA   B 1 153 ? 34.164  43.81  57.797 1 19.18  ? 134 ALA   B N     1 
ATOM   3069 C CA    . ALA   B 1 153 ? 34.373  42.926 56.638 1 18.98  ? 134 ALA   B CA    1 
ATOM   3070 C C     . ALA   B 1 153 ? 35.281  43.588 55.596 1 22.72  ? 134 ALA   B C     1 
ATOM   3071 O O     . ALA   B 1 153 ? 36.155  42.923 55.024 1 21.52  ? 134 ALA   B O     1 
ATOM   3072 C CB    . ALA   B 1 153 ? 33.032  42.553 56.013 1 19.78  ? 134 ALA   B CB    1 
ATOM   3073 N N     . VAL   B 1 154 ? 35.082  44.912 55.37  1 18.53  ? 135 VAL   B N     1 
ATOM   3074 C CA    . VAL   B 1 154 ? 35.841  45.709 54.409 1 17.42  ? 135 VAL   B CA    1 
ATOM   3075 C C     . VAL   B 1 154 ? 37.264  45.952 54.917 1 25.41  ? 135 VAL   B C     1 
ATOM   3076 O O     . VAL   B 1 154 ? 37.46   46.649 55.911 1 25.23  ? 135 VAL   B O     1 
ATOM   3077 C CB    . VAL   B 1 154 ? 35.112  47.004 53.972 1 19.3   ? 135 VAL   B CB    1 
ATOM   3078 C CG1   . VAL   B 1 154 ? 35.87   47.699 52.835 1 18.62  ? 135 VAL   B CG1   1 
ATOM   3079 C CG2   . VAL   B 1 154 ? 33.672  46.702 53.55  1 18.39  ? 135 VAL   B CG2   1 
ATOM   3080 N N     . LYS   B 1 155 ? 38.247  45.354 54.218 1 24.9   ? 136 LYS   B N     1 
ATOM   3081 C CA    . LYS   B 1 155 ? 39.677  45.404 54.545 1 25.46  ? 136 LYS   B CA    1 
ATOM   3082 C C     . LYS   B 1 155 ? 40.492  46.306 53.641 1 28.26  ? 136 LYS   B C     1 
ATOM   3083 O O     . LYS   B 1 155 ? 41.462  46.897 54.123 1 28.61  ? 136 LYS   B O     1 
ATOM   3084 C CB    . LYS   B 1 155 ? 40.295  43.981 54.566 1 28.27  ? 136 LYS   B CB    1 
ATOM   3085 C CG    . LYS   B 1 155 ? 39.544  42.937 55.431 1 40.82  ? 136 LYS   B CG    1 
ATOM   3086 C CD    . LYS   B 1 155 ? 39.372  43.318 56.916 1 48.16  ? 136 LYS   B CD    1 
ATOM   3087 C CE    . LYS   B 1 155 ? 39.157  42.13  57.825 1 53.87  ? 136 LYS   B CE    1 
ATOM   3088 N NZ    . LYS   B 1 155 ? 37.828  41.498 57.631 1 57.72  ? 136 LYS   B NZ    1 
ATOM   3089 N N     . GLN   B 1 156 ? 40.133  46.392 52.327 1 21.45  ? 137 GLN   B N     1 
ATOM   3090 C CA    . GLN   B 1 156 ? 40.856  47.212 51.327 1 18.39  ? 137 GLN   B CA    1 
ATOM   3091 C C     . GLN   B 1 156 ? 39.914  48.015 50.413 1 20.84  ? 137 GLN   B C     1 
ATOM   3092 O O     . GLN   B 1 156 ? 38.829  47.545 50.066 1 17.96  ? 137 GLN   B O     1 
ATOM   3093 C CB    . GLN   B 1 156 ? 41.79   46.332 50.492 1 18.7   ? 137 GLN   B CB    1 
ATOM   3094 C CG    . GLN   B 1 156 ? 42.927  45.71  51.295 1 28.53  ? 137 GLN   B CG    1 
ATOM   3095 C CD    . GLN   B 1 156 ? 43.696  44.689 50.51  1 37.91  ? 137 GLN   B CD    1 
ATOM   3096 O OE1   . GLN   B 1 156 ? 44.561  45.023 49.706 1 32.16  ? 137 GLN   B OE1   1 
ATOM   3097 N NE2   . GLN   B 1 156 ? 43.414  43.421 50.752 1 28.82  ? 137 GLN   B NE2   1 
ATOM   3098 N N     . VAL   B 1 157 ? 40.335  49.246 50.044 1 17.93  ? 138 VAL   B N     1 
ATOM   3099 C CA    . VAL   B 1 157 ? 39.599  50.178 49.192 1 16.9   ? 138 VAL   B CA    1 
ATOM   3100 C C     . VAL   B 1 157 ? 40.558  50.47  48.058 1 20.49  ? 138 VAL   B C     1 
ATOM   3101 O O     . VAL   B 1 157 ? 41.589  51.119 48.264 1 20.46  ? 138 VAL   B O     1 
ATOM   3102 C CB    . VAL   B 1 157 ? 39.179  51.449 49.975 1 20.76  ? 138 VAL   B CB    1 
ATOM   3103 C CG1   . VAL   B 1 157 ? 38.396  52.407 49.082 1 20.31  ? 138 VAL   B CG1   1 
ATOM   3104 C CG2   . VAL   B 1 157 ? 38.357  51.085 51.216 1 20.66  ? 138 VAL   B CG2   1 
ATOM   3105 N N     . LEU   B 1 158 ? 40.29   49.902 46.88  1 15.56  ? 139 LEU   B N     1 
ATOM   3106 C CA    . LEU   B 1 158 ? 41.292  49.983 45.831 1 14.92  ? 139 LEU   B CA    1 
ATOM   3107 C C     . LEU   B 1 158 ? 40.86   50.619 44.526 1 18.14  ? 139 LEU   B C     1 
ATOM   3108 O O     . LEU   B 1 158 ? 39.7    50.524 44.149 1 16.3   ? 139 LEU   B O     1 
ATOM   3109 C CB    . LEU   B 1 158 ? 41.837  48.567 45.55  1 14.87  ? 139 LEU   B CB    1 
ATOM   3110 C CG    . LEU   B 1 158 ? 42.411  47.743 46.73  1 19.64  ? 139 LEU   B CG    1 
ATOM   3111 C CD1   . LEU   B 1 158 ? 42.724  46.322 46.295 1 19.3   ? 139 LEU   B CD1   1 
ATOM   3112 C CD2   . LEU   B 1 158 ? 43.654  48.396 47.337 1 21.26  ? 139 LEU   B CD2   1 
ATOM   3113 N N     . LYS   B 1 159 ? 41.831  51.209 43.802 1 14.02  ? 140 LYS   B N     1 
ATOM   3114 C CA    . LYS   B 1 159 ? 41.632  51.758 42.469 1 14.06  ? 140 LYS   B CA    1 
ATOM   3115 C C     . LYS   B 1 159 ? 41.503  50.573 41.502 1 18.38  ? 140 LYS   B C     1 
ATOM   3116 O O     . LYS   B 1 159 ? 42.257  49.59  41.577 1 15.63  ? 140 LYS   B O     1 
ATOM   3117 C CB    . LYS   B 1 159 ? 42.843  52.619 42.055 1 17.21  ? 140 LYS   B CB    1 
ATOM   3118 C CG    . LYS   B 1 159 ? 42.688  53.331 40.704 1 22.12  ? 140 LYS   B CG    1 
ATOM   3119 C CD    . LYS   B 1 159 ? 42.179  54.756 40.883 1 33.03  ? 140 LYS   B CD    1 
ATOM   3120 C CE    . LYS   B 1 159 ? 42.661  55.688 39.797 1 39.6   ? 140 LYS   B CE    1 
ATOM   3121 N NZ    . LYS   B 1 159 ? 41.914  55.518 38.522 1 39.94  ? 140 LYS   B NZ    1 
ATOM   3122 N N     . CYS   B 1 160 ? 40.561  50.67  40.587 1 18.54  ? 141 CYS   B N     1 
ATOM   3123 C CA    . CYS   B 1 160 ? 40.408  49.604 39.612 1 19.81  ? 141 CYS   B CA    1 
ATOM   3124 C C     . CYS   B 1 160 ? 39.952  50.116 38.255 1 18.35  ? 141 CYS   B C     1 
ATOM   3125 O O     . CYS   B 1 160 ? 39.352  51.186 38.174 1 15.46  ? 141 CYS   B O     1 
ATOM   3126 C CB    . CYS   B 1 160 ? 39.516  48.487 40.146 1 22.32  ? 141 CYS   B CB    1 
ATOM   3127 S SG    . CYS   B 1 160 ? 37.792  48.588 39.636 1 27.59  ? 141 CYS   B SG    1 
ATOM   3128 N N     . ASP   B 1 161 ? 40.346  49.397 37.192 1 14.01  ? 142 ASP   B N     1 
ATOM   3129 C CA    . ASP   B 1 161 ? 39.979  49.699 35.821 1 13.81  ? 142 ASP   B CA    1 
ATOM   3130 C C     . ASP   B 1 161 ? 39.662  48.384 35.142 1 15.45  ? 142 ASP   B C     1 
ATOM   3131 O O     . ASP   B 1 161 ? 40.56   47.625 34.793 1 15.19  ? 142 ASP   B O     1 
ATOM   3132 C CB    . ASP   B 1 161 ? 41.072  50.499 35.077 1 15.61  ? 142 ASP   B CB    1 
ATOM   3133 C CG    . ASP   B 1 161 ? 40.692  50.979 33.68  1 18.09  ? 142 ASP   B CG    1 
ATOM   3134 O OD1   . ASP   B 1 161 ? 39.548  50.673 33.22  1 17.09  ? 142 ASP   B OD1   1 
ATOM   3135 O OD2   . ASP   B 1 161 ? 41.51   51.677 33.057 1 17.3   ? 142 ASP   B OD2   1 
ATOM   3136 N N     . VAL   B 1 162 ? 38.358  48.118 34.972 1 12.07  ? 143 VAL   B N     1 
ATOM   3137 C CA    . VAL   B 1 162 ? 37.804  46.895 34.364 1 11.26  ? 143 VAL   B CA    1 
ATOM   3138 C C     . VAL   B 1 162 ? 38.288  46.681 32.927 1 15.28  ? 143 VAL   B C     1 
ATOM   3139 O O     . VAL   B 1 162 ? 38.309  45.547 32.47  1 15.33  ? 143 VAL   B O     1 
ATOM   3140 C CB    . VAL   B 1 162 ? 36.253  46.816 34.473 1 13.73  ? 143 VAL   B CB    1 
ATOM   3141 C CG1   . VAL   B 1 162 ? 35.811  46.964 35.924 1 13.84  ? 143 VAL   B CG1   1 
ATOM   3142 C CG2   . VAL   B 1 162 ? 35.559  47.861 33.595 1 12.95  ? 143 VAL   B CG2   1 
ATOM   3143 N N     . THR   B 1 163 ? 38.714  47.747 32.241 1 13.57  ? 144 THR   B N     1 
ATOM   3144 C CA    . THR   B 1 163 ? 39.19   47.644 30.857 1 15.16  ? 144 THR   B CA    1 
ATOM   3145 C C     . THR   B 1 163 ? 40.638  47.134 30.781 1 21.15  ? 144 THR   B C     1 
ATOM   3146 O O     . THR   B 1 163 ? 41.125  46.856 29.676 1 21.28  ? 144 THR   B O     1 
ATOM   3147 C CB    . THR   B 1 163 ? 39.007  48.979 30.102 1 20.51  ? 144 THR   B CB    1 
ATOM   3148 O OG1   . THR   B 1 163 ? 39.95   49.943 30.576 1 19.26  ? 144 THR   B OG1   1 
ATOM   3149 C CG2   . THR   B 1 163 ? 37.579  49.508 30.151 1 14.25  ? 144 THR   B CG2   1 
ATOM   3150 N N     . GLN   B 1 164 ? 41.321  47.009 31.945 1 17.06  ? 145 GLN   B N     1 
ATOM   3151 C CA    . GLN   B 1 164 ? 42.722  46.567 32.009 1 16.93  ? 145 GLN   B CA    1 
ATOM   3152 C C     . GLN   B 1 164 ? 42.831  45.066 32.312 1 19.07  ? 145 GLN   B C     1 
ATOM   3153 O O     . GLN   B 1 164 ? 42.094  44.576 33.159 1 15.97  ? 145 GLN   B O     1 
ATOM   3154 C CB    . GLN   B 1 164 ? 43.511  47.398 33.048 1 18.06  ? 145 GLN   B CB    1 
ATOM   3155 C CG    . GLN   B 1 164 ? 43.588  48.905 32.773 1 29.26  ? 145 GLN   B CG    1 
ATOM   3156 C CD    . GLN   B 1 164 ? 44.415  49.238 31.557 1 48.08  ? 145 GLN   B CD    1 
ATOM   3157 O OE1   . GLN   B 1 164 ? 43.885  49.542 30.485 1 39.52  ? 145 GLN   B OE1   1 
ATOM   3158 N NE2   . GLN   B 1 164 ? 45.732  49.172 31.695 1 44.97  ? 145 GLN   B NE2   1 
ATOM   3159 N N     . SER   B 1 165 ? 43.769  44.334 31.659 1 16.84  ? 146 SER   B N     1 
ATOM   3160 C CA    . SER   B 1 165 ? 43.909  42.881 31.902 1 17.83  ? 146 SER   B CA    1 
ATOM   3161 C C     . SER   B 1 165 ? 44.153  42.566 33.398 1 21.2   ? 146 SER   B C     1 
ATOM   3162 O O     . SER   B 1 165 ? 43.689  41.542 33.894 1 19.93  ? 146 SER   B O     1 
ATOM   3163 C CB    . SER   B 1 165 ? 44.956  42.247 30.98  1 22.18  ? 146 SER   B CB    1 
ATOM   3164 O OG    . SER   B 1 165 ? 46.259  42.725 31.254 1 30.58  ? 146 SER   B OG    1 
ATOM   3165 N N     . GLN   B 1 166 ? 44.8    43.507 34.117 1 17.81  ? 147 GLN   B N     1 
ATOM   3166 C CA    . GLN   B 1 166 ? 44.984  43.486 35.554 1 17.24  ? 147 GLN   B CA    1 
ATOM   3167 C C     . GLN   B 1 166 ? 44.163  44.674 36.092 1 21.04  ? 147 GLN   B C     1 
ATOM   3168 O O     . GLN   B 1 166 ? 44.671  45.805 36.135 1 20.51  ? 147 GLN   B O     1 
ATOM   3169 C CB    . GLN   B 1 166 ? 46.469  43.607 35.932 1 19.07  ? 147 GLN   B CB    1 
ATOM   3170 C CG    . GLN   B 1 166 ? 47.23   42.292 35.829 1 39.19  ? 147 GLN   B CG    1 
ATOM   3171 C CD    . GLN   B 1 166 ? 48.527  42.432 35.079 1 66.7   ? 147 GLN   B CD    1 
ATOM   3172 O OE1   . GLN   B 1 166 ? 48.644  43.192 34.11  1 60.16  ? 147 GLN   B OE1   1 
ATOM   3173 N NE2   . GLN   B 1 166 ? 49.522  41.659 35.485 1 71     ? 147 GLN   B NE2   1 
ATOM   3174 N N     . PRO   B 1 167 ? 42.863  44.463 36.431 1 18.72  ? 148 PRO   B N     1 
ATOM   3175 C CA    . PRO   B 1 167 ? 42.03   45.591 36.892 1 18.66  ? 148 PRO   B CA    1 
ATOM   3176 C C     . PRO   B 1 167 ? 42.525  46.296 38.141 1 21.7   ? 148 PRO   B C     1 
ATOM   3177 O O     . PRO   B 1 167 ? 42.285  47.479 38.296 1 20.12  ? 148 PRO   B O     1 
ATOM   3178 C CB    . PRO   B 1 167 ? 40.647  44.954 37.124 1 20.14  ? 148 PRO   B CB    1 
ATOM   3179 C CG    . PRO   B 1 167 ? 40.663  43.701 36.361 1 23.9   ? 148 PRO   B CG    1 
ATOM   3180 C CD    . PRO   B 1 167 ? 42.078  43.211 36.397 1 19.84  ? 148 PRO   B CD    1 
ATOM   3181 N N     . LEU   B 1 168 ? 43.217  45.582 39.021 1 21.3   ? 149 LEU   B N     1 
ATOM   3182 C CA    . LEU   B 1 168 ? 43.745  46.172 40.253 1 22.26  ? 149 LEU   B CA    1 
ATOM   3183 C C     . LEU   B 1 168 ? 45.21   46.623 40.127 1 27.63  ? 149 LEU   B C     1 
ATOM   3184 O O     . LEU   B 1 168 ? 45.853  46.905 41.14  1 27.08  ? 149 LEU   B O     1 
ATOM   3185 C CB    . LEU   B 1 168 ? 43.526  45.208 41.426 1 22.36  ? 149 LEU   B CB    1 
ATOM   3186 C CG    . LEU   B 1 168 ? 42.075  44.717 41.583 1 27.53  ? 149 LEU   B CG    1 
ATOM   3187 C CD1   . LEU   B 1 168 ? 41.997  43.556 42.517 1 27.94  ? 149 LEU   B CD1   1 
ATOM   3188 C CD2   . LEU   B 1 168 ? 41.178  45.798 42.057 1 29.9   ? 149 LEU   B CD2   1 
ATOM   3189 N N     . GLY   B 1 169 ? 45.688  46.739 38.881 1 25.37  ? 150 GLY   B N     1 
ATOM   3190 C CA    . GLY   B 1 169 ? 47.043  47.161 38.55  1 26.63  ? 150 GLY   B CA    1 
ATOM   3191 C C     . GLY   B 1 169 ? 48.11   46.282 39.168 1 32.08  ? 150 GLY   B C     1 
ATOM   3192 O O     . GLY   B 1 169 ? 48.045  45.055 39.053 1 31.32  ? 150 GLY   B O     1 
ATOM   3193 N N     . ALA   B 1 170 ? 49.067  46.912 39.881 1 29.26  ? 151 ALA   B N     1 
ATOM   3194 C CA    . ALA   B 1 170 ? 50.18   46.229 40.548 1 29.45  ? 151 ALA   B CA    1 
ATOM   3195 C C     . ALA   B 1 170 ? 49.787  45.472 41.817 1 33.4   ? 151 ALA   B C     1 
ATOM   3196 O O     . ALA   B 1 170 ? 50.512  44.562 42.217 1 32.18  ? 151 ALA   B O     1 
ATOM   3197 C CB    . ALA   B 1 170 ? 51.295  47.221 40.858 1 30.52  ? 151 ALA   B CB    1 
ATOM   3198 N N     . VAL   B 1 171 ? 48.644  45.834 42.44  1 30.35  ? 152 VAL   B N     1 
ATOM   3199 C CA    . VAL   B 1 171 ? 48.16   45.234 43.694 1 29.86  ? 152 VAL   B CA    1 
ATOM   3200 C C     . VAL   B 1 171 ? 47.853  43.719 43.564 1 34.11  ? 152 VAL   B C     1 
ATOM   3201 O O     . VAL   B 1 171 ? 46.912  43.342 42.859 1 33.91  ? 152 VAL   B O     1 
ATOM   3202 C CB    . VAL   B 1 171 ? 46.963  46.012 44.313 1 33.63  ? 152 VAL   B CB    1 
ATOM   3203 C CG1   . VAL   B 1 171 ? 46.557  45.418 45.659 1 33.62  ? 152 VAL   B CG1   1 
ATOM   3204 C CG2   . VAL   B 1 171 ? 47.277  47.5   44.458 1 33.39  ? 152 VAL   B CG2   1 
ATOM   3205 N N     . PRO   B 1 172 ? 48.59   42.85  44.301 1 31.15  ? 153 PRO   B N     1 
ATOM   3206 C CA    . PRO   B 1 172 ? 48.307  41.41  44.24  1 30.63  ? 153 PRO   B CA    1 
ATOM   3207 C C     . PRO   B 1 172 ? 47.273  40.972 45.285 1 33.66  ? 153 PRO   B C     1 
ATOM   3208 O O     . PRO   B 1 172 ? 47.46   41.18  46.484 1 35.58  ? 153 PRO   B O     1 
ATOM   3209 C CB    . PRO   B 1 172 ? 49.683  40.777 44.467 1 32.63  ? 153 PRO   B CB    1 
ATOM   3210 C CG    . PRO   B 1 172 ? 50.438  41.781 45.29  1 37.56  ? 153 PRO   B CG    1 
ATOM   3211 C CD    . PRO   B 1 172 ? 49.741  43.122 45.19  1 33.39  ? 153 PRO   B CD    1 
ATOM   3212 N N     . LEU   B 1 173 ? 46.165  40.398 44.831 1 27     ? 154 LEU   B N     1 
ATOM   3213 C CA    . LEU   B 1 173 ? 45.115  39.938 45.731 1 25.23  ? 154 LEU   B CA    1 
ATOM   3214 C C     . LEU   B 1 173 ? 44.928  38.437 45.606 1 26.76  ? 154 LEU   B C     1 
ATOM   3215 O O     . LEU   B 1 173 ? 45.018  37.915 44.489 1 25.06  ? 154 LEU   B O     1 
ATOM   3216 C CB    . LEU   B 1 173 ? 43.767  40.633 45.414 1 24.62  ? 154 LEU   B CB    1 
ATOM   3217 C CG    . LEU   B 1 173 ? 43.412  41.954 46.125 1 28.99  ? 154 LEU   B CG    1 
ATOM   3218 C CD1   . LEU   B 1 173 ? 42.016  42.403 45.73  1 28.86  ? 154 LEU   B CD1   1 
ATOM   3219 C CD2   . LEU   B 1 173 ? 43.413  41.808 47.64  1 28.65  ? 154 LEU   B CD2   1 
ATOM   3220 N N     . PRO   B 1 174 ? 44.588  37.723 46.709 1 22.94  ? 155 PRO   B N     1 
ATOM   3221 C CA    . PRO   B 1 174 ? 44.279  36.287 46.575 1 22.8   ? 155 PRO   B CA    1 
ATOM   3222 C C     . PRO   B 1 174 ? 43.065  36.105 45.653 1 26.32  ? 155 PRO   B C     1 
ATOM   3223 O O     . PRO   B 1 174 ? 42.22   37.016 45.615 1 25.48  ? 155 PRO   B O     1 
ATOM   3224 C CB    . PRO   B 1 174 ? 43.928  35.851 48.015 1 24.08  ? 155 PRO   B CB    1 
ATOM   3225 C CG    . PRO   B 1 174 ? 44.462  36.912 48.896 1 28.43  ? 155 PRO   B CG    1 
ATOM   3226 C CD    . PRO   B 1 174 ? 44.423  38.185 48.104 1 24.21  ? 155 PRO   B CD    1 
ATOM   3227 N N     . PRO   B 1 175 ? 42.937  34.988 44.889 1 23.17  ? 156 PRO   B N     1 
ATOM   3228 C CA    . PRO   B 1 175 ? 41.757  34.836 44.014 1 22.22  ? 156 PRO   B CA    1 
ATOM   3229 C C     . PRO   B 1 175 ? 40.499  34.783 44.869 1 22.67  ? 156 PRO   B C     1 
ATOM   3230 O O     . PRO   B 1 175 ? 40.506  34.202 45.96  1 22.24  ? 156 PRO   B O     1 
ATOM   3231 C CB    . PRO   B 1 175 ? 42.033  33.536 43.25  1 24.26  ? 156 PRO   B CB    1 
ATOM   3232 C CG    . PRO   B 1 175 ? 43.51   33.324 43.39  1 29.33  ? 156 PRO   B CG    1 
ATOM   3233 C CD    . PRO   B 1 175 ? 43.823  33.815 44.773 1 24.94  ? 156 PRO   B CD    1 
ATOM   3234 N N     . ALA   B 1 176 ? 39.472  35.51  44.439 1 16.48  ? 157 ALA   B N     1 
ATOM   3235 C CA    . ALA   B 1 176 ? 38.243  35.649 45.203 1 15.57  ? 157 ALA   B CA    1 
ATOM   3236 C C     . ALA   B 1 176 ? 37.281  34.498 44.993 1 18.15  ? 157 ALA   B C     1 
ATOM   3237 O O     . ALA   B 1 176 ? 37.361  33.777 43.984 1 16.19  ? 157 ALA   B O     1 
ATOM   3238 C CB    . ALA   B 1 176 ? 37.566  36.981 44.87  1 16.04  ? 157 ALA   B CB    1 
ATOM   3239 N N     . ASP   B 1 177 ? 36.36   34.34  45.959 1 13.62  ? 158 ASP   B N     1 
ATOM   3240 C CA    . ASP   B 1 177 ? 35.301  33.336 45.903 1 13.47  ? 158 ASP   B CA    1 
ATOM   3241 C C     . ASP   B 1 177 ? 34.112  33.896 45.11  1 17.04  ? 158 ASP   B C     1 
ATOM   3242 O O     . ASP   B 1 177 ? 33.316  33.131 44.567 1 17.56  ? 158 ASP   B O     1 
ATOM   3243 C CB    . ASP   B 1 177 ? 34.853  32.975 47.326 1 15.25  ? 158 ASP   B CB    1 
ATOM   3244 C CG    . ASP   B 1 177 ? 35.959  32.341 48.14  1 21.78  ? 158 ASP   B CG    1 
ATOM   3245 O OD1   . ASP   B 1 177 ? 36.423  31.261 47.755 1 23.52  ? 158 ASP   B OD1   1 
ATOM   3246 O OD2   . ASP   B 1 177 ? 36.417  32.972 49.102 1 27.02  ? 158 ASP   B OD2   1 
ATOM   3247 N N     . CYS   B 1 178 ? 33.976  35.238 45.09  1 12.95  ? 159 CYS   B N     1 
ATOM   3248 C CA    . CYS   B 1 178 ? 32.91   35.95  44.379 1 11.85  ? 159 CYS   B CA    1 
ATOM   3249 C C     . CYS   B 1 178 ? 33.385  37.298 43.883 1 14.9   ? 159 CYS   B C     1 
ATOM   3250 O O     . CYS   B 1 178 ? 34.138  37.986 44.576 1 12.83  ? 159 CYS   B O     1 
ATOM   3251 C CB    . CYS   B 1 178 ? 31.671  36.098 45.261 1 11.54  ? 159 CYS   B CB    1 
ATOM   3252 S SG    . CYS   B 1 178 ? 30.271  36.943 44.462 1 15.2   ? 159 CYS   B SG    1 
ATOM   3253 N N     . VAL   B 1 179 ? 32.959  37.672 42.672 1 11.29  ? 160 VAL   B N     1 
ATOM   3254 C CA    . VAL   B 1 179 ? 33.206  38.999 42.121 1 10.32  ? 160 VAL   B CA    1 
ATOM   3255 C C     . VAL   B 1 179 ? 31.813  39.592 41.903 1 13.74  ? 160 VAL   B C     1 
ATOM   3256 O O     . VAL   B 1 179 ? 30.963  38.982 41.237 1 11.87  ? 160 VAL   B O     1 
ATOM   3257 C CB    . VAL   B 1 179 ? 34.135  39.047 40.866 1 14.26  ? 160 VAL   B CB    1 
ATOM   3258 C CG1   . VAL   B 1 179 ? 34.037  40.386 40.138 1 13.29  ? 160 VAL   B CG1   1 
ATOM   3259 C CG2   . VAL   B 1 179 ? 35.586  38.783 41.256 1 14.27  ? 160 VAL   B CG2   1 
ATOM   3260 N N     . LEU   B 1 180 ? 31.559  40.74  42.548 1 9.72   ? 161 LEU   B N     1 
ATOM   3261 C CA    . LEU   B 1 180 ? 30.288  41.429 42.462 1 10.24  ? 161 LEU   B CA    1 
ATOM   3262 C C     . LEU   B 1 180 ? 30.464  42.721 41.664 1 13.86  ? 161 LEU   B C     1 
ATOM   3263 O O     . LEU   B 1 180 ? 31.518  43.329 41.743 1 12.72  ? 161 LEU   B O     1 
ATOM   3264 C CB    . LEU   B 1 180 ? 29.791  41.737 43.893 1 10.84  ? 161 LEU   B CB    1 
ATOM   3265 C CG    . LEU   B 1 180 ? 28.495  42.55  44.07  1 15.28  ? 161 LEU   B CG    1 
ATOM   3266 C CD1   . LEU   B 1 180 ? 27.284  41.828 43.424 1 14.68  ? 161 LEU   B CD1   1 
ATOM   3267 C CD2   . LEU   B 1 180 ? 28.251  42.859 45.538 1 14.06  ? 161 LEU   B CD2   1 
ATOM   3268 N N     . SER   B 1 181 ? 29.459  43.123 40.878 1 10.03  ? 162 SER   B N     1 
ATOM   3269 C CA    . SER   B 1 181 ? 29.526  44.399 40.153 1 8.92   ? 162 SER   B CA    1 
ATOM   3270 C C     . SER   B 1 181 ? 28.126  44.862 39.838 1 14.77  ? 162 SER   B C     1 
ATOM   3271 O O     . SER   B 1 181 ? 27.446  44.278 38.978 1 13.4   ? 162 SER   B O     1 
ATOM   3272 C CB    . SER   B 1 181 ? 30.383  44.308 38.89  1 11.73  ? 162 SER   B CB    1 
ATOM   3273 O OG    . SER   B 1 181 ? 30.682  45.616 38.421 1 13.16  ? 162 SER   B OG    1 
ATOM   3274 N N     . THR   B 1 182 ? 27.688  45.927 40.549 1 11.48  ? 163 THR   B N     1 
ATOM   3275 C CA    . THR   B 1 182 ? 26.362  46.486 40.351 1 10.64  ? 163 THR   B CA    1 
ATOM   3276 C C     . THR   B 1 182 ? 26.433  47.81  39.622 1 12.05  ? 163 THR   B C     1 
ATOM   3277 O O     . THR   B 1 182 ? 27.142  48.709 40.057 1 12.16  ? 163 THR   B O     1 
ATOM   3278 C CB    . THR   B 1 182 ? 25.584  46.58  41.677 1 12.05  ? 163 THR   B CB    1 
ATOM   3279 O OG1   . THR   B 1 182 ? 26.28   47.434 42.589 1 12.2   ? 163 THR   B OG1   1 
ATOM   3280 C CG2   . THR   B 1 182 ? 25.329  45.223 42.304 1 10.71  ? 163 THR   B CG2   1 
ATOM   3281 N N     . LEU   B 1 183 ? 25.694  47.927 38.519 1 6.71   ? 164 LEU   B N     1 
ATOM   3282 C CA    . LEU   B 1 183 ? 25.561  49.161 37.736 1 6.69   ? 164 LEU   B CA    1 
ATOM   3283 C C     . LEU   B 1 183 ? 26.904  49.805 37.308 1 13.99  ? 164 LEU   B C     1 
ATOM   3284 O O     . LEU   B 1 183 ? 26.985  51.032 37.19  1 13.43  ? 164 LEU   B O     1 
ATOM   3285 C CB    . LEU   B 1 183 ? 24.675  50.177 38.519 1 6.41   ? 164 LEU   B CB    1 
ATOM   3286 C CG    . LEU   B 1 183 ? 23.182  49.818 38.701 1 9.34   ? 164 LEU   B CG    1 
ATOM   3287 C CD1   . LEU   B 1 183 ? 22.567  50.611 39.813 1 9.01   ? 164 LEU   B CD1   1 
ATOM   3288 C CD2   . LEU   B 1 183 ? 22.4    50.051 37.441 1 7.35   ? 164 LEU   B CD2   1 
ATOM   3289 N N     . CYS   B 1 184 ? 27.928  48.979 36.994 1 11.82  ? 165 CYS   B N     1 
ATOM   3290 C CA    . CYS   B 1 184 ? 29.251  49.459 36.583 1 10.15  ? 165 CYS   B CA    1 
ATOM   3291 C C     . CYS   B 1 184 ? 29.579  49.22  35.108 1 14.3   ? 165 CYS   B C     1 
ATOM   3292 O O     . CYS   B 1 184 ? 30.006  50.138 34.396 1 12.05  ? 165 CYS   B O     1 
ATOM   3293 C CB    . CYS   B 1 184 ? 30.326  48.846 37.486 1 10.02  ? 165 CYS   B CB    1 
ATOM   3294 S SG    . CYS   B 1 184 ? 32.023  49.04  36.867 1 13.51  ? 165 CYS   B SG    1 
ATOM   3295 N N     . LEU   B 1 185 ? 29.468  47.959 34.675 1 11.08  ? 166 LEU   B N     1 
ATOM   3296 C CA    . LEU   B 1 185 ? 29.937  47.525 33.361 1 10.9   ? 166 LEU   B CA    1 
ATOM   3297 C C     . LEU   B 1 185 ? 29.297  48.226 32.166 1 14.18  ? 166 LEU   B C     1 
ATOM   3298 O O     . LEU   B 1 185 ? 29.99   48.472 31.179 1 11.44  ? 166 LEU   B O     1 
ATOM   3299 C CB    . LEU   B 1 185 ? 29.826  46.02  33.219 1 11.14  ? 166 LEU   B CB    1 
ATOM   3300 C CG    . LEU   B 1 185 ? 30.632  45.168 34.208 1 15.17  ? 166 LEU   B CG    1 
ATOM   3301 C CD1   . LEU   B 1 185 ? 30.537  43.702 33.814 1 15.75  ? 166 LEU   B CD1   1 
ATOM   3302 C CD2   . LEU   B 1 185 ? 32.128  45.575 34.218 1 16.7   ? 166 LEU   B CD2   1 
ATOM   3303 N N     . ASP   B 1 186 ? 28.018  48.573 32.257 1 12.84  ? 167 ASP   B N     1 
ATOM   3304 C CA    . ASP   B 1 186 ? 27.322  49.293 31.195 1 14.39  ? 167 ASP   B CA    1 
ATOM   3305 C C     . ASP   B 1 186 ? 27.955  50.67  31.043 1 17.82  ? 167 ASP   B C     1 
ATOM   3306 O O     . ASP   B 1 186 ? 28.086  51.157 29.93  1 17.74  ? 167 ASP   B O     1 
ATOM   3307 C CB    . ASP   B 1 186 ? 25.84   49.487 31.571 1 17.48  ? 167 ASP   B CB    1 
ATOM   3308 C CG    . ASP   B 1 186 ? 24.845  48.482 31.036 1 31.16  ? 167 ASP   B CG    1 
ATOM   3309 O OD1   . ASP   B 1 186 ? 25.202  47.285 30.917 1 30.38  ? 167 ASP   B OD1   1 
ATOM   3310 O OD2   . ASP   B 1 186 ? 23.69   48.863 30.845 1 39.19  ? 167 ASP   B OD2   1 
ATOM   3311 N N     . ALA   B 1 187 ? 28.303  51.305 32.178 1 15.21  ? 168 ALA   B N     1 
ATOM   3312 C CA    . ALA   B 1 187 ? 28.911  52.64  32.247 1 15.05  ? 168 ALA   B CA    1 
ATOM   3313 C C     . ALA   B 1 187 ? 30.368  52.629 31.788 1 19.04  ? 168 ALA   B C     1 
ATOM   3314 O O     . ALA   B 1 187 ? 30.824  53.575 31.148 1 18.3   ? 168 ALA   B O     1 
ATOM   3315 C CB    . ALA   B 1 187 ? 28.83   53.167 33.676 1 15.78  ? 168 ALA   B CB    1 
ATOM   3316 N N     . ALA   B 1 188 ? 31.1    51.566 32.122 1 15.38  ? 169 ALA   B N     1 
ATOM   3317 C CA    . ALA   B 1 188 ? 32.529  51.479 31.864 1 14.6   ? 169 ALA   B CA    1 
ATOM   3318 C C     . ALA   B 1 188 ? 32.934  51.026 30.447 1 18.05  ? 169 ALA   B C     1 
ATOM   3319 O O     . ALA   B 1 188 ? 34.068  51.264 30.046 1 17.94  ? 169 ALA   B O     1 
ATOM   3320 C CB    . ALA   B 1 188 ? 33.172  50.573 32.914 1 14.78  ? 169 ALA   B CB    1 
ATOM   3321 N N     . CYS   B 1 189 ? 32.053  50.349 29.72  1 15.06  ? 170 CYS   B N     1 
ATOM   3322 C CA    . CYS   B 1 189 ? 32.384  49.767 28.414 1 14.46  ? 170 CYS   B CA    1 
ATOM   3323 C C     . CYS   B 1 189 ? 31.735  50.471 27.241 1 17.25  ? 170 CYS   B C     1 
ATOM   3324 O O     . CYS   B 1 189 ? 30.51   50.464 27.155 1 16.72  ? 170 CYS   B O     1 
ATOM   3325 C CB    . CYS   B 1 189 ? 32.07   48.277 28.405 1 13.95  ? 170 CYS   B CB    1 
ATOM   3326 S SG    . CYS   B 1 189 ? 32.749  47.383 29.815 1 17.83  ? 170 CYS   B SG    1 
ATOM   3327 N N     . PRO   B 1 190 ? 32.539  50.995 26.277 1 16.36  ? 171 PRO   B N     1 
ATOM   3328 C CA    . PRO   B 1 190 ? 31.947  51.708 25.12  1 16.99  ? 171 PRO   B CA    1 
ATOM   3329 C C     . PRO   B 1 190 ? 31.285  50.837 24.069 1 20.58  ? 171 PRO   B C     1 
ATOM   3330 O O     . PRO   B 1 190 ? 30.534  51.362 23.261 1 21.22  ? 171 PRO   B O     1 
ATOM   3331 C CB    . PRO   B 1 190 ? 33.13   52.494 24.52  1 19.15  ? 171 PRO   B CB    1 
ATOM   3332 C CG    . PRO   B 1 190 ? 34.268  52.318 25.475 1 22.93  ? 171 PRO   B CG    1 
ATOM   3333 C CD    . PRO   B 1 190 ? 34.011  51.07  26.245 1 18     ? 171 PRO   B CD    1 
ATOM   3334 N N     . ASP   B 1 191 ? 31.58   49.529 24.052 1 17.5   ? 172 ASP   B N     1 
ATOM   3335 C CA    . ASP   B 1 191 ? 31.02   48.591 23.072 1 17.82  ? 172 ASP   B CA    1 
ATOM   3336 C C     . ASP   B 1 191 ? 31.025  47.171 23.607 1 20.12  ? 172 ASP   B C     1 
ATOM   3337 O O     . ASP   B 1 191 ? 31.66   46.905 24.628 1 18     ? 172 ASP   B O     1 
ATOM   3338 C CB    . ASP   B 1 191 ? 31.762  48.678 21.711 1 20.05  ? 172 ASP   B CB    1 
ATOM   3339 C CG    . ASP   B 1 191 ? 33.281  48.682 21.811 1 31.02  ? 172 ASP   B CG    1 
ATOM   3340 O OD1   . ASP   B 1 191 ? 33.841  47.76  22.448 1 30.39  ? 172 ASP   B OD1   1 
ATOM   3341 O OD2   . ASP   B 1 191 ? 33.911  49.585 21.224 1 39.79  ? 172 ASP   B OD2   1 
ATOM   3342 N N     . LEU   B 1 192 ? 30.35   46.257 22.874 1 17.93  ? 173 LEU   B N     1 
ATOM   3343 C CA    . LEU   B 1 192 ? 30.212  44.838 23.178 1 18.13  ? 173 LEU   B CA    1 
ATOM   3344 C C     . LEU   B 1 192 ? 31.583  44.103 23.273 1 21.62  ? 173 LEU   B C     1 
ATOM   3345 O O     . LEU   B 1 192 ? 31.772  43.413 24.273 1 21.2   ? 173 LEU   B O     1 
ATOM   3346 C CB    . LEU   B 1 192 ? 29.226  44.159 22.203 1 18.34  ? 173 LEU   B CB    1 
ATOM   3347 C CG    . LEU   B 1 192 ? 28.806  42.696 22.474 1 22.81  ? 173 LEU   B CG    1 
ATOM   3348 C CD1   . LEU   B 1 192 ? 28.313  42.485 23.924 1 21.14  ? 173 LEU   B CD1   1 
ATOM   3349 C CD2   . LEU   B 1 192 ? 27.724  42.265 21.483 1 24.21  ? 173 LEU   B CD2   1 
ATOM   3350 N N     . PRO   B 1 193 ? 32.572  44.254 22.345 1 19.4   ? 174 PRO   B N     1 
ATOM   3351 C CA    . PRO   B 1 193 ? 33.865  43.557 22.537 1 18.48  ? 174 PRO   B CA    1 
ATOM   3352 C C     . PRO   B 1 193 ? 34.623  43.989 23.805 1 19.56  ? 174 PRO   B C     1 
ATOM   3353 O O     . PRO   B 1 193 ? 35.189  43.132 24.482 1 17.19  ? 174 PRO   B O     1 
ATOM   3354 C CB    . PRO   B 1 193 ? 34.625  43.855 21.237 1 20.14  ? 174 PRO   B CB    1 
ATOM   3355 C CG    . PRO   B 1 193 ? 33.535  44.139 20.233 1 24.86  ? 174 PRO   B CG    1 
ATOM   3356 C CD    . PRO   B 1 193 ? 32.566  44.961 21.045 1 21.19  ? 174 PRO   B CD    1 
ATOM   3357 N N     . THR   B 1 194 ? 34.557  45.285 24.182 1 16.32  ? 175 THR   B N     1 
ATOM   3358 C CA    . THR   B 1 194 ? 35.159  45.779 25.437 1 15.69  ? 175 THR   B CA    1 
ATOM   3359 C C     . THR   B 1 194 ? 34.387  45.181 26.627 1 16.78  ? 175 THR   B C     1 
ATOM   3360 O O     . THR   B 1 194 ? 35.003  44.793 27.615 1 15.21  ? 175 THR   B O     1 
ATOM   3361 C CB    . THR   B 1 194 ? 35.173  47.319 25.506 1 22.73  ? 175 THR   B CB    1 
ATOM   3362 O OG1   . THR   B 1 194 ? 35.812  47.836 24.342 1 25.85  ? 175 THR   B OG1   1 
ATOM   3363 C CG2   . THR   B 1 194 ? 35.894  47.845 26.749 1 19.38  ? 175 THR   B CG2   1 
ATOM   3364 N N     . TYR   B 1 195 ? 33.043  45.084 26.518 1 13.39  ? 176 TYR   B N     1 
ATOM   3365 C CA    . TYR   B 1 195 ? 32.209  44.489 27.576 1 12.51  ? 176 TYR   B CA    1 
ATOM   3366 C C     . TYR   B 1 195 ? 32.652  43.04  27.849 1 16.97  ? 176 TYR   B C     1 
ATOM   3367 O O     . TYR   B 1 195 ? 32.813  42.644 29.004 1 15.3   ? 176 TYR   B O     1 
ATOM   3368 C CB    . TYR   B 1 195 ? 30.724  44.558 27.175 1 13.53  ? 176 TYR   B CB    1 
ATOM   3369 C CG    . TYR   B 1 195 ? 29.766  44.129 28.266 1 13.93  ? 176 TYR   B CG    1 
ATOM   3370 C CD1   . TYR   B 1 195 ? 29.293  45.041 29.202 1 15.29  ? 176 TYR   B CD1   1 
ATOM   3371 C CD2   . TYR   B 1 195 ? 29.319  42.814 28.351 1 13.95  ? 176 TYR   B CD2   1 
ATOM   3372 C CE1   . TYR   B 1 195 ? 28.405  44.651 30.204 1 15.69  ? 176 TYR   B CE1   1 
ATOM   3373 C CE2   . TYR   B 1 195 ? 28.411  42.423 29.328 1 14.66  ? 176 TYR   B CE2   1 
ATOM   3374 C CZ    . TYR   B 1 195 ? 27.981  43.337 30.273 1 19.82  ? 176 TYR   B CZ    1 
ATOM   3375 O OH    . TYR   B 1 195 ? 27.102  42.948 31.252 1 18.64  ? 176 TYR   B OH    1 
ATOM   3376 N N     . CYS   B 1 196 ? 32.861  42.261 26.773 1 16.06  ? 177 CYS   B N     1 
ATOM   3377 C CA    . CYS   B 1 196 ? 33.328  40.883 26.847 1 16.84  ? 177 CYS   B CA    1 
ATOM   3378 C C     . CYS   B 1 196 ? 34.73   40.792 27.492 1 17.5   ? 177 CYS   B C     1 
ATOM   3379 O O     . CYS   B 1 196 ? 34.953  39.921 28.33  1 16.17  ? 177 CYS   B O     1 
ATOM   3380 C CB    . CYS   B 1 196 ? 33.294  40.232 25.469 1 19.33  ? 177 CYS   B CB    1 
ATOM   3381 S SG    . CYS   B 1 196 ? 33.682  38.465 25.489 1 24.62  ? 177 CYS   B SG    1 
ATOM   3382 N N     . ARG   B 1 197 ? 35.656  41.701 27.121 1 13.93  ? 178 ARG   B N     1 
ATOM   3383 C CA    . ARG   B 1 197 ? 37.007  41.756 27.694 1 13.47  ? 178 ARG   B CA    1 
ATOM   3384 C C     . ARG   B 1 197 ? 36.94   42.141 29.148 1 15.59  ? 178 ARG   B C     1 
ATOM   3385 O O     . ARG   B 1 197 ? 37.676  41.57  29.938 1 15.65  ? 178 ARG   B O     1 
ATOM   3386 C CB    . ARG   B 1 197 ? 37.896  42.772 26.977 1 15.47  ? 178 ARG   B CB    1 
ATOM   3387 C CG    . ARG   B 1 197 ? 38.461  42.297 25.649 1 28.66  ? 178 ARG   B CG    1 
ATOM   3388 C CD    . ARG   B 1 197 ? 39.602  43.177 25.14  1 30.71  ? 178 ARG   B CD    1 
ATOM   3389 N NE    . ARG   B 1 197 ? 39.333  44.619 25.226 1 38.28  ? 178 ARG   B NE    1 
ATOM   3390 C CZ    . ARG   B 1 197 ? 38.643  45.323 24.332 1 56.12  ? 178 ARG   B CZ    1 
ATOM   3391 N NH1   . ARG   B 1 197 ? 38.478  46.629 24.493 1 44.74  ? 178 ARG   B NH1   1 
ATOM   3392 N NH2   . ARG   B 1 197 ? 38.122  44.728 23.265 1 45.17  ? 178 ARG   B NH2   1 
ATOM   3393 N N     . ALA   B 1 198 ? 36.054  43.085 29.522 1 11.4   ? 179 ALA   B N     1 
ATOM   3394 C CA    . ALA   B 1 198 ? 35.926  43.498 30.935 1 11.98  ? 179 ALA   B CA    1 
ATOM   3395 C C     . ALA   B 1 198 ? 35.521  42.275 31.78  1 15.6   ? 179 ALA   B C     1 
ATOM   3396 O O     . ALA   B 1 198 ? 36.135  42.035 32.819 1 16.87  ? 179 ALA   B O     1 
ATOM   3397 C CB    . ALA   B 1 198 ? 34.905  44.623 31.075 1 11.86  ? 179 ALA   B CB    1 
ATOM   3398 N N     . LEU   B 1 199 ? 34.569  41.446 31.275 1 11.6   ? 180 LEU   B N     1 
ATOM   3399 C CA    . LEU   B 1 199 ? 34.129  40.207 31.935 1 11.82  ? 180 LEU   B CA    1 
ATOM   3400 C C     . LEU   B 1 199 ? 35.305  39.247 32.118 1 18.16  ? 180 LEU   B C     1 
ATOM   3401 O O     . LEU   B 1 199 ? 35.446  38.653 33.19  1 18.65  ? 180 LEU   B O     1 
ATOM   3402 C CB    . LEU   B 1 199 ? 32.979  39.519 31.159 1 11.46  ? 180 LEU   B CB    1 
ATOM   3403 C CG    . LEU   B 1 199 ? 31.602  40.211 31.168 1 14.22  ? 180 LEU   B CG    1 
ATOM   3404 C CD1   . LEU   B 1 199 ? 30.732  39.671 30.051 1 14.03  ? 180 LEU   B CD1   1 
ATOM   3405 C CD2   . LEU   B 1 199 ? 30.91   40.104 32.537 1 13.38  ? 180 LEU   B CD2   1 
ATOM   3406 N N     . ARG   B 1 200 ? 36.177  39.129 31.093 1 15.9   ? 181 ARG   B N     1 
ATOM   3407 C CA    . ARG   B 1 200 ? 37.394  38.295 31.159 1 15.88  ? 181 ARG   B CA    1 
ATOM   3408 C C     . ARG   B 1 200 ? 38.345  38.853 32.21  1 17.7   ? 181 ARG   B C     1 
ATOM   3409 O O     . ARG   B 1 200 ? 38.848  38.085 33.021 1 15.93  ? 181 ARG   B O     1 
ATOM   3410 C CB    . ARG   B 1 200 ? 38.122  38.249 29.808 1 14.36  ? 181 ARG   B CB    1 
ATOM   3411 C CG    . ARG   B 1 200 ? 37.376  37.517 28.724 1 12.92  ? 181 ARG   B CG    1 
ATOM   3412 C CD    . ARG   B 1 200 ? 38.268  37.359 27.506 1 19.79  ? 181 ARG   B CD    1 
ATOM   3413 N NE    . ARG   B 1 200 ? 37.561  36.797 26.344 1 25.74  ? 181 ARG   B NE    1 
ATOM   3414 C CZ    . ARG   B 1 200 ? 37.313  35.503 26.168 1 41.23  ? 181 ARG   B CZ    1 
ATOM   3415 N NH1   . ARG   B 1 200 ? 37.665  34.619 27.094 1 35.5   ? 181 ARG   B NH1   1 
ATOM   3416 N NH2   . ARG   B 1 200 ? 36.682  35.085 25.081 1 31.11  ? 181 ARG   B NH2   1 
ATOM   3417 N N     . ASN   B 1 201 ? 38.558  40.193 32.212 1 14.98  ? 182 ASN   B N     1 
ATOM   3418 C CA    . ASN   B 1 201 ? 39.424  40.918 33.157 1 14.11  ? 182 ASN   B CA    1 
ATOM   3419 C C     . ASN   B 1 201 ? 38.966  40.717 34.604 1 16.3   ? 182 ASN   B C     1 
ATOM   3420 O O     . ASN   B 1 201 ? 39.815  40.535 35.477 1 15.8   ? 182 ASN   B O     1 
ATOM   3421 C CB    . ASN   B 1 201 ? 39.497  42.407 32.804 1 15.87  ? 182 ASN   B CB    1 
ATOM   3422 C CG    . ASN   B 1 201 ? 40.07   42.666 31.437 1 21.68  ? 182 ASN   B CG    1 
ATOM   3423 O OD1   . ASN   B 1 201 ? 40.646  41.783 30.809 1 15.49  ? 182 ASN   B OD1   1 
ATOM   3424 N ND2   . ASN   B 1 201 ? 39.848  43.849 30.905 1 9.7    ? 182 ASN   B ND2   1 
ATOM   3425 N N     . LEU   B 1 202 ? 37.633  40.695 34.842 1 10.44  ? 183 LEU   B N     1 
ATOM   3426 C CA    . LEU   B 1 202 ? 37.049  40.443 36.166 1 10.34  ? 183 LEU   B CA    1 
ATOM   3427 C C     . LEU   B 1 202 ? 37.313  39.012 36.592 1 15.39  ? 183 LEU   B C     1 
ATOM   3428 O O     . LEU   B 1 202 ? 37.6    38.766 37.754 1 14.91  ? 183 LEU   B O     1 
ATOM   3429 C CB    . LEU   B 1 202 ? 35.53   40.727 36.239 1 9.9    ? 183 LEU   B CB    1 
ATOM   3430 C CG    . LEU   B 1 202 ? 34.985  42.147 36.011 1 14.82  ? 183 LEU   B CG    1 
ATOM   3431 C CD1   . LEU   B 1 202 ? 33.587  42.308 36.615 1 13.04  ? 183 LEU   B CD1   1 
ATOM   3432 C CD2   . LEU   B 1 202 ? 35.944  43.231 36.462 1 20.34  ? 183 LEU   B CD2   1 
ATOM   3433 N N     . GLY   B 1 203 ? 37.231  38.083 35.641 1 13.42  ? 184 GLY   B N     1 
ATOM   3434 C CA    . GLY   B 1 203 ? 37.486  36.667 35.873 1 12.96  ? 184 GLY   B CA    1 
ATOM   3435 C C     . GLY   B 1 203 ? 38.907  36.357 36.297 1 16.83  ? 184 GLY   B C     1 
ATOM   3436 O O     . GLY   B 1 203 ? 39.126  35.4   37.031 1 14.92  ? 184 GLY   B O     1 
ATOM   3437 N N     . SER   B 1 204 ? 39.887  37.173 35.878 1 15.82  ? 185 SER   B N     1 
ATOM   3438 C CA    . SER   B 1 204 ? 41.285  37.007 36.301 1 15.75  ? 185 SER   B CA    1 
ATOM   3439 C C     . SER   B 1 204 ? 41.414  37.165 37.846 1 19.34  ? 185 SER   B C     1 
ATOM   3440 O O     . SER   B 1 204 ? 42.395  36.692 38.431 1 17.06  ? 185 SER   B O     1 
ATOM   3441 C CB    . SER   B 1 204 ? 42.193  38.006 35.583 1 19.76  ? 185 SER   B CB    1 
ATOM   3442 O OG    . SER   B 1 204 ? 42.114  39.316 36.13  1 28.91  ? 185 SER   B OG    1 
ATOM   3443 N N     . LEU   B 1 205 ? 40.411  37.817 38.496 1 16.78  ? 186 LEU   B N     1 
ATOM   3444 C CA    . LEU   B 1 205 ? 40.381  38.031 39.96  1 16.08  ? 186 LEU   B CA    1 
ATOM   3445 C C     . LEU   B 1 205 ? 39.609  36.913 40.692 1 19.32  ? 186 LEU   B C     1 
ATOM   3446 O O     . LEU   B 1 205 ? 39.547  36.9   41.931 1 19.22  ? 186 LEU   B O     1 
ATOM   3447 C CB    . LEU   B 1 205 ? 39.71   39.387 40.286 1 16.63  ? 186 LEU   B CB    1 
ATOM   3448 C CG    . LEU   B 1 205 ? 40.212  40.632 39.556 1 20.91  ? 186 LEU   B CG    1 
ATOM   3449 C CD1   . LEU   B 1 205 ? 39.328  41.821 39.853 1 19.04  ? 186 LEU   B CD1   1 
ATOM   3450 C CD2   . LEU   B 1 205 ? 41.68   40.923 39.901 1 24.96  ? 186 LEU   B CD2   1 
ATOM   3451 N N     . LEU   B 1 206 ? 39.021  35.988 39.926 1 14.39  ? 187 LEU   B N     1 
ATOM   3452 C CA    . LEU   B 1 206 ? 38.155  34.944 40.44  1 15.08  ? 187 LEU   B CA    1 
ATOM   3453 C C     . LEU   B 1 206 ? 38.836  33.606 40.401 1 19.8   ? 187 LEU   B C     1 
ATOM   3454 O O     . LEU   B 1 206 ? 39.512  33.297 39.418 1 19.63  ? 187 LEU   B O     1 
ATOM   3455 C CB    . LEU   B 1 206 ? 36.899  34.846 39.557 1 15.59  ? 187 LEU   B CB    1 
ATOM   3456 C CG    . LEU   B 1 206 ? 35.51   35.211 40.057 1 20.19  ? 187 LEU   B CG    1 
ATOM   3457 C CD1   . LEU   B 1 206 ? 34.467  34.663 39.097 1 19.4   ? 187 LEU   B CD1   1 
ATOM   3458 C CD2   . LEU   B 1 206 ? 35.221  34.708 41.479 1 18.48  ? 187 LEU   B CD2   1 
ATOM   3459 N N     . LYS   B 1 207 ? 38.607  32.778 41.433 1 16.7   ? 188 LYS   B N     1 
ATOM   3460 C CA    . LYS   B 1 207 ? 39.148  31.426 41.429 1 17.32  ? 188 LYS   B CA    1 
ATOM   3461 C C     . LYS   B 1 207 ? 38.287  30.535 40.506 1 21.58  ? 188 LYS   B C     1 
ATOM   3462 O O     . LYS   B 1 207 ? 37.1    30.855 40.315 1 19.53  ? 188 LYS   B O     1 
ATOM   3463 C CB    . LYS   B 1 207 ? 39.246  30.844 42.86  1 20.94  ? 188 LYS   B CB    1 
ATOM   3464 C CG    . LYS   B 1 207 ? 37.937  30.665 43.64  1 37.41  ? 188 LYS   B CG    1 
ATOM   3465 C CD    . LYS   B 1 207 ? 38.173  30.026 45.041 1 43.9   ? 188 LYS   B CD    1 
ATOM   3466 C CE    . LYS   B 1 207 ? 39.179  30.745 45.93  1 45.76  ? 188 LYS   B CE    1 
ATOM   3467 N NZ    . LYS   B 1 207 ? 39.183  30.216 47.326 1 50.84  ? 188 LYS   B NZ    1 
ATOM   3468 N N     . PRO   B 1 208 ? 38.838  29.426 39.931 1 18.95  ? 189 PRO   B N     1 
ATOM   3469 C CA    . PRO   B 1 208 ? 37.995  28.518 39.124 1 17.99  ? 189 PRO   B CA    1 
ATOM   3470 C C     . PRO   B 1 208 ? 36.788  28.052 39.933 1 21.47  ? 189 PRO   B C     1 
ATOM   3471 O O     . PRO   B 1 208 ? 36.914  27.759 41.128 1 20.54  ? 189 PRO   B O     1 
ATOM   3472 C CB    . PRO   B 1 208 ? 38.936  27.335 38.826 1 19.62  ? 189 PRO   B CB    1 
ATOM   3473 C CG    . PRO   B 1 208 ? 40.303  27.924 38.889 1 23.97  ? 189 PRO   B CG    1 
ATOM   3474 C CD    . PRO   B 1 208 ? 40.223  28.916 40.021 1 20.4   ? 189 PRO   B CD    1 
ATOM   3475 N N     . GLY   B 1 209 ? 35.621  28.052 39.301 1 18.34  ? 190 GLY   B N     1 
ATOM   3476 C CA    . GLY   B 1 209 ? 34.388  27.671 39.977 1 18.62  ? 190 GLY   B CA    1 
ATOM   3477 C C     . GLY   B 1 209 ? 33.829  28.759 40.877 1 23.05  ? 190 GLY   B C     1 
ATOM   3478 O O     . GLY   B 1 209 ? 32.814  28.539 41.541 1 23.91  ? 190 GLY   B O     1 
ATOM   3479 N N     . GLY   B 1 210 ? 34.498  29.919 40.902 1 19.31  ? 191 GLY   B N     1 
ATOM   3480 C CA    . GLY   B 1 210 ? 34.094  31.099 41.663 1 19.18  ? 191 GLY   B CA    1 
ATOM   3481 C C     . GLY   B 1 210 ? 32.875  31.752 41.046 1 20.77  ? 191 GLY   B C     1 
ATOM   3482 O O     . GLY   B 1 210 ? 32.622  31.577 39.854 1 17.97  ? 191 GLY   B O     1 
ATOM   3483 N N     . PHE   B 1 211 ? 32.099  32.491 41.857 1 18.41  ? 192 PHE   B N     1 
ATOM   3484 C CA    . PHE   B 1 211 ? 30.879  33.14  41.391 1 18.03  ? 192 PHE   B CA    1 
ATOM   3485 C C     . PHE   B 1 211 ? 31.034  34.571 40.898 1 18.2   ? 192 PHE   B C     1 
ATOM   3486 O O     . PHE   B 1 211 ? 31.701  35.39  41.526 1 17.27  ? 192 PHE   B O     1 
ATOM   3487 C CB    . PHE   B 1 211 ? 29.794  33.099 42.467 1 20.67  ? 192 PHE   B CB    1 
ATOM   3488 C CG    . PHE   B 1 211 ? 29.213  31.732 42.727 1 23.9   ? 192 PHE   B CG    1 
ATOM   3489 C CD1   . PHE   B 1 211 ? 28.125  31.269 41.992 1 28.36  ? 192 PHE   B CD1   1 
ATOM   3490 C CD2   . PHE   B 1 211 ? 29.714  30.927 43.745 1 27.01  ? 192 PHE   B CD2   1 
ATOM   3491 C CE1   . PHE   B 1 211 ? 27.548  30.023 42.272 1 29.93  ? 192 PHE   B CE1   1 
ATOM   3492 C CE2   . PHE   B 1 211 ? 29.138  29.682 44.024 1 30.43  ? 192 PHE   B CE2   1 
ATOM   3493 C CZ    . PHE   B 1 211 ? 28.073  29.23  43.271 1 28.95  ? 192 PHE   B CZ    1 
ATOM   3494 N N     . LEU   B 1 212 ? 30.375  34.868 39.776 1 12.93  ? 193 LEU   B N     1 
ATOM   3495 C CA    . LEU   B 1 212 ? 30.296  36.206 39.203 1 11.68  ? 193 LEU   B CA    1 
ATOM   3496 C C     . LEU   B 1 212 ? 28.854  36.687 39.379 1 12.66  ? 193 LEU   B C     1 
ATOM   3497 O O     . LEU   B 1 212 ? 27.916  36.01  38.94  1 11.13  ? 193 LEU   B O     1 
ATOM   3498 C CB    . LEU   B 1 212 ? 30.679  36.202 37.712 1 11.53  ? 193 LEU   B CB    1 
ATOM   3499 C CG    . LEU   B 1 212 ? 30.736  37.582 37.025 1 15.33  ? 193 LEU   B CG    1 
ATOM   3500 C CD1   . LEU   B 1 212 ? 32.008  38.343 37.427 1 15.17  ? 193 LEU   B CD1   1 
ATOM   3501 C CD2   . LEU   B 1 212 ? 30.69   37.436 35.495 1 14.52  ? 193 LEU   B CD2   1 
ATOM   3502 N N     . VAL   B 1 213 ? 28.667  37.83  40.052 1 9.07   ? 194 VAL   B N     1 
ATOM   3503 C CA    . VAL   B 1 213 ? 27.316  38.376 40.269 1 9.23   ? 194 VAL   B CA    1 
ATOM   3504 C C     . VAL   B 1 213 ? 27.245  39.756 39.622 1 15.06  ? 194 VAL   B C     1 
ATOM   3505 O O     . VAL   B 1 213 ? 27.918  40.676 40.078 1 14.38  ? 194 VAL   B O     1 
ATOM   3506 C CB    . VAL   B 1 213 ? 26.884  38.391 41.771 1 12.92  ? 194 VAL   B CB    1 
ATOM   3507 C CG1   . VAL   B 1 213 ? 25.511  39.049 41.951 1 12.06  ? 194 VAL   B CG1   1 
ATOM   3508 C CG2   . VAL   B 1 213 ? 26.872  36.982 42.352 1 13.1   ? 194 VAL   B CG2   1 
ATOM   3509 N N     . ILE   B 1 214 ? 26.431  39.901 38.564 1 11.88  ? 195 ILE   B N     1 
ATOM   3510 C CA    . ILE   B 1 214 ? 26.276  41.187 37.876 1 11.4   ? 195 ILE   B CA    1 
ATOM   3511 C C     . ILE   B 1 214 ? 24.825  41.632 37.924 1 15.02  ? 195 ILE   B C     1 
ATOM   3512 O O     . ILE   B 1 214 ? 23.932  40.844 37.63  1 15.17  ? 195 ILE   B O     1 
ATOM   3513 C CB    . ILE   B 1 214 ? 26.794  41.159 36.388 1 14.31  ? 195 ILE   B CB    1 
ATOM   3514 C CG1   . ILE   B 1 214 ? 28.242  40.605 36.231 1 13.85  ? 195 ILE   B CG1   1 
ATOM   3515 C CG2   . ILE   B 1 214 ? 26.663  42.543 35.712 1 15.84  ? 195 ILE   B CG2   1 
ATOM   3516 C CD1   . ILE   B 1 214 ? 29.423  41.459 36.838 1 16.14  ? 195 ILE   B CD1   1 
ATOM   3517 N N     . MET   B 1 215 ? 24.593  42.908 38.276 1 10.83  ? 196 MET   B N     1 
ATOM   3518 C CA    . MET   B 1 215 ? 23.274  43.541 38.212 1 10.52  ? 196 MET   B CA    1 
ATOM   3519 C C     . MET   B 1 215 ? 23.506  44.838 37.429 1 13.18  ? 196 MET   B C     1 
ATOM   3520 O O     . MET   B 1 215 ? 24.493  45.517 37.682 1 12.32  ? 196 MET   B O     1 
ATOM   3521 C CB    . MET   B 1 215 ? 22.684  43.82  39.608 1 12.52  ? 196 MET   B CB    1 
ATOM   3522 C CG    . MET   B 1 215 ? 22.469  42.562 40.417 1 15.8   ? 196 MET   B CG    1 
ATOM   3523 S SD    . MET   B 1 215 ? 21.717  42.838 42.024 1 19.41  ? 196 MET   B SD    1 
ATOM   3524 C CE    . MET   B 1 215 ? 21.708  41.196 42.61  1 16.35  ? 196 MET   B CE    1 
ATOM   3525 N N     . ASP   B 1 216 ? 22.665  45.144 36.427 1 10.61  ? 197 ASP   B N     1 
ATOM   3526 C CA    . ASP   B 1 216 ? 22.865  46.361 35.63  1 10.17  ? 197 ASP   B CA    1 
ATOM   3527 C C     . ASP   B 1 216 ? 21.614  46.703 34.841 1 15.99  ? 197 ASP   B C     1 
ATOM   3528 O O     . ASP   B 1 216 ? 20.641  45.943 34.858 1 15.49  ? 197 ASP   B O     1 
ATOM   3529 C CB    . ASP   B 1 216 ? 24.068  46.205 34.67  1 11.72  ? 197 ASP   B CB    1 
ATOM   3530 C CG    . ASP   B 1 216 ? 24.923  47.444 34.511 1 16.15  ? 197 ASP   B CG    1 
ATOM   3531 O OD1   . ASP   B 1 216 ? 24.366  48.562 34.57  1 15.02  ? 197 ASP   B OD1   1 
ATOM   3532 O OD2   . ASP   B 1 216 ? 26.141  47.294 34.275 1 18.46  ? 197 ASP   B OD2   1 
ATOM   3533 N N     . ALA   B 1 217 ? 21.633  47.859 34.158 1 12.85  ? 198 ALA   B N     1 
ATOM   3534 C CA    . ALA   B 1 217 ? 20.489  48.319 33.377 1 12.8   ? 198 ALA   B CA    1 
ATOM   3535 C C     . ALA   B 1 217 ? 20.398  47.601 32.014 1 15.2   ? 198 ALA   B C     1 
ATOM   3536 O O     . ALA   B 1 217 ? 21.427  47.266 31.427 1 12.66  ? 198 ALA   B O     1 
ATOM   3537 C CB    . ALA   B 1 217 ? 20.598  49.822 33.161 1 13.54  ? 198 ALA   B CB    1 
ATOM   3538 N N     . LEU   B 1 218 ? 19.17   47.39  31.507 1 10.42  ? 199 LEU   B N     1 
ATOM   3539 C CA    . LEU   B 1 218 ? 19      46.832 30.162 1 10.47  ? 199 LEU   B CA    1 
ATOM   3540 C C     . LEU   B 1 218 ? 18.685  47.971 29.19  1 15.2   ? 199 LEU   B C     1 
ATOM   3541 O O     . LEU   B 1 218 ? 17.918  48.86  29.539 1 14.54  ? 199 LEU   B O     1 
ATOM   3542 C CB    . LEU   B 1 218 ? 17.873  45.76  30.101 1 9.88   ? 199 LEU   B CB    1 
ATOM   3543 C CG    . LEU   B 1 218 ? 18.187  44.401 30.755 1 13.3   ? 199 LEU   B CG    1 
ATOM   3544 C CD1   . LEU   B 1 218 ? 16.91   43.592 30.981 1 13.27  ? 199 LEU   B CD1   1 
ATOM   3545 C CD2   . LEU   B 1 218 ? 19.184  43.585 29.926 1 11.85  ? 199 LEU   B CD2   1 
ATOM   3546 N N     . LYS   B 1 219 ? 19.311  47.962 27.995 1 12.19  ? 200 LYS   B N     1 
ATOM   3547 C CA    . LYS   B 1 219 ? 19.067  48.879 26.874 1 12.5   ? 200 LYS   B CA    1 
ATOM   3548 C C     . LYS   B 1 219 ? 19.113  50.381 27.24  1 17.79  ? 200 LYS   B C     1 
ATOM   3549 O O     . LYS   B 1 219 ? 18.322  51.176 26.73  1 17.12  ? 200 LYS   B O     1 
ATOM   3550 C CB    . LYS   B 1 219 ? 17.722  48.512 26.195 1 16.14  ? 200 LYS   B CB    1 
ATOM   3551 C CG    . LYS   B 1 219 ? 17.621  47.027 25.812 1 20.51  ? 200 LYS   B CG    1 
ATOM   3552 C CD    . LYS   B 1 219 ? 16.447  46.738 24.898 1 30.96  ? 200 LYS   B CD    1 
ATOM   3553 C CE    . LYS   B 1 219 ? 16.865  45.838 23.763 1 45.13  ? 200 LYS   B CE    1 
ATOM   3554 N NZ    . LYS   B 1 219 ? 15.71   45.444 22.917 1 60.29  ? 200 LYS   B NZ    1 
ATOM   3555 N N     . SER   B 1 220 ? 20.046  50.757 28.122 1 13.48  ? 201 SER   B N     1 
ATOM   3556 C CA    . SER   B 1 220 ? 20.228  52.142 28.546 1 12.96  ? 201 SER   B CA    1 
ATOM   3557 C C     . SER   B 1 220 ? 21.405  52.734 27.765 1 15.04  ? 201 SER   B C     1 
ATOM   3558 O O     . SER   B 1 220 ? 22.478  52.13  27.745 1 14.26  ? 201 SER   B O     1 
ATOM   3559 C CB    . SER   B 1 220 ? 20.51   52.194 30.048 1 16.64  ? 201 SER   B CB    1 
ATOM   3560 O OG    . SER   B 1 220 ? 20.15   53.453 30.591 1 28.91  ? 201 SER   B OG    1 
ATOM   3561 N N     . SER   B 1 221 ? 21.212  53.9   27.12  1 12.06  ? 202 SER   B N     1 
ATOM   3562 C CA    . SER   B 1 221 ? 22.277  54.563 26.35  1 11.52  ? 202 SER   B CA    1 
ATOM   3563 C C     . SER   B 1 221 ? 22.899  55.751 27.105 1 14.65  ? 202 SER   B C     1 
ATOM   3564 O O     . SER   B 1 221 ? 23.914  56.3   26.673 1 13.45  ? 202 SER   B O     1 
ATOM   3565 C CB    . SER   B 1 221 ? 21.795  54.95  24.951 1 13.4   ? 202 SER   B CB    1 
ATOM   3566 O OG    . SER   B 1 221 ? 20.827  55.972 25.066 1 19.56  ? 202 SER   B OG    1 
ATOM   3567 N N     . TYR   B 1 222 ? 22.3    56.113 28.252 1 12.19  ? 203 TYR   B N     1 
ATOM   3568 C CA    . TYR   B 1 222 ? 22.756  57.131 29.189 1 12.3   ? 203 TYR   B CA    1 
ATOM   3569 C C     . TYR   B 1 222 ? 22.078  57.01  30.556 1 16.84  ? 203 TYR   B C     1 
ATOM   3570 O O     . TYR   B 1 222 ? 21.088  56.3   30.717 1 16.95  ? 203 TYR   B O     1 
ATOM   3571 C CB    . TYR   B 1 222 ? 22.63   58.589 28.632 1 12.76  ? 203 TYR   B CB    1 
ATOM   3572 C CG    . TYR   B 1 222 ? 21.202  59.098 28.592 1 14.08  ? 203 TYR   B CG    1 
ATOM   3573 C CD1   . TYR   B 1 222 ? 20.628  59.713 29.703 1 15.82  ? 203 TYR   B CD1   1 
ATOM   3574 C CD2   . TYR   B 1 222 ? 20.427  58.965 27.444 1 14.81  ? 203 TYR   B CD2   1 
ATOM   3575 C CE1   . TYR   B 1 222 ? 19.297  60.127 29.693 1 18.86  ? 203 TYR   B CE1   1 
ATOM   3576 C CE2   . TYR   B 1 222 ? 19.105  59.395 27.413 1 16.19  ? 203 TYR   B CE2   1 
ATOM   3577 C CZ    . TYR   B 1 222 ? 18.539  59.969 28.544 1 23.59  ? 203 TYR   B CZ    1 
ATOM   3578 O OH    . TYR   B 1 222 ? 17.234  60.399 28.524 1 20.79  ? 203 TYR   B OH    1 
ATOM   3579 N N     . TYR   B 1 223 ? 22.652  57.72  31.538 1 12.75  ? 204 TYR   B N     1 
ATOM   3580 C CA    . TYR   B 1 223 ? 22.15   57.954 32.879 1 12.65  ? 204 TYR   B CA    1 
ATOM   3581 C C     . TYR   B 1 223 ? 22.622  59.35  33.307 1 16.07  ? 204 TYR   B C     1 
ATOM   3582 O O     . TYR   B 1 223 ? 23.646  59.861 32.809 1 13.21  ? 204 TYR   B O     1 
ATOM   3583 C CB    . TYR   B 1 223 ? 22.472  56.828 33.893 1 13.03  ? 204 TYR   B CB    1 
ATOM   3584 C CG    . TYR   B 1 223 ? 23.909  56.767 34.357 1 14.2   ? 204 TYR   B CG    1 
ATOM   3585 C CD1   . TYR   B 1 223 ? 24.878  56.105 33.604 1 14.43  ? 204 TYR   B CD1   1 
ATOM   3586 C CD2   . TYR   B 1 223 ? 24.304  57.371 35.55  1 15.78  ? 204 TYR   B CD2   1 
ATOM   3587 C CE1   . TYR   B 1 223 ? 26.201  56.031 34.032 1 13.08  ? 204 TYR   B CE1   1 
ATOM   3588 C CE2   . TYR   B 1 223 ? 25.63   57.317 35.981 1 16.55  ? 204 TYR   B CE2   1 
ATOM   3589 C CZ    . TYR   B 1 223 ? 26.572  56.638 35.22  1 18.94  ? 204 TYR   B CZ    1 
ATOM   3590 O OH    . TYR   B 1 223 ? 27.871  56.553 35.638 1 16.38  ? 204 TYR   B OH    1 
ATOM   3591 N N     . MET   B 1 224 ? 21.843  59.979 34.189 1 13.05  ? 205 MET   B N     1 
ATOM   3592 C CA    . MET   B 1 224 ? 22.07   61.351 34.624 1 11.63  ? 205 MET   B CA    1 
ATOM   3593 C C     . MET   B 1 224 ? 22.382  61.484 36.1   1 15.38  ? 205 MET   B C     1 
ATOM   3594 O O     . MET   B 1 224 ? 21.8    60.776 36.899 1 15.58  ? 205 MET   B O     1 
ATOM   3595 C CB    . MET   B 1 224 ? 20.787  62.173 34.347 1 12.98  ? 205 MET   B CB    1 
ATOM   3596 C CG    . MET   B 1 224 ? 20.298  62.144 32.897 1 14.47  ? 205 MET   B CG    1 
ATOM   3597 S SD    . MET   B 1 224 ? 21.407  62.887 31.677 1 16.53  ? 205 MET   B SD    1 
ATOM   3598 C CE    . MET   B 1 224 ? 21.466  64.533 32.261 1 12.06  ? 205 MET   B CE    1 
ATOM   3599 N N     . ILE   B 1 225 ? 23.218  62.447 36.471 1 13.85  ? 206 ILE   B N     1 
ATOM   3600 C CA    . ILE   B 1 225 ? 23.462  62.819 37.881 1 14.78  ? 206 ILE   B CA    1 
ATOM   3601 C C     . ILE   B 1 225 ? 23.18   64.314 37.831 1 20.61  ? 206 ILE   B C     1 
ATOM   3602 O O     . ILE   B 1 225 ? 24.061  65.089 37.463 1 19.92  ? 206 ILE   B O     1 
ATOM   3603 C CB    . ILE   B 1 225 ? 24.886  62.506 38.422 1 17.79  ? 206 ILE   B CB    1 
ATOM   3604 C CG1   . ILE   B 1 225 ? 25.204  61.003 38.323 1 17.92  ? 206 ILE   B CG1   1 
ATOM   3605 C CG2   . ILE   B 1 225 ? 25.007  63.003 39.883 1 19.16  ? 206 ILE   B CG2   1 
ATOM   3606 C CD1   . ILE   B 1 225 ? 26.63   60.663 38.622 1 25.88  ? 206 ILE   B CD1   1 
ATOM   3607 N N     . GLY   B 1 226 ? 21.923  64.683 38.059 1 18.3   ? 207 GLY   B N     1 
ATOM   3608 C CA    . GLY   B 1 226 ? 21.491  66.062 37.903 1 18.98  ? 207 GLY   B CA    1 
ATOM   3609 C C     . GLY   B 1 226 ? 21.486  66.381 36.418 1 22.84  ? 207 GLY   B C     1 
ATOM   3610 O O     . GLY   B 1 226 ? 20.937  65.609 35.627 1 22.68  ? 207 GLY   B O     1 
ATOM   3611 N N     . GLU   B 1 227 ? 22.199  67.448 36.016 1 19.38  ? 208 GLU   B N     1 
ATOM   3612 C CA    . GLU   B 1 227 ? 22.312  67.86  34.613 1 18.55  ? 208 GLU   B CA    1 
ATOM   3613 C C     . GLU   B 1 227 ? 23.506  67.204 33.911 1 21.32  ? 208 GLU   B C     1 
ATOM   3614 O O     . GLU   B 1 227 ? 23.697  67.41  32.701 1 20.69  ? 208 GLU   B O     1 
ATOM   3615 C CB    . GLU   B 1 227 ? 22.416  69.382 34.503 1 20.19  ? 208 GLU   B CB    1 
ATOM   3616 C CG    . GLU   B 1 227 ? 21.145  70.131 34.84  1 29.96  ? 208 GLU   B CG    1 
ATOM   3617 C CD    . GLU   B 1 227 ? 21.357  71.621 34.687 1 52.88  ? 208 GLU   B CD    1 
ATOM   3618 O OE1   . GLU   B 1 227 ? 21.163  72.13  33.558 1 50.56  ? 208 GLU   B OE1   1 
ATOM   3619 O OE2   . GLU   B 1 227 ? 21.81   72.261 35.667 1 45     ? 208 GLU   B OE2   1 
ATOM   3620 N N     . GLN   B 1 228 ? 24.335  66.452 34.66  1 16.18  ? 209 GLN   B N     1 
ATOM   3621 C CA    . GLN   B 1 228 ? 25.484  65.763 34.062 1 15.2   ? 209 GLN   B CA    1 
ATOM   3622 C C     . GLN   B 1 228 ? 25.071  64.439 33.402 1 16.49  ? 209 GLN   B C     1 
ATOM   3623 O O     . GLN   B 1 228 ? 24.567  63.537 34.071 1 12.51  ? 209 GLN   B O     1 
ATOM   3624 C CB    . GLN   B 1 228 ? 26.612  65.541 35.09  1 16.19  ? 209 GLN   B CB    1 
ATOM   3625 C CG    . GLN   B 1 228 ? 27.833  64.762 34.56  1 12.96  ? 209 GLN   B CG    1 
ATOM   3626 C CD    . GLN   B 1 228 ? 28.667  65.51  33.549 1 25.82  ? 209 GLN   B CD    1 
ATOM   3627 O OE1   . GLN   B 1 228 ? 28.807  65.117 32.379 1 23.27  ? 209 GLN   B OE1   1 
ATOM   3628 N NE2   . GLN   B 1 228 ? 29.29   66.561 33.993 1 9.43   ? 209 GLN   B NE2   1 
ATOM   3629 N N     . LYS   B 1 229 ? 25.362  64.312 32.108 1 13.78  ? 210 LYS   B N     1 
ATOM   3630 C CA    . LYS   B 1 229 ? 25.101  63.086 31.357 1 12.88  ? 210 LYS   B CA    1 
ATOM   3631 C C     . LYS   B 1 229 ? 26.345  62.199 31.349 1 16.71  ? 210 LYS   B C     1 
ATOM   3632 O O     . LYS   B 1 229 ? 27.467  62.695 31.232 1 16.97  ? 210 LYS   B O     1 
ATOM   3633 C CB    . LYS   B 1 229 ? 24.695  63.429 29.919 1 14.3   ? 210 LYS   B CB    1 
ATOM   3634 C CG    . LYS   B 1 229 ? 24.168  62.271 29.079 1 17.11  ? 210 LYS   B CG    1 
ATOM   3635 C CD    . LYS   B 1 229 ? 23.397  62.867 27.915 1 21.71  ? 210 LYS   B CD    1 
ATOM   3636 C CE    . LYS   B 1 229 ? 23.066  61.877 26.841 1 26.83  ? 210 LYS   B CE    1 
ATOM   3637 N NZ    . LYS   B 1 229 ? 22.208  62.489 25.791 1 22.78  ? 210 LYS   B NZ    1 
ATOM   3638 N N     . PHE   B 1 230 ? 26.126  60.892 31.47  1 12.69  ? 211 PHE   B N     1 
ATOM   3639 C CA    . PHE   B 1 230 ? 27.129  59.829 31.388 1 11.49  ? 211 PHE   B CA    1 
ATOM   3640 C C     . PHE   B 1 230 ? 26.598  58.815 30.393 1 14.97  ? 211 PHE   B C     1 
ATOM   3641 O O     . PHE   B 1 230 ? 25.415  58.461 30.432 1 13.18  ? 211 PHE   B O     1 
ATOM   3642 C CB    . PHE   B 1 230 ? 27.326  59.134 32.742 1 12.89  ? 211 PHE   B CB    1 
ATOM   3643 C CG    . PHE   B 1 230 ? 28.124  59.955 33.72  1 13.78  ? 211 PHE   B CG    1 
ATOM   3644 C CD1   . PHE   B 1 230 ? 29.513  59.984 33.658 1 15.34  ? 211 PHE   B CD1   1 
ATOM   3645 C CD2   . PHE   B 1 230 ? 27.486  60.743 34.673 1 15.65  ? 211 PHE   B CD2   1 
ATOM   3646 C CE1   . PHE   B 1 230 ? 30.254  60.769 34.542 1 15.93  ? 211 PHE   B CE1   1 
ATOM   3647 C CE2   . PHE   B 1 230 ? 28.233  61.528 35.561 1 18.06  ? 211 PHE   B CE2   1 
ATOM   3648 C CZ    . PHE   B 1 230 ? 29.61   61.542 35.477 1 15.33  ? 211 PHE   B CZ    1 
ATOM   3649 N N     . SER   B 1 231 ? 27.474  58.329 29.516 1 12.01  ? 212 SER   B N     1 
ATOM   3650 C CA    . SER   B 1 231 ? 27.131  57.289 28.542 1 11.97  ? 212 SER   B CA    1 
ATOM   3651 C C     . SER   B 1 231 ? 26.833  55.966 29.248 1 14.32  ? 212 SER   B C     1 
ATOM   3652 O O     . SER   B 1 231 ? 27.305  55.739 30.356 1 12.7   ? 212 SER   B O     1 
ATOM   3653 C CB    . SER   B 1 231 ? 28.302  57.067 27.587 1 12.87  ? 212 SER   B CB    1 
ATOM   3654 O OG    . SER   B 1 231 ? 28.373  58.156 26.689 1 23.89  ? 212 SER   B OG    1 
ATOM   3655 N N     . SER   B 1 232 ? 26.061  55.1   28.592 1 11.8   ? 213 SER   B N     1 
ATOM   3656 C CA    . SER   B 1 232 ? 25.77   53.757 29.066 1 12.17  ? 213 SER   B CA    1 
ATOM   3657 C C     . SER   B 1 232 ? 25.706  52.859 27.834 1 16.45  ? 213 SER   B C     1 
ATOM   3658 O O     . SER   B 1 232 ? 25.196  53.299 26.809 1 16.82  ? 213 SER   B O     1 
ATOM   3659 C CB    . SER   B 1 232 ? 24.449  53.74  29.829 1 17.44  ? 213 SER   B CB    1 
ATOM   3660 O OG    . SER   B 1 232 ? 24.159  52.457 30.348 1 27.35  ? 213 SER   B OG    1 
ATOM   3661 N N     . LEU   B 1 233 ? 26.245  51.624 27.897 1 13.36  ? 214 LEU   B N     1 
ATOM   3662 C CA    . LEU   B 1 233 ? 26.177  50.719 26.736 1 12.58  ? 214 LEU   B CA    1 
ATOM   3663 C C     . LEU   B 1 233 ? 24.782  50.065 26.687 1 16.68  ? 214 LEU   B C     1 
ATOM   3664 O O     . LEU   B 1 233 ? 24.398  49.414 27.656 1 17.45  ? 214 LEU   B O     1 
ATOM   3665 C CB    . LEU   B 1 233 ? 27.314  49.694 26.764 1 12.19  ? 214 LEU   B CB    1 
ATOM   3666 C CG    . LEU   B 1 233 ? 27.337  48.553 25.757 1 16.75  ? 214 LEU   B CG    1 
ATOM   3667 C CD1   . LEU   B 1 233 ? 27.526  49.065 24.3   1 17.44  ? 214 LEU   B CD1   1 
ATOM   3668 C CD2   . LEU   B 1 233 ? 28.415  47.55  26.153 1 16.63  ? 214 LEU   B CD2   1 
ATOM   3669 N N     . PRO   B 1 234 ? 23.993  50.275 25.601 1 14.01  ? 215 PRO   B N     1 
ATOM   3670 C CA    . PRO   B 1 234 ? 22.635  49.739 25.585 1 14.59  ? 215 PRO   B CA    1 
ATOM   3671 C C     . PRO   B 1 234 ? 22.596  48.273 25.196 1 21.24  ? 215 PRO   B C     1 
ATOM   3672 O O     . PRO   B 1 234 ? 22.529  47.944 24.019 1 22.8   ? 215 PRO   B O     1 
ATOM   3673 C CB    . PRO   B 1 234 ? 21.896  50.663 24.599 1 15.62  ? 215 PRO   B CB    1 
ATOM   3674 C CG    . PRO   B 1 234 ? 22.943  51.203 23.705 1 18.89  ? 215 PRO   B CG    1 
ATOM   3675 C CD    . PRO   B 1 234 ? 24.28   51.056 24.372 1 14.22  ? 215 PRO   B CD    1 
ATOM   3676 N N     . LEU   B 1 235 ? 22.666  47.39  26.193 1 17.9   ? 216 LEU   B N     1 
ATOM   3677 C CA    . LEU   B 1 235 ? 22.652  45.951 25.937 1 16.85  ? 216 LEU   B CA    1 
ATOM   3678 C C     . LEU   B 1 235 ? 21.324  45.349 26.336 1 17.57  ? 216 LEU   B C     1 
ATOM   3679 O O     . LEU   B 1 235 ? 20.774  45.713 27.376 1 15.95  ? 216 LEU   B O     1 
ATOM   3680 C CB    . LEU   B 1 235 ? 23.776  45.236 26.73  1 17.21  ? 216 LEU   B CB    1 
ATOM   3681 C CG    . LEU   B 1 235 ? 25.229  45.386 26.296 1 22.04  ? 216 LEU   B CG    1 
ATOM   3682 C CD1   . LEU   B 1 235 ? 26.084  44.317 26.957 1 22.67  ? 216 LEU   B CD1   1 
ATOM   3683 C CD2   . LEU   B 1 235 ? 25.399  45.294 24.778 1 24.97  ? 216 LEU   B CD2   1 
ATOM   3684 N N     . GLY   B 1 236 ? 20.863  44.387 25.535 1 13.15  ? 217 GLY   B N     1 
ATOM   3685 C CA    . GLY   B 1 236 ? 19.663  43.602 25.8   1 12.47  ? 217 GLY   B CA    1 
ATOM   3686 C C     . GLY   B 1 236 ? 20.071  42.336 26.519 1 15.3   ? 217 GLY   B C     1 
ATOM   3687 O O     . GLY   B 1 236 ? 21.266  42.046 26.602 1 15.98  ? 217 GLY   B O     1 
ATOM   3688 N N     . ARG   B 1 237 ? 19.119  41.556 27.026 1 12.91  ? 218 ARG   B N     1 
ATOM   3689 C CA    . ARG   B 1 237 ? 19.452  40.34  27.786 1 13.37  ? 218 ARG   B CA    1 
ATOM   3690 C C     . ARG   B 1 237 ? 20.23   39.285 26.976 1 17.66  ? 218 ARG   B C     1 
ATOM   3691 O O     . ARG   B 1 237 ? 21.09   38.601 27.525 1 16.35  ? 218 ARG   B O     1 
ATOM   3692 C CB    . ARG   B 1 237 ? 18.209  39.715 28.469 1 14.86  ? 218 ARG   B CB    1 
ATOM   3693 C CG    . ARG   B 1 237 ? 17.25   38.951 27.558 1 32.47  ? 218 ARG   B CG    1 
ATOM   3694 C CD    . ARG   B 1 237 ? 16.318  38.023 28.33  1 48.77  ? 218 ARG   B CD    1 
ATOM   3695 N NE    . ARG   B 1 237 ? 17.031  36.917 28.982 1 52.4   ? 218 ARG   B NE    1 
ATOM   3696 C CZ    . ARG   B 1 237 ? 16.488  36.08  29.863 1 65.5   ? 218 ARG   B CZ    1 
ATOM   3697 N NH1   . ARG   B 1 237 ? 15.211  36.203 30.209 1 61.3   ? 218 ARG   B NH1   1 
ATOM   3698 N NH2   . ARG   B 1 237 ? 17.216  35.113 30.404 1 48.1   ? 218 ARG   B NH2   1 
ATOM   3699 N N     . GLU   B 1 238 ? 19.942  39.174 25.684 1 15.72  ? 219 GLU   B N     1 
ATOM   3700 C CA    . GLU   B 1 238 ? 20.591  38.188 24.812 1 15.26  ? 219 GLU   B CA    1 
ATOM   3701 C C     . GLU   B 1 238 ? 22.081  38.493 24.631 1 16.8   ? 219 GLU   B C     1 
ATOM   3702 O O     . GLU   B 1 238 ? 22.889  37.57  24.727 1 16.21  ? 219 GLU   B O     1 
ATOM   3703 C CB    . GLU   B 1 238 ? 19.858  38.066 23.457 1 16.48  ? 219 GLU   B CB    1 
ATOM   3704 C CG    . GLU   B 1 238 ? 18.363  37.783 23.555 1 27.7   ? 219 GLU   B CG    1 
ATOM   3705 C CD    . GLU   B 1 238 ? 17.412  38.92  23.92  1 61.38  ? 219 GLU   B CD    1 
ATOM   3706 O OE1   . GLU   B 1 238 ? 17.798  40.11  23.814 1 41.91  ? 219 GLU   B OE1   1 
ATOM   3707 O OE2   . GLU   B 1 238 ? 16.264  38.607 24.315 1 64.98  ? 219 GLU   B OE2   1 
ATOM   3708 N N     . ALA   B 1 239 ? 22.454  39.776 24.447 1 12.56  ? 220 ALA   B N     1 
ATOM   3709 C CA    . ALA   B 1 239 ? 23.874  40.151 24.308 1 12.19  ? 220 ALA   B CA    1 
ATOM   3710 C C     . ALA   B 1 239 ? 24.634  39.983 25.631 1 15.2   ? 220 ALA   B C     1 
ATOM   3711 O O     . ALA   B 1 239 ? 25.791  39.568 25.592 1 12.56  ? 220 ALA   B O     1 
ATOM   3712 C CB    . ALA   B 1 239 ? 24.02   41.573 23.781 1 13.03  ? 220 ALA   B CB    1 
ATOM   3713 N N     . VAL   B 1 240 ? 23.989  40.292 26.797 1 12.49  ? 221 VAL   B N     1 
ATOM   3714 C CA    . VAL   B 1 240 ? 24.598  40.109 28.129 1 12.74  ? 221 VAL   B CA    1 
ATOM   3715 C C     . VAL   B 1 240 ? 24.922  38.62  28.375 1 15.7   ? 221 VAL   B C     1 
ATOM   3716 O O     . VAL   B 1 240 ? 26.067  38.274 28.672 1 14.69  ? 221 VAL   B O     1 
ATOM   3717 C CB    . VAL   B 1 240 ? 23.755  40.732 29.273 1 16.42  ? 221 VAL   B CB    1 
ATOM   3718 C CG1   . VAL   B 1 240 ? 24.354  40.389 30.641 1 15.79  ? 221 VAL   B CG1   1 
ATOM   3719 C CG2   . VAL   B 1 240 ? 23.648  42.245 29.099 1 15.96  ? 221 VAL   B CG2   1 
ATOM   3720 N N     . GLU   B 1 241 ? 23.922  37.761 28.243 1 12.64  ? 222 GLU   B N     1 
ATOM   3721 C CA    . GLU   B 1 241 ? 24.075  36.308 28.391 1 13.8   ? 222 GLU   B CA    1 
ATOM   3722 C C     . GLU   B 1 241 ? 25.171  35.785 27.455 1 17.53  ? 222 GLU   B C     1 
ATOM   3723 O O     . GLU   B 1 241 ? 26.055  35.078 27.92  1 16.85  ? 222 GLU   B O     1 
ATOM   3724 C CB    . GLU   B 1 241 ? 22.751  35.59  28.051 1 15.85  ? 222 GLU   B CB    1 
ATOM   3725 C CG    . GLU   B 1 241 ? 21.709  35.659 29.14  1 31.98  ? 222 GLU   B CG    1 
ATOM   3726 C CD    . GLU   B 1 241 ? 20.376  35.035 28.778 1 58.16  ? 222 GLU   B CD    1 
ATOM   3727 O OE1   . GLU   B 1 241 ? 20.227  33.807 28.966 1 60.39  ? 222 GLU   B OE1   1 
ATOM   3728 O OE2   . GLU   B 1 241 ? 19.476  35.776 28.322 1 51.72  ? 222 GLU   B OE2   1 
ATOM   3729 N N     . ALA   B 1 242 ? 25.129  36.152 26.147 1 14.96  ? 223 ALA   B N     1 
ATOM   3730 C CA    . ALA   B 1 242 ? 26.133  35.693 25.186 1 15.22  ? 223 ALA   B CA    1 
ATOM   3731 C C     . ALA   B 1 242 ? 27.569  36.16  25.527 1 19.16  ? 223 ALA   B C     1 
ATOM   3732 O O     . ALA   B 1 242 ? 28.503  35.384 25.363 1 18.31  ? 223 ALA   B O     1 
ATOM   3733 C CB    . ALA   B 1 242 ? 25.755  36.108 23.776 1 15.75  ? 223 ALA   B CB    1 
ATOM   3734 N N     . ALA   B 1 243 ? 27.746  37.404 26.01  1 15.09  ? 224 ALA   B N     1 
ATOM   3735 C CA    . ALA   B 1 243 ? 29.071  37.93  26.366 1 14.52  ? 224 ALA   B CA    1 
ATOM   3736 C C     . ALA   B 1 243 ? 29.652  37.202 27.586 1 17.18  ? 224 ALA   B C     1 
ATOM   3737 O O     . ALA   B 1 243 ? 30.866  36.976 27.647 1 15.88  ? 224 ALA   B O     1 
ATOM   3738 C CB    . ALA   B 1 243 ? 28.986  39.42  26.635 1 15.66  ? 224 ALA   B CB    1 
ATOM   3739 N N     . VAL   B 1 244 ? 28.779  36.806 28.539 1 13.5   ? 225 VAL   B N     1 
ATOM   3740 C CA    . VAL   B 1 244 ? 29.165  36.087 29.762 1 12.09  ? 225 VAL   B CA    1 
ATOM   3741 C C     . VAL   B 1 244 ? 29.676  34.674 29.376 1 15.78  ? 225 VAL   B C     1 
ATOM   3742 O O     . VAL   B 1 244 ? 30.733  34.254 29.857 1 15.09  ? 225 VAL   B O     1 
ATOM   3743 C CB    . VAL   B 1 244 ? 28.037  36.127 30.847 1 14.9   ? 225 VAL   B CB    1 
ATOM   3744 C CG1   . VAL   B 1 244 ? 28.29   35.138 31.989 1 14.55  ? 225 VAL   B CG1   1 
ATOM   3745 C CG2   . VAL   B 1 244 ? 27.888  37.545 31.421 1 14.09  ? 225 VAL   B CG2   1 
ATOM   3746 N N     . LYS   B 1 245 ? 28.964  33.977 28.467 1 11.96  ? 226 LYS   B N     1 
ATOM   3747 C CA    . LYS   B 1 245 ? 29.382  32.652 27.965 1 12.1   ? 226 LYS   B CA    1 
ATOM   3748 C C     . LYS   B 1 245 ? 30.702  32.771 27.171 1 17.3   ? 226 LYS   B C     1 
ATOM   3749 O O     . LYS   B 1 245 ? 31.628  31.998 27.415 1 18.19  ? 226 LYS   B O     1 
ATOM   3750 C CB    . LYS   B 1 245 ? 28.277  32.002 27.126 1 13.66  ? 226 LYS   B CB    1 
ATOM   3751 C CG    . LYS   B 1 245 ? 27.078  31.553 27.956 1 18.25  ? 226 LYS   B CG    1 
ATOM   3752 C CD    . LYS   B 1 245 ? 25.885  31.298 27.065 1 27.18  ? 226 LYS   B CD    1 
ATOM   3753 C CE    . LYS   B 1 245 ? 24.795  30.544 27.783 1 40.66  ? 226 LYS   B CE    1 
ATOM   3754 N NZ    . LYS   B 1 245 ? 23.549  30.534 26.985 1 58.76  ? 226 LYS   B NZ    1 
ATOM   3755 N N     . GLU   B 1 246 ? 30.813  33.79  26.299 1 13.2   ? 227 GLU   B N     1 
ATOM   3756 C CA    . GLU   B 1 246 ? 32.011  34.082 25.495 1 13.26  ? 227 GLU   B CA    1 
ATOM   3757 C C     . GLU   B 1 246 ? 33.258  34.343 26.37  1 18.24  ? 227 GLU   B C     1 
ATOM   3758 O O     . GLU   B 1 246 ? 34.344  33.88  26.035 1 17.46  ? 227 GLU   B O     1 
ATOM   3759 C CB    . GLU   B 1 246 ? 31.734  35.271 24.571 1 14.42  ? 227 GLU   B CB    1 
ATOM   3760 C CG    . GLU   B 1 246 ? 32.821  35.565 23.559 1 19.29  ? 227 GLU   B CG    1 
ATOM   3761 C CD    . GLU   B 1 246 ? 32.534  36.762 22.673 1 29.5   ? 227 GLU   B CD    1 
ATOM   3762 O OE1   . GLU   B 1 246 ? 31.384  37.259 22.672 1 29.68  ? 227 GLU   B OE1   1 
ATOM   3763 O OE2   . GLU   B 1 246 ? 33.47   37.212 21.98  1 21.08  ? 227 GLU   B OE2   1 
ATOM   3764 N N     . ALA   B 1 247 ? 33.072  35.01  27.521 1 15.45  ? 228 ALA   B N     1 
ATOM   3765 C CA    . ALA   B 1 247 ? 34.115  35.339 28.49  1 15.49  ? 228 ALA   B CA    1 
ATOM   3766 C C     . ALA   B 1 247 ? 34.544  34.157 29.378 1 19.87  ? 228 ALA   B C     1 
ATOM   3767 O O     . ALA   B 1 247 ? 35.439  34.32  30.203 1 18.62  ? 228 ALA   B O     1 
ATOM   3768 C CB    . ALA   B 1 247 ? 33.666  36.514 29.351 1 16.04  ? 228 ALA   B CB    1 
ATOM   3769 N N     . GLY   B 1 248 ? 33.908  32.995 29.215 1 18.22  ? 229 GLY   B N     1 
ATOM   3770 C CA    . GLY   B 1 248 ? 34.285  31.783 29.949 1 18.93  ? 229 GLY   B CA    1 
ATOM   3771 C C     . GLY   B 1 248 ? 33.57   31.49  31.251 1 22.31  ? 229 GLY   B C     1 
ATOM   3772 O O     . GLY   B 1 248 ? 34.199  31.02  32.205 1 23.05  ? 229 GLY   B O     1 
ATOM   3773 N N     . TYR   B 1 249 ? 32.248  31.741 31.296 1 16.33  ? 230 TYR   B N     1 
ATOM   3774 C CA    . TYR   B 1 249 ? 31.425  31.469 32.465 1 15.14  ? 230 TYR   B CA    1 
ATOM   3775 C C     . TYR   B 1 249 ? 30.229  30.627 32.096 1 20.23  ? 230 TYR   B C     1 
ATOM   3776 O O     . TYR   B 1 249 ? 29.738  30.7   30.973 1 19.59  ? 230 TYR   B O     1 
ATOM   3777 C CB    . TYR   B 1 249 ? 30.88   32.776 33.101 1 14.48  ? 230 TYR   B CB    1 
ATOM   3778 C CG    . TYR   B 1 249 ? 31.923  33.774 33.56  1 14.02  ? 230 TYR   B CG    1 
ATOM   3779 C CD1   . TYR   B 1 249 ? 32.401  34.756 32.698 1 15.36  ? 230 TYR   B CD1   1 
ATOM   3780 C CD2   . TYR   B 1 249 ? 32.372  33.786 34.879 1 13.41  ? 230 TYR   B CD2   1 
ATOM   3781 C CE1   . TYR   B 1 249 ? 33.322  35.71  33.126 1 14.36  ? 230 TYR   B CE1   1 
ATOM   3782 C CE2   . TYR   B 1 249 ? 33.304  34.732 35.316 1 14.2   ? 230 TYR   B CE2   1 
ATOM   3783 C CZ    . TYR   B 1 249 ? 33.782  35.684 34.428 1 15.51  ? 230 TYR   B CZ    1 
ATOM   3784 O OH    . TYR   B 1 249 ? 34.673  36.642 34.821 1 17.52  ? 230 TYR   B OH    1 
ATOM   3785 N N     . THR   B 1 250 ? 29.689  29.92  33.074 1 18.41  ? 231 THR   B N     1 
ATOM   3786 C CA    . THR   B 1 250 ? 28.436  29.196 32.887 1 18.64  ? 231 THR   B CA    1 
ATOM   3787 C C     . THR   B 1 250 ? 27.401  29.984 33.65  1 22.17  ? 231 THR   B C     1 
ATOM   3788 O O     . THR   B 1 250 ? 27.664  30.408 34.773 1 22.34  ? 231 THR   B O     1 
ATOM   3789 C CB    . THR   B 1 250 ? 28.517  27.726 33.369 1 22.93  ? 231 THR   B CB    1 
ATOM   3790 O OG1   . THR   B 1 250 ? 28.85   27.689 34.758 1 22.67  ? 231 THR   B OG1   1 
ATOM   3791 C CG2   . THR   B 1 250 ? 29.513  26.912 32.569 1 19.46  ? 231 THR   B CG2   1 
ATOM   3792 N N     . ILE   B 1 251 ? 26.23   30.176 33.057 1 17.93  ? 232 ILE   B N     1 
ATOM   3793 C CA    . ILE   B 1 251 ? 25.131  30.908 33.69  1 17.42  ? 232 ILE   B CA    1 
ATOM   3794 C C     . ILE   B 1 251 ? 24.422  29.986 34.672 1 18.9   ? 232 ILE   B C     1 
ATOM   3795 O O     . ILE   B 1 251 ? 24.091  28.859 34.311 1 17.66  ? 232 ILE   B O     1 
ATOM   3796 C CB    . ILE   B 1 251 ? 24.198  31.545 32.611 1 20.95  ? 232 ILE   B CB    1 
ATOM   3797 C CG1   . ILE   B 1 251 ? 24.993  32.593 31.785 1 21.91  ? 232 ILE   B CG1   1 
ATOM   3798 C CG2   . ILE   B 1 251 ? 22.908  32.164 33.232 1 21.92  ? 232 ILE   B CG2   1 
ATOM   3799 C CD1   . ILE   B 1 251 ? 24.347  33.064 30.492 1 32.15  ? 232 ILE   B CD1   1 
ATOM   3800 N N     . GLU   B 1 252 ? 24.271  30.434 35.928 1 14.69  ? 233 GLU   B N     1 
ATOM   3801 C CA    . GLU   B 1 252 ? 23.57   29.706 36.997 1 14.81  ? 233 GLU   B CA    1 
ATOM   3802 C C     . GLU   B 1 252 ? 22.138  30.188 36.951 1 19.79  ? 233 GLU   B C     1 
ATOM   3803 O O     . GLU   B 1 252 ? 21.216  29.384 36.813 1 18.8   ? 233 GLU   B O     1 
ATOM   3804 C CB    . GLU   B 1 252 ? 24.194  29.969 38.38  1 16.07  ? 233 GLU   B CB    1 
ATOM   3805 C CG    . GLU   B 1 252 ? 25.562  29.338 38.575 1 29.72  ? 233 GLU   B CG    1 
ATOM   3806 C CD    . GLU   B 1 252 ? 25.528  27.892 39.036 1 54.18  ? 233 GLU   B CD    1 
ATOM   3807 O OE1   . GLU   B 1 252 ? 26.019  27.027 38.276 1 46.98  ? 233 GLU   B OE1   1 
ATOM   3808 O OE2   . GLU   B 1 252 ? 25.006  27.619 40.143 1 47.86  ? 233 GLU   B OE2   1 
ATOM   3809 N N     . TRP   B 1 253 ? 21.947  31.513 37.019 1 18.66  ? 234 TRP   B N     1 
ATOM   3810 C CA    . TRP   B 1 253 ? 20.621  32.071 36.859 1 20.54  ? 234 TRP   B CA    1 
ATOM   3811 C C     . TRP   B 1 253 ? 20.637  33.457 36.282 1 16.73  ? 234 TRP   B C     1 
ATOM   3812 O O     . TRP   B 1 253 ? 21.654  34.153 36.303 1 13.12  ? 234 TRP   B O     1 
ATOM   3813 C CB    . TRP   B 1 253 ? 19.697  31.981 38.076 1 22.1   ? 234 TRP   B CB    1 
ATOM   3814 C CG    . TRP   B 1 253 ? 20.141  32.464 39.409 1 24.82  ? 234 TRP   B CG    1 
ATOM   3815 C CD1   . TRP   B 1 253 ? 19.976  33.724 39.898 1 28.6   ? 234 TRP   B CD1   1 
ATOM   3816 C CD2   . TRP   B 1 253 ? 20.375  31.626 40.547 1 25.33  ? 234 TRP   B CD2   1 
ATOM   3817 N NE1   . TRP   B 1 253 ? 20.213  33.741 41.259 1 28.85  ? 234 TRP   B NE1   1 
ATOM   3818 C CE2   . TRP   B 1 253 ? 20.467  32.465 41.678 1 30.1   ? 234 TRP   B CE2   1 
ATOM   3819 C CE3   . TRP   B 1 253 ? 20.545  30.242 40.715 1 26.92  ? 234 TRP   B CE3   1 
ATOM   3820 C CZ2   . TRP   B 1 253 ? 20.765  31.973 42.951 1 30.18  ? 234 TRP   B CZ2   1 
ATOM   3821 C CZ3   . TRP   B 1 253 ? 20.851  29.759 41.968 1 29.34  ? 234 TRP   B CZ3   1 
ATOM   3822 C CH2   . TRP   B 1 253 ? 20.949  30.618 43.074 1 30.41  ? 234 TRP   B CH2   1 
ATOM   3823 N N     . PHE   B 1 254 ? 19.508  33.799 35.666 1 11.83  ? 235 PHE   B N     1 
ATOM   3824 C CA    . PHE   B 1 254 ? 19.345  35.061 34.967 1 11.73  ? 235 PHE   B CA    1 
ATOM   3825 C C     . PHE   B 1 254 ? 17.938  35.591 35.174 1 14.29  ? 235 PHE   B C     1 
ATOM   3826 O O     . PHE   B 1 254 ? 16.981  34.928 34.807 1 13.48  ? 235 PHE   B O     1 
ATOM   3827 C CB    . PHE   B 1 254 ? 19.688  34.908 33.464 1 12.79  ? 235 PHE   B CB    1 
ATOM   3828 C CG    . PHE   B 1 254 ? 20.002  36.23  32.789 1 14.22  ? 235 PHE   B CG    1 
ATOM   3829 C CD1   . PHE   B 1 254 ? 18.987  37.121 32.459 1 16.8   ? 235 PHE   B CD1   1 
ATOM   3830 C CD2   . PHE   B 1 254 ? 21.314  36.608 32.543 1 17.22  ? 235 PHE   B CD2   1 
ATOM   3831 C CE1   . PHE   B 1 254 ? 19.284  38.374 31.903 1 17.41  ? 235 PHE   B CE1   1 
ATOM   3832 C CE2   . PHE   B 1 254 ? 21.61   37.853 31.962 1 19.46  ? 235 PHE   B CE2   1 
ATOM   3833 C CZ    . PHE   B 1 254 ? 20.593  38.723 31.642 1 15.96  ? 235 PHE   B CZ    1 
ATOM   3834 N N     . GLU   B 1 255 ? 17.819  36.811 35.721 1 11.73  ? 236 GLU   B N     1 
ATOM   3835 C CA    . GLU   B 1 255 ? 16.532  37.448 35.954 1 11.51  ? 236 GLU   B CA    1 
ATOM   3836 C C     . GLU   B 1 255 ? 16.41   38.792 35.269 1 16.89  ? 236 GLU   B C     1 
ATOM   3837 O O     . GLU   B 1 255 ? 17.311  39.622 35.363 1 16     ? 236 GLU   B O     1 
ATOM   3838 C CB    . GLU   B 1 255 ? 16.304  37.629 37.448 1 13.11  ? 236 GLU   B CB    1 
ATOM   3839 C CG    . GLU   B 1 255 ? 14.885  38.03  37.809 1 21.45  ? 236 GLU   B CG    1 
ATOM   3840 C CD    . GLU   B 1 255 ? 14.619  38.163 39.292 1 36.47  ? 236 GLU   B CD    1 
ATOM   3841 O OE1   . GLU   B 1 255 ? 15.137  37.338 40.079 1 37.93  ? 236 GLU   B OE1   1 
ATOM   3842 O OE2   . GLU   B 1 255 ? 13.851  39.075 39.663 1 31.65  ? 236 GLU   B OE2   1 
ATOM   3843 N N     . VAL   B 1 256 ? 15.259  39.03  34.642 1 15.13  ? 237 VAL   B N     1 
ATOM   3844 C CA    . VAL   B 1 256 ? 14.923  40.298 33.999 1 15.68  ? 237 VAL   B CA    1 
ATOM   3845 C C     . VAL   B 1 256 ? 13.787  40.914 34.836 1 18.73  ? 237 VAL   B C     1 
ATOM   3846 O O     . VAL   B 1 256 ? 12.822  40.218 35.155 1 14.69  ? 237 VAL   B O     1 
ATOM   3847 C CB    . VAL   B 1 256 ? 14.498  40.071 32.528 1 21.22  ? 237 VAL   B CB    1 
ATOM   3848 C CG1   . VAL   B 1 256 ? 14.069  41.376 31.864 1 21.72  ? 237 VAL   B CG1   1 
ATOM   3849 C CG2   . VAL   B 1 256 ? 15.617  39.405 31.737 1 21.57  ? 237 VAL   B CG2   1 
ATOM   3850 N N     . ILE   B 1 257 ? 13.945  42.194 35.241 1 17.95  ? 238 ILE   B N     1 
ATOM   3851 C CA    . ILE   B 1 257 ? 12.942  42.952 35.995 1 19.18  ? 238 ILE   B CA    1 
ATOM   3852 C C     . ILE   B 1 257 ? 12.454  44.079 35.074 1 22.08  ? 238 ILE   B C     1 
ATOM   3853 O O     . ILE   B 1 257 ? 13.265  44.711 34.388 1 20.03  ? 238 ILE   B O     1 
ATOM   3854 C CB    . ILE   B 1 257 ? 13.39   43.381 37.436 1 23.74  ? 238 ILE   B CB    1 
ATOM   3855 C CG1   . ILE   B 1 257 ? 13.944  44.814 37.494 1 25.49  ? 238 ILE   B CG1   1 
ATOM   3856 C CG2   . ILE   B 1 257 ? 14.386  42.374 38.058 1 25.06  ? 238 ILE   B CG2   1 
ATOM   3857 C CD1   . ILE   B 1 257 ? 13.574  45.56  38.733 1 37.79  ? 238 ILE   B CD1   1 
ATOM   3858 N N     . SER   B 1 258 ? 11.133  44.247 34.968 1 19.69  ? 239 SER   B N     1 
ATOM   3859 C CA    . SER   B 1 258 ? 10.515  45.213 34.05  1 19.56  ? 239 SER   B CA    1 
ATOM   3860 C C     . SER   B 1 258 ? 10.699  46.695 34.455 1 23.03  ? 239 SER   B C     1 
ATOM   3861 O O     . SER   B 1 258 ? 10.702  47.576 33.583 1 22.22  ? 239 SER   B O     1 
ATOM   3862 C CB    . SER   B 1 258 ? 9.038   44.892 33.875 1 23.73  ? 239 SER   B CB    1 
ATOM   3863 O OG    . SER   B 1 258 ? 8.368   45.091 35.109 1 34.64  ? 239 SER   B OG    1 
ATOM   3864 N N     . GLN   B 1 259 ? 10.843  46.95  35.772 1 18.58  ? 240 GLN   B N     1 
ATOM   3865 C CA    . GLN   B 1 259 ? 11.03   48.279 36.374 1 18.24  ? 240 GLN   B CA    1 
ATOM   3866 C C     . GLN   B 1 259 ? 12.241  49.036 35.805 1 21.48  ? 240 GLN   B C     1 
ATOM   3867 O O     . GLN   B 1 259 ? 13.357  48.507 35.77  1 19.3   ? 240 GLN   B O     1 
ATOM   3868 C CB    . GLN   B 1 259 ? 11.11   48.158 37.901 1 19.69  ? 240 GLN   B CB    1 
ATOM   3869 C CG    . GLN   B 1 259 ? 11.243  49.476 38.672 1 32.56  ? 240 GLN   B CG    1 
ATOM   3870 C CD    . GLN   B 1 259 ? 9.981   50.287 38.722 1 49.47  ? 240 GLN   B CD    1 
ATOM   3871 O OE1   . GLN   B 1 259 ? 8.935   49.837 39.202 1 42.63  ? 240 GLN   B OE1   1 
ATOM   3872 N NE2   . GLN   B 1 259 ? 10.071  51.522 38.256 1 40.7   ? 240 GLN   B NE2   1 
ATOM   3873 N N     . SER   B 1 260 ? 11.982  50.275 35.342 1 17.29  ? 241 SER   B N     1 
ATOM   3874 C CA    . SER   B 1 260 ? 12.941  51.197 34.752 1 17.23  ? 241 SER   B CA    1 
ATOM   3875 C C     . SER   B 1 260 ? 13.122  52.413 35.67  1 19.59  ? 241 SER   B C     1 
ATOM   3876 O O     . SER   B 1 260 ? 12.316  52.608 36.58  1 18.78  ? 241 SER   B O     1 
ATOM   3877 C CB    . SER   B 1 260 ? 12.454  51.645 33.377 1 19.96  ? 241 SER   B CB    1 
ATOM   3878 O OG    . SER   B 1 260 ? 12.313  50.53  32.508 1 25.51  ? 241 SER   B OG    1 
ATOM   3879 N N     . TYR   B 1 261 ? 14.206  53.197 35.471 1 14.58  ? 242 TYR   B N     1 
ATOM   3880 C CA    . TYR   B 1 261 ? 14.448  54.426 36.242 1 13.54  ? 242 TYR   B CA    1 
ATOM   3881 C C     . TYR   B 1 261 ? 13.495  55.522 35.755 1 17.99  ? 242 TYR   B C     1 
ATOM   3882 O O     . TYR   B 1 261 ? 12.837  55.34  34.724 1 17.41  ? 242 TYR   B O     1 
ATOM   3883 C CB    . TYR   B 1 261 ? 15.918  54.887 36.081 1 13.54  ? 242 TYR   B CB    1 
ATOM   3884 C CG    . TYR   B 1 261 ? 16.902  54     36.815 1 14.01  ? 242 TYR   B CG    1 
ATOM   3885 C CD1   . TYR   B 1 261 ? 17.202  54.221 38.157 1 16.18  ? 242 TYR   B CD1   1 
ATOM   3886 C CD2   . TYR   B 1 261 ? 17.487  52.903 36.185 1 13.31  ? 242 TYR   B CD2   1 
ATOM   3887 C CE1   . TYR   B 1 261 ? 18.084  53.388 38.847 1 16.13  ? 242 TYR   B CE1   1 
ATOM   3888 C CE2   . TYR   B 1 261 ? 18.361  52.058 36.867 1 13.21  ? 242 TYR   B CE2   1 
ATOM   3889 C CZ    . TYR   B 1 261 ? 18.664  52.312 38.194 1 17.65  ? 242 TYR   B CZ    1 
ATOM   3890 O OH    . TYR   B 1 261 ? 19.537  51.493 38.86  1 19.39  ? 242 TYR   B OH    1 
ATOM   3891 N N     . SER   B 1 262 ? 13.436  56.669 36.464 1 15.81  ? 243 SER   B N     1 
ATOM   3892 C CA    . SER   B 1 262 ? 12.604  57.793 36.039 1 16.29  ? 243 SER   B CA    1 
ATOM   3893 C C     . SER   B 1 262 ? 13.142  58.265 34.667 1 21.99  ? 243 SER   B C     1 
ATOM   3894 O O     . SER   B 1 262 ? 14.357  58.224 34.45  1 20.59  ? 243 SER   B O     1 
ATOM   3895 C CB    . SER   B 1 262 ? 12.666  58.913 37.068 1 21.35  ? 243 SER   B CB    1 
ATOM   3896 O OG    . SER   B 1 262 ? 12.261  58.485 38.361 1 26.77  ? 243 SER   B OG    1 
ATOM   3897 N N     . SER   B 1 263 ? 12.251  58.65  33.725 1 19.05  ? 244 SER   B N     1 
ATOM   3898 C CA    . SER   B 1 263 ? 12.657  59.039 32.362 1 20.26  ? 244 SER   B CA    1 
ATOM   3899 C C     . SER   B 1 263 ? 13.605  60.256 32.313 1 25.28  ? 244 SER   B C     1 
ATOM   3900 O O     . SER   B 1 263 ? 14.334  60.428 31.335 1 23.29  ? 244 SER   B O     1 
ATOM   3901 C CB    . SER   B 1 263 ? 11.434  59.246 31.46  1 24.34  ? 244 SER   B CB    1 
ATOM   3902 O OG    . SER   B 1 263 ? 10.613  60.292 31.953 1 33.58  ? 244 SER   B OG    1 
ATOM   3903 N N     . THR   B 1 264 ? 13.629  61.048 33.392 1 25.21  ? 245 THR   B N     1 
ATOM   3904 C CA    . THR   B 1 264 ? 14.503  62.211 33.561 1 26.63  ? 245 THR   B CA    1 
ATOM   3905 C C     . THR   B 1 264 ? 15.885  61.778 34.103 1 31.53  ? 245 THR   B C     1 
ATOM   3906 O O     . THR   B 1 264 ? 16.801  62.607 34.149 1 32.72  ? 245 THR   B O     1 
ATOM   3907 C CB    . THR   B 1 264 ? 13.841  63.227 34.512 1 37.73  ? 245 THR   B CB    1 
ATOM   3908 O OG1   . THR   B 1 264 ? 13.574  62.594 35.771 1 38.03  ? 245 THR   B OG1   1 
ATOM   3909 C CG2   . THR   B 1 264 ? 12.566  63.831 33.93  1 39.09  ? 245 THR   B CG2   1 
ATOM   3910 N N     . MET   B 1 265 ? 16.025  60.489 34.524 1 26.43  ? 246 MET   B N     1 
ATOM   3911 C CA    . MET   B 1 265 ? 17.264  59.922 35.093 1 25.28  ? 246 MET   B CA    1 
ATOM   3912 C C     . MET   B 1 265 ? 18.019  59.015 34.117 1 23.38  ? 246 MET   B C     1 
ATOM   3913 O O     . MET   B 1 265 ? 19.238  59.076 34.088 1 20.51  ? 246 MET   B O     1 
ATOM   3914 C CB    . MET   B 1 265 ? 16.981  59.136 36.381 1 28.7   ? 246 MET   B CB    1 
ATOM   3915 C CG    . MET   B 1 265 ? 16.107  59.874 37.383 1 33.69  ? 246 MET   B CG    1 
ATOM   3916 S SD    . MET   B 1 265 ? 16.974  61.112 38.34  1 39.29  ? 246 MET   B SD    1 
ATOM   3917 C CE    . MET   B 1 265 ? 17.985  60.091 39.341 1 35.85  ? 246 MET   B CE    1 
ATOM   3918 N N     . ALA   B 1 266 ? 17.31   58.132 33.367 1 18.37  ? 247 ALA   B N     1 
ATOM   3919 C CA    . ALA   B 1 266 ? 17.905  57.212 32.365 1 17.54  ? 247 ALA   B CA    1 
ATOM   3920 C C     . ALA   B 1 266 ? 16.837  56.75  31.384 1 22.61  ? 247 ALA   B C     1 
ATOM   3921 O O     . ALA   B 1 266 ? 15.657  56.977 31.632 1 24.7   ? 247 ALA   B O     1 
ATOM   3922 C CB    . ALA   B 1 266 ? 18.558  56.006 33.045 1 17.86  ? 247 ALA   B CB    1 
ATOM   3923 N N     . ASN   B 1 267 ? 17.237  56.099 30.28  1 17.69  ? 248 ASN   B N     1 
ATOM   3924 C CA    . ASN   B 1 267 ? 16.304  55.622 29.261 1 17.22  ? 248 ASN   B CA    1 
ATOM   3925 C C     . ASN   B 1 267 ? 16.306  54.079 29.17  1 19.89  ? 248 ASN   B C     1 
ATOM   3926 O O     . ASN   B 1 267 ? 16.113  53.522 28.089 1 19.22  ? 248 ASN   B O     1 
ATOM   3927 C CB    . ASN   B 1 267 ? 16.65   56.286 27.894 1 16.88  ? 248 ASN   B CB    1 
ATOM   3928 C CG    . ASN   B 1 267 ? 18.016  55.916 27.356 1 19.94  ? 248 ASN   B CG    1 
ATOM   3929 O OD1   . ASN   B 1 267 ? 18.888  55.415 28.076 1 11.17  ? 248 ASN   B OD1   1 
ATOM   3930 N ND2   . ASN   B 1 267 ? 18.217  56.108 26.061 1 16.6   ? 248 ASN   B ND2   1 
ATOM   3931 N N     . ASN   B 1 268 ? 16.542  53.395 30.292 1 16.46  ? 249 ASN   B N     1 
ATOM   3932 C CA    . ASN   B 1 268 ? 16.618  51.935 30.299 1 16.85  ? 249 ASN   B CA    1 
ATOM   3933 C C     . ASN   B 1 268 ? 15.27   51.221 30.122 1 22.32  ? 249 ASN   B C     1 
ATOM   3934 O O     . ASN   B 1 268 ? 14.218  51.812 30.382 1 23.39  ? 249 ASN   B O     1 
ATOM   3935 C CB    . ASN   B 1 268 ? 17.324  51.439 31.565 1 17     ? 249 ASN   B CB    1 
ATOM   3936 C CG    . ASN   B 1 268 ? 16.515  51.574 32.814 1 22.15  ? 249 ASN   B CG    1 
ATOM   3937 O OD1   . ASN   B 1 268 ? 16.019  52.654 33.148 1 17.61  ? 249 ASN   B OD1   1 
ATOM   3938 N ND2   . ASN   B 1 268 ? 16.36   50.472 33.518 1 10.49  ? 249 ASN   B ND2   1 
ATOM   3939 N N     . GLU   B 1 269 ? 15.321  49.936 29.713 1 16.87  ? 250 GLU   B N     1 
ATOM   3940 C CA    . GLU   B 1 269 ? 14.152  49.069 29.559 1 16.36  ? 250 GLU   B CA    1 
ATOM   3941 C C     . GLU   B 1 269 ? 14.337  47.853 30.491 1 18.25  ? 250 GLU   B C     1 
ATOM   3942 O O     . GLU   B 1 269 ? 14.628  46.737 30.057 1 15.74  ? 250 GLU   B O     1 
ATOM   3943 C CB    . GLU   B 1 269 ? 13.909  48.678 28.087 1 17.69  ? 250 GLU   B CB    1 
ATOM   3944 C CG    . GLU   B 1 269 ? 13.251  49.795 27.288 1 32.84  ? 250 GLU   B CG    1 
ATOM   3945 C CD    . GLU   B 1 269 ? 13.072  49.599 25.791 1 66.53  ? 250 GLU   B CD    1 
ATOM   3946 O OE1   . GLU   B 1 269 ? 13.567  48.586 25.242 1 68.45  ? 250 GLU   B OE1   1 
ATOM   3947 O OE2   . GLU   B 1 269 ? 12.44   50.478 25.16  1 61.04  ? 250 GLU   B OE2   1 
ATOM   3948 N N     . GLY   B 1 270 ? 14.224  48.126 31.782 1 13.97  ? 251 GLY   B N     1 
ATOM   3949 C CA    . GLY   B 1 270 ? 14.378  47.122 32.816 1 13.9   ? 251 GLY   B CA    1 
ATOM   3950 C C     . GLY   B 1 270 ? 15.783  46.959 33.353 1 15.29  ? 251 GLY   B C     1 
ATOM   3951 O O     . GLY   B 1 270 ? 16.674  47.748 33.044 1 13.1   ? 251 GLY   B O     1 
ATOM   3952 N N     . LEU   B 1 271 ? 15.973  45.935 34.195 1 12.29  ? 252 LEU   B N     1 
ATOM   3953 C CA    . LEU   B 1 271 ? 17.254  45.614 34.824 1 13.1   ? 252 LEU   B CA    1 
ATOM   3954 C C     . LEU   B 1 271 ? 17.409  44.117 34.848 1 17.66  ? 252 LEU   B C     1 
ATOM   3955 O O     . LEU   B 1 271 ? 16.417  43.403 34.918 1 18.04  ? 252 LEU   B O     1 
ATOM   3956 C CB    . LEU   B 1 271 ? 17.299  46.119 36.286 1 13.79  ? 252 LEU   B CB    1 
ATOM   3957 C CG    . LEU   B 1 271 ? 17.731  47.562 36.486 1 20.01  ? 252 LEU   B CG    1 
ATOM   3958 C CD1   . LEU   B 1 271 ? 16.535  48.435 36.841 1 21.22  ? 252 LEU   B CD1   1 
ATOM   3959 C CD2   . LEU   B 1 271 ? 18.836  47.664 37.512 1 21.26  ? 252 LEU   B CD2   1 
ATOM   3960 N N     . PHE   B 1 272 ? 18.651  43.633 34.81  1 13.04  ? 253 PHE   B N     1 
ATOM   3961 C CA    . PHE   B 1 272 ? 18.909  42.209 34.925 1 10.74  ? 253 PHE   B CA    1 
ATOM   3962 C C     . PHE   B 1 272 ? 19.732  41.976 36.178 1 15.37  ? 253 PHE   B C     1 
ATOM   3963 O O     . PHE   B 1 272 ? 20.42   42.878 36.689 1 13.46  ? 253 PHE   B O     1 
ATOM   3964 C CB    . PHE   B 1 272 ? 19.655  41.638 33.683 1 11.63  ? 253 PHE   B CB    1 
ATOM   3965 C CG    . PHE   B 1 272 ? 21.107  42.062 33.533 1 12.13  ? 253 PHE   B CG    1 
ATOM   3966 C CD1   . PHE   B 1 272 ? 22.131  41.33  34.128 1 13.15  ? 253 PHE   B CD1   1 
ATOM   3967 C CD2   . PHE   B 1 272 ? 21.451  43.165 32.759 1 12.89  ? 253 PHE   B CD2   1 
ATOM   3968 C CE1   . PHE   B 1 272 ? 23.469  41.722 33.987 1 12.72  ? 253 PHE   B CE1   1 
ATOM   3969 C CE2   . PHE   B 1 272 ? 22.793  43.568 32.636 1 14.22  ? 253 PHE   B CE2   1 
ATOM   3970 C CZ    . PHE   B 1 272 ? 23.789  42.844 33.25  1 11.76  ? 253 PHE   B CZ    1 
ATOM   3971 N N     . SER   B 1 273 ? 19.721  40.73  36.612 1 12.81  ? 254 SER   B N     1 
ATOM   3972 C CA    . SER   B 1 273 ? 20.52   40.249 37.704 1 13.59  ? 254 SER   B CA    1 
ATOM   3973 C C     . SER   B 1 273 ? 20.991  38.881 37.201 1 16.37  ? 254 SER   B C     1 
ATOM   3974 O O     . SER   B 1 273 ? 20.189  38.11  36.673 1 14.5   ? 254 SER   B O     1 
ATOM   3975 C CB    . SER   B 1 273 ? 19.656  40.136 38.961 1 17.03  ? 254 SER   B CB    1 
ATOM   3976 O OG    . SER   B 1 273 ? 20.287  39.445 40.022 1 25.08  ? 254 SER   B OG    1 
ATOM   3977 N N     . LEU   B 1 274 ? 22.291  38.619 37.277 1 13.06  ? 255 LEU   B N     1 
ATOM   3978 C CA    . LEU   B 1 274 ? 22.815  37.32  36.871 1 13.29  ? 255 LEU   B CA    1 
ATOM   3979 C C     . LEU   B 1 274 ? 23.801  36.771 37.855 1 15.04  ? 255 LEU   B C     1 
ATOM   3980 O O     . LEU   B 1 274 ? 24.546  37.531 38.459 1 12.75  ? 255 LEU   B O     1 
ATOM   3981 C CB    . LEU   B 1 274 ? 23.39   37.315 35.443 1 13.77  ? 255 LEU   B CB    1 
ATOM   3982 C CG    . LEU   B 1 274 ? 24.741  37.951 35.143 1 18.33  ? 255 LEU   B CG    1 
ATOM   3983 C CD1   . LEU   B 1 274 ? 25.897  36.991 35.41  1 17.65  ? 255 LEU   B CD1   1 
ATOM   3984 C CD2   . LEU   B 1 274 ? 24.816  38.362 33.677 1 22.04  ? 255 LEU   B CD2   1 
ATOM   3985 N N     . VAL   B 1 275 ? 23.835  35.449 37.965 1 13.91  ? 256 VAL   B N     1 
ATOM   3986 C CA    . VAL   B 1 275 ? 24.785  34.683 38.766 1 14.54  ? 256 VAL   B CA    1 
ATOM   3987 C C     . VAL   B 1 275 ? 25.426  33.68  37.786 1 18.57  ? 256 VAL   B C     1 
ATOM   3988 O O     . VAL   B 1 275 ? 24.72   32.89  37.165 1 18.43  ? 256 VAL   B O     1 
ATOM   3989 C CB    . VAL   B 1 275 ? 24.125  33.983 39.986 1 18.4   ? 256 VAL   B CB    1 
ATOM   3990 C CG1   . VAL   B 1 275 ? 25.139  33.147 40.765 1 18.33  ? 256 VAL   B CG1   1 
ATOM   3991 C CG2   . VAL   B 1 275 ? 23.467  34.999 40.906 1 18.14  ? 256 VAL   B CG2   1 
ATOM   3992 N N     . ALA   B 1 276 ? 26.743  33.776 37.592 1 14.18  ? 257 ALA   B N     1 
ATOM   3993 C CA    . ALA   B 1 276 ? 27.493  32.897 36.704 1 11.87  ? 257 ALA   B CA    1 
ATOM   3994 C C     . ALA   B 1 276 ? 28.649  32.262 37.486 1 16.43  ? 257 ALA   B C     1 
ATOM   3995 O O     . ALA   B 1 276 ? 29.008  32.748 38.559 1 15.27  ? 257 ALA   B O     1 
ATOM   3996 C CB    . ALA   B 1 276 ? 28.032  33.697 35.516 1 12.35  ? 257 ALA   B CB    1 
ATOM   3997 N N     . ARG   B 1 277 ? 29.21   31.173 36.966 1 16.05  ? 258 ARG   B N     1 
ATOM   3998 C CA    . ARG   B 1 277 ? 30.383  30.527 37.564 1 17.34  ? 258 ARG   B CA    1 
ATOM   3999 C C     . ARG   B 1 277 ? 31.5    30.486 36.56  1 19.56  ? 258 ARG   B C     1 
ATOM   4000 O O     . ARG   B 1 277 ? 31.258  30.153 35.404 1 18.16  ? 258 ARG   B O     1 
ATOM   4001 C CB    . ARG   B 1 277 ? 30.075  29.111 38.064 1 18.54  ? 258 ARG   B CB    1 
ATOM   4002 C CG    . ARG   B 1 277 ? 29.603  29.102 39.488 1 30.73  ? 258 ARG   B CG    1 
ATOM   4003 C CD    . ARG   B 1 277 ? 29.244  27.717 39.959 1 42.6   ? 258 ARG   B CD    1 
ATOM   4004 N NE    . ARG   B 1 277 ? 30.414  26.991 40.448 1 50.68  ? 258 ARG   B NE    1 
ATOM   4005 C CZ    . ARG   B 1 277 ? 30.371  26.052 41.387 1 66.19  ? 258 ARG   B CZ    1 
ATOM   4006 N NH1   . ARG   B 1 277 ? 29.217  25.727 41.96  1 48.98  ? 258 ARG   B NH1   1 
ATOM   4007 N NH2   . ARG   B 1 277 ? 31.481  25.435 41.768 1 58.31  ? 258 ARG   B NH2   1 
ATOM   4008 N N     . LYS   B 1 278 ? 32.728  30.829 36.99  1 16.69  ? 259 LYS   B N     1 
ATOM   4009 C CA    . LYS   B 1 278 ? 33.909  30.798 36.136 1 16.6   ? 259 LYS   B CA    1 
ATOM   4010 C C     . LYS   B 1 278 ? 34.327  29.333 35.912 1 25.37  ? 259 LYS   B C     1 
ATOM   4011 O O     . LYS   B 1 278 ? 34.308  28.549 36.862 1 25.14  ? 259 LYS   B O     1 
ATOM   4012 C CB    . LYS   B 1 278 ? 35.053  31.582 36.808 1 17.74  ? 259 LYS   B CB    1 
ATOM   4013 C CG    . LYS   B 1 278 ? 36.246  31.863 35.903 1 18.05  ? 259 LYS   B CG    1 
ATOM   4014 C CD    . LYS   B 1 278 ? 37.506  31.997 36.73  1 18.2   ? 259 LYS   B CD    1 
ATOM   4015 C CE    . LYS   B 1 278 ? 38.684  32.37  35.902 1 20.01  ? 259 LYS   B CE    1 
ATOM   4016 N NZ    . LYS   B 1 278 ? 39.83   32.751 36.762 1 15.24  ? 259 LYS   B NZ    1 
ATOM   4017 N N     . LEU   B 1 279 ? 34.707  28.975 34.671 1 24.47  ? 260 LEU   B N     1 
ATOM   4018 C CA    . LEU   B 1 279 ? 35.186  27.62  34.334 1 26.9   ? 260 LEU   B CA    1 
ATOM   4019 C C     . LEU   B 1 279 ? 36.618  27.376 34.874 1 37.14  ? 260 LEU   B C     1 
ATOM   4020 O O     . LEU   B 1 279 ? 37.322  28.342 35.195 1 38.8   ? 260 LEU   B O     1 
ATOM   4021 C CB    . LEU   B 1 279 ? 35.16   27.403 32.809 1 26.74  ? 260 LEU   B CB    1 
ATOM   4022 C CG    . LEU   B 1 279 ? 33.779  27.352 32.133 1 32.57  ? 260 LEU   B CG    1 
ATOM   4023 C CD1   . LEU   B 1 279 ? 33.91   27.497 30.619 1 33.36  ? 260 LEU   B CD1   1 
ATOM   4024 C CD2   . LEU   B 1 279 ? 33.036  26.066 32.478 1 35     ? 260 LEU   B CD2   1 
ATOM   4025 N N     . SER   B 1 280 ? 37.057  26.09  34.951 1 35.74  ? 261 SER   B N     1 
ATOM   4026 C CA    . SER   B 1 280 ? 38.41   25.711 35.414 1 71.75  ? 261 SER   B CA    1 
ATOM   4027 C C     . SER   B 1 280 ? 39.557  25.923 34.383 1 90.73  ? 261 SER   B C     1 
ATOM   4028 O O     . SER   B 1 280 ? 39.678  25.242 33.352 1 36.61  ? 261 SER   B O     1 
ATOM   4029 C CB    . SER   B 1 280 ? 38.428  24.297 35.989 1 75.14  ? 261 SER   B CB    1 
ATOM   4030 O OG    . SER   B 1 280 ? 38.229  24.311 37.393 1 82.94  ? 261 SER   B OG    1 
HETATM 4031 N N     . SAH   C 2 .   ? 2.381   21.37  42.186 1 15.1   ? 301 SAH   A N     1 
HETATM 4032 C CA    . SAH   C 2 .   ? 3.032   20.077 42.462 1 16.45  ? 301 SAH   A CA    1 
HETATM 4033 C CB    . SAH   C 2 .   ? 2.69    18.922 41.448 1 18.27  ? 301 SAH   A CB    1 
HETATM 4034 C CG    . SAH   C 2 .   ? 3.166   19.21  40.028 1 16.59  ? 301 SAH   A CG    1 
HETATM 4035 S SD    . SAH   C 2 .   ? 2.986   17.641 39.138 1 14.36  ? 301 SAH   A SD    1 
HETATM 4036 C C     . SAH   C 2 .   ? 4.561   20.391 42.519 1 16.74  ? 301 SAH   A C     1 
HETATM 4037 O O     . SAH   C 2 .   ? 5.019   21.518 42.459 1 15.09  ? 301 SAH   A O     1 
HETATM 4038 O OXT   . SAH   C 2 .   ? 5.289   19.308 42.625 1 13.88  ? 301 SAH   A OXT   1 
HETATM 4039 C "C5'" . SAH   C 2 .   ? 1.679   17.982 37.926 1 15.96  ? 301 SAH   A "C5'" 1 
HETATM 4040 C "C4'" . SAH   C 2 .   ? 0.3     18.056 38.552 1 15.52  ? 301 SAH   A "C4'" 1 
HETATM 4041 O "O4'" . SAH   C 2 .   ? -0.653  18.565 37.591 1 17.89  ? 301 SAH   A "O4'" 1 
HETATM 4042 C "C3'" . SAH   C 2 .   ? -0.275  16.736 39.08  1 13.91  ? 301 SAH   A "C3'" 1 
HETATM 4043 O "O3'" . SAH   C 2 .   ? -0.666  16.871 40.442 1 15.16  ? 301 SAH   A "O3'" 1 
HETATM 4044 C "C2'" . SAH   C 2 .   ? -1.466  16.464 38.153 1 15.27  ? 301 SAH   A "C2'" 1 
HETATM 4045 O "O2'" . SAH   C 2 .   ? -2.508  15.709 38.762 1 15.26  ? 301 SAH   A "O2'" 1 
HETATM 4046 C "C1'" . SAH   C 2 .   ? -1.877  17.887 37.781 1 17.09  ? 301 SAH   A "C1'" 1 
HETATM 4047 N N9    . SAH   C 2 .   ? -2.676  18.016 36.558 1 15.42  ? 301 SAH   A N9    1 
HETATM 4048 C C8    . SAH   C 2 .   ? -2.501  17.332 35.383 1 16.34  ? 301 SAH   A C8    1 
HETATM 4049 N N7    . SAH   C 2 .   ? -3.336  17.677 34.433 1 15.17  ? 301 SAH   A N7    1 
HETATM 4050 C C5    . SAH   C 2 .   ? -4.124  18.65  35.025 1 15.84  ? 301 SAH   A C5    1 
HETATM 4051 C C6    . SAH   C 2 .   ? -5.197  19.429 34.542 1 18.06  ? 301 SAH   A C6    1 
HETATM 4052 N N6    . SAH   C 2 .   ? -5.717  19.304 33.312 1 16.33  ? 301 SAH   A N6    1 
HETATM 4053 N N1    . SAH   C 2 .   ? -5.737  20.34  35.382 1 16.44  ? 301 SAH   A N1    1 
HETATM 4054 C C2    . SAH   C 2 .   ? -5.249  20.445 36.622 1 18.29  ? 301 SAH   A C2    1 
HETATM 4055 N N3    . SAH   C 2 .   ? -4.247  19.767 37.19  1 18.55  ? 301 SAH   A N3    1 
HETATM 4056 C C4    . SAH   C 2 .   ? -3.724  18.876 36.335 1 16.04  ? 301 SAH   A C4    1 
HETATM 4057 C C2    . A1IQR D 3 .   ? 6.677   17.856 37.077 1 16.79  ? 302 A1IQR A C2    1 
HETATM 4058 C C7    . A1IQR D 3 .   ? 10.071  17.902 35.523 1 15.75  ? 302 A1IQR A C7    1 
HETATM 4059 C C8    . A1IQR D 3 .   ? 9.763   18.244 34.221 1 15.85  ? 302 A1IQR A C8    1 
HETATM 4060 C C9    . A1IQR D 3 .   ? 8.454   18.459 33.833 1 16.28  ? 302 A1IQR A C9    1 
HETATM 4061 C C10   . A1IQR D 3 .   ? 7.441   18.33  34.762 1 17.77  ? 302 A1IQR A C10   1 
HETATM 4062 C C11   . A1IQR D 3 .   ? 7.747   17.987 36.069 1 17.33  ? 302 A1IQR A C11   1 
HETATM 4063 N N1    . A1IQR D 3 .   ? 5.448   18.357 36.721 1 15.84  ? 302 A1IQR A N1    1 
HETATM 4064 N N3    . A1IQR D 3 .   ? 6.887   17.379 38.269 1 17.03  ? 302 A1IQR A N3    1 
HETATM 4065 C C4    . A1IQR D 3 .   ? 8.209   16.821 38.578 1 19.51  ? 302 A1IQR A C4    1 
HETATM 4066 C C5    . A1IQR D 3 .   ? 9.382   17.427 37.848 1 18.35  ? 302 A1IQR A C5    1 
HETATM 4067 C C6    . A1IQR D 3 .   ? 9.054   17.769 36.45  1 18.83  ? 302 A1IQR A C6    1 
HETATM 4068 N N     . SAH   E 2 .   ? 28.227  50.196 42.152 1 12.51  ? 301 SAH   B N     1 
HETATM 4069 C CA    . SAH   E 2 .   ? 27.592  51.529 42.336 1 12.83  ? 301 SAH   B CA    1 
HETATM 4070 C CB    . SAH   E 2 .   ? 28.043  52.647 41.325 1 13.59  ? 301 SAH   B CB    1 
HETATM 4071 C CG    . SAH   E 2 .   ? 27.732  52.305 39.872 1 13.13  ? 301 SAH   B CG    1 
HETATM 4072 S SD    . SAH   E 2 .   ? 27.892  53.843 38.916 1 13.35  ? 301 SAH   B SD    1 
HETATM 4073 C C     . SAH   E 2 .   ? 26.039  51.306 42.288 1 12.19  ? 301 SAH   B C     1 
HETATM 4074 O O     . SAH   E 2 .   ? 25.536  50.216 42.311 1 15.46  ? 301 SAH   B O     1 
HETATM 4075 O OXT   . SAH   E 2 .   ? 25.351  52.413 42.231 1 12.32  ? 301 SAH   B OXT   1 
HETATM 4076 C "C5'" . SAH   E 2 .   ? 29.191  53.464 37.712 1 12.61  ? 301 SAH   B "C5'" 1 
HETATM 4077 C "C4'" . SAH   E 2 .   ? 30.544  53.353 38.382 1 12.21  ? 301 SAH   B "C4'" 1 
HETATM 4078 O "O4'" . SAH   E 2 .   ? 31.505  52.776 37.473 1 10.95  ? 301 SAH   B "O4'" 1 
HETATM 4079 C "C3'" . SAH   E 2 .   ? 31.174  54.639 38.935 1 11.15  ? 301 SAH   B "C3'" 1 
HETATM 4080 O "O3'" . SAH   E 2 .   ? 31.527  54.426 40.296 1 11.96  ? 301 SAH   B "O3'" 1 
HETATM 4081 C "C2'" . SAH   E 2 .   ? 32.428  54.827 38.067 1 9.2    ? 301 SAH   B "C2'" 1 
HETATM 4082 O "O2'" . SAH   E 2 .   ? 33.501  55.498 38.727 1 9.25   ? 301 SAH   B "O2'" 1 
HETATM 4083 C "C1'" . SAH   E 2 .   ? 32.755  53.377 37.724 1 12.25  ? 301 SAH   B "C1'" 1 
HETATM 4084 N N9    . SAH   E 2 .   ? 33.627  53.16  36.569 1 11.23  ? 301 SAH   B N9    1 
HETATM 4085 C C8    . SAH   E 2 .   ? 33.613  53.809 35.36  1 10.01  ? 301 SAH   B C8    1 
HETATM 4086 N N7    . SAH   E 2 .   ? 34.527  53.389 34.519 1 12.29  ? 301 SAH   B N7    1 
HETATM 4087 C C5    . SAH   E 2 .   ? 35.182  52.385 35.217 1 11.27  ? 301 SAH   B C5    1 
HETATM 4088 C C6    . SAH   E 2 .   ? 36.277  51.558 34.894 1 11.39  ? 301 SAH   B C6    1 
HETATM 4089 N N6    . SAH   E 2 .   ? 36.889  51.563 33.702 1 14.53  ? 301 SAH   B N6    1 
HETATM 4090 N N1    . SAH   E 2 .   ? 36.711  50.691 35.84  1 10.1   ? 301 SAH   B N1    1 
HETATM 4091 C C2    . SAH   E 2 .   ? 36.09   50.658 37.022 1 13.58  ? 301 SAH   B C2    1 
HETATM 4092 N N3    . SAH   E 2 .   ? 35.048  51.386 37.441 1 12.53  ? 301 SAH   B N3    1 
HETATM 4093 C C4    . SAH   E 2 .   ? 34.634  52.232 36.482 1 12.16  ? 301 SAH   B C4    1 
HETATM 4094 C C2    . A1IQR F 3 .   ? 24.203  53.612 36.614 1 20.96  ? 302 A1IQR B C2    1 
HETATM 4095 C C7    . A1IQR F 3 .   ? 20.826  53.779 35.046 1 22.53  ? 302 A1IQR B C7    1 
HETATM 4096 C C8    . A1IQR F 3 .   ? 21.099  53.344 33.763 1 22.9   ? 302 A1IQR B C8    1 
HETATM 4097 C C9    . A1IQR F 3 .   ? 22.385  52.994 33.411 1 22.41  ? 302 A1IQR B C9    1 
HETATM 4098 C C10   . A1IQR F 3 .   ? 23.402  53.072 34.343 1 21.27  ? 302 A1IQR B C10   1 
HETATM 4099 C C11   . A1IQR F 3 .   ? 23.12   53.517 35.619 1 20.24  ? 302 A1IQR B C11   1 
HETATM 4100 N N1    . A1IQR F 3 .   ? 25.4    53.043 36.244 1 22.37  ? 302 A1IQR B N1    1 
HETATM 4101 N N3    . A1IQR F 3 .   ? 24.049  54.198 37.763 1 19.22  ? 302 A1IQR B N3    1 
HETATM 4102 C C4    . A1IQR F 3 .   ? 22.757  54.829 38.084 1 18.13  ? 302 A1IQR B C4    1 
HETATM 4103 C C5    . A1IQR F 3 .   ? 21.53   54.319 37.369 1 17.43  ? 302 A1IQR B C5    1 
HETATM 4104 C C6    . A1IQR F 3 .   ? 21.837  53.871 35.984 1 20.7   ? 302 A1IQR B C6    1 
HETATM 4105 O O     . HOH   G 4 .   ? 1.315   14.929 31.281 1 16.52  ? 401 HOH   A O     1 
HETATM 4106 O O     . HOH   G 4 .   ? -8.605  35.462 31.51  1 23.56  ? 402 HOH   A O     1 
HETATM 4107 O O     . HOH   G 4 .   ? -3.519  9.934  41.075 1 32.13  ? 403 HOH   A O     1 
HETATM 4108 O O     . HOH   G 4 .   ? 13.463  30.163 38.243 1 20.51  ? 404 HOH   A O     1 
HETATM 4109 O O     . HOH   G 4 .   ? 4.867   29.646 49.317 1 15.71  ? 405 HOH   A O     1 
HETATM 4110 O O     . HOH   G 4 .   ? 9.427   29.36  50.66  1 22.39  ? 406 HOH   A O     1 
HETATM 4111 O O     . HOH   G 4 .   ? -0.693  41.373 27.687 1 22.97  ? 407 HOH   A O     1 
HETATM 4112 O O     . HOH   G 4 .   ? 1.531   8.957  30.842 1 16.54  ? 408 HOH   A O     1 
HETATM 4113 O O     . HOH   G 4 .   ? 9.05    22.387 29.199 1 30.25  ? 409 HOH   A O     1 
HETATM 4114 O O     . HOH   G 4 .   ? 4.745   20.751 34.674 1 15.64  ? 410 HOH   A O     1 
HETATM 4115 O O     . HOH   G 4 .   ? 4.681   26.201 32.434 1 32.2   ? 411 HOH   A O     1 
HETATM 4116 O O     . HOH   G 4 .   ? 0.733   24.201 42.108 1 10.88  ? 412 HOH   A O     1 
HETATM 4117 O O     . HOH   G 4 .   ? 10.33   19.562 41.853 1 20.25  ? 413 HOH   A O     1 
HETATM 4118 O O     . HOH   G 4 .   ? 3.601   31.503 23.157 1 25.82  ? 414 HOH   A O     1 
HETATM 4119 O O     . HOH   G 4 .   ? -4.832  18.027 30.65  1 17.48  ? 415 HOH   A O     1 
HETATM 4120 O O     . HOH   G 4 .   ? 8.687   36.098 24.026 1 20.24  ? 416 HOH   A O     1 
HETATM 4121 O O     . HOH   G 4 .   ? -4.648  29.41  22.242 1 20.37  ? 417 HOH   A O     1 
HETATM 4122 O O     . HOH   G 4 .   ? -3.694  16.125 32.175 1 20.17  ? 418 HOH   A O     1 
HETATM 4123 O O     . HOH   G 4 .   ? -4.681  7.019  27.420 1 21.44  ? 419 HOH   A O     1 
HETATM 4124 O O     . HOH   G 4 .   ? 12.485  18.507 43.25  1 16.45  ? 420 HOH   A O     1 
HETATM 4125 O O     . HOH   G 4 .   ? 2.662   25.537 36.518 1 14.18  ? 421 HOH   A O     1 
HETATM 4126 O O     . HOH   G 4 .   ? 6.981   28.194 50.411 1 21.75  ? 422 HOH   A O     1 
HETATM 4127 O O     . HOH   G 4 .   ? -13.901 27.746 37.563 1 26.09  ? 423 HOH   A O     1 
HETATM 4128 O O     . HOH   G 4 .   ? 9.208   -3.655 34.043 1 31.89  ? 424 HOH   A O     1 
HETATM 4129 O O     . HOH   G 4 .   ? 5.365   4.525  31.397 1 15.43  ? 425 HOH   A O     1 
HETATM 4130 O O     . HOH   G 4 .   ? -7.504  36.815 28.007 1 26.38  ? 426 HOH   A O     1 
HETATM 4131 O O     . HOH   G 4 .   ? 10.588  29.545 23.195 1 15.69  ? 427 HOH   A O     1 
HETATM 4132 O O     . HOH   G 4 .   ? 14.519  28.58  27.657 1 15.89  ? 428 HOH   A O     1 
HETATM 4133 O O     . HOH   G 4 .   ? -7.13   24.462 37.574 1 59.71  ? 429 HOH   A O     1 
HETATM 4134 O O     . HOH   H 4 .   ? 21.956  48.656 28.936 1 24.14  ? 401 HOH   B O     1 
HETATM 4135 O O     . HOH   H 4 .   ? 29.574  47.328 42.24  1 6.44   ? 402 HOH   B O     1 
HETATM 4136 O O     . HOH   H 4 .   ? 29.846  56.237 31.08  1 15.36  ? 403 HOH   B O     1 
HETATM 4137 O O     . HOH   H 4 .   ? 24.884  42.294 49.434 1 14.67  ? 404 HOH   B O     1 
HETATM 4138 O O     . HOH   H 4 .   ? 18.221  53.767 42.701 1 16.63  ? 405 HOH   B O     1 
HETATM 4139 O O     . HOH   H 4 .   ? 29.779  62.427 29.878 1 19.63  ? 406 HOH   B O     1 
HETATM 4140 O O     . HOH   H 4 .   ? 36.136  52.727 30.997 1 14.99  ? 407 HOH   B O     1 
HETATM 4141 O O     . HOH   H 4 .   ? 20.098  43.177 50.49  1 17.96  ? 408 HOH   B O     1 
HETATM 4142 O O     . HOH   H 4 .   ? 32.504  41.241 59.213 1 14.32  ? 409 HOH   B O     1 
HETATM 4143 O O     . HOH   H 4 .   ? 41.711  38.289 43.257 1 16.77  ? 410 HOH   B O     1 
HETATM 4144 O O     . HOH   H 4 .   ? 26.054  45.135 32.512 1 19.93  ? 411 HOH   B O     1 
HETATM 4145 O O     . HOH   H 4 .   ? 39.037  35.377 32.682 1 18.39  ? 412 HOH   B O     1 
HETATM 4146 O O     . HOH   H 4 .   ? 36.098  40.862 23.25  1 23.77  ? 413 HOH   B O     1 
HETATM 4147 O O     . HOH   H 4 .   ? 24.794  54.931 57.537 1 19.2   ? 414 HOH   B O     1 
HETATM 4148 O O     . HOH   H 4 .   ? 20.189  52.432 41.354 1 23.52  ? 415 HOH   B O     1 
HETATM 4149 O O     . HOH   H 4 .   ? 30.869  29.532 28.763 1 19.4   ? 416 HOH   B O     1 
HETATM 4150 O O     . HOH   H 4 .   ? 44.604  48.736 42.762 1 15.72  ? 417 HOH   B O     1 
HETATM 4151 O O     . HOH   H 4 .   ? 28.734  55.903 51.329 1 10.51  ? 418 HOH   B O     1 
HETATM 4152 O O     . HOH   H 4 .   ? 44.189  40.476 37.538 1 12.86  ? 419 HOH   B O     1 
HETATM 4153 O O     . HOH   H 4 .   ? 22.743  44.008 50.063 1 16.82  ? 420 HOH   B O     1 
HETATM 4154 O O     . HOH   H 4 .   ? 19.754  36.76  39.489 1 31.76  ? 421 HOH   B O     1 
HETATM 4155 O O     . HOH   H 4 .   ? 26.025  50.802 34.436 1 20.42  ? 422 HOH   B O     1 
HETATM 4156 O O     . HOH   H 4 .   ? 26.211  66.335 30.344 1 16.04  ? 423 HOH   B O     1 
HETATM 4157 O O     . HOH   H 4 .   ? 37.009  31.26  32.085 1 19.71  ? 424 HOH   B O     1 
HETATM 4158 O O     . HOH   H 4 .   ? 34.761  54.826 32.074 1 12.51  ? 425 HOH   B O     1 
HETATM 4159 O O     . HOH   H 4 .   ? 15.576  59.788 26.262 1 18.13  ? 426 HOH   B O     1 
HETATM 4160 O O     . HOH   H 4 .   ? 44.264  42.906 38.951 1 24.03  ? 427 HOH   B O     1 
HETATM 4161 O O     . HOH   H 4 .   ? 12.826  37.232 41.827 1 32.89  ? 428 HOH   B O     1 
HETATM 4162 O O     . HOH   H 4 .   ? 25.971  54.659 24.335 1 17.23  ? 429 HOH   B O     1 
HETATM 4163 O O     . HOH   H 4 .   ? 27.841  45.971 36.615 1 9.67   ? 430 HOH   B O     1 
HETATM 4164 O O     . HOH   H 4 .   ? 25.906  28.808 30.443 1 17.35  ? 431 HOH   B O     1 
HETATM 4165 O O     . HOH   H 4 .   ? 38.085  55.855 27.985 1 28.58  ? 432 HOH   B O     1 
HETATM 4166 O O     . HOH   H 4 .   ? 20.662  41.612 22.814 1 23.54  ? 433 HOH   B O     1 
HETATM 4167 O O     . HOH   H 4 .   ? 9.716   59.476 55.629 1 60.57  ? 434 HOH   B O     1 
HETATM 4168 O O     . HOH   H 4 .   ? 21.929  44.2   22.597 1 18.47  ? 435 HOH   B O     1 
HETATM 4169 O O     . HOH   H 4 .   ? 21.411  40.244 20.639 1 21.19  ? 436 HOH   B O     1 
# 
