data_8SCW
# 
_entry.id   8SCW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8SCW         pdb_00008scw 10.2210/pdb8scw/pdb 
WWPDB D_1000273560 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-12 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8SCW 
_pdbx_database_status.recvd_initial_deposition_date   2023-04-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jodi.muckelbauer@bms.com 
_pdbx_contact_author.name_first         Jodi 
_pdbx_contact_author.name_last          Muckelbauer 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7848-3178 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Muckelbauer, J.K.' 1 0000-0001-7848-3178 
'Ghosh, K.'         2 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'The Discovery of IRAK4 Inhibitor Clinical Candidates BMS-986126 and BMS-986147 for the Treatment of Autoimmune Diseases' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kumar, S.R.'        1  ? 
primary 'Dudhgoankar, S.'    2  ? 
primary 'Santella, J.B.'     3  ? 
primary 'Paidi, V.R.R.'      4  ? 
primary 'Nair, S.'           5  ? 
primary 'Sistla, R.'         6  ? 
primary 'Wu, H.'             7  ? 
primary 'Gardner, D.S.'      8  ? 
primary 'Stachura, S.'       9  ? 
primary 'Cavallaro, C.L.'    10 ? 
primary 'Brown, G.D.'        11 ? 
primary 'Pitts, W.J.'        12 ? 
primary 'Kempson, J.'        13 ? 
primary 'Tebben, A.J.'       14 ? 
primary 'Tokarski, J.S.'     15 ? 
primary 'Zhu, X.'            16 ? 
primary 'Carman, J.A.'       17 ? 
primary 'Foster, K.'         18 ? 
primary 'Caceres Cortes, J.' 19 ? 
primary 'Everlof, G.'        20 ? 
primary 'Galella, M.A.'      21 ? 
primary 'Sarjeant, A.'       22 ? 
primary 'Holloway, D.A.'     23 ? 
primary 'Fan, L.'            24 ? 
primary 'Li, X.'             25 ? 
primary 'Chaudhry, C.'       26 ? 
primary 'Locke, G.'          27 ? 
primary 'Chimalakondra, A.'  28 ? 
primary 'Mariappan, T.T.'    29 ? 
primary 'Ruepp, S.'          30 ? 
primary 'Elzinga, P.A.'      31 ? 
primary 'Saxena, A.'         32 ? 
primary 'Xie, D.'            33 ? 
primary 'Kiefer, S.E.'       34 ? 
primary 'Yan, C.'            35 ? 
primary 'Newitt, J.A.'       36 ? 
primary 'Ghosh, K.'          37 ? 
primary 'Anumula, R.K.'      38 ? 
primary 'Sack, J.S.'         39 ? 
primary 'Tino, J.A.'         40 ? 
primary 'Carter, P.H.'       41 ? 
primary 'Hynes, J.'          42 ? 
primary 'Duncia, J.V.'       43 ? 
# 
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 'Interleukin-1 receptor-associated kinase 4' 34272.566 4  2.7.11.1 ? 'KINASE DOMAIN' ? 
2 non-polymer syn 'SULFATE ION' 96.063    8  ?        ? ?               ? 
3 non-polymer syn 
;(6M)-6-(5-cyano-1H-pyrazolo[3,4-b]pyridin-1-yl)-N-[(2R)-2-fluoro-3-hydroxy-3-methylbutyl]-4-[(propan-2-yl)amino]pyridine-3-carboxamide
;
425.459   4  ?        ? ?               ? 
4 water       nat water 18.015    59 ?        ? ?               ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'IRAK-4,Renal carcinoma antigen NY-REN-64' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;GAMGVSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIK
VMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSA
NILLDEAFTAKISDFGLARASEKFAQ(TPO)VM(TPO)(SEP)RIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITG
LPAVDEHREPQLLLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAMGVSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIK
VMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSA
NILLDEAFTAKISDFGLARASEKFAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQL
LLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 
;(6M)-6-(5-cyano-1H-pyrazolo[3,4-b]pyridin-1-yl)-N-[(2R)-2-fluoro-3-hydroxy-3-methylbutyl]-4-[(propan-2-yl)amino]pyridine-3-carboxamide
;
ZVA 
4 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   GLY n 
1 5   VAL n 
1 6   SER n 
1 7   ASP n 
1 8   THR n 
1 9   ARG n 
1 10  PHE n 
1 11  HIS n 
1 12  SER n 
1 13  PHE n 
1 14  SER n 
1 15  PHE n 
1 16  TYR n 
1 17  GLU n 
1 18  LEU n 
1 19  LYS n 
1 20  ASN n 
1 21  VAL n 
1 22  THR n 
1 23  ASN n 
1 24  ASN n 
1 25  PHE n 
1 26  ASP n 
1 27  GLU n 
1 28  ARG n 
1 29  PRO n 
1 30  ILE n 
1 31  SER n 
1 32  VAL n 
1 33  GLY n 
1 34  GLY n 
1 35  ASN n 
1 36  LYS n 
1 37  MET n 
1 38  GLY n 
1 39  GLU n 
1 40  GLY n 
1 41  GLY n 
1 42  PHE n 
1 43  GLY n 
1 44  VAL n 
1 45  VAL n 
1 46  TYR n 
1 47  LYS n 
1 48  GLY n 
1 49  TYR n 
1 50  VAL n 
1 51  ASN n 
1 52  ASN n 
1 53  THR n 
1 54  THR n 
1 55  VAL n 
1 56  ALA n 
1 57  VAL n 
1 58  LYS n 
1 59  LYS n 
1 60  LEU n 
1 61  ALA n 
1 62  ALA n 
1 63  MET n 
1 64  VAL n 
1 65  ASP n 
1 66  ILE n 
1 67  THR n 
1 68  THR n 
1 69  GLU n 
1 70  GLU n 
1 71  LEU n 
1 72  LYS n 
1 73  GLN n 
1 74  GLN n 
1 75  PHE n 
1 76  ASP n 
1 77  GLN n 
1 78  GLU n 
1 79  ILE n 
1 80  LYS n 
1 81  VAL n 
1 82  MET n 
1 83  ALA n 
1 84  LYS n 
1 85  CYS n 
1 86  GLN n 
1 87  HIS n 
1 88  GLU n 
1 89  ASN n 
1 90  LEU n 
1 91  VAL n 
1 92  GLU n 
1 93  LEU n 
1 94  LEU n 
1 95  GLY n 
1 96  PHE n 
1 97  SER n 
1 98  SER n 
1 99  ASP n 
1 100 GLY n 
1 101 ASP n 
1 102 ASP n 
1 103 LEU n 
1 104 CYS n 
1 105 LEU n 
1 106 VAL n 
1 107 TYR n 
1 108 VAL n 
1 109 TYR n 
1 110 MET n 
1 111 PRO n 
1 112 ASN n 
1 113 GLY n 
1 114 SER n 
1 115 LEU n 
1 116 LEU n 
1 117 ASP n 
1 118 ARG n 
1 119 LEU n 
1 120 SER n 
1 121 CYS n 
1 122 LEU n 
1 123 ASP n 
1 124 GLY n 
1 125 THR n 
1 126 PRO n 
1 127 PRO n 
1 128 LEU n 
1 129 SER n 
1 130 TRP n 
1 131 HIS n 
1 132 MET n 
1 133 ARG n 
1 134 CYS n 
1 135 LYS n 
1 136 ILE n 
1 137 ALA n 
1 138 GLN n 
1 139 GLY n 
1 140 ALA n 
1 141 ALA n 
1 142 ASN n 
1 143 GLY n 
1 144 ILE n 
1 145 ASN n 
1 146 PHE n 
1 147 LEU n 
1 148 HIS n 
1 149 GLU n 
1 150 ASN n 
1 151 HIS n 
1 152 HIS n 
1 153 ILE n 
1 154 HIS n 
1 155 ARG n 
1 156 ASP n 
1 157 ILE n 
1 158 LYS n 
1 159 SER n 
1 160 ALA n 
1 161 ASN n 
1 162 ILE n 
1 163 LEU n 
1 164 LEU n 
1 165 ASP n 
1 166 GLU n 
1 167 ALA n 
1 168 PHE n 
1 169 THR n 
1 170 ALA n 
1 171 LYS n 
1 172 ILE n 
1 173 SER n 
1 174 ASP n 
1 175 PHE n 
1 176 GLY n 
1 177 LEU n 
1 178 ALA n 
1 179 ARG n 
1 180 ALA n 
1 181 SER n 
1 182 GLU n 
1 183 LYS n 
1 184 PHE n 
1 185 ALA n 
1 186 GLN n 
1 187 TPO n 
1 188 VAL n 
1 189 MET n 
1 190 TPO n 
1 191 SEP n 
1 192 ARG n 
1 193 ILE n 
1 194 VAL n 
1 195 GLY n 
1 196 THR n 
1 197 THR n 
1 198 ALA n 
1 199 TYR n 
1 200 MET n 
1 201 ALA n 
1 202 PRO n 
1 203 GLU n 
1 204 ALA n 
1 205 LEU n 
1 206 ARG n 
1 207 GLY n 
1 208 GLU n 
1 209 ILE n 
1 210 THR n 
1 211 PRO n 
1 212 LYS n 
1 213 SER n 
1 214 ASP n 
1 215 ILE n 
1 216 TYR n 
1 217 SER n 
1 218 PHE n 
1 219 GLY n 
1 220 VAL n 
1 221 VAL n 
1 222 LEU n 
1 223 LEU n 
1 224 GLU n 
1 225 ILE n 
1 226 ILE n 
1 227 THR n 
1 228 GLY n 
1 229 LEU n 
1 230 PRO n 
1 231 ALA n 
1 232 VAL n 
1 233 ASP n 
1 234 GLU n 
1 235 HIS n 
1 236 ARG n 
1 237 GLU n 
1 238 PRO n 
1 239 GLN n 
1 240 LEU n 
1 241 LEU n 
1 242 LEU n 
1 243 ASP n 
1 244 ILE n 
1 245 LYS n 
1 246 GLU n 
1 247 GLU n 
1 248 ILE n 
1 249 GLU n 
1 250 ASP n 
1 251 GLU n 
1 252 GLU n 
1 253 LYS n 
1 254 THR n 
1 255 ILE n 
1 256 GLU n 
1 257 ASP n 
1 258 TYR n 
1 259 ILE n 
1 260 ASP n 
1 261 LYS n 
1 262 LYS n 
1 263 MET n 
1 264 ASN n 
1 265 ASP n 
1 266 ALA n 
1 267 ASP n 
1 268 SER n 
1 269 THR n 
1 270 SER n 
1 271 VAL n 
1 272 GLU n 
1 273 ALA n 
1 274 MET n 
1 275 TYR n 
1 276 SER n 
1 277 VAL n 
1 278 ALA n 
1 279 SER n 
1 280 GLN n 
1 281 CYS n 
1 282 LEU n 
1 283 HIS n 
1 284 GLU n 
1 285 LYS n 
1 286 LYS n 
1 287 ASN n 
1 288 LYS n 
1 289 ARG n 
1 290 PRO n 
1 291 ASP n 
1 292 ILE n 
1 293 LYS n 
1 294 LYS n 
1 295 VAL n 
1 296 GLN n 
1 297 GLN n 
1 298 LEU n 
1 299 LEU n 
1 300 GLN n 
1 301 GLU n 
1 302 MET n 
1 303 THR n 
1 304 ALA n 
1 305 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                   305 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 IRAK4 
_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      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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 
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 
SEP 'L-peptide linking' n PHOSPHOSERINE PHOSPHONOSERINE    'C3 H8 N O6 P'    185.072 
SER 'L-peptide linking' y SERINE ?                  'C3 H7 N O3'      105.093 
SO4 non-polymer         . 'SULFATE ION' ?                  'O4 S -2'         96.063  
THR 'L-peptide linking' y THREONINE ?                  'C4 H9 N O3'      119.119 
TPO 'L-peptide linking' n PHOSPHOTHREONINE PHOSPHONOTHREONINE 'C4 H10 N O6 P'   199.099 
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 
ZVA non-polymer         . 
;(6M)-6-(5-cyano-1H-pyrazolo[3,4-b]pyridin-1-yl)-N-[(2R)-2-fluoro-3-hydroxy-3-methylbutyl]-4-[(propan-2-yl)amino]pyridine-3-carboxamide
;
?                  'C21 H24 F N7 O2' 425.459 
# 
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   GLY 1   156 ?   ?   ?   A . n 
A 1 2   ALA 2   157 ?   ?   ?   A . n 
A 1 3   MET 3   158 ?   ?   ?   A . n 
A 1 4   GLY 4   159 ?   ?   ?   A . n 
A 1 5   VAL 5   160 ?   ?   ?   A . n 
A 1 6   SER 6   161 ?   ?   ?   A . n 
A 1 7   ASP 7   162 ?   ?   ?   A . n 
A 1 8   THR 8   163 ?   ?   ?   A . n 
A 1 9   ARG 9   164 164 ARG ARG A . n 
A 1 10  PHE 10  165 165 PHE PHE A . n 
A 1 11  HIS 11  166 166 HIS HIS A . n 
A 1 12  SER 12  167 167 SER SER A . n 
A 1 13  PHE 13  168 168 PHE PHE A . n 
A 1 14  SER 14  169 169 SER SER A . n 
A 1 15  PHE 15  170 170 PHE PHE A . n 
A 1 16  TYR 16  171 171 TYR TYR A . n 
A 1 17  GLU 17  172 172 GLU GLU A . n 
A 1 18  LEU 18  173 173 LEU LEU A . n 
A 1 19  LYS 19  174 174 LYS LYS A . n 
A 1 20  ASN 20  175 175 ASN ASN A . n 
A 1 21  VAL 21  176 176 VAL VAL A . n 
A 1 22  THR 22  177 177 THR THR A . n 
A 1 23  ASN 23  178 178 ASN ASN A . n 
A 1 24  ASN 24  179 179 ASN ASN A . n 
A 1 25  PHE 25  180 180 PHE PHE A . n 
A 1 26  ASP 26  181 181 ASP ASP A . n 
A 1 27  GLU 27  182 182 GLU GLU A . n 
A 1 28  ARG 28  183 183 ARG ARG A . n 
A 1 29  PRO 29  184 184 PRO PRO A . n 
A 1 30  ILE 30  185 185 ILE ILE A . n 
A 1 31  SER 31  186 186 SER SER A . n 
A 1 32  VAL 32  187 187 VAL VAL A . n 
A 1 33  GLY 33  188 188 GLY GLY A . n 
A 1 34  GLY 34  189 189 GLY GLY A . n 
A 1 35  ASN 35  190 190 ASN ASN A . n 
A 1 36  LYS 36  191 191 LYS LYS A . n 
A 1 37  MET 37  192 192 MET MET A . n 
A 1 38  GLY 38  193 193 GLY GLY A . n 
A 1 39  GLU 39  194 194 GLU GLU A . n 
A 1 40  GLY 40  195 195 GLY GLY A . n 
A 1 41  GLY 41  196 196 GLY GLY A . n 
A 1 42  PHE 42  197 197 PHE PHE A . n 
A 1 43  GLY 43  198 198 GLY GLY A . n 
A 1 44  VAL 44  199 199 VAL VAL A . n 
A 1 45  VAL 45  200 200 VAL VAL A . n 
A 1 46  TYR 46  201 201 TYR TYR A . n 
A 1 47  LYS 47  202 202 LYS LYS A . n 
A 1 48  GLY 48  203 203 GLY GLY A . n 
A 1 49  TYR 49  204 204 TYR TYR A . n 
A 1 50  VAL 50  205 205 VAL VAL A . n 
A 1 51  ASN 51  206 206 ASN ASN A . n 
A 1 52  ASN 52  207 207 ASN ASN A . n 
A 1 53  THR 53  208 208 THR THR A . n 
A 1 54  THR 54  209 209 THR THR A . n 
A 1 55  VAL 55  210 210 VAL VAL A . n 
A 1 56  ALA 56  211 211 ALA ALA A . n 
A 1 57  VAL 57  212 212 VAL VAL A . n 
A 1 58  LYS 58  213 213 LYS LYS A . n 
A 1 59  LYS 59  214 214 LYS LYS A . n 
A 1 60  LEU 60  215 215 LEU LEU A . n 
A 1 61  ALA 61  216 216 ALA ALA A . n 
A 1 62  ALA 62  217 217 ALA ALA A . n 
A 1 63  MET 63  218 ?   ?   ?   A . n 
A 1 64  VAL 64  219 ?   ?   ?   A . n 
A 1 65  ASP 65  220 ?   ?   ?   A . n 
A 1 66  ILE 66  221 ?   ?   ?   A . n 
A 1 67  THR 67  222 222 THR THR A . n 
A 1 68  THR 68  223 223 THR THR A . n 
A 1 69  GLU 69  224 224 GLU GLU A . n 
A 1 70  GLU 70  225 225 GLU GLU A . n 
A 1 71  LEU 71  226 226 LEU LEU A . n 
A 1 72  LYS 72  227 227 LYS LYS A . n 
A 1 73  GLN 73  228 228 GLN GLN A . n 
A 1 74  GLN 74  229 229 GLN GLN A . n 
A 1 75  PHE 75  230 230 PHE PHE A . n 
A 1 76  ASP 76  231 231 ASP ASP A . n 
A 1 77  GLN 77  232 232 GLN GLN A . n 
A 1 78  GLU 78  233 233 GLU GLU A . n 
A 1 79  ILE 79  234 234 ILE ILE A . n 
A 1 80  LYS 80  235 235 LYS LYS A . n 
A 1 81  VAL 81  236 236 VAL VAL A . n 
A 1 82  MET 82  237 237 MET MET A . n 
A 1 83  ALA 83  238 238 ALA ALA A . n 
A 1 84  LYS 84  239 239 LYS LYS A . n 
A 1 85  CYS 85  240 240 CYS CYS A . n 
A 1 86  GLN 86  241 241 GLN GLN A . n 
A 1 87  HIS 87  242 242 HIS HIS A . n 
A 1 88  GLU 88  243 243 GLU GLU A . n 
A 1 89  ASN 89  244 244 ASN ASN A . n 
A 1 90  LEU 90  245 245 LEU LEU A . n 
A 1 91  VAL 91  246 246 VAL VAL A . n 
A 1 92  GLU 92  247 247 GLU GLU A . n 
A 1 93  LEU 93  248 248 LEU LEU A . n 
A 1 94  LEU 94  249 249 LEU LEU A . n 
A 1 95  GLY 95  250 250 GLY GLY A . n 
A 1 96  PHE 96  251 251 PHE PHE A . n 
A 1 97  SER 97  252 252 SER SER A . n 
A 1 98  SER 98  253 253 SER SER A . n 
A 1 99  ASP 99  254 254 ASP ASP A . n 
A 1 100 GLY 100 255 255 GLY GLY A . n 
A 1 101 ASP 101 256 256 ASP ASP A . n 
A 1 102 ASP 102 257 257 ASP ASP A . n 
A 1 103 LEU 103 258 258 LEU LEU A . n 
A 1 104 CYS 104 259 259 CYS CYS A . n 
A 1 105 LEU 105 260 260 LEU LEU A . n 
A 1 106 VAL 106 261 261 VAL VAL A . n 
A 1 107 TYR 107 262 262 TYR TYR A . n 
A 1 108 VAL 108 263 263 VAL VAL A . n 
A 1 109 TYR 109 264 264 TYR TYR A . n 
A 1 110 MET 110 265 265 MET MET A . n 
A 1 111 PRO 111 266 266 PRO PRO A . n 
A 1 112 ASN 112 267 267 ASN ASN A . n 
A 1 113 GLY 113 268 268 GLY GLY A . n 
A 1 114 SER 114 269 269 SER SER A . n 
A 1 115 LEU 115 270 270 LEU LEU A . n 
A 1 116 LEU 116 271 271 LEU LEU A . n 
A 1 117 ASP 117 272 272 ASP ASP A . n 
A 1 118 ARG 118 273 273 ARG ARG A . n 
A 1 119 LEU 119 274 274 LEU LEU A . n 
A 1 120 SER 120 275 275 SER SER A . n 
A 1 121 CYS 121 276 276 CYS CYS A . n 
A 1 122 LEU 122 277 277 LEU LEU A . n 
A 1 123 ASP 123 278 278 ASP ASP A . n 
A 1 124 GLY 124 279 279 GLY GLY A . n 
A 1 125 THR 125 280 280 THR THR A . n 
A 1 126 PRO 126 281 281 PRO PRO A . n 
A 1 127 PRO 127 282 282 PRO PRO A . n 
A 1 128 LEU 128 283 283 LEU LEU A . n 
A 1 129 SER 129 284 284 SER SER A . n 
A 1 130 TRP 130 285 285 TRP TRP A . n 
A 1 131 HIS 131 286 286 HIS HIS A . n 
A 1 132 MET 132 287 287 MET MET A . n 
A 1 133 ARG 133 288 288 ARG ARG A . n 
A 1 134 CYS 134 289 289 CYS CYS A . n 
A 1 135 LYS 135 290 290 LYS LYS A . n 
A 1 136 ILE 136 291 291 ILE ILE A . n 
A 1 137 ALA 137 292 292 ALA ALA A . n 
A 1 138 GLN 138 293 293 GLN GLN A . n 
A 1 139 GLY 139 294 294 GLY GLY A . n 
A 1 140 ALA 140 295 295 ALA ALA A . n 
A 1 141 ALA 141 296 296 ALA ALA A . n 
A 1 142 ASN 142 297 297 ASN ASN A . n 
A 1 143 GLY 143 298 298 GLY GLY A . n 
A 1 144 ILE 144 299 299 ILE ILE A . n 
A 1 145 ASN 145 300 300 ASN ASN A . n 
A 1 146 PHE 146 301 301 PHE PHE A . n 
A 1 147 LEU 147 302 302 LEU LEU A . n 
A 1 148 HIS 148 303 303 HIS HIS A . n 
A 1 149 GLU 149 304 304 GLU GLU A . n 
A 1 150 ASN 150 305 305 ASN ASN A . n 
A 1 151 HIS 151 306 306 HIS HIS A . n 
A 1 152 HIS 152 307 307 HIS HIS A . n 
A 1 153 ILE 153 308 308 ILE ILE A . n 
A 1 154 HIS 154 309 309 HIS HIS A . n 
A 1 155 ARG 155 310 310 ARG ARG A . n 
A 1 156 ASP 156 311 311 ASP ASP A . n 
A 1 157 ILE 157 312 312 ILE ILE A . n 
A 1 158 LYS 158 313 313 LYS LYS A . n 
A 1 159 SER 159 314 314 SER SER A . n 
A 1 160 ALA 160 315 315 ALA ALA A . n 
A 1 161 ASN 161 316 316 ASN ASN A . n 
A 1 162 ILE 162 317 317 ILE ILE A . n 
A 1 163 LEU 163 318 318 LEU LEU A . n 
A 1 164 LEU 164 319 319 LEU LEU A . n 
A 1 165 ASP 165 320 320 ASP ASP A . n 
A 1 166 GLU 166 321 321 GLU GLU A . n 
A 1 167 ALA 167 322 322 ALA ALA A . n 
A 1 168 PHE 168 323 323 PHE PHE A . n 
A 1 169 THR 169 324 324 THR THR A . n 
A 1 170 ALA 170 325 325 ALA ALA A . n 
A 1 171 LYS 171 326 326 LYS LYS A . n 
A 1 172 ILE 172 327 327 ILE ILE A . n 
A 1 173 SER 173 328 328 SER SER A . n 
A 1 174 ASP 174 329 329 ASP ASP A . n 
A 1 175 PHE 175 330 330 PHE PHE A . n 
A 1 176 GLY 176 331 331 GLY GLY A . n 
A 1 177 LEU 177 332 332 LEU LEU A . n 
A 1 178 ALA 178 333 333 ALA ALA A . n 
A 1 179 ARG 179 334 334 ARG ARG A . n 
A 1 180 ALA 180 335 335 ALA ALA A . n 
A 1 181 SER 181 336 336 SER SER A . n 
A 1 182 GLU 182 337 ?   ?   ?   A . n 
A 1 183 LYS 183 338 ?   ?   ?   A . n 
A 1 184 PHE 184 339 ?   ?   ?   A . n 
A 1 185 ALA 185 340 ?   ?   ?   A . n 
A 1 186 GLN 186 341 ?   ?   ?   A . n 
A 1 187 TPO 187 342 342 TPO TPO A . n 
A 1 188 VAL 188 343 343 VAL VAL A . n 
A 1 189 MET 189 344 344 MET MET A . n 
A 1 190 TPO 190 345 345 TPO TPO A . n 
A 1 191 SEP 191 346 346 SEP SEP A . n 
A 1 192 ARG 192 347 347 ARG ARG A . n 
A 1 193 ILE 193 348 348 ILE ILE A . n 
A 1 194 VAL 194 349 349 VAL VAL A . n 
A 1 195 GLY 195 350 350 GLY GLY A . n 
A 1 196 THR 196 351 351 THR THR A . n 
A 1 197 THR 197 352 352 THR THR A . n 
A 1 198 ALA 198 353 353 ALA ALA A . n 
A 1 199 TYR 199 354 354 TYR TYR A . n 
A 1 200 MET 200 355 355 MET MET A . n 
A 1 201 ALA 201 356 356 ALA ALA A . n 
A 1 202 PRO 202 357 357 PRO PRO A . n 
A 1 203 GLU 203 358 358 GLU GLU A . n 
A 1 204 ALA 204 359 359 ALA ALA A . n 
A 1 205 LEU 205 360 360 LEU LEU A . n 
A 1 206 ARG 206 361 361 ARG ARG A . n 
A 1 207 GLY 207 362 362 GLY GLY A . n 
A 1 208 GLU 208 363 363 GLU GLU A . n 
A 1 209 ILE 209 364 364 ILE ILE A . n 
A 1 210 THR 210 365 365 THR THR A . n 
A 1 211 PRO 211 366 366 PRO PRO A . n 
A 1 212 LYS 212 367 367 LYS LYS A . n 
A 1 213 SER 213 368 368 SER SER A . n 
A 1 214 ASP 214 369 369 ASP ASP A . n 
A 1 215 ILE 215 370 370 ILE ILE A . n 
A 1 216 TYR 216 371 371 TYR TYR A . n 
A 1 217 SER 217 372 372 SER SER A . n 
A 1 218 PHE 218 373 373 PHE PHE A . n 
A 1 219 GLY 219 374 374 GLY GLY A . n 
A 1 220 VAL 220 375 375 VAL VAL A . n 
A 1 221 VAL 221 376 376 VAL VAL A . n 
A 1 222 LEU 222 377 377 LEU LEU A . n 
A 1 223 LEU 223 378 378 LEU LEU A . n 
A 1 224 GLU 224 379 379 GLU GLU A . n 
A 1 225 ILE 225 380 380 ILE ILE A . n 
A 1 226 ILE 226 381 381 ILE ILE A . n 
A 1 227 THR 227 382 382 THR THR A . n 
A 1 228 GLY 228 383 383 GLY GLY A . n 
A 1 229 LEU 229 384 384 LEU LEU A . n 
A 1 230 PRO 230 385 385 PRO PRO A . n 
A 1 231 ALA 231 386 386 ALA ALA A . n 
A 1 232 VAL 232 387 387 VAL VAL A . n 
A 1 233 ASP 233 388 388 ASP ASP A . n 
A 1 234 GLU 234 389 389 GLU GLU A . n 
A 1 235 HIS 235 390 390 HIS HIS A . n 
A 1 236 ARG 236 391 391 ARG ARG A . n 
A 1 237 GLU 237 392 392 GLU GLU A . n 
A 1 238 PRO 238 393 393 PRO PRO A . n 
A 1 239 GLN 239 394 394 GLN GLN A . n 
A 1 240 LEU 240 395 395 LEU LEU A . n 
A 1 241 LEU 241 396 396 LEU LEU A . n 
A 1 242 LEU 242 397 397 LEU LEU A . n 
A 1 243 ASP 243 398 398 ASP ASP A . n 
A 1 244 ILE 244 399 399 ILE ILE A . n 
A 1 245 LYS 245 400 400 LYS LYS A . n 
A 1 246 GLU 246 401 401 GLU GLU A . n 
A 1 247 GLU 247 402 402 GLU GLU A . n 
A 1 248 ILE 248 403 403 ILE ILE A . n 
A 1 249 GLU 249 404 404 GLU GLU A . n 
A 1 250 ASP 250 405 405 ASP ASP A . n 
A 1 251 GLU 251 406 406 GLU GLU A . n 
A 1 252 GLU 252 407 407 GLU GLU A . n 
A 1 253 LYS 253 408 408 LYS LYS A . n 
A 1 254 THR 254 409 409 THR THR A . n 
A 1 255 ILE 255 410 410 ILE ILE A . n 
A 1 256 GLU 256 411 411 GLU GLU A . n 
A 1 257 ASP 257 412 412 ASP ASP A . n 
A 1 258 TYR 258 413 413 TYR TYR A . n 
A 1 259 ILE 259 414 414 ILE ILE A . n 
A 1 260 ASP 260 415 415 ASP ASP A . n 
A 1 261 LYS 261 416 416 LYS LYS A . n 
A 1 262 LYS 262 417 417 LYS LYS A . n 
A 1 263 MET 263 418 418 MET MET A . n 
A 1 264 ASN 264 419 419 ASN ASN A . n 
A 1 265 ASP 265 420 420 ASP ASP A . n 
A 1 266 ALA 266 421 421 ALA ALA A . n 
A 1 267 ASP 267 422 422 ASP ASP A . n 
A 1 268 SER 268 423 423 SER SER A . n 
A 1 269 THR 269 424 424 THR THR A . n 
A 1 270 SER 270 425 425 SER SER A . n 
A 1 271 VAL 271 426 426 VAL VAL A . n 
A 1 272 GLU 272 427 427 GLU GLU A . n 
A 1 273 ALA 273 428 428 ALA ALA A . n 
A 1 274 MET 274 429 429 MET MET A . n 
A 1 275 TYR 275 430 430 TYR TYR A . n 
A 1 276 SER 276 431 431 SER SER A . n 
A 1 277 VAL 277 432 432 VAL VAL A . n 
A 1 278 ALA 278 433 433 ALA ALA A . n 
A 1 279 SER 279 434 434 SER SER A . n 
A 1 280 GLN 280 435 435 GLN GLN A . n 
A 1 281 CYS 281 436 436 CYS CYS A . n 
A 1 282 LEU 282 437 437 LEU LEU A . n 
A 1 283 HIS 283 438 438 HIS HIS A . n 
A 1 284 GLU 284 439 439 GLU GLU A . n 
A 1 285 LYS 285 440 440 LYS LYS A . n 
A 1 286 LYS 286 441 441 LYS LYS A . n 
A 1 287 ASN 287 442 442 ASN ASN A . n 
A 1 288 LYS 288 443 443 LYS LYS A . n 
A 1 289 ARG 289 444 444 ARG ARG A . n 
A 1 290 PRO 290 445 445 PRO PRO A . n 
A 1 291 ASP 291 446 446 ASP ASP A . n 
A 1 292 ILE 292 447 447 ILE ILE A . n 
A 1 293 LYS 293 448 448 LYS LYS A . n 
A 1 294 LYS 294 449 449 LYS LYS A . n 
A 1 295 VAL 295 450 450 VAL VAL A . n 
A 1 296 GLN 296 451 451 GLN GLN A . n 
A 1 297 GLN 297 452 452 GLN GLN A . n 
A 1 298 LEU 298 453 453 LEU LEU A . n 
A 1 299 LEU 299 454 454 LEU LEU A . n 
A 1 300 GLN 300 455 455 GLN GLN A . n 
A 1 301 GLU 301 456 456 GLU GLU A . n 
A 1 302 MET 302 457 457 MET MET A . n 
A 1 303 THR 303 458 458 THR THR A . n 
A 1 304 ALA 304 459 ?   ?   ?   A . n 
A 1 305 SER 305 460 ?   ?   ?   A . n 
B 1 1   GLY 1   156 ?   ?   ?   B . n 
B 1 2   ALA 2   157 ?   ?   ?   B . n 
B 1 3   MET 3   158 ?   ?   ?   B . n 
B 1 4   GLY 4   159 ?   ?   ?   B . n 
B 1 5   VAL 5   160 ?   ?   ?   B . n 
B 1 6   SER 6   161 ?   ?   ?   B . n 
B 1 7   ASP 7   162 ?   ?   ?   B . n 
B 1 8   THR 8   163 ?   ?   ?   B . n 
B 1 9   ARG 9   164 164 ARG ARG B . n 
B 1 10  PHE 10  165 165 PHE PHE B . n 
B 1 11  HIS 11  166 166 HIS HIS B . n 
B 1 12  SER 12  167 167 SER SER B . n 
B 1 13  PHE 13  168 168 PHE PHE B . n 
B 1 14  SER 14  169 169 SER SER B . n 
B 1 15  PHE 15  170 170 PHE PHE B . n 
B 1 16  TYR 16  171 171 TYR TYR B . n 
B 1 17  GLU 17  172 172 GLU GLU B . n 
B 1 18  LEU 18  173 173 LEU LEU B . n 
B 1 19  LYS 19  174 174 LYS LYS B . n 
B 1 20  ASN 20  175 175 ASN ASN B . n 
B 1 21  VAL 21  176 176 VAL VAL B . n 
B 1 22  THR 22  177 177 THR THR B . n 
B 1 23  ASN 23  178 178 ASN ASN B . n 
B 1 24  ASN 24  179 179 ASN ASN B . n 
B 1 25  PHE 25  180 180 PHE PHE B . n 
B 1 26  ASP 26  181 181 ASP ASP B . n 
B 1 27  GLU 27  182 182 GLU GLU B . n 
B 1 28  ARG 28  183 183 ARG ARG B . n 
B 1 29  PRO 29  184 184 PRO PRO B . n 
B 1 30  ILE 30  185 185 ILE ILE B . n 
B 1 31  SER 31  186 186 SER SER B . n 
B 1 32  VAL 32  187 187 VAL VAL B . n 
B 1 33  GLY 33  188 188 GLY GLY B . n 
B 1 34  GLY 34  189 189 GLY GLY B . n 
B 1 35  ASN 35  190 190 ASN ASN B . n 
B 1 36  LYS 36  191 191 LYS LYS B . n 
B 1 37  MET 37  192 192 MET MET B . n 
B 1 38  GLY 38  193 193 GLY GLY B . n 
B 1 39  GLU 39  194 194 GLU GLU B . n 
B 1 40  GLY 40  195 195 GLY GLY B . n 
B 1 41  GLY 41  196 196 GLY GLY B . n 
B 1 42  PHE 42  197 197 PHE PHE B . n 
B 1 43  GLY 43  198 198 GLY GLY B . n 
B 1 44  VAL 44  199 199 VAL VAL B . n 
B 1 45  VAL 45  200 200 VAL VAL B . n 
B 1 46  TYR 46  201 201 TYR TYR B . n 
B 1 47  LYS 47  202 202 LYS LYS B . n 
B 1 48  GLY 48  203 203 GLY GLY B . n 
B 1 49  TYR 49  204 204 TYR TYR B . n 
B 1 50  VAL 50  205 205 VAL VAL B . n 
B 1 51  ASN 51  206 206 ASN ASN B . n 
B 1 52  ASN 52  207 207 ASN ASN B . n 
B 1 53  THR 53  208 208 THR THR B . n 
B 1 54  THR 54  209 209 THR THR B . n 
B 1 55  VAL 55  210 210 VAL VAL B . n 
B 1 56  ALA 56  211 211 ALA ALA B . n 
B 1 57  VAL 57  212 212 VAL VAL B . n 
B 1 58  LYS 58  213 213 LYS LYS B . n 
B 1 59  LYS 59  214 214 LYS LYS B . n 
B 1 60  LEU 60  215 215 LEU LEU B . n 
B 1 61  ALA 61  216 216 ALA ALA B . n 
B 1 62  ALA 62  217 217 ALA ALA B . n 
B 1 63  MET 63  218 ?   ?   ?   B . n 
B 1 64  VAL 64  219 ?   ?   ?   B . n 
B 1 65  ASP 65  220 ?   ?   ?   B . n 
B 1 66  ILE 66  221 ?   ?   ?   B . n 
B 1 67  THR 67  222 222 THR THR B . n 
B 1 68  THR 68  223 223 THR THR B . n 
B 1 69  GLU 69  224 224 GLU GLU B . n 
B 1 70  GLU 70  225 225 GLU GLU B . n 
B 1 71  LEU 71  226 226 LEU LEU B . n 
B 1 72  LYS 72  227 227 LYS LYS B . n 
B 1 73  GLN 73  228 228 GLN GLN B . n 
B 1 74  GLN 74  229 229 GLN GLN B . n 
B 1 75  PHE 75  230 230 PHE PHE B . n 
B 1 76  ASP 76  231 231 ASP ASP B . n 
B 1 77  GLN 77  232 232 GLN GLN B . n 
B 1 78  GLU 78  233 233 GLU GLU B . n 
B 1 79  ILE 79  234 234 ILE ILE B . n 
B 1 80  LYS 80  235 235 LYS LYS B . n 
B 1 81  VAL 81  236 236 VAL VAL B . n 
B 1 82  MET 82  237 237 MET MET B . n 
B 1 83  ALA 83  238 238 ALA ALA B . n 
B 1 84  LYS 84  239 239 LYS LYS B . n 
B 1 85  CYS 85  240 240 CYS CYS B . n 
B 1 86  GLN 86  241 241 GLN GLN B . n 
B 1 87  HIS 87  242 242 HIS HIS B . n 
B 1 88  GLU 88  243 243 GLU GLU B . n 
B 1 89  ASN 89  244 244 ASN ASN B . n 
B 1 90  LEU 90  245 245 LEU LEU B . n 
B 1 91  VAL 91  246 246 VAL VAL B . n 
B 1 92  GLU 92  247 247 GLU GLU B . n 
B 1 93  LEU 93  248 248 LEU LEU B . n 
B 1 94  LEU 94  249 249 LEU LEU B . n 
B 1 95  GLY 95  250 250 GLY GLY B . n 
B 1 96  PHE 96  251 251 PHE PHE B . n 
B 1 97  SER 97  252 252 SER SER B . n 
B 1 98  SER 98  253 253 SER SER B . n 
B 1 99  ASP 99  254 254 ASP ASP B . n 
B 1 100 GLY 100 255 255 GLY GLY B . n 
B 1 101 ASP 101 256 256 ASP ASP B . n 
B 1 102 ASP 102 257 257 ASP ASP B . n 
B 1 103 LEU 103 258 258 LEU LEU B . n 
B 1 104 CYS 104 259 259 CYS CYS B . n 
B 1 105 LEU 105 260 260 LEU LEU B . n 
B 1 106 VAL 106 261 261 VAL VAL B . n 
B 1 107 TYR 107 262 262 TYR TYR B . n 
B 1 108 VAL 108 263 263 VAL VAL B . n 
B 1 109 TYR 109 264 264 TYR TYR B . n 
B 1 110 MET 110 265 265 MET MET B . n 
B 1 111 PRO 111 266 266 PRO PRO B . n 
B 1 112 ASN 112 267 267 ASN ASN B . n 
B 1 113 GLY 113 268 268 GLY GLY B . n 
B 1 114 SER 114 269 269 SER SER B . n 
B 1 115 LEU 115 270 270 LEU LEU B . n 
B 1 116 LEU 116 271 271 LEU LEU B . n 
B 1 117 ASP 117 272 272 ASP ASP B . n 
B 1 118 ARG 118 273 273 ARG ARG B . n 
B 1 119 LEU 119 274 274 LEU LEU B . n 
B 1 120 SER 120 275 275 SER SER B . n 
B 1 121 CYS 121 276 276 CYS CYS B . n 
B 1 122 LEU 122 277 277 LEU LEU B . n 
B 1 123 ASP 123 278 278 ASP ASP B . n 
B 1 124 GLY 124 279 279 GLY GLY B . n 
B 1 125 THR 125 280 280 THR THR B . n 
B 1 126 PRO 126 281 281 PRO PRO B . n 
B 1 127 PRO 127 282 282 PRO PRO B . n 
B 1 128 LEU 128 283 283 LEU LEU B . n 
B 1 129 SER 129 284 284 SER SER B . n 
B 1 130 TRP 130 285 285 TRP TRP B . n 
B 1 131 HIS 131 286 286 HIS HIS B . n 
B 1 132 MET 132 287 287 MET MET B . n 
B 1 133 ARG 133 288 288 ARG ARG B . n 
B 1 134 CYS 134 289 289 CYS CYS B . n 
B 1 135 LYS 135 290 290 LYS LYS B . n 
B 1 136 ILE 136 291 291 ILE ILE B . n 
B 1 137 ALA 137 292 292 ALA ALA B . n 
B 1 138 GLN 138 293 293 GLN GLN B . n 
B 1 139 GLY 139 294 294 GLY GLY B . n 
B 1 140 ALA 140 295 295 ALA ALA B . n 
B 1 141 ALA 141 296 296 ALA ALA B . n 
B 1 142 ASN 142 297 297 ASN ASN B . n 
B 1 143 GLY 143 298 298 GLY GLY B . n 
B 1 144 ILE 144 299 299 ILE ILE B . n 
B 1 145 ASN 145 300 300 ASN ASN B . n 
B 1 146 PHE 146 301 301 PHE PHE B . n 
B 1 147 LEU 147 302 302 LEU LEU B . n 
B 1 148 HIS 148 303 303 HIS HIS B . n 
B 1 149 GLU 149 304 304 GLU GLU B . n 
B 1 150 ASN 150 305 305 ASN ASN B . n 
B 1 151 HIS 151 306 306 HIS HIS B . n 
B 1 152 HIS 152 307 307 HIS HIS B . n 
B 1 153 ILE 153 308 308 ILE ILE B . n 
B 1 154 HIS 154 309 309 HIS HIS B . n 
B 1 155 ARG 155 310 310 ARG ARG B . n 
B 1 156 ASP 156 311 311 ASP ASP B . n 
B 1 157 ILE 157 312 312 ILE ILE B . n 
B 1 158 LYS 158 313 313 LYS LYS B . n 
B 1 159 SER 159 314 314 SER SER B . n 
B 1 160 ALA 160 315 315 ALA ALA B . n 
B 1 161 ASN 161 316 316 ASN ASN B . n 
B 1 162 ILE 162 317 317 ILE ILE B . n 
B 1 163 LEU 163 318 318 LEU LEU B . n 
B 1 164 LEU 164 319 319 LEU LEU B . n 
B 1 165 ASP 165 320 320 ASP ASP B . n 
B 1 166 GLU 166 321 321 GLU GLU B . n 
B 1 167 ALA 167 322 322 ALA ALA B . n 
B 1 168 PHE 168 323 323 PHE PHE B . n 
B 1 169 THR 169 324 324 THR THR B . n 
B 1 170 ALA 170 325 325 ALA ALA B . n 
B 1 171 LYS 171 326 326 LYS LYS B . n 
B 1 172 ILE 172 327 327 ILE ILE B . n 
B 1 173 SER 173 328 328 SER SER B . n 
B 1 174 ASP 174 329 329 ASP ASP B . n 
B 1 175 PHE 175 330 330 PHE PHE B . n 
B 1 176 GLY 176 331 331 GLY GLY B . n 
B 1 177 LEU 177 332 332 LEU LEU B . n 
B 1 178 ALA 178 333 333 ALA ALA B . n 
B 1 179 ARG 179 334 334 ARG ARG B . n 
B 1 180 ALA 180 335 335 ALA ALA B . n 
B 1 181 SER 181 336 336 SER SER B . n 
B 1 182 GLU 182 337 ?   ?   ?   B . n 
B 1 183 LYS 183 338 ?   ?   ?   B . n 
B 1 184 PHE 184 339 ?   ?   ?   B . n 
B 1 185 ALA 185 340 ?   ?   ?   B . n 
B 1 186 GLN 186 341 ?   ?   ?   B . n 
B 1 187 TPO 187 342 342 TPO TPO B . n 
B 1 188 VAL 188 343 343 VAL VAL B . n 
B 1 189 MET 189 344 344 MET MET B . n 
B 1 190 TPO 190 345 345 TPO TPO B . n 
B 1 191 SEP 191 346 346 SEP SEP B . n 
B 1 192 ARG 192 347 347 ARG ARG B . n 
B 1 193 ILE 193 348 348 ILE ILE B . n 
B 1 194 VAL 194 349 349 VAL VAL B . n 
B 1 195 GLY 195 350 350 GLY GLY B . n 
B 1 196 THR 196 351 351 THR THR B . n 
B 1 197 THR 197 352 352 THR THR B . n 
B 1 198 ALA 198 353 353 ALA ALA B . n 
B 1 199 TYR 199 354 354 TYR TYR B . n 
B 1 200 MET 200 355 355 MET MET B . n 
B 1 201 ALA 201 356 356 ALA ALA B . n 
B 1 202 PRO 202 357 357 PRO PRO B . n 
B 1 203 GLU 203 358 358 GLU GLU B . n 
B 1 204 ALA 204 359 359 ALA ALA B . n 
B 1 205 LEU 205 360 360 LEU LEU B . n 
B 1 206 ARG 206 361 361 ARG ARG B . n 
B 1 207 GLY 207 362 362 GLY GLY B . n 
B 1 208 GLU 208 363 363 GLU GLU B . n 
B 1 209 ILE 209 364 364 ILE ILE B . n 
B 1 210 THR 210 365 365 THR THR B . n 
B 1 211 PRO 211 366 366 PRO PRO B . n 
B 1 212 LYS 212 367 367 LYS LYS B . n 
B 1 213 SER 213 368 368 SER SER B . n 
B 1 214 ASP 214 369 369 ASP ASP B . n 
B 1 215 ILE 215 370 370 ILE ILE B . n 
B 1 216 TYR 216 371 371 TYR TYR B . n 
B 1 217 SER 217 372 372 SER SER B . n 
B 1 218 PHE 218 373 373 PHE PHE B . n 
B 1 219 GLY 219 374 374 GLY GLY B . n 
B 1 220 VAL 220 375 375 VAL VAL B . n 
B 1 221 VAL 221 376 376 VAL VAL B . n 
B 1 222 LEU 222 377 377 LEU LEU B . n 
B 1 223 LEU 223 378 378 LEU LEU B . n 
B 1 224 GLU 224 379 379 GLU GLU B . n 
B 1 225 ILE 225 380 380 ILE ILE B . n 
B 1 226 ILE 226 381 381 ILE ILE B . n 
B 1 227 THR 227 382 382 THR THR B . n 
B 1 228 GLY 228 383 383 GLY GLY B . n 
B 1 229 LEU 229 384 384 LEU LEU B . n 
B 1 230 PRO 230 385 385 PRO PRO B . n 
B 1 231 ALA 231 386 386 ALA ALA B . n 
B 1 232 VAL 232 387 387 VAL VAL B . n 
B 1 233 ASP 233 388 388 ASP ASP B . n 
B 1 234 GLU 234 389 389 GLU GLU B . n 
B 1 235 HIS 235 390 390 HIS HIS B . n 
B 1 236 ARG 236 391 391 ARG ARG B . n 
B 1 237 GLU 237 392 392 GLU GLU B . n 
B 1 238 PRO 238 393 393 PRO PRO B . n 
B 1 239 GLN 239 394 394 GLN GLN B . n 
B 1 240 LEU 240 395 395 LEU LEU B . n 
B 1 241 LEU 241 396 396 LEU LEU B . n 
B 1 242 LEU 242 397 397 LEU LEU B . n 
B 1 243 ASP 243 398 398 ASP ASP B . n 
B 1 244 ILE 244 399 399 ILE ILE B . n 
B 1 245 LYS 245 400 400 LYS LYS B . n 
B 1 246 GLU 246 401 401 GLU GLU B . n 
B 1 247 GLU 247 402 402 GLU GLU B . n 
B 1 248 ILE 248 403 403 ILE ILE B . n 
B 1 249 GLU 249 404 404 GLU GLU B . n 
B 1 250 ASP 250 405 405 ASP ASP B . n 
B 1 251 GLU 251 406 406 GLU GLU B . n 
B 1 252 GLU 252 407 407 GLU GLU B . n 
B 1 253 LYS 253 408 408 LYS LYS B . n 
B 1 254 THR 254 409 409 THR THR B . n 
B 1 255 ILE 255 410 410 ILE ILE B . n 
B 1 256 GLU 256 411 411 GLU GLU B . n 
B 1 257 ASP 257 412 412 ASP ASP B . n 
B 1 258 TYR 258 413 413 TYR TYR B . n 
B 1 259 ILE 259 414 414 ILE ILE B . n 
B 1 260 ASP 260 415 415 ASP ASP B . n 
B 1 261 LYS 261 416 416 LYS LYS B . n 
B 1 262 LYS 262 417 417 LYS LYS B . n 
B 1 263 MET 263 418 418 MET MET B . n 
B 1 264 ASN 264 419 419 ASN ASN B . n 
B 1 265 ASP 265 420 420 ASP ASP B . n 
B 1 266 ALA 266 421 421 ALA ALA B . n 
B 1 267 ASP 267 422 422 ASP ASP B . n 
B 1 268 SER 268 423 423 SER SER B . n 
B 1 269 THR 269 424 424 THR THR B . n 
B 1 270 SER 270 425 425 SER SER B . n 
B 1 271 VAL 271 426 426 VAL VAL B . n 
B 1 272 GLU 272 427 427 GLU GLU B . n 
B 1 273 ALA 273 428 428 ALA ALA B . n 
B 1 274 MET 274 429 429 MET MET B . n 
B 1 275 TYR 275 430 430 TYR TYR B . n 
B 1 276 SER 276 431 431 SER SER B . n 
B 1 277 VAL 277 432 432 VAL VAL B . n 
B 1 278 ALA 278 433 433 ALA ALA B . n 
B 1 279 SER 279 434 434 SER SER B . n 
B 1 280 GLN 280 435 435 GLN GLN B . n 
B 1 281 CYS 281 436 436 CYS CYS B . n 
B 1 282 LEU 282 437 437 LEU LEU B . n 
B 1 283 HIS 283 438 438 HIS HIS B . n 
B 1 284 GLU 284 439 439 GLU GLU B . n 
B 1 285 LYS 285 440 440 LYS LYS B . n 
B 1 286 LYS 286 441 441 LYS LYS B . n 
B 1 287 ASN 287 442 442 ASN ASN B . n 
B 1 288 LYS 288 443 443 LYS LYS B . n 
B 1 289 ARG 289 444 444 ARG ARG B . n 
B 1 290 PRO 290 445 445 PRO PRO B . n 
B 1 291 ASP 291 446 446 ASP ASP B . n 
B 1 292 ILE 292 447 447 ILE ILE B . n 
B 1 293 LYS 293 448 448 LYS LYS B . n 
B 1 294 LYS 294 449 449 LYS LYS B . n 
B 1 295 VAL 295 450 450 VAL VAL B . n 
B 1 296 GLN 296 451 451 GLN GLN B . n 
B 1 297 GLN 297 452 452 GLN GLN B . n 
B 1 298 LEU 298 453 453 LEU LEU B . n 
B 1 299 LEU 299 454 454 LEU LEU B . n 
B 1 300 GLN 300 455 455 GLN GLN B . n 
B 1 301 GLU 301 456 456 GLU GLU B . n 
B 1 302 MET 302 457 457 MET MET B . n 
B 1 303 THR 303 458 458 THR THR B . n 
B 1 304 ALA 304 459 ?   ?   ?   B . n 
B 1 305 SER 305 460 ?   ?   ?   B . n 
C 1 1   GLY 1   156 ?   ?   ?   C . n 
C 1 2   ALA 2   157 ?   ?   ?   C . n 
C 1 3   MET 3   158 ?   ?   ?   C . n 
C 1 4   GLY 4   159 ?   ?   ?   C . n 
C 1 5   VAL 5   160 ?   ?   ?   C . n 
C 1 6   SER 6   161 ?   ?   ?   C . n 
C 1 7   ASP 7   162 ?   ?   ?   C . n 
C 1 8   THR 8   163 ?   ?   ?   C . n 
C 1 9   ARG 9   164 164 ARG ARG C . n 
C 1 10  PHE 10  165 165 PHE PHE C . n 
C 1 11  HIS 11  166 166 HIS HIS C . n 
C 1 12  SER 12  167 167 SER SER C . n 
C 1 13  PHE 13  168 168 PHE PHE C . n 
C 1 14  SER 14  169 169 SER SER C . n 
C 1 15  PHE 15  170 170 PHE PHE C . n 
C 1 16  TYR 16  171 171 TYR TYR C . n 
C 1 17  GLU 17  172 172 GLU GLU C . n 
C 1 18  LEU 18  173 173 LEU LEU C . n 
C 1 19  LYS 19  174 174 LYS LYS C . n 
C 1 20  ASN 20  175 175 ASN ASN C . n 
C 1 21  VAL 21  176 176 VAL VAL C . n 
C 1 22  THR 22  177 177 THR THR C . n 
C 1 23  ASN 23  178 178 ASN ASN C . n 
C 1 24  ASN 24  179 179 ASN ASN C . n 
C 1 25  PHE 25  180 180 PHE PHE C . n 
C 1 26  ASP 26  181 181 ASP ASP C . n 
C 1 27  GLU 27  182 182 GLU GLU C . n 
C 1 28  ARG 28  183 183 ARG ARG C . n 
C 1 29  PRO 29  184 184 PRO PRO C . n 
C 1 30  ILE 30  185 185 ILE ILE C . n 
C 1 31  SER 31  186 186 SER SER C . n 
C 1 32  VAL 32  187 187 VAL VAL C . n 
C 1 33  GLY 33  188 188 GLY GLY C . n 
C 1 34  GLY 34  189 189 GLY GLY C . n 
C 1 35  ASN 35  190 190 ASN ASN C . n 
C 1 36  LYS 36  191 191 LYS LYS C . n 
C 1 37  MET 37  192 192 MET MET C . n 
C 1 38  GLY 38  193 193 GLY GLY C . n 
C 1 39  GLU 39  194 194 GLU GLU C . n 
C 1 40  GLY 40  195 195 GLY GLY C . n 
C 1 41  GLY 41  196 196 GLY GLY C . n 
C 1 42  PHE 42  197 197 PHE PHE C . n 
C 1 43  GLY 43  198 198 GLY GLY C . n 
C 1 44  VAL 44  199 199 VAL VAL C . n 
C 1 45  VAL 45  200 200 VAL VAL C . n 
C 1 46  TYR 46  201 201 TYR TYR C . n 
C 1 47  LYS 47  202 202 LYS LYS C . n 
C 1 48  GLY 48  203 203 GLY GLY C . n 
C 1 49  TYR 49  204 204 TYR TYR C . n 
C 1 50  VAL 50  205 205 VAL VAL C . n 
C 1 51  ASN 51  206 206 ASN ASN C . n 
C 1 52  ASN 52  207 207 ASN ASN C . n 
C 1 53  THR 53  208 208 THR THR C . n 
C 1 54  THR 54  209 209 THR THR C . n 
C 1 55  VAL 55  210 210 VAL VAL C . n 
C 1 56  ALA 56  211 211 ALA ALA C . n 
C 1 57  VAL 57  212 212 VAL VAL C . n 
C 1 58  LYS 58  213 213 LYS LYS C . n 
C 1 59  LYS 59  214 214 LYS LYS C . n 
C 1 60  LEU 60  215 215 LEU LEU C . n 
C 1 61  ALA 61  216 216 ALA ALA C . n 
C 1 62  ALA 62  217 217 ALA ALA C . n 
C 1 63  MET 63  218 ?   ?   ?   C . n 
C 1 64  VAL 64  219 ?   ?   ?   C . n 
C 1 65  ASP 65  220 ?   ?   ?   C . n 
C 1 66  ILE 66  221 ?   ?   ?   C . n 
C 1 67  THR 67  222 ?   ?   ?   C . n 
C 1 68  THR 68  223 223 THR THR C . n 
C 1 69  GLU 69  224 224 GLU GLU C . n 
C 1 70  GLU 70  225 225 GLU GLU C . n 
C 1 71  LEU 71  226 226 LEU LEU C . n 
C 1 72  LYS 72  227 227 LYS LYS C . n 
C 1 73  GLN 73  228 228 GLN GLN C . n 
C 1 74  GLN 74  229 229 GLN GLN C . n 
C 1 75  PHE 75  230 230 PHE PHE C . n 
C 1 76  ASP 76  231 231 ASP ASP C . n 
C 1 77  GLN 77  232 232 GLN GLN C . n 
C 1 78  GLU 78  233 233 GLU GLU C . n 
C 1 79  ILE 79  234 234 ILE ILE C . n 
C 1 80  LYS 80  235 235 LYS LYS C . n 
C 1 81  VAL 81  236 236 VAL VAL C . n 
C 1 82  MET 82  237 237 MET MET C . n 
C 1 83  ALA 83  238 238 ALA ALA C . n 
C 1 84  LYS 84  239 239 LYS LYS C . n 
C 1 85  CYS 85  240 240 CYS CYS C . n 
C 1 86  GLN 86  241 241 GLN GLN C . n 
C 1 87  HIS 87  242 242 HIS HIS C . n 
C 1 88  GLU 88  243 243 GLU GLU C . n 
C 1 89  ASN 89  244 244 ASN ASN C . n 
C 1 90  LEU 90  245 245 LEU LEU C . n 
C 1 91  VAL 91  246 246 VAL VAL C . n 
C 1 92  GLU 92  247 247 GLU GLU C . n 
C 1 93  LEU 93  248 248 LEU LEU C . n 
C 1 94  LEU 94  249 249 LEU LEU C . n 
C 1 95  GLY 95  250 250 GLY GLY C . n 
C 1 96  PHE 96  251 251 PHE PHE C . n 
C 1 97  SER 97  252 252 SER SER C . n 
C 1 98  SER 98  253 253 SER SER C . n 
C 1 99  ASP 99  254 254 ASP ASP C . n 
C 1 100 GLY 100 255 255 GLY GLY C . n 
C 1 101 ASP 101 256 256 ASP ASP C . n 
C 1 102 ASP 102 257 257 ASP ASP C . n 
C 1 103 LEU 103 258 258 LEU LEU C . n 
C 1 104 CYS 104 259 259 CYS CYS C . n 
C 1 105 LEU 105 260 260 LEU LEU C . n 
C 1 106 VAL 106 261 261 VAL VAL C . n 
C 1 107 TYR 107 262 262 TYR TYR C . n 
C 1 108 VAL 108 263 263 VAL VAL C . n 
C 1 109 TYR 109 264 264 TYR TYR C . n 
C 1 110 MET 110 265 265 MET MET C . n 
C 1 111 PRO 111 266 266 PRO PRO C . n 
C 1 112 ASN 112 267 267 ASN ASN C . n 
C 1 113 GLY 113 268 268 GLY GLY C . n 
C 1 114 SER 114 269 269 SER SER C . n 
C 1 115 LEU 115 270 270 LEU LEU C . n 
C 1 116 LEU 116 271 271 LEU LEU C . n 
C 1 117 ASP 117 272 272 ASP ASP C . n 
C 1 118 ARG 118 273 273 ARG ARG C . n 
C 1 119 LEU 119 274 274 LEU LEU C . n 
C 1 120 SER 120 275 275 SER SER C . n 
C 1 121 CYS 121 276 276 CYS CYS C . n 
C 1 122 LEU 122 277 277 LEU LEU C . n 
C 1 123 ASP 123 278 278 ASP ASP C . n 
C 1 124 GLY 124 279 279 GLY GLY C . n 
C 1 125 THR 125 280 280 THR THR C . n 
C 1 126 PRO 126 281 281 PRO PRO C . n 
C 1 127 PRO 127 282 282 PRO PRO C . n 
C 1 128 LEU 128 283 283 LEU LEU C . n 
C 1 129 SER 129 284 284 SER SER C . n 
C 1 130 TRP 130 285 285 TRP TRP C . n 
C 1 131 HIS 131 286 286 HIS HIS C . n 
C 1 132 MET 132 287 287 MET MET C . n 
C 1 133 ARG 133 288 288 ARG ARG C . n 
C 1 134 CYS 134 289 289 CYS CYS C . n 
C 1 135 LYS 135 290 290 LYS LYS C . n 
C 1 136 ILE 136 291 291 ILE ILE C . n 
C 1 137 ALA 137 292 292 ALA ALA C . n 
C 1 138 GLN 138 293 293 GLN GLN C . n 
C 1 139 GLY 139 294 294 GLY GLY C . n 
C 1 140 ALA 140 295 295 ALA ALA C . n 
C 1 141 ALA 141 296 296 ALA ALA C . n 
C 1 142 ASN 142 297 297 ASN ASN C . n 
C 1 143 GLY 143 298 298 GLY GLY C . n 
C 1 144 ILE 144 299 299 ILE ILE C . n 
C 1 145 ASN 145 300 300 ASN ASN C . n 
C 1 146 PHE 146 301 301 PHE PHE C . n 
C 1 147 LEU 147 302 302 LEU LEU C . n 
C 1 148 HIS 148 303 303 HIS HIS C . n 
C 1 149 GLU 149 304 304 GLU GLU C . n 
C 1 150 ASN 150 305 305 ASN ASN C . n 
C 1 151 HIS 151 306 306 HIS HIS C . n 
C 1 152 HIS 152 307 307 HIS HIS C . n 
C 1 153 ILE 153 308 308 ILE ILE C . n 
C 1 154 HIS 154 309 309 HIS HIS C . n 
C 1 155 ARG 155 310 310 ARG ARG C . n 
C 1 156 ASP 156 311 311 ASP ASP C . n 
C 1 157 ILE 157 312 312 ILE ILE C . n 
C 1 158 LYS 158 313 313 LYS LYS C . n 
C 1 159 SER 159 314 314 SER SER C . n 
C 1 160 ALA 160 315 315 ALA ALA C . n 
C 1 161 ASN 161 316 316 ASN ASN C . n 
C 1 162 ILE 162 317 317 ILE ILE C . n 
C 1 163 LEU 163 318 318 LEU LEU C . n 
C 1 164 LEU 164 319 319 LEU LEU C . n 
C 1 165 ASP 165 320 320 ASP ASP C . n 
C 1 166 GLU 166 321 321 GLU GLU C . n 
C 1 167 ALA 167 322 322 ALA ALA C . n 
C 1 168 PHE 168 323 323 PHE PHE C . n 
C 1 169 THR 169 324 324 THR THR C . n 
C 1 170 ALA 170 325 325 ALA ALA C . n 
C 1 171 LYS 171 326 326 LYS LYS C . n 
C 1 172 ILE 172 327 327 ILE ILE C . n 
C 1 173 SER 173 328 328 SER SER C . n 
C 1 174 ASP 174 329 329 ASP ASP C . n 
C 1 175 PHE 175 330 330 PHE PHE C . n 
C 1 176 GLY 176 331 331 GLY GLY C . n 
C 1 177 LEU 177 332 332 LEU LEU C . n 
C 1 178 ALA 178 333 333 ALA ALA C . n 
C 1 179 ARG 179 334 334 ARG ARG C . n 
C 1 180 ALA 180 335 335 ALA ALA C . n 
C 1 181 SER 181 336 ?   ?   ?   C . n 
C 1 182 GLU 182 337 ?   ?   ?   C . n 
C 1 183 LYS 183 338 ?   ?   ?   C . n 
C 1 184 PHE 184 339 ?   ?   ?   C . n 
C 1 185 ALA 185 340 ?   ?   ?   C . n 
C 1 186 GLN 186 341 ?   ?   ?   C . n 
C 1 187 TPO 187 342 342 TPO TPO C . n 
C 1 188 VAL 188 343 343 VAL VAL C . n 
C 1 189 MET 189 344 344 MET MET C . n 
C 1 190 TPO 190 345 345 TPO TPO C . n 
C 1 191 SEP 191 346 346 SEP SEP C . n 
C 1 192 ARG 192 347 347 ARG ARG C . n 
C 1 193 ILE 193 348 348 ILE ILE C . n 
C 1 194 VAL 194 349 349 VAL VAL C . n 
C 1 195 GLY 195 350 350 GLY GLY C . n 
C 1 196 THR 196 351 351 THR THR C . n 
C 1 197 THR 197 352 352 THR THR C . n 
C 1 198 ALA 198 353 353 ALA ALA C . n 
C 1 199 TYR 199 354 354 TYR TYR C . n 
C 1 200 MET 200 355 355 MET MET C . n 
C 1 201 ALA 201 356 356 ALA ALA C . n 
C 1 202 PRO 202 357 357 PRO PRO C . n 
C 1 203 GLU 203 358 358 GLU GLU C . n 
C 1 204 ALA 204 359 359 ALA ALA C . n 
C 1 205 LEU 205 360 360 LEU LEU C . n 
C 1 206 ARG 206 361 361 ARG ARG C . n 
C 1 207 GLY 207 362 362 GLY GLY C . n 
C 1 208 GLU 208 363 363 GLU GLU C . n 
C 1 209 ILE 209 364 364 ILE ILE C . n 
C 1 210 THR 210 365 365 THR THR C . n 
C 1 211 PRO 211 366 366 PRO PRO C . n 
C 1 212 LYS 212 367 367 LYS LYS C . n 
C 1 213 SER 213 368 368 SER SER C . n 
C 1 214 ASP 214 369 369 ASP ASP C . n 
C 1 215 ILE 215 370 370 ILE ILE C . n 
C 1 216 TYR 216 371 371 TYR TYR C . n 
C 1 217 SER 217 372 372 SER SER C . n 
C 1 218 PHE 218 373 373 PHE PHE C . n 
C 1 219 GLY 219 374 374 GLY GLY C . n 
C 1 220 VAL 220 375 375 VAL VAL C . n 
C 1 221 VAL 221 376 376 VAL VAL C . n 
C 1 222 LEU 222 377 377 LEU LEU C . n 
C 1 223 LEU 223 378 378 LEU LEU C . n 
C 1 224 GLU 224 379 379 GLU GLU C . n 
C 1 225 ILE 225 380 380 ILE ILE C . n 
C 1 226 ILE 226 381 381 ILE ILE C . n 
C 1 227 THR 227 382 382 THR THR C . n 
C 1 228 GLY 228 383 383 GLY GLY C . n 
C 1 229 LEU 229 384 384 LEU LEU C . n 
C 1 230 PRO 230 385 385 PRO PRO C . n 
C 1 231 ALA 231 386 386 ALA ALA C . n 
C 1 232 VAL 232 387 387 VAL VAL C . n 
C 1 233 ASP 233 388 388 ASP ASP C . n 
C 1 234 GLU 234 389 389 GLU GLU C . n 
C 1 235 HIS 235 390 390 HIS HIS C . n 
C 1 236 ARG 236 391 391 ARG ARG C . n 
C 1 237 GLU 237 392 392 GLU GLU C . n 
C 1 238 PRO 238 393 393 PRO PRO C . n 
C 1 239 GLN 239 394 394 GLN GLN C . n 
C 1 240 LEU 240 395 395 LEU LEU C . n 
C 1 241 LEU 241 396 396 LEU LEU C . n 
C 1 242 LEU 242 397 397 LEU LEU C . n 
C 1 243 ASP 243 398 398 ASP ASP C . n 
C 1 244 ILE 244 399 399 ILE ILE C . n 
C 1 245 LYS 245 400 400 LYS LYS C . n 
C 1 246 GLU 246 401 401 GLU GLU C . n 
C 1 247 GLU 247 402 402 GLU GLU C . n 
C 1 248 ILE 248 403 403 ILE ILE C . n 
C 1 249 GLU 249 404 404 GLU GLU C . n 
C 1 250 ASP 250 405 405 ASP ASP C . n 
C 1 251 GLU 251 406 406 GLU GLU C . n 
C 1 252 GLU 252 407 407 GLU GLU C . n 
C 1 253 LYS 253 408 408 LYS LYS C . n 
C 1 254 THR 254 409 409 THR THR C . n 
C 1 255 ILE 255 410 410 ILE ILE C . n 
C 1 256 GLU 256 411 411 GLU GLU C . n 
C 1 257 ASP 257 412 412 ASP ASP C . n 
C 1 258 TYR 258 413 413 TYR TYR C . n 
C 1 259 ILE 259 414 414 ILE ILE C . n 
C 1 260 ASP 260 415 415 ASP ASP C . n 
C 1 261 LYS 261 416 416 LYS LYS C . n 
C 1 262 LYS 262 417 417 LYS LYS C . n 
C 1 263 MET 263 418 418 MET MET C . n 
C 1 264 ASN 264 419 419 ASN ASN C . n 
C 1 265 ASP 265 420 420 ASP ASP C . n 
C 1 266 ALA 266 421 421 ALA ALA C . n 
C 1 267 ASP 267 422 422 ASP ASP C . n 
C 1 268 SER 268 423 423 SER SER C . n 
C 1 269 THR 269 424 424 THR THR C . n 
C 1 270 SER 270 425 425 SER SER C . n 
C 1 271 VAL 271 426 426 VAL VAL C . n 
C 1 272 GLU 272 427 427 GLU GLU C . n 
C 1 273 ALA 273 428 428 ALA ALA C . n 
C 1 274 MET 274 429 429 MET MET C . n 
C 1 275 TYR 275 430 430 TYR TYR C . n 
C 1 276 SER 276 431 431 SER SER C . n 
C 1 277 VAL 277 432 432 VAL VAL C . n 
C 1 278 ALA 278 433 433 ALA ALA C . n 
C 1 279 SER 279 434 434 SER SER C . n 
C 1 280 GLN 280 435 435 GLN GLN C . n 
C 1 281 CYS 281 436 436 CYS CYS C . n 
C 1 282 LEU 282 437 437 LEU LEU C . n 
C 1 283 HIS 283 438 438 HIS HIS C . n 
C 1 284 GLU 284 439 439 GLU GLU C . n 
C 1 285 LYS 285 440 440 LYS LYS C . n 
C 1 286 LYS 286 441 441 LYS LYS C . n 
C 1 287 ASN 287 442 442 ASN ASN C . n 
C 1 288 LYS 288 443 443 LYS LYS C . n 
C 1 289 ARG 289 444 444 ARG ARG C . n 
C 1 290 PRO 290 445 445 PRO PRO C . n 
C 1 291 ASP 291 446 446 ASP ASP C . n 
C 1 292 ILE 292 447 447 ILE ILE C . n 
C 1 293 LYS 293 448 448 LYS LYS C . n 
C 1 294 LYS 294 449 449 LYS LYS C . n 
C 1 295 VAL 295 450 450 VAL VAL C . n 
C 1 296 GLN 296 451 451 GLN GLN C . n 
C 1 297 GLN 297 452 452 GLN GLN C . n 
C 1 298 LEU 298 453 453 LEU LEU C . n 
C 1 299 LEU 299 454 454 LEU LEU C . n 
C 1 300 GLN 300 455 455 GLN GLN C . n 
C 1 301 GLU 301 456 456 GLU GLU C . n 
C 1 302 MET 302 457 457 MET MET C . n 
C 1 303 THR 303 458 458 THR THR C . n 
C 1 304 ALA 304 459 ?   ?   ?   C . n 
C 1 305 SER 305 460 ?   ?   ?   C . n 
D 1 1   GLY 1   156 ?   ?   ?   D . n 
D 1 2   ALA 2   157 ?   ?   ?   D . n 
D 1 3   MET 3   158 ?   ?   ?   D . n 
D 1 4   GLY 4   159 ?   ?   ?   D . n 
D 1 5   VAL 5   160 ?   ?   ?   D . n 
D 1 6   SER 6   161 ?   ?   ?   D . n 
D 1 7   ASP 7   162 ?   ?   ?   D . n 
D 1 8   THR 8   163 ?   ?   ?   D . n 
D 1 9   ARG 9   164 164 ARG ARG D . n 
D 1 10  PHE 10  165 165 PHE PHE D . n 
D 1 11  HIS 11  166 166 HIS HIS D . n 
D 1 12  SER 12  167 167 SER SER D . n 
D 1 13  PHE 13  168 168 PHE PHE D . n 
D 1 14  SER 14  169 169 SER SER D . n 
D 1 15  PHE 15  170 170 PHE PHE D . n 
D 1 16  TYR 16  171 171 TYR TYR D . n 
D 1 17  GLU 17  172 172 GLU GLU D . n 
D 1 18  LEU 18  173 173 LEU LEU D . n 
D 1 19  LYS 19  174 174 LYS LYS D . n 
D 1 20  ASN 20  175 175 ASN ASN D . n 
D 1 21  VAL 21  176 176 VAL VAL D . n 
D 1 22  THR 22  177 177 THR THR D . n 
D 1 23  ASN 23  178 178 ASN ASN D . n 
D 1 24  ASN 24  179 179 ASN ASN D . n 
D 1 25  PHE 25  180 180 PHE PHE D . n 
D 1 26  ASP 26  181 181 ASP ASP D . n 
D 1 27  GLU 27  182 182 GLU GLU D . n 
D 1 28  ARG 28  183 183 ARG ARG D . n 
D 1 29  PRO 29  184 184 PRO PRO D . n 
D 1 30  ILE 30  185 185 ILE ILE D . n 
D 1 31  SER 31  186 186 SER SER D . n 
D 1 32  VAL 32  187 187 VAL VAL D . n 
D 1 33  GLY 33  188 188 GLY GLY D . n 
D 1 34  GLY 34  189 189 GLY GLY D . n 
D 1 35  ASN 35  190 190 ASN ASN D . n 
D 1 36  LYS 36  191 191 LYS LYS D . n 
D 1 37  MET 37  192 192 MET MET D . n 
D 1 38  GLY 38  193 193 GLY GLY D . n 
D 1 39  GLU 39  194 194 GLU GLU D . n 
D 1 40  GLY 40  195 195 GLY GLY D . n 
D 1 41  GLY 41  196 196 GLY GLY D . n 
D 1 42  PHE 42  197 197 PHE PHE D . n 
D 1 43  GLY 43  198 198 GLY GLY D . n 
D 1 44  VAL 44  199 199 VAL VAL D . n 
D 1 45  VAL 45  200 200 VAL VAL D . n 
D 1 46  TYR 46  201 201 TYR TYR D . n 
D 1 47  LYS 47  202 202 LYS LYS D . n 
D 1 48  GLY 48  203 203 GLY GLY D . n 
D 1 49  TYR 49  204 204 TYR TYR D . n 
D 1 50  VAL 50  205 205 VAL VAL D . n 
D 1 51  ASN 51  206 206 ASN ASN D . n 
D 1 52  ASN 52  207 207 ASN ASN D . n 
D 1 53  THR 53  208 208 THR THR D . n 
D 1 54  THR 54  209 209 THR THR D . n 
D 1 55  VAL 55  210 210 VAL VAL D . n 
D 1 56  ALA 56  211 211 ALA ALA D . n 
D 1 57  VAL 57  212 212 VAL VAL D . n 
D 1 58  LYS 58  213 213 LYS LYS D . n 
D 1 59  LYS 59  214 214 LYS LYS D . n 
D 1 60  LEU 60  215 215 LEU LEU D . n 
D 1 61  ALA 61  216 216 ALA ALA D . n 
D 1 62  ALA 62  217 217 ALA ALA D . n 
D 1 63  MET 63  218 ?   ?   ?   D . n 
D 1 64  VAL 64  219 ?   ?   ?   D . n 
D 1 65  ASP 65  220 ?   ?   ?   D . n 
D 1 66  ILE 66  221 ?   ?   ?   D . n 
D 1 67  THR 67  222 ?   ?   ?   D . n 
D 1 68  THR 68  223 223 THR THR D . n 
D 1 69  GLU 69  224 224 GLU GLU D . n 
D 1 70  GLU 70  225 225 GLU GLU D . n 
D 1 71  LEU 71  226 226 LEU LEU D . n 
D 1 72  LYS 72  227 227 LYS LYS D . n 
D 1 73  GLN 73  228 228 GLN GLN D . n 
D 1 74  GLN 74  229 229 GLN GLN D . n 
D 1 75  PHE 75  230 230 PHE PHE D . n 
D 1 76  ASP 76  231 231 ASP ASP D . n 
D 1 77  GLN 77  232 232 GLN GLN D . n 
D 1 78  GLU 78  233 233 GLU GLU D . n 
D 1 79  ILE 79  234 234 ILE ILE D . n 
D 1 80  LYS 80  235 235 LYS LYS D . n 
D 1 81  VAL 81  236 236 VAL VAL D . n 
D 1 82  MET 82  237 237 MET MET D . n 
D 1 83  ALA 83  238 238 ALA ALA D . n 
D 1 84  LYS 84  239 239 LYS LYS D . n 
D 1 85  CYS 85  240 240 CYS CYS D . n 
D 1 86  GLN 86  241 241 GLN GLN D . n 
D 1 87  HIS 87  242 242 HIS HIS D . n 
D 1 88  GLU 88  243 243 GLU GLU D . n 
D 1 89  ASN 89  244 244 ASN ASN D . n 
D 1 90  LEU 90  245 245 LEU LEU D . n 
D 1 91  VAL 91  246 246 VAL VAL D . n 
D 1 92  GLU 92  247 247 GLU GLU D . n 
D 1 93  LEU 93  248 248 LEU LEU D . n 
D 1 94  LEU 94  249 249 LEU LEU D . n 
D 1 95  GLY 95  250 250 GLY GLY D . n 
D 1 96  PHE 96  251 251 PHE PHE D . n 
D 1 97  SER 97  252 252 SER SER D . n 
D 1 98  SER 98  253 253 SER SER D . n 
D 1 99  ASP 99  254 254 ASP ASP D . n 
D 1 100 GLY 100 255 255 GLY GLY D . n 
D 1 101 ASP 101 256 256 ASP ASP D . n 
D 1 102 ASP 102 257 257 ASP ASP D . n 
D 1 103 LEU 103 258 258 LEU LEU D . n 
D 1 104 CYS 104 259 259 CYS CYS D . n 
D 1 105 LEU 105 260 260 LEU LEU D . n 
D 1 106 VAL 106 261 261 VAL VAL D . n 
D 1 107 TYR 107 262 262 TYR TYR D . n 
D 1 108 VAL 108 263 263 VAL VAL D . n 
D 1 109 TYR 109 264 264 TYR TYR D . n 
D 1 110 MET 110 265 265 MET MET D . n 
D 1 111 PRO 111 266 266 PRO PRO D . n 
D 1 112 ASN 112 267 267 ASN ASN D . n 
D 1 113 GLY 113 268 268 GLY GLY D . n 
D 1 114 SER 114 269 269 SER SER D . n 
D 1 115 LEU 115 270 270 LEU LEU D . n 
D 1 116 LEU 116 271 271 LEU LEU D . n 
D 1 117 ASP 117 272 272 ASP ASP D . n 
D 1 118 ARG 118 273 273 ARG ARG D . n 
D 1 119 LEU 119 274 274 LEU LEU D . n 
D 1 120 SER 120 275 275 SER SER D . n 
D 1 121 CYS 121 276 276 CYS CYS D . n 
D 1 122 LEU 122 277 277 LEU LEU D . n 
D 1 123 ASP 123 278 278 ASP ASP D . n 
D 1 124 GLY 124 279 279 GLY GLY D . n 
D 1 125 THR 125 280 280 THR THR D . n 
D 1 126 PRO 126 281 281 PRO PRO D . n 
D 1 127 PRO 127 282 282 PRO PRO D . n 
D 1 128 LEU 128 283 283 LEU LEU D . n 
D 1 129 SER 129 284 284 SER SER D . n 
D 1 130 TRP 130 285 285 TRP TRP D . n 
D 1 131 HIS 131 286 286 HIS HIS D . n 
D 1 132 MET 132 287 287 MET MET D . n 
D 1 133 ARG 133 288 288 ARG ARG D . n 
D 1 134 CYS 134 289 289 CYS CYS D . n 
D 1 135 LYS 135 290 290 LYS LYS D . n 
D 1 136 ILE 136 291 291 ILE ILE D . n 
D 1 137 ALA 137 292 292 ALA ALA D . n 
D 1 138 GLN 138 293 293 GLN GLN D . n 
D 1 139 GLY 139 294 294 GLY GLY D . n 
D 1 140 ALA 140 295 295 ALA ALA D . n 
D 1 141 ALA 141 296 296 ALA ALA D . n 
D 1 142 ASN 142 297 297 ASN ASN D . n 
D 1 143 GLY 143 298 298 GLY GLY D . n 
D 1 144 ILE 144 299 299 ILE ILE D . n 
D 1 145 ASN 145 300 300 ASN ASN D . n 
D 1 146 PHE 146 301 301 PHE PHE D . n 
D 1 147 LEU 147 302 302 LEU LEU D . n 
D 1 148 HIS 148 303 303 HIS HIS D . n 
D 1 149 GLU 149 304 304 GLU GLU D . n 
D 1 150 ASN 150 305 305 ASN ASN D . n 
D 1 151 HIS 151 306 306 HIS HIS D . n 
D 1 152 HIS 152 307 307 HIS HIS D . n 
D 1 153 ILE 153 308 308 ILE ILE D . n 
D 1 154 HIS 154 309 309 HIS HIS D . n 
D 1 155 ARG 155 310 310 ARG ARG D . n 
D 1 156 ASP 156 311 311 ASP ASP D . n 
D 1 157 ILE 157 312 312 ILE ILE D . n 
D 1 158 LYS 158 313 313 LYS LYS D . n 
D 1 159 SER 159 314 314 SER SER D . n 
D 1 160 ALA 160 315 315 ALA ALA D . n 
D 1 161 ASN 161 316 316 ASN ASN D . n 
D 1 162 ILE 162 317 317 ILE ILE D . n 
D 1 163 LEU 163 318 318 LEU LEU D . n 
D 1 164 LEU 164 319 319 LEU LEU D . n 
D 1 165 ASP 165 320 320 ASP ASP D . n 
D 1 166 GLU 166 321 321 GLU GLU D . n 
D 1 167 ALA 167 322 322 ALA ALA D . n 
D 1 168 PHE 168 323 323 PHE PHE D . n 
D 1 169 THR 169 324 324 THR THR D . n 
D 1 170 ALA 170 325 325 ALA ALA D . n 
D 1 171 LYS 171 326 326 LYS LYS D . n 
D 1 172 ILE 172 327 327 ILE ILE D . n 
D 1 173 SER 173 328 328 SER SER D . n 
D 1 174 ASP 174 329 329 ASP ASP D . n 
D 1 175 PHE 175 330 330 PHE PHE D . n 
D 1 176 GLY 176 331 331 GLY GLY D . n 
D 1 177 LEU 177 332 332 LEU LEU D . n 
D 1 178 ALA 178 333 333 ALA ALA D . n 
D 1 179 ARG 179 334 334 ARG ARG D . n 
D 1 180 ALA 180 335 335 ALA ALA D . n 
D 1 181 SER 181 336 ?   ?   ?   D . n 
D 1 182 GLU 182 337 ?   ?   ?   D . n 
D 1 183 LYS 183 338 ?   ?   ?   D . n 
D 1 184 PHE 184 339 ?   ?   ?   D . n 
D 1 185 ALA 185 340 ?   ?   ?   D . n 
D 1 186 GLN 186 341 ?   ?   ?   D . n 
D 1 187 TPO 187 342 342 TPO TPO D . n 
D 1 188 VAL 188 343 343 VAL VAL D . n 
D 1 189 MET 189 344 344 MET MET D . n 
D 1 190 TPO 190 345 345 TPO TPO D . n 
D 1 191 SEP 191 346 346 SEP SEP D . n 
D 1 192 ARG 192 347 347 ARG ARG D . n 
D 1 193 ILE 193 348 348 ILE ILE D . n 
D 1 194 VAL 194 349 349 VAL VAL D . n 
D 1 195 GLY 195 350 350 GLY GLY D . n 
D 1 196 THR 196 351 351 THR THR D . n 
D 1 197 THR 197 352 352 THR THR D . n 
D 1 198 ALA 198 353 353 ALA ALA D . n 
D 1 199 TYR 199 354 354 TYR TYR D . n 
D 1 200 MET 200 355 355 MET MET D . n 
D 1 201 ALA 201 356 356 ALA ALA D . n 
D 1 202 PRO 202 357 357 PRO PRO D . n 
D 1 203 GLU 203 358 358 GLU GLU D . n 
D 1 204 ALA 204 359 359 ALA ALA D . n 
D 1 205 LEU 205 360 360 LEU LEU D . n 
D 1 206 ARG 206 361 361 ARG ARG D . n 
D 1 207 GLY 207 362 362 GLY GLY D . n 
D 1 208 GLU 208 363 363 GLU GLU D . n 
D 1 209 ILE 209 364 364 ILE ILE D . n 
D 1 210 THR 210 365 365 THR THR D . n 
D 1 211 PRO 211 366 366 PRO PRO D . n 
D 1 212 LYS 212 367 367 LYS LYS D . n 
D 1 213 SER 213 368 368 SER SER D . n 
D 1 214 ASP 214 369 369 ASP ASP D . n 
D 1 215 ILE 215 370 370 ILE ILE D . n 
D 1 216 TYR 216 371 371 TYR TYR D . n 
D 1 217 SER 217 372 372 SER SER D . n 
D 1 218 PHE 218 373 373 PHE PHE D . n 
D 1 219 GLY 219 374 374 GLY GLY D . n 
D 1 220 VAL 220 375 375 VAL VAL D . n 
D 1 221 VAL 221 376 376 VAL VAL D . n 
D 1 222 LEU 222 377 377 LEU LEU D . n 
D 1 223 LEU 223 378 378 LEU LEU D . n 
D 1 224 GLU 224 379 379 GLU GLU D . n 
D 1 225 ILE 225 380 380 ILE ILE D . n 
D 1 226 ILE 226 381 381 ILE ILE D . n 
D 1 227 THR 227 382 382 THR THR D . n 
D 1 228 GLY 228 383 383 GLY GLY D . n 
D 1 229 LEU 229 384 384 LEU LEU D . n 
D 1 230 PRO 230 385 385 PRO PRO D . n 
D 1 231 ALA 231 386 386 ALA ALA D . n 
D 1 232 VAL 232 387 387 VAL VAL D . n 
D 1 233 ASP 233 388 388 ASP ASP D . n 
D 1 234 GLU 234 389 389 GLU GLU D . n 
D 1 235 HIS 235 390 390 HIS HIS D . n 
D 1 236 ARG 236 391 391 ARG ARG D . n 
D 1 237 GLU 237 392 392 GLU GLU D . n 
D 1 238 PRO 238 393 393 PRO PRO D . n 
D 1 239 GLN 239 394 394 GLN GLN D . n 
D 1 240 LEU 240 395 395 LEU LEU D . n 
D 1 241 LEU 241 396 396 LEU LEU D . n 
D 1 242 LEU 242 397 397 LEU LEU D . n 
D 1 243 ASP 243 398 398 ASP ASP D . n 
D 1 244 ILE 244 399 399 ILE ILE D . n 
D 1 245 LYS 245 400 400 LYS LYS D . n 
D 1 246 GLU 246 401 401 GLU GLU D . n 
D 1 247 GLU 247 402 402 GLU GLU D . n 
D 1 248 ILE 248 403 403 ILE ILE D . n 
D 1 249 GLU 249 404 404 GLU GLU D . n 
D 1 250 ASP 250 405 405 ASP ASP D . n 
D 1 251 GLU 251 406 406 GLU GLU D . n 
D 1 252 GLU 252 407 407 GLU GLU D . n 
D 1 253 LYS 253 408 408 LYS LYS D . n 
D 1 254 THR 254 409 409 THR THR D . n 
D 1 255 ILE 255 410 410 ILE ILE D . n 
D 1 256 GLU 256 411 411 GLU GLU D . n 
D 1 257 ASP 257 412 412 ASP ASP D . n 
D 1 258 TYR 258 413 413 TYR TYR D . n 
D 1 259 ILE 259 414 414 ILE ILE D . n 
D 1 260 ASP 260 415 415 ASP ASP D . n 
D 1 261 LYS 261 416 416 LYS LYS D . n 
D 1 262 LYS 262 417 417 LYS LYS D . n 
D 1 263 MET 263 418 418 MET MET D . n 
D 1 264 ASN 264 419 419 ASN ASN D . n 
D 1 265 ASP 265 420 420 ASP ASP D . n 
D 1 266 ALA 266 421 421 ALA ALA D . n 
D 1 267 ASP 267 422 422 ASP ASP D . n 
D 1 268 SER 268 423 423 SER SER D . n 
D 1 269 THR 269 424 424 THR THR D . n 
D 1 270 SER 270 425 425 SER SER D . n 
D 1 271 VAL 271 426 426 VAL VAL D . n 
D 1 272 GLU 272 427 427 GLU GLU D . n 
D 1 273 ALA 273 428 428 ALA ALA D . n 
D 1 274 MET 274 429 429 MET MET D . n 
D 1 275 TYR 275 430 430 TYR TYR D . n 
D 1 276 SER 276 431 431 SER SER D . n 
D 1 277 VAL 277 432 432 VAL VAL D . n 
D 1 278 ALA 278 433 433 ALA ALA D . n 
D 1 279 SER 279 434 434 SER SER D . n 
D 1 280 GLN 280 435 435 GLN GLN D . n 
D 1 281 CYS 281 436 436 CYS CYS D . n 
D 1 282 LEU 282 437 437 LEU LEU D . n 
D 1 283 HIS 283 438 438 HIS HIS D . n 
D 1 284 GLU 284 439 439 GLU GLU D . n 
D 1 285 LYS 285 440 440 LYS LYS D . n 
D 1 286 LYS 286 441 441 LYS LYS D . n 
D 1 287 ASN 287 442 442 ASN ASN D . n 
D 1 288 LYS 288 443 443 LYS LYS D . n 
D 1 289 ARG 289 444 444 ARG ARG D . n 
D 1 290 PRO 290 445 445 PRO PRO D . n 
D 1 291 ASP 291 446 446 ASP ASP D . n 
D 1 292 ILE 292 447 447 ILE ILE D . n 
D 1 293 LYS 293 448 448 LYS LYS D . n 
D 1 294 LYS 294 449 449 LYS LYS D . n 
D 1 295 VAL 295 450 450 VAL VAL D . n 
D 1 296 GLN 296 451 451 GLN GLN D . n 
D 1 297 GLN 297 452 452 GLN GLN D . n 
D 1 298 LEU 298 453 453 LEU LEU D . n 
D 1 299 LEU 299 454 454 LEU LEU D . n 
D 1 300 GLN 300 455 455 GLN GLN D . n 
D 1 301 GLU 301 456 456 GLU GLU D . n 
D 1 302 MET 302 457 457 MET MET D . n 
D 1 303 THR 303 458 458 THR THR D . n 
D 1 304 ALA 304 459 ?   ?   ?   D . n 
D 1 305 SER 305 460 ?   ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZVA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZVA 
_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 
E 2 SO4 1  501 501 SO4 SO4 A . 
F 3 ZVA 1  502 502 ZVA LG1 A . 
G 2 SO4 1  501 501 SO4 SO4 B . 
H 2 SO4 1  502 502 SO4 SO4 B . 
I 3 ZVA 1  503 503 ZVA LG1 B . 
J 2 SO4 1  501 501 SO4 SO4 C . 
K 2 SO4 1  502 502 SO4 SO4 C . 
L 2 SO4 1  503 503 SO4 SO4 C . 
M 3 ZVA 1  504 504 ZVA LG1 C . 
N 2 SO4 1  501 501 SO4 SO4 D . 
O 2 SO4 1  502 502 SO4 SO4 D . 
P 3 ZVA 1  503 503 ZVA LG1 D . 
Q 4 HOH 1  601 601 HOH HOH A . 
Q 4 HOH 2  602 602 HOH HOH A . 
Q 4 HOH 3  603 603 HOH HOH A . 
Q 4 HOH 4  604 604 HOH HOH A . 
Q 4 HOH 5  605 605 HOH HOH A . 
Q 4 HOH 6  606 606 HOH HOH A . 
Q 4 HOH 7  607 607 HOH HOH A . 
Q 4 HOH 8  608 608 HOH HOH A . 
Q 4 HOH 9  609 609 HOH HOH A . 
Q 4 HOH 10 610 610 HOH HOH A . 
Q 4 HOH 11 611 611 HOH HOH A . 
Q 4 HOH 12 612 612 HOH HOH A . 
Q 4 HOH 13 613 613 HOH HOH A . 
Q 4 HOH 14 614 614 HOH HOH A . 
R 4 HOH 1  601 601 HOH HOH B . 
R 4 HOH 2  602 602 HOH HOH B . 
R 4 HOH 3  603 603 HOH HOH B . 
R 4 HOH 4  604 604 HOH HOH B . 
R 4 HOH 5  605 605 HOH HOH B . 
R 4 HOH 6  606 606 HOH HOH B . 
R 4 HOH 7  607 607 HOH HOH B . 
R 4 HOH 8  608 608 HOH HOH B . 
R 4 HOH 9  609 609 HOH HOH B . 
R 4 HOH 10 610 610 HOH HOH B . 
R 4 HOH 11 611 611 HOH HOH B . 
R 4 HOH 12 612 612 HOH HOH B . 
R 4 HOH 13 613 613 HOH HOH B . 
R 4 HOH 14 614 614 HOH HOH B . 
R 4 HOH 15 615 615 HOH HOH B . 
R 4 HOH 16 616 616 HOH HOH B . 
R 4 HOH 17 617 617 HOH HOH B . 
R 4 HOH 18 618 618 HOH HOH B . 
R 4 HOH 19 619 619 HOH HOH B . 
R 4 HOH 20 620 620 HOH HOH B . 
S 4 HOH 1  601 601 HOH HOH C . 
S 4 HOH 2  602 602 HOH HOH C . 
S 4 HOH 3  603 603 HOH HOH C . 
S 4 HOH 4  604 604 HOH HOH C . 
S 4 HOH 5  605 605 HOH HOH C . 
S 4 HOH 6  606 606 HOH HOH C . 
S 4 HOH 7  607 607 HOH HOH C . 
S 4 HOH 8  608 608 HOH HOH C . 
S 4 HOH 9  609 609 HOH HOH C . 
S 4 HOH 10 610 610 HOH HOH C . 
T 4 HOH 1  601 601 HOH HOH D . 
T 4 HOH 2  602 602 HOH HOH D . 
T 4 HOH 3  603 603 HOH HOH D . 
T 4 HOH 4  604 604 HOH HOH D . 
T 4 HOH 5  605 605 HOH HOH D . 
T 4 HOH 6  606 606 HOH HOH D . 
T 4 HOH 7  607 607 HOH HOH D . 
T 4 HOH 8  608 608 HOH HOH D . 
T 4 HOH 9  609 609 HOH HOH D . 
T 4 HOH 10 610 610 HOH HOH D . 
T 4 HOH 11 611 611 HOH HOH D . 
T 4 HOH 12 612 612 HOH HOH D . 
T 4 HOH 13 613 613 HOH HOH D . 
T 4 HOH 14 614 614 HOH HOH D . 
T 4 HOH 15 615 615 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A PHE 197 ? CG  ? A PHE 42  CG  
2   1 Y 1 A PHE 197 ? CD1 ? A PHE 42  CD1 
3   1 Y 1 A PHE 197 ? CD2 ? A PHE 42  CD2 
4   1 Y 1 A PHE 197 ? CE1 ? A PHE 42  CE1 
5   1 Y 1 A PHE 197 ? CE2 ? A PHE 42  CE2 
6   1 Y 1 A PHE 197 ? CZ  ? A PHE 42  CZ  
7   1 Y 1 A LYS 227 ? CG  ? A LYS 72  CG  
8   1 Y 1 A LYS 227 ? CD  ? A LYS 72  CD  
9   1 Y 1 A LYS 227 ? CE  ? A LYS 72  CE  
10  1 Y 1 A LYS 227 ? NZ  ? A LYS 72  NZ  
11  1 Y 1 A GLN 228 ? CG  ? A GLN 73  CG  
12  1 Y 1 A GLN 228 ? CD  ? A GLN 73  CD  
13  1 Y 1 A GLN 228 ? OE1 ? A GLN 73  OE1 
14  1 Y 1 A GLN 228 ? NE2 ? A GLN 73  NE2 
15  1 Y 1 A LYS 235 ? CG  ? A LYS 80  CG  
16  1 Y 1 A LYS 235 ? CD  ? A LYS 80  CD  
17  1 Y 1 A LYS 235 ? CE  ? A LYS 80  CE  
18  1 Y 1 A LYS 235 ? NZ  ? A LYS 80  NZ  
19  1 Y 1 A LYS 239 ? CG  ? A LYS 84  CG  
20  1 Y 1 A LYS 239 ? CD  ? A LYS 84  CD  
21  1 Y 1 A LYS 239 ? CE  ? A LYS 84  CE  
22  1 Y 1 A LYS 239 ? NZ  ? A LYS 84  NZ  
23  1 Y 1 A ASP 254 ? CG  ? A ASP 99  CG  
24  1 Y 1 A ASP 254 ? OD1 ? A ASP 99  OD1 
25  1 Y 1 A ASP 254 ? OD2 ? A ASP 99  OD2 
26  1 Y 1 A SER 336 ? OG  ? A SER 181 OG  
27  1 Y 1 A GLU 363 ? CG  ? A GLU 208 CG  
28  1 Y 1 A GLU 363 ? CD  ? A GLU 208 CD  
29  1 Y 1 A GLU 363 ? OE1 ? A GLU 208 OE1 
30  1 Y 1 A GLU 363 ? OE2 ? A GLU 208 OE2 
31  1 Y 1 A LYS 367 ? CG  ? A LYS 212 CG  
32  1 Y 1 A LYS 367 ? CD  ? A LYS 212 CD  
33  1 Y 1 A LYS 367 ? CE  ? A LYS 212 CE  
34  1 Y 1 A LYS 367 ? NZ  ? A LYS 212 NZ  
35  1 Y 1 A GLU 389 ? CG  ? A GLU 234 CG  
36  1 Y 1 A GLU 389 ? CD  ? A GLU 234 CD  
37  1 Y 1 A GLU 389 ? OE1 ? A GLU 234 OE1 
38  1 Y 1 A GLU 389 ? OE2 ? A GLU 234 OE2 
39  1 Y 1 A GLU 392 ? CG  ? A GLU 237 CG  
40  1 Y 1 A GLU 392 ? CD  ? A GLU 237 CD  
41  1 Y 1 A GLU 392 ? OE1 ? A GLU 237 OE1 
42  1 Y 1 A GLU 392 ? OE2 ? A GLU 237 OE2 
43  1 Y 1 A GLN 394 ? CG  ? A GLN 239 CG  
44  1 Y 1 A GLN 394 ? CD  ? A GLN 239 CD  
45  1 Y 1 A GLN 394 ? OE1 ? A GLN 239 OE1 
46  1 Y 1 A GLN 394 ? NE2 ? A GLN 239 NE2 
47  1 Y 1 A LYS 400 ? CG  ? A LYS 245 CG  
48  1 Y 1 A LYS 400 ? CD  ? A LYS 245 CD  
49  1 Y 1 A LYS 400 ? CE  ? A LYS 245 CE  
50  1 Y 1 A LYS 400 ? NZ  ? A LYS 245 NZ  
51  1 Y 1 A GLU 401 ? CG  ? A GLU 246 CG  
52  1 Y 1 A GLU 401 ? CD  ? A GLU 246 CD  
53  1 Y 1 A GLU 401 ? OE1 ? A GLU 246 OE1 
54  1 Y 1 A GLU 401 ? OE2 ? A GLU 246 OE2 
55  1 Y 1 A GLU 406 ? CG  ? A GLU 251 CG  
56  1 Y 1 A GLU 406 ? CD  ? A GLU 251 CD  
57  1 Y 1 A GLU 406 ? OE1 ? A GLU 251 OE1 
58  1 Y 1 A GLU 406 ? OE2 ? A GLU 251 OE2 
59  1 Y 1 A GLU 407 ? CG  ? A GLU 252 CG  
60  1 Y 1 A GLU 407 ? CD  ? A GLU 252 CD  
61  1 Y 1 A GLU 407 ? OE1 ? A GLU 252 OE1 
62  1 Y 1 A GLU 407 ? OE2 ? A GLU 252 OE2 
63  1 Y 1 A LYS 440 ? CG  ? A LYS 285 CG  
64  1 Y 1 A LYS 440 ? CD  ? A LYS 285 CD  
65  1 Y 1 A LYS 440 ? CE  ? A LYS 285 CE  
66  1 Y 1 A LYS 440 ? NZ  ? A LYS 285 NZ  
67  1 Y 1 A LYS 441 ? CG  ? A LYS 286 CG  
68  1 Y 1 A LYS 441 ? CD  ? A LYS 286 CD  
69  1 Y 1 A LYS 441 ? CE  ? A LYS 286 CE  
70  1 Y 1 A LYS 441 ? NZ  ? A LYS 286 NZ  
71  1 Y 1 A LYS 443 ? CG  ? A LYS 288 CG  
72  1 Y 1 A LYS 443 ? CD  ? A LYS 288 CD  
73  1 Y 1 A LYS 443 ? CE  ? A LYS 288 CE  
74  1 Y 1 A LYS 443 ? NZ  ? A LYS 288 NZ  
75  1 Y 1 A LYS 448 ? CG  ? A LYS 293 CG  
76  1 Y 1 A LYS 448 ? CD  ? A LYS 293 CD  
77  1 Y 1 A LYS 448 ? CE  ? A LYS 293 CE  
78  1 Y 1 A LYS 448 ? NZ  ? A LYS 293 NZ  
79  1 Y 1 A GLN 452 ? CG  ? A GLN 297 CG  
80  1 Y 1 A GLN 452 ? CD  ? A GLN 297 CD  
81  1 Y 1 A GLN 452 ? OE1 ? A GLN 297 OE1 
82  1 Y 1 A GLN 452 ? NE2 ? A GLN 297 NE2 
83  1 Y 1 A GLN 455 ? CG  ? A GLN 300 CG  
84  1 Y 1 A GLN 455 ? CD  ? A GLN 300 CD  
85  1 Y 1 A GLN 455 ? OE1 ? A GLN 300 OE1 
86  1 Y 1 A GLN 455 ? NE2 ? A GLN 300 NE2 
87  1 Y 1 B PHE 197 ? CG  ? B PHE 42  CG  
88  1 Y 1 B PHE 197 ? CD1 ? B PHE 42  CD1 
89  1 Y 1 B PHE 197 ? CD2 ? B PHE 42  CD2 
90  1 Y 1 B PHE 197 ? CE1 ? B PHE 42  CE1 
91  1 Y 1 B PHE 197 ? CE2 ? B PHE 42  CE2 
92  1 Y 1 B PHE 197 ? CZ  ? B PHE 42  CZ  
93  1 Y 1 B GLU 224 ? CG  ? B GLU 69  CG  
94  1 Y 1 B GLU 224 ? CD  ? B GLU 69  CD  
95  1 Y 1 B GLU 224 ? OE1 ? B GLU 69  OE1 
96  1 Y 1 B GLU 224 ? OE2 ? B GLU 69  OE2 
97  1 Y 1 B LYS 227 ? CG  ? B LYS 72  CG  
98  1 Y 1 B LYS 227 ? CD  ? B LYS 72  CD  
99  1 Y 1 B LYS 227 ? CE  ? B LYS 72  CE  
100 1 Y 1 B LYS 227 ? NZ  ? B LYS 72  NZ  
101 1 Y 1 B GLN 228 ? CG  ? B GLN 73  CG  
102 1 Y 1 B GLN 228 ? CD  ? B GLN 73  CD  
103 1 Y 1 B GLN 228 ? OE1 ? B GLN 73  OE1 
104 1 Y 1 B GLN 228 ? NE2 ? B GLN 73  NE2 
105 1 Y 1 B GLN 229 ? CG  ? B GLN 74  CG  
106 1 Y 1 B GLN 229 ? CD  ? B GLN 74  CD  
107 1 Y 1 B GLN 229 ? OE1 ? B GLN 74  OE1 
108 1 Y 1 B GLN 229 ? NE2 ? B GLN 74  NE2 
109 1 Y 1 B LYS 235 ? CG  ? B LYS 80  CG  
110 1 Y 1 B LYS 235 ? CD  ? B LYS 80  CD  
111 1 Y 1 B LYS 235 ? CE  ? B LYS 80  CE  
112 1 Y 1 B LYS 235 ? NZ  ? B LYS 80  NZ  
113 1 Y 1 B LYS 239 ? CG  ? B LYS 84  CG  
114 1 Y 1 B LYS 239 ? CD  ? B LYS 84  CD  
115 1 Y 1 B LYS 239 ? CE  ? B LYS 84  CE  
116 1 Y 1 B LYS 239 ? NZ  ? B LYS 84  NZ  
117 1 Y 1 B ASP 254 ? CG  ? B ASP 99  CG  
118 1 Y 1 B ASP 254 ? OD1 ? B ASP 99  OD1 
119 1 Y 1 B ASP 254 ? OD2 ? B ASP 99  OD2 
120 1 Y 1 B HIS 286 ? CG  ? B HIS 131 CG  
121 1 Y 1 B HIS 286 ? ND1 ? B HIS 131 ND1 
122 1 Y 1 B HIS 286 ? CD2 ? B HIS 131 CD2 
123 1 Y 1 B HIS 286 ? CE1 ? B HIS 131 CE1 
124 1 Y 1 B HIS 286 ? NE2 ? B HIS 131 NE2 
125 1 Y 1 B SER 336 ? OG  ? B SER 181 OG  
126 1 Y 1 B TPO 342 ? CG2 ? B TPO 187 CG2 
127 1 Y 1 B TPO 342 ? OG1 ? B TPO 187 OG1 
128 1 Y 1 B TPO 342 ? P   ? B TPO 187 P   
129 1 Y 1 B TPO 342 ? O1P ? B TPO 187 O1P 
130 1 Y 1 B TPO 342 ? O2P ? B TPO 187 O2P 
131 1 Y 1 B TPO 342 ? O3P ? B TPO 187 O3P 
132 1 Y 1 B GLU 363 ? CG  ? B GLU 208 CG  
133 1 Y 1 B GLU 363 ? CD  ? B GLU 208 CD  
134 1 Y 1 B GLU 363 ? OE1 ? B GLU 208 OE1 
135 1 Y 1 B GLU 363 ? OE2 ? B GLU 208 OE2 
136 1 Y 1 B LYS 367 ? CG  ? B LYS 212 CG  
137 1 Y 1 B LYS 367 ? CD  ? B LYS 212 CD  
138 1 Y 1 B LYS 367 ? CE  ? B LYS 212 CE  
139 1 Y 1 B LYS 367 ? NZ  ? B LYS 212 NZ  
140 1 Y 1 B GLU 389 ? CG  ? B GLU 234 CG  
141 1 Y 1 B GLU 389 ? CD  ? B GLU 234 CD  
142 1 Y 1 B GLU 389 ? OE1 ? B GLU 234 OE1 
143 1 Y 1 B GLU 389 ? OE2 ? B GLU 234 OE2 
144 1 Y 1 B GLU 392 ? CG  ? B GLU 237 CG  
145 1 Y 1 B GLU 392 ? CD  ? B GLU 237 CD  
146 1 Y 1 B GLU 392 ? OE1 ? B GLU 237 OE1 
147 1 Y 1 B GLU 392 ? OE2 ? B GLU 237 OE2 
148 1 Y 1 B GLU 401 ? CG  ? B GLU 246 CG  
149 1 Y 1 B GLU 401 ? CD  ? B GLU 246 CD  
150 1 Y 1 B GLU 401 ? OE1 ? B GLU 246 OE1 
151 1 Y 1 B GLU 401 ? OE2 ? B GLU 246 OE2 
152 1 Y 1 B GLU 406 ? CG  ? B GLU 251 CG  
153 1 Y 1 B GLU 406 ? CD  ? B GLU 251 CD  
154 1 Y 1 B GLU 406 ? OE1 ? B GLU 251 OE1 
155 1 Y 1 B GLU 406 ? OE2 ? B GLU 251 OE2 
156 1 Y 1 B GLU 407 ? CG  ? B GLU 252 CG  
157 1 Y 1 B GLU 407 ? CD  ? B GLU 252 CD  
158 1 Y 1 B GLU 407 ? OE1 ? B GLU 252 OE1 
159 1 Y 1 B GLU 407 ? OE2 ? B GLU 252 OE2 
160 1 Y 1 B LYS 440 ? CG  ? B LYS 285 CG  
161 1 Y 1 B LYS 440 ? CD  ? B LYS 285 CD  
162 1 Y 1 B LYS 440 ? CE  ? B LYS 285 CE  
163 1 Y 1 B LYS 440 ? NZ  ? B LYS 285 NZ  
164 1 Y 1 B LYS 441 ? CG  ? B LYS 286 CG  
165 1 Y 1 B LYS 441 ? CD  ? B LYS 286 CD  
166 1 Y 1 B LYS 441 ? CE  ? B LYS 286 CE  
167 1 Y 1 B LYS 441 ? NZ  ? B LYS 286 NZ  
168 1 Y 1 B LYS 443 ? CG  ? B LYS 288 CG  
169 1 Y 1 B LYS 443 ? CD  ? B LYS 288 CD  
170 1 Y 1 B LYS 443 ? CE  ? B LYS 288 CE  
171 1 Y 1 B LYS 443 ? NZ  ? B LYS 288 NZ  
172 1 Y 1 B LYS 448 ? CG  ? B LYS 293 CG  
173 1 Y 1 B LYS 448 ? CD  ? B LYS 293 CD  
174 1 Y 1 B LYS 448 ? CE  ? B LYS 293 CE  
175 1 Y 1 B LYS 448 ? NZ  ? B LYS 293 NZ  
176 1 Y 1 B GLN 455 ? CG  ? B GLN 300 CG  
177 1 Y 1 B GLN 455 ? CD  ? B GLN 300 CD  
178 1 Y 1 B GLN 455 ? OE1 ? B GLN 300 OE1 
179 1 Y 1 B GLN 455 ? NE2 ? B GLN 300 NE2 
180 1 Y 1 C TYR 171 ? CG  ? C TYR 16  CG  
181 1 Y 1 C TYR 171 ? CD1 ? C TYR 16  CD1 
182 1 Y 1 C TYR 171 ? CD2 ? C TYR 16  CD2 
183 1 Y 1 C TYR 171 ? CE1 ? C TYR 16  CE1 
184 1 Y 1 C TYR 171 ? CE2 ? C TYR 16  CE2 
185 1 Y 1 C TYR 171 ? CZ  ? C TYR 16  CZ  
186 1 Y 1 C TYR 171 ? OH  ? C TYR 16  OH  
187 1 Y 1 C PHE 197 ? CG  ? C PHE 42  CG  
188 1 Y 1 C PHE 197 ? CD1 ? C PHE 42  CD1 
189 1 Y 1 C PHE 197 ? CD2 ? C PHE 42  CD2 
190 1 Y 1 C PHE 197 ? CE1 ? C PHE 42  CE1 
191 1 Y 1 C PHE 197 ? CE2 ? C PHE 42  CE2 
192 1 Y 1 C PHE 197 ? CZ  ? C PHE 42  CZ  
193 1 Y 1 C GLU 224 ? CG  ? C GLU 69  CG  
194 1 Y 1 C GLU 224 ? CD  ? C GLU 69  CD  
195 1 Y 1 C GLU 224 ? OE1 ? C GLU 69  OE1 
196 1 Y 1 C GLU 224 ? OE2 ? C GLU 69  OE2 
197 1 Y 1 C LYS 227 ? CG  ? C LYS 72  CG  
198 1 Y 1 C LYS 227 ? CD  ? C LYS 72  CD  
199 1 Y 1 C LYS 227 ? CE  ? C LYS 72  CE  
200 1 Y 1 C LYS 227 ? NZ  ? C LYS 72  NZ  
201 1 Y 1 C GLN 228 ? CG  ? C GLN 73  CG  
202 1 Y 1 C GLN 228 ? CD  ? C GLN 73  CD  
203 1 Y 1 C GLN 228 ? OE1 ? C GLN 73  OE1 
204 1 Y 1 C GLN 228 ? NE2 ? C GLN 73  NE2 
205 1 Y 1 C LYS 235 ? CG  ? C LYS 80  CG  
206 1 Y 1 C LYS 235 ? CD  ? C LYS 80  CD  
207 1 Y 1 C LYS 235 ? CE  ? C LYS 80  CE  
208 1 Y 1 C LYS 235 ? NZ  ? C LYS 80  NZ  
209 1 Y 1 C LYS 239 ? CG  ? C LYS 84  CG  
210 1 Y 1 C LYS 239 ? CD  ? C LYS 84  CD  
211 1 Y 1 C LYS 239 ? CE  ? C LYS 84  CE  
212 1 Y 1 C LYS 239 ? NZ  ? C LYS 84  NZ  
213 1 Y 1 C ASP 254 ? CG  ? C ASP 99  CG  
214 1 Y 1 C ASP 254 ? OD1 ? C ASP 99  OD1 
215 1 Y 1 C ASP 254 ? OD2 ? C ASP 99  OD2 
216 1 Y 1 C SEP 346 ? OG  ? C SEP 191 OG  
217 1 Y 1 C SEP 346 ? P   ? C SEP 191 P   
218 1 Y 1 C SEP 346 ? O1P ? C SEP 191 O1P 
219 1 Y 1 C SEP 346 ? O2P ? C SEP 191 O2P 
220 1 Y 1 C SEP 346 ? O3P ? C SEP 191 O3P 
221 1 Y 1 C LYS 367 ? CG  ? C LYS 212 CG  
222 1 Y 1 C LYS 367 ? CD  ? C LYS 212 CD  
223 1 Y 1 C LYS 367 ? CE  ? C LYS 212 CE  
224 1 Y 1 C LYS 367 ? NZ  ? C LYS 212 NZ  
225 1 Y 1 C GLU 389 ? CG  ? C GLU 234 CG  
226 1 Y 1 C GLU 389 ? CD  ? C GLU 234 CD  
227 1 Y 1 C GLU 389 ? OE1 ? C GLU 234 OE1 
228 1 Y 1 C GLU 389 ? OE2 ? C GLU 234 OE2 
229 1 Y 1 C GLU 392 ? CG  ? C GLU 237 CG  
230 1 Y 1 C GLU 392 ? CD  ? C GLU 237 CD  
231 1 Y 1 C GLU 392 ? OE1 ? C GLU 237 OE1 
232 1 Y 1 C GLU 392 ? OE2 ? C GLU 237 OE2 
233 1 Y 1 C GLU 401 ? CG  ? C GLU 246 CG  
234 1 Y 1 C GLU 401 ? CD  ? C GLU 246 CD  
235 1 Y 1 C GLU 401 ? OE1 ? C GLU 246 OE1 
236 1 Y 1 C GLU 401 ? OE2 ? C GLU 246 OE2 
237 1 Y 1 C GLU 406 ? CG  ? C GLU 251 CG  
238 1 Y 1 C GLU 406 ? CD  ? C GLU 251 CD  
239 1 Y 1 C GLU 406 ? OE1 ? C GLU 251 OE1 
240 1 Y 1 C GLU 406 ? OE2 ? C GLU 251 OE2 
241 1 Y 1 C GLU 407 ? CG  ? C GLU 252 CG  
242 1 Y 1 C GLU 407 ? CD  ? C GLU 252 CD  
243 1 Y 1 C GLU 407 ? OE1 ? C GLU 252 OE1 
244 1 Y 1 C GLU 407 ? OE2 ? C GLU 252 OE2 
245 1 Y 1 C LYS 440 ? CG  ? C LYS 285 CG  
246 1 Y 1 C LYS 440 ? CD  ? C LYS 285 CD  
247 1 Y 1 C LYS 440 ? CE  ? C LYS 285 CE  
248 1 Y 1 C LYS 440 ? NZ  ? C LYS 285 NZ  
249 1 Y 1 C LYS 441 ? CG  ? C LYS 286 CG  
250 1 Y 1 C LYS 441 ? CD  ? C LYS 286 CD  
251 1 Y 1 C LYS 441 ? CE  ? C LYS 286 CE  
252 1 Y 1 C LYS 441 ? NZ  ? C LYS 286 NZ  
253 1 Y 1 C LYS 443 ? CG  ? C LYS 288 CG  
254 1 Y 1 C LYS 443 ? CD  ? C LYS 288 CD  
255 1 Y 1 C LYS 443 ? CE  ? C LYS 288 CE  
256 1 Y 1 C LYS 443 ? NZ  ? C LYS 288 NZ  
257 1 Y 1 C LYS 448 ? CG  ? C LYS 293 CG  
258 1 Y 1 C LYS 448 ? CD  ? C LYS 293 CD  
259 1 Y 1 C LYS 448 ? CE  ? C LYS 293 CE  
260 1 Y 1 C LYS 448 ? NZ  ? C LYS 293 NZ  
261 1 Y 1 C GLN 452 ? CG  ? C GLN 297 CG  
262 1 Y 1 C GLN 452 ? CD  ? C GLN 297 CD  
263 1 Y 1 C GLN 452 ? OE1 ? C GLN 297 OE1 
264 1 Y 1 C GLN 452 ? NE2 ? C GLN 297 NE2 
265 1 Y 1 C GLN 455 ? CG  ? C GLN 300 CG  
266 1 Y 1 C GLN 455 ? CD  ? C GLN 300 CD  
267 1 Y 1 C GLN 455 ? OE1 ? C GLN 300 OE1 
268 1 Y 1 C GLN 455 ? NE2 ? C GLN 300 NE2 
269 1 Y 1 D PHE 197 ? CG  ? D PHE 42  CG  
270 1 Y 1 D PHE 197 ? CD1 ? D PHE 42  CD1 
271 1 Y 1 D PHE 197 ? CD2 ? D PHE 42  CD2 
272 1 Y 1 D PHE 197 ? CE1 ? D PHE 42  CE1 
273 1 Y 1 D PHE 197 ? CE2 ? D PHE 42  CE2 
274 1 Y 1 D PHE 197 ? CZ  ? D PHE 42  CZ  
275 1 Y 1 D GLU 224 ? CG  ? D GLU 69  CG  
276 1 Y 1 D GLU 224 ? CD  ? D GLU 69  CD  
277 1 Y 1 D GLU 224 ? OE1 ? D GLU 69  OE1 
278 1 Y 1 D GLU 224 ? OE2 ? D GLU 69  OE2 
279 1 Y 1 D LYS 227 ? CG  ? D LYS 72  CG  
280 1 Y 1 D LYS 227 ? CD  ? D LYS 72  CD  
281 1 Y 1 D LYS 227 ? CE  ? D LYS 72  CE  
282 1 Y 1 D LYS 227 ? NZ  ? D LYS 72  NZ  
283 1 Y 1 D GLN 228 ? CG  ? D GLN 73  CG  
284 1 Y 1 D GLN 228 ? CD  ? D GLN 73  CD  
285 1 Y 1 D GLN 228 ? OE1 ? D GLN 73  OE1 
286 1 Y 1 D GLN 228 ? NE2 ? D GLN 73  NE2 
287 1 Y 1 D GLN 232 ? CG  ? D GLN 77  CG  
288 1 Y 1 D GLN 232 ? CD  ? D GLN 77  CD  
289 1 Y 1 D GLN 232 ? OE1 ? D GLN 77  OE1 
290 1 Y 1 D GLN 232 ? NE2 ? D GLN 77  NE2 
291 1 Y 1 D LYS 235 ? CG  ? D LYS 80  CG  
292 1 Y 1 D LYS 235 ? CD  ? D LYS 80  CD  
293 1 Y 1 D LYS 235 ? CE  ? D LYS 80  CE  
294 1 Y 1 D LYS 235 ? NZ  ? D LYS 80  NZ  
295 1 Y 1 D LYS 239 ? CG  ? D LYS 84  CG  
296 1 Y 1 D LYS 239 ? CD  ? D LYS 84  CD  
297 1 Y 1 D LYS 239 ? CE  ? D LYS 84  CE  
298 1 Y 1 D LYS 239 ? NZ  ? D LYS 84  NZ  
299 1 Y 1 D ASP 254 ? CG  ? D ASP 99  CG  
300 1 Y 1 D ASP 254 ? OD1 ? D ASP 99  OD1 
301 1 Y 1 D ASP 254 ? OD2 ? D ASP 99  OD2 
302 1 Y 1 D LYS 367 ? CG  ? D LYS 212 CG  
303 1 Y 1 D LYS 367 ? CD  ? D LYS 212 CD  
304 1 Y 1 D LYS 367 ? CE  ? D LYS 212 CE  
305 1 Y 1 D LYS 367 ? NZ  ? D LYS 212 NZ  
306 1 Y 1 D GLU 389 ? CG  ? D GLU 234 CG  
307 1 Y 1 D GLU 389 ? CD  ? D GLU 234 CD  
308 1 Y 1 D GLU 389 ? OE1 ? D GLU 234 OE1 
309 1 Y 1 D GLU 389 ? OE2 ? D GLU 234 OE2 
310 1 Y 1 D GLU 392 ? CG  ? D GLU 237 CG  
311 1 Y 1 D GLU 392 ? CD  ? D GLU 237 CD  
312 1 Y 1 D GLU 392 ? OE1 ? D GLU 237 OE1 
313 1 Y 1 D GLU 392 ? OE2 ? D GLU 237 OE2 
314 1 Y 1 D GLU 401 ? CG  ? D GLU 246 CG  
315 1 Y 1 D GLU 401 ? CD  ? D GLU 246 CD  
316 1 Y 1 D GLU 401 ? OE1 ? D GLU 246 OE1 
317 1 Y 1 D GLU 401 ? OE2 ? D GLU 246 OE2 
318 1 Y 1 D GLU 406 ? CG  ? D GLU 251 CG  
319 1 Y 1 D GLU 406 ? CD  ? D GLU 251 CD  
320 1 Y 1 D GLU 406 ? OE1 ? D GLU 251 OE1 
321 1 Y 1 D GLU 406 ? OE2 ? D GLU 251 OE2 
322 1 Y 1 D GLU 407 ? CG  ? D GLU 252 CG  
323 1 Y 1 D GLU 407 ? CD  ? D GLU 252 CD  
324 1 Y 1 D GLU 407 ? OE1 ? D GLU 252 OE1 
325 1 Y 1 D GLU 407 ? OE2 ? D GLU 252 OE2 
326 1 Y 1 D LYS 440 ? CG  ? D LYS 285 CG  
327 1 Y 1 D LYS 440 ? CD  ? D LYS 285 CD  
328 1 Y 1 D LYS 440 ? CE  ? D LYS 285 CE  
329 1 Y 1 D LYS 440 ? NZ  ? D LYS 285 NZ  
330 1 Y 1 D LYS 441 ? CG  ? D LYS 286 CG  
331 1 Y 1 D LYS 441 ? CD  ? D LYS 286 CD  
332 1 Y 1 D LYS 441 ? CE  ? D LYS 286 CE  
333 1 Y 1 D LYS 441 ? NZ  ? D LYS 286 NZ  
334 1 Y 1 D LYS 443 ? CG  ? D LYS 288 CG  
335 1 Y 1 D LYS 443 ? CD  ? D LYS 288 CD  
336 1 Y 1 D LYS 443 ? CE  ? D LYS 288 CE  
337 1 Y 1 D LYS 443 ? NZ  ? D LYS 288 NZ  
338 1 Y 1 D LYS 448 ? CG  ? D LYS 293 CG  
339 1 Y 1 D LYS 448 ? CD  ? D LYS 293 CD  
340 1 Y 1 D LYS 448 ? CE  ? D LYS 293 CE  
341 1 Y 1 D LYS 448 ? NZ  ? D LYS 293 NZ  
342 1 Y 1 D GLN 452 ? CG  ? D GLN 297 CG  
343 1 Y 1 D GLN 452 ? CD  ? D GLN 297 CD  
344 1 Y 1 D GLN 452 ? OE1 ? D GLN 297 OE1 
345 1 Y 1 D GLN 452 ? NE2 ? D GLN 297 NE2 
346 1 Y 1 D GLN 455 ? CG  ? D GLN 300 CG  
347 1 Y 1 D GLN 455 ? CD  ? D GLN 300 CD  
348 1 Y 1 D GLN 455 ? OE1 ? D GLN 300 OE1 
349 1 Y 1 D GLN 455 ? NE2 ? D GLN 300 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? .      1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER    ? ? ? 2.11.1 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000  ? ? ? .      3 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   126.60 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8SCW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     135.286 
_cell.length_a_esd                 ? 
_cell.length_b                     140.394 
_cell.length_b_esd                 ? 
_cell.length_c                     85.915 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         8SCW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8SCW 
_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             2.39 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.51 
_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    '2.6 to 2.9 M ammonium sulphate in 25 mM HEPES pH 6.4 to 7.5 at 293K' 
_exptl_crystal_grow.pdbx_pH_range   6.4-7.5 
_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                         'RAYONIX MX-300' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-03-03 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 22-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   22-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8SCW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.76 
_reflns.d_resolution_low                               50.00 
_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                                     33116 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.1 
_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                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.101 
_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                                    2.76 
_reflns_shell.d_res_low                                     2.86 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3359 
_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                               3.7 
_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                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.551 
_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]                            -7.37250 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -16.16460 
_refine.aniso_B[2][2]                            27.51210 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -20.13960 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               59.07 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.875 
_refine.correlation_coeff_Fo_to_Fc_free          0.852 
_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                                 8SCW 
_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                            2.76 
_refine.ls_d_res_low                             36.68 
_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                     33104 
_refine.ls_number_reflns_R_free                  1676 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.9 
_refine.ls_percent_reflns_R_free                 5.060 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.197 
_refine.ls_R_factor_R_free                       0.238 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.195 
_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                          0.000 
_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   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.337 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        8SCW 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.341 
_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                       2.76 
_refine_hist.d_res_low                        36.68 
_refine_hist.number_atoms_solvent             59 
_refine_hist.number_atoms_total               8884 
_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        8661 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         164 
_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' ? 0.010 ? 8967  ? t_bond_d                  2.000  HARMONIC     
'X-RAY DIFFRACTION' ? 1.17  ? 12186 ? t_angle_deg               2.000  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 3025  ? t_dihedral_angle_d        2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_incorr_chiral_ct        ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_pseud_angle             ?      ?            
'X-RAY DIFFRACTION' ? ?     ? 225   ? t_trig_c_planes           2.000  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1398  ? t_gen_planes              5.000  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 8967  ? t_it                      20.000 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_nbd                     ?      ?            
'X-RAY DIFFRACTION' ? 2.62  ? ?     ? t_omega_torsion           ?      ?            
'X-RAY DIFFRACTION' ? 20.20 ? ?     ? t_other_torsion           ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_improper_torsion        ?      ?            
'X-RAY DIFFRACTION' ? ?     ? 1205  ? t_chiral_improper_torsion 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_sum_occupancies         ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_distance        ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_angle           ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_torsion         ?      ?            
'X-RAY DIFFRACTION' ? ?     ? 10415 ? t_ideal_dist_contact      4.000  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.76 
_refine_ls_shell.d_res_low                        2.83 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             122 
_refine_ls_shell.number_reflns_R_work             2485 
_refine_ls_shell.percent_reflns_obs               98.85 
_refine_ls_shell.percent_reflns_R_free            4.68 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2400 
_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                  0.2872 
# 
_struct.entry_id                     8SCW 
_struct.title                        
;Crystal structure of IRAK4-HSA complexed with BMS-986147; 6-{5-CYANO-1H-PYRAZOLO[3,4-B]PYRIDIN-1-YL}-N-[(2R)-2-FLUORROXY-3-METHYLBUTYL]-4-[(PROPAN-2-YL)AMINO]PYRIDINE-3-CARBOXAMIDE
;
_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        8SCW 
_struct_keywords.text            'kinase, IRAK4, ligand, TRANSFERASE-TRANSFERASE INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'TRANSFERASE/TRANSFERASE INHIBITOR' 
# 
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 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 3 ? 
N N N 2 ? 
O N N 2 ? 
P N N 3 ? 
Q N N 4 ? 
R N N 4 ? 
S N N 4 ? 
T N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    IRAK4_HUMAN 
_struct_ref.pdbx_db_accession          Q9NWZ3 
_struct_ref.pdbx_db_isoform            Q9NWZ3-2 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIKVMAK
CQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANILL
DEAFTAKISDFGLARASEKFAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQLLLDI
KEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS
;
_struct_ref.pdbx_align_begin           36 
# 
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 8SCW A 5 ? 305 ? Q9NWZ3 36 ? 336 ? 160 460 
2 1 8SCW B 5 ? 305 ? Q9NWZ3 36 ? 336 ? 160 460 
3 1 8SCW C 5 ? 305 ? Q9NWZ3 36 ? 336 ? 160 460 
4 1 8SCW D 5 ? 305 ? Q9NWZ3 36 ? 336 ? 160 460 
# 
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 8SCW GLY A 1 ? UNP Q9NWZ3 ? ? 'expression tag' 156 1  
1 8SCW ALA A 2 ? UNP Q9NWZ3 ? ? 'expression tag' 157 2  
1 8SCW MET A 3 ? UNP Q9NWZ3 ? ? 'expression tag' 158 3  
1 8SCW GLY A 4 ? UNP Q9NWZ3 ? ? 'expression tag' 159 4  
2 8SCW GLY B 1 ? UNP Q9NWZ3 ? ? 'expression tag' 156 5  
2 8SCW ALA B 2 ? UNP Q9NWZ3 ? ? 'expression tag' 157 6  
2 8SCW MET B 3 ? UNP Q9NWZ3 ? ? 'expression tag' 158 7  
2 8SCW GLY B 4 ? UNP Q9NWZ3 ? ? 'expression tag' 159 8  
3 8SCW GLY C 1 ? UNP Q9NWZ3 ? ? 'expression tag' 156 9  
3 8SCW ALA C 2 ? UNP Q9NWZ3 ? ? 'expression tag' 157 10 
3 8SCW MET C 3 ? UNP Q9NWZ3 ? ? 'expression tag' 158 11 
3 8SCW GLY C 4 ? UNP Q9NWZ3 ? ? 'expression tag' 159 12 
4 8SCW GLY D 1 ? UNP Q9NWZ3 ? ? 'expression tag' 156 13 
4 8SCW ALA D 2 ? UNP Q9NWZ3 ? ? 'expression tag' 157 14 
4 8SCW MET D 3 ? UNP Q9NWZ3 ? ? 'expression tag' 158 15 
4 8SCW GLY D 4 ? UNP Q9NWZ3 ? ? 'expression tag' 159 16 
# 
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 
3 author_defined_assembly ? monomeric 1 
4 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,E,F,Q     
2 1 B,G,H,I,R   
3 1 C,J,K,L,M,S 
4 1 D,N,O,P,T   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 14  ? THR A 22  ? SER A 169 THR A 177 1 ? 9  
HELX_P HELX_P2  AA2 PRO A 29  ? GLY A 33  ? PRO A 184 GLY A 188 5 ? 5  
HELX_P HELX_P3  AA3 THR A 68  ? CYS A 85  ? THR A 223 CYS A 240 1 ? 18 
HELX_P HELX_P4  AA4 SER A 114 ? CYS A 121 ? SER A 269 CYS A 276 1 ? 8  
HELX_P HELX_P5  AA5 LEU A 122 ? THR A 125 ? LEU A 277 THR A 280 5 ? 4  
HELX_P HELX_P6  AA6 SER A 129 ? ASN A 150 ? SER A 284 ASN A 305 1 ? 22 
HELX_P HELX_P7  AA7 LYS A 158 ? ALA A 160 ? LYS A 313 ALA A 315 5 ? 3  
HELX_P HELX_P8  AA8 ALA A 201 ? GLY A 207 ? ALA A 356 GLY A 362 1 ? 7  
HELX_P HELX_P9  AA9 THR A 210 ? GLY A 228 ? THR A 365 GLY A 383 1 ? 19 
HELX_P HELX_P10 AB1 LEU A 241 ? ASP A 250 ? LEU A 396 ASP A 405 1 ? 10 
HELX_P HELX_P11 AB2 THR A 254 ? TYR A 258 ? THR A 409 TYR A 413 5 ? 5  
HELX_P HELX_P12 AB3 ASP A 267 ? LEU A 282 ? ASP A 422 LEU A 437 1 ? 16 
HELX_P HELX_P13 AB4 LYS A 285 ? ARG A 289 ? LYS A 440 ARG A 444 5 ? 5  
HELX_P HELX_P14 AB5 ASP A 291 ? THR A 303 ? ASP A 446 THR A 458 1 ? 13 
HELX_P HELX_P15 AB6 SER B 14  ? THR B 22  ? SER B 169 THR B 177 1 ? 9  
HELX_P HELX_P16 AB7 PRO B 29  ? GLY B 33  ? PRO B 184 GLY B 188 5 ? 5  
HELX_P HELX_P17 AB8 THR B 68  ? CYS B 85  ? THR B 223 CYS B 240 1 ? 18 
HELX_P HELX_P18 AB9 SER B 114 ? SER B 120 ? SER B 269 SER B 275 1 ? 7  
HELX_P HELX_P19 AC1 CYS B 121 ? THR B 125 ? CYS B 276 THR B 280 5 ? 5  
HELX_P HELX_P20 AC2 SER B 129 ? ASN B 150 ? SER B 284 ASN B 305 1 ? 22 
HELX_P HELX_P21 AC3 LYS B 158 ? ALA B 160 ? LYS B 313 ALA B 315 5 ? 3  
HELX_P HELX_P22 AC4 ALA B 201 ? ARG B 206 ? ALA B 356 ARG B 361 1 ? 6  
HELX_P HELX_P23 AC5 THR B 210 ? GLY B 228 ? THR B 365 GLY B 383 1 ? 19 
HELX_P HELX_P24 AC6 LEU B 241 ? ASP B 250 ? LEU B 396 ASP B 405 1 ? 10 
HELX_P HELX_P25 AC7 THR B 254 ? TYR B 258 ? THR B 409 TYR B 413 5 ? 5  
HELX_P HELX_P26 AC8 ASP B 267 ? LEU B 282 ? ASP B 422 LEU B 437 1 ? 16 
HELX_P HELX_P27 AC9 LYS B 285 ? ARG B 289 ? LYS B 440 ARG B 444 5 ? 5  
HELX_P HELX_P28 AD1 ASP B 291 ? MET B 302 ? ASP B 446 MET B 457 1 ? 12 
HELX_P HELX_P29 AD2 SER C 14  ? THR C 22  ? SER C 169 THR C 177 1 ? 9  
HELX_P HELX_P30 AD3 PRO C 29  ? GLY C 33  ? PRO C 184 GLY C 188 5 ? 5  
HELX_P HELX_P31 AD4 GLU C 69  ? CYS C 85  ? GLU C 224 CYS C 240 1 ? 17 
HELX_P HELX_P32 AD5 SER C 114 ? CYS C 121 ? SER C 269 CYS C 276 1 ? 8  
HELX_P HELX_P33 AD6 LEU C 122 ? THR C 125 ? LEU C 277 THR C 280 5 ? 4  
HELX_P HELX_P34 AD7 SER C 129 ? ASN C 150 ? SER C 284 ASN C 305 1 ? 22 
HELX_P HELX_P35 AD8 LYS C 158 ? ALA C 160 ? LYS C 313 ALA C 315 5 ? 3  
HELX_P HELX_P36 AD9 ALA C 201 ? ARG C 206 ? ALA C 356 ARG C 361 1 ? 6  
HELX_P HELX_P37 AE1 THR C 210 ? GLY C 228 ? THR C 365 GLY C 383 1 ? 19 
HELX_P HELX_P38 AE2 LEU C 241 ? ASP C 250 ? LEU C 396 ASP C 405 1 ? 10 
HELX_P HELX_P39 AE3 THR C 254 ? TYR C 258 ? THR C 409 TYR C 413 5 ? 5  
HELX_P HELX_P40 AE4 ASP C 267 ? LEU C 282 ? ASP C 422 LEU C 437 1 ? 16 
HELX_P HELX_P41 AE5 LYS C 285 ? ARG C 289 ? LYS C 440 ARG C 444 5 ? 5  
HELX_P HELX_P42 AE6 ASP C 291 ? MET C 302 ? ASP C 446 MET C 457 1 ? 12 
HELX_P HELX_P43 AE7 SER D 14  ? THR D 22  ? SER D 169 THR D 177 1 ? 9  
HELX_P HELX_P44 AE8 PRO D 29  ? GLY D 33  ? PRO D 184 GLY D 188 5 ? 5  
HELX_P HELX_P45 AE9 GLU D 69  ? CYS D 85  ? GLU D 224 CYS D 240 1 ? 17 
HELX_P HELX_P46 AF1 SER D 114 ? CYS D 121 ? SER D 269 CYS D 276 1 ? 8  
HELX_P HELX_P47 AF2 LEU D 122 ? THR D 125 ? LEU D 277 THR D 280 5 ? 4  
HELX_P HELX_P48 AF3 SER D 129 ? ASN D 150 ? SER D 284 ASN D 305 1 ? 22 
HELX_P HELX_P49 AF4 LYS D 158 ? ALA D 160 ? LYS D 313 ALA D 315 5 ? 3  
HELX_P HELX_P50 AF5 ALA D 201 ? ARG D 206 ? ALA D 356 ARG D 361 1 ? 6  
HELX_P HELX_P51 AF6 THR D 210 ? GLY D 228 ? THR D 365 GLY D 383 1 ? 19 
HELX_P HELX_P52 AF7 LEU D 241 ? ASP D 250 ? LEU D 396 ASP D 405 1 ? 10 
HELX_P HELX_P53 AF8 THR D 254 ? TYR D 258 ? THR D 409 TYR D 413 5 ? 5  
HELX_P HELX_P54 AF9 ASP D 267 ? LEU D 282 ? ASP D 422 LEU D 437 1 ? 16 
HELX_P HELX_P55 AG1 LYS D 285 ? ARG D 289 ? LYS D 440 ARG D 444 5 ? 5  
HELX_P HELX_P56 AG2 ASP D 291 ? THR D 303 ? ASP D 446 THR D 458 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? A TPO 187 C ? ? ? 1_555 A VAL 188 N ? ? A TPO 342 A VAL 343 1_555 ? ? ? ? ? ? ? 1.347 ? ? 
covale2  covale both ? A MET 189 C ? ? ? 1_555 A TPO 190 N ? ? A MET 344 A TPO 345 1_555 ? ? ? ? ? ? ? 1.347 ? ? 
covale3  covale both ? A TPO 190 C ? ? ? 1_555 A SEP 191 N ? ? A TPO 345 A SEP 346 1_555 ? ? ? ? ? ? ? 1.350 ? ? 
covale4  covale both ? A SEP 191 C ? ? ? 1_555 A ARG 192 N ? ? A SEP 346 A ARG 347 1_555 ? ? ? ? ? ? ? 1.355 ? ? 
covale5  covale both ? B TPO 187 C ? ? ? 1_555 B VAL 188 N ? ? B TPO 342 B VAL 343 1_555 ? ? ? ? ? ? ? 1.351 ? ? 
covale6  covale both ? B MET 189 C ? ? ? 1_555 B TPO 190 N ? ? B MET 344 B TPO 345 1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale7  covale both ? B TPO 190 C ? ? ? 1_555 B SEP 191 N ? ? B TPO 345 B SEP 346 1_555 ? ? ? ? ? ? ? 1.350 ? ? 
covale8  covale both ? B SEP 191 C ? ? ? 1_555 B ARG 192 N ? ? B SEP 346 B ARG 347 1_555 ? ? ? ? ? ? ? 1.354 ? ? 
covale9  covale both ? C TPO 187 C ? ? ? 1_555 C VAL 188 N ? ? C TPO 342 C VAL 343 1_555 ? ? ? ? ? ? ? 1.348 ? ? 
covale10 covale both ? C MET 189 C ? ? ? 1_555 C TPO 190 N ? ? C MET 344 C TPO 345 1_555 ? ? ? ? ? ? ? 1.343 ? ? 
covale11 covale both ? C TPO 190 C ? ? ? 1_555 C SEP 191 N ? ? C TPO 345 C SEP 346 1_555 ? ? ? ? ? ? ? 1.349 ? ? 
covale12 covale both ? C SEP 191 C ? ? ? 1_555 C ARG 192 N ? ? C SEP 346 C ARG 347 1_555 ? ? ? ? ? ? ? 1.353 ? ? 
covale13 covale both ? D TPO 187 C ? ? ? 1_555 D VAL 188 N ? ? D TPO 342 D VAL 343 1_555 ? ? ? ? ? ? ? 1.347 ? ? 
covale14 covale both ? D MET 189 C ? ? ? 1_555 D TPO 190 N ? ? D MET 344 D TPO 345 1_555 ? ? ? ? ? ? ? 1.346 ? ? 
covale15 covale both ? D TPO 190 C ? ? ? 1_555 D SEP 191 N ? ? D TPO 345 D SEP 346 1_555 ? ? ? ? ? ? ? 1.347 ? ? 
covale16 covale both ? D SEP 191 C ? ? ? 1_555 D ARG 192 N ? ? D SEP 346 D ARG 347 1_555 ? ? ? ? ? ? ? 1.359 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  TPO A 187 ? . . . . TPO A 342 ? 1_555 . . . . . . . THR 1 TPO Phosphorylation 'Named protein modification' 
2  TPO A 190 ? . . . . TPO A 345 ? 1_555 . . . . . . . THR 1 TPO Phosphorylation 'Named protein modification' 
3  SEP A 191 ? . . . . SEP A 346 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
4  TPO B 187 ? . . . . TPO B 342 ? 1_555 . . . . . . . THR 1 TPO Phosphorylation 'Named protein modification' 
5  TPO B 190 ? . . . . TPO B 345 ? 1_555 . . . . . . . THR 1 TPO Phosphorylation 'Named protein modification' 
6  SEP B 191 ? . . . . SEP B 346 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
7  TPO C 187 ? . . . . TPO C 342 ? 1_555 . . . . . . . THR 1 TPO Phosphorylation 'Named protein modification' 
8  TPO C 190 ? . . . . TPO C 345 ? 1_555 . . . . . . . THR 1 TPO Phosphorylation 'Named protein modification' 
9  SEP C 191 ? . . . . SEP C 346 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
10 TPO D 187 ? . . . . TPO D 342 ? 1_555 . . . . . . . THR 1 TPO Phosphorylation 'Named protein modification' 
11 TPO D 190 ? . . . . TPO D 345 ? 1_555 . . . . . . . THR 1 TPO Phosphorylation 'Named protein modification' 
12 SEP D 191 ? . . . . SEP D 346 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 237 A . ? GLU 392 A PRO 238 A ? PRO 393 A 1 0.50 
2 GLU 237 B . ? GLU 392 B PRO 238 B ? PRO 393 B 1 2.26 
3 GLU 237 C . ? GLU 392 C PRO 238 C ? PRO 393 C 1 1.86 
4 GLU 237 D . ? GLU 392 D PRO 238 D ? PRO 393 D 1 1.84 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 6 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 6 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 6 ? 
AB2 ? 2 ? 
AB3 ? 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 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 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 HIS A 11  ? SER A 12  ? HIS A 166 SER A 167 
AA1 2 LEU A 93  ? SER A 97  ? LEU A 248 SER A 252 
AA1 3 CYS A 104 ? VAL A 108 ? CYS A 259 VAL A 263 
AA1 4 THR A 53  ? LEU A 60  ? THR A 208 LEU A 215 
AA1 5 GLY A 43  ? VAL A 50  ? GLY A 198 VAL A 205 
AA1 6 LYS A 36  ? GLU A 39  ? LYS A 191 GLU A 194 
AA2 1 ILE A 162 ? LEU A 164 ? ILE A 317 LEU A 319 
AA2 2 ALA A 170 ? ILE A 172 ? ALA A 325 ILE A 327 
AA3 1 VAL A 188 ? MET A 189 ? VAL A 343 MET A 344 
AA3 2 GLU A 208 ? ILE A 209 ? GLU A 363 ILE A 364 
AA4 1 HIS B 11  ? SER B 12  ? HIS B 166 SER B 167 
AA4 2 LEU B 93  ? SER B 97  ? LEU B 248 SER B 252 
AA4 3 CYS B 104 ? VAL B 108 ? CYS B 259 VAL B 263 
AA4 4 THR B 53  ? LEU B 60  ? THR B 208 LEU B 215 
AA4 5 GLY B 43  ? VAL B 50  ? GLY B 198 VAL B 205 
AA4 6 LYS B 36  ? GLU B 39  ? LYS B 191 GLU B 194 
AA5 1 HIS B 152 ? ILE B 153 ? HIS B 307 ILE B 308 
AA5 2 ARG B 179 ? ALA B 180 ? ARG B 334 ALA B 335 
AA6 1 ILE B 162 ? LEU B 164 ? ILE B 317 LEU B 319 
AA6 2 ALA B 170 ? ILE B 172 ? ALA B 325 ILE B 327 
AA7 1 HIS C 11  ? SER C 12  ? HIS C 166 SER C 167 
AA7 2 LEU C 93  ? SER C 97  ? LEU C 248 SER C 252 
AA7 3 CYS C 104 ? VAL C 108 ? CYS C 259 VAL C 263 
AA7 4 THR C 53  ? LEU C 60  ? THR C 208 LEU C 215 
AA7 5 GLY C 43  ? VAL C 50  ? GLY C 198 VAL C 205 
AA7 6 LYS C 36  ? GLU C 39  ? LYS C 191 GLU C 194 
AA8 1 ILE C 162 ? LEU C 164 ? ILE C 317 LEU C 319 
AA8 2 ALA C 170 ? ILE C 172 ? ALA C 325 ILE C 327 
AA9 1 VAL C 188 ? MET C 189 ? VAL C 343 MET C 344 
AA9 2 GLU C 208 ? ILE C 209 ? GLU C 363 ILE C 364 
AB1 1 HIS D 11  ? SER D 12  ? HIS D 166 SER D 167 
AB1 2 LEU D 93  ? SER D 97  ? LEU D 248 SER D 252 
AB1 3 CYS D 104 ? VAL D 108 ? CYS D 259 VAL D 263 
AB1 4 THR D 54  ? LEU D 60  ? THR D 209 LEU D 215 
AB1 5 GLY D 43  ? TYR D 49  ? GLY D 198 TYR D 204 
AB1 6 LYS D 36  ? GLU D 39  ? LYS D 191 GLU D 194 
AB2 1 ILE D 162 ? LEU D 164 ? ILE D 317 LEU D 319 
AB2 2 ALA D 170 ? ILE D 172 ? ALA D 325 ILE D 327 
AB3 1 VAL D 188 ? MET D 189 ? VAL D 343 MET D 344 
AB3 2 GLU D 208 ? ILE D 209 ? GLU D 363 ILE D 364 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N HIS A 11  ? N HIS A 166 O LEU A 94  ? O LEU A 249 
AA1 2 3 N GLY A 95  ? N GLY A 250 O VAL A 106 ? O VAL A 261 
AA1 3 4 O LEU A 105 ? O LEU A 260 N LYS A 58  ? N LYS A 213 
AA1 4 5 O VAL A 57  ? O VAL A 212 N TYR A 46  ? N TYR A 201 
AA1 5 6 O VAL A 45  ? O VAL A 200 N MET A 37  ? N MET A 192 
AA2 1 2 N LEU A 163 ? N LEU A 318 O LYS A 171 ? O LYS A 326 
AA3 1 2 N VAL A 188 ? N VAL A 343 O ILE A 209 ? O ILE A 364 
AA4 1 2 N HIS B 11  ? N HIS B 166 O LEU B 94  ? O LEU B 249 
AA4 2 3 N LEU B 94  ? N LEU B 249 O VAL B 106 ? O VAL B 261 
AA4 3 4 O LEU B 105 ? O LEU B 260 N LYS B 58  ? N LYS B 213 
AA4 4 5 O VAL B 57  ? O VAL B 212 N TYR B 46  ? N TYR B 201 
AA4 5 6 O VAL B 45  ? O VAL B 200 N MET B 37  ? N MET B 192 
AA5 1 2 N ILE B 153 ? N ILE B 308 O ARG B 179 ? O ARG B 334 
AA6 1 2 N LEU B 163 ? N LEU B 318 O LYS B 171 ? O LYS B 326 
AA7 1 2 N HIS C 11  ? N HIS C 166 O LEU C 94  ? O LEU C 249 
AA7 2 3 N LEU C 94  ? N LEU C 249 O VAL C 106 ? O VAL C 261 
AA7 3 4 O LEU C 105 ? O LEU C 260 N LYS C 58  ? N LYS C 213 
AA7 4 5 O VAL C 57  ? O VAL C 212 N TYR C 46  ? N TYR C 201 
AA7 5 6 O VAL C 45  ? O VAL C 200 N MET C 37  ? N MET C 192 
AA8 1 2 N LEU C 163 ? N LEU C 318 O LYS C 171 ? O LYS C 326 
AA9 1 2 N VAL C 188 ? N VAL C 343 O ILE C 209 ? O ILE C 364 
AB1 1 2 N HIS D 11  ? N HIS D 166 O LEU D 94  ? O LEU D 249 
AB1 2 3 N LEU D 94  ? N LEU D 249 O VAL D 106 ? O VAL D 261 
AB1 3 4 O TYR D 107 ? O TYR D 262 N ALA D 56  ? N ALA D 211 
AB1 4 5 O VAL D 57  ? O VAL D 212 N TYR D 46  ? N TYR D 201 
AB1 5 6 O VAL D 45  ? O VAL D 200 N MET D 37  ? N MET D 192 
AB2 1 2 N LEU D 163 ? N LEU D 318 O LYS D 171 ? O LYS D 326 
AB3 1 2 N VAL D 188 ? N VAL D 343 O ILE D 209 ? O ILE D 364 
# 
_pdbx_entry_details.entry_id                   8SCW 
_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   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 207 ? ? 74.03   -9.72   
2  1 ARG A 310 ? ? 78.36   -5.77   
3  1 ASP A 311 ? ? -144.23 42.54   
4  1 ASP A 329 ? ? 58.18   81.05   
5  1 ALA A 335 ? ? -82.02  -149.74 
6  1 GLU A 406 ? ? 44.07   9.57    
7  1 ASN B 206 ? ? 71.70   -111.85 
8  1 ARG B 310 ? ? 74.19   -3.24   
9  1 ASP B 311 ? ? -148.75 49.30   
10 1 ASP B 329 ? ? 57.88   81.14   
11 1 GLU B 406 ? ? 44.78   9.11    
12 1 ASN C 207 ? ? 71.95   -21.18  
13 1 ARG C 310 ? ? 78.38   -7.14   
14 1 ASP C 311 ? ? -144.43 42.74   
15 1 ASP C 329 ? ? 58.46   80.95   
16 1 HIS C 390 ? ? -96.93  30.94   
17 1 GLU C 406 ? ? 43.57   10.08   
18 1 ASN D 206 ? ? 72.43   56.16   
19 1 ASN D 207 ? ? 64.71   -14.30  
20 1 ARG D 310 ? ? 79.30   -9.60   
21 1 ASP D 311 ? ? -141.26 42.57   
22 1 ASP D 329 ? ? 58.45   80.62   
23 1 HIS D 390 ? ? -96.26  30.66   
24 1 GLU D 406 ? ? 44.07   9.60    
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  A TPO 187 A TPO 342 ? THR 'modified residue' 
2  A TPO 190 A TPO 345 ? THR 'modified residue' 
3  A SEP 191 A SEP 346 ? SER 'modified residue' 
4  B TPO 187 B TPO 342 ? THR 'modified residue' 
5  B TPO 190 B TPO 345 ? THR 'modified residue' 
6  B SEP 191 B SEP 346 ? SER 'modified residue' 
7  C TPO 187 C TPO 342 ? THR 'modified residue' 
8  C TPO 190 C TPO 345 ? THR 'modified residue' 
9  C SEP 191 C SEP 346 ? SER 'modified residue' 
10 D TPO 187 D TPO 342 ? THR 'modified residue' 
11 D TPO 190 D TPO 345 ? THR 'modified residue' 
12 D SEP 191 D SEP 346 ? SER 'modified residue' 
# 
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 GLY 156 ? A GLY 1   
2  1 Y 1 A ALA 157 ? A ALA 2   
3  1 Y 1 A MET 158 ? A MET 3   
4  1 Y 1 A GLY 159 ? A GLY 4   
5  1 Y 1 A VAL 160 ? A VAL 5   
6  1 Y 1 A SER 161 ? A SER 6   
7  1 Y 1 A ASP 162 ? A ASP 7   
8  1 Y 1 A THR 163 ? A THR 8   
9  1 Y 1 A MET 218 ? A MET 63  
10 1 Y 1 A VAL 219 ? A VAL 64  
11 1 Y 1 A ASP 220 ? A ASP 65  
12 1 Y 1 A ILE 221 ? A ILE 66  
13 1 Y 1 A GLU 337 ? A GLU 182 
14 1 Y 1 A LYS 338 ? A LYS 183 
15 1 Y 1 A PHE 339 ? A PHE 184 
16 1 Y 1 A ALA 340 ? A ALA 185 
17 1 Y 1 A GLN 341 ? A GLN 186 
18 1 Y 1 A ALA 459 ? A ALA 304 
19 1 Y 1 A SER 460 ? A SER 305 
20 1 Y 1 B GLY 156 ? B GLY 1   
21 1 Y 1 B ALA 157 ? B ALA 2   
22 1 Y 1 B MET 158 ? B MET 3   
23 1 Y 1 B GLY 159 ? B GLY 4   
24 1 Y 1 B VAL 160 ? B VAL 5   
25 1 Y 1 B SER 161 ? B SER 6   
26 1 Y 1 B ASP 162 ? B ASP 7   
27 1 Y 1 B THR 163 ? B THR 8   
28 1 Y 1 B MET 218 ? B MET 63  
29 1 Y 1 B VAL 219 ? B VAL 64  
30 1 Y 1 B ASP 220 ? B ASP 65  
31 1 Y 1 B ILE 221 ? B ILE 66  
32 1 Y 1 B GLU 337 ? B GLU 182 
33 1 Y 1 B LYS 338 ? B LYS 183 
34 1 Y 1 B PHE 339 ? B PHE 184 
35 1 Y 1 B ALA 340 ? B ALA 185 
36 1 Y 1 B GLN 341 ? B GLN 186 
37 1 Y 1 B ALA 459 ? B ALA 304 
38 1 Y 1 B SER 460 ? B SER 305 
39 1 Y 1 C GLY 156 ? C GLY 1   
40 1 Y 1 C ALA 157 ? C ALA 2   
41 1 Y 1 C MET 158 ? C MET 3   
42 1 Y 1 C GLY 159 ? C GLY 4   
43 1 Y 1 C VAL 160 ? C VAL 5   
44 1 Y 1 C SER 161 ? C SER 6   
45 1 Y 1 C ASP 162 ? C ASP 7   
46 1 Y 1 C THR 163 ? C THR 8   
47 1 Y 1 C MET 218 ? C MET 63  
48 1 Y 1 C VAL 219 ? C VAL 64  
49 1 Y 1 C ASP 220 ? C ASP 65  
50 1 Y 1 C ILE 221 ? C ILE 66  
51 1 Y 1 C THR 222 ? C THR 67  
52 1 Y 1 C SER 336 ? C SER 181 
53 1 Y 1 C GLU 337 ? C GLU 182 
54 1 Y 1 C LYS 338 ? C LYS 183 
55 1 Y 1 C PHE 339 ? C PHE 184 
56 1 Y 1 C ALA 340 ? C ALA 185 
57 1 Y 1 C GLN 341 ? C GLN 186 
58 1 Y 1 C ALA 459 ? C ALA 304 
59 1 Y 1 C SER 460 ? C SER 305 
60 1 Y 1 D GLY 156 ? D GLY 1   
61 1 Y 1 D ALA 157 ? D ALA 2   
62 1 Y 1 D MET 158 ? D MET 3   
63 1 Y 1 D GLY 159 ? D GLY 4   
64 1 Y 1 D VAL 160 ? D VAL 5   
65 1 Y 1 D SER 161 ? D SER 6   
66 1 Y 1 D ASP 162 ? D ASP 7   
67 1 Y 1 D THR 163 ? D THR 8   
68 1 Y 1 D MET 218 ? D MET 63  
69 1 Y 1 D VAL 219 ? D VAL 64  
70 1 Y 1 D ASP 220 ? D ASP 65  
71 1 Y 1 D ILE 221 ? D ILE 66  
72 1 Y 1 D THR 222 ? D THR 67  
73 1 Y 1 D SER 336 ? D SER 181 
74 1 Y 1 D GLU 337 ? D GLU 182 
75 1 Y 1 D LYS 338 ? D LYS 183 
76 1 Y 1 D PHE 339 ? D PHE 184 
77 1 Y 1 D ALA 340 ? D ALA 185 
78 1 Y 1 D GLN 341 ? D GLN 186 
79 1 Y 1 D ALA 459 ? D ALA 304 
80 1 Y 1 D SER 460 ? D SER 305 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SEP N    N N N 290 
SEP CA   C N S 291 
SEP CB   C N N 292 
SEP OG   O N N 293 
SEP C    C N N 294 
SEP O    O N N 295 
SEP OXT  O N N 296 
SEP P    P N N 297 
SEP O1P  O N N 298 
SEP O2P  O N N 299 
SEP O3P  O N N 300 
SEP H    H N N 301 
SEP H2   H N N 302 
SEP HA   H N N 303 
SEP HB2  H N N 304 
SEP HB3  H N N 305 
SEP HXT  H N N 306 
SEP HOP2 H N N 307 
SEP HOP3 H N N 308 
SER N    N N N 309 
SER CA   C N S 310 
SER C    C N N 311 
SER O    O N N 312 
SER CB   C N N 313 
SER OG   O N N 314 
SER OXT  O N N 315 
SER H    H N N 316 
SER H2   H N N 317 
SER HA   H N N 318 
SER HB2  H N N 319 
SER HB3  H N N 320 
SER HG   H N N 321 
SER HXT  H N N 322 
SO4 S    S N N 323 
SO4 O1   O N N 324 
SO4 O2   O N N 325 
SO4 O3   O N N 326 
SO4 O4   O N N 327 
THR N    N N N 328 
THR CA   C N S 329 
THR C    C N N 330 
THR O    O N N 331 
THR CB   C N R 332 
THR OG1  O N N 333 
THR CG2  C N N 334 
THR OXT  O N N 335 
THR H    H N N 336 
THR H2   H N N 337 
THR HA   H N N 338 
THR HB   H N N 339 
THR HG1  H N N 340 
THR HG21 H N N 341 
THR HG22 H N N 342 
THR HG23 H N N 343 
THR HXT  H N N 344 
TPO N    N N N 345 
TPO CA   C N S 346 
TPO CB   C N R 347 
TPO CG2  C N N 348 
TPO OG1  O N N 349 
TPO P    P N N 350 
TPO O1P  O N N 351 
TPO O2P  O N N 352 
TPO O3P  O N N 353 
TPO C    C N N 354 
TPO O    O N N 355 
TPO OXT  O N N 356 
TPO H    H N N 357 
TPO H2   H N N 358 
TPO HA   H N N 359 
TPO HB   H N N 360 
TPO HG21 H N N 361 
TPO HG22 H N N 362 
TPO HG23 H N N 363 
TPO HOP2 H N N 364 
TPO HOP3 H N N 365 
TPO HXT  H N N 366 
TRP N    N N N 367 
TRP CA   C N S 368 
TRP C    C N N 369 
TRP O    O N N 370 
TRP CB   C N N 371 
TRP CG   C Y N 372 
TRP CD1  C Y N 373 
TRP CD2  C Y N 374 
TRP NE1  N Y N 375 
TRP CE2  C Y N 376 
TRP CE3  C Y N 377 
TRP CZ2  C Y N 378 
TRP CZ3  C Y N 379 
TRP CH2  C Y N 380 
TRP OXT  O N N 381 
TRP H    H N N 382 
TRP H2   H N N 383 
TRP HA   H N N 384 
TRP HB2  H N N 385 
TRP HB3  H N N 386 
TRP HD1  H N N 387 
TRP HE1  H N N 388 
TRP HE3  H N N 389 
TRP HZ2  H N N 390 
TRP HZ3  H N N 391 
TRP HH2  H N N 392 
TRP HXT  H N N 393 
TYR N    N N N 394 
TYR CA   C N S 395 
TYR C    C N N 396 
TYR O    O N N 397 
TYR CB   C N N 398 
TYR CG   C Y N 399 
TYR CD1  C Y N 400 
TYR CD2  C Y N 401 
TYR CE1  C Y N 402 
TYR CE2  C Y N 403 
TYR CZ   C Y N 404 
TYR OH   O N N 405 
TYR OXT  O N N 406 
TYR H    H N N 407 
TYR H2   H N N 408 
TYR HA   H N N 409 
TYR HB2  H N N 410 
TYR HB3  H N N 411 
TYR HD1  H N N 412 
TYR HD2  H N N 413 
TYR HE1  H N N 414 
TYR HE2  H N N 415 
TYR HH   H N N 416 
TYR HXT  H N N 417 
VAL N    N N N 418 
VAL CA   C N S 419 
VAL C    C N N 420 
VAL O    O N N 421 
VAL CB   C N N 422 
VAL CG1  C N N 423 
VAL CG2  C N N 424 
VAL OXT  O N N 425 
VAL H    H N N 426 
VAL H2   H N N 427 
VAL HA   H N N 428 
VAL HB   H N N 429 
VAL HG11 H N N 430 
VAL HG12 H N N 431 
VAL HG13 H N N 432 
VAL HG21 H N N 433 
VAL HG22 H N N 434 
VAL HG23 H N N 435 
VAL HXT  H N N 436 
ZVA C13  C Y N 437 
ZVA C18  C N N 438 
ZVA C17  C N R 439 
ZVA C16  C N N 440 
ZVA C15  C N N 441 
ZVA C19  C N N 442 
ZVA C20  C N N 443 
ZVA C11  C N N 444 
ZVA C12  C N N 445 
ZVA F    F N N 446 
ZVA O1   O N N 447 
ZVA N6   N N N 448 
ZVA O    O N N 449 
ZVA C14  C Y N 450 
ZVA C9   C Y N 451 
ZVA N4   N N N 452 
ZVA C10  C N N 453 
ZVA C8   C Y N 454 
ZVA N5   N Y N 455 
ZVA C7   C Y N 456 
ZVA N3   N Y N 457 
ZVA C5   C Y N 458 
ZVA N1   N Y N 459 
ZVA C2   C Y N 460 
ZVA N2   N Y N 461 
ZVA C6   C Y N 462 
ZVA C4   C Y N 463 
ZVA C3   C Y N 464 
ZVA C1   C Y N 465 
ZVA C    C N N 466 
ZVA N    N N N 467 
ZVA H1   H N N 468 
ZVA H2   H N N 469 
ZVA H3   H N N 470 
ZVA H4   H N N 471 
ZVA H5   H N N 472 
ZVA H6   H N N 473 
ZVA H7   H N N 474 
ZVA H8   H N N 475 
ZVA H9   H N N 476 
ZVA H10  H N N 477 
ZVA H11  H N N 478 
ZVA H12  H N N 479 
ZVA H13  H N N 480 
ZVA H14  H N N 481 
ZVA H15  H N N 482 
ZVA H16  H N N 483 
ZVA H17  H N N 484 
ZVA H18  H N N 485 
ZVA H19  H N N 486 
ZVA H20  H N N 487 
ZVA H21  H N N 488 
ZVA H22  H N N 489 
ZVA H23  H N N 490 
ZVA H24  H N N 491 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SEP N   CA   sing N N 277 
SEP N   H    sing N N 278 
SEP N   H2   sing N N 279 
SEP CA  CB   sing N N 280 
SEP CA  C    sing N N 281 
SEP CA  HA   sing N N 282 
SEP CB  OG   sing N N 283 
SEP CB  HB2  sing N N 284 
SEP CB  HB3  sing N N 285 
SEP OG  P    sing N N 286 
SEP C   O    doub N N 287 
SEP C   OXT  sing N N 288 
SEP OXT HXT  sing N N 289 
SEP P   O1P  doub N N 290 
SEP P   O2P  sing N N 291 
SEP P   O3P  sing N N 292 
SEP O2P HOP2 sing N N 293 
SEP O3P HOP3 sing N N 294 
SER N   CA   sing N N 295 
SER N   H    sing N N 296 
SER N   H2   sing N N 297 
SER CA  C    sing N N 298 
SER CA  CB   sing N N 299 
SER CA  HA   sing N N 300 
SER C   O    doub N N 301 
SER C   OXT  sing N N 302 
SER CB  OG   sing N N 303 
SER CB  HB2  sing N N 304 
SER CB  HB3  sing N N 305 
SER OG  HG   sing N N 306 
SER OXT HXT  sing N N 307 
SO4 S   O1   doub N N 308 
SO4 S   O2   doub N N 309 
SO4 S   O3   sing N N 310 
SO4 S   O4   sing N N 311 
THR N   CA   sing N N 312 
THR N   H    sing N N 313 
THR N   H2   sing N N 314 
THR CA  C    sing N N 315 
THR CA  CB   sing N N 316 
THR CA  HA   sing N N 317 
THR C   O    doub N N 318 
THR C   OXT  sing N N 319 
THR CB  OG1  sing N N 320 
THR CB  CG2  sing N N 321 
THR CB  HB   sing N N 322 
THR OG1 HG1  sing N N 323 
THR CG2 HG21 sing N N 324 
THR CG2 HG22 sing N N 325 
THR CG2 HG23 sing N N 326 
THR OXT HXT  sing N N 327 
TPO N   CA   sing N N 328 
TPO N   H    sing N N 329 
TPO N   H2   sing N N 330 
TPO CA  CB   sing N N 331 
TPO CA  C    sing N N 332 
TPO CA  HA   sing N N 333 
TPO CB  CG2  sing N N 334 
TPO CB  OG1  sing N N 335 
TPO CB  HB   sing N N 336 
TPO CG2 HG21 sing N N 337 
TPO CG2 HG22 sing N N 338 
TPO CG2 HG23 sing N N 339 
TPO OG1 P    sing N N 340 
TPO P   O1P  doub N N 341 
TPO P   O2P  sing N N 342 
TPO P   O3P  sing N N 343 
TPO O2P HOP2 sing N N 344 
TPO O3P HOP3 sing N N 345 
TPO C   O    doub N N 346 
TPO C   OXT  sing N N 347 
TPO OXT HXT  sing N N 348 
TRP N   CA   sing N N 349 
TRP N   H    sing N N 350 
TRP N   H2   sing N N 351 
TRP CA  C    sing N N 352 
TRP CA  CB   sing N N 353 
TRP CA  HA   sing N N 354 
TRP C   O    doub N N 355 
TRP C   OXT  sing N N 356 
TRP CB  CG   sing N N 357 
TRP CB  HB2  sing N N 358 
TRP CB  HB3  sing N N 359 
TRP CG  CD1  doub Y N 360 
TRP CG  CD2  sing Y N 361 
TRP CD1 NE1  sing Y N 362 
TRP CD1 HD1  sing N N 363 
TRP CD2 CE2  doub Y N 364 
TRP CD2 CE3  sing Y N 365 
TRP NE1 CE2  sing Y N 366 
TRP NE1 HE1  sing N N 367 
TRP CE2 CZ2  sing Y N 368 
TRP CE3 CZ3  doub Y N 369 
TRP CE3 HE3  sing N N 370 
TRP CZ2 CH2  doub Y N 371 
TRP CZ2 HZ2  sing N N 372 
TRP CZ3 CH2  sing Y N 373 
TRP CZ3 HZ3  sing N N 374 
TRP CH2 HH2  sing N N 375 
TRP OXT HXT  sing N N 376 
TYR N   CA   sing N N 377 
TYR N   H    sing N N 378 
TYR N   H2   sing N N 379 
TYR CA  C    sing N N 380 
TYR CA  CB   sing N N 381 
TYR CA  HA   sing N N 382 
TYR C   O    doub N N 383 
TYR C   OXT  sing N N 384 
TYR CB  CG   sing N N 385 
TYR CB  HB2  sing N N 386 
TYR CB  HB3  sing N N 387 
TYR CG  CD1  doub Y N 388 
TYR CG  CD2  sing Y N 389 
TYR CD1 CE1  sing Y N 390 
TYR CD1 HD1  sing N N 391 
TYR CD2 CE2  doub Y N 392 
TYR CD2 HD2  sing N N 393 
TYR CE1 CZ   doub Y N 394 
TYR CE1 HE1  sing N N 395 
TYR CE2 CZ   sing Y N 396 
TYR CE2 HE2  sing N N 397 
TYR CZ  OH   sing N N 398 
TYR OH  HH   sing N N 399 
TYR OXT HXT  sing N N 400 
VAL N   CA   sing N N 401 
VAL N   H    sing N N 402 
VAL N   H2   sing N N 403 
VAL CA  C    sing N N 404 
VAL CA  CB   sing N N 405 
VAL CA  HA   sing N N 406 
VAL C   O    doub N N 407 
VAL C   OXT  sing N N 408 
VAL CB  CG1  sing N N 409 
VAL CB  CG2  sing N N 410 
VAL CB  HB   sing N N 411 
VAL CG1 HG11 sing N N 412 
VAL CG1 HG12 sing N N 413 
VAL CG1 HG13 sing N N 414 
VAL CG2 HG21 sing N N 415 
VAL CG2 HG22 sing N N 416 
VAL CG2 HG23 sing N N 417 
VAL OXT HXT  sing N N 418 
ZVA N5  C13  doub Y N 419 
ZVA N5  C7   sing Y N 420 
ZVA C13 C14  sing Y N 421 
ZVA N2  N3   sing Y N 422 
ZVA N2  C6   doub Y N 423 
ZVA N3  C5   sing Y N 424 
ZVA N3  C7   sing N N 425 
ZVA C6  C4   sing Y N 426 
ZVA C5  N1   doub Y N 427 
ZVA C5  C4   sing Y N 428 
ZVA C7  C8   doub Y N 429 
ZVA N1  C2   sing Y N 430 
ZVA C4  C3   doub Y N 431 
ZVA C2  C1   doub Y N 432 
ZVA C16 N6   sing N N 433 
ZVA C16 C17  sing N N 434 
ZVA C3  C1   sing Y N 435 
ZVA N6  C15  sing N N 436 
ZVA C12 C10  sing N N 437 
ZVA C1  C    sing N N 438 
ZVA C14 C15  sing N N 439 
ZVA C14 C9   doub Y N 440 
ZVA C15 O    doub N N 441 
ZVA C8  C9   sing Y N 442 
ZVA C20 C18  sing N N 443 
ZVA C   N    trip N N 444 
ZVA C9  N4   sing N N 445 
ZVA O1  C18  sing N N 446 
ZVA N4  C10  sing N N 447 
ZVA C18 C17  sing N N 448 
ZVA C18 C19  sing N N 449 
ZVA C10 C11  sing N N 450 
ZVA C17 F    sing N N 451 
ZVA C13 H1   sing N N 452 
ZVA C17 H2   sing N N 453 
ZVA C16 H3   sing N N 454 
ZVA C16 H4   sing N N 455 
ZVA C19 H5   sing N N 456 
ZVA C19 H6   sing N N 457 
ZVA C19 H7   sing N N 458 
ZVA C20 H8   sing N N 459 
ZVA C20 H9   sing N N 460 
ZVA C20 H10  sing N N 461 
ZVA C11 H11  sing N N 462 
ZVA C11 H12  sing N N 463 
ZVA C11 H13  sing N N 464 
ZVA C12 H14  sing N N 465 
ZVA C12 H15  sing N N 466 
ZVA C12 H16  sing N N 467 
ZVA O1  H17  sing N N 468 
ZVA N6  H18  sing N N 469 
ZVA N4  H19  sing N N 470 
ZVA C10 H20  sing N N 471 
ZVA C8  H21  sing N N 472 
ZVA C2  H22  sing N N 473 
ZVA C6  H23  sing N N 474 
ZVA C3  H24  sing N N 475 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Unpublished IRAK4 structure' 
# 
_atom_sites.entry_id                    8SCW 
_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.fract_transf_matrix[1][1]   -0.002321 
_atom_sites.fract_transf_matrix[1][2]   -0.000079 
_atom_sites.fract_transf_matrix[1][3]   0.008910 
_atom_sites.fract_transf_matrix[2][1]   0.006757 
_atom_sites.fract_transf_matrix[2][2]   -0.001426 
_atom_sites.fract_transf_matrix[2][3]   0.001748 
_atom_sites.fract_transf_matrix[3][1]   0.000050 
_atom_sites.fract_transf_matrix[3][2]   0.011329 
_atom_sites.fract_transf_matrix[3][3]   0.009046 
_atom_sites.fract_transf_vector[1]      0.08285 
_atom_sites.fract_transf_vector[2]      -0.15475 
_atom_sites.fract_transf_vector[3]      -0.44547 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
F 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ARG A 1 9   ? 8.754   14.857 5.604   1.00 73.39  ?  164 ARG A N   1 
ATOM   2    C CA  . ARG A 1 9   ? 8.599   15.619 6.853   1.00 72.64  ?  164 ARG A CA  1 
ATOM   3    C C   . ARG A 1 9   ? 8.891   17.124 6.629   1.00 73.92  ?  164 ARG A C   1 
ATOM   4    O O   . ARG A 1 9   ? 8.094   17.984 7.033   1.00 73.99  ?  164 ARG A O   1 
ATOM   5    C CB  . ARG A 1 9   ? 9.529   15.035 7.933   1.00 71.69  ?  164 ARG A CB  1 
ATOM   6    C CG  . ARG A 1 9   ? 8.798   14.413 9.110   1.00 78.61  ?  164 ARG A CG  1 
ATOM   7    C CD  . ARG A 1 9   ? 9.190   15.078 10.411  1.00 81.69  ?  164 ARG A CD  1 
ATOM   8    N NE  . ARG A 1 9   ? 8.057   15.729 11.077  1.00 85.88  ?  164 ARG A NE  1 
ATOM   9    C CZ  . ARG A 1 9   ? 7.639   16.963 10.808  1.00 98.07  ?  164 ARG A CZ  1 
ATOM   10   N NH1 . ARG A 1 9   ? 8.227   17.679 9.860   1.00 89.13  ?  164 ARG A NH1 1 
ATOM   11   N NH2 . ARG A 1 9   ? 6.613   17.481 11.467  1.00 81.07  1  164 ARG A NH2 1 
ATOM   12   N N   . PHE A 1 10  ? 10.049  17.420 5.987   1.00 66.26  ?  165 PHE A N   1 
ATOM   13   C CA  . PHE A 1 10  ? 10.533  18.763 5.671   1.00 63.84  ?  165 PHE A CA  1 
ATOM   14   C C   . PHE A 1 10  ? 10.680  18.956 4.161   1.00 65.12  ?  165 PHE A C   1 
ATOM   15   O O   . PHE A 1 10  ? 11.026  18.018 3.443   1.00 64.13  ?  165 PHE A O   1 
ATOM   16   C CB  . PHE A 1 10  ? 11.890  19.017 6.341   1.00 64.98  ?  165 PHE A CB  1 
ATOM   17   C CG  . PHE A 1 10  ? 11.951  18.781 7.829   1.00 65.90  ?  165 PHE A CG  1 
ATOM   18   C CD1 . PHE A 1 10  ? 11.206  19.562 8.707   1.00 68.44  ?  165 PHE A CD1 1 
ATOM   19   C CD2 . PHE A 1 10  ? 12.798  17.820 8.360   1.00 67.52  ?  165 PHE A CD2 1 
ATOM   20   C CE1 . PHE A 1 10  ? 11.280  19.353 10.090  1.00 69.34  ?  165 PHE A CE1 1 
ATOM   21   C CE2 . PHE A 1 10  ? 12.876  17.617 9.741   1.00 70.48  ?  165 PHE A CE2 1 
ATOM   22   C CZ  . PHE A 1 10  ? 12.118  18.387 10.597  1.00 68.67  ?  165 PHE A CZ  1 
ATOM   23   N N   . HIS A 1 11  ? 10.461  20.187 3.692   1.00 60.54  ?  166 HIS A N   1 
ATOM   24   C CA  . HIS A 1 11  ? 10.574  20.530 2.284   1.00 59.94  ?  166 HIS A CA  1 
ATOM   25   C C   . HIS A 1 11  ? 12.027  20.587 1.826   1.00 59.49  ?  166 HIS A C   1 
ATOM   26   O O   . HIS A 1 11  ? 12.846  21.242 2.456   1.00 57.60  ?  166 HIS A O   1 
ATOM   27   C CB  . HIS A 1 11  ? 9.830   21.842 1.962   1.00 61.54  ?  166 HIS A CB  1 
ATOM   28   C CG  . HIS A 1 11  ? 9.902   22.224 0.517   1.00 65.79  ?  166 HIS A CG  1 
ATOM   29   N ND1 . HIS A 1 11  ? 10.762  23.216 0.076   1.00 67.93  ?  166 HIS A ND1 1 
ATOM   30   C CD2 . HIS A 1 11  ? 9.273   21.685 -0.557  1.00 68.43  ?  166 HIS A CD2 1 
ATOM   31   C CE1 . HIS A 1 11  ? 10.608  23.278 -1.240  1.00 67.72  ?  166 HIS A CE1 1 
ATOM   32   N NE2 . HIS A 1 11  ? 9.730   22.372 -1.671  1.00 68.25  ?  166 HIS A NE2 1 
ATOM   33   N N   . SER A 1 12  ? 12.341  19.888 0.728   1.00 53.82  ?  167 SER A N   1 
ATOM   34   C CA  . SER A 1 12  ? 13.679  19.924 0.157   1.00 52.54  ?  167 SER A CA  1 
ATOM   35   C C   . SER A 1 12  ? 13.778  21.107 -0.830  1.00 53.98  ?  167 SER A C   1 
ATOM   36   O O   . SER A 1 12  ? 12.976  21.238 -1.739  1.00 54.30  ?  167 SER A O   1 
ATOM   37   C CB  . SER A 1 12  ? 14.004  18.611 -0.542  1.00 55.51  ?  167 SER A CB  1 
ATOM   38   O OG  . SER A 1 12  ? 15.343  18.654 -1.009  1.00 64.56  ?  167 SER A OG  1 
ATOM   39   N N   . PHE A 1 13  ? 14.730  21.978 -0.633  1.00 48.89  ?  168 PHE A N   1 
ATOM   40   C CA  . PHE A 1 13  ? 14.895  23.129 -1.509  1.00 47.59  ?  168 PHE A CA  1 
ATOM   41   C C   . PHE A 1 13  ? 16.066  22.928 -2.405  1.00 53.05  ?  168 PHE A C   1 
ATOM   42   O O   . PHE A 1 13  ? 16.999  22.185 -2.076  1.00 53.92  ?  168 PHE A O   1 
ATOM   43   C CB  . PHE A 1 13  ? 15.169  24.403 -0.684  1.00 47.99  ?  168 PHE A CB  1 
ATOM   44   C CG  . PHE A 1 13  ? 13.958  24.990 -0.020  1.00 47.85  ?  168 PHE A CG  1 
ATOM   45   C CD1 . PHE A 1 13  ? 13.124  25.860 -0.709  1.00 49.99  ?  168 PHE A CD1 1 
ATOM   46   C CD2 . PHE A 1 13  ? 13.660  24.688 1.300   1.00 49.11  ?  168 PHE A CD2 1 
ATOM   47   C CE1 . PHE A 1 13  ? 12.013  26.423 -0.087  1.00 51.27  ?  168 PHE A CE1 1 
ATOM   48   C CE2 . PHE A 1 13  ? 12.546  25.247 1.924   1.00 52.54  ?  168 PHE A CE2 1 
ATOM   49   C CZ  . PHE A 1 13  ? 11.729  26.113 1.227   1.00 51.00  ?  168 PHE A CZ  1 
ATOM   50   N N   . SER A 1 14  ? 16.076  23.675 -3.494  1.00 49.58  ?  169 SER A N   1 
ATOM   51   C CA  . SER A 1 14  ? 17.222  23.679 -4.370  1.00 48.97  ?  169 SER A CA  1 
ATOM   52   C C   . SER A 1 14  ? 18.011  24.922 -3.939  1.00 52.66  ?  169 SER A C   1 
ATOM   53   O O   . SER A 1 14  ? 17.411  25.964 -3.643  1.00 52.87  ?  169 SER A O   1 
ATOM   54   C CB  . SER A 1 14  ? 16.781  23.749 -5.826  1.00 52.22  ?  169 SER A CB  1 
ATOM   55   O OG  . SER A 1 14  ? 17.910  23.672 -6.680  1.00 67.67  ?  169 SER A OG  1 
ATOM   56   N N   . PHE A 1 15  ? 19.331  24.808 -3.851  1.00 48.60  ?  170 PHE A N   1 
ATOM   57   C CA  . PHE A 1 15  ? 20.164  25.917 -3.429  1.00 49.20  ?  170 PHE A CA  1 
ATOM   58   C C   . PHE A 1 15  ? 19.870  27.254 -4.119  1.00 55.32  ?  170 PHE A C   1 
ATOM   59   O O   . PHE A 1 15  ? 19.986  28.298 -3.464  1.00 57.84  ?  170 PHE A O   1 
ATOM   60   C CB  . PHE A 1 15  ? 21.647  25.562 -3.534  1.00 51.59  ?  170 PHE A CB  1 
ATOM   61   C CG  . PHE A 1 15  ? 22.551  26.620 -2.950  1.00 53.81  ?  170 PHE A CG  1 
ATOM   62   C CD1 . PHE A 1 15  ? 22.530  26.903 -1.584  1.00 57.97  ?  170 PHE A CD1 1 
ATOM   63   C CD2 . PHE A 1 15  ? 23.410  27.348 -3.765  1.00 55.89  ?  170 PHE A CD2 1 
ATOM   64   C CE1 . PHE A 1 15  ? 23.353  27.900 -1.047  1.00 59.46  ?  170 PHE A CE1 1 
ATOM   65   C CE2 . PHE A 1 15  ? 24.243  28.336 -3.225  1.00 59.06  ?  170 PHE A CE2 1 
ATOM   66   C CZ  . PHE A 1 15  ? 24.221  28.595 -1.867  1.00 57.96  ?  170 PHE A CZ  1 
ATOM   67   N N   . TYR A 1 16  ? 19.471  27.240 -5.418  1.00 48.96  ?  171 TYR A N   1 
ATOM   68   C CA  . TYR A 1 16  ? 19.182  28.483 -6.136  1.00 46.99  ?  171 TYR A CA  1 
ATOM   69   C C   . TYR A 1 16  ? 17.947  29.179 -5.604  1.00 49.39  ?  171 TYR A C   1 
ATOM   70   O O   . TYR A 1 16  ? 17.931  30.398 -5.565  1.00 48.66  ?  171 TYR A O   1 
ATOM   71   C CB  . TYR A 1 16  ? 19.124  28.289 -7.676  1.00 47.66  ?  171 TYR A CB  1 
ATOM   72   C CG  . TYR A 1 16  ? 17.800  27.775 -8.190  1.00 48.24  ?  171 TYR A CG  1 
ATOM   73   C CD1 . TYR A 1 16  ? 17.524  26.414 -8.219  1.00 49.25  ?  171 TYR A CD1 1 
ATOM   74   C CD2 . TYR A 1 16  ? 16.796  28.652 -8.587  1.00 48.71  ?  171 TYR A CD2 1 
ATOM   75   C CE1 . TYR A 1 16  ? 16.293  25.936 -8.655  1.00 48.18  ?  171 TYR A CE1 1 
ATOM   76   C CE2 . TYR A 1 16  ? 15.546  28.184 -8.988  1.00 49.01  ?  171 TYR A CE2 1 
ATOM   77   C CZ  . TYR A 1 16  ? 15.303  26.825 -9.027  1.00 53.14  ?  171 TYR A CZ  1 
ATOM   78   O OH  . TYR A 1 16  ? 14.082  26.349 -9.436  1.00 55.00  ?  171 TYR A OH  1 
ATOM   79   N N   . GLU A 1 17  ? 16.907  28.417 -5.198  1.00 46.21  ?  172 GLU A N   1 
ATOM   80   C CA  . GLU A 1 17  ? 15.689  29.020 -4.653  1.00 45.82  ?  172 GLU A CA  1 
ATOM   81   C C   . GLU A 1 17  ? 16.093  29.888 -3.462  1.00 51.02  ?  172 GLU A C   1 
ATOM   82   O O   . GLU A 1 17  ? 15.644  31.022 -3.345  1.00 49.58  ?  172 GLU A O   1 
ATOM   83   C CB  . GLU A 1 17  ? 14.721  27.952 -4.144  1.00 46.94  ?  172 GLU A CB  1 
ATOM   84   C CG  . GLU A 1 17  ? 14.190  26.964 -5.157  1.00 50.69  ?  172 GLU A CG  1 
ATOM   85   C CD  . GLU A 1 17  ? 13.253  25.965 -4.510  1.00 63.60  ?  172 GLU A CD  1 
ATOM   86   O OE1 . GLU A 1 17  ? 12.203  26.395 -3.980  1.00 65.46  ?  172 GLU A OE1 1 
ATOM   87   O OE2 . GLU A 1 17  ? 13.586  24.759 -4.491  1.00 55.07  -1 172 GLU A OE2 1 
ATOM   88   N N   . LEU A 1 18  ? 16.999  29.364 -2.623  1.00 49.36  ?  173 LEU A N   1 
ATOM   89   C CA  . LEU A 1 18  ? 17.485  30.036 -1.427  1.00 50.23  ?  173 LEU A CA  1 
ATOM   90   C C   . LEU A 1 18  ? 18.360  31.239 -1.703  1.00 56.49  ?  173 LEU A C   1 
ATOM   91   O O   . LEU A 1 18  ? 18.361  32.191 -0.915  1.00 54.24  ?  173 LEU A O   1 
ATOM   92   C CB  . LEU A 1 18  ? 18.144  29.053 -0.466  1.00 50.09  ?  173 LEU A CB  1 
ATOM   93   C CG  . LEU A 1 18  ? 17.272  27.870 -0.043  1.00 54.90  ?  173 LEU A CG  1 
ATOM   94   C CD1 . LEU A 1 18  ? 17.972  27.067 0.994   1.00 55.24  ?  173 LEU A CD1 1 
ATOM   95   C CD2 . LEU A 1 18  ? 15.877  28.320 0.467   1.00 55.57  ?  173 LEU A CD2 1 
ATOM   96   N N   . LYS A 1 19  ? 19.077  31.213 -2.844  1.00 56.18  ?  174 LYS A N   1 
ATOM   97   C CA  . LYS A 1 19  ? 19.879  32.336 -3.317  1.00 57.13  ?  174 LYS A CA  1 
ATOM   98   C C   . LYS A 1 19  ? 18.889  33.453 -3.667  1.00 61.37  ?  174 LYS A C   1 
ATOM   99   O O   . LYS A 1 19  ? 19.098  34.592 -3.272  1.00 61.50  ?  174 LYS A O   1 
ATOM   100  C CB  . LYS A 1 19  ? 20.662  31.936 -4.567  1.00 61.37  ?  174 LYS A CB  1 
ATOM   101  C CG  . LYS A 1 19  ? 21.974  31.241 -4.293  1.00 85.46  ?  174 LYS A CG  1 
ATOM   102  C CD  . LYS A 1 19  ? 23.166  32.119 -4.684  1.00 100.67 ?  174 LYS A CD  1 
ATOM   103  C CE  . LYS A 1 19  ? 23.699  31.770 -6.059  1.00 118.43 ?  174 LYS A CE  1 
ATOM   104  N NZ  . LYS A 1 19  ? 24.740  32.726 -6.510  1.00 131.54 1  174 LYS A NZ  1 
ATOM   105  N N   . ASN A 1 20  ? 17.768  33.103 -4.333  1.00 57.46  ?  175 ASN A N   1 
ATOM   106  C CA  . ASN A 1 20  ? 16.736  34.062 -4.698  1.00 57.63  ?  175 ASN A CA  1 
ATOM   107  C C   . ASN A 1 20  ? 16.105  34.693 -3.465  1.00 61.70  ?  175 ASN A C   1 
ATOM   108  O O   . ASN A 1 20  ? 16.132  35.916 -3.355  1.00 61.79  ?  175 ASN A O   1 
ATOM   109  C CB  . ASN A 1 20  ? 15.674  33.447 -5.626  1.00 60.95  ?  175 ASN A CB  1 
ATOM   110  C CG  . ASN A 1 20  ? 16.184  32.912 -6.961  1.00 105.38 ?  175 ASN A CG  1 
ATOM   111  O OD1 . ASN A 1 20  ? 15.672  31.923 -7.511  1.00 102.35 ?  175 ASN A OD1 1 
ATOM   112  N ND2 . ASN A 1 20  ? 17.193  33.551 -7.537  1.00 101.84 ?  175 ASN A ND2 1 
ATOM   113  N N   . VAL A 1 21  ? 15.604  33.864 -2.515  1.00 57.79  ?  176 VAL A N   1 
ATOM   114  C CA  . VAL A 1 21  ? 14.920  34.315 -1.290  1.00 57.18  ?  176 VAL A CA  1 
ATOM   115  C C   . VAL A 1 21  ? 15.728  35.236 -0.384  1.00 59.46  ?  176 VAL A C   1 
ATOM   116  O O   . VAL A 1 21  ? 15.138  36.124 0.247   1.00 60.30  ?  176 VAL A O   1 
ATOM   117  C CB  . VAL A 1 21  ? 14.188  33.201 -0.497  1.00 61.28  ?  176 VAL A CB  1 
ATOM   118  C CG1 . VAL A 1 21  ? 13.355  32.329 -1.424  1.00 61.62  ?  176 VAL A CG1 1 
ATOM   119  C CG2 . VAL A 1 21  ? 15.147  32.357 0.338   1.00 60.94  ?  176 VAL A CG2 1 
ATOM   120  N N   . THR A 1 22  ? 17.059  35.042 -0.341  1.00 52.62  ?  177 THR A N   1 
ATOM   121  C CA  . THR A 1 22  ? 17.976  35.781 0.524   1.00 51.07  ?  177 THR A CA  1 
ATOM   122  C C   . THR A 1 22  ? 18.711  36.925 -0.171  1.00 54.80  ?  177 THR A C   1 
ATOM   123  O O   . THR A 1 22  ? 19.684  37.434 0.382   1.00 53.14  ?  177 THR A O   1 
ATOM   124  C CB  . THR A 1 22  ? 18.988  34.815 1.157   1.00 53.47  ?  177 THR A CB  1 
ATOM   125  O OG1 . THR A 1 22  ? 19.767  34.212 0.114   1.00 44.94  ?  177 THR A OG1 1 
ATOM   126  C CG2 . THR A 1 22  ? 18.322  33.768 2.056   1.00 52.12  ?  177 THR A CG2 1 
ATOM   127  N N   . ASN A 1 23  ? 18.265  37.323 -1.387  1.00 53.87  ?  178 ASN A N   1 
ATOM   128  C CA  . ASN A 1 23  ? 18.853  38.396 -2.206  1.00 54.44  ?  178 ASN A CA  1 
ATOM   129  C C   . ASN A 1 23  ? 20.321  38.054 -2.475  1.00 58.40  ?  178 ASN A C   1 
ATOM   130  O O   . ASN A 1 23  ? 21.224  38.876 -2.303  1.00 59.13  ?  178 ASN A O   1 
ATOM   131  C CB  . ASN A 1 23  ? 18.660  39.772 -1.528  1.00 59.46  ?  178 ASN A CB  1 
ATOM   132  C CG  . ASN A 1 23  ? 18.861  40.946 -2.429  1.00 95.10  ?  178 ASN A CG  1 
ATOM   133  O OD1 . ASN A 1 23  ? 18.067  41.197 -3.344  1.00 99.10  ?  178 ASN A OD1 1 
ATOM   134  N ND2 . ASN A 1 23  ? 19.901  41.722 -2.146  1.00 84.71  ?  178 ASN A ND2 1 
ATOM   135  N N   . ASN A 1 24  ? 20.537  36.785 -2.852  1.00 54.74  ?  179 ASN A N   1 
ATOM   136  C CA  . ASN A 1 24  ? 21.823  36.142 -3.132  1.00 54.76  ?  179 ASN A CA  1 
ATOM   137  C C   . ASN A 1 24  ? 22.798  36.231 -1.978  1.00 55.88  ?  179 ASN A C   1 
ATOM   138  O O   . ASN A 1 24  ? 23.930  36.674 -2.142  1.00 54.98  ?  179 ASN A O   1 
ATOM   139  C CB  . ASN A 1 24  ? 22.391  36.558 -4.483  1.00 61.16  ?  179 ASN A CB  1 
ATOM   140  C CG  . ASN A 1 24  ? 21.582  35.963 -5.604  1.00 100.82 ?  179 ASN A CG  1 
ATOM   141  O OD1 . ASN A 1 24  ? 21.868  34.864 -6.089  1.00 104.43 ?  179 ASN A OD1 1 
ATOM   142  N ND2 . ASN A 1 24  ? 20.538  36.662 -6.032  1.00 92.00  ?  179 ASN A ND2 1 
ATOM   143  N N   . PHE A 1 25  ? 22.323  35.799 -0.795  1.00 51.03  ?  180 PHE A N   1 
ATOM   144  C CA  . PHE A 1 25  ? 23.038  35.794 0.473   1.00 50.00  ?  180 PHE A CA  1 
ATOM   145  C C   . PHE A 1 25  ? 23.738  37.124 0.791   1.00 53.81  ?  180 PHE A C   1 
ATOM   146  O O   . PHE A 1 25  ? 24.931  37.146 1.095   1.00 53.29  ?  180 PHE A O   1 
ATOM   147  C CB  . PHE A 1 25  ? 23.963  34.575 0.583   1.00 51.30  ?  180 PHE A CB  1 
ATOM   148  C CG  . PHE A 1 25  ? 23.227  33.255 0.501   1.00 51.98  ?  180 PHE A CG  1 
ATOM   149  C CD1 . PHE A 1 25  ? 22.576  32.730 1.615   1.00 53.87  ?  180 PHE A CD1 1 
ATOM   150  C CD2 . PHE A 1 25  ? 23.195  32.531 -0.683  1.00 52.09  ?  180 PHE A CD2 1 
ATOM   151  C CE1 . PHE A 1 25  ? 21.901  31.509 1.540   1.00 53.92  ?  180 PHE A CE1 1 
ATOM   152  C CE2 . PHE A 1 25  ? 22.520  31.304 -0.749  1.00 54.14  ?  180 PHE A CE2 1 
ATOM   153  C CZ  . PHE A 1 25  ? 21.882  30.801 0.362   1.00 51.92  ?  180 PHE A CZ  1 
ATOM   154  N N   . ASP A 1 26  ? 22.974  38.233 0.710   1.00 50.92  ?  181 ASP A N   1 
ATOM   155  C CA  . ASP A 1 26  ? 23.441  39.589 1.002   1.00 52.04  ?  181 ASP A CA  1 
ATOM   156  C C   . ASP A 1 26  ? 24.016  39.654 2.426   1.00 58.13  ?  181 ASP A C   1 
ATOM   157  O O   . ASP A 1 26  ? 23.314  39.342 3.399   1.00 58.71  ?  181 ASP A O   1 
ATOM   158  C CB  . ASP A 1 26  ? 22.290  40.592 0.821   1.00 54.32  ?  181 ASP A CB  1 
ATOM   159  C CG  . ASP A 1 26  ? 22.629  42.075 0.899   1.00 69.22  ?  181 ASP A CG  1 
ATOM   160  O OD1 . ASP A 1 26  ? 23.770  42.415 1.293   1.00 70.92  ?  181 ASP A OD1 1 
ATOM   161  O OD2 . ASP A 1 26  ? 21.749  42.899 0.581   1.00 77.53  -1 181 ASP A OD2 1 
ATOM   162  N N   . GLU A 1 27  ? 25.311  40.010 2.527   1.00 54.18  ?  182 GLU A N   1 
ATOM   163  C CA  . GLU A 1 27  ? 26.025  40.064 3.800   1.00 53.92  ?  182 GLU A CA  1 
ATOM   164  C C   . GLU A 1 27  ? 25.795  41.352 4.631   1.00 55.40  ?  182 GLU A C   1 
ATOM   165  O O   . GLU A 1 27  ? 26.226  41.437 5.788   1.00 54.77  ?  182 GLU A O   1 
ATOM   166  C CB  . GLU A 1 27  ? 27.506  39.706 3.618   1.00 55.83  ?  182 GLU A CB  1 
ATOM   167  C CG  . GLU A 1 27  ? 27.739  38.212 3.380   1.00 73.56  ?  182 GLU A CG  1 
ATOM   168  C CD  . GLU A 1 27  ? 28.431  37.435 4.488   1.00 102.08 ?  182 GLU A CD  1 
ATOM   169  O OE1 . GLU A 1 27  ? 29.108  36.430 4.167   1.00 109.39 ?  182 GLU A OE1 1 
ATOM   170  O OE2 . GLU A 1 27  ? 28.289  37.818 5.673   1.00 86.43  -1 182 GLU A OE2 1 
ATOM   171  N N   . ARG A 1 28  ? 25.054  42.321 4.067   1.00 49.93  ?  183 ARG A N   1 
ATOM   172  C CA  . ARG A 1 28  ? 24.688  43.562 4.762   1.00 48.54  ?  183 ARG A CA  1 
ATOM   173  C C   . ARG A 1 28  ? 23.642  43.232 5.838   1.00 51.33  ?  183 ARG A C   1 
ATOM   174  O O   . ARG A 1 28  ? 22.829  42.311 5.627   1.00 49.91  ?  183 ARG A O   1 
ATOM   175  C CB  . ARG A 1 28  ? 24.096  44.570 3.783   1.00 48.96  ?  183 ARG A CB  1 
ATOM   176  C CG  . ARG A 1 28  ? 25.053  45.674 3.379   1.00 64.02  ?  183 ARG A CG  1 
ATOM   177  C CD  . ARG A 1 28  ? 24.536  46.448 2.187   1.00 83.49  ?  183 ARG A CD  1 
ATOM   178  N NE  . ARG A 1 28  ? 23.355  47.258 2.498   1.00 107.72 ?  183 ARG A NE  1 
ATOM   179  C CZ  . ARG A 1 28  ? 22.101  46.936 2.169   1.00 133.27 ?  183 ARG A CZ  1 
ATOM   180  N NH1 . ARG A 1 28  ? 21.849  45.825 1.483   1.00 122.78 ?  183 ARG A NH1 1 
ATOM   181  N NH2 . ARG A 1 28  ? 21.098  47.749 2.477   1.00 123.57 1  183 ARG A NH2 1 
ATOM   182  N N   . PRO A 1 29  ? 23.650  43.944 7.001   1.00 45.42  ?  184 PRO A N   1 
ATOM   183  C CA  . PRO A 1 29  ? 22.692  43.631 8.055   1.00 43.79  ?  184 PRO A CA  1 
ATOM   184  C C   . PRO A 1 29  ? 21.266  43.977 7.666   1.00 47.27  ?  184 PRO A C   1 
ATOM   185  O O   . PRO A 1 29  ? 21.024  44.897 6.879   1.00 46.21  ?  184 PRO A O   1 
ATOM   186  C CB  . PRO A 1 29  ? 23.161  44.497 9.228   1.00 45.12  ?  184 PRO A CB  1 
ATOM   187  C CG  . PRO A 1 29  ? 24.515  44.892 8.911   1.00 49.33  ?  184 PRO A CG  1 
ATOM   188  C CD  . PRO A 1 29  ? 24.530  45.040 7.430   1.00 46.05  ?  184 PRO A CD  1 
ATOM   189  N N   . ILE A 1 30  ? 20.319  43.212 8.226   1.00 44.18  ?  185 ILE A N   1 
ATOM   190  C CA  . ILE A 1 30  ? 18.888  43.387 7.997   1.00 43.43  ?  185 ILE A CA  1 
ATOM   191  C C   . ILE A 1 30  ? 18.403  44.776 8.402   1.00 48.12  ?  185 ILE A C   1 
ATOM   192  O O   . ILE A 1 30  ? 17.492  45.299 7.772   1.00 48.69  ?  185 ILE A O   1 
ATOM   193  C CB  . ILE A 1 30  ? 18.046  42.235 8.626   1.00 45.94  ?  185 ILE A CB  1 
ATOM   194  C CG1 . ILE A 1 30  ? 18.500  41.863 10.078  1.00 46.21  ?  185 ILE A CG1 1 
ATOM   195  C CG2 . ILE A 1 30  ? 18.038  41.031 7.717   1.00 44.34  ?  185 ILE A CG2 1 
ATOM   196  C CD1 . ILE A 1 30  ? 17.397  41.662 11.081  1.00 34.62  ?  185 ILE A CD1 1 
ATOM   197  N N   . SER A 1 31  ? 19.043  45.381 9.417   1.00 46.10  ?  186 SER A N   1 
ATOM   198  C CA  . SER A 1 31  ? 18.760  46.730 9.948   1.00 46.94  ?  186 SER A CA  1 
ATOM   199  C C   . SER A 1 31  ? 19.013  47.851 8.937   1.00 52.77  ?  186 SER A C   1 
ATOM   200  O O   . SER A 1 31  ? 18.515  48.967 9.090   1.00 52.95  ?  186 SER A O   1 
ATOM   201  C CB  . SER A 1 31  ? 19.629  46.987 11.179  1.00 50.78  ?  186 SER A CB  1 
ATOM   202  O OG  . SER A 1 31  ? 21.017  46.854 10.886  1.00 57.89  ?  186 SER A OG  1 
ATOM   203  N N   . VAL A 1 32  ? 19.856  47.557 7.950   1.00 51.71  ?  187 VAL A N   1 
ATOM   204  C CA  . VAL A 1 32  ? 20.340  48.454 6.903   1.00 52.06  ?  187 VAL A CA  1 
ATOM   205  C C   . VAL A 1 32  ? 19.676  48.127 5.547   1.00 55.60  ?  187 VAL A C   1 
ATOM   206  O O   . VAL A 1 32  ? 19.818  48.885 4.588   1.00 57.50  ?  187 VAL A O   1 
ATOM   207  C CB  . VAL A 1 32  ? 21.893  48.370 6.936   1.00 56.89  ?  187 VAL A CB  1 
ATOM   208  C CG1 . VAL A 1 32  ? 22.557  48.584 5.587   1.00 56.81  ?  187 VAL A CG1 1 
ATOM   209  C CG2 . VAL A 1 32  ? 22.443  49.329 7.979   1.00 57.35  ?  187 VAL A CG2 1 
ATOM   210  N N   . GLY A 1 33  ? 18.881  47.060 5.521   1.00 49.27  ?  188 GLY A N   1 
ATOM   211  C CA  . GLY A 1 33  ? 18.154  46.618 4.342   1.00 47.88  ?  188 GLY A CA  1 
ATOM   212  C C   . GLY A 1 33  ? 18.788  45.417 3.677   1.00 52.48  ?  188 GLY A C   1 
ATOM   213  O O   . GLY A 1 33  ? 18.394  45.045 2.565   1.00 52.55  ?  188 GLY A O   1 
ATOM   214  N N   . GLY A 1 34  ? 19.786  44.829 4.347   1.00 47.63  ?  189 GLY A N   1 
ATOM   215  C CA  . GLY A 1 34  ? 20.493  43.660 3.852   1.00 46.30  ?  189 GLY A CA  1 
ATOM   216  C C   . GLY A 1 34  ? 19.826  42.373 4.286   1.00 48.02  ?  189 GLY A C   1 
ATOM   217  O O   . GLY A 1 34  ? 18.664  42.377 4.701   1.00 45.39  ?  189 GLY A O   1 
ATOM   218  N N   . ASN A 1 35  ? 20.567  41.258 4.223   1.00 44.97  ?  190 ASN A N   1 
ATOM   219  C CA  . ASN A 1 35  ? 20.001  39.975 4.611   1.00 43.42  ?  190 ASN A CA  1 
ATOM   220  C C   . ASN A 1 35  ? 20.624  39.288 5.828   1.00 46.09  ?  190 ASN A C   1 
ATOM   221  O O   . ASN A 1 35  ? 19.961  38.440 6.431   1.00 43.39  ?  190 ASN A O   1 
ATOM   222  C CB  . ASN A 1 35  ? 19.884  39.061 3.420   1.00 37.03  ?  190 ASN A CB  1 
ATOM   223  C CG  . ASN A 1 35  ? 18.826  39.539 2.460   1.00 41.67  ?  190 ASN A CG  1 
ATOM   224  O OD1 . ASN A 1 35  ? 18.999  40.522 1.746   1.00 38.19  ?  190 ASN A OD1 1 
ATOM   225  N ND2 . ASN A 1 35  ? 17.703  38.846 2.396   1.00 24.62  ?  190 ASN A ND2 1 
ATOM   226  N N   . LYS A 1 36  ? 21.862  39.681 6.212   1.00 44.32  ?  191 LYS A N   1 
ATOM   227  C CA  . LYS A 1 36  ? 22.570  39.065 7.341   1.00 44.97  ?  191 LYS A CA  1 
ATOM   228  C C   . LYS A 1 36  ? 21.917  39.364 8.690   1.00 49.78  ?  191 LYS A C   1 
ATOM   229  O O   . LYS A 1 36  ? 21.653  40.536 9.031   1.00 49.06  ?  191 LYS A O   1 
ATOM   230  C CB  . LYS A 1 36  ? 24.063  39.451 7.339   1.00 47.70  ?  191 LYS A CB  1 
ATOM   231  C CG  . LYS A 1 36  ? 24.913  38.648 8.332   1.00 52.36  ?  191 LYS A CG  1 
ATOM   232  C CD  . LYS A 1 36  ? 26.386  38.973 8.262   1.00 53.02  ?  191 LYS A CD  1 
ATOM   233  C CE  . LYS A 1 36  ? 27.195  38.207 9.285   1.00 65.35  ?  191 LYS A CE  1 
ATOM   234  N NZ  . LYS A 1 36  ? 28.626  38.634 9.323   1.00 75.51  1  191 LYS A NZ  1 
ATOM   235  N N   . MET A 1 37  ? 21.649  38.279 9.450   1.00 46.15  ?  192 MET A N   1 
ATOM   236  C CA  . MET A 1 37  ? 21.038  38.395 10.782  1.00 45.33  ?  192 MET A CA  1 
ATOM   237  C C   . MET A 1 37  ? 22.046  38.107 11.894  1.00 48.17  ?  192 MET A C   1 
ATOM   238  O O   . MET A 1 37  ? 21.952  38.698 12.969  1.00 47.83  ?  192 MET A O   1 
ATOM   239  C CB  . MET A 1 37  ? 19.782  37.516 10.921  1.00 46.89  ?  192 MET A CB  1 
ATOM   240  C CG  . MET A 1 37  ? 18.644  37.936 9.992   1.00 49.01  ?  192 MET A CG  1 
ATOM   241  S SD  . MET A 1 37  ? 17.040  37.201 10.415  1.00 51.00  ?  192 MET A SD  1 
ATOM   242  C CE  . MET A 1 37  ? 17.324  35.543 10.049  1.00 46.69  ?  192 MET A CE  1 
ATOM   243  N N   . GLY A 1 38  ? 23.035  37.270 11.595  1.00 44.59  ?  193 GLY A N   1 
ATOM   244  C CA  . GLY A 1 38  ? 24.087  36.905 12.539  1.00 45.49  ?  193 GLY A CA  1 
ATOM   245  C C   . GLY A 1 38  ? 24.892  35.712 12.085  1.00 53.09  ?  193 GLY A C   1 
ATOM   246  O O   . GLY A 1 38  ? 24.638  35.156 11.010  1.00 52.59  ?  193 GLY A O   1 
ATOM   247  N N   . GLU A 1 39  ? 25.869  35.312 12.904  1.00 53.47  ?  194 GLU A N   1 
ATOM   248  C CA  . GLU A 1 39  ? 26.772  34.205 12.585  1.00 54.64  ?  194 GLU A CA  1 
ATOM   249  C C   . GLU A 1 39  ? 27.362  33.485 13.783  1.00 61.17  ?  194 GLU A C   1 
ATOM   250  O O   . GLU A 1 39  ? 27.797  34.132 14.737  1.00 60.81  ?  194 GLU A O   1 
ATOM   251  C CB  . GLU A 1 39  ? 27.902  34.643 11.621  1.00 55.88  ?  194 GLU A CB  1 
ATOM   252  C CG  . GLU A 1 39  ? 28.737  35.830 12.062  1.00 68.17  ?  194 GLU A CG  1 
ATOM   253  C CD  . GLU A 1 39  ? 30.043  35.976 11.303  1.00 106.01 ?  194 GLU A CD  1 
ATOM   254  O OE1 . GLU A 1 39  ? 31.112  35.782 11.926  1.00 108.14 ?  194 GLU A OE1 1 
ATOM   255  O OE2 . GLU A 1 39  ? 30.000  36.274 10.087  1.00 103.85 -1 194 GLU A OE2 1 
ATOM   256  N N   . GLY A 1 40  ? 27.409  32.155 13.673  1.00 59.91  ?  195 GLY A N   1 
ATOM   257  C CA  . GLY A 1 40  ? 28.022  31.242 14.632  1.00 61.14  ?  195 GLY A CA  1 
ATOM   258  C C   . GLY A 1 40  ? 29.319  30.687 14.063  1.00 68.68  ?  195 GLY A C   1 
ATOM   259  O O   . GLY A 1 40  ? 29.851  31.226 13.080  1.00 70.68  ?  195 GLY A O   1 
ATOM   260  N N   . GLY A 1 41  ? 29.840  29.623 14.668  1.00 63.94  ?  196 GLY A N   1 
ATOM   261  C CA  . GLY A 1 41  ? 31.073  29.002 14.191  1.00 62.99  ?  196 GLY A CA  1 
ATOM   262  C C   . GLY A 1 41  ? 30.857  28.121 12.976  1.00 65.92  ?  196 GLY A C   1 
ATOM   263  O O   . GLY A 1 41  ? 31.737  28.011 12.115  1.00 65.46  ?  196 GLY A O   1 
ATOM   264  N N   . PHE A 1 42  ? 29.662  27.500 12.896  1.00 62.21  ?  197 PHE A N   1 
ATOM   265  C CA  . PHE A 1 42  ? 29.277  26.591 11.816  1.00 60.91  ?  197 PHE A CA  1 
ATOM   266  C C   . PHE A 1 42  ? 28.419  27.215 10.692  1.00 62.24  ?  197 PHE A C   1 
ATOM   267  O O   . PHE A 1 42  ? 27.979  26.497 9.802   1.00 61.83  ?  197 PHE A O   1 
ATOM   268  C CB  . PHE A 1 42  ? 28.684  25.283 12.377  1.00 62.57  ?  197 PHE A CB  1 
ATOM   269  N N   . GLY A 1 43  ? 28.233  28.533 10.703  1.00 58.25  ?  198 GLY A N   1 
ATOM   270  C CA  . GLY A 1 43  ? 27.482  29.208 9.642   1.00 57.21  ?  198 GLY A CA  1 
ATOM   271  C C   . GLY A 1 43  ? 26.965  30.608 9.919   1.00 58.89  ?  198 GLY A C   1 
ATOM   272  O O   . GLY A 1 43  ? 27.069  31.117 11.039  1.00 59.55  ?  198 GLY A O   1 
ATOM   273  N N   . VAL A 1 44  ? 26.392  31.234 8.873   1.00 52.25  ?  199 VAL A N   1 
ATOM   274  C CA  . VAL A 1 44  ? 25.789  32.577 8.883   1.00 49.98  ?  199 VAL A CA  1 
ATOM   275  C C   . VAL A 1 44  ? 24.288  32.417 8.629   1.00 51.96  ?  199 VAL A C   1 
ATOM   276  O O   . VAL A 1 44  ? 23.884  31.615 7.774   1.00 49.63  ?  199 VAL A O   1 
ATOM   277  C CB  . VAL A 1 44  ? 26.468  33.558 7.849   1.00 52.95  ?  199 VAL A CB  1 
ATOM   278  C CG1 . VAL A 1 44  ? 25.817  34.957 7.846   1.00 52.42  ?  199 VAL A CG1 1 
ATOM   279  C CG2 . VAL A 1 44  ? 27.970  33.674 8.092   1.00 52.07  ?  199 VAL A CG2 1 
ATOM   280  N N   . VAL A 1 45  ? 23.463  33.196 9.380   1.00 49.47  ?  200 VAL A N   1 
ATOM   281  C CA  . VAL A 1 45  ? 22.002  33.179 9.274   1.00 48.25  ?  200 VAL A CA  1 
ATOM   282  C C   . VAL A 1 45  ? 21.504  34.394 8.499   1.00 48.89  ?  200 VAL A C   1 
ATOM   283  O O   . VAL A 1 45  ? 21.873  35.534 8.816   1.00 47.94  ?  200 VAL A O   1 
ATOM   284  C CB  . VAL A 1 45  ? 21.314  32.993 10.660  1.00 52.04  ?  200 VAL A CB  1 
ATOM   285  C CG1 . VAL A 1 45  ? 19.804  32.778 10.516  1.00 51.80  ?  200 VAL A CG1 1 
ATOM   286  C CG2 . VAL A 1 45  ? 21.935  31.821 11.430  1.00 51.17  ?  200 VAL A CG2 1 
ATOM   287  N N   . TYR A 1 46  ? 20.689  34.133 7.461   1.00 45.46  ?  201 TYR A N   1 
ATOM   288  C CA  . TYR A 1 46  ? 20.097  35.151 6.575   1.00 45.19  ?  201 TYR A CA  1 
ATOM   289  C C   . TYR A 1 46  ? 18.564  35.194 6.657   1.00 47.32  ?  201 TYR A C   1 
ATOM   290  O O   . TYR A 1 46  ? 17.921  34.158 6.845   1.00 47.35  ?  201 TYR A O   1 
ATOM   291  C CB  . TYR A 1 46  ? 20.503  34.900 5.102   1.00 47.10  ?  201 TYR A CB  1 
ATOM   292  C CG  . TYR A 1 46  ? 21.999  34.865 4.872   1.00 50.97  ?  201 TYR A CG  1 
ATOM   293  C CD1 . TYR A 1 46  ? 22.724  33.680 5.026   1.00 52.63  ?  201 TYR A CD1 1 
ATOM   294  C CD2 . TYR A 1 46  ? 22.696  36.018 4.505   1.00 52.50  ?  201 TYR A CD2 1 
ATOM   295  C CE1 . TYR A 1 46  ? 24.106  33.651 4.842   1.00 53.39  ?  201 TYR A CE1 1 
ATOM   296  C CE2 . TYR A 1 46  ? 24.078  36.001 4.320   1.00 54.05  ?  201 TYR A CE2 1 
ATOM   297  C CZ  . TYR A 1 46  ? 24.778  34.814 4.479   1.00 63.77  ?  201 TYR A CZ  1 
ATOM   298  O OH  . TYR A 1 46  ? 26.141  34.805 4.273   1.00 69.33  ?  201 TYR A OH  1 
ATOM   299  N N   . LYS A 1 47  ? 17.983  36.382 6.441   1.00 41.99  ?  202 LYS A N   1 
ATOM   300  C CA  . LYS A 1 47  ? 16.532  36.565 6.352   1.00 40.31  ?  202 LYS A CA  1 
ATOM   301  C C   . LYS A 1 47  ? 16.069  36.325 4.903   1.00 40.46  ?  202 LYS A C   1 
ATOM   302  O O   . LYS A 1 47  ? 16.786  36.622 3.949   1.00 38.12  ?  202 LYS A O   1 
ATOM   303  C CB  . LYS A 1 47  ? 16.127  37.983 6.797   1.00 42.07  ?  202 LYS A CB  1 
ATOM   304  C CG  . LYS A 1 47  ? 14.640  38.125 7.205   1.00 31.68  ?  202 LYS A CG  1 
ATOM   305  C CD  . LYS A 1 47  ? 14.343  39.557 7.619   1.00 35.66  ?  202 LYS A CD  1 
ATOM   306  C CE  . LYS A 1 47  ? 12.874  39.848 7.768   1.00 44.51  ?  202 LYS A CE  1 
ATOM   307  N NZ  . LYS A 1 47  ? 12.621  41.238 8.217   1.00 55.37  1  202 LYS A NZ  1 
ATOM   308  N N   . GLY A 1 48  ? 14.860  35.810 4.760   1.00 37.70  ?  203 GLY A N   1 
ATOM   309  C CA  . GLY A 1 48  ? 14.261  35.591 3.451   1.00 37.79  ?  203 GLY A CA  1 
ATOM   310  C C   . GLY A 1 48  ? 12.753  35.503 3.486   1.00 40.98  ?  203 GLY A C   1 
ATOM   311  O O   . GLY A 1 48  ? 12.139  35.560 4.559   1.00 40.55  ?  203 GLY A O   1 
ATOM   312  N N   . TYR A 1 49  ? 12.154  35.336 2.313   1.00 36.93  ?  204 TYR A N   1 
ATOM   313  C CA  . TYR A 1 49  ? 10.716  35.134 2.205   1.00 36.30  ?  204 TYR A CA  1 
ATOM   314  C C   . TYR A 1 49  ? 10.433  34.010 1.234   1.00 42.20  ?  204 TYR A C   1 
ATOM   315  O O   . TYR A 1 49  ? 10.839  34.080 0.064   1.00 42.58  ?  204 TYR A O   1 
ATOM   316  C CB  . TYR A 1 49  ? 9.991   36.414 1.808   1.00 37.07  ?  204 TYR A CB  1 
ATOM   317  C CG  . TYR A 1 49  ? 10.117  37.531 2.814   1.00 41.26  ?  204 TYR A CG  1 
ATOM   318  C CD1 . TYR A 1 49  ? 9.271   37.600 3.924   1.00 44.05  ?  204 TYR A CD1 1 
ATOM   319  C CD2 . TYR A 1 49  ? 11.035  38.558 2.633   1.00 42.75  ?  204 TYR A CD2 1 
ATOM   320  C CE1 . TYR A 1 49  ? 9.362   38.649 4.844   1.00 44.76  ?  204 TYR A CE1 1 
ATOM   321  C CE2 . TYR A 1 49  ? 11.129  39.618 3.541   1.00 43.99  ?  204 TYR A CE2 1 
ATOM   322  C CZ  . TYR A 1 49  ? 10.289  39.659 4.648   1.00 52.50  ?  204 TYR A CZ  1 
ATOM   323  O OH  . TYR A 1 49  ? 10.344  40.688 5.563   1.00 55.46  ?  204 TYR A OH  1 
ATOM   324  N N   . VAL A 1 50  ? 9.817   32.941 1.740   1.00 40.30  ?  205 VAL A N   1 
ATOM   325  C CA  . VAL A 1 50  ? 9.435   31.776 0.945   1.00 41.55  ?  205 VAL A CA  1 
ATOM   326  C C   . VAL A 1 50  ? 7.914   31.698 1.035   1.00 47.66  ?  205 VAL A C   1 
ATOM   327  O O   . VAL A 1 50  ? 7.377   31.417 2.108   1.00 48.15  ?  205 VAL A O   1 
ATOM   328  C CB  . VAL A 1 50  ? 10.123  30.458 1.410   1.00 46.06  ?  205 VAL A CB  1 
ATOM   329  C CG1 . VAL A 1 50  ? 9.662   29.262 0.579   1.00 46.36  ?  205 VAL A CG1 1 
ATOM   330  C CG2 . VAL A 1 50  ? 11.626  30.581 1.325   1.00 45.95  ?  205 VAL A CG2 1 
ATOM   331  N N   . ASN A 1 51  ? 7.221   32.011 -0.075  1.00 44.36  ?  206 ASN A N   1 
ATOM   332  C CA  . ASN A 1 51  ? 5.752   31.968 -0.203  1.00 43.14  ?  206 ASN A CA  1 
ATOM   333  C C   . ASN A 1 51  ? 5.028   32.792 0.901   1.00 44.16  ?  206 ASN A C   1 
ATOM   334  O O   . ASN A 1 51  ? 4.141   32.309 1.612   1.00 44.12  ?  206 ASN A O   1 
ATOM   335  C CB  . ASN A 1 51  ? 5.286   30.497 -0.315  1.00 42.77  ?  206 ASN A CB  1 
ATOM   336  C CG  . ASN A 1 51  ? 3.826   30.279 -0.531  1.00 56.29  ?  206 ASN A CG  1 
ATOM   337  O OD1 . ASN A 1 51  ? 3.229   29.422 0.114   1.00 53.74  ?  206 ASN A OD1 1 
ATOM   338  N ND2 . ASN A 1 51  ? 3.221   31.035 -1.429  1.00 45.49  ?  206 ASN A ND2 1 
ATOM   339  N N   . ASN A 1 52  ? 5.464   34.050 1.042   1.00 39.10  ?  207 ASN A N   1 
ATOM   340  C CA  . ASN A 1 52  ? 4.968   35.056 1.985   1.00 38.09  ?  207 ASN A CA  1 
ATOM   341  C C   . ASN A 1 52  ? 5.406   34.801 3.417   1.00 40.94  ?  207 ASN A C   1 
ATOM   342  O O   . ASN A 1 52  ? 5.330   35.713 4.249   1.00 41.18  ?  207 ASN A O   1 
ATOM   343  C CB  . ASN A 1 52  ? 3.468   35.319 1.826   1.00 37.77  ?  207 ASN A CB  1 
ATOM   344  C CG  . ASN A 1 52  ? 3.065   35.944 0.501   1.00 48.96  ?  207 ASN A CG  1 
ATOM   345  O OD1 . ASN A 1 52  ? 3.888   36.469 -0.277  1.00 40.36  ?  207 ASN A OD1 1 
ATOM   346  N ND2 . ASN A 1 52  ? 1.767   36.004 0.267   1.00 39.95  ?  207 ASN A ND2 1 
ATOM   347  N N   . THR A 1 53  ? 6.001   33.602 3.656   1.00 36.17  ?  208 THR A N   1 
ATOM   348  C CA  . THR A 1 53  ? 6.560   33.151 4.935   1.00 35.43  ?  208 THR A CA  1 
ATOM   349  C C   . THR A 1 53  ? 7.954   33.765 5.160   1.00 38.45  ?  208 THR A C   1 
ATOM   350  O O   . THR A 1 53  ? 8.824   33.588 4.319   1.00 38.06  ?  208 THR A O   1 
ATOM   351  C CB  . THR A 1 53  ? 6.619   31.593 4.951   1.00 39.35  ?  208 THR A CB  1 
ATOM   352  O OG1 . THR A 1 53  ? 5.326   31.042 4.664   1.00 43.43  ?  208 THR A OG1 1 
ATOM   353  C CG2 . THR A 1 53  ? 7.147   31.021 6.251   1.00 31.16  ?  208 THR A CG2 1 
ATOM   354  N N   . THR A 1 54  ? 8.168   34.468 6.294   1.00 36.01  ?  209 THR A N   1 
ATOM   355  C CA  . THR A 1 54  ? 9.499   34.996 6.649   1.00 35.57  ?  209 THR A CA  1 
ATOM   356  C C   . THR A 1 54  ? 10.264  33.803 7.217   1.00 41.58  ?  209 THR A C   1 
ATOM   357  O O   . THR A 1 54  ? 9.769   33.104 8.118   1.00 42.56  ?  209 THR A O   1 
ATOM   358  C CB  . THR A 1 54  ? 9.460   36.138 7.695   1.00 42.21  ?  209 THR A CB  1 
ATOM   359  O OG1 . THR A 1 54  ? 8.355   37.014 7.459   1.00 51.44  ?  209 THR A OG1 1 
ATOM   360  C CG2 . THR A 1 54  ? 10.732  36.936 7.705   1.00 36.91  ?  209 THR A CG2 1 
ATOM   361  N N   . VAL A 1 55  ? 11.454  33.553 6.683   1.00 37.16  ?  210 VAL A N   1 
ATOM   362  C CA  . VAL A 1 55  ? 12.275  32.415 7.061   1.00 35.83  ?  210 VAL A CA  1 
ATOM   363  C C   . VAL A 1 55  ? 13.657  32.883 7.559   1.00 43.71  ?  210 VAL A C   1 
ATOM   364  O O   . VAL A 1 55  ? 14.095  34.000 7.266   1.00 44.90  ?  210 VAL A O   1 
ATOM   365  C CB  . VAL A 1 55  ? 12.416  31.434 5.839   1.00 38.24  ?  210 VAL A CB  1 
ATOM   366  C CG1 . VAL A 1 55  ? 11.078  30.858 5.392   1.00 37.71  ?  210 VAL A CG1 1 
ATOM   367  C CG2 . VAL A 1 55  ? 13.139  32.073 4.649   1.00 37.62  ?  210 VAL A CG2 1 
ATOM   368  N N   . ALA A 1 56  ? 14.356  32.004 8.281   1.00 40.67  ?  211 ALA A N   1 
ATOM   369  C CA  . ALA A 1 56  ? 15.755  32.178 8.689   1.00 39.01  ?  211 ALA A CA  1 
ATOM   370  C C   . ALA A 1 56  ? 16.520  31.072 7.946   1.00 40.70  ?  211 ALA A C   1 
ATOM   371  O O   . ALA A 1 56  ? 16.162  29.889 8.038   1.00 38.29  ?  211 ALA A O   1 
ATOM   372  C CB  . ALA A 1 56  ? 15.916  32.009 10.185  1.00 39.30  ?  211 ALA A CB  1 
ATOM   373  N N   . VAL A 1 57  ? 17.504  31.469 7.135   1.00 38.31  ?  212 VAL A N   1 
ATOM   374  C CA  . VAL A 1 57  ? 18.280  30.509 6.353   1.00 38.83  ?  212 VAL A CA  1 
ATOM   375  C C   . VAL A 1 57  ? 19.689  30.430 6.909   1.00 44.24  ?  212 VAL A C   1 
ATOM   376  O O   . VAL A 1 57  ? 20.439  31.420 6.846   1.00 43.28  ?  212 VAL A O   1 
ATOM   377  C CB  . VAL A 1 57  ? 18.263  30.778 4.819   1.00 41.65  ?  212 VAL A CB  1 
ATOM   378  C CG1 . VAL A 1 57  ? 18.962  29.646 4.066   1.00 40.91  ?  212 VAL A CG1 1 
ATOM   379  C CG2 . VAL A 1 57  ? 16.838  30.973 4.300   1.00 40.83  ?  212 VAL A CG2 1 
ATOM   380  N N   . LYS A 1 58  ? 20.029  29.269 7.496   1.00 41.60  ?  213 LYS A N   1 
ATOM   381  C CA  . LYS A 1 58  ? 21.361  29.066 8.043   1.00 42.60  ?  213 LYS A CA  1 
ATOM   382  C C   . LYS A 1 58  ? 22.215  28.409 6.958   1.00 50.39  ?  213 LYS A C   1 
ATOM   383  O O   . LYS A 1 58  ? 21.969  27.245 6.609   1.00 49.77  ?  213 LYS A O   1 
ATOM   384  C CB  . LYS A 1 58  ? 21.310  28.188 9.303   1.00 43.82  ?  213 LYS A CB  1 
ATOM   385  C CG  . LYS A 1 58  ? 22.598  28.218 10.133  1.00 38.34  ?  213 LYS A CG  1 
ATOM   386  C CD  . LYS A 1 58  ? 22.794  26.907 10.828  1.00 49.66  ?  213 LYS A CD  1 
ATOM   387  C CE  . LYS A 1 58  ? 22.676  26.968 12.328  1.00 60.22  ?  213 LYS A CE  1 
ATOM   388  N NZ  . LYS A 1 58  ? 22.517  25.604 12.918  1.00 65.84  1  213 LYS A NZ  1 
ATOM   389  N N   . LYS A 1 59  ? 23.182  29.170 6.392   1.00 48.73  ?  214 LYS A N   1 
ATOM   390  C CA  . LYS A 1 59  ? 24.101  28.648 5.383   1.00 49.57  ?  214 LYS A CA  1 
ATOM   391  C C   . LYS A 1 59  ? 25.341  28.151 6.120   1.00 57.38  ?  214 LYS A C   1 
ATOM   392  O O   . LYS A 1 59  ? 26.099  28.959 6.674   1.00 57.27  ?  214 LYS A O   1 
ATOM   393  C CB  . LYS A 1 59  ? 24.452  29.710 4.333   1.00 51.37  ?  214 LYS A CB  1 
ATOM   394  C CG  . LYS A 1 59  ? 25.113  29.115 3.085   1.00 63.21  ?  214 LYS A CG  1 
ATOM   395  C CD  . LYS A 1 59  ? 25.619  30.207 2.117   1.00 71.99  ?  214 LYS A CD  1 
ATOM   396  C CE  . LYS A 1 59  ? 27.032  30.668 2.402   1.00 82.78  ?  214 LYS A CE  1 
ATOM   397  N NZ  . LYS A 1 59  ? 27.395  31.877 1.623   1.00 97.17  1  214 LYS A NZ  1 
ATOM   398  N N   . LEU A 1 60  ? 25.508  26.812 6.173   1.00 57.00  ?  215 LEU A N   1 
ATOM   399  C CA  . LEU A 1 60  ? 26.614  26.128 6.861   1.00 57.71  ?  215 LEU A CA  1 
ATOM   400  C C   . LEU A 1 60  ? 27.967  26.456 6.257   1.00 62.54  ?  215 LEU A C   1 
ATOM   401  O O   . LEU A 1 60  ? 28.145  26.362 5.038   1.00 61.10  ?  215 LEU A O   1 
ATOM   402  C CB  . LEU A 1 60  ? 26.382  24.610 6.906   1.00 57.46  ?  215 LEU A CB  1 
ATOM   403  C CG  . LEU A 1 60  ? 25.740  24.032 8.171   1.00 61.36  ?  215 LEU A CG  1 
ATOM   404  C CD1 . LEU A 1 60  ? 24.337  24.540 8.369   1.00 61.47  ?  215 LEU A CD1 1 
ATOM   405  C CD2 . LEU A 1 60  ? 25.661  22.536 8.080   1.00 63.16  ?  215 LEU A CD2 1 
ATOM   406  N N   . ALA A 1 61  ? 28.899  26.896 7.116   1.00 61.51  ?  216 ALA A N   1 
ATOM   407  C CA  . ALA A 1 61  ? 30.256  27.295 6.727   1.00 62.73  ?  216 ALA A CA  1 
ATOM   408  C C   . ALA A 1 61  ? 31.293  26.773 7.718   1.00 66.98  ?  216 ALA A C   1 
ATOM   409  O O   . ALA A 1 61  ? 31.110  26.902 8.931   1.00 65.73  ?  216 ALA A O   1 
ATOM   410  C CB  . ALA A 1 61  ? 30.344  28.815 6.631   1.00 63.80  ?  216 ALA A CB  1 
ATOM   411  N N   . ALA A 1 62  ? 32.387  26.200 7.197   1.00 65.24  ?  217 ALA A N   1 
ATOM   412  C CA  . ALA A 1 62  ? 33.482  25.657 8.010   1.00 105.75 ?  217 ALA A CA  1 
ATOM   413  C C   . ALA A 1 62  ? 34.494  26.741 8.400   1.00 119.35 ?  217 ALA A C   1 
ATOM   414  O O   . ALA A 1 62  ? 34.113  27.789 8.927   1.00 71.47  ?  217 ALA A O   1 
ATOM   415  C CB  . ALA A 1 62  ? 34.177  24.532 7.261   1.00 106.51 ?  217 ALA A CB  1 
ATOM   416  N N   . THR A 1 67  ? 35.587  20.899 9.229   1.00 81.72  ?  222 THR A N   1 
ATOM   417  C CA  . THR A 1 67  ? 35.695  19.940 8.127   1.00 82.52  ?  222 THR A CA  1 
ATOM   418  C C   . THR A 1 67  ? 34.346  19.512 7.504   1.00 86.04  ?  222 THR A C   1 
ATOM   419  O O   . THR A 1 67  ? 33.352  19.361 8.226   1.00 85.74  ?  222 THR A O   1 
ATOM   420  C CB  . THR A 1 67  ? 36.635  18.766 8.474   1.00 96.78  ?  222 THR A CB  1 
ATOM   421  O OG1 . THR A 1 67  ? 36.961  18.056 7.274   1.00 98.37  ?  222 THR A OG1 1 
ATOM   422  C CG2 . THR A 1 67  ? 36.048  17.805 9.515   1.00 96.77  ?  222 THR A CG2 1 
ATOM   423  N N   . THR A 1 68  ? 34.341  19.287 6.167   1.00 81.37  ?  223 THR A N   1 
ATOM   424  C CA  . THR A 1 68  ? 33.160  18.932 5.357   1.00 80.38  ?  223 THR A CA  1 
ATOM   425  C C   . THR A 1 68  ? 32.353  17.717 5.792   1.00 82.28  ?  223 THR A C   1 
ATOM   426  O O   . THR A 1 68  ? 31.126  17.770 5.734   1.00 81.68  ?  223 THR A O   1 
ATOM   427  C CB  . THR A 1 68  ? 33.474  18.886 3.863   1.00 86.22  ?  223 THR A CB  1 
ATOM   428  O OG1 . THR A 1 68  ? 34.532  17.957 3.648   1.00 90.23  ?  223 THR A OG1 1 
ATOM   429  C CG2 . THR A 1 68  ? 33.820  20.251 3.291   1.00 81.95  ?  223 THR A CG2 1 
ATOM   430  N N   . GLU A 1 69  ? 33.011  16.626 6.208   1.00 77.98  ?  224 GLU A N   1 
ATOM   431  C CA  . GLU A 1 69  ? 32.266  15.440 6.633   1.00 77.38  ?  224 GLU A CA  1 
ATOM   432  C C   . GLU A 1 69  ? 31.617  15.651 8.002   1.00 78.40  ?  224 GLU A C   1 
ATOM   433  O O   . GLU A 1 69  ? 30.538  15.114 8.262   1.00 77.28  ?  224 GLU A O   1 
ATOM   434  C CB  . GLU A 1 69  ? 33.130  14.172 6.590   1.00 78.98  ?  224 GLU A CB  1 
ATOM   435  C CG  . GLU A 1 69  ? 32.428  12.999 5.928   1.00 91.42  ?  224 GLU A CG  1 
ATOM   436  C CD  . GLU A 1 69  ? 31.317  12.375 6.749   1.00 112.75 ?  224 GLU A CD  1 
ATOM   437  O OE1 . GLU A 1 69  ? 31.623  11.518 7.610   1.00 112.23 ?  224 GLU A OE1 1 
ATOM   438  O OE2 . GLU A 1 69  ? 30.142  12.757 6.546   1.00 99.53  -1 224 GLU A OE2 1 
ATOM   439  N N   . GLU A 1 70  ? 32.260  16.481 8.850   1.00 74.14  ?  225 GLU A N   1 
ATOM   440  C CA  . GLU A 1 70  ? 31.749  16.841 10.172  1.00 73.50  ?  225 GLU A CA  1 
ATOM   441  C C   . GLU A 1 70  ? 30.563  17.775 10.029  1.00 74.65  ?  225 GLU A C   1 
ATOM   442  O O   . GLU A 1 70  ? 29.557  17.578 10.712  1.00 74.70  ?  225 GLU A O   1 
ATOM   443  C CB  . GLU A 1 70  ? 32.829  17.478 11.062  1.00 75.17  ?  225 GLU A CB  1 
ATOM   444  C CG  . GLU A 1 70  ? 33.055  16.740 12.375  1.00 89.43  ?  225 GLU A CG  1 
ATOM   445  C CD  . GLU A 1 70  ? 31.871  16.629 13.329  1.00 117.98 ?  225 GLU A CD  1 
ATOM   446  O OE1 . GLU A 1 70  ? 31.161  15.598 13.272  1.00 102.97 ?  225 GLU A OE1 1 
ATOM   447  O OE2 . GLU A 1 70  ? 31.674  17.551 14.154  1.00 115.65 -1 225 GLU A OE2 1 
ATOM   448  N N   . LEU A 1 71  ? 30.669  18.770 9.110   1.00 68.25  ?  226 LEU A N   1 
ATOM   449  C CA  . LEU A 1 71  ? 29.603  19.725 8.794   1.00 66.23  ?  226 LEU A CA  1 
ATOM   450  C C   . LEU A 1 71  ? 28.371  18.941 8.320   1.00 65.41  ?  226 LEU A C   1 
ATOM   451  O O   . LEU A 1 71  ? 27.295  19.117 8.901   1.00 64.70  ?  226 LEU A O   1 
ATOM   452  C CB  . LEU A 1 71  ? 30.077  20.728 7.725   1.00 66.29  ?  226 LEU A CB  1 
ATOM   453  C CG  . LEU A 1 71  ? 29.820  22.223 7.972   1.00 70.84  ?  226 LEU A CG  1 
ATOM   454  C CD1 . LEU A 1 71  ? 30.681  22.771 9.117   1.00 71.12  ?  226 LEU A CD1 1 
ATOM   455  C CD2 . LEU A 1 71  ? 30.150  23.027 6.737   1.00 72.10  ?  226 LEU A CD2 1 
ATOM   456  N N   . LYS A 1 72  ? 28.552  18.002 7.344   1.00 58.31  ?  227 LYS A N   1 
ATOM   457  C CA  . LYS A 1 72  ? 27.471  17.137 6.856   1.00 56.83  ?  227 LYS A CA  1 
ATOM   458  C C   . LYS A 1 72  ? 26.864  16.360 8.021   1.00 58.59  ?  227 LYS A C   1 
ATOM   459  O O   . LYS A 1 72  ? 25.646  16.337 8.152   1.00 57.47  ?  227 LYS A O   1 
ATOM   460  C CB  . LYS A 1 72  ? 27.930  16.191 5.732   1.00 58.24  ?  227 LYS A CB  1 
ATOM   461  N N   . GLN A 1 73  ? 27.704  15.825 8.922   1.00 54.93  ?  228 GLN A N   1 
ATOM   462  C CA  . GLN A 1 73  ? 27.225  15.096 10.098  1.00 54.84  ?  228 GLN A CA  1 
ATOM   463  C C   . GLN A 1 73  ? 26.380  15.992 11.023  1.00 60.23  ?  228 GLN A C   1 
ATOM   464  O O   . GLN A 1 73  ? 25.311  15.563 11.446  1.00 61.13  ?  228 GLN A O   1 
ATOM   465  C CB  . GLN A 1 73  ? 28.373  14.412 10.846  1.00 55.59  ?  228 GLN A CB  1 
ATOM   466  N N   . GLN A 1 74  ? 26.816  17.252 11.257  1.00 56.26  ?  229 GLN A N   1 
ATOM   467  C CA  . GLN A 1 74  ? 26.091  18.233 12.067  1.00 56.37  ?  229 GLN A CA  1 
ATOM   468  C C   . GLN A 1 74  ? 24.758  18.651 11.397  1.00 61.58  ?  229 GLN A C   1 
ATOM   469  O O   . GLN A 1 74  ? 23.750  18.846 12.088  1.00 62.13  ?  229 GLN A O   1 
ATOM   470  C CB  . GLN A 1 74  ? 26.965  19.464 12.349  1.00 58.01  ?  229 GLN A CB  1 
ATOM   471  C CG  . GLN A 1 74  ? 27.912  19.295 13.537  1.00 76.90  ?  229 GLN A CG  1 
ATOM   472  C CD  . GLN A 1 74  ? 29.056  20.279 13.559  1.00 100.97 ?  229 GLN A CD  1 
ATOM   473  O OE1 . GLN A 1 74  ? 28.975  21.401 13.044  1.00 97.39  ?  229 GLN A OE1 1 
ATOM   474  N NE2 . GLN A 1 74  ? 30.156  19.880 14.183  1.00 97.25  ?  229 GLN A NE2 1 
ATOM   475  N N   . PHE A 1 75  ? 24.758  18.752 10.049  1.00 56.52  ?  230 PHE A N   1 
ATOM   476  C CA  . PHE A 1 75  ? 23.605  19.061 9.205   1.00 55.01  ?  230 PHE A CA  1 
ATOM   477  C C   . PHE A 1 75  ? 22.564  17.942 9.348   1.00 58.00  ?  230 PHE A C   1 
ATOM   478  O O   . PHE A 1 75  ? 21.412  18.231 9.665   1.00 58.20  ?  230 PHE A O   1 
ATOM   479  C CB  . PHE A 1 75  ? 24.079  19.191 7.740   1.00 56.67  ?  230 PHE A CB  1 
ATOM   480  C CG  . PHE A 1 75  ? 23.017  19.393 6.682   1.00 57.49  ?  230 PHE A CG  1 
ATOM   481  C CD1 . PHE A 1 75  ? 22.521  20.662 6.405   1.00 59.52  ?  230 PHE A CD1 1 
ATOM   482  C CD2 . PHE A 1 75  ? 22.532  18.318 5.942   1.00 58.51  ?  230 PHE A CD2 1 
ATOM   483  C CE1 . PHE A 1 75  ? 21.542  20.847 5.422   1.00 60.52  ?  230 PHE A CE1 1 
ATOM   484  C CE2 . PHE A 1 75  ? 21.553  18.507 4.957   1.00 60.62  ?  230 PHE A CE2 1 
ATOM   485  C CZ  . PHE A 1 75  ? 21.068  19.769 4.700   1.00 58.79  ?  230 PHE A CZ  1 
ATOM   486  N N   . ASP A 1 76  ? 22.976  16.665 9.156   1.00 53.53  ?  231 ASP A N   1 
ATOM   487  C CA  . ASP A 1 76  ? 22.122  15.474 9.272   1.00 52.55  ?  231 ASP A CA  1 
ATOM   488  C C   . ASP A 1 76  ? 21.565  15.324 10.692  1.00 56.50  ?  231 ASP A C   1 
ATOM   489  O O   . ASP A 1 76  ? 20.437  14.839 10.871  1.00 55.74  ?  231 ASP A O   1 
ATOM   490  C CB  . ASP A 1 76  ? 22.918  14.211 8.915   1.00 53.78  ?  231 ASP A CB  1 
ATOM   491  C CG  . ASP A 1 76  ? 23.483  14.142 7.515   1.00 60.60  ?  231 ASP A CG  1 
ATOM   492  O OD1 . ASP A 1 76  ? 22.765  14.522 6.563   1.00 61.71  ?  231 ASP A OD1 1 
ATOM   493  O OD2 . ASP A 1 76  ? 24.618  13.643 7.360   1.00 65.71  -1 231 ASP A OD2 1 
ATOM   494  N N   . GLN A 1 77  ? 22.379  15.725 11.690  1.00 52.92  ?  232 GLN A N   1 
ATOM   495  C CA  . GLN A 1 77  ? 22.046  15.691 13.113  1.00 53.87  ?  232 GLN A CA  1 
ATOM   496  C C   . GLN A 1 77  ? 20.901  16.652 13.467  1.00 59.15  ?  232 GLN A C   1 
ATOM   497  O O   . GLN A 1 77  ? 20.020  16.289 14.253  1.00 60.18  ?  232 GLN A O   1 
ATOM   498  C CB  . GLN A 1 77  ? 23.293  16.001 13.969  1.00 55.46  ?  232 GLN A CB  1 
ATOM   499  C CG  . GLN A 1 77  ? 23.139  15.712 15.471  1.00 68.16  ?  232 GLN A CG  1 
ATOM   500  C CD  . GLN A 1 77  ? 22.691  14.295 15.754  1.00 81.17  ?  232 GLN A CD  1 
ATOM   501  O OE1 . GLN A 1 77  ? 23.224  13.315 15.209  1.00 71.14  ?  232 GLN A OE1 1 
ATOM   502  N NE2 . GLN A 1 77  ? 21.682  14.164 16.601  1.00 74.59  ?  232 GLN A NE2 1 
ATOM   503  N N   . GLU A 1 78  ? 20.943  17.879 12.916  1.00 54.02  ?  233 GLU A N   1 
ATOM   504  C CA  . GLU A 1 78  ? 19.932  18.907 13.116  1.00 53.52  ?  233 GLU A CA  1 
ATOM   505  C C   . GLU A 1 78  ? 18.588  18.428 12.554  1.00 58.13  ?  233 GLU A C   1 
ATOM   506  O O   . GLU A 1 78  ? 17.557  18.580 13.223  1.00 57.92  ?  233 GLU A O   1 
ATOM   507  C CB  . GLU A 1 78  ? 20.377  20.214 12.449  1.00 54.86  ?  233 GLU A CB  1 
ATOM   508  C CG  . GLU A 1 78  ? 19.474  21.396 12.740  1.00 66.39  ?  233 GLU A CG  1 
ATOM   509  C CD  . GLU A 1 78  ? 20.060  22.471 13.631  1.00 91.36  ?  233 GLU A CD  1 
ATOM   510  O OE1 . GLU A 1 78  ? 21.235  22.860 13.417  1.00 80.30  ?  233 GLU A OE1 1 
ATOM   511  O OE2 . GLU A 1 78  ? 19.301  22.997 14.479  1.00 86.68  -1 233 GLU A OE2 1 
ATOM   512  N N   . ILE A 1 79  ? 18.616  17.810 11.354  1.00 54.85  ?  234 ILE A N   1 
ATOM   513  C CA  . ILE A 1 79  ? 17.429  17.268 10.685  1.00 54.69  ?  234 ILE A CA  1 
ATOM   514  C C   . ILE A 1 79  ? 16.806  16.101 11.481  1.00 59.51  ?  234 ILE A C   1 
ATOM   515  O O   . ILE A 1 79  ? 15.601  16.128 11.750  1.00 59.44  ?  234 ILE A O   1 
ATOM   516  C CB  . ILE A 1 79  ? 17.718  16.951 9.188   1.00 57.05  ?  234 ILE A CB  1 
ATOM   517  C CG1 . ILE A 1 79  ? 18.051  18.272 8.422   1.00 57.49  ?  234 ILE A CG1 1 
ATOM   518  C CG2 . ILE A 1 79  ? 16.538  16.210 8.541   1.00 56.43  ?  234 ILE A CG2 1 
ATOM   519  C CD1 . ILE A 1 79  ? 18.725  18.146 7.111   1.00 64.08  ?  234 ILE A CD1 1 
ATOM   520  N N   . LYS A 1 80  ? 17.629  15.125 11.902  1.00 56.16  ?  235 LYS A N   1 
ATOM   521  C CA  . LYS A 1 80  ? 17.153  13.972 12.669  1.00 56.48  ?  235 LYS A CA  1 
ATOM   522  C C   . LYS A 1 80  ? 16.457  14.391 13.968  1.00 60.69  ?  235 LYS A C   1 
ATOM   523  O O   . LYS A 1 80  ? 15.345  13.918 14.221  1.00 59.74  ?  235 LYS A O   1 
ATOM   524  C CB  . LYS A 1 80  ? 18.290  12.970 12.943  1.00 59.45  ?  235 LYS A CB  1 
ATOM   525  N N   . VAL A 1 81  ? 17.082  15.321 14.754  1.00 57.42  ?  236 VAL A N   1 
ATOM   526  C CA  . VAL A 1 81  ? 16.548  15.837 16.026  1.00 57.61  ?  236 VAL A CA  1 
ATOM   527  C C   . VAL A 1 81  ? 15.248  16.596 15.801  1.00 61.85  ?  236 VAL A C   1 
ATOM   528  O O   . VAL A 1 81  ? 14.266  16.352 16.514  1.00 61.26  ?  236 VAL A O   1 
ATOM   529  C CB  . VAL A 1 81  ? 17.579  16.704 16.795  1.00 62.42  ?  236 VAL A CB  1 
ATOM   530  C CG1 . VAL A 1 81  ? 16.939  17.465 17.966  1.00 61.92  ?  236 VAL A CG1 1 
ATOM   531  C CG2 . VAL A 1 81  ? 18.747  15.857 17.285  1.00 62.82  ?  236 VAL A CG2 1 
ATOM   532  N N   . MET A 1 82  ? 15.245  17.518 14.810  1.00 57.60  ?  237 MET A N   1 
ATOM   533  C CA  . MET A 1 82  ? 14.083  18.335 14.502  1.00 56.91  ?  237 MET A CA  1 
ATOM   534  C C   . MET A 1 82  ? 12.897  17.531 14.078  1.00 60.29  ?  237 MET A C   1 
ATOM   535  O O   . MET A 1 82  ? 11.769  17.902 14.412  1.00 61.06  ?  237 MET A O   1 
ATOM   536  C CB  . MET A 1 82  ? 14.407  19.371 13.457  1.00 59.72  ?  237 MET A CB  1 
ATOM   537  C CG  . MET A 1 82  ? 13.763  20.676 13.767  1.00 64.58  ?  237 MET A CG  1 
ATOM   538  S SD  . MET A 1 82  ? 14.657  21.613 15.009  1.00 68.75  ?  237 MET A SD  1 
ATOM   539  C CE  . MET A 1 82  ? 15.977  22.213 14.014  1.00 65.88  ?  237 MET A CE  1 
ATOM   540  N N   . ALA A 1 83  ? 13.146  16.414 13.353  1.00 54.07  ?  238 ALA A N   1 
ATOM   541  C CA  . ALA A 1 83  ? 12.118  15.494 12.890  1.00 52.05  ?  238 ALA A CA  1 
ATOM   542  C C   . ALA A 1 83  ? 11.394  14.888 14.074  1.00 55.77  ?  238 ALA A C   1 
ATOM   543  O O   . ALA A 1 83  ? 10.174  14.797 14.046  1.00 56.42  ?  238 ALA A O   1 
ATOM   544  C CB  . ALA A 1 83  ? 12.742  14.406 12.043  1.00 52.49  ?  238 ALA A CB  1 
ATOM   545  N N   . LYS A 1 84  ? 12.134  14.524 15.131  1.00 52.80  ?  239 LYS A N   1 
ATOM   546  C CA  . LYS A 1 84  ? 11.582  13.918 16.343  1.00 52.91  ?  239 LYS A CA  1 
ATOM   547  C C   . LYS A 1 84  ? 10.977  14.952 17.317  1.00 56.19  ?  239 LYS A C   1 
ATOM   548  O O   . LYS A 1 84  ? 9.879   14.750 17.827  1.00 56.11  ?  239 LYS A O   1 
ATOM   549  C CB  . LYS A 1 84  ? 12.666  13.068 17.044  1.00 55.85  ?  239 LYS A CB  1 
ATOM   550  N N   . CYS A 1 85  ? 11.684  16.072 17.533  1.00 52.27  ?  240 CYS A N   1 
ATOM   551  C CA  . CYS A 1 85  ? 11.335  17.100 18.510  1.00 51.19  ?  240 CYS A CA  1 
ATOM   552  C C   . CYS A 1 85  ? 10.559  18.298 17.984  1.00 52.48  ?  240 CYS A C   1 
ATOM   553  O O   . CYS A 1 85  ? 11.098  19.116 17.238  1.00 53.20  ?  240 CYS A O   1 
ATOM   554  C CB  . CYS A 1 85  ? 12.572  17.541 19.290  1.00 51.65  ?  240 CYS A CB  1 
ATOM   555  S SG  . CYS A 1 85  ? 13.582  16.174 19.919  1.00 55.82  ?  240 CYS A SG  1 
ATOM   556  N N   . GLN A 1 86  ? 9.300   18.416 18.422  1.00 45.29  ?  241 GLN A N   1 
ATOM   557  C CA  . GLN A 1 86  ? 8.401   19.512 18.098  1.00 43.72  ?  241 GLN A CA  1 
ATOM   558  C C   . GLN A 1 86  ? 7.807   19.994 19.402  1.00 43.51  ?  241 GLN A C   1 
ATOM   559  O O   . GLN A 1 86  ? 7.111   19.248 20.085  1.00 43.46  ?  241 GLN A O   1 
ATOM   560  C CB  . GLN A 1 86  ? 7.290   19.096 17.102  1.00 45.74  ?  241 GLN A CB  1 
ATOM   561  C CG  . GLN A 1 86  ? 7.737   18.987 15.632  1.00 67.73  ?  241 GLN A CG  1 
ATOM   562  C CD  . GLN A 1 86  ? 7.956   17.566 15.169  1.00 99.93  ?  241 GLN A CD  1 
ATOM   563  O OE1 . GLN A 1 86  ? 7.543   16.591 15.823  1.00 99.81  ?  241 GLN A OE1 1 
ATOM   564  N NE2 . GLN A 1 86  ? 8.602   17.417 14.015  1.00 92.98  ?  241 GLN A NE2 1 
ATOM   565  N N   . HIS A 1 87  ? 8.123   21.237 19.772  1.00 37.05  ?  242 HIS A N   1 
ATOM   566  C CA  . HIS A 1 87  ? 7.650   21.849 20.996  1.00 35.29  ?  242 HIS A CA  1 
ATOM   567  C C   . HIS A 1 87  ? 7.579   23.368 20.833  1.00 40.55  ?  242 HIS A C   1 
ATOM   568  O O   . HIS A 1 87  ? 8.332   23.939 20.041  1.00 40.93  ?  242 HIS A O   1 
ATOM   569  C CB  . HIS A 1 87  ? 8.587   21.464 22.130  1.00 35.32  ?  242 HIS A CB  1 
ATOM   570  C CG  . HIS A 1 87  ? 8.091   21.855 23.476  1.00 38.29  ?  242 HIS A CG  1 
ATOM   571  N ND1 . HIS A 1 87  ? 8.330   23.114 23.986  1.00 40.25  ?  242 HIS A ND1 1 
ATOM   572  C CD2 . HIS A 1 87  ? 7.411   21.133 24.386  1.00 40.02  ?  242 HIS A CD2 1 
ATOM   573  C CE1 . HIS A 1 87  ? 7.777   23.124 25.181  1.00 40.25  ?  242 HIS A CE1 1 
ATOM   574  N NE2 . HIS A 1 87  ? 7.205   21.948 25.461  1.00 40.62  ?  242 HIS A NE2 1 
ATOM   575  N N   . GLU A 1 88  ? 6.697   24.026 21.612  1.00 37.91  ?  243 GLU A N   1 
ATOM   576  C CA  . GLU A 1 88  ? 6.511   25.484 21.610  1.00 38.71  ?  243 GLU A CA  1 
ATOM   577  C C   . GLU A 1 88  ? 7.757   26.289 22.011  1.00 44.62  ?  243 GLU A C   1 
ATOM   578  O O   . GLU A 1 88  ? 7.826   27.484 21.728  1.00 44.99  ?  243 GLU A O   1 
ATOM   579  C CB  . GLU A 1 88  ? 5.288   25.913 22.441  1.00 40.47  ?  243 GLU A CB  1 
ATOM   580  C CG  . GLU A 1 88  ? 5.380   25.568 23.916  1.00 58.21  ?  243 GLU A CG  1 
ATOM   581  C CD  . GLU A 1 88  ? 4.079   25.652 24.695  1.00 78.11  ?  243 GLU A CD  1 
ATOM   582  O OE1 . GLU A 1 88  ? 3.236   26.519 24.363  1.00 67.17  ?  243 GLU A OE1 1 
ATOM   583  O OE2 . GLU A 1 88  ? 3.920   24.870 25.662  1.00 67.53  -1 243 GLU A OE2 1 
ATOM   584  N N   . ASN A 1 89  ? 8.739   25.628 22.652  1.00 41.82  ?  244 ASN A N   1 
ATOM   585  C CA  . ASN A 1 89  ? 9.986   26.245 23.101  1.00 39.96  ?  244 ASN A CA  1 
ATOM   586  C C   . ASN A 1 89  ? 11.186  25.745 22.336  1.00 41.09  ?  244 ASN A C   1 
ATOM   587  O O   . ASN A 1 89  ? 12.328  25.862 22.783  1.00 41.26  ?  244 ASN A O   1 
ATOM   588  C CB  . ASN A 1 89  ? 10.133  26.179 24.625  1.00 37.08  ?  244 ASN A CB  1 
ATOM   589  C CG  . ASN A 1 89  ? 8.989   26.874 25.351  1.00 41.63  ?  244 ASN A CG  1 
ATOM   590  O OD1 . ASN A 1 89  ? 8.155   26.236 25.980  1.00 39.14  ?  244 ASN A OD1 1 
ATOM   591  N ND2 . ASN A 1 89  ? 8.863   28.183 25.209  1.00 29.03  ?  244 ASN A ND2 1 
ATOM   592  N N   . LEU A 1 90  ? 10.922  25.229 21.135  1.00 35.30  ?  245 LEU A N   1 
ATOM   593  C CA  . LEU A 1 90  ? 11.968  24.805 20.198  1.00 33.46  ?  245 LEU A CA  1 
ATOM   594  C C   . LEU A 1 90  ? 11.709  25.477 18.891  1.00 38.19  ?  245 LEU A C   1 
ATOM   595  O O   . LEU A 1 90  ? 10.565  25.699 18.507  1.00 40.01  ?  245 LEU A O   1 
ATOM   596  C CB  . LEU A 1 90  ? 12.016  23.286 19.976  1.00 32.41  ?  245 LEU A CB  1 
ATOM   597  C CG  . LEU A 1 90  ? 12.264  22.391 21.158  1.00 36.74  ?  245 LEU A CG  1 
ATOM   598  C CD1 . LEU A 1 90  ? 12.368  20.992 20.697  1.00 37.94  ?  245 LEU A CD1 1 
ATOM   599  C CD2 . LEU A 1 90  ? 13.552  22.750 21.912  1.00 37.80  ?  245 LEU A CD2 1 
ATOM   600  N N   . VAL A 1 91  ? 12.764  25.777 18.194  1.00 35.15  ?  246 VAL A N   1 
ATOM   601  C CA  . VAL A 1 91  ? 12.740  26.410 16.885  1.00 34.07  ?  246 VAL A CA  1 
ATOM   602  C C   . VAL A 1 91  ? 12.147  25.401 15.875  1.00 35.55  ?  246 VAL A C   1 
ATOM   603  O O   . VAL A 1 91  ? 12.149  24.204 16.148  1.00 35.27  ?  246 VAL A O   1 
ATOM   604  C CB  . VAL A 1 91  ? 14.197  26.892 16.627  1.00 38.32  ?  246 VAL A CB  1 
ATOM   605  C CG1 . VAL A 1 91  ? 14.880  26.204 15.451  1.00 37.89  ?  246 VAL A CG1 1 
ATOM   606  C CG2 . VAL A 1 91  ? 14.266  28.411 16.544  1.00 38.13  ?  246 VAL A CG2 1 
ATOM   607  N N   . GLU A 1 92  ? 11.544  25.875 14.785  1.00 32.69  ?  247 GLU A N   1 
ATOM   608  C CA  . GLU A 1 92  ? 10.894  24.999 13.802  1.00 32.19  ?  247 GLU A CA  1 
ATOM   609  C C   . GLU A 1 92  ? 11.639  24.977 12.463  1.00 34.36  ?  247 GLU A C   1 
ATOM   610  O O   . GLU A 1 92  ? 11.930  26.014 11.898  1.00 32.53  ?  247 GLU A O   1 
ATOM   611  C CB  . GLU A 1 92  ? 9.410   25.385 13.615  1.00 33.79  ?  247 GLU A CB  1 
ATOM   612  C CG  . GLU A 1 92  ? 8.529   24.288 13.018  1.00 44.53  ?  247 GLU A CG  1 
ATOM   613  C CD  . GLU A 1 92  ? 7.181   24.694 12.431  1.00 71.38  ?  247 GLU A CD  1 
ATOM   614  O OE1 . GLU A 1 92  ? 6.622   25.749 12.821  1.00 74.76  ?  247 GLU A OE1 1 
ATOM   615  O OE2 . GLU A 1 92  ? 6.673   23.926 11.581  1.00 55.58  -1 247 GLU A OE2 1 
ATOM   616  N N   . LEU A 1 93  ? 11.932  23.790 11.968  1.00 33.66  ?  248 LEU A N   1 
ATOM   617  C CA  . LEU A 1 93  ? 12.592  23.593 10.685  1.00 35.22  ?  248 LEU A CA  1 
ATOM   618  C C   . LEU A 1 93  ? 11.529  23.443 9.594   1.00 40.13  ?  248 LEU A C   1 
ATOM   619  O O   . LEU A 1 93  ? 10.571  22.668 9.747   1.00 39.90  ?  248 LEU A O   1 
ATOM   620  C CB  . LEU A 1 93  ? 13.491  22.339 10.728  1.00 35.79  ?  248 LEU A CB  1 
ATOM   621  C CG  . LEU A 1 93  ? 14.475  22.127 9.575   1.00 40.93  ?  248 LEU A CG  1 
ATOM   622  C CD1 . LEU A 1 93  ? 15.588  23.178 9.579   1.00 41.19  ?  248 LEU A CD1 1 
ATOM   623  C CD2 . LEU A 1 93  ? 15.072  20.751 9.640   1.00 43.26  ?  248 LEU A CD2 1 
ATOM   624  N N   . LEU A 1 94  ? 11.675  24.208 8.507   1.00 35.47  ?  249 LEU A N   1 
ATOM   625  C CA  . LEU A 1 94  ? 10.705  24.106 7.419   1.00 34.40  ?  249 LEU A CA  1 
ATOM   626  C C   . LEU A 1 94  ? 11.237  23.167 6.363   1.00 41.72  ?  249 LEU A C   1 
ATOM   627  O O   . LEU A 1 94  ? 10.503  22.337 5.828   1.00 39.51  ?  249 LEU A O   1 
ATOM   628  C CB  . LEU A 1 94  ? 10.350  25.480 6.835   1.00 32.72  ?  249 LEU A CB  1 
ATOM   629  C CG  . LEU A 1 94  ? 9.595   26.400 7.771   1.00 34.72  ?  249 LEU A CG  1 
ATOM   630  C CD1 . LEU A 1 94  ? 9.592   27.818 7.248   1.00 35.40  ?  249 LEU A CD1 1 
ATOM   631  C CD2 . LEU A 1 94  ? 8.220   25.889 8.074   1.00 28.95  ?  249 LEU A CD2 1 
ATOM   632  N N   . GLY A 1 95  ? 12.535  23.297 6.124   1.00 42.69  ?  250 GLY A N   1 
ATOM   633  C CA  . GLY A 1 95  ? 13.290  22.520 5.161   1.00 43.19  ?  250 GLY A CA  1 
ATOM   634  C C   . GLY A 1 95  ? 14.781  22.775 5.177   1.00 47.54  ?  250 GLY A C   1 
ATOM   635  O O   . GLY A 1 95  ? 15.339  23.339 6.127   1.00 46.67  ?  250 GLY A O   1 
ATOM   636  N N   . PHE A 1 96  ? 15.415  22.397 4.073   1.00 45.42  ?  251 PHE A N   1 
ATOM   637  C CA  . PHE A 1 96  ? 16.853  22.389 3.891   1.00 45.52  ?  251 PHE A CA  1 
ATOM   638  C C   . PHE A 1 96  ? 17.232  22.307 2.426   1.00 50.41  ?  251 PHE A C   1 
ATOM   639  O O   . PHE A 1 96  ? 16.405  21.989 1.587   1.00 49.22  ?  251 PHE A O   1 
ATOM   640  C CB  . PHE A 1 96  ? 17.424  21.135 4.625   1.00 47.35  ?  251 PHE A CB  1 
ATOM   641  C CG  . PHE A 1 96  ? 16.780  19.823 4.223   1.00 49.03  ?  251 PHE A CG  1 
ATOM   642  C CD1 . PHE A 1 96  ? 17.258  19.097 3.134   1.00 52.42  ?  251 PHE A CD1 1 
ATOM   643  C CD2 . PHE A 1 96  ? 15.667  19.339 4.903   1.00 51.67  ?  251 PHE A CD2 1 
ATOM   644  C CE1 . PHE A 1 96  ? 16.630  17.916 2.730   1.00 53.49  ?  251 PHE A CE1 1 
ATOM   645  C CE2 . PHE A 1 96  ? 15.038  18.160 4.495   1.00 54.67  ?  251 PHE A CE2 1 
ATOM   646  C CZ  . PHE A 1 96  ? 15.534  17.450 3.419   1.00 52.80  ?  251 PHE A CZ  1 
ATOM   647  N N   . SER A 1 97  ? 18.516  22.464 2.150   1.00 50.91  ?  252 SER A N   1 
ATOM   648  C CA  . SER A 1 97  ? 19.117  22.363 0.829   1.00 52.47  ?  252 SER A CA  1 
ATOM   649  C C   . SER A 1 97  ? 20.482  21.688 0.990   1.00 59.32  ?  252 SER A C   1 
ATOM   650  O O   . SER A 1 97  ? 21.301  22.145 1.792   1.00 57.80  ?  252 SER A O   1 
ATOM   651  C CB  . SER A 1 97  ? 19.244  23.753 0.199   1.00 55.88  ?  252 SER A CB  1 
ATOM   652  O OG  . SER A 1 97  ? 20.403  23.915 -0.602  1.00 69.14  ?  252 SER A OG  1 
ATOM   653  N N   . SER A 1 98  ? 20.710  20.593 0.246   1.00 59.61  ?  253 SER A N   1 
ATOM   654  C CA  . SER A 1 98  ? 21.983  19.851 0.244   1.00 60.54  ?  253 SER A CA  1 
ATOM   655  C C   . SER A 1 98  ? 22.533  19.675 -1.189  1.00 69.57  ?  253 SER A C   1 
ATOM   656  O O   . SER A 1 98  ? 23.265  18.726 -1.462  1.00 70.26  ?  253 SER A O   1 
ATOM   657  C CB  . SER A 1 98  ? 21.834  18.514 0.966   1.00 61.89  ?  253 SER A CB  1 
ATOM   658  O OG  . SER A 1 98  ? 20.796  17.727 0.403   1.00 67.64  ?  253 SER A OG  1 
ATOM   659  N N   . ASP A 1 99  ? 22.173  20.603 -2.101  1.00 69.54  ?  254 ASP A N   1 
ATOM   660  C CA  . ASP A 1 99  ? 22.588  20.606 -3.513  1.00 70.43  ?  254 ASP A CA  1 
ATOM   661  C C   . ASP A 1 99  ? 24.064  21.028 -3.647  1.00 78.48  ?  254 ASP A C   1 
ATOM   662  O O   . ASP A 1 99  ? 24.398  22.217 -3.565  1.00 78.86  ?  254 ASP A O   1 
ATOM   663  C CB  . ASP A 1 99  ? 21.658  21.512 -4.350  1.00 71.94  ?  254 ASP A CB  1 
ATOM   664  N N   . GLY A 1 100 ? 24.932  20.034 -3.809  1.00 77.44  ?  255 GLY A N   1 
ATOM   665  C CA  . GLY A 1 100 ? 26.367  20.234 -3.946  1.00 78.35  ?  255 GLY A CA  1 
ATOM   666  C C   . GLY A 1 100 ? 27.113  20.522 -2.657  1.00 84.83  ?  255 GLY A C   1 
ATOM   667  O O   . GLY A 1 100 ? 26.794  19.953 -1.601  1.00 85.70  ?  255 GLY A O   1 
ATOM   668  N N   . ASP A 1 101 ? 28.123  21.415 -2.750  1.00 81.80  ?  256 ASP A N   1 
ATOM   669  C CA  . ASP A 1 101 ? 29.006  21.807 -1.644  1.00 82.34  ?  256 ASP A CA  1 
ATOM   670  C C   . ASP A 1 101 ? 28.340  22.655 -0.542  1.00 84.71  ?  256 ASP A C   1 
ATOM   671  O O   . ASP A 1 101 ? 28.853  22.699 0.585   1.00 84.68  ?  256 ASP A O   1 
ATOM   672  C CB  . ASP A 1 101 ? 30.268  22.509 -2.188  1.00 85.06  ?  256 ASP A CB  1 
ATOM   673  C CG  . ASP A 1 101 ? 31.204  21.643 -3.029  1.00 100.04 ?  256 ASP A CG  1 
ATOM   674  O OD1 . ASP A 1 101 ? 30.815  20.501 -3.380  1.00 101.09 ?  256 ASP A OD1 1 
ATOM   675  O OD2 . ASP A 1 101 ? 32.327  22.110 -3.341  1.00 106.18 -1 256 ASP A OD2 1 
ATOM   676  N N   . ASP A 1 102 ? 27.210  23.328 -0.867  1.00 78.77  ?  257 ASP A N   1 
ATOM   677  C CA  . ASP A 1 102 ? 26.491  24.190 0.072   1.00 76.82  ?  257 ASP A CA  1 
ATOM   678  C C   . ASP A 1 102 ? 25.341  23.502 0.783   1.00 73.59  ?  257 ASP A C   1 
ATOM   679  O O   . ASP A 1 102 ? 24.481  22.889 0.145   1.00 74.54  ?  257 ASP A O   1 
ATOM   680  C CB  . ASP A 1 102 ? 26.059  25.501 -0.597  1.00 79.81  ?  257 ASP A CB  1 
ATOM   681  C CG  . ASP A 1 102 ? 27.212  26.464 -0.834  1.00 97.03  ?  257 ASP A CG  1 
ATOM   682  O OD1 . ASP A 1 102 ? 27.647  27.126 0.144   1.00 98.59  ?  257 ASP A OD1 1 
ATOM   683  O OD2 . ASP A 1 102 ? 27.680  26.560 -1.998  1.00 103.06 -1 257 ASP A OD2 1 
ATOM   684  N N   . LEU A 1 103 ? 25.346  23.604 2.115   1.00 64.22  ?  258 LEU A N   1 
ATOM   685  C CA  . LEU A 1 103 ? 24.352  23.010 3.011   1.00 61.73  ?  258 LEU A CA  1 
ATOM   686  C C   . LEU A 1 103 ? 23.565  24.105 3.743   1.00 58.81  ?  258 LEU A C   1 
ATOM   687  O O   . LEU A 1 103 ? 24.152  24.938 4.442   1.00 57.26  ?  258 LEU A O   1 
ATOM   688  C CB  . LEU A 1 103 ? 25.048  22.065 4.000   1.00 62.18  ?  258 LEU A CB  1 
ATOM   689  C CG  . LEU A 1 103 ? 25.006  20.563 3.718   1.00 68.08  ?  258 LEU A CG  1 
ATOM   690  C CD1 . LEU A 1 103 ? 25.265  20.231 2.239   1.00 69.29  ?  258 LEU A CD1 1 
ATOM   691  C CD2 . LEU A 1 103 ? 26.017  19.853 4.576   1.00 71.50  ?  258 LEU A CD2 1 
ATOM   692  N N   . CYS A 1 104 ? 22.239  24.121 3.535   1.00 51.25  ?  259 CYS A N   1 
ATOM   693  C CA  . CYS A 1 104 ? 21.342  25.128 4.105   1.00 49.57  ?  259 CYS A CA  1 
ATOM   694  C C   . CYS A 1 104 ? 20.227  24.534 4.942   1.00 49.03  ?  259 CYS A C   1 
ATOM   695  O O   . CYS A 1 104 ? 19.721  23.453 4.647   1.00 48.12  ?  259 CYS A O   1 
ATOM   696  C CB  . CYS A 1 104 ? 20.780  26.042 3.015   1.00 49.59  ?  259 CYS A CB  1 
ATOM   697  S SG  . CYS A 1 104 ? 22.017  27.107 2.212   1.00 53.10  ?  259 CYS A SG  1 
ATOM   698  N N   . LEU A 1 105 ? 19.830  25.271 5.973   1.00 41.89  ?  260 LEU A N   1 
ATOM   699  C CA  . LEU A 1 105 ? 18.728  24.887 6.833   1.00 40.35  ?  260 LEU A CA  1 
ATOM   700  C C   . LEU A 1 105 ? 17.753  26.042 6.893   1.00 40.94  ?  260 LEU A C   1 
ATOM   701  O O   . LEU A 1 105 ? 18.152  27.202 7.074   1.00 39.22  ?  260 LEU A O   1 
ATOM   702  C CB  . LEU A 1 105 ? 19.205  24.430 8.218   1.00 40.23  ?  260 LEU A CB  1 
ATOM   703  C CG  . LEU A 1 105 ? 19.873  23.041 8.261   1.00 44.05  ?  260 LEU A CG  1 
ATOM   704  C CD1 . LEU A 1 105 ? 20.782  22.913 9.457   1.00 44.41  ?  260 LEU A CD1 1 
ATOM   705  C CD2 . LEU A 1 105 ? 18.850  21.916 8.271   1.00 42.29  ?  260 LEU A CD2 1 
ATOM   706  N N   . VAL A 1 106 ? 16.487  25.729 6.612   1.00 36.60  ?  261 VAL A N   1 
ATOM   707  C CA  . VAL A 1 106 ? 15.459  26.750 6.566   1.00 36.27  ?  261 VAL A CA  1 
ATOM   708  C C   . VAL A 1 106 ? 14.534  26.621 7.767   1.00 41.25  ?  261 VAL A C   1 
ATOM   709  O O   . VAL A 1 106 ? 13.968  25.544 8.019   1.00 42.35  ?  261 VAL A O   1 
ATOM   710  C CB  . VAL A 1 106 ? 14.743  26.845 5.184   1.00 39.04  ?  261 VAL A CB  1 
ATOM   711  C CG1 . VAL A 1 106 ? 13.917  28.114 5.082   1.00 38.19  ?  261 VAL A CG1 1 
ATOM   712  C CG2 . VAL A 1 106 ? 15.754  26.816 4.044   1.00 38.81  ?  261 VAL A CG2 1 
ATOM   713  N N   . TYR A 1 107 ? 14.392  27.732 8.508   1.00 35.83  ?  262 TYR A N   1 
ATOM   714  C CA  . TYR A 1 107 ? 13.582  27.801 9.719   1.00 35.08  ?  262 TYR A CA  1 
ATOM   715  C C   . TYR A 1 107 ? 12.520  28.879 9.663   1.00 36.60  ?  262 TYR A C   1 
ATOM   716  O O   . TYR A 1 107 ? 12.651  29.844 8.904   1.00 38.18  ?  262 TYR A O   1 
ATOM   717  C CB  . TYR A 1 107 ? 14.480  28.156 10.910  1.00 36.66  ?  262 TYR A CB  1 
ATOM   718  C CG  . TYR A 1 107 ? 15.616  27.199 11.168  1.00 40.16  ?  262 TYR A CG  1 
ATOM   719  C CD1 . TYR A 1 107 ? 16.867  27.388 10.569  1.00 41.89  ?  262 TYR A CD1 1 
ATOM   720  C CD2 . TYR A 1 107 ? 15.479  26.163 12.090  1.00 40.43  ?  262 TYR A CD2 1 
ATOM   721  C CE1 . TYR A 1 107 ? 17.930  26.538 10.846  1.00 41.24  ?  262 TYR A CE1 1 
ATOM   722  C CE2 . TYR A 1 107 ? 16.538  25.307 12.374  1.00 41.08  ?  262 TYR A CE2 1 
ATOM   723  C CZ  . TYR A 1 107 ? 17.753  25.485 11.733  1.00 49.96  ?  262 TYR A CZ  1 
ATOM   724  O OH  . TYR A 1 107 ? 18.781  24.630 12.020  1.00 51.25  ?  262 TYR A OH  1 
ATOM   725  N N   . VAL A 1 108 ? 11.548  28.789 10.580  1.00 28.32  ?  263 VAL A N   1 
ATOM   726  C CA  . VAL A 1 108 ? 10.561  29.839 10.760  1.00 26.80  ?  263 VAL A CA  1 
ATOM   727  C C   . VAL A 1 108 ? 11.326  30.958 11.467  1.00 31.33  ?  263 VAL A C   1 
ATOM   728  O O   . VAL A 1 108 ? 11.874  30.732 12.539  1.00 33.49  ?  263 VAL A O   1 
ATOM   729  C CB  . VAL A 1 108 ? 9.336   29.372 11.602  1.00 29.37  ?  263 VAL A CB  1 
ATOM   730  C CG1 . VAL A 1 108 ? 8.409   30.540 11.915  1.00 27.88  ?  263 VAL A CG1 1 
ATOM   731  C CG2 . VAL A 1 108 ? 8.575   28.207 10.934  1.00 28.56  ?  263 VAL A CG2 1 
ATOM   732  N N   . TYR A 1 109 ? 11.396  32.131 10.850  1.00 27.71  ?  264 TYR A N   1 
ATOM   733  C CA  . TYR A 1 109 ? 12.065  33.330 11.348  1.00 27.91  ?  264 TYR A CA  1 
ATOM   734  C C   . TYR A 1 109 ? 11.597  33.765 12.755  1.00 36.33  ?  264 TYR A C   1 
ATOM   735  O O   . TYR A 1 109 ? 10.422  33.643 13.061  1.00 35.99  ?  264 TYR A O   1 
ATOM   736  C CB  . TYR A 1 109 ? 11.842  34.420 10.324  1.00 27.73  ?  264 TYR A CB  1 
ATOM   737  C CG  . TYR A 1 109 ? 12.089  35.840 10.756  1.00 28.18  ?  264 TYR A CG  1 
ATOM   738  C CD1 . TYR A 1 109 ? 13.310  36.450 10.520  1.00 30.28  ?  264 TYR A CD1 1 
ATOM   739  C CD2 . TYR A 1 109 ? 11.043  36.636 11.226  1.00 27.09  ?  264 TYR A CD2 1 
ATOM   740  C CE1 . TYR A 1 109 ? 13.513  37.797 10.813  1.00 31.40  ?  264 TYR A CE1 1 
ATOM   741  C CE2 . TYR A 1 109 ? 11.234  37.977 11.524  1.00 26.53  ?  264 TYR A CE2 1 
ATOM   742  C CZ  . TYR A 1 109 ? 12.474  38.559 11.315  1.00 34.06  ?  264 TYR A CZ  1 
ATOM   743  O OH  . TYR A 1 109 ? 12.683  39.900 11.591  1.00 36.59  ?  264 TYR A OH  1 
ATOM   744  N N   . MET A 1 110 ? 12.538  34.261 13.598  1.00 35.16  ?  265 MET A N   1 
ATOM   745  C CA  . MET A 1 110 ? 12.279  34.739 14.963  1.00 35.92  ?  265 MET A CA  1 
ATOM   746  C C   . MET A 1 110 ? 12.289  36.280 15.000  1.00 43.12  ?  265 MET A C   1 
ATOM   747  O O   . MET A 1 110 ? 13.366  36.895 15.019  1.00 42.69  ?  265 MET A O   1 
ATOM   748  C CB  . MET A 1 110 ? 13.287  34.152 15.991  1.00 38.05  ?  265 MET A CB  1 
ATOM   749  C CG  . MET A 1 110 ? 13.084  32.665 16.319  1.00 40.61  ?  265 MET A CG  1 
ATOM   750  S SD  . MET A 1 110 ? 11.498  32.232 17.094  1.00 43.74  ?  265 MET A SD  1 
ATOM   751  C CE  . MET A 1 110 ? 10.930  31.065 15.901  1.00 40.93  ?  265 MET A CE  1 
ATOM   752  N N   . PRO A 1 111 ? 11.098  36.933 15.025  1.00 40.64  ?  266 PRO A N   1 
ATOM   753  C CA  . PRO A 1 111 ? 11.065  38.418 15.033  1.00 40.19  ?  266 PRO A CA  1 
ATOM   754  C C   . PRO A 1 111 ? 11.940  39.133 16.059  1.00 43.98  ?  266 PRO A C   1 
ATOM   755  O O   . PRO A 1 111 ? 12.253  40.322 15.868  1.00 44.73  ?  266 PRO A O   1 
ATOM   756  C CB  . PRO A 1 111 ? 9.591   38.748 15.263  1.00 41.57  ?  266 PRO A CB  1 
ATOM   757  C CG  . PRO A 1 111 ? 8.868   37.535 14.768  1.00 46.01  ?  266 PRO A CG  1 
ATOM   758  C CD  . PRO A 1 111 ? 9.737   36.356 15.027  1.00 41.31  ?  266 PRO A CD  1 
ATOM   759  N N   . ASN A 1 112 ? 12.310  38.439 17.152  1.00 38.21  ?  267 ASN A N   1 
ATOM   760  C CA  . ASN A 1 112 ? 13.110  39.093 18.175  1.00 37.63  ?  267 ASN A CA  1 
ATOM   761  C C   . ASN A 1 112 ? 14.524  38.605 18.327  1.00 41.10  ?  267 ASN A C   1 
ATOM   762  O O   . ASN A 1 112 ? 15.173  38.943 19.331  1.00 41.77  ?  267 ASN A O   1 
ATOM   763  C CB  . ASN A 1 112 ? 12.371  39.211 19.506  1.00 37.26  ?  267 ASN A CB  1 
ATOM   764  C CG  . ASN A 1 112 ? 11.334  40.262 19.481  1.00 45.61  ?  267 ASN A CG  1 
ATOM   765  O OD1 . ASN A 1 112 ? 11.607  41.434 19.302  1.00 39.18  ?  267 ASN A OD1 1 
ATOM   766  N ND2 . ASN A 1 112 ? 10.110  39.854 19.650  1.00 45.72  ?  267 ASN A ND2 1 
ATOM   767  N N   . GLY A 1 113 ? 15.016  37.882 17.313  1.00 36.14  ?  268 GLY A N   1 
ATOM   768  C CA  . GLY A 1 113 ? 16.377  37.344 17.262  1.00 34.43  ?  268 GLY A CA  1 
ATOM   769  C C   . GLY A 1 113 ? 16.764  36.516 18.468  1.00 36.48  ?  268 GLY A C   1 
ATOM   770  O O   . GLY A 1 113 ? 15.928  35.808 19.034  1.00 35.25  ?  268 GLY A O   1 
ATOM   771  N N   . SER A 1 114 ? 18.025  36.616 18.881  1.00 33.41  ?  269 SER A N   1 
ATOM   772  C CA  . SER A 1 114 ? 18.562  35.896 20.027  1.00 34.22  ?  269 SER A CA  1 
ATOM   773  C C   . SER A 1 114 ? 18.492  36.687 21.347  1.00 39.74  ?  269 SER A C   1 
ATOM   774  O O   . SER A 1 114 ? 18.501  37.920 21.350  1.00 39.78  ?  269 SER A O   1 
ATOM   775  C CB  . SER A 1 114 ? 20.004  35.474 19.758  1.00 38.58  ?  269 SER A CB  1 
ATOM   776  O OG  . SER A 1 114 ? 20.885  36.577 19.625  1.00 50.52  ?  269 SER A OG  1 
ATOM   777  N N   . LEU A 1 115 ? 18.466  35.947 22.468  1.00 35.12  ?  270 LEU A N   1 
ATOM   778  C CA  . LEU A 1 115 ? 18.495  36.494 23.815  1.00 34.13  ?  270 LEU A CA  1 
ATOM   779  C C   . LEU A 1 115 ? 19.796  37.304 24.014  1.00 38.52  ?  270 LEU A C   1 
ATOM   780  O O   . LEU A 1 115 ? 19.757  38.363 24.642  1.00 39.96  ?  270 LEU A O   1 
ATOM   781  C CB  . LEU A 1 115 ? 18.402  35.333 24.827  1.00 33.45  ?  270 LEU A CB  1 
ATOM   782  C CG  . LEU A 1 115 ? 18.513  35.679 26.295  1.00 37.03  ?  270 LEU A CG  1 
ATOM   783  C CD1 . LEU A 1 115 ? 17.477  36.759 26.717  1.00 35.91  ?  270 LEU A CD1 1 
ATOM   784  C CD2 . LEU A 1 115 ? 18.388  34.434 27.123  1.00 40.71  ?  270 LEU A CD2 1 
ATOM   785  N N   . LEU A 1 116 ? 20.934  36.816 23.445  1.00 32.51  ?  271 LEU A N   1 
ATOM   786  C CA  . LEU A 1 116 ? 22.231  37.483 23.522  1.00 31.11  ?  271 LEU A CA  1 
ATOM   787  C C   . LEU A 1 116 ? 22.066  38.922 22.988  1.00 37.47  ?  271 LEU A C   1 
ATOM   788  O O   . LEU A 1 116 ? 22.296  39.892 23.726  1.00 37.31  ?  271 LEU A O   1 
ATOM   789  C CB  . LEU A 1 116 ? 23.281  36.705 22.699  1.00 30.08  ?  271 LEU A CB  1 
ATOM   790  C CG  . LEU A 1 116 ? 24.745  37.207 22.766  1.00 32.67  ?  271 LEU A CG  1 
ATOM   791  C CD1 . LEU A 1 116 ? 25.445  36.708 23.987  1.00 32.42  ?  271 LEU A CD1 1 
ATOM   792  C CD2 . LEU A 1 116 ? 25.529  36.767 21.563  1.00 29.92  ?  271 LEU A CD2 1 
ATOM   793  N N   . ASP A 1 117 ? 21.553  39.042 21.746  1.00 33.37  ?  272 ASP A N   1 
ATOM   794  C CA  . ASP A 1 117 ? 21.341  40.317 21.078  1.00 31.94  ?  272 ASP A CA  1 
ATOM   795  C C   . ASP A 1 117 ? 20.386  41.253 21.816  1.00 37.10  ?  272 ASP A C   1 
ATOM   796  O O   . ASP A 1 117 ? 20.665  42.444 21.900  1.00 37.31  ?  272 ASP A O   1 
ATOM   797  C CB  . ASP A 1 117 ? 20.991  40.105 19.604  1.00 32.22  ?  272 ASP A CB  1 
ATOM   798  C CG  . ASP A 1 117 ? 22.129  39.443 18.839  1.00 52.52  ?  272 ASP A CG  1 
ATOM   799  O OD1 . ASP A 1 117 ? 23.277  39.428 19.363  1.00 55.91  ?  272 ASP A OD1 1 
ATOM   800  O OD2 . ASP A 1 117 ? 21.888  38.962 17.708  1.00 60.96  -1 272 ASP A OD2 1 
ATOM   801  N N   . ARG A 1 118 ? 19.317  40.701 22.423  1.00 33.13  ?  273 ARG A N   1 
ATOM   802  C CA  . ARG A 1 118 ? 18.346  41.484 23.171  1.00 32.58  ?  273 ARG A CA  1 
ATOM   803  C C   . ARG A 1 118 ? 18.891  41.960 24.500  1.00 35.18  ?  273 ARG A C   1 
ATOM   804  O O   . ARG A 1 118 ? 18.557  43.064 24.937  1.00 33.37  ?  273 ARG A O   1 
ATOM   805  C CB  . ARG A 1 118 ? 16.983  40.770 23.295  1.00 34.06  ?  273 ARG A CB  1 
ATOM   806  C CG  . ARG A 1 118 ? 16.305  40.425 21.949  1.00 38.01  ?  273 ARG A CG  1 
ATOM   807  C CD  . ARG A 1 118 ? 15.823  41.596 21.118  1.00 33.47  ?  273 ARG A CD  1 
ATOM   808  N NE  . ARG A 1 118 ? 16.881  42.382 20.470  1.00 36.81  ?  273 ARG A NE  1 
ATOM   809  C CZ  . ARG A 1 118 ? 17.580  42.006 19.402  1.00 48.26  ?  273 ARG A CZ  1 
ATOM   810  N NH1 . ARG A 1 118 ? 18.490  42.809 18.886  1.00 34.11  ?  273 ARG A NH1 1 
ATOM   811  N NH2 . ARG A 1 118 ? 17.387  40.811 18.855  1.00 32.01  1  273 ARG A NH2 1 
ATOM   812  N N   . LEU A 1 119 ? 19.801  41.164 25.104  1.00 31.55  ?  274 LEU A N   1 
ATOM   813  C CA  . LEU A 1 119 ? 20.469  41.519 26.358  1.00 29.12  ?  274 LEU A CA  1 
ATOM   814  C C   . LEU A 1 119 ? 21.479  42.629 26.125  1.00 34.57  ?  274 LEU A C   1 
ATOM   815  O O   . LEU A 1 119 ? 21.711  43.440 27.027  1.00 35.89  ?  274 LEU A O   1 
ATOM   816  C CB  . LEU A 1 119 ? 21.136  40.314 27.004  1.00 27.94  ?  274 LEU A CB  1 
ATOM   817  C CG  . LEU A 1 119 ? 20.222  39.309 27.702  1.00 30.47  ?  274 LEU A CG  1 
ATOM   818  C CD1 . LEU A 1 119 ? 21.042  38.131 28.248  1.00 29.85  ?  274 LEU A CD1 1 
ATOM   819  C CD2 . LEU A 1 119 ? 19.409  39.959 28.799  1.00 28.52  ?  274 LEU A CD2 1 
ATOM   820  N N   . SER A 1 120 ? 22.045  42.701 24.910  1.00 30.95  ?  275 SER A N   1 
ATOM   821  C CA  . SER A 1 120 ? 23.005  43.748 24.576  1.00 30.88  ?  275 SER A CA  1 
ATOM   822  C C   . SER A 1 120 ? 22.347  44.954 23.883  1.00 36.60  ?  275 SER A C   1 
ATOM   823  O O   . SER A 1 120 ? 23.039  45.939 23.636  1.00 35.72  ?  275 SER A O   1 
ATOM   824  C CB  . SER A 1 120 ? 24.112  43.179 23.699  1.00 34.90  ?  275 SER A CB  1 
ATOM   825  O OG  . SER A 1 120 ? 23.610  42.728 22.451  1.00 44.88  ?  275 SER A OG  1 
ATOM   826  N N   . CYS A 1 121 ? 21.015  44.858 23.543  1.00 33.42  ?  276 CYS A N   1 
ATOM   827  C CA  . CYS A 1 121 ? 20.199  45.847 22.841  1.00 32.66  ?  276 CYS A CA  1 
ATOM   828  C C   . CYS A 1 121 ? 20.694  46.069 21.456  1.00 37.81  ?  276 CYS A C   1 
ATOM   829  O O   . CYS A 1 121 ? 20.650  47.192 20.961  1.00 39.54  ?  276 CYS A O   1 
ATOM   830  C CB  . CYS A 1 121 ? 20.118  47.156 23.608  1.00 33.63  ?  276 CYS A CB  1 
ATOM   831  S SG  . CYS A 1 121 ? 19.387  46.994 25.237  1.00 38.18  ?  276 CYS A SG  1 
ATOM   832  N N   . LEU A 1 122 ? 21.198  45.023 20.824  1.00 34.16  ?  277 LEU A N   1 
ATOM   833  C CA  . LEU A 1 122 ? 21.702  45.100 19.466  1.00 34.13  ?  277 LEU A CA  1 
ATOM   834  C C   . LEU A 1 122 ? 20.620  45.666 18.511  1.00 40.71  ?  277 LEU A C   1 
ATOM   835  O O   . LEU A 1 122 ? 19.449  45.291 18.618  1.00 41.31  ?  277 LEU A O   1 
ATOM   836  C CB  . LEU A 1 122 ? 22.191  43.718 19.033  1.00 33.58  ?  277 LEU A CB  1 
ATOM   837  C CG  . LEU A 1 122 ? 22.863  43.639 17.665  1.00 36.87  ?  277 LEU A CG  1 
ATOM   838  C CD1 . LEU A 1 122 ? 24.214  44.335 17.661  1.00 36.93  ?  277 LEU A CD1 1 
ATOM   839  C CD2 . LEU A 1 122 ? 23.032  42.214 17.236  1.00 33.69  ?  277 LEU A CD2 1 
ATOM   840  N N   . ASP A 1 123 ? 20.998  46.637 17.660  1.00 37.52  ?  278 ASP A N   1 
ATOM   841  C CA  . ASP A 1 123 ? 20.101  47.306 16.691  1.00 37.14  ?  278 ASP A CA  1 
ATOM   842  C C   . ASP A 1 123 ? 19.028  48.186 17.319  1.00 40.47  ?  278 ASP A C   1 
ATOM   843  O O   . ASP A 1 123 ? 17.976  48.438 16.717  1.00 39.71  ?  278 ASP A O   1 
ATOM   844  C CB  . ASP A 1 123 ? 19.536  46.342 15.638  1.00 38.69  ?  278 ASP A CB  1 
ATOM   845  C CG  . ASP A 1 123 ? 20.609  45.511 14.940  1.00 46.38  ?  278 ASP A CG  1 
ATOM   846  O OD1 . ASP A 1 123 ? 21.599  46.106 14.461  1.00 44.47  ?  278 ASP A OD1 1 
ATOM   847  O OD2 . ASP A 1 123 ? 20.430  44.268 14.834  1.00 51.47  -1 278 ASP A OD2 1 
ATOM   848  N N   . GLY A 1 124 ? 19.342  48.674 18.517  1.00 35.81  ?  279 GLY A N   1 
ATOM   849  C CA  . GLY A 1 124 ? 18.544  49.627 19.265  1.00 34.93  ?  279 GLY A CA  1 
ATOM   850  C C   . GLY A 1 124 ? 17.262  49.153 19.871  1.00 39.53  ?  279 GLY A C   1 
ATOM   851  O O   . GLY A 1 124 ? 16.416  49.989 20.201  1.00 41.92  ?  279 GLY A O   1 
ATOM   852  N N   . THR A 1 125 ? 17.099  47.834 20.051  1.00 34.03  ?  280 THR A N   1 
ATOM   853  C CA  . THR A 1 125 ? 15.893  47.275 20.678  1.00 32.35  ?  280 THR A CA  1 
ATOM   854  C C   . THR A 1 125 ? 15.867  47.718 22.148  1.00 36.44  ?  280 THR A C   1 
ATOM   855  O O   . THR A 1 125 ? 16.926  47.942 22.738  1.00 34.01  ?  280 THR A O   1 
ATOM   856  C CB  . THR A 1 125 ? 15.851  45.769 20.546  1.00 36.01  ?  280 THR A CB  1 
ATOM   857  O OG1 . THR A 1 125 ? 16.727  45.170 21.523  1.00 33.31  ?  280 THR A OG1 1 
ATOM   858  C CG2 . THR A 1 125 ? 16.130  45.290 19.111  1.00 34.18  ?  280 THR A CG2 1 
ATOM   859  N N   . PRO A 1 126 ? 14.693  47.909 22.771  1.00 36.09  ?  281 PRO A N   1 
ATOM   860  C CA  . PRO A 1 126 ? 14.706  48.364 24.172  1.00 36.67  ?  281 PRO A CA  1 
ATOM   861  C C   . PRO A 1 126 ? 15.230  47.280 25.124  1.00 41.93  ?  281 PRO A C   1 
ATOM   862  O O   . PRO A 1 126 ? 15.115  46.088 24.806  1.00 41.66  ?  281 PRO A O   1 
ATOM   863  C CB  . PRO A 1 126 ? 13.236  48.711 24.436  1.00 37.88  ?  281 PRO A CB  1 
ATOM   864  C CG  . PRO A 1 126 ? 12.471  47.866 23.475  1.00 40.99  ?  281 PRO A CG  1 
ATOM   865  C CD  . PRO A 1 126 ? 13.315  47.707 22.268  1.00 36.59  ?  281 PRO A CD  1 
ATOM   866  N N   . PRO A 1 127 ? 15.828  47.650 26.279  1.00 39.61  ?  282 PRO A N   1 
ATOM   867  C CA  . PRO A 1 127 ? 16.250  46.606 27.253  1.00 39.11  ?  282 PRO A CA  1 
ATOM   868  C C   . PRO A 1 127 ? 15.074  45.740 27.751  1.00 41.15  ?  282 PRO A C   1 
ATOM   869  O O   . PRO A 1 127 ? 13.968  46.271 27.945  1.00 42.78  ?  282 PRO A O   1 
ATOM   870  C CB  . PRO A 1 127 ? 16.820  47.417 28.417  1.00 40.43  ?  282 PRO A CB  1 
ATOM   871  C CG  . PRO A 1 127 ? 17.060  48.790 27.873  1.00 44.77  ?  282 PRO A CG  1 
ATOM   872  C CD  . PRO A 1 127 ? 16.046  49.011 26.813  1.00 40.71  ?  282 PRO A CD  1 
ATOM   873  N N   . LEU A 1 128 ? 15.281  44.425 27.924  1.00 33.71  ?  283 LEU A N   1 
ATOM   874  C CA  . LEU A 1 128 ? 14.225  43.524 28.425  1.00 32.94  ?  283 LEU A CA  1 
ATOM   875  C C   . LEU A 1 128 ? 13.960  43.794 29.907  1.00 38.87  ?  283 LEU A C   1 
ATOM   876  O O   . LEU A 1 128 ? 14.901  44.010 30.685  1.00 37.55  ?  283 LEU A O   1 
ATOM   877  C CB  . LEU A 1 128 ? 14.631  42.056 28.251  1.00 32.39  ?  283 LEU A CB  1 
ATOM   878  C CG  . LEU A 1 128 ? 14.826  41.570 26.827  1.00 35.02  ?  283 LEU A CG  1 
ATOM   879  C CD1 . LEU A 1 128 ? 15.627  40.276 26.805  1.00 33.67  ?  283 LEU A CD1 1 
ATOM   880  C CD2 . LEU A 1 128 ? 13.476  41.463 26.092  1.00 31.74  ?  283 LEU A CD2 1 
ATOM   881  N N   . SER A 1 129 ? 12.676  43.802 30.297  1.00 38.30  ?  284 SER A N   1 
ATOM   882  C CA  . SER A 1 129 ? 12.267  43.992 31.697  1.00 38.77  ?  284 SER A CA  1 
ATOM   883  C C   . SER A 1 129 ? 12.534  42.711 32.495  1.00 46.40  ?  284 SER A C   1 
ATOM   884  O O   . SER A 1 129 ? 12.641  41.632 31.900  1.00 47.32  ?  284 SER A O   1 
ATOM   885  C CB  . SER A 1 129 ? 10.787  44.335 31.773  1.00 38.98  ?  284 SER A CB  1 
ATOM   886  O OG  . SER A 1 129 ? 10.003  43.219 31.384  1.00 43.01  ?  284 SER A OG  1 
ATOM   887  N N   . TRP A 1 130 ? 12.598  42.814 33.825  1.00 45.41  ?  285 TRP A N   1 
ATOM   888  C CA  . TRP A 1 130 ? 12.814  41.652 34.694  1.00 46.99  ?  285 TRP A CA  1 
ATOM   889  C C   . TRP A 1 130 ? 11.748  40.556 34.496  1.00 52.21  ?  285 TRP A C   1 
ATOM   890  O O   . TRP A 1 130 ? 12.099  39.381 34.296  1.00 51.24  ?  285 TRP A O   1 
ATOM   891  C CB  . TRP A 1 130 ? 12.927  42.069 36.166  1.00 46.28  ?  285 TRP A CB  1 
ATOM   892  C CG  . TRP A 1 130 ? 13.101  40.907 37.090  1.00 47.61  ?  285 TRP A CG  1 
ATOM   893  C CD1 . TRP A 1 130 ? 12.185  40.418 37.970  1.00 50.52  ?  285 TRP A CD1 1 
ATOM   894  C CD2 . TRP A 1 130 ? 14.208  40.002 37.119  1.00 47.64  ?  285 TRP A CD2 1 
ATOM   895  N NE1 . TRP A 1 130 ? 12.671  39.287 38.578  1.00 50.14  ?  285 TRP A NE1 1 
ATOM   896  C CE2 . TRP A 1 130 ? 13.916  39.014 38.084  1.00 51.45  ?  285 TRP A CE2 1 
ATOM   897  C CE3 . TRP A 1 130 ? 15.413  39.912 36.400  1.00 49.12  ?  285 TRP A CE3 1 
ATOM   898  C CZ2 . TRP A 1 130 ? 14.789  37.960 38.366  1.00 50.95  ?  285 TRP A CZ2 1 
ATOM   899  C CZ3 . TRP A 1 130 ? 16.289  38.875 36.694  1.00 50.84  ?  285 TRP A CZ3 1 
ATOM   900  C CH2 . TRP A 1 130 ? 15.993  37.937 37.698  1.00 51.38  ?  285 TRP A CH2 1 
ATOM   901  N N   . HIS A 1 131 ? 10.458  40.970 34.494  1.00 50.20  ?  286 HIS A N   1 
ATOM   902  C CA  . HIS A 1 131 ? 9.288   40.128 34.256  1.00 50.82  ?  286 HIS A CA  1 
ATOM   903  C C   . HIS A 1 131 ? 9.466   39.343 32.942  1.00 53.07  ?  286 HIS A C   1 
ATOM   904  O O   . HIS A 1 131 ? 9.203   38.135 32.910  1.00 51.12  ?  286 HIS A O   1 
ATOM   905  C CB  . HIS A 1 131 ? 8.020   40.997 34.220  1.00 52.87  ?  286 HIS A CB  1 
ATOM   906  C CG  . HIS A 1 131 ? 6.779   40.266 33.803  1.00 58.12  ?  286 HIS A CG  1 
ATOM   907  N ND1 . HIS A 1 131 ? 6.321   40.303 32.487  1.00 60.96  ?  286 HIS A ND1 1 
ATOM   908  C CD2 . HIS A 1 131 ? 5.960   39.465 34.527  1.00 61.06  ?  286 HIS A CD2 1 
ATOM   909  C CE1 . HIS A 1 131 ? 5.254   39.519 32.455  1.00 60.73  ?  286 HIS A CE1 1 
ATOM   910  N NE2 . HIS A 1 131 ? 4.995   38.995 33.656  1.00 61.17  ?  286 HIS A NE2 1 
ATOM   911  N N   . MET A 1 132 ? 9.951   40.023 31.885  1.00 48.99  ?  287 MET A N   1 
ATOM   912  C CA  . MET A 1 132 ? 10.179  39.389 30.610  1.00 48.44  ?  287 MET A CA  1 
ATOM   913  C C   . MET A 1 132 ? 11.343  38.403 30.692  1.00 48.21  ?  287 MET A C   1 
ATOM   914  O O   . MET A 1 132 ? 11.227  37.271 30.201  1.00 48.45  ?  287 MET A O   1 
ATOM   915  C CB  . MET A 1 132 ? 10.346  40.432 29.499  1.00 51.61  ?  287 MET A CB  1 
ATOM   916  C CG  . MET A 1 132 ? 10.012  39.887 28.110  1.00 57.22  ?  287 MET A CG  1 
ATOM   917  S SD  . MET A 1 132 ? 8.469   38.871 27.889  1.00 63.21  ?  287 MET A SD  1 
ATOM   918  C CE  . MET A 1 132 ? 7.202   40.046 28.467  1.00 59.60  ?  287 MET A CE  1 
ATOM   919  N N   . ARG A 1 133 ? 12.441  38.807 31.334  1.00 40.67  ?  288 ARG A N   1 
ATOM   920  C CA  . ARG A 1 133 ? 13.619  37.948 31.514  1.00 40.16  ?  288 ARG A CA  1 
ATOM   921  C C   . ARG A 1 133 ? 13.269  36.618 32.271  1.00 41.56  ?  288 ARG A C   1 
ATOM   922  O O   . ARG A 1 133 ? 13.745  35.543 31.894  1.00 38.98  ?  288 ARG A O   1 
ATOM   923  C CB  . ARG A 1 133 ? 14.708  38.738 32.244  1.00 40.93  ?  288 ARG A CB  1 
ATOM   924  C CG  . ARG A 1 133 ? 15.304  39.860 31.411  1.00 44.47  ?  288 ARG A CG  1 
ATOM   925  C CD  . ARG A 1 133 ? 16.365  40.581 32.192  1.00 40.12  ?  288 ARG A CD  1 
ATOM   926  N NE  . ARG A 1 133 ? 16.496  41.965 31.756  1.00 41.39  ?  288 ARG A NE  1 
ATOM   927  C CZ  . ARG A 1 133 ? 17.648  42.596 31.576  1.00 50.61  ?  288 ARG A CZ  1 
ATOM   928  N NH1 . ARG A 1 133 ? 18.801  41.970 31.808  1.00 36.58  ?  288 ARG A NH1 1 
ATOM   929  N NH2 . ARG A 1 133 ? 17.662  43.868 31.196  1.00 28.94  1  288 ARG A NH2 1 
ATOM   930  N N   . CYS A 1 134 ? 12.389  36.717 33.303  1.00 37.53  ?  289 CYS A N   1 
ATOM   931  C CA  . CYS A 1 134 ? 11.836  35.595 34.057  1.00 37.14  ?  289 CYS A CA  1 
ATOM   932  C C   . CYS A 1 134 ? 11.025  34.642 33.154  1.00 40.83  ?  289 CYS A C   1 
ATOM   933  O O   . CYS A 1 134 ? 11.256  33.425 33.167  1.00 40.07  ?  289 CYS A O   1 
ATOM   934  C CB  . CYS A 1 134 ? 11.000  36.090 35.235  1.00 37.45  ?  289 CYS A CB  1 
ATOM   935  S SG  . CYS A 1 134 ? 11.974  36.874 36.537  1.00 41.75  ?  289 CYS A SG  1 
ATOM   936  N N   . LYS A 1 135 ? 10.066  35.191 32.394  1.00 37.02  ?  290 LYS A N   1 
ATOM   937  C CA  . LYS A 1 135 ? 9.258   34.412 31.466  1.00 37.50  ?  290 LYS A CA  1 
ATOM   938  C C   . LYS A 1 135 ? 10.201  33.729 30.454  1.00 43.17  ?  290 LYS A C   1 
ATOM   939  O O   . LYS A 1 135 ? 10.054  32.528 30.211  1.00 44.89  ?  290 LYS A O   1 
ATOM   940  C CB  . LYS A 1 135 ? 8.206   35.295 30.754  1.00 40.28  ?  290 LYS A CB  1 
ATOM   941  C CG  . LYS A 1 135 ? 7.033   35.769 31.635  1.00 56.80  ?  290 LYS A CG  1 
ATOM   942  C CD  . LYS A 1 135 ? 5.851   34.790 31.614  1.00 70.93  ?  290 LYS A CD  1 
ATOM   943  C CE  . LYS A 1 135 ? 5.285   34.484 32.989  1.00 76.06  ?  290 LYS A CE  1 
ATOM   944  N NZ  . LYS A 1 135 ? 4.610   33.159 33.020  1.00 75.08  1  290 LYS A NZ  1 
ATOM   945  N N   . ILE A 1 136 ? 11.223  34.463 29.946  1.00 37.34  ?  291 ILE A N   1 
ATOM   946  C CA  . ILE A 1 136 ? 12.162  33.887 28.975  1.00 36.55  ?  291 ILE A CA  1 
ATOM   947  C C   . ILE A 1 136 ? 12.910  32.654 29.534  1.00 43.34  ?  291 ILE A C   1 
ATOM   948  O O   . ILE A 1 136 ? 12.987  31.633 28.849  1.00 43.51  ?  291 ILE A O   1 
ATOM   949  C CB  . ILE A 1 136 ? 13.050  34.972 28.297  1.00 37.78  ?  291 ILE A CB  1 
ATOM   950  C CG1 . ILE A 1 136 ? 12.204  35.839 27.363  1.00 35.08  ?  291 ILE A CG1 1 
ATOM   951  C CG2 . ILE A 1 136 ? 14.229  34.359 27.532  1.00 39.18  ?  291 ILE A CG2 1 
ATOM   952  C CD1 . ILE A 1 136 ? 12.637  37.201 27.194  1.00 32.36  ?  291 ILE A CD1 1 
ATOM   953  N N   . ALA A 1 137 ? 13.411  32.747 30.795  1.00 40.11  ?  292 ALA A N   1 
ATOM   954  C CA  . ALA A 1 137 ? 14.103  31.674 31.516  1.00 38.90  ?  292 ALA A CA  1 
ATOM   955  C C   . ALA A 1 137 ? 13.204  30.441 31.616  1.00 42.13  ?  292 ALA A C   1 
ATOM   956  O O   . ALA A 1 137 ? 13.638  29.328 31.283  1.00 41.95  ?  292 ALA A O   1 
ATOM   957  C CB  . ALA A 1 137 ? 14.477  32.150 32.907  1.00 39.47  ?  292 ALA A CB  1 
ATOM   958  N N   . GLN A 1 138 ? 11.932  30.668 32.020  1.00 37.69  ?  293 GLN A N   1 
ATOM   959  C CA  . GLN A 1 138 ? 10.873  29.668 32.165  1.00 36.56  ?  293 GLN A CA  1 
ATOM   960  C C   . GLN A 1 138 ? 10.638  28.933 30.850  1.00 41.37  ?  293 GLN A C   1 
ATOM   961  O O   . GLN A 1 138 ? 10.548  27.709 30.844  1.00 41.92  ?  293 GLN A O   1 
ATOM   962  C CB  . GLN A 1 138 ? 9.585   30.320 32.682  1.00 37.11  ?  293 GLN A CB  1 
ATOM   963  C CG  . GLN A 1 138 ? 9.652   30.637 34.174  1.00 48.23  ?  293 GLN A CG  1 
ATOM   964  C CD  . GLN A 1 138 ? 8.604   31.624 34.631  1.00 65.65  ?  293 GLN A CD  1 
ATOM   965  O OE1 . GLN A 1 138 ? 8.364   32.656 34.006  1.00 70.65  ?  293 GLN A OE1 1 
ATOM   966  N NE2 . GLN A 1 138 ? 8.027   31.392 35.791  1.00 44.27  ?  293 GLN A NE2 1 
ATOM   967  N N   . GLY A 1 139 ? 10.621  29.677 29.750  1.00 38.39  ?  294 GLY A N   1 
ATOM   968  C CA  . GLY A 1 139 ? 10.472  29.123 28.413  1.00 38.49  ?  294 GLY A CA  1 
ATOM   969  C C   . GLY A 1 139 ? 11.634  28.233 28.041  1.00 43.04  ?  294 GLY A C   1 
ATOM   970  O O   . GLY A 1 139 ? 11.431  27.072 27.665  1.00 42.99  ?  294 GLY A O   1 
ATOM   971  N N   . ALA A 1 140 ? 12.864  28.763 28.224  1.00 39.67  ?  295 ALA A N   1 
ATOM   972  C CA  . ALA A 1 140 ? 14.118  28.086 27.922  1.00 40.20  ?  295 ALA A CA  1 
ATOM   973  C C   . ALA A 1 140 ? 14.202  26.741 28.620  1.00 46.73  ?  295 ALA A C   1 
ATOM   974  O O   . ALA A 1 140 ? 14.486  25.734 27.965  1.00 46.25  ?  295 ALA A O   1 
ATOM   975  C CB  . ALA A 1 140 ? 15.287  28.965 28.304  1.00 41.01  ?  295 ALA A CB  1 
ATOM   976  N N   . ALA A 1 141 ? 13.861  26.722 29.936  1.00 45.17  ?  296 ALA A N   1 
ATOM   977  C CA  . ALA A 1 141 ? 13.820  25.536 30.795  1.00 44.89  ?  296 ALA A CA  1 
ATOM   978  C C   . ALA A 1 141 ? 12.843  24.485 30.243  1.00 46.88  ?  296 ALA A C   1 
ATOM   979  O O   . ALA A 1 141 ? 13.220  23.326 30.137  1.00 45.31  ?  296 ALA A O   1 
ATOM   980  C CB  . ALA A 1 141 ? 13.415  25.936 32.203  1.00 45.86  ?  296 ALA A CB  1 
ATOM   981  N N   . ASN A 1 142 ? 11.617  24.893 29.841  1.00 43.37  ?  297 ASN A N   1 
ATOM   982  C CA  . ASN A 1 142 ? 10.640  23.979 29.246  1.00 43.55  ?  297 ASN A CA  1 
ATOM   983  C C   . ASN A 1 142 ? 11.157  23.352 27.956  1.00 49.30  ?  297 ASN A C   1 
ATOM   984  O O   . ASN A 1 142 ? 10.787  22.221 27.628  1.00 50.38  ?  297 ASN A O   1 
ATOM   985  C CB  . ASN A 1 142 ? 9.343   24.682 28.969  1.00 45.73  ?  297 ASN A CB  1 
ATOM   986  C CG  . ASN A 1 142 ? 8.290   24.384 29.988  1.00 86.13  ?  297 ASN A CG  1 
ATOM   987  O OD1 . ASN A 1 142 ? 8.300   24.950 31.100  1.00 82.45  ?  297 ASN A OD1 1 
ATOM   988  N ND2 . ASN A 1 142 ? 7.363   23.482 29.629  1.00 78.70  ?  297 ASN A ND2 1 
ATOM   989  N N   . GLY A 1 143 ? 11.991  24.093 27.237  1.00 45.53  ?  298 GLY A N   1 
ATOM   990  C CA  . GLY A 1 143 ? 12.596  23.618 26.006  1.00 45.95  ?  298 GLY A CA  1 
ATOM   991  C C   . GLY A 1 143 ? 13.661  22.589 26.306  1.00 51.60  ?  298 GLY A C   1 
ATOM   992  O O   . GLY A 1 143 ? 13.635  21.502 25.726  1.00 52.54  ?  298 GLY A O   1 
ATOM   993  N N   . ILE A 1 144 ? 14.605  22.923 27.235  1.00 47.01  ?  299 ILE A N   1 
ATOM   994  C CA  . ILE A 1 144 ? 15.667  21.994 27.643  1.00 47.05  ?  299 ILE A CA  1 
ATOM   995  C C   . ILE A 1 144 ? 15.005  20.700 28.194  1.00 50.14  ?  299 ILE A C   1 
ATOM   996  O O   . ILE A 1 144 ? 15.404  19.595 27.824  1.00 50.76  ?  299 ILE A O   1 
ATOM   997  C CB  . ILE A 1 144 ? 16.686  22.629 28.656  1.00 50.14  ?  299 ILE A CB  1 
ATOM   998  C CG1 . ILE A 1 144 ? 17.330  23.922 28.120  1.00 49.40  ?  299 ILE A CG1 1 
ATOM   999  C CG2 . ILE A 1 144 ? 17.776  21.611 29.077  1.00 51.85  ?  299 ILE A CG2 1 
ATOM   1000 C CD1 . ILE A 1 144 ? 17.973  24.750 29.168  1.00 49.06  ?  299 ILE A CD1 1 
ATOM   1001 N N   . ASN A 1 145 ? 13.947  20.865 28.991  1.00 44.04  ?  300 ASN A N   1 
ATOM   1002 C CA  . ASN A 1 145 ? 13.200  19.777 29.579  1.00 43.66  ?  300 ASN A CA  1 
ATOM   1003 C C   . ASN A 1 145 ? 12.571  18.846 28.545  1.00 47.25  ?  300 ASN A C   1 
ATOM   1004 O O   . ASN A 1 145 ? 12.585  17.635 28.746  1.00 46.28  ?  300 ASN A O   1 
ATOM   1005 C CB  . ASN A 1 145 ? 12.152  20.299 30.545  1.00 45.27  ?  300 ASN A CB  1 
ATOM   1006 C CG  . ASN A 1 145 ? 11.352  19.181 31.129  1.00 64.86  ?  300 ASN A CG  1 
ATOM   1007 O OD1 . ASN A 1 145 ? 11.860  18.379 31.924  1.00 58.37  ?  300 ASN A OD1 1 
ATOM   1008 N ND2 . ASN A 1 145 ? 10.132  19.035 30.637  1.00 53.30  ?  300 ASN A ND2 1 
ATOM   1009 N N   . PHE A 1 146 ? 12.013  19.395 27.458  1.00 43.63  ?  301 PHE A N   1 
ATOM   1010 C CA  . PHE A 1 146 ? 11.425  18.582 26.400  1.00 43.30  ?  301 PHE A CA  1 
ATOM   1011 C C   . PHE A 1 146 ? 12.525  17.741 25.738  1.00 49.74  ?  301 PHE A C   1 
ATOM   1012 O O   . PHE A 1 146 ? 12.344  16.543 25.558  1.00 50.73  ?  301 PHE A O   1 
ATOM   1013 C CB  . PHE A 1 146 ? 10.686  19.462 25.375  1.00 44.49  ?  301 PHE A CB  1 
ATOM   1014 C CG  . PHE A 1 146 ? 10.084  18.703 24.206  1.00 45.10  ?  301 PHE A CG  1 
ATOM   1015 C CD1 . PHE A 1 146 ? 8.856   18.067 24.326  1.00 46.15  ?  301 PHE A CD1 1 
ATOM   1016 C CD2 . PHE A 1 146 ? 10.753  18.614 22.988  1.00 47.54  ?  301 PHE A CD2 1 
ATOM   1017 C CE1 . PHE A 1 146 ? 8.297   17.377 23.250  1.00 46.79  ?  301 PHE A CE1 1 
ATOM   1018 C CE2 . PHE A 1 146 ? 10.201  17.899 21.916  1.00 50.39  ?  301 PHE A CE2 1 
ATOM   1019 C CZ  . PHE A 1 146 ? 8.973   17.296 22.051  1.00 47.20  ?  301 PHE A CZ  1 
ATOM   1020 N N   . LEU A 1 147 ? 13.675  18.356 25.433  1.00 47.40  ?  302 LEU A N   1 
ATOM   1021 C CA  . LEU A 1 147 ? 14.807  17.660 24.822  1.00 48.20  ?  302 LEU A CA  1 
ATOM   1022 C C   . LEU A 1 147 ? 15.331  16.539 25.714  1.00 51.44  ?  302 LEU A C   1 
ATOM   1023 O O   . LEU A 1 147 ? 15.647  15.459 25.220  1.00 51.13  ?  302 LEU A O   1 
ATOM   1024 C CB  . LEU A 1 147 ? 15.948  18.645 24.514  1.00 48.26  ?  302 LEU A CB  1 
ATOM   1025 C CG  . LEU A 1 147 ? 15.737  19.555 23.325  1.00 52.62  ?  302 LEU A CG  1 
ATOM   1026 C CD1 . LEU A 1 147 ? 16.662  20.724 23.417  1.00 53.39  ?  302 LEU A CD1 1 
ATOM   1027 C CD2 . LEU A 1 147 ? 15.943  18.821 21.998  1.00 52.46  ?  302 LEU A CD2 1 
ATOM   1028 N N   . HIS A 1 148 ? 15.427  16.808 27.023  1.00 46.64  ?  303 HIS A N   1 
ATOM   1029 C CA  . HIS A 1 148 ? 15.915  15.862 28.016  1.00 45.81  ?  303 HIS A CA  1 
ATOM   1030 C C   . HIS A 1 148 ? 14.963  14.668 28.177  1.00 50.40  ?  303 HIS A C   1 
ATOM   1031 O O   . HIS A 1 148 ? 15.434  13.521 28.177  1.00 50.77  ?  303 HIS A O   1 
ATOM   1032 C CB  . HIS A 1 148 ? 16.204  16.583 29.340  1.00 46.02  ?  303 HIS A CB  1 
ATOM   1033 C CG  . HIS A 1 148 ? 17.544  17.252 29.378  1.00 48.90  ?  303 HIS A CG  1 
ATOM   1034 N ND1 . HIS A 1 148 ? 18.302  17.604 30.437  1.00 50.35  ?  303 HIS A ND1 1 
ATOM   1035 C CD2 . HIS A 1 148 ? 18.214  17.600 28.217  1.00 50.60  ?  303 HIS A CD2 1 
ATOM   1036 C CE1 . HIS A 1 148 ? 19.450  18.169 29.931  1.00 49.90  ?  303 HIS A CE1 1 
ATOM   1037 N NE2 . HIS A 1 148 ? 19.348  18.150 28.604  1.00 50.55  ?  303 HIS A NE2 1 
ATOM   1038 N N   . GLU A 1 149 ? 13.624  14.941 28.227  1.00 44.92  ?  304 GLU A N   1 
ATOM   1039 C CA  . GLU A 1 149 ? 12.562  13.938 28.286  1.00 44.39  ?  304 GLU A CA  1 
ATOM   1040 C C   . GLU A 1 149 ? 12.628  13.060 27.026  1.00 51.50  ?  304 GLU A C   1 
ATOM   1041 O O   . GLU A 1 149 ? 12.258  11.886 27.074  1.00 53.66  ?  304 GLU A O   1 
ATOM   1042 C CB  . GLU A 1 149 ? 11.190  14.610 28.319  1.00 45.51  ?  304 GLU A CB  1 
ATOM   1043 C CG  . GLU A 1 149 ? 10.717  15.008 29.705  1.00 56.82  ?  304 GLU A CG  1 
ATOM   1044 C CD  . GLU A 1 149 ? 9.364   15.708 29.762  1.00 82.26  ?  304 GLU A CD  1 
ATOM   1045 O OE1 . GLU A 1 149 ? 8.754   15.970 28.691  1.00 57.06  ?  304 GLU A OE1 1 
ATOM   1046 O OE2 . GLU A 1 149 ? 8.919   16.005 30.896  1.00 75.09  -1 304 GLU A OE2 1 
ATOM   1047 N N   . ASN A 1 150 ? 13.124  13.623 25.914  1.00 47.02  ?  305 ASN A N   1 
ATOM   1048 C CA  . ASN A 1 150 ? 13.251  12.910 24.660  1.00 47.34  ?  305 ASN A CA  1 
ATOM   1049 C C   . ASN A 1 150 ? 14.659  12.373 24.449  1.00 53.21  ?  305 ASN A C   1 
ATOM   1050 O O   . ASN A 1 150 ? 15.042  12.056 23.314  1.00 51.46  ?  305 ASN A O   1 
ATOM   1051 C CB  . ASN A 1 150 ? 12.756  13.777 23.505  1.00 50.25  ?  305 ASN A CB  1 
ATOM   1052 C CG  . ASN A 1 150 ? 11.256  13.877 23.446  1.00 71.86  ?  305 ASN A CG  1 
ATOM   1053 O OD1 . ASN A 1 150 ? 10.623  13.343 22.533  1.00 71.05  ?  305 ASN A OD1 1 
ATOM   1054 N ND2 . ASN A 1 150 ? 10.649  14.558 24.412  1.00 62.88  ?  305 ASN A ND2 1 
ATOM   1055 N N   . HIS A 1 151 ? 15.421  12.247 25.564  1.00 53.32  ?  306 HIS A N   1 
ATOM   1056 C CA  . HIS A 1 151 ? 16.771  11.674 25.613  1.00 55.56  ?  306 HIS A CA  1 
ATOM   1057 C C   . HIS A 1 151 ? 17.727  12.330 24.640  1.00 60.62  ?  306 HIS A C   1 
ATOM   1058 O O   . HIS A 1 151 ? 18.427  11.656 23.886  1.00 60.57  ?  306 HIS A O   1 
ATOM   1059 C CB  . HIS A 1 151 ? 16.729  10.137 25.449  1.00 58.15  ?  306 HIS A CB  1 
ATOM   1060 C CG  . HIS A 1 151 ? 15.636  9.509  26.256  1.00 63.06  ?  306 HIS A CG  1 
ATOM   1061 N ND1 . HIS A 1 151 ? 15.788  9.276  27.619  1.00 65.30  ?  306 HIS A ND1 1 
ATOM   1062 C CD2 . HIS A 1 151 ? 14.367  9.197  25.893  1.00 65.67  ?  306 HIS A CD2 1 
ATOM   1063 C CE1 . HIS A 1 151 ? 14.625  8.798  28.030  1.00 65.25  ?  306 HIS A CE1 1 
ATOM   1064 N NE2 . HIS A 1 151 ? 13.735  8.739  27.029  1.00 65.77  ?  306 HIS A NE2 1 
ATOM   1065 N N   . HIS A 1 152 ? 17.729  13.671 24.649  1.00 57.53  ?  307 HIS A N   1 
ATOM   1066 C CA  . HIS A 1 152 ? 18.636  14.475 23.842  1.00 56.36  ?  307 HIS A CA  1 
ATOM   1067 C C   . HIS A 1 152 ? 19.386  15.445 24.709  1.00 58.22  ?  307 HIS A C   1 
ATOM   1068 O O   . HIS A 1 152 ? 18.821  15.997 25.660  1.00 58.08  ?  307 HIS A O   1 
ATOM   1069 C CB  . HIS A 1 152 ? 17.895  15.221 22.742  1.00 57.37  ?  307 HIS A CB  1 
ATOM   1070 C CG  . HIS A 1 152 ? 17.459  14.340 21.621  1.00 60.96  ?  307 HIS A CG  1 
ATOM   1071 N ND1 . HIS A 1 152 ? 18.369  13.815 20.728  1.00 62.72  ?  307 HIS A ND1 1 
ATOM   1072 C CD2 . HIS A 1 152 ? 16.222  13.921 21.282  1.00 62.32  ?  307 HIS A CD2 1 
ATOM   1073 C CE1 . HIS A 1 152 ? 17.664  13.083 19.890  1.00 61.77  ?  307 HIS A CE1 1 
ATOM   1074 N NE2 . HIS A 1 152 ? 16.367  13.117 20.187  1.00 62.10  ?  307 HIS A NE2 1 
ATOM   1075 N N   . ILE A 1 153 ? 20.675  15.606 24.414  1.00 53.10  ?  308 ILE A N   1 
ATOM   1076 C CA  . ILE A 1 153 ? 21.554  16.559 25.078  1.00 52.19  ?  308 ILE A CA  1 
ATOM   1077 C C   . ILE A 1 153 ? 21.864  17.583 24.001  1.00 55.71  ?  308 ILE A C   1 
ATOM   1078 O O   . ILE A 1 153 ? 22.291  17.200 22.900  1.00 56.47  ?  308 ILE A O   1 
ATOM   1079 C CB  . ILE A 1 153 ? 22.846  15.928 25.656  1.00 55.33  ?  308 ILE A CB  1 
ATOM   1080 C CG1 . ILE A 1 153 ? 22.574  14.612 26.428  1.00 54.77  ?  308 ILE A CG1 1 
ATOM   1081 C CG2 . ILE A 1 153 ? 23.606  16.949 26.530  1.00 56.53  ?  308 ILE A CG2 1 
ATOM   1082 C CD1 . ILE A 1 153 ? 23.710  13.606 26.333  1.00 48.67  ?  308 ILE A CD1 1 
ATOM   1083 N N   . HIS A 1 154 ? 21.615  18.875 24.297  1.00 49.68  ?  309 HIS A N   1 
ATOM   1084 C CA  . HIS A 1 154 ? 21.828  19.948 23.337  1.00 48.22  ?  309 HIS A CA  1 
ATOM   1085 C C   . HIS A 1 154 ? 23.292  20.113 22.963  1.00 49.71  ?  309 HIS A C   1 
ATOM   1086 O O   . HIS A 1 154 ? 23.602  20.148 21.769  1.00 49.61  ?  309 HIS A O   1 
ATOM   1087 C CB  . HIS A 1 154 ? 21.213  21.260 23.842  1.00 49.02  ?  309 HIS A CB  1 
ATOM   1088 C CG  . HIS A 1 154 ? 21.203  22.352 22.824  1.00 52.10  ?  309 HIS A CG  1 
ATOM   1089 N ND1 . HIS A 1 154 ? 22.347  23.064 22.518  1.00 53.55  ?  309 HIS A ND1 1 
ATOM   1090 C CD2 . HIS A 1 154 ? 20.195  22.787 22.038  1.00 53.62  ?  309 HIS A CD2 1 
ATOM   1091 C CE1 . HIS A 1 154 ? 21.991  23.921 21.580  1.00 52.83  ?  309 HIS A CE1 1 
ATOM   1092 N NE2 . HIS A 1 154 ? 20.707  23.789 21.260  1.00 53.23  ?  309 HIS A NE2 1 
ATOM   1093 N N   . ARG A 1 155 ? 24.184  20.223 23.977  1.00 45.08  ?  310 ARG A N   1 
ATOM   1094 C CA  . ARG A 1 155 ? 25.655  20.384 23.862  1.00 44.27  ?  310 ARG A CA  1 
ATOM   1095 C C   . ARG A 1 155 ? 26.138  21.803 23.516  1.00 48.96  ?  310 ARG A C   1 
ATOM   1096 O O   . ARG A 1 155 ? 27.346  22.031 23.493  1.00 51.21  ?  310 ARG A O   1 
ATOM   1097 C CB  . ARG A 1 155 ? 26.307  19.359 22.905  1.00 44.41  ?  310 ARG A CB  1 
ATOM   1098 C CG  . ARG A 1 155 ? 26.273  17.891 23.347  1.00 58.02  ?  310 ARG A CG  1 
ATOM   1099 C CD  . ARG A 1 155 ? 27.584  17.192 22.959  1.00 73.96  ?  310 ARG A CD  1 
ATOM   1100 N NE  . ARG A 1 155 ? 27.795  17.132 21.506  1.00 82.35  ?  310 ARG A NE  1 
ATOM   1101 C CZ  . ARG A 1 155 ? 28.952  16.872 20.900  1.00 92.21  ?  310 ARG A CZ  1 
ATOM   1102 N NH1 . ARG A 1 155 ? 30.048  16.640 21.613  1.00 77.62  ?  310 ARG A NH1 1 
ATOM   1103 N NH2 . ARG A 1 155 ? 29.023  16.849 19.577  1.00 75.00  1  310 ARG A NH2 1 
ATOM   1104 N N   . ASP A 1 156 ? 25.226  22.752 23.229  1.00 43.65  ?  311 ASP A N   1 
ATOM   1105 C CA  . ASP A 1 156 ? 25.609  24.128 22.896  1.00 42.42  ?  311 ASP A CA  1 
ATOM   1106 C C   . ASP A 1 156 ? 24.587  25.154 23.457  1.00 42.99  ?  311 ASP A C   1 
ATOM   1107 O O   . ASP A 1 156 ? 24.201  26.102 22.780  1.00 42.45  ?  311 ASP A O   1 
ATOM   1108 C CB  . ASP A 1 156 ? 25.859  24.276 21.371  1.00 45.00  ?  311 ASP A CB  1 
ATOM   1109 C CG  . ASP A 1 156 ? 26.707  25.471 20.931  1.00 66.10  ?  311 ASP A CG  1 
ATOM   1110 O OD1 . ASP A 1 156 ? 27.420  26.057 21.795  1.00 68.28  ?  311 ASP A OD1 1 
ATOM   1111 O OD2 . ASP A 1 156 ? 26.704  25.791 19.712  1.00 73.07  -1 311 ASP A OD2 1 
ATOM   1112 N N   . ILE A 1 157 ? 24.142  24.942 24.695  1.00 37.70  ?  312 ILE A N   1 
ATOM   1113 C CA  . ILE A 1 157 ? 23.227  25.851 25.355  1.00 37.48  ?  312 ILE A CA  1 
ATOM   1114 C C   . ILE A 1 157 ? 23.913  27.135 25.715  1.00 41.63  ?  312 ILE A C   1 
ATOM   1115 O O   . ILE A 1 157 ? 24.879  27.142 26.481  1.00 42.44  ?  312 ILE A O   1 
ATOM   1116 C CB  . ILE A 1 157 ? 22.440  25.207 26.513  1.00 41.47  ?  312 ILE A CB  1 
ATOM   1117 C CG1 . ILE A 1 157 ? 21.247  24.407 25.898  1.00 43.49  ?  312 ILE A CG1 1 
ATOM   1118 C CG2 . ILE A 1 157 ? 21.954  26.271 27.548  1.00 40.53  ?  312 ILE A CG2 1 
ATOM   1119 C CD1 . ILE A 1 157 ? 20.786  23.347 26.707  1.00 59.86  ?  312 ILE A CD1 1 
ATOM   1120 N N   . LYS A 1 158 ? 23.436  28.228 25.104  1.00 36.18  ?  313 LYS A N   1 
ATOM   1121 C CA  . LYS A 1 158 ? 23.940  29.587 25.278  1.00 33.35  ?  313 LYS A CA  1 
ATOM   1122 C C   . LYS A 1 158 ? 22.858  30.566 24.856  1.00 37.13  ?  313 LYS A C   1 
ATOM   1123 O O   . LYS A 1 158 ? 21.906  30.163 24.172  1.00 37.04  ?  313 LYS A O   1 
ATOM   1124 C CB  . LYS A 1 158 ? 25.262  29.796 24.512  1.00 32.08  ?  313 LYS A CB  1 
ATOM   1125 C CG  . LYS A 1 158 ? 25.240  29.443 23.039  1.00 26.60  ?  313 LYS A CG  1 
ATOM   1126 C CD  . LYS A 1 158 ? 26.629  29.590 22.476  1.00 27.18  ?  313 LYS A CD  1 
ATOM   1127 C CE  . LYS A 1 158 ? 26.671  29.498 20.980  1.00 27.45  ?  313 LYS A CE  1 
ATOM   1128 N NZ  . LYS A 1 158 ? 27.965  29.980 20.436  1.00 41.55  1  313 LYS A NZ  1 
ATOM   1129 N N   . SER A 1 159 ? 22.996  31.849 25.250  1.00 32.73  ?  314 SER A N   1 
ATOM   1130 C CA  . SER A 1 159 ? 22.009  32.871 24.915  1.00 30.93  ?  314 SER A CA  1 
ATOM   1131 C C   . SER A 1 159 ? 21.876  33.156 23.428  1.00 33.05  ?  314 SER A C   1 
ATOM   1132 O O   . SER A 1 159 ? 20.770  33.476 22.979  1.00 31.32  ?  314 SER A O   1 
ATOM   1133 C CB  . SER A 1 159 ? 22.162  34.120 25.772  1.00 32.39  ?  314 SER A CB  1 
ATOM   1134 O OG  . SER A 1 159 ? 23.459  34.666 25.648  1.00 39.38  ?  314 SER A OG  1 
ATOM   1135 N N   . ALA A 1 160 ? 22.950  32.930 22.644  1.00 30.84  ?  315 ALA A N   1 
ATOM   1136 C CA  . ALA A 1 160 ? 22.894  33.084 21.180  1.00 31.03  ?  315 ALA A CA  1 
ATOM   1137 C C   . ALA A 1 160 ? 21.976  32.022 20.590  1.00 37.38  ?  315 ALA A C   1 
ATOM   1138 O O   . ALA A 1 160 ? 21.376  32.260 19.534  1.00 37.92  ?  315 ALA A O   1 
ATOM   1139 C CB  . ALA A 1 160 ? 24.277  32.963 20.574  1.00 31.33  ?  315 ALA A CB  1 
ATOM   1140 N N   . ASN A 1 161 ? 21.840  30.864 21.297  1.00 33.96  ?  316 ASN A N   1 
ATOM   1141 C CA  . ASN A 1 161 ? 20.980  29.734 20.906  1.00 34.19  ?  316 ASN A CA  1 
ATOM   1142 C C   . ASN A 1 161 ? 19.573  29.700 21.562  1.00 36.82  ?  316 ASN A C   1 
ATOM   1143 O O   . ASN A 1 161 ? 18.851  28.711 21.418  1.00 37.16  ?  316 ASN A O   1 
ATOM   1144 C CB  . ASN A 1 161 ? 21.716  28.405 21.095  1.00 34.65  ?  316 ASN A CB  1 
ATOM   1145 C CG  . ASN A 1 161 ? 22.796  28.180 20.083  1.00 47.01  ?  316 ASN A CG  1 
ATOM   1146 O OD1 . ASN A 1 161 ? 22.858  28.830 19.024  1.00 41.50  ?  316 ASN A OD1 1 
ATOM   1147 N ND2 . ASN A 1 161 ? 23.669  27.243 20.380  1.00 34.53  ?  316 ASN A ND2 1 
ATOM   1148 N N   . ILE A 1 162 ? 19.202  30.761 22.283  1.00 31.56  ?  317 ILE A N   1 
ATOM   1149 C CA  . ILE A 1 162 ? 17.863  30.915 22.844  1.00 30.83  ?  317 ILE A CA  1 
ATOM   1150 C C   . ILE A 1 162 ? 17.256  32.055 22.062  1.00 34.30  ?  317 ILE A C   1 
ATOM   1151 O O   . ILE A 1 162 ? 17.651  33.223 22.232  1.00 35.94  ?  317 ILE A O   1 
ATOM   1152 C CB  . ILE A 1 162 ? 17.833  31.156 24.365  1.00 33.81  ?  317 ILE A CB  1 
ATOM   1153 C CG1 . ILE A 1 162 ? 18.492  29.986 25.106  1.00 34.58  ?  317 ILE A CG1 1 
ATOM   1154 C CG2 . ILE A 1 162 ? 16.387  31.358 24.835  1.00 33.13  ?  317 ILE A CG2 1 
ATOM   1155 C CD1 . ILE A 1 162 ? 18.958  30.332 26.492  1.00 40.10  ?  317 ILE A CD1 1 
ATOM   1156 N N   . LEU A 1 163 ? 16.381  31.711 21.134  1.00 28.71  ?  318 LEU A N   1 
ATOM   1157 C CA  . LEU A 1 163 ? 15.766  32.705 20.267  1.00 27.84  ?  318 LEU A CA  1 
ATOM   1158 C C   . LEU A 1 163 ? 14.414  33.177 20.799  1.00 35.88  ?  318 LEU A C   1 
ATOM   1159 O O   . LEU A 1 163 ? 13.833  32.542 21.694  1.00 37.12  ?  318 LEU A O   1 
ATOM   1160 C CB  . LEU A 1 163 ? 15.686  32.209 18.818  1.00 26.61  ?  318 LEU A CB  1 
ATOM   1161 C CG  . LEU A 1 163 ? 16.983  31.714 18.215  1.00 28.15  ?  318 LEU A CG  1 
ATOM   1162 C CD1 . LEU A 1 163 ? 16.780  31.264 16.837  1.00 27.51  ?  318 LEU A CD1 1 
ATOM   1163 C CD2 . LEU A 1 163 ? 18.026  32.779 18.214  1.00 25.73  ?  318 LEU A CD2 1 
ATOM   1164 N N   . LEU A 1 164 ? 13.945  34.320 20.282  1.00 32.88  ?  319 LEU A N   1 
ATOM   1165 C CA  . LEU A 1 164 ? 12.707  34.949 20.716  1.00 33.20  ?  319 LEU A CA  1 
ATOM   1166 C C   . LEU A 1 164 ? 11.745  35.253 19.573  1.00 39.61  ?  319 LEU A C   1 
ATOM   1167 O O   . LEU A 1 164 ? 12.119  35.920 18.598  1.00 39.85  ?  319 LEU A O   1 
ATOM   1168 C CB  . LEU A 1 164 ? 13.050  36.227 21.504  1.00 32.94  ?  319 LEU A CB  1 
ATOM   1169 C CG  . LEU A 1 164 ? 13.967  36.053 22.701  1.00 37.62  ?  319 LEU A CG  1 
ATOM   1170 C CD1 . LEU A 1 164 ? 14.524  37.377 23.142  1.00 37.94  ?  319 LEU A CD1 1 
ATOM   1171 C CD2 . LEU A 1 164 ? 13.246  35.334 23.844  1.00 39.90  ?  319 LEU A CD2 1 
ATOM   1172 N N   . ASP A 1 165 ? 10.494  34.772 19.696  1.00 38.27  ?  320 ASP A N   1 
ATOM   1173 C CA  . ASP A 1 165 ? 9.424   35.048 18.715  1.00 38.49  ?  320 ASP A CA  1 
ATOM   1174 C C   . ASP A 1 165 ? 8.785   36.431 18.956  1.00 44.51  ?  320 ASP A C   1 
ATOM   1175 O O   . ASP A 1 165 ? 9.207   37.164 19.859  1.00 43.95  ?  320 ASP A O   1 
ATOM   1176 C CB  . ASP A 1 165 ? 8.373   33.928 18.695  1.00 39.86  ?  320 ASP A CB  1 
ATOM   1177 C CG  . ASP A 1 165 ? 7.355   33.900 19.821  1.00 47.81  ?  320 ASP A CG  1 
ATOM   1178 O OD1 . ASP A 1 165 ? 7.383   34.811 20.677  1.00 50.29  ?  320 ASP A OD1 1 
ATOM   1179 O OD2 . ASP A 1 165 ? 6.527   32.953 19.851  1.00 46.50  -1 320 ASP A OD2 1 
ATOM   1180 N N   . GLU A 1 166 ? 7.742   36.758 18.187  1.00 44.56  ?  321 GLU A N   1 
ATOM   1181 C CA  . GLU A 1 166 ? 6.980   38.025 18.282  1.00 45.09  ?  321 GLU A CA  1 
ATOM   1182 C C   . GLU A 1 166 ? 6.444   38.325 19.678  1.00 47.90  ?  321 GLU A C   1 
ATOM   1183 O O   . GLU A 1 166 ? 6.321   39.492 20.008  1.00 48.04  ?  321 GLU A O   1 
ATOM   1184 C CB  . GLU A 1 166 ? 5.811   38.076 17.287  1.00 46.75  ?  321 GLU A CB  1 
ATOM   1185 C CG  . GLU A 1 166 ? 5.022   36.784 17.160  1.00 59.27  ?  321 GLU A CG  1 
ATOM   1186 C CD  . GLU A 1 166 ? 5.577   36.014 15.979  1.00 78.92  ?  321 GLU A CD  1 
ATOM   1187 O OE1 . GLU A 1 166 ? 6.398   35.103 16.229  1.00 57.18  ?  321 GLU A OE1 1 
ATOM   1188 O OE2 . GLU A 1 166 ? 5.396   36.482 14.827  1.00 77.31  -1 321 GLU A OE2 1 
ATOM   1189 N N   . ALA A 1 167 ? 6.130   37.287 20.483  1.00 42.55  ?  322 ALA A N   1 
ATOM   1190 C CA  . ALA A 1 167 ? 5.610   37.399 21.851  1.00 40.36  ?  322 ALA A CA  1 
ATOM   1191 C C   . ALA A 1 167 ? 6.718   37.224 22.905  1.00 42.29  ?  322 ALA A C   1 
ATOM   1192 O O   . ALA A 1 167 ? 6.400   37.218 24.100  1.00 42.01  ?  322 ALA A O   1 
ATOM   1193 C CB  . ALA A 1 167 ? 4.522   36.356 22.072  1.00 40.51  ?  322 ALA A CB  1 
ATOM   1194 N N   . PHE A 1 168 ? 8.007   37.087 22.468  1.00 36.18  ?  323 PHE A N   1 
ATOM   1195 C CA  . PHE A 1 168 ? 9.182   36.855 23.320  1.00 35.79  ?  323 PHE A CA  1 
ATOM   1196 C C   . PHE A 1 168 ? 9.161   35.469 23.951  1.00 41.68  ?  323 PHE A C   1 
ATOM   1197 O O   . PHE A 1 168 ? 9.648   35.269 25.073  1.00 41.48  ?  323 PHE A O   1 
ATOM   1198 C CB  . PHE A 1 168 ? 9.427   37.963 24.369  1.00 37.58  ?  323 PHE A CB  1 
ATOM   1199 C CG  . PHE A 1 168 ? 9.834   39.270 23.744  1.00 40.43  ?  323 PHE A CG  1 
ATOM   1200 C CD1 . PHE A 1 168 ? 8.875   40.159 23.263  1.00 43.97  ?  323 PHE A CD1 1 
ATOM   1201 C CD2 . PHE A 1 168 ? 11.178  39.593 23.582  1.00 42.52  ?  323 PHE A CD2 1 
ATOM   1202 C CE1 . PHE A 1 168 ? 9.257   41.351 22.653  1.00 45.10  ?  323 PHE A CE1 1 
ATOM   1203 C CE2 . PHE A 1 168 ? 11.555  40.774 22.949  1.00 45.11  ?  323 PHE A CE2 1 
ATOM   1204 C CZ  . PHE A 1 168 ? 10.595  41.651 22.510  1.00 44.11  ?  323 PHE A CZ  1 
ATOM   1205 N N   . THR A 1 169 ? 8.597   34.494 23.217  1.00 38.19  ?  324 THR A N   1 
ATOM   1206 C CA  . THR A 1 169 ? 8.614   33.098 23.640  1.00 38.00  ?  324 THR A CA  1 
ATOM   1207 C C   . THR A 1 169 ? 10.027  32.579 23.351  1.00 41.12  ?  324 THR A C   1 
ATOM   1208 O O   . THR A 1 169 ? 10.552  32.797 22.254  1.00 39.69  ?  324 THR A O   1 
ATOM   1209 C CB  . THR A 1 169 ? 7.535   32.295 22.894  1.00 39.79  ?  324 THR A CB  1 
ATOM   1210 O OG1 . THR A 1 169 ? 6.274   32.798 23.291  1.00 35.41  ?  324 THR A OG1 1 
ATOM   1211 C CG2 . THR A 1 169 ? 7.620   30.805 23.143  1.00 37.43  ?  324 THR A CG2 1 
ATOM   1212 N N   . ALA A 1 170 ? 10.645  31.959 24.363  1.00 38.39  ?  325 ALA A N   1 
ATOM   1213 C CA  . ALA A 1 170 ? 11.981  31.377 24.244  1.00 38.34  ?  325 ALA A CA  1 
ATOM   1214 C C   . ALA A 1 170 ? 11.913  30.145 23.339  1.00 41.75  ?  325 ALA A C   1 
ATOM   1215 O O   . ALA A 1 170 ? 10.994  29.322 23.462  1.00 41.79  ?  325 ALA A O   1 
ATOM   1216 C CB  . ALA A 1 170 ? 12.514  30.999 25.607  1.00 38.80  ?  325 ALA A CB  1 
ATOM   1217 N N   . LYS A 1 171 ? 12.845  30.071 22.382  1.00 36.26  ?  326 LYS A N   1 
ATOM   1218 C CA  . LYS A 1 171 ? 12.932  28.950 21.455  1.00 35.75  ?  326 LYS A CA  1 
ATOM   1219 C C   . LYS A 1 171 ? 14.362  28.538 21.305  1.00 43.45  ?  326 LYS A C   1 
ATOM   1220 O O   . LYS A 1 171 ? 15.179  29.307 20.796  1.00 44.80  ?  326 LYS A O   1 
ATOM   1221 C CB  . LYS A 1 171 ? 12.277  29.271 20.113  1.00 36.41  ?  326 LYS A CB  1 
ATOM   1222 C CG  . LYS A 1 171 ? 10.792  29.018 20.161  1.00 36.20  ?  326 LYS A CG  1 
ATOM   1223 C CD  . LYS A 1 171 ? 9.982   30.021 19.394  1.00 46.75  ?  326 LYS A CD  1 
ATOM   1224 C CE  . LYS A 1 171 ? 8.493   29.772 19.524  1.00 54.17  ?  326 LYS A CE  1 
ATOM   1225 N NZ  . LYS A 1 171 ? 8.114   28.396 19.077  1.00 49.03  1  326 LYS A NZ  1 
ATOM   1226 N N   . ILE A 1 172 ? 14.688  27.344 21.822  1.00 40.64  ?  327 ILE A N   1 
ATOM   1227 C CA  . ILE A 1 172 ? 16.027  26.738 21.756  1.00 39.41  ?  327 ILE A CA  1 
ATOM   1228 C C   . ILE A 1 172 ? 16.324  26.381 20.286  1.00 41.73  ?  327 ILE A C   1 
ATOM   1229 O O   . ILE A 1 172 ? 15.471  25.808 19.599  1.00 38.49  ?  327 ILE A O   1 
ATOM   1230 C CB  . ILE A 1 172 ? 16.127  25.471 22.678  1.00 41.72  ?  327 ILE A CB  1 
ATOM   1231 C CG1 . ILE A 1 172 ? 15.501  25.672 24.107  1.00 41.46  ?  327 ILE A CG1 1 
ATOM   1232 C CG2 . ILE A 1 172 ? 17.531  24.891 22.711  1.00 40.24  ?  327 ILE A CG2 1 
ATOM   1233 C CD1 . ILE A 1 172 ? 16.198  26.623 25.073  1.00 42.42  ?  327 ILE A CD1 1 
ATOM   1234 N N   . SER A 1 173 ? 17.514  26.761 19.806  1.00 41.48  ?  328 SER A N   1 
ATOM   1235 C CA  . SER A 1 173 ? 17.936  26.492 18.428  1.00 43.33  ?  328 SER A CA  1 
ATOM   1236 C C   . SER A 1 173 ? 19.295  25.817 18.406  1.00 49.40  ?  328 SER A C   1 
ATOM   1237 O O   . SER A 1 173 ? 19.859  25.566 19.471  1.00 48.90  ?  328 SER A O   1 
ATOM   1238 C CB  . SER A 1 173 ? 17.965  27.781 17.607  1.00 47.46  ?  328 SER A CB  1 
ATOM   1239 O OG  . SER A 1 173 ? 18.967  28.655 18.098  1.00 57.75  ?  328 SER A OG  1 
ATOM   1240 N N   . ASP A 1 174 ? 19.818  25.537 17.188  1.00 47.41  ?  329 ASP A N   1 
ATOM   1241 C CA  . ASP A 1 174 ? 21.117  24.915 16.918  1.00 48.13  ?  329 ASP A CA  1 
ATOM   1242 C C   . ASP A 1 174 ? 21.317  23.555 17.534  1.00 53.51  ?  329 ASP A C   1 
ATOM   1243 O O   . ASP A 1 174 ? 21.949  23.431 18.573  1.00 54.11  ?  329 ASP A O   1 
ATOM   1244 C CB  . ASP A 1 174 ? 22.284  25.863 17.216  1.00 50.56  ?  329 ASP A CB  1 
ATOM   1245 C CG  . ASP A 1 174 ? 23.364  25.848 16.160  1.00 66.62  ?  329 ASP A CG  1 
ATOM   1246 O OD1 . ASP A 1 174 ? 23.514  24.801 15.469  1.00 66.94  ?  329 ASP A OD1 1 
ATOM   1247 O OD2 . ASP A 1 174 ? 24.073  26.878 16.023  1.00 77.03  -1 329 ASP A OD2 1 
ATOM   1248 N N   . PHE A 1 175 ? 20.780  22.531 16.875  1.00 52.20  ?  330 PHE A N   1 
ATOM   1249 C CA  . PHE A 1 175 ? 20.851  21.124 17.285  1.00 53.31  ?  330 PHE A CA  1 
ATOM   1250 C C   . PHE A 1 175 ? 21.889  20.310 16.485  1.00 61.02  ?  330 PHE A C   1 
ATOM   1251 O O   . PHE A 1 175 ? 21.847  19.077 16.514  1.00 62.17  ?  330 PHE A O   1 
ATOM   1252 C CB  . PHE A 1 175 ? 19.462  20.472 17.188  1.00 55.09  ?  330 PHE A CB  1 
ATOM   1253 C CG  . PHE A 1 175 ? 18.410  21.216 17.971  1.00 56.88  ?  330 PHE A CG  1 
ATOM   1254 C CD1 . PHE A 1 175 ? 18.311  21.070 19.353  1.00 59.27  ?  330 PHE A CD1 1 
ATOM   1255 C CD2 . PHE A 1 175 ? 17.542  22.098 17.333  1.00 59.03  ?  330 PHE A CD2 1 
ATOM   1256 C CE1 . PHE A 1 175 ? 17.341  21.768 20.074  1.00 60.17  ?  330 PHE A CE1 1 
ATOM   1257 C CE2 . PHE A 1 175 ? 16.570  22.793 18.054  1.00 61.60  ?  330 PHE A CE2 1 
ATOM   1258 C CZ  . PHE A 1 175 ? 16.476  22.624 19.418  1.00 59.84  ?  330 PHE A CZ  1 
ATOM   1259 N N   . GLY A 1 176 ? 22.810  21.002 15.794  1.00 59.28  ?  331 GLY A N   1 
ATOM   1260 C CA  . GLY A 1 176 ? 23.886  20.390 15.011  1.00 60.28  ?  331 GLY A CA  1 
ATOM   1261 C C   . GLY A 1 176 ? 24.869  19.557 15.829  1.00 66.83  ?  331 GLY A C   1 
ATOM   1262 O O   . GLY A 1 176 ? 25.467  18.614 15.313  1.00 66.43  ?  331 GLY A O   1 
ATOM   1263 N N   . LEU A 1 177 ? 25.034  19.907 17.120  1.00 65.12  ?  332 LEU A N   1 
ATOM   1264 C CA  . LEU A 1 177 ? 25.888  19.227 18.087  1.00 65.09  ?  332 LEU A CA  1 
ATOM   1265 C C   . LEU A 1 177 ? 25.105  18.333 19.054  1.00 71.04  ?  332 LEU A C   1 
ATOM   1266 O O   . LEU A 1 177 ? 25.730  17.655 19.859  1.00 71.35  ?  332 LEU A O   1 
ATOM   1267 C CB  . LEU A 1 177 ? 26.776  20.225 18.872  1.00 64.79  ?  332 LEU A CB  1 
ATOM   1268 C CG  . LEU A 1 177 ? 28.087  20.709 18.221  1.00 69.58  ?  332 LEU A CG  1 
ATOM   1269 C CD1 . LEU A 1 177 ? 28.733  19.640 17.346  1.00 69.96  ?  332 LEU A CD1 1 
ATOM   1270 C CD2 . LEU A 1 177 ? 27.889  21.983 17.438  1.00 73.01  ?  332 LEU A CD2 1 
ATOM   1271 N N   . ALA A 1 178 ? 23.760  18.297 18.966  1.00 68.72  ?  333 ALA A N   1 
ATOM   1272 C CA  . ALA A 1 178 ? 22.920  17.478 19.852  1.00 69.43  ?  333 ALA A CA  1 
ATOM   1273 C C   . ALA A 1 178 ? 23.218  15.977 19.797  1.00 76.71  ?  333 ALA A C   1 
ATOM   1274 O O   . ALA A 1 178 ? 23.589  15.451 18.738  1.00 77.18  ?  333 ALA A O   1 
ATOM   1275 C CB  . ALA A 1 178 ? 21.452  17.736 19.590  1.00 69.98  ?  333 ALA A CB  1 
ATOM   1276 N N   . ARG A 1 179 ? 23.079  15.299 20.951  1.00 74.12  ?  334 ARG A N   1 
ATOM   1277 C CA  . ARG A 1 179 ? 23.347  13.868 21.104  1.00 74.33  ?  334 ARG A CA  1 
ATOM   1278 C C   . ARG A 1 179 ? 22.177  13.121 21.732  1.00 79.87  ?  334 ARG A C   1 
ATOM   1279 O O   . ARG A 1 179 ? 21.479  13.679 22.574  1.00 78.87  ?  334 ARG A O   1 
ATOM   1280 C CB  . ARG A 1 179 ? 24.613  13.655 21.957  1.00 73.96  ?  334 ARG A CB  1 
ATOM   1281 C CG  . ARG A 1 179 ? 25.935  13.931 21.233  1.00 79.27  ?  334 ARG A CG  1 
ATOM   1282 C CD  . ARG A 1 179 ? 26.357  12.798 20.308  1.00 86.66  ?  334 ARG A CD  1 
ATOM   1283 N NE  . ARG A 1 179 ? 27.807  12.759 20.095  1.00 99.65  ?  334 ARG A NE  1 
ATOM   1284 C CZ  . ARG A 1 179 ? 28.447  13.450 19.156  1.00 116.10 ?  334 ARG A CZ  1 
ATOM   1285 N NH1 . ARG A 1 179 ? 29.762  13.351 19.033  1.00 102.58 ?  334 ARG A NH1 1 
ATOM   1286 N NH2 . ARG A 1 179 ? 27.776  14.249 18.336  1.00 103.99 1  334 ARG A NH2 1 
ATOM   1287 N N   . ALA A 1 180 ? 22.022  11.829 21.389  1.00 79.12  ?  335 ALA A N   1 
ATOM   1288 C CA  . ALA A 1 180 ? 20.956  10.962 21.918  1.00 80.35  ?  335 ALA A CA  1 
ATOM   1289 C C   . ALA A 1 180 ? 21.252  10.340 23.331  1.00 86.20  ?  335 ALA A C   1 
ATOM   1290 O O   . ALA A 1 180 ? 21.907  11.002 24.149  1.00 86.53  ?  335 ALA A O   1 
ATOM   1291 C CB  . ALA A 1 180 ? 20.612  9.885  20.898  1.00 81.22  ?  335 ALA A CB  1 
ATOM   1292 N N   . SER A 1 181 ? 20.700  9.102  23.620  1.00 82.47  ?  336 SER A N   1 
ATOM   1293 C CA  . SER A 1 181 ? 20.786  8.222  24.824  1.00 98.34  ?  336 SER A CA  1 
ATOM   1294 C C   . SER A 1 181 ? 19.415  7.671  25.270  1.00 108.35 ?  336 SER A C   1 
ATOM   1295 O O   . SER A 1 181 ? 19.273  6.490  25.616  1.00 64.14  ?  336 SER A O   1 
ATOM   1296 C CB  . SER A 1 181 ? 21.432  8.981  25.985  1.00 20.00  ?  336 SER A CB  1 
HETATM 1297 N N   . TPO A 1 187 ? 27.017  8.805  31.017  1.00 119.69 ?  342 TPO A N   1 
HETATM 1298 C CA  . TPO A 1 187 ? 28.109  9.719  30.694  1.00 119.92 ?  342 TPO A CA  1 
HETATM 1299 C CB  . TPO A 1 187 ? 28.728  10.336 31.968  1.00 122.99 ?  342 TPO A CB  1 
HETATM 1300 C CG2 . TPO A 1 187 ? 29.886  11.284 31.579  1.00 123.12 ?  342 TPO A CG2 1 
HETATM 1301 O OG1 . TPO A 1 187 ? 27.721  11.129 32.659  1.00 125.75 ?  342 TPO A OG1 1 
HETATM 1302 P P   . TPO A 1 187 ? 27.592  10.870 34.208  1.00 127.57 ?  342 TPO A P   1 
HETATM 1303 O O1P . TPO A 1 187 ? 26.091  11.035 34.518  1.00 127.73 -1 342 TPO A O1P 1 
HETATM 1304 O O2P . TPO A 1 187 ? 28.341  11.929 35.020  1.00 127.54 -1 342 TPO A O2P 1 
HETATM 1305 O O3P . TPO A 1 187 ? 28.130  9.476  34.630  1.00 127.50 ?  342 TPO A O3P 1 
HETATM 1306 C C   . TPO A 1 187 ? 29.136  9.058  29.772  1.00 120.85 ?  342 TPO A C   1 
HETATM 1307 O O   . TPO A 1 187 ? 29.766  8.071  30.161  1.00 120.67 ?  342 TPO A O   1 
ATOM   1308 N N   . VAL A 1 188 ? 29.296  9.605  28.551  1.00 114.78 ?  343 VAL A N   1 
ATOM   1309 C CA  . VAL A 1 188 ? 30.232  9.101  27.527  1.00 113.28 ?  343 VAL A CA  1 
ATOM   1310 C C   . VAL A 1 188 ? 31.410  10.070 27.256  1.00 113.57 ?  343 VAL A C   1 
ATOM   1311 O O   . VAL A 1 188 ? 31.547  11.065 27.969  1.00 113.02 ?  343 VAL A O   1 
ATOM   1312 C CB  . VAL A 1 188 ? 29.525  8.576  26.235  1.00 117.36 ?  343 VAL A CB  1 
ATOM   1313 C CG1 . VAL A 1 188 ? 28.638  7.369  26.535  1.00 117.12 ?  343 VAL A CG1 1 
ATOM   1314 C CG2 . VAL A 1 188 ? 28.726  9.670  25.530  1.00 117.27 ?  343 VAL A CG2 1 
ATOM   1315 N N   . MET A 1 189 ? 32.261  9.771  26.252  1.00 108.07 ?  344 MET A N   1 
ATOM   1316 C CA  . MET A 1 189 ? 33.437  10.582 25.917  1.00 107.39 ?  344 MET A CA  1 
ATOM   1317 C C   . MET A 1 189 ? 33.590  10.856 24.418  1.00 111.96 ?  344 MET A C   1 
ATOM   1318 O O   . MET A 1 189 ? 33.003  10.148 23.605  1.00 111.74 ?  344 MET A O   1 
ATOM   1319 C CB  . MET A 1 189 ? 34.705  9.896  26.434  1.00 109.35 ?  344 MET A CB  1 
ATOM   1320 C CG  . MET A 1 189 ? 35.059  10.223 27.876  1.00 112.28 ?  344 MET A CG  1 
ATOM   1321 S SD  . MET A 1 189 ? 35.793  11.863 28.152  1.00 115.79 ?  344 MET A SD  1 
ATOM   1322 C CE  . MET A 1 189 ? 37.136  11.866 26.954  1.00 112.19 ?  344 MET A CE  1 
HETATM 1323 N N   . TPO A 1 190 ? 34.410  11.860 24.053  1.00 109.30 ?  345 TPO A N   1 
HETATM 1324 C CA  . TPO A 1 190 ? 34.649  12.226 22.652  1.00 109.85 ?  345 TPO A CA  1 
HETATM 1325 C CB  . TPO A 1 190 ? 33.568  13.246 22.124  1.00 110.82 ?  345 TPO A CB  1 
HETATM 1326 C CG2 . TPO A 1 190 ? 33.620  14.568 22.899  1.00 110.48 ?  345 TPO A CG2 1 
HETATM 1327 O OG1 . TPO A 1 190 ? 33.684  13.609 20.712  1.00 111.89 ?  345 TPO A OG1 1 
HETATM 1328 P P   . TPO A 1 190 ? 33.110  12.598 19.670  1.00 112.52 ?  345 TPO A P   1 
HETATM 1329 O O1P . TPO A 1 190 ? 32.650  13.415 18.459  1.00 112.36 -1 345 TPO A O1P 1 
HETATM 1330 O O2P . TPO A 1 190 ? 34.221  11.645 19.192  1.00 112.68 -1 345 TPO A O2P 1 
HETATM 1331 O O3P . TPO A 1 190 ? 31.957  11.749 20.260  1.00 112.52 ?  345 TPO A O3P 1 
HETATM 1332 C C   . TPO A 1 190 ? 36.067  12.758 22.406  1.00 113.84 ?  345 TPO A C   1 
HETATM 1333 O O   . TPO A 1 190 ? 36.687  13.320 23.314  1.00 112.28 ?  345 TPO A O   1 
HETATM 1334 N N   . SEP A 1 191 ? 36.570  12.581 21.166  1.00 112.02 ?  346 SEP A N   1 
HETATM 1335 C CA  . SEP A 1 191 ? 37.891  13.060 20.749  1.00 112.62 ?  346 SEP A CA  1 
HETATM 1336 C CB  . SEP A 1 191 ? 38.753  12.116 19.891  1.00 115.18 ?  346 SEP A CB  1 
HETATM 1337 O OG  . SEP A 1 191 ? 38.157  11.861 18.607  1.00 117.71 ?  346 SEP A OG  1 
HETATM 1338 C C   . SEP A 1 191 ? 37.830  14.471 20.148  1.00 114.28 ?  346 SEP A C   1 
HETATM 1339 O O   . SEP A 1 191 ? 38.872  15.122 20.018  1.00 113.77 ?  346 SEP A O   1 
HETATM 1340 P P   . SEP A 1 191 ? 37.919  10.344 18.414  1.00 120.22 ?  346 SEP A P   1 
HETATM 1341 O O1P . SEP A 1 191 ? 37.257  10.104 17.052  1.00 120.65 -1 346 SEP A O1P 1 
HETATM 1342 O O2P . SEP A 1 191 ? 37.007  9.766  19.541  1.00 120.29 -1 346 SEP A O2P 1 
HETATM 1343 O O3P . SEP A 1 191 ? 39.281  9.636  18.378  1.00 120.50 ?  346 SEP A O3P 1 
ATOM   1344 N N   . ARG A 1 192 ? 36.612  14.930 19.771  1.00 108.89 ?  347 ARG A N   1 
ATOM   1345 C CA  . ARG A 1 192 ? 36.366  16.267 19.227  1.00 107.48 ?  347 ARG A CA  1 
ATOM   1346 C C   . ARG A 1 192 ? 35.530  17.086 20.224  1.00 107.51 ?  347 ARG A C   1 
ATOM   1347 O O   . ARG A 1 192 ? 34.320  16.854 20.373  1.00 107.94 ?  347 ARG A O   1 
ATOM   1348 C CB  . ARG A 1 192 ? 35.719  16.204 17.822  1.00 108.62 ?  347 ARG A CB  1 
ATOM   1349 C CG  . ARG A 1 192 ? 35.422  17.570 17.177  1.00 122.20 ?  347 ARG A CG  1 
ATOM   1350 C CD  . ARG A 1 192 ? 36.661  18.354 16.750  1.00 134.63 ?  347 ARG A CD  1 
ATOM   1351 N NE  . ARG A 1 192 ? 37.022  19.395 17.718  1.00 141.44 ?  347 ARG A NE  1 
ATOM   1352 C CZ  . ARG A 1 192 ? 36.920  20.705 17.497  1.00 149.39 ?  347 ARG A CZ  1 
ATOM   1353 N NH1 . ARG A 1 192 ? 36.468  21.158 16.332  1.00 131.95 ?  347 ARG A NH1 1 
ATOM   1354 N NH2 . ARG A 1 192 ? 37.279  21.572 18.436  1.00 132.24 1  347 ARG A NH2 1 
ATOM   1355 N N   . ILE A 1 193 ? 36.202  18.019 20.931  1.00 99.45  ?  348 ILE A N   1 
ATOM   1356 C CA  . ILE A 1 193 ? 35.590  18.900 21.931  1.00 96.77  ?  348 ILE A CA  1 
ATOM   1357 C C   . ILE A 1 193 ? 34.943  20.090 21.219  1.00 94.54  ?  348 ILE A C   1 
ATOM   1358 O O   . ILE A 1 193 ? 35.621  20.831 20.503  1.00 93.43  ?  348 ILE A O   1 
ATOM   1359 C CB  . ILE A 1 193 ? 36.592  19.286 23.060  1.00 99.81  ?  348 ILE A CB  1 
ATOM   1360 C CG1 . ILE A 1 193 ? 37.029  18.023 23.842  1.00 99.93  ?  348 ILE A CG1 1 
ATOM   1361 C CG2 . ILE A 1 193 ? 35.999  20.347 24.019  1.00 100.99 ?  348 ILE A CG2 1 
ATOM   1362 C CD1 . ILE A 1 193 ? 38.349  18.122 24.560  1.00 106.73 ?  348 ILE A CD1 1 
ATOM   1363 N N   . VAL A 1 194 ? 33.617  20.231 21.390  1.00 86.93  ?  349 VAL A N   1 
ATOM   1364 C CA  . VAL A 1 194 ? 32.795  21.259 20.744  1.00 84.36  ?  349 VAL A CA  1 
ATOM   1365 C C   . VAL A 1 194 ? 31.808  21.960 21.696  1.00 83.05  ?  349 VAL A C   1 
ATOM   1366 O O   . VAL A 1 194 ? 31.265  21.344 22.628  1.00 81.99  ?  349 VAL A O   1 
ATOM   1367 C CB  . VAL A 1 194 ? 32.099  20.734 19.454  1.00 87.89  ?  349 VAL A CB  1 
ATOM   1368 C CG1 . VAL A 1 194 ? 33.052  20.735 18.259  1.00 87.36  ?  349 VAL A CG1 1 
ATOM   1369 C CG2 . VAL A 1 194 ? 31.474  19.349 19.667  1.00 87.70  ?  349 VAL A CG2 1 
ATOM   1370 N N   . GLY A 1 195 ? 31.574  23.238 21.404  1.00 75.83  ?  350 GLY A N   1 
ATOM   1371 C CA  . GLY A 1 195 ? 30.713  24.143 22.159  1.00 73.58  ?  350 GLY A CA  1 
ATOM   1372 C C   . GLY A 1 195 ? 31.374  25.496 22.333  1.00 73.43  ?  350 GLY A C   1 
ATOM   1373 O O   . GLY A 1 195 ? 32.403  25.776 21.703  1.00 73.42  ?  350 GLY A O   1 
ATOM   1374 N N   . THR A 1 196 ? 30.788  26.361 23.177  1.00 66.04  ?  351 THR A N   1 
ATOM   1375 C CA  . THR A 1 196 ? 31.341  27.691 23.457  1.00 63.08  ?  351 THR A CA  1 
ATOM   1376 C C   . THR A 1 196 ? 31.905  27.637 24.872  1.00 60.50  ?  351 THR A C   1 
ATOM   1377 O O   . THR A 1 196 ? 31.153  27.566 25.844  1.00 58.15  ?  351 THR A O   1 
ATOM   1378 C CB  . THR A 1 196 ? 30.294  28.781 23.203  1.00 71.49  ?  351 THR A CB  1 
ATOM   1379 O OG1 . THR A 1 196 ? 29.774  28.599 21.889  1.00 70.19  ?  351 THR A OG1 1 
ATOM   1380 C CG2 . THR A 1 196 ? 30.857  30.197 23.350  1.00 70.22  ?  351 THR A CG2 1 
ATOM   1381 N N   . THR A 1 197 ? 33.240  27.622 24.964  1.00 55.12  ?  352 THR A N   1 
ATOM   1382 C CA  . THR A 1 197 ? 34.013  27.496 26.198  1.00 54.12  ?  352 THR A CA  1 
ATOM   1383 C C   . THR A 1 197 ? 33.483  28.312 27.372  1.00 57.25  ?  352 THR A C   1 
ATOM   1384 O O   . THR A 1 197 ? 33.479  27.807 28.498  1.00 57.70  ?  352 THR A O   1 
ATOM   1385 C CB  . THR A 1 197 ? 35.515  27.711 25.958  1.00 57.33  ?  352 THR A CB  1 
ATOM   1386 O OG1 . THR A 1 197 ? 35.763  29.077 25.627  1.00 61.71  ?  352 THR A OG1 1 
ATOM   1387 C CG2 . THR A 1 197 ? 36.076  26.802 24.894  1.00 51.36  ?  352 THR A CG2 1 
ATOM   1388 N N   . ALA A 1 198 ? 32.999  29.547 27.106  1.00 50.45  ?  353 ALA A N   1 
ATOM   1389 C CA  . ALA A 1 198 ? 32.477  30.445 28.129  1.00 48.64  ?  353 ALA A CA  1 
ATOM   1390 C C   . ALA A 1 198 ? 31.244  29.928 28.863  1.00 50.58  ?  353 ALA A C   1 
ATOM   1391 O O   . ALA A 1 198 ? 30.959  30.386 29.972  1.00 51.11  ?  353 ALA A O   1 
ATOM   1392 C CB  . ALA A 1 198 ? 32.188  31.792 27.514  1.00 49.35  ?  353 ALA A CB  1 
ATOM   1393 N N   . TYR A 1 199 ? 30.519  28.979 28.256  1.00 45.48  ?  354 TYR A N   1 
ATOM   1394 C CA  . TYR A 1 199 ? 29.291  28.394 28.809  1.00 44.54  ?  354 TYR A CA  1 
ATOM   1395 C C   . TYR A 1 199 ? 29.474  26.957 29.234  1.00 49.65  ?  354 TYR A C   1 
ATOM   1396 O O   . TYR A 1 199 ? 28.668  26.448 30.013  1.00 50.22  ?  354 TYR A O   1 
ATOM   1397 C CB  . TYR A 1 199 ? 28.174  28.431 27.752  1.00 45.25  ?  354 TYR A CB  1 
ATOM   1398 C CG  . TYR A 1 199 ? 27.786  29.813 27.276  1.00 45.96  ?  354 TYR A CG  1 
ATOM   1399 C CD1 . TYR A 1 199 ? 28.478  30.434 26.240  1.00 48.27  ?  354 TYR A CD1 1 
ATOM   1400 C CD2 . TYR A 1 199 ? 26.690  30.477 27.818  1.00 45.78  ?  354 TYR A CD2 1 
ATOM   1401 C CE1 . TYR A 1 199 ? 28.121  31.706 25.793  1.00 50.36  ?  354 TYR A CE1 1 
ATOM   1402 C CE2 . TYR A 1 199 ? 26.319  31.744 27.374  1.00 46.27  ?  354 TYR A CE2 1 
ATOM   1403 C CZ  . TYR A 1 199 ? 27.024  32.346 26.345  1.00 52.70  ?  354 TYR A CZ  1 
ATOM   1404 O OH  . TYR A 1 199 ? 26.688  33.597 25.901  1.00 50.83  ?  354 TYR A OH  1 
ATOM   1405 N N   . MET A 1 200 ? 30.484  26.286 28.669  1.00 47.83  ?  355 MET A N   1 
ATOM   1406 C CA  . MET A 1 200 ? 30.774  24.873 28.879  1.00 47.65  ?  355 MET A CA  1 
ATOM   1407 C C   . MET A 1 200 ? 31.112  24.471 30.299  1.00 54.76  ?  355 MET A C   1 
ATOM   1408 O O   . MET A 1 200 ? 31.929  25.118 30.967  1.00 54.75  ?  355 MET A O   1 
ATOM   1409 C CB  . MET A 1 200 ? 31.857  24.387 27.914  1.00 49.18  ?  355 MET A CB  1 
ATOM   1410 C CG  . MET A 1 200 ? 31.376  24.340 26.495  1.00 52.58  ?  355 MET A CG  1 
ATOM   1411 S SD  . MET A 1 200 ? 32.645  23.895 25.312  1.00 56.12  ?  355 MET A SD  1 
ATOM   1412 C CE  . MET A 1 200 ? 32.691  22.158 25.561  1.00 53.02  ?  355 MET A CE  1 
ATOM   1413 N N   . ALA A 1 201 ? 30.499  23.354 30.735  1.00 51.76  ?  356 ALA A N   1 
ATOM   1414 C CA  . ALA A 1 201 ? 30.756  22.721 32.018  1.00 51.82  ?  356 ALA A CA  1 
ATOM   1415 C C   . ALA A 1 201 ? 32.204  22.173 32.000  1.00 54.88  ?  356 ALA A C   1 
ATOM   1416 O O   . ALA A 1 201 ? 32.706  21.835 30.919  1.00 52.63  ?  356 ALA A O   1 
ATOM   1417 C CB  . ALA A 1 201 ? 29.759  21.596 32.240  1.00 52.93  ?  356 ALA A CB  1 
ATOM   1418 N N   . PRO A 1 202 ? 32.920  22.141 33.153  1.00 52.42  ?  357 PRO A N   1 
ATOM   1419 C CA  . PRO A 1 202 ? 34.317  21.653 33.140  1.00 51.66  ?  357 PRO A CA  1 
ATOM   1420 C C   . PRO A 1 202 ? 34.517  20.293 32.449  1.00 55.44  ?  357 PRO A C   1 
ATOM   1421 O O   . PRO A 1 202 ? 35.415  20.179 31.607  1.00 54.58  ?  357 PRO A O   1 
ATOM   1422 C CB  . PRO A 1 202 ? 34.710  21.639 34.622  1.00 53.26  ?  357 PRO A CB  1 
ATOM   1423 C CG  . PRO A 1 202 ? 33.417  21.708 35.387  1.00 58.48  ?  357 PRO A CG  1 
ATOM   1424 C CD  . PRO A 1 202 ? 32.498  22.516 34.519  1.00 54.32  ?  357 PRO A CD  1 
ATOM   1425 N N   . GLU A 1 203 ? 33.634  19.298 32.734  1.00 51.94  ?  358 GLU A N   1 
ATOM   1426 C CA  . GLU A 1 203 ? 33.688  17.969 32.117  1.00 52.33  ?  358 GLU A CA  1 
ATOM   1427 C C   . GLU A 1 203 ? 33.492  18.009 30.597  1.00 57.24  ?  358 GLU A C   1 
ATOM   1428 O O   . GLU A 1 203 ? 34.105  17.218 29.872  1.00 56.32  ?  358 GLU A O   1 
ATOM   1429 C CB  . GLU A 1 203 ? 32.710  16.986 32.780  1.00 53.72  ?  358 GLU A CB  1 
ATOM   1430 C CG  . GLU A 1 203 ? 31.225  17.256 32.544  1.00 65.91  ?  358 GLU A CG  1 
ATOM   1431 C CD  . GLU A 1 203 ? 30.548  18.307 33.406  1.00 83.64  ?  358 GLU A CD  1 
ATOM   1432 O OE1 . GLU A 1 203 ? 31.241  19.046 34.145  1.00 81.71  ?  358 GLU A OE1 1 
ATOM   1433 O OE2 . GLU A 1 203 ? 29.305  18.406 33.317  1.00 72.62  -1 358 GLU A OE2 1 
ATOM   1434 N N   . ALA A 1 204 ? 32.649  18.941 30.122  1.00 54.27  ?  359 ALA A N   1 
ATOM   1435 C CA  . ALA A 1 204 ? 32.394  19.104 28.698  1.00 53.82  ?  359 ALA A CA  1 
ATOM   1436 C C   . ALA A 1 204 ? 33.689  19.598 28.010  1.00 56.52  ?  359 ALA A C   1 
ATOM   1437 O O   . ALA A 1 204 ? 34.004  19.156 26.899  1.00 56.96  ?  359 ALA A O   1 
ATOM   1438 C CB  . ALA A 1 204 ? 31.249  20.076 28.480  1.00 54.12  ?  359 ALA A CB  1 
ATOM   1439 N N   . LEU A 1 205 ? 34.459  20.467 28.704  1.00 50.45  ?  360 LEU A N   1 
ATOM   1440 C CA  . LEU A 1 205 ? 35.729  20.993 28.209  1.00 50.06  ?  360 LEU A CA  1 
ATOM   1441 C C   . LEU A 1 205 ? 36.782  19.889 28.137  1.00 57.52  ?  360 LEU A C   1 
ATOM   1442 O O   . LEU A 1 205 ? 37.705  19.978 27.321  1.00 55.27  ?  360 LEU A O   1 
ATOM   1443 C CB  . LEU A 1 205 ? 36.224  22.162 29.078  1.00 48.92  ?  360 LEU A CB  1 
ATOM   1444 C CG  . LEU A 1 205 ? 35.456  23.486 28.948  1.00 50.87  ?  360 LEU A CG  1 
ATOM   1445 C CD1 . LEU A 1 205 ? 35.775  24.403 30.094  1.00 49.25  ?  360 LEU A CD1 1 
ATOM   1446 C CD2 . LEU A 1 205 ? 35.739  24.184 27.617  1.00 48.24  ?  360 LEU A CD2 1 
ATOM   1447 N N   . ARG A 1 206 ? 36.608  18.833 28.964  1.00 57.69  ?  361 ARG A N   1 
ATOM   1448 C CA  . ARG A 1 206 ? 37.454  17.637 29.009  1.00 58.40  ?  361 ARG A CA  1 
ATOM   1449 C C   . ARG A 1 206 ? 37.134  16.714 27.824  1.00 62.80  ?  361 ARG A C   1 
ATOM   1450 O O   . ARG A 1 206 ? 38.044  16.116 27.263  1.00 62.06  ?  361 ARG A O   1 
ATOM   1451 C CB  . ARG A 1 206 ? 37.222  16.855 30.331  1.00 59.75  ?  361 ARG A CB  1 
ATOM   1452 C CG  . ARG A 1 206 ? 37.570  17.610 31.606  1.00 65.75  ?  361 ARG A CG  1 
ATOM   1453 C CD  . ARG A 1 206 ? 38.932  18.237 31.449  1.00 72.83  ?  361 ARG A CD  1 
ATOM   1454 N NE  . ARG A 1 206 ? 39.254  19.150 32.533  1.00 77.09  ?  361 ARG A NE  1 
ATOM   1455 C CZ  . ARG A 1 206 ? 40.400  19.806 32.606  1.00 78.55  ?  361 ARG A CZ  1 
ATOM   1456 N NH1 . ARG A 1 206 ? 41.319  19.656 31.659  1.00 47.64  ?  361 ARG A NH1 1 
ATOM   1457 N NH2 . ARG A 1 206 ? 40.644  20.614 33.630  1.00 63.42  1  361 ARG A NH2 1 
ATOM   1458 N N   . GLY A 1 207 ? 35.848  16.604 27.484  1.00 59.74  ?  362 GLY A N   1 
ATOM   1459 C CA  . GLY A 1 207 ? 35.352  15.737 26.420  1.00 60.01  ?  362 GLY A CA  1 
ATOM   1460 C C   . GLY A 1 207 ? 34.190  14.858 26.845  1.00 66.29  ?  362 GLY A C   1 
ATOM   1461 O O   . GLY A 1 207 ? 33.796  13.967 26.093  1.00 65.64  ?  362 GLY A O   1 
ATOM   1462 N N   . GLU A 1 208 ? 33.623  15.089 28.053  1.00 64.64  ?  363 GLU A N   1 
ATOM   1463 C CA  . GLU A 1 208 ? 32.502  14.296 28.552  1.00 65.08  ?  363 GLU A CA  1 
ATOM   1464 C C   . GLU A 1 208 ? 31.185  14.815 28.007  1.00 71.18  ?  363 GLU A C   1 
ATOM   1465 O O   . GLU A 1 208 ? 30.984  16.030 27.902  1.00 70.57  ?  363 GLU A O   1 
ATOM   1466 C CB  . GLU A 1 208 ? 32.469  14.238 30.087  1.00 66.44  ?  363 GLU A CB  1 
ATOM   1467 N N   . ILE A 1 209 ? 30.282  13.870 27.669  1.00 69.19  ?  364 ILE A N   1 
ATOM   1468 C CA  . ILE A 1 209 ? 28.945  14.111 27.116  1.00 68.80  ?  364 ILE A CA  1 
ATOM   1469 C C   . ILE A 1 209 ? 27.875  13.648 28.131  1.00 70.18  ?  364 ILE A C   1 
ATOM   1470 O O   . ILE A 1 209 ? 27.707  12.445 28.361  1.00 71.06  ?  364 ILE A O   1 
ATOM   1471 C CB  . ILE A 1 209 ? 28.826  13.485 25.682  1.00 72.36  ?  364 ILE A CB  1 
ATOM   1472 C CG1 . ILE A 1 209 ? 29.799  14.218 24.686  1.00 73.33  ?  364 ILE A CG1 1 
ATOM   1473 C CG2 . ILE A 1 209 ? 27.372  13.499 25.165  1.00 72.57  ?  364 ILE A CG2 1 
ATOM   1474 C CD1 . ILE A 1 209 ? 30.195  13.478 23.426  1.00 82.36  ?  364 ILE A CD1 1 
ATOM   1475 N N   . THR A 1 210 ? 27.207  14.613 28.782  1.00 63.46  ?  365 THR A N   1 
ATOM   1476 C CA  . THR A 1 210 ? 26.191  14.335 29.807  1.00 62.04  ?  365 THR A CA  1 
ATOM   1477 C C   . THR A 1 210 ? 25.072  15.382 29.818  1.00 62.39  ?  365 THR A C   1 
ATOM   1478 O O   . THR A 1 210 ? 25.368  16.563 29.658  1.00 61.36  ?  365 THR A O   1 
ATOM   1479 C CB  . THR A 1 210 ? 26.838  14.122 31.204  1.00 68.52  ?  365 THR A CB  1 
ATOM   1480 O OG1 . THR A 1 210 ? 25.823  14.139 32.212  1.00 72.00  ?  365 THR A OG1 1 
ATOM   1481 C CG2 . THR A 1 210 ? 27.881  15.166 31.537  1.00 64.41  ?  365 THR A CG2 1 
ATOM   1482 N N   . PRO A 1 211 ? 23.795  15.005 30.055  1.00 57.61  ?  366 PRO A N   1 
ATOM   1483 C CA  . PRO A 1 211 ? 22.728  16.027 30.094  1.00 57.38  ?  366 PRO A CA  1 
ATOM   1484 C C   . PRO A 1 211 ? 22.945  17.067 31.197  1.00 61.46  ?  366 PRO A C   1 
ATOM   1485 O O   . PRO A 1 211 ? 22.431  18.179 31.103  1.00 62.21  ?  366 PRO A O   1 
ATOM   1486 C CB  . PRO A 1 211 ? 21.463  15.204 30.349  1.00 58.63  ?  366 PRO A CB  1 
ATOM   1487 C CG  . PRO A 1 211 ? 21.956  13.957 30.995  1.00 62.81  ?  366 PRO A CG  1 
ATOM   1488 C CD  . PRO A 1 211 ? 23.238  13.662 30.288  1.00 58.45  ?  366 PRO A CD  1 
ATOM   1489 N N   . LYS A 1 212 ? 23.724  16.705 32.224  1.00 56.07  ?  367 LYS A N   1 
ATOM   1490 C CA  . LYS A 1 212 ? 24.052  17.571 33.351  1.00 54.80  ?  367 LYS A CA  1 
ATOM   1491 C C   . LYS A 1 212 ? 24.918  18.763 32.903  1.00 54.54  ?  367 LYS A C   1 
ATOM   1492 O O   . LYS A 1 212 ? 24.940  19.778 33.595  1.00 53.25  ?  367 LYS A O   1 
ATOM   1493 C CB  . LYS A 1 212 ? 24.725  16.754 34.478  1.00 57.60  ?  367 LYS A CB  1 
ATOM   1494 N N   . SER A 1 213 ? 25.597  18.649 31.733  1.00 49.28  ?  368 SER A N   1 
ATOM   1495 C CA  . SER A 1 213 ? 26.416  19.727 31.161  1.00 48.23  ?  368 SER A CA  1 
ATOM   1496 C C   . SER A 1 213 ? 25.499  20.869 30.675  1.00 50.09  ?  368 SER A C   1 
ATOM   1497 O O   . SER A 1 213 ? 25.844  22.034 30.850  1.00 49.08  ?  368 SER A O   1 
ATOM   1498 C CB  . SER A 1 213 ? 27.278  19.215 30.014  1.00 51.33  ?  368 SER A CB  1 
ATOM   1499 O OG  . SER A 1 213 ? 28.306  18.352 30.464  1.00 63.43  ?  368 SER A OG  1 
ATOM   1500 N N   . ASP A 1 214 ? 24.324  20.518 30.097  1.00 45.06  ?  369 ASP A N   1 
ATOM   1501 C CA  . ASP A 1 214 ? 23.291  21.434 29.617  1.00 43.87  ?  369 ASP A CA  1 
ATOM   1502 C C   . ASP A 1 214 ? 22.768  22.298 30.774  1.00 46.33  ?  369 ASP A C   1 
ATOM   1503 O O   . ASP A 1 214 ? 22.534  23.493 30.578  1.00 46.31  ?  369 ASP A O   1 
ATOM   1504 C CB  . ASP A 1 214 ? 22.129  20.653 28.946  1.00 45.99  ?  369 ASP A CB  1 
ATOM   1505 C CG  . ASP A 1 214 ? 22.346  20.217 27.492  1.00 58.10  ?  369 ASP A CG  1 
ATOM   1506 O OD1 . ASP A 1 214 ? 23.460  20.464 26.943  1.00 60.28  ?  369 ASP A OD1 1 
ATOM   1507 O OD2 . ASP A 1 214 ? 21.405  19.638 26.897  1.00 58.45  -1 369 ASP A OD2 1 
ATOM   1508 N N   . ILE A 1 215 ? 22.629  21.707 31.982  1.00 41.10  ?  370 ILE A N   1 
ATOM   1509 C CA  . ILE A 1 215 ? 22.212  22.390 33.213  1.00 40.29  ?  370 ILE A CA  1 
ATOM   1510 C C   . ILE A 1 215 ? 23.238  23.461 33.621  1.00 46.25  ?  370 ILE A C   1 
ATOM   1511 O O   . ILE A 1 215 ? 22.846  24.579 33.994  1.00 48.07  ?  370 ILE A O   1 
ATOM   1512 C CB  . ILE A 1 215 ? 21.966  21.375 34.350  1.00 42.83  ?  370 ILE A CB  1 
ATOM   1513 C CG1 . ILE A 1 215 ? 20.940  20.300 33.948  1.00 42.55  ?  370 ILE A CG1 1 
ATOM   1514 C CG2 . ILE A 1 215 ? 21.624  22.056 35.691  1.00 43.82  ?  370 ILE A CG2 1 
ATOM   1515 C CD1 . ILE A 1 215 ? 19.529  20.770 33.815  1.00 49.45  ?  370 ILE A CD1 1 
ATOM   1516 N N   . TYR A 1 216 ? 24.546  23.136 33.511  1.00 40.61  ?  371 TYR A N   1 
ATOM   1517 C CA  . TYR A 1 216 ? 25.616  24.081 33.829  1.00 39.56  ?  371 TYR A CA  1 
ATOM   1518 C C   . TYR A 1 216 ? 25.565  25.275 32.876  1.00 44.50  ?  371 TYR A C   1 
ATOM   1519 O O   . TYR A 1 216 ? 25.601  26.410 33.336  1.00 45.61  ?  371 TYR A O   1 
ATOM   1520 C CB  . TYR A 1 216 ? 26.980  23.385 33.789  1.00 39.97  ?  371 TYR A CB  1 
ATOM   1521 C CG  . TYR A 1 216 ? 28.143  24.237 34.259  1.00 42.08  ?  371 TYR A CG  1 
ATOM   1522 C CD1 . TYR A 1 216 ? 28.807  25.095 33.382  1.00 44.32  ?  371 TYR A CD1 1 
ATOM   1523 C CD2 . TYR A 1 216 ? 28.604  24.161 35.573  1.00 42.42  ?  371 TYR A CD2 1 
ATOM   1524 C CE1 . TYR A 1 216 ? 29.885  25.871 33.804  1.00 45.62  ?  371 TYR A CE1 1 
ATOM   1525 C CE2 . TYR A 1 216 ? 29.692  24.915 36.003  1.00 43.20  ?  371 TYR A CE2 1 
ATOM   1526 C CZ  . TYR A 1 216 ? 30.334  25.768 35.115  1.00 53.58  ?  371 TYR A CZ  1 
ATOM   1527 O OH  . TYR A 1 216 ? 31.416  26.515 35.532  1.00 55.40  ?  371 TYR A OH  1 
ATOM   1528 N N   . SER A 1 217 ? 25.444  25.014 31.565  1.00 40.21  ?  372 SER A N   1 
ATOM   1529 C CA  . SER A 1 217 ? 25.384  26.023 30.523  1.00 39.64  ?  372 SER A CA  1 
ATOM   1530 C C   . SER A 1 217 ? 24.199  26.984 30.715  1.00 40.37  ?  372 SER A C   1 
ATOM   1531 O O   . SER A 1 217 ? 24.346  28.195 30.524  1.00 37.49  ?  372 SER A O   1 
ATOM   1532 C CB  . SER A 1 217 ? 25.323  25.351 29.159  1.00 42.76  ?  372 SER A CB  1 
ATOM   1533 O OG  . SER A 1 217 ? 26.590  24.817 28.834  1.00 44.70  ?  372 SER A OG  1 
ATOM   1534 N N   . PHE A 1 218 ? 23.066  26.443 31.146  1.00 37.09  ?  373 PHE A N   1 
ATOM   1535 C CA  . PHE A 1 218 ? 21.868  27.209 31.440  1.00 37.91  ?  373 PHE A CA  1 
ATOM   1536 C C   . PHE A 1 218 ? 22.081  28.137 32.642  1.00 45.04  ?  373 PHE A C   1 
ATOM   1537 O O   . PHE A 1 218 ? 21.512  29.221 32.667  1.00 47.16  ?  373 PHE A O   1 
ATOM   1538 C CB  . PHE A 1 218 ? 20.676  26.278 31.667  1.00 40.95  ?  373 PHE A CB  1 
ATOM   1539 C CG  . PHE A 1 218 ? 19.363  27.015 31.806  1.00 44.60  ?  373 PHE A CG  1 
ATOM   1540 C CD1 . PHE A 1 218 ? 18.842  27.743 30.750  1.00 47.79  ?  373 PHE A CD1 1 
ATOM   1541 C CD2 . PHE A 1 218 ? 18.664  27.007 33.009  1.00 48.06  ?  373 PHE A CD2 1 
ATOM   1542 C CE1 . PHE A 1 218 ? 17.651  28.447 30.894  1.00 49.28  ?  373 PHE A CE1 1 
ATOM   1543 C CE2 . PHE A 1 218 ? 17.471  27.713 33.150  1.00 50.80  ?  373 PHE A CE2 1 
ATOM   1544 C CZ  . PHE A 1 218 ? 16.968  28.425 32.092  1.00 48.64  ?  373 PHE A CZ  1 
ATOM   1545 N N   . GLY A 1 219 ? 22.937  27.746 33.591  1.00 41.59  ?  374 GLY A N   1 
ATOM   1546 C CA  . GLY A 1 219 ? 23.272  28.563 34.748  1.00 40.96  ?  374 GLY A CA  1 
ATOM   1547 C C   . GLY A 1 219 ? 24.069  29.784 34.340  1.00 46.10  ?  374 GLY A C   1 
ATOM   1548 O O   . GLY A 1 219 ? 23.887  30.871 34.907  1.00 47.74  ?  374 GLY A O   1 
ATOM   1549 N N   . VAL A 1 220 ? 24.920  29.633 33.306  1.00 41.30  ?  375 VAL A N   1 
ATOM   1550 C CA  . VAL A 1 220 ? 25.703  30.752 32.750  1.00 40.37  ?  375 VAL A CA  1 
ATOM   1551 C C   . VAL A 1 220 ? 24.728  31.741 32.083  1.00 40.98  ?  375 VAL A C   1 
ATOM   1552 O O   . VAL A 1 220 ? 24.887  32.963 32.200  1.00 40.21  ?  375 VAL A O   1 
ATOM   1553 C CB  . VAL A 1 220 ? 26.814  30.268 31.772  1.00 45.38  ?  375 VAL A CB  1 
ATOM   1554 C CG1 . VAL A 1 220 ? 27.599  31.446 31.190  1.00 45.25  ?  375 VAL A CG1 1 
ATOM   1555 C CG2 . VAL A 1 220 ? 27.773  29.290 32.458  1.00 45.07  ?  375 VAL A CG2 1 
ATOM   1556 N N   . VAL A 1 221 ? 23.684  31.189 31.431  1.00 34.40  ?  376 VAL A N   1 
ATOM   1557 C CA  . VAL A 1 221 ? 22.634  31.949 30.770  1.00 31.44  ?  376 VAL A CA  1 
ATOM   1558 C C   . VAL A 1 221 ? 21.860  32.731 31.807  1.00 35.31  ?  376 VAL A C   1 
ATOM   1559 O O   . VAL A 1 221 ? 21.627  33.933 31.601  1.00 34.67  ?  376 VAL A O   1 
ATOM   1560 C CB  . VAL A 1 221 ? 21.748  31.058 29.872  1.00 32.69  ?  376 VAL A CB  1 
ATOM   1561 C CG1 . VAL A 1 221 ? 20.525  31.820 29.375  1.00 32.37  ?  376 VAL A CG1 1 
ATOM   1562 C CG2 . VAL A 1 221 ? 22.551  30.503 28.690  1.00 31.47  ?  376 VAL A CG2 1 
ATOM   1563 N N   . LEU A 1 222 ? 21.512  32.080 32.944  1.00 32.15  ?  377 LEU A N   1 
ATOM   1564 C CA  . LEU A 1 222 ? 20.785  32.773 34.017  1.00 33.67  ?  377 LEU A CA  1 
ATOM   1565 C C   . LEU A 1 222 ? 21.616  33.925 34.593  1.00 39.53  ?  377 LEU A C   1 
ATOM   1566 O O   . LEU A 1 222 ? 21.067  34.986 34.860  1.00 41.89  ?  377 LEU A O   1 
ATOM   1567 C CB  . LEU A 1 222 ? 20.291  31.821 35.109  1.00 34.21  ?  377 LEU A CB  1 
ATOM   1568 C CG  . LEU A 1 222 ? 19.252  30.769 34.697  1.00 40.03  ?  377 LEU A CG  1 
ATOM   1569 C CD1 . LEU A 1 222 ? 18.997  29.822 35.819  1.00 41.40  ?  377 LEU A CD1 1 
ATOM   1570 C CD2 . LEU A 1 222 ? 17.926  31.393 34.270  1.00 41.83  ?  377 LEU A CD2 1 
ATOM   1571 N N   . LEU A 1 223 ? 22.942  33.764 34.667  1.00 34.49  ?  378 LEU A N   1 
ATOM   1572 C CA  . LEU A 1 223 ? 23.795  34.858 35.096  1.00 34.58  ?  378 LEU A CA  1 
ATOM   1573 C C   . LEU A 1 223 ? 23.771  36.003 34.060  1.00 41.40  ?  378 LEU A C   1 
ATOM   1574 O O   . LEU A 1 223 ? 23.760  37.174 34.452  1.00 43.08  ?  378 LEU A O   1 
ATOM   1575 C CB  . LEU A 1 223 ? 25.237  34.392 35.345  1.00 34.39  ?  378 LEU A CB  1 
ATOM   1576 C CG  . LEU A 1 223 ? 25.534  33.467 36.532  1.00 37.94  ?  378 LEU A CG  1 
ATOM   1577 C CD1 . LEU A 1 223 ? 27.025  33.347 36.713  1.00 38.39  ?  378 LEU A CD1 1 
ATOM   1578 C CD2 . LEU A 1 223 ? 24.932  33.984 37.844  1.00 36.51  ?  378 LEU A CD2 1 
ATOM   1579 N N   . GLU A 1 224 ? 23.741  35.670 32.751  1.00 37.36  ?  379 GLU A N   1 
ATOM   1580 C CA  . GLU A 1 224 ? 23.654  36.679 31.685  1.00 36.36  ?  379 GLU A CA  1 
ATOM   1581 C C   . GLU A 1 224 ? 22.338  37.407 31.840  1.00 42.13  ?  379 GLU A C   1 
ATOM   1582 O O   . GLU A 1 224 ? 22.313  38.629 31.757  1.00 42.74  ?  379 GLU A O   1 
ATOM   1583 C CB  . GLU A 1 224 ? 23.701  36.040 30.294  1.00 36.84  ?  379 GLU A CB  1 
ATOM   1584 C CG  . GLU A 1 224 ? 25.066  35.530 29.898  1.00 40.40  ?  379 GLU A CG  1 
ATOM   1585 C CD  . GLU A 1 224 ? 25.099  34.936 28.508  1.00 67.68  ?  379 GLU A CD  1 
ATOM   1586 O OE1 . GLU A 1 224 ? 24.284  34.027 28.222  1.00 67.39  ?  379 GLU A OE1 1 
ATOM   1587 O OE2 . GLU A 1 224 ? 25.941  35.389 27.699  1.00 66.04  -1 379 GLU A OE2 1 
ATOM   1588 N N   . ILE A 1 225 ? 21.251  36.663 32.103  1.00 39.60  ?  380 ILE A N   1 
ATOM   1589 C CA  . ILE A 1 225 ? 19.928  37.260 32.308  1.00 40.08  ?  380 ILE A CA  1 
ATOM   1590 C C   . ILE A 1 225 ? 19.908  38.263 33.499  1.00 44.77  ?  380 ILE A C   1 
ATOM   1591 O O   . ILE A 1 225 ? 19.384  39.375 33.337  1.00 45.94  ?  380 ILE A O   1 
ATOM   1592 C CB  . ILE A 1 225 ? 18.796  36.193 32.340  1.00 43.27  ?  380 ILE A CB  1 
ATOM   1593 C CG1 . ILE A 1 225 ? 18.610  35.517 30.948  1.00 43.79  ?  380 ILE A CG1 1 
ATOM   1594 C CG2 . ILE A 1 225 ? 17.486  36.817 32.799  1.00 43.60  ?  380 ILE A CG2 1 
ATOM   1595 C CD1 . ILE A 1 225 ? 17.653  34.319 30.892  1.00 50.35  ?  380 ILE A CD1 1 
ATOM   1596 N N   . ILE A 1 226 ? 20.541  37.912 34.645  1.00 37.94  ?  381 ILE A N   1 
ATOM   1597 C CA  . ILE A 1 226 ? 20.569  38.814 35.790  1.00 37.04  ?  381 ILE A CA  1 
ATOM   1598 C C   . ILE A 1 226 ? 21.415  40.090 35.535  1.00 42.81  ?  381 ILE A C   1 
ATOM   1599 O O   . ILE A 1 226 ? 21.020  41.201 35.907  1.00 41.00  ?  381 ILE A O   1 
ATOM   1600 C CB  . ILE A 1 226 ? 21.039  38.062 37.067  1.00 39.38  ?  381 ILE A CB  1 
ATOM   1601 C CG1 . ILE A 1 226 ? 20.079  36.938 37.455  1.00 37.55  ?  381 ILE A CG1 1 
ATOM   1602 C CG2 . ILE A 1 226 ? 21.238  39.036 38.261  1.00 42.16  ?  381 ILE A CG2 1 
ATOM   1603 C CD1 . ILE A 1 226 ? 20.763  35.718 38.202  1.00 26.43  ?  381 ILE A CD1 1 
ATOM   1604 N N   . THR A 1 227 ? 22.599  39.899 34.948  1.00 40.81  ?  382 THR A N   1 
ATOM   1605 C CA  . THR A 1 227 ? 23.609  40.942 34.765  1.00 40.08  ?  382 THR A CA  1 
ATOM   1606 C C   . THR A 1 227 ? 23.560  41.725 33.457  1.00 44.59  ?  382 THR A C   1 
ATOM   1607 O O   . THR A 1 227 ? 24.074  42.847 33.406  1.00 46.13  ?  382 THR A O   1 
ATOM   1608 C CB  . THR A 1 227 ? 25.013  40.346 34.982  1.00 41.28  ?  382 THR A CB  1 
ATOM   1609 O OG1 . THR A 1 227 ? 25.371  39.534 33.868  1.00 43.22  ?  382 THR A OG1 1 
ATOM   1610 C CG2 . THR A 1 227 ? 25.122  39.541 36.248  1.00 34.17  ?  382 THR A CG2 1 
ATOM   1611 N N   . GLY A 1 228 ? 23.031  41.113 32.405  1.00 39.45  ?  383 GLY A N   1 
ATOM   1612 C CA  . GLY A 1 228 ? 22.992  41.719 31.078  1.00 39.73  ?  383 GLY A CA  1 
ATOM   1613 C C   . GLY A 1 228 ? 24.351  41.713 30.399  1.00 44.53  ?  383 GLY A C   1 
ATOM   1614 O O   . GLY A 1 228 ? 24.528  42.347 29.346  1.00 44.42  ?  383 GLY A O   1 
ATOM   1615 N N   . LEU A 1 229 ? 25.327  41.014 31.021  1.00 40.38  ?  384 LEU A N   1 
ATOM   1616 C CA  . LEU A 1 229 ? 26.712  40.875 30.564  1.00 40.03  ?  384 LEU A CA  1 
ATOM   1617 C C   . LEU A 1 229 ? 26.895  39.604 29.762  1.00 45.79  ?  384 LEU A C   1 
ATOM   1618 O O   . LEU A 1 229 ? 26.381  38.564 30.193  1.00 47.47  ?  384 LEU A O   1 
ATOM   1619 C CB  . LEU A 1 229 ? 27.655  40.790 31.767  1.00 39.78  ?  384 LEU A CB  1 
ATOM   1620 C CG  . LEU A 1 229 ? 27.782  42.012 32.648  1.00 43.68  ?  384 LEU A CG  1 
ATOM   1621 C CD1 . LEU A 1 229 ? 28.390  41.635 33.972  1.00 43.24  ?  384 LEU A CD1 1 
ATOM   1622 C CD2 . LEU A 1 229 ? 28.641  43.069 31.980  1.00 45.54  ?  384 LEU A CD2 1 
ATOM   1623 N N   . PRO A 1 230 ? 27.668  39.635 28.639  1.00 42.14  ?  385 PRO A N   1 
ATOM   1624 C CA  . PRO A 1 230 ? 27.922  38.381 27.892  1.00 42.36  ?  385 PRO A CA  1 
ATOM   1625 C C   . PRO A 1 230 ? 28.814  37.441 28.726  1.00 48.07  ?  385 PRO A C   1 
ATOM   1626 O O   . PRO A 1 230 ? 29.570  37.940 29.577  1.00 48.98  ?  385 PRO A O   1 
ATOM   1627 C CB  . PRO A 1 230 ? 28.624  38.866 26.621  1.00 44.27  ?  385 PRO A CB  1 
ATOM   1628 C CG  . PRO A 1 230 ? 29.301  40.171 27.024  1.00 48.64  ?  385 PRO A CG  1 
ATOM   1629 C CD  . PRO A 1 230 ? 28.373  40.790 28.033  1.00 43.85  ?  385 PRO A CD  1 
ATOM   1630 N N   . ALA A 1 231 ? 28.708  36.097 28.521  1.00 43.07  ?  386 ALA A N   1 
ATOM   1631 C CA  . ALA A 1 231 ? 29.482  35.084 29.272  1.00 41.55  ?  386 ALA A CA  1 
ATOM   1632 C C   . ALA A 1 231 ? 31.004  35.339 29.235  1.00 48.41  ?  386 ALA A C   1 
ATOM   1633 O O   . ALA A 1 231 ? 31.714  35.065 30.209  1.00 47.14  ?  386 ALA A O   1 
ATOM   1634 C CB  . ALA A 1 231 ? 29.180  33.698 28.744  1.00 41.23  ?  386 ALA A CB  1 
ATOM   1635 N N   . VAL A 1 232 ? 31.484  35.853 28.096  1.00 47.17  ?  387 VAL A N   1 
ATOM   1636 C CA  . VAL A 1 232 ? 32.867  36.218 27.871  1.00 47.82  ?  387 VAL A CA  1 
ATOM   1637 C C   . VAL A 1 232 ? 32.901  37.562 27.178  1.00 54.36  ?  387 VAL A C   1 
ATOM   1638 O O   . VAL A 1 232 ? 32.082  37.839 26.301  1.00 53.28  ?  387 VAL A O   1 
ATOM   1639 C CB  . VAL A 1 232 ? 33.708  35.133 27.129  1.00 51.14  ?  387 VAL A CB  1 
ATOM   1640 C CG1 . VAL A 1 232 ? 33.219  34.897 25.698  1.00 51.00  ?  387 VAL A CG1 1 
ATOM   1641 C CG2 . VAL A 1 232 ? 35.195  35.460 27.148  1.00 50.13  ?  387 VAL A CG2 1 
ATOM   1642 N N   . ASP A 1 233 ? 33.833  38.401 27.610  1.00 54.47  ?  388 ASP A N   1 
ATOM   1643 C CA  . ASP A 1 233 ? 34.112  39.716 27.067  1.00 56.10  ?  388 ASP A CA  1 
ATOM   1644 C C   . ASP A 1 233 ? 35.605  39.935 27.255  1.00 64.26  ?  388 ASP A C   1 
ATOM   1645 O O   . ASP A 1 233 ? 36.067  40.091 28.386  1.00 63.97  ?  388 ASP A O   1 
ATOM   1646 C CB  . ASP A 1 233 ? 33.276  40.787 27.776  1.00 57.87  ?  388 ASP A CB  1 
ATOM   1647 C CG  . ASP A 1 233 ? 33.371  42.191 27.202  1.00 70.20  ?  388 ASP A CG  1 
ATOM   1648 O OD1 . ASP A 1 233 ? 33.991  42.359 26.109  1.00 70.66  ?  388 ASP A OD1 1 
ATOM   1649 O OD2 . ASP A 1 233 ? 32.789  43.122 27.815  1.00 76.91  -1 388 ASP A OD2 1 
ATOM   1650 N N   . GLU A 1 234 ? 36.363  39.865 26.145  1.00 64.20  ?  389 GLU A N   1 
ATOM   1651 C CA  . GLU A 1 234 ? 37.820  40.010 26.116  1.00 65.54  ?  389 GLU A CA  1 
ATOM   1652 C C   . GLU A 1 234 ? 38.287  41.341 26.729  1.00 71.42  ?  389 GLU A C   1 
ATOM   1653 O O   . GLU A 1 234 ? 39.351  41.397 27.347  1.00 70.53  ?  389 GLU A O   1 
ATOM   1654 C CB  . GLU A 1 234 ? 38.334  39.864 24.672  1.00 66.85  ?  389 GLU A CB  1 
ATOM   1655 N N   . HIS A 1 235 ? 37.466  42.394 26.578  1.00 68.96  ?  390 HIS A N   1 
ATOM   1656 C CA  . HIS A 1 235 ? 37.750  43.745 27.059  1.00 68.62  ?  390 HIS A CA  1 
ATOM   1657 C C   . HIS A 1 235 ? 37.107  44.042 28.418  1.00 68.14  ?  390 HIS A C   1 
ATOM   1658 O O   . HIS A 1 235 ? 36.797  45.198 28.709  1.00 69.54  ?  390 HIS A O   1 
ATOM   1659 C CB  . HIS A 1 235 ? 37.315  44.758 25.990  1.00 70.33  ?  390 HIS A CB  1 
ATOM   1660 C CG  . HIS A 1 235 ? 37.982  44.546 24.659  1.00 75.00  ?  390 HIS A CG  1 
ATOM   1661 N ND1 . HIS A 1 235 ? 39.355  44.314 24.555  1.00 77.42  ?  390 HIS A ND1 1 
ATOM   1662 C CD2 . HIS A 1 235 ? 37.446  44.556 23.415  1.00 77.55  ?  390 HIS A CD2 1 
ATOM   1663 C CE1 . HIS A 1 235 ? 39.600  44.188 23.257  1.00 77.15  ?  390 HIS A CE1 1 
ATOM   1664 N NE2 . HIS A 1 235 ? 38.486  44.338 22.530  1.00 77.50  ?  390 HIS A NE2 1 
ATOM   1665 N N   . ARG A 1 236 ? 36.926  43.010 29.256  1.00 58.77  ?  391 ARG A N   1 
ATOM   1666 C CA  . ARG A 1 236 ? 36.287  43.176 30.557  1.00 56.63  ?  391 ARG A CA  1 
ATOM   1667 C C   . ARG A 1 236 ? 37.067  42.478 31.652  1.00 60.07  ?  391 ARG A C   1 
ATOM   1668 O O   . ARG A 1 236 ? 37.689  41.446 31.414  1.00 60.09  ?  391 ARG A O   1 
ATOM   1669 C CB  . ARG A 1 236 ? 34.834  42.658 30.500  1.00 52.59  ?  391 ARG A CB  1 
ATOM   1670 C CG  . ARG A 1 236 ? 34.026  42.744 31.798  1.00 50.19  ?  391 ARG A CG  1 
ATOM   1671 C CD  . ARG A 1 236 ? 32.672  42.063 31.693  1.00 58.52  ?  391 ARG A CD  1 
ATOM   1672 N NE  . ARG A 1 236 ? 32.774  40.604 31.593  1.00 58.52  ?  391 ARG A NE  1 
ATOM   1673 C CZ  . ARG A 1 236 ? 31.913  39.827 30.932  1.00 69.76  ?  391 ARG A CZ  1 
ATOM   1674 N NH1 . ARG A 1 236 ? 30.871  40.362 30.298  1.00 50.99  ?  391 ARG A NH1 1 
ATOM   1675 N NH2 . ARG A 1 236 ? 32.098  38.514 30.883  1.00 56.30  1  391 ARG A NH2 1 
ATOM   1676 N N   . GLU A 1 237 ? 37.035  43.058 32.853  1.00 55.92  ?  392 GLU A N   1 
ATOM   1677 C CA  . GLU A 1 237 ? 37.675  42.523 34.036  1.00 55.69  ?  392 GLU A CA  1 
ATOM   1678 C C   . GLU A 1 237 ? 36.566  42.235 35.032  1.00 60.15  ?  392 GLU A C   1 
ATOM   1679 O O   . GLU A 1 237 ? 35.948  43.178 35.547  1.00 60.94  ?  392 GLU A O   1 
ATOM   1680 C CB  . GLU A 1 237 ? 38.712  43.514 34.605  1.00 57.35  ?  392 GLU A CB  1 
ATOM   1681 N N   . PRO A 1 238 ? 36.240  40.948 35.284  1.00 56.52  ?  393 PRO A N   1 
ATOM   1682 C CA  . PRO A 1 238 ? 36.842  39.747 34.711  1.00 56.17  ?  393 PRO A CA  1 
ATOM   1683 C C   . PRO A 1 238 ? 36.213  39.369 33.381  1.00 60.99  ?  393 PRO A C   1 
ATOM   1684 O O   . PRO A 1 238 ? 35.003  39.531 33.187  1.00 61.90  ?  393 PRO A O   1 
ATOM   1685 C CB  . PRO A 1 238 ? 36.610  38.702 35.797  1.00 57.97  ?  393 PRO A CB  1 
ATOM   1686 C CG  . PRO A 1 238 ? 35.353  39.128 36.490  1.00 62.52  ?  393 PRO A CG  1 
ATOM   1687 C CD  . PRO A 1 238 ? 35.161  40.601 36.232  1.00 58.25  ?  393 PRO A CD  1 
ATOM   1688 N N   . GLN A 1 239 ? 37.056  38.890 32.458  1.00 56.49  ?  394 GLN A N   1 
ATOM   1689 C CA  . GLN A 1 239 ? 36.681  38.464 31.111  1.00 55.19  ?  394 GLN A CA  1 
ATOM   1690 C C   . GLN A 1 239 ? 35.552  37.428 31.107  1.00 56.20  ?  394 GLN A C   1 
ATOM   1691 O O   . GLN A 1 239 ? 34.649  37.517 30.280  1.00 54.81  ?  394 GLN A O   1 
ATOM   1692 C CB  . GLN A 1 239 ? 37.921  37.922 30.389  1.00 56.53  ?  394 GLN A CB  1 
ATOM   1693 N N   . LEU A 1 240 ? 35.584  36.485 32.070  1.00 52.41  ?  395 LEU A N   1 
ATOM   1694 C CA  . LEU A 1 240 ? 34.604  35.405 32.199  1.00 51.56  ?  395 LEU A CA  1 
ATOM   1695 C C   . LEU A 1 240 ? 33.586  35.714 33.285  1.00 54.54  ?  395 LEU A C   1 
ATOM   1696 O O   . LEU A 1 240 ? 33.966  36.045 34.411  1.00 54.59  ?  395 LEU A O   1 
ATOM   1697 C CB  . LEU A 1 240 ? 35.305  34.041 32.462  1.00 51.22  ?  395 LEU A CB  1 
ATOM   1698 C CG  . LEU A 1 240 ? 35.645  33.108 31.271  1.00 55.68  ?  395 LEU A CG  1 
ATOM   1699 C CD1 . LEU A 1 240 ? 34.406  32.614 30.584  1.00 57.13  ?  395 LEU A CD1 1 
ATOM   1700 C CD2 . LEU A 1 240 ? 36.560  33.744 30.260  1.00 56.60  ?  395 LEU A CD2 1 
ATOM   1701 N N   . LEU A 1 241 ? 32.285  35.615 32.934  1.00 49.77  ?  396 LEU A N   1 
ATOM   1702 C CA  . LEU A 1 241 ? 31.151  35.879 33.827  1.00 49.74  ?  396 LEU A CA  1 
ATOM   1703 C C   . LEU A 1 241 ? 31.114  34.880 34.987  1.00 55.63  ?  396 LEU A C   1 
ATOM   1704 O O   . LEU A 1 241 ? 30.687  35.223 36.088  1.00 53.59  ?  396 LEU A O   1 
ATOM   1705 C CB  . LEU A 1 241 ? 29.849  35.854 33.015  1.00 49.85  ?  396 LEU A CB  1 
ATOM   1706 C CG  . LEU A 1 241 ? 28.556  36.341 33.672  1.00 53.50  ?  396 LEU A CG  1 
ATOM   1707 C CD1 . LEU A 1 241 ? 28.624  37.830 34.032  1.00 52.57  ?  396 LEU A CD1 1 
ATOM   1708 C CD2 . LEU A 1 241 ? 27.394  36.090 32.752  1.00 54.73  ?  396 LEU A CD2 1 
ATOM   1709 N N   . LEU A 1 242 ? 31.606  33.652 34.736  1.00 55.64  ?  397 LEU A N   1 
ATOM   1710 C CA  . LEU A 1 242 ? 31.773  32.589 35.722  1.00 55.84  ?  397 LEU A CA  1 
ATOM   1711 C C   . LEU A 1 242 ? 32.637  33.079 36.922  1.00 62.34  ?  397 LEU A C   1 
ATOM   1712 O O   . LEU A 1 242 ? 32.346  32.692 38.058  1.00 62.62  ?  397 LEU A O   1 
ATOM   1713 C CB  . LEU A 1 242 ? 32.443  31.380 35.041  1.00 55.11  ?  397 LEU A CB  1 
ATOM   1714 C CG  . LEU A 1 242 ? 31.644  30.100 34.867  1.00 58.20  ?  397 LEU A CG  1 
ATOM   1715 C CD1 . LEU A 1 242 ? 30.190  30.304 35.134  1.00 57.24  ?  397 LEU A CD1 1 
ATOM   1716 C CD2 . LEU A 1 242 ? 31.882  29.493 33.486  1.00 59.96  ?  397 LEU A CD2 1 
ATOM   1717 N N   . ASP A 1 243 ? 33.651  33.953 36.669  1.00 59.89  ?  398 ASP A N   1 
ATOM   1718 C CA  . ASP A 1 243 ? 34.518  34.528 37.705  1.00 62.13  ?  398 ASP A CA  1 
ATOM   1719 C C   . ASP A 1 243 ? 33.757  35.407 38.704  1.00 70.32  ?  398 ASP A C   1 
ATOM   1720 O O   . ASP A 1 243 ? 34.137  35.462 39.876  1.00 71.54  ?  398 ASP A O   1 
ATOM   1721 C CB  . ASP A 1 243 ? 35.705  35.302 37.106  1.00 64.37  ?  398 ASP A CB  1 
ATOM   1722 C CG  . ASP A 1 243 ? 36.681  34.479 36.264  1.00 78.89  ?  398 ASP A CG  1 
ATOM   1723 O OD1 . ASP A 1 243 ? 36.755  33.236 36.468  1.00 79.31  ?  398 ASP A OD1 1 
ATOM   1724 O OD2 . ASP A 1 243 ? 37.395  35.081 35.424  1.00 84.67  -1 398 ASP A OD2 1 
ATOM   1725 N N   . ILE A 1 244 ? 32.682  36.079 38.239  1.00 67.60  ?  399 ILE A N   1 
ATOM   1726 C CA  . ILE A 1 244 ? 31.784  36.919 39.038  1.00 67.47  ?  399 ILE A CA  1 
ATOM   1727 C C   . ILE A 1 244 ? 31.085  36.061 40.124  1.00 72.73  ?  399 ILE A C   1 
ATOM   1728 O O   . ILE A 1 244 ? 30.941  36.532 41.247  1.00 72.90  ?  399 ILE A O   1 
ATOM   1729 C CB  . ILE A 1 244 ? 30.827  37.744 38.113  1.00 69.99  ?  399 ILE A CB  1 
ATOM   1730 C CG1 . ILE A 1 244 ? 31.534  38.991 37.560  1.00 69.75  ?  399 ILE A CG1 1 
ATOM   1731 C CG2 . ILE A 1 244 ? 29.477  38.107 38.751  1.00 70.43  ?  399 ILE A CG2 1 
ATOM   1732 C CD1 . ILE A 1 244 ? 31.699  38.976 36.094  1.00 76.20  ?  399 ILE A CD1 1 
ATOM   1733 N N   . LYS A 1 245 ? 30.722  34.796 39.825  1.00 70.11  ?  400 LYS A N   1 
ATOM   1734 C CA  . LYS A 1 245 ? 30.130  33.903 40.841  1.00 70.14  ?  400 LYS A CA  1 
ATOM   1735 C C   . LYS A 1 245 ? 31.168  33.595 41.958  1.00 73.49  ?  400 LYS A C   1 
ATOM   1736 O O   . LYS A 1 245 ? 30.805  33.566 43.137  1.00 72.97  ?  400 LYS A O   1 
ATOM   1737 C CB  . LYS A 1 245 ? 29.573  32.607 40.214  1.00 72.04  ?  400 LYS A CB  1 
ATOM   1738 N N   . GLU A 1 246 ? 32.465  33.428 41.589  1.00 68.70  ?  401 GLU A N   1 
ATOM   1739 C CA  . GLU A 1 246 ? 33.524  33.184 42.568  1.00 68.05  ?  401 GLU A CA  1 
ATOM   1740 C C   . GLU A 1 246 ? 33.621  34.373 43.541  1.00 71.57  ?  401 GLU A C   1 
ATOM   1741 O O   . GLU A 1 246 ? 33.614  34.155 44.752  1.00 70.87  ?  401 GLU A O   1 
ATOM   1742 C CB  . GLU A 1 246 ? 34.861  32.902 41.878  1.00 69.15  ?  401 GLU A CB  1 
ATOM   1743 N N   . GLU A 1 247 ? 33.601  35.625 42.997  1.00 67.06  ?  402 GLU A N   1 
ATOM   1744 C CA  . GLU A 1 247 ? 33.632  36.885 43.743  1.00 66.63  ?  402 GLU A CA  1 
ATOM   1745 C C   . GLU A 1 247 ? 32.455  36.996 44.736  1.00 72.19  ?  402 GLU A C   1 
ATOM   1746 O O   . GLU A 1 247 ? 32.648  37.450 45.867  1.00 71.35  ?  402 GLU A O   1 
ATOM   1747 C CB  . GLU A 1 247 ? 33.634  38.079 42.781  1.00 67.71  ?  402 GLU A CB  1 
ATOM   1748 C CG  . GLU A 1 247 ? 34.933  38.250 42.024  1.00 78.31  ?  402 GLU A CG  1 
ATOM   1749 C CD  . GLU A 1 247 ? 35.011  39.471 41.128  1.00 110.17 ?  402 GLU A CD  1 
ATOM   1750 O OE1 . GLU A 1 247 ? 34.862  40.607 41.634  1.00 105.01 ?  402 GLU A OE1 1 
ATOM   1751 O OE2 . GLU A 1 247 ? 35.282  39.290 39.922  1.00 114.01 -1 402 GLU A OE2 1 
ATOM   1752 N N   . ILE A 1 248 ? 31.248  36.561 44.309  1.00 70.12  ?  403 ILE A N   1 
ATOM   1753 C CA  . ILE A 1 248 ? 30.041  36.576 45.133  1.00 71.03  ?  403 ILE A CA  1 
ATOM   1754 C C   . ILE A 1 248 ? 30.158  35.501 46.201  1.00 79.18  ?  403 ILE A C   1 
ATOM   1755 O O   . ILE A 1 248 ? 29.937  35.806 47.379  1.00 79.72  ?  403 ILE A O   1 
ATOM   1756 C CB  . ILE A 1 248 ? 28.728  36.464 44.301  1.00 74.22  ?  403 ILE A CB  1 
ATOM   1757 C CG1 . ILE A 1 248 ? 28.572  37.666 43.325  1.00 74.92  ?  403 ILE A CG1 1 
ATOM   1758 C CG2 . ILE A 1 248 ? 27.487  36.333 45.215  1.00 74.41  ?  403 ILE A CG2 1 
ATOM   1759 C CD1 . ILE A 1 248 ? 27.636  37.432 42.107  1.00 82.01  ?  403 ILE A CD1 1 
ATOM   1760 N N   . GLU A 1 249 ? 30.521  34.252 45.794  1.00 77.96  ?  404 GLU A N   1 
ATOM   1761 C CA  . GLU A 1 249 ? 30.694  33.102 46.694  1.00 78.72  ?  404 GLU A CA  1 
ATOM   1762 C C   . GLU A 1 249 ? 31.741  33.394 47.778  1.00 83.22  ?  404 GLU A C   1 
ATOM   1763 O O   . GLU A 1 249 ? 31.514  33.070 48.947  1.00 83.70  ?  404 GLU A O   1 
ATOM   1764 C CB  . GLU A 1 249 ? 31.038  31.803 45.924  1.00 80.39  ?  404 GLU A CB  1 
ATOM   1765 C CG  . GLU A 1 249 ? 29.941  31.255 45.009  1.00 94.52  ?  404 GLU A CG  1 
ATOM   1766 C CD  . GLU A 1 249 ? 28.571  30.980 45.615  1.00 123.85 ?  404 GLU A CD  1 
ATOM   1767 O OE1 . GLU A 1 249 ? 28.489  30.165 46.563  1.00 128.34 ?  404 GLU A OE1 1 
ATOM   1768 O OE2 . GLU A 1 249 ? 27.575  31.560 45.122  1.00 111.52 -1 404 GLU A OE2 1 
ATOM   1769 N N   . ASP A 1 250 ? 32.844  34.072 47.402  1.00 79.23  ?  405 ASP A N   1 
ATOM   1770 C CA  . ASP A 1 250 ? 33.911  34.446 48.331  1.00 79.31  ?  405 ASP A CA  1 
ATOM   1771 C C   . ASP A 1 250 ? 33.604  35.780 49.035  1.00 84.30  ?  405 ASP A C   1 
ATOM   1772 O O   . ASP A 1 250 ? 34.532  36.503 49.401  1.00 84.91  ?  405 ASP A O   1 
ATOM   1773 C CB  . ASP A 1 250 ? 35.291  34.477 47.624  1.00 81.05  ?  405 ASP A CB  1 
ATOM   1774 C CG  . ASP A 1 250 ? 35.716  33.166 46.981  1.00 91.64  ?  405 ASP A CG  1 
ATOM   1775 O OD1 . ASP A 1 250 ? 35.477  32.092 47.595  1.00 89.78  ?  405 ASP A OD1 1 
ATOM   1776 O OD2 . ASP A 1 250 ? 36.302  33.211 45.867  1.00 101.30 -1 405 ASP A OD2 1 
ATOM   1777 N N   . GLU A 1 251 ? 32.292  36.105 49.212  1.00 80.31  ?  406 GLU A N   1 
ATOM   1778 C CA  . GLU A 1 251 ? 31.739  37.311 49.865  1.00 79.43  ?  406 GLU A CA  1 
ATOM   1779 C C   . GLU A 1 251 ? 32.389  38.680 49.514  1.00 81.60  ?  406 GLU A C   1 
ATOM   1780 O O   . GLU A 1 251 ? 32.052  39.688 50.135  1.00 82.02  ?  406 GLU A O   1 
ATOM   1781 C CB  . GLU A 1 251 ? 31.584  37.102 51.388  1.00 80.77  ?  406 GLU A CB  1 
ATOM   1782 N N   . GLU A 1 252 ? 33.279  38.715 48.495  1.00 76.42  ?  407 GLU A N   1 
ATOM   1783 C CA  . GLU A 1 252 ? 33.968  39.920 48.026  1.00 75.83  ?  407 GLU A CA  1 
ATOM   1784 C C   . GLU A 1 252 ? 33.004  40.916 47.328  1.00 80.07  ?  407 GLU A C   1 
ATOM   1785 O O   . GLU A 1 252 ? 33.315  42.115 47.258  1.00 80.85  ?  407 GLU A O   1 
ATOM   1786 C CB  . GLU A 1 252 ? 35.141  39.545 47.106  1.00 76.94  ?  407 GLU A CB  1 
ATOM   1787 N N   . LYS A 1 253 ? 31.843  40.411 46.812  1.00 73.74  ?  408 LYS A N   1 
ATOM   1788 C CA  . LYS A 1 253 ? 30.776  41.161 46.123  1.00 71.64  ?  408 LYS A CA  1 
ATOM   1789 C C   . LYS A 1 253 ? 29.420  40.453 46.356  1.00 72.71  ?  408 LYS A C   1 
ATOM   1790 O O   . LYS A 1 253 ? 29.389  39.338 46.891  1.00 73.48  ?  408 LYS A O   1 
ATOM   1791 C CB  . LYS A 1 253 ? 31.050  41.210 44.597  1.00 73.80  ?  408 LYS A CB  1 
ATOM   1792 C CG  . LYS A 1 253 ? 32.344  41.898 44.143  1.00 83.21  ?  408 LYS A CG  1 
ATOM   1793 C CD  . LYS A 1 253 ? 32.208  43.422 44.009  1.00 92.28  ?  408 LYS A CD  1 
ATOM   1794 C CE  . LYS A 1 253 ? 33.537  44.120 43.804  1.00 102.11 ?  408 LYS A CE  1 
ATOM   1795 N NZ  . LYS A 1 253 ? 34.111  43.893 42.447  1.00 105.85 1  408 LYS A NZ  1 
ATOM   1796 N N   . THR A 1 254 ? 28.304  41.098 45.956  1.00 66.08  ?  409 THR A N   1 
ATOM   1797 C CA  . THR A 1 254 ? 26.947  40.518 46.017  1.00 64.76  ?  409 THR A CA  1 
ATOM   1798 C C   . THR A 1 254 ? 26.320  40.527 44.621  1.00 65.73  ?  409 THR A C   1 
ATOM   1799 O O   . THR A 1 254 ? 26.825  41.211 43.715  1.00 65.09  ?  409 THR A O   1 
ATOM   1800 C CB  . THR A 1 254 ? 26.019  41.230 47.025  1.00 71.81  ?  409 THR A CB  1 
ATOM   1801 O OG1 . THR A 1 254 ? 26.071  42.649 46.839  1.00 72.90  ?  409 THR A OG1 1 
ATOM   1802 C CG2 . THR A 1 254 ? 26.300  40.844 48.463  1.00 68.12  ?  409 THR A CG2 1 
ATOM   1803 N N   . ILE A 1 255 ? 25.216  39.774 44.440  1.00 60.04  ?  410 ILE A N   1 
ATOM   1804 C CA  . ILE A 1 255 ? 24.506  39.753 43.159  1.00 58.74  ?  410 ILE A CA  1 
ATOM   1805 C C   . ILE A 1 255 ? 23.937  41.140 42.827  1.00 62.44  ?  410 ILE A C   1 
ATOM   1806 O O   . ILE A 1 255 ? 23.921  41.531 41.661  1.00 61.09  ?  410 ILE A O   1 
ATOM   1807 C CB  . ILE A 1 255 ? 23.500  38.572 43.013  1.00 61.04  ?  410 ILE A CB  1 
ATOM   1808 C CG1 . ILE A 1 255 ? 23.068  38.350 41.538  1.00 61.13  ?  410 ILE A CG1 1 
ATOM   1809 C CG2 . ILE A 1 255 ? 22.309  38.693 43.951  1.00 60.64  ?  410 ILE A CG2 1 
ATOM   1810 C CD1 . ILE A 1 255 ? 24.250  38.259 40.464  1.00 63.76  ?  410 ILE A CD1 1 
ATOM   1811 N N   . GLU A 1 256 ? 23.583  41.912 43.880  1.00 60.42  ?  411 GLU A N   1 
ATOM   1812 C CA  . GLU A 1 256 ? 23.060  43.285 43.812  1.00 60.72  ?  411 GLU A CA  1 
ATOM   1813 C C   . GLU A 1 256 ? 24.028  44.223 43.110  1.00 65.07  ?  411 GLU A C   1 
ATOM   1814 O O   . GLU A 1 256 ? 23.603  45.114 42.363  1.00 66.11  ?  411 GLU A O   1 
ATOM   1815 C CB  . GLU A 1 256 ? 22.706  43.811 45.213  1.00 61.99  ?  411 GLU A CB  1 
ATOM   1816 C CG  . GLU A 1 256 ? 21.375  43.297 45.746  1.00 75.17  ?  411 GLU A CG  1 
ATOM   1817 C CD  . GLU A 1 256 ? 21.286  41.832 46.144  1.00 97.48  ?  411 GLU A CD  1 
ATOM   1818 O OE1 . GLU A 1 256 ? 22.233  41.320 46.784  1.00 86.61  ?  411 GLU A OE1 1 
ATOM   1819 O OE2 . GLU A 1 256 ? 20.250  41.203 45.833  1.00 98.86  -1 411 GLU A OE2 1 
ATOM   1820 N N   . ASP A 1 257 ? 25.328  43.989 43.302  1.00 60.07  ?  412 ASP A N   1 
ATOM   1821 C CA  . ASP A 1 257 ? 26.364  44.785 42.661  1.00 60.14  ?  412 ASP A CA  1 
ATOM   1822 C C   . ASP A 1 257 ? 26.403  44.510 41.155  1.00 60.68  ?  412 ASP A C   1 
ATOM   1823 O O   . ASP A 1 257 ? 26.930  45.327 40.401  1.00 59.33  ?  412 ASP A O   1 
ATOM   1824 C CB  . ASP A 1 257 ? 27.744  44.487 43.297  1.00 63.46  ?  412 ASP A CB  1 
ATOM   1825 C CG  . ASP A 1 257 ? 27.829  44.744 44.799  1.00 82.39  ?  412 ASP A CG  1 
ATOM   1826 O OD1 . ASP A 1 257 ? 27.598  45.904 45.220  1.00 83.68  ?  412 ASP A OD1 1 
ATOM   1827 O OD2 . ASP A 1 257 ? 28.165  43.795 45.548  1.00 91.20  -1 412 ASP A OD2 1 
ATOM   1828 N N   . TYR A 1 258 ? 25.846  43.358 40.719  1.00 56.04  ?  413 TYR A N   1 
ATOM   1829 C CA  . TYR A 1 258 ? 25.862  42.928 39.317  1.00 54.38  ?  413 TYR A CA  1 
ATOM   1830 C C   . TYR A 1 258 ? 24.546  42.970 38.547  1.00 53.20  ?  413 TYR A C   1 
ATOM   1831 O O   . TYR A 1 258 ? 24.578  42.804 37.325  1.00 53.22  ?  413 TYR A O   1 
ATOM   1832 C CB  . TYR A 1 258 ? 26.593  41.589 39.153  1.00 56.05  ?  413 TYR A CB  1 
ATOM   1833 C CG  . TYR A 1 258 ? 28.088  41.713 39.350  1.00 58.96  ?  413 TYR A CG  1 
ATOM   1834 C CD1 . TYR A 1 258 ? 28.903  42.231 38.346  1.00 61.20  ?  413 TYR A CD1 1 
ATOM   1835 C CD2 . TYR A 1 258 ? 28.693  41.331 40.550  1.00 59.87  ?  413 TYR A CD2 1 
ATOM   1836 C CE1 . TYR A 1 258 ? 30.285  42.359 38.525  1.00 62.19  ?  413 TYR A CE1 1 
ATOM   1837 C CE2 . TYR A 1 258 ? 30.073  41.450 40.740  1.00 60.81  ?  413 TYR A CE2 1 
ATOM   1838 C CZ  . TYR A 1 258 ? 30.866  41.965 39.725  1.00 70.09  ?  413 TYR A CZ  1 
ATOM   1839 O OH  . TYR A 1 258 ? 32.228  42.091 39.908  1.00 72.57  ?  413 TYR A OH  1 
ATOM   1840 N N   . ILE A 1 259 ? 23.409  43.252 39.230  1.00 46.04  ?  414 ILE A N   1 
ATOM   1841 C CA  . ILE A 1 259 ? 22.090  43.362 38.584  1.00 44.16  ?  414 ILE A CA  1 
ATOM   1842 C C   . ILE A 1 259 ? 22.179  44.372 37.445  1.00 46.83  ?  414 ILE A C   1 
ATOM   1843 O O   . ILE A 1 259 ? 22.690  45.480 37.641  1.00 48.96  ?  414 ILE A O   1 
ATOM   1844 C CB  . ILE A 1 259 ? 20.927  43.709 39.560  1.00 46.25  ?  414 ILE A CB  1 
ATOM   1845 C CG1 . ILE A 1 259 ? 20.844  42.740 40.752  1.00 46.92  ?  414 ILE A CG1 1 
ATOM   1846 C CG2 . ILE A 1 259 ? 19.577  43.790 38.821  1.00 44.16  ?  414 ILE A CG2 1 
ATOM   1847 C CD1 . ILE A 1 259 ? 19.839  43.241 41.943  1.00 59.06  ?  414 ILE A CD1 1 
ATOM   1848 N N   . ASP A 1 260 ? 21.735  43.962 36.248  1.00 39.89  ?  415 ASP A N   1 
ATOM   1849 C CA  . ASP A 1 260 ? 21.708  44.788 35.049  1.00 38.49  ?  415 ASP A CA  1 
ATOM   1850 C C   . ASP A 1 260 ? 21.034  46.140 35.360  1.00 44.26  ?  415 ASP A C   1 
ATOM   1851 O O   . ASP A 1 260 ? 19.854  46.166 35.756  1.00 43.55  ?  415 ASP A O   1 
ATOM   1852 C CB  . ASP A 1 260 ? 20.917  44.055 33.958  1.00 38.75  ?  415 ASP A CB  1 
ATOM   1853 C CG  . ASP A 1 260 ? 21.009  44.633 32.572  1.00 40.93  ?  415 ASP A CG  1 
ATOM   1854 O OD1 . ASP A 1 260 ? 21.599  45.735 32.415  1.00 41.01  ?  415 ASP A OD1 1 
ATOM   1855 O OD2 . ASP A 1 260 ? 20.490  44.000 31.640  1.00 47.46  -1 415 ASP A OD2 1 
ATOM   1856 N N   . LYS A 1 261 ? 21.793  47.258 35.209  1.00 40.65  ?  416 LYS A N   1 
ATOM   1857 C CA  . LYS A 1 261 ? 21.257  48.609 35.459  1.00 39.17  ?  416 LYS A CA  1 
ATOM   1858 C C   . LYS A 1 261 ? 20.211  49.061 34.403  1.00 42.91  ?  416 LYS A C   1 
ATOM   1859 O O   . LYS A 1 261 ? 19.449  50.002 34.668  1.00 42.80  ?  416 LYS A O   1 
ATOM   1860 C CB  . LYS A 1 261 ? 22.377  49.631 35.650  1.00 41.01  ?  416 LYS A CB  1 
ATOM   1861 C CG  . LYS A 1 261 ? 23.086  49.498 36.987  1.00 55.63  ?  416 LYS A CG  1 
ATOM   1862 C CD  . LYS A 1 261 ? 24.268  50.474 37.118  1.00 60.64  ?  416 LYS A CD  1 
ATOM   1863 C CE  . LYS A 1 261 ? 25.513  49.833 37.726  1.00 74.60  ?  416 LYS A CE  1 
ATOM   1864 N NZ  . LYS A 1 261 ? 25.323  49.408 39.141  1.00 84.56  1  416 LYS A NZ  1 
ATOM   1865 N N   . LYS A 1 262 ? 20.126  48.332 33.241  1.00 38.73  ?  417 LYS A N   1 
ATOM   1866 C CA  . LYS A 1 262 ? 19.181  48.591 32.140  1.00 37.44  ?  417 LYS A CA  1 
ATOM   1867 C C   . LYS A 1 262 ? 17.749  48.115 32.445  1.00 44.86  ?  417 LYS A C   1 
ATOM   1868 O O   . LYS A 1 262 ? 16.916  48.017 31.549  1.00 44.26  ?  417 LYS A O   1 
ATOM   1869 C CB  . LYS A 1 262 ? 19.700  48.066 30.787  1.00 37.31  ?  417 LYS A CB  1 
ATOM   1870 C CG  . LYS A 1 262 ? 21.095  48.583 30.400  1.00 46.45  ?  417 LYS A CG  1 
ATOM   1871 C CD  . LYS A 1 262 ? 21.578  48.172 28.999  1.00 46.20  ?  417 LYS A CD  1 
ATOM   1872 C CE  . LYS A 1 262 ? 21.862  46.689 28.808  1.00 62.81  ?  417 LYS A CE  1 
ATOM   1873 N NZ  . LYS A 1 262 ? 22.909  46.143 29.724  1.00 66.13  1  417 LYS A NZ  1 
ATOM   1874 N N   . MET A 1 263 ? 17.449  47.805 33.700  1.00 44.53  ?  418 MET A N   1 
ATOM   1875 C CA  . MET A 1 263 ? 16.072  47.469 34.071  1.00 45.02  ?  418 MET A CA  1 
ATOM   1876 C C   . MET A 1 263 ? 15.654  48.245 35.310  1.00 54.74  ?  418 MET A C   1 
ATOM   1877 O O   . MET A 1 263 ? 16.533  48.797 35.978  1.00 53.84  ?  418 MET A O   1 
ATOM   1878 C CB  . MET A 1 263 ? 15.761  45.964 34.102  1.00 45.99  ?  418 MET A CB  1 
ATOM   1879 C CG  . MET A 1 263 ? 16.819  45.125 34.684  1.00 47.78  ?  418 MET A CG  1 
ATOM   1880 S SD  . MET A 1 263 ? 16.338  43.391 34.758  1.00 50.40  ?  418 MET A SD  1 
ATOM   1881 C CE  . MET A 1 263 ? 17.654  42.801 35.685  1.00 47.25  ?  418 MET A CE  1 
ATOM   1882 N N   . ASN A 1 264 ? 14.326  48.410 35.541  1.00 56.55  ?  419 ASN A N   1 
ATOM   1883 C CA  . ASN A 1 264 ? 13.803  49.173 36.696  1.00 58.13  ?  419 ASN A CA  1 
ATOM   1884 C C   . ASN A 1 264 ? 12.866  48.366 37.613  1.00 65.38  ?  419 ASN A C   1 
ATOM   1885 O O   . ASN A 1 264 ? 12.651  48.752 38.764  1.00 64.69  ?  419 ASN A O   1 
ATOM   1886 C CB  . ASN A 1 264 ? 13.125  50.468 36.235  1.00 58.63  ?  419 ASN A CB  1 
ATOM   1887 C CG  . ASN A 1 264 ? 11.895  50.241 35.396  1.00 83.71  ?  419 ASN A CG  1 
ATOM   1888 O OD1 . ASN A 1 264 ? 10.886  49.699 35.858  1.00 77.55  ?  419 ASN A OD1 1 
ATOM   1889 N ND2 . ASN A 1 264 ? 11.936  50.682 34.151  1.00 78.39  ?  419 ASN A ND2 1 
ATOM   1890 N N   . ASP A 1 265 ? 12.313  47.252 37.081  1.00 65.18  ?  420 ASP A N   1 
ATOM   1891 C CA  . ASP A 1 265 ? 11.351  46.330 37.716  1.00 65.82  ?  420 ASP A CA  1 
ATOM   1892 C C   . ASP A 1 265 ? 11.974  45.068 38.339  1.00 73.45  ?  420 ASP A C   1 
ATOM   1893 O O   . ASP A 1 265 ? 11.242  44.092 38.544  1.00 74.51  ?  420 ASP A O   1 
ATOM   1894 C CB  . ASP A 1 265 ? 10.308  45.893 36.666  1.00 66.94  ?  420 ASP A CB  1 
ATOM   1895 C CG  . ASP A 1 265 ? 10.855  45.004 35.554  1.00 70.58  ?  420 ASP A CG  1 
ATOM   1896 O OD1 . ASP A 1 265 ? 12.001  45.261 35.081  1.00 67.12  ?  420 ASP A OD1 1 
ATOM   1897 O OD2 . ASP A 1 265 ? 10.147  44.051 35.158  1.00 78.23  -1 420 ASP A OD2 1 
ATOM   1898 N N   . ALA A 1 266 ? 13.300  45.058 38.592  1.00 70.20  ?  421 ALA A N   1 
ATOM   1899 C CA  . ALA A 1 266 ? 13.970  43.894 39.148  1.00 70.08  ?  421 ALA A CA  1 
ATOM   1900 C C   . ALA A 1 266 ? 13.946  44.006 40.658  1.00 74.87  ?  421 ALA A C   1 
ATOM   1901 O O   . ALA A 1 266 ? 14.556  44.928 41.203  1.00 75.02  ?  421 ALA A O   1 
ATOM   1902 C CB  . ALA A 1 266 ? 15.404  43.804 38.622  1.00 70.71  ?  421 ALA A CB  1 
ATOM   1903 N N   . ASP A 1 267 ? 13.170  43.128 41.328  1.00 70.73  ?  422 ASP A N   1 
ATOM   1904 C CA  . ASP A 1 267 ? 13.097  43.111 42.785  1.00 70.07  ?  422 ASP A CA  1 
ATOM   1905 C C   . ASP A 1 267 ? 14.040  42.055 43.322  1.00 71.93  ?  422 ASP A C   1 
ATOM   1906 O O   . ASP A 1 267 ? 14.041  40.924 42.843  1.00 71.36  ?  422 ASP A O   1 
ATOM   1907 C CB  . ASP A 1 267 ? 11.661  42.927 43.298  1.00 72.34  ?  422 ASP A CB  1 
ATOM   1908 C CG  . ASP A 1 267 ? 11.024  41.624 42.896  1.00 86.49  ?  422 ASP A CG  1 
ATOM   1909 O OD1 . ASP A 1 267 ? 10.755  40.797 43.794  1.00 87.30  ?  422 ASP A OD1 1 
ATOM   1910 O OD2 . ASP A 1 267 ? 10.833  41.409 41.676  1.00 94.05  -1 422 ASP A OD2 1 
ATOM   1911 N N   . SER A 1 268 ? 14.871  42.454 44.297  1.00 68.08  ?  423 SER A N   1 
ATOM   1912 C CA  . SER A 1 268 ? 15.923  41.674 44.963  1.00 67.31  ?  423 SER A CA  1 
ATOM   1913 C C   . SER A 1 268 ? 15.559  40.242 45.376  1.00 69.10  ?  423 SER A C   1 
ATOM   1914 O O   . SER A 1 268 ? 16.397  39.346 45.242  1.00 68.39  ?  423 SER A O   1 
ATOM   1915 C CB  . SER A 1 268 ? 16.493  42.456 46.138  1.00 71.19  ?  423 SER A CB  1 
ATOM   1916 O OG  . SER A 1 268 ? 17.082  43.664 45.683  1.00 82.24  ?  423 SER A OG  1 
ATOM   1917 N N   . THR A 1 269 ? 14.322  40.025 45.861  1.00 64.02  ?  424 THR A N   1 
ATOM   1918 C CA  . THR A 1 269 ? 13.858  38.693 46.251  1.00 63.17  ?  424 THR A CA  1 
ATOM   1919 C C   . THR A 1 269 ? 13.897  37.746 45.053  1.00 65.53  ?  424 THR A C   1 
ATOM   1920 O O   . THR A 1 269 ? 14.560  36.718 45.141  1.00 65.32  ?  424 THR A O   1 
ATOM   1921 C CB  . THR A 1 269 ? 12.486  38.736 46.966  1.00 69.40  ?  424 THR A CB  1 
ATOM   1922 O OG1 . THR A 1 269 ? 12.489  39.763 47.966  1.00 74.23  ?  424 THR A OG1 1 
ATOM   1923 C CG2 . THR A 1 269 ? 12.125  37.407 47.597  1.00 59.98  ?  424 THR A CG2 1 
ATOM   1924 N N   . SER A 1 270 ? 13.230  38.109 43.924  1.00 61.12  ?  425 SER A N   1 
ATOM   1925 C CA  . SER A 1 270 ? 13.212  37.295 42.690  1.00 59.81  ?  425 SER A CA  1 
ATOM   1926 C C   . SER A 1 270 ? 14.578  37.255 42.036  1.00 60.07  ?  425 SER A C   1 
ATOM   1927 O O   . SER A 1 270 ? 14.914  36.238 41.422  1.00 59.90  ?  425 SER A O   1 
ATOM   1928 C CB  . SER A 1 270 ? 12.186  37.817 41.693  1.00 62.32  ?  425 SER A CB  1 
ATOM   1929 O OG  . SER A 1 270 ? 12.460  39.172 41.391  1.00 70.23  ?  425 SER A OG  1 
ATOM   1930 N N   . VAL A 1 271 ? 15.369  38.347 42.173  1.00 52.89  ?  426 VAL A N   1 
ATOM   1931 C CA  . VAL A 1 271 ? 16.709  38.387 41.603  1.00 52.01  ?  426 VAL A CA  1 
ATOM   1932 C C   . VAL A 1 271 ? 17.589  37.363 42.317  1.00 58.35  ?  426 VAL A C   1 
ATOM   1933 O O   . VAL A 1 271 ? 18.143  36.493 41.648  1.00 58.94  ?  426 VAL A O   1 
ATOM   1934 C CB  . VAL A 1 271 ? 17.321  39.814 41.475  1.00 54.67  ?  426 VAL A CB  1 
ATOM   1935 C CG1 . VAL A 1 271 ? 18.752  39.758 40.957  1.00 53.82  ?  426 VAL A CG1 1 
ATOM   1936 C CG2 . VAL A 1 271 ? 16.471  40.698 40.560  1.00 54.18  ?  426 VAL A CG2 1 
ATOM   1937 N N   . GLU A 1 272 ? 17.619  37.387 43.674  1.00 56.44  ?  427 GLU A N   1 
ATOM   1938 C CA  . GLU A 1 272 ? 18.372  36.429 44.510  1.00 56.34  ?  427 GLU A CA  1 
ATOM   1939 C C   . GLU A 1 272 ? 17.869  34.999 44.316  1.00 56.26  ?  427 GLU A C   1 
ATOM   1940 O O   . GLU A 1 272 ? 18.657  34.053 44.388  1.00 57.40  ?  427 GLU A O   1 
ATOM   1941 C CB  . GLU A 1 272 ? 18.295  36.807 45.994  1.00 58.36  ?  427 GLU A CB  1 
ATOM   1942 C CG  . GLU A 1 272 ? 19.275  37.897 46.396  1.00 77.09  ?  427 GLU A CG  1 
ATOM   1943 C CD  . GLU A 1 272 ? 19.112  38.475 47.795  1.00 113.31 ?  427 GLU A CD  1 
ATOM   1944 O OE1 . GLU A 1 272 ? 18.275  37.965 48.576  1.00 115.14 ?  427 GLU A OE1 1 
ATOM   1945 O OE2 . GLU A 1 272 ? 19.835  39.447 48.111  1.00 112.69 -1 427 GLU A OE2 1 
ATOM   1946 N N   . ALA A 1 273 ? 16.567  34.854 44.031  1.00 48.32  ?  428 ALA A N   1 
ATOM   1947 C CA  . ALA A 1 273 ? 15.952  33.556 43.825  1.00 47.96  ?  428 ALA A CA  1 
ATOM   1948 C C   . ALA A 1 273 ? 16.452  32.919 42.517  1.00 53.21  ?  428 ALA A C   1 
ATOM   1949 O O   . ALA A 1 273 ? 16.666  31.711 42.462  1.00 53.00  ?  428 ALA A O   1 
ATOM   1950 C CB  . ALA A 1 273 ? 14.431  33.684 43.840  1.00 48.59  ?  428 ALA A CB  1 
ATOM   1951 N N   . MET A 1 274 ? 16.687  33.745 41.488  1.00 50.58  ?  429 MET A N   1 
ATOM   1952 C CA  . MET A 1 274 ? 17.222  33.291 40.220  1.00 50.27  ?  429 MET A CA  1 
ATOM   1953 C C   . MET A 1 274 ? 18.715  33.005 40.368  1.00 54.87  ?  429 MET A C   1 
ATOM   1954 O O   . MET A 1 274 ? 19.209  32.028 39.787  1.00 54.93  ?  429 MET A O   1 
ATOM   1955 C CB  . MET A 1 274 ? 16.958  34.304 39.100  1.00 52.20  ?  429 MET A CB  1 
ATOM   1956 C CG  . MET A 1 274 ? 17.031  33.661 37.733  1.00 55.92  ?  429 MET A CG  1 
ATOM   1957 S SD  . MET A 1 274 ? 16.515  34.668 36.320  1.00 60.56  ?  429 MET A SD  1 
ATOM   1958 C CE  . MET A 1 274 ? 18.027  34.925 35.677  1.00 57.39  ?  429 MET A CE  1 
ATOM   1959 N N   . TYR A 1 275 ? 19.433  33.841 41.149  1.00 51.32  ?  430 TYR A N   1 
ATOM   1960 C CA  . TYR A 1 275 ? 20.868  33.621 41.379  1.00 51.39  ?  430 TYR A CA  1 
ATOM   1961 C C   . TYR A 1 275 ? 21.103  32.269 42.059  1.00 54.88  ?  430 TYR A C   1 
ATOM   1962 O O   . TYR A 1 275 ? 22.038  31.550 41.694  1.00 53.73  ?  430 TYR A O   1 
ATOM   1963 C CB  . TYR A 1 275 ? 21.517  34.773 42.173  1.00 52.34  ?  430 TYR A CB  1 
ATOM   1964 C CG  . TYR A 1 275 ? 22.995  34.545 42.367  1.00 53.92  ?  430 TYR A CG  1 
ATOM   1965 C CD1 . TYR A 1 275 ? 23.896  34.787 41.338  1.00 56.29  ?  430 TYR A CD1 1 
ATOM   1966 C CD2 . TYR A 1 275 ? 23.484  33.983 43.543  1.00 54.14  ?  430 TYR A CD2 1 
ATOM   1967 C CE1 . TYR A 1 275 ? 25.257  34.537 41.498  1.00 58.41  ?  430 TYR A CE1 1 
ATOM   1968 C CE2 . TYR A 1 275 ? 24.837  33.697 43.700  1.00 54.54  ?  430 TYR A CE2 1 
ATOM   1969 C CZ  . TYR A 1 275 ? 25.722  33.983 42.678  1.00 63.79  ?  430 TYR A CZ  1 
ATOM   1970 O OH  . TYR A 1 275 ? 27.062  33.715 42.828  1.00 68.51  ?  430 TYR A OH  1 
ATOM   1971 N N   . SER A 1 276 ? 20.225  31.925 43.029  1.00 51.73  ?  431 SER A N   1 
ATOM   1972 C CA  . SER A 1 276 ? 20.232  30.658 43.751  1.00 50.83  ?  431 SER A CA  1 
ATOM   1973 C C   . SER A 1 276 ? 20.140  29.477 42.758  1.00 52.81  ?  431 SER A C   1 
ATOM   1974 O O   . SER A 1 276 ? 20.942  28.550 42.868  1.00 54.40  ?  431 SER A O   1 
ATOM   1975 C CB  . SER A 1 276 ? 19.084  30.623 44.750  1.00 53.79  ?  431 SER A CB  1 
ATOM   1976 O OG  . SER A 1 276 ? 18.942  29.328 45.305  1.00 67.48  ?  431 SER A OG  1 
ATOM   1977 N N   . VAL A 1 277 ? 19.206  29.534 41.778  1.00 44.66  ?  432 VAL A N   1 
ATOM   1978 C CA  . VAL A 1 277 ? 19.046  28.491 40.751  1.00 43.33  ?  432 VAL A CA  1 
ATOM   1979 C C   . VAL A 1 277 ? 20.336  28.384 39.925  1.00 48.22  ?  432 VAL A C   1 
ATOM   1980 O O   . VAL A 1 277 ? 20.854  27.278 39.730  1.00 47.42  ?  432 VAL A O   1 
ATOM   1981 C CB  . VAL A 1 277 ? 17.807  28.712 39.835  1.00 45.92  ?  432 VAL A CB  1 
ATOM   1982 C CG1 . VAL A 1 277 ? 17.626  27.557 38.836  1.00 45.52  ?  432 VAL A CG1 1 
ATOM   1983 C CG2 . VAL A 1 277 ? 16.536  28.916 40.650  1.00 45.17  ?  432 VAL A CG2 1 
ATOM   1984 N N   . ALA A 1 278 ? 20.868  29.538 39.486  1.00 45.99  ?  433 ALA A N   1 
ATOM   1985 C CA  . ALA A 1 278 ? 22.095  29.628 38.691  1.00 45.89  ?  433 ALA A CA  1 
ATOM   1986 C C   . ALA A 1 278 ? 23.284  29.015 39.430  1.00 51.11  ?  433 ALA A C   1 
ATOM   1987 O O   . ALA A 1 278 ? 24.038  28.250 38.828  1.00 49.96  ?  433 ALA A O   1 
ATOM   1988 C CB  . ALA A 1 278 ? 22.390  31.083 38.332  1.00 46.32  ?  433 ALA A CB  1 
ATOM   1989 N N   . SER A 1 279 ? 23.450  29.336 40.738  1.00 49.44  ?  434 SER A N   1 
ATOM   1990 C CA  . SER A 1 279 ? 24.574  28.804 41.497  1.00 49.33  ?  434 SER A CA  1 
ATOM   1991 C C   . SER A 1 279 ? 24.440  27.294 41.726  1.00 53.58  ?  434 SER A C   1 
ATOM   1992 O O   . SER A 1 279 ? 25.452  26.593 41.718  1.00 55.14  ?  434 SER A O   1 
ATOM   1993 C CB  . SER A 1 279 ? 24.820  29.606 42.770  1.00 52.10  ?  434 SER A CB  1 
ATOM   1994 O OG  . SER A 1 279 ? 23.745  29.434 43.666  1.00 62.92  ?  434 SER A OG  1 
ATOM   1995 N N   . GLN A 1 280 ? 23.202  26.784 41.832  1.00 48.92  ?  435 GLN A N   1 
ATOM   1996 C CA  . GLN A 1 280 ? 22.951  25.342 41.951  1.00 48.53  ?  435 GLN A CA  1 
ATOM   1997 C C   . GLN A 1 280 ? 23.347  24.663 40.624  1.00 53.01  ?  435 GLN A C   1 
ATOM   1998 O O   . GLN A 1 280 ? 23.994  23.612 40.631  1.00 51.82  ?  435 GLN A O   1 
ATOM   1999 C CB  . GLN A 1 280 ? 21.480  25.055 42.274  1.00 49.45  ?  435 GLN A CB  1 
ATOM   2000 C CG  . GLN A 1 280 ? 21.160  25.230 43.743  1.00 69.91  ?  435 GLN A CG  1 
ATOM   2001 C CD  . GLN A 1 280 ? 19.670  25.255 43.994  1.00 97.03  ?  435 GLN A CD  1 
ATOM   2002 O OE1 . GLN A 1 280 ? 19.043  26.326 44.081  1.00 93.71  ?  435 GLN A OE1 1 
ATOM   2003 N NE2 . GLN A 1 280 ? 19.068  24.075 44.123  1.00 86.98  ?  435 GLN A NE2 1 
ATOM   2004 N N   . CYS A 1 281 ? 22.996  25.312 39.488  1.00 50.04  ?  436 CYS A N   1 
ATOM   2005 C CA  . CYS A 1 281 ? 23.331  24.866 38.136  1.00 49.69  ?  436 CYS A CA  1 
ATOM   2006 C C   . CYS A 1 281 ? 24.828  24.863 37.920  1.00 53.11  ?  436 CYS A C   1 
ATOM   2007 O O   . CYS A 1 281 ? 25.342  24.028 37.177  1.00 51.71  ?  436 CYS A O   1 
ATOM   2008 C CB  . CYS A 1 281 ? 22.648  25.747 37.098  1.00 49.97  ?  436 CYS A CB  1 
ATOM   2009 S SG  . CYS A 1 281 ? 20.866  25.504 36.971  1.00 54.15  ?  436 CYS A SG  1 
ATOM   2010 N N   . LEU A 1 282 ? 25.514  25.840 38.518  1.00 50.87  ?  437 LEU A N   1 
ATOM   2011 C CA  . LEU A 1 282 ? 26.949  26.018 38.365  1.00 51.10  ?  437 LEU A CA  1 
ATOM   2012 C C   . LEU A 1 282 ? 27.847  25.202 39.307  1.00 54.50  ?  437 LEU A C   1 
ATOM   2013 O O   . LEU A 1 282 ? 29.033  25.509 39.428  1.00 52.95  ?  437 LEU A O   1 
ATOM   2014 C CB  . LEU A 1 282 ? 27.315  27.513 38.339  1.00 51.31  ?  437 LEU A CB  1 
ATOM   2015 C CG  . LEU A 1 282 ? 26.773  28.345 37.182  1.00 55.34  ?  437 LEU A CG  1 
ATOM   2016 C CD1 . LEU A 1 282 ? 26.969  29.831 37.470  1.00 54.54  ?  437 LEU A CD1 1 
ATOM   2017 C CD2 . LEU A 1 282 ? 27.388  27.913 35.843  1.00 56.53  ?  437 LEU A CD2 1 
ATOM   2018 N N   . HIS A 1 283 ? 27.306  24.120 39.908  1.00 53.91  ?  438 HIS A N   1 
ATOM   2019 C CA  . HIS A 1 283 ? 28.083  23.200 40.740  1.00 54.74  ?  438 HIS A CA  1 
ATOM   2020 C C   . HIS A 1 283 ? 29.147  22.522 39.905  1.00 59.44  ?  438 HIS A C   1 
ATOM   2021 O O   . HIS A 1 283 ? 28.876  21.985 38.830  1.00 56.73  ?  438 HIS A O   1 
ATOM   2022 C CB  . HIS A 1 283 ? 27.218  22.138 41.430  1.00 56.10  ?  438 HIS A CB  1 
ATOM   2023 C CG  . HIS A 1 283 ? 26.615  22.577 42.730  1.00 60.13  ?  438 HIS A CG  1 
ATOM   2024 N ND1 . HIS A 1 283 ? 25.444  22.216 43.298  1.00 62.19  ?  438 HIS A ND1 1 
ATOM   2025 C CD2 . HIS A 1 283 ? 27.273  23.447 43.582  1.00 61.93  ?  438 HIS A CD2 1 
ATOM   2026 C CE1 . HIS A 1 283 ? 25.355  22.892 44.490  1.00 61.51  ?  438 HIS A CE1 1 
ATOM   2027 N NE2 . HIS A 1 283 ? 26.467  23.610 44.618  1.00 61.71  ?  438 HIS A NE2 1 
ATOM   2028 N N   . GLU A 1 284 ? 30.379  22.649 40.398  1.00 59.45  ?  439 GLU A N   1 
ATOM   2029 C CA  . GLU A 1 284 ? 31.653  22.107 39.931  1.00 60.54  ?  439 GLU A CA  1 
ATOM   2030 C C   . GLU A 1 284 ? 31.490  20.603 39.610  1.00 65.38  ?  439 GLU A C   1 
ATOM   2031 O O   . GLU A 1 284 ? 31.966  20.096 38.578  1.00 66.39  ?  439 GLU A O   1 
ATOM   2032 C CB  . GLU A 1 284 ? 32.722  22.286 41.053  1.00 62.20  ?  439 GLU A CB  1 
ATOM   2033 C CG  . GLU A 1 284 ? 32.285  23.013 42.348  1.00 74.87  ?  439 GLU A CG  1 
ATOM   2034 C CD  . GLU A 1 284 ? 31.313  22.458 43.401  1.00 77.72  ?  439 GLU A CD  1 
ATOM   2035 O OE1 . GLU A 1 284 ? 30.905  21.269 43.338  1.00 36.91  ?  439 GLU A OE1 1 
ATOM   2036 O OE2 . GLU A 1 284 ? 30.948  23.255 44.299  1.00 62.66  -1 439 GLU A OE2 1 
ATOM   2037 N N   . LYS A 1 285 ? 30.779  19.920 40.510  1.00 59.95  ?  440 LYS A N   1 
ATOM   2038 C CA  . LYS A 1 285 ? 30.492  18.506 40.486  1.00 59.43  ?  440 LYS A CA  1 
ATOM   2039 C C   . LYS A 1 285 ? 29.155  18.210 39.789  1.00 62.43  ?  440 LYS A C   1 
ATOM   2040 O O   . LYS A 1 285 ? 28.090  18.512 40.338  1.00 60.52  ?  440 LYS A O   1 
ATOM   2041 C CB  . LYS A 1 285 ? 30.520  17.963 41.935  1.00 61.65  ?  440 LYS A CB  1 
ATOM   2042 N N   . LYS A 1 286 ? 29.226  17.574 38.592  1.00 60.29  ?  441 LYS A N   1 
ATOM   2043 C CA  . LYS A 1 286 ? 28.093  17.153 37.743  1.00 59.92  ?  441 LYS A CA  1 
ATOM   2044 C C   . LYS A 1 286 ? 26.877  16.623 38.521  1.00 64.63  ?  441 LYS A C   1 
ATOM   2045 O O   . LYS A 1 286 ? 25.757  17.083 38.309  1.00 64.87  ?  441 LYS A O   1 
ATOM   2046 C CB  . LYS A 1 286 ? 28.552  16.113 36.708  1.00 61.69  ?  441 LYS A CB  1 
ATOM   2047 N N   . ASN A 1 287 ? 27.104  15.702 39.448  1.00 61.59  ?  442 ASN A N   1 
ATOM   2048 C CA  . ASN A 1 287 ? 26.037  15.067 40.234  1.00 61.10  ?  442 ASN A CA  1 
ATOM   2049 C C   . ASN A 1 287 ? 25.417  15.940 41.327  1.00 61.08  ?  442 ASN A C   1 
ATOM   2050 O O   . ASN A 1 287 ? 24.336  15.597 41.823  1.00 59.44  ?  442 ASN A O   1 
ATOM   2051 C CB  . ASN A 1 287 ? 26.498  13.698 40.771  1.00 65.81  ?  442 ASN A CB  1 
ATOM   2052 C CG  . ASN A 1 287 ? 26.892  12.700 39.701  1.00 91.10  ?  442 ASN A CG  1 
ATOM   2053 O OD1 . ASN A 1 287 ? 27.510  13.031 38.673  1.00 84.03  ?  442 ASN A OD1 1 
ATOM   2054 N ND2 . ASN A 1 287 ? 26.594  11.438 39.959  1.00 85.76  ?  442 ASN A ND2 1 
ATOM   2055 N N   . LYS A 1 288 ? 26.078  17.079 41.675  1.00 56.09  ?  443 LYS A N   1 
ATOM   2056 C CA  . LYS A 1 288 ? 25.590  18.035 42.680  1.00 54.58  ?  443 LYS A CA  1 
ATOM   2057 C C   . LYS A 1 288 ? 24.571  19.024 42.099  1.00 56.39  ?  443 LYS A C   1 
ATOM   2058 O O   . LYS A 1 288 ? 23.829  19.645 42.858  1.00 54.37  ?  443 LYS A O   1 
ATOM   2059 C CB  . LYS A 1 288 ? 26.754  18.783 43.323  1.00 56.75  ?  443 LYS A CB  1 
ATOM   2060 N N   . ARG A 1 289 ? 24.519  19.147 40.750  1.00 54.05  ?  444 ARG A N   1 
ATOM   2061 C CA  . ARG A 1 289 ? 23.622  20.058 40.013  1.00 54.32  ?  444 ARG A CA  1 
ATOM   2062 C C   . ARG A 1 289 ? 22.198  19.514 39.959  1.00 60.90  ?  444 ARG A C   1 
ATOM   2063 O O   . ARG A 1 289 ? 22.038  18.287 39.856  1.00 60.52  ?  444 ARG A O   1 
ATOM   2064 C CB  . ARG A 1 289 ? 24.102  20.249 38.570  1.00 49.68  ?  444 ARG A CB  1 
ATOM   2065 C CG  . ARG A 1 289 ? 25.433  20.934 38.418  1.00 43.48  ?  444 ARG A CG  1 
ATOM   2066 C CD  . ARG A 1 289 ? 25.894  20.749 37.010  1.00 39.05  ?  444 ARG A CD  1 
ATOM   2067 N NE  . ARG A 1 289 ? 27.348  20.832 36.910  1.00 46.91  ?  444 ARG A NE  1 
ATOM   2068 C CZ  . ARG A 1 289 ? 28.041  20.375 35.872  1.00 55.81  ?  444 ARG A CZ  1 
ATOM   2069 N NH1 . ARG A 1 289 ? 27.416  19.809 34.847  1.00 48.78  ?  444 ARG A NH1 1 
ATOM   2070 N NH2 . ARG A 1 289 ? 29.362  20.470 35.854  1.00 29.91  1  444 ARG A NH2 1 
ATOM   2071 N N   . PRO A 1 290 ? 21.152  20.395 39.935  1.00 58.83  ?  445 PRO A N   1 
ATOM   2072 C CA  . PRO A 1 290 ? 19.776  19.874 39.826  1.00 58.40  ?  445 PRO A CA  1 
ATOM   2073 C C   . PRO A 1 290 ? 19.472  19.362 38.421  1.00 63.45  ?  445 PRO A C   1 
ATOM   2074 O O   . PRO A 1 290 ? 20.163  19.735 37.474  1.00 63.88  ?  445 PRO A O   1 
ATOM   2075 C CB  . PRO A 1 290 ? 18.912  21.090 40.168  1.00 59.46  ?  445 PRO A CB  1 
ATOM   2076 C CG  . PRO A 1 290 ? 19.726  22.258 39.813  1.00 63.86  ?  445 PRO A CG  1 
ATOM   2077 C CD  . PRO A 1 290 ? 21.164  21.880 39.989  1.00 60.06  ?  445 PRO A CD  1 
ATOM   2078 N N   . ASP A 1 291 ? 18.452  18.515 38.280  1.00 59.91  ?  446 ASP A N   1 
ATOM   2079 C CA  . ASP A 1 291 ? 18.043  18.061 36.956  1.00 59.88  ?  446 ASP A CA  1 
ATOM   2080 C C   . ASP A 1 291 ? 17.062  19.114 36.416  1.00 63.84  ?  446 ASP A C   1 
ATOM   2081 O O   . ASP A 1 291 ? 16.574  19.948 37.191  1.00 63.74  ?  446 ASP A O   1 
ATOM   2082 C CB  . ASP A 1 291 ? 17.456  16.630 36.974  1.00 61.71  ?  446 ASP A CB  1 
ATOM   2083 C CG  . ASP A 1 291 ? 16.226  16.387 37.842  1.00 76.79  ?  446 ASP A CG  1 
ATOM   2084 O OD1 . ASP A 1 291 ? 15.906  17.252 38.692  1.00 76.79  ?  446 ASP A OD1 1 
ATOM   2085 O OD2 . ASP A 1 291 ? 15.612  15.309 37.705  1.00 87.96  -1 446 ASP A OD2 1 
ATOM   2086 N N   . ILE A 1 292 ? 16.812  19.100 35.091  1.00 59.49  ?  447 ILE A N   1 
ATOM   2087 C CA  . ILE A 1 292 ? 15.937  20.065 34.428  1.00 58.30  ?  447 ILE A CA  1 
ATOM   2088 C C   . ILE A 1 292 ? 14.553  20.255 35.048  1.00 58.53  ?  447 ILE A C   1 
ATOM   2089 O O   . ILE A 1 292 ? 14.159  21.404 35.242  1.00 57.10  ?  447 ILE A O   1 
ATOM   2090 C CB  . ILE A 1 292 ? 15.983  19.975 32.880  1.00 61.59  ?  447 ILE A CB  1 
ATOM   2091 C CG1 . ILE A 1 292 ? 15.509  21.281 32.186  1.00 61.88  ?  447 ILE A CG1 1 
ATOM   2092 C CG2 . ILE A 1 292 ? 15.352  18.700 32.324  1.00 61.90  ?  447 ILE A CG2 1 
ATOM   2093 C CD1 . ILE A 1 292 ? 16.409  22.553 32.467  1.00 72.46  ?  447 ILE A CD1 1 
ATOM   2094 N N   . LYS A 1 293 ? 13.866  19.167 35.445  1.00 54.51  ?  448 LYS A N   1 
ATOM   2095 C CA  . LYS A 1 293 ? 12.545  19.289 36.089  1.00 54.97  ?  448 LYS A CA  1 
ATOM   2096 C C   . LYS A 1 293 ? 12.637  20.084 37.410  1.00 59.83  ?  448 LYS A C   1 
ATOM   2097 O O   . LYS A 1 293 ? 11.713  20.857 37.715  1.00 60.61  ?  448 LYS A O   1 
ATOM   2098 C CB  . LYS A 1 293 ? 11.858  17.923 36.290  1.00 57.06  ?  448 LYS A CB  1 
ATOM   2099 N N   . LYS A 1 294 ? 13.778  19.944 38.156  1.00 53.42  ?  449 LYS A N   1 
ATOM   2100 C CA  . LYS A 1 294 ? 14.003  20.701 39.390  1.00 51.61  ?  449 LYS A CA  1 
ATOM   2101 C C   . LYS A 1 294 ? 14.201  22.173 39.049  1.00 53.91  ?  449 LYS A C   1 
ATOM   2102 O O   . LYS A 1 294 ? 13.570  23.026 39.687  1.00 53.61  ?  449 LYS A O   1 
ATOM   2103 C CB  . LYS A 1 294 ? 15.187  20.140 40.203  1.00 53.34  ?  449 LYS A CB  1 
ATOM   2104 C CG  . LYS A 1 294 ? 15.470  20.845 41.546  1.00 59.01  ?  449 LYS A CG  1 
ATOM   2105 C CD  . LYS A 1 294 ? 14.345  20.724 42.573  1.00 71.41  ?  449 LYS A CD  1 
ATOM   2106 C CE  . LYS A 1 294 ? 14.661  21.492 43.830  1.00 90.42  ?  449 LYS A CE  1 
ATOM   2107 N NZ  . LYS A 1 294 ? 13.484  21.570 44.730  1.00 102.29 1  449 LYS A NZ  1 
ATOM   2108 N N   . VAL A 1 295 ? 15.044  22.461 38.012  1.00 48.30  ?  450 VAL A N   1 
ATOM   2109 C CA  . VAL A 1 295 ? 15.309  23.807 37.492  1.00 47.45  ?  450 VAL A CA  1 
ATOM   2110 C C   . VAL A 1 295 ? 13.974  24.497 37.106  1.00 49.92  ?  450 VAL A C   1 
ATOM   2111 O O   . VAL A 1 295 ? 13.753  25.646 37.514  1.00 48.68  ?  450 VAL A O   1 
ATOM   2112 C CB  . VAL A 1 295 ? 16.328  23.793 36.334  1.00 51.37  ?  450 VAL A CB  1 
ATOM   2113 C CG1 . VAL A 1 295 ? 16.535  25.191 35.765  1.00 51.57  ?  450 VAL A CG1 1 
ATOM   2114 C CG2 . VAL A 1 295 ? 17.654  23.223 36.787  1.00 51.04  ?  450 VAL A CG2 1 
ATOM   2115 N N   . GLN A 1 296 ? 13.063  23.769 36.403  1.00 46.59  ?  451 GLN A N   1 
ATOM   2116 C CA  . GLN A 1 296 ? 11.737  24.289 36.024  1.00 46.74  ?  451 GLN A CA  1 
ATOM   2117 C C   . GLN A 1 296 ? 10.933  24.629 37.274  1.00 54.67  ?  451 GLN A C   1 
ATOM   2118 O O   . GLN A 1 296 ? 10.339  25.713 37.339  1.00 54.43  ?  451 GLN A O   1 
ATOM   2119 C CB  . GLN A 1 296 ? 10.940  23.264 35.238  1.00 47.17  ?  451 GLN A CB  1 
ATOM   2120 C CG  . GLN A 1 296 ? 11.380  22.992 33.821  1.00 52.10  ?  451 GLN A CG  1 
ATOM   2121 C CD  . GLN A 1 296 ? 10.319  22.152 33.162  1.00 66.07  ?  451 GLN A CD  1 
ATOM   2122 O OE1 . GLN A 1 296 ? 10.240  20.895 33.537  1.00 65.72  ?  451 GLN A OE1 1 
ATOM   2123 N NE2 . GLN A 1 296 ? 9.483   22.647 32.410  1.00 51.80  ?  451 GLN A NE2 1 
ATOM   2124 N N   . GLN A 1 297 ? 10.917  23.691 38.265  1.00 53.01  ?  452 GLN A N   1 
ATOM   2125 C CA  . GLN A 1 297 ? 10.187  23.844 39.522  1.00 53.44  ?  452 GLN A CA  1 
ATOM   2126 C C   . GLN A 1 297 ? 10.665  25.085 40.264  1.00 58.27  ?  452 GLN A C   1 
ATOM   2127 O O   . GLN A 1 297 ? 9.846   25.936 40.635  1.00 59.46  ?  452 GLN A O   1 
ATOM   2128 C CB  . GLN A 1 297 ? 10.311  22.581 40.392  1.00 54.99  ?  452 GLN A CB  1 
ATOM   2129 N N   . LEU A 1 298 ? 11.986  25.229 40.395  1.00 53.43  ?  453 LEU A N   1 
ATOM   2130 C CA  . LEU A 1 298 ? 12.586  26.374 41.055  1.00 53.63  ?  453 LEU A CA  1 
ATOM   2131 C C   . LEU A 1 298 ? 12.255  27.695 40.363  1.00 62.06  ?  453 LEU A C   1 
ATOM   2132 O O   . LEU A 1 298 ? 11.897  28.662 41.052  1.00 62.98  ?  453 LEU A O   1 
ATOM   2133 C CB  . LEU A 1 298 ? 14.091  26.179 41.202  1.00 53.34  ?  453 LEU A CB  1 
ATOM   2134 C CG  . LEU A 1 298 ? 14.550  25.019 42.105  1.00 56.78  ?  453 LEU A CG  1 
ATOM   2135 C CD1 . LEU A 1 298 ? 16.024  24.744 41.906  1.00 56.01  ?  453 LEU A CD1 1 
ATOM   2136 C CD2 . LEU A 1 298 ? 14.210  25.282 43.589  1.00 56.60  ?  453 LEU A CD2 1 
ATOM   2137 N N   . LEU A 1 299 ? 12.318  27.730 39.011  1.00 59.84  ?  454 LEU A N   1 
ATOM   2138 C CA  . LEU A 1 299 ? 11.994  28.926 38.226  1.00 59.39  ?  454 LEU A CA  1 
ATOM   2139 C C   . LEU A 1 299 ? 10.514  29.291 38.346  1.00 64.54  ?  454 LEU A C   1 
ATOM   2140 O O   . LEU A 1 299 ? 10.190  30.474 38.364  1.00 63.19  ?  454 LEU A O   1 
ATOM   2141 C CB  . LEU A 1 299 ? 12.379  28.761 36.741  1.00 58.99  ?  454 LEU A CB  1 
ATOM   2142 C CG  . LEU A 1 299 ? 13.861  28.653 36.377  1.00 62.70  ?  454 LEU A CG  1 
ATOM   2143 C CD1 . LEU A 1 299 ? 14.015  28.321 34.922  1.00 62.67  ?  454 LEU A CD1 1 
ATOM   2144 C CD2 . LEU A 1 299 ? 14.631  29.927 36.693  1.00 63.15  ?  454 LEU A CD2 1 
ATOM   2145 N N   . GLN A 1 300 ? 9.614   28.281 38.395  1.00 64.04  ?  455 GLN A N   1 
ATOM   2146 C CA  . GLN A 1 300 ? 8.169   28.512 38.534  1.00 64.98  ?  455 GLN A CA  1 
ATOM   2147 C C   . GLN A 1 300 ? 7.872   29.091 39.922  1.00 70.73  ?  455 GLN A C   1 
ATOM   2148 O O   . GLN A 1 300 ? 7.077   30.023 40.029  1.00 70.10  ?  455 GLN A O   1 
ATOM   2149 C CB  . GLN A 1 300 ? 7.360   27.230 38.277  1.00 66.41  ?  455 GLN A CB  1 
ATOM   2150 N N   . GLU A 1 301 ? 8.570   28.583 40.964  1.00 68.84  ?  456 GLU A N   1 
ATOM   2151 C CA  . GLU A 1 301 ? 8.456   29.030 42.355  1.00 69.95  ?  456 GLU A CA  1 
ATOM   2152 C C   . GLU A 1 301 ? 8.868   30.501 42.503  1.00 77.48  ?  456 GLU A C   1 
ATOM   2153 O O   . GLU A 1 301 ? 8.269   31.241 43.289  1.00 79.20  ?  456 GLU A O   1 
ATOM   2154 C CB  . GLU A 1 301 ? 9.326   28.148 43.269  1.00 71.57  ?  456 GLU A CB  1 
ATOM   2155 C CG  . GLU A 1 301 ? 8.658   26.851 43.701  1.00 86.00  ?  456 GLU A CG  1 
ATOM   2156 C CD  . GLU A 1 301 ? 9.571   25.711 44.119  1.00 110.49 ?  456 GLU A CD  1 
ATOM   2157 O OE1 . GLU A 1 301 ? 10.707  25.980 44.576  1.00 107.23 ?  456 GLU A OE1 1 
ATOM   2158 O OE2 . GLU A 1 301 ? 9.142   24.541 43.991  1.00 101.74 -1 456 GLU A OE2 1 
ATOM   2159 N N   . MET A 1 302 ? 9.896   30.909 41.739  1.00 73.74  ?  457 MET A N   1 
ATOM   2160 C CA  . MET A 1 302 ? 10.497  32.243 41.658  1.00 72.96  ?  457 MET A CA  1 
ATOM   2161 C C   . MET A 1 302 ? 9.466   33.376 41.461  1.00 77.61  ?  457 MET A C   1 
ATOM   2162 O O   . MET A 1 302 ? 9.653   34.469 42.005  1.00 77.25  ?  457 MET A O   1 
ATOM   2163 C CB  . MET A 1 302 ? 11.447  32.238 40.464  1.00 74.67  ?  457 MET A CB  1 
ATOM   2164 C CG  . MET A 1 302 ? 12.699  32.981 40.659  1.00 77.17  ?  457 MET A CG  1 
ATOM   2165 S SD  . MET A 1 302 ? 13.018  34.050 39.256  1.00 80.06  ?  457 MET A SD  1 
ATOM   2166 C CE  . MET A 1 302 ? 12.963  32.897 37.900  1.00 76.39  ?  457 MET A CE  1 
ATOM   2167 N N   . THR A 1 303 ? 8.399   33.111 40.666  1.00 74.53  ?  458 THR A N   1 
ATOM   2168 C CA  . THR A 1 303 ? 7.339   34.073 40.337  1.00 95.15  ?  458 THR A CA  1 
ATOM   2169 C C   . THR A 1 303 ? 6.077   33.928 41.207  1.00 128.60 ?  458 THR A C   1 
ATOM   2170 O O   . THR A 1 303 ? 5.589   32.822 41.455  1.00 92.38  ?  458 THR A O   1 
ATOM   2171 C CB  . THR A 1 303 ? 7.041   34.083 38.820  1.00 100.77 ?  458 THR A CB  1 
ATOM   2172 O OG1 . THR A 1 303 ? 6.701   32.767 38.383  1.00 102.69 ?  458 THR A OG1 1 
ATOM   2173 C CG2 . THR A 1 303 ? 8.203   34.612 37.988  1.00 96.74  ?  458 THR A CG2 1 
ATOM   2174 N N   . ARG B 1 9   ? 15.753  73.986 8.076   1.00 70.71  ?  164 ARG B N   1 
ATOM   2175 C CA  . ARG B 1 9   ? 15.191  73.196 9.178   1.00 71.14  ?  164 ARG B CA  1 
ATOM   2176 C C   . ARG B 1 9   ? 15.115  71.694 8.823   1.00 73.70  ?  164 ARG B C   1 
ATOM   2177 O O   . ARG B 1 9   ? 15.597  70.849 9.585   1.00 74.44  ?  164 ARG B O   1 
ATOM   2178 C CB  . ARG B 1 9   ? 13.797  73.734 9.568   1.00 73.38  ?  164 ARG B CB  1 
ATOM   2179 C CG  . ARG B 1 9   ? 13.745  74.355 10.958  1.00 85.87  ?  164 ARG B CG  1 
ATOM   2180 C CD  . ARG B 1 9   ? 12.765  73.619 11.847  1.00 92.85  ?  164 ARG B CD  1 
ATOM   2181 N NE  . ARG B 1 9   ? 13.401  72.986 13.005  1.00 101.79 ?  164 ARG B NE  1 
ATOM   2182 C CZ  . ARG B 1 9   ? 13.948  71.772 12.995  1.00 119.57 ?  164 ARG B CZ  1 
ATOM   2183 N NH1 . ARG B 1 9   ? 13.975  71.056 11.877  1.00 102.06 ?  164 ARG B NH1 1 
ATOM   2184 N NH2 . ARG B 1 9   ? 14.490  71.273 14.097  1.00 112.07 1  164 ARG B NH2 1 
ATOM   2185 N N   . PHE B 1 10  ? 14.493  71.379 7.665   1.00 66.92  ?  165 PHE B N   1 
ATOM   2186 C CA  . PHE B 1 10  ? 14.305  70.026 7.142   1.00 64.29  ?  165 PHE B CA  1 
ATOM   2187 C C   . PHE B 1 10  ? 14.982  69.897 5.809   1.00 64.20  ?  165 PHE B C   1 
ATOM   2188 O O   . PHE B 1 10  ? 15.021  70.859 5.040   1.00 63.10  ?  165 PHE B O   1 
ATOM   2189 C CB  . PHE B 1 10  ? 12.811  69.709 6.961   1.00 65.46  ?  165 PHE B CB  1 
ATOM   2190 C CG  . PHE B 1 10  ? 11.947  69.890 8.181   1.00 66.16  ?  165 PHE B CG  1 
ATOM   2191 C CD1 . PHE B 1 10  ? 12.128  69.096 9.309   1.00 68.85  ?  165 PHE B CD1 1 
ATOM   2192 C CD2 . PHE B 1 10  ? 10.919  70.821 8.185   1.00 67.39  ?  165 PHE B CD2 1 
ATOM   2193 C CE1 . PHE B 1 10  ? 11.315  69.257 10.430  1.00 69.78  ?  165 PHE B CE1 1 
ATOM   2194 C CE2 . PHE B 1 10  ? 10.107  70.982 9.305   1.00 70.20  ?  165 PHE B CE2 1 
ATOM   2195 C CZ  . PHE B 1 10  ? 10.308  70.199 10.420  1.00 68.54  ?  165 PHE B CZ  1 
ATOM   2196 N N   . HIS B 1 11  ? 15.476  68.697 5.510   1.00 59.49  ?  166 HIS B N   1 
ATOM   2197 C CA  . HIS B 1 11  ? 16.150  68.419 4.253   1.00 58.18  ?  166 HIS B CA  1 
ATOM   2198 C C   . HIS B 1 11  ? 15.190  68.376 3.086   1.00 58.18  ?  166 HIS B C   1 
ATOM   2199 O O   . HIS B 1 11  ? 14.205  67.669 3.144   1.00 56.13  ?  166 HIS B O   1 
ATOM   2200 C CB  . HIS B 1 11  ? 16.969  67.125 4.338   1.00 59.39  ?  166 HIS B CB  1 
ATOM   2201 C CG  . HIS B 1 11  ? 17.728  66.841 3.089   1.00 63.43  ?  166 HIS B CG  1 
ATOM   2202 N ND1 . HIS B 1 11  ? 17.278  65.912 2.177   1.00 65.67  ?  166 HIS B ND1 1 
ATOM   2203 C CD2 . HIS B 1 11  ? 18.840  67.434 2.603   1.00 65.70  ?  166 HIS B CD2 1 
ATOM   2204 C CE1 . HIS B 1 11  ? 18.150  65.935 1.186   1.00 65.51  ?  166 HIS B CE1 1 
ATOM   2205 N NE2 . HIS B 1 11  ? 19.105  66.845 1.398   1.00 65.86  ?  166 HIS B NE2 1 
ATOM   2206 N N   . SER B 1 12  ? 15.460  69.152 2.029   1.00 55.45  ?  167 SER B N   1 
ATOM   2207 C CA  . SER B 1 12  ? 14.612  69.098 0.846   1.00 55.23  ?  167 SER B CA  1 
ATOM   2208 C C   . SER B 1 12  ? 15.120  68.007 -0.084  1.00 60.01  ?  167 SER B C   1 
ATOM   2209 O O   . SER B 1 12  ? 16.300  67.984 -0.454  1.00 60.39  ?  167 SER B O   1 
ATOM   2210 C CB  . SER B 1 12  ? 14.520  70.435 0.131   1.00 57.47  ?  167 SER B CB  1 
ATOM   2211 O OG  . SER B 1 12  ? 13.460  70.363 -0.810  1.00 63.15  ?  167 SER B OG  1 
ATOM   2212 N N   . PHE B 1 13  ? 14.242  67.058 -0.383  1.00 55.63  ?  168 PHE B N   1 
ATOM   2213 C CA  . PHE B 1 13  ? 14.564  65.929 -1.236  1.00 55.13  ?  168 PHE B CA  1 
ATOM   2214 C C   . PHE B 1 13  ? 14.001  66.186 -2.615  1.00 63.43  ?  168 PHE B C   1 
ATOM   2215 O O   . PHE B 1 13  ? 13.024  66.924 -2.765  1.00 64.02  ?  168 PHE B O   1 
ATOM   2216 C CB  . PHE B 1 13  ? 13.946  64.626 -0.675  1.00 55.16  ?  168 PHE B CB  1 
ATOM   2217 C CG  . PHE B 1 13  ? 14.521  64.086 0.611   1.00 54.66  ?  168 PHE B CG  1 
ATOM   2218 C CD1 . PHE B 1 13  ? 13.992  64.463 1.841   1.00 55.02  ?  168 PHE B CD1 1 
ATOM   2219 C CD2 . PHE B 1 13  ? 15.554  63.155 0.594   1.00 55.82  ?  168 PHE B CD2 1 
ATOM   2220 C CE1 . PHE B 1 13  ? 14.525  63.958 3.035   1.00 54.81  ?  168 PHE B CE1 1 
ATOM   2221 C CE2 . PHE B 1 13  ? 16.086  62.652 1.790   1.00 57.19  ?  168 PHE B CE2 1 
ATOM   2222 C CZ  . PHE B 1 13  ? 15.565  63.056 2.999   1.00 54.11  ?  168 PHE B CZ  1 
ATOM   2223 N N   . SER B 1 14  ? 14.609  65.573 -3.628  1.00 61.72  ?  169 SER B N   1 
ATOM   2224 C CA  . SER B 1 14  ? 14.075  65.624 -4.983  1.00 62.30  ?  169 SER B CA  1 
ATOM   2225 C C   . SER B 1 14  ? 13.242  64.361 -5.074  1.00 65.28  ?  169 SER B C   1 
ATOM   2226 O O   . SER B 1 14  ? 13.661  63.320 -4.545  1.00 65.83  ?  169 SER B O   1 
ATOM   2227 C CB  . SER B 1 14  ? 15.193  65.584 -6.023  1.00 67.91  ?  169 SER B CB  1 
ATOM   2228 O OG  . SER B 1 14  ? 14.647  65.667 -7.331  1.00 79.60  ?  169 SER B OG  1 
ATOM   2229 N N   . PHE B 1 15  ? 12.061  64.442 -5.702  1.00 59.57  ?  170 PHE B N   1 
ATOM   2230 C CA  . PHE B 1 15  ? 11.171  63.286 -5.828  1.00 59.06  ?  170 PHE B CA  1 
ATOM   2231 C C   . PHE B 1 15  ? 11.861  61.982 -6.270  1.00 64.49  ?  170 PHE B C   1 
ATOM   2232 O O   . PHE B 1 15  ? 11.492  60.896 -5.829  1.00 63.98  ?  170 PHE B O   1 
ATOM   2233 C CB  . PHE B 1 15  ? 9.976   63.615 -6.732  1.00 60.14  ?  170 PHE B CB  1 
ATOM   2234 C CG  . PHE B 1 15  ? 8.952   62.509 -6.771  1.00 60.57  ?  170 PHE B CG  1 
ATOM   2235 C CD1 . PHE B 1 15  ? 8.236   62.161 -5.631  1.00 61.94  ?  170 PHE B CD1 1 
ATOM   2236 C CD2 . PHE B 1 15  ? 8.718   61.799 -7.941  1.00 61.52  ?  170 PHE B CD2 1 
ATOM   2237 C CE1 . PHE B 1 15  ? 7.306   61.127 -5.666  1.00 61.89  ?  170 PHE B CE1 1 
ATOM   2238 C CE2 . PHE B 1 15  ? 7.788   60.763 -7.971  1.00 63.39  ?  170 PHE B CE2 1 
ATOM   2239 C CZ  . PHE B 1 15  ? 7.081   60.447 -6.840  1.00 61.05  ?  170 PHE B CZ  1 
ATOM   2240 N N   . TYR B 1 16  ? 12.889  62.116 -7.089  1.00 62.80  ?  171 TYR B N   1 
ATOM   2241 C CA  . TYR B 1 16  ? 13.660  61.012 -7.642  1.00 63.55  ?  171 TYR B CA  1 
ATOM   2242 C C   . TYR B 1 16  ? 14.559  60.284 -6.620  1.00 65.86  ?  171 TYR B C   1 
ATOM   2243 O O   . TYR B 1 16  ? 14.797  59.091 -6.789  1.00 65.32  ?  171 TYR B O   1 
ATOM   2244 C CB  . TYR B 1 16  ? 14.405  61.484 -8.903  1.00 65.91  ?  171 TYR B CB  1 
ATOM   2245 C CG  . TYR B 1 16  ? 13.506  62.238 -9.864  1.00 68.92  ?  171 TYR B CG  1 
ATOM   2246 C CD1 . TYR B 1 16  ? 12.677  61.560 -10.755 1.00 71.12  ?  171 TYR B CD1 1 
ATOM   2247 C CD2 . TYR B 1 16  ? 13.442  63.631 -9.847  1.00 69.96  ?  171 TYR B CD2 1 
ATOM   2248 C CE1 . TYR B 1 16  ? 11.852  62.246 -11.649 1.00 72.38  ?  171 TYR B CE1 1 
ATOM   2249 C CE2 . TYR B 1 16  ? 12.613  64.329 -10.728 1.00 71.21  ?  171 TYR B CE2 1 
ATOM   2250 C CZ  . TYR B 1 16  ? 11.827  63.631 -11.637 1.00 80.74  ?  171 TYR B CZ  1 
ATOM   2251 O OH  . TYR B 1 16  ? 11.016  64.301 -12.527 1.00 84.30  ?  171 TYR B OH  1 
ATOM   2252 N N   . GLU B 1 17  ? 15.037  60.987 -5.560  1.00 60.98  ?  172 GLU B N   1 
ATOM   2253 C CA  . GLU B 1 17  ? 15.827  60.406 -4.458  1.00 59.66  ?  172 GLU B CA  1 
ATOM   2254 C C   . GLU B 1 17  ? 14.909  59.490 -3.660  1.00 59.65  ?  172 GLU B C   1 
ATOM   2255 O O   . GLU B 1 17  ? 15.307  58.389 -3.262  1.00 60.38  ?  172 GLU B O   1 
ATOM   2256 C CB  . GLU B 1 17  ? 16.318  61.485 -3.496  1.00 61.17  ?  172 GLU B CB  1 
ATOM   2257 C CG  . GLU B 1 17  ? 17.241  62.522 -4.095  1.00 75.99  ?  172 GLU B CG  1 
ATOM   2258 C CD  . GLU B 1 17  ? 17.693  63.532 -3.061  1.00 106.49 ?  172 GLU B CD  1 
ATOM   2259 O OE1 . GLU B 1 17  ? 18.305  63.115 -2.047  1.00 94.59  ?  172 GLU B OE1 1 
ATOM   2260 O OE2 . GLU B 1 17  ? 17.400  64.738 -3.248  1.00 102.61 -1 172 GLU B OE2 1 
ATOM   2261 N N   . LEU B 1 18  ? 13.660  59.953 -3.447  1.00 51.47  ?  173 LEU B N   1 
ATOM   2262 C CA  . LEU B 1 18  ? 12.650  59.207 -2.702  1.00 49.70  ?  173 LEU B CA  1 
ATOM   2263 C C   . LEU B 1 18  ? 12.157  57.974 -3.432  1.00 50.09  ?  173 LEU B C   1 
ATOM   2264 O O   . LEU B 1 18  ? 11.770  56.998 -2.789  1.00 46.85  ?  173 LEU B O   1 
ATOM   2265 C CB  . LEU B 1 18  ? 11.509  60.107 -2.250  1.00 49.35  ?  173 LEU B CB  1 
ATOM   2266 C CG  . LEU B 1 18  ? 11.928  61.307 -1.423  1.00 52.65  ?  173 LEU B CG  1 
ATOM   2267 C CD1 . LEU B 1 18  ? 10.750  62.001 -0.925  1.00 52.48  ?  173 LEU B CD1 1 
ATOM   2268 C CD2 . LEU B 1 18  ? 12.795  60.910 -0.240  1.00 53.32  ?  173 LEU B CD2 1 
ATOM   2269 N N   . LYS B 1 19  ? 12.224  58.012 -4.776  1.00 47.37  ?  174 LYS B N   1 
ATOM   2270 C CA  . LYS B 1 19  ? 11.910  56.893 -5.643  1.00 47.86  ?  174 LYS B CA  1 
ATOM   2271 C C   . LYS B 1 19  ? 12.985  55.823 -5.361  1.00 51.32  ?  174 LYS B C   1 
ATOM   2272 O O   . LYS B 1 19  ? 12.654  54.656 -5.182  1.00 49.49  ?  174 LYS B O   1 
ATOM   2273 C CB  . LYS B 1 19  ? 11.959  57.340 -7.117  1.00 51.15  ?  174 LYS B CB  1 
ATOM   2274 C CG  . LYS B 1 19  ? 10.679  58.001 -7.623  1.00 78.37  ?  174 LYS B CG  1 
ATOM   2275 C CD  . LYS B 1 19  ? 9.963   57.104 -8.624  1.00 96.67  ?  174 LYS B CD  1 
ATOM   2276 C CE  . LYS B 1 19  ? 10.257  57.515 -10.046 1.00 106.74 ?  174 LYS B CE  1 
ATOM   2277 N NZ  . LYS B 1 19  ? 9.848   56.493 -11.055 1.00 110.74 1  174 LYS B NZ  1 
ATOM   2278 N N   . ASN B 1 20  ? 14.257  56.245 -5.237  1.00 50.21  ?  175 ASN B N   1 
ATOM   2279 C CA  . ASN B 1 20  ? 15.368  55.347 -4.931  1.00 52.09  ?  175 ASN B CA  1 
ATOM   2280 C C   . ASN B 1 20  ? 15.206  54.686 -3.559  1.00 62.35  ?  175 ASN B C   1 
ATOM   2281 O O   . ASN B 1 20  ? 15.194  53.443 -3.482  1.00 64.18  ?  175 ASN B O   1 
ATOM   2282 C CB  . ASN B 1 20  ? 16.725  56.056 -5.031  1.00 46.27  ?  175 ASN B CB  1 
ATOM   2283 C CG  . ASN B 1 20  ? 17.113  56.521 -6.407  1.00 72.32  ?  175 ASN B CG  1 
ATOM   2284 O OD1 . ASN B 1 20  ? 16.671  55.815 -7.463  1.00 68.00  ?  175 ASN B OD1 1 
ATOM   2285 N ND2 . ASN B 1 20  ? 17.867  57.491 -6.538  1.00 65.95  ?  175 ASN B ND2 1 
ATOM   2286 N N   . VAL B 1 21  ? 15.012  55.514 -2.496  1.00 59.49  ?  176 VAL B N   1 
ATOM   2287 C CA  . VAL B 1 21  ? 14.857  55.055 -1.113  1.00 59.57  ?  176 VAL B CA  1 
ATOM   2288 C C   . VAL B 1 21  ? 13.732  54.041 -0.888  1.00 63.89  ?  176 VAL B C   1 
ATOM   2289 O O   . VAL B 1 21  ? 13.909  53.123 -0.086  1.00 66.78  ?  176 VAL B O   1 
ATOM   2290 C CB  . VAL B 1 21  ? 14.904  56.180 -0.029  1.00 63.88  ?  176 VAL B CB  1 
ATOM   2291 C CG1 . VAL B 1 21  ? 16.029  57.175 -0.282  1.00 64.44  ?  176 VAL B CG1 1 
ATOM   2292 C CG2 . VAL B 1 21  ? 13.602  56.918 0.088   1.00 63.59  ?  176 VAL B CG2 1 
ATOM   2293 N N   . THR B 1 22  ? 12.620  54.167 -1.635  1.00 57.76  ?  177 THR B N   1 
ATOM   2294 C CA  . THR B 1 22  ? 11.413  53.349 -1.483  1.00 56.87  ?  177 THR B CA  1 
ATOM   2295 C C   . THR B 1 22  ? 11.265  52.210 -2.487  1.00 61.21  ?  177 THR B C   1 
ATOM   2296 O O   . THR B 1 22  ? 10.162  51.639 -2.599  1.00 60.14  ?  177 THR B O   1 
ATOM   2297 C CB  . THR B 1 22  ? 10.176  54.250 -1.521  1.00 55.91  ?  177 THR B CB  1 
ATOM   2298 O OG1 . THR B 1 22  ? 10.112  54.889 -2.796  1.00 52.33  ?  177 THR B OG1 1 
ATOM   2299 C CG2 . THR B 1 22  ? 10.152  55.267 -0.390  1.00 47.46  ?  177 THR B CG2 1 
ATOM   2300 N N   . ASN B 1 23  ? 12.363  51.878 -3.217  1.00 58.08  ?  178 ASN B N   1 
ATOM   2301 C CA  . ASN B 1 23  ? 12.400  50.824 -4.250  1.00 57.95  ?  178 ASN B CA  1 
ATOM   2302 C C   . ASN B 1 23  ? 11.334  51.151 -5.313  1.00 60.86  ?  178 ASN B C   1 
ATOM   2303 O O   . ASN B 1 23  ? 10.521  50.301 -5.697  1.00 61.29  ?  178 ASN B O   1 
ATOM   2304 C CB  . ASN B 1 23  ? 12.221  49.418 -3.621  1.00 60.54  ?  178 ASN B CB  1 
ATOM   2305 C CG  . ASN B 1 23  ? 12.614  48.280 -4.522  1.00 99.23  ?  178 ASN B CG  1 
ATOM   2306 O OD1 . ASN B 1 23  ? 13.780  48.117 -4.896  1.00 100.50 ?  178 ASN B OD1 1 
ATOM   2307 N ND2 . ASN B 1 23  ? 11.648  47.447 -4.861  1.00 92.90  ?  178 ASN B ND2 1 
ATOM   2308 N N   . ASN B 1 24  ? 11.323  52.438 -5.725  1.00 56.12  ?  179 ASN B N   1 
ATOM   2309 C CA  . ASN B 1 24  ? 10.398  53.068 -6.675  1.00 55.56  ?  179 ASN B CA  1 
ATOM   2310 C C   . ASN B 1 24  ? 8.945   52.898 -6.288  1.00 56.66  ?  179 ASN B C   1 
ATOM   2311 O O   . ASN B 1 24  ? 8.133   52.420 -7.083  1.00 57.06  ?  179 ASN B O   1 
ATOM   2312 C CB  . ASN B 1 24  ? 10.710  52.695 -8.116  1.00 61.01  ?  179 ASN B CB  1 
ATOM   2313 C CG  . ASN B 1 24  ? 11.992  53.345 -8.577  1.00 109.27 ?  179 ASN B CG  1 
ATOM   2314 O OD1 . ASN B 1 24  ? 11.984  54.454 -9.127  1.00 108.01 ?  179 ASN B OD1 1 
ATOM   2315 N ND2 . ASN B 1 24  ? 13.132  52.700 -8.307  1.00 105.15 ?  179 ASN B ND2 1 
ATOM   2316 N N   . PHE B 1 25  ? 8.632   53.288 -5.029  1.00 48.98  ?  180 PHE B N   1 
ATOM   2317 C CA  . PHE B 1 25  ? 7.305   53.213 -4.410  1.00 46.10  ?  180 PHE B CA  1 
ATOM   2318 C C   . PHE B 1 25  ? 6.612   51.850 -4.604  1.00 51.46  ?  180 PHE B C   1 
ATOM   2319 O O   . PHE B 1 25  ? 5.475   51.800 -5.064  1.00 50.64  ?  180 PHE B O   1 
ATOM   2320 C CB  . PHE B 1 25  ? 6.416   54.409 -4.819  1.00 45.34  ?  180 PHE B CB  1 
ATOM   2321 C CG  . PHE B 1 25  ? 6.993   55.749 -4.430  1.00 44.13  ?  180 PHE B CG  1 
ATOM   2322 C CD1 . PHE B 1 25  ? 6.859   56.234 -3.133  1.00 44.08  ?  180 PHE B CD1 1 
ATOM   2323 C CD2 . PHE B 1 25  ? 7.679   56.522 -5.356  1.00 43.43  ?  180 PHE B CD2 1 
ATOM   2324 C CE1 . PHE B 1 25  ? 7.400   57.468 -2.773  1.00 42.62  ?  180 PHE B CE1 1 
ATOM   2325 C CE2 . PHE B 1 25  ? 8.215   57.756 -4.991  1.00 44.06  ?  180 PHE B CE2 1 
ATOM   2326 C CZ  . PHE B 1 25  ? 8.066   58.220 -3.704  1.00 41.10  ?  180 PHE B CZ  1 
ATOM   2327 N N   . ASP B 1 26  ? 7.321   50.748 -4.261  1.00 49.79  ?  181 ASP B N   1 
ATOM   2328 C CA  . ASP B 1 26  ? 6.837   49.370 -4.342  1.00 50.70  ?  181 ASP B CA  1 
ATOM   2329 C C   . ASP B 1 26  ? 5.545   49.245 -3.519  1.00 57.09  ?  181 ASP B C   1 
ATOM   2330 O O   . ASP B 1 26  ? 5.532   49.520 -2.311  1.00 57.73  ?  181 ASP B O   1 
ATOM   2331 C CB  . ASP B 1 26  ? 7.926   48.391 -3.843  1.00 53.73  ?  181 ASP B CB  1 
ATOM   2332 C CG  . ASP B 1 26  ? 7.657   46.896 -3.992  1.00 76.72  ?  181 ASP B CG  1 
ATOM   2333 O OD1 . ASP B 1 26  ? 6.524   46.528 -4.398  1.00 77.74  ?  181 ASP B OD1 1 
ATOM   2334 O OD2 . ASP B 1 26  ? 8.583   46.087 -3.698  1.00 91.41  -1 181 ASP B OD2 1 
ATOM   2335 N N   . GLU B 1 27  ? 4.444   48.886 -4.198  1.00 53.84  ?  182 GLU B N   1 
ATOM   2336 C CA  . GLU B 1 27  ? 3.124   48.779 -3.583  1.00 53.19  ?  182 GLU B CA  1 
ATOM   2337 C C   . GLU B 1 27  ? 2.872   47.467 -2.844  1.00 55.98  ?  182 GLU B C   1 
ATOM   2338 O O   . GLU B 1 27  ? 1.833   47.320 -2.196  1.00 55.13  ?  182 GLU B O   1 
ATOM   2339 C CB  . GLU B 1 27  ? 2.013   49.144 -4.585  1.00 54.73  ?  182 GLU B CB  1 
ATOM   2340 C CG  . GLU B 1 27  ? 1.891   50.644 -4.846  1.00 68.67  ?  182 GLU B CG  1 
ATOM   2341 C CD  . GLU B 1 27  ? 0.649   51.334 -4.295  1.00 110.97 ?  182 GLU B CD  1 
ATOM   2342 O OE1 . GLU B 1 27  ? 0.225   52.345 -4.900  1.00 121.95 ?  182 GLU B OE1 1 
ATOM   2343 O OE2 . GLU B 1 27  ? 0.097   50.873 -3.268  1.00 108.77 -1 182 GLU B OE2 1 
ATOM   2344 N N   . ARG B 1 28  ? 3.833   46.527 -2.905  1.00 53.99  ?  183 ARG B N   1 
ATOM   2345 C CA  . ARG B 1 28  ? 3.754   45.241 -2.183  1.00 54.42  ?  183 ARG B CA  1 
ATOM   2346 C C   . ARG B 1 28  ? 3.922   45.512 -0.688  1.00 54.21  ?  183 ARG B C   1 
ATOM   2347 O O   . ARG B 1 28  ? 4.675   46.427 -0.336  1.00 53.18  ?  183 ARG B O   1 
ATOM   2348 C CB  . ARG B 1 28  ? 4.845   44.274 -2.653  1.00 59.20  ?  183 ARG B CB  1 
ATOM   2349 C CG  . ARG B 1 28  ? 4.369   43.220 -3.638  1.00 78.95  ?  183 ARG B CG  1 
ATOM   2350 C CD  . ARG B 1 28  ? 5.535   42.461 -4.259  1.00 101.87 ?  183 ARG B CD  1 
ATOM   2351 N NE  . ARG B 1 28  ? 6.266   41.626 -3.291  1.00 119.59 ?  183 ARG B NE  1 
ATOM   2352 C CZ  . ARG B 1 28  ? 7.455   41.933 -2.775  1.00 138.02 ?  183 ARG B CZ  1 
ATOM   2353 N NH1 . ARG B 1 28  ? 8.069   43.059 -3.124  1.00 128.42 ?  183 ARG B NH1 1 
ATOM   2354 N NH2 . ARG B 1 28  ? 8.043   41.112 -1.914  1.00 122.41 1  183 ARG B NH2 1 
ATOM   2355 N N   . PRO B 1 29  ? 3.217   44.774 0.200   1.00 48.78  ?  184 PRO B N   1 
ATOM   2356 C CA  . PRO B 1 29  ? 3.332   45.055 1.642   1.00 48.33  ?  184 PRO B CA  1 
ATOM   2357 C C   . PRO B 1 29  ? 4.698   44.700 2.198   1.00 53.10  ?  184 PRO B C   1 
ATOM   2358 O O   . PRO B 1 29  ? 5.369   43.782 1.699   1.00 53.86  ?  184 PRO B O   1 
ATOM   2359 C CB  . PRO B 1 29  ? 2.233   44.191 2.273   1.00 49.97  ?  184 PRO B CB  1 
ATOM   2360 C CG  . PRO B 1 29  ? 1.355   43.778 1.142   1.00 54.36  ?  184 PRO B CG  1 
ATOM   2361 C CD  . PRO B 1 29  ? 2.268   43.674 -0.042  1.00 49.87  ?  184 PRO B CD  1 
ATOM   2362 N N   . ILE B 1 30  ? 5.106   45.439 3.234   1.00 47.91  ?  185 ILE B N   1 
ATOM   2363 C CA  . ILE B 1 30  ? 6.380   45.243 3.908   1.00 47.69  ?  185 ILE B CA  1 
ATOM   2364 C C   . ILE B 1 30  ? 6.502   43.838 4.506   1.00 53.30  ?  185 ILE B C   1 
ATOM   2365 O O   . ILE B 1 30  ? 7.616   43.313 4.568   1.00 56.48  ?  185 ILE B O   1 
ATOM   2366 C CB  . ILE B 1 30  ? 6.720   46.357 4.935   1.00 50.07  ?  185 ILE B CB  1 
ATOM   2367 C CG1 . ILE B 1 30  ? 5.514   46.689 5.858   1.00 49.42  ?  185 ILE B CG1 1 
ATOM   2368 C CG2 . ILE B 1 30  ? 7.268   47.590 4.233   1.00 49.94  ?  185 ILE B CG2 1 
ATOM   2369 C CD1 . ILE B 1 30  ? 5.836   46.873 7.312   1.00 43.74  ?  185 ILE B CD1 1 
ATOM   2370 N N   . SER B 1 31  ? 5.365   43.229 4.902   1.00 48.59  ?  186 SER B N   1 
ATOM   2371 C CA  . SER B 1 31  ? 5.239   41.866 5.470   1.00 49.15  ?  186 SER B CA  1 
ATOM   2372 C C   . SER B 1 31  ? 5.665   40.769 4.471   1.00 54.70  ?  186 SER B C   1 
ATOM   2373 O O   . SER B 1 31  ? 5.980   39.656 4.873   1.00 54.09  ?  186 SER B O   1 
ATOM   2374 C CB  . SER B 1 31  ? 3.797   41.608 5.913   1.00 51.35  ?  186 SER B CB  1 
ATOM   2375 O OG  . SER B 1 31  ? 2.894   41.754 4.826   1.00 55.29  ?  186 SER B OG  1 
ATOM   2376 N N   . VAL B 1 32  ? 5.632   41.101 3.174   1.00 53.46  ?  187 VAL B N   1 
ATOM   2377 C CA  . VAL B 1 32  ? 5.912   40.237 2.030   1.00 53.25  ?  187 VAL B CA  1 
ATOM   2378 C C   . VAL B 1 32  ? 7.275   40.582 1.390   1.00 56.22  ?  187 VAL B C   1 
ATOM   2379 O O   . VAL B 1 32  ? 7.755   39.845 0.514   1.00 55.75  ?  187 VAL B O   1 
ATOM   2380 C CB  . VAL B 1 32  ? 4.662   40.344 1.090   1.00 57.33  ?  187 VAL B CB  1 
ATOM   2381 C CG1 . VAL B 1 32  ? 4.976   40.180 -0.395  1.00 57.59  ?  187 VAL B CG1 1 
ATOM   2382 C CG2 . VAL B 1 32  ? 3.590   39.363 1.537   1.00 56.97  ?  187 VAL B CG2 1 
ATOM   2383 N N   . GLY B 1 33  ? 7.898   41.656 1.890   1.00 51.84  ?  188 GLY B N   1 
ATOM   2384 C CA  . GLY B 1 33  ? 9.188   42.148 1.423   1.00 52.26  ?  188 GLY B CA  1 
ATOM   2385 C C   . GLY B 1 33  ? 9.094   43.367 0.517   1.00 57.53  ?  188 GLY B C   1 
ATOM   2386 O O   . GLY B 1 33  ? 10.096  43.764 -0.096  1.00 56.65  ?  188 GLY B O   1 
ATOM   2387 N N   . GLY B 1 34  ? 7.890   43.946 0.424   1.00 54.49  ?  189 GLY B N   1 
ATOM   2388 C CA  . GLY B 1 34  ? 7.628   45.136 -0.380  1.00 54.11  ?  189 GLY B CA  1 
ATOM   2389 C C   . GLY B 1 34  ? 7.878   46.407 0.399   1.00 56.97  ?  189 GLY B C   1 
ATOM   2390 O O   . GLY B 1 34  ? 8.547   46.370 1.447   1.00 55.52  ?  189 GLY B O   1 
ATOM   2391 N N   . ASN B 1 35  ? 7.311   47.537 -0.086  1.00 52.07  ?  190 ASN B N   1 
ATOM   2392 C CA  . ASN B 1 35  ? 7.514   48.812 0.588   1.00 50.72  ?  190 ASN B CA  1 
ATOM   2393 C C   . ASN B 1 35  ? 6.291   49.435 1.227   1.00 50.26  ?  190 ASN B C   1 
ATOM   2394 O O   . ASN B 1 35  ? 6.466   50.247 2.134   1.00 50.41  ?  190 ASN B O   1 
ATOM   2395 C CB  . ASN B 1 35  ? 8.295   49.795 -0.294  1.00 52.67  ?  190 ASN B CB  1 
ATOM   2396 C CG  . ASN B 1 35  ? 9.738   49.394 -0.487  1.00 66.29  ?  190 ASN B CG  1 
ATOM   2397 O OD1 . ASN B 1 35  ? 10.067  48.410 -1.163  1.00 60.40  ?  190 ASN B OD1 1 
ATOM   2398 N ND2 . ASN B 1 35  ? 10.628  50.159 0.088   1.00 55.10  ?  190 ASN B ND2 1 
ATOM   2399 N N   . LYS B 1 36  ? 5.071   49.046 0.802   1.00 43.93  ?  191 LYS B N   1 
ATOM   2400 C CA  . LYS B 1 36  ? 3.819   49.606 1.328   1.00 43.14  ?  191 LYS B CA  1 
ATOM   2401 C C   . LYS B 1 36  ? 3.570   49.264 2.796   1.00 48.89  ?  191 LYS B C   1 
ATOM   2402 O O   . LYS B 1 36  ? 3.575   48.082 3.168   1.00 49.85  ?  191 LYS B O   1 
ATOM   2403 C CB  . LYS B 1 36  ? 2.617   49.219 0.451   1.00 44.60  ?  191 LYS B CB  1 
ATOM   2404 C CG  . LYS B 1 36  ? 1.328   49.963 0.809   1.00 61.78  ?  191 LYS B CG  1 
ATOM   2405 C CD  . LYS B 1 36  ? 0.179   49.591 -0.096  1.00 76.21  ?  191 LYS B CD  1 
ATOM   2406 C CE  . LYS B 1 36  ? -1.113  50.253 0.345   1.00 91.99  ?  191 LYS B CE  1 
ATOM   2407 N NZ  . LYS B 1 36  ? -2.272  49.818 -0.485  1.00 92.28  1  191 LYS B NZ  1 
ATOM   2408 N N   . MET B 1 37  ? 3.342   50.303 3.628   1.00 44.71  ?  192 MET B N   1 
ATOM   2409 C CA  . MET B 1 37  ? 3.087   50.115 5.059   1.00 45.41  ?  192 MET B CA  1 
ATOM   2410 C C   . MET B 1 37  ? 1.615   50.343 5.437   1.00 54.03  ?  192 MET B C   1 
ATOM   2411 O O   . MET B 1 37  ? 1.137   49.806 6.433   1.00 55.50  ?  192 MET B O   1 
ATOM   2412 C CB  . MET B 1 37  ? 4.026   50.981 5.920   1.00 47.05  ?  192 MET B CB  1 
ATOM   2413 C CG  . MET B 1 37  ? 5.495   50.612 5.761   1.00 49.80  ?  192 MET B CG  1 
ATOM   2414 S SD  . MET B 1 37  ? 6.589   51.289 7.027   1.00 53.28  ?  192 MET B SD  1 
ATOM   2415 C CE  . MET B 1 37  ? 6.513   53.017 6.675   1.00 48.84  ?  192 MET B CE  1 
ATOM   2416 N N   . GLY B 1 38  ? 0.920   51.127 4.638   1.00 51.61  ?  193 GLY B N   1 
ATOM   2417 C CA  . GLY B 1 38  ? -0.472  51.460 4.872   1.00 52.65  ?  193 GLY B CA  1 
ATOM   2418 C C   . GLY B 1 38  ? -0.923  52.658 4.066   1.00 60.30  ?  193 GLY B C   1 
ATOM   2419 O O   . GLY B 1 38  ? -0.121  53.282 3.360   1.00 58.15  ?  193 GLY B O   1 
ATOM   2420 N N   . GLU B 1 39  ? -2.220  52.973 4.171   1.00 62.04  ?  194 GLU B N   1 
ATOM   2421 C CA  . GLU B 1 39  ? -2.839  54.076 3.436   1.00 64.57  ?  194 GLU B CA  1 
ATOM   2422 C C   . GLU B 1 39  ? -4.055  54.699 4.096   1.00 71.87  ?  194 GLU B C   1 
ATOM   2423 O O   . GLU B 1 39  ? -4.926  53.994 4.603   1.00 70.44  ?  194 GLU B O   1 
ATOM   2424 C CB  . GLU B 1 39  ? -3.174  53.687 1.977   1.00 66.16  ?  194 GLU B CB  1 
ATOM   2425 C CG  . GLU B 1 39  ? -4.046  52.456 1.803   1.00 76.55  ?  194 GLU B CG  1 
ATOM   2426 C CD  . GLU B 1 39  ? -4.665  52.339 0.425   1.00 110.89 ?  194 GLU B CD  1 
ATOM   2427 O OE1 . GLU B 1 39  ? -5.902  52.506 0.312   1.00 126.11 ?  194 GLU B OE1 1 
ATOM   2428 O OE2 . GLU B 1 39  ? -3.915  52.083 -0.544  1.00 101.63 -1 194 GLU B OE2 1 
ATOM   2429 N N   . GLY B 1 40  ? -4.099  56.023 4.038   1.00 72.55  ?  195 GLY B N   1 
ATOM   2430 C CA  . GLY B 1 40  ? -5.207  56.841 4.507   1.00 74.05  ?  195 GLY B CA  1 
ATOM   2431 C C   . GLY B 1 40  ? -5.942  57.464 3.332   1.00 80.68  ?  195 GLY B C   1 
ATOM   2432 O O   . GLY B 1 40  ? -5.800  57.018 2.178   1.00 80.26  ?  195 GLY B O   1 
ATOM   2433 N N   . GLY B 1 41  ? -6.720  58.500 3.638   1.00 77.61  ?  196 GLY B N   1 
ATOM   2434 C CA  . GLY B 1 41  ? -7.472  59.256 2.646   1.00 76.94  ?  196 GLY B CA  1 
ATOM   2435 C C   . GLY B 1 41  ? -6.605  60.246 1.891   1.00 78.81  ?  196 GLY B C   1 
ATOM   2436 O O   . GLY B 1 41  ? -6.864  60.534 0.718   1.00 78.46  ?  196 GLY B O   1 
ATOM   2437 N N   . PHE B 1 42  ? -5.568  60.772 2.564   1.00 73.73  ?  197 PHE B N   1 
ATOM   2438 C CA  . PHE B 1 42  ? -4.635  61.753 2.006   1.00 72.60  ?  197 PHE B CA  1 
ATOM   2439 C C   . PHE B 1 42  ? -3.316  61.179 1.444   1.00 73.06  ?  197 PHE B C   1 
ATOM   2440 O O   . PHE B 1 42  ? -2.481  61.963 0.985   1.00 73.34  ?  197 PHE B O   1 
ATOM   2441 C CB  . PHE B 1 42  ? -4.381  62.897 3.011   1.00 74.43  ?  197 PHE B CB  1 
ATOM   2442 N N   . GLY B 1 43  ? -3.153  59.847 1.441   1.00 66.15  ?  198 GLY B N   1 
ATOM   2443 C CA  . GLY B 1 43  ? -1.943  59.224 0.907   1.00 64.42  ?  198 GLY B CA  1 
ATOM   2444 C C   . GLY B 1 43  ? -1.590  57.819 1.363   1.00 62.73  ?  198 GLY B C   1 
ATOM   2445 O O   . GLY B 1 43  ? -2.268  57.253 2.225   1.00 63.43  ?  198 GLY B O   1 
ATOM   2446 N N   . VAL B 1 44  ? -0.507  57.256 0.766   1.00 52.16  ?  199 VAL B N   1 
ATOM   2447 C CA  . VAL B 1 44  ? 0.055   55.925 1.045   1.00 49.11  ?  199 VAL B CA  1 
ATOM   2448 C C   . VAL B 1 44  ? 1.444   56.114 1.706   1.00 49.28  ?  199 VAL B C   1 
ATOM   2449 O O   . VAL B 1 44  ? 2.229   56.963 1.275   1.00 49.28  ?  199 VAL B O   1 
ATOM   2450 C CB  . VAL B 1 44  ? 0.132   55.009 -0.230  1.00 52.22  ?  199 VAL B CB  1 
ATOM   2451 C CG1 . VAL B 1 44  ? 0.736   53.627 0.068   1.00 51.56  ?  199 VAL B CG1 1 
ATOM   2452 C CG2 . VAL B 1 44  ? -1.225  54.850 -0.873  1.00 51.83  ?  199 VAL B CG2 1 
ATOM   2453 N N   . VAL B 1 45  ? 1.737   55.303 2.751   1.00 42.50  ?  200 VAL B N   1 
ATOM   2454 C CA  . VAL B 1 45  ? 2.994   55.356 3.490   1.00 40.24  ?  200 VAL B CA  1 
ATOM   2455 C C   . VAL B 1 45  ? 3.893   54.194 3.073   1.00 44.31  ?  200 VAL B C   1 
ATOM   2456 O O   . VAL B 1 45  ? 3.454   53.039 3.068   1.00 43.95  ?  200 VAL B O   1 
ATOM   2457 C CB  . VAL B 1 45  ? 2.782   55.470 5.032   1.00 41.86  ?  200 VAL B CB  1 
ATOM   2458 C CG1 . VAL B 1 45  ? 4.114   55.714 5.773   1.00 40.83  ?  200 VAL B CG1 1 
ATOM   2459 C CG2 . VAL B 1 45  ? 1.769   56.581 5.369   1.00 40.63  ?  200 VAL B CG2 1 
ATOM   2460 N N   . TYR B 1 46  ? 5.146   54.517 2.695   1.00 41.78  ?  201 TYR B N   1 
ATOM   2461 C CA  . TYR B 1 46  ? 6.171   53.563 2.256   1.00 42.72  ?  201 TYR B CA  1 
ATOM   2462 C C   . TYR B 1 46  ? 7.382   53.521 3.190   1.00 45.61  ?  201 TYR B C   1 
ATOM   2463 O O   . TYR B 1 46  ? 7.770   54.546 3.751   1.00 45.44  ?  201 TYR B O   1 
ATOM   2464 C CB  . TYR B 1 46  ? 6.671   53.899 0.833   1.00 45.29  ?  201 TYR B CB  1 
ATOM   2465 C CG  . TYR B 1 46  ? 5.575   53.922 -0.205  1.00 50.67  ?  201 TYR B CG  1 
ATOM   2466 C CD1 . TYR B 1 46  ? 4.823   55.079 -0.431  1.00 53.60  ?  201 TYR B CD1 1 
ATOM   2467 C CD2 . TYR B 1 46  ? 5.280   52.787 -0.960  1.00 52.21  ?  201 TYR B CD2 1 
ATOM   2468 C CE1 . TYR B 1 46  ? 3.791   55.097 -1.367  1.00 56.13  ?  201 TYR B CE1 1 
ATOM   2469 C CE2 . TYR B 1 46  ? 4.256   52.796 -1.905  1.00 53.79  ?  201 TYR B CE2 1 
ATOM   2470 C CZ  . TYR B 1 46  ? 3.518   53.954 -2.107  1.00 64.43  ?  201 TYR B CZ  1 
ATOM   2471 O OH  . TYR B 1 46  ? 2.514   53.963 -3.040  1.00 68.78  ?  201 TYR B OH  1 
ATOM   2472 N N   . LYS B 1 47  ? 8.024   52.353 3.295   1.00 40.82  ?  202 LYS B N   1 
ATOM   2473 C CA  . LYS B 1 47  ? 9.271   52.183 4.053   1.00 40.14  ?  202 LYS B CA  1 
ATOM   2474 C C   . LYS B 1 47  ? 10.462  52.516 3.127   1.00 44.54  ?  202 LYS B C   1 
ATOM   2475 O O   . LYS B 1 47  ? 10.409  52.311 1.921   1.00 43.67  ?  202 LYS B O   1 
ATOM   2476 C CB  . LYS B 1 47  ? 9.384   50.729 4.567   1.00 41.28  ?  202 LYS B CB  1 
ATOM   2477 C CG  . LYS B 1 47  ? 10.392  50.484 5.671   1.00 35.41  ?  202 LYS B CG  1 
ATOM   2478 C CD  . LYS B 1 47  ? 10.413  48.993 6.048   1.00 30.06  ?  202 LYS B CD  1 
ATOM   2479 C CE  . LYS B 1 47  ? 11.539  48.654 6.990   1.00 36.06  ?  202 LYS B CE  1 
ATOM   2480 N NZ  . LYS B 1 47  ? 11.581  47.210 7.337   1.00 52.09  1  202 LYS B NZ  1 
ATOM   2481 N N   . GLY B 1 48  ? 11.540  52.987 3.695   1.00 42.62  ?  203 GLY B N   1 
ATOM   2482 C CA  . GLY B 1 48  ? 12.738  53.254 2.924   1.00 41.85  ?  203 GLY B CA  1 
ATOM   2483 C C   . GLY B 1 48  ? 13.942  53.411 3.807   1.00 47.07  ?  203 GLY B C   1 
ATOM   2484 O O   . GLY B 1 48  ? 13.860  53.261 5.027   1.00 47.03  ?  203 GLY B O   1 
ATOM   2485 N N   . TYR B 1 49  ? 15.066  53.729 3.190   1.00 45.25  ?  204 TYR B N   1 
ATOM   2486 C CA  . TYR B 1 49  ? 16.303  53.982 3.904   1.00 44.86  ?  204 TYR B CA  1 
ATOM   2487 C C   . TYR B 1 49  ? 16.976  55.247 3.351   1.00 46.83  ?  204 TYR B C   1 
ATOM   2488 O O   . TYR B 1 49  ? 17.137  55.387 2.141   1.00 46.24  ?  204 TYR B O   1 
ATOM   2489 C CB  . TYR B 1 49  ? 17.241  52.760 3.808   1.00 46.33  ?  204 TYR B CB  1 
ATOM   2490 C CG  . TYR B 1 49  ? 16.721  51.508 4.495   1.00 46.94  ?  204 TYR B CG  1 
ATOM   2491 C CD1 . TYR B 1 49  ? 16.759  51.383 5.884   1.00 48.74  ?  204 TYR B CD1 1 
ATOM   2492 C CD2 . TYR B 1 49  ? 16.233  50.433 3.756   1.00 46.55  ?  204 TYR B CD2 1 
ATOM   2493 C CE1 . TYR B 1 49  ? 16.276  50.238 6.524   1.00 48.74  ?  204 TYR B CE1 1 
ATOM   2494 C CE2 . TYR B 1 49  ? 15.741  49.286 4.384   1.00 47.18  ?  204 TYR B CE2 1 
ATOM   2495 C CZ  . TYR B 1 49  ? 15.778  49.185 5.771   1.00 55.53  ?  204 TYR B CZ  1 
ATOM   2496 O OH  . TYR B 1 49  ? 15.328  48.049 6.416   1.00 56.16  ?  204 TYR B OH  1 
ATOM   2497 N N   . VAL B 1 50  ? 17.308  56.186 4.228   1.00 41.78  ?  205 VAL B N   1 
ATOM   2498 C CA  . VAL B 1 50  ? 18.065  57.365 3.842   1.00 41.33  ?  205 VAL B CA  1 
ATOM   2499 C C   . VAL B 1 50  ? 19.372  57.138 4.601   1.00 46.41  ?  205 VAL B C   1 
ATOM   2500 O O   . VAL B 1 50  ? 19.417  57.300 5.815   1.00 46.61  ?  205 VAL B O   1 
ATOM   2501 C CB  . VAL B 1 50  ? 17.343  58.704 4.109   1.00 44.73  ?  205 VAL B CB  1 
ATOM   2502 C CG1 . VAL B 1 50  ? 18.259  59.883 3.801   1.00 44.12  ?  205 VAL B CG1 1 
ATOM   2503 C CG2 . VAL B 1 50  ? 16.069  58.805 3.273   1.00 44.81  ?  205 VAL B CG2 1 
ATOM   2504 N N   . ASN B 1 51  ? 20.383  56.625 3.876   1.00 42.89  ?  206 ASN B N   1 
ATOM   2505 C CA  . ASN B 1 51  ? 21.684  56.126 4.343   1.00 42.19  ?  206 ASN B CA  1 
ATOM   2506 C C   . ASN B 1 51  ? 21.384  54.813 5.053   1.00 46.06  ?  206 ASN B C   1 
ATOM   2507 O O   . ASN B 1 51  ? 20.946  53.846 4.414   1.00 45.17  ?  206 ASN B O   1 
ATOM   2508 C CB  . ASN B 1 51  ? 22.452  57.121 5.227   1.00 39.56  ?  206 ASN B CB  1 
ATOM   2509 C CG  . ASN B 1 51  ? 22.939  58.338 4.474   1.00 67.60  ?  206 ASN B CG  1 
ATOM   2510 O OD1 . ASN B 1 51  ? 22.495  59.484 4.707   1.00 54.70  ?  206 ASN B OD1 1 
ATOM   2511 N ND2 . ASN B 1 51  ? 23.862  58.111 3.547   1.00 63.86  ?  206 ASN B ND2 1 
ATOM   2512 N N   . ASN B 1 52  ? 21.563  54.790 6.365   1.00 42.59  ?  207 ASN B N   1 
ATOM   2513 C CA  . ASN B 1 52  ? 21.229  53.621 7.175   1.00 41.18  ?  207 ASN B CA  1 
ATOM   2514 C C   . ASN B 1 52  ? 19.978  53.902 8.017   1.00 41.51  ?  207 ASN B C   1 
ATOM   2515 O O   . ASN B 1 52  ? 19.455  53.006 8.650   1.00 44.96  ?  207 ASN B O   1 
ATOM   2516 C CB  . ASN B 1 52  ? 22.434  53.164 8.011   1.00 39.76  ?  207 ASN B CB  1 
ATOM   2517 C CG  . ASN B 1 52  ? 23.530  52.485 7.212   1.00 49.77  ?  207 ASN B CG  1 
ATOM   2518 O OD1 . ASN B 1 52  ? 23.389  52.143 6.040   1.00 35.75  ?  207 ASN B OD1 1 
ATOM   2519 N ND2 . ASN B 1 52  ? 24.623  52.176 7.861   1.00 48.79  ?  207 ASN B ND2 1 
ATOM   2520 N N   . THR B 1 53  ? 19.456  55.121 7.924   1.00 33.55  ?  208 THR B N   1 
ATOM   2521 C CA  . THR B 1 53  ? 18.270  55.603 8.603   1.00 31.92  ?  208 THR B CA  1 
ATOM   2522 C C   . THR B 1 53  ? 17.021  55.057 7.915   1.00 37.57  ?  208 THR B C   1 
ATOM   2523 O O   . THR B 1 53  ? 16.702  55.457 6.791   1.00 37.23  ?  208 THR B O   1 
ATOM   2524 C CB  . THR B 1 53  ? 18.331  57.167 8.675   1.00 30.54  ?  208 THR B CB  1 
ATOM   2525 O OG1 . THR B 1 53  ? 19.491  57.560 9.431   1.00 43.96  ?  208 THR B OG1 1 
ATOM   2526 C CG2 . THR B 1 53  ? 17.110  57.795 9.291   1.00 13.25  ?  208 THR B CG2 1 
ATOM   2527 N N   . THR B 1 54  ? 16.291  54.160 8.611   1.00 36.00  ?  209 THR B N   1 
ATOM   2528 C CA  . THR B 1 54  ? 14.995  53.651 8.130   1.00 36.48  ?  209 THR B CA  1 
ATOM   2529 C C   . THR B 1 54  ? 13.998  54.829 8.180   1.00 40.68  ?  209 THR B C   1 
ATOM   2530 O O   . THR B 1 54  ? 13.924  55.571 9.187   1.00 40.83  ?  209 THR B O   1 
ATOM   2531 C CB  . THR B 1 54  ? 14.492  52.450 8.951   1.00 39.85  ?  209 THR B CB  1 
ATOM   2532 O OG1 . THR B 1 54  ? 15.574  51.556 9.193   1.00 45.99  ?  209 THR B OG1 1 
ATOM   2533 C CG2 . THR B 1 54  ? 13.359  51.718 8.269   1.00 31.48  ?  209 THR B CG2 1 
ATOM   2534 N N   . VAL B 1 55  ? 13.289  55.026 7.075   1.00 36.37  ?  210 VAL B N   1 
ATOM   2535 C CA  . VAL B 1 55  ? 12.331  56.130 6.962   1.00 36.42  ?  210 VAL B CA  1 
ATOM   2536 C C   . VAL B 1 55  ? 10.905  55.677 6.625   1.00 40.04  ?  210 VAL B C   1 
ATOM   2537 O O   . VAL B 1 55  ? 10.699  54.581 6.055   1.00 37.68  ?  210 VAL B O   1 
ATOM   2538 C CB  . VAL B 1 55  ? 12.813  57.283 5.992   1.00 38.72  ?  210 VAL B CB  1 
ATOM   2539 C CG1 . VAL B 1 55  ? 14.088  57.948 6.488   1.00 38.36  ?  210 VAL B CG1 1 
ATOM   2540 C CG2 . VAL B 1 55  ? 12.973  56.806 4.548   1.00 37.73  ?  210 VAL B CG2 1 
ATOM   2541 N N   . ALA B 1 56  ? 9.926   56.568 6.955   1.00 37.65  ?  211 ALA B N   1 
ATOM   2542 C CA  . ALA B 1 56  ? 8.520   56.431 6.536   1.00 37.40  ?  211 ALA B CA  1 
ATOM   2543 C C   . ALA B 1 56  ? 8.263   57.561 5.526   1.00 42.91  ?  211 ALA B C   1 
ATOM   2544 O O   . ALA B 1 56  ? 8.504   58.735 5.829   1.00 42.91  ?  211 ALA B O   1 
ATOM   2545 C CB  . ALA B 1 56  ? 7.578   56.537 7.713   1.00 37.71  ?  211 ALA B CB  1 
ATOM   2546 N N   . VAL B 1 57  ? 7.885   57.206 4.302   1.00 41.16  ?  212 VAL B N   1 
ATOM   2547 C CA  . VAL B 1 57  ? 7.629   58.209 3.267   1.00 41.84  ?  212 VAL B CA  1 
ATOM   2548 C C   . VAL B 1 57  ? 6.135   58.250 2.964   1.00 47.16  ?  212 VAL B C   1 
ATOM   2549 O O   . VAL B 1 57  ? 5.579   57.273 2.443   1.00 48.46  ?  212 VAL B O   1 
ATOM   2550 C CB  . VAL B 1 57  ? 8.501   58.028 1.991   1.00 45.30  ?  212 VAL B CB  1 
ATOM   2551 C CG1 . VAL B 1 57  ? 8.282   59.177 1.009   1.00 44.87  ?  212 VAL B CG1 1 
ATOM   2552 C CG2 . VAL B 1 57  ? 9.985   57.917 2.351   1.00 45.03  ?  212 VAL B CG2 1 
ATOM   2553 N N   . LYS B 1 58  ? 5.483   59.369 3.314   1.00 41.48  ?  213 LYS B N   1 
ATOM   2554 C CA  . LYS B 1 58  ? 4.063   59.537 3.029   1.00 40.18  ?  213 LYS B CA  1 
ATOM   2555 C C   . LYS B 1 58  ? 3.915   60.246 1.678   1.00 44.79  ?  213 LYS B C   1 
ATOM   2556 O O   . LYS B 1 58  ? 4.283   61.413 1.559   1.00 44.17  ?  213 LYS B O   1 
ATOM   2557 C CB  . LYS B 1 58  ? 3.397   60.345 4.138   1.00 40.81  ?  213 LYS B CB  1 
ATOM   2558 C CG  . LYS B 1 58  ? 1.872   60.263 4.134   1.00 35.07  ?  213 LYS B CG  1 
ATOM   2559 C CD  . LYS B 1 58  ? 1.321   61.559 4.701   1.00 40.41  ?  213 LYS B CD  1 
ATOM   2560 C CE  . LYS B 1 58  ? 0.637   61.463 6.031   1.00 48.64  ?  213 LYS B CE  1 
ATOM   2561 N NZ  . LYS B 1 58  ? 0.451   62.827 6.629   1.00 71.71  1  213 LYS B NZ  1 
ATOM   2562 N N   . LYS B 1 59  ? 3.456   59.515 0.649   1.00 42.95  ?  214 LYS B N   1 
ATOM   2563 C CA  . LYS B 1 59  ? 3.230   60.070 -0.693  1.00 43.25  ?  214 LYS B CA  1 
ATOM   2564 C C   . LYS B 1 59  ? 1.769   60.512 -0.753  1.00 50.69  ?  214 LYS B C   1 
ATOM   2565 O O   . LYS B 1 59  ? 0.864   59.670 -0.779  1.00 49.04  ?  214 LYS B O   1 
ATOM   2566 C CB  . LYS B 1 59  ? 3.566   59.062 -1.808  1.00 44.76  ?  214 LYS B CB  1 
ATOM   2567 C CG  . LYS B 1 59  ? 3.707   59.712 -3.184  1.00 55.54  ?  214 LYS B CG  1 
ATOM   2568 C CD  . LYS B 1 59  ? 3.923   58.679 -4.301  1.00 69.51  ?  214 LYS B CD  1 
ATOM   2569 C CE  . LYS B 1 59  ? 2.629   58.164 -4.886  1.00 90.20  ?  214 LYS B CE  1 
ATOM   2570 N NZ  . LYS B 1 59  ? 2.849   57.011 -5.801  1.00 104.32 1  214 LYS B NZ  1 
ATOM   2571 N N   . LEU B 1 60  ? 1.553   61.842 -0.705  1.00 51.21  ?  215 LEU B N   1 
ATOM   2572 C CA  . LEU B 1 60  ? 0.241   62.483 -0.707  1.00 52.94  ?  215 LEU B CA  1 
ATOM   2573 C C   . LEU B 1 60  ? -0.547  62.196 -1.980  1.00 62.13  ?  215 LEU B C   1 
ATOM   2574 O O   . LEU B 1 60  ? -0.018  62.321 -3.092  1.00 63.10  ?  215 LEU B O   1 
ATOM   2575 C CB  . LEU B 1 60  ? 0.374   64.002 -0.474  1.00 52.90  ?  215 LEU B CB  1 
ATOM   2576 C CG  . LEU B 1 60  ? 0.201   64.529 0.952   1.00 57.60  ?  215 LEU B CG  1 
ATOM   2577 C CD1 . LEU B 1 60  ? 1.277   64.025 1.856   1.00 57.90  ?  215 LEU B CD1 1 
ATOM   2578 C CD2 . LEU B 1 60  ? 0.261   66.034 0.975   1.00 61.03  ?  215 LEU B CD2 1 
ATOM   2579 N N   . ALA B 1 61  ? -1.805  61.759 -1.801  1.00 60.47  ?  216 ALA B N   1 
ATOM   2580 C CA  . ALA B 1 61  ? -2.726  61.431 -2.894  1.00 60.95  ?  216 ALA B CA  1 
ATOM   2581 C C   . ALA B 1 61  ? -4.130  61.947 -2.591  1.00 68.48  ?  216 ALA B C   1 
ATOM   2582 O O   . ALA B 1 61  ? -4.632  61.762 -1.474  1.00 69.39  ?  216 ALA B O   1 
ATOM   2583 C CB  . ALA B 1 61  ? -2.758  59.930 -3.110  1.00 61.57  ?  216 ALA B CB  1 
ATOM   2584 N N   . ALA B 1 62  ? -4.766  62.604 -3.578  1.00 66.42  ?  217 ALA B N   1 
ATOM   2585 C CA  . ALA B 1 62  ? -6.129  63.146 -3.432  1.00 93.21  ?  217 ALA B CA  1 
ATOM   2586 C C   . ALA B 1 62  ? -7.180  62.112 -3.827  1.00 94.12  ?  217 ALA B C   1 
ATOM   2587 O O   . ALA B 1 62  ? -7.156  60.983 -3.339  1.00 59.65  ?  217 ALA B O   1 
ATOM   2588 C CB  . ALA B 1 62  ? -6.295  64.406 -4.266  1.00 93.92  ?  217 ALA B CB  1 
ATOM   2589 N N   . THR B 1 67  ? -9.072  68.131 -3.588  1.00 81.09  ?  222 THR B N   1 
ATOM   2590 C CA  . THR B 1 67  ? -8.666  69.445 -4.104  1.00 82.07  ?  222 THR B CA  1 
ATOM   2591 C C   . THR B 1 67  ? -7.156  69.632 -4.030  1.00 87.73  ?  222 THR B C   1 
ATOM   2592 O O   . THR B 1 67  ? -6.588  69.538 -2.938  1.00 88.92  ?  222 THR B O   1 
ATOM   2593 C CB  . THR B 1 67  ? -9.363  70.610 -3.361  1.00 96.03  ?  222 THR B CB  1 
ATOM   2594 O OG1 . THR B 1 67  ? -10.008 70.166 -2.155  1.00 97.74  ?  222 THR B OG1 1 
ATOM   2595 C CG2 . THR B 1 67  ? -10.316 71.397 -4.257  1.00 95.00  ?  222 THR B CG2 1 
ATOM   2596 N N   . THR B 1 68  ? -6.508  69.928 -5.179  1.00 83.11  ?  223 THR B N   1 
ATOM   2597 C CA  . THR B 1 68  ? -5.059  70.139 -5.277  1.00 81.86  ?  223 THR B CA  1 
ATOM   2598 C C   . THR B 1 68  ? -4.589  71.292 -4.390  1.00 83.83  ?  223 THR B C   1 
ATOM   2599 O O   . THR B 1 68  ? -3.551  71.169 -3.741  1.00 83.26  ?  223 THR B O   1 
ATOM   2600 C CB  . THR B 1 68  ? -4.606  70.160 -6.754  1.00 87.69  ?  223 THR B CB  1 
ATOM   2601 O OG1 . THR B 1 68  ? -4.554  68.809 -7.225  1.00 85.20  ?  223 THR B OG1 1 
ATOM   2602 C CG2 . THR B 1 68  ? -3.237  70.827 -6.969  1.00 84.98  ?  223 THR B CG2 1 
ATOM   2603 N N   . GLU B 1 69  ? -5.378  72.378 -4.320  1.00 80.09  ?  224 GLU B N   1 
ATOM   2604 C CA  . GLU B 1 69  ? -5.079  73.548 -3.483  1.00 80.02  ?  224 GLU B CA  1 
ATOM   2605 C C   . GLU B 1 69  ? -5.123  73.143 -2.011  1.00 84.33  ?  224 GLU B C   1 
ATOM   2606 O O   . GLU B 1 69  ? -4.315  73.633 -1.212  1.00 84.79  ?  224 GLU B O   1 
ATOM   2607 C CB  . GLU B 1 69  ? -6.062  74.698 -3.756  1.00 81.17  ?  224 GLU B CB  1 
ATOM   2608 N N   . GLU B 1 70  ? -6.039  72.211 -1.669  1.00 79.22  ?  225 GLU B N   1 
ATOM   2609 C CA  . GLU B 1 70  ? -6.176  71.708 -0.310  1.00 78.16  ?  225 GLU B CA  1 
ATOM   2610 C C   . GLU B 1 70  ? -5.029  70.787 0.122   1.00 77.98  ?  225 GLU B C   1 
ATOM   2611 O O   . GLU B 1 70  ? -4.473  71.018 1.201   1.00 77.44  ?  225 GLU B O   1 
ATOM   2612 C CB  . GLU B 1 70  ? -7.550  71.065 -0.074  1.00 79.93  ?  225 GLU B CB  1 
ATOM   2613 C CG  . GLU B 1 70  ? -8.446  71.904 0.830   1.00 96.48  ?  225 GLU B CG  1 
ATOM   2614 C CD  . GLU B 1 70  ? -8.092  71.946 2.313   1.00 118.03 ?  225 GLU B CD  1 
ATOM   2615 O OE1 . GLU B 1 70  ? -7.180  72.718 2.699   1.00 103.25 ?  225 GLU B OE1 1 
ATOM   2616 O OE2 . GLU B 1 70  ? -8.772  71.240 3.097   1.00 106.64 -1 225 GLU B OE2 1 
ATOM   2617 N N   . LEU B 1 71  ? -4.675  69.754 -0.716  1.00 70.46  ?  226 LEU B N   1 
ATOM   2618 C CA  . LEU B 1 71  ? -3.601  68.783 -0.469  1.00 68.07  ?  226 LEU B CA  1 
ATOM   2619 C C   . LEU B 1 71  ? -2.285  69.522 -0.253  1.00 69.59  ?  226 LEU B C   1 
ATOM   2620 O O   . LEU B 1 71  ? -1.561  69.191 0.684   1.00 67.66  ?  226 LEU B O   1 
ATOM   2621 C CB  . LEU B 1 71  ? -3.504  67.751 -1.623  1.00 67.65  ?  226 LEU B CB  1 
ATOM   2622 C CG  . LEU B 1 71  ? -3.067  66.289 -1.295  1.00 71.55  ?  226 LEU B CG  1 
ATOM   2623 C CD1 . LEU B 1 71  ? -4.119  65.545 -0.471  1.00 71.60  ?  226 LEU B CD1 1 
ATOM   2624 C CD2 . LEU B 1 71  ? -2.856  65.492 -2.561  1.00 72.25  ?  226 LEU B CD2 1 
ATOM   2625 N N   . LYS B 1 72  ? -2.017  70.568 -1.078  1.00 66.39  ?  227 LYS B N   1 
ATOM   2626 C CA  . LYS B 1 72  ? -0.835  71.440 -0.974  1.00 65.89  ?  227 LYS B CA  1 
ATOM   2627 C C   . LYS B 1 72  ? -0.892  72.294 0.301   1.00 68.30  ?  227 LYS B C   1 
ATOM   2628 O O   . LYS B 1 72  ? 0.146   72.522 0.933   1.00 67.13  ?  227 LYS B O   1 
ATOM   2629 C CB  . LYS B 1 72  ? -0.663  72.314 -2.225  1.00 67.71  ?  227 LYS B CB  1 
ATOM   2630 N N   . GLN B 1 73  ? -2.105  72.740 0.692   1.00 63.96  ?  228 GLN B N   1 
ATOM   2631 C CA  . GLN B 1 73  ? -2.281  73.502 1.929   1.00 63.29  ?  228 GLN B CA  1 
ATOM   2632 C C   . GLN B 1 73  ? -2.032  72.588 3.138   1.00 66.88  ?  228 GLN B C   1 
ATOM   2633 O O   . GLN B 1 73  ? -1.373  73.014 4.088   1.00 66.62  ?  228 GLN B O   1 
ATOM   2634 C CB  . GLN B 1 73  ? -3.657  74.170 2.001   1.00 64.41  ?  228 GLN B CB  1 
ATOM   2635 N N   . GLN B 1 74  ? -2.488  71.309 3.063   1.00 63.19  ?  229 GLN B N   1 
ATOM   2636 C CA  . GLN B 1 74  ? -2.316  70.314 4.132   1.00 62.61  ?  229 GLN B CA  1 
ATOM   2637 C C   . GLN B 1 74  ? -0.828  69.936 4.296   1.00 67.89  ?  229 GLN B C   1 
ATOM   2638 O O   . GLN B 1 74  ? -0.339  69.776 5.427   1.00 69.65  ?  229 GLN B O   1 
ATOM   2639 C CB  . GLN B 1 74  ? -3.204  69.080 3.897   1.00 63.50  ?  229 GLN B CB  1 
ATOM   2640 N N   . PHE B 1 75  ? -0.108  69.845 3.157   1.00 61.11  ?  230 PHE B N   1 
ATOM   2641 C CA  . PHE B 1 75  ? 1.316   69.550 3.075   1.00 58.54  ?  230 PHE B CA  1 
ATOM   2642 C C   . PHE B 1 75  ? 2.112   70.668 3.777   1.00 61.25  ?  230 PHE B C   1 
ATOM   2643 O O   . PHE B 1 75  ? 2.917   70.379 4.662   1.00 60.47  ?  230 PHE B O   1 
ATOM   2644 C CB  . PHE B 1 75  ? 1.697   69.432 1.600   1.00 59.68  ?  230 PHE B CB  1 
ATOM   2645 C CG  . PHE B 1 75  ? 3.163   69.274 1.298   1.00 61.56  ?  230 PHE B CG  1 
ATOM   2646 C CD1 . PHE B 1 75  ? 3.757   68.017 1.295   1.00 63.73  ?  230 PHE B CD1 1 
ATOM   2647 C CD2 . PHE B 1 75  ? 3.942   70.373 0.956   1.00 64.56  ?  230 PHE B CD2 1 
ATOM   2648 C CE1 . PHE B 1 75  ? 5.105   67.868 0.977   1.00 64.30  ?  230 PHE B CE1 1 
ATOM   2649 C CE2 . PHE B 1 75  ? 5.294   70.221 0.642   1.00 67.22  ?  230 PHE B CE2 1 
ATOM   2650 C CZ  . PHE B 1 75  ? 5.866   68.970 0.660   1.00 64.45  ?  230 PHE B CZ  1 
ATOM   2651 N N   . ASP B 1 76  ? 1.850   71.943 3.396   1.00 57.74  ?  231 ASP B N   1 
ATOM   2652 C CA  . ASP B 1 76  ? 2.475   73.142 3.958   1.00 57.00  ?  231 ASP B CA  1 
ATOM   2653 C C   . ASP B 1 76  ? 2.200   73.254 5.446   1.00 59.95  ?  231 ASP B C   1 
ATOM   2654 O O   . ASP B 1 76  ? 3.072   73.716 6.196   1.00 59.80  ?  231 ASP B O   1 
ATOM   2655 C CB  . ASP B 1 76  ? 1.961   74.398 3.243   1.00 58.91  ?  231 ASP B CB  1 
ATOM   2656 C CG  . ASP B 1 76  ? 2.475   74.604 1.830   1.00 69.44  ?  231 ASP B CG  1 
ATOM   2657 O OD1 . ASP B 1 76  ? 3.462   73.935 1.450   1.00 69.92  ?  231 ASP B OD1 1 
ATOM   2658 O OD2 . ASP B 1 76  ? 1.900   75.457 1.108   1.00 73.52  -1 231 ASP B OD2 1 
ATOM   2659 N N   . GLN B 1 77  ? 0.994   72.812 5.870   1.00 55.01  ?  232 GLN B N   1 
ATOM   2660 C CA  . GLN B 1 77  ? 0.579   72.821 7.263   1.00 54.92  ?  232 GLN B CA  1 
ATOM   2661 C C   . GLN B 1 77  ? 1.400   71.853 8.135   1.00 60.57  ?  232 GLN B C   1 
ATOM   2662 O O   . GLN B 1 77  ? 1.835   72.218 9.235   1.00 60.57  ?  232 GLN B O   1 
ATOM   2663 C CB  . GLN B 1 77  ? -0.919  72.543 7.387   1.00 55.90  ?  232 GLN B CB  1 
ATOM   2664 C CG  . GLN B 1 77  ? -1.498  73.014 8.725   1.00 71.14  ?  232 GLN B CG  1 
ATOM   2665 C CD  . GLN B 1 77  ? -1.088  74.424 9.103   1.00 91.32  ?  232 GLN B CD  1 
ATOM   2666 O OE1 . GLN B 1 77  ? -1.163  75.380 8.303   1.00 85.60  ?  232 GLN B OE1 1 
ATOM   2667 N NE2 . GLN B 1 77  ? -0.616  74.572 10.329  1.00 84.97  ?  232 GLN B NE2 1 
ATOM   2668 N N   . GLU B 1 78  ? 1.624   70.630 7.624   1.00 57.22  ?  233 GLU B N   1 
ATOM   2669 C CA  . GLU B 1 78  ? 2.397   69.590 8.305   1.00 57.03  ?  233 GLU B CA  1 
ATOM   2670 C C   . GLU B 1 78  ? 3.827   70.084 8.576   1.00 59.66  ?  233 GLU B C   1 
ATOM   2671 O O   . GLU B 1 78  ? 4.332   69.924 9.691   1.00 59.54  ?  233 GLU B O   1 
ATOM   2672 C CB  . GLU B 1 78  ? 2.393   68.296 7.471   1.00 58.38  ?  233 GLU B CB  1 
ATOM   2673 C CG  . GLU B 1 78  ? 3.019   67.104 8.163   1.00 69.90  ?  233 GLU B CG  1 
ATOM   2674 C CD  . GLU B 1 78  ? 2.062   66.007 8.569   1.00 106.73 ?  233 GLU B CD  1 
ATOM   2675 O OE1 . GLU B 1 78  ? 1.190   65.627 7.749   1.00 97.72  ?  233 GLU B OE1 1 
ATOM   2676 O OE2 . GLU B 1 78  ? 2.256   65.454 9.677   1.00 113.05 -1 233 GLU B OE2 1 
ATOM   2677 N N   . ILE B 1 79  ? 4.439   70.724 7.569   1.00 54.02  ?  234 ILE B N   1 
ATOM   2678 C CA  . ILE B 1 79  ? 5.785   71.281 7.650   1.00 52.43  ?  234 ILE B CA  1 
ATOM   2679 C C   . ILE B 1 79  ? 5.851   72.439 8.661   1.00 58.41  ?  234 ILE B C   1 
ATOM   2680 O O   . ILE B 1 79  ? 6.722   72.426 9.524   1.00 58.17  ?  234 ILE B O   1 
ATOM   2681 C CB  . ILE B 1 79  ? 6.348   71.621 6.234   1.00 53.66  ?  234 ILE B CB  1 
ATOM   2682 C CG1 . ILE B 1 79  ? 6.491   70.327 5.385   1.00 52.06  ?  234 ILE B CG1 1 
ATOM   2683 C CG2 . ILE B 1 79  ? 7.675   72.385 6.332   1.00 53.40  ?  234 ILE B CG2 1 
ATOM   2684 C CD1 . ILE B 1 79  ? 6.579   70.509 3.934   1.00 50.90  ?  234 ILE B CD1 1 
ATOM   2685 N N   . LYS B 1 80  ? 4.911   73.397 8.587   1.00 57.20  ?  235 LYS B N   1 
ATOM   2686 C CA  . LYS B 1 80  ? 4.850   74.543 9.499   1.00 57.41  ?  235 LYS B CA  1 
ATOM   2687 C C   . LYS B 1 80  ? 4.761   74.102 10.968  1.00 62.59  ?  235 LYS B C   1 
ATOM   2688 O O   . LYS B 1 80  ? 5.556   74.564 11.782  1.00 63.76  ?  235 LYS B O   1 
ATOM   2689 C CB  . LYS B 1 80  ? 3.702   75.498 9.112   1.00 59.51  ?  235 LYS B CB  1 
ATOM   2690 N N   . VAL B 1 81  ? 3.852   73.160 11.282  1.00 59.80  ?  236 VAL B N   1 
ATOM   2691 C CA  . VAL B 1 81  ? 3.642   72.602 12.635  1.00 59.54  ?  236 VAL B CA  1 
ATOM   2692 C C   . VAL B 1 81  ? 4.870   71.850 13.127  1.00 62.18  ?  236 VAL B C   1 
ATOM   2693 O O   . VAL B 1 81  ? 5.312   72.074 14.250  1.00 61.00  ?  236 VAL B O   1 
ATOM   2694 C CB  . VAL B 1 81  ? 2.363   71.718 12.719  1.00 63.10  ?  236 VAL B CB  1 
ATOM   2695 C CG1 . VAL B 1 81  ? 2.295   70.935 14.046  1.00 62.93  ?  236 VAL B CG1 1 
ATOM   2696 C CG2 . VAL B 1 81  ? 1.104   72.559 12.515  1.00 62.29  ?  236 VAL B CG2 1 
ATOM   2697 N N   . MET B 1 82  ? 5.407   70.957 12.286  1.00 60.22  ?  237 MET B N   1 
ATOM   2698 C CA  . MET B 1 82  ? 6.571   70.157 12.629  1.00 61.23  ?  237 MET B CA  1 
ATOM   2699 C C   . MET B 1 82  ? 7.784   70.988 12.914  1.00 65.06  ?  237 MET B C   1 
ATOM   2700 O O   . MET B 1 82  ? 8.571   70.613 13.782  1.00 66.58  ?  237 MET B O   1 
ATOM   2701 C CB  . MET B 1 82  ? 6.884   69.133 11.553  1.00 64.56  ?  237 MET B CB  1 
ATOM   2702 C CG  . MET B 1 82  ? 7.282   67.811 12.135  1.00 69.68  ?  237 MET B CG  1 
ATOM   2703 S SD  . MET B 1 82  ? 5.854   66.839 12.642  1.00 74.58  ?  237 MET B SD  1 
ATOM   2704 C CE  . MET B 1 82  ? 5.318   66.246 11.082  1.00 71.42  ?  237 MET B CE  1 
ATOM   2705 N N   . ALA B 1 83  ? 7.930   72.126 12.205  1.00 59.50  ?  238 ALA B N   1 
ATOM   2706 C CA  . ALA B 1 83  ? 9.022   73.079 12.375  1.00 57.99  ?  238 ALA B CA  1 
ATOM   2707 C C   . ALA B 1 83  ? 8.985   73.665 13.780  1.00 61.72  ?  238 ALA B C   1 
ATOM   2708 O O   . ALA B 1 83  ? 10.023  73.770 14.426  1.00 61.58  ?  238 ALA B O   1 
ATOM   2709 C CB  . ALA B 1 83  ? 8.910   74.185 11.347  1.00 58.26  ?  238 ALA B CB  1 
ATOM   2710 N N   . LYS B 1 84  ? 7.789   73.985 14.272  1.00 58.41  ?  239 LYS B N   1 
ATOM   2711 C CA  . LYS B 1 84  ? 7.601   74.550 15.601  1.00 58.50  ?  239 LYS B CA  1 
ATOM   2712 C C   . LYS B 1 84  ? 7.628   73.484 16.727  1.00 64.87  ?  239 LYS B C   1 
ATOM   2713 O O   . LYS B 1 84  ? 8.297   73.678 17.747  1.00 66.72  ?  239 LYS B O   1 
ATOM   2714 C CB  . LYS B 1 84  ? 6.300   75.367 15.635  1.00 59.43  ?  239 LYS B CB  1 
ATOM   2715 N N   . CYS B 1 85  ? 6.947   72.347 16.508  1.00 59.88  ?  240 CYS B N   1 
ATOM   2716 C CA  . CYS B 1 85  ? 6.769   71.275 17.485  1.00 58.61  ?  240 CYS B CA  1 
ATOM   2717 C C   . CYS B 1 85  ? 7.730   70.093 17.413  1.00 55.60  ?  240 CYS B C   1 
ATOM   2718 O O   . CYS B 1 85  ? 7.670   69.293 16.478  1.00 55.68  ?  240 CYS B O   1 
ATOM   2719 C CB  . CYS B 1 85  ? 5.316   70.813 17.481  1.00 59.99  ?  240 CYS B CB  1 
ATOM   2720 S SG  . CYS B 1 85  ? 4.119   72.171 17.533  1.00 64.43  ?  240 CYS B SG  1 
ATOM   2721 N N   . GLN B 1 86  ? 8.574   69.956 18.437  1.00 47.15  ?  241 GLN B N   1 
ATOM   2722 C CA  . GLN B 1 86  ? 9.521   68.847 18.594  1.00 45.40  ?  241 GLN B CA  1 
ATOM   2723 C C   . GLN B 1 86  ? 9.357   68.310 20.018  1.00 46.09  ?  241 GLN B C   1 
ATOM   2724 O O   . GLN B 1 86  ? 9.583   69.044 21.000  1.00 46.29  ?  241 GLN B O   1 
ATOM   2725 C CB  . GLN B 1 86  ? 10.981  69.281 18.352  1.00 46.73  ?  241 GLN B CB  1 
ATOM   2726 C CG  . GLN B 1 86  ? 11.357  69.508 16.889  1.00 69.30  ?  241 GLN B CG  1 
ATOM   2727 C CD  . GLN B 1 86  ? 11.387  70.968 16.461  1.00 99.25  ?  241 GLN B CD  1 
ATOM   2728 O OE1 . GLN B 1 86  ? 11.363  71.910 17.277  1.00 95.43  ?  241 GLN B OE1 1 
ATOM   2729 N NE2 . GLN B 1 86  ? 11.456  71.185 15.152  1.00 92.76  ?  241 GLN B NE2 1 
ATOM   2730 N N   . HIS B 1 87  ? 8.902   67.043 20.127  1.00 38.29  ?  242 HIS B N   1 
ATOM   2731 C CA  . HIS B 1 87  ? 8.643   66.394 21.402  1.00 36.88  ?  242 HIS B CA  1 
ATOM   2732 C C   . HIS B 1 87  ? 8.783   64.879 21.268  1.00 40.53  ?  242 HIS B C   1 
ATOM   2733 O O   . HIS B 1 87  ? 8.532   64.348 20.197  1.00 38.81  ?  242 HIS B O   1 
ATOM   2734 C CB  . HIS B 1 87  ? 7.230   66.766 21.879  1.00 37.23  ?  242 HIS B CB  1 
ATOM   2735 C CG  . HIS B 1 87  ? 6.926   66.337 23.269  1.00 39.77  ?  242 HIS B CG  1 
ATOM   2736 N ND1 . HIS B 1 87  ? 6.469   65.065 23.542  1.00 41.33  ?  242 HIS B ND1 1 
ATOM   2737 C CD2 . HIS B 1 87  ? 7.037   67.024 24.420  1.00 41.06  ?  242 HIS B CD2 1 
ATOM   2738 C CE1 . HIS B 1 87  ? 6.321   65.018 24.853  1.00 40.83  ?  242 HIS B CE1 1 
ATOM   2739 N NE2 . HIS B 1 87  ? 6.654   66.175 25.421  1.00 41.18  ?  242 HIS B NE2 1 
ATOM   2740 N N   . GLU B 1 88  ? 9.144   64.188 22.366  1.00 39.54  ?  243 GLU B N   1 
ATOM   2741 C CA  . GLU B 1 88  ? 9.314   62.728 22.429  1.00 40.92  ?  243 GLU B CA  1 
ATOM   2742 C C   . GLU B 1 88  ? 8.038   61.925 22.087  1.00 47.70  ?  243 GLU B C   1 
ATOM   2743 O O   . GLU B 1 88  ? 8.127   60.730 21.775  1.00 47.73  ?  243 GLU B O   1 
ATOM   2744 C CB  . GLU B 1 88  ? 9.908   62.268 23.785  1.00 42.09  ?  243 GLU B CB  1 
ATOM   2745 C CG  . GLU B 1 88  ? 9.021   62.557 24.989  1.00 55.54  ?  243 GLU B CG  1 
ATOM   2746 C CD  . GLU B 1 88  ? 9.681   62.439 26.348  1.00 80.83  ?  243 GLU B CD  1 
ATOM   2747 O OE1 . GLU B 1 88  ? 10.556  61.559 26.515  1.00 90.54  ?  243 GLU B OE1 1 
ATOM   2748 O OE2 . GLU B 1 88  ? 9.284   63.197 27.263  1.00 75.72  -1 243 GLU B OE2 1 
ATOM   2749 N N   . ASN B 1 89  ? 6.862   62.579 22.162  1.00 43.62  ?  244 ASN B N   1 
ATOM   2750 C CA  . ASN B 1 89  ? 5.577   61.948 21.857  1.00 41.72  ?  244 ASN B CA  1 
ATOM   2751 C C   . ASN B 1 89  ? 4.960   62.479 20.567  1.00 43.25  ?  244 ASN B C   1 
ATOM   2752 O O   . ASN B 1 89  ? 3.751   62.397 20.345  1.00 41.80  ?  244 ASN B O   1 
ATOM   2753 C CB  . ASN B 1 89  ? 4.644   61.993 23.062  1.00 37.32  ?  244 ASN B CB  1 
ATOM   2754 C CG  . ASN B 1 89  ? 5.214   61.263 24.257  1.00 47.82  ?  244 ASN B CG  1 
ATOM   2755 O OD1 . ASN B 1 89  ? 5.594   61.861 25.260  1.00 46.08  ?  244 ASN B OD1 1 
ATOM   2756 N ND2 . ASN B 1 89  ? 5.354   59.954 24.160  1.00 34.01  ?  244 ASN B ND2 1 
ATOM   2757 N N   . LEU B 1 90  ? 5.823   63.008 19.701  1.00 39.86  ?  245 LEU B N   1 
ATOM   2758 C CA  . LEU B 1 90  ? 5.439   63.459 18.376  1.00 40.39  ?  245 LEU B CA  1 
ATOM   2759 C C   . LEU B 1 90  ? 6.357   62.797 17.400  1.00 45.81  ?  245 LEU B C   1 
ATOM   2760 O O   . LEU B 1 90  ? 7.535   62.562 17.681  1.00 47.63  ?  245 LEU B O   1 
ATOM   2761 C CB  . LEU B 1 90  ? 5.513   64.989 18.194  1.00 40.70  ?  245 LEU B CB  1 
ATOM   2762 C CG  . LEU B 1 90  ? 4.667   65.882 19.088  1.00 45.14  ?  245 LEU B CG  1 
ATOM   2763 C CD1 . LEU B 1 90  ? 4.820   67.293 18.658  1.00 44.94  ?  245 LEU B CD1 1 
ATOM   2764 C CD2 . LEU B 1 90  ? 3.189   65.504 19.039  1.00 47.85  ?  245 LEU B CD2 1 
ATOM   2765 N N   . VAL B 1 91  ? 5.832   62.521 16.238  1.00 41.66  ?  246 VAL B N   1 
ATOM   2766 C CA  . VAL B 1 91  ? 6.575   61.924 15.144  1.00 40.99  ?  246 VAL B CA  1 
ATOM   2767 C C   . VAL B 1 91  ? 7.607   62.989 14.641  1.00 43.43  ?  246 VAL B C   1 
ATOM   2768 O O   . VAL B 1 91  ? 7.411   64.186 14.878  1.00 44.40  ?  246 VAL B O   1 
ATOM   2769 C CB  . VAL B 1 91  ? 5.507   61.445 14.134  1.00 45.36  ?  246 VAL B CB  1 
ATOM   2770 C CG1 . VAL B 1 91  ? 5.546   62.168 12.804  1.00 45.83  ?  246 VAL B CG1 1 
ATOM   2771 C CG2 . VAL B 1 91  ? 5.525   59.948 13.972  1.00 45.41  ?  246 VAL B CG2 1 
ATOM   2772 N N   . GLU B 1 92  ? 8.734   62.556 14.073  1.00 36.47  ?  247 GLU B N   1 
ATOM   2773 C CA  . GLU B 1 92  ? 9.781   63.468 13.617  1.00 34.93  ?  247 GLU B CA  1 
ATOM   2774 C C   . GLU B 1 92  ? 9.863   63.508 12.091  1.00 39.09  ?  247 GLU B C   1 
ATOM   2775 O O   . GLU B 1 92  ? 9.927   62.464 11.435  1.00 37.22  ?  247 GLU B O   1 
ATOM   2776 C CB  . GLU B 1 92  ? 11.144  63.069 14.218  1.00 36.51  ?  247 GLU B CB  1 
ATOM   2777 C CG  . GLU B 1 92  ? 12.205  64.163 14.211  1.00 47.36  ?  247 GLU B CG  1 
ATOM   2778 C CD  . GLU B 1 92  ? 13.659  63.769 14.438  1.00 75.65  ?  247 GLU B CD  1 
ATOM   2779 O OE1 . GLU B 1 92  ? 13.928  62.727 15.084  1.00 72.88  ?  247 GLU B OE1 1 
ATOM   2780 O OE2 . GLU B 1 92  ? 14.537  64.546 13.994  1.00 71.55  -1 247 GLU B OE2 1 
ATOM   2781 N N   . LEU B 1 93  ? 9.864   64.731 11.536  1.00 37.95  ?  248 LEU B N   1 
ATOM   2782 C CA  . LEU B 1 93  ? 9.984   64.975 10.108  1.00 38.36  ?  248 LEU B CA  1 
ATOM   2783 C C   . LEU B 1 93  ? 11.459  65.164 9.773   1.00 46.06  ?  248 LEU B C   1 
ATOM   2784 O O   . LEU B 1 93  ? 12.156  65.945 10.425  1.00 46.11  ?  248 LEU B O   1 
ATOM   2785 C CB  . LEU B 1 93  ? 9.170   66.209 9.701   1.00 37.80  ?  248 LEU B CB  1 
ATOM   2786 C CG  . LEU B 1 93  ? 8.957   66.443 8.201   1.00 41.22  ?  248 LEU B CG  1 
ATOM   2787 C CD1 . LEU B 1 93  ? 8.045   65.371 7.588   1.00 39.54  ?  248 LEU B CD1 1 
ATOM   2788 C CD2 . LEU B 1 93  ? 8.417   67.851 7.948   1.00 41.24  ?  248 LEU B CD2 1 
ATOM   2789 N N   . LEU B 1 94  ? 11.951  64.421 8.785   1.00 44.63  ?  249 LEU B N   1 
ATOM   2790 C CA  . LEU B 1 94  ? 13.351  64.561 8.387   1.00 44.66  ?  249 LEU B CA  1 
ATOM   2791 C C   . LEU B 1 94  ? 13.455  65.548 7.220   1.00 53.52  ?  249 LEU B C   1 
ATOM   2792 O O   . LEU B 1 94  ? 14.336  66.412 7.199   1.00 54.61  ?  249 LEU B O   1 
ATOM   2793 C CB  . LEU B 1 94  ? 13.960  63.197 8.042   1.00 43.36  ?  249 LEU B CB  1 
ATOM   2794 C CG  . LEU B 1 94  ? 14.085  62.226 9.204   1.00 45.51  ?  249 LEU B CG  1 
ATOM   2795 C CD1 . LEU B 1 94  ? 14.415  60.848 8.711   1.00 45.42  ?  249 LEU B CD1 1 
ATOM   2796 C CD2 . LEU B 1 94  ? 15.083  62.696 10.229  1.00 41.76  ?  249 LEU B CD2 1 
ATOM   2797 N N   . GLY B 1 95  ? 12.521  65.410 6.290   1.00 51.31  ?  250 GLY B N   1 
ATOM   2798 C CA  . GLY B 1 95  ? 12.415  66.248 5.116   1.00 51.32  ?  250 GLY B CA  1 
ATOM   2799 C C   . GLY B 1 95  ? 11.087  66.130 4.403   1.00 54.85  ?  250 GLY B C   1 
ATOM   2800 O O   . GLY B 1 95  ? 10.084  65.736 5.001   1.00 52.93  ?  250 GLY B O   1 
ATOM   2801 N N   . PHE B 1 96  ? 11.089  66.501 3.112   1.00 53.01  ?  251 PHE B N   1 
ATOM   2802 C CA  . PHE B 1 96  ? 9.931   66.554 2.207   1.00 53.71  ?  251 PHE B CA  1 
ATOM   2803 C C   . PHE B 1 96  ? 10.392  66.653 0.760   1.00 61.73  ?  251 PHE B C   1 
ATOM   2804 O O   . PHE B 1 96  ? 11.554  66.946 0.503   1.00 62.49  ?  251 PHE B O   1 
ATOM   2805 C CB  . PHE B 1 96  ? 9.025   67.790 2.522   1.00 54.47  ?  251 PHE B CB  1 
ATOM   2806 C CG  . PHE B 1 96  ? 9.771   69.099 2.544   1.00 54.44  ?  251 PHE B CG  1 
ATOM   2807 C CD1 . PHE B 1 96  ? 10.101  69.753 1.360   1.00 57.28  ?  251 PHE B CD1 1 
ATOM   2808 C CD2 . PHE B 1 96  ? 10.229  69.635 3.743   1.00 54.85  ?  251 PHE B CD2 1 
ATOM   2809 C CE1 . PHE B 1 96  ? 10.869  70.919 1.376   1.00 57.99  ?  251 PHE B CE1 1 
ATOM   2810 C CE2 . PHE B 1 96  ? 10.977  70.808 3.763   1.00 58.06  ?  251 PHE B CE2 1 
ATOM   2811 C CZ  . PHE B 1 96  ? 11.298  71.444 2.579   1.00 56.94  ?  251 PHE B CZ  1 
ATOM   2812 N N   . SER B 1 97  ? 9.459   66.489 -0.170  1.00 61.09  ?  252 SER B N   1 
ATOM   2813 C CA  . SER B 1 97  ? 9.656   66.625 -1.612  1.00 62.53  ?  252 SER B CA  1 
ATOM   2814 C C   . SER B 1 97  ? 8.408   67.262 -2.201  1.00 72.12  ?  252 SER B C   1 
ATOM   2815 O O   . SER B 1 97  ? 7.301   66.749 -1.996  1.00 71.75  ?  252 SER B O   1 
ATOM   2816 C CB  . SER B 1 97  ? 9.947   65.275 -2.265  1.00 64.63  ?  252 SER B CB  1 
ATOM   2817 O OG  . SER B 1 97  ? 9.394   65.136 -3.567  1.00 71.79  ?  252 SER B OG  1 
ATOM   2818 N N   . SER B 1 98  ? 8.582   68.392 -2.910  1.00 72.70  ?  253 SER B N   1 
ATOM   2819 C CA  . SER B 1 98  ? 7.484   69.123 -3.550  1.00 74.41  ?  253 SER B CA  1 
ATOM   2820 C C   . SER B 1 98  ? 7.731   69.359 -5.041  1.00 81.12  ?  253 SER B C   1 
ATOM   2821 O O   . SER B 1 98  ? 7.194   70.309 -5.611  1.00 80.78  ?  253 SER B O   1 
ATOM   2822 C CB  . SER B 1 98  ? 7.206   70.433 -2.810  1.00 78.65  ?  253 SER B CB  1 
ATOM   2823 O OG  . SER B 1 98  ? 8.375   71.226 -2.668  1.00 87.93  ?  253 SER B OG  1 
ATOM   2824 N N   . ASP B 1 99  ? 8.530   68.470 -5.670  1.00 80.16  ?  254 ASP B N   1 
ATOM   2825 C CA  . ASP B 1 99  ? 8.888   68.525 -7.090  1.00 81.14  ?  254 ASP B CA  1 
ATOM   2826 C C   . ASP B 1 99  ? 7.694   68.123 -7.989  1.00 86.94  ?  254 ASP B C   1 
ATOM   2827 O O   . ASP B 1 99  ? 7.423   66.926 -8.166  1.00 86.53  ?  254 ASP B O   1 
ATOM   2828 C CB  . ASP B 1 99  ? 10.147  67.664 -7.366  1.00 82.78  ?  254 ASP B CB  1 
ATOM   2829 N N   . GLY B 1 100 ? 6.986   69.133 -8.513  1.00 84.77  ?  255 GLY B N   1 
ATOM   2830 C CA  . GLY B 1 100 ? 5.821   68.966 -9.384  1.00 85.09  ?  255 GLY B CA  1 
ATOM   2831 C C   . GLY B 1 100 ? 4.531   68.609 -8.672  1.00 89.97  ?  255 GLY B C   1 
ATOM   2832 O O   . GLY B 1 100 ? 4.261   69.122 -7.580  1.00 90.78  ?  255 GLY B O   1 
ATOM   2833 N N   . ASP B 1 101 ? 3.724   67.726 -9.296  1.00 85.69  ?  256 ASP B N   1 
ATOM   2834 C CA  . ASP B 1 101 ? 2.425   67.249 -8.794  1.00 85.38  ?  256 ASP B CA  1 
ATOM   2835 C C   . ASP B 1 101 ? 2.507   66.302 -7.589  1.00 86.96  ?  256 ASP B C   1 
ATOM   2836 O O   . ASP B 1 101 ? 1.503   66.140 -6.887  1.00 86.80  ?  256 ASP B O   1 
ATOM   2837 C CB  . ASP B 1 101 ? 1.611   66.586 -9.926  1.00 87.86  ?  256 ASP B CB  1 
ATOM   2838 C CG  . ASP B 1 101 ? 1.134   67.528 -11.027 1.00 101.67 ?  256 ASP B CG  1 
ATOM   2839 O OD1 . ASP B 1 101 ? 1.494   68.737 -10.983 1.00 102.75 ?  256 ASP B OD1 1 
ATOM   2840 O OD2 . ASP B 1 101 ? 0.411   67.055 -11.941 1.00 107.01 -1 256 ASP B OD2 1 
ATOM   2841 N N   . ASP B 1 102 ? 3.678   65.656 -7.365  1.00 80.99  ?  257 ASP B N   1 
ATOM   2842 C CA  . ASP B 1 102 ? 3.881   64.723 -6.247  1.00 78.63  ?  257 ASP B CA  1 
ATOM   2843 C C   . ASP B 1 102 ? 4.469   65.386 -5.005  1.00 75.70  ?  257 ASP B C   1 
ATOM   2844 O O   . ASP B 1 102 ? 5.513   66.038 -5.065  1.00 75.37  ?  257 ASP B O   1 
ATOM   2845 C CB  . ASP B 1 102 ? 4.686   63.495 -6.668  1.00 80.80  ?  257 ASP B CB  1 
ATOM   2846 C CG  . ASP B 1 102 ? 3.901   62.549 -7.555  1.00 98.30  ?  257 ASP B CG  1 
ATOM   2847 O OD1 . ASP B 1 102 ? 3.054   61.787 -7.015  1.00 100.22 ?  257 ASP B OD1 1 
ATOM   2848 O OD2 . ASP B 1 102 ? 4.138   62.558 -8.791  1.00 104.22 -1 257 ASP B OD2 1 
ATOM   2849 N N   . LEU B 1 103 ? 3.757   65.239 -3.882  1.00 66.34  ?  258 LEU B N   1 
ATOM   2850 C CA  . LEU B 1 103 ? 4.107   65.808 -2.592  1.00 63.07  ?  258 LEU B CA  1 
ATOM   2851 C C   . LEU B 1 103 ? 4.423   64.684 -1.596  1.00 62.05  ?  258 LEU B C   1 
ATOM   2852 O O   . LEU B 1 103 ? 3.587   63.818 -1.350  1.00 62.56  ?  258 LEU B O   1 
ATOM   2853 C CB  . LEU B 1 103 ? 2.947   66.688 -2.113  1.00 62.85  ?  258 LEU B CB  1 
ATOM   2854 C CG  . LEU B 1 103 ? 3.077   68.207 -2.277  1.00 67.77  ?  258 LEU B CG  1 
ATOM   2855 C CD1 . LEU B 1 103 ? 3.635   68.612 -3.631  1.00 68.64  ?  258 LEU B CD1 1 
ATOM   2856 C CD2 . LEU B 1 103 ? 1.757   68.860 -2.086  1.00 68.99  ?  258 LEU B CD2 1 
ATOM   2857 N N   . CYS B 1 104 ? 5.653   64.679 -1.065  1.00 54.02  ?  259 CYS B N   1 
ATOM   2858 C CA  . CYS B 1 104 ? 6.134   63.661 -0.127  1.00 50.38  ?  259 CYS B CA  1 
ATOM   2859 C C   . CYS B 1 104 ? 6.589   64.227 1.185   1.00 47.43  ?  259 CYS B C   1 
ATOM   2860 O O   . CYS B 1 104 ? 7.163   65.314 1.244   1.00 44.49  ?  259 CYS B O   1 
ATOM   2861 C CB  . CYS B 1 104 ? 7.236   62.825 -0.757  1.00 50.06  ?  259 CYS B CB  1 
ATOM   2862 S SG  . CYS B 1 104 ? 6.681   61.783 -2.117  1.00 54.28  ?  259 CYS B SG  1 
ATOM   2863 N N   . LEU B 1 105 ? 6.382   63.448 2.234   1.00 41.85  ?  260 LEU B N   1 
ATOM   2864 C CA  . LEU B 1 105 ? 6.849   63.787 3.566   1.00 39.82  ?  260 LEU B CA  1 
ATOM   2865 C C   . LEU B 1 105 ? 7.676   62.610 4.096   1.00 40.99  ?  260 LEU B C   1 
ATOM   2866 O O   . LEU B 1 105 ? 7.248   61.459 4.006   1.00 40.26  ?  260 LEU B O   1 
ATOM   2867 C CB  . LEU B 1 105 ? 5.690   64.180 4.479   1.00 39.12  ?  260 LEU B CB  1 
ATOM   2868 C CG  . LEU B 1 105 ? 5.097   65.564 4.189   1.00 43.28  ?  260 LEU B CG  1 
ATOM   2869 C CD1 . LEU B 1 105 ? 3.672   65.670 4.695   1.00 43.41  ?  260 LEU B CD1 1 
ATOM   2870 C CD2 . LEU B 1 105 ? 5.962   66.691 4.763   1.00 43.32  ?  260 LEU B CD2 1 
ATOM   2871 N N   . VAL B 1 106 ? 8.908   62.896 4.512   1.00 36.83  ?  261 VAL B N   1 
ATOM   2872 C CA  . VAL B 1 106 ? 9.864   61.903 4.998   1.00 37.21  ?  261 VAL B CA  1 
ATOM   2873 C C   . VAL B 1 106 ? 9.981   61.994 6.524   1.00 42.75  ?  261 VAL B C   1 
ATOM   2874 O O   . VAL B 1 106 ? 10.286  63.074 7.059   1.00 44.89  ?  261 VAL B O   1 
ATOM   2875 C CB  . VAL B 1 106 ? 11.234  62.038 4.266   1.00 40.71  ?  261 VAL B CB  1 
ATOM   2876 C CG1 . VAL B 1 106 ? 12.188  60.915 4.655   1.00 40.26  ?  261 VAL B CG1 1 
ATOM   2877 C CG2 . VAL B 1 106 ? 11.042  62.053 2.749   1.00 40.32  ?  261 VAL B CG2 1 
ATOM   2878 N N   . TYR B 1 107 ? 9.726   60.861 7.217   1.00 35.67  ?  262 TYR B N   1 
ATOM   2879 C CA  . TYR B 1 107 ? 9.744   60.763 8.669   1.00 34.31  ?  262 TYR B CA  1 
ATOM   2880 C C   . TYR B 1 107 ? 10.682  59.684 9.171   1.00 40.15  ?  262 TYR B C   1 
ATOM   2881 O O   . TYR B 1 107 ? 11.024  58.753 8.431   1.00 41.19  ?  262 TYR B O   1 
ATOM   2882 C CB  . TYR B 1 107 ? 8.360   60.375 9.159   1.00 35.35  ?  262 TYR B CB  1 
ATOM   2883 C CG  . TYR B 1 107 ? 7.238   61.322 8.794   1.00 38.54  ?  262 TYR B CG  1 
ATOM   2884 C CD1 . TYR B 1 107 ? 6.512   61.157 7.614   1.00 39.41  ?  262 TYR B CD1 1 
ATOM   2885 C CD2 . TYR B 1 107 ? 6.824   62.315 9.681   1.00 39.02  ?  262 TYR B CD2 1 
ATOM   2886 C CE1 . TYR B 1 107 ? 5.447   61.996 7.300   1.00 39.92  ?  262 TYR B CE1 1 
ATOM   2887 C CE2 . TYR B 1 107 ? 5.746   63.144 9.387   1.00 39.41  ?  262 TYR B CE2 1 
ATOM   2888 C CZ  . TYR B 1 107 ? 5.082   63.002 8.183   1.00 49.77  ?  262 TYR B CZ  1 
ATOM   2889 O OH  . TYR B 1 107 ? 4.046   63.850 7.898   1.00 56.98  ?  262 TYR B OH  1 
ATOM   2890 N N   . VAL B 1 108 ? 10.994  59.734 10.479  1.00 35.70  ?  263 VAL B N   1 
ATOM   2891 C CA  . VAL B 1 108 ? 11.753  58.675 11.142  1.00 34.77  ?  263 VAL B CA  1 
ATOM   2892 C C   . VAL B 1 108 ? 10.726  57.550 11.289  1.00 37.34  ?  263 VAL B C   1 
ATOM   2893 O O   . VAL B 1 108 ? 9.701   57.753 11.947  1.00 37.29  ?  263 VAL B O   1 
ATOM   2894 C CB  . VAL B 1 108 ? 12.302  59.117 12.541  1.00 37.80  ?  263 VAL B CB  1 
ATOM   2895 C CG1 . VAL B 1 108 ? 12.903  57.945 13.298  1.00 35.38  ?  263 VAL B CG1 1 
ATOM   2896 C CG2 . VAL B 1 108 ? 13.302  60.273 12.432  1.00 37.69  ?  263 VAL B CG2 1 
ATOM   2897 N N   . TYR B 1 109 ? 10.944  56.436 10.581  1.00 33.12  ?  264 TYR B N   1 
ATOM   2898 C CA  . TYR B 1 109 ? 10.128  55.219 10.592  1.00 32.96  ?  264 TYR B CA  1 
ATOM   2899 C C   . TYR B 1 109 ? 9.785   54.750 12.010  1.00 36.36  ?  264 TYR B C   1 
ATOM   2900 O O   . TYR B 1 109 ? 10.663  54.761 12.866  1.00 35.44  ?  264 TYR B O   1 
ATOM   2901 C CB  . TYR B 1 109 ? 10.954  54.122 9.923   1.00 34.01  ?  264 TYR B CB  1 
ATOM   2902 C CG  . TYR B 1 109 ? 10.468  52.695 10.061  1.00 34.93  ?  264 TYR B CG  1 
ATOM   2903 C CD1 . TYR B 1 109 ? 9.664   52.113 9.078   1.00 36.92  ?  264 TYR B CD1 1 
ATOM   2904 C CD2 . TYR B 1 109 ? 10.948  51.872 11.076  1.00 34.26  ?  264 TYR B CD2 1 
ATOM   2905 C CE1 . TYR B 1 109 ? 9.332   50.756 9.124   1.00 35.87  ?  264 TYR B CE1 1 
ATOM   2906 C CE2 . TYR B 1 109 ? 10.589  50.527 11.152  1.00 33.59  ?  264 TYR B CE2 1 
ATOM   2907 C CZ  . TYR B 1 109 ? 9.804   49.970 10.162  1.00 38.94  ?  264 TYR B CZ  1 
ATOM   2908 O OH  . TYR B 1 109 ? 9.468   48.645 10.243  1.00 43.82  ?  264 TYR B OH  1 
ATOM   2909 N N   . MET B 1 110 ? 8.554   54.223 12.208  1.00 33.12  ?  265 MET B N   1 
ATOM   2910 C CA  . MET B 1 110 ? 8.070   53.653 13.481  1.00 33.07  ?  265 MET B CA  1 
ATOM   2911 C C   . MET B 1 110 ? 8.053   52.087 13.489  1.00 38.81  ?  265 MET B C   1 
ATOM   2912 O O   . MET B 1 110 ? 7.218   51.486 12.790  1.00 40.33  ?  265 MET B O   1 
ATOM   2913 C CB  . MET B 1 110 ? 6.697   54.230 13.873  1.00 34.29  ?  265 MET B CB  1 
ATOM   2914 C CG  . MET B 1 110 ? 6.713   55.734 14.092  1.00 36.03  ?  265 MET B CG  1 
ATOM   2915 S SD  . MET B 1 110 ? 7.438   56.247 15.655  1.00 38.00  ?  265 MET B SD  1 
ATOM   2916 C CE  . MET B 1 110 ? 9.156   56.381 15.210  1.00 33.90  ?  265 MET B CE  1 
ATOM   2917 N N   . PRO B 1 111 ? 8.932   51.417 14.292  1.00 32.19  ?  266 PRO B N   1 
ATOM   2918 C CA  . PRO B 1 111 ? 8.996   49.940 14.251  1.00 31.97  ?  266 PRO B CA  1 
ATOM   2919 C C   . PRO B 1 111 ? 7.733   49.158 14.629  1.00 37.36  ?  266 PRO B C   1 
ATOM   2920 O O   . PRO B 1 111 ? 7.529   48.018 14.179  1.00 38.28  ?  266 PRO B O   1 
ATOM   2921 C CB  . PRO B 1 111 ? 10.241  49.610 15.106  1.00 32.90  ?  266 PRO B CB  1 
ATOM   2922 C CG  . PRO B 1 111 ? 11.071  50.860 15.056  1.00 35.32  ?  266 PRO B CG  1 
ATOM   2923 C CD  . PRO B 1 111 ? 10.038  51.962 15.104  1.00 31.83  ?  266 PRO B CD  1 
ATOM   2924 N N   . ASN B 1 112 ? 6.865   49.774 15.421  1.00 33.53  ?  267 ASN B N   1 
ATOM   2925 C CA  . ASN B 1 112 ? 5.627   49.127 15.826  1.00 32.09  ?  267 ASN B CA  1 
ATOM   2926 C C   . ASN B 1 112 ? 4.360   49.669 15.194  1.00 34.50  ?  267 ASN B C   1 
ATOM   2927 O O   . ASN B 1 112 ? 3.277   49.366 15.708  1.00 33.91  ?  267 ASN B O   1 
ATOM   2928 C CB  . ASN B 1 112 ? 5.534   49.013 17.333  1.00 26.58  ?  267 ASN B CB  1 
ATOM   2929 C CG  . ASN B 1 112 ? 6.415   47.947 17.860  1.00 40.80  ?  267 ASN B CG  1 
ATOM   2930 O OD1 . ASN B 1 112 ? 6.243   46.757 17.551  1.00 41.14  ?  267 ASN B OD1 1 
ATOM   2931 N ND2 . ASN B 1 112 ? 7.378   48.349 18.666  1.00 38.59  ?  267 ASN B ND2 1 
ATOM   2932 N N   . GLY B 1 113 ? 4.500   50.390 14.062  1.00 31.03  ?  268 GLY B N   1 
ATOM   2933 C CA  . GLY B 1 113 ? 3.388   50.976 13.302  1.00 31.47  ?  268 GLY B CA  1 
ATOM   2934 C C   . GLY B 1 113 ? 2.408   51.792 14.138  1.00 36.63  ?  268 GLY B C   1 
ATOM   2935 O O   . GLY B 1 113 ? 2.812   52.480 15.083  1.00 35.84  ?  268 GLY B O   1 
ATOM   2936 N N   . SER B 1 114 ? 1.108   51.685 13.819  1.00 33.72  ?  269 SER B N   1 
ATOM   2937 C CA  . SER B 1 114 ? 0.038   52.420 14.493  1.00 33.18  ?  269 SER B CA  1 
ATOM   2938 C C   . SER B 1 114 ? -0.615  51.635 15.608  1.00 37.84  ?  269 SER B C   1 
ATOM   2939 O O   . SER B 1 114 ? -0.632  50.398 15.573  1.00 39.37  ?  269 SER B O   1 
ATOM   2940 C CB  . SER B 1 114 ? -1.017  52.854 13.483  1.00 35.79  ?  269 SER B CB  1 
ATOM   2941 O OG  . SER B 1 114 ? -1.686  51.754 12.885  1.00 44.26  ?  269 SER B OG  1 
ATOM   2942 N N   . LEU B 1 115 ? -1.193  52.368 16.584  1.00 31.49  ?  270 LEU B N   1 
ATOM   2943 C CA  . LEU B 1 115 ? -1.941  51.816 17.712  1.00 30.38  ?  270 LEU B CA  1 
ATOM   2944 C C   . LEU B 1 115 ? -3.164  51.010 17.186  1.00 34.49  ?  270 LEU B C   1 
ATOM   2945 O O   . LEU B 1 115 ? -3.472  49.936 17.718  1.00 34.76  ?  270 LEU B O   1 
ATOM   2946 C CB  . LEU B 1 115 ? -2.380  52.961 18.653  1.00 29.67  ?  270 LEU B CB  1 
ATOM   2947 C CG  . LEU B 1 115 ? -3.274  52.612 19.828  1.00 31.77  ?  270 LEU B CG  1 
ATOM   2948 C CD1 . LEU B 1 115 ? -2.636  51.564 20.732  1.00 29.48  ?  270 LEU B CD1 1 
ATOM   2949 C CD2 . LEU B 1 115 ? -3.664  53.855 20.577  1.00 33.99  ?  270 LEU B CD2 1 
ATOM   2950 N N   . LEU B 1 116 ? -3.812  51.515 16.123  1.00 29.52  ?  271 LEU B N   1 
ATOM   2951 C CA  . LEU B 1 116 ? -4.940  50.853 15.460  1.00 28.39  ?  271 LEU B CA  1 
ATOM   2952 C C   . LEU B 1 116 ? -4.520  49.423 15.095  1.00 36.00  ?  271 LEU B C   1 
ATOM   2953 O O   . LEU B 1 116 ? -5.111  48.458 15.596  1.00 37.57  ?  271 LEU B O   1 
ATOM   2954 C CB  . LEU B 1 116 ? -5.372  51.644 14.191  1.00 26.54  ?  271 LEU B CB  1 
ATOM   2955 C CG  . LEU B 1 116 ? -6.645  51.162 13.469  1.00 28.28  ?  271 LEU B CG  1 
ATOM   2956 C CD1 . LEU B 1 116 ? -7.859  51.730 14.082  1.00 27.96  ?  271 LEU B CD1 1 
ATOM   2957 C CD2 . LEU B 1 116 ? -6.672  51.576 12.043  1.00 24.58  ?  271 LEU B CD2 1 
ATOM   2958 N N   . ASP B 1 117 ? -3.432  49.302 14.315  1.00 32.19  ?  272 ASP B N   1 
ATOM   2959 C CA  . ASP B 1 117 ? -2.920  48.023 13.838  1.00 32.14  ?  272 ASP B CA  1 
ATOM   2960 C C   . ASP B 1 117 ? -2.499  47.069 14.945  1.00 36.55  ?  272 ASP B C   1 
ATOM   2961 O O   . ASP B 1 117 ? -2.780  45.873 14.861  1.00 35.19  ?  272 ASP B O   1 
ATOM   2962 C CB  . ASP B 1 117 ? -1.856  48.233 12.758  1.00 33.77  ?  272 ASP B CB  1 
ATOM   2963 C CG  . ASP B 1 117 ? -2.412  48.930 11.527  1.00 46.19  ?  272 ASP B CG  1 
ATOM   2964 O OD1 . ASP B 1 117 ? -3.652  48.936 11.359  1.00 48.16  ?  272 ASP B OD1 1 
ATOM   2965 O OD2 . ASP B 1 117 ? -1.607  49.439 10.710  1.00 54.18  -1 272 ASP B OD2 1 
ATOM   2966 N N   . ARG B 1 118 ? -1.895  47.611 16.016  1.00 33.57  ?  273 ARG B N   1 
ATOM   2967 C CA  . ARG B 1 118 ? -1.467  46.822 17.166  1.00 32.39  ?  273 ARG B CA  1 
ATOM   2968 C C   . ARG B 1 118 ? -2.635  46.345 18.013  1.00 35.75  ?  273 ARG B C   1 
ATOM   2969 O O   . ARG B 1 118 ? -2.587  45.240 18.548  1.00 35.16  ?  273 ARG B O   1 
ATOM   2970 C CB  . ARG B 1 118 ? -0.395  47.548 17.992  1.00 32.07  ?  273 ARG B CB  1 
ATOM   2971 C CG  . ARG B 1 118 ? 0.891   47.865 17.217  1.00 34.27  ?  273 ARG B CG  1 
ATOM   2972 C CD  . ARG B 1 118 ? 1.728   46.671 16.746  1.00 31.76  ?  273 ARG B CD  1 
ATOM   2973 N NE  . ARG B 1 118 ? 1.175   45.914 15.605  1.00 28.04  ?  273 ARG B NE  1 
ATOM   2974 C CZ  . ARG B 1 118 ? 1.155   46.309 14.328  1.00 43.38  ?  273 ARG B CZ  1 
ATOM   2975 N NH1 . ARG B 1 118 ? 0.672   45.508 13.385  1.00 27.55  ?  273 ARG B NH1 1 
ATOM   2976 N NH2 . ARG B 1 118 ? 1.614   47.504 13.985  1.00 32.43  1  273 ARG B NH2 1 
ATOM   2977 N N   . LEU B 1 119 ? -3.724  47.141 18.057  1.00 31.17  ?  274 LEU B N   1 
ATOM   2978 C CA  . LEU B 1 119 ? -4.939  46.768 18.773  1.00 28.05  ?  274 LEU B CA  1 
ATOM   2979 C C   . LEU B 1 119 ? -5.675  45.670 18.018  1.00 30.24  ?  274 LEU B C   1 
ATOM   2980 O O   . LEU B 1 119 ? -6.368  44.859 18.641  1.00 32.43  ?  274 LEU B O   1 
ATOM   2981 C CB  . LEU B 1 119 ? -5.851  47.980 18.988  1.00 27.15  ?  274 LEU B CB  1 
ATOM   2982 C CG  . LEU B 1 119 ? -5.457  48.973 20.072  1.00 30.03  ?  274 LEU B CG  1 
ATOM   2983 C CD1 . LEU B 1 119 ? -6.455  50.156 20.102  1.00 29.29  ?  274 LEU B CD1 1 
ATOM   2984 C CD2 . LEU B 1 119 ? -5.359  48.299 21.432  1.00 27.76  ?  274 LEU B CD2 1 
ATOM   2985 N N   . SER B 1 120 ? -5.527  45.626 16.686  1.00 24.45  ?  275 SER B N   1 
ATOM   2986 C CA  . SER B 1 120 ? -6.193  44.588 15.903  1.00 24.34  ?  275 SER B CA  1 
ATOM   2987 C C   . SER B 1 120 ? -5.299  43.385 15.678  1.00 34.01  ?  275 SER B C   1 
ATOM   2988 O O   . SER B 1 120 ? -5.763  42.394 15.121  1.00 34.87  ?  275 SER B O   1 
ATOM   2989 C CB  . SER B 1 120 ? -6.670  45.145 14.573  1.00 26.42  ?  275 SER B CB  1 
ATOM   2990 O OG  . SER B 1 120 ? -5.597  45.621 13.789  1.00 40.16  ?  275 SER B OG  1 
ATOM   2991 N N   . CYS B 1 121 ? -4.025  43.454 16.165  1.00 32.95  ?  276 CYS B N   1 
ATOM   2992 C CA  . CYS B 1 121 ? -2.958  42.474 15.952  1.00 33.41  ?  276 CYS B CA  1 
ATOM   2993 C C   . CYS B 1 121 ? -2.664  42.225 14.465  1.00 38.52  ?  276 CYS B C   1 
ATOM   2994 O O   . CYS B 1 121 ? -2.352  41.102 14.081  1.00 38.99  ?  276 CYS B O   1 
ATOM   2995 C CB  . CYS B 1 121 ? -3.202  41.181 16.723  1.00 33.47  ?  276 CYS B CB  1 
ATOM   2996 S SG  . CYS B 1 121 ? -3.602  41.454 18.458  1.00 37.38  ?  276 CYS B SG  1 
ATOM   2997 N N   . LEU B 1 122 ? -2.719  43.294 13.648  1.00 35.53  ?  277 LEU B N   1 
ATOM   2998 C CA  . LEU B 1 122 ? -2.437  43.245 12.222  1.00 36.67  ?  277 LEU B CA  1 
ATOM   2999 C C   . LEU B 1 122 ? -1.032  42.660 11.953  1.00 39.91  ?  277 LEU B C   1 
ATOM   3000 O O   . LEU B 1 122 ? -0.066  43.034 12.641  1.00 39.33  ?  277 LEU B O   1 
ATOM   3001 C CB  . LEU B 1 122 ? -2.604  44.652 11.611  1.00 37.20  ?  277 LEU B CB  1 
ATOM   3002 C CG  . LEU B 1 122 ? -2.440  44.755 10.084  1.00 42.09  ?  277 LEU B CG  1 
ATOM   3003 C CD1 . LEU B 1 122 ? -3.609  44.093 9.343   1.00 42.60  ?  277 LEU B CD1 1 
ATOM   3004 C CD2 . LEU B 1 122 ? -2.307  46.169 9.663   1.00 38.98  ?  277 LEU B CD2 1 
ATOM   3005 N N   . ASP B 1 123 ? -0.953  41.689 11.009  1.00 35.09  ?  278 ASP B N   1 
ATOM   3006 C CA  . ASP B 1 123 ? 0.294   40.985 10.618  1.00 34.32  ?  278 ASP B CA  1 
ATOM   3007 C C   . ASP B 1 123 ? 0.876   40.068 11.700  1.00 37.85  ?  278 ASP B C   1 
ATOM   3008 O O   . ASP B 1 123 ? 2.093   39.759 11.687  1.00 35.49  ?  278 ASP B O   1 
ATOM   3009 C CB  . ASP B 1 123 ? 1.365   41.933 10.035  1.00 35.09  ?  278 ASP B CB  1 
ATOM   3010 C CG  . ASP B 1 123 ? 0.866   42.778 8.887   1.00 45.30  ?  278 ASP B CG  1 
ATOM   3011 O OD1 . ASP B 1 123 ? 0.302   42.217 7.950   1.00 47.59  ?  278 ASP B OD1 1 
ATOM   3012 O OD2 . ASP B 1 123 ? 1.086   43.998 8.912   1.00 52.78  -1 278 ASP B OD2 1 
ATOM   3013 N N   . GLY B 1 124 ? -0.008  39.623 12.607  1.00 33.16  ?  279 GLY B N   1 
ATOM   3014 C CA  . GLY B 1 124 ? 0.338   38.672 13.656  1.00 31.48  ?  279 GLY B CA  1 
ATOM   3015 C C   . GLY B 1 124 ? 1.151   39.184 14.811  1.00 33.21  ?  279 GLY B C   1 
ATOM   3016 O O   . GLY B 1 124 ? 1.799   38.396 15.503  1.00 35.62  ?  279 GLY B O   1 
ATOM   3017 N N   . THR B 1 125 ? 1.107   40.477 15.059  1.00 27.46  ?  280 THR B N   1 
ATOM   3018 C CA  . THR B 1 125 ? 1.796   41.058 16.221  1.00 26.76  ?  280 THR B CA  1 
ATOM   3019 C C   . THR B 1 125 ? 1.083   40.609 17.514  1.00 30.35  ?  280 THR B C   1 
ATOM   3020 O O   . THR B 1 125 ? -0.120  40.336 17.482  1.00 29.12  ?  280 THR B O   1 
ATOM   3021 C CB  . THR B 1 125 ? 1.864   42.572 16.098  1.00 32.33  ?  280 THR B CB  1 
ATOM   3022 O OG1 . THR B 1 125 ? 0.546   43.136 16.267  1.00 23.62  ?  280 THR B OG1 1 
ATOM   3023 C CG2 . THR B 1 125 ? 2.556   43.022 14.803  1.00 32.33  ?  280 THR B CG2 1 
ATOM   3024 N N   . PRO B 1 126 ? 1.784   40.453 18.653  1.00 28.46  ?  281 PRO B N   1 
ATOM   3025 C CA  . PRO B 1 126 ? 1.078   39.978 19.858  1.00 28.74  ?  281 PRO B CA  1 
ATOM   3026 C C   . PRO B 1 126 ? 0.145   41.023 20.447  1.00 36.92  ?  281 PRO B C   1 
ATOM   3027 O O   . PRO B 1 126 ? 0.387   42.217 20.236  1.00 38.15  ?  281 PRO B O   1 
ATOM   3028 C CB  . PRO B 1 126 ? 2.210   39.616 20.804  1.00 29.98  ?  281 PRO B CB  1 
ATOM   3029 C CG  . PRO B 1 126 ? 3.341   40.495 20.382  1.00 33.36  ?  281 PRO B CG  1 
ATOM   3030 C CD  . PRO B 1 126 ? 3.222   40.683 18.915  1.00 28.81  ?  281 PRO B CD  1 
ATOM   3031 N N   . PRO B 1 127 ? -0.971  40.635 21.116  1.00 36.51  ?  282 PRO B N   1 
ATOM   3032 C CA  . PRO B 1 127 ? -1.858  41.671 21.720  1.00 35.73  ?  282 PRO B CA  1 
ATOM   3033 C C   . PRO B 1 127 ? -1.109  42.544 22.748  1.00 37.82  ?  282 PRO B C   1 
ATOM   3034 O O   . PRO B 1 127 ? -0.269  42.034 23.476  1.00 37.05  ?  282 PRO B O   1 
ATOM   3035 C CB  . PRO B 1 127 ? -2.945  40.849 22.425  1.00 37.03  ?  282 PRO B CB  1 
ATOM   3036 C CG  . PRO B 1 127 ? -2.853  39.466 21.850  1.00 41.42  ?  282 PRO B CG  1 
ATOM   3037 C CD  . PRO B 1 127 ? -1.441  39.263 21.428  1.00 37.84  ?  282 PRO B CD  1 
ATOM   3038 N N   . LEU B 1 128 ? -1.389  43.841 22.797  1.00 33.71  ?  283 LEU B N   1 
ATOM   3039 C CA  . LEU B 1 128 ? -0.771  44.734 23.781  1.00 33.25  ?  283 LEU B CA  1 
ATOM   3040 C C   . LEU B 1 128 ? -1.360  44.455 25.160  1.00 35.72  ?  283 LEU B C   1 
ATOM   3041 O O   . LEU B 1 128 ? -2.575  44.319 25.297  1.00 36.16  ?  283 LEU B O   1 
ATOM   3042 C CB  . LEU B 1 128 ? -1.035  46.206 23.418  1.00 33.82  ?  283 LEU B CB  1 
ATOM   3043 C CG  . LEU B 1 128 ? -0.444  46.723 22.111  1.00 36.91  ?  283 LEU B CG  1 
ATOM   3044 C CD1 . LEU B 1 128 ? -1.063  48.035 21.716  1.00 34.18  ?  283 LEU B CD1 1 
ATOM   3045 C CD2 . LEU B 1 128 ? 1.057   46.873 22.234  1.00 40.04  ?  283 LEU B CD2 1 
ATOM   3046 N N   . SER B 1 129 ? -0.515  44.323 26.165  1.00 33.00  ?  284 SER B N   1 
ATOM   3047 C CA  . SER B 1 129 ? -0.977  44.126 27.543  1.00 33.90  ?  284 SER B CA  1 
ATOM   3048 C C   . SER B 1 129 ? -1.561  45.438 28.103  1.00 39.13  ?  284 SER B C   1 
ATOM   3049 O O   . SER B 1 129 ? -1.305  46.531 27.547  1.00 38.33  ?  284 SER B O   1 
ATOM   3050 C CB  . SER B 1 129 ? 0.168   43.642 28.435  1.00 37.07  ?  284 SER B CB  1 
ATOM   3051 O OG  . SER B 1 129 ? 1.055   44.679 28.826  1.00 43.30  ?  284 SER B OG  1 
ATOM   3052 N N   . TRP B 1 130 ? -2.331  45.324 29.212  1.00 37.09  ?  285 TRP B N   1 
ATOM   3053 C CA  . TRP B 1 130 ? -2.953  46.462 29.913  1.00 37.14  ?  285 TRP B CA  1 
ATOM   3054 C C   . TRP B 1 130 ? -1.943  47.497 30.305  1.00 37.66  ?  285 TRP B C   1 
ATOM   3055 O O   . TRP B 1 130 ? -2.158  48.680 30.046  1.00 34.82  ?  285 TRP B O   1 
ATOM   3056 C CB  . TRP B 1 130 ? -3.726  46.027 31.162  1.00 36.86  ?  285 TRP B CB  1 
ATOM   3057 C CG  . TRP B 1 130 ? -4.423  47.174 31.840  1.00 39.00  ?  285 TRP B CG  1 
ATOM   3058 C CD1 . TRP B 1 130 ? -4.200  47.640 33.106  1.00 41.88  ?  285 TRP B CD1 1 
ATOM   3059 C CD2 . TRP B 1 130 ? -5.357  48.081 31.239  1.00 39.08  ?  285 TRP B CD2 1 
ATOM   3060 N NE1 . TRP B 1 130 ? -4.951  48.767 33.334  1.00 41.41  ?  285 TRP B NE1 1 
ATOM   3061 C CE2 . TRP B 1 130 ? -5.712  49.028 32.225  1.00 43.26  ?  285 TRP B CE2 1 
ATOM   3062 C CE3 . TRP B 1 130 ? -5.912  48.197 29.953  1.00 40.64  ?  285 TRP B CE3 1 
ATOM   3063 C CZ2 . TRP B 1 130 ? -6.612  50.068 31.971  1.00 43.32  ?  285 TRP B CZ2 1 
ATOM   3064 C CZ3 . TRP B 1 130 ? -6.838  49.199 29.711  1.00 42.71  ?  285 TRP B CZ3 1 
ATOM   3065 C CH2 . TRP B 1 130 ? -7.203  50.106 30.718  1.00 43.69  ?  285 TRP B CH2 1 
ATOM   3066 N N   . HIS B 1 131 ? -0.825  47.038 30.896  1.00 36.53  ?  286 HIS B N   1 
ATOM   3067 C CA  . HIS B 1 131 ? 0.294   47.864 31.366  1.00 37.26  ?  286 HIS B CA  1 
ATOM   3068 C C   . HIS B 1 131 ? 0.819   48.744 30.238  1.00 44.30  ?  286 HIS B C   1 
ATOM   3069 O O   . HIS B 1 131 ? 0.962   49.982 30.414  1.00 44.14  ?  286 HIS B O   1 
ATOM   3070 C CB  . HIS B 1 131 ? 1.414   46.987 31.975  1.00 37.30  ?  286 HIS B CB  1 
ATOM   3071 N N   . MET B 1 132 ? 1.046   48.095 29.064  1.00 40.24  ?  287 MET B N   1 
ATOM   3072 C CA  . MET B 1 132 ? 1.508   48.778 27.871  1.00 39.78  ?  287 MET B CA  1 
ATOM   3073 C C   . MET B 1 132 ? 0.468   49.814 27.390  1.00 41.12  ?  287 MET B C   1 
ATOM   3074 O O   . MET B 1 132 ? 0.847   50.952 27.084  1.00 39.27  ?  287 MET B O   1 
ATOM   3075 C CB  . MET B 1 132 ? 1.872   47.760 26.791  1.00 42.40  ?  287 MET B CB  1 
ATOM   3076 C CG  . MET B 1 132 ? 2.869   48.287 25.775  1.00 46.62  ?  287 MET B CG  1 
ATOM   3077 S SD  . MET B 1 132 ? 4.298   49.251 26.358  1.00 51.05  ?  287 MET B SD  1 
ATOM   3078 C CE  . MET B 1 132 ? 5.125   47.984 27.487  1.00 48.11  ?  287 MET B CE  1 
ATOM   3079 N N   . ARG B 1 133 ? -0.838  49.444 27.408  1.00 36.59  ?  288 ARG B N   1 
ATOM   3080 C CA  . ARG B 1 133 ? -1.930  50.349 27.019  1.00 36.06  ?  288 ARG B CA  1 
ATOM   3081 C C   . ARG B 1 133 ? -1.991  51.592 27.871  1.00 38.43  ?  288 ARG B C   1 
ATOM   3082 O O   . ARG B 1 133 ? -2.300  52.655 27.343  1.00 38.57  ?  288 ARG B O   1 
ATOM   3083 C CB  . ARG B 1 133 ? -3.277  49.642 27.026  1.00 35.25  ?  288 ARG B CB  1 
ATOM   3084 C CG  . ARG B 1 133 ? -3.365  48.584 25.963  1.00 38.29  ?  288 ARG B CG  1 
ATOM   3085 C CD  . ARG B 1 133 ? -4.669  47.853 26.034  1.00 31.29  ?  288 ARG B CD  1 
ATOM   3086 N NE  . ARG B 1 133 ? -4.491  46.493 25.542  1.00 30.23  ?  288 ARG B NE  1 
ATOM   3087 C CZ  . ARG B 1 133 ? -5.347  45.847 24.766  1.00 35.91  ?  288 ARG B CZ  1 
ATOM   3088 N NH1 . ARG B 1 133 ? -6.484  46.424 24.390  1.00 23.36  ?  288 ARG B NH1 1 
ATOM   3089 N NH2 . ARG B 1 133 ? -5.109  44.593 24.413  1.00 24.12  1  288 ARG B NH2 1 
ATOM   3090 N N   . CYS B 1 134 ? -1.655  51.478 29.162  1.00 34.69  ?  289 CYS B N   1 
ATOM   3091 C CA  . CYS B 1 134 ? -1.606  52.612 30.077  1.00 35.56  ?  289 CYS B CA  1 
ATOM   3092 C C   . CYS B 1 134 ? -0.428  53.552 29.750  1.00 41.41  ?  289 CYS B C   1 
ATOM   3093 O O   . CYS B 1 134 ? -0.614  54.766 29.609  1.00 39.63  ?  289 CYS B O   1 
ATOM   3094 C CB  . CYS B 1 134 ? -1.578  52.132 31.519  1.00 36.68  ?  289 CYS B CB  1 
ATOM   3095 S SG  . CYS B 1 134 ? -3.030  51.150 31.974  1.00 41.79  ?  289 CYS B SG  1 
ATOM   3096 N N   . LYS B 1 135 ? 0.775   52.980 29.556  1.00 40.62  ?  290 LYS B N   1 
ATOM   3097 C CA  . LYS B 1 135 ? 1.959   53.748 29.163  1.00 39.72  ?  290 LYS B CA  1 
ATOM   3098 C C   . LYS B 1 135 ? 1.678   54.478 27.820  1.00 41.44  ?  290 LYS B C   1 
ATOM   3099 O O   . LYS B 1 135 ? 1.983   55.658 27.709  1.00 44.70  ?  290 LYS B O   1 
ATOM   3100 C CB  . LYS B 1 135 ? 3.200   52.841 29.090  1.00 42.73  ?  290 LYS B CB  1 
ATOM   3101 C CG  . LYS B 1 135 ? 3.716   52.349 30.451  1.00 55.97  ?  290 LYS B CG  1 
ATOM   3102 C CD  . LYS B 1 135 ? 4.588   53.399 31.174  1.00 67.27  ?  290 LYS B CD  1 
ATOM   3103 C CE  . LYS B 1 135 ? 4.543   53.291 32.679  1.00 79.52  ?  290 LYS B CE  1 
ATOM   3104 N NZ  . LYS B 1 135 ? 4.731   54.614 33.337  1.00 86.81  1  290 LYS B NZ  1 
ATOM   3105 N N   . ILE B 1 136 ? 0.997   53.829 26.871  1.00 33.08  ?  291 ILE B N   1 
ATOM   3106 C CA  . ILE B 1 136 ? 0.639   54.423 25.584  1.00 32.15  ?  291 ILE B CA  1 
ATOM   3107 C C   . ILE B 1 136 ? -0.355  55.579 25.717  1.00 35.73  ?  291 ILE B C   1 
ATOM   3108 O O   . ILE B 1 136 ? -0.146  56.627 25.101  1.00 35.91  ?  291 ILE B O   1 
ATOM   3109 C CB  . ILE B 1 136 ? 0.173   53.337 24.598  1.00 35.35  ?  291 ILE B CB  1 
ATOM   3110 C CG1 . ILE B 1 136 ? 1.381   52.549 24.050  1.00 34.89  ?  291 ILE B CG1 1 
ATOM   3111 C CG2 . ILE B 1 136 ? -0.713  53.913 23.468  1.00 36.20  ?  291 ILE B CG2 1 
ATOM   3112 C CD1 . ILE B 1 136 ? 1.091   51.071 23.662  1.00 35.79  ?  291 ILE B CD1 1 
ATOM   3113 N N   . ALA B 1 137 ? -1.452  55.376 26.487  1.00 30.51  ?  292 ALA B N   1 
ATOM   3114 C CA  . ALA B 1 137 ? -2.475  56.392 26.762  1.00 27.94  ?  292 ALA B CA  1 
ATOM   3115 C C   . ALA B 1 137 ? -1.767  57.639 27.344  1.00 32.19  ?  292 ALA B C   1 
ATOM   3116 O O   . ALA B 1 137 ? -1.957  58.750 26.827  1.00 31.68  ?  292 ALA B O   1 
ATOM   3117 C CB  . ALA B 1 137 ? -3.484  55.843 27.757  1.00 27.41  ?  292 ALA B CB  1 
ATOM   3118 N N   . GLN B 1 138 ? -0.878  57.419 28.351  1.00 28.29  ?  293 GLN B N   1 
ATOM   3119 C CA  . GLN B 1 138 ? -0.067  58.436 29.008  1.00 29.52  ?  293 GLN B CA  1 
ATOM   3120 C C   . GLN B 1 138 ? 0.779   59.229 28.002  1.00 37.44  ?  293 GLN B C   1 
ATOM   3121 O O   . GLN B 1 138 ? 0.679   60.459 27.953  1.00 39.40  ?  293 GLN B O   1 
ATOM   3122 C CB  . GLN B 1 138 ? 0.829   57.798 30.074  1.00 30.78  ?  293 GLN B CB  1 
ATOM   3123 C CG  . GLN B 1 138 ? 0.094   57.536 31.396  1.00 49.94  ?  293 GLN B CG  1 
ATOM   3124 C CD  . GLN B 1 138 ? 0.775   56.507 32.262  1.00 70.86  ?  293 GLN B CD  1 
ATOM   3125 O OE1 . GLN B 1 138 ? 2.010   56.415 32.340  1.00 72.85  ?  293 GLN B OE1 1 
ATOM   3126 N NE2 . GLN B 1 138 ? -0.020  55.719 32.952  1.00 57.84  ?  293 GLN B NE2 1 
ATOM   3127 N N   . GLY B 1 139 ? 1.539   58.513 27.174  1.00 32.71  ?  294 GLY B N   1 
ATOM   3128 C CA  . GLY B 1 139 ? 2.385   59.103 26.154  1.00 32.38  ?  294 GLY B CA  1 
ATOM   3129 C C   . GLY B 1 139 ? 1.629   59.935 25.156  1.00 38.72  ?  294 GLY B C   1 
ATOM   3130 O O   . GLY B 1 139 ? 2.003   61.074 24.901  1.00 39.49  ?  294 GLY B O   1 
ATOM   3131 N N   . ALA B 1 140 ? 0.561   59.375 24.593  1.00 37.43  ?  295 ALA B N   1 
ATOM   3132 C CA  . ALA B 1 140 ? -0.308  60.054 23.638  1.00 37.87  ?  295 ALA B CA  1 
ATOM   3133 C C   . ALA B 1 140 ? -0.907  61.321 24.281  1.00 41.87  ?  295 ALA B C   1 
ATOM   3134 O O   . ALA B 1 140 ? -0.998  62.351 23.618  1.00 41.95  ?  295 ALA B O   1 
ATOM   3135 C CB  . ALA B 1 140 ? -1.407  59.113 23.176  1.00 38.81  ?  295 ALA B CB  1 
ATOM   3136 N N   . ALA B 1 141 ? -1.227  61.268 25.587  1.00 38.33  ?  296 ALA B N   1 
ATOM   3137 C CA  . ALA B 1 141 ? -1.718  62.438 26.316  1.00 37.99  ?  296 ALA B CA  1 
ATOM   3138 C C   . ALA B 1 141 ? -0.623  63.506 26.432  1.00 42.20  ?  296 ALA B C   1 
ATOM   3139 O O   . ALA B 1 141 ? -0.942  64.693 26.467  1.00 42.32  ?  296 ALA B O   1 
ATOM   3140 C CB  . ALA B 1 141 ? -2.196  62.036 27.698  1.00 38.58  ?  296 ALA B CB  1 
ATOM   3141 N N   . ASN B 1 142 ? 0.656   63.096 26.487  1.00 39.67  ?  297 ASN B N   1 
ATOM   3142 C CA  . ASN B 1 142 ? 1.774   64.046 26.587  1.00 40.62  ?  297 ASN B CA  1 
ATOM   3143 C C   . ASN B 1 142 ? 1.999   64.820 25.289  1.00 44.10  ?  297 ASN B C   1 
ATOM   3144 O O   . ASN B 1 142 ? 2.158   66.051 25.347  1.00 42.57  ?  297 ASN B O   1 
ATOM   3145 C CB  . ASN B 1 142 ? 3.053   63.392 27.111  1.00 43.03  ?  297 ASN B CB  1 
ATOM   3146 C CG  . ASN B 1 142 ? 2.966   62.878 28.540  1.00 80.29  ?  297 ASN B CG  1 
ATOM   3147 O OD1 . ASN B 1 142 ? 1.885   62.740 29.155  1.00 70.59  ?  297 ASN B OD1 1 
ATOM   3148 N ND2 . ASN B 1 142 ? 4.127   62.550 29.096  1.00 77.77  ?  297 ASN B ND2 1 
ATOM   3149 N N   . GLY B 1 143 ? 1.923   64.099 24.153  1.00 39.99  ?  298 GLY B N   1 
ATOM   3150 C CA  . GLY B 1 143 ? 2.023   64.631 22.796  1.00 39.53  ?  298 GLY B CA  1 
ATOM   3151 C C   . GLY B 1 143 ? 0.946   65.659 22.522  1.00 44.82  ?  298 GLY B C   1 
ATOM   3152 O O   . GLY B 1 143 ? 1.275   66.783 22.134  1.00 45.56  ?  298 GLY B O   1 
ATOM   3153 N N   . ILE B 1 144 ? -0.349  65.307 22.786  1.00 41.07  ?  299 ILE B N   1 
ATOM   3154 C CA  . ILE B 1 144 ? -1.510  66.209 22.659  1.00 40.83  ?  299 ILE B CA  1 
ATOM   3155 C C   . ILE B 1 144 ? -1.291  67.434 23.537  1.00 47.20  ?  299 ILE B C   1 
ATOM   3156 O O   . ILE B 1 144 ? -1.445  68.563 23.069  1.00 48.02  ?  299 ILE B O   1 
ATOM   3157 C CB  . ILE B 1 144 ? -2.857  65.516 23.015  1.00 43.57  ?  299 ILE B CB  1 
ATOM   3158 C CG1 . ILE B 1 144 ? -3.123  64.313 22.086  1.00 43.65  ?  299 ILE B CG1 1 
ATOM   3159 C CG2 . ILE B 1 144 ? -4.041  66.533 22.997  1.00 43.45  ?  299 ILE B CG2 1 
ATOM   3160 C CD1 . ILE B 1 144 ? -4.180  63.403 22.557  1.00 48.61  ?  299 ILE B CD1 1 
ATOM   3161 N N   . ASN B 1 145 ? -0.907  67.214 24.797  1.00 44.49  ?  300 ASN B N   1 
ATOM   3162 C CA  . ASN B 1 145 ? -0.639  68.289 25.731  1.00 44.91  ?  300 ASN B CA  1 
ATOM   3163 C C   . ASN B 1 145 ? 0.427   69.261 25.224  1.00 48.47  ?  300 ASN B C   1 
ATOM   3164 O O   . ASN B 1 145 ? 0.287   70.465 25.417  1.00 48.29  ?  300 ASN B O   1 
ATOM   3165 C CB  . ASN B 1 145 ? -0.276  67.743 27.096  1.00 47.55  ?  300 ASN B CB  1 
ATOM   3166 C CG  . ASN B 1 145 ? 0.083   68.844 28.046  1.00 68.90  ?  300 ASN B CG  1 
ATOM   3167 O OD1 . ASN B 1 145 ? -0.774  69.617 28.476  1.00 59.66  ?  300 ASN B OD1 1 
ATOM   3168 N ND2 . ASN B 1 145 ? 1.370   69.018 28.282  1.00 62.30  ?  300 ASN B ND2 1 
ATOM   3169 N N   . PHE B 1 146 ? 1.483   68.741 24.583  1.00 43.90  ?  301 PHE B N   1 
ATOM   3170 C CA  . PHE B 1 146 ? 2.544   69.575 24.032  1.00 42.92  ?  301 PHE B CA  1 
ATOM   3171 C C   . PHE B 1 146 ? 1.965   70.453 22.912  1.00 47.71  ?  301 PHE B C   1 
ATOM   3172 O O   . PHE B 1 146 ? 2.197   71.660 22.904  1.00 46.92  ?  301 PHE B O   1 
ATOM   3173 C CB  . PHE B 1 146 ? 3.726   68.718 23.553  1.00 43.78  ?  301 PHE B CB  1 
ATOM   3174 C CG  . PHE B 1 146 ? 4.855   69.501 22.912  1.00 44.33  ?  301 PHE B CG  1 
ATOM   3175 C CD1 . PHE B 1 146 ? 5.824   70.123 23.694  1.00 45.92  ?  301 PHE B CD1 1 
ATOM   3176 C CD2 . PHE B 1 146 ? 4.939   69.629 21.527  1.00 45.26  ?  301 PHE B CD2 1 
ATOM   3177 C CE1 . PHE B 1 146 ? 6.866   70.834 23.104  1.00 46.51  ?  301 PHE B CE1 1 
ATOM   3178 C CE2 . PHE B 1 146 ? 5.971   70.355 20.941  1.00 48.45  ?  301 PHE B CE2 1 
ATOM   3179 C CZ  . PHE B 1 146 ? 6.938   70.942 21.732  1.00 46.68  ?  301 PHE B CZ  1 
ATOM   3180 N N   . LEU B 1 147 ? 1.167   69.856 22.010  1.00 44.81  ?  302 LEU B N   1 
ATOM   3181 C CA  . LEU B 1 147 ? 0.517   70.581 20.916  1.00 44.46  ?  302 LEU B CA  1 
ATOM   3182 C C   . LEU B 1 147 ? -0.405  71.675 21.424  1.00 46.43  ?  302 LEU B C   1 
ATOM   3183 O O   . LEU B 1 147 ? -0.400  72.769 20.878  1.00 44.97  ?  302 LEU B O   1 
ATOM   3184 C CB  . LEU B 1 147 ? -0.273  69.624 20.020  1.00 44.61  ?  302 LEU B CB  1 
ATOM   3185 C CG  . LEU B 1 147 ? 0.565   68.715 19.136  1.00 50.15  ?  302 LEU B CG  1 
ATOM   3186 C CD1 . LEU B 1 147 ? -0.238  67.516 18.714  1.00 51.54  ?  302 LEU B CD1 1 
ATOM   3187 C CD2 . LEU B 1 147 ? 1.075   69.451 17.918  1.00 52.16  ?  302 LEU B CD2 1 
ATOM   3188 N N   . HIS B 1 148 ? -1.195  71.369 22.463  1.00 43.54  ?  303 HIS B N   1 
ATOM   3189 C CA  . HIS B 1 148 ? -2.141  72.299 23.079  1.00 43.34  ?  303 HIS B CA  1 
ATOM   3190 C C   . HIS B 1 148 ? -1.432  73.475 23.755  1.00 48.92  ?  303 HIS B C   1 
ATOM   3191 O O   . HIS B 1 148 ? -1.828  74.632 23.530  1.00 49.08  ?  303 HIS B O   1 
ATOM   3192 C CB  . HIS B 1 148 ? -3.089  71.542 24.025  1.00 43.34  ?  303 HIS B CB  1 
ATOM   3193 C CG  . HIS B 1 148 ? -4.246  70.887 23.325  1.00 45.35  ?  303 HIS B CG  1 
ATOM   3194 N ND1 . HIS B 1 148 ? -5.473  70.563 23.799  1.00 46.32  ?  303 HIS B ND1 1 
ATOM   3195 C CD2 . HIS B 1 148 ? -4.187  70.565 21.977  1.00 45.73  ?  303 HIS B CD2 1 
ATOM   3196 C CE1 . HIS B 1 148 ? -6.178  70.031 22.740  1.00 44.95  ?  303 HIS B CE1 1 
ATOM   3197 N NE2 . HIS B 1 148 ? -5.373  70.059 21.678  1.00 45.18  ?  303 HIS B NE2 1 
ATOM   3198 N N   . GLU B 1 149 ? -0.323  73.181 24.498  1.00 45.70  ?  304 GLU B N   1 
ATOM   3199 C CA  . GLU B 1 149 ? 0.547   74.176 25.144  1.00 45.61  ?  304 GLU B CA  1 
ATOM   3200 C C   . GLU B 1 149 ? 1.160   75.095 24.073  1.00 51.24  ?  304 GLU B C   1 
ATOM   3201 O O   . GLU B 1 149 ? 1.450   76.259 24.343  1.00 52.15  ?  304 GLU B O   1 
ATOM   3202 C CB  . GLU B 1 149 ? 1.678   73.492 25.896  1.00 46.81  ?  304 GLU B CB  1 
ATOM   3203 C CG  . GLU B 1 149 ? 1.332   73.066 27.307  1.00 59.60  ?  304 GLU B CG  1 
ATOM   3204 C CD  . GLU B 1 149 ? 2.452   72.356 28.055  1.00 95.09  ?  304 GLU B CD  1 
ATOM   3205 O OE1 . GLU B 1 149 ? 3.542   72.148 27.468  1.00 83.86  ?  304 GLU B OE1 1 
ATOM   3206 O OE2 . GLU B 1 149 ? 2.237   72.009 29.240  1.00 98.59  -1 304 GLU B OE2 1 
ATOM   3207 N N   . ASN B 1 150 ? 1.333   74.565 22.862  1.00 47.85  ?  305 ASN B N   1 
ATOM   3208 C CA  . ASN B 1 150 ? 1.895   75.306 21.751  1.00 48.03  ?  305 ASN B CA  1 
ATOM   3209 C C   . ASN B 1 150 ? 0.820   75.864 20.837  1.00 54.37  ?  305 ASN B C   1 
ATOM   3210 O O   . ASN B 1 150 ? 1.100   76.194 19.678  1.00 54.66  ?  305 ASN B O   1 
ATOM   3211 C CB  . ASN B 1 150 ? 2.937   74.470 21.014  1.00 47.91  ?  305 ASN B CB  1 
ATOM   3212 C CG  . ASN B 1 150 ? 4.242   74.358 21.770  1.00 69.59  ?  305 ASN B CG  1 
ATOM   3213 O OD1 . ASN B 1 150 ? 5.258   74.921 21.357  1.00 57.41  ?  305 ASN B OD1 1 
ATOM   3214 N ND2 . ASN B 1 150 ? 4.244   73.639 22.896  1.00 65.13  ?  305 ASN B ND2 1 
ATOM   3215 N N   . HIS B 1 151 ? -0.417  75.993 21.382  1.00 51.72  ?  306 HIS B N   1 
ATOM   3216 C CA  . HIS B 1 151 ? -1.573  76.586 20.705  1.00 52.55  ?  306 HIS B CA  1 
ATOM   3217 C C   . HIS B 1 151 ? -1.867  75.956 19.358  1.00 56.15  ?  306 HIS B C   1 
ATOM   3218 O O   . HIS B 1 151 ? -2.042  76.656 18.358  1.00 55.58  ?  306 HIS B O   1 
ATOM   3219 C CB  . HIS B 1 151 ? -1.442  78.130 20.602  1.00 53.97  ?  306 HIS B CB  1 
ATOM   3220 C CG  . HIS B 1 151 ? -0.937  78.732 21.868  1.00 58.39  ?  306 HIS B CG  1 
ATOM   3221 N ND1 . HIS B 1 151 ? -1.788  78.970 22.934  1.00 60.75  ?  306 HIS B ND1 1 
ATOM   3222 C CD2 . HIS B 1 151 ? 0.335   79.008 22.247  1.00 60.72  ?  306 HIS B CD2 1 
ATOM   3223 C CE1 . HIS B 1 151 ? -1.019  79.424 23.911  1.00 60.55  ?  306 HIS B CE1 1 
ATOM   3224 N NE2 . HIS B 1 151 ? 0.268   79.450 23.549  1.00 60.93  ?  306 HIS B NE2 1 
ATOM   3225 N N   . HIS B 1 152 ? -1.899  74.622 19.342  1.00 52.80  ?  307 HIS B N   1 
ATOM   3226 C CA  . HIS B 1 152 ? -2.228  73.851 18.161  1.00 53.33  ?  307 HIS B CA  1 
ATOM   3227 C C   . HIS B 1 152 ? -3.327  72.882 18.472  1.00 55.31  ?  307 HIS B C   1 
ATOM   3228 O O   . HIS B 1 152 ? -3.362  72.303 19.564  1.00 54.30  ?  307 HIS B O   1 
ATOM   3229 C CB  . HIS B 1 152 ? -1.001  73.107 17.609  1.00 55.29  ?  307 HIS B CB  1 
ATOM   3230 C CG  . HIS B 1 152 ? -0.038  74.005 16.910  1.00 59.58  ?  307 HIS B CG  1 
ATOM   3231 N ND1 . HIS B 1 152 ? -0.343  74.577 15.682  1.00 61.73  ?  307 HIS B ND1 1 
ATOM   3232 C CD2 . HIS B 1 152 ? 1.188   74.423 17.296  1.00 60.94  ?  307 HIS B CD2 1 
ATOM   3233 C CE1 . HIS B 1 152 ? 0.710   75.318 15.370  1.00 60.63  ?  307 HIS B CE1 1 
ATOM   3234 N NE2 . HIS B 1 152 ? 1.652   75.251 16.309  1.00 60.64  ?  307 HIS B NE2 1 
ATOM   3235 N N   . ILE B 1 153 ? -4.237  72.718 17.507  1.00 51.46  ?  308 ILE B N   1 
ATOM   3236 C CA  . ILE B 1 153 ? -5.331  71.741 17.562  1.00 50.34  ?  308 ILE B CA  1 
ATOM   3237 C C   . ILE B 1 153 ? -4.970  70.732 16.470  1.00 52.86  ?  308 ILE B C   1 
ATOM   3238 O O   . ILE B 1 153 ? -4.689  71.138 15.332  1.00 53.34  ?  308 ILE B O   1 
ATOM   3239 C CB  . ILE B 1 153 ? -6.736  72.360 17.358  1.00 52.49  ?  308 ILE B CB  1 
ATOM   3240 C CG1 . ILE B 1 153 ? -6.942  73.642 18.185  1.00 52.68  ?  308 ILE B CG1 1 
ATOM   3241 C CG2 . ILE B 1 153 ? -7.824  71.340 17.659  1.00 52.43  ?  308 ILE B CG2 1 
ATOM   3242 C CD1 . ILE B 1 153 ? -7.854  74.667 17.501  1.00 64.02  ?  308 ILE B CD1 1 
ATOM   3243 N N   . HIS B 1 154 ? -4.917  69.437 16.826  1.00 45.89  ?  309 HIS B N   1 
ATOM   3244 C CA  . HIS B 1 154 ? -4.545  68.382 15.894  1.00 43.65  ?  309 HIS B CA  1 
ATOM   3245 C C   . HIS B 1 154 ? -5.565  68.224 14.804  1.00 45.43  ?  309 HIS B C   1 
ATOM   3246 O O   . HIS B 1 154 ? -5.191  68.181 13.633  1.00 45.59  ?  309 HIS B O   1 
ATOM   3247 C CB  . HIS B 1 154 ? -4.308  67.055 16.625  1.00 44.54  ?  309 HIS B CB  1 
ATOM   3248 C CG  . HIS B 1 154 ? -3.751  65.972 15.751  1.00 48.22  ?  309 HIS B CG  1 
ATOM   3249 N ND1 . HIS B 1 154 ? -4.559  65.276 14.856  1.00 49.65  ?  309 HIS B ND1 1 
ATOM   3250 C CD2 . HIS B 1 154 ? -2.479  65.524 15.630  1.00 49.56  ?  309 HIS B CD2 1 
ATOM   3251 C CE1 . HIS B 1 154 ? -3.759  64.420 14.248  1.00 48.97  ?  309 HIS B CE1 1 
ATOM   3252 N NE2 . HIS B 1 154 ? -2.498  64.542 14.668  1.00 49.29  ?  309 HIS B NE2 1 
ATOM   3253 N N   . ARG B 1 155 ? -6.854  68.165 15.179  1.00 41.13  ?  310 ARG B N   1 
ATOM   3254 C CA  . ARG B 1 155 ? -8.011  67.976 14.263  1.00 40.50  ?  310 ARG B CA  1 
ATOM   3255 C C   . ARG B 1 155 ? -8.204  66.535 13.686  1.00 44.26  ?  310 ARG B C   1 
ATOM   3256 O O   . ARG B 1 155 ? -9.185  66.298 12.981  1.00 43.49  ?  310 ARG B O   1 
ATOM   3257 C CB  . ARG B 1 155 ? -8.127  69.068 13.170  1.00 36.74  ?  310 ARG B CB  1 
ATOM   3258 C CG  . ARG B 1 155 ? -8.317  70.508 13.686  1.00 45.18  ?  310 ARG B CG  1 
ATOM   3259 C CD  . ARG B 1 155 ? -9.144  71.362 12.702  1.00 65.61  ?  310 ARG B CD  1 
ATOM   3260 N NE  . ARG B 1 155 ? -8.517  71.475 11.376  1.00 73.32  ?  310 ARG B NE  1 
ATOM   3261 C CZ  . ARG B 1 155 ? -9.150  71.724 10.228  1.00 79.46  ?  310 ARG B CZ  1 
ATOM   3262 N NH1 . ARG B 1 155 ? -10.468 71.911 10.213  1.00 60.55  ?  310 ARG B NH1 1 
ATOM   3263 N NH2 . ARG B 1 155 ? -8.470  71.784 9.090   1.00 61.26  1  310 ARG B NH2 1 
ATOM   3264 N N   . ASP B 1 156 ? -7.295  65.580 13.988  1.00 41.80  ?  311 ASP B N   1 
ATOM   3265 C CA  . ASP B 1 156 ? -7.429  64.191 13.506  1.00 42.00  ?  311 ASP B CA  1 
ATOM   3266 C C   . ASP B 1 156 ? -6.842  63.161 14.470  1.00 42.87  ?  311 ASP B C   1 
ATOM   3267 O O   . ASP B 1 156 ? -6.038  62.304 14.073  1.00 41.10  ?  311 ASP B O   1 
ATOM   3268 C CB  . ASP B 1 156 ? -6.880  64.005 12.076  1.00 44.69  ?  311 ASP B CB  1 
ATOM   3269 C CG  . ASP B 1 156 ? -7.650  62.979 11.262  1.00 62.30  ?  311 ASP B CG  1 
ATOM   3270 O OD1 . ASP B 1 156 ? -8.651  62.395 11.805  1.00 61.78  ?  311 ASP B OD1 1 
ATOM   3271 O OD2 . ASP B 1 156 ? -7.282  62.770 10.076  1.00 72.87  -1 311 ASP B OD2 1 
ATOM   3272 N N   . ILE B 1 157 ? -7.224  63.282 15.753  1.00 37.71  ?  312 ILE B N   1 
ATOM   3273 C CA  . ILE B 1 157 ? -6.781  62.381 16.803  1.00 36.61  ?  312 ILE B CA  1 
ATOM   3274 C C   . ILE B 1 157 ? -7.537  61.063 16.684  1.00 40.56  ?  312 ILE B C   1 
ATOM   3275 O O   . ILE B 1 157 ? -8.762  60.987 16.836  1.00 40.05  ?  312 ILE B O   1 
ATOM   3276 C CB  . ILE B 1 157 ? -6.902  63.048 18.177  1.00 39.36  ?  312 ILE B CB  1 
ATOM   3277 C CG1 . ILE B 1 157 ? -5.801  64.078 18.307  1.00 40.37  ?  312 ILE B CG1 1 
ATOM   3278 C CG2 . ILE B 1 157 ? -6.903  62.005 19.319  1.00 39.46  ?  312 ILE B CG2 1 
ATOM   3279 C CD1 . ILE B 1 157 ? -5.813  64.835 19.534  1.00 59.50  ?  312 ILE B CD1 1 
ATOM   3280 N N   . LYS B 1 158 ? -6.793  60.034 16.325  1.00 36.00  ?  313 LYS B N   1 
ATOM   3281 C CA  . LYS B 1 158 ? -7.318  58.690 16.155  1.00 34.23  ?  313 LYS B CA  1 
ATOM   3282 C C   . LYS B 1 158 ? -6.162  57.731 16.320  1.00 40.63  ?  313 LYS B C   1 
ATOM   3283 O O   . LYS B 1 158 ? -4.998  58.135 16.175  1.00 40.06  ?  313 LYS B O   1 
ATOM   3284 C CB  . LYS B 1 158 ? -8.041  58.522 14.808  1.00 33.14  ?  313 LYS B CB  1 
ATOM   3285 C CG  . LYS B 1 158 ? -7.250  58.828 13.561  1.00 26.50  ?  313 LYS B CG  1 
ATOM   3286 C CD  . LYS B 1 158 ? -8.158  58.718 12.383  1.00 35.17  ?  313 LYS B CD  1 
ATOM   3287 C CE  . LYS B 1 158 ? -7.472  58.910 11.064  1.00 45.16  ?  313 LYS B CE  1 
ATOM   3288 N NZ  . LYS B 1 158 ? -8.198  58.165 9.996   1.00 54.03  1  313 LYS B NZ  1 
ATOM   3289 N N   . SER B 1 159 ? -6.476  56.467 16.608  1.00 37.61  ?  314 SER B N   1 
ATOM   3290 C CA  . SER B 1 159 ? -5.467  55.456 16.820  1.00 36.80  ?  314 SER B CA  1 
ATOM   3291 C C   . SER B 1 159 ? -4.564  55.178 15.614  1.00 40.47  ?  314 SER B C   1 
ATOM   3292 O O   . SER B 1 159 ? -3.391  54.837 15.823  1.00 40.84  ?  314 SER B O   1 
ATOM   3293 C CB  . SER B 1 159 ? -6.065  54.198 17.428  1.00 40.03  ?  314 SER B CB  1 
ATOM   3294 O OG  . SER B 1 159 ? -7.074  53.655 16.598  1.00 46.96  ?  314 SER B OG  1 
ATOM   3295 N N   . ALA B 1 160 ? -5.055  55.414 14.371  1.00 34.84  ?  315 ALA B N   1 
ATOM   3296 C CA  . ALA B 1 160 ? -4.217  55.258 13.162  1.00 34.00  ?  315 ALA B CA  1 
ATOM   3297 C C   . ALA B 1 160 ? -3.125  56.320 13.173  1.00 38.79  ?  315 ALA B C   1 
ATOM   3298 O O   . ALA B 1 160 ? -2.071  56.101 12.586  1.00 37.04  ?  315 ALA B O   1 
ATOM   3299 C CB  . ALA B 1 160 ? -5.055  55.415 11.906  1.00 34.37  ?  315 ALA B CB  1 
ATOM   3300 N N   . ASN B 1 161 ? -3.386  57.467 13.863  1.00 37.90  ?  316 ASN B N   1 
ATOM   3301 C CA  . ASN B 1 161 ? -2.482  58.616 14.020  1.00 38.03  ?  316 ASN B CA  1 
ATOM   3302 C C   . ASN B 1 161 ? -1.646  58.614 15.323  1.00 42.81  ?  316 ASN B C   1 
ATOM   3303 O O   . ASN B 1 161 ? -0.988  59.611 15.627  1.00 44.48  ?  316 ASN B O   1 
ATOM   3304 C CB  . ASN B 1 161 ? -3.235  59.932 13.847  1.00 34.84  ?  316 ASN B CB  1 
ATOM   3305 C CG  . ASN B 1 161 ? -3.640  60.185 12.433  1.00 53.19  ?  316 ASN B CG  1 
ATOM   3306 O OD1 . ASN B 1 161 ? -3.138  59.560 11.480  1.00 39.17  ?  316 ASN B OD1 1 
ATOM   3307 N ND2 . ASN B 1 161 ? -4.563  61.119 12.270  1.00 49.29  ?  316 ASN B ND2 1 
ATOM   3308 N N   . ILE B 1 162 ? -1.687  57.514 16.097  1.00 35.52  ?  317 ILE B N   1 
ATOM   3309 C CA  . ILE B 1 162 ? -0.866  57.368 17.287  1.00 33.16  ?  317 ILE B CA  1 
ATOM   3310 C C   . ILE B 1 162 ? 0.065   56.233 16.927  1.00 35.81  ?  317 ILE B C   1 
ATOM   3311 O O   . ILE B 1 162 ? -0.350  55.070 16.866  1.00 35.30  ?  317 ILE B O   1 
ATOM   3312 C CB  . ILE B 1 162 ? -1.660  57.126 18.599  1.00 35.08  ?  317 ILE B CB  1 
ATOM   3313 C CG1 . ILE B 1 162 ? -2.610  58.308 18.889  1.00 33.87  ?  317 ILE B CG1 1 
ATOM   3314 C CG2 . ILE B 1 162 ? -0.687  56.885 19.773  1.00 34.72  ?  317 ILE B CG2 1 
ATOM   3315 C CD1 . ILE B 1 162 ? -3.750  57.994 19.788  1.00 37.78  ?  317 ILE B CD1 1 
ATOM   3316 N N   . LEU B 1 163 ? 1.309   56.584 16.614  1.00 31.36  ?  318 LEU B N   1 
ATOM   3317 C CA  . LEU B 1 163 ? 2.308   55.601 16.224  1.00 30.54  ?  318 LEU B CA  1 
ATOM   3318 C C   . LEU B 1 163 ? 3.163   55.109 17.377  1.00 34.42  ?  318 LEU B C   1 
ATOM   3319 O O   . LEU B 1 163 ? 3.169   55.720 18.446  1.00 33.51  ?  318 LEU B O   1 
ATOM   3320 C CB  . LEU B 1 163 ? 3.134   56.086 15.042  1.00 30.24  ?  318 LEU B CB  1 
ATOM   3321 C CG  . LEU B 1 163 ? 2.346   56.615 13.841  1.00 33.25  ?  318 LEU B CG  1 
ATOM   3322 C CD1 . LEU B 1 163 ? 3.259   57.128 12.805  1.00 32.12  ?  318 LEU B CD1 1 
ATOM   3323 C CD2 . LEU B 1 163 ? 1.463   55.574 13.262  1.00 33.61  ?  318 LEU B CD2 1 
ATOM   3324 N N   . LEU B 1 164 ? 3.818   53.947 17.185  1.00 32.37  ?  319 LEU B N   1 
ATOM   3325 C CA  . LEU B 1 164 ? 4.607   53.285 18.222  1.00 32.91  ?  319 LEU B CA  1 
ATOM   3326 C C   . LEU B 1 164 ? 6.021   52.949 17.797  1.00 39.95  ?  319 LEU B C   1 
ATOM   3327 O O   . LEU B 1 164 ? 6.213   52.267 16.795  1.00 40.12  ?  319 LEU B O   1 
ATOM   3328 C CB  . LEU B 1 164 ? 3.878   52.011 18.677  1.00 32.46  ?  319 LEU B CB  1 
ATOM   3329 C CG  . LEU B 1 164 ? 2.461   52.188 19.219  1.00 34.34  ?  319 LEU B CG  1 
ATOM   3330 C CD1 . LEU B 1 164 ? 1.750   50.882 19.269  1.00 32.08  ?  319 LEU B CD1 1 
ATOM   3331 C CD2 . LEU B 1 164 ? 2.470   52.900 20.579  1.00 34.83  ?  319 LEU B CD2 1 
ATOM   3332 N N   . ASP B 1 165 ? 7.019   53.431 18.562  1.00 38.12  ?  320 ASP B N   1 
ATOM   3333 C CA  . ASP B 1 165 ? 8.444   53.165 18.281  1.00 37.59  ?  320 ASP B CA  1 
ATOM   3334 C C   . ASP B 1 165 ? 8.850   51.764 18.812  1.00 43.36  ?  320 ASP B C   1 
ATOM   3335 O O   . ASP B 1 165 ? 8.003   51.051 19.353  1.00 41.95  ?  320 ASP B O   1 
ATOM   3336 C CB  . ASP B 1 165 ? 9.340   54.296 18.836  1.00 38.11  ?  320 ASP B CB  1 
ATOM   3337 C CG  . ASP B 1 165 ? 9.594   54.308 20.341  1.00 45.45  ?  320 ASP B CG  1 
ATOM   3338 O OD1 . ASP B 1 165 ? 9.118   53.374 21.044  1.00 43.42  ?  320 ASP B OD1 1 
ATOM   3339 O OD2 . ASP B 1 165 ? 10.279  55.244 20.818  1.00 51.61  -1 320 ASP B OD2 1 
ATOM   3340 N N   . GLU B 1 166 ? 10.133  51.382 18.688  1.00 42.63  ?  321 GLU B N   1 
ATOM   3341 C CA  . GLU B 1 166 ? 10.639  50.086 19.170  1.00 43.31  ?  321 GLU B CA  1 
ATOM   3342 C C   . GLU B 1 166 ? 10.329  49.822 20.667  1.00 45.09  ?  321 GLU B C   1 
ATOM   3343 O O   . GLU B 1 166 ? 10.146  48.666 21.047  1.00 43.66  ?  321 GLU B O   1 
ATOM   3344 C CB  . GLU B 1 166 ? 12.153  49.997 18.927  1.00 45.34  ?  321 GLU B CB  1 
ATOM   3345 C CG  . GLU B 1 166 ? 12.701  48.582 18.970  1.00 60.96  ?  321 GLU B CG  1 
ATOM   3346 C CD  . GLU B 1 166 ? 12.259  47.655 17.857  1.00 86.40  ?  321 GLU B CD  1 
ATOM   3347 O OE1 . GLU B 1 166 ? 12.761  47.811 16.718  1.00 102.09 ?  321 GLU B OE1 1 
ATOM   3348 O OE2 . GLU B 1 166 ? 11.449  46.741 18.137  1.00 67.89  -1 321 GLU B OE2 1 
ATOM   3349 N N   . ALA B 1 167 ? 10.281  50.897 21.504  1.00 40.84  ?  322 ALA B N   1 
ATOM   3350 C CA  . ALA B 1 167 ? 9.994   50.764 22.936  1.00 40.14  ?  322 ALA B CA  1 
ATOM   3351 C C   . ALA B 1 167 ? 8.488   50.948 23.248  1.00 43.53  ?  322 ALA B C   1 
ATOM   3352 O O   . ALA B 1 167 ? 8.113   50.947 24.423  1.00 43.79  ?  322 ALA B O   1 
ATOM   3353 C CB  . ALA B 1 167 ? 10.813  51.777 23.710  1.00 40.71  ?  322 ALA B CB  1 
ATOM   3354 N N   . PHE B 1 168 ? 7.633   51.095 22.194  1.00 35.94  ?  323 PHE B N   1 
ATOM   3355 C CA  . PHE B 1 168 ? 6.189   51.327 22.286  1.00 33.22  ?  323 PHE B CA  1 
ATOM   3356 C C   . PHE B 1 168 ? 5.865   52.711 22.845  1.00 36.25  ?  323 PHE B C   1 
ATOM   3357 O O   . PHE B 1 168 ? 4.848   52.897 23.539  1.00 33.71  ?  323 PHE B O   1 
ATOM   3358 C CB  . PHE B 1 168 ? 5.430   50.209 23.008  1.00 33.72  ?  323 PHE B CB  1 
ATOM   3359 C CG  . PHE B 1 168 ? 5.416   48.920 22.239  1.00 34.24  ?  323 PHE B CG  1 
ATOM   3360 C CD1 . PHE B 1 168 ? 6.480   48.025 22.332  1.00 35.84  ?  323 PHE B CD1 1 
ATOM   3361 C CD2 . PHE B 1 168 ? 4.360   48.611 21.381  1.00 33.93  ?  323 PHE B CD2 1 
ATOM   3362 C CE1 . PHE B 1 168 ? 6.483   46.841 21.596  1.00 35.95  ?  323 PHE B CE1 1 
ATOM   3363 C CE2 . PHE B 1 168 ? 4.366   47.427 20.648  1.00 35.85  ?  323 PHE B CE2 1 
ATOM   3364 C CZ  . PHE B 1 168 ? 5.420   46.540 20.770  1.00 33.78  ?  323 PHE B CZ  1 
ATOM   3365 N N   . THR B 1 169 ? 6.741   53.698 22.517  1.00 32.13  ?  324 THR B N   1 
ATOM   3366 C CA  . THR B 1 169 ? 6.509   55.091 22.881  1.00 31.75  ?  324 THR B CA  1 
ATOM   3367 C C   . THR B 1 169 ? 5.470   55.613 21.903  1.00 37.60  ?  324 THR B C   1 
ATOM   3368 O O   . THR B 1 169 ? 5.594   55.387 20.694  1.00 37.45  ?  324 THR B O   1 
ATOM   3369 C CB  . THR B 1 169 ? 7.819   55.887 22.877  1.00 35.83  ?  324 THR B CB  1 
ATOM   3370 O OG1 . THR B 1 169 ? 8.667   55.367 23.898  1.00 37.64  ?  324 THR B OG1 1 
ATOM   3371 C CG2 . THR B 1 169 ? 7.617   57.375 23.064  1.00 33.02  ?  324 THR B CG2 1 
ATOM   3372 N N   . ALA B 1 170 ? 4.410   56.249 22.441  1.00 34.93  ?  325 ALA B N   1 
ATOM   3373 C CA  . ALA B 1 170 ? 3.331   56.815 21.628  1.00 34.16  ?  325 ALA B CA  1 
ATOM   3374 C C   . ALA B 1 170 ? 3.858   58.059 20.942  1.00 40.25  ?  325 ALA B C   1 
ATOM   3375 O O   . ALA B 1 170 ? 4.560   58.872 21.566  1.00 40.57  ?  325 ALA B O   1 
ATOM   3376 C CB  . ALA B 1 170 ? 2.133   57.160 22.491  1.00 34.36  ?  325 ALA B CB  1 
ATOM   3377 N N   . LYS B 1 171 ? 3.579   58.168 19.632  1.00 35.43  ?  326 LYS B N   1 
ATOM   3378 C CA  . LYS B 1 171 ? 3.993   59.299 18.840  1.00 33.97  ?  326 LYS B CA  1 
ATOM   3379 C C   . LYS B 1 171 ? 2.853   59.730 17.946  1.00 38.92  ?  326 LYS B C   1 
ATOM   3380 O O   . LYS B 1 171 ? 2.450   58.977 17.051  1.00 40.00  ?  326 LYS B O   1 
ATOM   3381 C CB  . LYS B 1 171 ? 5.266   58.981 18.054  1.00 35.65  ?  326 LYS B CB  1 
ATOM   3382 C CG  . LYS B 1 171 ? 6.493   59.229 18.879  1.00 44.77  ?  326 LYS B CG  1 
ATOM   3383 C CD  . LYS B 1 171 ? 7.598   58.223 18.631  1.00 46.44  ?  326 LYS B CD  1 
ATOM   3384 C CE  . LYS B 1 171 ? 8.786   58.456 19.549  1.00 50.57  ?  326 LYS B CE  1 
ATOM   3385 N NZ  . LYS B 1 171 ? 9.317   59.850 19.444  1.00 62.20  1  326 LYS B NZ  1 
ATOM   3386 N N   . ILE B 1 172 ? 2.297   60.925 18.228  1.00 33.68  ?  327 ILE B N   1 
ATOM   3387 C CA  . ILE B 1 172 ? 1.202   61.537 17.470  1.00 32.87  ?  327 ILE B CA  1 
ATOM   3388 C C   . ILE B 1 172 ? 1.734   61.919 16.078  1.00 39.62  ?  327 ILE B C   1 
ATOM   3389 O O   . ILE B 1 172 ? 2.821   62.483 15.975  1.00 40.58  ?  327 ILE B O   1 
ATOM   3390 C CB  . ILE B 1 172 ? 0.629   62.774 18.215  1.00 35.10  ?  327 ILE B CB  1 
ATOM   3391 C CG1 . ILE B 1 172 ? 0.395   62.568 19.755  1.00 33.88  ?  327 ILE B CG1 1 
ATOM   3392 C CG2 . ILE B 1 172 ? -0.573  63.355 17.504  1.00 37.45  ?  327 ILE B CG2 1 
ATOM   3393 C CD1 . ILE B 1 172 ? -0.695  61.636 20.202  1.00 28.89  ?  327 ILE B CD1 1 
ATOM   3394 N N   . SER B 1 173 ? 0.997   61.571 15.021  1.00 37.60  ?  328 SER B N   1 
ATOM   3395 C CA  . SER B 1 173 ? 1.369   61.871 13.635  1.00 38.62  ?  328 SER B CA  1 
ATOM   3396 C C   . SER B 1 173 ? 0.211   62.562 12.906  1.00 47.13  ?  328 SER B C   1 
ATOM   3397 O O   . SER B 1 173 ? -0.829  62.806 13.508  1.00 46.04  ?  328 SER B O   1 
ATOM   3398 C CB  . SER B 1 173 ? 1.797   60.610 12.894  1.00 39.97  ?  328 SER B CB  1 
ATOM   3399 O OG  . SER B 1 173 ? 0.692   59.738 12.737  1.00 49.08  ?  328 SER B OG  1 
ATOM   3400 N N   . ASP B 1 174 ? 0.403   62.869 11.618  1.00 48.74  ?  329 ASP B N   1 
ATOM   3401 C CA  . ASP B 1 174 ? -0.556  63.499 10.722  1.00 51.86  ?  329 ASP B CA  1 
ATOM   3402 C C   . ASP B 1 174 ? -1.071  64.853 11.176  1.00 60.31  ?  329 ASP B C   1 
ATOM   3403 O O   . ASP B 1 174 ? -2.162  64.957 11.726  1.00 60.69  ?  329 ASP B O   1 
ATOM   3404 C CB  . ASP B 1 174 ? -1.692  62.545 10.322  1.00 54.94  ?  329 ASP B CB  1 
ATOM   3405 C CG  . ASP B 1 174 ? -2.081  62.618 8.855   1.00 74.90  ?  329 ASP B CG  1 
ATOM   3406 O OD1 . ASP B 1 174 ? -1.813  63.660 8.211   1.00 74.45  ?  329 ASP B OD1 1 
ATOM   3407 O OD2 . ASP B 1 174 ? -2.662  61.638 8.353   1.00 89.69  -1 329 ASP B OD2 1 
ATOM   3408 N N   . PHE B 1 175 ? -0.275  65.890 10.924  1.00 59.51  ?  330 PHE B N   1 
ATOM   3409 C CA  . PHE B 1 175 ? -0.568  67.281 11.272  1.00 60.61  ?  330 PHE B CA  1 
ATOM   3410 C C   . PHE B 1 175 ? -1.036  68.121 10.061  1.00 66.60  ?  330 PHE B C   1 
ATOM   3411 O O   . PHE B 1 175 ? -1.040  69.354 10.137  1.00 65.92  ?  330 PHE B O   1 
ATOM   3412 C CB  . PHE B 1 175 ? 0.651   67.928 11.950  1.00 62.28  ?  330 PHE B CB  1 
ATOM   3413 C CG  . PHE B 1 175 ? 1.142   67.157 13.145  1.00 64.33  ?  330 PHE B CG  1 
ATOM   3414 C CD1 . PHE B 1 175 ? 0.513   67.279 14.376  1.00 67.88  ?  330 PHE B CD1 1 
ATOM   3415 C CD2 . PHE B 1 175 ? 2.228   66.291 13.039  1.00 66.74  ?  330 PHE B CD2 1 
ATOM   3416 C CE1 . PHE B 1 175 ? 0.966   66.553 15.484  1.00 68.77  ?  330 PHE B CE1 1 
ATOM   3417 C CE2 . PHE B 1 175 ? 2.680   65.566 14.150  1.00 69.21  ?  330 PHE B CE2 1 
ATOM   3418 C CZ  . PHE B 1 175 ? 2.044   65.699 15.363  1.00 67.22  ?  330 PHE B CZ  1 
ATOM   3419 N N   . GLY B 1 176 ? -1.435  67.446 8.974   1.00 64.17  ?  331 GLY B N   1 
ATOM   3420 C CA  . GLY B 1 176 ? -1.932  68.077 7.754   1.00 64.84  ?  331 GLY B CA  1 
ATOM   3421 C C   . GLY B 1 176 ? -3.202  68.895 7.941   1.00 72.04  ?  331 GLY B C   1 
ATOM   3422 O O   . GLY B 1 176 ? -3.438  69.846 7.192   1.00 71.77  ?  331 GLY B O   1 
ATOM   3423 N N   . LEU B 1 177 ? -4.034  68.536 8.950   1.00 69.93  ?  332 LEU B N   1 
ATOM   3424 C CA  . LEU B 1 177 ? -5.274  69.237 9.297   1.00 69.54  ?  332 LEU B CA  1 
ATOM   3425 C C   . LEU B 1 177 ? -5.130  70.110 10.546  1.00 74.70  ?  332 LEU B C   1 
ATOM   3426 O O   . LEU B 1 177 ? -6.091  70.775 10.917  1.00 74.70  ?  332 LEU B O   1 
ATOM   3427 C CB  . LEU B 1 177 ? -6.446  68.245 9.471   1.00 69.49  ?  332 LEU B CB  1 
ATOM   3428 C CG  . LEU B 1 177 ? -7.148  67.729 8.201   1.00 74.39  ?  332 LEU B CG  1 
ATOM   3429 C CD1 . LEU B 1 177 ? -7.183  68.770 7.076   1.00 74.90  ?  332 LEU B CD1 1 
ATOM   3430 C CD2 . LEU B 1 177 ? -6.568  66.428 7.720   1.00 77.52  ?  332 LEU B CD2 1 
ATOM   3431 N N   . ALA B 1 178 ? -3.945  70.133 11.182  1.00 72.59  ?  333 ALA B N   1 
ATOM   3432 C CA  . ALA B 1 178 ? -3.709  70.927 12.395  1.00 73.28  ?  333 ALA B CA  1 
ATOM   3433 C C   . ALA B 1 178 ? -3.930  72.434 12.224  1.00 78.12  ?  333 ALA B C   1 
ATOM   3434 O O   . ALA B 1 178 ? -3.712  72.973 11.136  1.00 77.90  ?  333 ALA B O   1 
ATOM   3435 C CB  . ALA B 1 178 ? -2.318  70.655 12.948  1.00 74.12  ?  333 ALA B CB  1 
ATOM   3436 N N   . ARG B 1 179 ? -4.361  73.110 13.299  1.00 75.02  ?  334 ARG B N   1 
ATOM   3437 C CA  . ARG B 1 179 ? -4.597  74.556 13.262  1.00 75.01  ?  334 ARG B CA  1 
ATOM   3438 C C   . ARG B 1 179 ? -3.952  75.282 14.433  1.00 79.94  ?  334 ARG B C   1 
ATOM   3439 O O   . ARG B 1 179 ? -3.919  74.756 15.541  1.00 80.49  ?  334 ARG B O   1 
ATOM   3440 C CB  . ARG B 1 179 ? -6.113  74.860 13.254  1.00 74.36  ?  334 ARG B CB  1 
ATOM   3441 C CG  . ARG B 1 179 ? -6.819  74.632 11.916  1.00 80.14  ?  334 ARG B CG  1 
ATOM   3442 C CD  . ARG B 1 179 ? -6.727  75.813 10.956  1.00 80.94  ?  334 ARG B CD  1 
ATOM   3443 N NE  . ARG B 1 179 ? -7.766  75.770 9.922   1.00 87.15  ?  334 ARG B NE  1 
ATOM   3444 C CZ  . ARG B 1 179 ? -7.671  75.090 8.780   1.00 105.31 ?  334 ARG B CZ  1 
ATOM   3445 N NH1 . ARG B 1 179 ? -8.668  75.109 7.904   1.00 85.50  ?  334 ARG B NH1 1 
ATOM   3446 N NH2 . ARG B 1 179 ? -6.580  74.380 8.508   1.00 101.43 1  334 ARG B NH2 1 
ATOM   3447 N N   . ALA B 1 180 ? -3.492  76.504 14.206  1.00 76.48  ?  335 ALA B N   1 
ATOM   3448 C CA  . ALA B 1 180 ? -2.963  77.342 15.280  1.00 76.54  ?  335 ALA B CA  1 
ATOM   3449 C C   . ALA B 1 180 ? -4.123  78.216 15.792  1.00 81.11  ?  335 ALA B C   1 
ATOM   3450 O O   . ALA B 1 180 ? -4.750  78.896 14.972  1.00 81.24  ?  335 ALA B O   1 
ATOM   3451 C CB  . ALA B 1 180 ? -1.846  78.220 14.751  1.00 77.25  ?  335 ALA B CB  1 
ATOM   3452 N N   . SER B 1 181 ? -4.449  78.191 17.100  1.00 77.39  ?  336 SER B N   1 
ATOM   3453 C CA  . SER B 1 181 ? -5.564  79.008 17.615  1.00 89.18  ?  336 SER B CA  1 
ATOM   3454 C C   . SER B 1 181 ? -5.110  80.103 18.569  1.00 105.17 ?  336 SER B C   1 
ATOM   3455 O O   . SER B 1 181 ? -4.203  79.888 19.365  1.00 65.61  ?  336 SER B O   1 
ATOM   3456 C CB  . SER B 1 181 ? -6.591  78.115 18.315  1.00 20.00  ?  336 SER B CB  1 
HETATM 3457 N N   . TPO B 1 187 ? -13.210 79.415 19.758  1.00 90.96  ?  342 TPO B N   1 
HETATM 3458 C CA  . TPO B 1 187 ? -13.955 78.547 18.847  1.00 90.58  ?  342 TPO B CA  1 
HETATM 3459 C CB  . TPO B 1 187 ? -15.179 77.917 19.538  1.00 89.95  ?  342 TPO B CB  1 
HETATM 3460 C C   . TPO B 1 187 ? -14.268 79.254 17.522  1.00 94.35  ?  342 TPO B C   1 
HETATM 3461 O O   . TPO B 1 187 ? -14.978 80.266 17.514  1.00 93.74  ?  342 TPO B O   1 
ATOM   3462 N N   . VAL B 1 188 ? -13.718 78.722 16.408  1.00 90.63  ?  343 VAL B N   1 
ATOM   3463 C CA  . VAL B 1 188 ? -13.910 79.260 15.049  1.00 90.49  ?  343 VAL B CA  1 
ATOM   3464 C C   . VAL B 1 188 ? -14.753 78.327 14.145  1.00 94.17  ?  343 VAL B C   1 
ATOM   3465 O O   . VAL B 1 188 ? -15.271 77.322 14.637  1.00 94.26  ?  343 VAL B O   1 
ATOM   3466 C CB  . VAL B 1 188 ? -12.601 79.773 14.378  1.00 94.24  ?  343 VAL B CB  1 
ATOM   3467 C CG1 . VAL B 1 188 ? -12.023 80.966 15.136  1.00 94.20  ?  343 VAL B CG1 1 
ATOM   3468 C CG2 . VAL B 1 188 ? -11.564 78.664 14.214  1.00 93.96  ?  343 VAL B CG2 1 
ATOM   3469 N N   . MET B 1 189 ? -14.908 78.664 12.848  1.00 89.83  ?  344 MET B N   1 
ATOM   3470 C CA  . MET B 1 189 ? -15.709 77.883 11.899  1.00 89.64  ?  344 MET B CA  1 
ATOM   3471 C C   . MET B 1 189 ? -15.007 77.640 10.563  1.00 94.87  ?  344 MET B C   1 
ATOM   3472 O O   . MET B 1 189 ? -14.058 78.343 10.231  1.00 94.51  ?  344 MET B O   1 
ATOM   3473 C CB  . MET B 1 189 ? -17.058 78.575 11.657  1.00 91.80  ?  344 MET B CB  1 
ATOM   3474 C CG  . MET B 1 189 ? -18.139 78.206 12.663  1.00 95.05  ?  344 MET B CG  1 
ATOM   3475 S SD  . MET B 1 189 ? -18.870 76.547 12.503  1.00 98.70  ?  344 MET B SD  1 
ATOM   3476 C CE  . MET B 1 189 ? -19.339 76.526 10.758  1.00 94.92  ?  344 MET B CE  1 
HETATM 3477 N N   . TPO B 1 190 ? -15.491 76.667 9.781   1.00 93.62  ?  345 TPO B N   1 
HETATM 3478 C CA  . TPO B 1 190 ? -14.917 76.347 8.473   1.00 95.42  ?  345 TPO B CA  1 
HETATM 3479 C CB  . TPO B 1 190 ? -13.750 75.308 8.611   1.00 98.20  ?  345 TPO B CB  1 
HETATM 3480 C CG2 . TPO B 1 190 ? -14.250 73.977 9.200   1.00 98.04  ?  345 TPO B CG2 1 
HETATM 3481 O OG1 . TPO B 1 190 ? -13.071 74.977 7.351   1.00 100.72 ?  345 TPO B OG1 1 
HETATM 3482 P P   . TPO B 1 190 ? -12.000 75.983 6.819   1.00 102.01 ?  345 TPO B P   1 
HETATM 3483 O O1P . TPO B 1 190 ? -12.665 76.953 5.814   1.00 103.01 -1 345 TPO B O1P 1 
HETATM 3484 O O2P . TPO B 1 190 ? -11.338 76.747 7.986   1.00 101.24 ?  345 TPO B O2P 1 
HETATM 3485 O O3P . TPO B 1 190 ? -10.959 75.162 6.038   1.00 102.33 -1 345 TPO B O3P 1 
HETATM 3486 C C   . TPO B 1 190 ? -15.967 75.844 7.476   1.00 100.48 ?  345 TPO B C   1 
HETATM 3487 O O   . TPO B 1 190 ? -16.990 75.286 7.882   1.00 100.00 ?  345 TPO B O   1 
HETATM 3488 N N   . SEP B 1 191 ? -15.703 76.038 6.166   1.00 98.44  ?  346 SEP B N   1 
HETATM 3489 C CA  . SEP B 1 191 ? -16.584 75.581 5.083   1.00 99.35  ?  346 SEP B CA  1 
HETATM 3490 C CB  . SEP B 1 191 ? -16.860 76.532 3.918   1.00 102.62 ?  346 SEP B CB  1 
HETATM 3491 O OG  . SEP B 1 191 ? -15.673 76.838 3.191   1.00 106.17 ?  346 SEP B OG  1 
HETATM 3492 C C   . SEP B 1 191 ? -16.218 74.179 4.594   1.00 101.33 ?  346 SEP B C   1 
HETATM 3493 O O   . SEP B 1 191 ? -17.027 73.538 3.916   1.00 100.30 ?  346 SEP B O   1 
HETATM 3494 P P   . SEP B 1 191 ? -15.434 78.385 3.246   1.00 109.62 ?  346 SEP B P   1 
HETATM 3495 O O1P . SEP B 1 191 ? -14.136 78.734 2.506   1.00 110.39 -1 346 SEP B O1P 1 
HETATM 3496 O O2P . SEP B 1 191 ? -15.215 78.913 4.694   1.00 110.24 -1 346 SEP B O2P 1 
HETATM 3497 O O3P . SEP B 1 191 ? -16.614 79.122 2.584   1.00 109.61 ?  346 SEP B O3P 1 
ATOM   3498 N N   . ARG B 1 192 ? -15.001 73.702 4.946   1.00 97.18  ?  347 ARG B N   1 
ATOM   3499 C CA  . ARG B 1 192 ? -14.515 72.360 4.614   1.00 96.07  ?  347 ARG B CA  1 
ATOM   3500 C C   . ARG B 1 192 ? -14.386 71.519 5.898   1.00 95.94  ?  347 ARG B C   1 
ATOM   3501 O O   . ARG B 1 192 ? -13.460 71.733 6.689   1.00 95.37  ?  347 ARG B O   1 
ATOM   3502 C CB  . ARG B 1 192 ? -13.195 72.414 3.804   1.00 96.99  ?  347 ARG B CB  1 
ATOM   3503 C CG  . ARG B 1 192 ? -12.604 71.044 3.408   1.00 109.75 ?  347 ARG B CG  1 
ATOM   3504 C CD  . ARG B 1 192 ? -13.420 70.280 2.366   1.00 123.65 ?  347 ARG B CD  1 
ATOM   3505 N NE  . ARG B 1 192 ? -14.285 69.254 2.960   1.00 132.43 ?  347 ARG B NE  1 
ATOM   3506 C CZ  . ARG B 1 192 ? -14.114 67.941 2.810   1.00 143.48 ?  347 ARG B CZ  1 
ATOM   3507 N NH1 . ARG B 1 192 ? -13.106 67.474 2.080   1.00 128.66 ?  347 ARG B NH1 1 
ATOM   3508 N NH2 . ARG B 1 192 ? -14.950 67.088 3.385   1.00 127.41 1  347 ARG B NH2 1 
ATOM   3509 N N   . ILE B 1 193 ? -15.350 70.595 6.111   1.00 89.27  ?  348 ILE B N   1 
ATOM   3510 C CA  . ILE B 1 193 ? -15.388 69.703 7.276   1.00 87.43  ?  348 ILE B CA  1 
ATOM   3511 C C   . ILE B 1 193 ? -14.477 68.501 7.018   1.00 88.69  ?  348 ILE B C   1 
ATOM   3512 O O   . ILE B 1 193 ? -14.668 67.771 6.034   1.00 88.22  ?  348 ILE B O   1 
ATOM   3513 C CB  . ILE B 1 193 ? -16.840 69.324 7.688   1.00 89.91  ?  348 ILE B CB  1 
ATOM   3514 C CG1 . ILE B 1 193 ? -17.617 70.593 8.133   1.00 90.09  ?  348 ILE B CG1 1 
ATOM   3515 C CG2 . ILE B 1 193 ? -16.854 68.231 8.790   1.00 89.78  ?  348 ILE B CG2 1 
ATOM   3516 C CD1 . ILE B 1 193 ? -19.114 70.516 8.057   1.00 95.30  ?  348 ILE B CD1 1 
ATOM   3517 N N   . VAL B 1 194 ? -13.458 68.332 7.889   1.00 82.53  ?  349 VAL B N   1 
ATOM   3518 C CA  . VAL B 1 194 ? -12.443 67.284 7.768   1.00 81.00  ?  349 VAL B CA  1 
ATOM   3519 C C   . VAL B 1 194 ? -12.126 66.546 9.084   1.00 82.24  ?  349 VAL B C   1 
ATOM   3520 O O   . VAL B 1 194 ? -12.166 67.136 10.172  1.00 81.55  ?  349 VAL B O   1 
ATOM   3521 C CB  . VAL B 1 194 ? -11.155 67.807 7.077   1.00 84.48  ?  349 VAL B CB  1 
ATOM   3522 C CG1 . VAL B 1 194 ? -11.300 67.828 5.554   1.00 84.09  ?  349 VAL B CG1 1 
ATOM   3523 C CG2 . VAL B 1 194 ? -10.733 69.177 7.624   1.00 84.10  ?  349 VAL B CG2 1 
ATOM   3524 N N   . GLY B 1 195 ? -11.768 65.270 8.933   1.00 76.43  ?  350 GLY B N   1 
ATOM   3525 C CA  . GLY B 1 195 ? -11.386 64.362 10.010  1.00 74.77  ?  350 GLY B CA  1 
ATOM   3526 C C   . GLY B 1 195 ? -11.988 62.993 9.782   1.00 74.75  ?  350 GLY B C   1 
ATOM   3527 O O   . GLY B 1 195 ? -12.512 62.728 8.690   1.00 74.82  ?  350 GLY B O   1 
ATOM   3528 N N   . THR B 1 196 ? -11.919 62.105 10.802  1.00 66.59  ?  351 THR B N   1 
ATOM   3529 C CA  . THR B 1 196 ? -12.516 60.766 10.700  1.00 63.58  ?  351 THR B CA  1 
ATOM   3530 C C   . THR B 1 196 ? -13.776 60.770 11.556  1.00 60.35  ?  351 THR B C   1 
ATOM   3531 O O   . THR B 1 196 ? -13.688 60.815 12.788  1.00 58.00  ?  351 THR B O   1 
ATOM   3532 C CB  . THR B 1 196 ? -11.489 59.680 11.015  1.00 68.38  ?  351 THR B CB  1 
ATOM   3533 O OG1 . THR B 1 196 ? -10.347 59.913 10.193  1.00 67.01  ?  351 THR B OG1 1 
ATOM   3534 C CG2 . THR B 1 196 ? -12.026 58.265 10.779  1.00 63.04  ?  351 THR B CG2 1 
ATOM   3535 N N   . THR B 1 197 ? -14.948 60.771 10.882  1.00 52.93  ?  352 THR B N   1 
ATOM   3536 C CA  . THR B 1 197 ? -16.274 60.881 11.493  1.00 51.12  ?  352 THR B CA  1 
ATOM   3537 C C   . THR B 1 197 ? -16.466 60.041 12.747  1.00 51.94  ?  352 THR B C   1 
ATOM   3538 O O   . THR B 1 197 ? -17.088 60.520 13.708  1.00 53.20  ?  352 THR B O   1 
ATOM   3539 C CB  . THR B 1 197 ? -17.400 60.699 10.467  1.00 51.84  ?  352 THR B CB  1 
ATOM   3540 O OG1 . THR B 1 197 ? -17.391 59.358 9.984   1.00 55.16  ?  352 THR B OG1 1 
ATOM   3541 C CG2 . THR B 1 197 ? -17.310 61.670 9.313   1.00 44.10  ?  352 THR B CG2 1 
ATOM   3542 N N   . ALA B 1 198 ? -15.907 58.811 12.752  1.00 42.45  ?  353 ALA B N   1 
ATOM   3543 C CA  . ALA B 1 198 ? -16.018 57.878 13.864  1.00 40.34  ?  353 ALA B CA  1 
ATOM   3544 C C   . ALA B 1 198 ? -15.404 58.371 15.176  1.00 44.97  ?  353 ALA B C   1 
ATOM   3545 O O   . ALA B 1 198 ? -15.780 57.889 16.239  1.00 46.06  ?  353 ALA B O   1 
ATOM   3546 C CB  . ALA B 1 198 ? -15.424 56.549 13.474  1.00 40.84  ?  353 ALA B CB  1 
ATOM   3547 N N   . TYR B 1 199 ? -14.474 59.328 15.100  1.00 41.31  ?  354 TYR B N   1 
ATOM   3548 C CA  . TYR B 1 199 ? -13.765 59.891 16.255  1.00 41.08  ?  354 TYR B CA  1 
ATOM   3549 C C   . TYR B 1 199 ? -14.177 61.334 16.543  1.00 45.66  ?  354 TYR B C   1 
ATOM   3550 O O   . TYR B 1 199 ? -13.943 61.830 17.645  1.00 44.59  ?  354 TYR B O   1 
ATOM   3551 C CB  . TYR B 1 199 ? -12.249 59.880 15.988  1.00 41.54  ?  354 TYR B CB  1 
ATOM   3552 C CG  . TYR B 1 199 ? -11.658 58.508 15.771  1.00 43.14  ?  354 TYR B CG  1 
ATOM   3553 C CD1 . TYR B 1 199 ? -11.661 57.915 14.506  1.00 44.89  ?  354 TYR B CD1 1 
ATOM   3554 C CD2 . TYR B 1 199 ? -11.006 57.841 16.800  1.00 43.55  ?  354 TYR B CD2 1 
ATOM   3555 C CE1 . TYR B 1 199 ? -11.084 56.666 14.292  1.00 42.67  ?  354 TYR B CE1 1 
ATOM   3556 C CE2 . TYR B 1 199 ? -10.427 56.592 16.597  1.00 43.99  ?  354 TYR B CE2 1 
ATOM   3557 C CZ  . TYR B 1 199 ? -10.459 56.014 15.337  1.00 46.60  ?  354 TYR B CZ  1 
ATOM   3558 O OH  . TYR B 1 199 ? -9.917  54.771 15.123  1.00 41.80  ?  354 TYR B OH  1 
ATOM   3559 N N   . MET B 1 200 ? -14.735 62.008 15.541  1.00 44.13  ?  355 MET B N   1 
ATOM   3560 C CA  . MET B 1 200 ? -15.085 63.419 15.593  1.00 45.47  ?  355 MET B CA  1 
ATOM   3561 C C   . MET B 1 200 ? -16.143 63.807 16.600  1.00 51.73  ?  355 MET B C   1 
ATOM   3562 O O   . MET B 1 200 ? -17.195 63.169 16.682  1.00 51.18  ?  355 MET B O   1 
ATOM   3563 C CB  . MET B 1 200 ? -15.448 63.949 14.198  1.00 47.67  ?  355 MET B CB  1 
ATOM   3564 C CG  . MET B 1 200 ? -14.279 64.024 13.289  1.00 51.24  ?  355 MET B CG  1 
ATOM   3565 S SD  . MET B 1 200 ? -14.729 64.499 11.638  1.00 55.67  ?  355 MET B SD  1 
ATOM   3566 C CE  . MET B 1 200 ? -14.892 66.260 11.849  1.00 52.94  ?  355 MET B CE  1 
ATOM   3567 N N   . ALA B 1 201 ? -15.872 64.911 17.327  1.00 47.97  ?  356 ALA B N   1 
ATOM   3568 C CA  . ALA B 1 201 ? -16.790 65.507 18.282  1.00 47.46  ?  356 ALA B CA  1 
ATOM   3569 C C   . ALA B 1 201 ? -17.994 66.052 17.492  1.00 52.00  ?  356 ALA B C   1 
ATOM   3570 O O   . ALA B 1 201 ? -17.828 66.422 16.318  1.00 51.44  ?  356 ALA B O   1 
ATOM   3571 C CB  . ALA B 1 201 ? -16.092 66.618 19.042  1.00 48.28  ?  356 ALA B CB  1 
ATOM   3572 N N   . PRO B 1 202 ? -19.225 66.041 18.066  1.00 49.21  ?  357 PRO B N   1 
ATOM   3573 C CA  . PRO B 1 202 ? -20.394 66.522 17.294  1.00 48.52  ?  357 PRO B CA  1 
ATOM   3574 C C   . PRO B 1 202 ? -20.202 67.898 16.637  1.00 51.64  ?  357 PRO B C   1 
ATOM   3575 O O   . PRO B 1 202 ? -20.498 68.036 15.452  1.00 51.63  ?  357 PRO B O   1 
ATOM   3576 C CB  . PRO B 1 202 ? -21.540 66.493 18.316  1.00 50.10  ?  357 PRO B CB  1 
ATOM   3577 C CG  . PRO B 1 202 ? -20.878 66.376 19.660  1.00 54.72  ?  357 PRO B CG  1 
ATOM   3578 C CD  . PRO B 1 202 ? -19.618 65.612 19.427  1.00 50.35  ?  357 PRO B CD  1 
ATOM   3579 N N   . GLU B 1 203 ? -19.641 68.880 17.382  1.00 47.90  ?  358 GLU B N   1 
ATOM   3580 C CA  . GLU B 1 203 ? -19.386 70.232 16.880  1.00 48.40  ?  358 GLU B CA  1 
ATOM   3581 C C   . GLU B 1 203 ? -18.399 70.250 15.715  1.00 54.03  ?  358 GLU B C   1 
ATOM   3582 O O   . GLU B 1 203 ? -18.553 71.059 14.798  1.00 54.52  ?  358 GLU B O   1 
ATOM   3583 C CB  . GLU B 1 203 ? -18.947 71.195 18.009  1.00 49.65  ?  358 GLU B CB  1 
ATOM   3584 C CG  . GLU B 1 203 ? -17.567 70.943 18.604  1.00 58.45  ?  358 GLU B CG  1 
ATOM   3585 C CD  . GLU B 1 203 ? -17.447 69.862 19.666  1.00 77.99  ?  358 GLU B CD  1 
ATOM   3586 O OE1 . GLU B 1 203 ? -18.414 69.092 19.882  1.00 60.01  ?  358 GLU B OE1 1 
ATOM   3587 O OE2 . GLU B 1 203 ? -16.354 69.771 20.270  1.00 73.17  -1 358 GLU B OE2 1 
ATOM   3588 N N   . ALA B 1 204 ? -17.409 69.345 15.742  1.00 50.55  ?  359 ALA B N   1 
ATOM   3589 C CA  . ALA B 1 204 ? -16.403 69.232 14.692  1.00 50.50  ?  359 ALA B CA  1 
ATOM   3590 C C   . ALA B 1 204 ? -17.072 68.785 13.410  1.00 57.64  ?  359 ALA B C   1 
ATOM   3591 O O   . ALA B 1 204 ? -16.742 69.303 12.339  1.00 58.83  ?  359 ALA B O   1 
ATOM   3592 C CB  . ALA B 1 204 ? -15.316 68.252 15.105  1.00 50.90  ?  359 ALA B CB  1 
ATOM   3593 N N   . LEU B 1 205 ? -18.074 67.873 13.527  1.00 54.32  ?  360 LEU B N   1 
ATOM   3594 C CA  . LEU B 1 205 ? -18.864 67.374 12.397  1.00 53.03  ?  360 LEU B CA  1 
ATOM   3595 C C   . LEU B 1 205 ? -19.684 68.491 11.767  1.00 57.57  ?  360 LEU B C   1 
ATOM   3596 O O   . LEU B 1 205 ? -20.054 68.370 10.598  1.00 56.84  ?  360 LEU B O   1 
ATOM   3597 C CB  . LEU B 1 205 ? -19.743 66.184 12.822  1.00 52.17  ?  360 LEU B CB  1 
ATOM   3598 C CG  . LEU B 1 205 ? -19.014 64.870 13.096  1.00 54.69  ?  360 LEU B CG  1 
ATOM   3599 C CD1 . LEU B 1 205 ? -19.898 63.920 13.837  1.00 53.83  ?  360 LEU B CD1 1 
ATOM   3600 C CD2 . LEU B 1 205 ? -18.532 64.217 11.800  1.00 54.86  ?  360 LEU B CD2 1 
ATOM   3601 N N   . ARG B 1 206 ? -19.832 69.634 12.475  1.00 55.88  ?  361 ARG B N   1 
ATOM   3602 C CA  . ARG B 1 206 ? -20.536 70.808 11.958  1.00 56.11  ?  361 ARG B CA  1 
ATOM   3603 C C   . ARG B 1 206 ? -19.615 72.043 11.723  1.00 62.40  ?  361 ARG B C   1 
ATOM   3604 O O   . ARG B 1 206 ? -20.075 73.189 11.771  1.00 64.04  ?  361 ARG B O   1 
ATOM   3605 C CB  . ARG B 1 206 ? -21.838 71.085 12.743  1.00 53.59  ?  361 ARG B CB  1 
ATOM   3606 C CG  . ARG B 1 206 ? -22.958 70.105 12.340  1.00 59.75  ?  361 ARG B CG  1 
ATOM   3607 C CD  . ARG B 1 206 ? -24.256 70.173 13.139  1.00 62.12  ?  361 ARG B CD  1 
ATOM   3608 N NE  . ARG B 1 206 ? -24.073 69.892 14.567  1.00 69.69  ?  361 ARG B NE  1 
ATOM   3609 C CZ  . ARG B 1 206 ? -24.731 68.957 15.246  1.00 76.76  ?  361 ARG B CZ  1 
ATOM   3610 N NH1 . ARG B 1 206 ? -25.616 68.182 14.637  1.00 62.18  ?  361 ARG B NH1 1 
ATOM   3611 N NH2 . ARG B 1 206 ? -24.511 68.794 16.545  1.00 58.76  1  361 ARG B NH2 1 
ATOM   3612 N N   . GLY B 1 207 ? -18.339 71.785 11.429  1.00 57.97  ?  362 GLY B N   1 
ATOM   3613 C CA  . GLY B 1 207 ? -17.356 72.816 11.107  1.00 58.13  ?  362 GLY B CA  1 
ATOM   3614 C C   . GLY B 1 207 ? -16.681 73.591 12.230  1.00 62.98  ?  362 GLY B C   1 
ATOM   3615 O O   . GLY B 1 207 ? -15.717 74.307 11.963  1.00 62.73  ?  362 GLY B O   1 
ATOM   3616 N N   . GLU B 1 208 ? -17.174 73.499 13.479  1.00 60.13  ?  363 GLU B N   1 
ATOM   3617 C CA  . GLU B 1 208 ? -16.560 74.203 14.609  1.00 60.54  ?  363 GLU B CA  1 
ATOM   3618 C C   . GLU B 1 208 ? -15.152 73.627 14.958  1.00 66.61  ?  363 GLU B C   1 
ATOM   3619 O O   . GLU B 1 208 ? -14.990 72.415 15.103  1.00 65.38  ?  363 GLU B O   1 
ATOM   3620 C CB  . GLU B 1 208 ? -17.504 74.212 15.822  1.00 61.86  ?  363 GLU B CB  1 
ATOM   3621 N N   . ILE B 1 209 ? -14.140 74.522 15.060  1.00 65.48  ?  364 ILE B N   1 
ATOM   3622 C CA  . ILE B 1 209 ? -12.722 74.223 15.324  1.00 66.10  ?  364 ILE B CA  1 
ATOM   3623 C C   . ILE B 1 209 ? -12.358 74.662 16.766  1.00 70.11  ?  364 ILE B C   1 
ATOM   3624 O O   . ILE B 1 209 ? -12.331 75.859 17.063  1.00 70.37  ?  364 ILE B O   1 
ATOM   3625 C CB  . ILE B 1 209 ? -11.812 74.837 14.190  1.00 69.69  ?  364 ILE B CB  1 
ATOM   3626 C CG1 . ILE B 1 209 ? -12.086 74.138 12.816  1.00 70.65  ?  364 ILE B CG1 1 
ATOM   3627 C CG2 . ILE B 1 209 ? -10.317 74.772 14.540  1.00 71.21  ?  364 ILE B CG2 1 
ATOM   3628 C CD1 . ILE B 1 209 ? -11.702 74.895 11.552  1.00 80.88  ?  364 ILE B CD1 1 
ATOM   3629 N N   . THR B 1 210 ? -12.121 73.682 17.662  1.00 64.80  ?  365 THR B N   1 
ATOM   3630 C CA  . THR B 1 210 ? -11.817 73.935 19.079  1.00 62.96  ?  365 THR B CA  1 
ATOM   3631 C C   . THR B 1 210 ? -10.878 72.877 19.669  1.00 62.79  ?  365 THR B C   1 
ATOM   3632 O O   . THR B 1 210 ? -11.029 71.705 19.339  1.00 61.80  ?  365 THR B O   1 
ATOM   3633 C CB  . THR B 1 210 ? -13.123 74.127 19.906  1.00 67.96  ?  365 THR B CB  1 
ATOM   3634 O OG1 . THR B 1 210 ? -12.815 74.089 21.300  1.00 67.22  ?  365 THR B OG1 1 
ATOM   3635 C CG2 . THR B 1 210 ? -14.195 73.083 19.593  1.00 65.49  ?  365 THR B CG2 1 
ATOM   3636 N N   . PRO B 1 211 ? -9.935  73.231 20.576  1.00 57.76  ?  366 PRO B N   1 
ATOM   3637 C CA  . PRO B 1 211 ? -9.047  72.196 21.158  1.00 57.01  ?  366 PRO B CA  1 
ATOM   3638 C C   . PRO B 1 211 ? -9.820  71.144 21.940  1.00 60.45  ?  366 PRO B C   1 
ATOM   3639 O O   . PRO B 1 211 ? -9.327  70.035 22.106  1.00 59.75  ?  366 PRO B O   1 
ATOM   3640 C CB  . PRO B 1 211 ? -8.122  72.997 22.075  1.00 58.32  ?  366 PRO B CB  1 
ATOM   3641 C CG  . PRO B 1 211 ? -8.905  74.241 22.391  1.00 62.18  ?  366 PRO B CG  1 
ATOM   3642 C CD  . PRO B 1 211 ? -9.602  74.566 21.112  1.00 58.37  ?  366 PRO B CD  1 
ATOM   3643 N N   . LYS B 1 212 ? -11.047 71.489 22.395  1.00 57.01  ?  367 LYS B N   1 
ATOM   3644 C CA  . LYS B 1 212 ? -11.947 70.595 23.136  1.00 55.14  ?  367 LYS B CA  1 
ATOM   3645 C C   . LYS B 1 212 ? -12.431 69.428 22.256  1.00 54.07  ?  367 LYS B C   1 
ATOM   3646 O O   . LYS B 1 212 ? -12.805 68.386 22.789  1.00 52.51  ?  367 LYS B O   1 
ATOM   3647 C CB  . LYS B 1 212 ? -13.120 71.375 23.738  1.00 57.12  ?  367 LYS B CB  1 
ATOM   3648 N N   . SER B 1 213 ? -12.375 69.582 20.919  1.00 48.69  ?  368 SER B N   1 
ATOM   3649 C CA  . SER B 1 213 ? -12.722 68.523 19.964  1.00 48.55  ?  368 SER B CA  1 
ATOM   3650 C C   . SER B 1 213 ? -11.666 67.388 20.002  1.00 50.05  ?  368 SER B C   1 
ATOM   3651 O O   . SER B 1 213 ? -12.022 66.208 19.905  1.00 49.22  ?  368 SER B O   1 
ATOM   3652 C CB  . SER B 1 213 ? -12.845 69.072 18.549  1.00 53.39  ?  368 SER B CB  1 
ATOM   3653 O OG  . SER B 1 213 ? -13.967 69.928 18.402  1.00 63.35  ?  368 SER B OG  1 
ATOM   3654 N N   . ASP B 1 214 ? -10.376 67.759 20.187  1.00 44.32  ?  369 ASP B N   1 
ATOM   3655 C CA  . ASP B 1 214 ? -9.246  66.842 20.318  1.00 42.72  ?  369 ASP B CA  1 
ATOM   3656 C C   . ASP B 1 214 ? -9.432  65.949 21.538  1.00 47.63  ?  369 ASP B C   1 
ATOM   3657 O O   . ASP B 1 214 ? -9.139  64.757 21.466  1.00 49.71  ?  369 ASP B O   1 
ATOM   3658 C CB  . ASP B 1 214 ? -7.911  67.616 20.396  1.00 43.28  ?  369 ASP B CB  1 
ATOM   3659 C CG  . ASP B 1 214 ? -7.287  68.053 19.063  1.00 48.20  ?  369 ASP B CG  1 
ATOM   3660 O OD1 . ASP B 1 214 ? -7.906  67.811 17.998  1.00 48.90  ?  369 ASP B OD1 1 
ATOM   3661 O OD2 . ASP B 1 214 ? -6.181  68.635 19.086  1.00 51.34  -1 369 ASP B OD2 1 
ATOM   3662 N N   . ILE B 1 215 ? -9.958  66.507 22.641  1.00 42.49  ?  370 ILE B N   1 
ATOM   3663 C CA  . ILE B 1 215 ? -10.252 65.790 23.887  1.00 40.98  ?  370 ILE B CA  1 
ATOM   3664 C C   . ILE B 1 215 ? -11.316 64.717 23.647  1.00 46.60  ?  370 ILE B C   1 
ATOM   3665 O O   . ILE B 1 215 ? -11.168 63.596 24.139  1.00 48.40  ?  370 ILE B O   1 
ATOM   3666 C CB  . ILE B 1 215 ? -10.647 66.779 25.018  1.00 42.64  ?  370 ILE B CB  1 
ATOM   3667 C CG1 . ILE B 1 215 ? -9.559  67.838 25.257  1.00 41.73  ?  370 ILE B CG1 1 
ATOM   3668 C CG2 . ILE B 1 215 ? -11.063 66.062 26.317  1.00 43.10  ?  370 ILE B CG2 1 
ATOM   3669 C CD1 . ILE B 1 215 ? -8.297  67.334 25.895  1.00 51.25  ?  370 ILE B CD1 1 
ATOM   3670 N N   . TYR B 1 216 ? -12.368 65.049 22.880  1.00 42.67  ?  371 TYR B N   1 
ATOM   3671 C CA  . TYR B 1 216 ? -13.435 64.104 22.550  1.00 42.06  ?  371 TYR B CA  1 
ATOM   3672 C C   . TYR B 1 216 ? -12.870 62.938 21.725  1.00 47.16  ?  371 TYR B C   1 
ATOM   3673 O O   . TYR B 1 216 ? -13.135 61.790 22.060  1.00 47.88  ?  371 TYR B O   1 
ATOM   3674 C CB  . TYR B 1 216 ? -14.576 64.812 21.807  1.00 42.38  ?  371 TYR B CB  1 
ATOM   3675 C CG  . TYR B 1 216 ? -15.794 63.953 21.557  1.00 43.40  ?  371 TYR B CG  1 
ATOM   3676 C CD1 . TYR B 1 216 ? -15.864 63.107 20.441  1.00 45.39  ?  371 TYR B CD1 1 
ATOM   3677 C CD2 . TYR B 1 216 ? -16.887 63.993 22.421  1.00 43.59  ?  371 TYR B CD2 1 
ATOM   3678 C CE1 . TYR B 1 216 ? -16.981 62.308 20.206  1.00 46.20  ?  371 TYR B CE1 1 
ATOM   3679 C CE2 . TYR B 1 216 ? -18.016 63.207 22.192  1.00 45.15  ?  371 TYR B CE2 1 
ATOM   3680 C CZ  . TYR B 1 216 ? -18.059 62.366 21.081  1.00 55.71  ?  371 TYR B CZ  1 
ATOM   3681 O OH  . TYR B 1 216 ? -19.169 61.593 20.852  1.00 57.49  ?  371 TYR B OH  1 
ATOM   3682 N N   . SER B 1 217 ? -12.062 63.231 20.686  1.00 43.39  ?  372 SER B N   1 
ATOM   3683 C CA  . SER B 1 217 ? -11.431 62.233 19.829  1.00 42.62  ?  372 SER B CA  1 
ATOM   3684 C C   . SER B 1 217 ? -10.511 61.283 20.614  1.00 46.47  ?  372 SER B C   1 
ATOM   3685 O O   . SER B 1 217 ? -10.503 60.071 20.362  1.00 46.98  ?  372 SER B O   1 
ATOM   3686 C CB  . SER B 1 217 ? -10.648 62.920 18.731  1.00 45.66  ?  372 SER B CB  1 
ATOM   3687 O OG  . SER B 1 217 ? -11.540 63.459 17.780  1.00 54.46  ?  372 SER B OG  1 
ATOM   3688 N N   . PHE B 1 218 ? -9.797  61.826 21.605  1.00 41.10  ?  373 PHE B N   1 
ATOM   3689 C CA  . PHE B 1 218 ? -8.928  61.049 22.485  1.00 40.20  ?  373 PHE B CA  1 
ATOM   3690 C C   . PHE B 1 218 ? -9.738  60.104 23.368  1.00 44.56  ?  373 PHE B C   1 
ATOM   3691 O O   . PHE B 1 218 ? -9.255  59.019 23.681  1.00 46.41  ?  373 PHE B O   1 
ATOM   3692 C CB  . PHE B 1 218 ? -8.045  61.966 23.321  1.00 41.52  ?  373 PHE B CB  1 
ATOM   3693 C CG  . PHE B 1 218 ? -7.002  61.216 24.120  1.00 42.77  ?  373 PHE B CG  1 
ATOM   3694 C CD1 . PHE B 1 218 ? -5.992  60.513 23.485  1.00 44.61  ?  373 PHE B CD1 1 
ATOM   3695 C CD2 . PHE B 1 218 ? -7.046  61.198 25.509  1.00 44.50  ?  373 PHE B CD2 1 
ATOM   3696 C CE1 . PHE B 1 218 ? -5.047  59.807 24.218  1.00 45.27  ?  373 PHE B CE1 1 
ATOM   3697 C CE2 . PHE B 1 218 ? -6.099  60.496 26.241  1.00 47.16  ?  373 PHE B CE2 1 
ATOM   3698 C CZ  . PHE B 1 218 ? -5.101  59.810 25.591  1.00 45.70  ?  373 PHE B CZ  1 
ATOM   3699 N N   . GLY B 1 219 ? -10.953 60.514 23.741  1.00 39.33  ?  374 GLY B N   1 
ATOM   3700 C CA  . GLY B 1 219 ? -11.884 59.704 24.516  1.00 38.87  ?  374 GLY B CA  1 
ATOM   3701 C C   . GLY B 1 219 ? -12.296 58.466 23.740  1.00 43.41  ?  374 GLY B C   1 
ATOM   3702 O O   . GLY B 1 219 ? -12.413 57.389 24.330  1.00 43.21  ?  374 GLY B O   1 
ATOM   3703 N N   . VAL B 1 220 ? -12.473 58.599 22.386  1.00 39.07  ?  375 VAL B N   1 
ATOM   3704 C CA  . VAL B 1 220 ? -12.823 57.488 21.481  1.00 37.73  ?  375 VAL B CA  1 
ATOM   3705 C C   . VAL B 1 220 ? -11.629 56.517 21.446  1.00 39.59  ?  375 VAL B C   1 
ATOM   3706 O O   . VAL B 1 220 ? -11.812 55.311 21.472  1.00 37.45  ?  375 VAL B O   1 
ATOM   3707 C CB  . VAL B 1 220 ? -13.243 57.977 20.070  1.00 41.73  ?  375 VAL B CB  1 
ATOM   3708 C CG1 . VAL B 1 220 ? -13.568 56.812 19.137  1.00 41.26  ?  375 VAL B CG1 1 
ATOM   3709 C CG2 . VAL B 1 220 ? -14.431 58.928 20.149  1.00 42.06  ?  375 VAL B CG2 1 
ATOM   3710 N N   . VAL B 1 221 ? -10.410 57.066 21.444  1.00 37.40  ?  376 VAL B N   1 
ATOM   3711 C CA  . VAL B 1 221 ? -9.167  56.310 21.454  1.00 37.15  ?  376 VAL B CA  1 
ATOM   3712 C C   . VAL B 1 221 ? -9.068  55.506 22.745  1.00 40.19  ?  376 VAL B C   1 
ATOM   3713 O O   . VAL B 1 221 ? -8.778  54.316 22.685  1.00 40.39  ?  376 VAL B O   1 
ATOM   3714 C CB  . VAL B 1 221 ? -7.936  57.210 21.187  1.00 41.58  ?  376 VAL B CB  1 
ATOM   3715 C CG1 . VAL B 1 221 ? -6.631  56.455 21.421  1.00 41.51  ?  376 VAL B CG1 1 
ATOM   3716 C CG2 . VAL B 1 221 ? -7.978  57.775 19.767  1.00 41.69  ?  376 VAL B CG2 1 
ATOM   3717 N N   . LEU B 1 222 ? -9.376  56.126 23.894  1.00 36.23  ?  377 LEU B N   1 
ATOM   3718 C CA  . LEU B 1 222 ? -9.356  55.423 25.173  1.00 35.70  ?  377 LEU B CA  1 
ATOM   3719 C C   . LEU B 1 222 ? -10.362 54.264 25.180  1.00 39.02  ?  377 LEU B C   1 
ATOM   3720 O O   . LEU B 1 222 ? -10.040 53.192 25.692  1.00 38.33  ?  377 LEU B O   1 
ATOM   3721 C CB  . LEU B 1 222 ? -9.543  56.369 26.364  1.00 36.21  ?  377 LEU B CB  1 
ATOM   3722 C CG  . LEU B 1 222 ? -8.452  57.437 26.593  1.00 42.59  ?  377 LEU B CG  1 
ATOM   3723 C CD1 . LEU B 1 222 ? -8.834  58.345 27.702  1.00 44.11  ?  377 LEU B CD1 1 
ATOM   3724 C CD2 . LEU B 1 222 ? -7.093  56.835 26.935  1.00 44.78  ?  377 LEU B CD2 1 
ATOM   3725 N N   . LEU B 1 223 ? -11.534 54.432 24.525  1.00 35.68  ?  378 LEU B N   1 
ATOM   3726 C CA  . LEU B 1 223 ? -12.492 53.332 24.395  1.00 36.14  ?  378 LEU B CA  1 
ATOM   3727 C C   . LEU B 1 223 ? -11.900 52.216 23.522  1.00 42.83  ?  378 LEU B C   1 
ATOM   3728 O O   . LEU B 1 223 ? -12.099 51.042 23.839  1.00 44.75  ?  378 LEU B O   1 
ATOM   3729 C CB  . LEU B 1 223 ? -13.834 53.779 23.804  1.00 36.16  ?  378 LEU B CB  1 
ATOM   3730 C CG  . LEU B 1 223 ? -14.761 54.678 24.642  1.00 40.19  ?  378 LEU B CG  1 
ATOM   3731 C CD1 . LEU B 1 223 ? -16.119 54.815 23.934  1.00 38.50  ?  378 LEU B CD1 1 
ATOM   3732 C CD2 . LEU B 1 223 ? -14.903 54.175 26.121  1.00 42.46  ?  378 LEU B CD2 1 
ATOM   3733 N N   . GLU B 1 224 ? -11.143 52.572 22.453  1.00 37.39  ?  379 GLU B N   1 
ATOM   3734 C CA  . GLU B 1 224 ? -10.495 51.587 21.588  1.00 36.56  ?  379 GLU B CA  1 
ATOM   3735 C C   . GLU B 1 224 ? -9.456  50.835 22.431  1.00 42.42  ?  379 GLU B C   1 
ATOM   3736 O O   . GLU B 1 224 ? -9.355  49.612 22.352  1.00 41.36  ?  379 GLU B O   1 
ATOM   3737 C CB  . GLU B 1 224 ? -9.784  52.260 20.414  1.00 37.15  ?  379 GLU B CB  1 
ATOM   3738 C CG  . GLU B 1 224 ? -10.711 52.788 19.354  1.00 42.66  ?  379 GLU B CG  1 
ATOM   3739 C CD  . GLU B 1 224 ? -9.991  53.408 18.178  1.00 69.20  ?  379 GLU B CD  1 
ATOM   3740 O OE1 . GLU B 1 224 ? -9.162  54.319 18.401  1.00 62.69  ?  379 GLU B OE1 1 
ATOM   3741 O OE2 . GLU B 1 224 ? -10.255 52.984 17.031  1.00 71.78  -1 379 GLU B OE2 1 
ATOM   3742 N N   . ILE B 1 225 ? -8.702  51.570 23.259  1.00 39.70  ?  380 ILE B N   1 
ATOM   3743 C CA  . ILE B 1 225 ? -7.692  50.970 24.132  1.00 39.18  ?  380 ILE B CA  1 
ATOM   3744 C C   . ILE B 1 225 ? -8.327  49.952 25.134  1.00 43.04  ?  380 ILE B C   1 
ATOM   3745 O O   . ILE B 1 225 ? -7.792  48.842 25.288  1.00 45.49  ?  380 ILE B O   1 
ATOM   3746 C CB  . ILE B 1 225 ? -6.760  52.033 24.777  1.00 41.48  ?  380 ILE B CB  1 
ATOM   3747 C CG1 . ILE B 1 225 ? -5.856  52.705 23.714  1.00 41.20  ?  380 ILE B CG1 1 
ATOM   3748 C CG2 . ILE B 1 225 ? -5.918  51.422 25.872  1.00 42.89  ?  380 ILE B CG2 1 
ATOM   3749 C CD1 . ILE B 1 225 ? -5.003  53.929 24.195  1.00 47.19  ?  380 ILE B CD1 1 
ATOM   3750 N N   . ILE B 1 226 ? -9.490  50.282 25.734  1.00 33.69  ?  381 ILE B N   1 
ATOM   3751 C CA  . ILE B 1 226 ? -10.118 49.362 26.679  1.00 31.85  ?  381 ILE B CA  1 
ATOM   3752 C C   . ILE B 1 226 ? -10.699 48.108 25.988  1.00 36.92  ?  381 ILE B C   1 
ATOM   3753 O O   . ILE B 1 226 ? -10.596 47.000 26.509  1.00 35.34  ?  381 ILE B O   1 
ATOM   3754 C CB  . ILE B 1 226 ? -11.203 50.098 27.521  1.00 33.82  ?  381 ILE B CB  1 
ATOM   3755 C CG1 . ILE B 1 226 ? -10.601 51.216 28.376  1.00 32.47  ?  381 ILE B CG1 1 
ATOM   3756 C CG2 . ILE B 1 226 ? -12.020 49.114 28.388  1.00 34.57  ?  381 ILE B CG2 1 
ATOM   3757 C CD1 . ILE B 1 226 ? -11.597 52.435 28.659  1.00 24.08  ?  381 ILE B CD1 1 
ATOM   3758 N N   . THR B 1 227 ? -11.369 48.310 24.849  1.00 34.74  ?  382 THR B N   1 
ATOM   3759 C CA  . THR B 1 227 ? -12.113 47.279 24.142  1.00 34.10  ?  382 THR B CA  1 
ATOM   3760 C C   . THR B 1 227 ? -11.352 46.505 23.075  1.00 40.29  ?  382 THR B C   1 
ATOM   3761 O O   . THR B 1 227 ? -11.742 45.383 22.745  1.00 41.01  ?  382 THR B O   1 
ATOM   3762 C CB  . THR B 1 227 ? -13.401 47.883 23.551  1.00 36.63  ?  382 THR B CB  1 
ATOM   3763 O OG1 . THR B 1 227 ? -13.084 48.694 22.422  1.00 35.86  ?  382 THR B OG1 1 
ATOM   3764 C CG2 . THR B 1 227 ? -14.210 48.671 24.558  1.00 30.51  ?  382 THR B CG2 1 
ATOM   3765 N N   . GLY B 1 228 ? -10.336 47.122 22.486  1.00 37.32  ?  383 GLY B N   1 
ATOM   3766 C CA  . GLY B 1 228 ? -9.581  46.525 21.390  1.00 36.79  ?  383 GLY B CA  1 
ATOM   3767 C C   . GLY B 1 228 ? -10.358 46.562 20.087  1.00 40.19  ?  383 GLY B C   1 
ATOM   3768 O O   . GLY B 1 228 ? -9.962  45.941 19.101  1.00 41.42  ?  383 GLY B O   1 
ATOM   3769 N N   . LEU B 1 229 ? -11.476 47.290 20.081  1.00 36.33  ?  384 LEU B N   1 
ATOM   3770 C CA  . LEU B 1 229 ? -12.377 47.448 18.940  1.00 37.11  ?  384 LEU B CA  1 
ATOM   3771 C C   . LEU B 1 229 ? -12.098 48.735 18.193  1.00 41.79  ?  384 LEU B C   1 
ATOM   3772 O O   . LEU B 1 229 ? -11.934 49.773 18.846  1.00 42.73  ?  384 LEU B O   1 
ATOM   3773 C CB  . LEU B 1 229 ? -13.846 47.505 19.405  1.00 37.04  ?  384 LEU B CB  1 
ATOM   3774 C CG  . LEU B 1 229 ? -14.428 46.272 20.058  1.00 40.86  ?  384 LEU B CG  1 
ATOM   3775 C CD1 . LEU B 1 229 ? -15.638 46.625 20.801  1.00 41.00  ?  384 LEU B CD1 1 
ATOM   3776 C CD2 . LEU B 1 229 ? -14.761 45.230 19.042  1.00 42.88  ?  384 LEU B CD2 1 
ATOM   3777 N N   . PRO B 1 230 ? -12.103 48.718 16.834  1.00 35.96  ?  385 PRO B N   1 
ATOM   3778 C CA  . PRO B 1 230 ? -11.916 49.984 16.090  1.00 35.39  ?  385 PRO B CA  1 
ATOM   3779 C C   . PRO B 1 230 ? -13.140 50.899 16.271  1.00 39.90  ?  385 PRO B C   1 
ATOM   3780 O O   . PRO B 1 230 ? -14.225 50.387 16.519  1.00 39.28  ?  385 PRO B O   1 
ATOM   3781 C CB  . PRO B 1 230 ? -11.743 49.513 14.642  1.00 36.10  ?  385 PRO B CB  1 
ATOM   3782 C CG  . PRO B 1 230 ? -12.425 48.215 14.597  1.00 38.97  ?  385 PRO B CG  1 
ATOM   3783 C CD  . PRO B 1 230 ? -12.285 47.572 15.921  1.00 34.32  ?  385 PRO B CD  1 
ATOM   3784 N N   . ALA B 1 231 ? -12.978 52.238 16.172  1.00 38.10  ?  386 ALA B N   1 
ATOM   3785 C CA  . ALA B 1 231 ? -14.073 53.219 16.350  1.00 38.09  ?  386 ALA B CA  1 
ATOM   3786 C C   . ALA B 1 231 ? -15.268 52.961 15.437  1.00 44.79  ?  386 ALA B C   1 
ATOM   3787 O O   . ALA B 1 231 ? -16.413 53.195 15.825  1.00 43.53  ?  386 ALA B O   1 
ATOM   3788 C CB  . ALA B 1 231 ? -13.565 54.621 16.147  1.00 38.61  ?  386 ALA B CB  1 
ATOM   3789 N N   . VAL B 1 232 ? -14.986 52.475 14.222  1.00 44.76  ?  387 VAL B N   1 
ATOM   3790 C CA  . VAL B 1 232 ? -15.970 52.076 13.232  1.00 45.77  ?  387 VAL B CA  1 
ATOM   3791 C C   . VAL B 1 232 ? -15.554 50.732 12.640  1.00 52.06  ?  387 VAL B C   1 
ATOM   3792 O O   . VAL B 1 232 ? -14.368 50.512 12.383  1.00 51.13  ?  387 VAL B O   1 
ATOM   3793 C CB  . VAL B 1 232 ? -16.288 53.161 12.164  1.00 49.30  ?  387 VAL B CB  1 
ATOM   3794 C CG1 . VAL B 1 232 ? -15.075 53.477 11.299  1.00 49.27  ?  387 VAL B CG1 1 
ATOM   3795 C CG2 . VAL B 1 232 ? -17.478 52.751 11.295  1.00 48.87  ?  387 VAL B CG2 1 
ATOM   3796 N N   . ASP B 1 233 ? -16.532 49.833 12.471  1.00 50.84  ?  388 ASP B N   1 
ATOM   3797 C CA  . ASP B 1 233 ? -16.345 48.523 11.877  1.00 52.19  ?  388 ASP B CA  1 
ATOM   3798 C C   . ASP B 1 233 ? -17.617 48.205 11.131  1.00 59.07  ?  388 ASP B C   1 
ATOM   3799 O O   . ASP B 1 233 ? -18.662 48.015 11.755  1.00 59.15  ?  388 ASP B O   1 
ATOM   3800 C CB  . ASP B 1 233 ? -16.038 47.471 12.960  1.00 54.79  ?  388 ASP B CB  1 
ATOM   3801 C CG  . ASP B 1 233 ? -15.679 46.055 12.501  1.00 71.58  ?  388 ASP B CG  1 
ATOM   3802 O OD1 . ASP B 1 233 ? -15.494 45.845 11.282  1.00 73.53  ?  388 ASP B OD1 1 
ATOM   3803 O OD2 . ASP B 1 233 ? -15.541 45.166 13.372  1.00 77.29  -1 388 ASP B OD2 1 
ATOM   3804 N N   . GLU B 1 234 ? -17.528 48.201 9.785   1.00 56.99  ?  389 GLU B N   1 
ATOM   3805 C CA  . GLU B 1 234 ? -18.603 47.919 8.848   1.00 57.29  ?  389 GLU B CA  1 
ATOM   3806 C C   . GLU B 1 234 ? -19.264 46.551 9.108   1.00 63.28  ?  389 GLU B C   1 
ATOM   3807 O O   . GLU B 1 234 ? -20.475 46.405 8.933   1.00 64.62  ?  389 GLU B O   1 
ATOM   3808 C CB  . GLU B 1 234 ? -18.075 48.017 7.409   1.00 58.67  ?  389 GLU B CB  1 
ATOM   3809 N N   . HIS B 1 235 ? -18.477 45.570 9.552   1.00 59.69  ?  390 HIS B N   1 
ATOM   3810 C CA  . HIS B 1 235 ? -18.939 44.214 9.828   1.00 60.04  ?  390 HIS B CA  1 
ATOM   3811 C C   . HIS B 1 235 ? -19.262 43.976 11.318  1.00 61.33  ?  390 HIS B C   1 
ATOM   3812 O O   . HIS B 1 235 ? -19.151 42.854 11.803  1.00 60.12  ?  390 HIS B O   1 
ATOM   3813 C CB  . HIS B 1 235 ? -17.887 43.214 9.326   1.00 62.07  ?  390 HIS B CB  1 
ATOM   3814 C CG  . HIS B 1 235 ? -17.564 43.350 7.867   1.00 66.78  ?  390 HIS B CG  1 
ATOM   3815 N ND1 . HIS B 1 235 ? -18.565 43.458 6.910   1.00 69.17  ?  390 HIS B ND1 1 
ATOM   3816 C CD2 . HIS B 1 235 ? -16.359 43.365 7.245   1.00 69.01  ?  390 HIS B CD2 1 
ATOM   3817 C CE1 . HIS B 1 235 ? -17.938 43.541 5.746   1.00 68.77  ?  390 HIS B CE1 1 
ATOM   3818 N NE2 . HIS B 1 235 ? -16.610 43.483 5.896   1.00 68.93  ?  390 HIS B NE2 1 
ATOM   3819 N N   . ARG B 1 236 ? -19.689 45.027 12.036  1.00 56.47  ?  391 ARG B N   1 
ATOM   3820 C CA  . ARG B 1 236 ? -19.984 44.918 13.462  1.00 55.17  ?  391 ARG B CA  1 
ATOM   3821 C C   . ARG B 1 236 ? -21.280 45.587 13.856  1.00 57.44  ?  391 ARG B C   1 
ATOM   3822 O O   . ARG B 1 236 ? -21.635 46.611 13.283  1.00 57.06  ?  391 ARG B O   1 
ATOM   3823 C CB  . ARG B 1 236 ? -18.814 45.496 14.271  1.00 53.99  ?  391 ARG B CB  1 
ATOM   3824 C CG  . ARG B 1 236 ? -18.942 45.412 15.791  1.00 63.17  ?  391 ARG B CG  1 
ATOM   3825 C CD  . ARG B 1 236 ? -17.816 46.149 16.490  1.00 69.07  ?  391 ARG B CD  1 
ATOM   3826 N NE  . ARG B 1 236 ? -17.902 47.603 16.330  1.00 65.06  ?  391 ARG B NE  1 
ATOM   3827 C CZ  . ARG B 1 236 ? -16.848 48.415 16.282  1.00 81.49  ?  391 ARG B CZ  1 
ATOM   3828 N NH1 . ARG B 1 236 ? -15.618 47.927 16.370  1.00 70.46  ?  391 ARG B NH1 1 
ATOM   3829 N NH2 . ARG B 1 236 ? -17.019 49.722 16.127  1.00 69.48  1  391 ARG B NH2 1 
ATOM   3830 N N   . GLU B 1 237 ? -21.984 44.990 14.839  1.00 52.48  ?  392 GLU B N   1 
ATOM   3831 C CA  . GLU B 1 237 ? -23.207 45.525 15.402  1.00 51.46  ?  392 GLU B CA  1 
ATOM   3832 C C   . GLU B 1 237 ? -22.923 45.802 16.890  1.00 56.01  ?  392 GLU B C   1 
ATOM   3833 O O   . GLU B 1 237 ? -22.703 44.868 17.663  1.00 55.61  ?  392 GLU B O   1 
ATOM   3834 C CB  . GLU B 1 237 ? -24.384 44.567 15.195  1.00 52.59  ?  392 GLU B CB  1 
ATOM   3835 N N   . PRO B 1 238 ? -22.834 47.075 17.311  1.00 53.41  ?  393 PRO B N   1 
ATOM   3836 C CA  . PRO B 1 238 ? -23.024 48.279 16.509  1.00 53.16  ?  393 PRO B CA  1 
ATOM   3837 C C   . PRO B 1 238 ? -21.748 48.677 15.778  1.00 57.95  ?  393 PRO B C   1 
ATOM   3838 O O   . PRO B 1 238 ? -20.645 48.542 16.323  1.00 58.40  ?  393 PRO B O   1 
ATOM   3839 C CB  . PRO B 1 238 ? -23.486 49.308 17.548  1.00 55.25  ?  393 PRO B CB  1 
ATOM   3840 C CG  . PRO B 1 238 ? -22.832 48.885 18.855  1.00 59.87  ?  393 PRO B CG  1 
ATOM   3841 C CD  . PRO B 1 238 ? -22.551 47.400 18.732  1.00 55.75  ?  393 PRO B CD  1 
ATOM   3842 N N   . GLN B 1 239 ? -21.909 49.138 14.531  1.00 53.32  ?  394 GLN B N   1 
ATOM   3843 C CA  . GLN B 1 239 ? -20.868 49.631 13.632  1.00 52.05  ?  394 GLN B CA  1 
ATOM   3844 C C   . GLN B 1 239 ? -20.013 50.747 14.270  1.00 54.79  ?  394 GLN B C   1 
ATOM   3845 O O   . GLN B 1 239 ? -18.813 50.801 14.005  1.00 54.69  ?  394 GLN B O   1 
ATOM   3846 C CB  . GLN B 1 239 ? -21.550 50.163 12.374  1.00 53.21  ?  394 GLN B CB  1 
ATOM   3847 C CG  . GLN B 1 239 ? -20.811 49.889 11.086  1.00 67.46  ?  394 GLN B CG  1 
ATOM   3848 C CD  . GLN B 1 239 ? -21.672 49.155 10.085  1.00 95.31  ?  394 GLN B CD  1 
ATOM   3849 O OE1 . GLN B 1 239 ? -22.387 48.196 10.415  1.00 94.98  ?  394 GLN B OE1 1 
ATOM   3850 N NE2 . GLN B 1 239 ? -21.575 49.549 8.818   1.00 84.95  ?  394 GLN B NE2 1 
ATOM   3851 N N   . LEU B 1 240 ? -20.623 51.623 15.106  1.00 49.64  ?  395 LEU B N   1 
ATOM   3852 C CA  . LEU B 1 240 ? -19.914 52.720 15.770  1.00 49.67  ?  395 LEU B CA  1 
ATOM   3853 C C   . LEU B 1 240 ? -19.682 52.417 17.241  1.00 53.72  ?  395 LEU B C   1 
ATOM   3854 O O   . LEU B 1 240 ? -20.628 52.072 17.939  1.00 53.63  ?  395 LEU B O   1 
ATOM   3855 C CB  . LEU B 1 240 ? -20.675 54.066 15.597  1.00 49.60  ?  395 LEU B CB  1 
ATOM   3856 C CG  . LEU B 1 240 ? -20.325 55.020 14.425  1.00 53.16  ?  395 LEU B CG  1 
ATOM   3857 C CD1 . LEU B 1 240 ? -18.956 55.566 14.563  1.00 53.98  ?  395 LEU B CD1 1 
ATOM   3858 C CD2 . LEU B 1 240 ? -20.485 54.381 13.071  1.00 54.75  ?  395 LEU B CD2 1 
ATOM   3859 N N   . LEU B 1 241 ? -18.415 52.539 17.698  1.00 50.20  ?  396 LEU B N   1 
ATOM   3860 C CA  . LEU B 1 241 ? -17.971 52.304 19.081  1.00 50.33  ?  396 LEU B CA  1 
ATOM   3861 C C   . LEU B 1 241 ? -18.637 53.280 20.044  1.00 54.13  ?  396 LEU B C   1 
ATOM   3862 O O   . LEU B 1 241 ? -18.892 52.938 21.192  1.00 53.80  ?  396 LEU B O   1 
ATOM   3863 C CB  . LEU B 1 241 ? -16.422 52.404 19.193  1.00 49.99  ?  396 LEU B CB  1 
ATOM   3864 C CG  . LEU B 1 241 ? -15.708 51.935 20.490  1.00 53.30  ?  396 LEU B CG  1 
ATOM   3865 C CD1 . LEU B 1 241 ? -15.908 50.439 20.728  1.00 53.77  ?  396 LEU B CD1 1 
ATOM   3866 C CD2 . LEU B 1 241 ? -14.239 52.219 20.412  1.00 54.66  ?  396 LEU B CD2 1 
ATOM   3867 N N   . LEU B 1 242 ? -18.929 54.491 19.564  1.00 50.52  ?  397 LEU B N   1 
ATOM   3868 C CA  . LEU B 1 242 ? -19.635 55.521 20.304  1.00 49.61  ?  397 LEU B CA  1 
ATOM   3869 C C   . LEU B 1 242 ? -21.029 55.007 20.772  1.00 55.50  ?  397 LEU B C   1 
ATOM   3870 O O   . LEU B 1 242 ? -21.472 55.394 21.856  1.00 54.32  ?  397 LEU B O   1 
ATOM   3871 C CB  . LEU B 1 242 ? -19.763 56.754 19.408  1.00 48.63  ?  397 LEU B CB  1 
ATOM   3872 C CG  . LEU B 1 242 ? -19.031 58.040 19.848  1.00 51.31  ?  397 LEU B CG  1 
ATOM   3873 C CD1 . LEU B 1 242 ? -17.980 57.800 20.920  1.00 49.89  ?  397 LEU B CD1 1 
ATOM   3874 C CD2 . LEU B 1 242 ? -18.429 58.729 18.671  1.00 53.12  ?  397 LEU B CD2 1 
ATOM   3875 N N   . ASP B 1 243 ? -21.679 54.097 19.991  1.00 53.33  ?  398 ASP B N   1 
ATOM   3876 C CA  . ASP B 1 243 ? -22.972 53.484 20.362  1.00 54.22  ?  398 ASP B CA  1 
ATOM   3877 C C   . ASP B 1 243 ? -22.866 52.591 21.604  1.00 59.89  ?  398 ASP B C   1 
ATOM   3878 O O   . ASP B 1 243 ? -23.835 52.519 22.361  1.00 61.57  ?  398 ASP B O   1 
ATOM   3879 C CB  . ASP B 1 243 ? -23.616 52.709 19.194  1.00 56.05  ?  398 ASP B CB  1 
ATOM   3880 C CG  . ASP B 1 243 ? -23.953 53.531 17.949  1.00 68.28  ?  398 ASP B CG  1 
ATOM   3881 O OD1 . ASP B 1 243 ? -24.149 54.773 18.077  1.00 69.43  ?  398 ASP B OD1 1 
ATOM   3882 O OD2 . ASP B 1 243 ? -24.057 52.932 16.854  1.00 73.46  -1 398 ASP B OD2 1 
ATOM   3883 N N   . ILE B 1 244 ? -21.685 51.943 21.823  1.00 54.60  ?  399 ILE B N   1 
ATOM   3884 C CA  . ILE B 1 244 ? -21.366 51.093 22.985  1.00 53.80  ?  399 ILE B CA  1 
ATOM   3885 C C   . ILE B 1 244 ? -21.369 51.952 24.242  1.00 60.30  ?  399 ILE B C   1 
ATOM   3886 O O   . ILE B 1 244 ? -21.806 51.501 25.309  1.00 62.36  ?  399 ILE B O   1 
ATOM   3887 C CB  . ILE B 1 244 ? -20.041 50.311 22.762  1.00 56.11  ?  399 ILE B CB  1 
ATOM   3888 C CG1 . ILE B 1 244 ? -20.276 49.064 21.895  1.00 55.62  ?  399 ILE B CG1 1 
ATOM   3889 C CG2 . ILE B 1 244 ? -19.275 49.965 24.058  1.00 56.33  ?  399 ILE B CG2 1 
ATOM   3890 C CD1 . ILE B 1 244 ? -19.603 49.117 20.612  1.00 52.01  ?  399 ILE B CD1 1 
ATOM   3891 N N   . LYS B 1 245 ? -20.965 53.215 24.073  1.00 56.55  ?  400 LYS B N   1 
ATOM   3892 C CA  . LYS B 1 245 ? -20.965 54.168 25.158  1.00 57.45  ?  400 LYS B CA  1 
ATOM   3893 C C   . LYS B 1 245 ? -22.397 54.372 25.651  1.00 64.50  ?  400 LYS B C   1 
ATOM   3894 O O   . LYS B 1 245 ? -22.634 54.306 26.857  1.00 64.73  ?  400 LYS B O   1 
ATOM   3895 C CB  . LYS B 1 245 ? -20.324 55.482 24.704  1.00 59.48  ?  400 LYS B CB  1 
ATOM   3896 C CG  . LYS B 1 245 ? -20.433 56.605 25.710  1.00 66.85  ?  400 LYS B CG  1 
ATOM   3897 C CD  . LYS B 1 245 ? -19.349 56.524 26.751  1.00 66.85  ?  400 LYS B CD  1 
ATOM   3898 C CE  . LYS B 1 245 ? -19.205 57.878 27.372  1.00 73.57  ?  400 LYS B CE  1 
ATOM   3899 N NZ  . LYS B 1 245 ? -20.264 58.168 28.367  1.00 75.26  1  400 LYS B NZ  1 
ATOM   3900 N N   . GLU B 1 246 ? -23.344 54.561 24.715  1.00 63.62  ?  401 GLU B N   1 
ATOM   3901 C CA  . GLU B 1 246 ? -24.769 54.776 24.969  1.00 65.10  ?  401 GLU B CA  1 
ATOM   3902 C C   . GLU B 1 246 ? -25.350 53.594 25.726  1.00 71.11  ?  401 GLU B C   1 
ATOM   3903 O O   . GLU B 1 246 ? -26.019 53.810 26.731  1.00 72.46  ?  401 GLU B O   1 
ATOM   3904 C CB  . GLU B 1 246 ? -25.548 55.028 23.662  1.00 66.74  ?  401 GLU B CB  1 
ATOM   3905 N N   . GLU B 1 247 ? -25.027 52.351 25.292  1.00 66.67  ?  402 GLU B N   1 
ATOM   3906 C CA  . GLU B 1 247 ? -25.443 51.091 25.916  1.00 65.96  ?  402 GLU B CA  1 
ATOM   3907 C C   . GLU B 1 247 ? -25.006 51.014 27.392  1.00 69.51  ?  402 GLU B C   1 
ATOM   3908 O O   . GLU B 1 247 ? -25.797 50.588 28.237  1.00 68.65  ?  402 GLU B O   1 
ATOM   3909 C CB  . GLU B 1 247 ? -24.912 49.886 25.116  1.00 67.04  ?  402 GLU B CB  1 
ATOM   3910 C CG  . GLU B 1 247 ? -25.574 49.697 23.760  1.00 74.31  ?  402 GLU B CG  1 
ATOM   3911 C CD  . GLU B 1 247 ? -25.118 48.485 22.963  1.00 108.27 ?  402 GLU B CD  1 
ATOM   3912 O OE1 . GLU B 1 247 ? -25.236 47.349 23.479  1.00 102.20 ?  402 GLU B OE1 1 
ATOM   3913 O OE2 . GLU B 1 247 ? -24.682 48.667 21.800  1.00 114.24 -1 402 GLU B OE2 1 
ATOM   3914 N N   . ILE B 1 248 ? -23.768 51.458 27.695  1.00 67.34  ?  403 ILE B N   1 
ATOM   3915 C CA  . ILE B 1 248 ? -23.220 51.475 29.051  1.00 68.78  ?  403 ILE B CA  1 
ATOM   3916 C C   . ILE B 1 248 ? -23.921 52.548 29.878  1.00 74.34  ?  403 ILE B C   1 
ATOM   3917 O O   . ILE B 1 248 ? -24.369 52.264 30.993  1.00 72.63  ?  403 ILE B O   1 
ATOM   3918 C CB  . ILE B 1 248 ? -21.656 51.617 29.093  1.00 72.70  ?  403 ILE B CB  1 
ATOM   3919 C CG1 . ILE B 1 248 ? -20.956 50.429 28.373  1.00 73.25  ?  403 ILE B CG1 1 
ATOM   3920 C CG2 . ILE B 1 248 ? -21.146 51.751 30.562  1.00 73.96  ?  403 ILE B CG2 1 
ATOM   3921 C CD1 . ILE B 1 248 ? -19.498 50.691 27.927  1.00 79.18  ?  403 ILE B CD1 1 
ATOM   3922 N N   . GLU B 1 249 ? -24.025 53.769 29.321  1.00 73.20  ?  404 GLU B N   1 
ATOM   3923 C CA  . GLU B 1 249 ? -24.656 54.889 30.004  1.00 73.94  ?  404 GLU B CA  1 
ATOM   3924 C C   . GLU B 1 249 ? -26.173 54.707 30.216  1.00 80.52  ?  404 GLU B C   1 
ATOM   3925 O O   . GLU B 1 249 ? -26.695 55.130 31.250  1.00 82.04  ?  404 GLU B O   1 
ATOM   3926 C CB  . GLU B 1 249 ? -24.205 56.244 29.446  1.00 75.27  ?  404 GLU B CB  1 
ATOM   3927 C CG  . GLU B 1 249 ? -22.694 56.478 29.594  1.00 88.00  ?  404 GLU B CG  1 
ATOM   3928 C CD  . GLU B 1 249 ? -22.051 56.747 30.955  1.00 95.60  ?  404 GLU B CD  1 
ATOM   3929 O OE1 . GLU B 1 249 ? -21.941 57.941 31.323  1.00 88.82  ?  404 GLU B OE1 1 
ATOM   3930 O OE2 . GLU B 1 249 ? -21.528 55.791 31.579  1.00 63.68  -1 404 GLU B OE2 1 
ATOM   3931 N N   . ASP B 1 250 ? -26.839 53.947 29.333  1.00 76.47  ?  405 ASP B N   1 
ATOM   3932 C CA  . ASP B 1 250 ? -28.243 53.591 29.517  1.00 76.56  ?  405 ASP B CA  1 
ATOM   3933 C C   . ASP B 1 250 ? -28.362 52.270 30.305  1.00 78.40  ?  405 ASP B C   1 
ATOM   3934 O O   . ASP B 1 250 ? -29.336 51.540 30.113  1.00 78.70  ?  405 ASP B O   1 
ATOM   3935 C CB  . ASP B 1 250 ? -28.996 53.501 28.171  1.00 79.41  ?  405 ASP B CB  1 
ATOM   3936 C CG  . ASP B 1 250 ? -29.028 54.781 27.350  1.00 98.51  ?  405 ASP B CG  1 
ATOM   3937 O OD1 . ASP B 1 250 ? -29.186 55.878 27.951  1.00 100.57 ?  405 ASP B OD1 1 
ATOM   3938 O OD2 . ASP B 1 250 ? -28.911 54.688 26.105  1.00 106.20 -1 405 ASP B OD2 1 
ATOM   3939 N N   . GLU B 1 251 ? -27.365 51.968 31.184  1.00 71.78  ?  406 GLU B N   1 
ATOM   3940 C CA  . GLU B 1 251 ? -27.268 50.786 32.057  1.00 70.03  ?  406 GLU B CA  1 
ATOM   3941 C C   . GLU B 1 251 ? -27.600 49.400 31.435  1.00 69.77  ?  406 GLU B C   1 
ATOM   3942 O O   . GLU B 1 251 ? -27.650 48.409 32.163  1.00 70.04  ?  406 GLU B O   1 
ATOM   3943 C CB  . GLU B 1 251 ? -27.985 51.033 33.406  1.00 71.38  ?  406 GLU B CB  1 
ATOM   3944 N N   . GLU B 1 252 ? -27.773 49.333 30.099  1.00 63.11  ?  407 GLU B N   1 
ATOM   3945 C CA  . GLU B 1 252 ? -28.077 48.109 29.348  1.00 62.12  ?  407 GLU B CA  1 
ATOM   3946 C C   . GLU B 1 252 ? -26.877 47.115 29.316  1.00 66.39  ?  407 GLU B C   1 
ATOM   3947 O O   . GLU B 1 252 ? -27.081 45.908 29.115  1.00 66.76  ?  407 GLU B O   1 
ATOM   3948 C CB  . GLU B 1 252 ? -28.552 48.450 27.923  1.00 63.06  ?  407 GLU B CB  1 
ATOM   3949 N N   . LYS B 1 253 ? -25.635 47.638 29.501  1.00 61.09  ?  408 LYS B N   1 
ATOM   3950 C CA  . LYS B 1 253 ? -24.357 46.909 29.518  1.00 59.92  ?  408 LYS B CA  1 
ATOM   3951 C C   . LYS B 1 253 ? -23.358 47.637 30.460  1.00 64.79  ?  408 LYS B C   1 
ATOM   3952 O O   . LYS B 1 253 ? -23.630 48.759 30.905  1.00 64.47  ?  408 LYS B O   1 
ATOM   3953 C CB  . LYS B 1 253 ? -23.741 46.840 28.096  1.00 61.13  ?  408 LYS B CB  1 
ATOM   3954 C CG  . LYS B 1 253 ? -24.562 46.131 27.014  1.00 66.69  ?  408 LYS B CG  1 
ATOM   3955 C CD  . LYS B 1 253 ? -24.361 44.617 26.994  1.00 76.19  ?  408 LYS B CD  1 
ATOM   3956 C CE  . LYS B 1 253 ? -25.349 43.903 26.103  1.00 92.49  ?  408 LYS B CE  1 
ATOM   3957 N NZ  . LYS B 1 253 ? -25.073 44.121 24.655  1.00 107.98 1  408 LYS B NZ  1 
ATOM   3958 N N   . THR B 1 254 ? -22.213 46.993 30.772  1.00 61.47  ?  409 THR B N   1 
ATOM   3959 C CA  . THR B 1 254 ? -21.129 47.577 31.578  1.00 61.03  ?  409 THR B CA  1 
ATOM   3960 C C   . THR B 1 254 ? -19.831 47.576 30.777  1.00 61.67  ?  409 THR B C   1 
ATOM   3961 O O   . THR B 1 254 ? -19.741 46.892 29.744  1.00 59.44  ?  409 THR B O   1 
ATOM   3962 C CB  . THR B 1 254 ? -20.930 46.855 32.933  1.00 73.34  ?  409 THR B CB  1 
ATOM   3963 O OG1 . THR B 1 254 ? -20.852 45.438 32.748  1.00 74.22  ?  409 THR B OG1 1 
ATOM   3964 C CG2 . THR B 1 254 ? -21.982 47.224 33.958  1.00 71.54  ?  409 THR B CG2 1 
ATOM   3965 N N   . ILE B 1 255 ? -18.822 48.331 31.262  1.00 57.73  ?  410 ILE B N   1 
ATOM   3966 C CA  . ILE B 1 255 ? -17.511 48.358 30.610  1.00 57.14  ?  410 ILE B CA  1 
ATOM   3967 C C   . ILE B 1 255 ? -16.854 46.969 30.630  1.00 60.66  ?  410 ILE B C   1 
ATOM   3968 O O   . ILE B 1 255 ? -16.193 46.591 29.661  1.00 59.79  ?  410 ILE B O   1 
ATOM   3969 C CB  . ILE B 1 255 ? -16.576 49.524 31.073  1.00 59.14  ?  410 ILE B CB  1 
ATOM   3970 C CG1 . ILE B 1 255 ? -15.392 49.757 30.093  1.00 58.54  ?  410 ILE B CG1 1 
ATOM   3971 C CG2 . ILE B 1 255 ? -16.110 49.374 32.525  1.00 58.29  ?  410 ILE B CG2 1 
ATOM   3972 C CD1 . ILE B 1 255 ? -15.784 49.876 28.561  1.00 58.55  ?  410 ILE B CD1 1 
ATOM   3973 N N   . GLU B 1 256 ? -17.128 46.190 31.704  1.00 56.60  ?  411 GLU B N   1 
ATOM   3974 C CA  . GLU B 1 256 ? -16.646 44.828 31.924  1.00 55.50  ?  411 GLU B CA  1 
ATOM   3975 C C   . GLU B 1 256 ? -17.054 43.901 30.799  1.00 56.27  ?  411 GLU B C   1 
ATOM   3976 O O   . GLU B 1 256 ? -16.272 43.031 30.406  1.00 58.17  ?  411 GLU B O   1 
ATOM   3977 C CB  . GLU B 1 256 ? -17.131 44.290 33.273  1.00 57.25  ?  411 GLU B CB  1 
ATOM   3978 C CG  . GLU B 1 256 ? -16.342 44.791 34.475  1.00 73.53  ?  411 GLU B CG  1 
ATOM   3979 C CD  . GLU B 1 256 ? -16.514 46.250 34.866  1.00 108.35 ?  411 GLU B CD  1 
ATOM   3980 O OE1 . GLU B 1 256 ? -17.662 46.759 34.866  1.00 99.30  ?  411 GLU B OE1 1 
ATOM   3981 O OE2 . GLU B 1 256 ? -15.485 46.884 35.193  1.00 111.05 -1 411 GLU B OE2 1 
ATOM   3982 N N   . ASP B 1 257 ? -18.244 44.113 30.245  1.00 48.50  ?  412 ASP B N   1 
ATOM   3983 C CA  . ASP B 1 257 ? -18.741 43.320 29.133  1.00 47.65  ?  412 ASP B CA  1 
ATOM   3984 C C   . ASP B 1 257 ? -17.935 43.614 27.867  1.00 51.96  ?  412 ASP B C   1 
ATOM   3985 O O   . ASP B 1 257 ? -17.953 42.808 26.941  1.00 52.44  ?  412 ASP B O   1 
ATOM   3986 C CB  . ASP B 1 257 ? -20.239 43.610 28.889  1.00 49.56  ?  412 ASP B CB  1 
ATOM   3987 C CG  . ASP B 1 257 ? -21.153 43.352 30.077  1.00 65.64  ?  412 ASP B CG  1 
ATOM   3988 O OD1 . ASP B 1 257 ? -21.203 42.186 30.554  1.00 67.14  ?  412 ASP B OD1 1 
ATOM   3989 O OD2 . ASP B 1 257 ? -21.859 44.300 30.500  1.00 71.44  -1 412 ASP B OD2 1 
ATOM   3990 N N   . TYR B 1 258 ? -17.244 44.777 27.820  1.00 48.16  ?  413 TYR B N   1 
ATOM   3991 C CA  . TYR B 1 258 ? -16.483 45.227 26.649  1.00 47.04  ?  413 TYR B CA  1 
ATOM   3992 C C   . TYR B 1 258 ? -14.950 45.196 26.747  1.00 45.83  ?  413 TYR B C   1 
ATOM   3993 O O   . TYR B 1 258 ? -14.302 45.391 25.719  1.00 44.94  ?  413 TYR B O   1 
ATOM   3994 C CB  . TYR B 1 258 ? -17.023 46.566 26.111  1.00 47.98  ?  413 TYR B CB  1 
ATOM   3995 C CG  . TYR B 1 258 ? -18.364 46.413 25.417  1.00 50.27  ?  413 TYR B CG  1 
ATOM   3996 C CD1 . TYR B 1 258 ? -18.453 45.891 24.125  1.00 52.11  ?  413 TYR B CD1 1 
ATOM   3997 C CD2 . TYR B 1 258 ? -19.550 46.761 26.062  1.00 50.37  ?  413 TYR B CD2 1 
ATOM   3998 C CE1 . TYR B 1 258 ? -19.691 45.727 23.491  1.00 52.13  ?  413 TYR B CE1 1 
ATOM   3999 C CE2 . TYR B 1 258 ? -20.792 46.604 25.436  1.00 50.31  ?  413 TYR B CE2 1 
ATOM   4000 C CZ  . TYR B 1 258 ? -20.859 46.078 24.152  1.00 57.55  ?  413 TYR B CZ  1 
ATOM   4001 O OH  . TYR B 1 258 ? -22.079 45.920 23.514  1.00 60.54  ?  413 TYR B OH  1 
ATOM   4002 N N   . ILE B 1 259 ? -14.375 44.919 27.949  1.00 37.99  ?  414 ILE B N   1 
ATOM   4003 C CA  . ILE B 1 259 ? -12.925 44.817 28.146  1.00 37.12  ?  414 ILE B CA  1 
ATOM   4004 C C   . ILE B 1 259 ? -12.357 43.808 27.142  1.00 42.01  ?  414 ILE B C   1 
ATOM   4005 O O   . ILE B 1 259 ? -12.891 42.701 27.010  1.00 42.81  ?  414 ILE B O   1 
ATOM   4006 C CB  . ILE B 1 259 ? -12.491 44.458 29.602  1.00 39.18  ?  414 ILE B CB  1 
ATOM   4007 C CG1 . ILE B 1 259 ? -13.101 45.411 30.644  1.00 40.43  ?  414 ILE B CG1 1 
ATOM   4008 C CG2 . ILE B 1 259 ? -10.960 44.393 29.728  1.00 34.71  ?  414 ILE B CG2 1 
ATOM   4009 C CD1 . ILE B 1 259 ? -12.897 44.981 32.173  1.00 53.54  ?  414 ILE B CD1 1 
ATOM   4010 N N   . ASP B 1 260 ? -11.315 44.224 26.404  1.00 36.82  ?  415 ASP B N   1 
ATOM   4011 C CA  . ASP B 1 260 ? -10.645 43.418 25.404  1.00 35.81  ?  415 ASP B CA  1 
ATOM   4012 C C   . ASP B 1 260 ? -10.272 42.051 25.997  1.00 41.04  ?  415 ASP B C   1 
ATOM   4013 O O   . ASP B 1 260 ? -9.524  41.989 26.985  1.00 39.27  ?  415 ASP B O   1 
ATOM   4014 C CB  . ASP B 1 260 ? -9.394  44.160 24.919  1.00 36.59  ?  415 ASP B CB  1 
ATOM   4015 C CG  . ASP B 1 260 ? -8.729  43.596 23.688  1.00 35.50  ?  415 ASP B CG  1 
ATOM   4016 O OD1 . ASP B 1 260 ? -9.154  42.501 23.216  1.00 28.47  ?  415 ASP B OD1 1 
ATOM   4017 O OD2 . ASP B 1 260 ? -7.776  44.232 23.196  1.00 48.77  -1 415 ASP B OD2 1 
ATOM   4018 N N   . LYS B 1 261 ? -10.835 40.950 25.419  1.00 38.72  ?  416 LYS B N   1 
ATOM   4019 C CA  . LYS B 1 261 ? -10.520 39.604 25.936  1.00 38.94  ?  416 LYS B CA  1 
ATOM   4020 C C   . LYS B 1 261 ? -9.068  39.133 25.606  1.00 42.90  ?  416 LYS B C   1 
ATOM   4021 O O   . LYS B 1 261 ? -8.595  38.163 26.209  1.00 41.79  ?  416 LYS B O   1 
ATOM   4022 C CB  . LYS B 1 261 ? -11.578 38.574 25.532  1.00 41.17  ?  416 LYS B CB  1 
ATOM   4023 C CG  . LYS B 1 261 ? -12.898 38.742 26.255  1.00 52.14  ?  416 LYS B CG  1 
ATOM   4024 C CD  . LYS B 1 261 ? -13.962 37.800 25.721  1.00 61.58  ?  416 LYS B CD  1 
ATOM   4025 C CE  . LYS B 1 261 ? -15.341 38.402 25.701  1.00 72.43  ?  416 LYS B CE  1 
ATOM   4026 N NZ  . LYS B 1 261 ? -15.844 38.715 27.067  1.00 91.47  1  416 LYS B NZ  1 
ATOM   4027 N N   . LYS B 1 262 ? -8.356  39.868 24.692  1.00 38.91  ?  417 LYS B N   1 
ATOM   4028 C CA  . LYS B 1 262 ? -6.976  39.608 24.268  1.00 38.22  ?  417 LYS B CA  1 
ATOM   4029 C C   . LYS B 1 262 ? -5.941  40.072 25.296  1.00 43.83  ?  417 LYS B C   1 
ATOM   4030 O O   . LYS B 1 262 ? -4.763  40.259 24.989  1.00 44.25  ?  417 LYS B O   1 
ATOM   4031 C CB  . LYS B 1 262 ? -6.690  40.170 22.855  1.00 39.64  ?  417 LYS B CB  1 
ATOM   4032 C CG  . LYS B 1 262 ? -7.616  39.628 21.761  1.00 46.39  ?  417 LYS B CG  1 
ATOM   4033 C CD  . LYS B 1 262 ? -7.257  40.103 20.329  1.00 46.37  ?  417 LYS B CD  1 
ATOM   4034 C CE  . LYS B 1 262 ? -7.418  41.594 20.075  1.00 67.62  ?  417 LYS B CE  1 
ATOM   4035 N NZ  . LYS B 1 262 ? -8.817  42.101 20.250  1.00 72.23  1  417 LYS B NZ  1 
ATOM   4036 N N   . MET B 1 263 ? -6.377  40.243 26.521  1.00 42.37  ?  418 MET B N   1 
ATOM   4037 C CA  . MET B 1 263 ? -5.492  40.612 27.609  1.00 42.54  ?  418 MET B CA  1 
ATOM   4038 C C   . MET B 1 263 ? -5.805  39.867 28.883  1.00 52.91  ?  418 MET B C   1 
ATOM   4039 O O   . MET B 1 263 ? -6.940  39.445 29.066  1.00 52.64  ?  418 MET B O   1 
ATOM   4040 C CB  . MET B 1 263 ? -5.259  42.134 27.751  1.00 43.68  ?  418 MET B CB  1 
ATOM   4041 C CG  . MET B 1 263 ? -6.465  43.011 27.944  1.00 45.21  ?  418 MET B CG  1 
ATOM   4042 S SD  . MET B 1 263 ? -5.927  44.765 28.047  1.00 48.42  ?  418 MET B SD  1 
ATOM   4043 C CE  . MET B 1 263 ? -7.529  45.620 28.096  1.00 44.79  ?  418 MET B CE  1 
ATOM   4044 N N   . ASN B 1 264 ? -4.777  39.588 29.702  1.00 55.46  ?  419 ASN B N   1 
ATOM   4045 C CA  . ASN B 1 264 ? -4.946  38.844 30.961  1.00 56.70  ?  419 ASN B CA  1 
ATOM   4046 C C   . ASN B 1 264 ? -4.614  39.674 32.220  1.00 63.20  ?  419 ASN B C   1 
ATOM   4047 O O   . ASN B 1 264 ? -5.036  39.316 33.315  1.00 63.28  ?  419 ASN B O   1 
ATOM   4048 C CB  . ASN B 1 264 ? -4.143  37.542 30.927  1.00 56.28  ?  419 ASN B CB  1 
ATOM   4049 C CG  . ASN B 1 264 ? -2.660  37.758 30.807  1.00 90.47  ?  419 ASN B CG  1 
ATOM   4050 O OD1 . ASN B 1 264 ? -2.008  38.320 31.690  1.00 86.71  ?  419 ASN B OD1 1 
ATOM   4051 N ND2 . ASN B 1 264 ? -2.086  37.297 29.714  1.00 88.14  ?  419 ASN B ND2 1 
ATOM   4052 N N   . ASP B 1 265 ? -3.855  40.767 32.048  1.00 61.71  ?  420 ASP B N   1 
ATOM   4053 C CA  . ASP B 1 265 ? -3.354  41.654 33.107  1.00 62.35  ?  420 ASP B CA  1 
ATOM   4054 C C   . ASP B 1 265 ? -4.227  42.891 33.394  1.00 68.79  ?  420 ASP B C   1 
ATOM   4055 O O   . ASP B 1 265 ? -3.696  43.913 33.853  1.00 69.82  ?  420 ASP B O   1 
ATOM   4056 C CB  . ASP B 1 265 ? -1.910  42.096 32.737  1.00 64.04  ?  420 ASP B CB  1 
ATOM   4057 C CG  . ASP B 1 265 ? -1.799  42.990 31.498  1.00 69.04  ?  420 ASP B CG  1 
ATOM   4058 O OD1 . ASP B 1 265 ? -2.535  42.734 30.504  1.00 66.29  ?  420 ASP B OD1 1 
ATOM   4059 O OD2 . ASP B 1 265 ? -0.978  43.951 31.526  1.00 73.40  -1 420 ASP B OD2 1 
ATOM   4060 N N   . ALA B 1 266 ? -5.551  42.808 33.172  1.00 65.42  ?  421 ALA B N   1 
ATOM   4061 C CA  . ALA B 1 266 ? -6.395  43.989 33.354  1.00 65.20  ?  421 ALA B CA  1 
ATOM   4062 C C   . ALA B 1 266 ? -7.295  43.974 34.574  1.00 70.40  ?  421 ALA B C   1 
ATOM   4063 O O   . ALA B 1 266 ? -8.395  43.419 34.511  1.00 71.22  ?  421 ALA B O   1 
ATOM   4064 C CB  . ALA B 1 266 ? -7.201  44.274 32.085  1.00 65.65  ?  421 ALA B CB  1 
ATOM   4065 N N   . ASP B 1 267 ? -6.861  44.627 35.676  1.00 66.29  ?  422 ASP B N   1 
ATOM   4066 C CA  . ASP B 1 267 ? -7.704  44.699 36.872  1.00 65.78  ?  422 ASP B CA  1 
ATOM   4067 C C   . ASP B 1 267 ? -8.858  45.672 36.647  1.00 67.03  ?  422 ASP B C   1 
ATOM   4068 O O   . ASP B 1 267 ? -8.659  46.729 36.042  1.00 65.89  ?  422 ASP B O   1 
ATOM   4069 C CB  . ASP B 1 267 ? -6.900  45.035 38.135  1.00 68.13  ?  422 ASP B CB  1 
ATOM   4070 C CG  . ASP B 1 267 ? -6.204  46.369 38.099  1.00 84.05  ?  422 ASP B CG  1 
ATOM   4071 O OD1 . ASP B 1 267 ? -6.434  47.180 39.024  1.00 84.62  ?  422 ASP B OD1 1 
ATOM   4072 O OD2 . ASP B 1 267 ? -5.412  46.601 37.152  1.00 94.54  -1 422 ASP B OD2 1 
ATOM   4073 N N   . SER B 1 268 ? -10.068 45.289 37.098  1.00 62.77  ?  423 SER B N   1 
ATOM   4074 C CA  . SER B 1 268 ? -11.286 46.079 36.901  1.00 62.69  ?  423 SER B CA  1 
ATOM   4075 C C   . SER B 1 268 ? -11.293 47.515 37.440  1.00 68.15  ?  423 SER B C   1 
ATOM   4076 O O   . SER B 1 268 ? -12.035 48.351 36.910  1.00 69.30  ?  423 SER B O   1 
ATOM   4077 C CB  . SER B 1 268 ? -12.530 45.306 37.312  1.00 65.29  ?  423 SER B CB  1 
ATOM   4078 O OG  . SER B 1 268 ? -13.517 45.465 36.305  1.00 72.12  ?  423 SER B OG  1 
ATOM   4079 N N   . THR B 1 269 ? -10.460 47.798 38.462  1.00 63.54  ?  424 THR B N   1 
ATOM   4080 C CA  . THR B 1 269 ? -10.284 49.103 39.101  1.00 62.90  ?  424 THR B CA  1 
ATOM   4081 C C   . THR B 1 269 ? -9.677  50.109 38.121  1.00 65.15  ?  424 THR B C   1 
ATOM   4082 O O   . THR B 1 269 ? -10.279 51.166 37.907  1.00 65.36  ?  424 THR B O   1 
ATOM   4083 C CB  . THR B 1 269 ? -9.440  48.977 40.384  1.00 72.40  ?  424 THR B CB  1 
ATOM   4084 O OG1 . THR B 1 269 ? -9.953  47.916 41.190  1.00 77.15  ?  424 THR B OG1 1 
ATOM   4085 C CG2 . THR B 1 269 ? -9.400  50.263 41.185  1.00 67.64  ?  424 THR B CG2 1 
ATOM   4086 N N   . SER B 1 270 ? -8.505  49.793 37.528  1.00 59.79  ?  425 SER B N   1 
ATOM   4087 C CA  . SER B 1 270 ? -7.857  50.692 36.565  1.00 58.99  ?  425 SER B CA  1 
ATOM   4088 C C   . SER B 1 270 ? -8.626  50.749 35.241  1.00 60.58  ?  425 SER B C   1 
ATOM   4089 O O   . SER B 1 270 ? -8.687  51.810 34.607  1.00 59.77  ?  425 SER B O   1 
ATOM   4090 C CB  . SER B 1 270 ? -6.390  50.329 36.347  1.00 62.60  ?  425 SER B CB  1 
ATOM   4091 O OG  . SER B 1 270 ? -6.224  48.944 36.103  1.00 72.11  ?  425 SER B OG  1 
ATOM   4092 N N   . VAL B 1 271 ? -9.257  49.630 34.847  1.00 55.21  ?  426 VAL B N   1 
ATOM   4093 C CA  . VAL B 1 271 ? -10.057 49.638 33.627  1.00 54.49  ?  426 VAL B CA  1 
ATOM   4094 C C   . VAL B 1 271 ? -11.210 50.661 33.784  1.00 62.45  ?  426 VAL B C   1 
ATOM   4095 O O   . VAL B 1 271 ? -11.354 51.527 32.911  1.00 62.72  ?  426 VAL B O   1 
ATOM   4096 C CB  . VAL B 1 271 ? -10.505 48.233 33.163  1.00 55.91  ?  426 VAL B CB  1 
ATOM   4097 C CG1 . VAL B 1 271 ? -11.408 48.336 31.949  1.00 55.04  ?  426 VAL B CG1 1 
ATOM   4098 C CG2 . VAL B 1 271 ? -9.297  47.356 32.849  1.00 55.13  ?  426 VAL B CG2 1 
ATOM   4099 N N   . GLU B 1 272 ? -11.962 50.612 34.931  1.00 60.38  ?  427 GLU B N   1 
ATOM   4100 C CA  . GLU B 1 272 ? -13.038 51.560 35.251  1.00 60.75  ?  427 GLU B CA  1 
ATOM   4101 C C   . GLU B 1 272 ? -12.491 52.985 35.416  1.00 62.48  ?  427 GLU B C   1 
ATOM   4102 O O   . GLU B 1 272 ? -13.188 53.951 35.053  1.00 61.85  ?  427 GLU B O   1 
ATOM   4103 C CB  . GLU B 1 272 ? -13.802 51.142 36.507  1.00 62.74  ?  427 GLU B CB  1 
ATOM   4104 C CG  . GLU B 1 272 ? -14.878 50.106 36.248  1.00 78.83  ?  427 GLU B CG  1 
ATOM   4105 C CD  . GLU B 1 272 ? -15.573 49.547 37.478  1.00 115.90 ?  427 GLU B CD  1 
ATOM   4106 O OE1 . GLU B 1 272 ? -15.261 49.981 38.614  1.00 120.30 ?  427 GLU B OE1 1 
ATOM   4107 O OE2 . GLU B 1 272 ? -16.469 48.690 37.297  1.00 110.49 -1 427 GLU B OE2 1 
ATOM   4108 N N   . ALA B 1 273 ? -11.238 53.110 35.950  1.00 55.88  ?  428 ALA B N   1 
ATOM   4109 C CA  . ALA B 1 273 ? -10.559 54.398 36.109  1.00 54.25  ?  428 ALA B CA  1 
ATOM   4110 C C   . ALA B 1 273 ? -10.362 55.060 34.742  1.00 58.83  ?  428 ALA B C   1 
ATOM   4111 O O   . ALA B 1 273 ? -10.699 56.235 34.593  1.00 60.12  ?  428 ALA B O   1 
ATOM   4112 C CB  . ALA B 1 273 ? -9.227  54.216 36.803  1.00 54.46  ?  428 ALA B CB  1 
ATOM   4113 N N   . MET B 1 274 ? -9.890  54.282 33.726  1.00 53.23  ?  429 MET B N   1 
ATOM   4114 C CA  . MET B 1 274 ? -9.693  54.752 32.353  1.00 50.83  ?  429 MET B CA  1 
ATOM   4115 C C   . MET B 1 274 ? -11.035 55.032 31.666  1.00 54.36  ?  429 MET B C   1 
ATOM   4116 O O   . MET B 1 274 ? -11.128 56.018 30.923  1.00 54.83  ?  429 MET B O   1 
ATOM   4117 C CB  . MET B 1 274 ? -8.860  53.773 31.526  1.00 52.50  ?  429 MET B CB  1 
ATOM   4118 C CG  . MET B 1 274 ? -8.206  54.449 30.331  1.00 56.05  ?  429 MET B CG  1 
ATOM   4119 S SD  . MET B 1 274 ? -7.008  53.476 29.385  1.00 60.08  ?  429 MET B SD  1 
ATOM   4120 C CE  . MET B 1 274 ? -7.903  53.261 28.011  1.00 56.52  ?  429 MET B CE  1 
ATOM   4121 N N   . TYR B 1 275 ? -12.083 54.188 31.921  1.00 48.70  ?  430 TYR B N   1 
ATOM   4122 C CA  . TYR B 1 275 ? -13.412 54.421 31.335  1.00 47.55  ?  430 TYR B CA  1 
ATOM   4123 C C   . TYR B 1 275 ? -13.974 55.745 31.810  1.00 49.50  ?  430 TYR B C   1 
ATOM   4124 O O   . TYR B 1 275 ? -14.563 56.472 31.014  1.00 47.65  ?  430 TYR B O   1 
ATOM   4125 C CB  . TYR B 1 275 ? -14.397 53.275 31.595  1.00 48.59  ?  430 TYR B CB  1 
ATOM   4126 C CG  . TYR B 1 275 ? -15.749 53.523 30.959  1.00 50.01  ?  430 TYR B CG  1 
ATOM   4127 C CD1 . TYR B 1 275 ? -15.949 53.318 29.595  1.00 52.26  ?  430 TYR B CD1 1 
ATOM   4128 C CD2 . TYR B 1 275 ? -16.808 54.050 31.703  1.00 50.43  ?  430 TYR B CD2 1 
ATOM   4129 C CE1 . TYR B 1 275 ? -17.190 53.577 28.997  1.00 53.75  ?  430 TYR B CE1 1 
ATOM   4130 C CE2 . TYR B 1 275 ? -18.044 54.331 31.111  1.00 51.01  ?  430 TYR B CE2 1 
ATOM   4131 C CZ  . TYR B 1 275 ? -18.231 54.085 29.762  1.00 61.53  ?  430 TYR B CZ  1 
ATOM   4132 O OH  . TYR B 1 275 ? -19.447 54.346 29.180  1.00 70.38  ?  430 TYR B OH  1 
ATOM   4133 N N   . SER B 1 276 ? -13.748 56.066 33.103  1.00 46.89  ?  431 SER B N   1 
ATOM   4134 C CA  . SER B 1 276 ? -14.146 57.326 33.725  1.00 47.16  ?  431 SER B CA  1 
ATOM   4135 C C   . SER B 1 276 ? -13.527 58.529 32.962  1.00 53.27  ?  431 SER B C   1 
ATOM   4136 O O   . SER B 1 276 ? -14.260 59.459 32.631  1.00 55.46  ?  431 SER B O   1 
ATOM   4137 C CB  . SER B 1 276 ? -13.738 57.344 35.193  1.00 49.87  ?  431 SER B CB  1 
ATOM   4138 O OG  . SER B 1 276 ? -13.856 58.643 35.749  1.00 61.81  ?  431 SER B OG  1 
ATOM   4139 N N   . VAL B 1 277 ? -12.216 58.480 32.640  1.00 47.78  ?  432 VAL B N   1 
ATOM   4140 C CA  . VAL B 1 277 ? -11.535 59.537 31.884  1.00 47.75  ?  432 VAL B CA  1 
ATOM   4141 C C   . VAL B 1 277 ? -12.189 59.656 30.494  1.00 56.61  ?  432 VAL B C   1 
ATOM   4142 O O   . VAL B 1 277 ? -12.523 60.765 30.071  1.00 57.20  ?  432 VAL B O   1 
ATOM   4143 C CB  . VAL B 1 277 ? -9.998  59.312 31.778  1.00 50.57  ?  432 VAL B CB  1 
ATOM   4144 C CG1 . VAL B 1 277 ? -9.310  60.476 31.071  1.00 50.59  ?  432 VAL B CG1 1 
ATOM   4145 C CG2 . VAL B 1 277 ? -9.362  59.082 33.145  1.00 49.82  ?  432 VAL B CG2 1 
ATOM   4146 N N   . ALA B 1 278 ? -12.404 58.505 29.811  1.00 54.97  ?  433 ALA B N   1 
ATOM   4147 C CA  . ALA B 1 278 ? -13.011 58.438 28.481  1.00 54.24  ?  433 ALA B CA  1 
ATOM   4148 C C   . ALA B 1 278 ? -14.416 59.041 28.479  1.00 57.44  ?  433 ALA B C   1 
ATOM   4149 O O   . ALA B 1 278 ? -14.742 59.804 27.574  1.00 57.58  ?  433 ALA B O   1 
ATOM   4150 C CB  . ALA B 1 278 ? -13.054 57.000 27.989  1.00 54.76  ?  433 ALA B CB  1 
ATOM   4151 N N   . SER B 1 279 ? -15.247 58.719 29.494  1.00 52.74  ?  434 SER B N   1 
ATOM   4152 C CA  . SER B 1 279 ? -16.613 59.249 29.552  1.00 50.78  ?  434 SER B CA  1 
ATOM   4153 C C   . SER B 1 279 ? -16.617 60.747 29.844  1.00 49.92  ?  434 SER B C   1 
ATOM   4154 O O   . SER B 1 279 ? -17.464 61.453 29.293  1.00 49.03  ?  434 SER B O   1 
ATOM   4155 C CB  . SER B 1 279 ? -17.503 58.441 30.489  1.00 53.50  ?  434 SER B CB  1 
ATOM   4156 O OG  . SER B 1 279 ? -17.060 58.578 31.824  1.00 67.77  ?  434 SER B OG  1 
ATOM   4157 N N   . GLN B 1 280 ? -15.617 61.240 30.610  1.00 43.17  ?  435 GLN B N   1 
ATOM   4158 C CA  . GLN B 1 280 ? -15.459 62.672 30.863  1.00 43.42  ?  435 GLN B CA  1 
ATOM   4159 C C   . GLN B 1 280 ? -15.096 63.362 29.554  1.00 51.49  ?  435 GLN B C   1 
ATOM   4160 O O   . GLN B 1 280 ? -15.662 64.415 29.251  1.00 52.42  ?  435 GLN B O   1 
ATOM   4161 C CB  . GLN B 1 280 ? -14.388 62.946 31.925  1.00 43.99  ?  435 GLN B CB  1 
ATOM   4162 C CG  . GLN B 1 280 ? -14.901 62.773 33.340  1.00 46.32  ?  435 GLN B CG  1 
ATOM   4163 C CD  . GLN B 1 280 ? -13.794 62.720 34.348  1.00 68.71  ?  435 GLN B CD  1 
ATOM   4164 O OE1 . GLN B 1 280 ? -13.314 61.635 34.733  1.00 70.85  ?  435 GLN B OE1 1 
ATOM   4165 N NE2 . GLN B 1 280 ? -13.371 63.890 34.812  1.00 59.33  ?  435 GLN B NE2 1 
ATOM   4166 N N   . CYS B 1 281 ? -14.193 62.737 28.750  1.00 48.60  ?  436 CYS B N   1 
ATOM   4167 C CA  . CYS B 1 281 ? -13.773 63.216 27.423  1.00 48.43  ?  436 CYS B CA  1 
ATOM   4168 C C   . CYS B 1 281 ? -14.936 63.234 26.444  1.00 49.09  ?  436 CYS B C   1 
ATOM   4169 O O   . CYS B 1 281 ? -14.977 64.080 25.548  1.00 48.16  ?  436 CYS B O   1 
ATOM   4170 C CB  . CYS B 1 281 ? -12.652 62.344 26.875  1.00 49.58  ?  436 CYS B CB  1 
ATOM   4171 S SG  . CYS B 1 281 ? -11.077 62.528 27.724  1.00 53.71  ?  436 CYS B SG  1 
ATOM   4172 N N   . LEU B 1 282 ? -15.850 62.268 26.595  1.00 43.96  ?  437 LEU B N   1 
ATOM   4173 C CA  . LEU B 1 282 ? -16.980 62.131 25.703  1.00 43.97  ?  437 LEU B CA  1 
ATOM   4174 C C   . LEU B 1 282 ? -18.305 62.855 26.109  1.00 51.52  ?  437 LEU B C   1 
ATOM   4175 O O   . LEU B 1 282 ? -19.384 62.482 25.645  1.00 50.92  ?  437 LEU B O   1 
ATOM   4176 C CB  . LEU B 1 282 ? -17.154 60.663 25.328  1.00 43.26  ?  437 LEU B CB  1 
ATOM   4177 C CG  . LEU B 1 282 ? -15.950 60.012 24.680  1.00 45.96  ?  437 LEU B CG  1 
ATOM   4178 C CD1 . LEU B 1 282 ? -16.044 58.500 24.795  1.00 46.99  ?  437 LEU B CD1 1 
ATOM   4179 C CD2 . LEU B 1 282 ? -15.798 60.442 23.258  1.00 42.11  ?  437 LEU B CD2 1 
ATOM   4180 N N   . HIS B 1 283 ? -18.193 63.943 26.916  1.00 50.75  ?  438 HIS B N   1 
ATOM   4181 C CA  . HIS B 1 283 ? -19.294 64.801 27.343  1.00 51.18  ?  438 HIS B CA  1 
ATOM   4182 C C   . HIS B 1 283 ? -19.930 65.530 26.163  1.00 59.18  ?  438 HIS B C   1 
ATOM   4183 O O   . HIS B 1 283 ? -19.214 65.983 25.265  1.00 59.41  ?  438 HIS B O   1 
ATOM   4184 C CB  . HIS B 1 283 ? -18.793 65.833 28.360  1.00 52.01  ?  438 HIS B CB  1 
ATOM   4185 C CG  . HIS B 1 283 ? -18.859 65.358 29.777  1.00 56.23  ?  438 HIS B CG  1 
ATOM   4186 N ND1 . HIS B 1 283 ? -18.193 65.799 30.867  1.00 58.42  ?  438 HIS B ND1 1 
ATOM   4187 C CD2 . HIS B 1 283 ? -19.731 64.342 30.169  1.00 58.29  ?  438 HIS B CD2 1 
ATOM   4188 C CE1 . HIS B 1 283 ? -18.620 65.038 31.930  1.00 57.69  ?  438 HIS B CE1 1 
ATOM   4189 N NE2 . HIS B 1 283 ? -19.532 64.179 31.464  1.00 58.04  ?  438 HIS B NE2 1 
ATOM   4190 N N   . GLU B 1 284 ? -21.277 65.645 26.165  1.00 58.97  ?  439 GLU B N   1 
ATOM   4191 C CA  . GLU B 1 284 ? -22.037 66.352 25.128  1.00 60.14  ?  439 GLU B CA  1 
ATOM   4192 C C   . GLU B 1 284 ? -21.512 67.787 25.077  1.00 65.12  ?  439 GLU B C   1 
ATOM   4193 O O   . GLU B 1 284 ? -20.925 68.195 24.070  1.00 66.03  ?  439 GLU B O   1 
ATOM   4194 C CB  . GLU B 1 284 ? -23.545 66.404 25.480  1.00 61.93  ?  439 GLU B CB  1 
ATOM   4195 C CG  . GLU B 1 284 ? -24.385 65.166 25.203  1.00 73.31  ?  439 GLU B CG  1 
ATOM   4196 C CD  . GLU B 1 284 ? -25.878 65.431 25.057  1.00 83.33  ?  439 GLU B CD  1 
ATOM   4197 O OE1 . GLU B 1 284 ? -26.565 64.596 24.426  1.00 61.07  ?  439 GLU B OE1 1 
ATOM   4198 O OE2 . GLU B 1 284 ? -26.365 66.464 25.574  1.00 78.57  -1 439 GLU B OE2 1 
ATOM   4199 N N   . LYS B 1 285 ? -21.669 68.519 26.204  1.00 60.36  ?  440 LYS B N   1 
ATOM   4200 C CA  . LYS B 1 285 ? -21.256 69.905 26.336  1.00 59.84  ?  440 LYS B CA  1 
ATOM   4201 C C   . LYS B 1 285 ? -19.730 70.019 26.362  1.00 63.29  ?  440 LYS B C   1 
ATOM   4202 O O   . LYS B 1 285 ? -19.091 69.580 27.325  1.00 62.93  ?  440 LYS B O   1 
ATOM   4203 C CB  . LYS B 1 285 ? -21.923 70.550 27.564  1.00 62.30  ?  440 LYS B CB  1 
ATOM   4204 N N   . LYS B 1 286 ? -19.155 70.580 25.267  1.00 59.27  ?  441 LYS B N   1 
ATOM   4205 C CA  . LYS B 1 286 ? -17.716 70.793 25.068  1.00 58.74  ?  441 LYS B CA  1 
ATOM   4206 C C   . LYS B 1 286 ? -17.028 71.399 26.287  1.00 65.02  ?  441 LYS B C   1 
ATOM   4207 O O   . LYS B 1 286 ? -15.934 70.965 26.645  1.00 65.69  ?  441 LYS B O   1 
ATOM   4208 C CB  . LYS B 1 286 ? -17.449 71.635 23.811  1.00 59.79  ?  441 LYS B CB  1 
ATOM   4209 N N   . ASN B 1 287 ? -17.679 72.361 26.954  1.00 62.53  ?  442 ASN B N   1 
ATOM   4210 C CA  . ASN B 1 287 ? -17.115 73.016 28.140  1.00 62.45  ?  442 ASN B CA  1 
ATOM   4211 C C   . ASN B 1 287 ? -17.074 72.137 29.392  1.00 63.54  ?  442 ASN B C   1 
ATOM   4212 O O   . ASN B 1 287 ? -16.350 72.458 30.330  1.00 62.93  ?  442 ASN B O   1 
ATOM   4213 C CB  . ASN B 1 287 ? -17.820 74.354 28.398  1.00 67.83  ?  442 ASN B CB  1 
ATOM   4214 C CG  . ASN B 1 287 ? -17.533 75.438 27.364  1.00 91.34  ?  442 ASN B CG  1 
ATOM   4215 O OD1 . ASN B 1 287 ? -17.361 75.191 26.156  1.00 84.47  ?  442 ASN B OD1 1 
ATOM   4216 N ND2 . ASN B 1 287 ? -17.507 76.680 27.824  1.00 82.60  ?  442 ASN B ND2 1 
ATOM   4217 N N   . LYS B 1 288 ? -17.820 71.021 29.401  1.00 59.21  ?  443 LYS B N   1 
ATOM   4218 C CA  . LYS B 1 288 ? -17.855 70.082 30.536  1.00 57.72  ?  443 LYS B CA  1 
ATOM   4219 C C   . LYS B 1 288 ? -16.751 68.995 30.421  1.00 57.92  ?  443 LYS B C   1 
ATOM   4220 O O   . LYS B 1 288 ? -16.429 68.339 31.418  1.00 56.94  ?  443 LYS B O   1 
ATOM   4221 C CB  . LYS B 1 288 ? -19.264 69.486 30.731  1.00 59.32  ?  443 LYS B CB  1 
ATOM   4222 N N   . ARG B 1 289 ? -16.148 68.847 29.217  1.00 51.38  ?  444 ARG B N   1 
ATOM   4223 C CA  . ARG B 1 289 ? -15.030 67.920 28.999  1.00 49.82  ?  444 ARG B CA  1 
ATOM   4224 C C   . ARG B 1 289 ? -13.785 68.452 29.728  1.00 55.04  ?  444 ARG B C   1 
ATOM   4225 O O   . ARG B 1 289 ? -13.608 69.677 29.794  1.00 55.38  ?  444 ARG B O   1 
ATOM   4226 C CB  . ARG B 1 289 ? -14.673 67.798 27.506  1.00 45.78  ?  444 ARG B CB  1 
ATOM   4227 C CG  . ARG B 1 289 ? -15.720 67.131 26.642  1.00 48.21  ?  444 ARG B CG  1 
ATOM   4228 C CD  . ARG B 1 289 ? -15.414 67.378 25.193  1.00 45.98  ?  444 ARG B CD  1 
ATOM   4229 N NE  . ARG B 1 289 ? -16.603 67.302 24.334  1.00 51.57  ?  444 ARG B NE  1 
ATOM   4230 C CZ  . ARG B 1 289 ? -16.644 67.752 23.079  1.00 70.36  ?  444 ARG B CZ  1 
ATOM   4231 N NH1 . ARG B 1 289 ? -15.576 68.335 22.538  1.00 68.66  ?  444 ARG B NH1 1 
ATOM   4232 N NH2 . ARG B 1 289 ? -17.757 67.633 22.357  1.00 45.19  1  444 ARG B NH2 1 
ATOM   4233 N N   . PRO B 1 290 ? -12.873 67.579 30.222  1.00 50.20  ?  445 PRO B N   1 
ATOM   4234 C CA  . PRO B 1 290 ? -11.664 68.094 30.875  1.00 49.65  ?  445 PRO B CA  1 
ATOM   4235 C C   . PRO B 1 290 ? -10.660 68.638 29.862  1.00 55.12  ?  445 PRO B C   1 
ATOM   4236 O O   . PRO B 1 290 ? -10.745 68.318 28.670  1.00 56.41  ?  445 PRO B O   1 
ATOM   4237 C CB  . PRO B 1 290 ? -11.108 66.861 31.601  1.00 50.98  ?  445 PRO B CB  1 
ATOM   4238 C CG  . PRO B 1 290 ? -11.595 65.710 30.834  1.00 54.54  ?  445 PRO B CG  1 
ATOM   4239 C CD  . PRO B 1 290 ? -12.887 66.098 30.204  1.00 50.72  ?  445 PRO B CD  1 
ATOM   4240 N N   . ASP B 1 291 ? -9.708  69.459 30.320  1.00 50.19  ?  446 ASP B N   1 
ATOM   4241 C CA  . ASP B 1 291 ? -8.660  69.921 29.418  1.00 49.13  ?  446 ASP B CA  1 
ATOM   4242 C C   . ASP B 1 291 ? -7.546  68.854 29.466  1.00 51.93  ?  446 ASP B C   1 
ATOM   4243 O O   . ASP B 1 291 ? -7.557  67.995 30.362  1.00 49.96  ?  446 ASP B O   1 
ATOM   4244 C CB  . ASP B 1 291 ? -8.169  71.345 29.759  1.00 50.52  ?  446 ASP B CB  1 
ATOM   4245 C CG  . ASP B 1 291 ? -7.590  71.567 31.138  1.00 66.57  ?  446 ASP B CG  1 
ATOM   4246 O OD1 . ASP B 1 291 ? -7.788  70.702 32.016  1.00 68.33  ?  446 ASP B OD1 1 
ATOM   4247 O OD2 . ASP B 1 291 ? -6.979  72.640 31.357  1.00 79.25  -1 446 ASP B OD2 1 
ATOM   4248 N N   . ILE B 1 292 ? -6.629  68.883 28.479  1.00 48.09  ?  447 ILE B N   1 
ATOM   4249 C CA  . ILE B 1 292 ? -5.546  67.922 28.358  1.00 47.62  ?  447 ILE B CA  1 
ATOM   4250 C C   . ILE B 1 292 ? -4.693  67.706 29.622  1.00 53.21  ?  447 ILE B C   1 
ATOM   4251 O O   . ILE B 1 292 ? -4.458  66.539 29.973  1.00 53.00  ?  447 ILE B O   1 
ATOM   4252 C CB  . ILE B 1 292 ? -4.765  68.049 27.022  1.00 50.45  ?  447 ILE B CB  1 
ATOM   4253 C CG1 . ILE B 1 292 ? -3.986  66.751 26.663  1.00 50.55  ?  447 ILE B CG1 1 
ATOM   4254 C CG2 . ILE B 1 292 ? -3.928  69.328 26.928  1.00 50.22  ?  447 ILE B CG2 1 
ATOM   4255 C CD1 . ILE B 1 292 ? -4.892  65.534 26.383  1.00 51.40  ?  447 ILE B CD1 1 
ATOM   4256 N N   . LYS B 1 293 ? -4.318  68.797 30.356  1.00 49.41  ?  448 LYS B N   1 
ATOM   4257 C CA  . LYS B 1 293 ? -3.548  68.656 31.609  1.00 48.19  ?  448 LYS B CA  1 
ATOM   4258 C C   . LYS B 1 293 ? -4.326  67.848 32.649  1.00 51.15  ?  448 LYS B C   1 
ATOM   4259 O O   . LYS B 1 293 ? -3.707  67.070 33.384  1.00 50.73  ?  448 LYS B O   1 
ATOM   4260 C CB  . LYS B 1 293 ? -3.078  70.004 32.176  1.00 49.95  ?  448 LYS B CB  1 
ATOM   4261 N N   . LYS B 1 294 ? -5.687  67.988 32.675  1.00 46.86  ?  449 LYS B N   1 
ATOM   4262 C CA  . LYS B 1 294 ? -6.544  67.218 33.588  1.00 46.78  ?  449 LYS B CA  1 
ATOM   4263 C C   . LYS B 1 294 ? -6.524  65.742 33.180  1.00 55.01  ?  449 LYS B C   1 
ATOM   4264 O O   . LYS B 1 294 ? -6.333  64.880 34.047  1.00 56.52  ?  449 LYS B O   1 
ATOM   4265 C CB  . LYS B 1 294 ? -7.978  67.775 33.642  1.00 47.68  ?  449 LYS B CB  1 
ATOM   4266 C CG  . LYS B 1 294 ? -8.932  67.064 34.619  1.00 58.33  ?  449 LYS B CG  1 
ATOM   4267 C CD  . LYS B 1 294 ? -8.531  67.171 36.092  1.00 66.61  ?  449 LYS B CD  1 
ATOM   4268 C CE  . LYS B 1 294 ? -9.476  66.396 36.975  1.00 78.65  ?  449 LYS B CE  1 
ATOM   4269 N NZ  . LYS B 1 294 ? -8.969  66.286 38.367  1.00 90.32  1  449 LYS B NZ  1 
ATOM   4270 N N   . VAL B 1 295 ? -6.678  65.468 31.854  1.00 50.55  ?  450 VAL B N   1 
ATOM   4271 C CA  . VAL B 1 295 ? -6.619  64.137 31.256  1.00 49.52  ?  450 VAL B CA  1 
ATOM   4272 C C   . VAL B 1 295 ? -5.275  63.448 31.656  1.00 52.89  ?  450 VAL B C   1 
ATOM   4273 O O   . VAL B 1 295 ? -5.292  62.298 32.119  1.00 52.54  ?  450 VAL B O   1 
ATOM   4274 C CB  . VAL B 1 295 ? -6.856  64.189 29.712  1.00 52.71  ?  450 VAL B CB  1 
ATOM   4275 C CG1 . VAL B 1 295 ? -6.711  62.811 29.085  1.00 52.67  ?  450 VAL B CG1 1 
ATOM   4276 C CG2 . VAL B 1 295 ? -8.232  64.763 29.381  1.00 52.29  ?  450 VAL B CG2 1 
ATOM   4277 N N   . GLN B 1 296 ? -4.138  64.179 31.551  1.00 47.63  ?  451 GLN B N   1 
ATOM   4278 C CA  . GLN B 1 296 ? -2.820  63.660 31.943  1.00 47.14  ?  451 GLN B CA  1 
ATOM   4279 C C   . GLN B 1 296 ? -2.795  63.312 33.430  1.00 54.31  ?  451 GLN B C   1 
ATOM   4280 O O   . GLN B 1 296 ? -2.302  62.244 33.800  1.00 54.02  ?  451 GLN B O   1 
ATOM   4281 C CB  . GLN B 1 296 ? -1.718  64.690 31.698  1.00 47.45  ?  451 GLN B CB  1 
ATOM   4282 C CG  . GLN B 1 296 ? -1.360  64.980 30.256  1.00 47.77  ?  451 GLN B CG  1 
ATOM   4283 C CD  . GLN B 1 296 ? -0.101  65.796 30.242  1.00 66.64  ?  451 GLN B CD  1 
ATOM   4284 O OE1 . GLN B 1 296 ? -0.212  67.066 30.629  1.00 61.52  ?  451 GLN B OE1 1 
ATOM   4285 N NE2 . GLN B 1 296 ? 1.000   65.274 29.990  1.00 52.04  ?  451 GLN B NE2 1 
ATOM   4286 N N   . GLN B 1 297 ? -3.317  64.226 34.281  1.00 53.21  ?  452 GLN B N   1 
ATOM   4287 C CA  . GLN B 1 297 ? -3.370  64.062 35.743  1.00 53.26  ?  452 GLN B CA  1 
ATOM   4288 C C   . GLN B 1 297 ? -4.168  62.807 36.098  1.00 57.30  ?  452 GLN B C   1 
ATOM   4289 O O   . GLN B 1 297 ? -3.679  61.947 36.844  1.00 57.42  ?  452 GLN B O   1 
ATOM   4290 C CB  . GLN B 1 297 ? -3.957  65.313 36.412  1.00 54.68  ?  452 GLN B CB  1 
ATOM   4291 C CG  . GLN B 1 297 ? -3.872  65.333 37.926  1.00 77.21  ?  452 GLN B CG  1 
ATOM   4292 C CD  . GLN B 1 297 ? -5.094  66.004 38.507  1.00 108.37 ?  452 GLN B CD  1 
ATOM   4293 O OE1 . GLN B 1 297 ? -6.083  65.206 38.890  1.00 105.48 ?  452 GLN B OE1 1 
ATOM   4294 N NE2 . GLN B 1 297 ? -5.184  67.235 38.585  1.00 102.49 ?  452 GLN B NE2 1 
ATOM   4295 N N   . LEU B 1 298 ? -5.351  62.663 35.494  1.00 52.81  ?  453 LEU B N   1 
ATOM   4296 C CA  . LEU B 1 298 ? -6.206  61.502 35.704  1.00 52.40  ?  453 LEU B CA  1 
ATOM   4297 C C   . LEU B 1 298 ? -5.536  60.193 35.256  1.00 57.63  ?  453 LEU B C   1 
ATOM   4298 O O   . LEU B 1 298 ? -5.595  59.213 36.010  1.00 57.71  ?  453 LEU B O   1 
ATOM   4299 C CB  . LEU B 1 298 ? -7.562  61.702 35.038  1.00 52.44  ?  453 LEU B CB  1 
ATOM   4300 C CG  . LEU B 1 298 ? -8.440  62.873 35.574  1.00 57.00  ?  453 LEU B CG  1 
ATOM   4301 C CD1 . LEU B 1 298 ? -9.607  63.156 34.631  1.00 57.39  ?  453 LEU B CD1 1 
ATOM   4302 C CD2 . LEU B 1 298 ? -8.932  62.619 37.000  1.00 56.14  ?  453 LEU B CD2 1 
ATOM   4303 N N   . LEU B 1 299 ? -4.842  60.190 34.063  1.00 53.40  ?  454 LEU B N   1 
ATOM   4304 C CA  . LEU B 1 299 ? -4.118  59.009 33.534  1.00 51.82  ?  454 LEU B CA  1 
ATOM   4305 C C   . LEU B 1 299 ? -2.908  58.642 34.404  1.00 59.06  ?  454 LEU B C   1 
ATOM   4306 O O   . LEU B 1 299 ? -2.573  57.460 34.506  1.00 57.23  ?  454 LEU B O   1 
ATOM   4307 C CB  . LEU B 1 299 ? -3.658  59.184 32.077  1.00 50.54  ?  454 LEU B CB  1 
ATOM   4308 C CG  . LEU B 1 299 ? -4.700  59.168 30.965  1.00 53.27  ?  454 LEU B CG  1 
ATOM   4309 C CD1 . LEU B 1 299 ? -4.081  59.542 29.646  1.00 52.59  ?  454 LEU B CD1 1 
ATOM   4310 C CD2 . LEU B 1 299 ? -5.394  57.822 30.834  1.00 53.73  ?  454 LEU B CD2 1 
ATOM   4311 N N   . GLN B 1 300 ? -2.242  59.650 35.020  1.00 60.04  ?  455 GLN B N   1 
ATOM   4312 C CA  . GLN B 1 300 ? -1.097  59.418 35.919  1.00 61.36  ?  455 GLN B CA  1 
ATOM   4313 C C   . GLN B 1 300 ? -1.588  58.802 37.233  1.00 68.39  ?  455 GLN B C   1 
ATOM   4314 O O   . GLN B 1 300 ? -0.953  57.883 37.751  1.00 67.80  ?  455 GLN B O   1 
ATOM   4315 C CB  . GLN B 1 300 ? -0.294  60.706 36.168  1.00 62.38  ?  455 GLN B CB  1 
ATOM   4316 N N   . GLU B 1 301 ? -2.752  59.275 37.729  1.00 68.02  ?  456 GLU B N   1 
ATOM   4317 C CA  . GLU B 1 301 ? -3.401  58.795 38.959  1.00 69.61  ?  456 GLU B CA  1 
ATOM   4318 C C   . GLU B 1 301 ? -3.798  57.314 38.838  1.00 74.90  ?  456 GLU B C   1 
ATOM   4319 O O   . GLU B 1 301 ? -3.681  56.553 39.805  1.00 75.90  ?  456 GLU B O   1 
ATOM   4320 C CB  . GLU B 1 301 ? -4.646  59.654 39.281  1.00 71.38  ?  456 GLU B CB  1 
ATOM   4321 C CG  . GLU B 1 301 ? -4.326  60.930 40.044  1.00 84.81  ?  456 GLU B CG  1 
ATOM   4322 C CD  . GLU B 1 301 ? -5.309  62.078 39.924  1.00 105.26 ?  456 GLU B CD  1 
ATOM   4323 O OE1 . GLU B 1 301 ? -6.514  61.825 39.693  1.00 102.92 ?  456 GLU B OE1 1 
ATOM   4324 O OE2 . GLU B 1 301 ? -4.872  63.237 40.101  1.00 93.82  -1 456 GLU B OE2 1 
ATOM   4325 N N   . MET B 1 302 ? -4.253  56.924 37.630  1.00 69.45  ?  457 MET B N   1 
ATOM   4326 C CA  . MET B 1 302 ? -4.691  55.596 37.203  1.00 67.18  ?  457 MET B CA  1 
ATOM   4327 C C   . MET B 1 302 ? -3.702  54.481 37.571  1.00 67.72  ?  457 MET B C   1 
ATOM   4328 O O   . MET B 1 302 ? -4.140  53.378 37.905  1.00 67.56  ?  457 MET B O   1 
ATOM   4329 C CB  . MET B 1 302 ? -4.836  55.628 35.685  1.00 69.13  ?  457 MET B CB  1 
ATOM   4330 C CG  . MET B 1 302 ? -6.006  54.900 35.158  1.00 72.56  ?  457 MET B CG  1 
ATOM   4331 S SD  . MET B 1 302 ? -5.536  53.860 33.776  1.00 76.76  ?  457 MET B SD  1 
ATOM   4332 C CE  . MET B 1 302 ? -4.802  55.002 32.693  1.00 73.19  ?  457 MET B CE  1 
ATOM   4333 N N   . THR B 1 303 ? -2.385  54.764 37.489  1.00 61.60  ?  458 THR B N   1 
ATOM   4334 C CA  . THR B 1 303 ? -1.305  53.803 37.749  1.00 72.13  ?  458 THR B CA  1 
ATOM   4335 C C   . THR B 1 303 ? -0.691  53.927 39.149  1.00 120.23 ?  458 THR B C   1 
ATOM   4336 O O   . THR B 1 303 ? -0.403  55.027 39.621  1.00 93.76  ?  458 THR B O   1 
ATOM   4337 C CB  . THR B 1 303 ? -0.242  53.828 36.618  1.00 75.96  ?  458 THR B CB  1 
ATOM   4338 O OG1 . THR B 1 303 ? 0.286   55.147 36.470  1.00 73.18  ?  458 THR B OG1 1 
ATOM   4339 C CG2 . THR B 1 303 ? -0.785  53.321 35.274  1.00 71.00  ?  458 THR B CG2 1 
ATOM   4340 N N   . ARG C 1 9   ? -8.017  -0.302 31.935  1.00 92.89  ?  164 ARG C N   1 
ATOM   4341 C CA  . ARG C 1 9   ? -7.744  0.581  30.800  1.00 93.03  ?  164 ARG C CA  1 
ATOM   4342 C C   . ARG C 1 9   ? -7.392  2.014  31.261  1.00 95.89  ?  164 ARG C C   1 
ATOM   4343 O O   . ARG C 1 9   ? -6.339  2.546  30.897  1.00 94.93  ?  164 ARG C O   1 
ATOM   4344 C CB  . ARG C 1 9   ? -8.933  0.599  29.804  1.00 94.98  ?  164 ARG C CB  1 
ATOM   4345 C CG  . ARG C 1 9   ? -8.627  -0.041 28.453  1.00 110.32 ?  164 ARG C CG  1 
ATOM   4346 C CD  . ARG C 1 9   ? -8.716  0.963  27.316  1.00 124.31 ?  164 ARG C CD  1 
ATOM   4347 N NE  . ARG C 1 9   ? -7.423  1.173  26.655  1.00 134.49 ?  164 ARG C NE  1 
ATOM   4348 C CZ  . ARG C 1 9   ? -6.499  2.048  27.052  1.00 146.78 ?  164 ARG C CZ  1 
ATOM   4349 N NH1 . ARG C 1 9   ? -6.708  2.809  28.120  1.00 129.54 ?  164 ARG C NH1 1 
ATOM   4350 N NH2 . ARG C 1 9   ? -5.356  2.162  26.387  1.00 135.22 1  164 ARG C NH2 1 
ATOM   4351 N N   . PHE C 1 10  ? -8.289  2.625  32.054  1.00 91.76  ?  165 PHE C N   1 
ATOM   4352 C CA  . PHE C 1 10  ? -8.154  3.975  32.591  1.00 90.84  ?  165 PHE C CA  1 
ATOM   4353 C C   . PHE C 1 10  ? -8.115  3.912  34.106  1.00 94.53  ?  165 PHE C C   1 
ATOM   4354 O O   . PHE C 1 10  ? -8.785  3.058  34.704  1.00 94.48  ?  165 PHE C O   1 
ATOM   4355 C CB  . PHE C 1 10  ? -9.354  4.847  32.150  1.00 92.30  ?  165 PHE C CB  1 
ATOM   4356 C CG  . PHE C 1 10  ? -9.573  4.953  30.658  1.00 93.20  ?  165 PHE C CG  1 
ATOM   4357 C CD1 . PHE C 1 10  ? -8.601  5.516  29.832  1.00 95.58  ?  165 PHE C CD1 1 
ATOM   4358 C CD2 . PHE C 1 10  ? -10.764 4.523  30.081  1.00 94.34  ?  165 PHE C CD2 1 
ATOM   4359 C CE1 . PHE C 1 10  ? -8.801  5.611  28.456  1.00 96.05  ?  165 PHE C CE1 1 
ATOM   4360 C CE2 . PHE C 1 10  ? -10.965 4.622  28.702  1.00 96.74  ?  165 PHE C CE2 1 
ATOM   4361 C CZ  . PHE C 1 10  ? -9.985  5.168  27.901  1.00 94.85  ?  165 PHE C CZ  1 
ATOM   4362 N N   . HIS C 1 11  ? -7.365  4.835  34.736  1.00 90.12  ?  166 HIS C N   1 
ATOM   4363 C CA  . HIS C 1 11  ? -7.263  4.901  36.188  1.00 89.38  ?  166 HIS C CA  1 
ATOM   4364 C C   . HIS C 1 11  ? -8.565  5.397  36.803  1.00 87.86  ?  166 HIS C C   1 
ATOM   4365 O O   . HIS C 1 11  ? -9.090  6.427  36.383  1.00 87.38  ?  166 HIS C O   1 
ATOM   4366 C CB  . HIS C 1 11  ? -6.080  5.773  36.631  1.00 91.43  ?  166 HIS C CB  1 
ATOM   4367 C CG  . HIS C 1 11  ? -5.949  5.867  38.123  1.00 96.22  ?  166 HIS C CG  1 
ATOM   4368 N ND1 . HIS C 1 11  ? -6.394  6.976  38.821  1.00 98.61  ?  166 HIS C ND1 1 
ATOM   4369 C CD2 . HIS C 1 11  ? -5.491  4.953  39.012  1.00 98.82  ?  166 HIS C CD2 1 
ATOM   4370 C CE1 . HIS C 1 11  ? -6.158  6.723  40.099  1.00 98.24  ?  166 HIS C CE1 1 
ATOM   4371 N NE2 . HIS C 1 11  ? -5.620  5.517  40.265  1.00 98.66  ?  166 HIS C NE2 1 
ATOM   4372 N N   . SER C 1 12  ? -9.106  4.646  37.770  1.00 80.79  ?  167 SER C N   1 
ATOM   4373 C CA  . SER C 1 12  ? -10.331 5.073  38.435  1.00 78.78  ?  167 SER C CA  1 
ATOM   4374 C C   . SER C 1 12  ? -9.956  5.999  39.570  1.00 78.74  ?  167 SER C C   1 
ATOM   4375 O O   . SER C 1 12  ? -9.142  5.654  40.439  1.00 78.60  ?  167 SER C O   1 
ATOM   4376 C CB  . SER C 1 12  ? -11.157 3.895  38.936  1.00 80.71  ?  167 SER C CB  1 
ATOM   4377 O OG  . SER C 1 12  ? -12.460 4.368  39.235  1.00 84.77  ?  167 SER C OG  1 
ATOM   4378 N N   . PHE C 1 13  ? -10.497 7.208  39.509  1.00 70.99  ?  168 PHE C N   1 
ATOM   4379 C CA  . PHE C 1 13  ? -10.226 8.227  40.496  1.00 68.76  ?  168 PHE C CA  1 
ATOM   4380 C C   . PHE C 1 13  ? -11.382 8.341  41.486  1.00 72.97  ?  168 PHE C C   1 
ATOM   4381 O O   . PHE C 1 13  ? -12.525 8.007  41.150  1.00 72.20  ?  168 PHE C O   1 
ATOM   4382 C CB  . PHE C 1 13  ? -9.958  9.570  39.799  1.00 68.73  ?  168 PHE C CB  1 
ATOM   4383 C CG  . PHE C 1 13  ? -8.675  9.657  39.006  1.00 67.97  ?  168 PHE C CG  1 
ATOM   4384 C CD1 . PHE C 1 13  ? -7.495  10.080 39.606  1.00 69.18  ?  168 PHE C CD1 1 
ATOM   4385 C CD2 . PHE C 1 13  ? -8.661  9.385  37.643  1.00 68.71  ?  168 PHE C CD2 1 
ATOM   4386 C CE1 . PHE C 1 13  ? -6.318  10.218 38.858  1.00 69.48  ?  168 PHE C CE1 1 
ATOM   4387 C CE2 . PHE C 1 13  ? -7.482  9.506  36.899  1.00 70.76  ?  168 PHE C CE2 1 
ATOM   4388 C CZ  . PHE C 1 13  ? -6.320  9.925  37.511  1.00 68.54  ?  168 PHE C CZ  1 
ATOM   4389 N N   . SER C 1 14  ? -11.065 8.789  42.719  1.00 69.68  ?  169 SER C N   1 
ATOM   4390 C CA  . SER C 1 14  ? -12.034 9.054  43.786  1.00 68.92  ?  169 SER C CA  1 
ATOM   4391 C C   . SER C 1 14  ? -12.451 10.490 43.587  1.00 70.32  ?  169 SER C C   1 
ATOM   4392 O O   . SER C 1 14  ? -11.639 11.279 43.101  1.00 70.13  ?  169 SER C O   1 
ATOM   4393 C CB  . SER C 1 14  ? -11.360 8.924  45.153  1.00 72.35  ?  169 SER C CB  1 
ATOM   4394 O OG  . SER C 1 14  ? -12.248 9.154  46.236  1.00 79.04  ?  169 SER C OG  1 
ATOM   4395 N N   . PHE C 1 15  ? -13.675 10.861 43.977  1.00 65.19  ?  170 PHE C N   1 
ATOM   4396 C CA  . PHE C 1 15  ? -14.048 12.269 43.865  1.00 64.53  ?  170 PHE C CA  1 
ATOM   4397 C C   . PHE C 1 15  ? -13.179 13.150 44.797  1.00 68.05  ?  170 PHE C C   1 
ATOM   4398 O O   . PHE C 1 15  ? -12.732 14.215 44.376  1.00 66.54  ?  170 PHE C O   1 
ATOM   4399 C CB  . PHE C 1 15  ? -15.543 12.496 44.077  1.00 66.16  ?  170 PHE C CB  1 
ATOM   4400 C CG  . PHE C 1 15  ? -15.995 13.915 43.792  1.00 67.47  ?  170 PHE C CG  1 
ATOM   4401 C CD1 . PHE C 1 15  ? -16.033 14.404 42.487  1.00 70.33  ?  170 PHE C CD1 1 
ATOM   4402 C CD2 . PHE C 1 15  ? -16.413 14.750 44.823  1.00 68.57  ?  170 PHE C CD2 1 
ATOM   4403 C CE1 . PHE C 1 15  ? -16.461 15.708 42.227  1.00 71.28  ?  170 PHE C CE1 1 
ATOM   4404 C CE2 . PHE C 1 15  ? -16.856 16.049 44.558  1.00 71.31  ?  170 PHE C CE2 1 
ATOM   4405 C CZ  . PHE C 1 15  ? -16.886 16.517 43.262  1.00 69.60  ?  170 PHE C CZ  1 
ATOM   4406 N N   . TYR C 1 16  ? -12.870 12.649 46.013  1.00 65.81  ?  171 TYR C N   1 
ATOM   4407 C CA  . TYR C 1 16  ? -12.011 13.321 46.996  1.00 66.19  ?  171 TYR C CA  1 
ATOM   4408 C C   . TYR C 1 16  ? -10.563 13.488 46.467  1.00 71.41  ?  171 TYR C C   1 
ATOM   4409 O O   . TYR C 1 16  ? -9.916  14.492 46.790  1.00 71.46  ?  171 TYR C O   1 
ATOM   4410 C CB  . TYR C 1 16  ? -12.036 12.585 48.351  1.00 66.82  ?  171 TYR C CB  1 
ATOM   4411 N N   . GLU C 1 17  ? -10.090 12.532 45.619  1.00 67.42  ?  172 GLU C N   1 
ATOM   4412 C CA  . GLU C 1 17  ? -8.766  12.526 44.960  1.00 66.93  ?  172 GLU C CA  1 
ATOM   4413 C C   . GLU C 1 17  ? -8.671  13.706 43.985  1.00 70.63  ?  172 GLU C C   1 
ATOM   4414 O O   . GLU C 1 17  ? -7.688  14.444 44.021  1.00 70.05  ?  172 GLU C O   1 
ATOM   4415 C CB  . GLU C 1 17  ? -8.597  11.210 44.185  1.00 68.30  ?  172 GLU C CB  1 
ATOM   4416 C CG  . GLU C 1 17  ? -7.186  10.675 44.043  1.00 79.30  ?  172 GLU C CG  1 
ATOM   4417 C CD  . GLU C 1 17  ? -7.130  9.213  43.626  1.00 108.75 ?  172 GLU C CD  1 
ATOM   4418 O OE1 . GLU C 1 17  ? -6.114  8.810  43.013  1.00 103.42 ?  172 GLU C OE1 1 
ATOM   4419 O OE2 . GLU C 1 17  ? -8.100  8.469  43.905  1.00 105.42 -1 172 GLU C OE2 1 
ATOM   4420 N N   . LEU C 1 18  ? -9.714  13.878 43.125  1.00 67.26  ?  173 LEU C N   1 
ATOM   4421 C CA  . LEU C 1 18  ? -9.862  14.935 42.118  1.00 66.88  ?  173 LEU C CA  1 
ATOM   4422 C C   . LEU C 1 18  ? -10.141 16.292 42.728  1.00 72.88  ?  173 LEU C C   1 
ATOM   4423 O O   . LEU C 1 18  ? -9.785  17.315 42.143  1.00 72.52  ?  173 LEU C O   1 
ATOM   4424 C CB  . LEU C 1 18  ? -10.913 14.558 41.064  1.00 66.44  ?  173 LEU C CB  1 
ATOM   4425 C CG  . LEU C 1 18  ? -10.632 13.280 40.283  1.00 70.17  ?  173 LEU C CG  1 
ATOM   4426 C CD1 . LEU C 1 18  ? -11.651 13.081 39.221  1.00 70.12  ?  173 LEU C CD1 1 
ATOM   4427 C CD2 . LEU C 1 18  ? -9.230  13.281 39.682  1.00 70.12  ?  173 LEU C CD2 1 
ATOM   4428 N N   . LYS C 1 19  ? -10.741 16.295 43.927  1.00 71.84  ?  174 LYS C N   1 
ATOM   4429 C CA  . LYS C 1 19  ? -10.995 17.493 44.718  1.00 72.26  ?  174 LYS C CA  1 
ATOM   4430 C C   . LYS C 1 19  ? -9.616  18.035 45.121  1.00 77.29  ?  174 LYS C C   1 
ATOM   4431 O O   . LYS C 1 19  ? -9.364  19.227 44.984  1.00 76.77  ?  174 LYS C O   1 
ATOM   4432 C CB  . LYS C 1 19  ? -11.816 17.145 45.975  1.00 74.24  ?  174 LYS C CB  1 
ATOM   4433 C CG  . LYS C 1 19  ? -13.317 17.088 45.747  1.00 84.65  ?  174 LYS C CG  1 
ATOM   4434 C CD  . LYS C 1 19  ? -14.034 18.253 46.403  1.00 93.19  ?  174 LYS C CD  1 
ATOM   4435 C CE  . LYS C 1 19  ? -14.668 17.889 47.722  1.00 103.09 ?  174 LYS C CE  1 
ATOM   4436 N NZ  . LYS C 1 19  ? -15.177 19.091 48.435  1.00 110.81 1  174 LYS C NZ  1 
ATOM   4437 N N   . ASN C 1 20  ? -8.703  17.134 45.531  1.00 75.37  ?  175 ASN C N   1 
ATOM   4438 C CA  . ASN C 1 20  ? -7.342  17.506 45.912  1.00 76.55  ?  175 ASN C CA  1 
ATOM   4439 C C   . ASN C 1 20  ? -6.567  18.112 44.743  1.00 82.22  ?  175 ASN C C   1 
ATOM   4440 O O   . ASN C 1 20  ? -6.091  19.251 44.862  1.00 82.08  ?  175 ASN C O   1 
ATOM   4441 C CB  . ASN C 1 20  ? -6.578  16.320 46.538  1.00 77.52  ?  175 ASN C CB  1 
ATOM   4442 C CG  . ASN C 1 20  ? -7.151  15.796 47.849  1.00 96.91  ?  175 ASN C CG  1 
ATOM   4443 O OD1 . ASN C 1 20  ? -7.761  16.662 48.664  1.00 88.14  ?  175 ASN C OD1 1 
ATOM   4444 N ND2 . ASN C 1 20  ? -7.044  14.602 48.157  1.00 85.32  ?  175 ASN C ND2 1 
ATOM   4445 N N   . VAL C 1 21  ? -6.506  17.383 43.598  1.00 78.95  ?  176 VAL C N   1 
ATOM   4446 C CA  . VAL C 1 21  ? -5.786  17.800 42.384  1.00 78.34  ?  176 VAL C CA  1 
ATOM   4447 C C   . VAL C 1 21  ? -6.205  19.164 41.803  1.00 80.86  ?  176 VAL C C   1 
ATOM   4448 O O   . VAL C 1 21  ? -5.355  19.887 41.282  1.00 79.80  ?  176 VAL C O   1 
ATOM   4449 C CB  . VAL C 1 21  ? -5.634  16.694 41.287  1.00 82.10  ?  176 VAL C CB  1 
ATOM   4450 C CG1 . VAL C 1 21  ? -5.198  15.365 41.882  1.00 82.09  ?  176 VAL C CG1 1 
ATOM   4451 C CG2 . VAL C 1 21  ? -6.902  16.515 40.472  1.00 81.78  ?  176 VAL C CG2 1 
ATOM   4452 N N   . THR C 1 22  ? -7.493  19.518 41.927  1.00 77.27  ?  177 THR C N   1 
ATOM   4453 C CA  . THR C 1 22  ? -8.074  20.742 41.362  1.00 77.22  ?  177 THR C CA  1 
ATOM   4454 C C   . THR C 1 22  ? -8.247  21.896 42.353  1.00 82.66  ?  177 THR C C   1 
ATOM   4455 O O   . THR C 1 22  ? -8.978  22.852 42.043  1.00 82.20  ?  177 THR C O   1 
ATOM   4456 C CB  . THR C 1 22  ? -9.423  20.405 40.696  1.00 79.02  ?  177 THR C CB  1 
ATOM   4457 O OG1 . THR C 1 22  ? -10.323 19.904 41.691  1.00 74.03  ?  177 THR C OG1 1 
ATOM   4458 C CG2 . THR C 1 22  ? -9.285  19.425 39.534  1.00 74.63  ?  177 THR C CG2 1 
ATOM   4459 N N   . ASN C 1 23  ? -7.597  21.806 43.546  1.00 80.33  ?  178 ASN C N   1 
ATOM   4460 C CA  . ASN C 1 23  ? -7.687  22.802 44.625  1.00 80.49  ?  178 ASN C CA  1 
ATOM   4461 C C   . ASN C 1 23  ? -9.168  22.974 45.022  1.00 84.42  ?  178 ASN C C   1 
ATOM   4462 O O   . ASN C 1 23  ? -9.691  24.096 45.129  1.00 83.77  ?  178 ASN C O   1 
ATOM   4463 C CB  . ASN C 1 23  ? -7.026  24.140 44.208  1.00 83.11  ?  178 ASN C CB  1 
ATOM   4464 C CG  . ASN C 1 23  ? -6.748  25.084 45.351  1.00 115.78 ?  178 ASN C CG  1 
ATOM   4465 O OD1 . ASN C 1 23  ? -5.903  24.816 46.214  1.00 115.02 ?  178 ASN C OD1 1 
ATOM   4466 N ND2 . ASN C 1 23  ? -7.440  26.222 45.368  1.00 107.53 ?  178 ASN C ND2 1 
ATOM   4467 N N   . ASN C 1 24  ? -9.843  21.816 45.179  1.00 81.55  ?  179 ASN C N   1 
ATOM   4468 C CA  . ASN C 1 24  ? -11.263 21.657 45.503  1.00 82.11  ?  179 ASN C CA  1 
ATOM   4469 C C   . ASN C 1 24  ? -12.181 22.368 44.523  1.00 85.05  ?  179 ASN C C   1 
ATOM   4470 O O   . ASN C 1 24  ? -13.047 23.151 44.922  1.00 84.45  ?  179 ASN C O   1 
ATOM   4471 C CB  . ASN C 1 24  ? -11.546 21.961 46.976  1.00 88.32  ?  179 ASN C CB  1 
ATOM   4472 C CG  . ASN C 1 24  ? -11.004 20.878 47.866  1.00 133.91 ?  179 ASN C CG  1 
ATOM   4473 O OD1 . ASN C 1 24  ? -11.691 19.898 48.167  1.00 133.52 ?  179 ASN C OD1 1 
ATOM   4474 N ND2 . ASN C 1 24  ? -9.734  20.996 48.247  1.00 131.76 ?  179 ASN C ND2 1 
ATOM   4475 N N   . PHE C 1 25  ? -11.968 22.079 43.223  1.00 81.39  ?  180 PHE C N   1 
ATOM   4476 C CA  . PHE C 1 25  ? -12.703 22.628 42.077  1.00 81.03  ?  180 PHE C CA  1 
ATOM   4477 C C   . PHE C 1 25  ? -12.867 24.145 42.133  1.00 88.31  ?  180 PHE C C   1 
ATOM   4478 O O   . PHE C 1 25  ? -13.993 24.658 42.031  1.00 87.72  ?  180 PHE C O   1 
ATOM   4479 C CB  . PHE C 1 25  ? -14.041 21.902 41.853  1.00 81.57  ?  180 PHE C CB  1 
ATOM   4480 C CG  . PHE C 1 25  ? -13.894 20.432 41.577  1.00 81.70  ?  180 PHE C CG  1 
ATOM   4481 C CD1 . PHE C 1 25  ? -13.573 19.980 40.308  1.00 84.26  ?  180 PHE C CD1 1 
ATOM   4482 C CD2 . PHE C 1 25  ? -14.079 19.500 42.585  1.00 83.47  ?  180 PHE C CD2 1 
ATOM   4483 C CE1 . PHE C 1 25  ? -13.441 18.617 40.052  1.00 85.18  ?  180 PHE C CE1 1 
ATOM   4484 C CE2 . PHE C 1 25  ? -13.941 18.140 42.332  1.00 86.28  ?  180 PHE C CE2 1 
ATOM   4485 C CZ  . PHE C 1 25  ? -13.633 17.707 41.065  1.00 84.41  ?  180 PHE C CZ  1 
ATOM   4486 N N   . ASP C 1 26  ? -11.727 24.855 42.313  1.00 87.56  ?  181 ASP C N   1 
ATOM   4487 C CA  . ASP C 1 26  ? -11.661 26.319 42.373  1.00 88.70  ?  181 ASP C CA  1 
ATOM   4488 C C   . ASP C 1 26  ? -12.257 26.904 41.081  1.00 94.16  ?  181 ASP C C   1 
ATOM   4489 O O   . ASP C 1 26  ? -11.775 26.602 39.984  1.00 93.79  ?  181 ASP C O   1 
ATOM   4490 C CB  . ASP C 1 26  ? -10.203 26.783 42.598  1.00 90.92  ?  181 ASP C CB  1 
ATOM   4491 C CG  . ASP C 1 26  ? -9.980  28.272 42.855  1.00 103.49 ?  181 ASP C CG  1 
ATOM   4492 O OD1 . ASP C 1 26  ? -10.949 29.064 42.704  1.00 103.36 ?  181 ASP C OD1 1 
ATOM   4493 O OD2 . ASP C 1 26  ? -8.832  28.649 43.187  1.00 111.40 -1 181 ASP C OD2 1 
ATOM   4494 N N   . GLU C 1 27  ? -13.344 27.687 41.221  1.00 91.66  ?  182 GLU C N   1 
ATOM   4495 C CA  . GLU C 1 27  ? -14.054 28.267 40.083  1.00 92.24  ?  182 GLU C CA  1 
ATOM   4496 C C   . GLU C 1 27  ? -13.422 29.536 39.505  1.00 97.11  ?  182 GLU C C   1 
ATOM   4497 O O   . GLU C 1 27  ? -13.879 30.035 38.470  1.00 96.13  ?  182 GLU C O   1 
ATOM   4498 C CB  . GLU C 1 27  ? -15.548 28.431 40.389  1.00 93.80  ?  182 GLU C CB  1 
ATOM   4499 C CG  . GLU C 1 27  ? -16.316 27.121 40.317  1.00 105.21 ?  182 GLU C CG  1 
ATOM   4500 C CD  . GLU C 1 27  ? -17.301 26.980 39.169  1.00 130.26 ?  182 GLU C CD  1 
ATOM   4501 O OE1 . GLU C 1 27  ? -18.305 26.255 39.355  1.00 130.15 ?  182 GLU C OE1 1 
ATOM   4502 O OE2 . GLU C 1 27  ? -17.075 27.575 38.088  1.00 122.90 -1 182 GLU C OE2 1 
ATOM   4503 N N   . ARG C 1 28  ? -12.357 30.040 40.150  1.00 94.83  ?  183 ARG C N   1 
ATOM   4504 C CA  . ARG C 1 28  ? -11.632 31.211 39.671  1.00 95.40  ?  183 ARG C CA  1 
ATOM   4505 C C   . ARG C 1 28  ? -10.845 30.825 38.413  1.00 100.13 ?  183 ARG C C   1 
ATOM   4506 O O   . ARG C 1 28  ? -10.390 29.678 38.332  1.00 99.66  ?  183 ARG C O   1 
ATOM   4507 C CB  . ARG C 1 28  ? -10.672 31.717 40.748  1.00 96.42  ?  183 ARG C CB  1 
ATOM   4508 C CG  . ARG C 1 28  ? -11.180 32.920 41.524  1.00 105.32 ?  183 ARG C CG  1 
ATOM   4509 C CD  . ARG C 1 28  ? -10.325 33.200 42.746  1.00 117.87 ?  183 ARG C CD  1 
ATOM   4510 N NE  . ARG C 1 28  ? -8.974  33.654 42.401  1.00 131.64 ?  183 ARG C NE  1 
ATOM   4511 C CZ  . ARG C 1 28  ? -7.881  32.898 42.480  1.00 147.15 ?  183 ARG C CZ  1 
ATOM   4512 N NH1 . ARG C 1 28  ? -7.961  31.641 42.905  1.00 133.32 ?  183 ARG C NH1 1 
ATOM   4513 N NH2 . ARG C 1 28  ? -6.698  33.397 42.144  1.00 133.48 1  183 ARG C NH2 1 
ATOM   4514 N N   . PRO C 1 29  ? -10.703 31.729 37.409  1.00 97.28  ?  184 PRO C N   1 
ATOM   4515 C CA  . PRO C 1 29  ? -9.979  31.355 36.182  1.00 97.18  ?  184 PRO C CA  1 
ATOM   4516 C C   . PRO C 1 29  ? -8.497  31.131 36.424  1.00 101.76 ?  184 PRO C C   1 
ATOM   4517 O O   . PRO C 1 29  ? -7.914  31.743 37.324  1.00 101.09 ?  184 PRO C O   1 
ATOM   4518 C CB  . PRO C 1 29  ? -10.221 32.540 35.237  1.00 98.89  ?  184 PRO C CB  1 
ATOM   4519 C CG  . PRO C 1 29  ? -11.357 33.291 35.831  1.00 103.49 ?  184 PRO C CG  1 
ATOM   4520 C CD  . PRO C 1 29  ? -11.207 33.109 37.311  1.00 99.07  ?  184 PRO C CD  1 
ATOM   4521 N N   . ILE C 1 30  ? -7.897  30.237 35.621  1.00 98.72  ?  185 ILE C N   1 
ATOM   4522 C CA  . ILE C 1 30  ? -6.475  29.890 35.685  1.00 98.62  ?  185 ILE C CA  1 
ATOM   4523 C C   . ILE C 1 30  ? -5.582  31.121 35.459  1.00 103.61 ?  185 ILE C C   1 
ATOM   4524 O O   . ILE C 1 30  ? -4.504  31.198 36.044  1.00 103.18 ?  185 ILE C O   1 
ATOM   4525 C CB  . ILE C 1 30  ? -6.098  28.687 34.770  1.00 101.53 ?  185 ILE C CB  1 
ATOM   4526 C CG1 . ILE C 1 30  ? -6.718  28.811 33.350  1.00 102.21 ?  185 ILE C CG1 1 
ATOM   4527 C CG2 . ILE C 1 30  ? -6.466  27.363 35.430  1.00 101.58 ?  185 ILE C CG2 1 
ATOM   4528 C CD1 . ILE C 1 30  ? -5.793  28.452 32.179  1.00 108.28 ?  185 ILE C CD1 1 
ATOM   4529 N N   . SER C 1 31  ? -6.067  32.095 34.653  1.00 101.09 ?  186 SER C N   1 
ATOM   4530 C CA  . SER C 1 31  ? -5.408  33.370 34.311  1.00 101.33 ?  186 SER C CA  1 
ATOM   4531 C C   . SER C 1 31  ? -5.236  34.291 35.539  1.00 105.00 ?  186 SER C C   1 
ATOM   4532 O O   . SER C 1 31  ? -4.396  35.193 35.523  1.00 105.37 ?  186 SER C O   1 
ATOM   4533 C CB  . SER C 1 31  ? -6.205  34.096 33.225  1.00 105.11 ?  186 SER C CB  1 
ATOM   4534 O OG  . SER C 1 31  ? -7.538  34.339 33.646  1.00 114.34 ?  186 SER C OG  1 
ATOM   4535 N N   . VAL C 1 32  ? -6.047  34.057 36.578  1.00 99.90  ?  187 VAL C N   1 
ATOM   4536 C CA  . VAL C 1 32  ? -6.116  34.806 37.831  1.00 98.93  ?  187 VAL C CA  1 
ATOM   4537 C C   . VAL C 1 32  ? -5.494  34.012 39.005  1.00 101.76 ?  187 VAL C C   1 
ATOM   4538 O O   . VAL C 1 32  ? -5.295  34.557 40.095  1.00 101.08 ?  187 VAL C O   1 
ATOM   4539 C CB  . VAL C 1 32  ? -7.598  35.226 38.019  1.00 102.63 ?  187 VAL C CB  1 
ATOM   4540 C CG1 . VAL C 1 32  ? -8.028  35.354 39.484  1.00 102.27 ?  187 VAL C CG1 1 
ATOM   4541 C CG2 . VAL C 1 32  ? -7.897  36.497 37.233  1.00 102.49 ?  187 VAL C CG2 1 
ATOM   4542 N N   . GLY C 1 33  ? -5.114  32.763 38.727  1.00 97.62  ?  188 GLY C N   1 
ATOM   4543 C CA  . GLY C 1 33  ? -4.497  31.855 39.692  1.00 96.43  ?  188 GLY C CA  1 
ATOM   4544 C C   . GLY C 1 33  ? -5.441  30.792 40.223  1.00 96.92  ?  188 GLY C C   1 
ATOM   4545 O O   . GLY C 1 33  ? -5.104  30.071 41.169  1.00 96.89  ?  188 GLY C O   1 
ATOM   4546 N N   . GLY C 1 34  ? -6.625  30.704 39.620  1.00 89.84  ?  189 GLY C N   1 
ATOM   4547 C CA  . GLY C 1 34  ? -7.638  29.726 39.990  1.00 87.37  ?  189 GLY C CA  1 
ATOM   4548 C C   . GLY C 1 34  ? -7.491  28.422 39.231  1.00 85.93  ?  189 GLY C C   1 
ATOM   4549 O O   . GLY C 1 34  ? -6.421  28.141 38.671  1.00 86.21  ?  189 GLY C O   1 
ATOM   4550 N N   . ASN C 1 35  ? -8.571  27.617 39.187  1.00 76.45  ?  190 ASN C N   1 
ATOM   4551 C CA  . ASN C 1 35  ? -8.528  26.334 38.489  1.00 73.36  ?  190 ASN C CA  1 
ATOM   4552 C C   . ASN C 1 35  ? -9.423  26.204 37.262  1.00 71.38  ?  190 ASN C C   1 
ATOM   4553 O O   . ASN C 1 35  ? -9.156  25.341 36.433  1.00 71.02  ?  190 ASN C O   1 
ATOM   4554 C CB  . ASN C 1 35  ? -8.692  25.169 39.456  1.00 72.07  ?  190 ASN C CB  1 
ATOM   4555 C CG  . ASN C 1 35  ? -7.493  24.982 40.343  1.00 82.93  ?  190 ASN C CG  1 
ATOM   4556 O OD1 . ASN C 1 35  ? -7.225  25.784 41.241  1.00 78.18  ?  190 ASN C OD1 1 
ATOM   4557 N ND2 . ASN C 1 35  ? -6.756  23.904 40.118  1.00 71.31  ?  190 ASN C ND2 1 
ATOM   4558 N N   . LYS C 1 36  ? -10.450 27.061 37.121  1.00 64.59  ?  191 LYS C N   1 
ATOM   4559 C CA  . LYS C 1 36  ? -11.384 27.016 35.989  1.00 63.64  ?  191 LYS C CA  1 
ATOM   4560 C C   . LYS C 1 36  ? -10.720 27.366 34.644  1.00 67.68  ?  191 LYS C C   1 
ATOM   4561 O O   . LYS C 1 36  ? -10.076 28.409 34.517  1.00 69.33  ?  191 LYS C O   1 
ATOM   4562 C CB  . LYS C 1 36  ? -12.631 27.871 36.253  1.00 65.18  ?  191 LYS C CB  1 
ATOM   4563 C CG  . LYS C 1 36  ? -13.738 27.711 35.216  1.00 83.07  ?  191 LYS C CG  1 
ATOM   4564 C CD  . LYS C 1 36  ? -14.951 28.575 35.537  1.00 99.18  ?  191 LYS C CD  1 
ATOM   4565 C CE  . LYS C 1 36  ? -16.004 28.474 34.457  1.00 115.58 ?  191 LYS C CE  1 
ATOM   4566 N NZ  . LYS C 1 36  ? -17.163 29.371 34.720  1.00 129.20 1  191 LYS C NZ  1 
ATOM   4567 N N   . MET C 1 37  ? -10.880 26.486 33.648  1.00 60.84  ?  192 MET C N   1 
ATOM   4568 C CA  . MET C 1 37  ? -10.308 26.679 32.316  1.00 59.06  ?  192 MET C CA  1 
ATOM   4569 C C   . MET C 1 37  ? -11.362 27.011 31.267  1.00 63.90  ?  192 MET C C   1 
ATOM   4570 O O   . MET C 1 37  ? -11.038 27.571 30.224  1.00 63.39  ?  192 MET C O   1 
ATOM   4571 C CB  . MET C 1 37  ? -9.477  25.460 31.882  1.00 60.46  ?  192 MET C CB  1 
ATOM   4572 C CG  . MET C 1 37  ? -8.257  25.229 32.743  1.00 62.68  ?  192 MET C CG  1 
ATOM   4573 S SD  . MET C 1 37  ? -7.060  24.095 32.013  1.00 65.97  ?  192 MET C SD  1 
ATOM   4574 C CE  . MET C 1 37  ? -7.956  22.565 32.036  1.00 62.18  ?  192 MET C CE  1 
ATOM   4575 N N   . GLY C 1 38  ? -12.601 26.646 31.537  1.00 62.92  ?  193 GLY C N   1 
ATOM   4576 C CA  . GLY C 1 38  ? -13.712 26.886 30.631  1.00 64.42  ?  193 GLY C CA  1 
ATOM   4577 C C   . GLY C 1 38  ? -14.918 26.029 30.940  1.00 72.57  ?  193 GLY C C   1 
ATOM   4578 O O   . GLY C 1 38  ? -14.879 25.181 31.839  1.00 72.23  ?  193 GLY C O   1 
ATOM   4579 N N   . GLU C 1 39  ? -15.998 26.254 30.187  1.00 72.24  ?  194 GLU C N   1 
ATOM   4580 C CA  . GLU C 1 39  ? -17.250 25.531 30.366  1.00 73.54  ?  194 GLU C CA  1 
ATOM   4581 C C   . GLU C 1 39  ? -18.088 25.406 29.108  1.00 79.53  ?  194 GLU C C   1 
ATOM   4582 O O   . GLU C 1 39  ? -18.245 26.374 28.358  1.00 78.89  ?  194 GLU C O   1 
ATOM   4583 C CB  . GLU C 1 39  ? -18.099 26.108 31.531  1.00 74.96  ?  194 GLU C CB  1 
ATOM   4584 C CG  . GLU C 1 39  ? -18.414 27.591 31.454  1.00 82.81  ?  194 GLU C CG  1 
ATOM   4585 C CD  . GLU C 1 39  ? -19.539 28.017 32.374  1.00 109.63 ?  194 GLU C CD  1 
ATOM   4586 O OE1 . GLU C 1 39  ? -20.617 28.387 31.854  1.00 107.13 ?  194 GLU C OE1 1 
ATOM   4587 O OE2 . GLU C 1 39  ? -19.351 27.974 33.612  1.00 108.84 -1 194 GLU C OE2 1 
ATOM   4588 N N   . GLY C 1 40  ? -18.643 24.208 28.932  1.00 78.07  ?  195 GLY C N   1 
ATOM   4589 C CA  . GLY C 1 40  ? -19.571 23.855 27.867  1.00 78.82  ?  195 GLY C CA  1 
ATOM   4590 C C   . GLY C 1 40  ? -20.974 23.693 28.431  1.00 85.28  ?  195 GLY C C   1 
ATOM   4591 O O   . GLY C 1 40  ? -21.257 24.132 29.557  1.00 84.49  ?  195 GLY C O   1 
ATOM   4592 N N   . GLY C 1 41  ? -21.850 23.061 27.650  1.00 83.68  ?  196 GLY C N   1 
ATOM   4593 C CA  . GLY C 1 41  ? -23.227 22.800 28.050  1.00 83.66  ?  196 GLY C CA  1 
ATOM   4594 C C   . GLY C 1 41  ? -23.331 21.643 29.025  1.00 88.38  ?  196 GLY C C   1 
ATOM   4595 O O   . GLY C 1 41  ? -24.203 21.643 29.904  1.00 88.77  ?  196 GLY C O   1 
ATOM   4596 N N   . PHE C 1 42  ? -22.426 20.650 28.876  1.00 83.89  ?  197 PHE C N   1 
ATOM   4597 C CA  . PHE C 1 42  ? -22.386 19.438 29.694  1.00 82.41  ?  197 PHE C CA  1 
ATOM   4598 C C   . PHE C 1 42  ? -21.380 19.455 30.872  1.00 81.85  ?  197 PHE C C   1 
ATOM   4599 O O   . PHE C 1 42  ? -21.258 18.444 31.561  1.00 82.08  ?  197 PHE C O   1 
ATOM   4600 C CB  . PHE C 1 42  ? -22.233 18.189 28.802  1.00 84.15  ?  197 PHE C CB  1 
ATOM   4601 N N   . GLY C 1 43  ? -20.720 20.591 31.130  1.00 74.04  ?  198 GLY C N   1 
ATOM   4602 C CA  . GLY C 1 43  ? -19.790 20.686 32.253  1.00 72.12  ?  198 GLY C CA  1 
ATOM   4603 C C   . GLY C 1 43  ? -18.763 21.795 32.233  1.00 72.53  ?  198 GLY C C   1 
ATOM   4604 O O   . GLY C 1 43  ? -18.678 22.544 31.264  1.00 72.27  ?  198 GLY C O   1 
ATOM   4605 N N   . VAL C 1 44  ? -17.968 21.889 33.325  1.00 66.96  ?  199 VAL C N   1 
ATOM   4606 C CA  . VAL C 1 44  ? -16.871 22.847 33.547  1.00 65.48  ?  199 VAL C CA  1 
ATOM   4607 C C   . VAL C 1 44  ? -15.539 22.075 33.585  1.00 65.74  ?  199 VAL C C   1 
ATOM   4608 O O   . VAL C 1 44  ? -15.465 21.007 34.193  1.00 65.11  ?  199 VAL C O   1 
ATOM   4609 C CB  . VAL C 1 44  ? -17.085 23.691 34.834  1.00 69.45  ?  199 VAL C CB  1 
ATOM   4610 C CG1 . VAL C 1 44  ? -15.939 24.679 35.070  1.00 69.30  ?  199 VAL C CG1 1 
ATOM   4611 C CG2 . VAL C 1 44  ? -18.421 24.427 34.785  1.00 69.18  ?  199 VAL C CG2 1 
ATOM   4612 N N   . VAL C 1 45  ? -14.493 22.626 32.934  1.00 60.02  ?  200 VAL C N   1 
ATOM   4613 C CA  . VAL C 1 45  ? -13.161 22.021 32.857  1.00 57.68  ?  200 VAL C CA  1 
ATOM   4614 C C   . VAL C 1 45  ? -12.208 22.727 33.808  1.00 59.38  ?  200 VAL C C   1 
ATOM   4615 O O   . VAL C 1 45  ? -12.110 23.950 33.779  1.00 59.14  ?  200 VAL C O   1 
ATOM   4616 C CB  . VAL C 1 45  ? -12.630 21.922 31.391  1.00 59.96  ?  200 VAL C CB  1 
ATOM   4617 C CG1 . VAL C 1 45  ? -11.332 21.118 31.316  1.00 59.21  ?  200 VAL C CG1 1 
ATOM   4618 C CG2 . VAL C 1 45  ? -13.681 21.309 30.467  1.00 59.19  ?  200 VAL C CG2 1 
ATOM   4619 N N   . TYR C 1 46  ? -11.523 21.947 34.662  1.00 54.93  ?  201 TYR C N   1 
ATOM   4620 C CA  . TYR C 1 46  ? -10.554 22.431 35.660  1.00 54.62  ?  201 TYR C CA  1 
ATOM   4621 C C   . TYR C 1 46  ? -9.134  21.931 35.412  1.00 54.23  ?  201 TYR C C   1 
ATOM   4622 O O   . TYR C 1 46  ? -8.948  20.815 34.929  1.00 52.32  ?  201 TYR C O   1 
ATOM   4623 C CB  . TYR C 1 46  ? -10.971 21.997 37.085  1.00 56.68  ?  201 TYR C CB  1 
ATOM   4624 C CG  . TYR C 1 46  ? -12.351 22.462 37.492  1.00 58.91  ?  201 TYR C CG  1 
ATOM   4625 C CD1 . TYR C 1 46  ? -13.484 21.717 37.176  1.00 60.85  ?  201 TYR C CD1 1 
ATOM   4626 C CD2 . TYR C 1 46  ? -12.526 23.652 38.186  1.00 59.89  ?  201 TYR C CD2 1 
ATOM   4627 C CE1 . TYR C 1 46  ? -14.758 22.160 37.515  1.00 62.34  ?  201 TYR C CE1 1 
ATOM   4628 C CE2 . TYR C 1 46  ? -13.795 24.098 38.541  1.00 61.23  ?  201 TYR C CE2 1 
ATOM   4629 C CZ  . TYR C 1 46  ? -14.906 23.346 38.205  1.00 70.82  ?  201 TYR C CZ  1 
ATOM   4630 O OH  . TYR C 1 46  ? -16.156 23.777 38.558  1.00 75.57  ?  201 TYR C OH  1 
ATOM   4631 N N   . LYS C 1 47  ? -8.138  22.739 35.799  1.00 50.51  ?  202 LYS C N   1 
ATOM   4632 C CA  . LYS C 1 47  ? -6.724  22.376 35.722  1.00 51.93  ?  202 LYS C CA  1 
ATOM   4633 C C   . LYS C 1 47  ? -6.339  21.598 37.000  1.00 59.17  ?  202 LYS C C   1 
ATOM   4634 O O   . LYS C 1 47  ? -6.837  21.895 38.095  1.00 59.31  ?  202 LYS C O   1 
ATOM   4635 C CB  . LYS C 1 47  ? -5.834  23.630 35.564  1.00 53.80  ?  202 LYS C CB  1 
ATOM   4636 C CG  . LYS C 1 47  ? -4.422  23.339 35.069  1.00 57.29  ?  202 LYS C CG  1 
ATOM   4637 C CD  . LYS C 1 47  ? -3.642  24.618 34.880  1.00 68.92  ?  202 LYS C CD  1 
ATOM   4638 C CE  . LYS C 1 47  ? -2.191  24.344 34.583  1.00 84.96  ?  202 LYS C CE  1 
ATOM   4639 N NZ  . LYS C 1 47  ? -1.403  25.595 34.442  1.00 96.44  1  202 LYS C NZ  1 
ATOM   4640 N N   . GLY C 1 48  ? -5.467  20.611 36.838  1.00 56.96  ?  203 GLY C N   1 
ATOM   4641 C CA  . GLY C 1 48  ? -5.000  19.778 37.936  1.00 58.10  ?  203 GLY C CA  1 
ATOM   4642 C C   . GLY C 1 48  ? -3.643  19.164 37.694  1.00 65.07  ?  203 GLY C C   1 
ATOM   4643 O O   . GLY C 1 48  ? -3.064  19.339 36.621  1.00 64.76  ?  203 GLY C O   1 
ATOM   4644 N N   . TYR C 1 49  ? -3.112  18.463 38.707  1.00 64.02  ?  204 TYR C N   1 
ATOM   4645 C CA  . TYR C 1 49  ? -1.833  17.761 38.615  1.00 64.68  ?  204 TYR C CA  1 
ATOM   4646 C C   . TYR C 1 49  ? -1.952  16.380 39.245  1.00 72.02  ?  204 TYR C C   1 
ATOM   4647 O O   . TYR C 1 49  ? -2.290  16.264 40.418  1.00 71.80  ?  204 TYR C O   1 
ATOM   4648 C CB  . TYR C 1 49  ? -0.701  18.570 39.255  1.00 65.38  ?  204 TYR C CB  1 
ATOM   4649 C CG  . TYR C 1 49  ? -0.473  19.925 38.624  1.00 67.38  ?  204 TYR C CG  1 
ATOM   4650 C CD1 . TYR C 1 49  ? 0.339   20.064 37.501  1.00 69.86  ?  204 TYR C CD1 1 
ATOM   4651 C CD2 . TYR C 1 49  ? -1.034  21.078 39.173  1.00 68.00  ?  204 TYR C CD2 1 
ATOM   4652 C CE1 . TYR C 1 49  ? 0.569   21.318 36.925  1.00 71.40  ?  204 TYR C CE1 1 
ATOM   4653 C CE2 . TYR C 1 49  ? -0.816  22.335 38.605  1.00 68.97  ?  204 TYR C CE2 1 
ATOM   4654 C CZ  . TYR C 1 49  ? -0.009  22.453 37.483  1.00 80.85  ?  204 TYR C CZ  1 
ATOM   4655 O OH  . TYR C 1 49  ? 0.219   23.702 36.942  1.00 86.50  ?  204 TYR C OH  1 
ATOM   4656 N N   . VAL C 1 50  ? -1.765  15.340 38.440  1.00 71.19  ?  205 VAL C N   1 
ATOM   4657 C CA  . VAL C 1 50  ? -1.782  13.948 38.888  1.00 72.72  ?  205 VAL C CA  1 
ATOM   4658 C C   . VAL C 1 50  ? -0.394  13.385 38.546  1.00 82.86  ?  205 VAL C C   1 
ATOM   4659 O O   . VAL C 1 50  ? -0.049  13.274 37.371  1.00 83.71  ?  205 VAL C O   1 
ATOM   4660 C CB  . VAL C 1 50  ? -2.922  13.115 38.253  1.00 76.50  ?  205 VAL C CB  1 
ATOM   4661 C CG1 . VAL C 1 50  ? -2.825  11.644 38.652  1.00 75.92  ?  205 VAL C CG1 1 
ATOM   4662 C CG2 . VAL C 1 50  ? -4.287  13.681 38.628  1.00 76.71  ?  205 VAL C CG2 1 
ATOM   4663 N N   . ASN C 1 51  ? 0.427   13.122 39.571  1.00 82.72  ?  206 ASN C N   1 
ATOM   4664 C CA  . ASN C 1 51  ? 1.792   12.574 39.467  1.00 83.53  ?  206 ASN C CA  1 
ATOM   4665 C C   . ASN C 1 51  ? 2.714   13.406 38.552  1.00 88.40  ?  206 ASN C C   1 
ATOM   4666 O O   . ASN C 1 51  ? 3.303   12.883 37.590  1.00 88.25  ?  206 ASN C O   1 
ATOM   4667 C CB  . ASN C 1 51  ? 1.755   11.068 39.111  1.00 86.38  ?  206 ASN C CB  1 
ATOM   4668 C CG  . ASN C 1 51  ? 3.089   10.360 39.195  1.00 124.73 ?  206 ASN C CG  1 
ATOM   4669 O OD1 . ASN C 1 51  ? 3.470   9.604  38.295  1.00 124.59 ?  206 ASN C OD1 1 
ATOM   4670 N ND2 . ASN C 1 51  ? 3.846   10.612 40.256  1.00 119.27 ?  206 ASN C ND2 1 
ATOM   4671 N N   . ASN C 1 52  ? 2.794   14.730 38.844  1.00 85.10  ?  207 ASN C N   1 
ATOM   4672 C CA  . ASN C 1 52  ? 3.590   15.722 38.096  1.00 84.69  ?  207 ASN C CA  1 
ATOM   4673 C C   . ASN C 1 52  ? 3.018   16.071 36.709  1.00 84.91  ?  207 ASN C C   1 
ATOM   4674 O O   . ASN C 1 52  ? 3.372   17.126 36.179  1.00 85.63  ?  207 ASN C O   1 
ATOM   4675 C CB  . ASN C 1 52  ? 5.094   15.346 38.004  1.00 88.36  ?  207 ASN C CB  1 
ATOM   4676 C CG  . ASN C 1 52  ? 5.845   15.334 39.320  1.00 118.96 ?  207 ASN C CG  1 
ATOM   4677 O OD1 . ASN C 1 52  ? 5.390   15.854 40.355  1.00 116.79 ?  207 ASN C OD1 1 
ATOM   4678 N ND2 . ASN C 1 52  ? 7.040   14.759 39.301  1.00 108.79 ?  207 ASN C ND2 1 
ATOM   4679 N N   . THR C 1 53  ? 2.167   15.192 36.121  1.00 75.82  ?  208 THR C N   1 
ATOM   4680 C CA  . THR C 1 53  ? 1.496   15.394 34.845  1.00 73.29  ?  208 THR C CA  1 
ATOM   4681 C C   . THR C 1 53  ? 0.360   16.420 35.051  1.00 72.86  ?  208 THR C C   1 
ATOM   4682 O O   . THR C 1 53  ? -0.452  16.257 35.966  1.00 72.78  ?  208 THR C O   1 
ATOM   4683 C CB  . THR C 1 53  ? 0.947   14.034 34.341  1.00 81.61  ?  208 THR C CB  1 
ATOM   4684 O OG1 . THR C 1 53  ? 2.018   13.096 34.172  1.00 84.18  ?  208 THR C OG1 1 
ATOM   4685 C CG2 . THR C 1 53  ? 0.124   14.152 33.053  1.00 77.65  ?  208 THR C CG2 1 
ATOM   4686 N N   . THR C 1 54  ? 0.303   17.471 34.207  1.00 65.15  ?  209 THR C N   1 
ATOM   4687 C CA  . THR C 1 54  ? -0.779  18.456 34.252  1.00 62.96  ?  209 THR C CA  1 
ATOM   4688 C C   . THR C 1 54  ? -2.003  17.799 33.591  1.00 61.02  ?  209 THR C C   1 
ATOM   4689 O O   . THR C 1 54  ? -1.860  17.170 32.536  1.00 60.05  ?  209 THR C O   1 
ATOM   4690 C CB  . THR C 1 54  ? -0.391  19.778 33.548  1.00 73.04  ?  209 THR C CB  1 
ATOM   4691 O OG1 . THR C 1 54  ? 0.956   20.147 33.854  1.00 72.97  ?  209 THR C OG1 1 
ATOM   4692 C CG2 . THR C 1 54  ? -1.334  20.929 33.905  1.00 69.23  ?  209 THR C CG2 1 
ATOM   4693 N N   . VAL C 1 55  ? -3.190  17.908 34.229  1.00 53.83  ?  210 VAL C N   1 
ATOM   4694 C CA  . VAL C 1 55  ? -4.428  17.300 33.706  1.00 52.14  ?  210 VAL C CA  1 
ATOM   4695 C C   . VAL C 1 55  ? -5.573  18.278 33.537  1.00 53.51  ?  210 VAL C C   1 
ATOM   4696 O O   . VAL C 1 55  ? -5.589  19.324 34.174  1.00 53.56  ?  210 VAL C O   1 
ATOM   4697 C CB  . VAL C 1 55  ? -4.911  15.990 34.421  1.00 55.30  ?  210 VAL C CB  1 
ATOM   4698 C CG1 . VAL C 1 55  ? -3.868  14.891 34.366  1.00 54.75  ?  210 VAL C CG1 1 
ATOM   4699 C CG2 . VAL C 1 55  ? -5.379  16.242 35.853  1.00 55.10  ?  210 VAL C CG2 1 
ATOM   4700 N N   . ALA C 1 56  ? -6.560  17.899 32.706  1.00 47.77  ?  211 ALA C N   1 
ATOM   4701 C CA  . ALA C 1 56  ? -7.793  18.639 32.502  1.00 45.88  ?  211 ALA C CA  1 
ATOM   4702 C C   . ALA C 1 56  ? -8.912  17.766 33.092  1.00 50.69  ?  211 ALA C C   1 
ATOM   4703 O O   . ALA C 1 56  ? -9.066  16.603 32.700  1.00 51.58  ?  211 ALA C O   1 
ATOM   4704 C CB  . ALA C 1 56  ? -8.027  18.872 31.026  1.00 45.91  ?  211 ALA C CB  1 
ATOM   4705 N N   . VAL C 1 57  ? -9.643  18.295 34.080  1.00 45.75  ?  212 VAL C N   1 
ATOM   4706 C CA  . VAL C 1 57  ? -10.723 17.548 34.714  1.00 44.85  ?  212 VAL C CA  1 
ATOM   4707 C C   . VAL C 1 57  ? -12.053 18.141 34.315  1.00 48.57  ?  212 VAL C C   1 
ATOM   4708 O O   . VAL C 1 57  ? -12.352 19.285 34.679  1.00 48.23  ?  212 VAL C O   1 
ATOM   4709 C CB  . VAL C 1 57  ? -10.562 17.431 36.257  1.00 48.45  ?  212 VAL C CB  1 
ATOM   4710 C CG1 . VAL C 1 57  ? -11.640 16.532 36.858  1.00 48.02  ?  212 VAL C CG1 1 
ATOM   4711 C CG2 . VAL C 1 57  ? -9.171  16.925 36.625  1.00 48.16  ?  212 VAL C CG2 1 
ATOM   4712 N N   . LYS C 1 58  ? -12.849 17.372 33.563  1.00 45.91  ?  213 LYS C N   1 
ATOM   4713 C CA  . LYS C 1 58  ? -14.170 17.830 33.136  1.00 46.57  ?  213 LYS C CA  1 
ATOM   4714 C C   . LYS C 1 58  ? -15.187 17.332 34.142  1.00 52.83  ?  213 LYS C C   1 
ATOM   4715 O O   . LYS C 1 58  ? -15.417 16.130 34.217  1.00 52.87  ?  213 LYS C O   1 
ATOM   4716 C CB  . LYS C 1 58  ? -14.493 17.329 31.706  1.00 49.35  ?  213 LYS C CB  1 
ATOM   4717 C CG  . LYS C 1 58  ? -15.660 18.037 31.031  1.00 46.60  ?  213 LYS C CG  1 
ATOM   4718 C CD  . LYS C 1 58  ? -16.377 17.090 30.092  1.00 57.65  ?  213 LYS C CD  1 
ATOM   4719 C CE  . LYS C 1 58  ? -16.267 17.424 28.619  1.00 69.50  ?  213 LYS C CE  1 
ATOM   4720 N NZ  . LYS C 1 58  ? -16.666 16.268 27.756  1.00 76.03  1  213 LYS C NZ  1 
ATOM   4721 N N   . LYS C 1 59  ? -15.756 18.241 34.949  1.00 52.36  ?  214 LYS C N   1 
ATOM   4722 C CA  . LYS C 1 59  ? -16.790 17.904 35.929  1.00 53.63  ?  214 LYS C CA  1 
ATOM   4723 C C   . LYS C 1 59  ? -18.148 18.107 35.250  1.00 61.76  ?  214 LYS C C   1 
ATOM   4724 O O   . LYS C 1 59  ? -18.547 19.239 34.982  1.00 62.21  ?  214 LYS C O   1 
ATOM   4725 C CB  . LYS C 1 59  ? -16.654 18.728 37.223  1.00 55.61  ?  214 LYS C CB  1 
ATOM   4726 C CG  . LYS C 1 59  ? -17.443 18.157 38.400  1.00 70.41  ?  214 LYS C CG  1 
ATOM   4727 C CD  . LYS C 1 59  ? -17.388 19.041 39.638  1.00 80.89  ?  214 LYS C CD  1 
ATOM   4728 C CE  . LYS C 1 59  ? -18.495 20.069 39.653  1.00 91.32  ?  214 LYS C CE  1 
ATOM   4729 N NZ  . LYS C 1 59  ? -18.313 21.046 40.759  1.00 101.84 1  214 LYS C NZ  1 
ATOM   4730 N N   . LEU C 1 60  ? -18.818 16.997 34.925  1.00 61.21  ?  215 LEU C N   1 
ATOM   4731 C CA  . LEU C 1 60  ? -20.113 16.972 34.243  1.00 62.68  ?  215 LEU C CA  1 
ATOM   4732 C C   . LEU C 1 60  ? -21.224 17.659 35.029  1.00 71.47  ?  215 LEU C C   1 
ATOM   4733 O O   . LEU C 1 60  ? -21.404 17.391 36.218  1.00 71.50  ?  215 LEU C O   1 
ATOM   4734 C CB  . LEU C 1 60  ? -20.505 15.529 33.887  1.00 62.38  ?  215 LEU C CB  1 
ATOM   4735 C CG  . LEU C 1 60  ? -20.176 15.041 32.483  1.00 66.44  ?  215 LEU C CG  1 
ATOM   4736 C CD1 . LEU C 1 60  ? -18.683 15.005 32.221  1.00 66.38  ?  215 LEU C CD1 1 
ATOM   4737 C CD2 . LEU C 1 60  ? -20.717 13.662 32.278  1.00 68.50  ?  215 LEU C CD2 1 
ATOM   4738 N N   . ALA C 1 61  ? -21.947 18.566 34.356  1.00 71.62  ?  216 ALA C N   1 
ATOM   4739 C CA  . ALA C 1 61  ? -23.054 19.334 34.925  1.00 73.25  ?  216 ALA C CA  1 
ATOM   4740 C C   . ALA C 1 61  ? -24.210 19.454 33.926  1.00 80.32  ?  216 ALA C C   1 
ATOM   4741 O O   . ALA C 1 61  ? -23.983 19.757 32.749  1.00 80.71  ?  216 ALA C O   1 
ATOM   4742 C CB  . ALA C 1 61  ? -22.571 20.717 35.329  1.00 74.26  ?  216 ALA C CB  1 
ATOM   4743 N N   . ALA C 1 62  ? -25.451 19.210 34.394  1.00 78.12  ?  217 ALA C N   1 
ATOM   4744 C CA  . ALA C 1 62  ? -26.653 19.293 33.553  1.00 107.85 ?  217 ALA C CA  1 
ATOM   4745 C C   . ALA C 1 62  ? -27.214 20.718 33.519  1.00 147.31 ?  217 ALA C C   1 
ATOM   4746 O O   . ALA C 1 62  ? -26.490 21.667 33.209  1.00 109.77 ?  217 ALA C O   1 
ATOM   4747 C CB  . ALA C 1 62  ? -27.710 18.316 34.046  1.00 108.45 ?  217 ALA C CB  1 
ATOM   4748 N N   . THR C 1 68  ? -29.509 13.701 35.616  1.00 95.45  ?  223 THR C N   1 
ATOM   4749 C CA  . THR C 1 68  ? -30.161 13.036 34.484  1.00 95.33  ?  223 THR C CA  1 
ATOM   4750 C C   . THR C 1 68  ? -29.420 11.779 34.004  1.00 99.70  ?  223 THR C C   1 
ATOM   4751 O O   . THR C 1 68  ? -28.191 11.698 34.097  1.00 98.38  ?  223 THR C O   1 
ATOM   4752 C CB  . THR C 1 68  ? -30.502 14.037 33.336  1.00 99.96  ?  223 THR C CB  1 
ATOM   4753 O OG1 . THR C 1 68  ? -31.101 13.345 32.230  1.00 96.13  ?  223 THR C OG1 1 
ATOM   4754 C CG2 . THR C 1 68  ? -29.293 14.828 32.851  1.00 97.88  ?  223 THR C CG2 1 
ATOM   4755 N N   . GLU C 1 69  ? -30.191 10.810 33.469  1.00 97.36  ?  224 GLU C N   1 
ATOM   4756 C CA  . GLU C 1 69  ? -29.682 9.565  32.887  1.00 97.41  ?  224 GLU C CA  1 
ATOM   4757 C C   . GLU C 1 69  ? -28.988 9.870  31.557  1.00 101.97 ?  224 GLU C C   1 
ATOM   4758 O O   . GLU C 1 69  ? -28.186 9.055  31.095  1.00 102.03 ?  224 GLU C O   1 
ATOM   4759 C CB  . GLU C 1 69  ? -30.818 8.551  32.673  1.00 98.72  ?  224 GLU C CB  1 
ATOM   4760 N N   . GLU C 1 70  ? -29.292 11.046 30.947  1.00 97.99  ?  225 GLU C N   1 
ATOM   4761 C CA  . GLU C 1 70  ? -28.685 11.506 29.697  1.00 97.29  ?  225 GLU C CA  1 
ATOM   4762 C C   . GLU C 1 70  ? -27.212 11.849 29.900  1.00 97.87  ?  225 GLU C C   1 
ATOM   4763 O O   . GLU C 1 70  ? -26.377 11.426 29.098  1.00 97.99  ?  225 GLU C O   1 
ATOM   4764 C CB  . GLU C 1 70  ? -29.452 12.698 29.101  1.00 99.03  ?  225 GLU C CB  1 
ATOM   4765 C CG  . GLU C 1 70  ? -29.972 12.433 27.694  1.00 114.61 ?  225 GLU C CG  1 
ATOM   4766 C CD  . GLU C 1 70  ? -28.921 12.224 26.614  1.00 146.79 ?  225 GLU C CD  1 
ATOM   4767 O OE1 . GLU C 1 70  ? -28.522 11.058 26.379  1.00 142.38 ?  225 GLU C OE1 1 
ATOM   4768 O OE2 . GLU C 1 70  ? -28.520 13.228 25.980  1.00 145.94 -1 225 GLU C OE2 1 
ATOM   4769 N N   . LEU C 1 71  ? -26.895 12.586 30.991  1.00 90.82  ?  226 LEU C N   1 
ATOM   4770 C CA  . LEU C 1 71  ? -25.534 12.979 31.381  1.00 88.59  ?  226 LEU C CA  1 
ATOM   4771 C C   . LEU C 1 71  ? -24.693 11.734 31.692  1.00 88.83  ?  226 LEU C C   1 
ATOM   4772 O O   . LEU C 1 71  ? -23.532 11.682 31.305  1.00 88.07  ?  226 LEU C O   1 
ATOM   4773 C CB  . LEU C 1 71  ? -25.586 13.928 32.592  1.00 88.36  ?  226 LEU C CB  1 
ATOM   4774 C CG  . LEU C 1 71  ? -24.517 15.019 32.703  1.00 92.64  ?  226 LEU C CG  1 
ATOM   4775 C CD1 . LEU C 1 71  ? -24.657 16.057 31.602  1.00 92.81  ?  226 LEU C CD1 1 
ATOM   4776 C CD2 . LEU C 1 71  ? -24.632 15.739 34.024  1.00 94.61  ?  226 LEU C CD2 1 
ATOM   4777 N N   . LYS C 1 72  ? -25.302 10.714 32.331  1.00 83.68  ?  227 LYS C N   1 
ATOM   4778 C CA  . LYS C 1 72  ? -24.652 9.435  32.634  1.00 82.67  ?  227 LYS C CA  1 
ATOM   4779 C C   . LYS C 1 72  ? -24.431 8.640  31.335  1.00 84.18  ?  227 LYS C C   1 
ATOM   4780 O O   . LYS C 1 72  ? -23.411 7.956  31.207  1.00 82.53  ?  227 LYS C O   1 
ATOM   4781 C CB  . LYS C 1 72  ? -25.467 8.616  33.651  1.00 84.82  ?  227 LYS C CB  1 
ATOM   4782 N N   . GLN C 1 73  ? -25.376 8.752  30.365  1.00 79.44  ?  228 GLN C N   1 
ATOM   4783 C CA  . GLN C 1 73  ? -25.263 8.089  29.061  1.00 78.27  ?  228 GLN C CA  1 
ATOM   4784 C C   . GLN C 1 73  ? -24.109 8.721  28.276  1.00 78.39  ?  228 GLN C C   1 
ATOM   4785 O O   . GLN C 1 73  ? -23.301 7.998  27.688  1.00 77.46  ?  228 GLN C O   1 
ATOM   4786 C CB  . GLN C 1 73  ? -26.584 8.171  28.267  1.00 79.56  ?  228 GLN C CB  1 
ATOM   4787 N N   . GLN C 1 74  ? -24.025 10.069 28.327  1.00 71.95  ?  229 GLN C N   1 
ATOM   4788 C CA  . GLN C 1 74  ? -23.011 10.910 27.696  1.00 70.50  ?  229 GLN C CA  1 
ATOM   4789 C C   . GLN C 1 74  ? -21.614 10.545 28.216  1.00 73.16  ?  229 GLN C C   1 
ATOM   4790 O O   . GLN C 1 74  ? -20.687 10.389 27.415  1.00 72.36  ?  229 GLN C O   1 
ATOM   4791 C CB  . GLN C 1 74  ? -23.335 12.393 27.972  1.00 71.43  ?  229 GLN C CB  1 
ATOM   4792 C CG  . GLN C 1 74  ? -23.408 13.264 26.724  1.00 74.03  ?  229 GLN C CG  1 
ATOM   4793 C CD  . GLN C 1 74  ? -24.571 14.213 26.753  1.00 87.13  ?  229 GLN C CD  1 
ATOM   4794 O OE1 . GLN C 1 74  ? -25.705 13.827 26.486  1.00 86.50  ?  229 GLN C OE1 1 
ATOM   4795 N NE2 . GLN C 1 74  ? -24.316 15.486 27.030  1.00 74.69  ?  229 GLN C NE2 1 
ATOM   4796 N N   . PHE C 1 75  ? -21.494 10.369 29.559  1.00 69.62  ?  230 PHE C N   1 
ATOM   4797 C CA  . PHE C 1 75  ? -20.294 10.005 30.330  1.00 68.70  ?  230 PHE C CA  1 
ATOM   4798 C C   . PHE C 1 75  ? -19.787 8.634  29.892  1.00 72.69  ?  230 PHE C C   1 
ATOM   4799 O O   . PHE C 1 75  ? -18.620 8.502  29.533  1.00 72.05  ?  230 PHE C O   1 
ATOM   4800 C CB  . PHE C 1 75  ? -20.639 10.014 31.834  1.00 69.94  ?  230 PHE C CB  1 
ATOM   4801 C CG  . PHE C 1 75  ? -19.566 9.550  32.789  1.00 71.15  ?  230 PHE C CG  1 
ATOM   4802 C CD1 . PHE C 1 75  ? -18.594 10.430 33.247  1.00 74.15  ?  230 PHE C CD1 1 
ATOM   4803 C CD2 . PHE C 1 75  ? -19.559 8.248  33.271  1.00 72.67  ?  230 PHE C CD2 1 
ATOM   4804 C CE1 . PHE C 1 75  ? -17.615 10.005 34.146  1.00 75.01  ?  230 PHE C CE1 1 
ATOM   4805 C CE2 . PHE C 1 75  ? -18.579 7.824  34.169  1.00 75.39  ?  230 PHE C CE2 1 
ATOM   4806 C CZ  . PHE C 1 75  ? -17.611 8.702  34.596  1.00 73.88  ?  230 PHE C CZ  1 
ATOM   4807 N N   . ASP C 1 76  ? -20.685 7.629  29.897  1.00 70.54  ?  231 ASP C N   1 
ATOM   4808 C CA  . ASP C 1 76  ? -20.415 6.249  29.496  1.00 71.08  ?  231 ASP C CA  1 
ATOM   4809 C C   . ASP C 1 76  ? -19.955 6.165  28.054  1.00 74.77  ?  231 ASP C C   1 
ATOM   4810 O O   . ASP C 1 76  ? -19.092 5.344  27.752  1.00 74.60  ?  231 ASP C O   1 
ATOM   4811 C CB  . ASP C 1 76  ? -21.660 5.367  29.694  1.00 73.57  ?  231 ASP C CB  1 
ATOM   4812 C CG  . ASP C 1 76  ? -22.019 5.046  31.139  1.00 87.20  ?  231 ASP C CG  1 
ATOM   4813 O OD1 . ASP C 1 76  ? -21.159 5.257  32.031  1.00 87.31  ?  231 ASP C OD1 1 
ATOM   4814 O OD2 . ASP C 1 76  ? -23.150 4.560  31.376  1.00 95.05  -1 231 ASP C OD2 1 
ATOM   4815 N N   . GLN C 1 77  ? -20.517 7.007  27.164  1.00 70.98  ?  232 GLN C N   1 
ATOM   4816 C CA  . GLN C 1 77  ? -20.138 7.016  25.753  1.00 70.52  ?  232 GLN C CA  1 
ATOM   4817 C C   . GLN C 1 77  ? -18.728 7.554  25.556  1.00 74.64  ?  232 GLN C C   1 
ATOM   4818 O O   . GLN C 1 77  ? -17.970 6.954  24.791  1.00 75.20  ?  232 GLN C O   1 
ATOM   4819 C CB  . GLN C 1 77  ? -21.150 7.784  24.898  1.00 71.77  ?  232 GLN C CB  1 
ATOM   4820 C CG  . GLN C 1 77  ? -22.084 6.881  24.087  1.00 82.21  ?  232 GLN C CG  1 
ATOM   4821 C CD  . GLN C 1 77  ? -21.416 6.202  22.909  1.00 97.34  ?  232 GLN C CD  1 
ATOM   4822 O OE1 . GLN C 1 77  ? -20.794 6.967  22.028  1.00 95.23  ?  232 GLN C OE1 1 
ATOM   4823 N NE2 . GLN C 1 77  ? -21.465 4.981  22.764  1.00 84.70  ?  232 GLN C NE2 1 
ATOM   4824 N N   . GLU C 1 78  ? -18.356 8.652  26.269  1.00 69.39  ?  233 GLU C N   1 
ATOM   4825 C CA  . GLU C 1 78  ? -17.017 9.236  26.177  1.00 68.25  ?  233 GLU C CA  1 
ATOM   4826 C C   . GLU C 1 78  ? -15.959 8.169  26.531  1.00 70.59  ?  233 GLU C C   1 
ATOM   4827 O O   . GLU C 1 78  ? -14.973 8.022  25.802  1.00 70.22  ?  233 GLU C O   1 
ATOM   4828 C CB  . GLU C 1 78  ? -16.907 10.476 27.082  1.00 69.41  ?  233 GLU C CB  1 
ATOM   4829 C CG  . GLU C 1 78  ? -15.606 11.245 26.932  1.00 77.60  ?  233 GLU C CG  1 
ATOM   4830 C CD  . GLU C 1 78  ? -15.722 12.619 26.297  1.00 109.10 ?  233 GLU C CD  1 
ATOM   4831 O OE1 . GLU C 1 78  ? -16.640 13.387 26.673  1.00 111.87 ?  233 GLU C OE1 1 
ATOM   4832 O OE2 . GLU C 1 78  ? -14.821 12.967 25.497  1.00 105.55 -1 233 GLU C OE2 1 
ATOM   4833 N N   . ILE C 1 79  ? -16.200 7.396  27.613  1.00 65.49  ?  234 ILE C N   1 
ATOM   4834 C CA  . ILE C 1 79  ? -15.305 6.324  28.077  1.00 64.32  ?  234 ILE C CA  1 
ATOM   4835 C C   . ILE C 1 79  ? -15.242 5.159  27.065  1.00 67.34  ?  234 ILE C C   1 
ATOM   4836 O O   . ILE C 1 79  ? -14.144 4.725  26.720  1.00 66.41  ?  234 ILE C O   1 
ATOM   4837 C CB  . ILE C 1 79  ? -15.656 5.869  29.517  1.00 66.57  ?  234 ILE C CB  1 
ATOM   4838 C CG1 . ILE C 1 79  ? -15.430 7.018  30.501  1.00 66.45  ?  234 ILE C CG1 1 
ATOM   4839 C CG2 . ILE C 1 79  ? -14.839 4.645  29.937  1.00 66.50  ?  234 ILE C CG2 1 
ATOM   4840 C CD1 . ILE C 1 79  ? -16.127 6.882  31.805  1.00 71.69  ?  234 ILE C CD1 1 
ATOM   4841 N N   . LYS C 1 80  ? -16.411 4.692  26.563  1.00 62.96  ?  235 LYS C N   1 
ATOM   4842 C CA  . LYS C 1 80  ? -16.485 3.608  25.581  1.00 62.44  ?  235 LYS C CA  1 
ATOM   4843 C C   . LYS C 1 80  ? -15.686 3.941  24.319  1.00 66.30  ?  235 LYS C C   1 
ATOM   4844 O O   . LYS C 1 80  ? -14.868 3.126  23.903  1.00 67.38  ?  235 LYS C O   1 
ATOM   4845 C CB  . LYS C 1 80  ? -17.945 3.250  25.256  1.00 64.45  ?  235 LYS C CB  1 
ATOM   4846 N N   . VAL C 1 81  ? -15.868 5.160  23.766  1.00 61.88  ?  236 VAL C N   1 
ATOM   4847 C CA  . VAL C 1 81  ? -15.177 5.682  22.573  1.00 61.11  ?  236 VAL C CA  1 
ATOM   4848 C C   . VAL C 1 81  ? -13.677 5.784  22.818  1.00 67.54  ?  236 VAL C C   1 
ATOM   4849 O O   . VAL C 1 81  ? -12.886 5.300  22.008  1.00 67.39  ?  236 VAL C O   1 
ATOM   4850 C CB  . VAL C 1 81  ? -15.783 7.040  22.063  1.00 63.27  ?  236 VAL C CB  1 
ATOM   4851 C CG1 . VAL C 1 81  ? -14.911 7.685  20.984  1.00 62.53  ?  236 VAL C CG1 1 
ATOM   4852 C CG2 . VAL C 1 81  ? -17.219 6.861  21.554  1.00 62.75  ?  236 VAL C CG2 1 
ATOM   4853 N N   . MET C 1 82  ? -13.289 6.420  23.932  1.00 66.34  ?  237 MET C N   1 
ATOM   4854 C CA  . MET C 1 82  ? -11.891 6.623  24.270  1.00 67.26  ?  237 MET C CA  1 
ATOM   4855 C C   . MET C 1 82  ? -11.131 5.337  24.459  1.00 70.21  ?  237 MET C C   1 
ATOM   4856 O O   . MET C 1 82  ? -9.949  5.282  24.113  1.00 69.26  ?  237 MET C O   1 
ATOM   4857 C CB  . MET C 1 82  ? -11.742 7.507  25.493  1.00 70.58  ?  237 MET C CB  1 
ATOM   4858 C CG  . MET C 1 82  ? -10.625 8.499  25.323  1.00 75.86  ?  237 MET C CG  1 
ATOM   4859 S SD  . MET C 1 82  ? -11.092 9.932  24.333  1.00 81.49  ?  237 MET C SD  1 
ATOM   4860 C CE  . MET C 1 82  ? -12.065 10.821 25.553  1.00 78.59  ?  237 MET C CE  1 
ATOM   4861 N N   . ALA C 1 83  ? -11.811 4.299  24.991  1.00 66.53  ?  238 ALA C N   1 
ATOM   4862 C CA  . ALA C 1 83  ? -11.248 2.971  25.212  1.00 65.74  ?  238 ALA C CA  1 
ATOM   4863 C C   . ALA C 1 83  ? -10.851 2.345  23.885  1.00 67.23  ?  238 ALA C C   1 
ATOM   4864 O O   . ALA C 1 83  ? -9.769  1.773  23.778  1.00 65.84  ?  238 ALA C O   1 
ATOM   4865 C CB  . ALA C 1 83  ? -12.262 2.092  25.914  1.00 66.70  ?  238 ALA C CB  1 
ATOM   4866 N N   . LYS C 1 84  ? -11.696 2.511  22.863  1.00 63.87  ?  239 LYS C N   1 
ATOM   4867 C CA  . LYS C 1 84  ? -11.453 1.986  21.523  1.00 64.02  ?  239 LYS C CA  1 
ATOM   4868 C C   . LYS C 1 84  ? -10.482 2.852  20.709  1.00 69.23  ?  239 LYS C C   1 
ATOM   4869 O O   . LYS C 1 84  ? -9.566  2.311  20.081  1.00 68.96  ?  239 LYS C O   1 
ATOM   4870 C CB  . LYS C 1 84  ? -12.784 1.815  20.772  1.00 66.51  ?  239 LYS C CB  1 
ATOM   4871 N N   . CYS C 1 85  ? -10.669 4.193  20.750  1.00 66.25  ?  240 CYS C N   1 
ATOM   4872 C CA  . CYS C 1 85  ? -9.922  5.176  19.966  1.00 66.27  ?  240 CYS C CA  1 
ATOM   4873 C C   . CYS C 1 85  ? -8.702  5.826  20.631  1.00 68.09  ?  240 CYS C C   1 
ATOM   4874 O O   . CYS C 1 85  ? -8.843  6.639  21.541  1.00 69.78  ?  240 CYS C O   1 
ATOM   4875 C CB  . CYS C 1 85  ? -10.872 6.224  19.386  1.00 67.37  ?  240 CYS C CB  1 
ATOM   4876 S SG  . CYS C 1 85  ? -12.380 5.542  18.648  1.00 71.87  ?  240 CYS C SG  1 
ATOM   4877 N N   . GLN C 1 86  ? -7.510  5.503  20.130  1.00 61.16  ?  241 GLN C N   1 
ATOM   4878 C CA  . GLN C 1 86  ? -6.235  6.086  20.560  1.00 59.41  ?  241 GLN C CA  1 
ATOM   4879 C C   . GLN C 1 86  ? -5.501  6.547  19.287  1.00 59.20  ?  241 GLN C C   1 
ATOM   4880 O O   . GLN C 1 86  ? -5.174  5.725  18.418  1.00 59.05  ?  241 GLN C O   1 
ATOM   4881 C CB  . GLN C 1 86  ? -5.370  5.094  21.352  1.00 60.69  ?  241 GLN C CB  1 
ATOM   4882 C CG  . GLN C 1 86  ? -5.832  4.835  22.778  1.00 88.60  ?  241 GLN C CG  1 
ATOM   4883 C CD  . GLN C 1 86  ? -6.615  3.543  22.963  1.00 121.05 ?  241 GLN C CD  1 
ATOM   4884 O OE1 . GLN C 1 86  ? -6.641  2.639  22.105  1.00 117.86 ?  241 GLN C OE1 1 
ATOM   4885 N NE2 . GLN C 1 86  ? -7.258  3.418  24.119  1.00 114.77 ?  241 GLN C NE2 1 
ATOM   4886 N N   . HIS C 1 87  ? -5.297  7.866  19.156  1.00 50.57  ?  242 HIS C N   1 
ATOM   4887 C CA  . HIS C 1 87  ? -4.655  8.454  17.996  1.00 48.05  ?  242 HIS C CA  1 
ATOM   4888 C C   . HIS C 1 87  ? -3.972  9.769  18.390  1.00 53.24  ?  242 HIS C C   1 
ATOM   4889 O O   . HIS C 1 87  ? -4.422  10.442 19.333  1.00 54.32  ?  242 HIS C O   1 
ATOM   4890 C CB  . HIS C 1 87  ? -5.715  8.690  16.906  1.00 47.32  ?  242 HIS C CB  1 
ATOM   4891 C CG  . HIS C 1 87  ? -5.153  9.117  15.591  1.00 49.73  ?  242 HIS C CG  1 
ATOM   4892 N ND1 . HIS C 1 87  ? -4.873  10.446 15.321  1.00 50.85  ?  242 HIS C ND1 1 
ATOM   4893 C CD2 . HIS C 1 87  ? -4.822  8.372  14.515  1.00 50.55  ?  242 HIS C CD2 1 
ATOM   4894 C CE1 . HIS C 1 87  ? -4.396  10.468 14.089  1.00 49.92  ?  242 HIS C CE1 1 
ATOM   4895 N NE2 . HIS C 1 87  ? -4.348  9.242  13.563  1.00 50.14  ?  242 HIS C NE2 1 
ATOM   4896 N N   . GLU C 1 88  ? -2.912  10.153 17.634  1.00 48.21  ?  243 GLU C N   1 
ATOM   4897 C CA  . GLU C 1 88  ? -2.150  11.380 17.861  1.00 48.09  ?  243 GLU C CA  1 
ATOM   4898 C C   . GLU C 1 88  ? -2.986  12.686 17.747  1.00 50.95  ?  243 GLU C C   1 
ATOM   4899 O O   . GLU C 1 88  ? -2.555  13.739 18.239  1.00 49.86  ?  243 GLU C O   1 
ATOM   4900 C CB  . GLU C 1 88  ? -0.891  11.432 16.979  1.00 49.62  ?  243 GLU C CB  1 
ATOM   4901 C CG  . GLU C 1 88  ? -1.167  11.485 15.487  1.00 69.94  ?  243 GLU C CG  1 
ATOM   4902 C CD  . GLU C 1 88  ? 0.023   11.283 14.564  1.00 112.02 ?  243 GLU C CD  1 
ATOM   4903 O OE1 . GLU C 1 88  ? 1.128   11.786 14.884  1.00 111.39 ?  243 GLU C OE1 1 
ATOM   4904 O OE2 . GLU C 1 88  ? -0.175  10.682 13.482  1.00 111.52 -1 243 GLU C OE2 1 
ATOM   4905 N N   . ASN C 1 89  ? -4.158  12.604 17.091  1.00 46.05  ?  244 ASN C N   1 
ATOM   4906 C CA  . ASN C 1 89  ? -5.038  13.747 16.873  1.00 45.49  ?  244 ASN C CA  1 
ATOM   4907 C C   . ASN C 1 89  ? -6.328  13.632 17.647  1.00 49.85  ?  244 ASN C C   1 
ATOM   4908 O O   . ASN C 1 89  ? -7.335  14.262 17.330  1.00 48.82  ?  244 ASN C O   1 
ATOM   4909 C CB  . ASN C 1 89  ? -5.233  14.044 15.390  1.00 43.60  ?  244 ASN C CB  1 
ATOM   4910 C CG  . ASN C 1 89  ? -3.946  14.355 14.682  1.00 55.72  ?  244 ASN C CG  1 
ATOM   4911 O OD1 . ASN C 1 89  ? -3.471  13.572 13.856  1.00 47.40  ?  244 ASN C OD1 1 
ATOM   4912 N ND2 . ASN C 1 89  ? -3.323  15.474 15.024  1.00 45.99  ?  244 ASN C ND2 1 
ATOM   4913 N N   . LEU C 1 90  ? -6.275  12.840 18.712  1.00 47.32  ?  245 LEU C N   1 
ATOM   4914 C CA  . LEU C 1 90  ? -7.396  12.704 19.637  1.00 45.91  ?  245 LEU C CA  1 
ATOM   4915 C C   . LEU C 1 90  ? -6.862  12.983 21.012  1.00 49.34  ?  245 LEU C C   1 
ATOM   4916 O O   . LEU C 1 90  ? -5.719  12.660 21.321  1.00 49.48  ?  245 LEU C O   1 
ATOM   4917 C CB  . LEU C 1 90  ? -8.050  11.313 19.618  1.00 44.67  ?  245 LEU C CB  1 
ATOM   4918 C CG  . LEU C 1 90  ? -8.652  10.809 18.333  1.00 47.71  ?  245 LEU C CG  1 
ATOM   4919 C CD1 . LEU C 1 90  ? -9.299  9.494  18.580  1.00 47.64  ?  245 LEU C CD1 1 
ATOM   4920 C CD2 . LEU C 1 90  ? -9.680  11.807 17.739  1.00 48.25  ?  245 LEU C CD2 1 
ATOM   4921 N N   . VAL C 1 91  ? -7.699  13.557 21.833  1.00 44.99  ?  246 VAL C N   1 
ATOM   4922 C CA  . VAL C 1 91  ? -7.408  13.886 23.207  1.00 43.81  ?  246 VAL C CA  1 
ATOM   4923 C C   . VAL C 1 91  ? -7.258  12.557 23.967  1.00 48.53  ?  246 VAL C C   1 
ATOM   4924 O O   . VAL C 1 91  ? -7.764  11.527 23.505  1.00 49.24  ?  246 VAL C O   1 
ATOM   4925 C CB  . VAL C 1 91  ? -8.541  14.839 23.673  1.00 47.41  ?  246 VAL C CB  1 
ATOM   4926 C CG1 . VAL C 1 91  ? -9.446  14.247 24.745  1.00 46.60  ?  246 VAL C CG1 1 
ATOM   4927 C CG2 . VAL C 1 91  ? -8.004  16.209 24.046  1.00 47.44  ?  246 VAL C CG2 1 
ATOM   4928 N N   . GLU C 1 92  ? -6.468  12.545 25.045  1.00 44.75  ?  247 GLU C N   1 
ATOM   4929 C CA  . GLU C 1 92  ? -6.204  11.316 25.790  1.00 43.79  ?  247 GLU C CA  1 
ATOM   4930 C C   . GLU C 1 92  ? -6.899  11.321 27.141  1.00 47.65  ?  247 GLU C C   1 
ATOM   4931 O O   . GLU C 1 92  ? -6.772  12.277 27.908  1.00 46.79  ?  247 GLU C O   1 
ATOM   4932 C CB  . GLU C 1 92  ? -4.683  11.127 25.949  1.00 45.30  ?  247 GLU C CB  1 
ATOM   4933 C CG  . GLU C 1 92  ? -4.251  9.695  26.245  1.00 64.37  ?  247 GLU C CG  1 
ATOM   4934 C CD  . GLU C 1 92  ? -2.836  9.459  26.758  1.00 97.56  ?  247 GLU C CD  1 
ATOM   4935 O OE1 . GLU C 1 92  ? -1.924  10.266 26.451  1.00 82.57  ?  247 GLU C OE1 1 
ATOM   4936 O OE2 . GLU C 1 92  ? -2.638  8.430  27.446  1.00 102.81 -1 247 GLU C OE2 1 
ATOM   4937 N N   . LEU C 1 93  ? -7.627  10.246 27.437  1.00 45.93  ?  248 LEU C N   1 
ATOM   4938 C CA  . LEU C 1 93  ? -8.305  10.075 28.718  1.00 46.22  ?  248 LEU C CA  1 
ATOM   4939 C C   . LEU C 1 93  ? -7.370  9.318  29.644  1.00 54.74  ?  248 LEU C C   1 
ATOM   4940 O O   . LEU C 1 93  ? -6.825  8.287  29.262  1.00 56.61  ?  248 LEU C O   1 
ATOM   4941 C CB  . LEU C 1 93  ? -9.626  9.324  28.537  1.00 45.56  ?  248 LEU C CB  1 
ATOM   4942 C CG  . LEU C 1 93  ? -10.594 9.300  29.717  1.00 49.85  ?  248 LEU C CG  1 
ATOM   4943 C CD1 . LEU C 1 93  ? -11.194 10.669 29.980  1.00 49.13  ?  248 LEU C CD1 1 
ATOM   4944 C CD2 . LEU C 1 93  ? -11.716 8.293  29.471  1.00 50.87  ?  248 LEU C CD2 1 
ATOM   4945 N N   . LEU C 1 94  ? -7.127  9.858  30.834  1.00 52.84  ?  249 LEU C N   1 
ATOM   4946 C CA  . LEU C 1 94  ? -6.271  9.197  31.806  1.00 52.74  ?  249 LEU C CA  1 
ATOM   4947 C C   . LEU C 1 94  ? -7.138  8.361  32.710  1.00 59.01  ?  249 LEU C C   1 
ATOM   4948 O O   . LEU C 1 94  ? -6.763  7.247  33.045  1.00 58.34  ?  249 LEU C O   1 
ATOM   4949 C CB  . LEU C 1 94  ? -5.427  10.197 32.595  1.00 52.55  ?  249 LEU C CB  1 
ATOM   4950 C CG  . LEU C 1 94  ? -4.392  10.954 31.762  1.00 57.31  ?  249 LEU C CG  1 
ATOM   4951 C CD1 . LEU C 1 94  ? -3.827  12.118 32.520  1.00 57.55  ?  249 LEU C CD1 1 
ATOM   4952 C CD2 . LEU C 1 94  ? -3.285  10.041 31.247  1.00 57.12  ?  249 LEU C CD2 1 
ATOM   4953 N N   . GLY C 1 95  ? -8.343  8.854  32.975  1.00 58.75  ?  250 GLY C N   1 
ATOM   4954 C CA  . GLY C 1 95  ? -9.322  8.177  33.808  1.00 60.31  ?  250 GLY C CA  1 
ATOM   4955 C C   . GLY C 1 95  ? -10.641 8.900  33.991  1.00 67.64  ?  250 GLY C C   1 
ATOM   4956 O O   . GLY C 1 95  ? -11.009 9.770  33.202  1.00 67.09  ?  250 GLY C O   1 
ATOM   4957 N N   . PHE C 1 96  ? -11.363 8.527  35.048  1.00 66.49  ?  251 PHE C N   1 
ATOM   4958 C CA  . PHE C 1 96  ? -12.684 9.054  35.357  1.00 66.76  ?  251 PHE C CA  1 
ATOM   4959 C C   . PHE C 1 96  ? -13.003 8.883  36.834  1.00 69.72  ?  251 PHE C C   1 
ATOM   4960 O O   . PHE C 1 96  ? -12.281 8.183  37.540  1.00 69.03  ?  251 PHE C O   1 
ATOM   4961 C CB  . PHE C 1 96  ? -13.737 8.301  34.515  1.00 69.23  ?  251 PHE C CB  1 
ATOM   4962 C CG  . PHE C 1 96  ? -13.781 6.807  34.775  1.00 71.42  ?  251 PHE C CG  1 
ATOM   4963 C CD1 . PHE C 1 96  ? -12.922 5.939  34.105  1.00 74.55  ?  251 PHE C CD1 1 
ATOM   4964 C CD2 . PHE C 1 96  ? -14.699 6.268  35.673  1.00 73.75  ?  251 PHE C CD2 1 
ATOM   4965 C CE1 . PHE C 1 96  ? -12.962 4.565  34.351  1.00 75.59  ?  251 PHE C CE1 1 
ATOM   4966 C CE2 . PHE C 1 96  ? -14.732 4.894  35.922  1.00 76.59  ?  251 PHE C CE2 1 
ATOM   4967 C CZ  . PHE C 1 96  ? -13.861 4.053  35.261  1.00 74.57  ?  251 PHE C CZ  1 
ATOM   4968 N N   . SER C 1 97  ? -14.118 9.486  37.275  1.00 66.56  ?  252 SER C N   1 
ATOM   4969 C CA  . SER C 1 97  ? -14.666 9.373  38.621  1.00 66.66  ?  252 SER C CA  1 
ATOM   4970 C C   . SER C 1 97  ? -16.186 9.352  38.513  1.00 71.55  ?  252 SER C C   1 
ATOM   4971 O O   . SER C 1 97  ? -16.767 10.260 37.920  1.00 70.12  ?  252 SER C O   1 
ATOM   4972 C CB  . SER C 1 97  ? -14.175 10.508 39.518  1.00 70.19  ?  252 SER C CB  1 
ATOM   4973 O OG  . SER C 1 97  ? -15.139 10.934 40.469  1.00 79.30  ?  252 SER C OG  1 
ATOM   4974 N N   . SER C 1 98  ? -16.820 8.294  39.051  1.00 70.26  ?  253 SER C N   1 
ATOM   4975 C CA  . SER C 1 98  ? -18.277 8.138  39.055  1.00 71.23  ?  253 SER C CA  1 
ATOM   4976 C C   . SER C 1 98  ? -18.820 7.895  40.478  1.00 79.56  ?  253 SER C C   1 
ATOM   4977 O O   . SER C 1 98  ? -19.891 7.310  40.639  1.00 79.64  ?  253 SER C O   1 
ATOM   4978 C CB  . SER C 1 98  ? -18.715 7.047  38.080  1.00 73.34  ?  253 SER C CB  1 
ATOM   4979 O OG  . SER C 1 98  ? -18.049 5.827  38.350  1.00 81.11  ?  253 SER C OG  1 
ATOM   4980 N N   . ASP C 1 99  ? -18.090 8.387  41.499  1.00 79.11  ?  254 ASP C N   1 
ATOM   4981 C CA  . ASP C 1 99  ? -18.439 8.272  42.919  1.00 80.26  ?  254 ASP C CA  1 
ATOM   4982 C C   . ASP C 1 99  ? -19.609 9.198  43.288  1.00 87.50  ?  254 ASP C C   1 
ATOM   4983 O O   . ASP C 1 99  ? -19.433 10.405 43.480  1.00 87.10  ?  254 ASP C O   1 
ATOM   4984 C CB  . ASP C 1 99  ? -17.203 8.529  43.810  1.00 81.90  ?  254 ASP C CB  1 
ATOM   4985 N N   . GLY C 1 100 ? -20.796 8.607  43.353  1.00 87.14  ?  255 GLY C N   1 
ATOM   4986 C CA  . GLY C 1 100 ? -22.039 9.295  43.681  1.00 88.47  ?  255 GLY C CA  1 
ATOM   4987 C C   . GLY C 1 100 ? -22.658 10.076 42.532  1.00 96.24  ?  255 GLY C C   1 
ATOM   4988 O O   . GLY C 1 100 ? -22.623 9.651  41.368  1.00 96.62  ?  255 GLY C O   1 
ATOM   4989 N N   . ASP C 1 101 ? -23.243 11.236 42.871  1.00 94.21  ?  256 ASP C N   1 
ATOM   4990 C CA  . ASP C 1 101 ? -23.928 12.148 41.942  1.00 94.43  ?  256 ASP C CA  1 
ATOM   4991 C C   . ASP C 1 101 ? -22.993 12.888 40.969  1.00 95.66  ?  256 ASP C C   1 
ATOM   4992 O O   . ASP C 1 101 ? -23.466 13.353 39.931  1.00 95.36  ?  256 ASP C O   1 
ATOM   4993 C CB  . ASP C 1 101 ? -24.797 13.174 42.720  1.00 97.07  ?  256 ASP C CB  1 
ATOM   4994 C CG  . ASP C 1 101 ? -25.870 12.606 43.635  1.00 109.97 ?  256 ASP C CG  1 
ATOM   4995 O OD1 . ASP C 1 101 ? -26.070 11.365 43.626  1.00 110.60 ?  256 ASP C OD1 1 
ATOM   4996 O OD2 . ASP C 1 101 ? -26.504 13.400 44.371  1.00 116.12 -1 256 ASP C OD2 1 
ATOM   4997 N N   . ASP C 1 102 ? -21.689 13.024 41.319  1.00 89.50  ?  257 ASP C N   1 
ATOM   4998 C CA  . ASP C 1 102 ? -20.690 13.727 40.503  1.00 87.76  ?  257 ASP C CA  1 
ATOM   4999 C C   . ASP C 1 102 ? -19.899 12.823 39.558  1.00 83.31  ?  257 ASP C C   1 
ATOM   5000 O O   . ASP C 1 102 ? -19.322 11.810 39.977  1.00 83.16  ?  257 ASP C O   1 
ATOM   5001 C CB  . ASP C 1 102 ? -19.763 14.583 41.372  1.00 90.56  ?  257 ASP C CB  1 
ATOM   5002 C CG  . ASP C 1 102 ? -20.454 15.814 41.916  1.00 108.09 ?  257 ASP C CG  1 
ATOM   5003 O OD1 . ASP C 1 102 ? -20.655 16.783 41.131  1.00 108.85 ?  257 ASP C OD1 1 
ATOM   5004 O OD2 . ASP C 1 102 ? -20.799 15.816 43.120  1.00 117.21 -1 257 ASP C OD2 1 
ATOM   5005 N N   . LEU C 1 103 ? -19.888 13.209 38.275  1.00 72.25  ?  258 LEU C N   1 
ATOM   5006 C CA  . LEU C 1 103 ? -19.230 12.489 37.195  1.00 68.73  ?  258 LEU C CA  1 
ATOM   5007 C C   . LEU C 1 103 ? -18.077 13.314 36.608  1.00 67.51  ?  258 LEU C C   1 
ATOM   5008 O O   . LEU C 1 103 ? -18.287 14.430 36.146  1.00 65.71  ?  258 LEU C O   1 
ATOM   5009 C CB  . LEU C 1 103 ? -20.274 12.135 36.124  1.00 68.12  ?  258 LEU C CB  1 
ATOM   5010 C CG  . LEU C 1 103 ? -20.859 10.724 36.107  1.00 71.60  ?  258 LEU C CG  1 
ATOM   5011 C CD1 . LEU C 1 103 ? -21.190 10.195 37.512  1.00 72.16  ?  258 LEU C CD1 1 
ATOM   5012 C CD2 . LEU C 1 103 ? -22.093 10.684 35.248  1.00 71.99  ?  258 LEU C CD2 1 
ATOM   5013 N N   . CYS C 1 104 ? -16.853 12.772 36.670  1.00 62.32  ?  259 CYS C N   1 
ATOM   5014 C CA  . CYS C 1 104 ? -15.626 13.427 36.199  1.00 60.35  ?  259 CYS C CA  1 
ATOM   5015 C C   . CYS C 1 104 ? -14.888 12.643 35.143  1.00 57.36  ?  259 CYS C C   1 
ATOM   5016 O O   . CYS C 1 104 ? -14.871 11.416 35.171  1.00 57.07  ?  259 CYS C O   1 
ATOM   5017 C CB  . CYS C 1 104 ? -14.702 13.755 37.365  1.00 61.01  ?  259 CYS C CB  1 
ATOM   5018 S SG  . CYS C 1 104 ? -15.370 14.974 38.511  1.00 65.51  ?  259 CYS C SG  1 
ATOM   5019 N N   . LEU C 1 105 ? -14.227 13.365 34.247  1.00 48.30  ?  260 LEU C N   1 
ATOM   5020 C CA  . LEU C 1 105 ? -13.382 12.796 33.210  1.00 45.51  ?  260 LEU C CA  1 
ATOM   5021 C C   . LEU C 1 105 ? -12.032 13.501 33.273  1.00 47.37  ?  260 LEU C C   1 
ATOM   5022 O O   . LEU C 1 105 ? -11.973 14.734 33.338  1.00 46.74  ?  260 LEU C O   1 
ATOM   5023 C CB  . LEU C 1 105 ? -14.042 12.879 31.830  1.00 44.91  ?  260 LEU C CB  1 
ATOM   5024 C CG  . LEU C 1 105 ? -15.206 11.925 31.607  1.00 48.53  ?  260 LEU C CG  1 
ATOM   5025 C CD1 . LEU C 1 105 ? -16.111 12.409 30.511  1.00 48.97  ?  260 LEU C CD1 1 
ATOM   5026 C CD2 . LEU C 1 105 ? -14.727 10.542 31.310  1.00 50.47  ?  260 LEU C CD2 1 
ATOM   5027 N N   . VAL C 1 106 ? -10.960 12.720 33.369  1.00 42.80  ?  261 VAL C N   1 
ATOM   5028 C CA  . VAL C 1 106 ? -9.606  13.231 33.533  1.00 42.50  ?  261 VAL C CA  1 
ATOM   5029 C C   . VAL C 1 106 ? -8.804  13.003 32.260  1.00 49.50  ?  261 VAL C C   1 
ATOM   5030 O O   . VAL C 1 106 ? -8.700  11.878 31.766  1.00 50.47  ?  261 VAL C O   1 
ATOM   5031 C CB  . VAL C 1 106 ? -8.939  12.635 34.792  1.00 45.11  ?  261 VAL C CB  1 
ATOM   5032 C CG1 . VAL C 1 106 ? -7.522  13.156 34.973  1.00 44.42  ?  261 VAL C CG1 1 
ATOM   5033 C CG2 . VAL C 1 106 ? -9.770  12.943 36.025  1.00 44.81  ?  261 VAL C CG2 1 
ATOM   5034 N N   . TYR C 1 107 ? -8.263  14.092 31.719  1.00 45.12  ?  262 TYR C N   1 
ATOM   5035 C CA  . TYR C 1 107 ? -7.527  14.082 30.469  1.00 43.74  ?  262 TYR C CA  1 
ATOM   5036 C C   . TYR C 1 107 ? -6.150  14.658 30.608  1.00 46.29  ?  262 TYR C C   1 
ATOM   5037 O O   . TYR C 1 107 ? -5.884  15.417 31.537  1.00 45.46  ?  262 TYR C O   1 
ATOM   5038 C CB  . TYR C 1 107 ? -8.258  14.981 29.469  1.00 44.97  ?  262 TYR C CB  1 
ATOM   5039 C CG  . TYR C 1 107 ? -9.687  14.606 29.154  1.00 45.35  ?  262 TYR C CG  1 
ATOM   5040 C CD1 . TYR C 1 107 ? -10.746 15.147 29.879  1.00 46.59  ?  262 TYR C CD1 1 
ATOM   5041 C CD2 . TYR C 1 107 ? -9.990  13.800 28.059  1.00 44.97  ?  262 TYR C CD2 1 
ATOM   5042 C CE1 . TYR C 1 107 ? -12.067 14.866 29.542  1.00 45.41  ?  262 TYR C CE1 1 
ATOM   5043 C CE2 . TYR C 1 107 ? -11.305 13.517 27.712  1.00 44.64  ?  262 TYR C CE2 1 
ATOM   5044 C CZ  . TYR C 1 107 ? -12.337 14.035 28.467  1.00 50.43  ?  262 TYR C CZ  1 
ATOM   5045 O OH  . TYR C 1 107 ? -13.630 13.754 28.117  1.00 55.98  ?  262 TYR C OH  1 
ATOM   5046 N N   . VAL C 1 108 ? -5.310  14.406 29.605  1.00 44.08  ?  263 VAL C N   1 
ATOM   5047 C CA  . VAL C 1 108 ? -3.987  15.027 29.513  1.00 44.84  ?  263 VAL C CA  1 
ATOM   5048 C C   . VAL C 1 108 ? -4.265  16.486 29.120  1.00 49.97  ?  263 VAL C C   1 
ATOM   5049 O O   . VAL C 1 108 ? -4.887  16.722 28.079  1.00 51.15  ?  263 VAL C O   1 
ATOM   5050 C CB  . VAL C 1 108 ? -3.078  14.324 28.469  1.00 47.47  ?  263 VAL C CB  1 
ATOM   5051 C CG1 . VAL C 1 108 ? -1.787  15.104 28.238  1.00 46.53  ?  263 VAL C CG1 1 
ATOM   5052 C CG2 . VAL C 1 108 ? -2.793  12.884 28.881  1.00 47.14  ?  263 VAL C CG2 1 
ATOM   5053 N N   . TYR C 1 109 ? -3.853  17.438 29.976  1.00 44.10  ?  264 TYR C N   1 
ATOM   5054 C CA  . TYR C 1 109 ? -4.011  18.883 29.786  1.00 42.97  ?  264 TYR C CA  1 
ATOM   5055 C C   . TYR C 1 109 ? -3.383  19.351 28.479  1.00 44.94  ?  264 TYR C C   1 
ATOM   5056 O O   . TYR C 1 109 ? -2.321  18.853 28.101  1.00 43.64  ?  264 TYR C O   1 
ATOM   5057 C CB  . TYR C 1 109 ? -3.395  19.605 30.980  1.00 43.92  ?  264 TYR C CB  1 
ATOM   5058 C CG  . TYR C 1 109 ? -3.086  21.072 30.825  1.00 45.61  ?  264 TYR C CG  1 
ATOM   5059 C CD1 . TYR C 1 109 ? -3.983  22.041 31.265  1.00 47.58  ?  264 TYR C CD1 1 
ATOM   5060 C CD2 . TYR C 1 109 ? -1.821  21.495 30.429  1.00 46.74  ?  264 TYR C CD2 1 
ATOM   5061 C CE1 . TYR C 1 109 ? -3.646  23.396 31.271  1.00 47.53  ?  264 TYR C CE1 1 
ATOM   5062 C CE2 . TYR C 1 109 ? -1.480  22.848 30.412  1.00 47.86  ?  264 TYR C CE2 1 
ATOM   5063 C CZ  . TYR C 1 109 ? -2.404  23.797 30.818  1.00 52.91  ?  264 TYR C CZ  1 
ATOM   5064 O OH  . TYR C 1 109 ? -2.095  25.134 30.785  1.00 52.03  ?  264 TYR C OH  1 
ATOM   5065 N N   . MET C 1 110 ? -4.061  20.296 27.789  1.00 40.85  ?  265 MET C N   1 
ATOM   5066 C CA  . MET C 1 110 ? -3.659  20.872 26.502  1.00 39.19  ?  265 MET C CA  1 
ATOM   5067 C C   . MET C 1 110 ? -3.059  22.259 26.721  1.00 43.30  ?  265 MET C C   1 
ATOM   5068 O O   . MET C 1 110 ? -3.812  23.218 26.905  1.00 43.80  ?  265 MET C O   1 
ATOM   5069 C CB  . MET C 1 110 ? -4.840  20.885 25.521  1.00 40.75  ?  265 MET C CB  1 
ATOM   5070 C CG  . MET C 1 110 ? -5.318  19.514 25.141  1.00 43.69  ?  265 MET C CG  1 
ATOM   5071 S SD  . MET C 1 110 ? -4.175  18.659 24.048  1.00 48.12  ?  265 MET C SD  1 
ATOM   5072 C CE  . MET C 1 110 ? -3.315  17.619 25.165  1.00 44.74  ?  265 MET C CE  1 
ATOM   5073 N N   . PRO C 1 111 ? -1.702  22.375 26.767  1.00 39.24  ?  266 PRO C N   1 
ATOM   5074 C CA  . PRO C 1 111 ? -1.057  23.684 27.030  1.00 39.14  ?  266 PRO C CA  1 
ATOM   5075 C C   . PRO C 1 111 ? -1.557  24.867 26.183  1.00 44.33  ?  266 PRO C C   1 
ATOM   5076 O O   . PRO C 1 111 ? -1.406  26.029 26.601  1.00 44.47  ?  266 PRO C O   1 
ATOM   5077 C CB  . PRO C 1 111 ? 0.418   23.400 26.743  1.00 40.40  ?  266 PRO C CB  1 
ATOM   5078 C CG  . PRO C 1 111 ? 0.580   21.963 26.974  1.00 43.91  ?  266 PRO C CG  1 
ATOM   5079 C CD  . PRO C 1 111 ? -0.689  21.320 26.562  1.00 39.85  ?  266 PRO C CD  1 
ATOM   5080 N N   . ASN C 1 112 ? -2.149  24.581 24.993  1.00 38.42  ?  267 ASN C N   1 
ATOM   5081 C CA  . ASN C 1 112 ? -2.597  25.670 24.145  1.00 37.39  ?  267 ASN C CA  1 
ATOM   5082 C C   . ASN C 1 112 ? -4.088  25.850 23.992  1.00 41.49  ?  267 ASN C C   1 
ATOM   5083 O O   . ASN C 1 112 ? -4.516  26.570 23.092  1.00 40.76  ?  267 ASN C O   1 
ATOM   5084 C CB  . ASN C 1 112 ? -1.852  25.689 22.835  1.00 32.62  ?  267 ASN C CB  1 
ATOM   5085 C CG  . ASN C 1 112 ? -0.445  26.167 23.015  1.00 50.27  ?  267 ASN C CG  1 
ATOM   5086 O OD1 . ASN C 1 112 ? -0.203  27.324 23.405  1.00 42.09  ?  267 ASN C OD1 1 
ATOM   5087 N ND2 . ASN C 1 112 ? 0.511   25.278 22.736  1.00 43.21  ?  267 ASN C ND2 1 
ATOM   5088 N N   . GLY C 1 113 ? -4.852  25.245 24.906  1.00 37.74  ?  268 GLY C N   1 
ATOM   5089 C CA  . GLY C 1 113 ? -6.306  25.316 24.948  1.00 36.98  ?  268 GLY C CA  1 
ATOM   5090 C C   . GLY C 1 113 ? -6.978  24.901 23.656  1.00 39.80  ?  268 GLY C C   1 
ATOM   5091 O O   . GLY C 1 113 ? -6.488  24.007 22.958  1.00 38.46  ?  268 GLY C O   1 
ATOM   5092 N N   . SER C 1 114 ? -8.090  25.581 23.329  1.00 35.63  ?  269 SER C N   1 
ATOM   5093 C CA  . SER C 1 114 ? -8.877  25.333 22.128  1.00 35.50  ?  269 SER C CA  1 
ATOM   5094 C C   . SER C 1 114 ? -8.474  26.239 20.956  1.00 38.61  ?  269 SER C C   1 
ATOM   5095 O O   . SER C 1 114 ? -7.975  27.363 21.144  1.00 37.87  ?  269 SER C O   1 
ATOM   5096 C CB  . SER C 1 114 ? -10.368 25.502 22.425  1.00 39.76  ?  269 SER C CB  1 
ATOM   5097 O OG  . SER C 1 114 ? -10.713 26.831 22.786  1.00 45.59  ?  269 SER C OG  1 
ATOM   5098 N N   . LEU C 1 115 ? -8.741  25.746 19.742  1.00 32.11  ?  270 LEU C N   1 
ATOM   5099 C CA  . LEU C 1 115 ? -8.525  26.460 18.496  1.00 30.28  ?  270 LEU C CA  1 
ATOM   5100 C C   . LEU C 1 115 ? -9.376  27.747 18.481  1.00 33.39  ?  270 LEU C C   1 
ATOM   5101 O O   . LEU C 1 115 ? -8.915  28.782 17.994  1.00 31.72  ?  270 LEU C O   1 
ATOM   5102 C CB  . LEU C 1 115 ? -8.906  25.530 17.314  1.00 29.32  ?  270 LEU C CB  1 
ATOM   5103 C CG  . LEU C 1 115 ? -8.822  26.099 15.905  1.00 30.53  ?  270 LEU C CG  1 
ATOM   5104 C CD1 . LEU C 1 115 ? -7.435  26.666 15.598  1.00 28.47  ?  270 LEU C CD1 1 
ATOM   5105 C CD2 . LEU C 1 115 ? -9.201  25.065 14.909  1.00 32.75  ?  270 LEU C CD2 1 
ATOM   5106 N N   . LEU C 1 116 ? -10.600 27.684 19.043  1.00 30.89  ?  271 LEU C N   1 
ATOM   5107 C CA  . LEU C 1 116 ? -11.519 28.829 19.141  1.00 29.64  ?  271 LEU C CA  1 
ATOM   5108 C C   . LEU C 1 116 ? -10.788 29.957 19.876  1.00 37.62  ?  271 LEU C C   1 
ATOM   5109 O O   . LEU C 1 116 ? -10.582 31.025 19.302  1.00 39.29  ?  271 LEU C O   1 
ATOM   5110 C CB  . LEU C 1 116 ? -12.816 28.428 19.883  1.00 28.21  ?  271 LEU C CB  1 
ATOM   5111 C CG  . LEU C 1 116 ? -13.935 29.486 19.948  1.00 30.88  ?  271 LEU C CG  1 
ATOM   5112 C CD1 . LEU C 1 116 ? -14.790 29.484 18.690  1.00 30.26  ?  271 LEU C CD1 1 
ATOM   5113 C CD2 . LEU C 1 116 ? -14.826 29.247 21.103  1.00 30.24  ?  271 LEU C CD2 1 
ATOM   5114 N N   . ASP C 1 117 ? -10.283 29.668 21.089  1.00 35.29  ?  272 ASP C N   1 
ATOM   5115 C CA  . ASP C 1 117 ? -9.584  30.632 21.933  1.00 35.46  ?  272 ASP C CA  1 
ATOM   5116 C C   . ASP C 1 117 ? -8.319  31.194 21.320  1.00 41.56  ?  272 ASP C C   1 
ATOM   5117 O O   . ASP C 1 117 ? -8.082  32.403 21.429  1.00 43.19  ?  272 ASP C O   1 
ATOM   5118 C CB  . ASP C 1 117 ? -9.381  30.077 23.341  1.00 37.31  ?  272 ASP C CB  1 
ATOM   5119 C CG  . ASP C 1 117 ? -10.695 29.807 24.054  1.00 53.31  ?  272 ASP C CG  1 
ATOM   5120 O OD1 . ASP C 1 117 ? -11.744 30.344 23.603  1.00 54.96  ?  272 ASP C OD1 1 
ATOM   5121 O OD2 . ASP C 1 117 ? -10.677 29.095 25.089  1.00 64.73  -1 272 ASP C OD2 1 
ATOM   5122 N N   . ARG C 1 118 ? -7.555  30.347 20.604  1.00 36.42  ?  273 ARG C N   1 
ATOM   5123 C CA  . ARG C 1 118 ? -6.333  30.771 19.923  1.00 34.86  ?  273 ARG C CA  1 
ATOM   5124 C C   . ARG C 1 118 ? -6.620  31.626 18.695  1.00 39.43  ?  273 ARG C C   1 
ATOM   5125 O O   . ARG C 1 118 ? -5.847  32.546 18.406  1.00 39.63  ?  273 ARG C O   1 
ATOM   5126 C CB  . ARG C 1 118 ? -5.389  29.586 19.623  1.00 30.70  ?  273 ARG C CB  1 
ATOM   5127 C CG  . ARG C 1 118 ? -4.933  28.807 20.861  1.00 26.08  ?  273 ARG C CG  1 
ATOM   5128 C CD  . ARG C 1 118 ? -4.016  29.546 21.846  1.00 31.24  ?  273 ARG C CD  1 
ATOM   5129 N NE  . ARG C 1 118 ? -4.663  30.593 22.670  1.00 40.98  ?  273 ARG C NE  1 
ATOM   5130 C CZ  . ARG C 1 118 ? -5.475  30.367 23.703  1.00 52.34  ?  273 ARG C CZ  1 
ATOM   5131 N NH1 . ARG C 1 118 ? -5.989  31.388 24.388  1.00 40.77  ?  273 ARG C NH1 1 
ATOM   5132 N NH2 . ARG C 1 118 ? -5.793  29.122 24.049  1.00 34.54  1  273 ARG C NH2 1 
ATOM   5133 N N   . LEU C 1 119 ? -7.768  31.373 18.022  1.00 35.85  ?  274 LEU C N   1 
ATOM   5134 C CA  . LEU C 1 119 ? -8.195  32.152 16.862  1.00 35.46  ?  274 LEU C CA  1 
ATOM   5135 C C   . LEU C 1 119 ? -8.659  33.524 17.296  1.00 38.95  ?  274 LEU C C   1 
ATOM   5136 O O   . LEU C 1 119 ? -8.515  34.487 16.536  1.00 37.83  ?  274 LEU C O   1 
ATOM   5137 C CB  . LEU C 1 119 ? -9.288  31.438 16.056  1.00 35.21  ?  274 LEU C CB  1 
ATOM   5138 C CG  . LEU C 1 119 ? -8.846  30.253 15.164  1.00 40.44  ?  274 LEU C CG  1 
ATOM   5139 C CD1 . LEU C 1 119 ? -10.045 29.608 14.464  1.00 39.82  ?  274 LEU C CD1 1 
ATOM   5140 C CD2 . LEU C 1 119 ? -7.775  30.651 14.131  1.00 42.31  ?  274 LEU C CD2 1 
ATOM   5141 N N   . SER C 1 120 ? -9.180  33.629 18.535  1.00 36.00  ?  275 SER C N   1 
ATOM   5142 C CA  . SER C 1 120 ? -9.637  34.924 19.052  1.00 35.87  ?  275 SER C CA  1 
ATOM   5143 C C   . SER C 1 120 ? -8.557  35.629 19.864  1.00 43.42  ?  275 SER C C   1 
ATOM   5144 O O   . SER C 1 120 ? -8.791  36.778 20.252  1.00 44.85  ?  275 SER C O   1 
ATOM   5145 C CB  . SER C 1 120 ? -10.897 34.762 19.885  1.00 36.80  ?  275 SER C CB  1 
ATOM   5146 O OG  . SER C 1 120 ? -10.663 33.940 21.015  1.00 50.71  ?  275 SER C OG  1 
ATOM   5147 N N   . CYS C 1 121 ? -7.372  34.947 20.114  1.00 38.41  ?  276 CYS C N   1 
ATOM   5148 C CA  . CYS C 1 121 ? -6.234  35.430 20.915  1.00 38.40  ?  276 CYS C CA  1 
ATOM   5149 C C   . CYS C 1 121 ? -6.635  35.666 22.364  1.00 44.06  ?  276 CYS C C   1 
ATOM   5150 O O   . CYS C 1 121 ? -6.149  36.601 23.014  1.00 43.44  ?  276 CYS C O   1 
ATOM   5151 C CB  . CYS C 1 121 ? -5.573  36.667 20.312  1.00 38.51  ?  276 CYS C CB  1 
ATOM   5152 S SG  . CYS C 1 121 ? -4.940  36.417 18.644  1.00 42.86  ?  276 CYS C SG  1 
ATOM   5153 N N   . LEU C 1 122 ? -7.535  34.804 22.867  1.00 39.91  ?  277 LEU C N   1 
ATOM   5154 C CA  . LEU C 1 122 ? -8.017  34.859 24.237  1.00 37.87  ?  277 LEU C CA  1 
ATOM   5155 C C   . LEU C 1 122 ? -6.833  34.810 25.233  1.00 42.57  ?  277 LEU C C   1 
ATOM   5156 O O   . LEU C 1 122 ? -5.914  33.995 25.086  1.00 41.81  ?  277 LEU C O   1 
ATOM   5157 C CB  . LEU C 1 122 ? -9.028  33.725 24.483  1.00 36.55  ?  277 LEU C CB  1 
ATOM   5158 C CG  . LEU C 1 122 ? -9.733  33.739 25.836  1.00 39.86  ?  277 LEU C CG  1 
ATOM   5159 C CD1 . LEU C 1 122 ? -10.719 34.898 25.951  1.00 41.19  ?  277 LEU C CD1 1 
ATOM   5160 C CD2 . LEU C 1 122 ? -10.434 32.452 26.089  1.00 36.89  ?  277 LEU C CD2 1 
ATOM   5161 N N   . ASP C 1 123 ? -6.846  35.736 26.203  1.00 39.69  ?  278 ASP C N   1 
ATOM   5162 C CA  . ASP C 1 123 ? -5.826  35.891 27.252  1.00 39.74  ?  278 ASP C CA  1 
ATOM   5163 C C   . ASP C 1 123 ? -4.465  36.376 26.748  1.00 46.62  ?  278 ASP C C   1 
ATOM   5164 O O   . ASP C 1 123 ? -3.429  36.144 27.381  1.00 46.96  ?  278 ASP C O   1 
ATOM   5165 C CB  . ASP C 1 123 ? -5.732  34.664 28.171  1.00 40.94  ?  278 ASP C CB  1 
ATOM   5166 C CG  . ASP C 1 123 ? -7.058  34.257 28.786  1.00 56.32  ?  278 ASP C CG  1 
ATOM   5167 O OD1 . ASP C 1 123 ? -7.803  35.168 29.287  1.00 56.98  ?  278 ASP C OD1 1 
ATOM   5168 O OD2 . ASP C 1 123 ? -7.377  33.036 28.752  1.00 62.22  -1 278 ASP C OD2 1 
ATOM   5169 N N   . GLY C 1 124 ? -4.495  37.085 25.620  1.00 43.26  ?  279 GLY C N   1 
ATOM   5170 C CA  . GLY C 1 124 ? -3.311  37.671 25.004  1.00 41.72  ?  279 GLY C CA  1 
ATOM   5171 C C   . GLY C 1 124 ? -2.354  36.757 24.285  1.00 41.80  ?  279 GLY C C   1 
ATOM   5172 O O   . GLY C 1 124 ? -1.200  37.126 24.087  1.00 41.59  ?  279 GLY C O   1 
ATOM   5173 N N   . THR C 1 125 ? -2.809  35.601 23.842  1.00 37.46  ?  280 THR C N   1 
ATOM   5174 C CA  . THR C 1 125 ? -1.913  34.678 23.120  1.00 37.00  ?  280 THR C CA  1 
ATOM   5175 C C   . THR C 1 125 ? -1.574  35.226 21.721  1.00 39.76  ?  280 THR C C   1 
ATOM   5176 O O   . THR C 1 125 ? -2.390  35.945 21.162  1.00 39.14  ?  280 THR C O   1 
ATOM   5177 C CB  . THR C 1 125 ? -2.447  33.254 23.170  1.00 37.77  ?  280 THR C CB  1 
ATOM   5178 O OG1 . THR C 1 125 ? -3.663  33.188 22.415  1.00 46.64  ?  280 THR C OG1 1 
ATOM   5179 C CG2 . THR C 1 125 ? -2.706  32.800 24.600  1.00 28.65  ?  280 THR C CG2 1 
ATOM   5180 N N   . PRO C 1 126 ? -0.367  35.037 21.161  1.00 35.45  ?  281 PRO C N   1 
ATOM   5181 C CA  . PRO C 1 126 ? -0.119  35.631 19.831  1.00 34.98  ?  281 PRO C CA  1 
ATOM   5182 C C   . PRO C 1 126 ? -0.930  34.956 18.729  1.00 38.69  ?  281 PRO C C   1 
ATOM   5183 O O   . PRO C 1 126 ? -1.207  33.748 18.834  1.00 40.14  ?  281 PRO C O   1 
ATOM   5184 C CB  . PRO C 1 126 ? 1.386   35.451 19.631  1.00 36.92  ?  281 PRO C CB  1 
ATOM   5185 C CG  . PRO C 1 126 ? 1.725   34.251 20.453  1.00 40.79  ?  281 PRO C CG  1 
ATOM   5186 C CD  . PRO C 1 126 ? 0.803   34.276 21.650  1.00 36.11  ?  281 PRO C CD  1 
ATOM   5187 N N   . PRO C 1 127 ? -1.357  35.717 17.691  1.00 33.40  ?  282 PRO C N   1 
ATOM   5188 C CA  . PRO C 1 127 ? -2.146  35.107 16.592  1.00 32.41  ?  282 PRO C CA  1 
ATOM   5189 C C   . PRO C 1 127 ? -1.484  33.889 15.943  1.00 35.65  ?  282 PRO C C   1 
ATOM   5190 O O   . PRO C 1 127 ? -0.266  33.867 15.795  1.00 38.63  ?  282 PRO C O   1 
ATOM   5191 C CB  . PRO C 1 127 ? -2.255  36.245 15.572  1.00 34.03  ?  282 PRO C CB  1 
ATOM   5192 C CG  . PRO C 1 127 ? -1.993  37.484 16.323  1.00 37.95  ?  282 PRO C CG  1 
ATOM   5193 C CD  . PRO C 1 127 ? -1.109  37.153 17.455  1.00 33.88  ?  282 PRO C CD  1 
ATOM   5194 N N   . LEU C 1 128 ? -2.262  32.875 15.572  1.00 28.95  ?  283 LEU C N   1 
ATOM   5195 C CA  . LEU C 1 128 ? -1.696  31.701 14.869  1.00 28.18  ?  283 LEU C CA  1 
ATOM   5196 C C   . LEU C 1 128 ? -1.366  32.052 13.432  1.00 28.64  ?  283 LEU C C   1 
ATOM   5197 O O   . LEU C 1 128 ? -2.148  32.687 12.743  1.00 23.79  ?  283 LEU C O   1 
ATOM   5198 C CB  . LEU C 1 128 ? -2.647  30.488 14.849  1.00 28.15  ?  283 LEU C CB  1 
ATOM   5199 C CG  . LEU C 1 128 ? -3.050  29.922 16.182  1.00 32.19  ?  283 LEU C CG  1 
ATOM   5200 C CD1 . LEU C 1 128 ? -4.293  29.070 16.028  1.00 32.26  ?  283 LEU C CD1 1 
ATOM   5201 C CD2 . LEU C 1 128 ? -1.861  29.183 16.859  1.00 33.88  ?  283 LEU C CD2 1 
ATOM   5202 N N   . SER C 1 129 ? -0.191  31.659 12.994  1.00 28.84  ?  284 SER C N   1 
ATOM   5203 C CA  . SER C 1 129 ? 0.263   31.899 11.625  1.00 28.27  ?  284 SER C CA  1 
ATOM   5204 C C   . SER C 1 129 ? -0.484  30.984 10.657  1.00 31.82  ?  284 SER C C   1 
ATOM   5205 O O   . SER C 1 129 ? -1.072  29.982 11.086  1.00 29.76  ?  284 SER C O   1 
ATOM   5206 C CB  . SER C 1 129 ? 1.755   31.624 11.535  1.00 28.46  ?  284 SER C CB  1 
ATOM   5207 O OG  . SER C 1 129 ? 2.042   30.296 11.931  1.00 34.18  ?  284 SER C OG  1 
ATOM   5208 N N   . TRP C 1 130 ? -0.448  31.319 9.364   1.00 30.93  ?  285 TRP C N   1 
ATOM   5209 C CA  . TRP C 1 130 ? -1.026  30.484 8.314   1.00 33.51  ?  285 TRP C CA  1 
ATOM   5210 C C   . TRP C 1 130 ? -0.402  29.080 8.318   1.00 37.79  ?  285 TRP C C   1 
ATOM   5211 O O   . TRP C 1 130 ? -1.125  28.082 8.184   1.00 36.36  ?  285 TRP C O   1 
ATOM   5212 C CB  . TRP C 1 130 ? -0.817  31.130 6.954   1.00 34.16  ?  285 TRP C CB  1 
ATOM   5213 C CG  . TRP C 1 130 ? -1.418  30.345 5.850   1.00 36.41  ?  285 TRP C CG  1 
ATOM   5214 C CD1 . TRP C 1 130 ? -0.764  29.794 4.794   1.00 39.64  ?  285 TRP C CD1 1 
ATOM   5215 C CD2 . TRP C 1 130 ? -2.781  29.899 5.762   1.00 36.68  ?  285 TRP C CD2 1 
ATOM   5216 N NE1 . TRP C 1 130 ? -1.642  29.073 4.017   1.00 40.19  ?  285 TRP C NE1 1 
ATOM   5217 C CE2 . TRP C 1 130 ? -2.888  29.118 4.589   1.00 41.44  ?  285 TRP C CE2 1 
ATOM   5218 C CE3 . TRP C 1 130 ? -3.926  30.094 6.557   1.00 37.69  ?  285 TRP C CE3 1 
ATOM   5219 C CZ2 . TRP C 1 130 ? -4.090  28.520 4.191   1.00 40.45  ?  285 TRP C CZ2 1 
ATOM   5220 C CZ3 . TRP C 1 130 ? -5.115  29.503 6.164   1.00 39.48  ?  285 TRP C CZ3 1 
ATOM   5221 C CH2 . TRP C 1 130 ? -5.195  28.747 4.980   1.00 40.47  ?  285 TRP C CH2 1 
ATOM   5222 N N   . HIS C 1 131 ? 0.927   29.014 8.567   1.00 36.08  ?  286 HIS C N   1 
ATOM   5223 C CA  . HIS C 1 131 ? 1.697   27.785 8.680   1.00 37.66  ?  286 HIS C CA  1 
ATOM   5224 C C   . HIS C 1 131 ? 1.180   26.902 9.807   1.00 44.47  ?  286 HIS C C   1 
ATOM   5225 O O   . HIS C 1 131 ? 1.088   25.682 9.613   1.00 44.11  ?  286 HIS C O   1 
ATOM   5226 C CB  . HIS C 1 131 ? 3.187   28.076 8.887   1.00 39.48  ?  286 HIS C CB  1 
ATOM   5227 C CG  . HIS C 1 131 ? 4.031   26.834 8.936   1.00 43.84  ?  286 HIS C CG  1 
ATOM   5228 N ND1 . HIS C 1 131 ? 4.408   26.003 7.933   1.00 46.20  ?  286 HIS C ND1 1 
ATOM   5229 C CD2 . HIS C 1 131 ? 4.485   26.317 10.138  1.00 45.76  ?  286 HIS C CD2 1 
ATOM   5230 C CE1 . HIS C 1 131 ? 5.120   24.983 8.511   1.00 45.42  ?  286 HIS C CE1 1 
ATOM   5231 N NE2 . HIS C 1 131 ? 5.155   25.221 9.820   1.00 45.62  ?  286 HIS C NE2 1 
ATOM   5232 N N   . MET C 1 132 ? 0.855   27.503 10.984  1.00 41.37  ?  287 MET C N   1 
ATOM   5233 C CA  . MET C 1 132 ? 0.325   26.731 12.112  1.00 41.83  ?  287 MET C CA  1 
ATOM   5234 C C   . MET C 1 132 ? -1.091  26.218 11.790  1.00 42.94  ?  287 MET C C   1 
ATOM   5235 O O   . MET C 1 132 ? -1.391  25.026 11.950  1.00 41.51  ?  287 MET C O   1 
ATOM   5236 C CB  . MET C 1 132 ? 0.338   27.564 13.392  1.00 45.35  ?  287 MET C CB  1 
ATOM   5237 C CG  . MET C 1 132 ? 1.725   27.819 13.933  1.00 51.09  ?  287 MET C CG  1 
ATOM   5238 S SD  . MET C 1 132 ? 1.691   28.630 15.561  1.00 57.90  ?  287 MET C SD  1 
ATOM   5239 C CE  . MET C 1 132 ? 1.976   30.374 15.097  1.00 54.58  ?  287 MET C CE  1 
ATOM   5240 N N   . ARG C 1 133 ? -1.933  27.122 11.275  1.00 38.69  ?  288 ARG C N   1 
ATOM   5241 C CA  . ARG C 1 133 ? -3.317  26.867 10.849  1.00 37.47  ?  288 ARG C CA  1 
ATOM   5242 C C   . ARG C 1 133 ? -3.435  25.708 9.872   1.00 39.69  ?  288 ARG C C   1 
ATOM   5243 O O   . ARG C 1 133 ? -4.269  24.819 10.088  1.00 38.95  ?  288 ARG C O   1 
ATOM   5244 C CB  . ARG C 1 133 ? -3.906  28.126 10.261  1.00 33.86  ?  288 ARG C CB  1 
ATOM   5245 C CG  . ARG C 1 133 ? -4.084  29.169 11.328  1.00 28.60  ?  288 ARG C CG  1 
ATOM   5246 C CD  . ARG C 1 133 ? -4.671  30.403 10.733  1.00 25.70  ?  288 ARG C CD  1 
ATOM   5247 N NE  . ARG C 1 133 ? -4.339  31.545 11.560  1.00 33.14  ?  288 ARG C NE  1 
ATOM   5248 C CZ  . ARG C 1 133 ? -5.141  32.573 11.776  1.00 40.26  ?  288 ARG C CZ  1 
ATOM   5249 N NH1 . ARG C 1 133 ? -6.366  32.589 11.255  1.00 22.91  ?  288 ARG C NH1 1 
ATOM   5250 N NH2 . ARG C 1 133 ? -4.725  33.601 12.513  1.00 20.49  1  288 ARG C NH2 1 
ATOM   5251 N N   . CYS C 1 134 ? -2.552  25.665 8.846   1.00 34.52  ?  289 CYS C N   1 
ATOM   5252 C CA  . CYS C 1 134 ? -2.528  24.537 7.910   1.00 33.21  ?  289 CYS C CA  1 
ATOM   5253 C C   . CYS C 1 134 ? -2.287  23.187 8.616   1.00 34.88  ?  289 CYS C C   1 
ATOM   5254 O O   . CYS C 1 134 ? -2.996  22.233 8.309   1.00 33.22  ?  289 CYS C O   1 
ATOM   5255 C CB  . CYS C 1 134 ? -1.517  24.771 6.798   1.00 33.64  ?  289 CYS C CB  1 
ATOM   5256 S SG  . CYS C 1 134 ? -1.974  26.097 5.659   1.00 38.08  ?  289 CYS C SG  1 
ATOM   5257 N N   . LYS C 1 135 ? -1.320  23.107 9.569   1.00 31.98  ?  290 LYS C N   1 
ATOM   5258 C CA  . LYS C 1 135 ? -1.003  21.853 10.275  1.00 33.13  ?  290 LYS C CA  1 
ATOM   5259 C C   . LYS C 1 135 ? -2.140  21.409 11.175  1.00 41.32  ?  290 LYS C C   1 
ATOM   5260 O O   . LYS C 1 135 ? -2.390  20.203 11.264  1.00 42.17  ?  290 LYS C O   1 
ATOM   5261 C CB  . LYS C 1 135 ? 0.330   21.900 11.040  1.00 36.68  ?  290 LYS C CB  1 
ATOM   5262 C CG  . LYS C 1 135 ? 1.530   22.268 10.160  1.00 65.02  ?  290 LYS C CG  1 
ATOM   5263 C CD  . LYS C 1 135 ? 2.871   21.798 10.738  1.00 76.51  ?  290 LYS C CD  1 
ATOM   5264 C CE  . LYS C 1 135 ? 4.019   21.971 9.762   1.00 89.87  ?  290 LYS C CE  1 
ATOM   5265 N NZ  . LYS C 1 135 ? 3.829   21.210 8.492   1.00 102.72 1  290 LYS C NZ  1 
ATOM   5266 N N   . ILE C 1 136 ? -2.870  22.377 11.790  1.00 38.42  ?  291 ILE C N   1 
ATOM   5267 C CA  . ILE C 1 136 ? -4.043  22.082 12.636  1.00 38.49  ?  291 ILE C CA  1 
ATOM   5268 C C   . ILE C 1 136 ? -5.178  21.482 11.766  1.00 43.79  ?  291 ILE C C   1 
ATOM   5269 O O   . ILE C 1 136 ? -5.835  20.536 12.194  1.00 45.43  ?  291 ILE C O   1 
ATOM   5270 C CB  . ILE C 1 136 ? -4.470  23.334 13.476  1.00 40.73  ?  291 ILE C CB  1 
ATOM   5271 C CG1 . ILE C 1 136 ? -3.378  23.681 14.509  1.00 42.04  ?  291 ILE C CG1 1 
ATOM   5272 C CG2 . ILE C 1 136 ? -5.829  23.170 14.147  1.00 36.91  ?  291 ILE C CG2 1 
ATOM   5273 C CD1 . ILE C 1 136 ? -3.228  25.246 14.850  1.00 52.52  ?  291 ILE C CD1 1 
ATOM   5274 N N   . ALA C 1 137 ? -5.379  22.008 10.556  1.00 39.23  ?  292 ALA C N   1 
ATOM   5275 C CA  . ALA C 1 137 ? -6.374  21.490 9.610   1.00 39.45  ?  292 ALA C CA  1 
ATOM   5276 C C   . ALA C 1 137 ? -6.018  20.053 9.206   1.00 44.01  ?  292 ALA C C   1 
ATOM   5277 O O   . ALA C 1 137 ? -6.900  19.182 9.172   1.00 43.22  ?  292 ALA C O   1 
ATOM   5278 C CB  . ALA C 1 137 ? -6.417  22.365 8.360   1.00 39.97  ?  292 ALA C CB  1 
ATOM   5279 N N   . GLN C 1 138 ? -4.721  19.809 8.918   1.00 40.36  ?  293 GLN C N   1 
ATOM   5280 C CA  . GLN C 1 138 ? -4.263  18.489 8.507   1.00 40.46  ?  293 GLN C CA  1 
ATOM   5281 C C   . GLN C 1 138 ? -4.491  17.523 9.662   1.00 41.99  ?  293 GLN C C   1 
ATOM   5282 O O   . GLN C 1 138 ? -5.144  16.503 9.483   1.00 40.52  ?  293 GLN C O   1 
ATOM   5283 C CB  . GLN C 1 138 ? -2.789  18.511 8.025   1.00 41.90  ?  293 GLN C CB  1 
ATOM   5284 C CG  . GLN C 1 138 ? -2.532  19.406 6.800   1.00 51.45  ?  293 GLN C CG  1 
ATOM   5285 C CD  . GLN C 1 138 ? -1.066  19.770 6.532   1.00 66.11  ?  293 GLN C CD  1 
ATOM   5286 O OE1 . GLN C 1 138 ? -0.222  19.943 7.450   1.00 53.51  ?  293 GLN C OE1 1 
ATOM   5287 N NE2 . GLN C 1 138 ? -0.745  19.938 5.241   1.00 52.97  ?  293 GLN C NE2 1 
ATOM   5288 N N   . GLY C 1 139 ? -4.064  17.944 10.843  1.00 38.88  ?  294 GLY C N   1 
ATOM   5289 C CA  . GLY C 1 139 ? -4.191  17.219 12.096  1.00 39.04  ?  294 GLY C CA  1 
ATOM   5290 C C   . GLY C 1 139 ? -5.616  16.846 12.405  1.00 45.35  ?  294 GLY C C   1 
ATOM   5291 O O   . GLY C 1 139 ? -5.909  15.655 12.500  1.00 47.27  ?  294 GLY C O   1 
ATOM   5292 N N   . ALA C 1 140 ? -6.528  17.846 12.499  1.00 41.50  ?  295 ALA C N   1 
ATOM   5293 C CA  . ALA C 1 140 ? -7.947  17.620 12.800  1.00 41.13  ?  295 ALA C CA  1 
ATOM   5294 C C   . ALA C 1 140 ? -8.617  16.631 11.850  1.00 44.37  ?  295 ALA C C   1 
ATOM   5295 O O   . ALA C 1 140 ? -9.360  15.780 12.317  1.00 44.42  ?  295 ALA C O   1 
ATOM   5296 C CB  . ALA C 1 140 ? -8.711  18.936 12.842  1.00 42.12  ?  295 ALA C CB  1 
ATOM   5297 N N   . ALA C 1 141 ? -8.302  16.689 10.538  1.00 40.88  ?  296 ALA C N   1 
ATOM   5298 C CA  . ALA C 1 141 ? -8.840  15.773 9.528   1.00 40.03  ?  296 ALA C CA  1 
ATOM   5299 C C   . ALA C 1 141 ? -8.388  14.365 9.801   1.00 46.07  ?  296 ALA C C   1 
ATOM   5300 O O   . ALA C 1 141 ? -9.183  13.457 9.604   1.00 47.87  ?  296 ALA C O   1 
ATOM   5301 C CB  . ALA C 1 141 ? -8.406  16.192 8.144   1.00 40.64  ?  296 ALA C CB  1 
ATOM   5302 N N   . ASN C 1 142 ? -7.146  14.162 10.289  1.00 42.42  ?  297 ASN C N   1 
ATOM   5303 C CA  . ASN C 1 142 ? -6.679  12.825 10.658  1.00 43.33  ?  297 ASN C CA  1 
ATOM   5304 C C   . ASN C 1 142 ? -7.473  12.301 11.876  1.00 51.80  ?  297 ASN C C   1 
ATOM   5305 O O   . ASN C 1 142 ? -7.864  11.124 11.889  1.00 53.65  ?  297 ASN C O   1 
ATOM   5306 C CB  . ASN C 1 142 ? -5.187  12.801 10.932  1.00 43.55  ?  297 ASN C CB  1 
ATOM   5307 C CG  . ASN C 1 142 ? -4.324  13.471 9.885   1.00 66.99  ?  297 ASN C CG  1 
ATOM   5308 O OD1 . ASN C 1 142 ? -4.711  13.667 8.722   1.00 64.43  ?  297 ASN C OD1 1 
ATOM   5309 N ND2 . ASN C 1 142 ? -3.141  13.898 10.306  1.00 54.10  ?  297 ASN C ND2 1 
ATOM   5310 N N   . GLY C 1 143 ? -7.754  13.194 12.839  1.00 47.67  ?  298 GLY C N   1 
ATOM   5311 C CA  . GLY C 1 143 ? -8.571  12.901 14.011  1.00 47.03  ?  298 GLY C CA  1 
ATOM   5312 C C   . GLY C 1 143 ? -9.951  12.403 13.615  1.00 50.67  ?  298 GLY C C   1 
ATOM   5313 O O   . GLY C 1 143 ? -10.372 11.331 14.058  1.00 50.77  ?  298 GLY C O   1 
ATOM   5314 N N   . ILE C 1 144 ? -10.651 13.163 12.747  1.00 46.03  ?  299 ILE C N   1 
ATOM   5315 C CA  . ILE C 1 144 ? -11.974 12.818 12.201  1.00 45.19  ?  299 ILE C CA  1 
ATOM   5316 C C   . ILE C 1 144 ? -11.894 11.520 11.358  1.00 50.17  ?  299 ILE C C   1 
ATOM   5317 O O   . ILE C 1 144 ? -12.792 10.666 11.455  1.00 50.17  ?  299 ILE C O   1 
ATOM   5318 C CB  . ILE C 1 144 ? -12.611 14.010 11.422  1.00 46.97  ?  299 ILE C CB  1 
ATOM   5319 C CG1 . ILE C 1 144 ? -12.689 15.252 12.335  1.00 47.67  ?  299 ILE C CG1 1 
ATOM   5320 C CG2 . ILE C 1 144 ? -14.006 13.649 10.876  1.00 45.41  ?  299 ILE C CG2 1 
ATOM   5321 C CD1 . ILE C 1 144 ? -12.884 16.579 11.659  1.00 54.84  ?  299 ILE C CD1 1 
ATOM   5322 N N   . ASN C 1 145 ? -10.802 11.365 10.578  1.00 45.83  ?  300 ASN C N   1 
ATOM   5323 C CA  . ASN C 1 145 ? -10.584 10.188 9.761   1.00 46.23  ?  300 ASN C CA  1 
ATOM   5324 C C   . ASN C 1 145 ? -10.421 8.923  10.589  1.00 52.01  ?  300 ASN C C   1 
ATOM   5325 O O   . ASN C 1 145 ? -10.937 7.871  10.210  1.00 52.51  ?  300 ASN C O   1 
ATOM   5326 C CB  . ASN C 1 145 ? -9.395  10.361 8.837   1.00 46.98  ?  300 ASN C CB  1 
ATOM   5327 C CG  . ASN C 1 145 ? -9.131  9.112  8.059   1.00 63.33  ?  300 ASN C CG  1 
ATOM   5328 O OD1 . ASN C 1 145 ? -9.902  8.743  7.176   1.00 53.07  ?  300 ASN C OD1 1 
ATOM   5329 N ND2 . ASN C 1 145 ? -8.111  8.376  8.466   1.00 62.18  ?  300 ASN C ND2 1 
ATOM   5330 N N   . PHE C 1 146 ? -9.698  9.020  11.697  1.00 48.68  ?  301 PHE C N   1 
ATOM   5331 C CA  . PHE C 1 146 ? -9.510  7.892  12.582  1.00 48.66  ?  301 PHE C CA  1 
ATOM   5332 C C   . PHE C 1 146 ? -10.846 7.464  13.183  1.00 54.22  ?  301 PHE C C   1 
ATOM   5333 O O   . PHE C 1 146 ? -11.167 6.280  13.161  1.00 54.82  ?  301 PHE C O   1 
ATOM   5334 C CB  . PHE C 1 146 ? -8.484  8.239  13.658  1.00 50.59  ?  301 PHE C CB  1 
ATOM   5335 C CG  . PHE C 1 146 ? -8.207  7.117  14.613  1.00 52.39  ?  301 PHE C CG  1 
ATOM   5336 C CD1 . PHE C 1 146 ? -7.325  6.092  14.274  1.00 55.71  ?  301 PHE C CD1 1 
ATOM   5337 C CD2 . PHE C 1 146 ? -8.838  7.070  15.845  1.00 54.45  ?  301 PHE C CD2 1 
ATOM   5338 C CE1 . PHE C 1 146 ? -7.066  5.049  15.166  1.00 57.28  ?  301 PHE C CE1 1 
ATOM   5339 C CE2 . PHE C 1 146 ? -8.588  6.024  16.728  1.00 57.63  ?  301 PHE C CE2 1 
ATOM   5340 C CZ  . PHE C 1 146 ? -7.699  5.020  16.388  1.00 55.99  ?  301 PHE C CZ  1 
ATOM   5341 N N   . LEU C 1 147 ? -11.646 8.432  13.658  1.00 51.26  ?  302 LEU C N   1 
ATOM   5342 C CA  . LEU C 1 147 ? -12.962 8.171  14.226  1.00 51.11  ?  302 LEU C CA  1 
ATOM   5343 C C   . LEU C 1 147 ? -13.885 7.519  13.210  1.00 53.38  ?  302 LEU C C   1 
ATOM   5344 O O   . LEU C 1 147 ? -14.600 6.584  13.552  1.00 53.68  ?  302 LEU C O   1 
ATOM   5345 C CB  . LEU C 1 147 ? -13.595 9.467  14.746  1.00 51.39  ?  302 LEU C CB  1 
ATOM   5346 C CG  . LEU C 1 147 ? -13.006 10.027 16.015  1.00 56.40  ?  302 LEU C CG  1 
ATOM   5347 C CD1 . LEU C 1 147 ? -13.348 11.488 16.142  1.00 56.69  ?  302 LEU C CD1 1 
ATOM   5348 C CD2 . LEU C 1 147 ? -13.481 9.251  17.223  1.00 59.90  ?  302 LEU C CD2 1 
ATOM   5349 N N   . HIS C 1 148 ? -13.870 8.019  11.967  1.00 47.52  ?  303 HIS C N   1 
ATOM   5350 C CA  . HIS C 1 148 ? -14.697 7.508  10.873  1.00 45.59  ?  303 HIS C CA  1 
ATOM   5351 C C   . HIS C 1 148 ? -14.303 6.076  10.482  1.00 48.89  ?  303 HIS C C   1 
ATOM   5352 O O   . HIS C 1 148 ? -15.189 5.236  10.340  1.00 48.74  ?  303 HIS C O   1 
ATOM   5353 C CB  . HIS C 1 148 ? -14.658 8.477  9.689   1.00 44.96  ?  303 HIS C CB  1 
ATOM   5354 C CG  . HIS C 1 148 ? -15.595 9.636  9.840   1.00 47.14  ?  303 HIS C CG  1 
ATOM   5355 N ND1 . HIS C 1 148 ? -16.148 10.425 8.891   1.00 48.25  ?  303 HIS C ND1 1 
ATOM   5356 C CD2 . HIS C 1 148 ? -16.045 10.058 11.090  1.00 47.14  ?  303 HIS C CD2 1 
ATOM   5357 C CE1 . HIS C 1 148 ? -16.955 11.322 9.547   1.00 46.47  ?  303 HIS C CE1 1 
ATOM   5358 N NE2 . HIS C 1 148 ? -16.868 11.062 10.854  1.00 46.64  ?  303 HIS C NE2 1 
ATOM   5359 N N   . GLU C 1 149 ? -12.972 5.789  10.395  1.00 43.47  ?  304 GLU C N   1 
ATOM   5360 C CA  . GLU C 1 149 ? -12.406 4.463  10.123  1.00 42.24  ?  304 GLU C CA  1 
ATOM   5361 C C   . GLU C 1 149 ? -12.839 3.494  11.234  1.00 47.84  ?  304 GLU C C   1 
ATOM   5362 O O   . GLU C 1 149 ? -12.972 2.291  11.003  1.00 47.62  ?  304 GLU C O   1 
ATOM   5363 C CB  . GLU C 1 149 ? -10.884 4.518  10.110  1.00 42.69  ?  304 GLU C CB  1 
ATOM   5364 C CG  . GLU C 1 149 ? -10.290 4.885  8.772   1.00 59.19  ?  304 GLU C CG  1 
ATOM   5365 C CD  . GLU C 1 149 ? -8.772  4.971  8.730   1.00 92.34  ?  304 GLU C CD  1 
ATOM   5366 O OE1 . GLU C 1 149 ? -8.131  4.754  9.783   1.00 72.29  ?  304 GLU C OE1 1 
ATOM   5367 O OE2 . GLU C 1 149 ? -8.221  5.246  7.637   1.00 97.06  -1 304 GLU C OE2 1 
ATOM   5368 N N   . ASN C 1 150 ? -13.070 4.029  12.434  1.00 44.83  ?  305 ASN C N   1 
ATOM   5369 C CA  . ASN C 1 150 ? -13.473 3.234  13.576  1.00 44.65  ?  305 ASN C CA  1 
ATOM   5370 C C   . ASN C 1 150 ? -14.968 3.285  13.793  1.00 49.51  ?  305 ASN C C   1 
ATOM   5371 O O   . ASN C 1 150 ? -15.439 2.977  14.889  1.00 47.89  ?  305 ASN C O   1 
ATOM   5372 C CB  . ASN C 1 150 ? -12.664 3.617  14.815  1.00 46.25  ?  305 ASN C CB  1 
ATOM   5373 C CG  . ASN C 1 150 ? -11.237 3.100  14.766  1.00 75.02  ?  305 ASN C CG  1 
ATOM   5374 O OD1 . ASN C 1 150 ? -10.865 2.168  15.476  1.00 72.28  ?  305 ASN C OD1 1 
ATOM   5375 N ND2 . ASN C 1 150 ? -10.414 3.639  13.876  1.00 67.69  ?  305 ASN C ND2 1 
ATOM   5376 N N   . HIS C 1 151 ? -15.719 3.651  12.726  1.00 48.64  ?  306 HIS C N   1 
ATOM   5377 C CA  . HIS C 1 151 ? -17.183 3.688  12.683  1.00 50.63  ?  306 HIS C CA  1 
ATOM   5378 C C   . HIS C 1 151 ? -17.788 4.517  13.793  1.00 57.68  ?  306 HIS C C   1 
ATOM   5379 O O   . HIS C 1 151 ? -18.670 4.067  14.516  1.00 58.16  ?  306 HIS C O   1 
ATOM   5380 C CB  . HIS C 1 151 ? -17.763 2.258  12.630  1.00 52.57  ?  306 HIS C CB  1 
ATOM   5381 C CG  . HIS C 1 151 ? -17.026 1.400  11.653  1.00 57.08  ?  306 HIS C CG  1 
ATOM   5382 N ND1 . HIS C 1 151 ? -17.272 1.484  10.281  1.00 59.33  ?  306 HIS C ND1 1 
ATOM   5383 C CD2 . HIS C 1 151 ? -15.990 0.553  11.865  1.00 59.00  ?  306 HIS C CD2 1 
ATOM   5384 C CE1 . HIS C 1 151 ? -16.408 0.660  9.715   1.00 58.98  ?  306 HIS C CE1 1 
ATOM   5385 N NE2 . HIS C 1 151 ? -15.608 0.083  10.629  1.00 59.30  ?  306 HIS C NE2 1 
ATOM   5386 N N   . HIS C 1 152 ? -17.277 5.730  13.951  1.00 56.62  ?  307 HIS C N   1 
ATOM   5387 C CA  . HIS C 1 152 ? -17.764 6.689  14.935  1.00 56.89  ?  307 HIS C CA  1 
ATOM   5388 C C   . HIS C 1 152 ? -18.050 8.007  14.279  1.00 55.81  ?  307 HIS C C   1 
ATOM   5389 O O   . HIS C 1 152 ? -17.301 8.435  13.401  1.00 55.18  ?  307 HIS C O   1 
ATOM   5390 C CB  . HIS C 1 152 ? -16.777 6.878  16.092  1.00 59.05  ?  307 HIS C CB  1 
ATOM   5391 C CG  . HIS C 1 152 ? -16.738 5.715  17.027  1.00 63.67  ?  307 HIS C CG  1 
ATOM   5392 N ND1 . HIS C 1 152 ? -17.803 5.427  17.865  1.00 66.28  ?  307 HIS C ND1 1 
ATOM   5393 C CD2 . HIS C 1 152 ? -15.767 4.795  17.223  1.00 66.20  ?  307 HIS C CD2 1 
ATOM   5394 C CE1 . HIS C 1 152 ? -17.452 4.342  18.536  1.00 65.72  ?  307 HIS C CE1 1 
ATOM   5395 N NE2 . HIS C 1 152 ? -16.239 3.921  18.181  1.00 66.16  ?  307 HIS C NE2 1 
ATOM   5396 N N   . ILE C 1 153 ? -19.150 8.628  14.685  1.00 49.72  ?  308 ILE C N   1 
ATOM   5397 C CA  . ILE C 1 153 ? -19.571 9.965  14.246  1.00 48.27  ?  308 ILE C CA  1 
ATOM   5398 C C   . ILE C 1 153 ? -19.411 10.833 15.486  1.00 49.51  ?  308 ILE C C   1 
ATOM   5399 O O   . ILE C 1 153 ? -19.942 10.479 16.543  1.00 48.68  ?  308 ILE C O   1 
ATOM   5400 C CB  . ILE C 1 153 ? -21.019 10.029 13.677  1.00 50.38  ?  308 ILE C CB  1 
ATOM   5401 C CG1 . ILE C 1 153 ? -21.307 8.878  12.707  1.00 50.04  ?  308 ILE C CG1 1 
ATOM   5402 C CG2 . ILE C 1 153 ? -21.272 11.383 13.003  1.00 50.68  ?  308 ILE C CG2 1 
ATOM   5403 C CD1 . ILE C 1 153 ? -22.746 8.448  12.702  1.00 51.78  ?  308 ILE C CD1 1 
ATOM   5404 N N   . HIS C 1 154 ? -18.642 11.926 15.371  1.00 44.13  ?  309 HIS C N   1 
ATOM   5405 C CA  . HIS C 1 154 ? -18.382 12.817 16.495  1.00 43.54  ?  309 HIS C CA  1 
ATOM   5406 C C   . HIS C 1 154 ? -19.659 13.519 16.982  1.00 46.49  ?  309 HIS C C   1 
ATOM   5407 O O   . HIS C 1 154 ? -19.934 13.498 18.182  1.00 46.07  ?  309 HIS C O   1 
ATOM   5408 C CB  . HIS C 1 154 ? -17.267 13.821 16.162  1.00 43.79  ?  309 HIS C CB  1 
ATOM   5409 C CG  . HIS C 1 154 ? -16.817 14.637 17.339  1.00 46.68  ?  309 HIS C CG  1 
ATOM   5410 N ND1 . HIS C 1 154 ? -17.573 15.690 17.830  1.00 48.22  ?  309 HIS C ND1 1 
ATOM   5411 C CD2 . HIS C 1 154 ? -15.715 14.504 18.108  1.00 48.18  ?  309 HIS C CD2 1 
ATOM   5412 C CE1 . HIS C 1 154 ? -16.901 16.161 18.867  1.00 47.46  ?  309 HIS C CE1 1 
ATOM   5413 N NE2 . HIS C 1 154 ? -15.773 15.482 19.068  1.00 47.76  ?  309 HIS C NE2 1 
ATOM   5414 N N   . ARG C 1 155 ? -20.413 14.131 16.059  1.00 43.36  ?  310 ARG C N   1 
ATOM   5415 C CA  . ARG C 1 155 ? -21.682 14.862 16.277  1.00 44.31  ?  310 ARG C CA  1 
ATOM   5416 C C   . ARG C 1 155 ? -21.531 16.298 16.848  1.00 48.21  ?  310 ARG C C   1 
ATOM   5417 O O   . ARG C 1 155 ? -22.530 17.007 16.938  1.00 46.39  ?  310 ARG C O   1 
ATOM   5418 C CB  . ARG C 1 155 ? -22.730 14.055 17.090  1.00 45.06  ?  310 ARG C CB  1 
ATOM   5419 C CG  . ARG C 1 155 ? -23.288 12.799 16.417  1.00 55.17  ?  310 ARG C CG  1 
ATOM   5420 C CD  . ARG C 1 155 ? -24.773 12.618 16.735  1.00 67.79  ?  310 ARG C CD  1 
ATOM   5421 N NE  . ARG C 1 155 ? -25.009 12.406 18.165  1.00 77.30  ?  310 ARG C NE  1 
ATOM   5422 C CZ  . ARG C 1 155 ? -26.183 12.538 18.780  1.00 88.31  ?  310 ARG C CZ  1 
ATOM   5423 N NH1 . ARG C 1 155 ? -27.271 12.880 18.092  1.00 56.96  ?  310 ARG C NH1 1 
ATOM   5424 N NH2 . ARG C 1 155 ? -26.279 12.326 20.086  1.00 81.89  1  310 ARG C NH2 1 
ATOM   5425 N N   . ASP C 1 156 ? -20.307 16.718 17.237  1.00 46.05  ?  311 ASP C N   1 
ATOM   5426 C CA  . ASP C 1 156 ? -20.084 18.051 17.810  1.00 46.67  ?  311 ASP C CA  1 
ATOM   5427 C C   . ASP C 1 156 ? -18.717 18.648 17.382  1.00 50.37  ?  311 ASP C C   1 
ATOM   5428 O O   . ASP C 1 156 ? -17.979 19.231 18.189  1.00 48.02  ?  311 ASP C O   1 
ATOM   5429 C CB  . ASP C 1 156 ? -20.295 18.027 19.345  1.00 49.14  ?  311 ASP C CB  1 
ATOM   5430 C CG  . ASP C 1 156 ? -20.601 19.359 20.006  1.00 65.40  ?  311 ASP C CG  1 
ATOM   5431 O OD1 . ASP C 1 156 ? -20.984 20.319 19.277  1.00 66.71  ?  311 ASP C OD1 1 
ATOM   5432 O OD2 . ASP C 1 156 ? -20.480 19.442 21.258  1.00 73.25  -1 311 ASP C OD2 1 
ATOM   5433 N N   . ILE C 1 157 ? -18.382 18.483 16.085  1.00 47.62  ?  312 ILE C N   1 
ATOM   5434 C CA  . ILE C 1 157 ? -17.148 19.026 15.522  1.00 45.96  ?  312 ILE C CA  1 
ATOM   5435 C C   . ILE C 1 157 ? -17.252 20.537 15.408  1.00 46.20  ?  312 ILE C C   1 
ATOM   5436 O O   . ILE C 1 157 ? -18.147 21.056 14.729  1.00 47.77  ?  312 ILE C O   1 
ATOM   5437 C CB  . ILE C 1 157 ? -16.730 18.312 14.221  1.00 48.46  ?  312 ILE C CB  1 
ATOM   5438 C CG1 . ILE C 1 157 ? -16.014 17.003 14.608  1.00 48.72  ?  312 ILE C CG1 1 
ATOM   5439 C CG2 . ILE C 1 157 ? -15.807 19.230 13.359  1.00 48.18  ?  312 ILE C CG2 1 
ATOM   5440 C CD1 . ILE C 1 157 ? -16.060 16.004 13.627  1.00 58.15  ?  312 ILE C CD1 1 
ATOM   5441 N N   . LYS C 1 158 ? -16.375 21.224 16.143  1.00 37.25  ?  313 LYS C N   1 
ATOM   5442 C CA  . LYS C 1 158 ? -16.271 22.672 16.226  1.00 35.45  ?  313 LYS C CA  1 
ATOM   5443 C C   . LYS C 1 158 ? -14.895 23.070 16.756  1.00 41.42  ?  313 LYS C C   1 
ATOM   5444 O O   . LYS C 1 158 ? -14.181 22.229 17.302  1.00 40.24  ?  313 LYS C O   1 
ATOM   5445 C CB  . LYS C 1 158 ? -17.405 23.275 17.071  1.00 35.54  ?  313 LYS C CB  1 
ATOM   5446 C CG  . LYS C 1 158 ? -17.546 22.742 18.478  1.00 32.41  ?  313 LYS C CG  1 
ATOM   5447 C CD  . LYS C 1 158 ? -18.804 23.294 19.078  1.00 32.03  ?  313 LYS C CD  1 
ATOM   5448 C CE  . LYS C 1 158 ? -18.923 22.979 20.545  1.00 44.26  ?  313 LYS C CE  1 
ATOM   5449 N NZ  . LYS C 1 158 ? -19.913 23.873 21.209  1.00 56.71  1  313 LYS C NZ  1 
ATOM   5450 N N   . SER C 1 159 ? -14.508 24.345 16.586  1.00 40.35  ?  314 SER C N   1 
ATOM   5451 C CA  . SER C 1 159 ? -13.193 24.795 17.028  1.00 40.89  ?  314 SER C CA  1 
ATOM   5452 C C   . SER C 1 159 ? -12.979 24.766 18.534  1.00 45.17  ?  314 SER C C   1 
ATOM   5453 O O   . SER C 1 159 ? -11.852 24.537 18.961  1.00 46.87  ?  314 SER C O   1 
ATOM   5454 C CB  . SER C 1 159 ? -12.801 26.116 16.384  1.00 44.82  ?  314 SER C CB  1 
ATOM   5455 O OG  . SER C 1 159 ? -13.757 27.119 16.664  1.00 52.66  ?  314 SER C OG  1 
ATOM   5456 N N   . ALA C 1 160 ? -14.055 24.876 19.336  1.00 39.60  ?  315 ALA C N   1 
ATOM   5457 C CA  . ALA C 1 160 ? -13.979 24.752 20.803  1.00 36.77  ?  315 ALA C CA  1 
ATOM   5458 C C   . ALA C 1 160 ? -13.589 23.312 21.173  1.00 40.35  ?  315 ALA C C   1 
ATOM   5459 O O   . ALA C 1 160 ? -12.997 23.101 22.239  1.00 41.56  ?  315 ALA C O   1 
ATOM   5460 C CB  . ALA C 1 160 ? -15.311 25.100 21.433  1.00 36.39  ?  315 ALA C CB  1 
ATOM   5461 N N   . ASN C 1 161 ? -13.898 22.332 20.276  1.00 34.60  ?  316 ASN C N   1 
ATOM   5462 C CA  . ASN C 1 161 ? -13.594 20.897 20.439  1.00 34.10  ?  316 ASN C CA  1 
ATOM   5463 C C   . ASN C 1 161 ? -12.319 20.424 19.729  1.00 38.37  ?  316 ASN C C   1 
ATOM   5464 O O   . ASN C 1 161 ? -12.072 19.213 19.639  1.00 39.05  ?  316 ASN C O   1 
ATOM   5465 C CB  . ASN C 1 161 ? -14.805 20.027 20.059  1.00 31.12  ?  316 ASN C CB  1 
ATOM   5466 C CG  . ASN C 1 161 ? -15.908 20.083 21.071  1.00 47.63  ?  316 ASN C CG  1 
ATOM   5467 O OD1 . ASN C 1 161 ? -15.737 20.511 22.218  1.00 32.53  ?  316 ASN C OD1 1 
ATOM   5468 N ND2 . ASN C 1 161 ? -17.073 19.640 20.669  1.00 52.47  ?  316 ASN C ND2 1 
ATOM   5469 N N   . ILE C 1 162 ? -11.517 21.369 19.202  1.00 33.29  ?  317 ILE C N   1 
ATOM   5470 C CA  . ILE C 1 162 ? -10.243 21.043 18.578  1.00 32.06  ?  317 ILE C CA  1 
ATOM   5471 C C   . ILE C 1 162 ? -9.239  21.686 19.486  1.00 37.71  ?  317 ILE C C   1 
ATOM   5472 O O   . ILE C 1 162 ? -9.102  22.919 19.526  1.00 38.54  ?  317 ILE C O   1 
ATOM   5473 C CB  . ILE C 1 162 ? -10.102 21.489 17.100  1.00 35.05  ?  317 ILE C CB  1 
ATOM   5474 C CG1 . ILE C 1 162 ? -11.162 20.810 16.219  1.00 35.14  ?  317 ILE C CG1 1 
ATOM   5475 C CG2 . ILE C 1 162 ? -8.694  21.160 16.577  1.00 36.74  ?  317 ILE C CG2 1 
ATOM   5476 C CD1 . ILE C 1 162 ? -11.445 21.531 14.908  1.00 34.18  ?  317 ILE C CD1 1 
ATOM   5477 N N   . LEU C 1 163 ? -8.584  20.856 20.284  1.00 34.63  ?  318 LEU C N   1 
ATOM   5478 C CA  . LEU C 1 163 ? -7.608  21.353 21.242  1.00 34.09  ?  318 LEU C CA  1 
ATOM   5479 C C   . LEU C 1 163 ? -6.192  21.324 20.701  1.00 40.14  ?  318 LEU C C   1 
ATOM   5480 O O   . LEU C 1 163 ? -5.911  20.677 19.685  1.00 38.23  ?  318 LEU C O   1 
ATOM   5481 C CB  . LEU C 1 163 ? -7.746  20.649 22.591  1.00 33.59  ?  318 LEU C CB  1 
ATOM   5482 C CG  . LEU C 1 163 ? -9.158  20.607 23.179  1.00 38.43  ?  318 LEU C CG  1 
ATOM   5483 C CD1 . LEU C 1 163 ? -9.176  19.826 24.445  1.00 40.03  ?  318 LEU C CD1 1 
ATOM   5484 C CD2 . LEU C 1 163 ? -9.726  22.002 23.424  1.00 36.22  ?  318 LEU C CD2 1 
ATOM   5485 N N   . LEU C 1 164 ? -5.307  22.077 21.361  1.00 39.94  ?  319 LEU C N   1 
ATOM   5486 C CA  . LEU C 1 164 ? -3.920  22.229 20.945  1.00 39.98  ?  319 LEU C CA  1 
ATOM   5487 C C   . LEU C 1 164 ? -2.918  21.924 22.051  1.00 43.96  ?  319 LEU C C   1 
ATOM   5488 O O   . LEU C 1 164 ? -2.954  22.549 23.121  1.00 41.54  ?  319 LEU C O   1 
ATOM   5489 C CB  . LEU C 1 164 ? -3.709  23.654 20.403  1.00 39.47  ?  319 LEU C CB  1 
ATOM   5490 C CG  . LEU C 1 164 ? -4.593  24.080 19.254  1.00 42.16  ?  319 LEU C CG  1 
ATOM   5491 C CD1 . LEU C 1 164 ? -4.541  25.538 19.079  1.00 42.23  ?  319 LEU C CD1 1 
ATOM   5492 C CD2 . LEU C 1 164 ? -4.217  23.365 17.979  1.00 42.92  ?  319 LEU C CD2 1 
ATOM   5493 N N   . ASP C 1 165 ? -2.006  20.976 21.771  1.00 42.93  ?  320 ASP C N   1 
ATOM   5494 C CA  . ASP C 1 165 ? -0.955  20.576 22.712  1.00 43.25  ?  320 ASP C CA  1 
ATOM   5495 C C   . ASP C 1 165 ? 0.230   21.566 22.696  1.00 47.78  ?  320 ASP C C   1 
ATOM   5496 O O   . ASP C 1 165 ? 0.199   22.576 21.984  1.00 46.90  ?  320 ASP C O   1 
ATOM   5497 C CB  . ASP C 1 165 ? -0.504  19.116 22.425  1.00 44.66  ?  320 ASP C CB  1 
ATOM   5498 C CG  . ASP C 1 165 ? 0.434   18.883 21.239  1.00 53.19  ?  320 ASP C CG  1 
ATOM   5499 O OD1 . ASP C 1 165 ? 0.823   19.872 20.577  1.00 53.37  ?  320 ASP C OD1 1 
ATOM   5500 O OD2 . ASP C 1 165 ? 0.805   17.710 20.991  1.00 59.45  -1 320 ASP C OD2 1 
ATOM   5501 N N   . GLU C 1 166 ? 1.289   21.227 23.442  1.00 46.15  ?  321 GLU C N   1 
ATOM   5502 C CA  . GLU C 1 166 ? 2.543   21.983 23.531  1.00 46.55  ?  321 GLU C CA  1 
ATOM   5503 C C   . GLU C 1 166 ? 3.197   22.283 22.174  1.00 49.39  ?  321 GLU C C   1 
ATOM   5504 O O   . GLU C 1 166 ? 3.853   23.313 22.054  1.00 50.93  ?  321 GLU C O   1 
ATOM   5505 C CB  . GLU C 1 166 ? 3.541   21.287 24.455  1.00 48.14  ?  321 GLU C CB  1 
ATOM   5506 C CG  . GLU C 1 166 ? 3.731   19.799 24.186  1.00 61.03  ?  321 GLU C CG  1 
ATOM   5507 C CD  . GLU C 1 166 ? 4.616   19.024 25.150  1.00 88.19  ?  321 GLU C CD  1 
ATOM   5508 O OE1 . GLU C 1 166 ? 5.002   19.579 26.209  1.00 84.22  ?  321 GLU C OE1 1 
ATOM   5509 O OE2 . GLU C 1 166 ? 4.911   17.843 24.850  1.00 74.49  -1 321 GLU C OE2 1 
ATOM   5510 N N   . ALA C 1 167 ? 2.997   21.427 21.159  1.00 42.24  ?  322 ALA C N   1 
ATOM   5511 C CA  . ALA C 1 167 ? 3.546   21.629 19.815  1.00 40.91  ?  322 ALA C CA  1 
ATOM   5512 C C   . ALA C 1 167 ? 2.494   22.166 18.829  1.00 45.72  ?  322 ALA C C   1 
ATOM   5513 O O   . ALA C 1 167 ? 2.788   22.298 17.636  1.00 47.03  ?  322 ALA C O   1 
ATOM   5514 C CB  . ALA C 1 167 ? 4.116   20.320 19.293  1.00 41.15  ?  322 ALA C CB  1 
ATOM   5515 N N   . PHE C 1 168 ? 1.286   22.494 19.320  1.00 41.05  ?  323 PHE C N   1 
ATOM   5516 C CA  . PHE C 1 168 ? 0.127   22.950 18.523  1.00 39.78  ?  323 PHE C CA  1 
ATOM   5517 C C   . PHE C 1 168 ? -0.449  21.840 17.640  1.00 42.56  ?  323 PHE C C   1 
ATOM   5518 O O   . PHE C 1 168 ? -0.970  22.104 16.544  1.00 43.02  ?  323 PHE C O   1 
ATOM   5519 C CB  . PHE C 1 168 ? 0.394   24.238 17.740  1.00 40.72  ?  323 PHE C CB  1 
ATOM   5520 C CG  . PHE C 1 168 ? 0.554   25.431 18.631  1.00 41.38  ?  323 PHE C CG  1 
ATOM   5521 C CD1 . PHE C 1 168 ? 1.788   25.729 19.204  1.00 42.83  ?  323 PHE C CD1 1 
ATOM   5522 C CD2 . PHE C 1 168 ? -0.528  26.264 18.903  1.00 42.82  ?  323 PHE C CD2 1 
ATOM   5523 C CE1 . PHE C 1 168 ? 1.941   26.839 20.033  1.00 42.79  ?  323 PHE C CE1 1 
ATOM   5524 C CE2 . PHE C 1 168 ? -0.378  27.370 19.734  1.00 44.43  ?  323 PHE C CE2 1 
ATOM   5525 C CZ  . PHE C 1 168 ? 0.860   27.656 20.289  1.00 41.97  ?  323 PHE C CZ  1 
ATOM   5526 N N   . THR C 1 169 ? -0.371  20.596 18.136  1.00 37.18  ?  324 THR C N   1 
ATOM   5527 C CA  . THR C 1 169 ? -0.955  19.453 17.448  1.00 37.12  ?  324 THR C CA  1 
ATOM   5528 C C   . THR C 1 169 ? -2.453  19.506 17.741  1.00 41.37  ?  324 THR C C   1 
ATOM   5529 O O   . THR C 1 169 ? -2.849  19.733 18.885  1.00 41.53  ?  324 THR C O   1 
ATOM   5530 C CB  . THR C 1 169 ? -0.298  18.142 17.906  1.00 44.86  ?  324 THR C CB  1 
ATOM   5531 O OG1 . THR C 1 169 ? 1.072   18.149 17.520  1.00 49.92  ?  324 THR C OG1 1 
ATOM   5532 C CG2 . THR C 1 169 ? -0.983  16.898 17.348  1.00 40.80  ?  324 THR C CG2 1 
ATOM   5533 N N   . ALA C 1 170 ? -3.268  19.359 16.700  1.00 38.29  ?  325 ALA C N   1 
ATOM   5534 C CA  . ALA C 1 170 ? -4.713  19.373 16.822  1.00 39.26  ?  325 ALA C CA  1 
ATOM   5535 C C   . ALA C 1 170 ? -5.155  18.076 17.486  1.00 45.40  ?  325 ALA C C   1 
ATOM   5536 O O   . ALA C 1 170 ? -4.679  16.989 17.127  1.00 44.54  ?  325 ALA C O   1 
ATOM   5537 C CB  . ALA C 1 170 ? -5.357  19.512 15.445  1.00 40.22  ?  325 ALA C CB  1 
ATOM   5538 N N   . LYS C 1 171 ? -6.040  18.200 18.487  1.00 42.26  ?  326 LYS C N   1 
ATOM   5539 C CA  . LYS C 1 171 ? -6.574  17.060 19.194  1.00 41.65  ?  326 LYS C CA  1 
ATOM   5540 C C   . LYS C 1 171 ? -8.044  17.234 19.390  1.00 45.11  ?  326 LYS C C   1 
ATOM   5541 O O   . LYS C 1 171 ? -8.466  18.155 20.109  1.00 46.74  ?  326 LYS C O   1 
ATOM   5542 C CB  . LYS C 1 171 ? -5.826  16.849 20.512  1.00 44.71  ?  326 LYS C CB  1 
ATOM   5543 C CG  . LYS C 1 171 ? -4.579  16.016 20.293  1.00 45.96  ?  326 LYS C CG  1 
ATOM   5544 C CD  . LYS C 1 171 ? -3.441  16.419 21.161  1.00 47.55  ?  326 LYS C CD  1 
ATOM   5545 C CE  . LYS C 1 171 ? -2.186  15.618 20.828  1.00 65.78  ?  326 LYS C CE  1 
ATOM   5546 N NZ  . LYS C 1 171 ? -2.364  14.142 20.979  1.00 74.47  1  326 LYS C NZ  1 
ATOM   5547 N N   . ILE C 1 172 ? -8.838  16.383 18.692  1.00 38.92  ?  327 ILE C N   1 
ATOM   5548 C CA  . ILE C 1 172 ? -10.306 16.368 18.761  1.00 37.91  ?  327 ILE C CA  1 
ATOM   5549 C C   . ILE C 1 172 ? -10.715 15.899 20.182  1.00 41.13  ?  327 ILE C C   1 
ATOM   5550 O O   . ILE C 1 172 ? -10.164 14.920 20.704  1.00 36.60  ?  327 ILE C O   1 
ATOM   5551 C CB  . ILE C 1 172 ? -10.920 15.436 17.672  1.00 41.01  ?  327 ILE C CB  1 
ATOM   5552 C CG1 . ILE C 1 172 ? -10.285 15.577 16.257  1.00 41.40  ?  327 ILE C CG1 1 
ATOM   5553 C CG2 . ILE C 1 172 ? -12.450 15.525 17.649  1.00 41.34  ?  327 ILE C CG2 1 
ATOM   5554 C CD1 . ILE C 1 172 ? -10.532 16.903 15.486  1.00 54.27  ?  327 ILE C CD1 1 
ATOM   5555 N N   . SER C 1 173 ? -11.655 16.620 20.799  1.00 41.50  ?  328 SER C N   1 
ATOM   5556 C CA  . SER C 1 173 ? -12.157 16.302 22.135  1.00 42.54  ?  328 SER C CA  1 
ATOM   5557 C C   . SER C 1 173 ? -13.670 16.235 22.131  1.00 50.63  ?  328 SER C C   1 
ATOM   5558 O O   . SER C 1 173 ? -14.290 16.421 21.074  1.00 51.03  ?  328 SER C O   1 
ATOM   5559 C CB  . SER C 1 173 ? -11.663 17.333 23.148  1.00 44.54  ?  328 SER C CB  1 
ATOM   5560 O OG  . SER C 1 173 ? -12.234 18.603 22.888  1.00 48.20  ?  328 SER C OG  1 
ATOM   5561 N N   . ASP C 1 174 ? -14.260 15.972 23.314  1.00 49.99  ?  329 ASP C N   1 
ATOM   5562 C CA  . ASP C 1 174 ? -15.709 15.895 23.569  1.00 51.11  ?  329 ASP C CA  1 
ATOM   5563 C C   . ASP C 1 174 ? -16.446 14.869 22.747  1.00 58.98  ?  329 ASP C C   1 
ATOM   5564 O O   . ASP C 1 174 ? -17.079 15.215 21.747  1.00 57.97  ?  329 ASP C O   1 
ATOM   5565 C CB  . ASP C 1 174 ? -16.389 17.271 23.519  1.00 52.54  ?  329 ASP C CB  1 
ATOM   5566 C CG  . ASP C 1 174 ? -17.355 17.495 24.656  1.00 68.48  ?  329 ASP C CG  1 
ATOM   5567 O OD1 . ASP C 1 174 ? -17.892 16.494 25.190  1.00 70.87  ?  329 ASP C OD1 1 
ATOM   5568 O OD2 . ASP C 1 174 ? -17.602 18.675 25.000  1.00 77.11  -1 329 ASP C OD2 1 
ATOM   5569 N N   . PHE C 1 175 ? -16.378 13.599 23.190  1.00 59.65  ?  330 PHE C N   1 
ATOM   5570 C CA  . PHE C 1 175 ? -17.017 12.442 22.548  1.00 61.42  ?  330 PHE C CA  1 
ATOM   5571 C C   . PHE C 1 175 ? -18.301 11.986 23.269  1.00 69.56  ?  330 PHE C C   1 
ATOM   5572 O O   . PHE C 1 175 ? -18.769 10.864 23.040  1.00 69.21  ?  330 PHE C O   1 
ATOM   5573 C CB  . PHE C 1 175 ? -16.012 11.282 22.428  1.00 63.03  ?  330 PHE C CB  1 
ATOM   5574 C CG  . PHE C 1 175 ? -14.745 11.673 21.714  1.00 64.90  ?  330 PHE C CG  1 
ATOM   5575 C CD1 . PHE C 1 175 ? -14.705 11.745 20.331  1.00 68.45  ?  330 PHE C CD1 1 
ATOM   5576 C CD2 . PHE C 1 175 ? -13.592 11.982 22.428  1.00 67.31  ?  330 PHE C CD2 1 
ATOM   5577 C CE1 . PHE C 1 175 ? -13.525 12.110 19.670  1.00 69.92  ?  330 PHE C CE1 1 
ATOM   5578 C CE2 . PHE C 1 175 ? -12.417 12.362 21.768  1.00 70.52  ?  330 PHE C CE2 1 
ATOM   5579 C CZ  . PHE C 1 175 ? -12.389 12.419 20.394  1.00 68.90  ?  330 PHE C CZ  1 
ATOM   5580 N N   . GLY C 1 176 ? -18.849 12.861 24.117  1.00 69.06  ?  331 GLY C N   1 
ATOM   5581 C CA  . GLY C 1 176 ? -20.079 12.599 24.856  1.00 70.47  ?  331 GLY C CA  1 
ATOM   5582 C C   . GLY C 1 176 ? -21.267 12.344 23.940  1.00 78.01  ?  331 GLY C C   1 
ATOM   5583 O O   . GLY C 1 176 ? -22.077 11.455 24.225  1.00 78.12  ?  331 GLY C O   1 
ATOM   5584 N N   . LEU C 1 177 ? -21.351 13.101 22.801  1.00 75.83  ?  332 LEU C N   1 
ATOM   5585 C CA  . LEU C 1 177 ? -22.413 12.975 21.795  1.00 75.63  ?  332 LEU C CA  1 
ATOM   5586 C C   . LEU C 1 177 ? -22.086 11.996 20.657  1.00 78.97  ?  332 LEU C C   1 
ATOM   5587 O O   . LEU C 1 177 ? -22.942 11.760 19.803  1.00 78.50  ?  332 LEU C O   1 
ATOM   5588 C CB  . LEU C 1 177 ? -22.834 14.355 21.226  1.00 75.69  ?  332 LEU C CB  1 
ATOM   5589 C CG  . LEU C 1 177 ? -23.881 15.206 22.000  1.00 80.20  ?  332 LEU C CG  1 
ATOM   5590 C CD1 . LEU C 1 177 ? -24.929 14.339 22.713  1.00 80.39  ?  332 LEU C CD1 1 
ATOM   5591 C CD2 . LEU C 1 177 ? -23.211 16.125 23.005  1.00 82.33  ?  332 LEU C CD2 1 
ATOM   5592 N N   . ALA C 1 178 ? -20.878 11.403 20.659  1.00 75.61  ?  333 ALA C N   1 
ATOM   5593 C CA  . ALA C 1 178 ? -20.440 10.464 19.618  1.00 75.41  ?  333 ALA C CA  1 
ATOM   5594 C C   . ALA C 1 178 ? -21.329 9.238  19.465  1.00 79.89  ?  333 ALA C C   1 
ATOM   5595 O O   . ALA C 1 178 ? -21.901 8.760  20.446  1.00 79.59  ?  333 ALA C O   1 
ATOM   5596 C CB  . ALA C 1 178 ? -18.983 10.058 19.816  1.00 76.02  ?  333 ALA C CB  1 
ATOM   5597 N N   . ARG C 1 179 ? -21.478 8.769  18.218  1.00 77.07  ?  334 ARG C N   1 
ATOM   5598 C CA  . ARG C 1 179 ? -22.304 7.616  17.876  1.00 77.24  ?  334 ARG C CA  1 
ATOM   5599 C C   . ARG C 1 179 ? -21.529 6.574  17.088  1.00 81.66  ?  334 ARG C C   1 
ATOM   5600 O O   . ARG C 1 179 ? -20.697 6.923  16.257  1.00 81.53  ?  334 ARG C O   1 
ATOM   5601 C CB  . ARG C 1 179 ? -23.527 8.065  17.055  1.00 78.38  ?  334 ARG C CB  1 
ATOM   5602 C CG  . ARG C 1 179 ? -24.644 8.741  17.847  1.00 90.85  ?  334 ARG C CG  1 
ATOM   5603 C CD  . ARG C 1 179 ? -25.523 7.737  18.579  1.00 98.58  ?  334 ARG C CD  1 
ATOM   5604 N NE  . ARG C 1 179 ? -26.864 8.263  18.857  1.00 104.14 ?  334 ARG C NE  1 
ATOM   5605 C CZ  . ARG C 1 179 ? -27.190 8.984  19.928  1.00 114.20 ?  334 ARG C CZ  1 
ATOM   5606 N NH1 . ARG C 1 179 ? -28.437 9.401  20.099  1.00 92.76  ?  334 ARG C NH1 1 
ATOM   5607 N NH2 . ARG C 1 179 ? -26.268 9.303  20.832  1.00 104.11 1  334 ARG C NH2 1 
ATOM   5608 N N   . ALA C 1 180 ? -21.823 5.295  17.330  1.00 78.97  ?  335 ALA C N   1 
ATOM   5609 C CA  . ALA C 1 180 ? -21.218 4.193  16.591  1.00 108.54 ?  335 ALA C CA  1 
ATOM   5610 C C   . ALA C 1 180 ? -22.115 3.880  15.393  1.00 114.81 ?  335 ALA C C   1 
ATOM   5611 O O   . ALA C 1 180 ? -22.316 4.757  14.546  1.00 68.17  ?  335 ALA C O   1 
ATOM   5612 C CB  . ALA C 1 180 ? -21.066 2.971  17.479  1.00 109.30 ?  335 ALA C CB  1 
HETATM 5613 N N   . TPO C 1 187 ? -27.605 6.097  7.483   1.00 116.53 ?  342 TPO C N   1 
HETATM 5614 C CA  . TPO C 1 187 ? -28.261 7.318  7.953   1.00 116.58 ?  342 TPO C CA  1 
HETATM 5615 C CB  . TPO C 1 187 ? -28.535 8.346  6.805   1.00 118.45 ?  342 TPO C CB  1 
HETATM 5616 C CG2 . TPO C 1 187 ? -29.231 9.601  7.378   1.00 118.46 ?  342 TPO C CG2 1 
HETATM 5617 O OG1 . TPO C 1 187 ? -27.251 8.756  6.224   1.00 119.71 ?  342 TPO C OG1 1 
HETATM 5618 P P   . TPO C 1 187 ? -27.167 8.713  4.685   1.00 120.46 ?  342 TPO C P   1 
HETATM 5619 O O1P . TPO C 1 187 ? -28.222 7.754  4.056   1.00 120.32 ?  342 TPO C O1P 1 
HETATM 5620 O O2P . TPO C 1 187 ? -27.429 10.112 4.080   1.00 120.84 -1 342 TPO C O2P 1 
HETATM 5621 O O3P . TPO C 1 187 ? -25.717 8.282  4.396   1.00 120.07 -1 342 TPO C O3P 1 
HETATM 5622 C C   . TPO C 1 187 ? -29.496 7.005  8.803   1.00 117.08 ?  342 TPO C C   1 
HETATM 5623 O O   . TPO C 1 187 ? -30.467 6.439  8.295   1.00 116.06 ?  342 TPO C O   1 
ATOM   5624 N N   . VAL C 1 188 ? -29.448 7.384  10.096  1.00 111.43 ?  343 VAL C N   1 
ATOM   5625 C CA  . VAL C 1 188 ? -30.524 7.166  11.075  1.00 110.16 ?  343 VAL C CA  1 
ATOM   5626 C C   . VAL C 1 188 ? -31.201 8.486  11.534  1.00 111.24 ?  343 VAL C C   1 
ATOM   5627 O O   . VAL C 1 188 ? -30.909 9.544  10.976  1.00 110.15 ?  343 VAL C O   1 
ATOM   5628 C CB  . VAL C 1 188 ? -30.121 6.207  12.245  1.00 114.08 ?  343 VAL C CB  1 
ATOM   5629 C CG1 . VAL C 1 188 ? -29.820 4.799  11.732  1.00 114.01 ?  343 VAL C CG1 1 
ATOM   5630 C CG2 . VAL C 1 188 ? -28.952 6.753  13.068  1.00 113.74 ?  343 VAL C CG2 1 
ATOM   5631 N N   . MET C 1 189 ? -32.115 8.411  12.523  1.00 106.35 ?  344 MET C N   1 
ATOM   5632 C CA  . MET C 1 189 ? -32.865 9.561  13.034  1.00 105.43 ?  344 MET C CA  1 
ATOM   5633 C C   . MET C 1 189 ? -32.897 9.624  14.558  1.00 105.61 ?  344 MET C C   1 
ATOM   5634 O O   . MET C 1 189 ? -32.668 8.615  15.225  1.00 104.68 ?  344 MET C O   1 
ATOM   5635 C CB  . MET C 1 189 ? -34.300 9.513  12.499  1.00 108.26 ?  344 MET C CB  1 
ATOM   5636 C CG  . MET C 1 189 ? -34.477 10.178 11.153  1.00 112.33 ?  344 MET C CG  1 
ATOM   5637 S SD  . MET C 1 189 ? -34.584 11.997 11.156  1.00 116.62 ?  344 MET C SD  1 
ATOM   5638 C CE  . MET C 1 189 ? -35.820 12.294 12.430  1.00 112.94 ?  344 MET C CE  1 
HETATM 5639 N N   . TPO C 1 190 ? -33.214 10.807 15.108  1.00 100.28 ?  345 TPO C N   1 
HETATM 5640 C CA  . TPO C 1 190 ? -33.287 11.006 16.555  1.00 99.39  ?  345 TPO C CA  1 
HETATM 5641 C CB  . TPO C 1 190 ? -31.895 11.374 17.170  1.00 99.87  ?  345 TPO C CB  1 
HETATM 5642 C CG2 . TPO C 1 190 ? -31.394 12.713 16.601  1.00 99.25  ?  345 TPO C CG2 1 
HETATM 5643 O OG1 . TPO C 1 190 ? -31.864 11.497 18.630  1.00 101.08 ?  345 TPO C OG1 1 
HETATM 5644 P P   . TPO C 1 190 ? -31.796 10.182 19.473  1.00 101.27 ?  345 TPO C P   1 
HETATM 5645 O O1P . TPO C 1 190 ? -31.068 9.061  18.697  1.00 100.96 ?  345 TPO C O1P 1 
HETATM 5646 O O2P . TPO C 1 190 ? -33.209 9.718  19.863  1.00 101.06 -1 345 TPO C O2P 1 
HETATM 5647 O O3P . TPO C 1 190 ? -31.067 10.531 20.779  1.00 101.46 -1 345 TPO C O3P 1 
HETATM 5648 C C   . TPO C 1 190 ? -34.358 12.027 16.959  1.00 100.50 ?  345 TPO C C   1 
HETATM 5649 O O   . TPO C 1 190 ? -34.679 12.930 16.187  1.00 98.56  ?  345 TPO C O   1 
HETATM 5650 N N   . SEP C 1 191 ? -34.906 11.875 18.182  1.00 96.88  ?  346 SEP C N   1 
HETATM 5651 C CA  . SEP C 1 191 ? -35.910 12.779 18.747  1.00 96.28  ?  346 SEP C CA  1 
HETATM 5652 C CB  . SEP C 1 191 ? -37.069 12.109 19.511  1.00 96.21  ?  346 SEP C CB  1 
HETATM 5653 C C   . SEP C 1 191 ? -35.257 13.912 19.551  1.00 99.20  ?  346 SEP C C   1 
HETATM 5654 O O   . SEP C 1 191 ? -35.922 14.909 19.838  1.00 99.38  ?  346 SEP C O   1 
ATOM   5655 N N   . ARG C 1 192 ? -33.964 13.753 19.917  1.00 94.21  ?  347 ARG C N   1 
ATOM   5656 C CA  . ARG C 1 192 ? -33.182 14.755 20.641  1.00 93.51  ?  347 ARG C CA  1 
ATOM   5657 C C   . ARG C 1 192 ? -32.080 15.316 19.725  1.00 95.90  ?  347 ARG C C   1 
ATOM   5658 O O   . ARG C 1 192 ? -31.073 14.635 19.469  1.00 94.97  ?  347 ARG C O   1 
ATOM   5659 C CB  . ARG C 1 192 ? -32.620 14.196 21.975  1.00 93.38  ?  347 ARG C CB  1 
ATOM   5660 C CG  . ARG C 1 192 ? -31.786 15.189 22.817  1.00 103.88 ?  347 ARG C CG  1 
ATOM   5661 C CD  . ARG C 1 192 ? -32.603 16.333 23.424  1.00 115.88 ?  347 ARG C CD  1 
ATOM   5662 N NE  . ARG C 1 192 ? -32.523 17.574 22.640  1.00 125.74 ?  347 ARG C NE  1 
ATOM   5663 C CZ  . ARG C 1 192 ? -31.921 18.690 23.049  1.00 139.72 ?  347 ARG C CZ  1 
ATOM   5664 N NH1 . ARG C 1 192 ? -31.342 18.744 24.243  1.00 129.44 ?  347 ARG C NH1 1 
ATOM   5665 N NH2 . ARG C 1 192 ? -31.903 19.763 22.272  1.00 121.76 1  347 ARG C NH2 1 
ATOM   5666 N N   . ILE C 1 193 ? -32.307 16.550 19.205  1.00 91.26  ?  348 ILE C N   1 
ATOM   5667 C CA  . ILE C 1 193 ? -31.378 17.266 18.318  1.00 90.23  ?  348 ILE C CA  1 
ATOM   5668 C C   . ILE C 1 193 ? -30.304 17.948 19.172  1.00 92.30  ?  348 ILE C C   1 
ATOM   5669 O O   . ILE C 1 193 ? -30.624 18.761 20.038  1.00 91.85  ?  348 ILE C O   1 
ATOM   5670 C CB  . ILE C 1 193 ? -32.118 18.205 17.309  1.00 92.98  ?  348 ILE C CB  1 
ATOM   5671 C CG1 . ILE C 1 193 ? -33.022 17.371 16.362  1.00 93.56  ?  348 ILE C CG1 1 
ATOM   5672 C CG2 . ILE C 1 193 ? -31.127 19.057 16.491  1.00 92.82  ?  348 ILE C CG2 1 
ATOM   5673 C CD1 . ILE C 1 193 ? -34.177 18.109 15.727  1.00 102.11 ?  348 ILE C CD1 1 
ATOM   5674 N N   . VAL C 1 194 ? -29.034 17.561 18.958  1.00 87.59  ?  349 VAL C N   1 
ATOM   5675 C CA  . VAL C 1 194 ? -27.877 18.049 19.722  1.00 86.61  ?  349 VAL C CA  1 
ATOM   5676 C C   . VAL C 1 194 ? -26.668 18.445 18.851  1.00 86.94  ?  349 VAL C C   1 
ATOM   5677 O O   . VAL C 1 194 ? -26.401 17.825 17.812  1.00 86.20  ?  349 VAL C O   1 
ATOM   5678 C CB  . VAL C 1 194 ? -27.472 17.079 20.869  1.00 91.25  ?  349 VAL C CB  1 
ATOM   5679 C CG1 . VAL C 1 194 ? -28.371 17.255 22.096  1.00 91.11  ?  349 VAL C CG1 1 
ATOM   5680 C CG2 . VAL C 1 194 ? -27.450 15.620 20.395  1.00 91.07  ?  349 VAL C CG2 1 
ATOM   5681 N N   . GLY C 1 195 ? -25.935 19.448 19.334  1.00 80.87  ?  350 GLY C N   1 
ATOM   5682 C CA  . GLY C 1 195 ? -24.769 20.040 18.688  1.00 79.12  ?  350 GLY C CA  1 
ATOM   5683 C C   . GLY C 1 195 ? -24.814 21.559 18.759  1.00 79.23  ?  350 GLY C C   1 
ATOM   5684 O O   . GLY C 1 195 ? -25.658 22.127 19.463  1.00 77.77  ?  350 GLY C O   1 
ATOM   5685 N N   . THR C 1 196 ? -23.897 22.230 18.041  1.00 73.65  ?  351 THR C N   1 
ATOM   5686 C CA  . THR C 1 196 ? -23.837 23.696 17.993  1.00 71.59  ?  351 THR C CA  1 
ATOM   5687 C C   . THR C 1 196 ? -24.342 24.132 16.629  1.00 71.26  ?  351 THR C C   1 
ATOM   5688 O O   . THR C 1 196 ? -23.650 23.924 15.629  1.00 71.34  ?  351 THR C O   1 
ATOM   5689 C CB  . THR C 1 196 ? -22.440 24.192 18.371  1.00 77.90  ?  351 THR C CB  1 
ATOM   5690 O OG1 . THR C 1 196 ? -22.076 23.592 19.621  1.00 76.06  ?  351 THR C OG1 1 
ATOM   5691 C CG2 . THR C 1 196 ? -22.364 25.723 18.473  1.00 76.72  ?  351 THR C CG2 1 
ATOM   5692 N N   . THR C 1 197 ? -25.575 24.694 16.594  1.00 63.31  ?  352 THR C N   1 
ATOM   5693 C CA  . THR C 1 197 ? -26.293 25.111 15.383  1.00 61.16  ?  352 THR C CA  1 
ATOM   5694 C C   . THR C 1 197 ? -25.451 25.812 14.328  1.00 60.09  ?  352 THR C C   1 
ATOM   5695 O O   . THR C 1 197 ? -25.618 25.533 13.149  1.00 58.08  ?  352 THR C O   1 
ATOM   5696 C CB  . THR C 1 197 ? -27.582 25.870 15.702  1.00 74.07  ?  352 THR C CB  1 
ATOM   5697 O OG1 . THR C 1 197 ? -27.262 27.126 16.282  1.00 80.51  ?  352 THR C OG1 1 
ATOM   5698 C CG2 . THR C 1 197 ? -28.512 25.095 16.622  1.00 74.60  ?  352 THR C CG2 1 
ATOM   5699 N N   . ALA C 1 198 ? -24.514 26.678 14.748  1.00 55.87  ?  353 ALA C N   1 
ATOM   5700 C CA  . ALA C 1 198 ? -23.629 27.428 13.847  1.00 54.51  ?  353 ALA C CA  1 
ATOM   5701 C C   . ALA C 1 198 ? -22.690 26.549 13.004  1.00 55.73  ?  353 ALA C C   1 
ATOM   5702 O O   . ALA C 1 198 ? -22.203 26.997 11.961  1.00 56.12  ?  353 ALA C O   1 
ATOM   5703 C CB  . ALA C 1 198 ? -22.822 28.429 14.639  1.00 55.09  ?  353 ALA C CB  1 
ATOM   5704 N N   . TYR C 1 199 ? -22.450 25.310 13.443  1.00 48.99  ?  354 TYR C N   1 
ATOM   5705 C CA  . TYR C 1 199 ? -21.573 24.374 12.753  1.00 48.94  ?  354 TYR C CA  1 
ATOM   5706 C C   . TYR C 1 199 ? -22.345 23.221 12.114  1.00 50.67  ?  354 TYR C C   1 
ATOM   5707 O O   . TYR C 1 199 ? -21.813 22.557 11.229  1.00 50.31  ?  354 TYR C O   1 
ATOM   5708 C CB  . TYR C 1 199 ? -20.551 23.776 13.750  1.00 50.65  ?  354 TYR C CB  1 
ATOM   5709 C CG  . TYR C 1 199 ? -19.639 24.776 14.416  1.00 52.36  ?  354 TYR C CG  1 
ATOM   5710 C CD1 . TYR C 1 199 ? -20.038 25.460 15.561  1.00 54.02  ?  354 TYR C CD1 1 
ATOM   5711 C CD2 . TYR C 1 199 ? -18.354 25.000 13.937  1.00 53.78  ?  354 TYR C CD2 1 
ATOM   5712 C CE1 . TYR C 1 199 ? -19.203 26.384 16.180  1.00 54.55  ?  354 TYR C CE1 1 
ATOM   5713 C CE2 . TYR C 1 199 ? -17.501 25.913 14.555  1.00 54.80  ?  354 TYR C CE2 1 
ATOM   5714 C CZ  . TYR C 1 199 ? -17.926 26.598 15.684  1.00 61.70  ?  354 TYR C CZ  1 
ATOM   5715 O OH  . TYR C 1 199 ? -17.105 27.514 16.303  1.00 61.00  ?  354 TYR C OH  1 
ATOM   5716 N N   . MET C 1 200 ? -23.562 22.957 12.599  1.00 46.35  ?  355 MET C N   1 
ATOM   5717 C CA  . MET C 1 200 ? -24.388 21.832 12.197  1.00 46.46  ?  355 MET C CA  1 
ATOM   5718 C C   . MET C 1 200 ? -24.852 21.837 10.757  1.00 51.22  ?  355 MET C C   1 
ATOM   5719 O O   . MET C 1 200 ? -25.315 22.861 10.252  1.00 50.83  ?  355 MET C O   1 
ATOM   5720 C CB  . MET C 1 200 ? -25.583 21.673 13.136  1.00 48.78  ?  355 MET C CB  1 
ATOM   5721 C CG  . MET C 1 200 ? -25.184 21.206 14.494  1.00 52.43  ?  355 MET C CG  1 
ATOM   5722 S SD  . MET C 1 200 ? -26.568 21.142 15.634  1.00 57.54  ?  355 MET C SD  1 
ATOM   5723 C CE  . MET C 1 200 ? -27.369 19.611 15.091  1.00 53.92  ?  355 MET C CE  1 
ATOM   5724 N N   . ALA C 1 201 ? -24.770 20.654 10.116  1.00 46.60  ?  356 ALA C N   1 
ATOM   5725 C CA  . ALA C 1 201 ? -25.233 20.417 8.757   1.00 45.93  ?  356 ALA C CA  1 
ATOM   5726 C C   . ALA C 1 201 ? -26.770 20.540 8.734   1.00 49.80  ?  356 ALA C C   1 
ATOM   5727 O O   . ALA C 1 201 ? -27.401 20.277 9.760   1.00 50.32  ?  356 ALA C O   1 
ATOM   5728 C CB  . ALA C 1 201 ? -24.802 19.034 8.304   1.00 46.51  ?  356 ALA C CB  1 
ATOM   5729 N N   . PRO C 1 202 ? -27.394 20.987 7.617   1.00 45.69  ?  357 PRO C N   1 
ATOM   5730 C CA  . PRO C 1 202 ? -28.863 21.152 7.622   1.00 45.29  ?  357 PRO C CA  1 
ATOM   5731 C C   . PRO C 1 202 ? -29.644 19.915 8.082   1.00 49.33  ?  357 PRO C C   1 
ATOM   5732 O O   . PRO C 1 202 ? -30.525 20.048 8.935   1.00 48.82  ?  357 PRO C O   1 
ATOM   5733 C CB  . PRO C 1 202 ? -29.186 21.581 6.185   1.00 46.66  ?  357 PRO C CB  1 
ATOM   5734 C CG  . PRO C 1 202 ? -27.955 21.251 5.383   1.00 51.42  ?  357 PRO C CG  1 
ATOM   5735 C CD  . PRO C 1 202 ? -26.815 21.408 6.324   1.00 47.09  ?  357 PRO C CD  1 
ATOM   5736 N N   . GLU C 1 203 ? -29.267 18.712 7.589   1.00 44.51  ?  358 GLU C N   1 
ATOM   5737 C CA  . GLU C 1 203 ? -29.916 17.442 7.955   1.00 42.77  ?  358 GLU C CA  1 
ATOM   5738 C C   . GLU C 1 203 ? -29.749 17.122 9.439   1.00 46.13  ?  358 GLU C C   1 
ATOM   5739 O O   . GLU C 1 203 ? -30.639 16.512 10.026  1.00 46.79  ?  358 GLU C O   1 
ATOM   5740 C CB  . GLU C 1 203 ? -29.426 16.272 7.072   1.00 43.28  ?  358 GLU C CB  1 
ATOM   5741 C CG  . GLU C 1 203 ? -27.980 15.817 7.295   1.00 49.11  ?  358 GLU C CG  1 
ATOM   5742 C CD  . GLU C 1 203 ? -26.875 16.622 6.628   1.00 63.47  ?  358 GLU C CD  1 
ATOM   5743 O OE1 . GLU C 1 203 ? -27.162 17.700 6.050   1.00 67.13  ?  358 GLU C OE1 1 
ATOM   5744 O OE2 . GLU C 1 203 ? -25.709 16.173 6.701   1.00 41.34  -1 358 GLU C OE2 1 
ATOM   5745 N N   . ALA C 1 204 ? -28.616 17.529 10.040  1.00 40.78  ?  359 ALA C N   1 
ATOM   5746 C CA  . ALA C 1 204 ? -28.352 17.296 11.456  1.00 40.83  ?  359 ALA C CA  1 
ATOM   5747 C C   . ALA C 1 204 ? -29.330 18.137 12.287  1.00 44.78  ?  359 ALA C C   1 
ATOM   5748 O O   . ALA C 1 204 ? -29.848 17.656 13.298  1.00 44.73  ?  359 ALA C O   1 
ATOM   5749 C CB  . ALA C 1 204 ? -26.909 17.649 11.797  1.00 41.16  ?  359 ALA C CB  1 
ATOM   5750 N N   . LEU C 1 205 ? -29.624 19.359 11.814  1.00 40.37  ?  360 LEU C N   1 
ATOM   5751 C CA  . LEU C 1 205 ? -30.569 20.266 12.463  1.00 40.40  ?  360 LEU C CA  1 
ATOM   5752 C C   . LEU C 1 205 ? -32.011 19.715 12.337  1.00 48.07  ?  360 LEU C C   1 
ATOM   5753 O O   . LEU C 1 205 ? -32.865 20.029 13.165  1.00 48.87  ?  360 LEU C O   1 
ATOM   5754 C CB  . LEU C 1 205 ? -30.478 21.674 11.846  1.00 39.69  ?  360 LEU C CB  1 
ATOM   5755 C CG  . LEU C 1 205 ? -29.226 22.492 12.159  1.00 43.43  ?  360 LEU C CG  1 
ATOM   5756 C CD1 . LEU C 1 205 ? -29.093 23.647 11.218  1.00 43.72  ?  360 LEU C CD1 1 
ATOM   5757 C CD2 . LEU C 1 205 ? -29.222 22.996 13.585  1.00 42.76  ?  360 LEU C CD2 1 
ATOM   5758 N N   . ARG C 1 206 ? -32.250 18.900 11.267  1.00 44.35  ?  361 ARG C N   1 
ATOM   5759 C CA  . ARG C 1 206 ? -33.485 18.220 10.878  1.00 43.61  ?  361 ARG C CA  1 
ATOM   5760 C C   . ARG C 1 206 ? -33.585 16.828 11.505  1.00 49.64  ?  361 ARG C C   1 
ATOM   5761 O O   . ARG C 1 206 ? -34.570 16.113 11.274  1.00 50.83  ?  361 ARG C O   1 
ATOM   5762 C CB  . ARG C 1 206 ? -33.597 18.120 9.340   1.00 41.35  ?  361 ARG C CB  1 
ATOM   5763 C CG  . ARG C 1 206 ? -33.792 19.471 8.632   1.00 48.07  ?  361 ARG C CG  1 
ATOM   5764 C CD  . ARG C 1 206 ? -34.389 19.290 7.267   1.00 43.32  ?  361 ARG C CD  1 
ATOM   5765 N NE  . ARG C 1 206 ? -33.636 19.938 6.192   1.00 47.63  ?  361 ARG C NE  1 
ATOM   5766 C CZ  . ARG C 1 206 ? -33.944 21.124 5.662   1.00 64.96  ?  361 ARG C CZ  1 
ATOM   5767 N NH1 . ARG C 1 206 ? -34.926 21.852 6.174   1.00 41.79  ?  361 ARG C NH1 1 
ATOM   5768 N NH2 . ARG C 1 206 ? -33.238 21.612 4.647   1.00 56.03  1  361 ARG C NH2 1 
ATOM   5769 N N   . GLY C 1 207 ? -32.561 16.452 12.271  1.00 46.05  ?  362 GLY C N   1 
ATOM   5770 C CA  . GLY C 1 207 ? -32.532 15.194 13.011  1.00 45.81  ?  362 GLY C CA  1 
ATOM   5771 C C   . GLY C 1 207 ? -31.885 13.967 12.409  1.00 48.91  ?  362 GLY C C   1 
ATOM   5772 O O   . GLY C 1 207 ? -32.052 12.889 12.969  1.00 46.65  ?  362 GLY C O   1 
ATOM   5773 N N   . GLU C 1 208 ? -31.132 14.087 11.315  1.00 48.89  ?  363 GLU C N   1 
ATOM   5774 C CA  . GLU C 1 208 ? -30.431 12.927 10.739  1.00 50.86  ?  363 GLU C CA  1 
ATOM   5775 C C   . GLU C 1 208 ? -29.051 12.732 11.376  1.00 60.44  ?  363 GLU C C   1 
ATOM   5776 O O   . GLU C 1 208 ? -28.347 13.713 11.607  1.00 62.94  ?  363 GLU C O   1 
ATOM   5777 C CB  . GLU C 1 208 ? -30.249 13.067 9.224   1.00 52.12  ?  363 GLU C CB  1 
ATOM   5778 C CG  . GLU C 1 208 ? -31.533 13.004 8.418   1.00 58.29  ?  363 GLU C CG  1 
ATOM   5779 C CD  . GLU C 1 208 ? -31.316 13.014 6.918   1.00 79.48  ?  363 GLU C CD  1 
ATOM   5780 O OE1 . GLU C 1 208 ? -32.173 13.578 6.202   1.00 83.15  ?  363 GLU C OE1 1 
ATOM   5781 O OE2 . GLU C 1 208 ? -30.291 12.463 6.452   1.00 76.02  -1 363 GLU C OE2 1 
ATOM   5782 N N   . ILE C 1 209 ? -28.647 11.470 11.617  1.00 58.18  ?  364 ILE C N   1 
ATOM   5783 C CA  . ILE C 1 209 ? -27.334 11.090 12.172  1.00 58.14  ?  364 ILE C CA  1 
ATOM   5784 C C   . ILE C 1 209 ? -26.519 10.399 11.051  1.00 60.36  ?  364 ILE C C   1 
ATOM   5785 O O   . ILE C 1 209 ? -26.851 9.294  10.623  1.00 60.34  ?  364 ILE C O   1 
ATOM   5786 C CB  . ILE C 1 209 ? -27.486 10.257 13.505  1.00 61.09  ?  364 ILE C CB  1 
ATOM   5787 C CG1 . ILE C 1 209 ? -28.046 11.167 14.646  1.00 60.96  ?  364 ILE C CG1 1 
ATOM   5788 C CG2 . ILE C 1 209 ? -26.155 9.582  13.943  1.00 60.37  ?  364 ILE C CG2 1 
ATOM   5789 C CD1 . ILE C 1 209 ? -28.711 10.476 15.788  1.00 57.47  ?  364 ILE C CD1 1 
ATOM   5790 N N   . THR C 1 210 ? -25.494 11.095 10.540  1.00 55.25  ?  365 THR C N   1 
ATOM   5791 C CA  . THR C 1 210 ? -24.654 10.599 9.451   1.00 54.36  ?  365 THR C CA  1 
ATOM   5792 C C   . THR C 1 210 ? -23.210 11.104 9.571   1.00 57.28  ?  365 THR C C   1 
ATOM   5793 O O   . THR C 1 210 ? -23.003 12.266 9.929   1.00 56.82  ?  365 THR C O   1 
ATOM   5794 C CB  . THR C 1 210 ? -25.296 10.903 8.073   1.00 66.13  ?  365 THR C CB  1 
ATOM   5795 O OG1 . THR C 1 210 ? -24.343 10.640 7.041   1.00 71.68  ?  365 THR C OG1 1 
ATOM   5796 C CG2 . THR C 1 210 ? -25.815 12.351 7.942   1.00 63.24  ?  365 THR C CG2 1 
ATOM   5797 N N   . PRO C 1 211 ? -22.192 10.276 9.226   1.00 53.04  ?  366 PRO C N   1 
ATOM   5798 C CA  . PRO C 1 211 ? -20.802 10.761 9.286   1.00 51.45  ?  366 PRO C CA  1 
ATOM   5799 C C   . PRO C 1 211 ? -20.553 11.956 8.357   1.00 52.23  ?  366 PRO C C   1 
ATOM   5800 O O   . PRO C 1 211 ? -19.630 12.729 8.599   1.00 52.77  ?  366 PRO C O   1 
ATOM   5801 C CB  . PRO C 1 211 ? -19.995 9.531  8.854   1.00 52.91  ?  366 PRO C CB  1 
ATOM   5802 C CG  . PRO C 1 211 ? -20.930 8.726  8.050   1.00 57.83  ?  366 PRO C CG  1 
ATOM   5803 C CD  . PRO C 1 211 ? -22.230 8.875  8.760   1.00 54.21  ?  366 PRO C CD  1 
ATOM   5804 N N   . LYS C 1 212 ? -21.397 12.120 7.312   1.00 44.90  ?  367 LYS C N   1 
ATOM   5805 C CA  . LYS C 1 212 ? -21.316 13.216 6.349   1.00 42.80  ?  367 LYS C CA  1 
ATOM   5806 C C   . LYS C 1 212 ? -21.606 14.569 7.022   1.00 46.63  ?  367 LYS C C   1 
ATOM   5807 O O   . LYS C 1 212 ? -21.187 15.603 6.507   1.00 46.60  ?  367 LYS C O   1 
ATOM   5808 C CB  . LYS C 1 212 ? -22.252 12.956 5.154   1.00 43.80  ?  367 LYS C CB  1 
ATOM   5809 N N   . SER C 1 213 ? -22.293 14.562 8.191   1.00 43.41  ?  368 SER C N   1 
ATOM   5810 C CA  . SER C 1 213 ? -22.594 15.774 8.957   1.00 43.04  ?  368 SER C CA  1 
ATOM   5811 C C   . SER C 1 213 ? -21.299 16.344 9.582   1.00 47.63  ?  368 SER C C   1 
ATOM   5812 O O   . SER C 1 213 ? -21.112 17.564 9.618   1.00 49.85  ?  368 SER C O   1 
ATOM   5813 C CB  . SER C 1 213 ? -23.643 15.482 10.021  1.00 46.54  ?  368 SER C CB  1 
ATOM   5814 O OG  . SER C 1 213 ? -24.918 15.208 9.456   1.00 59.29  ?  368 SER C OG  1 
ATOM   5815 N N   . ASP C 1 214 ? -20.392 15.451 10.020  1.00 41.22  ?  369 ASP C N   1 
ATOM   5816 C CA  . ASP C 1 214 ? -19.090 15.773 10.586  1.00 40.38  ?  369 ASP C CA  1 
ATOM   5817 C C   . ASP C 1 214 ? -18.230 16.518 9.558   1.00 43.31  ?  369 ASP C C   1 
ATOM   5818 O O   . ASP C 1 214 ? -17.522 17.452 9.925   1.00 42.36  ?  369 ASP C O   1 
ATOM   5819 C CB  . ASP C 1 214 ? -18.377 14.482 11.072  1.00 42.33  ?  369 ASP C CB  1 
ATOM   5820 C CG  . ASP C 1 214 ? -18.774 13.947 12.455  1.00 54.00  ?  369 ASP C CG  1 
ATOM   5821 O OD1 . ASP C 1 214 ? -19.682 14.543 13.102  1.00 52.63  ?  369 ASP C OD1 1 
ATOM   5822 O OD2 . ASP C 1 214 ? -18.157 12.954 12.903  1.00 63.77  -1 369 ASP C OD2 1 
ATOM   5823 N N   . ILE C 1 215 ? -18.324 16.124 8.266   1.00 39.72  ?  370 ILE C N   1 
ATOM   5824 C CA  . ILE C 1 215 ? -17.623 16.755 7.138   1.00 38.41  ?  370 ILE C CA  1 
ATOM   5825 C C   . ILE C 1 215 ? -18.086 18.214 6.974   1.00 39.02  ?  370 ILE C C   1 
ATOM   5826 O O   . ILE C 1 215 ? -17.265 19.108 6.768   1.00 37.69  ?  370 ILE C O   1 
ATOM   5827 C CB  . ILE C 1 215 ? -17.819 15.923 5.833   1.00 41.65  ?  370 ILE C CB  1 
ATOM   5828 C CG1 . ILE C 1 215 ? -17.343 14.475 5.994   1.00 42.49  ?  370 ILE C CG1 1 
ATOM   5829 C CG2 . ILE C 1 215 ? -17.218 16.602 4.571   1.00 41.83  ?  370 ILE C CG2 1 
ATOM   5830 C CD1 . ILE C 1 215 ? -15.894 14.285 6.068   1.00 51.14  ?  370 ILE C CD1 1 
ATOM   5831 N N   . TYR C 1 216 ? -19.394 18.447 7.085   1.00 36.13  ?  371 TYR C N   1 
ATOM   5832 C CA  . TYR C 1 216 ? -19.967 19.792 6.975   1.00 36.35  ?  371 TYR C CA  1 
ATOM   5833 C C   . TYR C 1 216 ? -19.447 20.693 8.112   1.00 42.48  ?  371 TYR C C   1 
ATOM   5834 O O   . TYR C 1 216 ? -18.993 21.801 7.840   1.00 42.78  ?  371 TYR C O   1 
ATOM   5835 C CB  . TYR C 1 216 ? -21.497 19.723 6.967   1.00 36.57  ?  371 TYR C CB  1 
ATOM   5836 C CG  . TYR C 1 216 ? -22.172 21.052 6.691   1.00 36.88  ?  371 TYR C CG  1 
ATOM   5837 C CD1 . TYR C 1 216 ? -22.426 21.961 7.727   1.00 37.28  ?  371 TYR C CD1 1 
ATOM   5838 C CD2 . TYR C 1 216 ? -22.579 21.397 5.397   1.00 36.48  ?  371 TYR C CD2 1 
ATOM   5839 C CE1 . TYR C 1 216 ? -23.037 23.187 7.479   1.00 35.78  ?  371 TYR C CE1 1 
ATOM   5840 C CE2 . TYR C 1 216 ? -23.213 22.612 5.143   1.00 37.05  ?  371 TYR C CE2 1 
ATOM   5841 C CZ  . TYR C 1 216 ? -23.432 23.507 6.187   1.00 46.75  ?  371 TYR C CZ  1 
ATOM   5842 O OH  . TYR C 1 216 ? -24.034 24.713 5.944   1.00 50.32  ?  371 TYR C OH  1 
ATOM   5843 N N   . SER C 1 217 ? -19.469 20.195 9.364   1.00 39.08  ?  372 SER C N   1 
ATOM   5844 C CA  . SER C 1 217 ? -18.987 20.900 10.541  1.00 39.11  ?  372 SER C CA  1 
ATOM   5845 C C   . SER C 1 217 ? -17.514 21.280 10.436  1.00 43.68  ?  372 SER C C   1 
ATOM   5846 O O   . SER C 1 217 ? -17.121 22.393 10.822  1.00 44.21  ?  372 SER C O   1 
ATOM   5847 C CB  . SER C 1 217 ? -19.229 20.062 11.781  1.00 44.29  ?  372 SER C CB  1 
ATOM   5848 O OG  . SER C 1 217 ? -20.611 20.049 12.075  1.00 55.43  ?  372 SER C OG  1 
ATOM   5849 N N   . PHE C 1 218 ? -16.712 20.378 9.868   1.00 40.25  ?  373 PHE C N   1 
ATOM   5850 C CA  . PHE C 1 218 ? -15.284 20.605 9.620   1.00 39.74  ?  373 PHE C CA  1 
ATOM   5851 C C   . PHE C 1 218 ? -15.057 21.713 8.598   1.00 41.97  ?  373 PHE C C   1 
ATOM   5852 O O   . PHE C 1 218 ? -14.085 22.457 8.731   1.00 41.93  ?  373 PHE C O   1 
ATOM   5853 C CB  . PHE C 1 218 ? -14.601 19.323 9.173   1.00 41.60  ?  373 PHE C CB  1 
ATOM   5854 C CG  . PHE C 1 218 ? -13.100 19.462 9.097   1.00 43.53  ?  373 PHE C CG  1 
ATOM   5855 C CD1 . PHE C 1 218 ? -12.349 19.750 10.239  1.00 45.99  ?  373 PHE C CD1 1 
ATOM   5856 C CD2 . PHE C 1 218 ? -12.437 19.334 7.882   1.00 45.69  ?  373 PHE C CD2 1 
ATOM   5857 C CE1 . PHE C 1 218 ? -10.967 19.892 10.162  1.00 47.08  ?  373 PHE C CE1 1 
ATOM   5858 C CE2 . PHE C 1 218 ? -11.051 19.465 7.808   1.00 48.44  ?  373 PHE C CE2 1 
ATOM   5859 C CZ  . PHE C 1 218 ? -10.323 19.729 8.948   1.00 46.83  ?  373 PHE C CZ  1 
ATOM   5860 N N   . GLY C 1 219 ? -15.966 21.827 7.622   1.00 36.42  ?  374 GLY C N   1 
ATOM   5861 C CA  . GLY C 1 219 ? -15.955 22.885 6.624   1.00 35.26  ?  374 GLY C CA  1 
ATOM   5862 C C   . GLY C 1 219 ? -16.129 24.251 7.262   1.00 38.95  ?  374 GLY C C   1 
ATOM   5863 O O   . GLY C 1 219 ? -15.468 25.216 6.855   1.00 40.40  ?  374 GLY C O   1 
ATOM   5864 N N   . VAL C 1 220 ? -16.964 24.339 8.310   1.00 34.14  ?  375 VAL C N   1 
ATOM   5865 C CA  . VAL C 1 220 ? -17.201 25.593 9.053   1.00 34.96  ?  375 VAL C CA  1 
ATOM   5866 C C   . VAL C 1 220 ? -15.918 25.962 9.817   1.00 40.46  ?  375 VAL C C   1 
ATOM   5867 O O   . VAL C 1 220 ? -15.536 27.130 9.889   1.00 40.41  ?  375 VAL C O   1 
ATOM   5868 C CB  . VAL C 1 220 ? -18.445 25.487 9.993   1.00 39.32  ?  375 VAL C CB  1 
ATOM   5869 C CG1 . VAL C 1 220 ? -18.668 26.767 10.776  1.00 39.03  ?  375 VAL C CG1 1 
ATOM   5870 C CG2 . VAL C 1 220 ? -19.711 25.132 9.216   1.00 38.72  ?  375 VAL C CG2 1 
ATOM   5871 N N   . VAL C 1 221 ? -15.234 24.936 10.339  1.00 37.65  ?  376 VAL C N   1 
ATOM   5872 C CA  . VAL C 1 221 ? -13.984 25.083 11.068  1.00 36.99  ?  376 VAL C CA  1 
ATOM   5873 C C   . VAL C 1 221 ? -12.916 25.613 10.128  1.00 40.55  ?  376 VAL C C   1 
ATOM   5874 O O   . VAL C 1 221 ? -12.209 26.553 10.498  1.00 40.90  ?  376 VAL C O   1 
ATOM   5875 C CB  . VAL C 1 221 ? -13.581 23.770 11.788  1.00 41.06  ?  376 VAL C CB  1 
ATOM   5876 C CG1 . VAL C 1 221 ? -12.173 23.870 12.355  1.00 41.07  ?  376 VAL C CG1 1 
ATOM   5877 C CG2 . VAL C 1 221 ? -14.574 23.423 12.899  1.00 40.94  ?  376 VAL C CG2 1 
ATOM   5878 N N   . LEU C 1 222 ? -12.835 25.066 8.895   1.00 36.34  ?  377 LEU C N   1 
ATOM   5879 C CA  . LEU C 1 222 ? -11.865 25.540 7.903   1.00 35.58  ?  377 LEU C CA  1 
ATOM   5880 C C   . LEU C 1 222 ? -12.108 27.010 7.557   1.00 38.96  ?  377 LEU C C   1 
ATOM   5881 O O   . LEU C 1 222 ? -11.146 27.772 7.449   1.00 39.58  ?  377 LEU C O   1 
ATOM   5882 C CB  . LEU C 1 222 ? -11.835 24.664 6.641   1.00 35.54  ?  377 LEU C CB  1 
ATOM   5883 C CG  . LEU C 1 222 ? -11.349 23.213 6.830   1.00 39.65  ?  377 LEU C CG  1 
ATOM   5884 C CD1 . LEU C 1 222 ? -11.513 22.429 5.554   1.00 39.33  ?  377 LEU C CD1 1 
ATOM   5885 C CD2 . LEU C 1 222 ? -9.888  23.140 7.313   1.00 38.95  ?  377 LEU C CD2 1 
ATOM   5886 N N   . LEU C 1 223 ? -13.378 27.439 7.492   1.00 33.48  ?  378 LEU C N   1 
ATOM   5887 C CA  . LEU C 1 223 ? -13.674 28.850 7.280   1.00 32.44  ?  378 LEU C CA  1 
ATOM   5888 C C   . LEU C 1 223 ? -13.205 29.693 8.476   1.00 36.18  ?  378 LEU C C   1 
ATOM   5889 O O   . LEU C 1 223 ? -12.691 30.788 8.268   1.00 36.00  ?  378 LEU C O   1 
ATOM   5890 C CB  . LEU C 1 223 ? -15.163 29.083 7.026   1.00 32.46  ?  378 LEU C CB  1 
ATOM   5891 C CG  . LEU C 1 223 ? -15.779 28.591 5.711   1.00 36.22  ?  378 LEU C CG  1 
ATOM   5892 C CD1 . LEU C 1 223 ? -17.233 29.106 5.584   1.00 34.81  ?  378 LEU C CD1 1 
ATOM   5893 C CD2 . LEU C 1 223 ? -14.945 29.027 4.457   1.00 34.61  ?  378 LEU C CD2 1 
ATOM   5894 N N   . GLU C 1 224 ? -13.348 29.172 9.722   1.00 33.19  ?  379 GLU C N   1 
ATOM   5895 C CA  . GLU C 1 224 ? -12.875 29.861 10.928  1.00 33.54  ?  379 GLU C CA  1 
ATOM   5896 C C   . GLU C 1 224 ? -11.370 29.990 10.837  1.00 39.77  ?  379 GLU C C   1 
ATOM   5897 O O   . GLU C 1 224 ? -10.821 31.057 11.126  1.00 40.52  ?  379 GLU C O   1 
ATOM   5898 C CB  . GLU C 1 224 ? -13.229 29.079 12.204  1.00 34.43  ?  379 GLU C CB  1 
ATOM   5899 C CG  . GLU C 1 224 ? -14.694 29.134 12.573  1.00 41.57  ?  379 GLU C CG  1 
ATOM   5900 C CD  . GLU C 1 224 ? -15.021 28.416 13.863  1.00 73.31  ?  379 GLU C CD  1 
ATOM   5901 O OE1 . GLU C 1 224 ? -14.676 27.218 13.973  1.00 76.53  ?  379 GLU C OE1 1 
ATOM   5902 O OE2 . GLU C 1 224 ? -15.630 29.047 14.760  1.00 70.08  -1 379 GLU C OE2 1 
ATOM   5903 N N   . ILE C 1 225 ? -10.698 28.912 10.406  1.00 36.96  ?  380 ILE C N   1 
ATOM   5904 C CA  . ILE C 1 225 ? -9.241  28.916 10.243  1.00 37.16  ?  380 ILE C CA  1 
ATOM   5905 C C   . ILE C 1 225 ? -8.761  29.997 9.234   1.00 39.95  ?  380 ILE C C   1 
ATOM   5906 O O   . ILE C 1 225 ? -7.823  30.753 9.551   1.00 38.77  ?  380 ILE C O   1 
ATOM   5907 C CB  . ILE C 1 225 ? -8.670  27.485 10.005  1.00 39.92  ?  380 ILE C CB  1 
ATOM   5908 C CG1 . ILE C 1 225 ? -8.813  26.611 11.291  1.00 39.39  ?  380 ILE C CG1 1 
ATOM   5909 C CG2 . ILE C 1 225 ? -7.213  27.550 9.568   1.00 40.92  ?  380 ILE C CG2 1 
ATOM   5910 C CD1 . ILE C 1 225 ? -8.476  25.089 11.128  1.00 40.02  ?  380 ILE C CD1 1 
ATOM   5911 N N   . ILE C 1 226 ? -9.451  30.125 8.077   1.00 34.67  ?  381 ILE C N   1 
ATOM   5912 C CA  . ILE C 1 226 ? -9.065  31.121 7.072   1.00 33.84  ?  381 ILE C CA  1 
ATOM   5913 C C   . ILE C 1 226 ? -9.305  32.576 7.553   1.00 37.11  ?  381 ILE C C   1 
ATOM   5914 O O   . ILE C 1 226 ? -8.465  33.454 7.355   1.00 37.34  ?  381 ILE C O   1 
ATOM   5915 C CB  . ILE C 1 226 ? -9.772  30.842 5.704   1.00 35.95  ?  381 ILE C CB  1 
ATOM   5916 C CG1 . ILE C 1 226 ? -9.377  29.484 5.104   1.00 35.51  ?  381 ILE C CG1 1 
ATOM   5917 C CG2 . ILE C 1 226 ? -9.509  31.962 4.707   1.00 35.49  ?  381 ILE C CG2 1 
ATOM   5918 C CD1 . ILE C 1 226 ? -10.488 28.794 4.196   1.00 31.89  ?  381 ILE C CD1 1 
ATOM   5919 N N   . THR C 1 227 ? -10.467 32.814 8.139   1.00 33.01  ?  382 THR C N   1 
ATOM   5920 C CA  . THR C 1 227 ? -10.934 34.134 8.532   1.00 33.79  ?  382 THR C CA  1 
ATOM   5921 C C   . THR C 1 227 ? -10.596 34.617 9.941   1.00 41.31  ?  382 THR C C   1 
ATOM   5922 O O   . THR C 1 227 ? -10.599 35.831 10.181  1.00 43.35  ?  382 THR C O   1 
ATOM   5923 C CB  . THR C 1 227 ? -12.449 34.238 8.297   1.00 31.93  ?  382 THR C CB  1 
ATOM   5924 O OG1 . THR C 1 227 ? -13.117 33.505 9.324   1.00 27.75  ?  382 THR C OG1 1 
ATOM   5925 C CG2 . THR C 1 227 ? -12.869 33.770 6.901   1.00 26.19  ?  382 THR C CG2 1 
ATOM   5926 N N   . GLY C 1 228 ? -10.406 33.691 10.867  1.00 38.08  ?  383 GLY C N   1 
ATOM   5927 C CA  . GLY C 1 228 ? -10.165 34.016 12.273  1.00 38.62  ?  383 GLY C CA  1 
ATOM   5928 C C   . GLY C 1 228 ? -11.419 34.475 12.993  1.00 43.33  ?  383 GLY C C   1 
ATOM   5929 O O   . GLY C 1 228 ? -11.352 34.948 14.132  1.00 42.72  ?  383 GLY C O   1 
ATOM   5930 N N   . LEU C 1 229 ? -12.574 34.323 12.322  1.00 41.37  ?  384 LEU C N   1 
ATOM   5931 C CA  . LEU C 1 229 ? -13.896 34.711 12.816  1.00 40.31  ?  384 LEU C CA  1 
ATOM   5932 C C   . LEU C 1 229 ? -14.616 33.511 13.404  1.00 47.00  ?  384 LEU C C   1 
ATOM   5933 O O   . LEU C 1 229 ? -14.560 32.426 12.795  1.00 47.11  ?  384 LEU C O   1 
ATOM   5934 C CB  . LEU C 1 229 ? -14.749 35.236 11.649  1.00 39.19  ?  384 LEU C CB  1 
ATOM   5935 C CG  . LEU C 1 229 ? -14.320 36.522 10.977  1.00 41.65  ?  384 LEU C CG  1 
ATOM   5936 C CD1 . LEU C 1 229 ? -14.974 36.653 9.609   1.00 42.18  ?  384 LEU C CD1 1 
ATOM   5937 C CD2 . LEU C 1 229 ? -14.612 37.721 11.850  1.00 38.38  ?  384 LEU C CD2 1 
ATOM   5938 N N   . PRO C 1 230 ? -15.361 33.688 14.537  1.00 44.10  ?  385 PRO C N   1 
ATOM   5939 C CA  . PRO C 1 230 ? -16.151 32.557 15.088  1.00 44.21  ?  385 PRO C CA  1 
ATOM   5940 C C   . PRO C 1 230 ? -17.331 32.231 14.162  1.00 48.83  ?  385 PRO C C   1 
ATOM   5941 O O   . PRO C 1 230 ? -17.762 33.115 13.437  1.00 48.30  ?  385 PRO C O   1 
ATOM   5942 C CB  . PRO C 1 230 ? -16.618 33.082 16.443  1.00 45.42  ?  385 PRO C CB  1 
ATOM   5943 C CG  . PRO C 1 230 ? -16.641 34.539 16.281  1.00 48.77  ?  385 PRO C CG  1 
ATOM   5944 C CD  . PRO C 1 230 ? -15.531 34.904 15.347  1.00 44.19  ?  385 PRO C CD  1 
ATOM   5945 N N   . ALA C 1 231 ? -17.819 30.968 14.147  1.00 47.83  ?  386 ALA C N   1 
ATOM   5946 C CA  . ALA C 1 231 ? -18.924 30.510 13.263  1.00 47.95  ?  386 ALA C CA  1 
ATOM   5947 C C   . ALA C 1 231 ? -20.183 31.361 13.383  1.00 51.89  ?  386 ALA C C   1 
ATOM   5948 O O   . ALA C 1 231 ? -20.889 31.560 12.400  1.00 49.68  ?  386 ALA C O   1 
ATOM   5949 C CB  . ALA C 1 231 ? -19.254 29.060 13.549  1.00 48.51  ?  386 ALA C CB  1 
ATOM   5950 N N   . VAL C 1 232 ? -20.449 31.843 14.601  1.00 51.44  ?  387 VAL C N   1 
ATOM   5951 C CA  . VAL C 1 232 ? -21.553 32.740 14.922  1.00 52.58  ?  387 VAL C CA  1 
ATOM   5952 C C   . VAL C 1 232 ? -21.033 33.833 15.830  1.00 58.20  ?  387 VAL C C   1 
ATOM   5953 O O   . VAL C 1 232 ? -20.209 33.570 16.716  1.00 58.63  ?  387 VAL C O   1 
ATOM   5954 C CB  . VAL C 1 232 ? -22.823 32.037 15.494  1.00 56.55  ?  387 VAL C CB  1 
ATOM   5955 C CG1 . VAL C 1 232 ? -22.563 31.423 16.864  1.00 56.62  ?  387 VAL C CG1 1 
ATOM   5956 C CG2 . VAL C 1 232 ? -24.012 32.995 15.557  1.00 56.04  ?  387 VAL C CG2 1 
ATOM   5957 N N   . ASP C 1 233 ? -21.495 35.061 15.580  1.00 54.79  ?  388 ASP C N   1 
ATOM   5958 C CA  . ASP C 1 233 ? -21.158 36.241 16.355  1.00 54.79  ?  388 ASP C CA  1 
ATOM   5959 C C   . ASP C 1 233 ? -22.356 37.156 16.261  1.00 58.93  ?  388 ASP C C   1 
ATOM   5960 O O   . ASP C 1 233 ? -22.641 37.680 15.189  1.00 58.40  ?  388 ASP C O   1 
ATOM   5961 C CB  . ASP C 1 233 ? -19.888 36.905 15.800  1.00 56.67  ?  388 ASP C CB  1 
ATOM   5962 C CG  . ASP C 1 233 ? -19.308 38.056 16.609  1.00 66.44  ?  388 ASP C CG  1 
ATOM   5963 O OD1 . ASP C 1 233 ? -19.809 38.309 17.739  1.00 65.29  ?  388 ASP C OD1 1 
ATOM   5964 O OD2 . ASP C 1 233 ? -18.313 38.683 16.128  1.00 72.37  -1 388 ASP C OD2 1 
ATOM   5965 N N   . GLU C 1 234 ? -23.090 37.302 17.373  1.00 56.43  ?  389 GLU C N   1 
ATOM   5966 C CA  . GLU C 1 234 ? -24.291 38.149 17.473  1.00 56.75  ?  389 GLU C CA  1 
ATOM   5967 C C   . GLU C 1 234 ? -24.005 39.615 17.138  1.00 59.98  ?  389 GLU C C   1 
ATOM   5968 O O   . GLU C 1 234 ? -24.868 40.297 16.600  1.00 59.86  ?  389 GLU C O   1 
ATOM   5969 C CB  . GLU C 1 234 ? -24.897 38.056 18.884  1.00 58.64  ?  389 GLU C CB  1 
ATOM   5970 N N   . HIS C 1 235 ? -22.780 40.082 17.418  1.00 55.95  ?  390 HIS C N   1 
ATOM   5971 C CA  . HIS C 1 235 ? -22.342 41.455 17.178  1.00 55.06  ?  390 HIS C CA  1 
ATOM   5972 C C   . HIS C 1 235 ? -21.578 41.616 15.859  1.00 56.83  ?  390 HIS C C   1 
ATOM   5973 O O   . HIS C 1 235 ? -20.707 42.479 15.744  1.00 55.22  ?  390 HIS C O   1 
ATOM   5974 C CB  . HIS C 1 235 ? -21.497 41.925 18.381  1.00 55.88  ?  390 HIS C CB  1 
ATOM   5975 C CG  . HIS C 1 235 ? -22.217 41.854 19.692  1.00 59.38  ?  390 HIS C CG  1 
ATOM   5976 N ND1 . HIS C 1 235 ? -23.514 42.330 19.835  1.00 61.19  ?  390 HIS C ND1 1 
ATOM   5977 C CD2 . HIS C 1 235 ? -21.795 41.375 20.884  1.00 61.11  ?  390 HIS C CD2 1 
ATOM   5978 C CE1 . HIS C 1 235 ? -23.832 42.128 21.101  1.00 60.56  ?  390 HIS C CE1 1 
ATOM   5979 N NE2 . HIS C 1 235 ? -22.829 41.561 21.773  1.00 60.97  ?  390 HIS C NE2 1 
ATOM   5980 N N   . ARG C 1 236 ? -21.919 40.800 14.857  1.00 53.97  ?  391 ARG C N   1 
ATOM   5981 C CA  . ARG C 1 236 ? -21.264 40.840 13.553  1.00 54.13  ?  391 ARG C CA  1 
ATOM   5982 C C   . ARG C 1 236 ? -22.246 40.763 12.392  1.00 60.84  ?  391 ARG C C   1 
ATOM   5983 O O   . ARG C 1 236 ? -23.280 40.100 12.489  1.00 59.87  ?  391 ARG C O   1 
ATOM   5984 C CB  . ARG C 1 236 ? -20.234 39.715 13.474  1.00 52.48  ?  391 ARG C CB  1 
ATOM   5985 C CG  . ARG C 1 236 ? -19.444 39.635 12.181  1.00 66.32  ?  391 ARG C CG  1 
ATOM   5986 C CD  . ARG C 1 236 ? -18.589 38.391 12.134  1.00 82.35  ?  391 ARG C CD  1 
ATOM   5987 N NE  . ARG C 1 236 ? -19.372 37.162 11.980  1.00 85.75  ?  391 ARG C NE  1 
ATOM   5988 C CZ  . ARG C 1 236 ? -18.993 35.996 12.469  1.00 93.94  ?  391 ARG C CZ  1 
ATOM   5989 N NH1 . ARG C 1 236 ? -17.860 35.898 13.151  1.00 76.39  ?  391 ARG C NH1 1 
ATOM   5990 N NH2 . ARG C 1 236 ? -19.744 34.920 12.296  1.00 86.52  1  391 ARG C NH2 1 
ATOM   5991 N N   . GLU C 1 237 ? -21.904 41.443 11.293  1.00 60.06  ?  392 GLU C N   1 
ATOM   5992 C CA  . GLU C 1 237 ? -22.662 41.431 10.052  1.00 60.93  ?  392 GLU C CA  1 
ATOM   5993 C C   . GLU C 1 237 ? -21.763 40.803 8.974   1.00 65.58  ?  392 GLU C C   1 
ATOM   5994 O O   . GLU C 1 237 ? -20.763 41.412 8.593   1.00 65.00  ?  392 GLU C O   1 
ATOM   5995 C CB  . GLU C 1 237 ? -23.100 42.848 9.663   1.00 62.64  ?  392 GLU C CB  1 
ATOM   5996 N N   . PRO C 1 238 ? -22.048 39.562 8.515   1.00 63.42  ?  393 PRO C N   1 
ATOM   5997 C CA  . PRO C 1 238 ? -23.181 38.704 8.903   1.00 62.62  ?  393 PRO C CA  1 
ATOM   5998 C C   . PRO C 1 238 ? -22.884 37.895 10.146  1.00 63.80  ?  393 PRO C C   1 
ATOM   5999 O O   . PRO C 1 238 ? -21.748 37.478 10.353  1.00 62.95  ?  393 PRO C O   1 
ATOM   6000 C CB  . PRO C 1 238 ? -23.397 37.831 7.661   1.00 64.90  ?  393 PRO C CB  1 
ATOM   6001 C CG  . PRO C 1 238 ? -22.034 37.726 6.994   1.00 70.19  ?  393 PRO C CG  1 
ATOM   6002 C CD  . PRO C 1 238 ? -21.203 38.915 7.481   1.00 65.79  ?  393 PRO C CD  1 
ATOM   6003 N N   . GLN C 1 239 ? -23.907 37.663 10.965  1.00 59.56  ?  394 GLN C N   1 
ATOM   6004 C CA  . GLN C 1 239 ? -23.758 36.873 12.188  1.00 58.74  ?  394 GLN C CA  1 
ATOM   6005 C C   . GLN C 1 239 ? -23.215 35.477 11.942  1.00 60.59  ?  394 GLN C C   1 
ATOM   6006 O O   . GLN C 1 239 ? -22.389 35.014 12.717  1.00 60.47  ?  394 GLN C O   1 
ATOM   6007 C CB  . GLN C 1 239 ? -25.074 36.806 12.958  1.00 59.66  ?  394 GLN C CB  1 
ATOM   6008 C CG  . GLN C 1 239 ? -25.330 38.072 13.744  1.00 68.47  ?  394 GLN C CG  1 
ATOM   6009 C CD  . GLN C 1 239 ? -26.752 38.184 14.169  1.00 79.62  ?  394 GLN C CD  1 
ATOM   6010 O OE1 . GLN C 1 239 ? -27.472 39.061 13.690  1.00 76.54  ?  394 GLN C OE1 1 
ATOM   6011 N NE2 . GLN C 1 239 ? -27.196 37.280 15.046  1.00 62.42  ?  394 GLN C NE2 1 
ATOM   6012 N N   . LEU C 1 240 ? -23.669 34.815 10.875  1.00 56.02  ?  395 LEU C N   1 
ATOM   6013 C CA  . LEU C 1 240 ? -23.247 33.454 10.545  1.00 55.98  ?  395 LEU C CA  1 
ATOM   6014 C C   . LEU C 1 240 ? -22.170 33.469 9.488   1.00 56.18  ?  395 LEU C C   1 
ATOM   6015 O O   . LEU C 1 240 ? -22.325 34.094 8.441   1.00 55.47  ?  395 LEU C O   1 
ATOM   6016 C CB  . LEU C 1 240 ? -24.449 32.574 10.094  1.00 57.15  ?  395 LEU C CB  1 
ATOM   6017 C CG  . LEU C 1 240 ? -25.193 31.660 11.128  1.00 62.67  ?  395 LEU C CG  1 
ATOM   6018 C CD1 . LEU C 1 240 ? -24.305 30.549 11.687  1.00 64.29  ?  395 LEU C CD1 1 
ATOM   6019 C CD2 . LEU C 1 240 ? -25.801 32.437 12.252  1.00 63.94  ?  395 LEU C CD2 1 
ATOM   6020 N N   . LEU C 1 241 ? -21.057 32.801 9.783   1.00 52.04  ?  396 LEU C N   1 
ATOM   6021 C CA  . LEU C 1 241 ? -19.888 32.674 8.911   1.00 50.70  ?  396 LEU C CA  1 
ATOM   6022 C C   . LEU C 1 241 ? -20.253 31.946 7.586   1.00 56.08  ?  396 LEU C C   1 
ATOM   6023 O O   . LEU C 1 241 ? -19.680 32.253 6.549   1.00 54.27  ?  396 LEU C O   1 
ATOM   6024 C CB  . LEU C 1 241 ? -18.764 31.962 9.694   1.00 49.89  ?  396 LEU C CB  1 
ATOM   6025 C CG  . LEU C 1 241 ? -17.373 31.943 9.097   1.00 53.06  ?  396 LEU C CG  1 
ATOM   6026 C CD1 . LEU C 1 241 ? -16.776 33.343 8.976   1.00 52.63  ?  396 LEU C CD1 1 
ATOM   6027 C CD2 . LEU C 1 241 ? -16.478 31.088 9.928   1.00 54.95  ?  396 LEU C CD2 1 
ATOM   6028 N N   . LEU C 1 242 ? -21.262 31.049 7.608   1.00 55.25  ?  397 LEU C N   1 
ATOM   6029 C CA  . LEU C 1 242 ? -21.771 30.355 6.422   1.00 55.41  ?  397 LEU C CA  1 
ATOM   6030 C C   . LEU C 1 242 ? -22.254 31.342 5.381   1.00 62.30  ?  397 LEU C C   1 
ATOM   6031 O O   . LEU C 1 242 ? -22.110 31.075 4.187   1.00 62.68  ?  397 LEU C O   1 
ATOM   6032 C CB  . LEU C 1 242 ? -22.950 29.458 6.806   1.00 54.94  ?  397 LEU C CB  1 
ATOM   6033 C CG  . LEU C 1 242 ? -22.716 27.966 6.823   1.00 58.06  ?  397 LEU C CG  1 
ATOM   6034 C CD1 . LEU C 1 242 ? -21.259 27.608 6.537   1.00 57.26  ?  397 LEU C CD1 1 
ATOM   6035 C CD2 . LEU C 1 242 ? -23.236 27.360 8.117   1.00 58.43  ?  397 LEU C CD2 1 
ATOM   6036 N N   . ASP C 1 243 ? -22.845 32.474 5.829   1.00 60.22  ?  398 ASP C N   1 
ATOM   6037 C CA  . ASP C 1 243 ? -23.350 33.527 4.930   1.00 60.88  ?  398 ASP C CA  1 
ATOM   6038 C C   . ASP C 1 243 ? -22.253 34.101 4.041   1.00 63.34  ?  398 ASP C C   1 
ATOM   6039 O O   . ASP C 1 243 ? -22.532 34.492 2.905   1.00 62.60  ?  398 ASP C O   1 
ATOM   6040 C CB  . ASP C 1 243 ? -24.097 34.649 5.694   1.00 63.35  ?  398 ASP C CB  1 
ATOM   6041 C CG  . ASP C 1 243 ? -25.342 34.202 6.454   1.00 81.71  ?  398 ASP C CG  1 
ATOM   6042 O OD1 . ASP C 1 243 ? -25.931 33.142 6.080   1.00 83.90  ?  398 ASP C OD1 1 
ATOM   6043 O OD2 . ASP C 1 243 ? -25.743 34.917 7.416   1.00 88.90  -1 398 ASP C OD2 1 
ATOM   6044 N N   . ILE C 1 244 ? -21.004 34.131 4.559   1.00 59.59  ?  399 ILE C N   1 
ATOM   6045 C CA  . ILE C 1 244 ? -19.799 34.602 3.868   1.00 58.56  ?  399 ILE C CA  1 
ATOM   6046 C C   . ILE C 1 244 ? -19.522 33.727 2.631   1.00 59.63  ?  399 ILE C C   1 
ATOM   6047 O O   . ILE C 1 244 ? -19.146 34.259 1.592   1.00 58.17  ?  399 ILE C O   1 
ATOM   6048 C CB  . ILE C 1 244 ? -18.609 34.754 4.876   1.00 62.21  ?  399 ILE C CB  1 
ATOM   6049 C CG1 . ILE C 1 244 ? -18.714 36.090 5.652   1.00 63.65  ?  399 ILE C CG1 1 
ATOM   6050 C CG2 . ILE C 1 244 ? -17.221 34.585 4.255   1.00 62.70  ?  399 ILE C CG2 1 
ATOM   6051 C CD1 . ILE C 1 244 ? -18.915 35.950 7.160   1.00 75.76  ?  399 ILE C CD1 1 
ATOM   6052 N N   . LYS C 1 245 ? -19.781 32.406 2.718   1.00 56.37  ?  400 LYS C N   1 
ATOM   6053 C CA  . LYS C 1 245 ? -19.647 31.466 1.591   1.00 56.32  ?  400 LYS C CA  1 
ATOM   6054 C C   . LYS C 1 245 ? -20.590 31.883 0.456   1.00 61.91  ?  400 LYS C C   1 
ATOM   6055 O O   . LYS C 1 245 ? -20.176 31.859 -0.699  1.00 61.89  ?  400 LYS C O   1 
ATOM   6056 C CB  . LYS C 1 245 ? -19.974 30.010 2.017   1.00 57.59  ?  400 LYS C CB  1 
ATOM   6057 C CG  . LYS C 1 245 ? -19.800 28.987 0.892   1.00 56.24  ?  400 LYS C CG  1 
ATOM   6058 C CD  . LYS C 1 245 ? -20.750 27.810 0.998   1.00 60.87  ?  400 LYS C CD  1 
ATOM   6059 C CE  . LYS C 1 245 ? -20.582 26.875 -0.184  1.00 74.71  ?  400 LYS C CE  1 
ATOM   6060 N NZ  . LYS C 1 245 ? -21.674 25.864 -0.290  1.00 79.26  1  400 LYS C NZ  1 
ATOM   6061 N N   . GLU C 1 246 ? -21.859 32.257 0.792   1.00 59.10  ?  401 GLU C N   1 
ATOM   6062 C CA  . GLU C 1 246 ? -22.885 32.684 -0.168  1.00 58.29  ?  401 GLU C CA  1 
ATOM   6063 C C   . GLU C 1 246 ? -22.423 33.927 -0.920  1.00 60.89  ?  401 GLU C C   1 
ATOM   6064 O O   . GLU C 1 246 ? -22.472 33.934 -2.150  1.00 57.95  ?  401 GLU C O   1 
ATOM   6065 C CB  . GLU C 1 246 ? -24.231 32.922 0.532   1.00 59.73  ?  401 GLU C CB  1 
ATOM   6066 N N   . GLU C 1 247 ? -21.889 34.937 -0.176  1.00 59.41  ?  402 GLU C N   1 
ATOM   6067 C CA  . GLU C 1 247 ? -21.319 36.197 -0.700  1.00 59.45  ?  402 GLU C CA  1 
ATOM   6068 C C   . GLU C 1 247 ? -20.184 35.947 -1.720  1.00 63.63  ?  402 GLU C C   1 
ATOM   6069 O O   . GLU C 1 247 ? -20.126 36.611 -2.758  1.00 62.59  ?  402 GLU C O   1 
ATOM   6070 C CB  . GLU C 1 247 ? -20.824 37.093 0.447   1.00 60.66  ?  402 GLU C CB  1 
ATOM   6071 C CG  . GLU C 1 247 ? -21.946 37.670 1.288   1.00 73.54  ?  402 GLU C CG  1 
ATOM   6072 C CD  . GLU C 1 247 ? -21.523 38.624 2.387   1.00 108.32 ?  402 GLU C CD  1 
ATOM   6073 O OE1 . GLU C 1 247 ? -20.872 39.646 2.065   1.00 111.69 ?  402 GLU C OE1 1 
ATOM   6074 O OE2 . GLU C 1 247 ? -21.879 38.378 3.563   1.00 112.51 -1 402 GLU C OE2 1 
ATOM   6075 N N   . ILE C 1 248 ? -19.313 34.965 -1.429  1.00 60.97  ?  403 ILE C N   1 
ATOM   6076 C CA  . ILE C 1 248 ? -18.205 34.574 -2.294  1.00 61.52  ?  403 ILE C CA  1 
ATOM   6077 C C   . ILE C 1 248 ? -18.756 33.863 -3.522  1.00 68.83  ?  403 ILE C C   1 
ATOM   6078 O O   . ILE C 1 248 ? -18.393 34.238 -4.636  1.00 68.25  ?  403 ILE C O   1 
ATOM   6079 C CB  . ILE C 1 248 ? -17.102 33.750 -1.540  1.00 64.28  ?  403 ILE C CB  1 
ATOM   6080 C CG1 . ILE C 1 248 ? -16.465 34.583 -0.388  1.00 64.52  ?  403 ILE C CG1 1 
ATOM   6081 C CG2 . ILE C 1 248 ? -16.017 33.211 -2.511  1.00 63.56  ?  403 ILE C CG2 1 
ATOM   6082 C CD1 . ILE C 1 248 ? -15.783 33.784 0.743   1.00 66.23  ?  403 ILE C CD1 1 
ATOM   6083 N N   . GLU C 1 249 ? -19.640 32.855 -3.317  1.00 69.02  ?  404 GLU C N   1 
ATOM   6084 C CA  . GLU C 1 249 ? -20.269 32.062 -4.386  1.00 70.66  ?  404 GLU C CA  1 
ATOM   6085 C C   . GLU C 1 249 ? -21.051 32.963 -5.354  1.00 77.22  ?  404 GLU C C   1 
ATOM   6086 O O   . GLU C 1 249 ? -20.959 32.776 -6.567  1.00 76.00  ?  404 GLU C O   1 
ATOM   6087 C CB  . GLU C 1 249 ? -21.177 30.934 -3.827  1.00 72.42  ?  404 GLU C CB  1 
ATOM   6088 C CG  . GLU C 1 249 ? -20.481 29.816 -3.051  1.00 88.33  ?  404 GLU C CG  1 
ATOM   6089 C CD  . GLU C 1 249 ? -19.320 29.074 -3.701  1.00 118.58 ?  404 GLU C CD  1 
ATOM   6090 O OE1 . GLU C 1 249 ? -19.532 28.473 -4.779  1.00 119.98 ?  404 GLU C OE1 1 
ATOM   6091 O OE2 . GLU C 1 249 ? -18.217 29.048 -3.105  1.00 108.78 -1 404 GLU C OE2 1 
ATOM   6092 N N   . ASP C 1 250 ? -21.759 33.985 -4.813  1.00 76.87  ?  405 ASP C N   1 
ATOM   6093 C CA  . ASP C 1 250 ? -22.529 34.952 -5.602  1.00 78.05  ?  405 ASP C CA  1 
ATOM   6094 C C   . ASP C 1 250 ? -21.652 36.118 -6.085  1.00 82.69  ?  405 ASP C C   1 
ATOM   6095 O O   . ASP C 1 250 ? -22.159 37.231 -6.263  1.00 82.19  ?  405 ASP C O   1 
ATOM   6096 C CB  . ASP C 1 250 ? -23.761 35.462 -4.818  1.00 80.75  ?  405 ASP C CB  1 
ATOM   6097 C CG  . ASP C 1 250 ? -24.745 34.378 -4.388  1.00 99.33  ?  405 ASP C CG  1 
ATOM   6098 O OD1 . ASP C 1 250 ? -25.001 33.444 -5.196  1.00 99.96  ?  405 ASP C OD1 1 
ATOM   6099 O OD2 . ASP C 1 250 ? -25.279 34.474 -3.255  1.00 108.09 -1 405 ASP C OD2 1 
ATOM   6100 N N   . GLU C 1 251 ? -20.329 35.855 -6.285  1.00 79.54  ?  406 GLU C N   1 
ATOM   6101 C CA  . GLU C 1 251 ? -19.273 36.773 -6.761  1.00 78.73  ?  406 GLU C CA  1 
ATOM   6102 C C   . GLU C 1 251 ? -19.249 38.207 -6.160  1.00 80.83  ?  406 GLU C C   1 
ATOM   6103 O O   . GLU C 1 251 ? -18.480 39.055 -6.626  1.00 79.84  ?  406 GLU C O   1 
ATOM   6104 C CB  . GLU C 1 251 ? -19.183 36.769 -8.300  1.00 80.04  ?  406 GLU C CB  1 
ATOM   6105 N N   . GLU C 1 252 ? -20.053 38.456 -5.100  1.00 76.50  ?  407 GLU C N   1 
ATOM   6106 C CA  . GLU C 1 252 ? -20.143 39.744 -4.406  1.00 75.84  ?  407 GLU C CA  1 
ATOM   6107 C C   . GLU C 1 252 ? -18.852 40.072 -3.611  1.00 79.47  ?  407 GLU C C   1 
ATOM   6108 O O   . GLU C 1 252 ? -18.593 41.247 -3.332  1.00 80.16  ?  407 GLU C O   1 
ATOM   6109 C CB  . GLU C 1 252 ? -21.391 39.789 -3.504  1.00 76.95  ?  407 GLU C CB  1 
ATOM   6110 N N   . LYS C 1 253 ? -18.052 39.027 -3.252  1.00 73.19  ?  408 LYS C N   1 
ATOM   6111 C CA  . LYS C 1 253 ? -16.783 39.090 -2.513  1.00 71.38  ?  408 LYS C CA  1 
ATOM   6112 C C   . LYS C 1 253 ? -15.868 37.891 -2.934  1.00 71.81  ?  408 LYS C C   1 
ATOM   6113 O O   . LYS C 1 253 ? -16.317 36.986 -3.647  1.00 70.61  ?  408 LYS C O   1 
ATOM   6114 C CB  . LYS C 1 253 ? -17.056 39.004 -0.979  1.00 74.35  ?  408 LYS C CB  1 
ATOM   6115 C CG  . LYS C 1 253 ? -17.932 40.097 -0.347  1.00 91.18  ?  408 LYS C CG  1 
ATOM   6116 C CD  . LYS C 1 253 ? -17.156 41.364 0.027   1.00 98.58  ?  408 LYS C CD  1 
ATOM   6117 C CE  . LYS C 1 253 ? -18.056 42.529 0.397   1.00 107.93 ?  408 LYS C CE  1 
ATOM   6118 N NZ  . LYS C 1 253 ? -18.757 42.336 1.701   1.00 114.59 1  408 LYS C NZ  1 
ATOM   6119 N N   . THR C 1 254 ? -14.596 37.885 -2.475  1.00 66.55  ?  409 THR C N   1 
ATOM   6120 C CA  . THR C 1 254 ? -13.630 36.777 -2.661  1.00 65.22  ?  409 THR C CA  1 
ATOM   6121 C C   . THR C 1 254 ? -13.131 36.310 -1.296  1.00 66.94  ?  409 THR C C   1 
ATOM   6122 O O   . THR C 1 254 ? -13.322 37.014 -0.291  1.00 67.05  ?  409 THR C O   1 
ATOM   6123 C CB  . THR C 1 254 ? -12.430 37.133 -3.566  1.00 71.32  ?  409 THR C CB  1 
ATOM   6124 O OG1 . THR C 1 254 ? -11.845 38.375 -3.169  1.00 72.59  ?  409 THR C OG1 1 
ATOM   6125 C CG2 . THR C 1 254 ? -12.778 37.122 -5.026  1.00 70.28  ?  409 THR C CG2 1 
ATOM   6126 N N   . ILE C 1 255 ? -12.479 35.132 -1.252  1.00 61.34  ?  410 ILE C N   1 
ATOM   6127 C CA  . ILE C 1 255 ? -11.910 34.627 0.001   1.00 60.07  ?  410 ILE C CA  1 
ATOM   6128 C C   . ILE C 1 255 ? -10.802 35.562 0.536   1.00 65.61  ?  410 ILE C C   1 
ATOM   6129 O O   . ILE C 1 255 ? -10.683 35.748 1.749   1.00 66.51  ?  410 ILE C O   1 
ATOM   6130 C CB  . ILE C 1 255 ? -11.534 33.123 -0.047  1.00 61.40  ?  410 ILE C CB  1 
ATOM   6131 C CG1 . ILE C 1 255 ? -11.313 32.541 1.363   1.00 60.18  ?  410 ILE C CG1 1 
ATOM   6132 C CG2 . ILE C 1 255 ? -10.361 32.837 -0.989  1.00 61.70  ?  410 ILE C CG2 1 
ATOM   6133 C CD1 . ILE C 1 255 ? -12.424 32.830 2.421   1.00 54.93  ?  410 ILE C CD1 1 
ATOM   6134 N N   . GLU C 1 256 ? -10.079 36.220 -0.393  1.00 61.10  ?  411 GLU C N   1 
ATOM   6135 C CA  . GLU C 1 256 ? -9.018  37.196 -0.128  1.00 60.23  ?  411 GLU C CA  1 
ATOM   6136 C C   . GLU C 1 256 ? -9.529  38.361 0.713   1.00 62.45  ?  411 GLU C C   1 
ATOM   6137 O O   . GLU C 1 256 ? -8.800  38.867 1.560   1.00 63.81  ?  411 GLU C O   1 
ATOM   6138 C CB  . GLU C 1 256 ? -8.397  37.703 -1.442  1.00 61.31  ?  411 GLU C CB  1 
ATOM   6139 C CG  . GLU C 1 256 ? -7.397  36.739 -2.066  1.00 69.03  ?  411 GLU C CG  1 
ATOM   6140 C CD  . GLU C 1 256 ? -7.949  35.470 -2.694  1.00 89.90  ?  411 GLU C CD  1 
ATOM   6141 O OE1 . GLU C 1 256 ? -8.995  35.536 -3.381  1.00 89.14  ?  411 GLU C OE1 1 
ATOM   6142 O OE2 . GLU C 1 256 ? -7.307  34.409 -2.525  1.00 81.13  -1 411 GLU C OE2 1 
ATOM   6143 N N   . ASP C 1 257 ? -10.794 38.741 0.523   1.00 55.71  ?  412 ASP C N   1 
ATOM   6144 C CA  . ASP C 1 257 ? -11.409 39.810 1.288   1.00 54.49  ?  412 ASP C CA  1 
ATOM   6145 C C   . ASP C 1 257 ? -11.628 39.373 2.730   1.00 55.45  ?  412 ASP C C   1 
ATOM   6146 O O   . ASP C 1 257 ? -11.798 40.226 3.598   1.00 56.16  ?  412 ASP C O   1 
ATOM   6147 C CB  . ASP C 1 257 ? -12.746 40.237 0.644   1.00 56.35  ?  412 ASP C CB  1 
ATOM   6148 C CG  . ASP C 1 257 ? -12.632 40.710 -0.804  1.00 72.38  ?  412 ASP C CG  1 
ATOM   6149 O OD1 . ASP C 1 257 ? -11.937 41.720 -1.052  1.00 76.38  ?  412 ASP C OD1 1 
ATOM   6150 O OD2 . ASP C 1 257 ? -13.295 40.118 -1.674  1.00 74.52  -1 412 ASP C OD2 1 
ATOM   6151 N N   . TYR C 1 258 ? -11.639 38.045 2.983   1.00 49.30  ?  413 TYR C N   1 
ATOM   6152 C CA  . TYR C 1 258 ? -11.904 37.479 4.311   1.00 48.16  ?  413 TYR C CA  1 
ATOM   6153 C C   . TYR C 1 258 ? -10.744 36.862 5.072   1.00 46.93  ?  413 TYR C C   1 
ATOM   6154 O O   . TYR C 1 258 ? -10.907 36.585 6.273   1.00 46.27  ?  413 TYR C O   1 
ATOM   6155 C CB  . TYR C 1 258 ? -13.131 36.569 4.303   1.00 50.52  ?  413 TYR C CB  1 
ATOM   6156 C CG  . TYR C 1 258 ? -14.415 37.347 4.176   1.00 53.32  ?  413 TYR C CG  1 
ATOM   6157 C CD1 . TYR C 1 258 ? -14.960 38.010 5.275   1.00 56.21  ?  413 TYR C CD1 1 
ATOM   6158 C CD2 . TYR C 1 258 ? -15.086 37.426 2.959   1.00 53.88  ?  413 TYR C CD2 1 
ATOM   6159 C CE1 . TYR C 1 258 ? -16.149 38.720 5.170   1.00 59.58  ?  413 TYR C CE1 1 
ATOM   6160 C CE2 . TYR C 1 258 ? -16.268 38.142 2.838   1.00 55.69  ?  413 TYR C CE2 1 
ATOM   6161 C CZ  . TYR C 1 258 ? -16.799 38.785 3.949   1.00 68.66  ?  413 TYR C CZ  1 
ATOM   6162 O OH  . TYR C 1 258 ? -17.960 39.515 3.851   1.00 73.75  ?  413 TYR C OH  1 
ATOM   6163 N N   . ILE C 1 259 ? -9.564  36.702 4.409   1.00 39.61  ?  414 ILE C N   1 
ATOM   6164 C CA  . ILE C 1 259 ? -8.347  36.186 5.044   1.00 38.17  ?  414 ILE C CA  1 
ATOM   6165 C C   . ILE C 1 259 ? -8.061  36.988 6.326   1.00 41.45  ?  414 ILE C C   1 
ATOM   6166 O O   . ILE C 1 259 ? -8.036  38.232 6.296   1.00 41.80  ?  414 ILE C O   1 
ATOM   6167 C CB  . ILE C 1 259 ? -7.113  36.155 4.091   1.00 40.89  ?  414 ILE C CB  1 
ATOM   6168 C CG1 . ILE C 1 259 ? -7.396  35.354 2.794   1.00 41.95  ?  414 ILE C CG1 1 
ATOM   6169 C CG2 . ILE C 1 259 ? -5.900  35.594 4.803   1.00 40.78  ?  414 ILE C CG2 1 
ATOM   6170 C CD1 . ILE C 1 259 ? -6.252  35.437 1.670   1.00 51.06  ?  414 ILE C CD1 1 
ATOM   6171 N N   . ASP C 1 260 ? -7.891  36.271 7.449   1.00 35.71  ?  415 ASP C N   1 
ATOM   6172 C CA  . ASP C 1 260 ? -7.590  36.849 8.753   1.00 33.64  ?  415 ASP C CA  1 
ATOM   6173 C C   . ASP C 1 260 ? -6.422  37.838 8.640   1.00 38.29  ?  415 ASP C C   1 
ATOM   6174 O O   . ASP C 1 260 ? -5.322  37.448 8.228   1.00 39.61  ?  415 ASP C O   1 
ATOM   6175 C CB  . ASP C 1 260 ? -7.234  35.721 9.719   1.00 33.93  ?  415 ASP C CB  1 
ATOM   6176 C CG  . ASP C 1 260 ? -7.138  36.084 11.185  1.00 32.06  ?  415 ASP C CG  1 
ATOM   6177 O OD1 . ASP C 1 260 ? -7.211  37.295 11.518  1.00 26.36  ?  415 ASP C OD1 1 
ATOM   6178 O OD2 . ASP C 1 260 ? -6.983  35.168 12.003  1.00 36.07  -1 415 ASP C OD2 1 
ATOM   6179 N N   . LYS C 1 261 ? -6.675  39.126 8.963   1.00 32.85  ?  416 LYS C N   1 
ATOM   6180 C CA  . LYS C 1 261 ? -5.653  40.176 8.939   1.00 31.30  ?  416 LYS C CA  1 
ATOM   6181 C C   . LYS C 1 261 ? -4.537  40.027 10.021  1.00 38.65  ?  416 LYS C C   1 
ATOM   6182 O O   . LYS C 1 261 ? -3.442  40.622 9.892   1.00 38.01  ?  416 LYS C O   1 
ATOM   6183 C CB  . LYS C 1 261 ? -6.274  41.569 8.886   1.00 30.51  ?  416 LYS C CB  1 
ATOM   6184 C CG  . LYS C 1 261 ? -6.764  41.912 7.482   1.00 35.37  ?  416 LYS C CG  1 
ATOM   6185 C CD  . LYS C 1 261 ? -7.402  43.286 7.388   1.00 42.75  ?  416 LYS C CD  1 
ATOM   6186 C CE  . LYS C 1 261 ? -8.649  43.315 6.543   1.00 59.16  ?  416 LYS C CE  1 
ATOM   6187 N NZ  . LYS C 1 261 ? -8.370  43.043 5.094   1.00 79.03  1  416 LYS C NZ  1 
ATOM   6188 N N   . LYS C 1 262 ? -4.792  39.164 11.042  1.00 36.64  ?  417 LYS C N   1 
ATOM   6189 C CA  . LYS C 1 262 ? -3.845  38.870 12.130  1.00 36.38  ?  417 LYS C CA  1 
ATOM   6190 C C   . LYS C 1 262 ? -2.720  37.897 11.704  1.00 40.29  ?  417 LYS C C   1 
ATOM   6191 O O   . LYS C 1 262 ? -2.051  37.303 12.555  1.00 40.03  ?  417 LYS C O   1 
ATOM   6192 C CB  . LYS C 1 262 ? -4.568  38.401 13.407  1.00 38.55  ?  417 LYS C CB  1 
ATOM   6193 C CG  . LYS C 1 262 ? -5.646  39.379 13.912  1.00 49.32  ?  417 LYS C CG  1 
ATOM   6194 C CD  . LYS C 1 262 ? -6.307  38.969 15.255  1.00 53.46  ?  417 LYS C CD  1 
ATOM   6195 C CE  . LYS C 1 262 ? -7.178  37.720 15.225  1.00 66.30  ?  417 LYS C CE  1 
ATOM   6196 N NZ  . LYS C 1 262 ? -8.331  37.834 14.278  1.00 71.98  1  417 LYS C NZ  1 
ATOM   6197 N N   . MET C 1 263 ? -2.516  37.735 10.374  1.00 36.10  ?  418 MET C N   1 
ATOM   6198 C CA  . MET C 1 263 ? -1.466  36.870 9.812   1.00 34.98  ?  418 MET C CA  1 
ATOM   6199 C C   . MET C 1 263 ? -0.541  37.692 8.908   1.00 39.98  ?  418 MET C C   1 
ATOM   6200 O O   . MET C 1 263 ? -0.991  38.662 8.306   1.00 42.79  ?  418 MET C O   1 
ATOM   6201 C CB  . MET C 1 263 ? -2.083  35.744 8.966   1.00 36.43  ?  418 MET C CB  1 
ATOM   6202 C CG  . MET C 1 263 ? -2.862  34.753 9.738   1.00 40.32  ?  418 MET C CG  1 
ATOM   6203 S SD  . MET C 1 263 ? -3.267  33.306 8.726   1.00 46.71  ?  418 MET C SD  1 
ATOM   6204 C CE  . MET C 1 263 ? -4.702  33.897 7.811   1.00 43.08  ?  418 MET C CE  1 
ATOM   6205 N N   . ASN C 1 264 ? 0.715   37.289 8.755   1.00 34.67  ?  419 ASN C N   1 
ATOM   6206 C CA  . ASN C 1 264 ? 1.607   37.952 7.796   1.00 34.14  ?  419 ASN C CA  1 
ATOM   6207 C C   . ASN C 1 264 ? 2.164   36.994 6.703   1.00 39.23  ?  419 ASN C C   1 
ATOM   6208 O O   . ASN C 1 264 ? 2.700   37.463 5.692   1.00 38.62  ?  419 ASN C O   1 
ATOM   6209 C CB  . ASN C 1 264 ? 2.724   38.683 8.494   1.00 30.43  ?  419 ASN C CB  1 
ATOM   6210 C CG  . ASN C 1 264 ? 3.625   37.806 9.301   1.00 41.68  ?  419 ASN C CG  1 
ATOM   6211 O OD1 . ASN C 1 264 ? 4.255   36.880 8.803   1.00 34.23  ?  419 ASN C OD1 1 
ATOM   6212 N ND2 . ASN C 1 264 ? 3.716   38.099 10.577  1.00 41.93  ?  419 ASN C ND2 1 
ATOM   6213 N N   . ASP C 1 265 ? 2.021   35.660 6.920   1.00 36.30  ?  420 ASP C N   1 
ATOM   6214 C CA  . ASP C 1 265 ? 2.521   34.568 6.076   1.00 36.57  ?  420 ASP C CA  1 
ATOM   6215 C C   . ASP C 1 265 ? 1.452   33.853 5.219   1.00 42.78  ?  420 ASP C C   1 
ATOM   6216 O O   . ASP C 1 265 ? 1.684   32.728 4.754   1.00 42.96  ?  420 ASP C O   1 
ATOM   6217 C CB  . ASP C 1 265 ? 3.247   33.541 6.968   1.00 38.17  ?  420 ASP C CB  1 
ATOM   6218 C CG  . ASP C 1 265 ? 2.345   32.881 8.017   1.00 47.90  ?  420 ASP C CG  1 
ATOM   6219 O OD1 . ASP C 1 265 ? 1.379   33.552 8.496   1.00 46.82  ?  420 ASP C OD1 1 
ATOM   6220 O OD2 . ASP C 1 265 ? 2.636   31.722 8.406   1.00 54.17  -1 420 ASP C OD2 1 
ATOM   6221 N N   . ALA C 1 266 ? 0.308   34.488 4.982   1.00 40.57  ?  421 ALA C N   1 
ATOM   6222 C CA  . ALA C 1 266 ? -0.700  33.825 4.147   1.00 40.78  ?  421 ALA C CA  1 
ATOM   6223 C C   . ALA C 1 266 ? -0.423  34.017 2.650   1.00 44.75  ?  421 ALA C C   1 
ATOM   6224 O O   . ALA C 1 266 ? 0.219   34.997 2.270   1.00 46.31  ?  421 ALA C O   1 
ATOM   6225 C CB  . ALA C 1 266 ? -2.092  34.327 4.497   1.00 41.43  ?  421 ALA C CB  1 
ATOM   6226 N N   . ASP C 1 267 ? -0.909  33.093 1.804   1.00 38.86  ?  422 ASP C N   1 
ATOM   6227 C CA  . ASP C 1 267 ? -0.776  33.206 0.351   1.00 37.91  ?  422 ASP C CA  1 
ATOM   6228 C C   . ASP C 1 267 ? -2.069  32.789 -0.342  1.00 42.43  ?  422 ASP C C   1 
ATOM   6229 O O   . ASP C 1 267 ? -2.718  31.822 0.065   1.00 42.01  ?  422 ASP C O   1 
ATOM   6230 C CB  . ASP C 1 267 ? 0.383   32.367 -0.172  1.00 39.63  ?  422 ASP C CB  1 
ATOM   6231 C CG  . ASP C 1 267 ? 0.236   30.883 0.104   1.00 61.69  ?  422 ASP C CG  1 
ATOM   6232 O OD1 . ASP C 1 267 ? -0.264  30.161 -0.786  1.00 63.72  ?  422 ASP C OD1 1 
ATOM   6233 O OD2 . ASP C 1 267 ? 0.573   30.451 1.230   1.00 73.10  -1 422 ASP C OD2 1 
ATOM   6234 N N   . SER C 1 268 ? -2.413  33.492 -1.408  1.00 38.70  ?  423 SER C N   1 
ATOM   6235 C CA  . SER C 1 268 ? -3.573  33.217 -2.246  1.00 39.23  ?  423 SER C CA  1 
ATOM   6236 C C   . SER C 1 268 ? -3.703  31.716 -2.657  1.00 45.41  ?  423 SER C C   1 
ATOM   6237 O O   . SER C 1 268 ? -4.803  31.180 -2.637  1.00 45.68  ?  423 SER C O   1 
ATOM   6238 C CB  . SER C 1 268 ? -3.504  34.083 -3.493  1.00 43.46  ?  423 SER C CB  1 
ATOM   6239 O OG  . SER C 1 268 ? -2.240  33.894 -4.114  1.00 58.18  ?  423 SER C OG  1 
ATOM   6240 N N   . THR C 1 269 ? -2.599  31.043 -3.007  1.00 42.91  ?  424 THR C N   1 
ATOM   6241 C CA  . THR C 1 269 ? -2.666  29.653 -3.461  1.00 43.36  ?  424 THR C CA  1 
ATOM   6242 C C   . THR C 1 269 ? -3.152  28.700 -2.380  1.00 48.34  ?  424 THR C C   1 
ATOM   6243 O O   . THR C 1 269 ? -4.153  28.028 -2.603  1.00 49.78  ?  424 THR C O   1 
ATOM   6244 C CB  . THR C 1 269 ? -1.345  29.221 -4.130  1.00 53.00  ?  424 THR C CB  1 
ATOM   6245 O OG1 . THR C 1 269 ? -0.981  30.198 -5.110  1.00 59.47  ?  424 THR C OG1 1 
ATOM   6246 C CG2 . THR C 1 269 ? -1.424  27.843 -4.752  1.00 43.53  ?  424 THR C CG2 1 
ATOM   6247 N N   . SER C 1 270 ? -2.471  28.634 -1.223  1.00 44.72  ?  425 SER C N   1 
ATOM   6248 C CA  . SER C 1 270 ? -2.899  27.718 -0.152  1.00 44.13  ?  425 SER C CA  1 
ATOM   6249 C C   . SER C 1 270 ? -4.241  28.116 0.477   1.00 47.70  ?  425 SER C C   1 
ATOM   6250 O O   . SER C 1 270 ? -5.045  27.231 0.787   1.00 47.37  ?  425 SER C O   1 
ATOM   6251 C CB  . SER C 1 270 ? -1.805  27.490 0.892   1.00 43.49  ?  425 SER C CB  1 
ATOM   6252 O OG  . SER C 1 270 ? -1.447  28.695 1.533   1.00 38.73  ?  425 SER C OG  1 
ATOM   6253 N N   . VAL C 1 271 ? -4.522  29.431 0.566   1.00 43.85  ?  426 VAL C N   1 
ATOM   6254 C CA  . VAL C 1 271 ? -5.791  29.927 1.094   1.00 43.93  ?  426 VAL C CA  1 
ATOM   6255 C C   . VAL C 1 271 ? -6.926  29.466 0.202   1.00 50.95  ?  426 VAL C C   1 
ATOM   6256 O O   . VAL C 1 271 ? -7.918  28.948 0.711   1.00 51.62  ?  426 VAL C O   1 
ATOM   6257 C CB  . VAL C 1 271 ? -5.830  31.449 1.364   1.00 46.47  ?  426 VAL C CB  1 
ATOM   6258 C CG1 . VAL C 1 271 ? -7.260  31.919 1.566   1.00 45.91  ?  426 VAL C CG1 1 
ATOM   6259 C CG2 . VAL C 1 271 ? -4.981  31.799 2.584   1.00 45.97  ?  426 VAL C CG2 1 
ATOM   6260 N N   . GLU C 1 272 ? -6.760  29.600 -1.119  1.00 48.55  ?  427 GLU C N   1 
ATOM   6261 C CA  . GLU C 1 272 ? -7.778  29.174 -2.076  1.00 48.40  ?  427 GLU C CA  1 
ATOM   6262 C C   . GLU C 1 272 ? -7.964  27.671 -2.098  1.00 49.56  ?  427 GLU C C   1 
ATOM   6263 O O   . GLU C 1 272 ? -9.093  27.211 -2.248  1.00 50.90  ?  427 GLU C O   1 
ATOM   6264 C CB  . GLU C 1 272 ? -7.484  29.711 -3.472  1.00 50.16  ?  427 GLU C CB  1 
ATOM   6265 C CG  . GLU C 1 272 ? -7.979  31.137 -3.680  1.00 63.61  ?  427 GLU C CG  1 
ATOM   6266 C CD  . GLU C 1 272 ? -7.534  31.798 -4.974  1.00 98.20  ?  427 GLU C CD  1 
ATOM   6267 O OE1 . GLU C 1 272 ? -6.971  31.099 -5.850  1.00 77.52  ?  427 GLU C OE1 1 
ATOM   6268 O OE2 . GLU C 1 272 ? -7.742  33.028 -5.105  1.00 106.62 -1 427 GLU C OE2 1 
ATOM   6269 N N   . ALA C 1 273 ? -6.886  26.909 -1.914  1.00 43.93  ?  428 ALA C N   1 
ATOM   6270 C CA  . ALA C 1 273 ? -6.932  25.440 -1.877  1.00 43.03  ?  428 ALA C CA  1 
ATOM   6271 C C   . ALA C 1 273 ? -7.760  24.983 -0.681  1.00 48.81  ?  428 ALA C C   1 
ATOM   6272 O O   . ALA C 1 273 ? -8.607  24.101 -0.833  1.00 48.78  ?  428 ALA C O   1 
ATOM   6273 C CB  . ALA C 1 273 ? -5.529  24.863 -1.808  1.00 42.89  ?  428 ALA C CB  1 
ATOM   6274 N N   . MET C 1 274 ? -7.568  25.644 0.493   1.00 45.54  ?  429 MET C N   1 
ATOM   6275 C CA  . MET C 1 274 ? -8.311  25.352 1.717   1.00 43.89  ?  429 MET C CA  1 
ATOM   6276 C C   . MET C 1 274 ? -9.767  25.787 1.566   1.00 46.56  ?  429 MET C C   1 
ATOM   6277 O O   . MET C 1 274 ? -10.649 25.062 2.010   1.00 46.68  ?  429 MET C O   1 
ATOM   6278 C CB  . MET C 1 274 ? -7.677  26.016 2.942   1.00 45.93  ?  429 MET C CB  1 
ATOM   6279 C CG  . MET C 1 274 ? -8.036  25.299 4.218   1.00 49.51  ?  429 MET C CG  1 
ATOM   6280 S SD  . MET C 1 274 ? -7.170  25.839 5.708   1.00 53.14  ?  429 MET C SD  1 
ATOM   6281 C CE  . MET C 1 274 ? -8.419  26.553 6.479   1.00 49.88  ?  429 MET C CE  1 
ATOM   6282 N N   . TYR C 1 275 ? -10.026 26.947 0.938   1.00 41.84  ?  430 TYR C N   1 
ATOM   6283 C CA  . TYR C 1 275 ? -11.393 27.414 0.730   1.00 41.76  ?  430 TYR C CA  1 
ATOM   6284 C C   . TYR C 1 275 ? -12.174 26.418 -0.139  1.00 47.43  ?  430 TYR C C   1 
ATOM   6285 O O   . TYR C 1 275 ? -13.338 26.128 0.150   1.00 46.91  ?  430 TYR C O   1 
ATOM   6286 C CB  . TYR C 1 275 ? -11.452 28.833 0.136   1.00 42.61  ?  430 TYR C CB  1 
ATOM   6287 C CG  . TYR C 1 275 ? -12.882 29.295 -0.042  1.00 45.55  ?  430 TYR C CG  1 
ATOM   6288 C CD1 . TYR C 1 275 ? -13.631 29.742 1.043   1.00 47.77  ?  430 TYR C CD1 1 
ATOM   6289 C CD2 . TYR C 1 275 ? -13.530 29.168 -1.272  1.00 46.65  ?  430 TYR C CD2 1 
ATOM   6290 C CE1 . TYR C 1 275 ? -14.969 30.124 0.894   1.00 50.60  ?  430 TYR C CE1 1 
ATOM   6291 C CE2 . TYR C 1 275 ? -14.873 29.515 -1.427  1.00 47.63  ?  430 TYR C CE2 1 
ATOM   6292 C CZ  . TYR C 1 275 ? -15.586 30.013 -0.345  1.00 57.45  ?  430 TYR C CZ  1 
ATOM   6293 O OH  . TYR C 1 275 ? -16.913 30.361 -0.503  1.00 58.36  ?  430 TYR C OH  1 
ATOM   6294 N N   . SER C 1 276 ? -11.513 25.884 -1.187  1.00 43.85  ?  431 SER C N   1 
ATOM   6295 C CA  . SER C 1 276 ? -12.066 24.882 -2.080  1.00 42.81  ?  431 SER C CA  1 
ATOM   6296 C C   . SER C 1 276 ? -12.519 23.639 -1.282  1.00 48.21  ?  431 SER C C   1 
ATOM   6297 O O   . SER C 1 276 ? -13.633 23.172 -1.490  1.00 49.02  ?  431 SER C O   1 
ATOM   6298 C CB  . SER C 1 276 ? -11.046 24.513 -3.149  1.00 43.16  ?  431 SER C CB  1 
ATOM   6299 O OG  . SER C 1 276 ? -11.459 23.359 -3.859  1.00 48.12  ?  431 SER C OG  1 
ATOM   6300 N N   . VAL C 1 277 ? -11.680 23.137 -0.348  1.00 44.23  ?  432 VAL C N   1 
ATOM   6301 C CA  . VAL C 1 277 ? -12.013 21.982 0.497   1.00 43.96  ?  432 VAL C CA  1 
ATOM   6302 C C   . VAL C 1 277 ? -13.242 22.338 1.358   1.00 48.96  ?  432 VAL C C   1 
ATOM   6303 O O   . VAL C 1 277 ? -14.187 21.556 1.408   1.00 50.49  ?  432 VAL C O   1 
ATOM   6304 C CB  . VAL C 1 277 ? -10.817 21.521 1.375   1.00 48.02  ?  432 VAL C CB  1 
ATOM   6305 C CG1 . VAL C 1 277 ? -11.165 20.278 2.171   1.00 48.15  ?  432 VAL C CG1 1 
ATOM   6306 C CG2 . VAL C 1 277 ? -9.559  21.279 0.551   1.00 47.40  ?  432 VAL C CG2 1 
ATOM   6307 N N   . ALA C 1 278 ? -13.242 23.539 1.987   1.00 43.76  ?  433 ALA C N   1 
ATOM   6308 C CA  . ALA C 1 278 ? -14.326 24.031 2.835   1.00 42.60  ?  433 ALA C CA  1 
ATOM   6309 C C   . ALA C 1 278 ? -15.638 24.112 2.064   1.00 51.10  ?  433 ALA C C   1 
ATOM   6310 O O   . ALA C 1 278 ? -16.661 23.661 2.579   1.00 52.47  ?  433 ALA C O   1 
ATOM   6311 C CB  . ALA C 1 278 ? -13.974 25.393 3.416   1.00 42.62  ?  433 ALA C CB  1 
ATOM   6312 N N   . SER C 1 279 ? -15.625 24.658 0.820   1.00 48.22  ?  434 SER C N   1 
ATOM   6313 C CA  . SER C 1 279 ? -16.850 24.785 0.035   1.00 46.71  ?  434 SER C CA  1 
ATOM   6314 C C   . SER C 1 279 ? -17.362 23.420 -0.421  1.00 51.59  ?  434 SER C C   1 
ATOM   6315 O O   . SER C 1 279 ? -18.576 23.233 -0.487  1.00 53.10  ?  434 SER C O   1 
ATOM   6316 C CB  . SER C 1 279 ? -16.685 25.771 -1.111  1.00 48.69  ?  434 SER C CB  1 
ATOM   6317 O OG  . SER C 1 279 ? -15.769 25.279 -2.071  1.00 59.62  ?  434 SER C OG  1 
ATOM   6318 N N   . GLN C 1 280 ? -16.455 22.444 -0.643  1.00 46.72  ?  435 GLN C N   1 
ATOM   6319 C CA  . GLN C 1 280 ? -16.841 21.080 -0.998  1.00 46.16  ?  435 GLN C CA  1 
ATOM   6320 C C   . GLN C 1 280 ? -17.506 20.448 0.218   1.00 49.39  ?  435 GLN C C   1 
ATOM   6321 O O   . GLN C 1 280 ? -18.526 19.788 0.080   1.00 50.59  ?  435 GLN C O   1 
ATOM   6322 C CB  . GLN C 1 280 ? -15.627 20.255 -1.442  1.00 47.44  ?  435 GLN C CB  1 
ATOM   6323 C CG  . GLN C 1 280 ? -15.243 20.485 -2.884  1.00 60.72  ?  435 GLN C CG  1 
ATOM   6324 C CD  . GLN C 1 280 ? -13.882 19.900 -3.192  1.00 86.78  ?  435 GLN C CD  1 
ATOM   6325 O OE1 . GLN C 1 280 ? -12.851 20.590 -3.107  1.00 87.72  ?  435 GLN C OE1 1 
ATOM   6326 N NE2 . GLN C 1 280 ? -13.850 18.624 -3.576  1.00 67.44  ?  435 GLN C NE2 1 
ATOM   6327 N N   . CYS C 1 281 ? -16.953 20.692 1.413   1.00 45.02  ?  436 CYS C N   1 
ATOM   6328 C CA  . CYS C 1 281 ? -17.496 20.223 2.697   1.00 44.43  ?  436 CYS C CA  1 
ATOM   6329 C C   . CYS C 1 281 ? -18.860 20.834 2.979   1.00 47.63  ?  436 CYS C C   1 
ATOM   6330 O O   . CYS C 1 281 ? -19.687 20.184 3.616   1.00 47.04  ?  436 CYS C O   1 
ATOM   6331 C CB  . CYS C 1 281 ? -16.534 20.546 3.836   1.00 43.85  ?  436 CYS C CB  1 
ATOM   6332 S SG  . CYS C 1 281 ? -15.029 19.560 3.826   1.00 47.49  ?  436 CYS C SG  1 
ATOM   6333 N N   . LEU C 1 282 ? -19.061 22.105 2.543   1.00 43.78  ?  437 LEU C N   1 
ATOM   6334 C CA  . LEU C 1 282 ? -20.232 22.922 2.840   1.00 43.79  ?  437 LEU C CA  1 
ATOM   6335 C C   . LEU C 1 282 ? -21.504 22.782 1.979   1.00 51.32  ?  437 LEU C C   1 
ATOM   6336 O O   . LEU C 1 282 ? -22.463 23.555 2.167   1.00 51.95  ?  437 LEU C O   1 
ATOM   6337 C CB  . LEU C 1 282 ? -19.839 24.374 3.116   1.00 43.17  ?  437 LEU C CB  1 
ATOM   6338 C CG  . LEU C 1 282 ? -18.998 24.601 4.378   1.00 47.06  ?  437 LEU C CG  1 
ATOM   6339 C CD1 . LEU C 1 282 ? -18.462 26.005 4.420   1.00 46.58  ?  437 LEU C CD1 1 
ATOM   6340 C CD2 . LEU C 1 282 ? -19.786 24.321 5.627   1.00 49.50  ?  437 LEU C CD2 1 
ATOM   6341 N N   . HIS C 1 283 ? -21.533 21.759 1.085   1.00 48.29  ?  438 HIS C N   1 
ATOM   6342 C CA  . HIS C 1 283 ? -22.687 21.425 0.251   1.00 47.78  ?  438 HIS C CA  1 
ATOM   6343 C C   . HIS C 1 283 ? -23.863 21.117 1.158   1.00 52.60  ?  438 HIS C C   1 
ATOM   6344 O O   . HIS C 1 283 ? -23.733 20.315 2.084   1.00 50.90  ?  438 HIS C O   1 
ATOM   6345 C CB  . HIS C 1 283 ? -22.424 20.152 -0.581  1.00 48.39  ?  438 HIS C CB  1 
ATOM   6346 C CG  . HIS C 1 283 ? -21.570 20.351 -1.789  1.00 51.91  ?  438 HIS C CG  1 
ATOM   6347 N ND1 . HIS C 1 283 ? -21.945 21.210 -2.808  1.00 53.50  ?  438 HIS C ND1 1 
ATOM   6348 C CD2 . HIS C 1 283 ? -20.417 19.734 -2.139  1.00 54.05  ?  438 HIS C CD2 1 
ATOM   6349 C CE1 . HIS C 1 283 ? -20.980 21.139 -3.711  1.00 53.07  ?  438 HIS C CE1 1 
ATOM   6350 N NE2 . HIS C 1 283 ? -20.041 20.259 -3.356  1.00 53.73  ?  438 HIS C NE2 1 
ATOM   6351 N N   . GLU C 1 284 ? -25.014 21.738 0.875   1.00 51.88  ?  439 GLU C N   1 
ATOM   6352 C CA  . GLU C 1 284 ? -26.288 21.510 1.557   1.00 52.35  ?  439 GLU C CA  1 
ATOM   6353 C C   . GLU C 1 284 ? -26.733 20.046 1.364   1.00 56.24  ?  439 GLU C C   1 
ATOM   6354 O O   . GLU C 1 284 ? -27.335 19.479 2.276   1.00 57.00  ?  439 GLU C O   1 
ATOM   6355 C CB  . GLU C 1 284 ? -27.346 22.489 1.019   1.00 53.78  ?  439 GLU C CB  1 
ATOM   6356 C CG  . GLU C 1 284 ? -27.667 23.647 1.959   1.00 65.77  ?  439 GLU C CG  1 
ATOM   6357 C CD  . GLU C 1 284 ? -26.513 24.409 2.585   1.00 92.17  ?  439 GLU C CD  1 
ATOM   6358 O OE1 . GLU C 1 284 ? -25.568 24.787 1.854   1.00 101.55 ?  439 GLU C OE1 1 
ATOM   6359 O OE2 . GLU C 1 284 ? -26.570 24.652 3.812   1.00 85.97  -1 439 GLU C OE2 1 
ATOM   6360 N N   . LYS C 1 285 ? -26.367 19.432 0.206   1.00 51.11  ?  440 LYS C N   1 
ATOM   6361 C CA  . LYS C 1 285 ? -26.635 18.044 -0.147  1.00 50.48  ?  440 LYS C CA  1 
ATOM   6362 C C   . LYS C 1 285 ? -25.557 17.104 0.371   1.00 54.70  ?  440 LYS C C   1 
ATOM   6363 O O   . LYS C 1 285 ? -24.449 17.029 -0.178  1.00 55.78  ?  440 LYS C O   1 
ATOM   6364 C CB  . LYS C 1 285 ? -26.838 17.887 -1.658  1.00 53.41  ?  440 LYS C CB  1 
ATOM   6365 N N   . LYS C 1 286 ? -25.913 16.371 1.436   1.00 50.92  ?  441 LYS C N   1 
ATOM   6366 C CA  . LYS C 1 286 ? -25.090 15.388 2.150   1.00 50.75  ?  441 LYS C CA  1 
ATOM   6367 C C   . LYS C 1 286 ? -24.185 14.558 1.271   1.00 55.09  ?  441 LYS C C   1 
ATOM   6368 O O   . LYS C 1 286 ? -23.001 14.481 1.556   1.00 56.35  ?  441 LYS C O   1 
ATOM   6369 C CB  . LYS C 1 286 ? -25.965 14.476 3.034   1.00 53.11  ?  441 LYS C CB  1 
ATOM   6370 N N   . ASN C 1 287 ? -24.727 13.963 0.196   1.00 52.40  ?  442 ASN C N   1 
ATOM   6371 C CA  . ASN C 1 287 ? -24.013 13.082 -0.741  1.00 52.53  ?  442 ASN C CA  1 
ATOM   6372 C C   . ASN C 1 287 ? -23.120 13.794 -1.765  1.00 53.46  ?  442 ASN C C   1 
ATOM   6373 O O   . ASN C 1 287 ? -22.312 13.144 -2.441  1.00 52.30  ?  442 ASN C O   1 
ATOM   6374 C CB  . ASN C 1 287 ? -24.981 12.077 -1.396  1.00 61.21  ?  442 ASN C CB  1 
ATOM   6375 C CG  . ASN C 1 287 ? -25.600 11.080 -0.422  1.00 100.52 ?  442 ASN C CG  1 
ATOM   6376 O OD1 . ASN C 1 287 ? -26.085 11.438 0.663   1.00 91.78  ?  442 ASN C OD1 1 
ATOM   6377 N ND2 . ASN C 1 287 ? -25.610 9.798  -0.798  1.00 99.16  ?  442 ASN C ND2 1 
ATOM   6378 N N   . LYS C 1 288 ? -23.224 15.131 -1.843  1.00 49.65  ?  443 LYS C N   1 
ATOM   6379 C CA  . LYS C 1 288 ? -22.379 15.941 -2.735  1.00 49.56  ?  443 LYS C CA  1 
ATOM   6380 C C   . LYS C 1 288 ? -21.007 16.274 -2.077  1.00 55.30  ?  443 LYS C C   1 
ATOM   6381 O O   . LYS C 1 288 ? -20.065 16.640 -2.781  1.00 56.65  ?  443 LYS C O   1 
ATOM   6382 C CB  . LYS C 1 288 ? -23.115 17.216 -3.183  1.00 50.91  ?  443 LYS C CB  1 
ATOM   6383 N N   . ARG C 1 289 ? -20.902 16.124 -0.734  1.00 49.76  ?  444 ARG C N   1 
ATOM   6384 C CA  . ARG C 1 289 ? -19.710 16.404 0.075   1.00 47.80  ?  444 ARG C CA  1 
ATOM   6385 C C   . ARG C 1 289 ? -18.660 15.298 -0.066  1.00 50.71  ?  444 ARG C C   1 
ATOM   6386 O O   . ARG C 1 289 ? -19.034 14.131 -0.213  1.00 50.83  ?  444 ARG C O   1 
ATOM   6387 C CB  . ARG C 1 289 ? -20.090 16.499 1.564   1.00 45.80  ?  444 ARG C CB  1 
ATOM   6388 C CG  . ARG C 1 289 ? -21.003 17.628 1.925   1.00 49.78  ?  444 ARG C CG  1 
ATOM   6389 C CD  . ARG C 1 289 ? -21.529 17.405 3.317   1.00 40.98  ?  444 ARG C CD  1 
ATOM   6390 N NE  . ARG C 1 289 ? -22.798 18.090 3.495   1.00 44.55  ?  444 ARG C NE  1 
ATOM   6391 C CZ  . ARG C 1 289 ? -23.644 17.824 4.474   1.00 57.91  ?  444 ARG C CZ  1 
ATOM   6392 N NH1 . ARG C 1 289 ? -23.355 16.887 5.370   1.00 52.55  ?  444 ARG C NH1 1 
ATOM   6393 N NH2 . ARG C 1 289 ? -24.796 18.477 4.556   1.00 35.32  1  444 ARG C NH2 1 
ATOM   6394 N N   . PRO C 1 290 ? -17.349 15.617 0.090   1.00 46.21  ?  445 PRO C N   1 
ATOM   6395 C CA  . PRO C 1 290 ? -16.336 14.556 0.034   1.00 45.61  ?  445 PRO C CA  1 
ATOM   6396 C C   . PRO C 1 290 ? -16.305 13.744 1.327   1.00 50.38  ?  445 PRO C C   1 
ATOM   6397 O O   . PRO C 1 290 ? -16.800 14.196 2.361   1.00 49.88  ?  445 PRO C O   1 
ATOM   6398 C CB  . PRO C 1 290 ? -15.022 15.333 -0.150  1.00 47.13  ?  445 PRO C CB  1 
ATOM   6399 C CG  . PRO C 1 290 ? -15.265 16.654 0.438   1.00 51.49  ?  445 PRO C CG  1 
ATOM   6400 C CD  . PRO C 1 290 ? -16.731 16.942 0.323   1.00 47.79  ?  445 PRO C CD  1 
ATOM   6401 N N   . ASP C 1 291 ? -15.706 12.552 1.279   1.00 47.50  ?  446 ASP C N   1 
ATOM   6402 C CA  . ASP C 1 291 ? -15.543 11.765 2.487   1.00 47.03  ?  446 ASP C CA  1 
ATOM   6403 C C   . ASP C 1 291 ? -14.233 12.222 3.142   1.00 51.79  ?  446 ASP C C   1 
ATOM   6404 O O   . ASP C 1 291 ? -13.420 12.897 2.496   1.00 50.64  ?  446 ASP C O   1 
ATOM   6405 C CB  . ASP C 1 291 ? -15.600 10.249 2.220   1.00 48.88  ?  446 ASP C CB  1 
ATOM   6406 C CG  . ASP C 1 291 ? -14.582 9.659  1.266   1.00 70.74  ?  446 ASP C CG  1 
ATOM   6407 O OD1 . ASP C 1 291 ? -13.922 10.434 0.537   1.00 73.96  ?  446 ASP C OD1 1 
ATOM   6408 O OD2 . ASP C 1 291 ? -14.479 8.414  1.208   1.00 81.94  -1 446 ASP C OD2 1 
ATOM   6409 N N   . ILE C 1 292 ? -14.044 11.887 4.431   1.00 48.23  ?  447 ILE C N   1 
ATOM   6410 C CA  . ILE C 1 292 ? -12.870 12.294 5.198   1.00 45.88  ?  447 ILE C CA  1 
ATOM   6411 C C   . ILE C 1 292 ? -11.527 11.981 4.562   1.00 48.08  ?  447 ILE C C   1 
ATOM   6412 O O   . ILE C 1 292 ? -10.682 12.879 4.540   1.00 49.29  ?  447 ILE C O   1 
ATOM   6413 C CB  . ILE C 1 292 ? -12.999 12.000 6.714   1.00 48.00  ?  447 ILE C CB  1 
ATOM   6414 C CG1 . ILE C 1 292 ? -12.041 12.873 7.579   1.00 46.99  ?  447 ILE C CG1 1 
ATOM   6415 C CG2 . ILE C 1 292 ? -12.961 10.508 7.032   1.00 48.44  ?  447 ILE C CG2 1 
ATOM   6416 C CD1 . ILE C 1 292 ? -12.346 14.399 7.537   1.00 41.47  ?  447 ILE C CD1 1 
ATOM   6417 N N   . LYS C 1 293 ? -11.347 10.772 3.965   1.00 42.64  ?  448 LYS C N   1 
ATOM   6418 C CA  . LYS C 1 293 ? -10.084 10.423 3.274   1.00 41.41  ?  448 LYS C CA  1 
ATOM   6419 C C   . LYS C 1 293 ? -9.805  11.392 2.119   1.00 44.19  ?  448 LYS C C   1 
ATOM   6420 O O   . LYS C 1 293 ? -8.656  11.751 1.911   1.00 42.89  ?  448 LYS C O   1 
ATOM   6421 C CB  . LYS C 1 293 ? -10.026 8.947  2.817   1.00 42.26  ?  448 LYS C CB  1 
ATOM   6422 N N   . LYS C 1 294 ? -10.861 11.864 1.416   1.00 42.15  ?  449 LYS C N   1 
ATOM   6423 C CA  . LYS C 1 294 ? -10.711 12.838 0.329   1.00 42.86  ?  449 LYS C CA  1 
ATOM   6424 C C   . LYS C 1 294 ? -10.267 14.184 0.912   1.00 48.26  ?  449 LYS C C   1 
ATOM   6425 O O   . LYS C 1 294 ? -9.311  14.774 0.404   1.00 47.46  ?  449 LYS C O   1 
ATOM   6426 C CB  . LYS C 1 294 ? -12.008 12.976 -0.505  1.00 45.02  ?  449 LYS C CB  1 
ATOM   6427 C CG  . LYS C 1 294 ? -11.936 13.931 -1.708  1.00 59.50  ?  449 LYS C CG  1 
ATOM   6428 C CD  . LYS C 1 294 ? -10.926 13.505 -2.784  1.00 77.03  ?  449 LYS C CD  1 
ATOM   6429 C CE  . LYS C 1 294 ? -10.837 14.518 -3.895  1.00 96.90  ?  449 LYS C CE  1 
ATOM   6430 N NZ  . LYS C 1 294 ? -9.701  14.232 -4.809  1.00 110.76 1  449 LYS C NZ  1 
ATOM   6431 N N   . VAL C 1 295 ? -10.938 14.632 2.003   1.00 45.26  ?  450 VAL C N   1 
ATOM   6432 C CA  . VAL C 1 295 ? -10.621 15.852 2.744   1.00 45.17  ?  450 VAL C CA  1 
ATOM   6433 C C   . VAL C 1 295 ? -9.122  15.836 3.177   1.00 48.55  ?  450 VAL C C   1 
ATOM   6434 O O   . VAL C 1 295 ? -8.407  16.823 2.947   1.00 48.08  ?  450 VAL C O   1 
ATOM   6435 C CB  . VAL C 1 295 ? -11.601 16.081 3.933   1.00 49.16  ?  450 VAL C CB  1 
ATOM   6436 C CG1 . VAL C 1 295 ? -11.215 17.313 4.747   1.00 49.05  ?  450 VAL C CG1 1 
ATOM   6437 C CG2 . VAL C 1 295 ? -13.041 16.200 3.449   1.00 48.62  ?  450 VAL C CG2 1 
ATOM   6438 N N   . GLN C 1 296 ? -8.640  14.697 3.720   1.00 44.27  ?  451 GLN C N   1 
ATOM   6439 C CA  . GLN C 1 296 ? -7.235  14.537 4.116   1.00 44.24  ?  451 GLN C CA  1 
ATOM   6440 C C   . GLN C 1 296 ? -6.323  14.676 2.907   1.00 51.57  ?  451 GLN C C   1 
ATOM   6441 O O   . GLN C 1 296 ? -5.304  15.362 2.995   1.00 52.40  ?  451 GLN C O   1 
ATOM   6442 C CB  . GLN C 1 296 ? -6.978  13.149 4.693   1.00 45.34  ?  451 GLN C CB  1 
ATOM   6443 C CG  . GLN C 1 296 ? -7.501  12.870 6.064   1.00 47.79  ?  451 GLN C CG  1 
ATOM   6444 C CD  . GLN C 1 296 ? -6.874  11.558 6.486   1.00 71.85  ?  451 GLN C CD  1 
ATOM   6445 O OE1 . GLN C 1 296 ? -7.324  10.448 5.895   1.00 69.99  ?  451 GLN C OE1 1 
ATOM   6446 N NE2 . GLN C 1 296 ? -5.897  11.523 7.244   1.00 66.93  ?  451 GLN C NE2 1 
ATOM   6447 N N   . GLN C 1 297 ? -6.672  13.982 1.784   1.00 49.90  ?  452 GLN C N   1 
ATOM   6448 C CA  . GLN C 1 297 ? -5.902  13.984 0.542   1.00 49.87  ?  452 GLN C CA  1 
ATOM   6449 C C   . GLN C 1 297 ? -5.768  15.411 0.023   1.00 54.75  ?  452 GLN C C   1 
ATOM   6450 O O   . GLN C 1 297 ? -4.649  15.861 -0.235  1.00 56.08  ?  452 GLN C O   1 
ATOM   6451 C CB  . GLN C 1 297 ? -6.526  13.057 -0.515  1.00 50.74  ?  452 GLN C CB  1 
ATOM   6452 N N   . LEU C 1 298 ? -6.893  16.141 -0.035  1.00 49.50  ?  453 LEU C N   1 
ATOM   6453 C CA  . LEU C 1 298 ? -6.914  17.511 -0.492  1.00 49.03  ?  453 LEU C CA  1 
ATOM   6454 C C   . LEU C 1 298 ? -6.064  18.420 0.420   1.00 54.52  ?  453 LEU C C   1 
ATOM   6455 O O   . LEU C 1 298 ? -5.285  19.244 -0.100  1.00 55.56  ?  453 LEU C O   1 
ATOM   6456 C CB  . LEU C 1 298 ? -8.358  18.008 -0.603  1.00 49.14  ?  453 LEU C CB  1 
ATOM   6457 C CG  . LEU C 1 298 ? -9.248  17.323 -1.662  1.00 53.20  ?  453 LEU C CG  1 
ATOM   6458 C CD1 . LEU C 1 298 ? -10.729 17.684 -1.462  1.00 52.19  ?  453 LEU C CD1 1 
ATOM   6459 C CD2 . LEU C 1 298 ? -8.788  17.641 -3.070  1.00 54.65  ?  453 LEU C CD2 1 
ATOM   6460 N N   . LEU C 1 299 ? -6.150  18.207 1.769   1.00 48.03  ?  454 LEU C N   1 
ATOM   6461 C CA  . LEU C 1 299 ? -5.385  19.004 2.733   1.00 46.14  ?  454 LEU C CA  1 
ATOM   6462 C C   . LEU C 1 299 ? -3.905  18.728 2.679   1.00 51.18  ?  454 LEU C C   1 
ATOM   6463 O O   . LEU C 1 299 ? -3.122  19.647 2.896   1.00 50.98  ?  454 LEU C O   1 
ATOM   6464 C CB  . LEU C 1 299 ? -5.920  18.892 4.173   1.00 45.15  ?  454 LEU C CB  1 
ATOM   6465 C CG  . LEU C 1 299 ? -7.259  19.565 4.481   1.00 46.59  ?  454 LEU C CG  1 
ATOM   6466 C CD1 . LEU C 1 299 ? -7.926  18.898 5.646   1.00 46.01  ?  454 LEU C CD1 1 
ATOM   6467 C CD2 . LEU C 1 299 ? -7.108  21.039 4.725   1.00 43.24  ?  454 LEU C CD2 1 
ATOM   6468 N N   . GLN C 1 300 ? -3.511  17.482 2.380   1.00 50.80  ?  455 GLN C N   1 
ATOM   6469 C CA  . GLN C 1 300 ? -2.101  17.085 2.240   1.00 51.72  ?  455 GLN C CA  1 
ATOM   6470 C C   . GLN C 1 300 ? -1.518  17.688 0.951   1.00 58.38  ?  455 GLN C C   1 
ATOM   6471 O O   . GLN C 1 300 ? -0.400  18.203 0.981   1.00 57.86  ?  455 GLN C O   1 
ATOM   6472 C CB  . GLN C 1 300 ? -1.944  15.557 2.268   1.00 52.86  ?  455 GLN C CB  1 
ATOM   6473 N N   . GLU C 1 301 ? -2.320  17.693 -0.144  1.00 57.30  ?  456 GLU C N   1 
ATOM   6474 C CA  . GLU C 1 301 ? -1.979  18.257 -1.453  1.00 58.38  ?  456 GLU C CA  1 
ATOM   6475 C C   . GLU C 1 301 ? -1.710  19.757 -1.365  1.00 64.52  ?  456 GLU C C   1 
ATOM   6476 O O   . GLU C 1 301 ? -0.812  20.263 -2.037  1.00 64.82  ?  456 GLU C O   1 
ATOM   6477 C CB  . GLU C 1 301 ? -3.112  17.999 -2.462  1.00 59.78  ?  456 GLU C CB  1 
ATOM   6478 C CG  . GLU C 1 301 ? -3.053  16.630 -3.125  1.00 69.21  ?  456 GLU C CG  1 
ATOM   6479 C CD  . GLU C 1 301 ? -4.358  16.096 -3.697  1.00 92.03  ?  456 GLU C CD  1 
ATOM   6480 O OE1 . GLU C 1 301 ? -5.254  16.898 -4.061  1.00 70.81  ?  456 GLU C OE1 1 
ATOM   6481 O OE2 . GLU C 1 301 ? -4.472  14.851 -3.789  1.00 88.15  -1 456 GLU C OE2 1 
ATOM   6482 N N   . MET C 1 302 ? -2.497  20.452 -0.529  1.00 62.19  ?  457 MET C N   1 
ATOM   6483 C CA  . MET C 1 302 ? -2.474  21.899 -0.267  1.00 61.86  ?  457 MET C CA  1 
ATOM   6484 C C   . MET C 1 302 ? -1.078  22.449 0.159   1.00 65.24  ?  457 MET C C   1 
ATOM   6485 O O   . MET C 1 302 ? -0.761  23.612 -0.129  1.00 65.42  ?  457 MET C O   1 
ATOM   6486 C CB  . MET C 1 302 ? -3.606  22.220 0.735   1.00 64.22  ?  457 MET C CB  1 
ATOM   6487 C CG  . MET C 1 302 ? -3.681  23.639 1.217   1.00 68.25  ?  457 MET C CG  1 
ATOM   6488 S SD  . MET C 1 302 ? -3.394  23.633 2.991   1.00 72.97  ?  457 MET C SD  1 
ATOM   6489 C CE  . MET C 1 302 ? -4.961  23.775 3.554   1.00 69.08  ?  457 MET C CE  1 
ATOM   6490 N N   . THR C 1 303 ? -0.238  21.602 0.779   1.00 60.37  ?  458 THR C N   1 
ATOM   6491 C CA  . THR C 1 303 ? 1.103   21.987 1.239   1.00 81.36  ?  458 THR C CA  1 
ATOM   6492 C C   . THR C 1 303 ? 2.235   21.413 0.370   1.00 119.59 ?  458 THR C C   1 
ATOM   6493 O O   . THR C 1 303 ? 2.211   20.246 -0.028  1.00 83.10  ?  458 THR C O   1 
ATOM   6494 C CB  . THR C 1 303 ? 1.278   21.701 2.744   1.00 87.21  ?  458 THR C CB  1 
ATOM   6495 O OG1 . THR C 1 303 ? 0.965   20.332 3.017   1.00 91.86  ?  458 THR C OG1 1 
ATOM   6496 C CG2 . THR C 1 303 ? 0.429   22.616 3.618   1.00 81.68  ?  458 THR C CG2 1 
ATOM   6497 N N   . ARG D 1 9   ? 15.786  88.576 38.577  1.00 90.53  ?  164 ARG D N   1 
ATOM   6498 C CA  . ARG D 1 9   ? 16.171  87.664 37.499  1.00 90.38  ?  164 ARG D CA  1 
ATOM   6499 C C   . ARG D 1 9   ? 15.655  86.231 37.753  1.00 92.99  ?  164 ARG D C   1 
ATOM   6500 O O   . ARG D 1 9   ? 14.969  85.658 36.899  1.00 92.39  ?  164 ARG D O   1 
ATOM   6501 C CB  . ARG D 1 9   ? 17.708  87.660 37.299  1.00 92.01  ?  164 ARG D CB  1 
ATOM   6502 C CG  . ARG D 1 9   ? 18.173  88.270 35.976  1.00 104.63 ?  164 ARG D CG  1 
ATOM   6503 C CD  . ARG D 1 9   ? 18.888  87.255 35.104  1.00 113.79 ?  164 ARG D CD  1 
ATOM   6504 N NE  . ARG D 1 9   ? 18.162  86.996 33.857  1.00 119.20 ?  164 ARG D NE  1 
ATOM   6505 C CZ  . ARG D 1 9   ? 17.186  86.101 33.716  1.00 127.68 ?  164 ARG D CZ  1 
ATOM   6506 N NH1 . ARG D 1 9   ? 16.792  85.366 34.750  1.00 108.30 ?  164 ARG D NH1 1 
ATOM   6507 N NH2 . ARG D 1 9   ? 16.588  85.943 32.542  1.00 114.70 1  164 ARG D NH2 1 
ATOM   6508 N N   . PHE D 1 10  ? 16.003  85.661 38.925  1.00 87.96  ?  165 PHE D N   1 
ATOM   6509 C CA  . PHE D 1 10  ? 15.625  84.318 39.360  1.00 86.56  ?  165 PHE D CA  1 
ATOM   6510 C C   . PHE D 1 10  ? 14.776  84.403 40.622  1.00 88.73  ?  165 PHE D C   1 
ATOM   6511 O O   . PHE D 1 10  ? 14.995  85.290 41.449  1.00 88.37  ?  165 PHE D O   1 
ATOM   6512 C CB  . PHE D 1 10  ? 16.884  83.474 39.641  1.00 88.07  ?  165 PHE D CB  1 
ATOM   6513 C CG  . PHE D 1 10  ? 17.868  83.355 38.496  1.00 89.56  ?  165 PHE D CG  1 
ATOM   6514 C CD1 . PHE D 1 10  ? 17.497  82.749 37.297  1.00 92.73  ?  165 PHE D CD1 1 
ATOM   6515 C CD2 . PHE D 1 10  ? 19.182  83.800 38.633  1.00 91.73  ?  165 PHE D CD2 1 
ATOM   6516 C CE1 . PHE D 1 10  ? 18.407  82.629 36.239  1.00 93.45  ?  165 PHE D CE1 1 
ATOM   6517 C CE2 . PHE D 1 10  ? 20.095  83.676 37.573  1.00 94.60  ?  165 PHE D CE2 1 
ATOM   6518 C CZ  . PHE D 1 10  ? 19.700  83.089 36.385  1.00 92.73  ?  165 PHE D CZ  1 
ATOM   6519 N N   . HIS D 1 11  ? 13.824  83.472 40.783  1.00 84.12  ?  166 HIS D N   1 
ATOM   6520 C CA  . HIS D 1 11  ? 12.961  83.433 41.962  1.00 83.58  ?  166 HIS D CA  1 
ATOM   6521 C C   . HIS D 1 11  ? 13.728  82.952 43.192  1.00 82.52  ?  166 HIS D C   1 
ATOM   6522 O O   . HIS D 1 11  ? 14.387  81.920 43.135  1.00 81.28  ?  166 HIS D O   1 
ATOM   6523 C CB  . HIS D 1 11  ? 11.709  82.569 41.720  1.00 85.29  ?  166 HIS D CB  1 
ATOM   6524 C CG  . HIS D 1 11  ? 10.805  82.497 42.915  1.00 89.62  ?  166 HIS D CG  1 
ATOM   6525 N ND1 . HIS D 1 11  ? 10.798  81.389 43.749  1.00 92.08  ?  166 HIS D ND1 1 
ATOM   6526 C CD2 . HIS D 1 11  ? 9.967   83.431 43.425  1.00 91.86  ?  166 HIS D CD2 1 
ATOM   6527 C CE1 . HIS D 1 11  ? 9.926   81.659 44.708  1.00 91.69  ?  166 HIS D CE1 1 
ATOM   6528 N NE2 . HIS D 1 11  ? 9.403   82.880 44.559  1.00 91.96  ?  166 HIS D NE2 1 
ATOM   6529 N N   . SER D 1 12  ? 13.661  83.707 44.293  1.00 76.47  ?  167 SER D N   1 
ATOM   6530 C CA  . SER D 1 12  ? 14.336  83.285 45.509  1.00 74.96  ?  167 SER D CA  1 
ATOM   6531 C C   . SER D 1 12  ? 13.422  82.361 46.290  1.00 76.39  ?  167 SER D C   1 
ATOM   6532 O O   . SER D 1 12  ? 12.283  82.718 46.602  1.00 76.32  ?  167 SER D O   1 
ATOM   6533 C CB  . SER D 1 12  ? 14.781  84.471 46.357  1.00 77.14  ?  167 SER D CB  1 
ATOM   6534 O OG  . SER D 1 12  ? 15.639  84.004 47.387  1.00 83.54  ?  167 SER D OG  1 
ATOM   6535 N N   . PHE D 1 13  ? 13.905  81.141 46.540  1.00 70.08  ?  168 PHE D N   1 
ATOM   6536 C CA  . PHE D 1 13  ? 13.171  80.140 47.293  1.00 68.51  ?  168 PHE D CA  1 
ATOM   6537 C C   . PHE D 1 13  ? 13.727  80.109 48.701  1.00 75.74  ?  168 PHE D C   1 
ATOM   6538 O O   . PHE D 1 13  ? 14.904  80.423 48.934  1.00 75.69  ?  168 PHE D O   1 
ATOM   6539 C CB  . PHE D 1 13  ? 13.301  78.734 46.657  1.00 68.51  ?  168 PHE D CB  1 
ATOM   6540 C CG  . PHE D 1 13  ? 12.582  78.539 45.343  1.00 67.87  ?  168 PHE D CG  1 
ATOM   6541 C CD1 . PHE D 1 13  ? 11.214  78.289 45.308  1.00 69.47  ?  168 PHE D CD1 1 
ATOM   6542 C CD2 . PHE D 1 13  ? 13.277  78.565 44.144  1.00 68.40  ?  168 PHE D CD2 1 
ATOM   6543 C CE1 . PHE D 1 13  ? 10.556  78.082 44.094  1.00 70.09  ?  168 PHE D CE1 1 
ATOM   6544 C CE2 . PHE D 1 13  ? 12.618  78.371 42.928  1.00 70.85  ?  168 PHE D CE2 1 
ATOM   6545 C CZ  . PHE D 1 13  ? 11.263  78.136 42.909  1.00 69.08  ?  168 PHE D CZ  1 
ATOM   6546 N N   . SER D 1 14  ? 12.878  79.742 49.643  1.00 74.11  ?  169 SER D N   1 
ATOM   6547 C CA  . SER D 1 14  ? 13.296  79.575 51.012  1.00 74.88  ?  169 SER D CA  1 
ATOM   6548 C C   . SER D 1 14  ? 13.576  78.088 51.140  1.00 78.33  ?  169 SER D C   1 
ATOM   6549 O O   . SER D 1 14  ? 12.851  77.281 50.548  1.00 78.21  ?  169 SER D O   1 
ATOM   6550 C CB  . SER D 1 14  ? 12.191  80.018 51.958  1.00 80.98  ?  169 SER D CB  1 
ATOM   6551 O OG  . SER D 1 14  ? 12.674  80.075 53.290  1.00 95.79  ?  169 SER D OG  1 
ATOM   6552 N N   . PHE D 1 15  ? 14.646  77.722 51.863  1.00 74.40  ?  170 PHE D N   1 
ATOM   6553 C CA  . PHE D 1 15  ? 15.040  76.324 52.043  1.00 74.56  ?  170 PHE D CA  1 
ATOM   6554 C C   . PHE D 1 15  ? 13.873  75.382 52.427  1.00 77.81  ?  170 PHE D C   1 
ATOM   6555 O O   . PHE D 1 15  ? 13.845  74.229 51.971  1.00 77.03  ?  170 PHE D O   1 
ATOM   6556 C CB  . PHE D 1 15  ? 16.244  76.195 53.009  1.00 76.52  ?  170 PHE D CB  1 
ATOM   6557 C CG  . PHE D 1 15  ? 16.659  74.769 53.281  1.00 77.98  ?  170 PHE D CG  1 
ATOM   6558 C CD1 . PHE D 1 15  ? 16.335  74.150 54.484  1.00 81.22  ?  170 PHE D CD1 1 
ATOM   6559 C CD2 . PHE D 1 15  ? 17.298  74.015 52.301  1.00 79.94  ?  170 PHE D CD2 1 
ATOM   6560 C CE1 . PHE D 1 15  ? 16.672  72.813 54.714  1.00 82.09  ?  170 PHE D CE1 1 
ATOM   6561 C CE2 . PHE D 1 15  ? 17.629  72.678 52.531  1.00 82.79  ?  170 PHE D CE2 1 
ATOM   6562 C CZ  . PHE D 1 15  ? 17.318  72.087 53.739  1.00 81.01  ?  170 PHE D CZ  1 
ATOM   6563 N N   . TYR D 1 16  ? 12.905  75.892 53.235  1.00 73.84  ?  171 TYR D N   1 
ATOM   6564 C CA  . TYR D 1 16  ? 11.718  75.136 53.670  1.00 73.06  ?  171 TYR D CA  1 
ATOM   6565 C C   . TYR D 1 16  ? 10.815  74.691 52.512  1.00 73.49  ?  171 TYR D C   1 
ATOM   6566 O O   . TYR D 1 16  ? 10.298  73.576 52.541  1.00 72.03  ?  171 TYR D O   1 
ATOM   6567 C CB  . TYR D 1 16  ? 10.913  75.891 54.757  1.00 74.16  ?  171 TYR D CB  1 
ATOM   6568 C CG  . TYR D 1 16  ? 10.034  77.038 54.284  1.00 75.29  ?  171 TYR D CG  1 
ATOM   6569 C CD1 . TYR D 1 16  ? 8.781   76.799 53.726  1.00 77.44  ?  171 TYR D CD1 1 
ATOM   6570 C CD2 . TYR D 1 16  ? 10.399  78.361 54.512  1.00 75.44  ?  171 TYR D CD2 1 
ATOM   6571 C CE1 . TYR D 1 16  ? 7.972   77.848 53.287  1.00 78.15  ?  171 TYR D CE1 1 
ATOM   6572 C CE2 . TYR D 1 16  ? 9.585   79.420 54.098  1.00 75.84  ?  171 TYR D CE2 1 
ATOM   6573 C CZ  . TYR D 1 16  ? 8.377   79.157 53.477  1.00 82.42  ?  171 TYR D CZ  1 
ATOM   6574 O OH  . TYR D 1 16  ? 7.562   80.184 53.068  1.00 81.95  ?  171 TYR D OH  1 
ATOM   6575 N N   . GLU D 1 17  ? 10.640  75.572 51.496  1.00 68.85  ?  172 GLU D N   1 
ATOM   6576 C CA  . GLU D 1 17  ? 9.797   75.313 50.328  1.00 68.19  ?  172 GLU D CA  1 
ATOM   6577 C C   . GLU D 1 17  ? 10.341  74.107 49.603  1.00 72.34  ?  172 GLU D C   1 
ATOM   6578 O O   . GLU D 1 17  ? 9.587   73.211 49.235  1.00 71.89  ?  172 GLU D O   1 
ATOM   6579 C CB  . GLU D 1 17  ? 9.814   76.506 49.346  1.00 69.28  ?  172 GLU D CB  1 
ATOM   6580 C CG  . GLU D 1 17  ? 9.303   77.823 49.889  1.00 77.88  ?  172 GLU D CG  1 
ATOM   6581 C CD  . GLU D 1 17  ? 9.301   78.927 48.853  1.00 92.34  ?  172 GLU D CD  1 
ATOM   6582 O OE1 . GLU D 1 17  ? 8.659   78.759 47.790  1.00 78.89  ?  172 GLU D OE1 1 
ATOM   6583 O OE2 . GLU D 1 17  ? 9.958   79.962 49.104  1.00 86.82  -1 172 GLU D OE2 1 
ATOM   6584 N N   . LEU D 1 18  ? 11.669  74.080 49.432  1.00 68.57  ?  173 LEU D N   1 
ATOM   6585 C CA  . LEU D 1 18  ? 12.362  73.039 48.704  1.00 68.35  ?  173 LEU D CA  1 
ATOM   6586 C C   . LEU D 1 18  ? 12.360  71.699 49.393  1.00 73.40  ?  173 LEU D C   1 
ATOM   6587 O O   . LEU D 1 18  ? 12.369  70.666 48.712  1.00 72.23  ?  173 LEU D O   1 
ATOM   6588 C CB  . LEU D 1 18  ? 13.763  73.497 48.293  1.00 68.27  ?  173 LEU D CB  1 
ATOM   6589 C CG  . LEU D 1 18  ? 13.831  74.795 47.468  1.00 71.88  ?  173 LEU D CG  1 
ATOM   6590 C CD1 . LEU D 1 18  ? 15.241  75.075 47.047  1.00 71.95  ?  173 LEU D CD1 1 
ATOM   6591 C CD2 . LEU D 1 18  ? 12.889  74.757 46.252  1.00 71.48  ?  173 LEU D CD2 1 
ATOM   6592 N N   . LYS D 1 19  ? 12.303  71.708 50.744  1.00 71.56  ?  174 LYS D N   1 
ATOM   6593 C CA  . LYS D 1 19  ? 12.183  70.494 51.559  1.00 72.02  ?  174 LYS D CA  1 
ATOM   6594 C C   . LYS D 1 19  ? 10.818  69.890 51.247  1.00 75.81  ?  174 LYS D C   1 
ATOM   6595 O O   . LYS D 1 19  ? 10.716  68.691 51.002  1.00 74.50  ?  174 LYS D O   1 
ATOM   6596 C CB  . LYS D 1 19  ? 12.270  70.843 53.051  1.00 76.09  ?  174 LYS D CB  1 
ATOM   6597 C CG  . LYS D 1 19  ? 13.684  70.956 53.596  1.00 100.13 ?  174 LYS D CG  1 
ATOM   6598 C CD  . LYS D 1 19  ? 14.013  69.802 54.543  1.00 114.20 ?  174 LYS D CD  1 
ATOM   6599 C CE  . LYS D 1 19  ? 13.834  70.169 55.998  1.00 128.76 ?  174 LYS D CE  1 
ATOM   6600 N NZ  . LYS D 1 19  ? 14.011  68.985 56.880  1.00 138.08 1  174 LYS D NZ  1 
ATOM   6601 N N   . ASN D 1 20  ? 9.779   70.752 51.175  1.00 73.73  ?  175 ASN D N   1 
ATOM   6602 C CA  . ASN D 1 20  ? 8.414   70.330 50.865  1.00 73.85  ?  175 ASN D CA  1 
ATOM   6603 C C   . ASN D 1 20  ? 8.321   69.713 49.468  1.00 78.69  ?  175 ASN D C   1 
ATOM   6604 O O   . ASN D 1 20  ? 7.885   68.565 49.352  1.00 78.09  ?  175 ASN D O   1 
ATOM   6605 C CB  . ASN D 1 20  ? 7.407   71.486 51.039  1.00 72.91  ?  175 ASN D CB  1 
ATOM   6606 C CG  . ASN D 1 20  ? 7.318   72.089 52.426  1.00 79.38  ?  175 ASN D CG  1 
ATOM   6607 O OD1 . ASN D 1 20  ? 7.072   73.294 52.580  1.00 69.84  ?  175 ASN D OD1 1 
ATOM   6608 N ND2 . ASN D 1 20  ? 7.516   71.279 53.464  1.00 65.04  ?  175 ASN D ND2 1 
ATOM   6609 N N   . VAL D 1 21  ? 8.794   70.447 48.430  1.00 75.54  ?  176 VAL D N   1 
ATOM   6610 C CA  . VAL D 1 21  ? 8.749   70.019 47.028  1.00 75.50  ?  176 VAL D CA  1 
ATOM   6611 C C   . VAL D 1 21  ? 9.471   68.700 46.711  1.00 78.94  ?  176 VAL D C   1 
ATOM   6612 O O   . VAL D 1 21  ? 9.030   67.967 45.834  1.00 77.15  ?  176 VAL D O   1 
ATOM   6613 C CB  . VAL D 1 21  ? 9.076   71.145 46.002  1.00 79.71  ?  176 VAL D CB  1 
ATOM   6614 C CG1 . VAL D 1 21  ? 8.312   72.425 46.317  1.00 79.19  ?  176 VAL D CG1 1 
ATOM   6615 C CG2 . VAL D 1 21  ? 10.583  71.412 45.886  1.00 79.70  ?  176 VAL D CG2 1 
ATOM   6616 N N   . THR D 1 22  ? 10.558  68.400 47.438  1.00 77.28  ?  177 THR D N   1 
ATOM   6617 C CA  . THR D 1 22  ? 11.389  67.210 47.216  1.00 78.14  ?  177 THR D CA  1 
ATOM   6618 C C   . THR D 1 22  ? 11.094  66.038 48.159  1.00 85.54  ?  177 THR D C   1 
ATOM   6619 O O   . THR D 1 22  ? 11.908  65.108 48.234  1.00 85.46  ?  177 THR D O   1 
ATOM   6620 C CB  . THR D 1 22  ? 12.871  67.597 47.296  1.00 82.60  ?  177 THR D CB  1 
ATOM   6621 O OG1 . THR D 1 22  ? 13.139  68.100 48.603  1.00 80.51  ?  177 THR D OG1 1 
ATOM   6622 C CG2 . THR D 1 22  ? 13.287  68.600 46.217  1.00 80.48  ?  177 THR D CG2 1 
ATOM   6623 N N   . ASN D 1 23  ? 9.940   66.080 48.881  1.00 84.01  ?  178 ASN D N   1 
ATOM   6624 C CA  . ASN D 1 23  ? 9.517   65.063 49.858  1.00 84.04  ?  178 ASN D CA  1 
ATOM   6625 C C   . ASN D 1 23  ? 10.611  64.926 50.939  1.00 87.39  ?  178 ASN D C   1 
ATOM   6626 O O   . ASN D 1 23  ? 11.046  63.821 51.285  1.00 87.08  ?  178 ASN D O   1 
ATOM   6627 C CB  . ASN D 1 23  ? 9.186   63.725 49.156  1.00 85.98  ?  178 ASN D CB  1 
ATOM   6628 C CG  . ASN D 1 23  ? 8.400   62.749 50.001  1.00 113.29 ?  178 ASN D CG  1 
ATOM   6629 O OD1 . ASN D 1 23  ? 7.231   62.980 50.348  1.00 108.59 ?  178 ASN D OD1 1 
ATOM   6630 N ND2 . ASN D 1 23  ? 9.024   61.621 50.327  1.00 102.35 ?  178 ASN D ND2 1 
ATOM   6631 N N   . ASN D 1 24  ? 11.083  66.099 51.415  1.00 83.38  ?  179 ASN D N   1 
ATOM   6632 C CA  . ASN D 1 24  ? 12.149  66.290 52.394  1.00 83.26  ?  179 ASN D CA  1 
ATOM   6633 C C   . ASN D 1 24  ? 13.449  65.619 51.993  1.00 85.09  ?  179 ASN D C   1 
ATOM   6634 O O   . ASN D 1 24  ? 14.021  64.839 52.757  1.00 84.62  ?  179 ASN D O   1 
ATOM   6635 C CB  . ASN D 1 24  ? 11.688  65.980 53.816  1.00 87.07  ?  179 ASN D CB  1 
ATOM   6636 C CG  . ASN D 1 24  ? 10.753  67.041 54.325  1.00 127.70 ?  179 ASN D CG  1 
ATOM   6637 O OD1 . ASN D 1 24  ? 11.177  68.036 54.926  1.00 125.52 ?  179 ASN D OD1 1 
ATOM   6638 N ND2 . ASN D 1 24  ? 9.467   66.884 54.043  1.00 124.03 ?  179 ASN D ND2 1 
ATOM   6639 N N   . PHE D 1 25  ? 13.894  65.934 50.758  1.00 79.80  ?  180 PHE D N   1 
ATOM   6640 C CA  . PHE D 1 25  ? 15.110  65.428 50.119  1.00 78.25  ?  180 PHE D CA  1 
ATOM   6641 C C   . PHE D 1 25  ? 15.272  63.910 50.229  1.00 82.33  ?  180 PHE D C   1 
ATOM   6642 O O   . PHE D 1 25  ? 16.320  63.421 50.675  1.00 82.08  ?  180 PHE D O   1 
ATOM   6643 C CB  . PHE D 1 25  ? 16.351  66.197 50.594  1.00 78.88  ?  180 PHE D CB  1 
ATOM   6644 C CG  . PHE D 1 25  ? 16.297  67.669 50.278  1.00 79.06  ?  180 PHE D CG  1 
ATOM   6645 C CD1 . PHE D 1 25  ? 16.626  68.138 49.012  1.00 81.51  ?  180 PHE D CD1 1 
ATOM   6646 C CD2 . PHE D 1 25  ? 15.939  68.590 51.249  1.00 79.94  ?  180 PHE D CD2 1 
ATOM   6647 C CE1 . PHE D 1 25  ? 16.590  69.503 48.720  1.00 81.77  ?  180 PHE D CE1 1 
ATOM   6648 C CE2 . PHE D 1 25  ? 15.908  69.953 50.958  1.00 82.57  ?  180 PHE D CE2 1 
ATOM   6649 C CZ  . PHE D 1 25  ? 16.232  70.402 49.694  1.00 80.56  ?  180 PHE D CZ  1 
ATOM   6650 N N   . ASP D 1 26  ? 14.218  63.174 49.821  1.00 79.41  ?  181 ASP D N   1 
ATOM   6651 C CA  . ASP D 1 26  ? 14.177  61.713 49.820  1.00 80.24  ?  181 ASP D CA  1 
ATOM   6652 C C   . ASP D 1 26  ? 15.346  61.175 48.985  1.00 84.37  ?  181 ASP D C   1 
ATOM   6653 O O   . ASP D 1 26  ? 15.457  61.491 47.795  1.00 83.14  ?  181 ASP D O   1 
ATOM   6654 C CB  . ASP D 1 26  ? 12.816  61.216 49.281  1.00 82.81  ?  181 ASP D CB  1 
ATOM   6655 C CG  . ASP D 1 26  ? 12.538  59.720 49.381  1.00 95.72  ?  181 ASP D CG  1 
ATOM   6656 O OD1 . ASP D 1 26  ? 13.472  58.957 49.726  1.00 96.60  ?  181 ASP D OD1 1 
ATOM   6657 O OD2 . ASP D 1 26  ? 11.387  59.310 49.097  1.00 101.75 -1 181 ASP D OD2 1 
ATOM   6658 N N   . GLU D 1 27  ? 16.246  60.415 49.639  1.00 81.74  ?  182 GLU D N   1 
ATOM   6659 C CA  . GLU D 1 27  ? 17.447  59.866 49.004  1.00 81.54  ?  182 GLU D CA  1 
ATOM   6660 C C   . GLU D 1 27  ? 17.217  58.605 48.187  1.00 83.58  ?  182 GLU D C   1 
ATOM   6661 O O   . GLU D 1 27  ? 18.134  58.145 47.514  1.00 82.62  ?  182 GLU D O   1 
ATOM   6662 C CB  . GLU D 1 27  ? 18.595  59.715 50.013  1.00 83.33  ?  182 GLU D CB  1 
ATOM   6663 C CG  . GLU D 1 27  ? 19.254  61.043 50.358  1.00 97.90  ?  182 GLU D CG  1 
ATOM   6664 C CD  . GLU D 1 27  ? 20.671  61.239 49.849  1.00 121.55 ?  182 GLU D CD  1 
ATOM   6665 O OE1 . GLU D 1 27  ? 21.430  61.978 50.516  1.00 117.21 ?  182 GLU D OE1 1 
ATOM   6666 O OE2 . GLU D 1 27  ? 21.025  60.669 48.790  1.00 114.03 -1 182 GLU D OE2 1 
ATOM   6667 N N   . ARG D 1 28  ? 15.992  58.061 48.216  1.00 80.27  ?  183 ARG D N   1 
ATOM   6668 C CA  . ARG D 1 28  ? 15.633  56.880 47.437  1.00 80.38  ?  183 ARG D CA  1 
ATOM   6669 C C   . ARG D 1 28  ? 15.565  57.271 45.959  1.00 85.47  ?  183 ARG D C   1 
ATOM   6670 O O   . ARG D 1 28  ? 15.182  58.410 45.664  1.00 85.49  ?  183 ARG D O   1 
ATOM   6671 C CB  . ARG D 1 28  ? 14.282  56.331 47.894  1.00 80.07  ?  183 ARG D CB  1 
ATOM   6672 C CG  . ARG D 1 28  ? 14.373  55.136 48.829  1.00 89.76  ?  183 ARG D CG  1 
ATOM   6673 C CD  . ARG D 1 28  ? 13.031  54.820 49.474  1.00 104.20 ?  183 ARG D CD  1 
ATOM   6674 N NE  . ARG D 1 28  ? 12.035  54.333 48.514  1.00 116.62 ?  183 ARG D NE  1 
ATOM   6675 C CZ  . ARG D 1 28  ? 11.026  55.060 48.044  1.00 132.51 ?  183 ARG D CZ  1 
ATOM   6676 N NH1 . ARG D 1 28  ? 10.853  56.313 48.451  1.00 119.95 ?  183 ARG D NH1 1 
ATOM   6677 N NH2 . ARG D 1 28  ? 10.176  54.537 47.170  1.00 119.69 1  183 ARG D NH2 1 
ATOM   6678 N N   . PRO D 1 29  ? 15.970  56.382 45.017  1.00 82.59  ?  184 PRO D N   1 
ATOM   6679 C CA  . PRO D 1 29  ? 15.930  56.754 43.593  1.00 82.43  ?  184 PRO D CA  1 
ATOM   6680 C C   . PRO D 1 29  ? 14.515  56.943 43.072  1.00 86.41  ?  184 PRO D C   1 
ATOM   6681 O O   . PRO D 1 29  ? 13.581  56.305 43.565  1.00 85.68  ?  184 PRO D O   1 
ATOM   6682 C CB  . PRO D 1 29  ? 16.638  55.584 42.889  1.00 83.81  ?  184 PRO D CB  1 
ATOM   6683 C CG  . PRO D 1 29  ? 17.348  54.852 43.964  1.00 88.03  ?  184 PRO D CG  1 
ATOM   6684 C CD  . PRO D 1 29  ? 16.493  55.013 45.178  1.00 83.82  ?  184 PRO D CD  1 
ATOM   6685 N N   . ILE D 1 30  ? 14.368  57.835 42.083  1.00 83.91  ?  185 ILE D N   1 
ATOM   6686 C CA  . ILE D 1 30  ? 13.092  58.146 41.433  1.00 84.44  ?  185 ILE D CA  1 
ATOM   6687 C C   . ILE D 1 30  ? 12.462  56.892 40.800  1.00 90.03  ?  185 ILE D C   1 
ATOM   6688 O O   . ILE D 1 30  ? 11.241  56.781 40.776  1.00 89.86  ?  185 ILE D O   1 
ATOM   6689 C CB  . ILE D 1 30  ? 13.183  59.364 40.451  1.00 87.34  ?  185 ILE D CB  1 
ATOM   6690 C CG1 . ILE D 1 30  ? 14.429  59.280 39.531  1.00 87.99  ?  185 ILE D CG1 1 
ATOM   6691 C CG2 . ILE D 1 30  ? 13.141  60.690 41.209  1.00 87.47  ?  185 ILE D CG2 1 
ATOM   6692 C CD1 . ILE D 1 30  ? 14.194  59.639 38.068  1.00 92.79  ?  185 ILE D CD1 1 
ATOM   6693 N N   . SER D 1 31  ? 13.300  55.936 40.344  1.00 87.66  ?  186 SER D N   1 
ATOM   6694 C CA  . SER D 1 31  ? 12.914  54.652 39.734  1.00 88.19  ?  186 SER D CA  1 
ATOM   6695 C C   . SER D 1 31  ? 12.200  53.705 40.708  1.00 94.09  ?  186 SER D C   1 
ATOM   6696 O O   . SER D 1 31  ? 11.536  52.752 40.283  1.00 93.99  ?  186 SER D O   1 
ATOM   6697 C CB  . SER D 1 31  ? 14.151  53.939 39.198  1.00 91.10  ?  186 SER D CB  1 
ATOM   6698 O OG  . SER D 1 31  ? 15.118  53.722 40.214  1.00 98.22  ?  186 SER D OG  1 
ATOM   6699 N N   . VAL D 1 32  ? 12.388  53.950 42.010  1.00 91.10  ?  187 VAL D N   1 
ATOM   6700 C CA  . VAL D 1 32  ? 11.857  53.180 43.135  1.00 90.70  ?  187 VAL D CA  1 
ATOM   6701 C C   . VAL D 1 32  ? 10.706  53.944 43.844  1.00 94.73  ?  187 VAL D C   1 
ATOM   6702 O O   . VAL D 1 32  ? 10.002  53.379 44.685  1.00 94.27  ?  187 VAL D O   1 
ATOM   6703 C CB  . VAL D 1 32  ? 13.066  52.802 44.031  1.00 94.12  ?  187 VAL D CB  1 
ATOM   6704 C CG1 . VAL D 1 32  ? 12.719  52.673 45.514  1.00 93.87  ?  187 VAL D CG1 1 
ATOM   6705 C CG2 . VAL D 1 32  ? 13.751  51.547 43.505  1.00 93.81  ?  187 VAL D CG2 1 
ATOM   6706 N N   . GLY D 1 33  ? 10.484  55.188 43.416  1.00 91.10  ?  188 GLY D N   1 
ATOM   6707 C CA  . GLY D 1 33  ? 9.441   56.060 43.942  1.00 90.44  ?  188 GLY D CA  1 
ATOM   6708 C C   . GLY D 1 33  ? 9.968   57.139 44.867  1.00 92.42  ?  188 GLY D C   1 
ATOM   6709 O O   . GLY D 1 33  ? 9.183   57.839 45.521  1.00 92.80  ?  188 GLY D O   1 
ATOM   6710 N N   . GLY D 1 34  ? 11.293  57.266 44.920  1.00 85.93  ?  189 GLY D N   1 
ATOM   6711 C CA  . GLY D 1 34  ? 11.964  58.267 45.740  1.00 84.35  ?  189 GLY D CA  1 
ATOM   6712 C C   . GLY D 1 34  ? 12.173  59.580 45.011  1.00 84.01  ?  189 GLY D C   1 
ATOM   6713 O O   . GLY D 1 34  ? 11.513  59.844 43.997  1.00 83.86  ?  189 GLY D O   1 
ATOM   6714 N N   . ASN D 1 35  ? 13.102  60.411 45.511  1.00 76.51  ?  190 ASN D N   1 
ATOM   6715 C CA  . ASN D 1 35  ? 13.370  61.712 44.885  1.00 75.09  ?  190 ASN D CA  1 
ATOM   6716 C C   . ASN D 1 35  ? 14.750  61.891 44.260  1.00 75.61  ?  190 ASN D C   1 
ATOM   6717 O O   . ASN D 1 35  ? 14.899  62.768 43.412  1.00 74.99  ?  190 ASN D O   1 
ATOM   6718 C CB  . ASN D 1 35  ? 13.007  62.864 45.818  1.00 75.78  ?  190 ASN D CB  1 
ATOM   6719 C CG  . ASN D 1 35  ? 11.519  63.002 46.000  1.00 105.73 ?  190 ASN D CG  1 
ATOM   6720 O OD1 . ASN D 1 35  ? 10.857  62.170 46.639  1.00 106.16 ?  190 ASN D OD1 1 
ATOM   6721 N ND2 . ASN D 1 35  ? 10.962  64.065 45.443  1.00 96.07  ?  190 ASN D ND2 1 
ATOM   6722 N N   . LYS D 1 36  ? 15.745  61.056 44.647  1.00 69.01  ?  191 LYS D N   1 
ATOM   6723 C CA  . LYS D 1 36  ? 17.110  61.151 44.134  1.00 67.16  ?  191 LYS D CA  1 
ATOM   6724 C C   . LYS D 1 36  ? 17.210  60.808 42.648  1.00 69.02  ?  191 LYS D C   1 
ATOM   6725 O O   . LYS D 1 36  ? 16.754  59.748 42.217  1.00 67.84  ?  191 LYS D O   1 
ATOM   6726 C CB  . LYS D 1 36  ? 18.083  60.319 44.978  1.00 69.91  ?  191 LYS D CB  1 
ATOM   6727 C CG  . LYS D 1 36  ? 19.561  60.524 44.644  1.00 77.47  ?  191 LYS D CG  1 
ATOM   6728 C CD  . LYS D 1 36  ? 20.474  59.675 45.515  1.00 83.34  ?  191 LYS D CD  1 
ATOM   6729 C CE  . LYS D 1 36  ? 21.910  59.808 45.103  1.00 93.69  ?  191 LYS D CE  1 
ATOM   6730 N NZ  . LYS D 1 36  ? 22.798  58.918 45.897  1.00 105.82 1  191 LYS D NZ  1 
ATOM   6731 N N   . MET D 1 37  ? 17.818  61.725 41.867  1.00 64.69  ?  192 MET D N   1 
ATOM   6732 C CA  . MET D 1 37  ? 18.000  61.548 40.428  1.00 63.27  ?  192 MET D CA  1 
ATOM   6733 C C   . MET D 1 37  ? 19.457  61.252 40.061  1.00 64.55  ?  192 MET D C   1 
ATOM   6734 O O   . MET D 1 37  ? 19.717  60.630 39.035  1.00 63.96  ?  192 MET D O   1 
ATOM   6735 C CB  . MET D 1 37  ? 17.465  62.760 39.648  1.00 65.40  ?  192 MET D CB  1 
ATOM   6736 C CG  . MET D 1 37  ? 15.978  62.956 39.789  1.00 68.89  ?  192 MET D CG  1 
ATOM   6737 S SD  . MET D 1 37  ? 15.272  64.083 38.563  1.00 73.55  ?  192 MET D SD  1 
ATOM   6738 C CE  . MET D 1 37  ? 15.988  65.647 39.035  1.00 69.82  ?  192 MET D CE  1 
ATOM   6739 N N   . GLY D 1 38  ? 20.382  61.687 40.904  1.00 59.88  ?  193 GLY D N   1 
ATOM   6740 C CA  . GLY D 1 38  ? 21.804  61.489 40.678  1.00 59.88  ?  193 GLY D CA  1 
ATOM   6741 C C   . GLY D 1 38  ? 22.657  62.356 41.566  1.00 65.78  ?  193 GLY D C   1 
ATOM   6742 O O   . GLY D 1 38  ? 22.139  63.157 42.351  1.00 64.46  ?  193 GLY D O   1 
ATOM   6743 N N   . GLU D 1 39  ? 23.980  62.183 41.456  1.00 66.20  ?  194 GLU D N   1 
ATOM   6744 C CA  . GLU D 1 39  ? 24.944  62.914 42.270  1.00 67.57  ?  194 GLU D CA  1 
ATOM   6745 C C   . GLU D 1 39  ? 26.317  63.086 41.637  1.00 72.38  ?  194 GLU D C   1 
ATOM   6746 O O   . GLU D 1 39  ? 26.860  62.149 41.050  1.00 71.12  ?  194 GLU D O   1 
ATOM   6747 C CB  . GLU D 1 39  ? 25.076  62.307 43.692  1.00 69.32  ?  194 GLU D CB  1 
ATOM   6748 C CG  . GLU D 1 39  ? 25.434  60.828 43.759  1.00 83.77  ?  194 GLU D CG  1 
ATOM   6749 C CD  . GLU D 1 39  ? 25.965  60.374 45.106  1.00 120.12 ?  194 GLU D CD  1 
ATOM   6750 O OE1 . GLU D 1 39  ? 27.158  59.997 45.175  1.00 123.84 ?  194 GLU D OE1 1 
ATOM   6751 O OE2 . GLU D 1 39  ? 25.198  60.421 46.097  1.00 118.89 -1 194 GLU D OE2 1 
ATOM   6752 N N   . GLY D 1 40  ? 26.863  64.285 41.819  1.00 70.86  ?  195 GLY D N   1 
ATOM   6753 C CA  . GLY D 1 40  ? 28.207  64.672 41.410  1.00 71.55  ?  195 GLY D CA  1 
ATOM   6754 C C   . GLY D 1 40  ? 29.094  64.830 42.633  1.00 77.47  ?  195 GLY D C   1 
ATOM   6755 O O   . GLY D 1 40  ? 28.741  64.362 43.725  1.00 78.17  ?  195 GLY D O   1 
ATOM   6756 N N   . GLY D 1 41  ? 30.238  65.487 42.463  1.00 73.23  ?  196 GLY D N   1 
ATOM   6757 C CA  . GLY D 1 41  ? 31.158  65.724 43.572  1.00 72.24  ?  196 GLY D CA  1 
ATOM   6758 C C   . GLY D 1 41  ? 30.703  66.843 44.492  1.00 73.43  ?  196 GLY D C   1 
ATOM   6759 O O   . GLY D 1 41  ? 30.922  66.787 45.710  1.00 72.50  ?  196 GLY D O   1 
ATOM   6760 N N   . PHE D 1 42  ? 30.035  67.859 43.896  1.00 67.72  ?  197 PHE D N   1 
ATOM   6761 C CA  . PHE D 1 42  ? 29.551  69.054 44.581  1.00 66.26  ?  197 PHE D CA  1 
ATOM   6762 C C   . PHE D 1 42  ? 28.067  69.029 45.016  1.00 67.03  ?  197 PHE D C   1 
ATOM   6763 O O   . PHE D 1 42  ? 27.577  70.028 45.546  1.00 66.78  ?  197 PHE D O   1 
ATOM   6764 C CB  . PHE D 1 42  ? 29.915  70.323 43.784  1.00 67.92  ?  197 PHE D CB  1 
ATOM   6765 N N   . GLY D 1 43  ? 27.384  67.897 44.844  1.00 61.06  ?  198 GLY D N   1 
ATOM   6766 C CA  . GLY D 1 43  ? 25.997  67.788 45.274  1.00 60.28  ?  198 GLY D CA  1 
ATOM   6767 C C   . GLY D 1 43  ? 25.174  66.653 44.700  1.00 64.82  ?  198 GLY D C   1 
ATOM   6768 O O   . GLY D 1 43  ? 25.630  65.910 43.827  1.00 65.47  ?  198 GLY D O   1 
ATOM   6769 N N   . VAL D 1 44  ? 23.936  66.517 45.220  1.00 60.51  ?  199 VAL D N   1 
ATOM   6770 C CA  . VAL D 1 44  ? 22.934  65.519 44.827  1.00 59.69  ?  199 VAL D CA  1 
ATOM   6771 C C   . VAL D 1 44  ? 21.736  66.263 44.201  1.00 62.35  ?  199 VAL D C   1 
ATOM   6772 O O   . VAL D 1 44  ? 21.320  67.316 44.708  1.00 61.41  ?  199 VAL D O   1 
ATOM   6773 C CB  . VAL D 1 44  ? 22.502  64.633 46.033  1.00 63.22  ?  199 VAL D CB  1 
ATOM   6774 C CG1 . VAL D 1 44  ? 21.433  63.607 45.640  1.00 62.52  ?  199 VAL D CG1 1 
ATOM   6775 C CG2 . VAL D 1 44  ? 23.706  63.937 46.659  1.00 62.98  ?  199 VAL D CG2 1 
ATOM   6776 N N   . VAL D 1 45  ? 21.191  65.701 43.098  1.00 57.40  ?  200 VAL D N   1 
ATOM   6777 C CA  . VAL D 1 45  ? 20.061  66.272 42.367  1.00 56.01  ?  200 VAL D CA  1 
ATOM   6778 C C   . VAL D 1 45  ? 18.777  65.514 42.698  1.00 59.37  ?  200 VAL D C   1 
ATOM   6779 O O   . VAL D 1 45  ? 18.738  64.286 42.607  1.00 57.67  ?  200 VAL D O   1 
ATOM   6780 C CB  . VAL D 1 45  ? 20.341  66.393 40.839  1.00 59.12  ?  200 VAL D CB  1 
ATOM   6781 C CG1 . VAL D 1 45  ? 19.225  67.170 40.122  1.00 58.50  ?  200 VAL D CG1 1 
ATOM   6782 C CG2 . VAL D 1 45  ? 21.698  67.057 40.587  1.00 58.57  ?  200 VAL D CG2 1 
ATOM   6783 N N   . TYR D 1 46  ? 17.733  66.263 43.098  1.00 57.43  ?  201 TYR D N   1 
ATOM   6784 C CA  . TYR D 1 46  ? 16.419  65.735 43.472  1.00 57.71  ?  201 TYR D CA  1 
ATOM   6785 C C   . TYR D 1 46  ? 15.309  66.222 42.544  1.00 62.06  ?  201 TYR D C   1 
ATOM   6786 O O   . TYR D 1 46  ? 15.363  67.348 42.039  1.00 60.62  ?  201 TYR D O   1 
ATOM   6787 C CB  . TYR D 1 46  ? 16.058  66.137 44.917  1.00 59.14  ?  201 TYR D CB  1 
ATOM   6788 C CG  . TYR D 1 46  ? 17.061  65.695 45.954  1.00 61.34  ?  201 TYR D CG  1 
ATOM   6789 C CD1 . TYR D 1 46  ? 18.167  66.483 46.264  1.00 63.80  ?  201 TYR D CD1 1 
ATOM   6790 C CD2 . TYR D 1 46  ? 16.915  64.486 46.623  1.00 62.24  ?  201 TYR D CD2 1 
ATOM   6791 C CE1 . TYR D 1 46  ? 19.111  66.071 47.203  1.00 65.12  ?  201 TYR D CE1 1 
ATOM   6792 C CE2 . TYR D 1 46  ? 17.853  64.063 47.566  1.00 63.69  ?  201 TYR D CE2 1 
ATOM   6793 C CZ  . TYR D 1 46  ? 18.947  64.864 47.860  1.00 72.71  ?  201 TYR D CZ  1 
ATOM   6794 O OH  . TYR D 1 46  ? 19.875  64.463 48.799  1.00 74.87  ?  201 TYR D OH  1 
ATOM   6795 N N   . LYS D 1 47  ? 14.276  65.379 42.367  1.00 60.29  ?  202 LYS D N   1 
ATOM   6796 C CA  . LYS D 1 47  ? 13.078  65.715 41.601  1.00 60.43  ?  202 LYS D CA  1 
ATOM   6797 C C   . LYS D 1 47  ? 12.092  66.437 42.540  1.00 68.61  ?  202 LYS D C   1 
ATOM   6798 O O   . LYS D 1 47  ? 12.014  66.126 43.737  1.00 68.66  ?  202 LYS D O   1 
ATOM   6799 C CB  . LYS D 1 47  ? 12.436  64.448 41.008  1.00 60.92  ?  202 LYS D CB  1 
ATOM   6800 C CG  . LYS D 1 47  ? 11.459  64.721 39.861  1.00 55.99  ?  202 LYS D CG  1 
ATOM   6801 C CD  . LYS D 1 47  ? 10.937  63.424 39.310  1.00 59.01  ?  202 LYS D CD  1 
ATOM   6802 C CE  . LYS D 1 47  ? 9.799   63.615 38.349  1.00 63.95  ?  202 LYS D CE  1 
ATOM   6803 N NZ  . LYS D 1 47  ? 9.247   62.313 37.872  1.00 70.72  1  202 LYS D NZ  1 
ATOM   6804 N N   . GLY D 1 48  ? 11.374  67.404 41.986  1.00 68.44  ?  203 GLY D N   1 
ATOM   6805 C CA  . GLY D 1 48  ? 10.384  68.184 42.724  1.00 69.72  ?  203 GLY D CA  1 
ATOM   6806 C C   . GLY D 1 48  ? 9.263   68.722 41.865  1.00 77.00  ?  203 GLY D C   1 
ATOM   6807 O O   . GLY D 1 48  ? 9.280   68.576 40.639  1.00 76.40  ?  203 GLY D O   1 
ATOM   6808 N N   . TYR D 1 49  ? 8.274   69.338 42.508  1.00 77.23  ?  204 TYR D N   1 
ATOM   6809 C CA  . TYR D 1 49  ? 7.142   69.947 41.824  1.00 78.82  ?  204 TYR D CA  1 
ATOM   6810 C C   . TYR D 1 49  ? 6.857   71.322 42.436  1.00 84.19  ?  204 TYR D C   1 
ATOM   6811 O O   . TYR D 1 49  ? 6.568   71.404 43.619  1.00 83.95  ?  204 TYR D O   1 
ATOM   6812 C CB  . TYR D 1 49  ? 5.911   69.028 41.880  1.00 81.28  ?  204 TYR D CB  1 
ATOM   6813 C CG  . TYR D 1 49  ? 6.102   67.676 41.220  1.00 85.32  ?  204 TYR D CG  1 
ATOM   6814 C CD1 . TYR D 1 49  ? 5.940   67.516 39.844  1.00 87.90  ?  204 TYR D CD1 1 
ATOM   6815 C CD2 . TYR D 1 49  ? 6.422   66.547 41.974  1.00 86.16  ?  204 TYR D CD2 1 
ATOM   6816 C CE1 . TYR D 1 49  ? 6.097   66.269 39.235  1.00 88.58  ?  204 TYR D CE1 1 
ATOM   6817 C CE2 . TYR D 1 49  ? 6.589   65.297 41.373  1.00 86.91  ?  204 TYR D CE2 1 
ATOM   6818 C CZ  . TYR D 1 49  ? 6.414   65.160 40.005  1.00 94.80  ?  204 TYR D CZ  1 
ATOM   6819 O OH  . TYR D 1 49  ? 6.559   63.920 39.422  1.00 96.26  ?  204 TYR D OH  1 
ATOM   6820 N N   . VAL D 1 50  ? 6.993   72.403 41.657  1.00 83.11  ?  205 VAL D N   1 
ATOM   6821 C CA  . VAL D 1 50  ? 6.735   73.779 42.120  1.00 84.62  ?  205 VAL D CA  1 
ATOM   6822 C C   . VAL D 1 50  ? 5.660   74.406 41.192  1.00 93.91  ?  205 VAL D C   1 
ATOM   6823 O O   . VAL D 1 50  ? 6.013   74.966 40.145  1.00 94.95  ?  205 VAL D O   1 
ATOM   6824 C CB  . VAL D 1 50  ? 8.033   74.646 42.202  1.00 88.32  ?  205 VAL D CB  1 
ATOM   6825 C CG1 . VAL D 1 50  ? 7.731   76.081 42.629  1.00 88.22  ?  205 VAL D CG1 1 
ATOM   6826 C CG2 . VAL D 1 50  ? 9.065   74.028 43.134  1.00 88.08  ?  205 VAL D CG2 1 
ATOM   6827 N N   . ASN D 1 51  ? 4.348   74.300 41.578  1.00 91.71  ?  206 ASN D N   1 
ATOM   6828 C CA  . ASN D 1 51  ? 3.192   74.797 40.806  1.00 91.54  ?  206 ASN D CA  1 
ATOM   6829 C C   . ASN D 1 51  ? 2.960   73.894 39.566  1.00 95.12  ?  206 ASN D C   1 
ATOM   6830 O O   . ASN D 1 51  ? 2.996   74.359 38.419  1.00 94.72  ?  206 ASN D O   1 
ATOM   6831 C CB  . ASN D 1 51  ? 3.360   76.303 40.451  1.00 93.35  ?  206 ASN D CB  1 
ATOM   6832 C CG  . ASN D 1 51  ? 2.267   76.933 39.623  1.00 116.56 ?  206 ASN D CG  1 
ATOM   6833 O OD1 . ASN D 1 51  ? 2.538   77.654 38.655  1.00 111.62 ?  206 ASN D OD1 1 
ATOM   6834 N ND2 . ASN D 1 51  ? 1.014   76.674 39.969  1.00 105.83 ?  206 ASN D ND2 1 
ATOM   6835 N N   . ASN D 1 52  ? 2.782   72.570 39.818  1.00 90.88  ?  207 ASN D N   1 
ATOM   6836 C CA  . ASN D 1 52  ? 2.562   71.514 38.808  1.00 90.18  ?  207 ASN D CA  1 
ATOM   6837 C C   . ASN D 1 52  ? 3.757   71.299 37.868  1.00 91.98  ?  207 ASN D C   1 
ATOM   6838 O O   . ASN D 1 52  ? 3.815   70.278 37.181  1.00 92.43  ?  207 ASN D O   1 
ATOM   6839 C CB  . ASN D 1 52  ? 1.266   71.736 38.012  1.00 93.40  ?  207 ASN D CB  1 
ATOM   6840 C CG  . ASN D 1 52  ? -0.012  71.682 38.822  1.00 121.54 ?  207 ASN D CG  1 
ATOM   6841 O OD1 . ASN D 1 52  ? -0.055  71.193 39.959  1.00 118.59 ?  207 ASN D OD1 1 
ATOM   6842 N ND2 . ASN D 1 52  ? -1.104  72.143 38.226  1.00 111.37 ?  207 ASN D ND2 1 
ATOM   6843 N N   . THR D 1 53  ? 4.712   72.263 37.868  1.00 85.47  ?  208 THR D N   1 
ATOM   6844 C CA  . THR D 1 53  ? 5.960   72.318 37.102  1.00 83.21  ?  208 THR D CA  1 
ATOM   6845 C C   . THR D 1 53  ? 6.998   71.373 37.729  1.00 81.29  ?  208 THR D C   1 
ATOM   6846 O O   . THR D 1 53  ? 7.338   71.531 38.908  1.00 81.56  ?  208 THR D O   1 
ATOM   6847 C CB  . THR D 1 53  ? 6.498   73.770 37.147  1.00 91.21  ?  208 THR D CB  1 
ATOM   6848 O OG1 . THR D 1 53  ? 5.476   74.677 36.738  1.00 95.07  ?  208 THR D OG1 1 
ATOM   6849 C CG2 . THR D 1 53  ? 7.778   73.977 36.342  1.00 87.41  ?  208 THR D CG2 1 
ATOM   6850 N N   . THR D 1 54  ? 7.535   70.432 36.936  1.00 71.82  ?  209 THR D N   1 
ATOM   6851 C CA  . THR D 1 54  ? 8.591   69.547 37.424  1.00 68.31  ?  209 THR D CA  1 
ATOM   6852 C C   . THR D 1 54  ? 9.930   70.304 37.397  1.00 64.04  ?  209 THR D C   1 
ATOM   6853 O O   . THR D 1 54  ? 10.272  70.962 36.410  1.00 61.25  ?  209 THR D O   1 
ATOM   6854 C CB  . THR D 1 54  ? 8.586   68.184 36.715  1.00 76.19  ?  209 THR D CB  1 
ATOM   6855 O OG1 . THR D 1 54  ? 7.238   67.749 36.548  1.00 79.92  ?  209 THR D OG1 1 
ATOM   6856 C CG2 . THR D 1 54  ? 9.317   67.128 37.510  1.00 73.49  ?  209 THR D CG2 1 
ATOM   6857 N N   . VAL D 1 55  ? 10.654  70.250 38.517  1.00 57.47  ?  210 VAL D N   1 
ATOM   6858 C CA  . VAL D 1 55  ? 11.944  70.932 38.693  1.00 55.17  ?  210 VAL D CA  1 
ATOM   6859 C C   . VAL D 1 55  ? 13.014  69.969 39.171  1.00 54.68  ?  210 VAL D C   1 
ATOM   6860 O O   . VAL D 1 55  ? 12.685  68.926 39.745  1.00 54.16  ?  210 VAL D O   1 
ATOM   6861 C CB  . VAL D 1 55  ? 11.862  72.194 39.610  1.00 58.65  ?  210 VAL D CB  1 
ATOM   6862 C CG1 . VAL D 1 55  ? 10.913  73.243 39.041  1.00 58.55  ?  210 VAL D CG1 1 
ATOM   6863 C CG2 . VAL D 1 55  ? 11.487  71.843 41.049  1.00 58.14  ?  210 VAL D CG2 1 
ATOM   6864 N N   . ALA D 1 56  ? 14.292  70.322 38.927  1.00 48.43  ?  211 ALA D N   1 
ATOM   6865 C CA  . ALA D 1 56  ? 15.480  69.592 39.371  1.00 47.03  ?  211 ALA D CA  1 
ATOM   6866 C C   . ALA D 1 56  ? 16.140  70.464 40.440  1.00 52.29  ?  211 ALA D C   1 
ATOM   6867 O O   . ALA D 1 56  ? 16.457  71.641 40.190  1.00 53.38  ?  211 ALA D O   1 
ATOM   6868 C CB  . ALA D 1 56  ? 16.432  69.363 38.213  1.00 47.13  ?  211 ALA D CB  1 
ATOM   6869 N N   . VAL D 1 57  ? 16.276  69.918 41.651  1.00 48.53  ?  212 VAL D N   1 
ATOM   6870 C CA  . VAL D 1 57  ? 16.871  70.664 42.750  1.00 48.81  ?  212 VAL D CA  1 
ATOM   6871 C C   . VAL D 1 57  ? 18.254  70.100 43.076  1.00 56.00  ?  212 VAL D C   1 
ATOM   6872 O O   . VAL D 1 57  ? 18.366  68.956 43.530  1.00 56.47  ?  212 VAL D O   1 
ATOM   6873 C CB  . VAL D 1 57  ? 15.952  70.741 44.000  1.00 51.61  ?  212 VAL D CB  1 
ATOM   6874 C CG1 . VAL D 1 57  ? 16.542  71.676 45.052  1.00 51.10  ?  212 VAL D CG1 1 
ATOM   6875 C CG2 . VAL D 1 57  ? 14.545  71.186 43.621  1.00 50.99  ?  212 VAL D CG2 1 
ATOM   6876 N N   . LYS D 1 58  ? 19.300  70.898 42.841  1.00 54.00  ?  213 LYS D N   1 
ATOM   6877 C CA  . LYS D 1 58  ? 20.659  70.479 43.159  1.00 55.16  ?  213 LYS D CA  1 
ATOM   6878 C C   . LYS D 1 58  ? 21.001  70.993 44.558  1.00 65.25  ?  213 LYS D C   1 
ATOM   6879 O O   . LYS D 1 58  ? 21.114  72.206 44.755  1.00 64.75  ?  213 LYS D O   1 
ATOM   6880 C CB  . LYS D 1 58  ? 21.652  71.014 42.112  1.00 56.71  ?  213 LYS D CB  1 
ATOM   6881 C CG  . LYS D 1 58  ? 23.020  70.349 42.144  1.00 56.24  ?  213 LYS D CG  1 
ATOM   6882 C CD  . LYS D 1 58  ? 24.100  71.318 41.756  1.00 59.37  ?  213 LYS D CD  1 
ATOM   6883 C CE  . LYS D 1 58  ? 24.808  70.974 40.485  1.00 66.03  ?  213 LYS D CE  1 
ATOM   6884 N NZ  . LYS D 1 58  ? 25.570  72.150 39.967  1.00 65.75  1  213 LYS D NZ  1 
ATOM   6885 N N   . LYS D 1 59  ? 21.101  70.079 45.539  1.00 66.50  ?  214 LYS D N   1 
ATOM   6886 C CA  . LYS D 1 59  ? 21.472  70.435 46.909  1.00 68.19  ?  214 LYS D CA  1 
ATOM   6887 C C   . LYS D 1 59  ? 22.984  70.254 47.028  1.00 76.17  ?  214 LYS D C   1 
ATOM   6888 O O   . LYS D 1 59  ? 23.497  69.126 46.979  1.00 75.76  ?  214 LYS D O   1 
ATOM   6889 C CB  . LYS D 1 59  ? 20.725  69.583 47.948  1.00 71.01  ?  214 LYS D CB  1 
ATOM   6890 C CG  . LYS D 1 59  ? 20.810  70.145 49.384  1.00 77.80  ?  214 LYS D CG  1 
ATOM   6891 C CD  . LYS D 1 59  ? 20.195  69.211 50.428  1.00 84.55  ?  214 LYS D CD  1 
ATOM   6892 C CE  . LYS D 1 59  ? 21.182  68.203 50.986  1.00 96.47  ?  214 LYS D CE  1 
ATOM   6893 N NZ  . LYS D 1 59  ? 20.518  67.157 51.817  1.00 96.50  1  214 LYS D NZ  1 
ATOM   6894 N N   . LEU D 1 60  ? 23.694  71.384 47.133  1.00 75.16  ?  215 LEU D N   1 
ATOM   6895 C CA  . LEU D 1 60  ? 25.148  71.440 47.229  1.00 76.23  ?  215 LEU D CA  1 
ATOM   6896 C C   . LEU D 1 60  ? 25.694  70.752 48.480  1.00 84.07  ?  215 LEU D C   1 
ATOM   6897 O O   . LEU D 1 60  ? 25.229  71.029 49.598  1.00 84.03  ?  215 LEU D O   1 
ATOM   6898 C CB  . LEU D 1 60  ? 25.626  72.895 47.141  1.00 76.00  ?  215 LEU D CB  1 
ATOM   6899 C CG  . LEU D 1 60  ? 26.085  73.388 45.773  1.00 80.03  ?  215 LEU D CG  1 
ATOM   6900 C CD1 . LEU D 1 60  ? 24.952  73.415 44.769  1.00 80.32  ?  215 LEU D CD1 1 
ATOM   6901 C CD2 . LEU D 1 60  ? 26.619  74.772 45.888  1.00 82.51  ?  215 LEU D CD2 1 
ATOM   6902 N N   . ALA D 1 61  ? 26.664  69.841 48.277  1.00 82.70  ?  216 ALA D N   1 
ATOM   6903 C CA  . ALA D 1 61  ? 27.303  69.060 49.334  1.00 83.47  ?  216 ALA D CA  1 
ATOM   6904 C C   . ALA D 1 61  ? 28.816  68.978 49.118  1.00 90.42  ?  216 ALA D C   1 
ATOM   6905 O O   . ALA D 1 61  ? 29.266  68.723 48.000  1.00 90.60  ?  216 ALA D O   1 
ATOM   6906 C CB  . ALA D 1 61  ? 26.701  67.661 49.383  1.00 84.01  ?  216 ALA D CB  1 
ATOM   6907 N N   . ALA D 1 62  ? 29.601  69.198 50.185  1.00 88.44  ?  217 ALA D N   1 
ATOM   6908 C CA  . ALA D 1 62  ? 31.066  69.144 50.116  1.00 118.60 ?  217 ALA D CA  1 
ATOM   6909 C C   . ALA D 1 62  ? 31.580  67.720 50.379  1.00 144.55 ?  217 ALA D C   1 
ATOM   6910 O O   . ALA D 1 62  ? 31.160  66.768 49.717  1.00 102.93 ?  217 ALA D O   1 
ATOM   6911 C CB  . ALA D 1 62  ? 31.677  70.127 51.105  1.00 119.26 ?  217 ALA D CB  1 
ATOM   6912 N N   . THR D 1 68  ? 32.359  74.950 53.616  1.00 86.21  ?  223 THR D N   1 
ATOM   6913 C CA  . THR D 1 68  ? 33.466  75.466 52.796  1.00 86.15  ?  223 THR D CA  1 
ATOM   6914 C C   . THR D 1 68  ? 33.060  76.707 51.947  1.00 89.73  ?  223 THR D C   1 
ATOM   6915 O O   . THR D 1 68  ? 31.980  76.730 51.336  1.00 88.72  ?  223 THR D O   1 
ATOM   6916 C CB  . THR D 1 68  ? 34.265  74.303 52.074  1.00 90.30  ?  223 THR D CB  1 
ATOM   6917 O OG1 . THR D 1 68  ? 35.556  74.725 51.603  1.00 83.97  ?  223 THR D OG1 1 
ATOM   6918 C CG2 . THR D 1 68  ? 33.493  73.652 50.942  1.00 89.73  ?  223 THR D CG2 1 
ATOM   6919 N N   . GLU D 1 69  ? 33.932  77.743 51.946  1.00 86.15  ?  224 GLU D N   1 
ATOM   6920 C CA  . GLU D 1 69  ? 33.768  78.972 51.166  1.00 86.10  ?  224 GLU D CA  1 
ATOM   6921 C C   . GLU D 1 69  ? 33.918  78.664 49.660  1.00 89.99  ?  224 GLU D C   1 
ATOM   6922 O O   . GLU D 1 69  ? 33.501  79.469 48.822  1.00 89.72  ?  224 GLU D O   1 
ATOM   6923 C CB  . GLU D 1 69  ? 34.791  80.031 51.609  1.00 87.53  ?  224 GLU D CB  1 
ATOM   6924 N N   . GLU D 1 70  ? 34.505  77.489 49.328  1.00 86.08  ?  225 GLU D N   1 
ATOM   6925 C CA  . GLU D 1 70  ? 34.675  77.011 47.959  1.00 85.46  ?  225 GLU D CA  1 
ATOM   6926 C C   . GLU D 1 70  ? 33.320  76.643 47.350  1.00 87.66  ?  225 GLU D C   1 
ATOM   6927 O O   . GLU D 1 70  ? 33.041  77.031 46.210  1.00 88.16  ?  225 GLU D O   1 
ATOM   6928 C CB  . GLU D 1 70  ? 35.644  75.818 47.902  1.00 86.95  ?  225 GLU D CB  1 
ATOM   6929 C CG  . GLU D 1 70  ? 36.815  76.034 46.951  1.00 101.32 ?  225 GLU D CG  1 
ATOM   6930 C CD  . GLU D 1 70  ? 36.474  76.202 45.477  1.00 127.86 ?  225 GLU D CD  1 
ATOM   6931 O OE1 . GLU D 1 70  ? 36.281  77.359 45.037  1.00 131.39 ?  225 GLU D OE1 1 
ATOM   6932 O OE2 . GLU D 1 70  ? 36.427  75.175 44.758  1.00 114.13 -1 225 GLU D OE2 1 
ATOM   6933 N N   . LEU D 1 71  ? 32.472  75.929 48.128  1.00 81.59  ?  226 LEU D N   1 
ATOM   6934 C CA  . LEU D 1 71  ? 31.120  75.519 47.740  1.00 80.09  ?  226 LEU D CA  1 
ATOM   6935 C C   . LEU D 1 71  ? 30.227  76.751 47.519  1.00 82.70  ?  226 LEU D C   1 
ATOM   6936 O O   . LEU D 1 71  ? 29.460  76.784 46.555  1.00 82.02  ?  226 LEU D O   1 
ATOM   6937 C CB  . LEU D 1 71  ? 30.535  74.581 48.801  1.00 79.84  ?  226 LEU D CB  1 
ATOM   6938 C CG  . LEU D 1 71  ? 29.626  73.445 48.316  1.00 84.25  ?  226 LEU D CG  1 
ATOM   6939 C CD1 . LEU D 1 71  ? 30.371  72.427 47.447  1.00 84.27  ?  226 LEU D CD1 1 
ATOM   6940 C CD2 . LEU D 1 71  ? 29.050  72.691 49.490  1.00 86.56  ?  226 LEU D CD2 1 
ATOM   6941 N N   . LYS D 1 72  ? 30.391  77.792 48.370  1.00 78.42  ?  227 LYS D N   1 
ATOM   6942 C CA  . LYS D 1 72  ? 29.681  79.069 48.245  1.00 77.73  ?  227 LYS D CA  1 
ATOM   6943 C C   . LYS D 1 72  ? 30.182  79.835 47.005  1.00 82.14  ?  227 LYS D C   1 
ATOM   6944 O O   . LYS D 1 72  ? 29.391  80.512 46.347  1.00 82.10  ?  227 LYS D O   1 
ATOM   6945 C CB  . LYS D 1 72  ? 29.829  79.919 49.513  1.00 79.26  ?  227 LYS D CB  1 
ATOM   6946 N N   . GLN D 1 73  ? 31.486  79.702 46.671  1.00 78.70  ?  228 GLN D N   1 
ATOM   6947 C CA  . GLN D 1 73  ? 32.077  80.329 45.487  1.00 78.36  ?  228 GLN D CA  1 
ATOM   6948 C C   . GLN D 1 73  ? 31.507  79.666 44.227  1.00 82.20  ?  228 GLN D C   1 
ATOM   6949 O O   . GLN D 1 73  ? 31.138  80.373 43.288  1.00 82.15  ?  228 GLN D O   1 
ATOM   6950 C CB  . GLN D 1 73  ? 33.616  80.243 45.516  1.00 79.57  ?  228 GLN D CB  1 
ATOM   6951 N N   . GLN D 1 74  ? 31.394  78.319 44.229  1.00 78.18  ?  229 GLN D N   1 
ATOM   6952 C CA  . GLN D 1 74  ? 30.852  77.521 43.117  1.00 77.82  ?  229 GLN D CA  1 
ATOM   6953 C C   . GLN D 1 74  ? 29.343  77.786 42.878  1.00 81.38  ?  229 GLN D C   1 
ATOM   6954 O O   . GLN D 1 74  ? 28.867  77.739 41.732  1.00 81.07  ?  229 GLN D O   1 
ATOM   6955 C CB  . GLN D 1 74  ? 31.117  76.022 43.342  1.00 78.77  ?  229 GLN D CB  1 
ATOM   6956 C CG  . GLN D 1 74  ? 32.546  75.574 43.020  1.00 80.97  ?  229 GLN D CG  1 
ATOM   6957 C CD  . GLN D 1 74  ? 32.707  74.065 42.999  1.00 93.97  ?  229 GLN D CD  1 
ATOM   6958 O OE1 . GLN D 1 74  ? 33.660  73.523 43.561  1.00 83.00  ?  229 GLN D OE1 1 
ATOM   6959 N NE2 . GLN D 1 74  ? 31.799  73.343 42.338  1.00 91.12  ?  229 GLN D NE2 1 
ATOM   6960 N N   . PHE D 1 75  ? 28.606  78.063 43.978  1.00 76.51  ?  230 PHE D N   1 
ATOM   6961 C CA  . PHE D 1 75  ? 27.184  78.408 44.000  1.00 75.22  ?  230 PHE D CA  1 
ATOM   6962 C C   . PHE D 1 75  ? 26.980  79.780 43.335  1.00 77.55  ?  230 PHE D C   1 
ATOM   6963 O O   . PHE D 1 75  ? 26.178  79.908 42.409  1.00 75.33  ?  230 PHE D O   1 
ATOM   6964 C CB  . PHE D 1 75  ? 26.700  78.435 45.458  1.00 76.91  ?  230 PHE D CB  1 
ATOM   6965 C CG  . PHE D 1 75  ? 25.276  78.879 45.691  1.00 78.73  ?  230 PHE D CG  1 
ATOM   6966 C CD1 . PHE D 1 75  ? 24.219  77.984 45.567  1.00 82.02  ?  230 PHE D CD1 1 
ATOM   6967 C CD2 . PHE D 1 75  ? 24.994  80.183 46.081  1.00 80.91  ?  230 PHE D CD2 1 
ATOM   6968 C CE1 . PHE D 1 75  ? 22.905  78.386 45.812  1.00 82.82  ?  230 PHE D CE1 1 
ATOM   6969 C CE2 . PHE D 1 75  ? 23.675  80.588 46.321  1.00 83.60  ?  230 PHE D CE2 1 
ATOM   6970 C CZ  . PHE D 1 75  ? 22.641  79.686 46.186  1.00 81.85  ?  230 PHE D CZ  1 
ATOM   6971 N N   . ASP D 1 76  ? 27.729  80.796 43.809  1.00 75.16  ?  231 ASP D N   1 
ATOM   6972 C CA  . ASP D 1 76  ? 27.709  82.168 43.299  1.00 75.15  ?  231 ASP D CA  1 
ATOM   6973 C C   . ASP D 1 76  ? 28.092  82.214 41.832  1.00 78.73  ?  231 ASP D C   1 
ATOM   6974 O O   . ASP D 1 76  ? 27.536  83.024 41.088  1.00 79.83  ?  231 ASP D O   1 
ATOM   6975 C CB  . ASP D 1 76  ? 28.664  83.063 44.106  1.00 77.24  ?  231 ASP D CB  1 
ATOM   6976 C CG  . ASP D 1 76  ? 28.204  83.394 45.513  1.00 92.55  ?  231 ASP D CG  1 
ATOM   6977 O OD1 . ASP D 1 76  ? 26.998  83.195 45.814  1.00 92.66  ?  231 ASP D OD1 1 
ATOM   6978 O OD2 . ASP D 1 76  ? 29.037  83.886 46.308  1.00 102.67 -1 231 ASP D OD2 1 
ATOM   6979 N N   . GLN D 1 77  ? 29.028  81.331 41.420  1.00 73.76  ?  232 GLN D N   1 
ATOM   6980 C CA  . GLN D 1 77  ? 29.515  81.220 40.042  1.00 72.91  ?  232 GLN D CA  1 
ATOM   6981 C C   . GLN D 1 77  ? 28.416  80.744 39.100  1.00 73.71  ?  232 GLN D C   1 
ATOM   6982 O O   . GLN D 1 77  ? 28.214  81.347 38.040  1.00 72.79  ?  232 GLN D O   1 
ATOM   6983 C CB  . GLN D 1 77  ? 30.746  80.299 39.966  1.00 74.27  ?  232 GLN D CB  1 
ATOM   6984 N N   . GLU D 1 78  ? 27.680  79.695 39.510  1.00 67.81  ?  233 GLU D N   1 
ATOM   6985 C CA  . GLU D 1 78  ? 26.588  79.124 38.728  1.00 66.53  ?  233 GLU D CA  1 
ATOM   6986 C C   . GLU D 1 78  ? 25.494  80.182 38.450  1.00 67.33  ?  233 GLU D C   1 
ATOM   6987 O O   . GLU D 1 78  ? 25.037  80.307 37.309  1.00 66.49  ?  233 GLU D O   1 
ATOM   6988 C CB  . GLU D 1 78  ? 26.016  77.899 39.453  1.00 67.77  ?  233 GLU D CB  1 
ATOM   6989 C CG  . GLU D 1 78  ? 24.997  77.124 38.641  1.00 75.75  ?  233 GLU D CG  1 
ATOM   6990 C CD  . GLU D 1 78  ? 25.449  75.754 38.181  1.00 102.76 ?  233 GLU D CD  1 
ATOM   6991 O OE1 . GLU D 1 78  ? 26.041  75.002 38.991  1.00 107.49 ?  233 GLU D OE1 1 
ATOM   6992 O OE2 . GLU D 1 78  ? 25.118  75.396 37.029  1.00 96.66  -1 233 GLU D OE2 1 
ATOM   6993 N N   . ILE D 1 79  ? 25.124  80.967 39.486  1.00 61.52  ?  234 ILE D N   1 
ATOM   6994 C CA  . ILE D 1 79  ? 24.120  82.033 39.391  1.00 60.07  ?  234 ILE D CA  1 
ATOM   6995 C C   . ILE D 1 79  ? 24.599  83.174 38.473  1.00 63.67  ?  234 ILE D C   1 
ATOM   6996 O O   . ILE D 1 79  ? 23.867  83.563 37.567  1.00 61.58  ?  234 ILE D O   1 
ATOM   6997 C CB  . ILE D 1 79  ? 23.655  82.506 40.789  1.00 62.16  ?  234 ILE D CB  1 
ATOM   6998 C CG1 . ILE D 1 79  ? 22.952  81.360 41.526  1.00 62.55  ?  234 ILE D CG1 1 
ATOM   6999 C CG2 . ILE D 1 79  ? 22.722  83.705 40.686  1.00 61.85  ?  234 ILE D CG2 1 
ATOM   7000 C CD1 . ILE D 1 79  ? 22.856  81.514 43.018  1.00 67.07  ?  234 ILE D CD1 1 
ATOM   7001 N N   . LYS D 1 80  ? 25.836  83.664 38.677  1.00 62.15  ?  235 LYS D N   1 
ATOM   7002 C CA  . LYS D 1 80  ? 26.420  84.731 37.865  1.00 62.96  ?  235 LYS D CA  1 
ATOM   7003 C C   . LYS D 1 80  ? 26.420  84.371 36.364  1.00 69.12  ?  235 LYS D C   1 
ATOM   7004 O O   . LYS D 1 80  ? 25.950  85.173 35.559  1.00 69.08  ?  235 LYS D O   1 
ATOM   7005 C CB  . LYS D 1 80  ? 27.831  85.101 38.367  1.00 65.20  ?  235 LYS D CB  1 
ATOM   7006 N N   . VAL D 1 81  ? 26.888  83.145 36.010  1.00 66.26  ?  236 VAL D N   1 
ATOM   7007 C CA  . VAL D 1 81  ? 26.957  82.620 34.634  1.00 65.68  ?  236 VAL D CA  1 
ATOM   7008 C C   . VAL D 1 81  ? 25.567  82.490 34.041  1.00 68.49  ?  236 VAL D C   1 
ATOM   7009 O O   . VAL D 1 81  ? 25.337  82.951 32.924  1.00 66.00  ?  236 VAL D O   1 
ATOM   7010 C CB  . VAL D 1 81  ? 27.759  81.283 34.535  1.00 69.76  ?  236 VAL D CB  1 
ATOM   7011 C CG1 . VAL D 1 81  ? 27.612  80.633 33.158  1.00 69.37  ?  236 VAL D CG1 1 
ATOM   7012 C CG2 . VAL D 1 81  ? 29.238  81.491 34.859  1.00 69.85  ?  236 VAL D CG2 1 
ATOM   7013 N N   . MET D 1 82  ? 24.645  81.851 34.783  1.00 67.32  ?  237 MET D N   1 
ATOM   7014 C CA  . MET D 1 82  ? 23.272  81.629 34.330  1.00 67.29  ?  237 MET D CA  1 
ATOM   7015 C C   . MET D 1 82  ? 22.517  82.908 34.058  1.00 68.73  ?  237 MET D C   1 
ATOM   7016 O O   . MET D 1 82  ? 21.713  82.944 33.130  1.00 66.10  ?  237 MET D O   1 
ATOM   7017 C CB  . MET D 1 82  ? 22.495  80.762 35.306  1.00 69.85  ?  237 MET D CB  1 
ATOM   7018 C CG  . MET D 1 82  ? 21.631  79.769 34.590  1.00 73.79  ?  237 MET D CG  1 
ATOM   7019 S SD  . MET D 1 82  ? 22.569  78.334 34.033  1.00 77.73  ?  237 MET D SD  1 
ATOM   7020 C CE  . MET D 1 82  ? 22.745  77.463 35.589  1.00 74.38  ?  237 MET D CE  1 
ATOM   7021 N N   . ALA D 1 83  ? 22.793  83.954 34.865  1.00 66.36  ?  238 ALA D N   1 
ATOM   7022 C CA  . ALA D 1 83  ? 22.188  85.272 34.732  1.00 66.50  ?  238 ALA D CA  1 
ATOM   7023 C C   . ALA D 1 83  ? 22.567  85.875 33.396  1.00 71.66  ?  238 ALA D C   1 
ATOM   7024 O O   . ALA D 1 83  ? 21.700  86.428 32.724  1.00 72.33  ?  238 ALA D O   1 
ATOM   7025 C CB  . ALA D 1 83  ? 22.647  86.174 35.859  1.00 67.12  ?  238 ALA D CB  1 
ATOM   7026 N N   . LYS D 1 84  ? 23.842  85.712 32.981  1.00 67.74  ?  239 LYS D N   1 
ATOM   7027 C CA  . LYS D 1 84  ? 24.365  86.233 31.720  1.00 67.33  ?  239 LYS D CA  1 
ATOM   7028 C C   . LYS D 1 84  ? 24.006  85.353 30.521  1.00 71.93  ?  239 LYS D C   1 
ATOM   7029 O O   . LYS D 1 84  ? 23.580  85.877 29.492  1.00 72.45  ?  239 LYS D O   1 
ATOM   7030 C CB  . LYS D 1 84  ? 25.888  86.436 31.813  1.00 69.12  ?  239 LYS D CB  1 
ATOM   7031 N N   . CYS D 1 85  ? 24.149  84.024 30.669  1.00 68.24  ?  240 CYS D N   1 
ATOM   7032 C CA  . CYS D 1 85  ? 23.959  83.039 29.607  1.00 68.29  ?  240 CYS D CA  1 
ATOM   7033 C C   . CYS D 1 85  ? 22.581  82.372 29.518  1.00 69.85  ?  240 CYS D C   1 
ATOM   7034 O O   . CYS D 1 85  ? 22.210  81.565 30.375  1.00 70.12  ?  240 CYS D O   1 
ATOM   7035 C CB  . CYS D 1 85  ? 25.084  82.006 29.624  1.00 69.64  ?  240 CYS D CB  1 
ATOM   7036 S SG  . CYS D 1 85  ? 26.752  82.711 29.797  1.00 74.42  ?  240 CYS D SG  1 
ATOM   7037 N N   . GLN D 1 86  ? 21.839  82.701 28.444  1.00 63.18  ?  241 GLN D N   1 
ATOM   7038 C CA  . GLN D 1 86  ? 20.534  82.126 28.116  1.00 60.55  ?  241 GLN D CA  1 
ATOM   7039 C C   . GLN D 1 86  ? 20.602  81.648 26.676  1.00 58.09  ?  241 GLN D C   1 
ATOM   7040 O O   . GLN D 1 86  ? 20.772  82.462 25.762  1.00 58.42  ?  241 GLN D O   1 
ATOM   7041 C CB  . GLN D 1 86  ? 19.389  83.131 28.305  1.00 61.82  ?  241 GLN D CB  1 
ATOM   7042 C CG  . GLN D 1 86  ? 18.987  83.353 29.757  1.00 82.72  ?  241 GLN D CG  1 
ATOM   7043 C CD  . GLN D 1 86  ? 19.528  84.640 30.344  1.00 114.81 ?  241 GLN D CD  1 
ATOM   7044 O OE1 . GLN D 1 86  ? 20.007  85.549 29.641  1.00 111.59 ?  241 GLN D OE1 1 
ATOM   7045 N NE2 . GLN D 1 86  ? 19.437  84.755 31.665  1.00 111.63 ?  241 GLN D NE2 1 
ATOM   7046 N N   . HIS D 1 87  ? 20.526  80.325 26.480  1.00 48.85  ?  242 HIS D N   1 
ATOM   7047 C CA  . HIS D 1 87  ? 20.594  79.719 25.162  1.00 47.10  ?  242 HIS D CA  1 
ATOM   7048 C C   . HIS D 1 87  ? 19.816  78.417 25.144  1.00 49.46  ?  242 HIS D C   1 
ATOM   7049 O O   . HIS D 1 87  ? 19.678  77.769 26.191  1.00 49.51  ?  242 HIS D O   1 
ATOM   7050 C CB  . HIS D 1 87  ? 22.060  79.491 24.796  1.00 47.69  ?  242 HIS D CB  1 
ATOM   7051 C CG  . HIS D 1 87  ? 22.280  79.051 23.394  1.00 50.60  ?  242 HIS D CG  1 
ATOM   7052 N ND1 . HIS D 1 87  ? 22.201  77.720 23.039  1.00 52.54  ?  242 HIS D ND1 1 
ATOM   7053 C CD2 . HIS D 1 87  ? 22.577  79.779 22.299  1.00 52.22  ?  242 HIS D CD2 1 
ATOM   7054 C CE1 . HIS D 1 87  ? 22.461  77.674 21.744  1.00 51.79  ?  242 HIS D CE1 1 
ATOM   7055 N NE2 . HIS D 1 87  ? 22.688  78.890 21.253  1.00 52.13  ?  242 HIS D NE2 1 
ATOM   7056 N N   . GLU D 1 88  ? 19.321  78.019 23.946  1.00 44.76  ?  243 GLU D N   1 
ATOM   7057 C CA  . GLU D 1 88  ? 18.540  76.782 23.741  1.00 43.97  ?  243 GLU D CA  1 
ATOM   7058 C C   . GLU D 1 88  ? 19.288  75.488 24.097  1.00 45.52  ?  243 GLU D C   1 
ATOM   7059 O O   . GLU D 1 88  ? 18.655  74.450 24.288  1.00 45.20  ?  243 GLU D O   1 
ATOM   7060 C CB  . GLU D 1 88  ? 17.946  76.716 22.319  1.00 45.47  ?  243 GLU D CB  1 
ATOM   7061 C CG  . GLU D 1 88  ? 18.978  76.675 21.207  1.00 59.93  ?  243 GLU D CG  1 
ATOM   7062 C CD  . GLU D 1 88  ? 18.453  76.919 19.805  1.00 82.83  ?  243 GLU D CD  1 
ATOM   7063 O OE1 . GLU D 1 88  ? 17.325  76.467 19.502  1.00 83.30  ?  243 GLU D OE1 1 
ATOM   7064 O OE2 . GLU D 1 88  ? 19.193  77.520 18.991  1.00 68.55  -1 243 GLU D OE2 1 
ATOM   7065 N N   . ASN D 1 89  ? 20.627  75.559 24.184  1.00 40.20  ?  244 ASN D N   1 
ATOM   7066 C CA  . ASN D 1 89  ? 21.482  74.425 24.504  1.00 37.97  ?  244 ASN D CA  1 
ATOM   7067 C C   . ASN D 1 89  ? 22.142  74.565 25.857  1.00 42.16  ?  244 ASN D C   1 
ATOM   7068 O O   . ASN D 1 89  ? 23.173  73.945 26.142  1.00 42.10  ?  244 ASN D O   1 
ATOM   7069 C CB  . ASN D 1 89  ? 22.449  74.125 23.365  1.00 32.98  ?  244 ASN D CB  1 
ATOM   7070 C CG  . ASN D 1 89  ? 21.740  73.797 22.072  1.00 60.03  ?  244 ASN D CG  1 
ATOM   7071 O OD1 . ASN D 1 89  ? 21.777  74.573 21.120  1.00 59.96  ?  244 ASN D OD1 1 
ATOM   7072 N ND2 . ASN D 1 89  ? 21.017  72.679 22.031  1.00 52.93  ?  244 ASN D ND2 1 
ATOM   7073 N N   . LEU D 1 90  ? 21.520  75.365 26.715  1.00 39.74  ?  245 LEU D N   1 
ATOM   7074 C CA  . LEU D 1 90  ? 21.967  75.539 28.099  1.00 40.44  ?  245 LEU D CA  1 
ATOM   7075 C C   . LEU D 1 90  ? 20.796  75.304 28.977  1.00 44.41  ?  245 LEU D C   1 
ATOM   7076 O O   . LEU D 1 90  ? 19.668  75.626 28.618  1.00 43.41  ?  245 LEU D O   1 
ATOM   7077 C CB  . LEU D 1 90  ? 22.579  76.927 28.411  1.00 40.42  ?  245 LEU D CB  1 
ATOM   7078 C CG  . LEU D 1 90  ? 23.770  77.413 27.612  1.00 43.95  ?  245 LEU D CG  1 
ATOM   7079 C CD1 . LEU D 1 90  ? 24.201  78.723 28.134  1.00 44.79  ?  245 LEU D CD1 1 
ATOM   7080 C CD2 . LEU D 1 90  ? 24.930  76.447 27.675  1.00 47.75  ?  245 LEU D CD2 1 
ATOM   7081 N N   . VAL D 1 91  ? 21.069  74.751 30.133  1.00 44.10  ?  246 VAL D N   1 
ATOM   7082 C CA  . VAL D 1 91  ? 20.085  74.422 31.145  1.00 45.34  ?  246 VAL D CA  1 
ATOM   7083 C C   . VAL D 1 91  ? 19.530  75.742 31.698  1.00 51.16  ?  246 VAL D C   1 
ATOM   7084 O O   . VAL D 1 91  ? 20.178  76.777 31.555  1.00 50.98  ?  246 VAL D O   1 
ATOM   7085 C CB  . VAL D 1 91  ? 20.779  73.462 32.157  1.00 49.45  ?  246 VAL D CB  1 
ATOM   7086 C CG1 . VAL D 1 91  ? 20.971  74.054 33.543  1.00 49.12  ?  246 VAL D CG1 1 
ATOM   7087 C CG2 . VAL D 1 91  ? 20.100  72.104 32.193  1.00 49.00  ?  246 VAL D CG2 1 
ATOM   7088 N N   . GLU D 1 92  ? 18.297  75.731 32.201  1.00 49.33  ?  247 GLU D N   1 
ATOM   7089 C CA  . GLU D 1 92  ? 17.638  76.934 32.700  1.00 49.80  ?  247 GLU D CA  1 
ATOM   7090 C C   . GLU D 1 92  ? 17.518  76.920 34.223  1.00 54.97  ?  247 GLU D C   1 
ATOM   7091 O O   . GLU D 1 92  ? 17.001  75.962 34.808  1.00 55.19  ?  247 GLU D O   1 
ATOM   7092 C CB  . GLU D 1 92  ? 16.253  77.087 32.049  1.00 51.33  ?  247 GLU D CB  1 
ATOM   7093 C CG  . GLU D 1 92  ? 15.725  78.516 32.061  1.00 72.68  ?  247 GLU D CG  1 
ATOM   7094 C CD  . GLU D 1 92  ? 14.252  78.737 31.738  1.00 102.82 ?  247 GLU D CD  1 
ATOM   7095 O OE1 . GLU D 1 92  ? 13.688  77.959 30.935  1.00 83.98  ?  247 GLU D OE1 1 
ATOM   7096 O OE2 . GLU D 1 92  ? 13.675  79.725 32.250  1.00 100.00 -1 247 GLU D OE2 1 
ATOM   7097 N N   . LEU D 1 93  ? 17.992  77.995 34.858  1.00 51.12  ?  248 LEU D N   1 
ATOM   7098 C CA  . LEU D 1 93  ? 17.890  78.168 36.302  1.00 50.21  ?  248 LEU D CA  1 
ATOM   7099 C C   . LEU D 1 93  ? 16.590  78.910 36.593  1.00 52.49  ?  248 LEU D C   1 
ATOM   7100 O O   . LEU D 1 93  ? 16.302  79.925 35.961  1.00 53.45  ?  248 LEU D O   1 
ATOM   7101 C CB  . LEU D 1 93  ? 19.097  78.952 36.833  1.00 49.92  ?  248 LEU D CB  1 
ATOM   7102 C CG  . LEU D 1 93  ? 19.294  79.005 38.350  1.00 53.59  ?  248 LEU D CG  1 
ATOM   7103 C CD1 . LEU D 1 93  ? 19.671  77.628 38.915  1.00 53.56  ?  248 LEU D CD1 1 
ATOM   7104 C CD2 . LEU D 1 93  ? 20.346  80.046 38.722  1.00 51.91  ?  248 LEU D CD2 1 
ATOM   7105 N N   . LEU D 1 94  ? 15.786  78.383 37.504  1.00 47.28  ?  249 LEU D N   1 
ATOM   7106 C CA  . LEU D 1 94  ? 14.526  79.037 37.849  1.00 45.91  ?  249 LEU D CA  1 
ATOM   7107 C C   . LEU D 1 94  ? 14.746  79.910 39.061  1.00 54.00  ?  249 LEU D C   1 
ATOM   7108 O O   . LEU D 1 94  ? 14.263  81.026 39.109  1.00 54.28  ?  249 LEU D O   1 
ATOM   7109 C CB  . LEU D 1 94  ? 13.393  78.025 38.066  1.00 44.33  ?  249 LEU D CB  1 
ATOM   7110 C CG  . LEU D 1 94  ? 12.976  77.236 36.812  1.00 46.28  ?  249 LEU D CG  1 
ATOM   7111 C CD1 . LEU D 1 94  ? 12.120  76.069 37.157  1.00 45.95  ?  249 LEU D CD1 1 
ATOM   7112 C CD2 . LEU D 1 94  ? 12.282  78.107 35.808  1.00 44.29  ?  249 LEU D CD2 1 
ATOM   7113 N N   . GLY D 1 95  ? 15.547  79.426 39.991  1.00 53.75  ?  250 GLY D N   1 
ATOM   7114 C CA  . GLY D 1 95  ? 15.875  80.130 41.216  1.00 54.66  ?  250 GLY D CA  1 
ATOM   7115 C C   . GLY D 1 95  ? 16.849  79.368 42.081  1.00 61.74  ?  250 GLY D C   1 
ATOM   7116 O O   . GLY D 1 95  ? 17.355  78.320 41.686  1.00 60.88  ?  250 GLY D O   1 
ATOM   7117 N N   . PHE D 1 96  ? 17.086  79.875 43.279  1.00 62.74  ?  251 PHE D N   1 
ATOM   7118 C CA  . PHE D 1 96  ? 18.032  79.297 44.228  1.00 65.21  ?  251 PHE D CA  1 
ATOM   7119 C C   . PHE D 1 96  ? 17.553  79.477 45.667  1.00 71.18  ?  251 PHE D C   1 
ATOM   7120 O O   . PHE D 1 96  ? 16.623  80.254 45.906  1.00 70.85  ?  251 PHE D O   1 
ATOM   7121 C CB  . PHE D 1 96  ? 19.400  79.999 44.057  1.00 68.11  ?  251 PHE D CB  1 
ATOM   7122 C CG  . PHE D 1 96  ? 19.272  81.504 44.014  1.00 71.20  ?  251 PHE D CG  1 
ATOM   7123 C CD1 . PHE D 1 96  ? 19.184  82.247 45.192  1.00 75.20  ?  251 PHE D CD1 1 
ATOM   7124 C CD2 . PHE D 1 96  ? 19.171  82.176 42.799  1.00 74.27  ?  251 PHE D CD2 1 
ATOM   7125 C CE1 . PHE D 1 96  ? 19.010  83.633 45.151  1.00 76.33  ?  251 PHE D CE1 1 
ATOM   7126 C CE2 . PHE D 1 96  ? 19.003  83.562 42.760  1.00 77.52  ?  251 PHE D CE2 1 
ATOM   7127 C CZ  . PHE D 1 96  ? 18.927  84.280 43.936  1.00 75.86  ?  251 PHE D CZ  1 
ATOM   7128 N N   . SER D 1 97  ? 18.239  78.810 46.621  1.00 69.49  ?  252 SER D N   1 
ATOM   7129 C CA  . SER D 1 97  ? 18.016  78.911 48.059  1.00 70.45  ?  252 SER D CA  1 
ATOM   7130 C C   . SER D 1 97  ? 19.381  78.960 48.764  1.00 80.40  ?  252 SER D C   1 
ATOM   7131 O O   . SER D 1 97  ? 20.212  78.063 48.574  1.00 80.37  ?  252 SER D O   1 
ATOM   7132 C CB  . SER D 1 97  ? 17.172  77.743 48.566  1.00 72.90  ?  252 SER D CB  1 
ATOM   7133 O OG  . SER D 1 97  ? 17.521  77.327 49.880  1.00 81.82  ?  252 SER D OG  1 
ATOM   7134 N N   . SER D 1 98  ? 19.611  80.022 49.552  1.00 81.13  ?  253 SER D N   1 
ATOM   7135 C CA  . SER D 1 98  ? 20.844  80.208 50.318  1.00 83.19  ?  253 SER D CA  1 
ATOM   7136 C C   . SER D 1 98  ? 20.541  80.455 51.813  1.00 93.17  ?  253 SER D C   1 
ATOM   7137 O O   . SER D 1 98  ? 21.325  81.102 52.508  1.00 93.70  ?  253 SER D O   1 
ATOM   7138 C CB  . SER D 1 98  ? 21.698  81.319 49.713  1.00 86.70  ?  253 SER D CB  1 
ATOM   7139 O OG  . SER D 1 98  ? 20.972  82.533 49.619  1.00 97.65  ?  253 SER D OG  1 
ATOM   7140 N N   . ASP D 1 99  ? 19.410  79.903 52.307  1.00 93.23  ?  254 ASP D N   1 
ATOM   7141 C CA  . ASP D 1 99  ? 18.967  80.016 53.702  1.00 94.43  ?  254 ASP D CA  1 
ATOM   7142 C C   . ASP D 1 99  ? 19.818  79.135 54.634  1.00 101.70 ?  254 ASP D C   1 
ATOM   7143 O O   . ASP D 1 99  ? 19.610  77.918 54.718  1.00 101.36 ?  254 ASP D O   1 
ATOM   7144 C CB  . ASP D 1 99  ? 17.466  79.694 53.827  1.00 96.21  ?  254 ASP D CB  1 
ATOM   7145 N N   . GLY D 1 100 ? 20.790  79.766 55.295  1.00 100.45 ?  255 GLY D N   1 
ATOM   7146 C CA  . GLY D 1 100 ? 21.705  79.108 56.223  1.00 100.96 ?  255 GLY D CA  1 
ATOM   7147 C C   . GLY D 1 100 ? 22.842  78.356 55.557  1.00 106.69 ?  255 GLY D C   1 
ATOM   7148 O O   . GLY D 1 100 ? 23.386  78.796 54.534  1.00 106.97 ?  255 GLY D O   1 
ATOM   7149 N N   . ASP D 1 101 ? 23.209  77.204 56.155  1.00 103.20 ?  256 ASP D N   1 
ATOM   7150 C CA  . ASP D 1 101 ? 24.296  76.323 55.705  1.00 102.28 ?  256 ASP D CA  1 
ATOM   7151 C C   . ASP D 1 101 ? 23.999  75.542 54.413  1.00 102.07 ?  256 ASP D C   1 
ATOM   7152 O O   . ASP D 1 101 ? 24.940  75.074 53.766  1.00 101.41 ?  256 ASP D O   1 
ATOM   7153 C CB  . ASP D 1 101 ? 24.717  75.361 56.839  1.00 104.55 ?  256 ASP D CB  1 
ATOM   7154 C CG  . ASP D 1 101 ? 25.347  76.020 58.068  1.00 116.48 ?  256 ASP D CG  1 
ATOM   7155 O OD1 . ASP D 1 101 ? 25.448  77.275 58.097  1.00 116.23 ?  256 ASP D OD1 1 
ATOM   7156 O OD2 . ASP D 1 101 ? 25.732  75.282 59.004  1.00 124.04 -1 256 ASP D OD2 1 
ATOM   7157 N N   . ASP D 1 102 ? 22.708  75.389 54.051  1.00 95.44  ?  257 ASP D N   1 
ATOM   7158 C CA  . ASP D 1 102 ? 22.290  74.657 52.850  1.00 93.51  ?  257 ASP D CA  1 
ATOM   7159 C C   . ASP D 1 102 ? 22.082  75.548 51.626  1.00 92.64  ?  257 ASP D C   1 
ATOM   7160 O O   . ASP D 1 102 ? 21.351  76.548 51.677  1.00 92.19  ?  257 ASP D O   1 
ATOM   7161 C CB  . ASP D 1 102 ? 21.066  73.775 53.125  1.00 95.23  ?  257 ASP D CB  1 
ATOM   7162 C CG  . ASP D 1 102 ? 21.387  72.554 53.963  1.00 102.88 ?  257 ASP D CG  1 
ATOM   7163 O OD1 . ASP D 1 102 ? 21.943  71.579 53.403  1.00 102.87 ?  257 ASP D OD1 1 
ATOM   7164 O OD2 . ASP D 1 102 ? 21.072  72.566 55.174  1.00 107.25 -1 257 ASP D OD2 1 
ATOM   7165 N N   . LEU D 1 103 ? 22.752  75.169 50.526  1.00 84.84  ?  258 LEU D N   1 
ATOM   7166 C CA  . LEU D 1 103 ? 22.741  75.890 49.258  1.00 82.35  ?  258 LEU D CA  1 
ATOM   7167 C C   . LEU D 1 103 ? 22.092  75.051 48.166  1.00 80.41  ?  258 LEU D C   1 
ATOM   7168 O O   . LEU D 1 103 ? 22.544  73.938 47.887  1.00 78.90  ?  258 LEU D O   1 
ATOM   7169 C CB  . LEU D 1 103 ? 24.181  76.275 48.892  1.00 82.43  ?  258 LEU D CB  1 
ATOM   7170 C CG  . LEU D 1 103 ? 24.655  77.710 49.184  1.00 87.45  ?  258 LEU D CG  1 
ATOM   7171 C CD1 . LEU D 1 103 ? 24.177  78.247 50.552  1.00 87.92  ?  258 LEU D CD1 1 
ATOM   7172 C CD2 . LEU D 1 103 ? 26.158  77.787 49.105  1.00 89.35  ?  258 LEU D CD2 1 
ATOM   7173 N N   . CYS D 1 104 ? 20.999  75.576 47.577  1.00 73.84  ?  259 CYS D N   1 
ATOM   7174 C CA  . CYS D 1 104 ? 20.221  74.890 46.548  1.00 72.09  ?  259 CYS D CA  1 
ATOM   7175 C C   . CYS D 1 104 ? 20.117  75.660 45.262  1.00 69.13  ?  259 CYS D C   1 
ATOM   7176 O O   . CYS D 1 104 ? 20.059  76.888 45.270  1.00 66.81  ?  259 CYS D O   1 
ATOM   7177 C CB  . CYS D 1 104 ? 18.836  74.518 47.067  1.00 73.00  ?  259 CYS D CB  1 
ATOM   7178 S SG  . CYS D 1 104 ? 18.847  73.254 48.355  1.00 77.50  ?  259 CYS D SG  1 
ATOM   7179 N N   . LEU D 1 105 ? 20.031  74.921 44.153  1.00 61.98  ?  260 LEU D N   1 
ATOM   7180 C CA  . LEU D 1 105 ? 19.830  75.494 42.836  1.00 60.18  ?  260 LEU D CA  1 
ATOM   7181 C C   . LEU D 1 105 ? 18.650  74.779 42.188  1.00 60.49  ?  260 LEU D C   1 
ATOM   7182 O O   . LEU D 1 105 ? 18.583  73.547 42.221  1.00 60.36  ?  260 LEU D O   1 
ATOM   7183 C CB  . LEU D 1 105 ? 21.119  75.434 41.998  1.00 60.12  ?  260 LEU D CB  1 
ATOM   7184 C CG  . LEU D 1 105 ? 22.222  76.417 42.421  1.00 63.96  ?  260 LEU D CG  1 
ATOM   7185 C CD1 . LEU D 1 105 ? 23.572  75.941 41.980  1.00 63.31  ?  260 LEU D CD1 1 
ATOM   7186 C CD2 . LEU D 1 105 ? 21.941  77.815 41.911  1.00 66.65  ?  260 LEU D CD2 1 
ATOM   7187 N N   . VAL D 1 106 ? 17.667  75.564 41.693  1.00 54.30  ?  261 VAL D N   1 
ATOM   7188 C CA  . VAL D 1 106 ? 16.413  75.052 41.105  1.00 52.34  ?  261 VAL D CA  1 
ATOM   7189 C C   . VAL D 1 106 ? 16.375  75.271 39.623  1.00 53.57  ?  261 VAL D C   1 
ATOM   7190 O O   . VAL D 1 106 ? 16.408  76.424 39.154  1.00 52.59  ?  261 VAL D O   1 
ATOM   7191 C CB  . VAL D 1 106 ? 15.124  75.565 41.800  1.00 54.70  ?  261 VAL D CB  1 
ATOM   7192 C CG1 . VAL D 1 106 ? 13.914  74.762 41.350  1.00 53.97  ?  261 VAL D CG1 1 
ATOM   7193 C CG2 . VAL D 1 106 ? 15.258  75.503 43.314  1.00 54.28  ?  261 VAL D CG2 1 
ATOM   7194 N N   . TYR D 1 107 ? 16.282  74.148 38.886  1.00 47.46  ?  262 TYR D N   1 
ATOM   7195 C CA  . TYR D 1 107 ? 16.306  74.135 37.416  1.00 45.68  ?  262 TYR D CA  1 
ATOM   7196 C C   . TYR D 1 107 ? 15.051  73.550 36.808  1.00 46.92  ?  262 TYR D C   1 
ATOM   7197 O O   . TYR D 1 107 ? 14.352  72.794 37.481  1.00 45.64  ?  262 TYR D O   1 
ATOM   7198 C CB  . TYR D 1 107 ? 17.461  73.258 36.939  1.00 46.14  ?  262 TYR D CB  1 
ATOM   7199 C CG  . TYR D 1 107 ? 18.835  73.659 37.426  1.00 47.33  ?  262 TYR D CG  1 
ATOM   7200 C CD1 . TYR D 1 107 ? 19.350  73.151 38.618  1.00 49.40  ?  262 TYR D CD1 1 
ATOM   7201 C CD2 . TYR D 1 107 ? 19.662  74.463 36.647  1.00 47.62  ?  262 TYR D CD2 1 
ATOM   7202 C CE1 . TYR D 1 107 ? 20.650  73.456 39.031  1.00 50.83  ?  262 TYR D CE1 1 
ATOM   7203 C CE2 . TYR D 1 107 ? 20.962  74.769 37.048  1.00 48.01  ?  262 TYR D CE2 1 
ATOM   7204 C CZ  . TYR D 1 107 ? 21.446  74.275 38.246  1.00 57.47  ?  262 TYR D CZ  1 
ATOM   7205 O OH  . TYR D 1 107 ? 22.725  74.580 38.635  1.00 61.06  ?  262 TYR D OH  1 
ATOM   7206 N N   . VAL D 1 108 ? 14.788  73.861 35.508  1.00 42.17  ?  263 VAL D N   1 
ATOM   7207 C CA  . VAL D 1 108 ? 13.700  73.286 34.721  1.00 41.39  ?  263 VAL D CA  1 
ATOM   7208 C C   . VAL D 1 108 ? 14.078  71.815 34.541  1.00 45.53  ?  263 VAL D C   1 
ATOM   7209 O O   . VAL D 1 108 ? 15.137  71.534 33.975  1.00 45.42  ?  263 VAL D O   1 
ATOM   7210 C CB  . VAL D 1 108 ? 13.547  73.985 33.342  1.00 45.88  ?  263 VAL D CB  1 
ATOM   7211 C CG1 . VAL D 1 108 ? 12.661  73.174 32.392  1.00 45.76  ?  263 VAL D CG1 1 
ATOM   7212 C CG2 . VAL D 1 108 ? 13.015  75.406 33.481  1.00 45.78  ?  263 VAL D CG2 1 
ATOM   7213 N N   . TYR D 1 109 ? 13.243  70.884 35.058  1.00 41.62  ?  264 TYR D N   1 
ATOM   7214 C CA  . TYR D 1 109 ? 13.493  69.445 34.972  1.00 41.14  ?  264 TYR D CA  1 
ATOM   7215 C C   . TYR D 1 109 ? 13.678  68.933 33.531  1.00 46.98  ?  264 TYR D C   1 
ATOM   7216 O O   . TYR D 1 109 ? 12.918  69.294 32.638  1.00 46.53  ?  264 TYR D O   1 
ATOM   7217 C CB  . TYR D 1 109 ? 12.420  68.678 35.738  1.00 41.23  ?  264 TYR D CB  1 
ATOM   7218 C CG  . TYR D 1 109 ? 12.309  67.194 35.476  1.00 43.44  ?  264 TYR D CG  1 
ATOM   7219 C CD1 . TYR D 1 109 ? 12.965  66.273 36.288  1.00 46.09  ?  264 TYR D CD1 1 
ATOM   7220 C CD2 . TYR D 1 109 ? 11.412  66.701 34.530  1.00 44.19  ?  264 TYR D CD2 1 
ATOM   7221 C CE1 . TYR D 1 109 ? 12.791  64.895 36.113  1.00 47.48  ?  264 TYR D CE1 1 
ATOM   7222 C CE2 . TYR D 1 109 ? 11.231  65.328 34.346  1.00 44.74  ?  264 TYR D CE2 1 
ATOM   7223 C CZ  . TYR D 1 109 ? 11.931  64.428 35.130  1.00 51.84  ?  264 TYR D CZ  1 
ATOM   7224 O OH  . TYR D 1 109 ? 11.734  63.076 34.955  1.00 53.27  ?  264 TYR D OH  1 
ATOM   7225 N N   . MET D 1 110 ? 14.719  68.100 33.336  1.00 44.25  ?  265 MET D N   1 
ATOM   7226 C CA  . MET D 1 110 ? 15.083  67.467 32.075  1.00 43.46  ?  265 MET D CA  1 
ATOM   7227 C C   . MET D 1 110 ? 14.437  66.079 31.976  1.00 48.50  ?  265 MET D C   1 
ATOM   7228 O O   . MET D 1 110 ? 14.912  65.122 32.591  1.00 48.81  ?  265 MET D O   1 
ATOM   7229 C CB  . MET D 1 110 ? 16.618  67.405 31.915  1.00 45.16  ?  265 MET D CB  1 
ATOM   7230 C CG  . MET D 1 110 ? 17.266  68.779 31.671  1.00 47.94  ?  265 MET D CG  1 
ATOM   7231 S SD  . MET D 1 110 ? 16.724  69.661 30.170  1.00 50.98  ?  265 MET D SD  1 
ATOM   7232 C CE  . MET D 1 110 ? 15.435  70.666 30.829  1.00 47.69  ?  265 MET D CE  1 
ATOM   7233 N N   . PRO D 1 111 ? 13.329  65.950 31.217  1.00 45.34  ?  266 PRO D N   1 
ATOM   7234 C CA  . PRO D 1 111 ? 12.653  64.642 31.105  1.00 44.76  ?  266 PRO D CA  1 
ATOM   7235 C C   . PRO D 1 111 ? 13.535  63.451 30.691  1.00 48.24  ?  266 PRO D C   1 
ATOM   7236 O O   . PRO D 1 111 ? 13.183  62.298 30.968  1.00 49.62  ?  266 PRO D O   1 
ATOM   7237 C CB  . PRO D 1 111 ? 11.578  64.906 30.050  1.00 46.37  ?  266 PRO D CB  1 
ATOM   7238 C CG  . PRO D 1 111 ? 11.313  66.366 30.128  1.00 50.79  ?  266 PRO D CG  1 
ATOM   7239 C CD  . PRO D 1 111 ? 12.618  66.991 30.443  1.00 46.81  ?  266 PRO D CD  1 
ATOM   7240 N N   . ASN D 1 112 ? 14.657  63.706 30.024  1.00 41.73  ?  267 ASN D N   1 
ATOM   7241 C CA  . ASN D 1 112 ? 15.485  62.593 29.586  1.00 41.31  ?  267 ASN D CA  1 
ATOM   7242 C C   . ASN D 1 112 ? 16.847  62.434 30.277  1.00 43.65  ?  267 ASN D C   1 
ATOM   7243 O O   . ASN D 1 112 ? 17.697  61.706 29.759  1.00 43.49  ?  267 ASN D O   1 
ATOM   7244 C CB  . ASN D 1 112 ? 15.583  62.556 28.069  1.00 40.70  ?  267 ASN D CB  1 
ATOM   7245 C CG  . ASN D 1 112 ? 14.319  62.076 27.456  1.00 47.93  ?  267 ASN D CG  1 
ATOM   7246 O OD1 . ASN D 1 112 ? 13.904  60.933 27.662  1.00 43.64  ?  267 ASN D OD1 1 
ATOM   7247 N ND2 . ASN D 1 112 ? 13.685  62.927 26.679  1.00 43.70  ?  267 ASN D ND2 1 
ATOM   7248 N N   . GLY D 1 113 ? 17.000  63.062 31.455  1.00 37.20  ?  268 GLY D N   1 
ATOM   7249 C CA  . GLY D 1 113 ? 18.213  63.043 32.268  1.00 35.41  ?  268 GLY D CA  1 
ATOM   7250 C C   . GLY D 1 113 ? 19.481  63.420 31.521  1.00 39.17  ?  268 GLY D C   1 
ATOM   7251 O O   . GLY D 1 113 ? 19.449  64.259 30.621  1.00 39.44  ?  268 GLY D O   1 
ATOM   7252 N N   . SER D 1 114 ? 20.607  62.762 31.868  1.00 35.48  ?  269 SER D N   1 
ATOM   7253 C CA  . SER D 1 114 ? 21.908  62.986 31.248  1.00 33.98  ?  269 SER D CA  1 
ATOM   7254 C C   . SER D 1 114 ? 22.193  62.062 30.051  1.00 38.02  ?  269 SER D C   1 
ATOM   7255 O O   . SER D 1 114 ? 21.656  60.954 29.962  1.00 38.71  ?  269 SER D O   1 
ATOM   7256 C CB  . SER D 1 114 ? 23.009  62.845 32.286  1.00 36.01  ?  269 SER D CB  1 
ATOM   7257 O OG  . SER D 1 114 ? 23.112  61.522 32.780  1.00 49.30  ?  269 SER D OG  1 
ATOM   7258 N N   . LEU D 1 115 ? 23.068  62.534 29.146  1.00 32.34  ?  270 LEU D N   1 
ATOM   7259 C CA  . LEU D 1 115 ? 23.544  61.808 27.987  1.00 31.46  ?  270 LEU D CA  1 
ATOM   7260 C C   . LEU D 1 115 ? 24.289  60.527 28.461  1.00 37.58  ?  270 LEU D C   1 
ATOM   7261 O O   . LEU D 1 115 ? 24.162  59.475 27.830  1.00 36.76  ?  270 LEU D O   1 
ATOM   7262 C CB  . LEU D 1 115 ? 24.481  62.726 27.181  1.00 31.38  ?  270 LEU D CB  1 
ATOM   7263 C CG  . LEU D 1 115 ? 25.185  62.118 25.965  1.00 37.09  ?  270 LEU D CG  1 
ATOM   7264 C CD1 . LEU D 1 115 ? 24.174  61.509 24.970  1.00 35.73  ?  270 LEU D CD1 1 
ATOM   7265 C CD2 . LEU D 1 115 ? 26.078  63.134 25.295  1.00 41.18  ?  270 LEU D CD2 1 
ATOM   7266 N N   . LEU D 1 116 ? 25.039  60.619 29.589  1.00 34.97  ?  271 LEU D N   1 
ATOM   7267 C CA  . LEU D 1 116 ? 25.758  59.493 30.181  1.00 34.47  ?  271 LEU D CA  1 
ATOM   7268 C C   . LEU D 1 116 ? 24.758  58.352 30.424  1.00 41.33  ?  271 LEU D C   1 
ATOM   7269 O O   . LEU D 1 116 ? 24.907  57.265 29.848  1.00 41.20  ?  271 LEU D O   1 
ATOM   7270 C CB  . LEU D 1 116 ? 26.435  59.924 31.500  1.00 33.58  ?  271 LEU D CB  1 
ATOM   7271 C CG  . LEU D 1 116 ? 27.373  58.873 32.169  1.00 35.51  ?  271 LEU D CG  1 
ATOM   7272 C CD1 . LEU D 1 116 ? 28.755  58.856 31.540  1.00 35.85  ?  271 LEU D CD1 1 
ATOM   7273 C CD2 . LEU D 1 116 ? 27.548  59.141 33.626  1.00 30.84  ?  271 LEU D CD2 1 
ATOM   7274 N N   . ASP D 1 117 ? 23.681  58.655 31.180  1.00 38.75  ?  272 ASP D N   1 
ATOM   7275 C CA  . ASP D 1 117 ? 22.638  57.695 31.529  1.00 38.13  ?  272 ASP D CA  1 
ATOM   7276 C C   . ASP D 1 117 ? 21.901  57.110 30.342  1.00 41.09  ?  272 ASP D C   1 
ATOM   7277 O O   . ASP D 1 117 ? 21.639  55.904 30.324  1.00 42.33  ?  272 ASP D O   1 
ATOM   7278 C CB  . ASP D 1 117 ? 21.710  58.256 32.605  1.00 40.13  ?  272 ASP D CB  1 
ATOM   7279 C CG  . ASP D 1 117 ? 22.441  58.544 33.908  1.00 57.36  ?  272 ASP D CG  1 
ATOM   7280 O OD1 . ASP D 1 117 ? 23.572  58.026 34.087  1.00 59.58  ?  272 ASP D OD1 1 
ATOM   7281 O OD2 . ASP D 1 117 ? 21.869  59.251 34.766  1.00 65.20  -1 272 ASP D OD2 1 
ATOM   7282 N N   . ARG D 1 118 ? 21.657  57.928 29.319  1.00 35.58  ?  273 ARG D N   1 
ATOM   7283 C CA  . ARG D 1 118 ? 20.971  57.484 28.115  1.00 35.28  ?  273 ARG D CA  1 
ATOM   7284 C C   . ARG D 1 118 ? 21.848  56.606 27.240  1.00 37.15  ?  273 ARG D C   1 
ATOM   7285 O O   . ARG D 1 118 ? 21.347  55.667 26.613  1.00 34.60  ?  273 ARG D O   1 
ATOM   7286 C CB  . ARG D 1 118 ? 20.317  58.664 27.342  1.00 35.45  ?  273 ARG D CB  1 
ATOM   7287 C CG  . ARG D 1 118 ? 19.260  59.457 28.137  1.00 31.58  ?  273 ARG D CG  1 
ATOM   7288 C CD  . ARG D 1 118 ? 17.960  58.715 28.491  1.00 36.98  ?  273 ARG D CD  1 
ATOM   7289 N NE  . ARG D 1 118 ? 18.088  57.686 29.534  1.00 42.71  ?  273 ARG D NE  1 
ATOM   7290 C CZ  . ARG D 1 118 ? 18.235  57.926 30.836  1.00 64.13  ?  273 ARG D CZ  1 
ATOM   7291 N NH1 . ARG D 1 118 ? 18.328  56.917 31.695  1.00 44.98  ?  273 ARG D NH1 1 
ATOM   7292 N NH2 . ARG D 1 118 ? 18.312  59.177 31.286  1.00 61.84  1  273 ARG D NH2 1 
ATOM   7293 N N   . LEU D 1 119 ? 23.168  56.866 27.263  1.00 35.26  ?  274 LEU D N   1 
ATOM   7294 C CA  . LEU D 1 119 ? 24.145  56.078 26.527  1.00 34.97  ?  274 LEU D CA  1 
ATOM   7295 C C   . LEU D 1 119 ? 24.299  54.711 27.171  1.00 40.40  ?  274 LEU D C   1 
ATOM   7296 O O   . LEU D 1 119 ? 24.577  53.732 26.473  1.00 42.83  ?  274 LEU D O   1 
ATOM   7297 C CB  . LEU D 1 119 ? 25.503  56.796 26.429  1.00 34.90  ?  274 LEU D CB  1 
ATOM   7298 C CG  . LEU D 1 119 ? 25.614  57.960 25.422  1.00 40.11  ?  274 LEU D CG  1 
ATOM   7299 C CD1 . LEU D 1 119 ? 27.012  58.589 25.470  1.00 41.00  ?  274 LEU D CD1 1 
ATOM   7300 C CD2 . LEU D 1 119 ? 25.268  57.540 23.979  1.00 39.33  ?  274 LEU D CD2 1 
ATOM   7301 N N   . SER D 1 120 ? 24.095  54.620 28.486  1.00 35.18  ?  275 SER D N   1 
ATOM   7302 C CA  . SER D 1 120 ? 24.180  53.345 29.185  1.00 34.17  ?  275 SER D CA  1 
ATOM   7303 C C   . SER D 1 120 ? 22.803  52.628 29.304  1.00 37.91  ?  275 SER D C   1 
ATOM   7304 O O   . SER D 1 120 ? 22.758  51.471 29.739  1.00 38.71  ?  275 SER D O   1 
ATOM   7305 C CB  . SER D 1 120 ? 24.816  53.540 30.556  1.00 37.19  ?  275 SER D CB  1 
ATOM   7306 O OG  . SER D 1 120 ? 24.027  54.384 31.378  1.00 46.98  ?  275 SER D OG  1 
ATOM   7307 N N   . CYS D 1 121 ? 21.678  53.326 28.935  1.00 32.70  ?  276 CYS D N   1 
ATOM   7308 C CA  . CYS D 1 121 ? 20.255  52.873 28.979  1.00 31.18  ?  276 CYS D CA  1 
ATOM   7309 C C   . CYS D 1 121 ? 19.817  52.683 30.402  1.00 33.91  ?  276 CYS D C   1 
ATOM   7310 O O   . CYS D 1 121 ? 18.942  51.860 30.703  1.00 32.49  ?  276 CYS D O   1 
ATOM   7311 C CB  . CYS D 1 121 ? 19.996  51.630 28.130  1.00 30.77  ?  276 CYS D CB  1 
ATOM   7312 S SG  . CYS D 1 121 ? 20.385  51.847 26.384  1.00 34.88  ?  276 CYS D SG  1 
ATOM   7313 N N   . LEU D 1 122 ? 20.410  53.495 31.284  1.00 30.92  ?  277 LEU D N   1 
ATOM   7314 C CA  . LEU D 1 122 ? 20.095  53.457 32.689  1.00 31.77  ?  277 LEU D CA  1 
ATOM   7315 C C   . LEU D 1 122 ? 18.569  53.502 32.897  1.00 36.96  ?  277 LEU D C   1 
ATOM   7316 O O   . LEU D 1 122 ? 17.866  54.301 32.267  1.00 35.43  ?  277 LEU D O   1 
ATOM   7317 C CB  . LEU D 1 122 ? 20.827  54.587 33.424  1.00 31.98  ?  277 LEU D CB  1 
ATOM   7318 C CG  . LEU D 1 122 ? 20.698  54.579 34.948  1.00 36.86  ?  277 LEU D CG  1 
ATOM   7319 C CD1 . LEU D 1 122 ? 21.452  53.405 35.561  1.00 37.23  ?  277 LEU D CD1 1 
ATOM   7320 C CD2 . LEU D 1 122 ? 21.178  55.874 35.524  1.00 38.58  ?  277 LEU D CD2 1 
ATOM   7321 N N   . ASP D 1 123 ? 18.068  52.570 33.719  1.00 35.16  ?  278 ASP D N   1 
ATOM   7322 C CA  . ASP D 1 123 ? 16.650  52.425 34.063  1.00 36.12  ?  278 ASP D CA  1 
ATOM   7323 C C   . ASP D 1 123 ? 15.785  51.890 32.928  1.00 41.03  ?  278 ASP D C   1 
ATOM   7324 O O   . ASP D 1 123 ? 14.555  52.056 32.955  1.00 40.26  ?  278 ASP D O   1 
ATOM   7325 C CB  . ASP D 1 123 ? 16.060  53.690 34.734  1.00 38.28  ?  278 ASP D CB  1 
ATOM   7326 C CG  . ASP D 1 123 ? 16.842  54.150 35.949  1.00 54.60  ?  278 ASP D CG  1 
ATOM   7327 O OD1 . ASP D 1 123 ? 17.138  53.297 36.823  1.00 56.47  ?  278 ASP D OD1 1 
ATOM   7328 O OD2 . ASP D 1 123 ? 17.162  55.366 36.027  1.00 63.90  -1 278 ASP D OD2 1 
ATOM   7329 N N   . GLY D 1 124 ? 16.437  51.211 31.974  1.00 36.92  ?  279 GLY D N   1 
ATOM   7330 C CA  . GLY D 1 124 ? 15.783  50.587 30.834  1.00 36.87  ?  279 GLY D CA  1 
ATOM   7331 C C   . GLY D 1 124 ? 15.245  51.482 29.739  1.00 41.69  ?  279 GLY D C   1 
ATOM   7332 O O   . GLY D 1 124 ? 14.378  51.061 28.972  1.00 42.31  ?  279 GLY D O   1 
ATOM   7333 N N   . THR D 1 125 ? 15.767  52.694 29.619  1.00 38.19  ?  280 THR D N   1 
ATOM   7334 C CA  . THR D 1 125 ? 15.368  53.620 28.552  1.00 37.30  ?  280 THR D CA  1 
ATOM   7335 C C   . THR D 1 125 ? 15.841  53.035 27.200  1.00 41.13  ?  280 THR D C   1 
ATOM   7336 O O   . THR D 1 125 ? 16.861  52.349 27.194  1.00 41.98  ?  280 THR D O   1 
ATOM   7337 C CB  . THR D 1 125 ? 15.959  55.003 28.833  1.00 38.96  ?  280 THR D CB  1 
ATOM   7338 O OG1 . THR D 1 125 ? 17.394  54.990 28.683  1.00 39.40  ?  280 THR D OG1 1 
ATOM   7339 C CG2 . THR D 1 125 ? 15.560  55.530 30.212  1.00 31.06  ?  280 THR D CG2 1 
ATOM   7340 N N   . PRO D 1 126 ? 15.143  53.237 26.061  1.00 35.78  ?  281 PRO D N   1 
ATOM   7341 C CA  . PRO D 1 126 ? 15.633  52.665 24.792  1.00 34.88  ?  281 PRO D CA  1 
ATOM   7342 C C   . PRO D 1 126 ? 16.948  53.285 24.320  1.00 39.96  ?  281 PRO D C   1 
ATOM   7343 O O   . PRO D 1 126 ? 17.219  54.456 24.649  1.00 39.97  ?  281 PRO D O   1 
ATOM   7344 C CB  . PRO D 1 126 ? 14.484  52.935 23.818  1.00 35.45  ?  281 PRO D CB  1 
ATOM   7345 C CG  . PRO D 1 126 ? 13.789  54.055 24.371  1.00 39.07  ?  281 PRO D CG  1 
ATOM   7346 C CD  . PRO D 1 126 ? 13.885  53.970 25.856  1.00 35.37  ?  281 PRO D CD  1 
ATOM   7347 N N   . PRO D 1 127 ? 17.782  52.540 23.557  1.00 37.26  ?  282 PRO D N   1 
ATOM   7348 C CA  . PRO D 1 127 ? 19.054  53.138 23.092  1.00 38.10  ?  282 PRO D CA  1 
ATOM   7349 C C   . PRO D 1 127 ? 18.852  54.340 22.176  1.00 40.98  ?  282 PRO D C   1 
ATOM   7350 O O   . PRO D 1 127 ? 17.899  54.356 21.397  1.00 39.56  ?  282 PRO D O   1 
ATOM   7351 C CB  . PRO D 1 127 ? 19.740  51.989 22.329  1.00 39.82  ?  282 PRO D CB  1 
ATOM   7352 C CG  . PRO D 1 127 ? 19.042  50.742 22.743  1.00 43.30  ?  282 PRO D CG  1 
ATOM   7353 C CD  . PRO D 1 127 ? 17.625  51.160 23.054  1.00 38.16  ?  282 PRO D CD  1 
ATOM   7354 N N   . LEU D 1 128 ? 19.743  55.343 22.272  1.00 37.35  ?  283 LEU D N   1 
ATOM   7355 C CA  . LEU D 1 128 ? 19.712  56.512 21.373  1.00 35.73  ?  283 LEU D CA  1 
ATOM   7356 C C   . LEU D 1 128 ? 20.205  56.127 19.968  1.00 39.30  ?  283 LEU D C   1 
ATOM   7357 O O   . LEU D 1 128 ? 21.219  55.475 19.828  1.00 38.31  ?  283 LEU D O   1 
ATOM   7358 C CB  . LEU D 1 128 ? 20.580  57.655 21.884  1.00 34.86  ?  283 LEU D CB  1 
ATOM   7359 C CG  . LEU D 1 128 ? 20.190  58.242 23.214  1.00 39.45  ?  283 LEU D CG  1 
ATOM   7360 C CD1 . LEU D 1 128 ? 21.288  59.105 23.740  1.00 38.20  ?  283 LEU D CD1 1 
ATOM   7361 C CD2 . LEU D 1 128 ? 18.862  59.015 23.126  1.00 44.05  ?  283 LEU D CD2 1 
ATOM   7362 N N   . SER D 1 129 ? 19.485  56.528 18.936  1.00 36.32  ?  284 SER D N   1 
ATOM   7363 C CA  . SER D 1 129 ? 19.864  56.256 17.554  1.00 34.80  ?  284 SER D CA  1 
ATOM   7364 C C   . SER D 1 129 ? 21.002  57.186 17.127  1.00 39.36  ?  284 SER D C   1 
ATOM   7365 O O   . SER D 1 129 ? 21.249  58.211 17.782  1.00 38.07  ?  284 SER D O   1 
ATOM   7366 C CB  . SER D 1 129 ? 18.663  56.499 16.654  1.00 34.02  ?  284 SER D CB  1 
ATOM   7367 O OG  . SER D 1 129 ? 18.137  57.792 16.909  1.00 34.62  ?  284 SER D OG  1 
ATOM   7368 N N   . TRP D 1 130 ? 21.653  56.863 15.993  1.00 37.09  ?  285 TRP D N   1 
ATOM   7369 C CA  . TRP D 1 130 ? 22.716  57.674 15.433  1.00 37.31  ?  285 TRP D CA  1 
ATOM   7370 C C   . TRP D 1 130 ? 22.274  59.109 15.184  1.00 40.82  ?  285 TRP D C   1 
ATOM   7371 O O   . TRP D 1 130 ? 23.000  60.048 15.519  1.00 40.75  ?  285 TRP D O   1 
ATOM   7372 C CB  . TRP D 1 130 ? 23.236  57.057 14.143  1.00 36.94  ?  285 TRP D CB  1 
ATOM   7373 C CG  . TRP D 1 130 ? 24.330  57.866 13.509  1.00 39.20  ?  285 TRP D CG  1 
ATOM   7374 C CD1 . TRP D 1 130 ? 24.335  58.386 12.251  1.00 42.15  ?  285 TRP D CD1 1 
ATOM   7375 C CD2 . TRP D 1 130 ? 25.570  58.279 14.122  1.00 39.63  ?  285 TRP D CD2 1 
ATOM   7376 N NE1 . TRP D 1 130 ? 25.505  59.070 12.026  1.00 42.43  ?  285 TRP D NE1 1 
ATOM   7377 C CE2 . TRP D 1 130 ? 26.282  59.027 13.158  1.00 44.20  ?  285 TRP D CE2 1 
ATOM   7378 C CE3 . TRP D 1 130 ? 26.166  58.062 15.388  1.00 40.91  ?  285 TRP D CE3 1 
ATOM   7379 C CZ2 . TRP D 1 130 ? 27.543  59.605 13.430  1.00 43.69  ?  285 TRP D CZ2 1 
ATOM   7380 C CZ3 . TRP D 1 130 ? 27.410  58.633 15.661  1.00 42.29  ?  285 TRP D CZ3 1 
ATOM   7381 C CH2 . TRP D 1 130 ? 28.103  59.359 14.676  1.00 43.18  ?  285 TRP D CH2 1 
ATOM   7382 N N   . HIS D 1 131 ? 21.073  59.262 14.607  1.00 37.07  ?  286 HIS D N   1 
ATOM   7383 C CA  . HIS D 1 131 ? 20.439  60.508 14.226  1.00 36.70  ?  286 HIS D CA  1 
ATOM   7384 C C   . HIS D 1 131 ? 20.254  61.429 15.434  1.00 40.75  ?  286 HIS D C   1 
ATOM   7385 O O   . HIS D 1 131 ? 20.607  62.604 15.370  1.00 39.82  ?  286 HIS D O   1 
ATOM   7386 C CB  . HIS D 1 131 ? 19.099  60.203 13.531  1.00 38.09  ?  286 HIS D CB  1 
ATOM   7387 C CG  . HIS D 1 131 ? 18.339  61.429 13.136  1.00 41.89  ?  286 HIS D CG  1 
ATOM   7388 N ND1 . HIS D 1 131 ? 18.487  62.218 12.045  1.00 43.76  ?  286 HIS D ND1 1 
ATOM   7389 C CD2 . HIS D 1 131 ? 17.347  61.962 13.955  1.00 43.49  ?  286 HIS D CD2 1 
ATOM   7390 C CE1 . HIS D 1 131 ? 17.599  63.256 12.192  1.00 43.39  ?  286 HIS D CE1 1 
ATOM   7391 N NE2 . HIS D 1 131 ? 16.942  63.060 13.344  1.00 43.67  ?  286 HIS D NE2 1 
ATOM   7392 N N   . MET D 1 132 ? 19.702  60.893 16.533  1.00 37.69  ?  287 MET D N   1 
ATOM   7393 C CA  . MET D 1 132 ? 19.504  61.605 17.788  1.00 37.70  ?  287 MET D CA  1 
ATOM   7394 C C   . MET D 1 132 ? 20.899  62.054 18.302  1.00 40.30  ?  287 MET D C   1 
ATOM   7395 O O   . MET D 1 132 ? 21.071  63.215 18.686  1.00 40.80  ?  287 MET D O   1 
ATOM   7396 C CB  . MET D 1 132 ? 18.918  60.627 18.797  1.00 40.65  ?  287 MET D CB  1 
ATOM   7397 C CG  . MET D 1 132 ? 17.611  61.011 19.437  1.00 45.46  ?  287 MET D CG  1 
ATOM   7398 S SD  . MET D 1 132 ? 16.763  59.395 19.640  1.00 50.61  ?  287 MET D SD  1 
ATOM   7399 C CE  . MET D 1 132 ? 15.861  59.723 21.116  1.00 47.32  ?  287 MET D CE  1 
ATOM   7400 N N   . ARG D 1 133 ? 21.894  61.149 18.254  1.00 35.75  ?  288 ARG D N   1 
ATOM   7401 C CA  . ARG D 1 133 ? 23.290  61.422 18.662  1.00 36.46  ?  288 ARG D CA  1 
ATOM   7402 C C   . ARG D 1 133 ? 23.926  62.577 17.850  1.00 41.30  ?  288 ARG D C   1 
ATOM   7403 O O   . ARG D 1 133 ? 24.659  63.398 18.409  1.00 40.68  ?  288 ARG D O   1 
ATOM   7404 C CB  . ARG D 1 133 ? 24.138  60.170 18.499  1.00 35.26  ?  288 ARG D CB  1 
ATOM   7405 C CG  . ARG D 1 133 ? 23.847  59.136 19.540  1.00 42.99  ?  288 ARG D CG  1 
ATOM   7406 C CD  . ARG D 1 133 ? 24.562  57.856 19.196  1.00 37.63  ?  288 ARG D CD  1 
ATOM   7407 N NE  . ARG D 1 133 ? 23.842  56.736 19.778  1.00 35.14  ?  288 ARG D NE  1 
ATOM   7408 C CZ  . ARG D 1 133 ? 24.363  55.827 20.586  1.00 44.14  ?  288 ARG D CZ  1 
ATOM   7409 N NH1 . ARG D 1 133 ? 25.655  55.868 20.897  1.00 39.42  ?  288 ARG D NH1 1 
ATOM   7410 N NH2 . ARG D 1 133 ? 23.610  54.833 21.048  1.00 21.46  1  288 ARG D NH2 1 
ATOM   7411 N N   . CYS D 1 134 ? 23.619  62.636 16.534  1.00 36.31  ?  289 CYS D N   1 
ATOM   7412 C CA  . CYS D 1 134 ? 24.081  63.690 15.665  1.00 34.94  ?  289 CYS D CA  1 
ATOM   7413 C C   . CYS D 1 134 ? 23.494  65.011 16.091  1.00 36.94  ?  289 CYS D C   1 
ATOM   7414 O O   . CYS D 1 134 ? 24.249  65.972 16.247  1.00 38.24  ?  289 CYS D O   1 
ATOM   7415 C CB  . CYS D 1 134 ? 23.813  63.372 14.196  1.00 35.21  ?  289 CYS D CB  1 
ATOM   7416 S SG  . CYS D 1 134 ? 24.880  62.065 13.524  1.00 39.09  ?  289 CYS D SG  1 
ATOM   7417 N N   . LYS D 1 135 ? 22.195  65.043 16.404  1.00 32.33  ?  290 LYS D N   1 
ATOM   7418 C CA  . LYS D 1 135 ? 21.530  66.261 16.895  1.00 32.39  ?  290 LYS D CA  1 
ATOM   7419 C C   . LYS D 1 135 ? 22.039  66.591 18.295  1.00 38.83  ?  290 LYS D C   1 
ATOM   7420 O O   . LYS D 1 135 ? 22.228  67.766 18.615  1.00 40.07  ?  290 LYS D O   1 
ATOM   7421 C CB  . LYS D 1 135 ? 19.993  66.170 16.835  1.00 34.46  ?  290 LYS D CB  1 
ATOM   7422 C CG  . LYS D 1 135 ? 19.449  66.345 15.404  1.00 63.54  ?  290 LYS D CG  1 
ATOM   7423 C CD  . LYS D 1 135 ? 17.924  66.623 15.334  1.00 76.01  ?  290 LYS D CD  1 
ATOM   7424 C CE  . LYS D 1 135 ? 17.459  67.380 14.090  1.00 70.71  ?  290 LYS D CE  1 
ATOM   7425 N NZ  . LYS D 1 135 ? 17.832  68.832 14.105  1.00 61.42  1  290 LYS D NZ  1 
ATOM   7426 N N   . ILE D 1 136 ? 22.345  65.562 19.106  1.00 34.69  ?  291 ILE D N   1 
ATOM   7427 C CA  . ILE D 1 136 ? 22.923  65.805 20.427  1.00 34.11  ?  291 ILE D CA  1 
ATOM   7428 C C   . ILE D 1 136 ? 24.292  66.511 20.254  1.00 40.27  ?  291 ILE D C   1 
ATOM   7429 O O   . ILE D 1 136 ? 24.467  67.611 20.777  1.00 39.48  ?  291 ILE D O   1 
ATOM   7430 C CB  . ILE D 1 136 ? 22.960  64.512 21.296  1.00 35.36  ?  291 ILE D CB  1 
ATOM   7431 C CG1 . ILE D 1 136 ? 21.554  64.254 21.883  1.00 33.78  ?  291 ILE D CG1 1 
ATOM   7432 C CG2 . ILE D 1 136 ? 24.002  64.642 22.422  1.00 35.06  ?  291 ILE D CG2 1 
ATOM   7433 C CD1 . ILE D 1 136 ? 21.164  62.805 22.132  1.00 30.06  ?  291 ILE D CD1 1 
ATOM   7434 N N   . ALA D 1 137 ? 25.206  65.912 19.447  1.00 39.00  ?  292 ALA D N   1 
ATOM   7435 C CA  . ALA D 1 137 ? 26.545  66.443 19.145  1.00 39.43  ?  292 ALA D CA  1 
ATOM   7436 C C   . ALA D 1 137 ? 26.478  67.918 18.703  1.00 43.97  ?  292 ALA D C   1 
ATOM   7437 O O   . ALA D 1 137 ? 27.104  68.761 19.348  1.00 43.56  ?  292 ALA D O   1 
ATOM   7438 C CB  . ALA D 1 137 ? 27.206  65.605 18.060  1.00 39.87  ?  292 ALA D CB  1 
ATOM   7439 N N   . GLN D 1 138 ? 25.644  68.229 17.666  1.00 39.26  ?  293 GLN D N   1 
ATOM   7440 C CA  . GLN D 1 138 ? 25.489  69.575 17.109  1.00 37.61  ?  293 GLN D CA  1 
ATOM   7441 C C   . GLN D 1 138 ? 25.149  70.586 18.164  1.00 41.45  ?  293 GLN D C   1 
ATOM   7442 O O   . GLN D 1 138 ? 25.924  71.511 18.351  1.00 42.25  ?  293 GLN D O   1 
ATOM   7443 C CB  . GLN D 1 138 ? 24.536  69.609 15.898  1.00 38.07  ?  293 GLN D CB  1 
ATOM   7444 C CG  . GLN D 1 138 ? 25.196  69.107 14.579  1.00 56.52  ?  293 GLN D CG  1 
ATOM   7445 C CD  . GLN D 1 138 ? 24.262  68.535 13.501  1.00 79.37  ?  293 GLN D CD  1 
ATOM   7446 O OE1 . GLN D 1 138 ? 23.093  68.177 13.729  1.00 76.16  ?  293 GLN D OE1 1 
ATOM   7447 N NE2 . GLN D 1 138 ? 24.772  68.407 12.289  1.00 65.81  ?  293 GLN D NE2 1 
ATOM   7448 N N   . GLY D 1 139 ? 24.100  70.308 18.933  1.00 37.55  ?  294 GLY D N   1 
ATOM   7449 C CA  . GLY D 1 139 ? 23.580  71.144 20.008  1.00 37.24  ?  294 GLY D CA  1 
ATOM   7450 C C   . GLY D 1 139 ? 24.535  71.377 21.153  1.00 42.70  ?  294 GLY D C   1 
ATOM   7451 O O   . GLY D 1 139 ? 24.672  72.513 21.605  1.00 43.90  ?  294 GLY D O   1 
ATOM   7452 N N   . ALA D 1 140 ? 25.231  70.331 21.616  1.00 39.18  ?  295 ALA D N   1 
ATOM   7453 C CA  . ALA D 1 140 ? 26.203  70.504 22.702  1.00 38.90  ?  295 ALA D CA  1 
ATOM   7454 C C   . ALA D 1 140 ? 27.289  71.527 22.283  1.00 43.80  ?  295 ALA D C   1 
ATOM   7455 O O   . ALA D 1 140 ? 27.553  72.476 23.031  1.00 43.52  ?  295 ALA D O   1 
ATOM   7456 C CB  . ALA D 1 140 ? 26.819  69.168 23.089  1.00 39.16  ?  295 ALA D CB  1 
ATOM   7457 N N   . ALA D 1 141 ? 27.828  71.377 21.042  1.00 40.38  ?  296 ALA D N   1 
ATOM   7458 C CA  . ALA D 1 141 ? 28.817  72.273 20.436  1.00 40.11  ?  296 ALA D CA  1 
ATOM   7459 C C   . ALA D 1 141 ? 28.257  73.686 20.308  1.00 44.26  ?  296 ALA D C   1 
ATOM   7460 O O   . ALA D 1 141 ? 28.967  74.643 20.640  1.00 45.11  ?  296 ALA D O   1 
ATOM   7461 C CB  . ALA D 1 141 ? 29.241  71.756 19.070  1.00 40.70  ?  296 ALA D CB  1 
ATOM   7462 N N   . ASN D 1 142 ? 26.973  73.821 19.903  1.00 38.55  ?  297 ASN D N   1 
ATOM   7463 C CA  . ASN D 1 142 ? 26.327  75.124 19.795  1.00 38.48  ?  297 ASN D CA  1 
ATOM   7464 C C   . ASN D 1 142 ? 26.228  75.797 21.181  1.00 47.18  ?  297 ASN D C   1 
ATOM   7465 O O   . ASN D 1 142 ? 26.334  77.029 21.279  1.00 49.56  ?  297 ASN D O   1 
ATOM   7466 C CB  . ASN D 1 142 ? 24.956  75.009 19.143  1.00 34.15  ?  297 ASN D CB  1 
ATOM   7467 C CG  . ASN D 1 142 ? 24.938  74.410 17.739  1.00 69.78  ?  297 ASN D CG  1 
ATOM   7468 O OD1 . ASN D 1 142 ? 25.961  74.198 17.075  1.00 59.65  ?  297 ASN D OD1 1 
ATOM   7469 N ND2 . ASN D 1 142 ? 23.752  74.082 17.256  1.00 71.81  ?  297 ASN D ND2 1 
ATOM   7470 N N   . GLY D 1 143 ? 26.052  74.984 22.228  1.00 42.63  ?  298 GLY D N   1 
ATOM   7471 C CA  . GLY D 1 143 ? 25.975  75.460 23.599  1.00 42.21  ?  298 GLY D CA  1 
ATOM   7472 C C   . GLY D 1 143 ? 27.336  75.940 24.042  1.00 48.38  ?  298 GLY D C   1 
ATOM   7473 O O   . GLY D 1 143 ? 27.433  77.056 24.567  1.00 48.49  ?  298 GLY D O   1 
ATOM   7474 N N   . ILE D 1 144 ? 28.413  75.089 23.815  1.00 44.92  ?  299 ILE D N   1 
ATOM   7475 C CA  . ILE D 1 144 ? 29.829  75.415 24.116  1.00 44.69  ?  299 ILE D CA  1 
ATOM   7476 C C   . ILE D 1 144 ? 30.207  76.723 23.371  1.00 46.40  ?  299 ILE D C   1 
ATOM   7477 O O   . ILE D 1 144 ? 30.878  77.603 23.933  1.00 44.61  ?  299 ILE D O   1 
ATOM   7478 C CB  . ILE D 1 144 ? 30.854  74.241 23.806  1.00 47.91  ?  299 ILE D CB  1 
ATOM   7479 C CG1 . ILE D 1 144 ? 30.502  72.931 24.547  1.00 48.51  ?  299 ILE D CG1 1 
ATOM   7480 C CG2 . ILE D 1 144 ? 32.324  74.637 24.122  1.00 46.93  ?  299 ILE D CG2 1 
ATOM   7481 C CD1 . ILE D 1 144 ? 31.307  71.684 24.105  1.00 44.15  ?  299 ILE D CD1 1 
ATOM   7482 N N   . ASN D 1 145 ? 29.749  76.839 22.120  1.00 42.69  ?  300 ASN D N   1 
ATOM   7483 C CA  . ASN D 1 145 ? 30.020  78.008 21.311  1.00 43.60  ?  300 ASN D CA  1 
ATOM   7484 C C   . ASN D 1 145 ? 29.430  79.274 21.906  1.00 50.14  ?  300 ASN D C   1 
ATOM   7485 O O   . ASN D 1 145 ? 30.070  80.323 21.860  1.00 50.96  ?  300 ASN D O   1 
ATOM   7486 C CB  . ASN D 1 145 ? 29.553  77.809 19.888  1.00 45.81  ?  300 ASN D CB  1 
ATOM   7487 C CG  . ASN D 1 145 ? 29.763  79.046 19.071  1.00 71.11  ?  300 ASN D CG  1 
ATOM   7488 O OD1 . ASN D 1 145 ? 30.901  79.403 18.748  1.00 73.09  ?  300 ASN D OD1 1 
ATOM   7489 N ND2 . ASN D 1 145 ? 28.679  79.792 18.842  1.00 56.11  ?  300 ASN D ND2 1 
ATOM   7490 N N   . PHE D 1 146 ? 28.221  79.185 22.447  1.00 46.79  ?  301 PHE D N   1 
ATOM   7491 C CA  . PHE D 1 146 ? 27.583  80.323 23.078  1.00 46.92  ?  301 PHE D CA  1 
ATOM   7492 C C   . PHE D 1 146 ? 28.387  80.760 24.301  1.00 53.18  ?  301 PHE D C   1 
ATOM   7493 O O   . PHE D 1 146 ? 28.676  81.946 24.432  1.00 54.34  ?  301 PHE D O   1 
ATOM   7494 C CB  . PHE D 1 146 ? 26.132  79.982 23.443  1.00 48.67  ?  301 PHE D CB  1 
ATOM   7495 C CG  . PHE D 1 146 ? 25.378  81.092 24.117  1.00 50.20  ?  301 PHE D CG  1 
ATOM   7496 C CD1 . PHE D 1 146 ? 24.805  82.117 23.369  1.00 52.04  ?  301 PHE D CD1 1 
ATOM   7497 C CD2 . PHE D 1 146 ? 25.267  81.137 25.506  1.00 52.31  ?  301 PHE D CD2 1 
ATOM   7498 C CE1 . PHE D 1 146 ? 24.119  83.154 23.991  1.00 51.91  ?  301 PHE D CE1 1 
ATOM   7499 C CE2 . PHE D 1 146 ? 24.586  82.180 26.125  1.00 54.67  ?  301 PHE D CE2 1 
ATOM   7500 C CZ  . PHE D 1 146 ? 24.006  83.175 25.361  1.00 51.54  ?  301 PHE D CZ  1 
ATOM   7501 N N   . LEU D 1 147 ? 28.790  79.806 25.151  1.00 50.65  ?  302 LEU D N   1 
ATOM   7502 C CA  . LEU D 1 147 ? 29.590  80.084 26.347  1.00 51.07  ?  302 LEU D CA  1 
ATOM   7503 C C   . LEU D 1 147 ? 30.919  80.734 25.990  1.00 53.62  ?  302 LEU D C   1 
ATOM   7504 O O   . LEU D 1 147 ? 31.336  81.673 26.666  1.00 52.73  ?  302 LEU D O   1 
ATOM   7505 C CB  . LEU D 1 147 ? 29.840  78.788 27.146  1.00 51.21  ?  302 LEU D CB  1 
ATOM   7506 C CG  . LEU D 1 147 ? 28.668  78.242 27.923  1.00 56.09  ?  302 LEU D CG  1 
ATOM   7507 C CD1 . LEU D 1 147 ? 28.878  76.769 28.233  1.00 57.76  ?  302 LEU D CD1 1 
ATOM   7508 C CD2 . LEU D 1 147 ? 28.448  79.029 29.204  1.00 56.37  ?  302 LEU D CD2 1 
ATOM   7509 N N   . HIS D 1 148 ? 31.578  80.226 24.933  1.00 49.56  ?  303 HIS D N   1 
ATOM   7510 C CA  . HIS D 1 148 ? 32.865  80.724 24.448  1.00 49.52  ?  303 HIS D CA  1 
ATOM   7511 C C   . HIS D 1 148 ? 32.774  82.147 23.903  1.00 53.43  ?  303 HIS D C   1 
ATOM   7512 O O   . HIS D 1 148 ? 33.602  82.995 24.267  1.00 53.28  ?  303 HIS D O   1 
ATOM   7513 C CB  . HIS D 1 148 ? 33.468  79.741 23.442  1.00 50.31  ?  303 HIS D CB  1 
ATOM   7514 C CG  . HIS D 1 148 ? 34.152  78.572 24.098  1.00 53.65  ?  303 HIS D CG  1 
ATOM   7515 N ND1 . HIS D 1 148 ? 35.110  77.755 23.612  1.00 55.10  ?  303 HIS D ND1 1 
ATOM   7516 C CD2 . HIS D 1 148 ? 33.844  78.172 25.402  1.00 54.98  ?  303 HIS D CD2 1 
ATOM   7517 C CE1 . HIS D 1 148 ? 35.414  76.865 24.618  1.00 54.24  ?  303 HIS D CE1 1 
ATOM   7518 N NE2 . HIS D 1 148 ? 34.647  77.161 25.668  1.00 54.79  ?  303 HIS D NE2 1 
ATOM   7519 N N   . GLU D 1 149 ? 31.709  82.430 23.105  1.00 48.56  ?  304 GLU D N   1 
ATOM   7520 C CA  . GLU D 1 149 ? 31.397  83.747 22.554  1.00 47.16  ?  304 GLU D CA  1 
ATOM   7521 C C   . GLU D 1 149 ? 31.145  84.720 23.707  1.00 51.55  ?  304 GLU D C   1 
ATOM   7522 O O   . GLU D 1 149 ? 31.395  85.919 23.566  1.00 53.22  ?  304 GLU D O   1 
ATOM   7523 C CB  . GLU D 1 149 ? 30.133  83.682 21.700  1.00 48.31  ?  304 GLU D CB  1 
ATOM   7524 C CG  . GLU D 1 149 ? 30.366  83.280 20.257  1.00 60.84  ?  304 GLU D CG  1 
ATOM   7525 C CD  . GLU D 1 149 ? 29.108  83.188 19.401  1.00 90.03  ?  304 GLU D CD  1 
ATOM   7526 O OE1 . GLU D 1 149 ? 27.989  83.394 19.934  1.00 73.68  ?  304 GLU D OE1 1 
ATOM   7527 O OE2 . GLU D 1 149 ? 29.248  82.894 18.188  1.00 84.68  -1 304 GLU D OE2 1 
ATOM   7528 N N   . ASN D 1 150 ? 30.659  84.211 24.837  1.00 46.34  ?  305 ASN D N   1 
ATOM   7529 C CA  . ASN D 1 150 ? 30.375  85.010 26.012  1.00 46.61  ?  305 ASN D CA  1 
ATOM   7530 C C   . ASN D 1 150 ? 31.511  84.980 27.012  1.00 53.05  ?  305 ASN D C   1 
ATOM   7531 O O   . ASN D 1 150 ? 31.321  85.312 28.183  1.00 53.01  ?  305 ASN D O   1 
ATOM   7532 C CB  . ASN D 1 150 ? 29.031  84.628 26.621  1.00 49.17  ?  305 ASN D CB  1 
ATOM   7533 C CG  . ASN D 1 150 ? 27.857  85.133 25.805  1.00 76.09  ?  305 ASN D CG  1 
ATOM   7534 O OD1 . ASN D 1 150 ? 27.132  86.039 26.230  1.00 70.42  ?  305 ASN D OD1 1 
ATOM   7535 N ND2 . ASN D 1 150 ? 27.647  84.580 24.602  1.00 64.17  ?  305 ASN D ND2 1 
ATOM   7536 N N   . HIS D 1 151 ? 32.710  84.624 26.531  1.00 52.26  ?  306 HIS D N   1 
ATOM   7537 C CA  . HIS D 1 151 ? 33.963  84.608 27.286  1.00 53.89  ?  306 HIS D CA  1 
ATOM   7538 C C   . HIS D 1 151 ? 33.888  83.785 28.547  1.00 59.05  ?  306 HIS D C   1 
ATOM   7539 O O   . HIS D 1 151 ? 34.279  84.243 29.617  1.00 58.86  ?  306 HIS D O   1 
ATOM   7540 C CB  . HIS D 1 151 ? 34.474  86.047 27.541  1.00 55.71  ?  306 HIS D CB  1 
ATOM   7541 C CG  . HIS D 1 151 ? 34.379  86.906 26.321  1.00 59.43  ?  306 HIS D CG  1 
ATOM   7542 N ND1 . HIS D 1 151 ? 35.321  86.822 25.300  1.00 61.24  ?  306 HIS D ND1 1 
ATOM   7543 C CD2 . HIS D 1 151 ? 33.389  87.745 25.938  1.00 60.81  ?  306 HIS D CD2 1 
ATOM   7544 C CE1 . HIS D 1 151 ? 34.896  87.649 24.359  1.00 60.29  ?  306 HIS D CE1 1 
ATOM   7545 N NE2 . HIS D 1 151 ? 33.738  88.224 24.699  1.00 60.54  ?  306 HIS D NE2 1 
ATOM   7546 N N   . HIS D 1 152 ? 33.352  82.563 28.416  1.00 56.35  ?  307 HIS D N   1 
ATOM   7547 C CA  . HIS D 1 152 ? 33.246  81.619 29.516  1.00 55.45  ?  307 HIS D CA  1 
ATOM   7548 C C   . HIS D 1 152 ? 33.851  80.298 29.129  1.00 57.11  ?  307 HIS D C   1 
ATOM   7549 O O   . HIS D 1 152 ? 33.702  79.859 27.991  1.00 56.99  ?  307 HIS D O   1 
ATOM   7550 C CB  . HIS D 1 152 ? 31.798  81.434 29.971  1.00 56.13  ?  307 HIS D CB  1 
ATOM   7551 C CG  . HIS D 1 152 ? 31.272  82.599 30.732  1.00 60.44  ?  307 HIS D CG  1 
ATOM   7552 N ND1 . HIS D 1 152 ? 31.730  82.900 32.014  1.00 62.62  ?  307 HIS D ND1 1 
ATOM   7553 C CD2 . HIS D 1 152 ? 30.345  83.515 30.373  1.00 63.20  ?  307 HIS D CD2 1 
ATOM   7554 C CE1 . HIS D 1 152 ? 31.073  83.987 32.384  1.00 62.32  ?  307 HIS D CE1 1 
ATOM   7555 N NE2 . HIS D 1 152 ? 30.234  84.399 31.430  1.00 63.01  ?  307 HIS D NE2 1 
ATOM   7556 N N   . ILE D 1 153 ? 34.559  79.685 30.077  1.00 51.25  ?  308 ILE D N   1 
ATOM   7557 C CA  . ILE D 1 153 ? 35.139  78.352 29.950  1.00 49.38  ?  308 ILE D CA  1 
ATOM   7558 C C   . ILE D 1 153 ? 34.337  77.508 30.943  1.00 51.74  ?  308 ILE D C   1 
ATOM   7559 O O   . ILE D 1 153 ? 34.219  77.888 32.126  1.00 51.91  ?  308 ILE D O   1 
ATOM   7560 C CB  . ILE D 1 153 ? 36.658  78.302 30.257  1.00 51.93  ?  308 ILE D CB  1 
ATOM   7561 C CG1 . ILE D 1 153 ? 37.415  79.443 29.564  1.00 52.52  ?  308 ILE D CG1 1 
ATOM   7562 C CG2 . ILE D 1 153 ? 37.248  76.949 29.868  1.00 52.15  ?  308 ILE D CG2 1 
ATOM   7563 C CD1 . ILE D 1 153 ? 38.618  79.963 30.312  1.00 56.68  ?  308 ILE D CD1 1 
ATOM   7564 N N   . HIS D 1 154 ? 33.744  76.397 30.459  1.00 44.58  ?  309 HIS D N   1 
ATOM   7565 C CA  . HIS D 1 154 ? 32.936  75.524 31.296  1.00 42.08  ?  309 HIS D CA  1 
ATOM   7566 C C   . HIS D 1 154 ? 33.758  74.860 32.404  1.00 43.61  ?  309 HIS D C   1 
ATOM   7567 O O   . HIS D 1 154 ? 33.357  74.922 33.568  1.00 41.28  ?  309 HIS D O   1 
ATOM   7568 C CB  . HIS D 1 154 ? 32.181  74.496 30.449  1.00 42.22  ?  309 HIS D CB  1 
ATOM   7569 C CG  . HIS D 1 154 ? 31.167  73.705 31.232  1.00 45.25  ?  309 HIS D CG  1 
ATOM   7570 N ND1 . HIS D 1 154 ? 31.546  72.679 32.080  1.00 46.61  ?  309 HIS D ND1 1 
ATOM   7571 C CD2 . HIS D 1 154 ? 29.822  73.837 31.287  1.00 46.55  ?  309 HIS D CD2 1 
ATOM   7572 C CE1 . HIS D 1 154 ? 30.430  72.213 32.604  1.00 45.76  ?  309 HIS D CE1 1 
ATOM   7573 N NE2 . HIS D 1 154 ? 29.365  72.881 32.158  1.00 46.24  ?  309 HIS D NE2 1 
ATOM   7574 N N   . ARG D 1 155 ? 34.899  74.223 32.031  1.00 40.98  ?  310 ARG D N   1 
ATOM   7575 C CA  . ARG D 1 155 ? 35.853  73.516 32.914  1.00 41.78  ?  310 ARG D CA  1 
ATOM   7576 C C   . ARG D 1 155 ? 35.426  72.096 33.343  1.00 47.85  ?  310 ARG D C   1 
ATOM   7577 O O   . ARG D 1 155 ? 36.250  71.381 33.919  1.00 47.93  ?  310 ARG D O   1 
ATOM   7578 C CB  . ARG D 1 155 ? 36.294  74.350 34.150  1.00 41.91  ?  310 ARG D CB  1 
ATOM   7579 C CG  . ARG D 1 155 ? 37.120  75.604 33.856  1.00 47.62  ?  310 ARG D CG  1 
ATOM   7580 C CD  . ARG D 1 155 ? 38.204  75.797 34.907  1.00 59.00  ?  310 ARG D CD  1 
ATOM   7581 N NE  . ARG D 1 155 ? 37.639  76.047 36.232  1.00 66.73  ?  310 ARG D NE  1 
ATOM   7582 C CZ  . ARG D 1 155 ? 38.309  75.951 37.374  1.00 78.02  ?  310 ARG D CZ  1 
ATOM   7583 N NH1 . ARG D 1 155 ? 39.594  75.614 37.372  1.00 70.90  ?  310 ARG D NH1 1 
ATOM   7584 N NH2 . ARG D 1 155 ? 37.701  76.184 38.527  1.00 61.88  1  310 ARG D NH2 1 
ATOM   7585 N N   . ASP D 1 156 ? 34.171  71.678 33.067  1.00 44.77  ?  311 ASP D N   1 
ATOM   7586 C CA  . ASP D 1 156 ? 33.684  70.340 33.439  1.00 44.56  ?  311 ASP D CA  1 
ATOM   7587 C C   . ASP D 1 156 ? 32.771  69.719 32.343  1.00 46.52  ?  311 ASP D C   1 
ATOM   7588 O O   . ASP D 1 156 ? 31.716  69.149 32.632  1.00 46.47  ?  311 ASP D O   1 
ATOM   7589 C CB  . ASP D 1 156 ? 33.027  70.367 34.839  1.00 46.61  ?  311 ASP D CB  1 
ATOM   7590 C CG  . ASP D 1 156 ? 32.944  69.032 35.578  1.00 62.15  ?  311 ASP D CG  1 
ATOM   7591 O OD1 . ASP D 1 156 ? 33.672  68.072 35.186  1.00 64.92  ?  311 ASP D OD1 1 
ATOM   7592 O OD2 . ASP D 1 156 ? 32.190  68.954 36.570  1.00 65.94  -1 311 ASP D OD2 1 
ATOM   7593 N N   . ILE D 1 157 ? 33.176  69.871 31.080  1.00 41.12  ?  312 ILE D N   1 
ATOM   7594 C CA  . ILE D 1 157 ? 32.433  69.299 29.972  1.00 40.76  ?  312 ILE D CA  1 
ATOM   7595 C C   . ILE D 1 157 ? 32.594  67.799 29.959  1.00 42.93  ?  312 ILE D C   1 
ATOM   7596 O O   . ILE D 1 157 ? 33.714  67.285 29.857  1.00 43.78  ?  312 ILE D O   1 
ATOM   7597 C CB  . ILE D 1 157 ? 32.751  69.989 28.622  1.00 44.52  ?  312 ILE D CB  1 
ATOM   7598 C CG1 . ILE D 1 157 ? 31.927  71.297 28.546  1.00 45.81  ?  312 ILE D CG1 1 
ATOM   7599 C CG2 . ILE D 1 157 ? 32.466  69.056 27.415  1.00 43.64  ?  312 ILE D CG2 1 
ATOM   7600 C CD1 . ILE D 1 157 ? 32.472  72.279 27.701  1.00 62.48  ?  312 ILE D CD1 1 
ATOM   7601 N N   . LYS D 1 158 ? 31.454  67.103 30.130  1.00 36.55  ?  313 LYS D N   1 
ATOM   7602 C CA  . LYS D 1 158 ? 31.328  65.648 30.157  1.00 33.32  ?  313 LYS D CA  1 
ATOM   7603 C C   . LYS D 1 158 ? 29.887  65.266 29.873  1.00 39.29  ?  313 LYS D C   1 
ATOM   7604 O O   . LYS D 1 158 ? 28.991  66.123 29.981  1.00 38.18  ?  313 LYS D O   1 
ATOM   7605 C CB  . LYS D 1 158 ? 31.825  65.075 31.483  1.00 32.21  ?  313 LYS D CB  1 
ATOM   7606 C CG  . LYS D 1 158 ? 31.196  65.641 32.739  1.00 32.60  ?  313 LYS D CG  1 
ATOM   7607 C CD  . LYS D 1 158 ? 31.945  65.097 33.932  1.00 37.16  ?  313 LYS D CD  1 
ATOM   7608 C CE  . LYS D 1 158 ? 31.259  65.396 35.219  1.00 34.12  ?  313 LYS D CE  1 
ATOM   7609 N NZ  . LYS D 1 158 ? 31.767  64.477 36.271  1.00 33.53  1  313 LYS D NZ  1 
ATOM   7610 N N   . SER D 1 159 ? 29.647  63.980 29.520  1.00 36.49  ?  314 SER D N   1 
ATOM   7611 C CA  . SER D 1 159 ? 28.296  63.509 29.207  1.00 35.50  ?  314 SER D CA  1 
ATOM   7612 C C   . SER D 1 159 ? 27.301  63.563 30.377  1.00 35.43  ?  314 SER D C   1 
ATOM   7613 O O   . SER D 1 159 ? 26.121  63.781 30.142  1.00 32.02  ?  314 SER D O   1 
ATOM   7614 C CB  . SER D 1 159 ? 28.312  62.180 28.463  1.00 38.90  ?  314 SER D CB  1 
ATOM   7615 O OG  . SER D 1 159 ? 28.977  61.199 29.235  1.00 51.80  ?  314 SER D OG  1 
ATOM   7616 N N   . ALA D 1 160 ? 27.790  63.492 31.621  1.00 34.91  ?  315 ALA D N   1 
ATOM   7617 C CA  . ALA D 1 160 ? 26.941  63.622 32.810  1.00 36.15  ?  315 ALA D CA  1 
ATOM   7618 C C   . ALA D 1 160 ? 26.393  65.056 32.896  1.00 44.53  ?  315 ALA D C   1 
ATOM   7619 O O   . ALA D 1 160 ? 25.302  65.272 33.447  1.00 44.84  ?  315 ALA D O   1 
ATOM   7620 C CB  . ALA D 1 160 ? 27.722  63.300 34.065  1.00 36.58  ?  315 ALA D CB  1 
ATOM   7621 N N   . ASN D 1 161 ? 27.143  66.025 32.311  1.00 43.16  ?  316 ASN D N   1 
ATOM   7622 C CA  . ASN D 1 161 ? 26.790  67.458 32.251  1.00 42.50  ?  316 ASN D CA  1 
ATOM   7623 C C   . ASN D 1 161 ? 26.085  67.900 30.952  1.00 43.54  ?  316 ASN D C   1 
ATOM   7624 O O   . ASN D 1 161 ? 25.887  69.089 30.743  1.00 42.88  ?  316 ASN D O   1 
ATOM   7625 C CB  . ASN D 1 161 ? 28.018  68.329 32.557  1.00 43.11  ?  316 ASN D CB  1 
ATOM   7626 C CG  . ASN D 1 161 ? 28.411  68.292 34.003  1.00 64.16  ?  316 ASN D CG  1 
ATOM   7627 O OD1 . ASN D 1 161 ? 27.643  67.874 34.889  1.00 53.50  ?  316 ASN D OD1 1 
ATOM   7628 N ND2 . ASN D 1 161 ? 29.622  68.741 34.274  1.00 59.53  ?  316 ASN D ND2 1 
ATOM   7629 N N   . ILE D 1 162 ? 25.723  66.956 30.087  1.00 39.65  ?  317 ILE D N   1 
ATOM   7630 C CA  . ILE D 1 162 ? 24.965  67.235 28.868  1.00 38.03  ?  317 ILE D CA  1 
ATOM   7631 C C   . ILE D 1 162 ? 23.614  66.587 29.115  1.00 39.58  ?  317 ILE D C   1 
ATOM   7632 O O   . ILE D 1 162 ? 23.494  65.355 29.114  1.00 37.17  ?  317 ILE D O   1 
ATOM   7633 C CB  . ILE D 1 162 ? 25.636  66.755 27.554  1.00 39.23  ?  317 ILE D CB  1 
ATOM   7634 C CG1 . ILE D 1 162 ? 26.998  67.429 27.372  1.00 38.67  ?  317 ILE D CG1 1 
ATOM   7635 C CG2 . ILE D 1 162 ? 24.719  67.035 26.354  1.00 37.56  ?  317 ILE D CG2 1 
ATOM   7636 C CD1 . ILE D 1 162 ? 27.919  66.720 26.409  1.00 41.17  ?  317 ILE D CD1 1 
ATOM   7637 N N   . LEU D 1 163 ? 22.628  67.423 29.410  1.00 34.81  ?  318 LEU D N   1 
ATOM   7638 C CA  . LEU D 1 163 ? 21.300  66.936 29.724  1.00 34.29  ?  318 LEU D CA  1 
ATOM   7639 C C   . LEU D 1 163 ? 20.390  66.937 28.516  1.00 39.34  ?  318 LEU D C   1 
ATOM   7640 O O   . LEU D 1 163 ? 20.709  67.552 27.493  1.00 38.62  ?  318 LEU D O   1 
ATOM   7641 C CB  . LEU D 1 163 ? 20.687  67.672 30.921  1.00 33.79  ?  318 LEU D CB  1 
ATOM   7642 C CG  . LEU D 1 163 ? 21.544  67.734 32.179  1.00 38.12  ?  318 LEU D CG  1 
ATOM   7643 C CD1 . LEU D 1 163 ? 20.861  68.506 33.218  1.00 37.33  ?  318 LEU D CD1 1 
ATOM   7644 C CD2 . LEU D 1 163 ? 21.900  66.360 32.701  1.00 41.26  ?  318 LEU D CD2 1 
ATOM   7645 N N   . LEU D 1 164 ? 19.282  66.184 28.619  1.00 36.04  ?  319 LEU D N   1 
ATOM   7646 C CA  . LEU D 1 164 ? 18.334  66.010 27.533  1.00 35.24  ?  319 LEU D CA  1 
ATOM   7647 C C   . LEU D 1 164 ? 16.904  66.332 27.927  1.00 39.49  ?  319 LEU D C   1 
ATOM   7648 O O   . LEU D 1 164 ? 16.384  65.766 28.896  1.00 36.80  ?  319 LEU D O   1 
ATOM   7649 C CB  . LEU D 1 164 ? 18.439  64.577 26.986  1.00 34.18  ?  319 LEU D CB  1 
ATOM   7650 C CG  . LEU D 1 164 ? 19.818  64.140 26.487  1.00 34.50  ?  319 LEU D CG  1 
ATOM   7651 C CD1 . LEU D 1 164 ? 19.873  62.682 26.327  1.00 31.52  ?  319 LEU D CD1 1 
ATOM   7652 C CD2 . LEU D 1 164 ? 20.179  64.839 25.196  1.00 35.37  ?  319 LEU D CD2 1 
ATOM   7653 N N   . ASP D 1 165 ? 16.274  67.263 27.163  1.00 38.09  ?  320 ASP D N   1 
ATOM   7654 C CA  . ASP D 1 165 ? 14.876  67.662 27.363  1.00 37.91  ?  320 ASP D CA  1 
ATOM   7655 C C   . ASP D 1 165 ? 13.901  66.645 26.720  1.00 42.40  ?  320 ASP D C   1 
ATOM   7656 O O   . ASP D 1 165 ? 14.331  65.646 26.147  1.00 40.80  ?  320 ASP D O   1 
ATOM   7657 C CB  . ASP D 1 165 ? 14.636  69.111 26.859  1.00 38.58  ?  320 ASP D CB  1 
ATOM   7658 C CG  . ASP D 1 165 ? 14.495  69.311 25.364  1.00 51.04  ?  320 ASP D CG  1 
ATOM   7659 O OD1 . ASP D 1 165 ? 14.547  68.316 24.619  1.00 53.68  ?  320 ASP D OD1 1 
ATOM   7660 O OD2 . ASP D 1 165 ? 14.318  70.469 24.935  1.00 61.19  -1 320 ASP D OD2 1 
ATOM   7661 N N   . GLU D 1 166 ? 12.606  66.956 26.759  1.00 41.99  ?  321 GLU D N   1 
ATOM   7662 C CA  . GLU D 1 166 ? 11.509  66.174 26.172  1.00 42.62  ?  321 GLU D CA  1 
ATOM   7663 C C   . GLU D 1 166 ? 11.685  65.886 24.684  1.00 47.60  ?  321 GLU D C   1 
ATOM   7664 O O   . GLU D 1 166 ? 11.167  64.881 24.229  1.00 51.08  ?  321 GLU D O   1 
ATOM   7665 C CB  . GLU D 1 166 ? 10.149  66.856 26.403  1.00 44.24  ?  321 GLU D CB  1 
ATOM   7666 C CG  . GLU D 1 166 ? 10.091  68.331 26.017  1.00 55.58  ?  321 GLU D CG  1 
ATOM   7667 C CD  . GLU D 1 166 ? 10.255  69.307 27.160  1.00 90.77  ?  321 GLU D CD  1 
ATOM   7668 O OE1 . GLU D 1 166 ? 11.370  69.397 27.731  1.00 88.19  ?  321 GLU D OE1 1 
ATOM   7669 O OE2 . GLU D 1 166 ? 9.271   70.030 27.438  1.00 87.09  -1 321 GLU D OE2 1 
ATOM   7670 N N   . ALA D 1 167 ? 12.396  66.740 23.928  1.00 40.51  ?  322 ALA D N   1 
ATOM   7671 C CA  . ALA D 1 167 ? 12.666  66.543 22.494  1.00 38.77  ?  322 ALA D CA  1 
ATOM   7672 C C   . ALA D 1 167 ? 14.088  66.002 22.248  1.00 41.57  ?  322 ALA D C   1 
ATOM   7673 O O   . ALA D 1 167 ? 14.487  65.879 21.084  1.00 40.94  ?  322 ALA D O   1 
ATOM   7674 C CB  . ALA D 1 167 ? 12.488  67.858 21.756  1.00 38.92  ?  322 ALA D CB  1 
ATOM   7675 N N   . PHE D 1 168 ? 14.842  65.682 23.333  1.00 37.26  ?  323 PHE D N   1 
ATOM   7676 C CA  . PHE D 1 168 ? 16.248  65.223 23.291  1.00 38.41  ?  323 PHE D CA  1 
ATOM   7677 C C   . PHE D 1 168 ? 17.217  66.321 22.845  1.00 42.62  ?  323 PHE D C   1 
ATOM   7678 O O   . PHE D 1 168 ? 18.237  66.046 22.181  1.00 40.40  ?  323 PHE D O   1 
ATOM   7679 C CB  . PHE D 1 168 ? 16.454  63.924 22.497  1.00 39.90  ?  323 PHE D CB  1 
ATOM   7680 C CG  . PHE D 1 168 ? 15.837  62.738 23.184  1.00 40.83  ?  323 PHE D CG  1 
ATOM   7681 C CD1 . PHE D 1 168 ? 14.484  62.440 23.015  1.00 42.29  ?  323 PHE D CD1 1 
ATOM   7682 C CD2 . PHE D 1 168 ? 16.597  61.930 24.022  1.00 41.21  ?  323 PHE D CD2 1 
ATOM   7683 C CE1 . PHE D 1 168 ? 13.911  61.353 23.661  1.00 42.10  ?  323 PHE D CE1 1 
ATOM   7684 C CE2 . PHE D 1 168 ? 16.024  60.844 24.675  1.00 43.38  ?  323 PHE D CE2 1 
ATOM   7685 C CZ  . PHE D 1 168 ? 14.688  60.552 24.471  1.00 41.61  ?  323 PHE D CZ  1 
ATOM   7686 N N   . THR D 1 169 ? 16.878  67.581 23.215  1.00 38.37  ?  324 THR D N   1 
ATOM   7687 C CA  . THR D 1 169 ? 17.741  68.726 22.951  1.00 37.09  ?  324 THR D CA  1 
ATOM   7688 C C   . THR D 1 169 ? 18.835  68.680 24.008  1.00 40.12  ?  324 THR D C   1 
ATOM   7689 O O   . THR D 1 169 ? 18.544  68.475 25.196  1.00 39.88  ?  324 THR D O   1 
ATOM   7690 C CB  . THR D 1 169 ? 16.950  70.018 22.974  1.00 40.34  ?  324 THR D CB  1 
ATOM   7691 O OG1 . THR D 1 169 ? 16.013  69.986 21.906  1.00 48.44  ?  324 THR D OG1 1 
ATOM   7692 C CG2 . THR D 1 169 ? 17.823  71.256 22.874  1.00 35.78  ?  324 THR D CG2 1 
ATOM   7693 N N   . ALA D 1 170 ? 20.093  68.817 23.563  1.00 35.68  ?  325 ALA D N   1 
ATOM   7694 C CA  . ALA D 1 170 ? 21.268  68.809 24.430  1.00 33.94  ?  325 ALA D CA  1 
ATOM   7695 C C   . ALA D 1 170 ? 21.304  70.108 25.212  1.00 34.69  ?  325 ALA D C   1 
ATOM   7696 O O   . ALA D 1 170 ? 21.058  71.157 24.653  1.00 33.28  ?  325 ALA D O   1 
ATOM   7697 C CB  . ALA D 1 170 ? 22.526  68.623 23.598  1.00 34.19  ?  325 ALA D CB  1 
ATOM   7698 N N   . LYS D 1 171 ? 21.470  70.025 26.506  1.00 32.45  ?  326 LYS D N   1 
ATOM   7699 C CA  . LYS D 1 171 ? 21.522  71.187 27.378  1.00 33.79  ?  326 LYS D CA  1 
ATOM   7700 C C   . LYS D 1 171 ? 22.646  71.033 28.343  1.00 45.72  ?  326 LYS D C   1 
ATOM   7701 O O   . LYS D 1 171 ? 22.627  70.121 29.180  1.00 47.11  ?  326 LYS D O   1 
ATOM   7702 C CB  . LYS D 1 171 ? 20.189  71.417 28.087  1.00 35.82  ?  326 LYS D CB  1 
ATOM   7703 C CG  . LYS D 1 171 ? 19.251  72.242 27.221  1.00 43.27  ?  326 LYS D CG  1 
ATOM   7704 C CD  . LYS D 1 171 ? 17.815  71.843 27.340  1.00 51.94  ?  326 LYS D CD  1 
ATOM   7705 C CE  . LYS D 1 171 ? 16.931  72.619 26.371  1.00 55.78  ?  326 LYS D CE  1 
ATOM   7706 N NZ  . LYS D 1 171 ? 17.020  74.092 26.566  1.00 70.72  1  326 LYS D NZ  1 
ATOM   7707 N N   . ILE D 1 172 ? 23.692  71.875 28.165  1.00 45.83  ?  327 ILE D N   1 
ATOM   7708 C CA  . ILE D 1 172 ? 24.893  71.906 29.007  1.00 45.96  ?  327 ILE D CA  1 
ATOM   7709 C C   . ILE D 1 172 ? 24.486  72.390 30.410  1.00 48.37  ?  327 ILE D C   1 
ATOM   7710 O O   . ILE D 1 172 ? 23.759  73.372 30.534  1.00 46.81  ?  327 ILE D O   1 
ATOM   7711 C CB  . ILE D 1 172 ? 26.002  72.817 28.393  1.00 49.97  ?  327 ILE D CB  1 
ATOM   7712 C CG1 . ILE D 1 172 ? 26.222  72.628 26.863  1.00 51.17  ?  327 ILE D CG1 1 
ATOM   7713 C CG2 . ILE D 1 172 ? 27.303  72.726 29.180  1.00 52.08  ?  327 ILE D CG2 1 
ATOM   7714 C CD1 . ILE D 1 172 ? 26.841  71.315 26.377  1.00 60.35  ?  327 ILE D CD1 1 
ATOM   7715 N N   . SER D 1 173 ? 24.929  71.684 31.449  1.00 47.03  ?  328 SER D N   1 
ATOM   7716 C CA  . SER D 1 173 ? 24.648  72.030 32.845  1.00 47.90  ?  328 SER D CA  1 
ATOM   7717 C C   . SER D 1 173 ? 25.953  72.109 33.648  1.00 52.68  ?  328 SER D C   1 
ATOM   7718 O O   . SER D 1 173 ? 27.035  71.922 33.087  1.00 50.98  ?  328 SER D O   1 
ATOM   7719 C CB  . SER D 1 173 ? 23.691  71.017 33.469  1.00 51.94  ?  328 SER D CB  1 
ATOM   7720 O OG  . SER D 1 173 ? 24.314  69.747 33.578  1.00 61.37  ?  328 SER D OG  1 
ATOM   7721 N N   . ASP D 1 174 ? 25.833  72.389 34.958  1.00 51.44  ?  329 ASP D N   1 
ATOM   7722 C CA  . ASP D 1 174 ? 26.925  72.491 35.929  1.00 52.30  ?  329 ASP D CA  1 
ATOM   7723 C C   . ASP D 1 174 ? 27.978  73.525 35.604  1.00 57.65  ?  329 ASP D C   1 
ATOM   7724 O O   . ASP D 1 174 ? 29.049  73.191 35.103  1.00 56.96  ?  329 ASP D O   1 
ATOM   7725 C CB  . ASP D 1 174 ? 27.540  71.122 36.269  1.00 55.01  ?  329 ASP D CB  1 
ATOM   7726 C CG  . ASP D 1 174 ? 27.840  70.936 37.743  1.00 78.25  ?  329 ASP D CG  1 
ATOM   7727 O OD1 . ASP D 1 174 ? 27.998  71.961 38.461  1.00 81.60  ?  329 ASP D OD1 1 
ATOM   7728 O OD2 . ASP D 1 174 ? 27.915  69.773 38.187  1.00 88.02  -1 329 ASP D OD2 1 
ATOM   7729 N N   . PHE D 1 175 ? 27.675  74.793 35.920  1.00 56.56  ?  330 PHE D N   1 
ATOM   7730 C CA  . PHE D 1 175 ? 28.545  75.953 35.697  1.00 56.65  ?  330 PHE D CA  1 
ATOM   7731 C C   . PHE D 1 175 ? 29.243  76.435 36.983  1.00 59.54  ?  330 PHE D C   1 
ATOM   7732 O O   . PHE D 1 175 ? 29.757  77.550 37.011  1.00 58.71  ?  330 PHE D O   1 
ATOM   7733 C CB  . PHE D 1 175 ? 27.744  77.086 35.041  1.00 58.66  ?  330 PHE D CB  1 
ATOM   7734 C CG  . PHE D 1 175 ? 27.060  76.670 33.763  1.00 60.64  ?  330 PHE D CG  1 
ATOM   7735 C CD1 . PHE D 1 175 ? 27.772  76.587 32.568  1.00 64.35  ?  330 PHE D CD1 1 
ATOM   7736 C CD2 . PHE D 1 175 ? 25.708  76.349 33.753  1.00 62.79  ?  330 PHE D CD2 1 
ATOM   7737 C CE1 . PHE D 1 175 ? 27.138  76.190 31.384  1.00 65.25  ?  330 PHE D CE1 1 
ATOM   7738 C CE2 . PHE D 1 175 ? 25.073  75.960 32.572  1.00 65.39  ?  330 PHE D CE2 1 
ATOM   7739 C CZ  . PHE D 1 175 ? 25.793  75.880 31.394  1.00 63.66  ?  330 PHE D CZ  1 
ATOM   7740 N N   . GLY D 1 176 ? 29.261  75.585 38.018  1.00 56.23  ?  331 GLY D N   1 
ATOM   7741 C CA  . GLY D 1 176 ? 29.910  75.858 39.298  1.00 56.52  ?  331 GLY D CA  1 
ATOM   7742 C C   . GLY D 1 176 ? 31.417  76.063 39.215  1.00 62.24  ?  331 GLY D C   1 
ATOM   7743 O O   . GLY D 1 176 ? 31.977  76.791 40.036  1.00 63.49  ?  331 GLY D O   1 
ATOM   7744 N N   . LEU D 1 177 ? 32.086  75.422 38.222  1.00 58.50  ?  332 LEU D N   1 
ATOM   7745 C CA  . LEU D 1 177 ? 33.524  75.533 37.951  1.00 57.81  ?  332 LEU D CA  1 
ATOM   7746 C C   . LEU D 1 177 ? 33.837  76.469 36.780  1.00 61.69  ?  332 LEU D C   1 
ATOM   7747 O O   . LEU D 1 177 ? 35.011  76.693 36.502  1.00 61.81  ?  332 LEU D O   1 
ATOM   7748 C CB  . LEU D 1 177 ? 34.173  74.149 37.711  1.00 58.02  ?  332 LEU D CB  1 
ATOM   7749 C CG  . LEU D 1 177 ? 34.623  73.314 38.921  1.00 63.62  ?  332 LEU D CG  1 
ATOM   7750 C CD1 . LEU D 1 177 ? 35.120  74.202 40.077  1.00 64.78  ?  332 LEU D CD1 1 
ATOM   7751 C CD2 . LEU D 1 177 ? 33.514  72.403 39.394  1.00 66.15  ?  332 LEU D CD2 1 
ATOM   7752 N N   . ALA D 1 178 ? 32.811  77.039 36.114  1.00 58.95  ?  333 ALA D N   1 
ATOM   7753 C CA  . ALA D 1 178 ? 32.997  77.943 34.966  1.00 58.54  ?  333 ALA D CA  1 
ATOM   7754 C C   . ALA D 1 178 ? 33.824  79.188 35.293  1.00 63.10  ?  333 ALA D C   1 
ATOM   7755 O O   . ALA D 1 178 ? 33.769  79.710 36.414  1.00 62.01  ?  333 ALA D O   1 
ATOM   7756 C CB  . ALA D 1 178 ? 31.656  78.326 34.351  1.00 59.05  ?  333 ALA D CB  1 
ATOM   7757 N N   . ARG D 1 179 ? 34.614  79.639 34.309  1.00 60.92  ?  334 ARG D N   1 
ATOM   7758 C CA  . ARG D 1 179 ? 35.497  80.799 34.438  1.00 60.86  ?  334 ARG D CA  1 
ATOM   7759 C C   . ARG D 1 179 ? 35.274  81.806 33.335  1.00 66.59  ?  334 ARG D C   1 
ATOM   7760 O O   . ARG D 1 179 ? 35.023  81.425 32.190  1.00 65.56  ?  334 ARG D O   1 
ATOM   7761 C CB  . ARG D 1 179 ? 36.975  80.359 34.418  1.00 59.43  ?  334 ARG D CB  1 
ATOM   7762 C CG  . ARG D 1 179 ? 37.468  79.707 35.701  1.00 66.61  ?  334 ARG D CG  1 
ATOM   7763 C CD  . ARG D 1 179 ? 37.772  80.730 36.788  1.00 72.96  ?  334 ARG D CD  1 
ATOM   7764 N NE  . ARG D 1 179 ? 38.784  80.250 37.730  1.00 75.44  ?  334 ARG D NE  1 
ATOM   7765 C CZ  . ARG D 1 179 ? 38.508  79.542 38.816  1.00 84.24  ?  334 ARG D CZ  1 
ATOM   7766 N NH1 . ARG D 1 179 ? 39.482  79.155 39.626  1.00 47.28  ?  334 ARG D NH1 1 
ATOM   7767 N NH2 . ARG D 1 179 ? 37.252  79.212 39.104  1.00 86.67  1  334 ARG D NH2 1 
ATOM   7768 N N   . ALA D 1 180 ? 35.391  83.097 33.676  1.00 64.95  ?  335 ALA D N   1 
ATOM   7769 C CA  . ALA D 1 180 ? 35.286  84.191 32.718  1.00 91.90  ?  335 ALA D CA  1 
ATOM   7770 C C   . ALA D 1 180 ? 36.684  84.511 32.203  1.00 101.24 ?  335 ALA D C   1 
ATOM   7771 O O   . ALA D 1 180 ? 37.315  83.645 31.593  1.00 59.50  ?  335 ALA D O   1 
ATOM   7772 C CB  . ALA D 1 180 ? 34.678  85.412 33.378  1.00 92.65  ?  335 ALA D CB  1 
HETATM 7773 N N   . TPO D 1 187 ? 45.347  82.292 28.370  1.00 82.22  ?  342 TPO D N   1 
HETATM 7774 C CA  . TPO D 1 187 ? 45.713  81.109 29.156  1.00 81.47  ?  342 TPO D CA  1 
HETATM 7775 C CB  . TPO D 1 187 ? 46.582  80.104 28.362  1.00 83.26  ?  342 TPO D CB  1 
HETATM 7776 C CG2 . TPO D 1 187 ? 46.891  78.887 29.247  1.00 83.03  ?  342 TPO D CG2 1 
HETATM 7777 O OG1 . TPO D 1 187 ? 45.818  79.629 27.219  1.00 85.65  ?  342 TPO D OG1 1 
HETATM 7778 P P   . TPO D 1 187 ? 46.547  79.655 25.842  1.00 87.83  ?  342 TPO D P   1 
HETATM 7779 O O1P . TPO D 1 187 ? 45.464  79.983 24.782  1.00 86.77  -1 342 TPO D O1P 1 
HETATM 7780 O O2P . TPO D 1 187 ? 47.182  78.251 25.542  1.00 88.29  -1 342 TPO D O2P 1 
HETATM 7781 O O3P . TPO D 1 187 ? 47.711  80.712 25.838  1.00 88.60  ?  342 TPO D O3P 1 
HETATM 7782 C C   . TPO D 1 187 ? 46.296  81.483 30.524  1.00 81.32  ?  342 TPO D C   1 
HETATM 7783 O O   . TPO D 1 187 ? 47.390  82.060 30.605  1.00 80.69  ?  342 TPO D O   1 
ATOM   7784 N N   . VAL D 1 188 ? 45.558  81.137 31.596  1.00 74.66  ?  343 VAL D N   1 
ATOM   7785 C CA  . VAL D 1 188 ? 45.937  81.411 32.993  1.00 72.57  ?  343 VAL D CA  1 
ATOM   7786 C C   . VAL D 1 188 ? 46.294  80.115 33.773  1.00 73.68  ?  343 VAL D C   1 
ATOM   7787 O O   . VAL D 1 188 ? 46.351  79.039 33.166  1.00 71.09  ?  343 VAL D O   1 
ATOM   7788 C CB  . VAL D 1 188 ? 44.955  82.370 33.745  1.00 74.92  ?  343 VAL D CB  1 
ATOM   7789 C CG1 . VAL D 1 188 ? 44.905  83.742 33.082  1.00 74.49  ?  343 VAL D CG1 1 
ATOM   7790 C CG2 . VAL D 1 188 ? 43.560  81.782 33.858  1.00 74.30  ?  343 VAL D CG2 1 
ATOM   7791 N N   . MET D 1 189 ? 46.566  80.221 35.095  1.00 70.65  ?  344 MET D N   1 
ATOM   7792 C CA  . MET D 1 189 ? 46.962  79.084 35.923  1.00 70.91  ?  344 MET D CA  1 
ATOM   7793 C C   . MET D 1 189 ? 46.208  79.002 37.233  1.00 75.35  ?  344 MET D C   1 
ATOM   7794 O O   . MET D 1 189 ? 45.663  80.009 37.679  1.00 75.70  ?  344 MET D O   1 
ATOM   7795 C CB  . MET D 1 189 ? 48.466  79.156 36.195  1.00 73.76  ?  344 MET D CB  1 
ATOM   7796 C CG  . MET D 1 189 ? 49.326  78.548 35.093  1.00 78.20  ?  344 MET D CG  1 
ATOM   7797 S SD  . MET D 1 189 ? 49.368  76.738 35.087  1.00 83.60  ?  344 MET D SD  1 
ATOM   7798 C CE  . MET D 1 189 ? 49.810  76.379 36.884  1.00 80.63  ?  344 MET D CE  1 
HETATM 7799 N N   . TPO D 1 190 ? 46.192  77.814 37.865  1.00 72.45  ?  345 TPO D N   1 
HETATM 7800 C CA  . TPO D 1 190 ? 45.501  77.615 39.142  1.00 73.00  ?  345 TPO D CA  1 
HETATM 7801 C CB  . TPO D 1 190 ? 43.990  77.231 38.942  1.00 73.52  ?  345 TPO D CB  1 
HETATM 7802 C CG2 . TPO D 1 190 ? 43.880  75.874 38.241  1.00 73.48  ?  345 TPO D CG2 1 
HETATM 7803 O OG1 . TPO D 1 190 ? 43.190  77.131 40.177  1.00 73.80  ?  345 TPO D OG1 1 
HETATM 7804 P P   . TPO D 1 190 ? 42.682  78.456 40.821  1.00 72.54  ?  345 TPO D P   1 
HETATM 7805 O O1P . TPO D 1 190 ? 42.478  79.544 39.786  1.00 72.48  ?  345 TPO D O1P 1 
HETATM 7806 O O2P . TPO D 1 190 ? 43.687  78.962 41.871  1.00 73.02  -1 345 TPO D O2P 1 
HETATM 7807 O O3P . TPO D 1 190 ? 41.398  78.151 41.563  1.00 72.47  -1 345 TPO D O3P 1 
HETATM 7808 C C   . TPO D 1 190 ? 46.208  76.627 40.077  1.00 78.35  ?  345 TPO D C   1 
HETATM 7809 O O   . TPO D 1 190 ? 46.896  75.719 39.611  1.00 76.89  ?  345 TPO D O   1 
HETATM 7810 N N   . SEP D 1 191 ? 46.027  76.814 41.399  1.00 77.85  ?  346 SEP D N   1 
HETATM 7811 C CA  . SEP D 1 191 ? 46.587  75.941 42.433  1.00 79.69  ?  346 SEP D CA  1 
HETATM 7812 C CB  . SEP D 1 191 ? 47.202  76.594 43.680  1.00 84.68  ?  346 SEP D CB  1 
HETATM 7813 O OG  . SEP D 1 191 ? 46.244  77.355 44.432  1.00 89.71  ?  346 SEP D OG  1 
HETATM 7814 C C   . SEP D 1 191 ? 45.603  74.831 42.832  1.00 80.88  ?  346 SEP D C   1 
HETATM 7815 O O   . SEP D 1 191 ? 46.018  73.863 43.472  1.00 80.03  ?  346 SEP D O   1 
HETATM 7816 P P   . SEP D 1 191 ? 46.712  78.869 44.463  1.00 94.21  ?  346 SEP D P   1 
HETATM 7817 O O1P . SEP D 1 191 ? 46.866  79.507 43.047  1.00 94.25  -1 346 SEP D O1P 1 
HETATM 7818 O O2P . SEP D 1 191 ? 48.077  78.979 45.189  1.00 94.06  ?  346 SEP D O2P 1 
HETATM 7819 O O3P . SEP D 1 191 ? 45.626  79.676 45.243  1.00 95.18  -1 346 SEP D O3P 1 
ATOM   7820 N N   . ARG D 1 192 ? 44.305  74.974 42.454  1.00 75.02  ?  347 ARG D N   1 
ATOM   7821 C CA  . ARG D 1 192 ? 43.258  73.976 42.692  1.00 73.50  ?  347 ARG D CA  1 
ATOM   7822 C C   . ARG D 1 192 ? 42.803  73.367 41.352  1.00 73.16  ?  347 ARG D C   1 
ATOM   7823 O O   . ARG D 1 192 ? 42.088  74.011 40.582  1.00 72.14  ?  347 ARG D O   1 
ATOM   7824 C CB  . ARG D 1 192 ? 42.079  74.551 43.513  1.00 74.20  ?  347 ARG D CB  1 
ATOM   7825 C CG  . ARG D 1 192 ? 40.928  73.559 43.803  1.00 88.78  ?  347 ARG D CG  1 
ATOM   7826 C CD  . ARG D 1 192 ? 41.290  72.455 44.793  1.00 103.39 ?  347 ARG D CD  1 
ATOM   7827 N NE  . ARG D 1 192 ? 41.642  71.194 44.129  1.00 116.05 ?  347 ARG D NE  1 
ATOM   7828 C CZ  . ARG D 1 192 ? 40.925  70.074 44.200  1.00 132.45 ?  347 ARG D CZ  1 
ATOM   7829 N NH1 . ARG D 1 192 ? 39.805  70.036 44.914  1.00 120.93 ?  347 ARG D NH1 1 
ATOM   7830 N NH2 . ARG D 1 192 ? 41.331  68.978 43.570  1.00 118.16 1  347 ARG D NH2 1 
ATOM   7831 N N   . ILE D 1 193 ? 43.265  72.130 41.079  1.00 66.73  ?  348 ILE D N   1 
ATOM   7832 C CA  . ILE D 1 193 ? 42.966  71.376 39.861  1.00 64.88  ?  348 ILE D CA  1 
ATOM   7833 C C   . ILE D 1 193 ? 41.622  70.670 40.034  1.00 65.35  ?  348 ILE D C   1 
ATOM   7834 O O   . ILE D 1 193 ? 41.446  69.877 40.956  1.00 63.46  ?  348 ILE D O   1 
ATOM   7835 C CB  . ILE D 1 193 ? 44.160  70.438 39.454  1.00 67.50  ?  348 ILE D CB  1 
ATOM   7836 C CG1 . ILE D 1 193 ? 45.427  71.273 39.120  1.00 66.80  ?  348 ILE D CG1 1 
ATOM   7837 C CG2 . ILE D 1 193 ? 43.777  69.511 38.276  1.00 67.67  ?  348 ILE D CG2 1 
ATOM   7838 C CD1 . ILE D 1 193 ? 46.732  70.549 39.230  1.00 72.90  ?  348 ILE D CD1 1 
ATOM   7839 N N   . VAL D 1 194 ? 40.664  71.005 39.162  1.00 61.57  ?  349 VAL D N   1 
ATOM   7840 C CA  . VAL D 1 194 ? 39.282  70.503 39.196  1.00 60.95  ?  349 VAL D CA  1 
ATOM   7841 C C   . VAL D 1 194 ? 38.736  70.071 37.812  1.00 63.57  ?  349 VAL D C   1 
ATOM   7842 O O   . VAL D 1 194 ? 39.069  70.663 36.776  1.00 62.04  ?  349 VAL D O   1 
ATOM   7843 C CB  . VAL D 1 194 ? 38.299  71.472 39.931  1.00 64.62  ?  349 VAL D CB  1 
ATOM   7844 C CG1 . VAL D 1 194 ? 38.407  71.336 41.448  1.00 64.08  ?  349 VAL D CG1 1 
ATOM   7845 C CG2 . VAL D 1 194 ? 38.500  72.921 39.490  1.00 64.30  ?  349 VAL D CG2 1 
ATOM   7846 N N   . GLY D 1 195 ? 37.855  69.071 37.850  1.00 59.82  ?  350 GLY D N   1 
ATOM   7847 C CA  . GLY D 1 195 ? 37.222  68.442 36.697  1.00 59.02  ?  350 GLY D CA  1 
ATOM   7848 C C   . GLY D 1 195 ? 37.234  66.930 36.839  1.00 63.41  ?  350 GLY D C   1 
ATOM   7849 O O   . GLY D 1 195 ? 37.561  66.393 37.911  1.00 61.38  ?  350 GLY D O   1 
ATOM   7850 N N   . THR D 1 196 ? 36.851  66.226 35.764  1.00 61.56  ?  351 THR D N   1 
ATOM   7851 C CA  . THR D 1 196 ? 36.832  64.764 35.752  1.00 61.72  ?  351 THR D CA  1 
ATOM   7852 C C   . THR D 1 196 ? 38.000  64.309 34.882  1.00 65.14  ?  351 THR D C   1 
ATOM   7853 O O   . THR D 1 196 ? 37.945  64.479 33.660  1.00 65.14  ?  351 THR D O   1 
ATOM   7854 C CB  . THR D 1 196 ? 35.446  64.243 35.335  1.00 74.29  ?  351 THR D CB  1 
ATOM   7855 O OG1 . THR D 1 196 ? 34.459  64.862 36.164  1.00 75.39  ?  351 THR D OG1 1 
ATOM   7856 C CG2 . THR D 1 196 ? 35.335  62.713 35.427  1.00 73.54  ?  351 THR D CG2 1 
ATOM   7857 N N   . THR D 1 197 ? 39.067  63.772 35.523  1.00 60.07  ?  352 THR D N   1 
ATOM   7858 C CA  . THR D 1 197 ? 40.320  63.352 34.880  1.00 59.61  ?  352 THR D CA  1 
ATOM   7859 C C   . THR D 1 197 ? 40.162  62.621 33.556  1.00 60.75  ?  352 THR D C   1 
ATOM   7860 O O   . THR D 1 197 ? 40.938  62.877 32.643  1.00 61.40  ?  352 THR D O   1 
ATOM   7861 C CB  . THR D 1 197 ? 41.260  62.618 35.846  1.00 79.66  ?  352 THR D CB  1 
ATOM   7862 O OG1 . THR D 1 197 ? 40.696  61.356 36.185  1.00 89.97  ?  352 THR D OG1 1 
ATOM   7863 C CG2 . THR D 1 197 ? 41.548  63.407 37.112  1.00 81.09  ?  352 THR D CG2 1 
ATOM   7864 N N   . ALA D 1 198 ? 39.137  61.753 33.435  1.00 55.67  ?  353 ALA D N   1 
ATOM   7865 C CA  . ALA D 1 198 ? 38.841  60.961 32.228  1.00 54.54  ?  353 ALA D CA  1 
ATOM   7866 C C   . ALA D 1 198 ? 38.508  61.806 30.993  1.00 56.25  ?  353 ALA D C   1 
ATOM   7867 O O   . ALA D 1 198 ? 38.660  61.320 29.870  1.00 55.35  ?  353 ALA D O   1 
ATOM   7868 C CB  . ALA D 1 198 ? 37.718  59.975 32.504  1.00 54.93  ?  353 ALA D CB  1 
ATOM   7869 N N   . TYR D 1 199 ? 38.076  63.063 31.205  1.00 51.29  ?  354 TYR D N   1 
ATOM   7870 C CA  . TYR D 1 199 ? 37.686  63.991 30.144  1.00 50.86  ?  354 TYR D CA  1 
ATOM   7871 C C   . TYR D 1 199 ? 38.673  65.153 29.988  1.00 53.90  ?  354 TYR D C   1 
ATOM   7872 O O   . TYR D 1 199 ? 38.691  65.801 28.938  1.00 52.84  ?  354 TYR D O   1 
ATOM   7873 C CB  . TYR D 1 199 ? 36.287  64.585 30.437  1.00 51.27  ?  354 TYR D CB  1 
ATOM   7874 C CG  . TYR D 1 199 ? 35.167  63.577 30.520  1.00 51.93  ?  354 TYR D CG  1 
ATOM   7875 C CD1 . TYR D 1 199 ? 34.890  62.910 31.709  1.00 54.01  ?  354 TYR D CD1 1 
ATOM   7876 C CD2 . TYR D 1 199 ? 34.338  63.331 29.423  1.00 52.08  ?  354 TYR D CD2 1 
ATOM   7877 C CE1 . TYR D 1 199 ? 33.848  61.985 31.795  1.00 55.22  ?  354 TYR D CE1 1 
ATOM   7878 C CE2 . TYR D 1 199 ? 33.288  62.412 29.499  1.00 52.54  ?  354 TYR D CE2 1 
ATOM   7879 C CZ  . TYR D 1 199 ? 33.037  61.752 30.690  1.00 62.52  ?  354 TYR D CZ  1 
ATOM   7880 O OH  . TYR D 1 199 ? 32.003  60.847 30.775  1.00 69.81  ?  354 TYR D OH  1 
ATOM   7881 N N   . MET D 1 200 ? 39.443  65.442 31.048  1.00 49.31  ?  355 MET D N   1 
ATOM   7882 C CA  . MET D 1 200 ? 40.391  66.557 31.129  1.00 48.45  ?  355 MET D CA  1 
ATOM   7883 C C   . MET D 1 200 ? 41.535  66.537 30.161  1.00 51.12  ?  355 MET D C   1 
ATOM   7884 O O   . MET D 1 200 ? 42.191  65.510 29.992  1.00 48.62  ?  355 MET D O   1 
ATOM   7885 C CB  . MET D 1 200 ? 40.928  66.738 32.546  1.00 50.50  ?  355 MET D CB  1 
ATOM   7886 C CG  . MET D 1 200 ? 39.879  67.202 33.478  1.00 55.11  ?  355 MET D CG  1 
ATOM   7887 S SD  . MET D 1 200 ? 40.432  67.271 35.177  1.00 61.15  ?  355 MET D SD  1 
ATOM   7888 C CE  . MET D 1 200 ? 41.369  68.828 35.137  1.00 58.09  ?  355 MET D CE  1 
ATOM   7889 N N   . ALA D 1 201 ? 41.788  67.712 29.548  1.00 49.65  ?  356 ALA D N   1 
ATOM   7890 C CA  . ALA D 1 201 ? 42.908  67.962 28.645  1.00 49.74  ?  356 ALA D CA  1 
ATOM   7891 C C   . ALA D 1 201 ? 44.222  67.904 29.451  1.00 53.03  ?  356 ALA D C   1 
ATOM   7892 O O   . ALA D 1 201 ? 44.208  68.223 30.641  1.00 51.85  ?  356 ALA D O   1 
ATOM   7893 C CB  . ALA D 1 201 ? 42.751  69.329 28.000  1.00 50.47  ?  356 ALA D CB  1 
ATOM   7894 N N   . PRO D 1 202 ? 45.345  67.439 28.862  1.00 50.82  ?  357 PRO D N   1 
ATOM   7895 C CA  . PRO D 1 202 ? 46.598  67.341 29.646  1.00 50.72  ?  357 PRO D CA  1 
ATOM   7896 C C   . PRO D 1 202 ? 46.978  68.617 30.414  1.00 55.93  ?  357 PRO D C   1 
ATOM   7897 O O   . PRO D 1 202 ? 47.294  68.520 31.604  1.00 57.31  ?  357 PRO D O   1 
ATOM   7898 C CB  . PRO D 1 202 ? 47.653  66.917 28.610  1.00 51.54  ?  357 PRO D CB  1 
ATOM   7899 C CG  . PRO D 1 202 ? 47.026  67.180 27.280  1.00 55.80  ?  357 PRO D CG  1 
ATOM   7900 C CD  . PRO D 1 202 ? 45.552  66.978 27.474  1.00 51.75  ?  357 PRO D CD  1 
ATOM   7901 N N   . GLU D 1 203 ? 46.878  69.804 29.768  1.00 50.38  ?  358 GLU D N   1 
ATOM   7902 C CA  . GLU D 1 203 ? 47.190  71.099 30.390  1.00 49.44  ?  358 GLU D CA  1 
ATOM   7903 C C   . GLU D 1 203 ? 46.269  71.434 31.552  1.00 53.51  ?  358 GLU D C   1 
ATOM   7904 O O   . GLU D 1 203 ? 46.699  72.073 32.511  1.00 54.32  ?  358 GLU D O   1 
ATOM   7905 C CB  . GLU D 1 203 ? 47.228  72.237 29.367  1.00 50.60  ?  358 GLU D CB  1 
ATOM   7906 C CG  . GLU D 1 203 ? 45.885  72.630 28.772  1.00 60.39  ?  358 GLU D CG  1 
ATOM   7907 C CD  . GLU D 1 203 ? 45.358  71.780 27.627  1.00 76.98  ?  358 GLU D CD  1 
ATOM   7908 O OE1 . GLU D 1 203 ? 45.940  70.710 27.321  1.00 80.97  ?  358 GLU D OE1 1 
ATOM   7909 O OE2 . GLU D 1 203 ? 44.325  72.180 27.049  1.00 54.66  -1 358 GLU D OE2 1 
ATOM   7910 N N   . ALA D 1 204 ? 45.010  70.986 31.478  1.00 49.14  ?  359 ALA D N   1 
ATOM   7911 C CA  . ALA D 1 204 ? 44.026  71.205 32.538  1.00 48.10  ?  359 ALA D CA  1 
ATOM   7912 C C   . ALA D 1 204 ? 44.461  70.393 33.772  1.00 52.95  ?  359 ALA D C   1 
ATOM   7913 O O   . ALA D 1 204 ? 44.381  70.888 34.902  1.00 52.52  ?  359 ALA D O   1 
ATOM   7914 C CB  . ALA D 1 204 ? 42.640  70.786 32.069  1.00 47.88  ?  359 ALA D CB  1 
ATOM   7915 N N   . LEU D 1 205 ? 45.005  69.178 33.534  1.00 48.54  ?  360 LEU D N   1 
ATOM   7916 C CA  . LEU D 1 205 ? 45.499  68.300 34.598  1.00 47.80  ?  360 LEU D CA  1 
ATOM   7917 C C   . LEU D 1 205 ? 46.770  68.907 35.244  1.00 52.09  ?  360 LEU D C   1 
ATOM   7918 O O   . LEU D 1 205 ? 47.058  68.634 36.411  1.00 51.63  ?  360 LEU D O   1 
ATOM   7919 C CB  . LEU D 1 205 ? 45.758  66.882 34.070  1.00 46.83  ?  360 LEU D CB  1 
ATOM   7920 C CG  . LEU D 1 205 ? 44.537  66.031 33.702  1.00 49.46  ?  360 LEU D CG  1 
ATOM   7921 C CD1 . LEU D 1 205 ? 44.925  64.875 32.839  1.00 48.34  ?  360 LEU D CD1 1 
ATOM   7922 C CD2 . LEU D 1 205 ? 43.804  65.529 34.930  1.00 51.20  ?  360 LEU D CD2 1 
ATOM   7923 N N   . ARG D 1 206 ? 47.498  69.746 34.449  1.00 47.38  ?  361 ARG D N   1 
ATOM   7924 C CA  . ARG D 1 206 ? 48.703  70.520 34.771  1.00 46.05  ?  361 ARG D CA  1 
ATOM   7925 C C   . ARG D 1 206 ? 48.395  71.938 35.373  1.00 50.65  ?  361 ARG D C   1 
ATOM   7926 O O   . ARG D 1 206 ? 49.330  72.691 35.660  1.00 47.98  ?  361 ARG D O   1 
ATOM   7927 C CB  . ARG D 1 206 ? 49.573  70.692 33.522  1.00 42.21  ?  361 ARG D CB  1 
ATOM   7928 C CG  . ARG D 1 206 ? 50.258  69.439 33.026  1.00 50.09  ?  361 ARG D CG  1 
ATOM   7929 C CD  . ARG D 1 206 ? 51.344  69.804 32.034  1.00 44.13  ?  361 ARG D CD  1 
ATOM   7930 N NE  . ARG D 1 206 ? 51.282  69.025 30.794  1.00 39.53  ?  361 ARG D NE  1 
ATOM   7931 C CZ  . ARG D 1 206 ? 52.009  67.934 30.590  1.00 58.86  ?  361 ARG D CZ  1 
ATOM   7932 N NH1 . ARG D 1 206 ? 52.818  67.486 31.539  1.00 59.42  ?  361 ARG D NH1 1 
ATOM   7933 N NH2 . ARG D 1 206 ? 51.948  67.293 29.430  1.00 37.55  1  361 ARG D NH2 1 
ATOM   7934 N N   . GLY D 1 207 ? 47.114  72.298 35.526  1.00 49.16  ?  362 GLY D N   1 
ATOM   7935 C CA  . GLY D 1 207 ? 46.702  73.567 36.131  1.00 49.07  ?  362 GLY D CA  1 
ATOM   7936 C C   . GLY D 1 207 ? 46.367  74.729 35.205  1.00 51.87  ?  362 GLY D C   1 
ATOM   7937 O O   . GLY D 1 207 ? 46.057  75.818 35.694  1.00 50.30  ?  362 GLY D O   1 
ATOM   7938 N N   . GLU D 1 208 ? 46.436  74.527 33.870  1.00 49.55  ?  363 GLU D N   1 
ATOM   7939 C CA  . GLU D 1 208 ? 46.092  75.581 32.906  1.00 50.51  ?  363 GLU D CA  1 
ATOM   7940 C C   . GLU D 1 208 ? 44.576  75.767 32.791  1.00 58.95  ?  363 GLU D C   1 
ATOM   7941 O O   . GLU D 1 208 ? 43.809  74.806 32.904  1.00 59.67  ?  363 GLU D O   1 
ATOM   7942 C CB  . GLU D 1 208 ? 46.667  75.296 31.517  1.00 51.77  ?  363 GLU D CB  1 
ATOM   7943 C CG  . GLU D 1 208 ? 48.057  75.864 31.310  1.00 64.49  ?  363 GLU D CG  1 
ATOM   7944 C CD  . GLU D 1 208 ? 48.722  75.493 29.995  1.00 81.84  ?  363 GLU D CD  1 
ATOM   7945 O OE1 . GLU D 1 208 ? 49.552  74.554 29.990  1.00 80.27  ?  363 GLU D OE1 1 
ATOM   7946 O OE2 . GLU D 1 208 ? 48.438  76.161 28.974  1.00 63.26  -1 363 GLU D OE2 1 
ATOM   7947 N N   . ILE D 1 209 ? 44.151  77.019 32.579  1.00 56.71  ?  364 ILE D N   1 
ATOM   7948 C CA  . ILE D 1 209 ? 42.748  77.392 32.375  1.00 56.19  ?  364 ILE D CA  1 
ATOM   7949 C C   . ILE D 1 209 ? 42.648  78.037 30.975  1.00 58.97  ?  364 ILE D C   1 
ATOM   7950 O O   . ILE D 1 209 ? 43.130  79.149 30.755  1.00 58.97  ?  364 ILE D O   1 
ATOM   7951 C CB  . ILE D 1 209 ? 42.175  78.245 33.564  1.00 58.81  ?  364 ILE D CB  1 
ATOM   7952 C CG1 . ILE D 1 209 ? 42.052  77.361 34.821  1.00 59.21  ?  364 ILE D CG1 1 
ATOM   7953 C CG2 . ILE D 1 209 ? 40.810  78.866 33.220  1.00 59.19  ?  364 ILE D CG2 1 
ATOM   7954 C CD1 . ILE D 1 209 ? 42.000  78.086 36.112  1.00 68.18  ?  364 ILE D CD1 1 
ATOM   7955 N N   . THR D 1 210 ? 42.097  77.288 30.019  1.00 53.68  ?  365 THR D N   1 
ATOM   7956 C CA  . THR D 1 210 ? 41.971  77.739 28.640  1.00 52.40  ?  365 THR D CA  1 
ATOM   7957 C C   . THR D 1 210 ? 40.688  77.214 27.980  1.00 55.84  ?  365 THR D C   1 
ATOM   7958 O O   . THR D 1 210 ? 40.321  76.060 28.208  1.00 54.51  ?  365 THR D O   1 
ATOM   7959 C CB  . THR D 1 210 ? 43.253  77.422 27.831  1.00 57.69  ?  365 THR D CB  1 
ATOM   7960 O OG1 . THR D 1 210 ? 42.999  77.609 26.441  1.00 64.12  ?  365 THR D OG1 1 
ATOM   7961 C CG2 . THR D 1 210 ? 43.773  76.011 28.051  1.00 51.60  ?  365 THR D CG2 1 
ATOM   7962 N N   . PRO D 1 211 ? 40.004  78.024 27.129  1.00 51.98  ?  366 PRO D N   1 
ATOM   7963 C CA  . PRO D 1 211 ? 38.809  77.513 26.450  1.00 51.21  ?  366 PRO D CA  1 
ATOM   7964 C C   . PRO D 1 211 ? 39.111  76.297 25.569  1.00 54.68  ?  366 PRO D C   1 
ATOM   7965 O O   . PRO D 1 211 ? 38.214  75.503 25.312  1.00 55.12  ?  366 PRO D O   1 
ATOM   7966 C CB  . PRO D 1 211 ? 38.357  78.712 25.617  1.00 52.61  ?  366 PRO D CB  1 
ATOM   7967 C CG  . PRO D 1 211 ? 39.567  79.538 25.443  1.00 56.73  ?  366 PRO D CG  1 
ATOM   7968 C CD  . PRO D 1 211 ? 40.275  79.422 26.728  1.00 52.37  ?  366 PRO D CD  1 
ATOM   7969 N N   . LYS D 1 212 ? 40.388  76.135 25.144  1.00 48.81  ?  367 LYS D N   1 
ATOM   7970 C CA  . LYS D 1 212 ? 40.844  75.021 24.320  1.00 47.39  ?  367 LYS D CA  1 
ATOM   7971 C C   . LYS D 1 212 ? 40.734  73.681 25.071  1.00 49.37  ?  367 LYS D C   1 
ATOM   7972 O O   . LYS D 1 212 ? 40.665  72.630 24.429  1.00 49.65  ?  367 LYS D O   1 
ATOM   7973 C CB  . LYS D 1 212 ? 42.273  75.286 23.794  1.00 49.54  ?  367 LYS D CB  1 
ATOM   7974 N N   . SER D 1 213 ? 40.682  73.721 26.421  1.00 44.16  ?  368 SER D N   1 
ATOM   7975 C CA  . SER D 1 213 ? 40.525  72.528 27.270  1.00 43.53  ?  368 SER D CA  1 
ATOM   7976 C C   . SER D 1 213 ? 39.100  71.944 27.112  1.00 45.74  ?  368 SER D C   1 
ATOM   7977 O O   . SER D 1 213 ? 38.934  70.722 27.059  1.00 44.01  ?  368 SER D O   1 
ATOM   7978 C CB  . SER D 1 213 ? 40.811  72.860 28.736  1.00 47.92  ?  368 SER D CB  1 
ATOM   7979 O OG  . SER D 1 213 ? 42.177  73.161 28.974  1.00 54.01  ?  368 SER D OG  1 
ATOM   7980 N N   . ASP D 1 214 ? 38.086  72.835 26.989  1.00 41.77  ?  369 ASP D N   1 
ATOM   7981 C CA  . ASP D 1 214 ? 36.679  72.500 26.759  1.00 40.65  ?  369 ASP D CA  1 
ATOM   7982 C C   . ASP D 1 214 ? 36.518  71.740 25.440  1.00 44.42  ?  369 ASP D C   1 
ATOM   7983 O O   . ASP D 1 214 ? 35.715  70.809 25.383  1.00 45.56  ?  369 ASP D O   1 
ATOM   7984 C CB  . ASP D 1 214 ? 35.814  73.769 26.755  1.00 42.17  ?  369 ASP D CB  1 
ATOM   7985 C CG  . ASP D 1 214 ? 35.409  74.337 28.117  1.00 52.97  ?  369 ASP D CG  1 
ATOM   7986 O OD1 . ASP D 1 214 ? 35.826  73.769 29.156  1.00 54.08  ?  369 ASP D OD1 1 
ATOM   7987 O OD2 . ASP D 1 214 ? 34.646  75.329 28.142  1.00 60.76  -1 369 ASP D OD2 1 
ATOM   7988 N N   . ILE D 1 215 ? 37.314  72.105 24.401  1.00 40.14  ?  370 ILE D N   1 
ATOM   7989 C CA  . ILE D 1 215 ? 37.343  71.440 23.086  1.00 40.50  ?  370 ILE D CA  1 
ATOM   7990 C C   . ILE D 1 215 ? 37.826  69.987 23.227  1.00 45.66  ?  370 ILE D C   1 
ATOM   7991 O O   . ILE D 1 215 ? 37.239  69.071 22.633  1.00 44.71  ?  370 ILE D O   1 
ATOM   7992 C CB  . ILE D 1 215 ? 38.195  72.244 22.068  1.00 42.82  ?  370 ILE D CB  1 
ATOM   7993 C CG1 . ILE D 1 215 ? 37.691  73.690 21.927  1.00 42.93  ?  370 ILE D CG1 1 
ATOM   7994 C CG2 . ILE D 1 215 ? 38.372  71.533 20.702  1.00 42.05  ?  370 ILE D CG2 1 
ATOM   7995 C CD1 . ILE D 1 215 ? 36.445  73.876 21.213  1.00 52.38  ?  370 ILE D CD1 1 
ATOM   7996 N N   . TYR D 1 216 ? 38.864  69.781 24.044  1.00 42.99  ?  371 TYR D N   1 
ATOM   7997 C CA  . TYR D 1 216 ? 39.408  68.439 24.296  1.00 42.60  ?  371 TYR D CA  1 
ATOM   7998 C C   . TYR D 1 216 ? 38.361  67.560 24.990  1.00 48.07  ?  371 TYR D C   1 
ATOM   7999 O O   . TYR D 1 216 ? 38.140  66.430 24.554  1.00 49.99  ?  371 TYR D O   1 
ATOM   8000 C CB  . TYR D 1 216 ? 40.702  68.525 25.115  1.00 42.47  ?  371 TYR D CB  1 
ATOM   8001 C CG  . TYR D 1 216 ? 41.430  67.212 25.283  1.00 43.49  ?  371 TYR D CG  1 
ATOM   8002 C CD1 . TYR D 1 216 ? 41.103  66.336 26.314  1.00 45.02  ?  371 TYR D CD1 1 
ATOM   8003 C CD2 . TYR D 1 216 ? 42.461  66.849 24.420  1.00 44.50  ?  371 TYR D CD2 1 
ATOM   8004 C CE1 . TYR D 1 216 ? 41.762  65.119 26.464  1.00 44.66  ?  371 TYR D CE1 1 
ATOM   8005 C CE2 . TYR D 1 216 ? 43.138  65.643 24.572  1.00 44.99  ?  371 TYR D CE2 1 
ATOM   8006 C CZ  . TYR D 1 216 ? 42.789  64.788 25.597  1.00 56.17  ?  371 TYR D CZ  1 
ATOM   8007 O OH  . TYR D 1 216 ? 43.462  63.604 25.742  1.00 67.03  ?  371 TYR D OH  1 
ATOM   8008 N N   . SER D 1 217 ? 37.694  68.093 26.026  1.00 42.49  ?  372 SER D N   1 
ATOM   8009 C CA  . SER D 1 217 ? 36.662  67.390 26.789  1.00 41.61  ?  372 SER D CA  1 
ATOM   8010 C C   . SER D 1 217 ? 35.484  66.973 25.918  1.00 44.35  ?  372 SER D C   1 
ATOM   8011 O O   . SER D 1 217 ? 34.944  65.880 26.073  1.00 43.28  ?  372 SER D O   1 
ATOM   8012 C CB  . SER D 1 217 ? 36.197  68.248 27.960  1.00 42.39  ?  372 SER D CB  1 
ATOM   8013 O OG  . SER D 1 217 ? 37.200  68.273 28.957  1.00 46.05  ?  372 SER D OG  1 
ATOM   8014 N N   . PHE D 1 218 ? 35.130  67.832 24.973  1.00 42.15  ?  373 PHE D N   1 
ATOM   8015 C CA  . PHE D 1 218 ? 34.052  67.584 24.028  1.00 42.28  ?  373 PHE D CA  1 
ATOM   8016 C C   . PHE D 1 218 ? 34.419  66.451 23.070  1.00 48.89  ?  373 PHE D C   1 
ATOM   8017 O O   . PHE D 1 218 ? 33.533  65.696 22.665  1.00 50.62  ?  373 PHE D O   1 
ATOM   8018 C CB  . PHE D 1 218 ? 33.707  68.856 23.261  1.00 43.44  ?  373 PHE D CB  1 
ATOM   8019 C CG  . PHE D 1 218 ? 32.505  68.699 22.377  1.00 45.03  ?  373 PHE D CG  1 
ATOM   8020 C CD1 . PHE D 1 218 ? 31.249  68.432 22.925  1.00 48.41  ?  373 PHE D CD1 1 
ATOM   8021 C CD2 . PHE D 1 218 ? 32.625  68.785 20.992  1.00 46.41  ?  373 PHE D CD2 1 
ATOM   8022 C CE1 . PHE D 1 218 ? 30.138  68.268 22.106  1.00 49.41  ?  373 PHE D CE1 1 
ATOM   8023 C CE2 . PHE D 1 218 ? 31.508  68.639 20.175  1.00 49.82  ?  373 PHE D CE2 1 
ATOM   8024 C CZ  . PHE D 1 218 ? 30.270  68.399 20.736  1.00 48.38  ?  373 PHE D CZ  1 
ATOM   8025 N N   . GLY D 1 219 ? 35.707  66.330 22.734  1.00 44.12  ?  374 GLY D N   1 
ATOM   8026 C CA  . GLY D 1 219 ? 36.211  65.246 21.902  1.00 43.40  ?  374 GLY D CA  1 
ATOM   8027 C C   . GLY D 1 219 ? 35.950  63.904 22.556  1.00 47.30  ?  374 GLY D C   1 
ATOM   8028 O O   . GLY D 1 219 ? 35.492  62.963 21.890  1.00 46.54  ?  374 GLY D O   1 
ATOM   8029 N N   . VAL D 1 220 ? 36.179  63.834 23.896  1.00 44.70  ?  375 VAL D N   1 
ATOM   8030 C CA  . VAL D 1 220 ? 35.979  62.624 24.713  1.00 45.17  ?  375 VAL D CA  1 
ATOM   8031 C C   . VAL D 1 220 ? 34.494  62.242 24.669  1.00 49.58  ?  375 VAL D C   1 
ATOM   8032 O O   . VAL D 1 220 ? 34.147  61.061 24.543  1.00 50.23  ?  375 VAL D O   1 
ATOM   8033 C CB  . VAL D 1 220 ? 36.508  62.796 26.177  1.00 49.46  ?  375 VAL D CB  1 
ATOM   8034 C CG1 . VAL D 1 220 ? 36.281  61.529 26.998  1.00 49.46  ?  375 VAL D CG1 1 
ATOM   8035 C CG2 . VAL D 1 220 ? 37.989  63.166 26.192  1.00 49.38  ?  375 VAL D CG2 1 
ATOM   8036 N N   . VAL D 1 221 ? 33.622  63.268 24.733  1.00 44.13  ?  376 VAL D N   1 
ATOM   8037 C CA  . VAL D 1 221 ? 32.180  63.124 24.671  1.00 42.07  ?  376 VAL D CA  1 
ATOM   8038 C C   . VAL D 1 221 ? 31.799  62.558 23.308  1.00 42.60  ?  376 VAL D C   1 
ATOM   8039 O O   . VAL D 1 221 ? 31.005  61.618 23.260  1.00 40.27  ?  376 VAL D O   1 
ATOM   8040 C CB  . VAL D 1 221 ? 31.455  64.445 25.011  1.00 45.60  ?  376 VAL D CB  1 
ATOM   8041 C CG1 . VAL D 1 221 ? 29.963  64.358 24.697  1.00 45.33  ?  376 VAL D CG1 1 
ATOM   8042 C CG2 . VAL D 1 221 ? 31.675  64.813 26.475  1.00 45.38  ?  376 VAL D CG2 1 
ATOM   8043 N N   . LEU D 1 222 ? 32.401  63.085 22.214  1.00 38.45  ?  377 LEU D N   1 
ATOM   8044 C CA  . LEU D 1 222 ? 32.100  62.587 20.869  1.00 38.21  ?  377 LEU D CA  1 
ATOM   8045 C C   . LEU D 1 222 ? 32.500  61.114 20.742  1.00 41.04  ?  377 LEU D C   1 
ATOM   8046 O O   . LEU D 1 222 ? 31.768  60.345 20.137  1.00 40.52  ?  377 LEU D O   1 
ATOM   8047 C CB  . LEU D 1 222 ? 32.720  63.448 19.768  1.00 38.35  ?  377 LEU D CB  1 
ATOM   8048 C CG  . LEU D 1 222 ? 32.229  64.883 19.634  1.00 42.07  ?  377 LEU D CG  1 
ATOM   8049 C CD1 . LEU D 1 222 ? 33.078  65.637 18.626  1.00 43.78  ?  377 LEU D CD1 1 
ATOM   8050 C CD2 . LEU D 1 222 ? 30.776  64.944 19.229  1.00 37.83  ?  377 LEU D CD2 1 
ATOM   8051 N N   . LEU D 1 223 ? 33.590  60.702 21.401  1.00 37.31  ?  378 LEU D N   1 
ATOM   8052 C CA  . LEU D 1 223 ? 33.953  59.290 21.401  1.00 37.67  ?  378 LEU D CA  1 
ATOM   8053 C C   . LEU D 1 223 ? 32.904  58.458 22.169  1.00 43.51  ?  378 LEU D C   1 
ATOM   8054 O O   . LEU D 1 223 ? 32.565  57.357 21.731  1.00 44.47  ?  378 LEU D O   1 
ATOM   8055 C CB  . LEU D 1 223 ? 35.344  59.042 21.978  1.00 37.33  ?  378 LEU D CB  1 
ATOM   8056 C CG  . LEU D 1 223 ? 36.569  59.515 21.190  1.00 42.20  ?  378 LEU D CG  1 
ATOM   8057 C CD1 . LEU D 1 223 ? 37.807  58.988 21.833  1.00 42.09  ?  378 LEU D CD1 1 
ATOM   8058 C CD2 . LEU D 1 223 ? 36.552  59.074 19.715  1.00 44.12  ?  378 LEU D CD2 1 
ATOM   8059 N N   . GLU D 1 224 ? 32.365  58.999 23.284  1.00 39.15  ?  379 GLU D N   1 
ATOM   8060 C CA  . GLU D 1 224 ? 31.315  58.328 24.056  1.00 37.92  ?  379 GLU D CA  1 
ATOM   8061 C C   . GLU D 1 224 ? 30.093  58.188 23.166  1.00 43.14  ?  379 GLU D C   1 
ATOM   8062 O O   . GLU D 1 224 ? 29.486  57.121 23.128  1.00 44.10  ?  379 GLU D O   1 
ATOM   8063 C CB  . GLU D 1 224 ? 30.934  59.131 25.300  1.00 38.46  ?  379 GLU D CB  1 
ATOM   8064 C CG  . GLU D 1 224 ? 31.966  59.094 26.401  1.00 47.88  ?  379 GLU D CG  1 
ATOM   8065 C CD  . GLU D 1 224 ? 31.553  59.842 27.650  1.00 73.56  ?  379 GLU D CD  1 
ATOM   8066 O OE1 . GLU D 1 224 ? 31.204  61.039 27.527  1.00 74.06  ?  379 GLU D OE1 1 
ATOM   8067 O OE2 . GLU D 1 224 ? 31.563  59.230 28.745  1.00 69.34  -1 379 GLU D OE2 1 
ATOM   8068 N N   . ILE D 1 225 ? 29.751  59.254 22.418  1.00 38.63  ?  380 ILE D N   1 
ATOM   8069 C CA  . ILE D 1 225 ? 28.610  59.245 21.503  1.00 36.85  ?  380 ILE D CA  1 
ATOM   8070 C C   . ILE D 1 225 ? 28.771  58.154 20.407  1.00 41.55  ?  380 ILE D C   1 
ATOM   8071 O O   . ILE D 1 225 ? 27.814  57.401 20.167  1.00 42.96  ?  380 ILE D O   1 
ATOM   8072 C CB  . ILE D 1 225 ? 28.275  60.654 20.966  1.00 38.56  ?  380 ILE D CB  1 
ATOM   8073 C CG1 . ILE D 1 225 ? 27.710  61.551 22.098  1.00 39.06  ?  380 ILE D CG1 1 
ATOM   8074 C CG2 . ILE D 1 225 ? 27.294  60.581 19.825  1.00 39.03  ?  380 ILE D CG2 1 
ATOM   8075 C CD1 . ILE D 1 225 ? 27.514  63.080 21.722  1.00 41.27  ?  380 ILE D CD1 1 
ATOM   8076 N N   . ILE D 1 226 ? 29.972  58.016 19.810  1.00 34.13  ?  381 ILE D N   1 
ATOM   8077 C CA  . ILE D 1 226 ? 30.176  57.011 18.774  1.00 34.06  ?  381 ILE D CA  1 
ATOM   8078 C C   . ILE D 1 226 ? 30.101  55.568 19.327  1.00 38.15  ?  381 ILE D C   1 
ATOM   8079 O O   . ILE D 1 226 ? 29.492  54.699 18.713  1.00 34.72  ?  381 ILE D O   1 
ATOM   8080 C CB  . ILE D 1 226 ? 31.510  57.269 17.996  1.00 37.16  ?  381 ILE D CB  1 
ATOM   8081 C CG1 . ILE D 1 226 ? 31.490  58.605 17.236  1.00 36.61  ?  381 ILE D CG1 1 
ATOM   8082 C CG2 . ILE D 1 226 ? 31.856  56.126 17.037  1.00 37.85  ?  381 ILE D CG2 1 
ATOM   8083 C CD1 . ILE D 1 226 ? 32.937  59.273 17.060  1.00 39.23  ?  381 ILE D CD1 1 
ATOM   8084 N N   . THR D 1 227 ? 30.754  55.329 20.463  1.00 37.75  ?  382 THR D N   1 
ATOM   8085 C CA  . THR D 1 227 ? 30.938  54.008 21.063  1.00 37.85  ?  382 THR D CA  1 
ATOM   8086 C C   . THR D 1 227 ? 29.911  53.549 22.061  1.00 41.83  ?  382 THR D C   1 
ATOM   8087 O O   . THR D 1 227 ? 29.773  52.345 22.255  1.00 42.85  ?  382 THR D O   1 
ATOM   8088 C CB  . THR D 1 227 ? 32.360  53.911 21.686  1.00 40.16  ?  382 THR D CB  1 
ATOM   8089 O OG1 . THR D 1 227 ? 32.394  54.666 22.897  1.00 38.91  ?  382 THR D OG1 1 
ATOM   8090 C CG2 . THR D 1 227 ? 33.471  54.380 20.732  1.00 27.18  ?  382 THR D CG2 1 
ATOM   8091 N N   . GLY D 1 228 ? 29.266  54.485 22.743  1.00 38.42  ?  383 GLY D N   1 
ATOM   8092 C CA  . GLY D 1 228 ? 28.303  54.179 23.799  1.00 39.04  ?  383 GLY D CA  1 
ATOM   8093 C C   . GLY D 1 228 ? 28.977  53.740 25.093  1.00 45.84  ?  383 GLY D C   1 
ATOM   8094 O O   . GLY D 1 228 ? 28.311  53.287 26.032  1.00 45.72  ?  383 GLY D O   1 
ATOM   8095 N N   . LEU D 1 229 ? 30.318  53.882 25.150  1.00 43.79  ?  384 LEU D N   1 
ATOM   8096 C CA  . LEU D 1 229 ? 31.164  53.509 26.284  1.00 43.29  ?  384 LEU D CA  1 
ATOM   8097 C C   . LEU D 1 229 ? 31.460  54.721 27.164  1.00 45.98  ?  384 LEU D C   1 
ATOM   8098 O O   . LEU D 1 229 ? 31.733  55.797 26.610  1.00 44.31  ?  384 LEU D O   1 
ATOM   8099 C CB  . LEU D 1 229 ? 32.509  52.967 25.777  1.00 43.13  ?  384 LEU D CB  1 
ATOM   8100 C CG  . LEU D 1 229 ? 32.501  51.683 24.998  1.00 47.33  ?  384 LEU D CG  1 
ATOM   8101 C CD1 . LEU D 1 229 ? 33.783  51.543 24.214  1.00 48.03  ?  384 LEU D CD1 1 
ATOM   8102 C CD2 . LEU D 1 229 ? 32.304  50.492 25.914  1.00 49.18  ?  384 LEU D CD2 1 
ATOM   8103 N N   . PRO D 1 230 ? 31.481  54.559 28.520  1.00 42.57  ?  385 PRO D N   1 
ATOM   8104 C CA  . PRO D 1 230 ? 31.849  55.705 29.392  1.00 42.53  ?  385 PRO D CA  1 
ATOM   8105 C C   . PRO D 1 230 ? 33.337  56.039 29.235  1.00 45.86  ?  385 PRO D C   1 
ATOM   8106 O O   . PRO D 1 230 ? 34.106  55.145 28.870  1.00 44.90  ?  385 PRO D O   1 
ATOM   8107 C CB  . PRO D 1 230 ? 31.536  55.193 30.804  1.00 44.35  ?  385 PRO D CB  1 
ATOM   8108 C CG  . PRO D 1 230 ? 31.650  53.681 30.705  1.00 48.56  ?  385 PRO D CG  1 
ATOM   8109 C CD  . PRO D 1 230 ? 31.201  53.333 29.311  1.00 43.72  ?  385 PRO D CD  1 
ATOM   8110 N N   . ALA D 1 231 ? 33.743  57.315 29.472  1.00 42.82  ?  386 ALA D N   1 
ATOM   8111 C CA  . ALA D 1 231 ? 35.144  57.780 29.316  1.00 42.46  ?  386 ALA D CA  1 
ATOM   8112 C C   . ALA D 1 231 ? 36.136  56.955 30.108  1.00 45.84  ?  386 ALA D C   1 
ATOM   8113 O O   . ALA D 1 231 ? 37.258  56.757 29.663  1.00 44.33  ?  386 ALA D O   1 
ATOM   8114 C CB  . ALA D 1 231 ? 35.271  59.252 29.683  1.00 43.12  ?  386 ALA D CB  1 
ATOM   8115 N N   . VAL D 1 232 ? 35.707  56.484 31.281  1.00 45.22  ?  387 VAL D N   1 
ATOM   8116 C CA  . VAL D 1 232 ? 36.468  55.617 32.177  1.00 46.46  ?  387 VAL D CA  1 
ATOM   8117 C C   . VAL D 1 232 ? 35.569  54.492 32.686  1.00 52.45  ?  387 VAL D C   1 
ATOM   8118 O O   . VAL D 1 232 ? 34.398  54.711 32.973  1.00 53.38  ?  387 VAL D O   1 
ATOM   8119 C CB  . VAL D 1 232 ? 37.201  56.376 33.325  1.00 50.26  ?  387 VAL D CB  1 
ATOM   8120 C CG1 . VAL D 1 232 ? 36.215  57.019 34.306  1.00 50.13  ?  387 VAL D CG1 1 
ATOM   8121 C CG2 . VAL D 1 232 ? 38.179  55.466 34.055  1.00 49.77  ?  387 VAL D CG2 1 
ATOM   8122 N N   . ASP D 1 233 ? 36.115  53.291 32.736  1.00 50.46  ?  388 ASP D N   1 
ATOM   8123 C CA  . ASP D 1 233 ? 35.475  52.087 33.236  1.00 51.07  ?  388 ASP D CA  1 
ATOM   8124 C C   . ASP D 1 233 ? 36.602  51.226 33.814  1.00 56.52  ?  388 ASP D C   1 
ATOM   8125 O O   . ASP D 1 233 ? 37.443  50.714 33.067  1.00 53.56  ?  388 ASP D O   1 
ATOM   8126 C CB  . ASP D 1 233 ? 34.719  51.362 32.113  1.00 53.06  ?  388 ASP D CB  1 
ATOM   8127 C CG  . ASP D 1 233 ? 33.884  50.150 32.522  1.00 63.83  ?  388 ASP D CG  1 
ATOM   8128 O OD1 . ASP D 1 233 ? 33.734  49.903 33.757  1.00 61.62  ?  388 ASP D OD1 1 
ATOM   8129 O OD2 . ASP D 1 233 ? 33.341  49.471 31.612  1.00 73.31  -1 388 ASP D OD2 1 
ATOM   8130 N N   . GLU D 1 234 ? 36.639  51.132 35.165  1.00 56.02  ?  389 GLU D N   1 
ATOM   8131 C CA  . GLU D 1 234 ? 37.637  50.376 35.921  1.00 57.54  ?  389 GLU D CA  1 
ATOM   8132 C C   . GLU D 1 234 ? 37.680  48.900 35.527  1.00 62.44  ?  389 GLU D C   1 
ATOM   8133 O O   . GLU D 1 234 ? 38.747  48.289 35.553  1.00 61.33  ?  389 GLU D O   1 
ATOM   8134 C CB  . GLU D 1 234 ? 37.386  50.517 37.426  1.00 59.58  ?  389 GLU D CB  1 
ATOM   8135 N N   . HIS D 1 235 ? 36.523  48.343 35.146  1.00 60.99  ?  390 HIS D N   1 
ATOM   8136 C CA  . HIS D 1 235 ? 36.366  46.944 34.753  1.00 61.45  ?  390 HIS D CA  1 
ATOM   8137 C C   . HIS D 1 235 ? 36.424  46.728 33.228  1.00 63.75  ?  390 HIS D C   1 
ATOM   8138 O O   . HIS D 1 235 ? 35.819  45.787 32.712  1.00 64.41  ?  390 HIS D O   1 
ATOM   8139 C CB  . HIS D 1 235 ? 35.074  46.394 35.356  1.00 62.83  ?  390 HIS D CB  1 
ATOM   8140 C CG  . HIS D 1 235 ? 35.023  46.489 36.847  1.00 66.96  ?  390 HIS D CG  1 
ATOM   8141 N ND1 . HIS D 1 235 ? 36.089  46.083 37.635  1.00 69.23  ?  390 HIS D ND1 1 
ATOM   8142 C CD2 . HIS D 1 235 ? 34.019  46.906 37.652  1.00 69.54  ?  390 HIS D CD2 1 
ATOM   8143 C CE1 . HIS D 1 235 ? 35.712  46.284 38.888  1.00 68.97  ?  390 HIS D CE1 1 
ATOM   8144 N NE2 . HIS D 1 235 ? 34.475  46.777 38.951  1.00 69.54  ?  390 HIS D NE2 1 
ATOM   8145 N N   . ARG D 1 236 ? 37.184  47.570 32.519  1.00 57.16  ?  391 ARG D N   1 
ATOM   8146 C CA  . ARG D 1 236 ? 37.289  47.470 31.070  1.00 55.79  ?  391 ARG D CA  1 
ATOM   8147 C C   . ARG D 1 236 ? 38.742  47.577 30.604  1.00 60.74  ?  391 ARG D C   1 
ATOM   8148 O O   . ARG D 1 236 ? 39.555  48.275 31.225  1.00 60.12  ?  391 ARG D O   1 
ATOM   8149 C CB  . ARG D 1 236 ? 36.410  48.554 30.412  1.00 51.43  ?  391 ARG D CB  1 
ATOM   8150 C CG  . ARG D 1 236 ? 36.409  48.599 28.887  1.00 51.14  ?  391 ARG D CG  1 
ATOM   8151 C CD  . ARG D 1 236 ? 35.643  49.807 28.353  1.00 60.11  ?  391 ARG D CD  1 
ATOM   8152 N NE  . ARG D 1 236 ? 36.321  51.080 28.623  1.00 56.49  ?  391 ARG D NE  1 
ATOM   8153 C CZ  . ARG D 1 236 ? 35.699  52.245 28.798  1.00 63.29  ?  391 ARG D CZ  1 
ATOM   8154 N NH1 . ARG D 1 236 ? 34.375  52.313 28.742  1.00 38.44  ?  391 ARG D NH1 1 
ATOM   8155 N NH2 . ARG D 1 236 ? 36.397  53.346 29.046  1.00 59.73  1  391 ARG D NH2 1 
ATOM   8156 N N   . GLU D 1 237 ? 39.059  46.872 29.508  1.00 57.43  ?  392 GLU D N   1 
ATOM   8157 C CA  . GLU D 1 237 ? 40.356  46.929 28.858  1.00 57.43  ?  392 GLU D CA  1 
ATOM   8158 C C   . GLU D 1 237 ? 40.131  47.517 27.450  1.00 62.20  ?  392 GLU D C   1 
ATOM   8159 O O   . GLU D 1 237 ? 39.510  46.865 26.602  1.00 62.17  ?  392 GLU D O   1 
ATOM   8160 C CB  . GLU D 1 237 ? 41.020  45.551 28.802  1.00 58.90  ?  392 GLU D CB  1 
ATOM   8161 N N   . PRO D 1 238 ? 40.556  48.774 27.194  1.00 58.13  ?  393 PRO D N   1 
ATOM   8162 C CA  . PRO D 1 238 ? 41.263  49.679 28.101  1.00 57.38  ?  393 PRO D CA  1 
ATOM   8163 C C   . PRO D 1 238 ? 40.319  50.478 28.970  1.00 60.68  ?  393 PRO D C   1 
ATOM   8164 O O   . PRO D 1 238 ? 39.229  50.857 28.547  1.00 62.32  ?  393 PRO D O   1 
ATOM   8165 C CB  . PRO D 1 238 ? 42.068  50.561 27.148  1.00 59.09  ?  393 PRO D CB  1 
ATOM   8166 C CG  . PRO D 1 238 ? 41.278  50.599 25.874  1.00 63.59  ?  393 PRO D CG  1 
ATOM   8167 C CD  . PRO D 1 238 ? 40.358  49.393 25.868  1.00 59.73  ?  393 PRO D CD  1 
ATOM   8168 N N   . GLN D 1 239 ? 40.771  50.734 30.177  1.00 55.17  ?  394 GLN D N   1 
ATOM   8169 C CA  . GLN D 1 239 ? 40.131  51.476 31.249  1.00 54.72  ?  394 GLN D CA  1 
ATOM   8170 C C   . GLN D 1 239 ? 39.711  52.897 30.847  1.00 60.13  ?  394 GLN D C   1 
ATOM   8171 O O   . GLN D 1 239 ? 38.731  53.408 31.374  1.00 59.60  ?  394 GLN D O   1 
ATOM   8172 C CB  . GLN D 1 239 ? 41.137  51.541 32.397  1.00 55.62  ?  394 GLN D CB  1 
ATOM   8173 C CG  . GLN D 1 239 ? 40.533  51.411 33.760  1.00 66.65  ?  394 GLN D CG  1 
ATOM   8174 C CD  . GLN D 1 239 ? 41.532  50.866 34.724  1.00 76.66  ?  394 GLN D CD  1 
ATOM   8175 O OE1 . GLN D 1 239 ? 42.135  49.817 34.482  1.00 78.32  ?  394 GLN D OE1 1 
ATOM   8176 N NE2 . GLN D 1 239 ? 41.730  51.567 35.833  1.00 60.13  ?  394 GLN D NE2 1 
ATOM   8177 N N   . LEU D 1 240 ? 40.487  53.539 29.953  1.00 58.23  ?  395 LEU D N   1 
ATOM   8178 C CA  . LEU D 1 240 ? 40.280  54.899 29.448  1.00 58.38  ?  395 LEU D CA  1 
ATOM   8179 C C   . LEU D 1 240 ? 39.940  54.860 27.973  1.00 60.30  ?  395 LEU D C   1 
ATOM   8180 O O   . LEU D 1 240 ? 40.655  54.242 27.185  1.00 59.04  ?  395 LEU D O   1 
ATOM   8181 C CB  . LEU D 1 240 ? 41.537  55.787 29.690  1.00 58.94  ?  395 LEU D CB  1 
ATOM   8182 C CG  . LEU D 1 240 ? 41.600  56.694 30.969  1.00 64.33  ?  395 LEU D CG  1 
ATOM   8183 C CD1 . LEU D 1 240 ? 40.544  57.775 30.970  1.00 64.75  ?  395 LEU D CD1 1 
ATOM   8184 C CD2 . LEU D 1 240 ? 41.505  55.907 32.247  1.00 67.05  ?  395 LEU D CD2 1 
ATOM   8185 N N   . LEU D 1 241 ? 38.832  55.516 27.608  1.00 56.93  ?  396 LEU D N   1 
ATOM   8186 C CA  . LEU D 1 241 ? 38.315  55.597 26.245  1.00 56.82  ?  396 LEU D CA  1 
ATOM   8187 C C   . LEU D 1 241 ? 39.306  56.316 25.323  1.00 61.42  ?  396 LEU D C   1 
ATOM   8188 O O   . LEU D 1 241 ? 39.397  55.989 24.144  1.00 60.84  ?  396 LEU D O   1 
ATOM   8189 C CB  . LEU D 1 241 ? 36.936  56.290 26.274  1.00 56.82  ?  396 LEU D CB  1 
ATOM   8190 C CG  . LEU D 1 241 ? 36.084  56.264 25.004  1.00 60.70  ?  396 LEU D CG  1 
ATOM   8191 C CD1 . LEU D 1 241 ? 35.660  54.848 24.619  1.00 60.42  ?  396 LEU D CD1 1 
ATOM   8192 C CD2 . LEU D 1 241 ? 34.876  57.119 25.185  1.00 62.61  ?  396 LEU D CD2 1 
ATOM   8193 N N   . LEU D 1 242 ? 40.067  57.264 25.882  1.00 58.99  ?  397 LEU D N   1 
ATOM   8194 C CA  . LEU D 1 242 ? 41.131  57.993 25.200  1.00 59.51  ?  397 LEU D CA  1 
ATOM   8195 C C   . LEU D 1 242 ? 42.164  57.014 24.559  1.00 62.88  ?  397 LEU D C   1 
ATOM   8196 O O   . LEU D 1 242 ? 42.672  57.301 23.472  1.00 61.25  ?  397 LEU D O   1 
ATOM   8197 C CB  . LEU D 1 242 ? 41.828  58.918 26.234  1.00 59.51  ?  397 LEU D CB  1 
ATOM   8198 C CG  . LEU D 1 242 ? 41.700  60.419 26.074  1.00 63.76  ?  397 LEU D CG  1 
ATOM   8199 C CD1 . LEU D 1 242 ? 40.662  60.791 25.051  1.00 63.83  ?  397 LEU D CD1 1 
ATOM   8200 C CD2 . LEU D 1 242 ? 41.446  61.097 27.417  1.00 65.71  ?  397 LEU D CD2 1 
ATOM   8201 N N   . ASP D 1 243 ? 42.436  55.856 25.228  1.00 60.92  ?  398 ASP D N   1 
ATOM   8202 C CA  . ASP D 1 243 ? 43.367  54.822 24.755  1.00 62.26  ?  398 ASP D CA  1 
ATOM   8203 C C   . ASP D 1 243 ? 42.915  54.194 23.434  1.00 68.14  ?  398 ASP D C   1 
ATOM   8204 O O   . ASP D 1 243 ? 43.764  53.801 22.631  1.00 67.84  ?  398 ASP D O   1 
ATOM   8205 C CB  . ASP D 1 243 ? 43.629  53.735 25.818  1.00 64.68  ?  398 ASP D CB  1 
ATOM   8206 C CG  . ASP D 1 243 ? 44.280  54.210 27.114  1.00 84.15  ?  398 ASP D CG  1 
ATOM   8207 O OD1 . ASP D 1 243 ? 44.972  55.262 27.090  1.00 85.28  ?  398 ASP D OD1 1 
ATOM   8208 O OD2 . ASP D 1 243 ? 44.122  53.511 28.151  1.00 93.83  -1 398 ASP D OD2 1 
ATOM   8209 N N   . ILE D 1 244 ? 41.581  54.121 23.212  1.00 65.61  ?  399 ILE D N   1 
ATOM   8210 C CA  . ILE D 1 244 ? 40.944  53.603 21.993  1.00 65.40  ?  399 ILE D CA  1 
ATOM   8211 C C   . ILE D 1 244 ? 41.360  54.454 20.770  1.00 70.25  ?  399 ILE D C   1 
ATOM   8212 O O   . ILE D 1 244 ? 41.611  53.895 19.697  1.00 68.62  ?  399 ILE D O   1 
ATOM   8213 C CB  . ILE D 1 244 ? 39.404  53.436 22.210  1.00 68.14  ?  399 ILE D CB  1 
ATOM   8214 C CG1 . ILE D 1 244 ? 39.103  52.113 22.955  1.00 68.93  ?  399 ILE D CG1 1 
ATOM   8215 C CG2 . ILE D 1 244 ? 38.567  53.577 20.924  1.00 67.07  ?  399 ILE D CG2 1 
ATOM   8216 C CD1 . ILE D 1 244 ? 38.481  52.272 24.313  1.00 77.58  ?  399 ILE D CD1 1 
ATOM   8217 N N   . LYS D 1 245 ? 41.510  55.790 20.950  1.00 68.85  ?  400 LYS D N   1 
ATOM   8218 C CA  . LYS D 1 245 ? 41.972  56.709 19.900  1.00 68.88  ?  400 LYS D CA  1 
ATOM   8219 C C   . LYS D 1 245 ? 43.391  56.318 19.471  1.00 73.93  ?  400 LYS D C   1 
ATOM   8220 O O   . LYS D 1 245 ? 43.671  56.310 18.273  1.00 73.57  ?  400 LYS D O   1 
ATOM   8221 C CB  . LYS D 1 245 ? 41.950  58.173 20.390  1.00 70.84  ?  400 LYS D CB  1 
ATOM   8222 C CG  . LYS D 1 245 ? 42.399  59.191 19.332  1.00 74.25  ?  400 LYS D CG  1 
ATOM   8223 C CD  . LYS D 1 245 ? 43.128  60.378 19.931  1.00 71.86  ?  400 LYS D CD  1 
ATOM   8224 C CE  . LYS D 1 245 ? 43.713  61.262 18.867  1.00 74.51  ?  400 LYS D CE  1 
ATOM   8225 N NZ  . LYS D 1 245 ? 44.601  62.295 19.455  1.00 85.28  1  400 LYS D NZ  1 
ATOM   8226 N N   . GLU D 1 246 ? 44.274  55.983 20.458  1.00 70.99  ?  401 GLU D N   1 
ATOM   8227 C CA  . GLU D 1 246 ? 45.667  55.574 20.207  1.00 70.75  ?  401 GLU D CA  1 
ATOM   8228 C C   . GLU D 1 246 ? 45.702  54.313 19.341  1.00 73.73  ?  401 GLU D C   1 
ATOM   8229 O O   . GLU D 1 246 ? 46.397  54.306 18.325  1.00 72.51  ?  401 GLU D O   1 
ATOM   8230 C CB  . GLU D 1 246 ? 46.444  55.381 21.525  1.00 71.95  ?  401 GLU D CB  1 
ATOM   8231 N N   . GLU D 1 247 ? 44.877  53.292 19.702  1.00 69.97  ?  402 GLU D N   1 
ATOM   8232 C CA  . GLU D 1 247 ? 44.712  52.010 18.993  1.00 69.05  ?  402 GLU D CA  1 
ATOM   8233 C C   . GLU D 1 247 ? 44.308  52.214 17.525  1.00 72.09  ?  402 GLU D C   1 
ATOM   8234 O O   . GLU D 1 247 ? 44.836  51.533 16.641  1.00 70.02  ?  402 GLU D O   1 
ATOM   8235 C CB  . GLU D 1 247 ? 43.689  51.116 19.716  1.00 70.14  ?  402 GLU D CB  1 
ATOM   8236 C CG  . GLU D 1 247 ? 44.190  50.577 21.042  1.00 81.19  ?  402 GLU D CG  1 
ATOM   8237 C CD  . GLU D 1 247 ? 43.252  49.620 21.747  1.00 107.88 ?  402 GLU D CD  1 
ATOM   8238 O OE1 . GLU D 1 247 ? 42.881  48.584 21.149  1.00 114.57 ?  402 GLU D OE1 1 
ATOM   8239 O OE2 . GLU D 1 247 ? 42.927  49.889 22.925  1.00 96.63  -1 402 GLU D OE2 1 
ATOM   8240 N N   . ILE D 1 248 ? 43.392  53.173 17.276  1.00 69.89  ?  403 ILE D N   1 
ATOM   8241 C CA  . ILE D 1 248 ? 42.922  53.520 15.932  1.00 70.74  ?  403 ILE D CA  1 
ATOM   8242 C C   . ILE D 1 248 ? 44.035  54.234 15.167  1.00 79.52  ?  403 ILE D C   1 
ATOM   8243 O O   . ILE D 1 248 ? 44.337  53.832 14.039  1.00 79.97  ?  403 ILE D O   1 
ATOM   8244 C CB  . ILE D 1 248 ? 41.580  54.315 15.942  1.00 72.58  ?  403 ILE D CB  1 
ATOM   8245 C CG1 . ILE D 1 248 ? 40.434  53.482 16.601  1.00 72.37  ?  403 ILE D CG1 1 
ATOM   8246 C CG2 . ILE D 1 248 ? 41.202  54.797 14.527  1.00 70.52  ?  403 ILE D CG2 1 
ATOM   8247 C CD1 . ILE D 1 248 ? 39.243  54.278 17.156  1.00 74.26  ?  403 ILE D CD1 1 
ATOM   8248 N N   . GLU D 1 249 ? 44.657  55.269 15.795  1.00 79.06  ?  404 GLU D N   1 
ATOM   8249 C CA  . GLU D 1 249 ? 45.755  56.057 15.217  1.00 80.48  ?  404 GLU D CA  1 
ATOM   8250 C C   . GLU D 1 249 ? 46.946  55.161 14.847  1.00 86.86  ?  404 GLU D C   1 
ATOM   8251 O O   . GLU D 1 249 ? 47.526  55.328 13.772  1.00 86.65  ?  404 GLU D O   1 
ATOM   8252 C CB  . GLU D 1 249 ? 46.205  57.204 16.154  1.00 82.31  ?  404 GLU D CB  1 
ATOM   8253 C CG  . GLU D 1 249 ? 45.184  58.306 16.428  1.00 98.19  ?  404 GLU D CG  1 
ATOM   8254 C CD  . GLU D 1 249 ? 44.597  59.028 15.233  1.00 129.45 ?  404 GLU D CD  1 
ATOM   8255 O OE1 . GLU D 1 249 ? 45.376  59.648 14.472  1.00 137.69 ?  404 GLU D OE1 1 
ATOM   8256 O OE2 . GLU D 1 249 ? 43.353  59.008 15.081  1.00 120.10 -1 404 GLU D OE2 1 
ATOM   8257 N N   . ASP D 1 250 ? 47.263  54.171 15.709  1.00 84.99  ?  405 ASP D N   1 
ATOM   8258 C CA  . ASP D 1 250 ? 48.350  53.214 15.484  1.00 85.46  ?  405 ASP D CA  1 
ATOM   8259 C C   . ASP D 1 250 ? 47.885  52.014 14.632  1.00 89.83  ?  405 ASP D C   1 
ATOM   8260 O O   . ASP D 1 250 ? 48.418  50.912 14.785  1.00 89.51  ?  405 ASP D O   1 
ATOM   8261 C CB  . ASP D 1 250 ? 48.977  52.751 16.825  1.00 87.63  ?  405 ASP D CB  1 
ATOM   8262 C CG  . ASP D 1 250 ? 49.538  53.862 17.701  1.00 99.69  ?  405 ASP D CG  1 
ATOM   8263 O OD1 . ASP D 1 250 ? 50.147  54.813 17.147  1.00 100.77 ?  405 ASP D OD1 1 
ATOM   8264 O OD2 . ASP D 1 250 ? 49.378  53.776 18.944  1.00 105.08 -1 405 ASP D OD2 1 
ATOM   8265 N N   . GLU D 1 251 ? 46.877  52.237 13.749  1.00 86.44  ?  406 GLU D N   1 
ATOM   8266 C CA  . GLU D 1 251 ? 46.266  51.274 12.812  1.00 86.03  ?  406 GLU D CA  1 
ATOM   8267 C C   . GLU D 1 251 ? 45.937  49.848 13.350  1.00 88.19  ?  406 GLU D C   1 
ATOM   8268 O O   . GLU D 1 251 ? 45.557  48.969 12.569  1.00 87.47  ?  406 GLU D O   1 
ATOM   8269 C CB  . GLU D 1 251 ? 47.039  51.237 11.476  1.00 87.43  ?  406 GLU D CB  1 
ATOM   8270 N N   . GLU D 1 252 ? 46.044  49.640 14.679  1.00 83.46  ?  407 GLU D N   1 
ATOM   8271 C CA  . GLU D 1 252 ? 45.756  48.368 15.347  1.00 82.51  ?  407 GLU D CA  1 
ATOM   8272 C C   . GLU D 1 252 ? 44.244  48.020 15.334  1.00 85.59  ?  407 GLU D C   1 
ATOM   8273 O O   . GLU D 1 252 ? 43.890  46.844 15.469  1.00 85.68  ?  407 GLU D O   1 
ATOM   8274 C CB  . GLU D 1 252 ? 46.313  48.384 16.783  1.00 83.72  ?  407 GLU D CB  1 
ATOM   8275 N N   . LYS D 1 253 ? 43.365  49.049 15.179  1.00 79.98  ?  408 LYS D N   1 
ATOM   8276 C CA  . LYS D 1 253 ? 41.895  48.965 15.125  1.00 78.32  ?  408 LYS D CA  1 
ATOM   8277 C C   . LYS D 1 253 ? 41.337  50.121 14.250  1.00 79.24  ?  408 LYS D C   1 
ATOM   8278 O O   . LYS D 1 253 ? 42.091  51.020 13.873  1.00 79.26  ?  408 LYS D O   1 
ATOM   8279 C CB  . LYS D 1 253 ? 41.295  49.086 16.552  1.00 80.49  ?  408 LYS D CB  1 
ATOM   8280 C CG  . LYS D 1 253 ? 41.702  48.016 17.573  1.00 94.85  ?  408 LYS D CG  1 
ATOM   8281 C CD  . LYS D 1 253 ? 40.849  46.743 17.503  1.00 105.97 ?  408 LYS D CD  1 
ATOM   8282 C CE  . LYS D 1 253 ? 41.429  45.608 18.330  1.00 118.25 ?  408 LYS D CE  1 
ATOM   8283 N NZ  . LYS D 1 253 ? 41.302  45.836 19.798  1.00 127.39 1  408 LYS D NZ  1 
ATOM   8284 N N   . THR D 1 254 ? 40.018  50.098 13.938  1.00 73.19  ?  409 THR D N   1 
ATOM   8285 C CA  . THR D 1 254 ? 39.297  51.176 13.223  1.00 71.29  ?  409 THR D CA  1 
ATOM   8286 C C   . THR D 1 254 ? 38.132  51.668 14.081  1.00 69.61  ?  409 THR D C   1 
ATOM   8287 O O   . THR D 1 254 ? 37.751  51.004 15.065  1.00 68.29  ?  409 THR D O   1 
ATOM   8288 C CB  . THR D 1 254 ? 38.795  50.770 11.826  1.00 82.52  ?  409 THR D CB  1 
ATOM   8289 O OG1 . THR D 1 254 ? 38.087  49.532 11.892  1.00 85.77  ?  409 THR D OG1 1 
ATOM   8290 C CG2 . THR D 1 254 ? 39.907  50.719 10.791  1.00 81.91  ?  409 THR D CG2 1 
ATOM   8291 N N   . ILE D 1 255 ? 37.565  52.837 13.718  1.00 62.79  ?  410 ILE D N   1 
ATOM   8292 C CA  . ILE D 1 255 ? 36.405  53.373 14.445  1.00 60.96  ?  410 ILE D CA  1 
ATOM   8293 C C   . ILE D 1 255 ? 35.183  52.438 14.316  1.00 65.36  ?  410 ILE D C   1 
ATOM   8294 O O   . ILE D 1 255 ? 34.418  52.289 15.271  1.00 65.28  ?  410 ILE D O   1 
ATOM   8295 C CB  . ILE D 1 255 ? 36.113  54.872 14.153  1.00 62.08  ?  410 ILE D CB  1 
ATOM   8296 C CG1 . ILE D 1 255 ? 35.160  55.491 15.201  1.00 60.72  ?  410 ILE D CG1 1 
ATOM   8297 C CG2 . ILE D 1 255 ? 35.635  55.106 12.731  1.00 60.96  ?  410 ILE D CG2 1 
ATOM   8298 C CD1 . ILE D 1 255 ? 35.528  55.233 16.730  1.00 49.14  ?  410 ILE D CD1 1 
ATOM   8299 N N   . GLU D 1 256 ? 35.091  51.733 13.169  1.00 62.06  ?  411 GLU D N   1 
ATOM   8300 C CA  . GLU D 1 256 ? 34.059  50.755 12.835  1.00 61.75  ?  411 GLU D CA  1 
ATOM   8301 C C   . GLU D 1 256 ? 34.016  49.632 13.858  1.00 66.19  ?  411 GLU D C   1 
ATOM   8302 O O   . GLU D 1 256 ? 32.933  49.160 14.195  1.00 67.65  ?  411 GLU D O   1 
ATOM   8303 C CB  . GLU D 1 256 ? 34.267  50.203 11.418  1.00 62.98  ?  411 GLU D CB  1 
ATOM   8304 C CG  . GLU D 1 256 ? 33.781  51.135 10.314  1.00 76.14  ?  411 GLU D CG  1 
ATOM   8305 C CD  . GLU D 1 256 ? 34.589  52.397 10.047  1.00 107.53 ?  411 GLU D CD  1 
ATOM   8306 O OE1 . GLU D 1 256 ? 35.840  52.327 10.045  1.00 110.69 ?  411 GLU D OE1 1 
ATOM   8307 O OE2 . GLU D 1 256 ? 33.962  53.454 9.806   1.00 106.11 -1 411 GLU D OE2 1 
ATOM   8308 N N   . ASP D 1 257 ? 35.175  49.247 14.394  1.00 60.82  ?  412 ASP D N   1 
ATOM   8309 C CA  . ASP D 1 257 ? 35.266  48.208 15.407  1.00 60.54  ?  412 ASP D CA  1 
ATOM   8310 C C   . ASP D 1 257 ? 34.669  48.695 16.731  1.00 62.68  ?  412 ASP D C   1 
ATOM   8311 O O   . ASP D 1 257 ? 34.330  47.873 17.583  1.00 63.47  ?  412 ASP D O   1 
ATOM   8312 C CB  . ASP D 1 257 ? 36.742  47.785 15.608  1.00 63.46  ?  412 ASP D CB  1 
ATOM   8313 C CG  . ASP D 1 257 ? 37.443  47.266 14.355  1.00 77.98  ?  412 ASP D CG  1 
ATOM   8314 O OD1 . ASP D 1 257 ? 36.974  46.261 13.783  1.00 78.64  ?  412 ASP D OD1 1 
ATOM   8315 O OD2 . ASP D 1 257 ? 38.488  47.838 13.977  1.00 86.70  -1 412 ASP D OD2 1 
ATOM   8316 N N   . TYR D 1 258 ? 34.542  50.025 16.908  1.00 56.60  ?  413 TYR D N   1 
ATOM   8317 C CA  . TYR D 1 258 ? 34.038  50.617 18.146  1.00 54.57  ?  413 TYR D CA  1 
ATOM   8318 C C   . TYR D 1 258 ? 32.637  51.245 18.110  1.00 51.67  ?  413 TYR D C   1 
ATOM   8319 O O   . TYR D 1 258 ? 32.113  51.564 19.186  1.00 49.10  ?  413 TYR D O   1 
ATOM   8320 C CB  . TYR D 1 258 ? 35.085  51.551 18.777  1.00 56.42  ?  413 TYR D CB  1 
ATOM   8321 C CG  . TYR D 1 258 ? 36.243  50.801 19.396  1.00 60.41  ?  413 TYR D CG  1 
ATOM   8322 C CD1 . TYR D 1 258 ? 36.117  50.184 20.638  1.00 62.91  ?  413 TYR D CD1 1 
ATOM   8323 C CD2 . TYR D 1 258 ? 37.468  50.696 18.734  1.00 61.59  ?  413 TYR D CD2 1 
ATOM   8324 C CE1 . TYR D 1 258 ? 37.180  49.479 21.206  1.00 64.75  ?  413 TYR D CE1 1 
ATOM   8325 C CE2 . TYR D 1 258 ? 38.534  49.988 19.289  1.00 62.30  ?  413 TYR D CE2 1 
ATOM   8326 C CZ  . TYR D 1 258 ? 38.386  49.383 20.526  1.00 72.04  ?  413 TYR D CZ  1 
ATOM   8327 O OH  . TYR D 1 258 ? 39.439  48.687 21.078  1.00 77.21  ?  413 TYR D OH  1 
ATOM   8328 N N   . ILE D 1 259 ? 32.025  51.397 16.897  1.00 45.22  ?  414 ILE D N   1 
ATOM   8329 C CA  . ILE D 1 259 ? 30.663  51.940 16.735  1.00 44.41  ?  414 ILE D CA  1 
ATOM   8330 C C   . ILE D 1 259 ? 29.686  51.176 17.657  1.00 50.17  ?  414 ILE D C   1 
ATOM   8331 O O   . ILE D 1 259 ? 29.670  49.942 17.659  1.00 51.47  ?  414 ILE D O   1 
ATOM   8332 C CB  . ILE D 1 259 ? 30.149  51.951 15.269  1.00 46.34  ?  414 ILE D CB  1 
ATOM   8333 C CG1 . ILE D 1 259 ? 31.114  52.676 14.315  1.00 46.87  ?  414 ILE D CG1 1 
ATOM   8334 C CG2 . ILE D 1 259 ? 28.778  52.594 15.194  1.00 45.39  ?  414 ILE D CG2 1 
ATOM   8335 C CD1 . ILE D 1 259 ? 30.762  52.541 12.719  1.00 42.80  ?  414 ILE D CD1 1 
ATOM   8336 N N   . ASP D 1 260 ? 28.924  51.920 18.476  1.00 45.27  ?  415 ASP D N   1 
ATOM   8337 C CA  . ASP D 1 260 ? 27.951  51.385 19.417  1.00 44.35  ?  415 ASP D CA  1 
ATOM   8338 C C   . ASP D 1 260 ? 27.028  50.411 18.706  1.00 48.40  ?  415 ASP D C   1 
ATOM   8339 O O   . ASP D 1 260 ? 26.348  50.805 17.759  1.00 49.93  ?  415 ASP D O   1 
ATOM   8340 C CB  . ASP D 1 260 ? 27.141  52.548 20.027  1.00 45.24  ?  415 ASP D CB  1 
ATOM   8341 C CG  . ASP D 1 260 ? 26.281  52.207 21.218  1.00 52.33  ?  415 ASP D CG  1 
ATOM   8342 O OD1 . ASP D 1 260 ? 26.162  51.004 21.553  1.00 55.30  ?  415 ASP D OD1 1 
ATOM   8343 O OD2 . ASP D 1 260 ? 25.717  53.122 21.804  1.00 53.68  -1 415 ASP D OD2 1 
ATOM   8344 N N   . LYS D 1 261 ? 27.032  49.138 19.127  1.00 42.86  ?  416 LYS D N   1 
ATOM   8345 C CA  . LYS D 1 261 ? 26.173  48.109 18.536  1.00 41.88  ?  416 LYS D CA  1 
ATOM   8346 C C   . LYS D 1 261 ? 24.662  48.280 18.864  1.00 43.92  ?  416 LYS D C   1 
ATOM   8347 O O   . LYS D 1 261 ? 23.800  47.719 18.153  1.00 43.72  ?  416 LYS D O   1 
ATOM   8348 C CB  . LYS D 1 261 ? 26.708  46.699 18.821  1.00 44.15  ?  416 LYS D CB  1 
ATOM   8349 C CG  . LYS D 1 261 ? 27.872  46.324 17.879  1.00 53.52  ?  416 LYS D CG  1 
ATOM   8350 C CD  . LYS D 1 261 ? 28.420  44.943 18.171  1.00 63.46  ?  416 LYS D CD  1 
ATOM   8351 C CE  . LYS D 1 261 ? 29.923  44.917 18.371  1.00 79.63  ?  416 LYS D CE  1 
ATOM   8352 N NZ  . LYS D 1 261 ? 30.649  45.136 17.096  1.00 95.27  1  416 LYS D NZ  1 
ATOM   8353 N N   . LYS D 1 262 ? 24.345  49.142 19.867  1.00 36.97  ?  417 LYS D N   1 
ATOM   8354 C CA  . LYS D 1 262 ? 22.967  49.436 20.279  1.00 35.81  ?  417 LYS D CA  1 
ATOM   8355 C C   . LYS D 1 262 ? 22.238  50.418 19.324  1.00 38.87  ?  417 LYS D C   1 
ATOM   8356 O O   . LYS D 1 262 ? 21.223  50.994 19.692  1.00 36.34  ?  417 LYS D O   1 
ATOM   8357 C CB  . LYS D 1 262 ? 22.896  49.927 21.744  1.00 37.55  ?  417 LYS D CB  1 
ATOM   8358 C CG  . LYS D 1 262 ? 23.518  48.967 22.749  1.00 45.50  ?  417 LYS D CG  1 
ATOM   8359 C CD  . LYS D 1 262 ? 23.331  49.366 24.225  1.00 50.43  ?  417 LYS D CD  1 
ATOM   8360 C CE  . LYS D 1 262 ? 24.112  50.598 24.653  1.00 67.96  ?  417 LYS D CE  1 
ATOM   8361 N NZ  . LYS D 1 262 ? 25.599  50.489 24.471  1.00 69.94  1  417 LYS D NZ  1 
ATOM   8362 N N   . MET D 1 263 ? 22.744  50.623 18.107  1.00 36.69  ?  418 MET D N   1 
ATOM   8363 C CA  . MET D 1 263 ? 22.083  51.510 17.138  1.00 36.63  ?  418 MET D CA  1 
ATOM   8364 C C   . MET D 1 263 ? 22.081  50.888 15.753  1.00 44.84  ?  418 MET D C   1 
ATOM   8365 O O   . MET D 1 263 ? 23.030  50.189 15.410  1.00 46.63  ?  418 MET D O   1 
ATOM   8366 C CB  . MET D 1 263 ? 22.563  52.972 17.200  1.00 37.92  ?  418 MET D CB  1 
ATOM   8367 C CG  . MET D 1 263 ? 24.015  53.146 17.053  1.00 41.03  ?  418 MET D CG  1 
ATOM   8368 S SD  . MET D 1 263 ? 24.534  54.867 17.229  1.00 45.32  ?  418 MET D SD  1 
ATOM   8369 C CE  . MET D 1 263 ? 26.162  54.715 16.725  1.00 41.68  ?  418 MET D CE  1 
ATOM   8370 N N   . ASN D 1 264 ? 20.991  51.072 14.990  1.00 42.53  ?  419 ASN D N   1 
ATOM   8371 C CA  . ASN D 1 264 ? 20.801  50.419 13.690  1.00 43.21  ?  419 ASN D CA  1 
ATOM   8372 C C   . ASN D 1 264 ? 20.984  51.318 12.455  1.00 46.40  ?  419 ASN D C   1 
ATOM   8373 O O   . ASN D 1 264 ? 21.043  50.812 11.311  1.00 45.69  ?  419 ASN D O   1 
ATOM   8374 C CB  . ASN D 1 264 ? 19.406  49.769 13.668  1.00 47.17  ?  419 ASN D CB  1 
ATOM   8375 C CG  . ASN D 1 264 ? 18.262  50.763 13.755  1.00 59.05  ?  419 ASN D CG  1 
ATOM   8376 O OD1 . ASN D 1 264 ? 18.005  51.537 12.824  1.00 57.32  ?  419 ASN D OD1 1 
ATOM   8377 N ND2 . ASN D 1 264 ? 17.568  50.780 14.878  1.00 44.19  ?  419 ASN D ND2 1 
ATOM   8378 N N   . ASP D 1 265 ? 21.039  52.647 12.706  1.00 42.32  ?  420 ASP D N   1 
ATOM   8379 C CA  . ASP D 1 265 ? 21.050  53.724 11.715  1.00 41.87  ?  420 ASP D CA  1 
ATOM   8380 C C   . ASP D 1 265 ? 22.371  54.451 11.505  1.00 48.62  ?  420 ASP D C   1 
ATOM   8381 O O   . ASP D 1 265 ? 22.382  55.493 10.849  1.00 48.51  ?  420 ASP D O   1 
ATOM   8382 C CB  . ASP D 1 265 ? 19.937  54.724 12.076  1.00 42.75  ?  420 ASP D CB  1 
ATOM   8383 C CG  . ASP D 1 265 ? 20.186  55.518 13.354  1.00 42.35  ?  420 ASP D CG  1 
ATOM   8384 O OD1 . ASP D 1 265 ? 20.626  54.908 14.366  1.00 34.43  ?  420 ASP D OD1 1 
ATOM   8385 O OD2 . ASP D 1 265 ? 19.933  56.747 13.344  1.00 53.13  -1 420 ASP D OD2 1 
ATOM   8386 N N   . ALA D 1 266 ? 23.473  53.915 12.031  1.00 47.68  ?  421 ALA D N   1 
ATOM   8387 C CA  . ALA D 1 266 ? 24.779  54.541 11.867  1.00 48.85  ?  421 ALA D CA  1 
ATOM   8388 C C   . ALA D 1 266 ? 25.433  54.114 10.563  1.00 55.23  ?  421 ALA D C   1 
ATOM   8389 O O   . ALA D 1 266 ? 25.437  52.922 10.235  1.00 55.80  ?  421 ALA D O   1 
ATOM   8390 C CB  . ALA D 1 266 ? 25.682  54.191 13.042  1.00 49.76  ?  421 ALA D CB  1 
ATOM   8391 N N   . ASP D 1 267 ? 25.993  55.094 9.829   1.00 52.15  ?  422 ASP D N   1 
ATOM   8392 C CA  . ASP D 1 267 ? 26.730  54.893 8.580   1.00 51.36  ?  422 ASP D CA  1 
ATOM   8393 C C   . ASP D 1 267 ? 28.194  55.282 8.762   1.00 54.89  ?  422 ASP D C   1 
ATOM   8394 O O   . ASP D 1 267 ? 28.491  56.199 9.520   1.00 55.96  ?  422 ASP D O   1 
ATOM   8395 C CB  . ASP D 1 267 ? 26.093  55.635 7.387   1.00 52.57  ?  422 ASP D CB  1 
ATOM   8396 C CG  . ASP D 1 267 ? 25.930  57.132 7.547   1.00 61.00  ?  422 ASP D CG  1 
ATOM   8397 O OD1 . ASP D 1 267 ? 26.383  57.882 6.647   1.00 61.75  ?  422 ASP D OD1 1 
ATOM   8398 O OD2 . ASP D 1 267 ? 25.287  57.555 8.532   1.00 67.15  -1 422 ASP D OD2 1 
ATOM   8399 N N   . SER D 1 268 ? 29.097  54.603 8.057   1.00 49.62  ?  423 SER D N   1 
ATOM   8400 C CA  . SER D 1 268 ? 30.534  54.827 8.132   1.00 48.62  ?  423 SER D CA  1 
ATOM   8401 C C   . SER D 1 268 ? 30.921  56.265 7.810   1.00 50.93  ?  423 SER D C   1 
ATOM   8402 O O   . SER D 1 268 ? 31.766  56.834 8.504   1.00 49.79  ?  423 SER D O   1 
ATOM   8403 C CB  . SER D 1 268 ? 31.260  53.894 7.174   1.00 51.70  ?  423 SER D CB  1 
ATOM   8404 O OG  . SER D 1 268 ? 30.629  52.630 7.120   1.00 63.18  ?  423 SER D OG  1 
ATOM   8405 N N   . THR D 1 269 ? 30.317  56.843 6.750   1.00 45.88  ?  424 THR D N   1 
ATOM   8406 C CA  . THR D 1 269 ? 30.661  58.182 6.316   1.00 44.89  ?  424 THR D CA  1 
ATOM   8407 C C   . THR D 1 269 ? 30.473  59.170 7.432   1.00 50.41  ?  424 THR D C   1 
ATOM   8408 O O   . THR D 1 269 ? 31.441  59.827 7.828   1.00 52.11  ?  424 THR D O   1 
ATOM   8409 C CB  . THR D 1 269 ? 29.995  58.528 4.992   1.00 49.23  ?  424 THR D CB  1 
ATOM   8410 O OG1 . THR D 1 269 ? 30.326  57.514 4.039   1.00 55.40  ?  424 THR D OG1 1 
ATOM   8411 C CG2 . THR D 1 269 ? 30.437  59.877 4.449   1.00 44.14  ?  424 THR D CG2 1 
ATOM   8412 N N   . SER D 1 270 ? 29.261  59.217 7.999   1.00 46.13  ?  425 SER D N   1 
ATOM   8413 C CA  . SER D 1 270 ? 28.952  60.135 9.100   1.00 44.72  ?  425 SER D CA  1 
ATOM   8414 C C   . SER D 1 270 ? 29.738  59.778 10.348  1.00 42.28  ?  425 SER D C   1 
ATOM   8415 O O   . SER D 1 270 ? 30.175  60.673 11.050  1.00 38.97  ?  425 SER D O   1 
ATOM   8416 C CB  . SER D 1 270 ? 27.450  60.163 9.385   1.00 48.24  ?  425 SER D CB  1 
ATOM   8417 O OG  . SER D 1 270 ? 26.995  58.866 9.732   1.00 57.48  ?  425 SER D OG  1 
ATOM   8418 N N   . VAL D 1 271 ? 29.928  58.478 10.615  1.00 38.80  ?  426 VAL D N   1 
ATOM   8419 C CA  . VAL D 1 271 ? 30.653  58.062 11.813  1.00 40.50  ?  426 VAL D CA  1 
ATOM   8420 C C   . VAL D 1 271 ? 32.114  58.509 11.758  1.00 51.06  ?  426 VAL D C   1 
ATOM   8421 O O   . VAL D 1 271 ? 32.618  59.112 12.729  1.00 51.55  ?  426 VAL D O   1 
ATOM   8422 C CB  . VAL D 1 271 ? 30.463  56.576 12.202  1.00 42.79  ?  426 VAL D CB  1 
ATOM   8423 C CG1 . VAL D 1 271 ? 31.445  56.171 13.300  1.00 41.99  ?  426 VAL D CG1 1 
ATOM   8424 C CG2 . VAL D 1 271 ? 29.023  56.314 12.645  1.00 42.05  ?  426 VAL D CG2 1 
ATOM   8425 N N   . GLU D 1 272 ? 32.752  58.288 10.581  1.00 48.61  ?  427 GLU D N   1 
ATOM   8426 C CA  . GLU D 1 272 ? 34.127  58.689 10.344  1.00 47.78  ?  427 GLU D CA  1 
ATOM   8427 C C   . GLU D 1 272 ? 34.257  60.206 10.384  1.00 50.29  ?  427 GLU D C   1 
ATOM   8428 O O   . GLU D 1 272 ? 35.276  60.703 10.859  1.00 49.41  ?  427 GLU D O   1 
ATOM   8429 C CB  . GLU D 1 272 ? 34.648  58.134 9.026   1.00 49.18  ?  427 GLU D CB  1 
ATOM   8430 C CG  . GLU D 1 272 ? 35.175  56.713 9.140   1.00 61.26  ?  427 GLU D CG  1 
ATOM   8431 C CD  . GLU D 1 272 ? 35.478  56.021 7.821   1.00 90.27  ?  427 GLU D CD  1 
ATOM   8432 O OE1 . GLU D 1 272 ? 35.526  56.713 6.776   1.00 74.53  ?  427 GLU D OE1 1 
ATOM   8433 O OE2 . GLU D 1 272 ? 35.645  54.778 7.831   1.00 90.07  -1 427 GLU D OE2 1 
ATOM   8434 N N   . ALA D 1 273 ? 33.228  60.935 9.913   1.00 46.35  ?  428 ALA D N   1 
ATOM   8435 C CA  . ALA D 1 273 ? 33.234  62.402 9.915   1.00 46.34  ?  428 ALA D CA  1 
ATOM   8436 C C   . ALA D 1 273 ? 33.242  62.954 11.349  1.00 54.53  ?  428 ALA D C   1 
ATOM   8437 O O   . ALA D 1 273 ? 33.954  63.930 11.620  1.00 55.38  ?  428 ALA D O   1 
ATOM   8438 C CB  . ALA D 1 273 ? 32.056  62.942 9.131   1.00 46.28  ?  428 ALA D CB  1 
ATOM   8439 N N   . MET D 1 274 ? 32.494  62.285 12.271  1.00 51.06  ?  429 MET D N   1 
ATOM   8440 C CA  . MET D 1 274 ? 32.431  62.635 13.683  1.00 49.84  ?  429 MET D CA  1 
ATOM   8441 C C   . MET D 1 274 ? 33.734  62.217 14.375  1.00 54.20  ?  429 MET D C   1 
ATOM   8442 O O   . MET D 1 274 ? 34.232  62.970 15.215  1.00 54.22  ?  429 MET D O   1 
ATOM   8443 C CB  . MET D 1 274 ? 31.207  62.013 14.376  1.00 51.28  ?  429 MET D CB  1 
ATOM   8444 C CG  . MET D 1 274 ? 30.847  62.752 15.648  1.00 53.87  ?  429 MET D CG  1 
ATOM   8445 S SD  . MET D 1 274 ? 29.317  62.260 16.467  1.00 57.18  ?  429 MET D SD  1 
ATOM   8446 C CE  . MET D 1 274 ? 29.972  61.537 17.820  1.00 53.69  ?  429 MET D CE  1 
ATOM   8447 N N   . TYR D 1 275 ? 34.295  61.039 14.016  1.00 50.45  ?  430 TYR D N   1 
ATOM   8448 C CA  . TYR D 1 275 ? 35.564  60.593 14.597  1.00 50.32  ?  430 TYR D CA  1 
ATOM   8449 C C   . TYR D 1 275 ? 36.688  61.574 14.262  1.00 54.32  ?  430 TYR D C   1 
ATOM   8450 O O   . TYR D 1 275 ? 37.507  61.878 15.132  1.00 54.03  ?  430 TYR D O   1 
ATOM   8451 C CB  . TYR D 1 275 ? 35.937  59.171 14.169  1.00 51.70  ?  430 TYR D CB  1 
ATOM   8452 C CG  . TYR D 1 275 ? 37.231  58.721 14.801  1.00 53.98  ?  430 TYR D CG  1 
ATOM   8453 C CD1 . TYR D 1 275 ? 37.272  58.304 16.127  1.00 56.40  ?  430 TYR D CD1 1 
ATOM   8454 C CD2 . TYR D 1 275 ? 38.434  58.817 14.111  1.00 55.01  ?  430 TYR D CD2 1 
ATOM   8455 C CE1 . TYR D 1 275 ? 38.471  57.921 16.728  1.00 57.41  ?  430 TYR D CE1 1 
ATOM   8456 C CE2 . TYR D 1 275 ? 39.644  58.490 14.718  1.00 55.83  ?  430 TYR D CE2 1 
ATOM   8457 C CZ  . TYR D 1 275 ? 39.656  58.027 16.021  1.00 63.01  ?  430 TYR D CZ  1 
ATOM   8458 O OH  . TYR D 1 275 ? 40.847  57.694 16.613  1.00 66.42  ?  430 TYR D OH  1 
ATOM   8459 N N   . SER D 1 276 ? 36.704  62.084 13.012  1.00 50.63  ?  431 SER D N   1 
ATOM   8460 C CA  . SER D 1 276 ? 37.651  63.079 12.526  1.00 49.83  ?  431 SER D CA  1 
ATOM   8461 C C   . SER D 1 276 ? 37.605  64.341 13.415  1.00 51.94  ?  431 SER D C   1 
ATOM   8462 O O   . SER D 1 276 ? 38.662  64.823 13.820  1.00 53.30  ?  431 SER D O   1 
ATOM   8463 C CB  . SER D 1 276 ? 37.349  63.427 11.072  1.00 54.01  ?  431 SER D CB  1 
ATOM   8464 O OG  . SER D 1 276 ? 38.091  64.549 10.622  1.00 61.73  ?  431 SER D OG  1 
ATOM   8465 N N   . VAL D 1 277 ? 36.406  64.842 13.748  1.00 44.78  ?  432 VAL D N   1 
ATOM   8466 C CA  . VAL D 1 277 ? 36.240  66.007 14.610  1.00 44.27  ?  432 VAL D CA  1 
ATOM   8467 C C   . VAL D 1 277 ? 36.812  65.682 16.005  1.00 52.22  ?  432 VAL D C   1 
ATOM   8468 O O   . VAL D 1 277 ? 37.586  66.477 16.542  1.00 52.49  ?  432 VAL D O   1 
ATOM   8469 C CB  . VAL D 1 277 ? 34.767  66.487 14.705  1.00 46.15  ?  432 VAL D CB  1 
ATOM   8470 C CG1 . VAL D 1 277 ? 34.651  67.756 15.538  1.00 45.25  ?  432 VAL D CG1 1 
ATOM   8471 C CG2 . VAL D 1 277 ? 34.167  66.701 13.331  1.00 45.61  ?  432 VAL D CG2 1 
ATOM   8472 N N   . ALA D 1 278 ? 36.453  64.499 16.559  1.00 49.82  ?  433 ALA D N   1 
ATOM   8473 C CA  . ALA D 1 278 ? 36.897  64.034 17.869  1.00 50.49  ?  433 ALA D CA  1 
ATOM   8474 C C   . ALA D 1 278 ? 38.430  63.936 17.934  1.00 56.92  ?  433 ALA D C   1 
ATOM   8475 O O   . ALA D 1 278 ? 39.022  64.403 18.912  1.00 57.17  ?  433 ALA D O   1 
ATOM   8476 C CB  . ALA D 1 278 ? 36.264  62.685 18.196  1.00 51.12  ?  433 ALA D CB  1 
ATOM   8477 N N   . SER D 1 279 ? 39.078  63.374 16.885  1.00 52.66  ?  434 SER D N   1 
ATOM   8478 C CA  . SER D 1 279 ? 40.534  63.252 16.877  1.00 51.78  ?  434 SER D CA  1 
ATOM   8479 C C   . SER D 1 279 ? 41.225  64.603 16.744  1.00 54.10  ?  434 SER D C   1 
ATOM   8480 O O   . SER D 1 279 ? 42.283  64.793 17.334  1.00 54.73  ?  434 SER D O   1 
ATOM   8481 C CB  . SER D 1 279 ? 41.017  62.248 15.841  1.00 55.56  ?  434 SER D CB  1 
ATOM   8482 O OG  . SER D 1 279 ? 40.760  62.712 14.530  1.00 71.97  ?  434 SER D OG  1 
ATOM   8483 N N   . GLN D 1 280 ? 40.594  65.563 16.047  1.00 48.70  ?  435 GLN D N   1 
ATOM   8484 C CA  . GLN D 1 280 ? 41.114  66.921 15.939  1.00 47.74  ?  435 GLN D CA  1 
ATOM   8485 C C   . GLN D 1 280 ? 41.026  67.577 17.319  1.00 53.11  ?  435 GLN D C   1 
ATOM   8486 O O   . GLN D 1 280 ? 41.969  68.244 17.733  1.00 54.42  ?  435 GLN D O   1 
ATOM   8487 C CB  . GLN D 1 280 ? 40.337  67.732 14.901  1.00 48.49  ?  435 GLN D CB  1 
ATOM   8488 C CG  . GLN D 1 280 ? 40.806  67.471 13.479  1.00 64.93  ?  435 GLN D CG  1 
ATOM   8489 C CD  . GLN D 1 280 ? 39.851  68.021 12.456  1.00 87.86  ?  435 GLN D CD  1 
ATOM   8490 O OE1 . GLN D 1 280 ? 38.934  67.330 11.990  1.00 89.90  ?  435 GLN D OE1 1 
ATOM   8491 N NE2 . GLN D 1 280 ? 40.045  69.276 12.077  1.00 69.04  ?  435 GLN D NE2 1 
ATOM   8492 N N   . CYS D 1 281 ? 39.915  67.335 18.050  1.00 48.28  ?  436 CYS D N   1 
ATOM   8493 C CA  . CYS D 1 281 ? 39.663  67.858 19.391  1.00 46.98  ?  436 CYS D CA  1 
ATOM   8494 C C   . CYS D 1 281 ? 40.638  67.285 20.382  1.00 53.50  ?  436 CYS D C   1 
ATOM   8495 O O   . CYS D 1 281 ? 40.977  67.965 21.345  1.00 52.28  ?  436 CYS D O   1 
ATOM   8496 C CB  . CYS D 1 281 ? 38.238  67.541 19.831  1.00 46.13  ?  436 CYS D CB  1 
ATOM   8497 S SG  . CYS D 1 281 ? 36.960  68.500 19.006  1.00 49.17  ?  436 CYS D SG  1 
ATOM   8498 N N   . LEU D 1 282 ? 40.996  66.000 20.220  1.00 53.47  ?  437 LEU D N   1 
ATOM   8499 C CA  . LEU D 1 282 ? 41.812  65.226 21.161  1.00 54.65  ?  437 LEU D CA  1 
ATOM   8500 C C   . LEU D 1 282 ? 43.343  65.334 21.067  1.00 63.57  ?  437 LEU D C   1 
ATOM   8501 O O   . LEU D 1 282 ? 44.065  64.503 21.651  1.00 63.50  ?  437 LEU D O   1 
ATOM   8502 C CB  . LEU D 1 282 ? 41.343  63.764 21.189  1.00 54.48  ?  437 LEU D CB  1 
ATOM   8503 C CG  . LEU D 1 282 ? 39.945  63.523 21.724  1.00 58.97  ?  437 LEU D CG  1 
ATOM   8504 C CD1 . LEU D 1 282 ? 39.519  62.087 21.502  1.00 58.38  ?  437 LEU D CD1 1 
ATOM   8505 C CD2 . LEU D 1 282 ? 39.825  63.942 23.187  1.00 61.19  ?  437 LEU D CD2 1 
ATOM   8506 N N   . HIS D 1 283 ? 43.840  66.368 20.351  1.00 62.75  ?  438 HIS D N   1 
ATOM   8507 C CA  . HIS D 1 283 ? 45.266  66.651 20.254  1.00 62.98  ?  438 HIS D CA  1 
ATOM   8508 C C   . HIS D 1 283 ? 45.762  67.020 21.641  1.00 69.07  ?  438 HIS D C   1 
ATOM   8509 O O   . HIS D 1 283 ? 45.067  67.724 22.401  1.00 68.58  ?  438 HIS D O   1 
ATOM   8510 C CB  . HIS D 1 283 ? 45.524  67.844 19.338  1.00 63.71  ?  438 HIS D CB  1 
ATOM   8511 C CG  . HIS D 1 283 ? 45.478  67.529 17.883  1.00 67.26  ?  438 HIS D CG  1 
ATOM   8512 N ND1 . HIS D 1 283 ? 46.053  66.376 17.373  1.00 68.97  ?  438 HIS D ND1 1 
ATOM   8513 C CD2 . HIS D 1 283 ? 45.005  68.278 16.857  1.00 69.13  ?  438 HIS D CD2 1 
ATOM   8514 C CE1 . HIS D 1 283 ? 45.856  66.433 16.065  1.00 68.63  ?  438 HIS D CE1 1 
ATOM   8515 N NE2 . HIS D 1 283 ? 45.234  67.565 15.708  1.00 68.96  ?  438 HIS D NE2 1 
ATOM   8516 N N   . GLU D 1 284 ? 46.961  66.522 21.971  1.00 66.43  ?  439 GLU D N   1 
ATOM   8517 C CA  . GLU D 1 284 ? 47.654  66.788 23.226  1.00 65.74  ?  439 GLU D CA  1 
ATOM   8518 C C   . GLU D 1 284 ? 48.141  68.242 23.233  1.00 67.78  ?  439 GLU D C   1 
ATOM   8519 O O   . GLU D 1 284 ? 48.235  68.851 24.304  1.00 66.83  ?  439 GLU D O   1 
ATOM   8520 C CB  . GLU D 1 284 ? 48.831  65.824 23.359  1.00 67.45  ?  439 GLU D CB  1 
ATOM   8521 C CG  . GLU D 1 284 ? 48.601  64.689 24.334  1.00 80.77  ?  439 GLU D CG  1 
ATOM   8522 C CD  . GLU D 1 284 ? 47.320  63.887 24.236  1.00 104.16 ?  439 GLU D CD  1 
ATOM   8523 O OE1 . GLU D 1 284 ? 46.992  63.419 23.122  1.00 118.14 ?  439 GLU D OE1 1 
ATOM   8524 O OE2 . GLU D 1 284 ? 46.672  63.684 25.288  1.00 91.50  -1 439 GLU D OE2 1 
ATOM   8525 N N   . LYS D 1 285 ? 48.404  68.806 22.026  1.00 63.81  ?  440 LYS D N   1 
ATOM   8526 C CA  . LYS D 1 285 ? 48.839  70.182 21.844  1.00 63.80  ?  440 LYS D CA  1 
ATOM   8527 C C   . LYS D 1 285 ? 47.650  71.161 21.676  1.00 66.45  ?  440 LYS D C   1 
ATOM   8528 O O   . LYS D 1 285 ? 47.039  71.211 20.611  1.00 64.80  ?  440 LYS D O   1 
ATOM   8529 C CB  . LYS D 1 285 ? 49.838  70.280 20.680  1.00 66.89  ?  440 LYS D CB  1 
ATOM   8530 N N   . LYS D 1 286 ? 47.354  71.955 22.731  1.00 63.48  ?  441 LYS D N   1 
ATOM   8531 C CA  . LYS D 1 286 ? 46.276  72.951 22.808  1.00 63.62  ?  441 LYS D CA  1 
ATOM   8532 C C   . LYS D 1 286 ? 46.048  73.730 21.524  1.00 69.89  ?  441 LYS D C   1 
ATOM   8533 O O   . LYS D 1 286 ? 44.908  73.833 21.055  1.00 70.03  ?  441 LYS D O   1 
ATOM   8534 C CB  . LYS D 1 286 ? 46.497  73.927 23.987  1.00 65.30  ?  441 LYS D CB  1 
ATOM   8535 N N   . ASN D 1 287 ? 47.125  74.268 20.946  1.00 68.10  ?  442 ASN D N   1 
ATOM   8536 C CA  . ASN D 1 287 ? 47.029  75.103 19.749  1.00 68.63  ?  442 ASN D CA  1 
ATOM   8537 C C   . ASN D 1 287 ? 46.798  74.340 18.445  1.00 71.44  ?  442 ASN D C   1 
ATOM   8538 O O   . ASN D 1 287 ? 46.424  74.967 17.447  1.00 71.48  ?  442 ASN D O   1 
ATOM   8539 C CB  . ASN D 1 287 ? 48.180  76.118 19.683  1.00 73.29  ?  442 ASN D CB  1 
ATOM   8540 C CG  . ASN D 1 287 ? 48.190  77.134 20.828  1.00 101.78 ?  442 ASN D CG  1 
ATOM   8541 O OD1 . ASN D 1 287 ? 47.981  76.809 22.013  1.00 93.31  ?  442 ASN D OD1 1 
ATOM   8542 N ND2 . ASN D 1 287 ? 48.451  78.398 20.504  1.00 94.00  ?  442 ASN D ND2 1 
ATOM   8543 N N   . LYS D 1 288 ? 46.959  72.988 18.467  1.00 65.66  ?  443 LYS D N   1 
ATOM   8544 C CA  . LYS D 1 288 ? 46.708  72.116 17.312  1.00 64.97  ?  443 LYS D CA  1 
ATOM   8545 C C   . LYS D 1 288 ? 45.199  71.763 17.149  1.00 70.36  ?  443 LYS D C   1 
ATOM   8546 O O   . LYS D 1 288 ? 44.782  71.325 16.072  1.00 71.59  ?  443 LYS D O   1 
ATOM   8547 C CB  . LYS D 1 288 ? 47.553  70.838 17.402  1.00 66.04  ?  443 LYS D CB  1 
ATOM   8548 N N   . ARG D 1 289 ? 44.391  71.965 18.215  1.00 65.05  ?  444 ARG D N   1 
ATOM   8549 C CA  . ARG D 1 289 ? 42.953  71.666 18.258  1.00 63.35  ?  444 ARG D CA  1 
ATOM   8550 C C   . ARG D 1 289 ? 42.139  72.739 17.530  1.00 65.72  ?  444 ARG D C   1 
ATOM   8551 O O   . ARG D 1 289 ? 42.528  73.908 17.554  1.00 65.44  ?  444 ARG D O   1 
ATOM   8552 C CB  . ARG D 1 289 ? 42.458  71.607 19.719  1.00 59.89  ?  444 ARG D CB  1 
ATOM   8553 C CG  . ARG D 1 289 ? 43.019  70.486 20.544  1.00 56.79  ?  444 ARG D CG  1 
ATOM   8554 C CD  . ARG D 1 289 ? 42.691  70.757 21.985  1.00 49.72  ?  444 ARG D CD  1 
ATOM   8555 N NE  . ARG D 1 289 ? 43.660  70.101 22.848  1.00 51.67  ?  444 ARG D NE  1 
ATOM   8556 C CZ  . ARG D 1 289 ? 43.854  70.429 24.115  1.00 67.38  ?  444 ARG D CZ  1 
ATOM   8557 N NH1 . ARG D 1 289 ? 43.120  71.381 24.681  1.00 63.49  ?  444 ARG D NH1 1 
ATOM   8558 N NH2 . ARG D 1 289 ? 44.785  69.811 24.827  1.00 41.79  1  444 ARG D NH2 1 
ATOM   8559 N N   . PRO D 1 290 ? 40.958  72.400 16.970  1.00 61.30  ?  445 PRO D N   1 
ATOM   8560 C CA  . PRO D 1 290 ? 40.132  73.453 16.357  1.00 61.30  ?  445 PRO D CA  1 
ATOM   8561 C C   . PRO D 1 290 ? 39.406  74.295 17.412  1.00 65.96  ?  445 PRO D C   1 
ATOM   8562 O O   . PRO D 1 290 ? 39.243  73.856 18.556  1.00 66.23  ?  445 PRO D O   1 
ATOM   8563 C CB  . PRO D 1 290 ? 39.125  72.665 15.511  1.00 62.85  ?  445 PRO D CB  1 
ATOM   8564 C CG  . PRO D 1 290 ? 39.014  71.351 16.185  1.00 66.80  ?  445 PRO D CG  1 
ATOM   8565 C CD  . PRO D 1 290 ? 40.310  71.071 16.881  1.00 62.05  ?  445 PRO D CD  1 
ATOM   8566 N N   . ASP D 1 291 ? 38.957  75.492 17.030  1.00 61.78  ?  446 ASP D N   1 
ATOM   8567 C CA  . ASP D 1 291 ? 38.165  76.301 17.944  1.00 61.33  ?  446 ASP D CA  1 
ATOM   8568 C C   . ASP D 1 291 ? 36.699  75.852 17.784  1.00 65.12  ?  446 ASP D C   1 
ATOM   8569 O O   . ASP D 1 291 ? 36.368  75.153 16.810  1.00 65.64  ?  446 ASP D O   1 
ATOM   8570 C CB  . ASP D 1 291 ? 38.368  77.816 17.717  1.00 63.28  ?  446 ASP D CB  1 
ATOM   8571 C CG  . ASP D 1 291 ? 38.041  78.376 16.340  1.00 81.63  ?  446 ASP D CG  1 
ATOM   8572 O OD1 . ASP D 1 291 ? 37.884  77.578 15.387  1.00 84.26  ?  446 ASP D OD1 1 
ATOM   8573 O OD2 . ASP D 1 291 ? 37.995  79.614 16.203  1.00 89.92  -1 446 ASP D OD2 1 
ATOM   8574 N N   . ILE D 1 292 ? 35.838  76.214 18.751  1.00 59.22  ?  447 ILE D N   1 
ATOM   8575 C CA  . ILE D 1 292 ? 34.435  75.821 18.756  1.00 56.89  ?  447 ILE D CA  1 
ATOM   8576 C C   . ILE D 1 292 ? 33.655  76.115 17.469  1.00 58.86  ?  447 ILE D C   1 
ATOM   8577 O O   . ILE D 1 292 ? 32.947  75.216 17.004  1.00 59.27  ?  447 ILE D O   1 
ATOM   8578 C CB  . ILE D 1 292 ? 33.707  76.143 20.090  1.00 58.57  ?  447 ILE D CB  1 
ATOM   8579 C CG1 . ILE D 1 292 ? 32.422  75.292 20.283  1.00 57.09  ?  447 ILE D CG1 1 
ATOM   8580 C CG2 . ILE D 1 292 ? 33.523  77.645 20.322  1.00 59.07  ?  447 ILE D CG2 1 
ATOM   8581 C CD1 . ILE D 1 292 ? 32.670  73.756 20.448  1.00 53.81  ?  447 ILE D CD1 1 
ATOM   8582 N N   . LYS D 1 293 ? 33.844  77.304 16.847  1.00 53.36  ?  448 LYS D N   1 
ATOM   8583 C CA  . LYS D 1 293 ? 33.158  77.621 15.576  1.00 52.85  ?  448 LYS D CA  1 
ATOM   8584 C C   . LYS D 1 293 ? 33.551  76.636 14.459  1.00 54.55  ?  448 LYS D C   1 
ATOM   8585 O O   . LYS D 1 293 ? 32.705  76.258 13.655  1.00 51.31  ?  448 LYS D O   1 
ATOM   8586 C CB  . LYS D 1 293 ? 33.364  79.079 15.141  1.00 55.57  ?  448 LYS D CB  1 
ATOM   8587 N N   . LYS D 1 294 ? 34.815  76.159 14.468  1.00 53.58  ?  449 LYS D N   1 
ATOM   8588 C CA  . LYS D 1 294 ? 35.286  75.163 13.497  1.00 53.96  ?  449 LYS D CA  1 
ATOM   8589 C C   . LYS D 1 294 ? 34.597  73.828 13.779  1.00 59.14  ?  449 LYS D C   1 
ATOM   8590 O O   . LYS D 1 294 ? 34.097  73.204 12.834  1.00 59.83  ?  449 LYS D O   1 
ATOM   8591 C CB  . LYS D 1 294 ? 36.826  75.024 13.519  1.00 56.59  ?  449 LYS D CB  1 
ATOM   8592 C CG  . LYS D 1 294 ? 37.421  74.042 12.496  1.00 75.52  ?  449 LYS D CG  1 
ATOM   8593 C CD  . LYS D 1 294 ? 37.192  74.436 11.034  1.00 89.64  ?  449 LYS D CD  1 
ATOM   8594 C CE  . LYS D 1 294 ? 37.732  73.382 10.094  1.00 104.56 ?  449 LYS D CE  1 
ATOM   8595 N NZ  . LYS D 1 294 ? 37.309  73.628 8.690   1.00 113.40 1  449 LYS D NZ  1 
ATOM   8596 N N   . VAL D 1 295 ? 34.536  73.420 15.086  1.00 54.03  ?  450 VAL D N   1 
ATOM   8597 C CA  . VAL D 1 295 ? 33.866  72.200 15.560  1.00 52.97  ?  450 VAL D CA  1 
ATOM   8598 C C   . VAL D 1 295 ? 32.385  72.209 15.098  1.00 57.31  ?  450 VAL D C   1 
ATOM   8599 O O   . VAL D 1 295 ? 31.917  71.208 14.542  1.00 56.88  ?  450 VAL D O   1 
ATOM   8600 C CB  . VAL D 1 295 ? 34.033  71.995 17.092  1.00 56.01  ?  450 VAL D CB  1 
ATOM   8601 C CG1 . VAL D 1 295 ? 33.251  70.784 17.591  1.00 55.48  ?  450 VAL D CG1 1 
ATOM   8602 C CG2 . VAL D 1 295 ? 35.509  71.868 17.475  1.00 55.65  ?  450 VAL D CG2 1 
ATOM   8603 N N   . GLN D 1 296 ? 31.688  73.365 15.243  1.00 53.46  ?  451 GLN D N   1 
ATOM   8604 C CA  . GLN D 1 296 ? 30.299  73.517 14.787  1.00 53.01  ?  451 GLN D CA  1 
ATOM   8605 C C   . GLN D 1 296 ? 30.205  73.313 13.282  1.00 57.14  ?  451 GLN D C   1 
ATOM   8606 O O   . GLN D 1 296 ? 29.318  72.585 12.823  1.00 56.90  ?  451 GLN D O   1 
ATOM   8607 C CB  . GLN D 1 296 ? 29.764  74.908 15.085  1.00 54.07  ?  451 GLN D CB  1 
ATOM   8608 C CG  . GLN D 1 296 ? 29.458  75.218 16.524  1.00 70.30  ?  451 GLN D CG  1 
ATOM   8609 C CD  . GLN D 1 296 ? 28.719  76.537 16.551  1.00 86.70  ?  451 GLN D CD  1 
ATOM   8610 O OE1 . GLN D 1 296 ? 29.429  77.631 16.300  1.00 76.50  ?  451 GLN D OE1 1 
ATOM   8611 N NE2 . GLN D 1 296 ? 27.496  76.588 16.688  1.00 86.06  ?  451 GLN D NE2 1 
ATOM   8612 N N   . GLN D 1 297 ? 31.114  73.981 12.517  1.00 53.28  ?  452 GLN D N   1 
ATOM   8613 C CA  . GLN D 1 297 ? 31.167  73.908 11.052  1.00 52.80  ?  452 GLN D CA  1 
ATOM   8614 C C   . GLN D 1 297 ? 31.355  72.459 10.597  1.00 54.79  ?  452 GLN D C   1 
ATOM   8615 O O   . GLN D 1 297 ? 30.583  71.965 9.766   1.00 54.00  ?  452 GLN D O   1 
ATOM   8616 C CB  . GLN D 1 297 ? 32.255  74.828 10.484  1.00 53.95  ?  452 GLN D CB  1 
ATOM   8617 N N   . LEU D 1 298 ? 32.320  71.769 11.206  1.00 49.59  ?  453 LEU D N   1 
ATOM   8618 C CA  . LEU D 1 298 ? 32.587  70.373 10.903  1.00 49.73  ?  453 LEU D CA  1 
ATOM   8619 C C   . LEU D 1 298 ? 31.386  69.454 11.211  1.00 55.10  ?  453 LEU D C   1 
ATOM   8620 O O   . LEU D 1 298 ? 31.059  68.584 10.386  1.00 55.34  ?  453 LEU D O   1 
ATOM   8621 C CB  . LEU D 1 298 ? 33.864  69.902 11.611  1.00 49.45  ?  453 LEU D CB  1 
ATOM   8622 C CG  . LEU D 1 298 ? 35.181  70.596 11.188  1.00 53.72  ?  453 LEU D CG  1 
ATOM   8623 C CD1 . LEU D 1 298 ? 36.292  70.292 12.157  1.00 53.81  ?  453 LEU D CD1 1 
ATOM   8624 C CD2 . LEU D 1 298 ? 35.592  70.216 9.775   1.00 54.25  ?  453 LEU D CD2 1 
ATOM   8625 N N   . LEU D 1 299 ? 30.698  69.679 12.360  1.00 50.37  ?  454 LEU D N   1 
ATOM   8626 C CA  . LEU D 1 299 ? 29.524  68.890 12.754  1.00 48.88  ?  454 LEU D CA  1 
ATOM   8627 C C   . LEU D 1 299 ? 28.339  69.139 11.802  1.00 53.81  ?  454 LEU D C   1 
ATOM   8628 O O   . LEU D 1 299 ? 27.623  68.187 11.461  1.00 52.71  ?  454 LEU D O   1 
ATOM   8629 C CB  . LEU D 1 299 ? 29.110  69.174 14.218  1.00 47.91  ?  454 LEU D CB  1 
ATOM   8630 C CG  . LEU D 1 299 ? 30.023  68.667 15.343  1.00 50.62  ?  454 LEU D CG  1 
ATOM   8631 C CD1 . LEU D 1 299 ? 29.454  69.045 16.683  1.00 50.29  ?  454 LEU D CD1 1 
ATOM   8632 C CD2 . LEU D 1 299 ? 30.358  67.134 15.224  1.00 45.83  ?  454 LEU D CD2 1 
ATOM   8633 N N   . GLN D 1 300 ? 28.144  70.420 11.368  1.00 50.92  ?  455 GLN D N   1 
ATOM   8634 C CA  . GLN D 1 300 ? 27.078  70.798 10.428  1.00 50.37  ?  455 GLN D CA  1 
ATOM   8635 C C   . GLN D 1 300 ? 27.325  70.135 9.071   1.00 57.76  ?  455 GLN D C   1 
ATOM   8636 O O   . GLN D 1 300 ? 26.378  69.638 8.468   1.00 58.30  ?  455 GLN D O   1 
ATOM   8637 C CB  . GLN D 1 300 ? 26.946  72.320 10.300  1.00 50.97  ?  455 GLN D CB  1 
ATOM   8638 N N   . GLU D 1 301 ? 28.604  70.057 8.641   1.00 56.76  ?  456 GLU D N   1 
ATOM   8639 C CA  . GLU D 1 301 ? 29.038  69.424 7.390   1.00 58.43  ?  456 GLU D CA  1 
ATOM   8640 C C   . GLU D 1 301 ? 28.746  67.914 7.402   1.00 66.41  ?  456 GLU D C   1 
ATOM   8641 O O   . GLU D 1 301 ? 28.390  67.334 6.372   1.00 66.55  ?  456 GLU D O   1 
ATOM   8642 C CB  . GLU D 1 301 ? 30.537  69.675 7.153   1.00 60.00  ?  456 GLU D CB  1 
ATOM   8643 C CG  . GLU D 1 301 ? 30.859  71.013 6.499   1.00 70.39  ?  456 GLU D CG  1 
ATOM   8644 C CD  . GLU D 1 301 ? 32.245  71.600 6.748   1.00 91.43  ?  456 GLU D CD  1 
ATOM   8645 O OE1 . GLU D 1 301 ? 33.208  70.832 6.992   1.00 66.55  ?  456 GLU D OE1 1 
ATOM   8646 O OE2 . GLU D 1 301 ? 32.367  72.844 6.675   1.00 92.51  -1 456 GLU D OE2 1 
ATOM   8647 N N   . MET D 1 302 ? 28.882  67.298 8.586   1.00 65.37  ?  457 MET D N   1 
ATOM   8648 C CA  . MET D 1 302 ? 28.656  65.885 8.902   1.00 66.00  ?  457 MET D CA  1 
ATOM   8649 C C   . MET D 1 302 ? 27.285  65.352 8.425   1.00 72.22  ?  457 MET D C   1 
ATOM   8650 O O   . MET D 1 302 ? 27.190  64.182 8.028   1.00 71.88  ?  457 MET D O   1 
ATOM   8651 C CB  . MET D 1 302 ? 28.715  65.742 10.410  1.00 68.10  ?  457 MET D CB  1 
ATOM   8652 C CG  . MET D 1 302 ? 29.368  64.511 10.880  1.00 71.75  ?  457 MET D CG  1 
ATOM   8653 S SD  . MET D 1 302 ? 28.406  63.714 12.170  1.00 76.18  ?  457 MET D SD  1 
ATOM   8654 C CE  . MET D 1 302 ? 28.194  65.035 13.346  1.00 72.56  ?  457 MET D CE  1 
ATOM   8655 N N   . THR D 1 303 ? 26.230  66.205 8.497   1.00 68.66  ?  458 THR D N   1 
ATOM   8656 C CA  . THR D 1 303 ? 24.857  65.863 8.115   1.00 88.33  ?  458 THR D CA  1 
ATOM   8657 C C   . THR D 1 303 ? 24.476  66.311 6.691   1.00 106.38 ?  458 THR D C   1 
ATOM   8658 O O   . THR D 1 303 ? 24.772  67.428 6.265   1.00 63.87  ?  458 THR D O   1 
ATOM   8659 C CB  . THR D 1 303 ? 23.851  66.308 9.190   1.00 94.24  ?  458 THR D CB  1 
ATOM   8660 O OG1 . THR D 1 303 ? 23.976  67.713 9.423   1.00 92.55  ?  458 THR D OG1 1 
ATOM   8661 C CG2 . THR D 1 303 ? 24.003  65.535 10.503  1.00 91.37  ?  458 THR D CG2 1 
HETATM 8662 S S   . SO4 E 2 .   ? 9.589   41.600 10.864  1.00 85.94  ?  501 SO4 A S   1 
HETATM 8663 O O1  . SO4 E 2 .   ? 9.413   43.027 10.442  1.00 91.73  -1 501 SO4 A O1  1 
HETATM 8664 O O2  . SO4 E 2 .   ? 9.754   40.758 9.624   1.00 89.89  ?  501 SO4 A O2  1 
HETATM 8665 O O3  . SO4 E 2 .   ? 8.380   41.152 11.626  1.00 90.04  ?  501 SO4 A O3  1 
HETATM 8666 O O4  . SO4 E 2 .   ? 10.792  41.516 11.770  1.00 90.08  -1 501 SO4 A O4  1 
HETATM 8667 C C13 . ZVA F 3 .   ? 15.613  35.605 13.384  1.00 27.57  ?  502 ZVA A C13 1 
HETATM 8668 C C18 . ZVA F 3 .   ? 15.256  42.210 14.977  1.00 34.97  ?  502 ZVA A C18 1 
HETATM 8669 C C17 . ZVA F 3 .   ? 15.400  40.626 15.111  1.00 34.51  ?  502 ZVA A C17 1 
HETATM 8670 C C16 . ZVA F 3 .   ? 15.679  39.913 13.762  1.00 30.52  ?  502 ZVA A C16 1 
HETATM 8671 C C15 . ZVA F 3 .   ? 16.868  37.731 13.966  1.00 33.08  ?  502 ZVA A C15 1 
HETATM 8672 C C19 . ZVA F 3 .   ? 15.120  42.948 16.304  1.00 28.30  ?  502 ZVA A C19 1 
HETATM 8673 C C20 . ZVA F 3 .   ? 14.101  42.570 14.057  1.00 36.78  ?  502 ZVA A C20 1 
HETATM 8674 C C11 . ZVA F 3 .   ? 21.138  36.202 15.984  1.00 31.34  ?  502 ZVA A C11 1 
HETATM 8675 C C12 . ZVA F 3 .   ? 21.140  34.951 13.790  1.00 32.14  ?  502 ZVA A C12 1 
HETATM 8676 F F   . ZVA F 3 .   ? 16.492  40.328 15.936  1.00 37.80  ?  502 ZVA A F   1 
HETATM 8677 O O1  . ZVA F 3 .   ? 16.472  42.661 14.339  1.00 35.81  ?  502 ZVA A O1  1 
HETATM 8678 N N6  . ZVA F 3 .   ? 15.687  38.452 13.789  1.00 29.97  ?  502 ZVA A N6  1 
HETATM 8679 O O   . ZVA F 3 .   ? 17.954  38.312 14.186  1.00 38.94  ?  502 ZVA A O   1 
HETATM 8680 C C14 . ZVA F 3 .   ? 16.788  36.241 13.901  1.00 29.52  ?  502 ZVA A C14 1 
HETATM 8681 C C9  . ZVA F 3 .   ? 17.912  35.414 14.237  1.00 30.76  ?  502 ZVA A C9  1 
HETATM 8682 N N4  . ZVA F 3 .   ? 19.065  36.010 14.685  1.00 31.07  ?  502 ZVA A N4  1 
HETATM 8683 C C10 . ZVA F 3 .   ? 20.343  35.329 15.031  1.00 34.00  ?  502 ZVA A C10 1 
HETATM 8684 C C8  . ZVA F 3 .   ? 17.804  33.980 14.039  1.00 31.70  ?  502 ZVA A C8  1 
HETATM 8685 N N5  . ZVA F 3 .   ? 15.469  34.248 13.189  1.00 26.45  ?  502 ZVA A N5  1 
HETATM 8686 C C7  . ZVA F 3 .   ? 16.576  33.460 13.540  1.00 28.84  ?  502 ZVA A C7  1 
HETATM 8687 N N3  . ZVA F 3 .   ? 16.399  32.064 13.417  1.00 29.72  ?  502 ZVA A N3  1 
HETATM 8688 C C5  . ZVA F 3 .   ? 17.327  31.013 13.523  1.00 32.34  ?  502 ZVA A C5  1 
HETATM 8689 N N1  . ZVA F 3 .   ? 18.708  31.035 13.560  1.00 36.63  ?  502 ZVA A N1  1 
HETATM 8690 C C2  . ZVA F 3 .   ? 19.331  29.837 13.699  1.00 38.47  ?  502 ZVA A C2  1 
HETATM 8691 N N2  . ZVA F 3 .   ? 15.120  31.548 13.404  1.00 33.00  ?  502 ZVA A N2  1 
HETATM 8692 C C6  . ZVA F 3 .   ? 15.206  30.214 13.519  1.00 33.08  ?  502 ZVA A C6  1 
HETATM 8693 C C4  . ZVA F 3 .   ? 16.567  29.819 13.607  1.00 34.22  ?  502 ZVA A C4  1 
HETATM 8694 C C3  . ZVA F 3 .   ? 17.232  28.613 13.782  1.00 38.46  ?  502 ZVA A C3  1 
HETATM 8695 C C1  . ZVA F 3 .   ? 18.616  28.625 13.836  1.00 40.84  ?  502 ZVA A C1  1 
HETATM 8696 C C   . ZVA F 3 .   ? 19.290  27.441 14.119  1.00 46.55  ?  502 ZVA A C   1 
HETATM 8697 N N   . ZVA F 3 .   ? 19.810  26.453 14.361  1.00 50.33  ?  502 ZVA A N   1 
HETATM 8698 S S   . SO4 G 2 .   ? -14.660 58.898 7.116   1.00 108.70 ?  501 SO4 B S   1 
HETATM 8699 O O1  . SO4 G 2 .   ? -15.961 58.508 6.553   1.00 113.71 -1 501 SO4 B O1  1 
HETATM 8700 O O2  . SO4 G 2 .   ? -14.127 60.036 6.365   1.00 113.75 ?  501 SO4 B O2  1 
HETATM 8701 O O3  . SO4 G 2 .   ? -13.717 57.769 6.996   1.00 113.23 ?  501 SO4 B O3  1 
HETATM 8702 O O4  . SO4 G 2 .   ? -14.817 59.291 8.545   1.00 113.92 -1 501 SO4 B O4  1 
HETATM 8703 S S   . SO4 H 2 .   ? 12.293  47.003 11.651  1.00 120.35 ?  502 SO4 B S   1 
HETATM 8704 O O1  . SO4 H 2 .   ? 12.791  45.609 11.531  1.00 125.18 ?  502 SO4 B O1  1 
HETATM 8705 O O2  . SO4 H 2 .   ? 12.672  47.760 10.439  1.00 124.68 ?  502 SO4 B O2  1 
HETATM 8706 O O3  . SO4 H 2 .   ? 10.818  46.964 11.792  1.00 125.42 -1 502 SO4 B O3  1 
HETATM 8707 O O4  . SO4 H 2 .   ? 12.905  47.651 12.848  1.00 125.36 -1 502 SO4 B O4  1 
HETATM 8708 C C13 . ZVA I 3 .   ? 6.006   52.579 10.309  1.00 33.56  ?  503 ZVA B C13 1 
HETATM 8709 C C18 . ZVA I 3 .   ? 5.413   46.159 11.949  1.00 32.06  ?  503 ZVA B C18 1 
HETATM 8710 C C17 . ZVA I 3 .   ? 5.346   47.720 11.843  1.00 37.10  ?  503 ZVA B C17 1 
HETATM 8711 C C16 . ZVA I 3 .   ? 5.784   48.341 10.499  1.00 32.81  ?  503 ZVA B C16 1 
HETATM 8712 C C15 . ZVA I 3 .   ? 4.681   50.530 9.915   1.00 36.17  ?  503 ZVA B C15 1 
HETATM 8713 C C19 . ZVA I 3 .   ? 4.771   45.682 13.244  1.00 27.28  ?  503 ZVA B C19 1 
HETATM 8714 C C20 . ZVA I 3 .   ? 6.825   45.614 11.824  1.00 31.83  ?  503 ZVA B C20 1 
HETATM 8715 C C11 . ZVA I 3 .   ? 0.031   51.827 9.251   1.00 32.45  ?  503 ZVA B C11 1 
HETATM 8716 C C12 . ZVA I 3 .   ? 1.147   53.376 7.630   1.00 29.77  ?  503 ZVA B C12 1 
HETATM 8717 F F   . ZVA I 3 .   ? 4.024   48.122 12.103  1.00 41.21  ?  503 ZVA B F   1 
HETATM 8718 O O1  . ZVA I 3 .   ? 4.660   45.634 10.837  1.00 31.77  ?  503 ZVA B O1  1 
HETATM 8719 N N6  . ZVA I 3 .   ? 5.694   49.800 10.563  1.00 33.83  ?  503 ZVA B N6  1 
HETATM 8720 O O   . ZVA I 3 .   ? 3.779   49.992 9.260   1.00 42.00  ?  503 ZVA B O   1 
HETATM 8721 C C14 . ZVA I 3 .   ? 4.745   51.991 10.021  1.00 34.55  ?  503 ZVA B C14 1 
HETATM 8722 C C9  . ZVA I 3 .   ? 3.601   52.856 9.786   1.00 35.89  ?  503 ZVA B C9  1 
HETATM 8723 N N4  . ZVA I 3 .   ? 2.394   52.261 9.463   1.00 34.66  ?  503 ZVA B N4  1 
HETATM 8724 C C10 . ZVA I 3 .   ? 1.096   52.887 9.062   1.00 33.74  ?  503 ZVA B C10 1 
HETATM 8725 C C8  . ZVA I 3 .   ? 3.799   54.300 9.853   1.00 34.89  ?  503 ZVA B C8  1 
HETATM 8726 N N5  . ZVA I 3 .   ? 6.207   53.919 10.376  1.00 35.64  ?  503 ZVA B N5  1 
HETATM 8727 C C7  . ZVA I 3 .   ? 5.112   54.763 10.144  1.00 34.91  ?  503 ZVA B C7  1 
HETATM 8728 N N3  . ZVA I 3 .   ? 5.424   56.169 10.163  1.00 37.53  ?  503 ZVA B N3  1 
HETATM 8729 C C5  . ZVA I 3 .   ? 4.596   57.240 9.768   1.00 37.71  ?  503 ZVA B C5  1 
HETATM 8730 N N1  . ZVA I 3 .   ? 3.416   57.197 9.045   1.00 39.49  ?  503 ZVA B N1  1 
HETATM 8731 C C2  . ZVA I 3 .   ? 2.794   58.356 8.928   1.00 37.43  ?  503 ZVA B C2  1 
HETATM 8732 N N2  . ZVA I 3 .   ? 6.543   56.683 10.876  1.00 37.70  ?  503 ZVA B N2  1 
HETATM 8733 C C6  . ZVA I 3 .   ? 6.397   58.023 10.972  1.00 35.88  ?  503 ZVA B C6  1 
HETATM 8734 C C4  . ZVA I 3 .   ? 5.180   58.430 10.313  1.00 35.42  ?  503 ZVA B C4  1 
HETATM 8735 C C3  . ZVA I 3 .   ? 4.484   59.606 10.172  1.00 36.43  ?  503 ZVA B C3  1 
HETATM 8736 C C1  . ZVA I 3 .   ? 3.274   59.549 9.476   1.00 36.03  ?  503 ZVA B C1  1 
HETATM 8737 C C   . ZVA I 3 .   ? 2.516   60.686 9.277   1.00 38.11  ?  503 ZVA B C   1 
HETATM 8738 N N   . ZVA I 3 .   ? 1.893   61.631 9.102   1.00 42.34  ?  503 ZVA B N   1 
HETATM 8739 S S   . SO4 J 2 .   ? -25.506 22.206 -2.773  1.00 84.80  ?  501 SO4 C S   1 
HETATM 8740 O O1  . SO4 J 2 .   ? -26.911 22.585 -2.944  1.00 90.88  -1 501 SO4 C O1  1 
HETATM 8741 O O2  . SO4 J 2 .   ? -24.843 22.007 -4.091  1.00 89.05  ?  501 SO4 C O2  1 
HETATM 8742 O O3  . SO4 J 2 .   ? -25.446 20.947 -2.050  1.00 89.25  ?  501 SO4 C O3  1 
HETATM 8743 O O4  . SO4 J 2 .   ? -24.832 23.291 -2.010  1.00 89.75  -1 501 SO4 C O4  1 
HETATM 8744 S S   . SO4 K 2 .   ? -26.163 26.429 19.809  1.00 142.89 ?  502 SO4 C S   1 
HETATM 8745 O O1  . SO4 K 2 .   ? -26.654 25.056 19.968  1.00 147.18 ?  502 SO4 C O1  1 
HETATM 8746 O O2  . SO4 K 2 .   ? -25.593 26.620 18.470  1.00 147.31 ?  502 SO4 C O2  1 
HETATM 8747 O O3  . SO4 K 2 .   ? -27.282 27.361 19.976  1.00 148.90 -1 502 SO4 C O3  1 
HETATM 8748 O O4  . SO4 K 2 .   ? -25.139 26.696 20.833  1.00 147.97 -1 502 SO4 C O4  1 
HETATM 8749 S S   . SO4 L 2 .   ? 0.014   36.227 -2.811  1.00 66.27  ?  503 SO4 C S   1 
HETATM 8750 O O1  . SO4 L 2 .   ? -0.944  36.671 -3.860  1.00 72.42  -1 503 SO4 C O1  1 
HETATM 8751 O O2  . SO4 L 2 .   ? 1.358   36.650 -3.145  1.00 70.72  ?  503 SO4 C O2  1 
HETATM 8752 O O3  . SO4 L 2 .   ? 0.012   34.744 -2.742  1.00 69.80  ?  503 SO4 C O3  1 
HETATM 8753 O O4  . SO4 L 2 .   ? -0.402  36.881 -1.530  1.00 71.14  -1 503 SO4 C O4  1 
HETATM 8754 C C13 . ZVA M 3 .   ? -6.316  22.873 28.492  1.00 37.10  ?  504 ZVA C C13 1 
HETATM 8755 C C18 . ZVA M 3 .   ? -3.388  28.868 27.848  1.00 46.33  ?  504 ZVA C C18 1 
HETATM 8756 C C17 . ZVA M 3 .   ? -4.137  27.479 27.590  1.00 43.10  ?  504 ZVA C C17 1 
HETATM 8757 C C16 . ZVA M 3 .   ? -4.567  26.722 28.854  1.00 40.12  ?  504 ZVA C C16 1 
HETATM 8758 C C15 . ZVA M 3 .   ? -6.587  25.340 28.566  1.00 39.21  ?  504 ZVA C C15 1 
HETATM 8759 C C19 . ZVA M 3 .   ? -3.107  29.614 26.546  1.00 45.56  ?  504 ZVA C C19 1 
HETATM 8760 C C20 . ZVA M 3 .   ? -2.092  28.632 28.613  1.00 42.62  ?  504 ZVA C C20 1 
HETATM 8761 C C11 . ZVA M 3 .   ? -11.097 26.131 26.727  1.00 50.76  ?  504 ZVA C C11 1 
HETATM 8762 C C12 . ZVA M 3 .   ? -11.708 24.498 28.532  1.00 51.86  ?  504 ZVA C C12 1 
HETATM 8763 F F   . ZVA M 3 .   ? -5.319  27.750 26.913  1.00 42.59  ?  504 ZVA C F   1 
HETATM 8764 O O1  . ZVA M 3 .   ? -4.244  29.701 28.666  1.00 44.19  ?  504 ZVA C O1  1 
HETATM 8765 N N6  . ZVA M 3 .   ? -5.196  25.440 28.587  1.00 36.74  ?  504 ZVA C N6  1 
HETATM 8766 O O   . ZVA M 3 .   ? -7.315  26.336 28.715  1.00 40.74  ?  504 ZVA C O   1 
HETATM 8767 C C14 . ZVA M 3 .   ? -7.149  23.987 28.329  1.00 40.45  ?  504 ZVA C C14 1 
HETATM 8768 C C9  . ZVA M 3 .   ? -8.516  23.758 27.974  1.00 46.03  ?  504 ZVA C C9  1 
HETATM 8769 N N4  . ZVA M 3 .   ? -9.363  24.848 27.822  1.00 48.85  ?  504 ZVA C N4  1 
HETATM 8770 C C10 . ZVA M 3 .   ? -10.780 24.802 27.375  1.00 51.04  ?  504 ZVA C C10 1 
HETATM 8771 C C8  . ZVA M 3 .   ? -8.954  22.386 27.789  1.00 43.33  ?  504 ZVA C C8  1 
HETATM 8772 N N5  . ZVA M 3 .   ? -6.693  21.595 28.334  1.00 38.04  ?  504 ZVA C N5  1 
HETATM 8773 C C7  . ZVA M 3 .   ? -8.012  21.358 27.978  1.00 41.44  ?  504 ZVA C C7  1 
HETATM 8774 N N3  . ZVA M 3 .   ? -8.390  19.946 27.876  1.00 40.83  ?  504 ZVA C N3  1 
HETATM 8775 C C5  . ZVA M 3 .   ? -9.682  19.386 27.783  1.00 36.22  ?  504 ZVA C C5  1 
HETATM 8776 N N1  . ZVA M 3 .   ? -10.917 20.002 27.993  1.00 34.18  ?  504 ZVA C N1  1 
HETATM 8777 C C2  . ZVA M 3 .   ? -11.963 19.210 27.743  1.00 36.47  ?  504 ZVA C C2  1 
HETATM 8778 N N2  . ZVA M 3 .   ? -7.441  18.956 27.632  1.00 37.47  ?  504 ZVA C N2  1 
HETATM 8779 C C6  . ZVA M 3 .   ? -8.095  17.816 27.348  1.00 35.16  ?  504 ZVA C C6  1 
HETATM 8780 C C4  . ZVA M 3 .   ? -9.492  18.011 27.405  1.00 34.67  ?  504 ZVA C C4  1 
HETATM 8781 C C3  . ZVA M 3 .   ? -10.608 17.212 27.141  1.00 36.71  ?  504 ZVA C C3  1 
HETATM 8782 C C1  . ZVA M 3 .   ? -11.851 17.833 27.287  1.00 37.37  ?  504 ZVA C C1  1 
HETATM 8783 C C   . ZVA M 3 .   ? -13.007 17.197 26.843  1.00 38.07  ?  504 ZVA C C   1 
HETATM 8784 N N   . ZVA M 3 .   ? -13.963 16.706 26.464  1.00 40.06  ?  504 ZVA C N   1 
HETATM 8785 S S   . SO4 N 2 .   ? 38.064  61.677 38.781  1.00 159.13 ?  501 SO4 D S   1 
HETATM 8786 O O1  . SO4 N 2 .   ? 37.678  60.804 37.655  1.00 163.58 ?  501 SO4 D O1  1 
HETATM 8787 O O2  . SO4 N 2 .   ? 38.388  63.016 38.274  1.00 163.55 ?  501 SO4 D O2  1 
HETATM 8788 O O3  . SO4 N 2 .   ? 36.949  61.765 39.737  1.00 164.77 -1 501 SO4 D O3  1 
HETATM 8789 O O4  . SO4 N 2 .   ? 39.238  61.121 39.456  1.00 164.31 -1 501 SO4 D O4  1 
HETATM 8790 S S   . SO4 O 2 .   ? 27.833  51.378 5.999   1.00 74.51  ?  502 SO4 D S   1 
HETATM 8791 O O1  . SO4 O 2 .   ? 26.586  50.685 6.396   1.00 81.95  -1 502 SO4 D O1  1 
HETATM 8792 O O2  . SO4 O 2 .   ? 27.918  51.486 4.497   1.00 77.70  ?  502 SO4 D O2  1 
HETATM 8793 O O3  . SO4 O 2 .   ? 28.963  50.618 6.505   1.00 79.39  ?  502 SO4 D O3  1 
HETATM 8794 O O4  . SO4 O 2 .   ? 27.867  52.678 6.610   1.00 79.42  -1 502 SO4 D O4  1 
HETATM 8795 C C13 . ZVA P 3 .   ? 16.314  65.299 35.281  1.00 34.99  ?  503 ZVA D C13 1 
HETATM 8796 C C18 . ZVA P 3 .   ? 14.098  59.342 33.133  1.00 30.72  ?  503 ZVA D C18 1 
HETATM 8797 C C17 . ZVA P 3 .   ? 14.925  60.678 33.327  1.00 37.70  ?  503 ZVA D C17 1 
HETATM 8798 C C16 . ZVA P 3 .   ? 14.610  61.464 34.646  1.00 38.58  ?  503 ZVA D C16 1 
HETATM 8799 C C15 . ZVA P 3 .   ? 16.527  62.862 35.407  1.00 37.08  ?  503 ZVA D C15 1 
HETATM 8800 C C19 . ZVA P 3 .   ? 14.249  58.834 31.706  1.00 29.81  ?  503 ZVA D C19 1 
HETATM 8801 C C20 . ZVA P 3 .   ? 12.626  59.519 33.491  1.00 22.84  ?  503 ZVA D C20 1 
HETATM 8802 C C11 . ZVA P 3 .   ? 21.562  62.404 35.795  1.00 43.60  ?  503 ZVA D C11 1 
HETATM 8803 C C12 . ZVA P 3 .   ? 21.035  63.787 37.826  1.00 45.60  ?  503 ZVA D C12 1 
HETATM 8804 F F   . ZVA P 3 .   ? 16.302  60.375 33.261  1.00 40.53  ?  503 ZVA D F   1 
HETATM 8805 O O1  . ZVA P 3 .   ? 14.655  58.331 33.993  1.00 28.24  ?  503 ZVA D O1  1 
HETATM 8806 N N6  . ZVA P 3 .   ? 15.290  62.786 34.739  1.00 37.53  ?  503 ZVA D N6  1 
HETATM 8807 O O   . ZVA P 3 .   ? 17.081  61.831 35.853  1.00 38.57  ?  503 ZVA D O   1 
HETATM 8808 C C14 . ZVA P 3 .   ? 17.141  64.196 35.500  1.00 34.46  ?  503 ZVA D C14 1 
HETATM 8809 C C9  . ZVA P 3 .   ? 18.522  64.438 35.797  1.00 38.24  ?  503 ZVA D C9  1 
HETATM 8810 N N4  . ZVA P 3 .   ? 19.396  63.401 36.025  1.00 39.39  ?  503 ZVA D N4  1 
HETATM 8811 C C10 . ZVA P 3 .   ? 20.817  63.602 36.335  1.00 42.82  ?  503 ZVA D C10 1 
HETATM 8812 C C8  . ZVA P 3 .   ? 18.982  65.805 35.849  1.00 39.18  ?  503 ZVA D C8  1 
HETATM 8813 N N5  . ZVA P 3 .   ? 16.698  66.596 35.309  1.00 35.44  ?  503 ZVA D N5  1 
HETATM 8814 C C7  . ZVA P 3 .   ? 18.048  66.832 35.599  1.00 38.30  ?  503 ZVA D C7  1 
HETATM 8815 N N3  . ZVA P 3 .   ? 18.409  68.224 35.716  1.00 36.14  ?  503 ZVA D N3  1 
HETATM 8816 C C5  . ZVA P 3 .   ? 19.541  68.800 36.244  1.00 34.37  ?  503 ZVA D C5  1 
HETATM 8817 N N1  . ZVA P 3 .   ? 20.565  68.212 36.965  1.00 38.13  ?  503 ZVA D N1  1 
HETATM 8818 C C2  . ZVA P 3 .   ? 21.545  69.047 37.318  1.00 39.52  ?  503 ZVA D C2  1 
HETATM 8819 N N2  . ZVA P 3 .   ? 17.631  69.187 35.106  1.00 38.23  ?  503 ZVA D N2  1 
HETATM 8820 C C6  . ZVA P 3 .   ? 18.257  70.339 35.216  1.00 37.86  ?  503 ZVA D C6  1 
HETATM 8821 C C4  . ZVA P 3 .   ? 19.477  70.177 35.909  1.00 35.27  ?  503 ZVA D C4  1 
HETATM 8822 C C3  . ZVA P 3 .   ? 20.523  71.020 36.266  1.00 37.03  ?  503 ZVA D C3  1 
HETATM 8823 C C1  . ZVA P 3 .   ? 21.562  70.431 36.981  1.00 39.13  ?  503 ZVA D C1  1 
HETATM 8824 C C   . ZVA P 3 .   ? 22.654  71.170 37.374  1.00 42.21  ?  503 ZVA D C   1 
HETATM 8825 N N   . ZVA P 3 .   ? 23.559  71.770 37.688  1.00 47.20  ?  503 ZVA D N   1 
HETATM 8826 O O   . HOH Q 4 .   ? 17.553  43.556 27.680  1.00 23.33  ?  601 HOH A O   1 
HETATM 8827 O O   . HOH Q 4 .   ? 21.120  29.456 17.112  1.00 62.61  ?  602 HOH A O   1 
HETATM 8828 O O   . HOH Q 4 .   ? 24.737  22.729 26.447  1.00 39.42  ?  603 HOH A O   1 
HETATM 8829 O O   . HOH Q 4 .   ? 19.879  44.120 28.944  1.00 36.32  ?  604 HOH A O   1 
HETATM 8830 O O   . HOH Q 4 .   ? 24.776  30.073 17.460  1.00 35.01  ?  605 HOH A O   1 
HETATM 8831 O O   . HOH Q 4 .   ? 9.243   31.618 26.764  1.00 35.53  ?  606 HOH A O   1 
HETATM 8832 O O   . HOH Q 4 .   ? 30.167  43.627 28.677  1.00 49.73  ?  607 HOH A O   1 
HETATM 8833 O O   . HOH Q 4 .   ? 18.959  39.006 17.195  1.00 31.44  ?  608 HOH A O   1 
HETATM 8834 O O   . HOH Q 4 .   ? 28.080  28.246 18.000  1.00 61.46  ?  609 HOH A O   1 
HETATM 8835 O O   . HOH Q 4 .   ? 12.131  44.248 8.383   1.00 40.53  ?  610 HOH A O   1 
HETATM 8836 O O   . HOH Q 4 .   ? 5.800   28.321 3.274   1.00 29.85  ?  611 HOH A O   1 
HETATM 8837 O O   . HOH Q 4 .   ? 7.176   44.158 29.933  1.00 45.06  ?  612 HOH A O   1 
HETATM 8838 O O   . HOH Q 4 .   ? 27.458  32.951 -1.518  1.00 38.87  ?  613 HOH A O   1 
HETATM 8839 O O   . HOH Q 4 .   ? 24.177  16.999 -5.015  1.00 54.65  ?  614 HOH A O   1 
HETATM 8840 O O   . HOH R 4 .   ? -19.765 60.975 28.499  1.00 33.95  ?  601 HOH B O   1 
HETATM 8841 O O   . HOH R 4 .   ? 14.389  66.071 11.503  1.00 36.94  ?  602 HOH B O   1 
HETATM 8842 O O   . HOH R 4 .   ? -14.187 44.432 23.356  1.00 29.08  ?  603 HOH B O   1 
HETATM 8843 O O   . HOH R 4 .   ? 1.675   45.930 10.619  1.00 34.09  ?  604 HOH B O   1 
HETATM 8844 O O   . HOH R 4 .   ? -4.112  66.608 11.028  1.00 45.00  ?  605 HOH B O   1 
HETATM 8845 O O   . HOH R 4 .   ? -3.529  44.530 21.358  1.00 38.08  ?  606 HOH B O   1 
HETATM 8846 O O   . HOH R 4 .   ? -17.028 55.625 17.034  1.00 32.85  ?  607 HOH B O   1 
HETATM 8847 O O   . HOH R 4 .   ? -7.692  55.353 13.685  1.00 25.93  ?  608 HOH B O   1 
HETATM 8848 O O   . HOH R 4 .   ? 16.552  53.818 11.307  1.00 42.54  ?  609 HOH B O   1 
HETATM 8849 O O   . HOH R 4 .   ? -14.856 44.495 15.933  1.00 58.99  ?  610 HOH B O   1 
HETATM 8850 O O   . HOH R 4 .   ? -3.776  58.577 8.992   1.00 48.04  ?  611 HOH B O   1 
HETATM 8851 O O   . HOH R 4 .   ? -0.413  58.328 10.497  1.00 66.70  ?  612 HOH B O   1 
HETATM 8852 O O   . HOH R 4 .   ? 9.290   65.487 17.570  1.00 35.24  ?  613 HOH B O   1 
HETATM 8853 O O   . HOH R 4 .   ? -14.948 56.800 10.243  1.00 47.66  ?  614 HOH B O   1 
HETATM 8854 O O   . HOH R 4 .   ? -5.689  42.272 12.091  1.00 56.05  ?  615 HOH B O   1 
HETATM 8855 O O   . HOH R 4 .   ? -6.815  71.482 26.753  1.00 45.30  ?  616 HOH B O   1 
HETATM 8856 O O   . HOH R 4 .   ? -9.006  62.190 7.471   1.00 52.87  ?  617 HOH B O   1 
HETATM 8857 O O   . HOH R 4 .   ? 4.199   44.203 28.994  1.00 45.45  ?  618 HOH B O   1 
HETATM 8858 O O   . HOH R 4 .   ? -10.913 63.017 14.137  1.00 51.84  ?  619 HOH B O   1 
HETATM 8859 O O   . HOH R 4 .   ? 8.591   56.987 26.858  1.00 44.27  ?  620 HOH B O   1 
HETATM 8860 O O   . HOH S 4 .   ? -6.868  34.604 14.229  1.00 26.06  ?  601 HOH C O   1 
HETATM 8861 O O   . HOH S 4 .   ? -13.734 20.156 24.202  1.00 41.07  ?  602 HOH C O   1 
HETATM 8862 O O   . HOH S 4 .   ? -2.214  19.003 14.135  1.00 39.87  ?  603 HOH C O   1 
HETATM 8863 O O   . HOH S 4 .   ? -5.024  33.276 15.768  1.00 21.57  ?  604 HOH C O   1 
HETATM 8864 O O   . HOH S 4 .   ? -20.141 17.269 13.652  1.00 40.41  ?  605 HOH C O   1 
HETATM 8865 O O   . HOH S 4 .   ? -0.530  31.295 20.276  1.00 41.80  ?  606 HOH C O   1 
HETATM 8866 O O   . HOH S 4 .   ? 1.051   31.556 18.067  1.00 48.72  ?  607 HOH C O   1 
HETATM 8867 O O   . HOH S 4 .   ? 1.465   24.154 33.969  1.00 62.56  ?  608 HOH C O   1 
HETATM 8868 O O   . HOH S 4 .   ? 0.903   13.657 21.047  1.00 52.64  ?  609 HOH C O   1 
HETATM 8869 O O   . HOH S 4 .   ? -0.479  16.412 13.415  1.00 32.17  ?  610 HOH C O   1 
HETATM 8870 O O   . HOH T 4 .   ? 24.243  53.592 23.865  1.00 28.41  ?  601 HOH D O   1 
HETATM 8871 O O   . HOH T 4 .   ? 22.696  56.707 8.584   1.00 32.63  ?  602 HOH D O   1 
HETATM 8872 O O   . HOH T 4 .   ? 18.628  55.807 26.496  1.00 38.39  ?  603 HOH D O   1 
HETATM 8873 O O   . HOH T 4 .   ? 24.844  68.144 35.671  1.00 41.24  ?  604 HOH D O   1 
HETATM 8874 O O   . HOH T 4 .   ? 21.947  54.962 23.824  1.00 32.25  ?  605 HOH D O   1 
HETATM 8875 O O   . HOH T 4 .   ? 24.558  60.933 35.031  1.00 35.67  ?  606 HOH D O   1 
HETATM 8876 O O   . HOH T 4 .   ? 20.550  69.183 20.745  1.00 42.76  ?  607 HOH D O   1 
HETATM 8877 O O   . HOH T 4 .   ? 28.996  48.214 21.038  1.00 37.03  ?  608 HOH D O   1 
HETATM 8878 O O   . HOH T 4 .   ? 38.860  58.775 28.335  1.00 40.18  ?  609 HOH D O   1 
HETATM 8879 O O   . HOH T 4 .   ? 19.412  53.187 16.490  1.00 39.66  ?  610 HOH D O   1 
HETATM 8880 O O   . HOH T 4 .   ? 28.564  50.220 24.044  1.00 36.41  ?  611 HOH D O   1 
HETATM 8881 O O   . HOH T 4 .   ? 19.176  79.052 28.921  1.00 36.81  ?  612 HOH D O   1 
HETATM 8882 O O   . HOH T 4 .   ? 24.031  50.452 11.972  1.00 36.97  ?  613 HOH D O   1 
HETATM 8883 O O   . HOH T 4 .   ? 32.619  58.403 32.835  1.00 44.47  ?  614 HOH D O   1 
HETATM 8884 O O   . HOH T 4 .   ? 31.230  65.769 39.318  1.00 49.31  ?  615 HOH D O   1 
# 
