data_9DRO
# 
_entry.id   9DRO 
# 
_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   9DRO         pdb_00009dro 10.2210/pdb9dro/pdb 
WWPDB D_1000288679 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'Structure model' 1 1 2025-03-26 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DRO 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              matthias.fellner@otago.ac.nz 
_pdbx_contact_author.name_first         Matthias 
_pdbx_contact_author.name_last          Fellner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3192-6984 
# 
_audit_author.name               'Fellner, M.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-3192-6984 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Am.Chem.Soc. 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            147 
_citation.language                  ? 
_citation.page_first                8312 
_citation.page_last                 8325 
_citation.title                     'An mRNA Display Approach for Covalent Targeting of a Staphylococcus aureus Virulence Factor.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.4c15713 
_citation.pdbx_database_id_PubMed   40013487 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, S.'          1  ? 
primary 'Woods, E.C.'       2  ? 
primary 'Jo, J.'            3  ? 
primary 'Zhu, J.'           4  ? 
primary 'Hansel-Harris, A.' 5  ? 
primary 'Holcomb, M.'       6  ? 
primary 'Llanos, M.'        7  ? 
primary 'Pedowitz, N.J.'    8  ? 
primary 'Upadhyay, T.'      9  ? 
primary 'Bennett, J.'       10 ? 
primary 'Fellner, M.'       11 ? 
primary 'Park, K.W.'        12 ? 
primary 'Zhang, A.'         13 ? 
primary 'Valdez, T.A.'      14 ? 
primary 'Forli, S.'         15 ? 
primary 'Chan, A.I.'        16 ? 
primary 'Cunningham, C.N.'  17 ? 
primary 'Bogyo, M.'         18 ? 
# 
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 'Uncharacterized hydrolase SAUSA300_2518'         31275.100 2   3.-.-.- ? ? ? 
2 non-polymer syn 'methyl 2-formyl-2-phenylhydrazine-1-carboxylate' 194.187   2   ?       ? 
;Reacted ligand: The Oxadiazolone ring is opened and a covalent bond is formed with the active site serine (a smilar ligand has been reported in PDB entry 8T88). The actual ligand has a peptide chain attached to the benzene ring that is shown but there is no density evidence, so it wss not modelled.
;
? 
3 non-polymer syn 'MAGNESIUM ION'                                   24.305    4   ?       ? ? ? 
4 water       nat water                                             18.015    323 ?       ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GPGMETLELQGAKLRYHQVGQGPVLIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRDYGESELTEPLPDSASNPDSDYR
VKRDAQDIAELAKSLSDEPVYILGSSSGSIVAMHVLKDYPEVVKKIAFHEPPINTFLPDSTYWKDKNDDIVHQILTEGLE
KGMKTFGETLNIAPIDAKMMSQPADTEEGRIEQYKRTMFWLEFEIRQYTHSNITLDDFTKYSDKITLLNGTDSRGSFPQD
VNFYINKETGIPIVDIPGGHLGYIQKPEGFADVLLNMWG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPGMETLELQGAKLRYHQVGQGPVLIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRDYGESELTEPLPDSASNPDSDYR
VKRDAQDIAELAKSLSDEPVYILGSSSGSIVAMHVLKDYPEVVKKIAFHEPPINTFLPDSTYWKDKNDDIVHQILTEGLE
KGMKTFGETLNIAPIDAKMMSQPADTEEGRIEQYKRTMFWLEFEIRQYTHSNITLDDFTKYSDKITLLNGTDSRGSFPQD
VNFYINKETGIPIVDIPGGHLGYIQKPEGFADVLLNMWG
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'methyl 2-formyl-2-phenylhydrazine-1-carboxylate' A1BA1 
3 'MAGNESIUM ION'                                   MG    
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   PRO n 
1 3   GLY n 
1 4   MET n 
1 5   GLU n 
1 6   THR n 
1 7   LEU n 
1 8   GLU n 
1 9   LEU n 
1 10  GLN n 
1 11  GLY n 
1 12  ALA n 
1 13  LYS n 
1 14  LEU n 
1 15  ARG n 
1 16  TYR n 
1 17  HIS n 
1 18  GLN n 
1 19  VAL n 
1 20  GLY n 
1 21  GLN n 
1 22  GLY n 
1 23  PRO n 
1 24  VAL n 
1 25  LEU n 
1 26  ILE n 
1 27  PHE n 
1 28  ILE n 
1 29  PRO n 
1 30  GLY n 
1 31  ALA n 
1 32  ASN n 
1 33  GLY n 
1 34  THR n 
1 35  GLY n 
1 36  ASP n 
1 37  ILE n 
1 38  PHE n 
1 39  LEU n 
1 40  PRO n 
1 41  LEU n 
1 42  ALA n 
1 43  GLU n 
1 44  GLN n 
1 45  LEU n 
1 46  LYS n 
1 47  ASP n 
1 48  HIS n 
1 49  PHE n 
1 50  THR n 
1 51  VAL n 
1 52  VAL n 
1 53  ALA n 
1 54  VAL n 
1 55  ASP n 
1 56  ARG n 
1 57  ARG n 
1 58  ASP n 
1 59  TYR n 
1 60  GLY n 
1 61  GLU n 
1 62  SER n 
1 63  GLU n 
1 64  LEU n 
1 65  THR n 
1 66  GLU n 
1 67  PRO n 
1 68  LEU n 
1 69  PRO n 
1 70  ASP n 
1 71  SER n 
1 72  ALA n 
1 73  SER n 
1 74  ASN n 
1 75  PRO n 
1 76  ASP n 
1 77  SER n 
1 78  ASP n 
1 79  TYR n 
1 80  ARG n 
1 81  VAL n 
1 82  LYS n 
1 83  ARG n 
1 84  ASP n 
1 85  ALA n 
1 86  GLN n 
1 87  ASP n 
1 88  ILE n 
1 89  ALA n 
1 90  GLU n 
1 91  LEU n 
1 92  ALA n 
1 93  LYS n 
1 94  SER n 
1 95  LEU n 
1 96  SER n 
1 97  ASP n 
1 98  GLU n 
1 99  PRO n 
1 100 VAL n 
1 101 TYR n 
1 102 ILE n 
1 103 LEU n 
1 104 GLY n 
1 105 SER n 
1 106 SER n 
1 107 SER n 
1 108 GLY n 
1 109 SER n 
1 110 ILE n 
1 111 VAL n 
1 112 ALA n 
1 113 MET n 
1 114 HIS n 
1 115 VAL n 
1 116 LEU n 
1 117 LYS n 
1 118 ASP n 
1 119 TYR n 
1 120 PRO n 
1 121 GLU n 
1 122 VAL n 
1 123 VAL n 
1 124 LYS n 
1 125 LYS n 
1 126 ILE n 
1 127 ALA n 
1 128 PHE n 
1 129 HIS n 
1 130 GLU n 
1 131 PRO n 
1 132 PRO n 
1 133 ILE n 
1 134 ASN n 
1 135 THR n 
1 136 PHE n 
1 137 LEU n 
1 138 PRO n 
1 139 ASP n 
1 140 SER n 
1 141 THR n 
1 142 TYR n 
1 143 TRP n 
1 144 LYS n 
1 145 ASP n 
1 146 LYS n 
1 147 ASN n 
1 148 ASP n 
1 149 ASP n 
1 150 ILE n 
1 151 VAL n 
1 152 HIS n 
1 153 GLN n 
1 154 ILE n 
1 155 LEU n 
1 156 THR n 
1 157 GLU n 
1 158 GLY n 
1 159 LEU n 
1 160 GLU n 
1 161 LYS n 
1 162 GLY n 
1 163 MET n 
1 164 LYS n 
1 165 THR n 
1 166 PHE n 
1 167 GLY n 
1 168 GLU n 
1 169 THR n 
1 170 LEU n 
1 171 ASN n 
1 172 ILE n 
1 173 ALA n 
1 174 PRO n 
1 175 ILE n 
1 176 ASP n 
1 177 ALA n 
1 178 LYS n 
1 179 MET n 
1 180 MET n 
1 181 SER n 
1 182 GLN n 
1 183 PRO n 
1 184 ALA n 
1 185 ASP n 
1 186 THR n 
1 187 GLU n 
1 188 GLU n 
1 189 GLY n 
1 190 ARG n 
1 191 ILE n 
1 192 GLU n 
1 193 GLN n 
1 194 TYR n 
1 195 LYS n 
1 196 ARG n 
1 197 THR n 
1 198 MET n 
1 199 PHE n 
1 200 TRP n 
1 201 LEU n 
1 202 GLU n 
1 203 PHE n 
1 204 GLU n 
1 205 ILE n 
1 206 ARG n 
1 207 GLN n 
1 208 TYR n 
1 209 THR n 
1 210 HIS n 
1 211 SER n 
1 212 ASN n 
1 213 ILE n 
1 214 THR n 
1 215 LEU n 
1 216 ASP n 
1 217 ASP n 
1 218 PHE n 
1 219 THR n 
1 220 LYS n 
1 221 TYR n 
1 222 SER n 
1 223 ASP n 
1 224 LYS n 
1 225 ILE n 
1 226 THR n 
1 227 LEU n 
1 228 LEU n 
1 229 ASN n 
1 230 GLY n 
1 231 THR n 
1 232 ASP n 
1 233 SER n 
1 234 ARG n 
1 235 GLY n 
1 236 SER n 
1 237 PHE n 
1 238 PRO n 
1 239 GLN n 
1 240 ASP n 
1 241 VAL n 
1 242 ASN n 
1 243 PHE n 
1 244 TYR n 
1 245 ILE n 
1 246 ASN n 
1 247 LYS n 
1 248 GLU n 
1 249 THR n 
1 250 GLY n 
1 251 ILE n 
1 252 PRO n 
1 253 ILE n 
1 254 VAL n 
1 255 ASP n 
1 256 ILE n 
1 257 PRO n 
1 258 GLY n 
1 259 GLY n 
1 260 HIS n 
1 261 LEU n 
1 262 GLY n 
1 263 TYR n 
1 264 ILE n 
1 265 GLN n 
1 266 LYS n 
1 267 PRO n 
1 268 GLU n 
1 269 GLY n 
1 270 PHE n 
1 271 ALA n 
1 272 ASP n 
1 273 VAL n 
1 274 LEU n 
1 275 LEU n 
1 276 ASN n 
1 277 MET n 
1 278 TRP n 
1 279 GLY 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                   279 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SAUSA300_2518 
_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      'Staphylococcus aureus subsp. aureus USA300' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     367830 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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 
A1BA1 non-polymer         . 'methyl 2-formyl-2-phenylhydrazine-1-carboxylate' ? 'C9 H10 N2 O3'   194.187 
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 
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 
MG    non-polymer         . 'MAGNESIUM ION'                                   ? 'Mg 2'           24.305  
PHE   'L-peptide linking' y PHENYLALANINE                                     ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                           ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                            ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                         ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                        ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                          ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                            ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   PRO 2   -1  ?   ?   ?   A . n 
A 1 3   GLY 3   0   0   GLY GLY A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   GLU 5   2   2   GLU GLU A . n 
A 1 6   THR 6   3   3   THR THR A . n 
A 1 7   LEU 7   4   4   LEU LEU A . n 
A 1 8   GLU 8   5   5   GLU GLU A . n 
A 1 9   LEU 9   6   6   LEU LEU A . n 
A 1 10  GLN 10  7   7   GLN GLN A . n 
A 1 11  GLY 11  8   8   GLY GLY A . n 
A 1 12  ALA 12  9   9   ALA ALA A . n 
A 1 13  LYS 13  10  10  LYS LYS A . n 
A 1 14  LEU 14  11  11  LEU LEU A . n 
A 1 15  ARG 15  12  12  ARG ARG A . n 
A 1 16  TYR 16  13  13  TYR TYR A . n 
A 1 17  HIS 17  14  14  HIS HIS A . n 
A 1 18  GLN 18  15  15  GLN GLN A . n 
A 1 19  VAL 19  16  16  VAL VAL A . n 
A 1 20  GLY 20  17  17  GLY GLY A . n 
A 1 21  GLN 21  18  18  GLN GLN A . n 
A 1 22  GLY 22  19  19  GLY GLY A . n 
A 1 23  PRO 23  20  20  PRO PRO A . n 
A 1 24  VAL 24  21  21  VAL VAL A . n 
A 1 25  LEU 25  22  22  LEU LEU A . n 
A 1 26  ILE 26  23  23  ILE ILE A . n 
A 1 27  PHE 27  24  24  PHE PHE A . n 
A 1 28  ILE 28  25  25  ILE ILE A . n 
A 1 29  PRO 29  26  26  PRO PRO A . n 
A 1 30  GLY 30  27  27  GLY GLY A . n 
A 1 31  ALA 31  28  28  ALA ALA A . n 
A 1 32  ASN 32  29  29  ASN ASN A . n 
A 1 33  GLY 33  30  30  GLY GLY A . n 
A 1 34  THR 34  31  31  THR THR A . n 
A 1 35  GLY 35  32  32  GLY GLY A . n 
A 1 36  ASP 36  33  33  ASP ASP A . n 
A 1 37  ILE 37  34  34  ILE ILE A . n 
A 1 38  PHE 38  35  35  PHE PHE A . n 
A 1 39  LEU 39  36  36  LEU LEU A . n 
A 1 40  PRO 40  37  37  PRO PRO A . n 
A 1 41  LEU 41  38  38  LEU LEU A . n 
A 1 42  ALA 42  39  39  ALA ALA A . n 
A 1 43  GLU 43  40  40  GLU GLU A . n 
A 1 44  GLN 44  41  41  GLN GLN A . n 
A 1 45  LEU 45  42  42  LEU LEU A . n 
A 1 46  LYS 46  43  43  LYS LYS A . n 
A 1 47  ASP 47  44  44  ASP ASP A . n 
A 1 48  HIS 48  45  45  HIS HIS A . n 
A 1 49  PHE 49  46  46  PHE PHE A . n 
A 1 50  THR 50  47  47  THR THR A . n 
A 1 51  VAL 51  48  48  VAL VAL A . n 
A 1 52  VAL 52  49  49  VAL VAL A . n 
A 1 53  ALA 53  50  50  ALA ALA A . n 
A 1 54  VAL 54  51  51  VAL VAL A . n 
A 1 55  ASP 55  52  52  ASP ASP A . n 
A 1 56  ARG 56  53  53  ARG ARG A . n 
A 1 57  ARG 57  54  54  ARG ARG A . n 
A 1 58  ASP 58  55  55  ASP ASP A . n 
A 1 59  TYR 59  56  56  TYR TYR A . n 
A 1 60  GLY 60  57  57  GLY GLY A . n 
A 1 61  GLU 61  58  58  GLU GLU A . n 
A 1 62  SER 62  59  59  SER SER A . n 
A 1 63  GLU 63  60  60  GLU GLU A . n 
A 1 64  LEU 64  61  61  LEU LEU A . n 
A 1 65  THR 65  62  62  THR THR A . n 
A 1 66  GLU 66  63  63  GLU GLU A . n 
A 1 67  PRO 67  64  64  PRO PRO A . n 
A 1 68  LEU 68  65  65  LEU LEU A . n 
A 1 69  PRO 69  66  66  PRO PRO A . n 
A 1 70  ASP 70  67  67  ASP ASP A . n 
A 1 71  SER 71  68  68  SER SER A . n 
A 1 72  ALA 72  69  69  ALA ALA A . n 
A 1 73  SER 73  70  70  SER SER A . n 
A 1 74  ASN 74  71  71  ASN ASN A . n 
A 1 75  PRO 75  72  72  PRO PRO A . n 
A 1 76  ASP 76  73  73  ASP ASP A . n 
A 1 77  SER 77  74  74  SER SER A . n 
A 1 78  ASP 78  75  75  ASP ASP A . n 
A 1 79  TYR 79  76  76  TYR TYR A . n 
A 1 80  ARG 80  77  77  ARG ARG A . n 
A 1 81  VAL 81  78  78  VAL VAL A . n 
A 1 82  LYS 82  79  79  LYS LYS A . n 
A 1 83  ARG 83  80  80  ARG ARG A . n 
A 1 84  ASP 84  81  81  ASP ASP A . n 
A 1 85  ALA 85  82  82  ALA ALA A . n 
A 1 86  GLN 86  83  83  GLN GLN A . n 
A 1 87  ASP 87  84  84  ASP ASP A . n 
A 1 88  ILE 88  85  85  ILE ILE A . n 
A 1 89  ALA 89  86  86  ALA ALA A . n 
A 1 90  GLU 90  87  87  GLU GLU A . n 
A 1 91  LEU 91  88  88  LEU LEU A . n 
A 1 92  ALA 92  89  89  ALA ALA A . n 
A 1 93  LYS 93  90  90  LYS LYS A . n 
A 1 94  SER 94  91  91  SER SER A . n 
A 1 95  LEU 95  92  92  LEU LEU A . n 
A 1 96  SER 96  93  93  SER SER A . n 
A 1 97  ASP 97  94  94  ASP ASP A . n 
A 1 98  GLU 98  95  95  GLU GLU A . n 
A 1 99  PRO 99  96  96  PRO PRO A . n 
A 1 100 VAL 100 97  97  VAL VAL A . n 
A 1 101 TYR 101 98  98  TYR TYR A . n 
A 1 102 ILE 102 99  99  ILE ILE A . n 
A 1 103 LEU 103 100 100 LEU LEU A . n 
A 1 104 GLY 104 101 101 GLY GLY A . n 
A 1 105 SER 105 102 102 SER SER A . n 
A 1 106 SER 106 103 103 SER SER A . n 
A 1 107 SER 107 104 104 SER SER A . n 
A 1 108 GLY 108 105 105 GLY GLY A . n 
A 1 109 SER 109 106 106 SER SER A . n 
A 1 110 ILE 110 107 107 ILE ILE A . n 
A 1 111 VAL 111 108 108 VAL VAL A . n 
A 1 112 ALA 112 109 109 ALA ALA A . n 
A 1 113 MET 113 110 110 MET MET A . n 
A 1 114 HIS 114 111 111 HIS HIS A . n 
A 1 115 VAL 115 112 112 VAL VAL A . n 
A 1 116 LEU 116 113 113 LEU LEU A . n 
A 1 117 LYS 117 114 114 LYS LYS A . n 
A 1 118 ASP 118 115 115 ASP ASP A . n 
A 1 119 TYR 119 116 116 TYR TYR A . n 
A 1 120 PRO 120 117 117 PRO PRO A . n 
A 1 121 GLU 121 118 118 GLU GLU A . n 
A 1 122 VAL 122 119 119 VAL VAL A . n 
A 1 123 VAL 123 120 120 VAL VAL A . n 
A 1 124 LYS 124 121 121 LYS LYS A . n 
A 1 125 LYS 125 122 122 LYS LYS A . n 
A 1 126 ILE 126 123 123 ILE ILE A . n 
A 1 127 ALA 127 124 124 ALA ALA A . n 
A 1 128 PHE 128 125 125 PHE PHE A . n 
A 1 129 HIS 129 126 126 HIS HIS A . n 
A 1 130 GLU 130 127 127 GLU GLU A . n 
A 1 131 PRO 131 128 128 PRO PRO A . n 
A 1 132 PRO 132 129 129 PRO PRO A . n 
A 1 133 ILE 133 130 130 ILE ILE A . n 
A 1 134 ASN 134 131 131 ASN ASN A . n 
A 1 135 THR 135 132 132 THR THR A . n 
A 1 136 PHE 136 133 133 PHE PHE A . n 
A 1 137 LEU 137 134 134 LEU LEU A . n 
A 1 138 PRO 138 135 135 PRO PRO A . n 
A 1 139 ASP 139 136 136 ASP ASP A . n 
A 1 140 SER 140 137 137 SER SER A . n 
A 1 141 THR 141 138 138 THR THR A . n 
A 1 142 TYR 142 139 139 TYR TYR A . n 
A 1 143 TRP 143 140 140 TRP TRP A . n 
A 1 144 LYS 144 141 141 LYS LYS A . n 
A 1 145 ASP 145 142 142 ASP ASP A . n 
A 1 146 LYS 146 143 143 LYS LYS A . n 
A 1 147 ASN 147 144 144 ASN ASN A . n 
A 1 148 ASP 148 145 145 ASP ASP A . n 
A 1 149 ASP 149 146 146 ASP ASP A . n 
A 1 150 ILE 150 147 147 ILE ILE A . n 
A 1 151 VAL 151 148 148 VAL VAL A . n 
A 1 152 HIS 152 149 149 HIS HIS A . n 
A 1 153 GLN 153 150 150 GLN GLN A . n 
A 1 154 ILE 154 151 151 ILE ILE A . n 
A 1 155 LEU 155 152 152 LEU LEU A . n 
A 1 156 THR 156 153 153 THR THR A . n 
A 1 157 GLU 157 154 154 GLU GLU A . n 
A 1 158 GLY 158 155 155 GLY GLY A . n 
A 1 159 LEU 159 156 156 LEU LEU A . n 
A 1 160 GLU 160 157 157 GLU GLU A . n 
A 1 161 LYS 161 158 158 LYS LYS A . n 
A 1 162 GLY 162 159 159 GLY GLY A . n 
A 1 163 MET 163 160 160 MET MET A . n 
A 1 164 LYS 164 161 161 LYS LYS A . n 
A 1 165 THR 165 162 162 THR THR A . n 
A 1 166 PHE 166 163 163 PHE PHE A . n 
A 1 167 GLY 167 164 164 GLY GLY A . n 
A 1 168 GLU 168 165 165 GLU GLU A . n 
A 1 169 THR 169 166 166 THR THR A . n 
A 1 170 LEU 170 167 167 LEU LEU A . n 
A 1 171 ASN 171 168 168 ASN ASN A . n 
A 1 172 ILE 172 169 169 ILE ILE A . n 
A 1 173 ALA 173 170 170 ALA ALA A . n 
A 1 174 PRO 174 171 171 PRO PRO A . n 
A 1 175 ILE 175 172 172 ILE ILE A . n 
A 1 176 ASP 176 173 173 ASP ASP A . n 
A 1 177 ALA 177 174 174 ALA ALA A . n 
A 1 178 LYS 178 175 175 LYS LYS A . n 
A 1 179 MET 179 176 176 MET MET A . n 
A 1 180 MET 180 177 177 MET MET A . n 
A 1 181 SER 181 178 178 SER SER A . n 
A 1 182 GLN 182 179 179 GLN GLN A . n 
A 1 183 PRO 183 180 180 PRO PRO A . n 
A 1 184 ALA 184 181 181 ALA ALA A . n 
A 1 185 ASP 185 182 182 ASP ASP A . n 
A 1 186 THR 186 183 183 THR THR A . n 
A 1 187 GLU 187 184 184 GLU GLU A . n 
A 1 188 GLU 188 185 185 GLU GLU A . n 
A 1 189 GLY 189 186 186 GLY GLY A . n 
A 1 190 ARG 190 187 187 ARG ARG A . n 
A 1 191 ILE 191 188 188 ILE ILE A . n 
A 1 192 GLU 192 189 189 GLU GLU A . n 
A 1 193 GLN 193 190 190 GLN GLN A . n 
A 1 194 TYR 194 191 191 TYR TYR A . n 
A 1 195 LYS 195 192 192 LYS LYS A . n 
A 1 196 ARG 196 193 193 ARG ARG A . n 
A 1 197 THR 197 194 194 THR THR A . n 
A 1 198 MET 198 195 195 MET MET A . n 
A 1 199 PHE 199 196 196 PHE PHE A . n 
A 1 200 TRP 200 197 197 TRP TRP A . n 
A 1 201 LEU 201 198 198 LEU LEU A . n 
A 1 202 GLU 202 199 199 GLU GLU A . n 
A 1 203 PHE 203 200 200 PHE PHE A . n 
A 1 204 GLU 204 201 201 GLU GLU A . n 
A 1 205 ILE 205 202 202 ILE ILE A . n 
A 1 206 ARG 206 203 203 ARG ARG A . n 
A 1 207 GLN 207 204 204 GLN GLN A . n 
A 1 208 TYR 208 205 205 TYR TYR A . n 
A 1 209 THR 209 206 206 THR THR A . n 
A 1 210 HIS 210 207 207 HIS HIS A . n 
A 1 211 SER 211 208 208 SER SER A . n 
A 1 212 ASN 212 209 209 ASN ASN A . n 
A 1 213 ILE 213 210 210 ILE ILE A . n 
A 1 214 THR 214 211 211 THR THR A . n 
A 1 215 LEU 215 212 212 LEU LEU A . n 
A 1 216 ASP 216 213 213 ASP ASP A . n 
A 1 217 ASP 217 214 214 ASP ASP A . n 
A 1 218 PHE 218 215 215 PHE PHE A . n 
A 1 219 THR 219 216 216 THR THR A . n 
A 1 220 LYS 220 217 217 LYS LYS A . n 
A 1 221 TYR 221 218 218 TYR TYR A . n 
A 1 222 SER 222 219 219 SER SER A . n 
A 1 223 ASP 223 220 220 ASP ASP A . n 
A 1 224 LYS 224 221 221 LYS LYS A . n 
A 1 225 ILE 225 222 222 ILE ILE A . n 
A 1 226 THR 226 223 223 THR THR A . n 
A 1 227 LEU 227 224 224 LEU LEU A . n 
A 1 228 LEU 228 225 225 LEU LEU A . n 
A 1 229 ASN 229 226 226 ASN ASN A . n 
A 1 230 GLY 230 227 227 GLY GLY A . n 
A 1 231 THR 231 228 228 THR THR A . n 
A 1 232 ASP 232 229 229 ASP ASP A . n 
A 1 233 SER 233 230 230 SER SER A . n 
A 1 234 ARG 234 231 231 ARG ARG A . n 
A 1 235 GLY 235 232 232 GLY GLY A . n 
A 1 236 SER 236 233 233 SER SER A . n 
A 1 237 PHE 237 234 234 PHE PHE A . n 
A 1 238 PRO 238 235 235 PRO PRO A . n 
A 1 239 GLN 239 236 236 GLN GLN A . n 
A 1 240 ASP 240 237 237 ASP ASP A . n 
A 1 241 VAL 241 238 238 VAL VAL A . n 
A 1 242 ASN 242 239 239 ASN ASN A . n 
A 1 243 PHE 243 240 240 PHE PHE A . n 
A 1 244 TYR 244 241 241 TYR TYR A . n 
A 1 245 ILE 245 242 242 ILE ILE A . n 
A 1 246 ASN 246 243 243 ASN ASN A . n 
A 1 247 LYS 247 244 244 LYS LYS A . n 
A 1 248 GLU 248 245 245 GLU GLU A . n 
A 1 249 THR 249 246 246 THR THR A . n 
A 1 250 GLY 250 247 247 GLY GLY A . n 
A 1 251 ILE 251 248 248 ILE ILE A . n 
A 1 252 PRO 252 249 249 PRO PRO A . n 
A 1 253 ILE 253 250 250 ILE ILE A . n 
A 1 254 VAL 254 251 251 VAL VAL A . n 
A 1 255 ASP 255 252 252 ASP ASP A . n 
A 1 256 ILE 256 253 253 ILE ILE A . n 
A 1 257 PRO 257 254 254 PRO PRO A . n 
A 1 258 GLY 258 255 255 GLY GLY A . n 
A 1 259 GLY 259 256 256 GLY GLY A . n 
A 1 260 HIS 260 257 257 HIS HIS A . n 
A 1 261 LEU 261 258 258 LEU LEU A . n 
A 1 262 GLY 262 259 259 GLY GLY A . n 
A 1 263 TYR 263 260 260 TYR TYR A . n 
A 1 264 ILE 264 261 261 ILE ILE A . n 
A 1 265 GLN 265 262 262 GLN GLN A . n 
A 1 266 LYS 266 263 263 LYS LYS A . n 
A 1 267 PRO 267 264 264 PRO PRO A . n 
A 1 268 GLU 268 265 265 GLU GLU A . n 
A 1 269 GLY 269 266 266 GLY GLY A . n 
A 1 270 PHE 270 267 267 PHE PHE A . n 
A 1 271 ALA 271 268 268 ALA ALA A . n 
A 1 272 ASP 272 269 269 ASP ASP A . n 
A 1 273 VAL 273 270 270 VAL VAL A . n 
A 1 274 LEU 274 271 271 LEU LEU A . n 
A 1 275 LEU 275 272 272 LEU LEU A . n 
A 1 276 ASN 276 273 273 ASN ASN A . n 
A 1 277 MET 277 274 274 MET MET A . n 
A 1 278 TRP 278 275 275 TRP TRP A . n 
A 1 279 GLY 279 276 276 GLY GLY A . n 
B 1 1   GLY 1   -2  ?   ?   ?   B . n 
B 1 2   PRO 2   -1  ?   ?   ?   B . n 
B 1 3   GLY 3   0   0   GLY GLY B . n 
B 1 4   MET 4   1   1   MET MET B . n 
B 1 5   GLU 5   2   2   GLU GLU B . n 
B 1 6   THR 6   3   3   THR THR B . n 
B 1 7   LEU 7   4   4   LEU LEU B . n 
B 1 8   GLU 8   5   5   GLU GLU B . n 
B 1 9   LEU 9   6   6   LEU LEU B . n 
B 1 10  GLN 10  7   7   GLN GLN B . n 
B 1 11  GLY 11  8   8   GLY GLY B . n 
B 1 12  ALA 12  9   9   ALA ALA B . n 
B 1 13  LYS 13  10  10  LYS LYS B . n 
B 1 14  LEU 14  11  11  LEU LEU B . n 
B 1 15  ARG 15  12  12  ARG ARG B . n 
B 1 16  TYR 16  13  13  TYR TYR B . n 
B 1 17  HIS 17  14  14  HIS HIS B . n 
B 1 18  GLN 18  15  15  GLN GLN B . n 
B 1 19  VAL 19  16  16  VAL VAL B . n 
B 1 20  GLY 20  17  17  GLY GLY B . n 
B 1 21  GLN 21  18  18  GLN GLN B . n 
B 1 22  GLY 22  19  19  GLY GLY B . n 
B 1 23  PRO 23  20  20  PRO PRO B . n 
B 1 24  VAL 24  21  21  VAL VAL B . n 
B 1 25  LEU 25  22  22  LEU LEU B . n 
B 1 26  ILE 26  23  23  ILE ILE B . n 
B 1 27  PHE 27  24  24  PHE PHE B . n 
B 1 28  ILE 28  25  25  ILE ILE B . n 
B 1 29  PRO 29  26  26  PRO PRO B . n 
B 1 30  GLY 30  27  27  GLY GLY B . n 
B 1 31  ALA 31  28  28  ALA ALA B . n 
B 1 32  ASN 32  29  29  ASN ASN B . n 
B 1 33  GLY 33  30  30  GLY GLY B . n 
B 1 34  THR 34  31  31  THR THR B . n 
B 1 35  GLY 35  32  32  GLY GLY B . n 
B 1 36  ASP 36  33  33  ASP ASP B . n 
B 1 37  ILE 37  34  34  ILE ILE B . n 
B 1 38  PHE 38  35  35  PHE PHE B . n 
B 1 39  LEU 39  36  36  LEU LEU B . n 
B 1 40  PRO 40  37  37  PRO PRO B . n 
B 1 41  LEU 41  38  38  LEU LEU B . n 
B 1 42  ALA 42  39  39  ALA ALA B . n 
B 1 43  GLU 43  40  40  GLU GLU B . n 
B 1 44  GLN 44  41  41  GLN GLN B . n 
B 1 45  LEU 45  42  42  LEU LEU B . n 
B 1 46  LYS 46  43  43  LYS LYS B . n 
B 1 47  ASP 47  44  44  ASP ASP B . n 
B 1 48  HIS 48  45  45  HIS HIS B . n 
B 1 49  PHE 49  46  46  PHE PHE B . n 
B 1 50  THR 50  47  47  THR THR B . n 
B 1 51  VAL 51  48  48  VAL VAL B . n 
B 1 52  VAL 52  49  49  VAL VAL B . n 
B 1 53  ALA 53  50  50  ALA ALA B . n 
B 1 54  VAL 54  51  51  VAL VAL B . n 
B 1 55  ASP 55  52  52  ASP ASP B . n 
B 1 56  ARG 56  53  53  ARG ARG B . n 
B 1 57  ARG 57  54  54  ARG ARG B . n 
B 1 58  ASP 58  55  55  ASP ASP B . n 
B 1 59  TYR 59  56  56  TYR TYR B . n 
B 1 60  GLY 60  57  57  GLY GLY B . n 
B 1 61  GLU 61  58  58  GLU GLU B . n 
B 1 62  SER 62  59  59  SER SER B . n 
B 1 63  GLU 63  60  60  GLU GLU B . n 
B 1 64  LEU 64  61  61  LEU LEU B . n 
B 1 65  THR 65  62  62  THR THR B . n 
B 1 66  GLU 66  63  63  GLU GLU B . n 
B 1 67  PRO 67  64  64  PRO PRO B . n 
B 1 68  LEU 68  65  65  LEU LEU B . n 
B 1 69  PRO 69  66  66  PRO PRO B . n 
B 1 70  ASP 70  67  67  ASP ASP B . n 
B 1 71  SER 71  68  68  SER SER B . n 
B 1 72  ALA 72  69  69  ALA ALA B . n 
B 1 73  SER 73  70  70  SER SER B . n 
B 1 74  ASN 74  71  71  ASN ASN B . n 
B 1 75  PRO 75  72  72  PRO PRO B . n 
B 1 76  ASP 76  73  73  ASP ASP B . n 
B 1 77  SER 77  74  74  SER SER B . n 
B 1 78  ASP 78  75  75  ASP ASP B . n 
B 1 79  TYR 79  76  76  TYR TYR B . n 
B 1 80  ARG 80  77  77  ARG ARG B . n 
B 1 81  VAL 81  78  78  VAL VAL B . n 
B 1 82  LYS 82  79  79  LYS LYS B . n 
B 1 83  ARG 83  80  80  ARG ARG B . n 
B 1 84  ASP 84  81  81  ASP ASP B . n 
B 1 85  ALA 85  82  82  ALA ALA B . n 
B 1 86  GLN 86  83  83  GLN GLN B . n 
B 1 87  ASP 87  84  84  ASP ASP B . n 
B 1 88  ILE 88  85  85  ILE ILE B . n 
B 1 89  ALA 89  86  86  ALA ALA B . n 
B 1 90  GLU 90  87  87  GLU GLU B . n 
B 1 91  LEU 91  88  88  LEU LEU B . n 
B 1 92  ALA 92  89  89  ALA ALA B . n 
B 1 93  LYS 93  90  90  LYS LYS B . n 
B 1 94  SER 94  91  91  SER SER B . n 
B 1 95  LEU 95  92  92  LEU LEU B . n 
B 1 96  SER 96  93  93  SER SER B . n 
B 1 97  ASP 97  94  94  ASP ASP B . n 
B 1 98  GLU 98  95  95  GLU GLU B . n 
B 1 99  PRO 99  96  96  PRO PRO B . n 
B 1 100 VAL 100 97  97  VAL VAL B . n 
B 1 101 TYR 101 98  98  TYR TYR B . n 
B 1 102 ILE 102 99  99  ILE ILE B . n 
B 1 103 LEU 103 100 100 LEU LEU B . n 
B 1 104 GLY 104 101 101 GLY GLY B . n 
B 1 105 SER 105 102 102 SER SER B . n 
B 1 106 SER 106 103 103 SER SER B . n 
B 1 107 SER 107 104 104 SER SER B . n 
B 1 108 GLY 108 105 105 GLY GLY B . n 
B 1 109 SER 109 106 106 SER SER B . n 
B 1 110 ILE 110 107 107 ILE ILE B . n 
B 1 111 VAL 111 108 108 VAL VAL B . n 
B 1 112 ALA 112 109 109 ALA ALA B . n 
B 1 113 MET 113 110 110 MET MET B . n 
B 1 114 HIS 114 111 111 HIS HIS B . n 
B 1 115 VAL 115 112 112 VAL VAL B . n 
B 1 116 LEU 116 113 113 LEU LEU B . n 
B 1 117 LYS 117 114 114 LYS LYS B . n 
B 1 118 ASP 118 115 115 ASP ASP B . n 
B 1 119 TYR 119 116 116 TYR TYR B . n 
B 1 120 PRO 120 117 117 PRO PRO B . n 
B 1 121 GLU 121 118 118 GLU GLU B . n 
B 1 122 VAL 122 119 119 VAL VAL B . n 
B 1 123 VAL 123 120 120 VAL VAL B . n 
B 1 124 LYS 124 121 121 LYS LYS B . n 
B 1 125 LYS 125 122 122 LYS LYS B . n 
B 1 126 ILE 126 123 123 ILE ILE B . n 
B 1 127 ALA 127 124 124 ALA ALA B . n 
B 1 128 PHE 128 125 125 PHE PHE B . n 
B 1 129 HIS 129 126 126 HIS HIS B . n 
B 1 130 GLU 130 127 127 GLU GLU B . n 
B 1 131 PRO 131 128 128 PRO PRO B . n 
B 1 132 PRO 132 129 129 PRO PRO B . n 
B 1 133 ILE 133 130 130 ILE ILE B . n 
B 1 134 ASN 134 131 131 ASN ASN B . n 
B 1 135 THR 135 132 132 THR THR B . n 
B 1 136 PHE 136 133 133 PHE PHE B . n 
B 1 137 LEU 137 134 134 LEU LEU B . n 
B 1 138 PRO 138 135 135 PRO PRO B . n 
B 1 139 ASP 139 136 136 ASP ASP B . n 
B 1 140 SER 140 137 137 SER SER B . n 
B 1 141 THR 141 138 138 THR THR B . n 
B 1 142 TYR 142 139 139 TYR TYR B . n 
B 1 143 TRP 143 140 140 TRP TRP B . n 
B 1 144 LYS 144 141 141 LYS LYS B . n 
B 1 145 ASP 145 142 142 ASP ASP B . n 
B 1 146 LYS 146 143 143 LYS LYS B . n 
B 1 147 ASN 147 144 144 ASN ASN B . n 
B 1 148 ASP 148 145 145 ASP ASP B . n 
B 1 149 ASP 149 146 146 ASP ASP B . n 
B 1 150 ILE 150 147 147 ILE ILE B . n 
B 1 151 VAL 151 148 148 VAL VAL B . n 
B 1 152 HIS 152 149 149 HIS HIS B . n 
B 1 153 GLN 153 150 150 GLN GLN B . n 
B 1 154 ILE 154 151 151 ILE ILE B . n 
B 1 155 LEU 155 152 152 LEU LEU B . n 
B 1 156 THR 156 153 153 THR THR B . n 
B 1 157 GLU 157 154 154 GLU GLU B . n 
B 1 158 GLY 158 155 155 GLY GLY B . n 
B 1 159 LEU 159 156 156 LEU LEU B . n 
B 1 160 GLU 160 157 157 GLU GLU B . n 
B 1 161 LYS 161 158 158 LYS LYS B . n 
B 1 162 GLY 162 159 159 GLY GLY B . n 
B 1 163 MET 163 160 160 MET MET B . n 
B 1 164 LYS 164 161 161 LYS LYS B . n 
B 1 165 THR 165 162 162 THR THR B . n 
B 1 166 PHE 166 163 163 PHE PHE B . n 
B 1 167 GLY 167 164 164 GLY GLY B . n 
B 1 168 GLU 168 165 165 GLU GLU B . n 
B 1 169 THR 169 166 166 THR THR B . n 
B 1 170 LEU 170 167 167 LEU LEU B . n 
B 1 171 ASN 171 168 168 ASN ASN B . n 
B 1 172 ILE 172 169 169 ILE ILE B . n 
B 1 173 ALA 173 170 170 ALA ALA B . n 
B 1 174 PRO 174 171 171 PRO PRO B . n 
B 1 175 ILE 175 172 172 ILE ILE B . n 
B 1 176 ASP 176 173 173 ASP ASP B . n 
B 1 177 ALA 177 174 174 ALA ALA B . n 
B 1 178 LYS 178 175 175 LYS LYS B . n 
B 1 179 MET 179 176 176 MET MET B . n 
B 1 180 MET 180 177 177 MET MET B . n 
B 1 181 SER 181 178 178 SER SER B . n 
B 1 182 GLN 182 179 179 GLN GLN B . n 
B 1 183 PRO 183 180 180 PRO PRO B . n 
B 1 184 ALA 184 181 181 ALA ALA B . n 
B 1 185 ASP 185 182 182 ASP ASP B . n 
B 1 186 THR 186 183 183 THR THR B . n 
B 1 187 GLU 187 184 184 GLU GLU B . n 
B 1 188 GLU 188 185 185 GLU GLU B . n 
B 1 189 GLY 189 186 186 GLY GLY B . n 
B 1 190 ARG 190 187 187 ARG ARG B . n 
B 1 191 ILE 191 188 188 ILE ILE B . n 
B 1 192 GLU 192 189 189 GLU GLU B . n 
B 1 193 GLN 193 190 190 GLN GLN B . n 
B 1 194 TYR 194 191 191 TYR TYR B . n 
B 1 195 LYS 195 192 192 LYS LYS B . n 
B 1 196 ARG 196 193 193 ARG ARG B . n 
B 1 197 THR 197 194 194 THR THR B . n 
B 1 198 MET 198 195 195 MET MET B . n 
B 1 199 PHE 199 196 196 PHE PHE B . n 
B 1 200 TRP 200 197 197 TRP TRP B . n 
B 1 201 LEU 201 198 198 LEU LEU B . n 
B 1 202 GLU 202 199 199 GLU GLU B . n 
B 1 203 PHE 203 200 200 PHE PHE B . n 
B 1 204 GLU 204 201 201 GLU GLU B . n 
B 1 205 ILE 205 202 202 ILE ILE B . n 
B 1 206 ARG 206 203 203 ARG ARG B . n 
B 1 207 GLN 207 204 204 GLN GLN B . n 
B 1 208 TYR 208 205 205 TYR TYR B . n 
B 1 209 THR 209 206 206 THR THR B . n 
B 1 210 HIS 210 207 207 HIS HIS B . n 
B 1 211 SER 211 208 208 SER SER B . n 
B 1 212 ASN 212 209 209 ASN ASN B . n 
B 1 213 ILE 213 210 210 ILE ILE B . n 
B 1 214 THR 214 211 211 THR THR B . n 
B 1 215 LEU 215 212 212 LEU LEU B . n 
B 1 216 ASP 216 213 213 ASP ASP B . n 
B 1 217 ASP 217 214 214 ASP ASP B . n 
B 1 218 PHE 218 215 215 PHE PHE B . n 
B 1 219 THR 219 216 216 THR THR B . n 
B 1 220 LYS 220 217 217 LYS LYS B . n 
B 1 221 TYR 221 218 218 TYR TYR B . n 
B 1 222 SER 222 219 219 SER SER B . n 
B 1 223 ASP 223 220 220 ASP ASP B . n 
B 1 224 LYS 224 221 221 LYS LYS B . n 
B 1 225 ILE 225 222 222 ILE ILE B . n 
B 1 226 THR 226 223 223 THR THR B . n 
B 1 227 LEU 227 224 224 LEU LEU B . n 
B 1 228 LEU 228 225 225 LEU LEU B . n 
B 1 229 ASN 229 226 226 ASN ASN B . n 
B 1 230 GLY 230 227 227 GLY GLY B . n 
B 1 231 THR 231 228 228 THR THR B . n 
B 1 232 ASP 232 229 229 ASP ASP B . n 
B 1 233 SER 233 230 230 SER SER B . n 
B 1 234 ARG 234 231 231 ARG ARG B . n 
B 1 235 GLY 235 232 232 GLY GLY B . n 
B 1 236 SER 236 233 233 SER SER B . n 
B 1 237 PHE 237 234 234 PHE PHE B . n 
B 1 238 PRO 238 235 235 PRO PRO B . n 
B 1 239 GLN 239 236 236 GLN GLN B . n 
B 1 240 ASP 240 237 237 ASP ASP B . n 
B 1 241 VAL 241 238 238 VAL VAL B . n 
B 1 242 ASN 242 239 239 ASN ASN B . n 
B 1 243 PHE 243 240 240 PHE PHE B . n 
B 1 244 TYR 244 241 241 TYR TYR B . n 
B 1 245 ILE 245 242 242 ILE ILE B . n 
B 1 246 ASN 246 243 243 ASN ASN B . n 
B 1 247 LYS 247 244 244 LYS LYS B . n 
B 1 248 GLU 248 245 245 GLU GLU B . n 
B 1 249 THR 249 246 246 THR THR B . n 
B 1 250 GLY 250 247 247 GLY GLY B . n 
B 1 251 ILE 251 248 248 ILE ILE B . n 
B 1 252 PRO 252 249 249 PRO PRO B . n 
B 1 253 ILE 253 250 250 ILE ILE B . n 
B 1 254 VAL 254 251 251 VAL VAL B . n 
B 1 255 ASP 255 252 252 ASP ASP B . n 
B 1 256 ILE 256 253 253 ILE ILE B . n 
B 1 257 PRO 257 254 254 PRO PRO B . n 
B 1 258 GLY 258 255 255 GLY GLY B . n 
B 1 259 GLY 259 256 256 GLY GLY B . n 
B 1 260 HIS 260 257 257 HIS HIS B . n 
B 1 261 LEU 261 258 258 LEU LEU B . n 
B 1 262 GLY 262 259 259 GLY GLY B . n 
B 1 263 TYR 263 260 260 TYR TYR B . n 
B 1 264 ILE 264 261 261 ILE ILE B . n 
B 1 265 GLN 265 262 262 GLN GLN B . n 
B 1 266 LYS 266 263 263 LYS LYS B . n 
B 1 267 PRO 267 264 264 PRO PRO B . n 
B 1 268 GLU 268 265 265 GLU GLU B . n 
B 1 269 GLY 269 266 266 GLY GLY B . n 
B 1 270 PHE 270 267 267 PHE PHE B . n 
B 1 271 ALA 271 268 268 ALA ALA B . n 
B 1 272 ASP 272 269 269 ASP ASP B . n 
B 1 273 VAL 273 270 270 VAL VAL B . n 
B 1 274 LEU 274 271 271 LEU LEU B . n 
B 1 275 LEU 275 272 272 LEU LEU B . n 
B 1 276 ASN 276 273 273 ASN ASN B . n 
B 1 277 MET 277 274 274 MET MET B . n 
B 1 278 TRP 278 275 275 TRP TRP B . n 
B 1 279 GLY 279 276 276 GLY GLY B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BA1 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BA1 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1BA1 1   301 301 A1BA1 OX5 A . 
D 3 MG    1   302 1   MG    MG  A . 
E 3 MG    1   303 3   MG    MG  A . 
F 2 A1BA1 1   301 301 A1BA1 OX5 B . 
G 3 MG    1   302 2   MG    MG  B . 
H 3 MG    1   303 4   MG    MG  B . 
I 4 HOH   1   401 352 HOH   HOH A . 
I 4 HOH   2   402 86  HOH   HOH A . 
I 4 HOH   3   403 291 HOH   HOH A . 
I 4 HOH   4   404 57  HOH   HOH A . 
I 4 HOH   5   405 255 HOH   HOH A . 
I 4 HOH   6   406 300 HOH   HOH A . 
I 4 HOH   7   407 87  HOH   HOH A . 
I 4 HOH   8   408 195 HOH   HOH A . 
I 4 HOH   9   409 119 HOH   HOH A . 
I 4 HOH   10  410 138 HOH   HOH A . 
I 4 HOH   11  411 124 HOH   HOH A . 
I 4 HOH   12  412 358 HOH   HOH A . 
I 4 HOH   13  413 322 HOH   HOH A . 
I 4 HOH   14  414 357 HOH   HOH A . 
I 4 HOH   15  415 331 HOH   HOH A . 
I 4 HOH   16  416 153 HOH   HOH A . 
I 4 HOH   17  417 65  HOH   HOH A . 
I 4 HOH   18  418 253 HOH   HOH A . 
I 4 HOH   19  419 134 HOH   HOH A . 
I 4 HOH   20  420 147 HOH   HOH A . 
I 4 HOH   21  421 214 HOH   HOH A . 
I 4 HOH   22  422 198 HOH   HOH A . 
I 4 HOH   23  423 99  HOH   HOH A . 
I 4 HOH   24  424 64  HOH   HOH A . 
I 4 HOH   25  425 258 HOH   HOH A . 
I 4 HOH   26  426 156 HOH   HOH A . 
I 4 HOH   27  427 63  HOH   HOH A . 
I 4 HOH   28  428 4   HOH   HOH A . 
I 4 HOH   29  429 44  HOH   HOH A . 
I 4 HOH   30  430 46  HOH   HOH A . 
I 4 HOH   31  431 2   HOH   HOH A . 
I 4 HOH   32  432 135 HOH   HOH A . 
I 4 HOH   33  433 21  HOH   HOH A . 
I 4 HOH   34  434 274 HOH   HOH A . 
I 4 HOH   35  435 158 HOH   HOH A . 
I 4 HOH   36  436 272 HOH   HOH A . 
I 4 HOH   37  437 93  HOH   HOH A . 
I 4 HOH   38  438 85  HOH   HOH A . 
I 4 HOH   39  439 137 HOH   HOH A . 
I 4 HOH   40  440 361 HOH   HOH A . 
I 4 HOH   41  441 211 HOH   HOH A . 
I 4 HOH   42  442 172 HOH   HOH A . 
I 4 HOH   43  443 29  HOH   HOH A . 
I 4 HOH   44  444 128 HOH   HOH A . 
I 4 HOH   45  445 9   HOH   HOH A . 
I 4 HOH   46  446 32  HOH   HOH A . 
I 4 HOH   47  447 91  HOH   HOH A . 
I 4 HOH   48  448 66  HOH   HOH A . 
I 4 HOH   49  449 350 HOH   HOH A . 
I 4 HOH   50  450 6   HOH   HOH A . 
I 4 HOH   51  451 155 HOH   HOH A . 
I 4 HOH   52  452 122 HOH   HOH A . 
I 4 HOH   53  453 250 HOH   HOH A . 
I 4 HOH   54  454 188 HOH   HOH A . 
I 4 HOH   55  455 236 HOH   HOH A . 
I 4 HOH   56  456 115 HOH   HOH A . 
I 4 HOH   57  457 121 HOH   HOH A . 
I 4 HOH   58  458 282 HOH   HOH A . 
I 4 HOH   59  459 33  HOH   HOH A . 
I 4 HOH   60  460 36  HOH   HOH A . 
I 4 HOH   61  461 206 HOH   HOH A . 
I 4 HOH   62  462 50  HOH   HOH A . 
I 4 HOH   63  463 48  HOH   HOH A . 
I 4 HOH   64  464 89  HOH   HOH A . 
I 4 HOH   65  465 95  HOH   HOH A . 
I 4 HOH   66  466 42  HOH   HOH A . 
I 4 HOH   67  467 203 HOH   HOH A . 
I 4 HOH   68  468 162 HOH   HOH A . 
I 4 HOH   69  469 254 HOH   HOH A . 
I 4 HOH   70  470 277 HOH   HOH A . 
I 4 HOH   71  471 20  HOH   HOH A . 
I 4 HOH   72  472 73  HOH   HOH A . 
I 4 HOH   73  473 332 HOH   HOH A . 
I 4 HOH   74  474 82  HOH   HOH A . 
I 4 HOH   75  475 116 HOH   HOH A . 
I 4 HOH   76  476 234 HOH   HOH A . 
I 4 HOH   77  477 10  HOH   HOH A . 
I 4 HOH   78  478 104 HOH   HOH A . 
I 4 HOH   79  479 83  HOH   HOH A . 
I 4 HOH   80  480 185 HOH   HOH A . 
I 4 HOH   81  481 302 HOH   HOH A . 
I 4 HOH   82  482 54  HOH   HOH A . 
I 4 HOH   83  483 61  HOH   HOH A . 
I 4 HOH   84  484 296 HOH   HOH A . 
I 4 HOH   85  485 69  HOH   HOH A . 
I 4 HOH   86  486 146 HOH   HOH A . 
I 4 HOH   87  487 328 HOH   HOH A . 
I 4 HOH   88  488 18  HOH   HOH A . 
I 4 HOH   89  489 212 HOH   HOH A . 
I 4 HOH   90  490 176 HOH   HOH A . 
I 4 HOH   91  491 111 HOH   HOH A . 
I 4 HOH   92  492 173 HOH   HOH A . 
I 4 HOH   93  493 118 HOH   HOH A . 
I 4 HOH   94  494 279 HOH   HOH A . 
I 4 HOH   95  495 232 HOH   HOH A . 
I 4 HOH   96  496 219 HOH   HOH A . 
I 4 HOH   97  497 102 HOH   HOH A . 
I 4 HOH   98  498 233 HOH   HOH A . 
I 4 HOH   99  499 356 HOH   HOH A . 
I 4 HOH   100 500 117 HOH   HOH A . 
I 4 HOH   101 501 316 HOH   HOH A . 
I 4 HOH   102 502 148 HOH   HOH A . 
I 4 HOH   103 503 179 HOH   HOH A . 
I 4 HOH   104 504 230 HOH   HOH A . 
I 4 HOH   105 505 37  HOH   HOH A . 
I 4 HOH   106 506 88  HOH   HOH A . 
I 4 HOH   107 507 183 HOH   HOH A . 
I 4 HOH   108 508 329 HOH   HOH A . 
I 4 HOH   109 509 22  HOH   HOH A . 
I 4 HOH   110 510 14  HOH   HOH A . 
I 4 HOH   111 511 35  HOH   HOH A . 
I 4 HOH   112 512 208 HOH   HOH A . 
I 4 HOH   113 513 267 HOH   HOH A . 
I 4 HOH   114 514 287 HOH   HOH A . 
I 4 HOH   115 515 77  HOH   HOH A . 
I 4 HOH   116 516 293 HOH   HOH A . 
I 4 HOH   117 517 81  HOH   HOH A . 
I 4 HOH   118 518 113 HOH   HOH A . 
I 4 HOH   119 519 221 HOH   HOH A . 
I 4 HOH   120 520 149 HOH   HOH A . 
I 4 HOH   121 521 178 HOH   HOH A . 
I 4 HOH   122 522 125 HOH   HOH A . 
I 4 HOH   123 523 100 HOH   HOH A . 
I 4 HOH   124 524 168 HOH   HOH A . 
I 4 HOH   125 525 41  HOH   HOH A . 
I 4 HOH   126 526 151 HOH   HOH A . 
I 4 HOH   127 527 196 HOH   HOH A . 
I 4 HOH   128 528 75  HOH   HOH A . 
I 4 HOH   129 529 344 HOH   HOH A . 
I 4 HOH   130 530 362 HOH   HOH A . 
I 4 HOH   131 531 349 HOH   HOH A . 
I 4 HOH   132 532 123 HOH   HOH A . 
I 4 HOH   133 533 56  HOH   HOH A . 
I 4 HOH   134 534 114 HOH   HOH A . 
I 4 HOH   135 535 323 HOH   HOH A . 
I 4 HOH   136 536 3   HOH   HOH A . 
I 4 HOH   137 537 261 HOH   HOH A . 
I 4 HOH   138 538 109 HOH   HOH A . 
I 4 HOH   139 539 343 HOH   HOH A . 
I 4 HOH   140 540 317 HOH   HOH A . 
I 4 HOH   141 541 265 HOH   HOH A . 
I 4 HOH   142 542 231 HOH   HOH A . 
I 4 HOH   143 543 17  HOH   HOH A . 
I 4 HOH   144 544 307 HOH   HOH A . 
I 4 HOH   145 545 238 HOH   HOH A . 
I 4 HOH   146 546 337 HOH   HOH A . 
I 4 HOH   147 547 346 HOH   HOH A . 
I 4 HOH   148 548 241 HOH   HOH A . 
I 4 HOH   149 549 247 HOH   HOH A . 
I 4 HOH   150 550 161 HOH   HOH A . 
I 4 HOH   151 551 276 HOH   HOH A . 
I 4 HOH   152 552 345 HOH   HOH A . 
I 4 HOH   153 553 311 HOH   HOH A . 
I 4 HOH   154 554 257 HOH   HOH A . 
I 4 HOH   155 555 110 HOH   HOH A . 
I 4 HOH   156 556 252 HOH   HOH A . 
I 4 HOH   157 557 227 HOH   HOH A . 
I 4 HOH   158 558 342 HOH   HOH A . 
I 4 HOH   159 559 243 HOH   HOH A . 
I 4 HOH   160 560 199 HOH   HOH A . 
I 4 HOH   161 561 159 HOH   HOH A . 
I 4 HOH   162 562 237 HOH   HOH A . 
I 4 HOH   163 563 297 HOH   HOH A . 
I 4 HOH   164 564 359 HOH   HOH A . 
I 4 HOH   165 565 226 HOH   HOH A . 
I 4 HOH   166 566 180 HOH   HOH A . 
I 4 HOH   167 567 223 HOH   HOH A . 
J 4 HOH   1   401 298 HOH   HOH B . 
J 4 HOH   2   402 191 HOH   HOH B . 
J 4 HOH   3   403 360 HOH   HOH B . 
J 4 HOH   4   404 270 HOH   HOH B . 
J 4 HOH   5   405 225 HOH   HOH B . 
J 4 HOH   6   406 251 HOH   HOH B . 
J 4 HOH   7   407 67  HOH   HOH B . 
J 4 HOH   8   408 273 HOH   HOH B . 
J 4 HOH   9   409 108 HOH   HOH B . 
J 4 HOH   10  410 38  HOH   HOH B . 
J 4 HOH   11  411 167 HOH   HOH B . 
J 4 HOH   12  412 106 HOH   HOH B . 
J 4 HOH   13  413 249 HOH   HOH B . 
J 4 HOH   14  414 52  HOH   HOH B . 
J 4 HOH   15  415 190 HOH   HOH B . 
J 4 HOH   16  416 169 HOH   HOH B . 
J 4 HOH   17  417 242 HOH   HOH B . 
J 4 HOH   18  418 224 HOH   HOH B . 
J 4 HOH   19  419 1   HOH   HOH B . 
J 4 HOH   20  420 101 HOH   HOH B . 
J 4 HOH   21  421 133 HOH   HOH B . 
J 4 HOH   22  422 266 HOH   HOH B . 
J 4 HOH   23  423 197 HOH   HOH B . 
J 4 HOH   24  424 235 HOH   HOH B . 
J 4 HOH   25  425 192 HOH   HOH B . 
J 4 HOH   26  426 80  HOH   HOH B . 
J 4 HOH   27  427 78  HOH   HOH B . 
J 4 HOH   28  428 16  HOH   HOH B . 
J 4 HOH   29  429 260 HOH   HOH B . 
J 4 HOH   30  430 25  HOH   HOH B . 
J 4 HOH   31  431 47  HOH   HOH B . 
J 4 HOH   32  432 130 HOH   HOH B . 
J 4 HOH   33  433 144 HOH   HOH B . 
J 4 HOH   34  434 353 HOH   HOH B . 
J 4 HOH   35  435 145 HOH   HOH B . 
J 4 HOH   36  436 90  HOH   HOH B . 
J 4 HOH   37  437 24  HOH   HOH B . 
J 4 HOH   38  438 186 HOH   HOH B . 
J 4 HOH   39  439 45  HOH   HOH B . 
J 4 HOH   40  440 59  HOH   HOH B . 
J 4 HOH   41  441 194 HOH   HOH B . 
J 4 HOH   42  442 31  HOH   HOH B . 
J 4 HOH   43  443 70  HOH   HOH B . 
J 4 HOH   44  444 5   HOH   HOH B . 
J 4 HOH   45  445 325 HOH   HOH B . 
J 4 HOH   46  446 220 HOH   HOH B . 
J 4 HOH   47  447 23  HOH   HOH B . 
J 4 HOH   48  448 94  HOH   HOH B . 
J 4 HOH   49  449 27  HOH   HOH B . 
J 4 HOH   50  450 76  HOH   HOH B . 
J 4 HOH   51  451 8   HOH   HOH B . 
J 4 HOH   52  452 181 HOH   HOH B . 
J 4 HOH   53  453 74  HOH   HOH B . 
J 4 HOH   54  454 209 HOH   HOH B . 
J 4 HOH   55  455 142 HOH   HOH B . 
J 4 HOH   56  456 12  HOH   HOH B . 
J 4 HOH   57  457 275 HOH   HOH B . 
J 4 HOH   58  458 326 HOH   HOH B . 
J 4 HOH   59  459 259 HOH   HOH B . 
J 4 HOH   60  460 97  HOH   HOH B . 
J 4 HOH   61  461 107 HOH   HOH B . 
J 4 HOH   62  462 40  HOH   HOH B . 
J 4 HOH   63  463 127 HOH   HOH B . 
J 4 HOH   64  464 177 HOH   HOH B . 
J 4 HOH   65  465 141 HOH   HOH B . 
J 4 HOH   66  466 39  HOH   HOH B . 
J 4 HOH   67  467 334 HOH   HOH B . 
J 4 HOH   68  468 13  HOH   HOH B . 
J 4 HOH   69  469 187 HOH   HOH B . 
J 4 HOH   70  470 30  HOH   HOH B . 
J 4 HOH   71  471 84  HOH   HOH B . 
J 4 HOH   72  472 271 HOH   HOH B . 
J 4 HOH   73  473 98  HOH   HOH B . 
J 4 HOH   74  474 292 HOH   HOH B . 
J 4 HOH   75  475 11  HOH   HOH B . 
J 4 HOH   76  476 295 HOH   HOH B . 
J 4 HOH   77  477 215 HOH   HOH B . 
J 4 HOH   78  478 281 HOH   HOH B . 
J 4 HOH   79  479 19  HOH   HOH B . 
J 4 HOH   80  480 335 HOH   HOH B . 
J 4 HOH   81  481 143 HOH   HOH B . 
J 4 HOH   82  482 72  HOH   HOH B . 
J 4 HOH   83  483 96  HOH   HOH B . 
J 4 HOH   84  484 175 HOH   HOH B . 
J 4 HOH   85  485 289 HOH   HOH B . 
J 4 HOH   86  486 264 HOH   HOH B . 
J 4 HOH   87  487 126 HOH   HOH B . 
J 4 HOH   88  488 327 HOH   HOH B . 
J 4 HOH   89  489 28  HOH   HOH B . 
J 4 HOH   90  490 304 HOH   HOH B . 
J 4 HOH   91  491 184 HOH   HOH B . 
J 4 HOH   92  492 318 HOH   HOH B . 
J 4 HOH   93  493 269 HOH   HOH B . 
J 4 HOH   94  494 309 HOH   HOH B . 
J 4 HOH   95  495 324 HOH   HOH B . 
J 4 HOH   96  496 92  HOH   HOH B . 
J 4 HOH   97  497 201 HOH   HOH B . 
J 4 HOH   98  498 60  HOH   HOH B . 
J 4 HOH   99  499 129 HOH   HOH B . 
J 4 HOH   100 500 154 HOH   HOH B . 
J 4 HOH   101 501 26  HOH   HOH B . 
J 4 HOH   102 502 120 HOH   HOH B . 
J 4 HOH   103 503 139 HOH   HOH B . 
J 4 HOH   104 504 205 HOH   HOH B . 
J 4 HOH   105 505 49  HOH   HOH B . 
J 4 HOH   106 506 222 HOH   HOH B . 
J 4 HOH   107 507 170 HOH   HOH B . 
J 4 HOH   108 508 140 HOH   HOH B . 
J 4 HOH   109 509 306 HOH   HOH B . 
J 4 HOH   110 510 338 HOH   HOH B . 
J 4 HOH   111 511 354 HOH   HOH B . 
J 4 HOH   112 512 268 HOH   HOH B . 
J 4 HOH   113 513 68  HOH   HOH B . 
J 4 HOH   114 514 163 HOH   HOH B . 
J 4 HOH   115 515 105 HOH   HOH B . 
J 4 HOH   116 516 207 HOH   HOH B . 
J 4 HOH   117 517 43  HOH   HOH B . 
J 4 HOH   118 518 299 HOH   HOH B . 
J 4 HOH   119 519 204 HOH   HOH B . 
J 4 HOH   120 520 263 HOH   HOH B . 
J 4 HOH   121 521 218 HOH   HOH B . 
J 4 HOH   122 522 7   HOH   HOH B . 
J 4 HOH   123 523 286 HOH   HOH B . 
J 4 HOH   124 524 53  HOH   HOH B . 
J 4 HOH   125 525 200 HOH   HOH B . 
J 4 HOH   126 526 210 HOH   HOH B . 
J 4 HOH   127 527 51  HOH   HOH B . 
J 4 HOH   128 528 333 HOH   HOH B . 
J 4 HOH   129 529 348 HOH   HOH B . 
J 4 HOH   130 530 193 HOH   HOH B . 
J 4 HOH   131 531 136 HOH   HOH B . 
J 4 HOH   132 532 131 HOH   HOH B . 
J 4 HOH   133 533 285 HOH   HOH B . 
J 4 HOH   134 534 164 HOH   HOH B . 
J 4 HOH   135 535 246 HOH   HOH B . 
J 4 HOH   136 536 245 HOH   HOH B . 
J 4 HOH   137 537 308 HOH   HOH B . 
J 4 HOH   138 538 165 HOH   HOH B . 
J 4 HOH   139 539 228 HOH   HOH B . 
J 4 HOH   140 540 152 HOH   HOH B . 
J 4 HOH   141 541 216 HOH   HOH B . 
J 4 HOH   142 542 336 HOH   HOH B . 
J 4 HOH   143 543 290 HOH   HOH B . 
J 4 HOH   144 544 189 HOH   HOH B . 
J 4 HOH   145 545 294 HOH   HOH B . 
J 4 HOH   146 546 280 HOH   HOH B . 
J 4 HOH   147 547 256 HOH   HOH B . 
J 4 HOH   148 548 340 HOH   HOH B . 
J 4 HOH   149 549 278 HOH   HOH B . 
J 4 HOH   150 550 132 HOH   HOH B . 
J 4 HOH   151 551 355 HOH   HOH B . 
J 4 HOH   152 552 166 HOH   HOH B . 
J 4 HOH   153 553 248 HOH   HOH B . 
J 4 HOH   154 554 160 HOH   HOH B . 
J 4 HOH   155 555 58  HOH   HOH B . 
J 4 HOH   156 556 171 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.8       2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? 2.8.3       4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.95 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DRO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.107 
_cell.length_a_esd                 ? 
_cell.length_b                     74.583 
_cell.length_b_esd                 ? 
_cell.length_c                     73.555 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9DRO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   9DRO 
_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             2.07 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.45 
_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              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;10 uL 15 mg/mL FphE (10 mM HEPES pH 7.5, 100 mM NaCl) were mixed with 4 uL Oxadiazolone-peptide-ligand (10 mM in DMSO) and incubated at 18C overnight. 0.15 uL FphE-ligand solution was mixed with 0.3 uL of reservoir solution. Sitting drop reservoir contained 25 uL of 180 mM Magnesium chloride, 100 mM MES pH 6.5, 22.5% PEG 2000 MME. Crystal was frozen in a solution of ~25% Ethylene glycol, 75% reservoir.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-02 
_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   0.954 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.954 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DRO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.54 
_reflns.d_resolution_low                               47.10 
_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                                     75123 
_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                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.01 
_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                                0.083 
_reflns.pdbx_Rpim_I_all                                0.032 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       513296 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.076 
_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                                    1.54 
_reflns_shell.d_res_low                                     1.57 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           23000 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3496 
_reflns_shell.percent_possible_obs                          94.1 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.6 
_reflns_shell.pdbx_chi_squared                              0.98 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               1.343 
_reflns_shell.pdbx_Rpim_I_all                               0.514 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.560 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.237 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DRO 
_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                            1.54 
_refine.ls_d_res_low                             39.82 
_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                     75083 
_refine.ls_number_reflns_R_free                  3604 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.63 
_refine.ls_percent_reflns_R_free                 4.80 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1568 
_refine.ls_R_factor_R_free                       0.1830 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1555 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 17.81 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.14 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4386 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_refine_hist.number_atoms_solvent             323 
_refine_hist.number_atoms_total               4741 
_refine_hist.d_res_high                       1.54 
_refine_hist.d_res_low                        39.82 
# 
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 ? 4577 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.067 ? 6222 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.019 ? 614  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.062 ? 673  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011 ? 825  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.54 1.56  . . 109 2529 92.00  . . . . 0.2664 . . . . . . . . . . . 0.2686 
'X-RAY DIFFRACTION' 1.56 1.58  . . 141 2766 100.00 . . . . 0.2299 . . . . . . . . . . . 0.2436 
'X-RAY DIFFRACTION' 1.58 1.60  . . 143 2731 100.00 . . . . 0.2252 . . . . . . . . . . . 0.2284 
'X-RAY DIFFRACTION' 1.60 1.63  . . 106 2806 100.00 . . . . 0.2016 . . . . . . . . . . . 0.2474 
'X-RAY DIFFRACTION' 1.63 1.65  . . 130 2720 100.00 . . . . 0.1973 . . . . . . . . . . . 0.2355 
'X-RAY DIFFRACTION' 1.65 1.68  . . 160 2725 100.00 . . . . 0.1978 . . . . . . . . . . . 0.2218 
'X-RAY DIFFRACTION' 1.68 1.71  . . 143 2726 100.00 . . . . 0.1965 . . . . . . . . . . . 0.2644 
'X-RAY DIFFRACTION' 1.71 1.74  . . 130 2797 100.00 . . . . 0.1951 . . . . . . . . . . . 0.2115 
'X-RAY DIFFRACTION' 1.74 1.77  . . 135 2740 100.00 . . . . 0.1910 . . . . . . . . . . . 0.2345 
'X-RAY DIFFRACTION' 1.77 1.81  . . 127 2758 100.00 . . . . 0.1956 . . . . . . . . . . . 0.2271 
'X-RAY DIFFRACTION' 1.81 1.85  . . 127 2754 100.00 . . . . 0.1815 . . . . . . . . . . . 0.2172 
'X-RAY DIFFRACTION' 1.85 1.89  . . 142 2759 100.00 . . . . 0.1586 . . . . . . . . . . . 0.2122 
'X-RAY DIFFRACTION' 1.89 1.94  . . 154 2756 100.00 . . . . 0.1585 . . . . . . . . . . . 0.1866 
'X-RAY DIFFRACTION' 1.94 1.99  . . 161 2703 100.00 . . . . 0.1476 . . . . . . . . . . . 0.1835 
'X-RAY DIFFRACTION' 1.99 2.05  . . 148 2779 100.00 . . . . 0.1500 . . . . . . . . . . . 0.1741 
'X-RAY DIFFRACTION' 2.05 2.12  . . 147 2723 100.00 . . . . 0.1480 . . . . . . . . . . . 0.1828 
'X-RAY DIFFRACTION' 2.12 2.19  . . 136 2757 100.00 . . . . 0.1523 . . . . . . . . . . . 0.1780 
'X-RAY DIFFRACTION' 2.19 2.28  . . 150 2735 100.00 . . . . 0.1470 . . . . . . . . . . . 0.1768 
'X-RAY DIFFRACTION' 2.28 2.38  . . 155 2771 100.00 . . . . 0.1405 . . . . . . . . . . . 0.1726 
'X-RAY DIFFRACTION' 2.38 2.51  . . 153 2736 100.00 . . . . 0.1494 . . . . . . . . . . . 0.1892 
'X-RAY DIFFRACTION' 2.51 2.67  . . 143 2750 100.00 . . . . 0.1500 . . . . . . . . . . . 0.1914 
'X-RAY DIFFRACTION' 2.67 2.87  . . 122 2780 100.00 . . . . 0.1531 . . . . . . . . . . . 0.2073 
'X-RAY DIFFRACTION' 2.87 3.16  . . 139 2787 100.00 . . . . 0.1554 . . . . . . . . . . . 0.1616 
'X-RAY DIFFRACTION' 3.16 3.62  . . 120 2799 100.00 . . . . 0.1529 . . . . . . . . . . . 0.1997 
'X-RAY DIFFRACTION' 3.62 4.56  . . 113 2785 99.00  . . . . 0.1299 . . . . . . . . . . . 0.1480 
'X-RAY DIFFRACTION' 4.56 39.82 . . 170 2807 100.00 . . . . 0.1566 . . . . . . . . . . . 0.1640 
# 
_struct.entry_id                     9DRO 
_struct.title                        
'FphE, Staphylococcus aureus fluorophosphonate-binding serine hydrolases E, Oxadiazolone-peptide bound' 
_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        9DRO 
_struct_keywords.text            
'FphE, Staphylococcus aureus, S. aureus, fluorophosphonate-binding, serine hydrolases, lipase, HYDROLASE, Oxadiazolone' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Y2518_STAA3 
_struct_ref.pdbx_db_accession          Q2FDS6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;METLELQGAKLRYHQVGQGPVLIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRDYGESELTEPLPDSASNPDSDYRVKR
DAQDIAELAKSLSDEPVYILGSSSGSIVAMHVLKDYPEVVKKIAFHEPPINTFLPDSTYWKDKNDDIVHQILTEGLEKGM
KTFGETLNIAPIDAKMMSQPADTEEGRIEQYKRTMFWLEFEIRQYTHSNITLDDFTKYSDKITLLNGTDSRGSFPQDVNF
YINKETGIPIVDIPGGHLGYIQKPEGFADVLLNMWG
;
_struct_ref.pdbx_align_begin           1 
# 
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 9DRO A 4 ? 279 ? Q2FDS6 1 ? 276 ? 1 276 
2 1 9DRO B 4 ? 279 ? Q2FDS6 1 ? 276 ? 1 276 
# 
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 9DRO GLY A 1 ? UNP Q2FDS6 ? ? 'expression tag' -2 1 
1 9DRO PRO A 2 ? UNP Q2FDS6 ? ? 'expression tag' -1 2 
1 9DRO GLY A 3 ? UNP Q2FDS6 ? ? 'expression tag' 0  3 
2 9DRO GLY B 1 ? UNP Q2FDS6 ? ? 'expression tag' -2 4 
2 9DRO PRO B 2 ? UNP Q2FDS6 ? ? 'expression tag' -1 5 
2 9DRO GLY B 3 ? UNP Q2FDS6 ? ? 'expression tag' 0  6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 13620 ? 
1 MORE         -106  ? 
1 'SSA (A^2)'  22670 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 34  ? ILE A 37  ? THR A 31  ILE A 34  5 ? 4  
HELX_P HELX_P2  AA2 PHE A 38  ? LYS A 46  ? PHE A 35  LYS A 43  1 ? 9  
HELX_P HELX_P3  AA3 PRO A 69  ? ASN A 74  ? PRO A 66  ASN A 71  5 ? 6  
HELX_P HELX_P4  AA4 ASP A 78  ? SER A 96  ? ASP A 75  SER A 93  1 ? 19 
HELX_P HELX_P5  AA5 SER A 106 ? TYR A 119 ? SER A 103 TYR A 116 1 ? 14 
HELX_P HELX_P6  AA6 ASP A 139 ? THR A 156 ? ASP A 136 THR A 153 1 ? 18 
HELX_P HELX_P7  AA7 THR A 156 ? LEU A 170 ? THR A 153 LEU A 167 1 ? 15 
HELX_P HELX_P8  AA8 ALA A 173 ? SER A 181 ? ALA A 170 SER A 178 1 ? 9  
HELX_P HELX_P9  AA9 THR A 186 ? GLU A 204 ? THR A 183 GLU A 201 1 ? 19 
HELX_P HELX_P10 AB1 GLU A 204 ? HIS A 210 ? GLU A 201 HIS A 207 1 ? 7  
HELX_P HELX_P11 AB2 THR A 214 ? TYR A 221 ? THR A 211 TYR A 218 1 ? 8  
HELX_P HELX_P12 AB3 SER A 236 ? GLY A 250 ? SER A 233 GLY A 247 1 ? 15 
HELX_P HELX_P13 AB4 LEU A 261 ? LYS A 266 ? LEU A 258 LYS A 263 1 ? 6  
HELX_P HELX_P14 AB5 LYS A 266 ? GLY A 279 ? LYS A 263 GLY A 276 1 ? 14 
HELX_P HELX_P15 AB6 THR B 34  ? ILE B 37  ? THR B 31  ILE B 34  5 ? 4  
HELX_P HELX_P16 AB7 PHE B 38  ? LYS B 46  ? PHE B 35  LYS B 43  1 ? 9  
HELX_P HELX_P17 AB8 PRO B 69  ? ASN B 74  ? PRO B 66  ASN B 71  5 ? 6  
HELX_P HELX_P18 AB9 ASP B 78  ? SER B 96  ? ASP B 75  SER B 93  1 ? 19 
HELX_P HELX_P19 AC1 SER B 106 ? TYR B 119 ? SER B 103 TYR B 116 1 ? 14 
HELX_P HELX_P20 AC2 ASP B 139 ? LEU B 155 ? ASP B 136 LEU B 152 1 ? 17 
HELX_P HELX_P21 AC3 THR B 156 ? LEU B 170 ? THR B 153 LEU B 167 1 ? 15 
HELX_P HELX_P22 AC4 ALA B 173 ? GLN B 182 ? ALA B 170 GLN B 179 1 ? 10 
HELX_P HELX_P23 AC5 THR B 186 ? GLU B 204 ? THR B 183 GLU B 201 1 ? 19 
HELX_P HELX_P24 AC6 GLU B 204 ? HIS B 210 ? GLU B 201 HIS B 207 1 ? 7  
HELX_P HELX_P25 AC7 THR B 214 ? LYS B 220 ? THR B 211 LYS B 217 1 ? 7  
HELX_P HELX_P26 AC8 TYR B 221 ? ASP B 223 ? TYR B 218 ASP B 220 5 ? 3  
HELX_P HELX_P27 AC9 SER B 236 ? GLY B 250 ? SER B 233 GLY B 247 1 ? 15 
HELX_P HELX_P28 AD1 LEU B 261 ? LYS B 266 ? LEU B 258 LYS B 263 1 ? 6  
HELX_P HELX_P29 AD2 LYS B 266 ? GLY B 279 ? LYS B 263 GLY B 276 1 ? 14 
# 
_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 none ? A SER 106 OG  ? ? ? 1_555 C A1BA1 .   C3 ? ? A SER 103 A A1BA1 301 1_555 ? ? ? ? ? ? ? 1.374 ? ? 
covale2  covale none ? B SER 106 OG  ? ? ? 1_555 F A1BA1 .   C3 ? ? B SER 103 B A1BA1 301 1_555 ? ? ? ? ? ? ? 1.380 ? ? 
metalc1  metalc ?    ? A GLN 86  OE1 ? ? ? 1_555 H MG    .   MG ? ? A GLN 83  B MG    303 1_655 ? ? ? ? ? ? ? 2.142 ? ? 
metalc2  metalc ?    ? A ASP 139 OD2 ? ? ? 1_555 E MG    .   MG ? ? A ASP 136 A MG    303 1_555 ? ? ? ? ? ? ? 2.202 ? ? 
metalc3  metalc ?    ? A ASN 276 OD1 ? ? ? 1_555 D MG    .   MG ? ? A ASN 273 A MG    302 1_555 ? ? ? ? ? ? ? 1.972 ? ? 
metalc4  metalc ?    ? D MG  .   MG  ? ? ? 1_555 I HOH   .   O  ? ? A MG  302 A HOH   466 1_555 ? ? ? ? ? ? ? 2.122 ? ? 
metalc5  metalc ?    ? D MG  .   MG  ? ? ? 1_555 I HOH   .   O  ? ? A MG  302 A HOH   533 1_555 ? ? ? ? ? ? ? 2.123 ? ? 
metalc6  metalc ?    ? D MG  .   MG  ? ? ? 1_555 J HOH   .   O  ? ? A MG  302 B HOH   431 1_454 ? ? ? ? ? ? ? 2.153 ? ? 
metalc7  metalc ?    ? D MG  .   MG  ? ? ? 1_555 J HOH   .   O  ? ? A MG  302 B HOH   458 1_454 ? ? ? ? ? ? ? 2.103 ? ? 
metalc8  metalc ?    ? D MG  .   MG  ? ? ? 1_555 J HOH   .   O  ? ? A MG  302 B HOH   488 1_454 ? ? ? ? ? ? ? 2.203 ? ? 
metalc9  metalc ?    ? E MG  .   MG  ? ? ? 1_555 I HOH   .   O  ? ? A MG  303 A HOH   414 2_445 ? ? ? ? ? ? ? 1.836 ? ? 
metalc10 metalc ?    ? E MG  .   MG  ? ? ? 1_555 I HOH   .   O  ? ? A MG  303 A HOH   451 1_555 ? ? ? ? ? ? ? 2.091 ? ? 
metalc11 metalc ?    ? E MG  .   MG  ? ? ? 2_455 B LYS   117 NZ ? ? A MG  303 B LYS   114 1_555 ? ? ? ? ? ? ? 2.798 ? ? 
metalc12 metalc ?    ? E MG  .   MG  ? ? ? 1_555 J HOH   .   O  ? ? A MG  303 B HOH   434 2_445 ? ? ? ? ? ? ? 2.020 ? ? 
metalc13 metalc ?    ? I HOH .   O   ? ? ? 1_455 H MG    .   MG ? ? A HOH 401 B MG    303 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
metalc14 metalc ?    ? I HOH .   O   ? ? ? 1_455 H MG    .   MG ? ? A HOH 440 B MG    303 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc15 metalc ?    ? I HOH .   O   ? ? ? 1_455 G MG    .   MG ? ? A HOH 456 B MG    302 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc16 metalc ?    ? I HOH .   O   ? ? ? 1_455 G MG    .   MG ? ? A HOH 487 B MG    302 1_555 ? ? ? ? ? ? ? 2.145 ? ? 
metalc17 metalc ?    ? I HOH .   O   ? ? ? 1_455 G MG    .   MG ? ? A HOH 508 B MG    302 1_555 ? ? ? ? ? ? ? 2.090 ? ? 
metalc18 metalc ?    ? I HOH .   O   ? ? ? 1_455 H MG    .   MG ? ? A HOH 530 B MG    303 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc19 metalc ?    ? B ASP 149 OD1 ? ? ? 1_555 H MG    .   MG ? ? B ASP 146 B MG    303 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc20 metalc ?    ? B HIS 152 NE2 ? ? ? 1_555 G MG    .   MG ? ? B HIS 149 B MG    302 1_555 ? ? ? ? ? ? ? 2.106 ? ? 
metalc21 metalc ?    ? G MG  .   MG  ? ? ? 1_555 J HOH   .   O  ? ? B MG  302 B HOH   402 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc22 metalc ?    ? G MG  .   MG  ? ? ? 1_555 J HOH   .   O  ? ? B MG  302 B HOH   541 1_555 ? ? ? ? ? ? ? 1.982 ? ? 
metalc23 metalc ?    ? H MG  .   MG  ? ? ? 1_555 J HOH   .   O  ? ? B MG  303 B HOH   417 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE1 ? A GLN 86  ? A GLN 83  ? 1_555 MG ? H MG . ? B MG 303 ? 1_655 O   ? I HOH .   ? A HOH 401 ? 1_455 55.7  ? 
2  OE1 ? A GLN 86  ? A GLN 83  ? 1_555 MG ? H MG . ? B MG 303 ? 1_655 O   ? I HOH .   ? A HOH 440 ? 1_455 57.9  ? 
3  O   ? I HOH .   ? A HOH 401 ? 1_455 MG ? H MG . ? B MG 303 ? 1_655 O   ? I HOH .   ? A HOH 440 ? 1_455 2.3   ? 
4  OE1 ? A GLN 86  ? A GLN 83  ? 1_555 MG ? H MG . ? B MG 303 ? 1_655 O   ? I HOH .   ? A HOH 530 ? 1_455 57.5  ? 
5  O   ? I HOH .   ? A HOH 401 ? 1_455 MG ? H MG . ? B MG 303 ? 1_655 O   ? I HOH .   ? A HOH 530 ? 1_455 2.7   ? 
6  O   ? I HOH .   ? A HOH 440 ? 1_455 MG ? H MG . ? B MG 303 ? 1_655 O   ? I HOH .   ? A HOH 530 ? 1_455 2.7   ? 
7  OE1 ? A GLN 86  ? A GLN 83  ? 1_555 MG ? H MG . ? B MG 303 ? 1_655 OD1 ? B ASP 149 ? B ASP 146 ? 1_555 59.3  ? 
8  O   ? I HOH .   ? A HOH 401 ? 1_455 MG ? H MG . ? B MG 303 ? 1_655 OD1 ? B ASP 149 ? B ASP 146 ? 1_555 3.8   ? 
9  O   ? I HOH .   ? A HOH 440 ? 1_455 MG ? H MG . ? B MG 303 ? 1_655 OD1 ? B ASP 149 ? B ASP 146 ? 1_555 1.6   ? 
10 O   ? I HOH .   ? A HOH 530 ? 1_455 MG ? H MG . ? B MG 303 ? 1_655 OD1 ? B ASP 149 ? B ASP 146 ? 1_555 4.0   ? 
11 OE1 ? A GLN 86  ? A GLN 83  ? 1_555 MG ? H MG . ? B MG 303 ? 1_655 O   ? J HOH .   ? B HOH 417 ? 1_555 56.7  ? 
12 O   ? I HOH .   ? A HOH 401 ? 1_455 MG ? H MG . ? B MG 303 ? 1_655 O   ? J HOH .   ? B HOH 417 ? 1_555 3.1   ? 
13 O   ? I HOH .   ? A HOH 440 ? 1_455 MG ? H MG . ? B MG 303 ? 1_655 O   ? J HOH .   ? B HOH 417 ? 1_555 2.6   ? 
14 O   ? I HOH .   ? A HOH 530 ? 1_455 MG ? H MG . ? B MG 303 ? 1_655 O   ? J HOH .   ? B HOH 417 ? 1_555 5.0   ? 
15 OD1 ? B ASP 149 ? B ASP 146 ? 1_555 MG ? H MG . ? B MG 303 ? 1_655 O   ? J HOH .   ? B HOH 417 ? 1_555 2.9   ? 
16 OD2 ? A ASP 139 ? A ASP 136 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? I HOH .   ? A HOH 414 ? 2_445 113.3 ? 
17 OD2 ? A ASP 139 ? A ASP 136 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? I HOH .   ? A HOH 451 ? 1_555 79.0  ? 
18 O   ? I HOH .   ? A HOH 414 ? 2_445 MG ? E MG . ? A MG 303 ? 1_555 O   ? I HOH .   ? A HOH 451 ? 1_555 102.5 ? 
19 OD2 ? A ASP 139 ? A ASP 136 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 NZ  ? B LYS 117 ? B LYS 114 ? 1_555 73.7  ? 
20 O   ? I HOH .   ? A HOH 414 ? 2_445 MG ? E MG . ? A MG 303 ? 1_555 NZ  ? B LYS 117 ? B LYS 114 ? 1_555 43.1  ? 
21 O   ? I HOH .   ? A HOH 451 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 NZ  ? B LYS 117 ? B LYS 114 ? 1_555 78.9  ? 
22 OD2 ? A ASP 139 ? A ASP 136 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? J HOH .   ? B HOH 434 ? 2_445 162.2 ? 
23 O   ? I HOH .   ? A HOH 414 ? 2_445 MG ? E MG . ? A MG 303 ? 1_555 O   ? J HOH .   ? B HOH 434 ? 2_445 73.4  ? 
24 O   ? I HOH .   ? A HOH 451 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? J HOH .   ? B HOH 434 ? 2_445 83.4  ? 
25 NZ  ? B LYS 117 ? B LYS 114 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? J HOH .   ? B HOH 434 ? 2_445 105.9 ? 
26 OD1 ? A ASN 276 ? A ASN 273 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 466 ? 1_555 85.4  ? 
27 OD1 ? A ASN 276 ? A ASN 273 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 533 ? 1_555 97.4  ? 
28 O   ? I HOH .   ? A HOH 466 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 533 ? 1_555 86.9  ? 
29 OD1 ? A ASN 276 ? A ASN 273 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? J HOH .   ? B HOH 431 ? 1_454 92.5  ? 
30 O   ? I HOH .   ? A HOH 466 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? J HOH .   ? B HOH 431 ? 1_454 86.9  ? 
31 O   ? I HOH .   ? A HOH 533 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? J HOH .   ? B HOH 431 ? 1_454 167.9 ? 
32 OD1 ? A ASN 276 ? A ASN 273 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? J HOH .   ? B HOH 458 ? 1_454 91.0  ? 
33 O   ? I HOH .   ? A HOH 466 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? J HOH .   ? B HOH 458 ? 1_454 176.0 ? 
34 O   ? I HOH .   ? A HOH 533 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? J HOH .   ? B HOH 458 ? 1_454 95.2  ? 
35 O   ? J HOH .   ? B HOH 431 ? 1_454 MG ? D MG . ? A MG 302 ? 1_555 O   ? J HOH .   ? B HOH 458 ? 1_454 91.7  ? 
36 OD1 ? A ASN 276 ? A ASN 273 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? J HOH .   ? B HOH 488 ? 1_454 176.9 ? 
37 O   ? I HOH .   ? A HOH 466 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? J HOH .   ? B HOH 488 ? 1_454 95.3  ? 
38 O   ? I HOH .   ? A HOH 533 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? J HOH .   ? B HOH 488 ? 1_454 85.7  ? 
39 O   ? J HOH .   ? B HOH 431 ? 1_454 MG ? D MG . ? A MG 302 ? 1_555 O   ? J HOH .   ? B HOH 488 ? 1_454 84.5  ? 
40 O   ? J HOH .   ? B HOH 458 ? 1_454 MG ? D MG . ? A MG 302 ? 1_555 O   ? J HOH .   ? B HOH 488 ? 1_454 88.3  ? 
41 O   ? I HOH .   ? A HOH 456 ? 1_455 MG ? G MG . ? B MG 302 ? 1_555 O   ? I HOH .   ? A HOH 487 ? 1_455 84.0  ? 
42 O   ? I HOH .   ? A HOH 456 ? 1_455 MG ? G MG . ? B MG 302 ? 1_555 O   ? I HOH .   ? A HOH 508 ? 1_455 83.5  ? 
43 O   ? I HOH .   ? A HOH 487 ? 1_455 MG ? G MG . ? B MG 302 ? 1_555 O   ? I HOH .   ? A HOH 508 ? 1_455 88.8  ? 
44 O   ? I HOH .   ? A HOH 456 ? 1_455 MG ? G MG . ? B MG 302 ? 1_555 NE2 ? B HIS 152 ? B HIS 149 ? 1_555 83.8  ? 
45 O   ? I HOH .   ? A HOH 487 ? 1_455 MG ? G MG . ? B MG 302 ? 1_555 NE2 ? B HIS 152 ? B HIS 149 ? 1_555 98.9  ? 
46 O   ? I HOH .   ? A HOH 508 ? 1_455 MG ? G MG . ? B MG 302 ? 1_555 NE2 ? B HIS 152 ? B HIS 149 ? 1_555 164.3 ? 
47 O   ? I HOH .   ? A HOH 456 ? 1_455 MG ? G MG . ? B MG 302 ? 1_555 O   ? J HOH .   ? B HOH 402 ? 1_555 90.6  ? 
48 O   ? I HOH .   ? A HOH 487 ? 1_455 MG ? G MG . ? B MG 302 ? 1_555 O   ? J HOH .   ? B HOH 402 ? 1_555 172.5 ? 
49 O   ? I HOH .   ? A HOH 508 ? 1_455 MG ? G MG . ? B MG 302 ? 1_555 O   ? J HOH .   ? B HOH 402 ? 1_555 85.5  ? 
50 NE2 ? B HIS 152 ? B HIS 149 ? 1_555 MG ? G MG . ? B MG 302 ? 1_555 O   ? J HOH .   ? B HOH 402 ? 1_555 85.6  ? 
51 O   ? I HOH .   ? A HOH 456 ? 1_455 MG ? G MG . ? B MG 302 ? 1_555 O   ? J HOH .   ? B HOH 541 ? 1_555 165.5 ? 
52 O   ? I HOH .   ? A HOH 487 ? 1_455 MG ? G MG . ? B MG 302 ? 1_555 O   ? J HOH .   ? B HOH 541 ? 1_555 89.8  ? 
53 O   ? I HOH .   ? A HOH 508 ? 1_455 MG ? G MG . ? B MG 302 ? 1_555 O   ? J HOH .   ? B HOH 541 ? 1_555 83.3  ? 
54 NE2 ? B HIS 152 ? B HIS 149 ? 1_555 MG ? G MG . ? B MG 302 ? 1_555 O   ? J HOH .   ? B HOH 541 ? 1_555 110.2 ? 
55 O   ? J HOH .   ? B HOH 402 ? 1_555 MG ? G MG . ? B MG 302 ? 1_555 O   ? J HOH .   ? B HOH 541 ? 1_555 94.3  ? 
# 
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 A1BA1 C . ? SER A 106 ? A1BA1 A 301 ? 1_555 SER A 103 ? 1_555 C3 OG SER 1 A1BA1 None 'Covalent chemical modification' 
2 A1BA1 F . ? SER B 106 ? A1BA1 B 301 ? 1_555 SER B 103 ? 1_555 C3 OG SER 1 A1BA1 None 'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
AA4 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA4 6 7 ? anti-parallel 
AA4 7 8 ? 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 GLU A 5   ? LEU A 9   ? GLU A 2   LEU A 6   
AA1 2 ALA A 12  ? GLY A 20  ? ALA A 9   GLY A 17  
AA1 3 GLU A 63  ? LEU A 64  ? GLU A 60  LEU A 61  
AA2 1 GLU A 5   ? LEU A 9   ? GLU A 2   LEU A 6   
AA2 2 ALA A 12  ? GLY A 20  ? ALA A 9   GLY A 17  
AA2 3 THR A 50  ? VAL A 54  ? THR A 47  VAL A 51  
AA2 4 VAL A 24  ? ILE A 28  ? VAL A 21  ILE A 25  
AA2 5 VAL A 100 ? SER A 105 ? VAL A 97  SER A 102 
AA2 6 VAL A 123 ? HIS A 129 ? VAL A 120 HIS A 126 
AA2 7 ILE B 225 ? GLY B 230 ? ILE B 222 GLY B 227 
AA2 8 ILE B 253 ? ILE B 256 ? ILE B 250 ILE B 253 
AA3 1 ILE A 253 ? ILE A 256 ? ILE A 250 ILE A 253 
AA3 2 ILE A 225 ? GLY A 230 ? ILE A 222 GLY A 227 
AA3 3 VAL B 123 ? HIS B 129 ? VAL B 120 HIS B 126 
AA3 4 VAL B 100 ? SER B 105 ? VAL B 97  SER B 102 
AA3 5 VAL B 24  ? ILE B 28  ? VAL B 21  ILE B 25  
AA3 6 THR B 50  ? VAL B 54  ? THR B 47  VAL B 51  
AA3 7 ALA B 12  ? GLY B 20  ? ALA B 9   GLY B 17  
AA3 8 GLU B 5   ? LEU B 9   ? GLU B 2   LEU B 6   
AA4 1 ILE A 253 ? ILE A 256 ? ILE A 250 ILE A 253 
AA4 2 ILE A 225 ? GLY A 230 ? ILE A 222 GLY A 227 
AA4 3 VAL B 123 ? HIS B 129 ? VAL B 120 HIS B 126 
AA4 4 VAL B 100 ? SER B 105 ? VAL B 97  SER B 102 
AA4 5 VAL B 24  ? ILE B 28  ? VAL B 21  ILE B 25  
AA4 6 THR B 50  ? VAL B 54  ? THR B 47  VAL B 51  
AA4 7 ALA B 12  ? GLY B 20  ? ALA B 9   GLY B 17  
AA4 8 GLU B 63  ? LEU B 64  ? GLU B 60  LEU B 61  
# 
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 LEU A 9   ? N LEU A 6   O ALA A 12  ? O ALA A 9   
AA1 2 3 N LYS A 13  ? N LYS A 10  O GLU A 63  ? O GLU A 60  
AA2 1 2 N LEU A 9   ? N LEU A 6   O ALA A 12  ? O ALA A 9   
AA2 2 3 N HIS A 17  ? N HIS A 14  O ALA A 53  ? O ALA A 50  
AA2 3 4 O VAL A 52  ? O VAL A 49  N PHE A 27  ? N PHE A 24  
AA2 4 5 N ILE A 26  ? N ILE A 23  O TYR A 101 ? O TYR A 98  
AA2 5 6 N VAL A 100 ? N VAL A 97  O LYS A 124 ? O LYS A 121 
AA2 6 7 N PHE A 128 ? N PHE A 125 O LEU B 228 ? O LEU B 225 
AA2 7 8 N LEU B 227 ? N LEU B 224 O VAL B 254 ? O VAL B 251 
AA3 1 2 O VAL A 254 ? O VAL A 251 N LEU A 227 ? N LEU A 224 
AA3 2 3 N LEU A 228 ? N LEU A 225 O PHE B 128 ? O PHE B 125 
AA3 3 4 O LYS B 124 ? O LYS B 121 N VAL B 100 ? N VAL B 97  
AA3 4 5 O TYR B 101 ? O TYR B 98  N ILE B 26  ? N ILE B 23  
AA3 5 6 N PHE B 27  ? N PHE B 24  O VAL B 52  ? O VAL B 49  
AA3 6 7 O ALA B 53  ? O ALA B 50  N HIS B 17  ? N HIS B 14  
AA3 7 8 O ALA B 12  ? O ALA B 9   N LEU B 9   ? N LEU B 6   
AA4 1 2 O VAL A 254 ? O VAL A 251 N LEU A 227 ? N LEU A 224 
AA4 2 3 N LEU A 228 ? N LEU A 225 O PHE B 128 ? O PHE B 125 
AA4 3 4 O LYS B 124 ? O LYS B 121 N VAL B 100 ? N VAL B 97  
AA4 4 5 O TYR B 101 ? O TYR B 98  N ILE B 26  ? N ILE B 23  
AA4 5 6 N PHE B 27  ? N PHE B 24  O VAL B 52  ? O VAL B 49  
AA4 6 7 O ALA B 53  ? O ALA B 50  N HIS B 17  ? N HIS B 14  
AA4 7 8 N LYS B 13  ? N LYS B 10  O GLU B 63  ? O GLU B 60  
# 
_pdbx_entry_details.entry_id                   9DRO 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OE1 A GLU   40  ? ? HZ3 A LYS 43  ? ? 1.54 
2  1 O   B HOH   479 ? ? O   B HOH 542 ? ? 1.75 
3  1 O   A HOH   477 ? ? O   A HOH 552 ? ? 1.77 
4  1 O   B HOH   426 ? ? O   B HOH 548 ? ? 1.78 
5  1 O   A HOH   526 ? ? O   A HOH 558 ? ? 1.81 
6  1 O   A HOH   561 ? ? O   B HOH 540 ? ? 2.00 
7  1 O   B HOH   459 ? ? O   B HOH 540 ? ? 2.01 
8  1 O   B HOH   413 ? ? O   B HOH 548 ? ? 2.01 
9  1 O   B HOH   519 ? ? O   B HOH 536 ? ? 2.03 
10 1 O   B HOH   429 ? ? O   B HOH 549 ? ? 2.03 
11 1 O   A HOH   473 ? ? O   B HOH 529 ? ? 2.07 
12 1 O3  B A1BA1 301 ? ? O   B HOH 401 ? ? 2.12 
13 1 O   A HOH   478 ? ? O   A HOH 552 ? ? 2.14 
14 1 O   A HOH   492 ? ? O   B HOH 529 ? ? 2.16 
15 1 O   B HOH   401 ? ? O   B HOH 518 ? ? 2.17 
16 1 O   A HOH   425 ? ? O   A HOH 535 ? ? 2.17 
17 1 O   B HOH   483 ? ? O   B HOH 542 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 494 ? ? 1_555 O B HOH 536 ? ? 2_444 2.04 
2 1 O A HOH 564 ? ? 1_555 O B HOH 536 ? ? 2_444 2.17 
# 
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 SER A 103 ? ? 61.85   -131.96 
2 1 GLU A 201 ? ? -124.53 -53.80  
3 1 SER B 103 ? ? 57.46   -131.78 
4 1 SER B 103 ? ? 60.23   -131.78 
5 1 LEU B 152 ? ? -75.47  -152.85 
6 1 THR B 153 ? ? 13.66   -56.53  
7 1 GLU B 201 ? ? -124.79 -51.00  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -1.7269  -9.6700  9.2221   0.1572 ? -0.0048 ? 0.0167  ? 0.1354 ? 0.0034  ? 0.1523 ? 1.2545 ? 
0.3161 ? 0.3651  ? 2.0921 ? -0.4212 ? 2.5050 ? 0.0112  ? 0.0348  ? 0.1585  ? 0.0681  ? -0.0494 ? -0.0262 ? -0.2510 ? -0.0300 ? 
0.0389  ? 
2 'X-RAY DIFFRACTION' ? refined -28.5617 -25.8112 -14.0525 0.6138 ? 0.0946  ? -0.0676 ? 0.3390 ? 0.0667  ? 0.5131 ? 5.1106 ? 
0.0141 ? 2.7491  ? 1.6984 ? -0.2128 ? 1.7407 ? 0.1156  ? -0.0178 ? -0.7264 ? 0.4487  ? -0.0889 ? -0.4692 ? 0.6538  ? 0.1207  ? 
-0.1291 ? 
3 'X-RAY DIFFRACTION' ? refined -33.7647 -13.4711 -24.5738 0.1636 ? 0.0262  ? 0.0269  ? 0.1257 ? 0.0080  ? 0.1827 ? 2.1432 ? 
0.2981 ? 0.4730  ? 1.3899 ? 0.8679  ? 2.7653 ? -0.0495 ? -0.1031 ? -0.1995 ? 0.0703  ? 0.0271  ? -0.0042 ? 0.2625  ? -0.0103 ? 
0.0334  ? 
4 'X-RAY DIFFRACTION' ? refined -25.5759 -7.0567  -24.0632 0.1442 ? 0.0228  ? -0.0039 ? 0.1332 ? -0.0186 ? 0.1589 ? 2.5756 ? 
0.1278 ? -0.2976 ? 1.1845 ? 0.7030  ? 2.3556 ? -0.1134 ? -0.0527 ? 0.0421  ? -0.0281 ? 0.1529  ? -0.0803 ? 0.0188  ? 0.2452  ? 
-0.0309 ? 
5 'X-RAY DIFFRACTION' ? refined -9.0183  -15.8985 16.3159  0.1863 ? -0.0148 ? 0.0336  ? 0.2342 ? -0.0133 ? 0.1906 ? 1.2533 ? 
0.6748 ? 0.7908  ? 1.7600 ? 0.1328  ? 3.2505 ? 0.0758  ? -0.2060 ? 0.1444  ? 0.2528  ? -0.0740 ? 0.1992  ? -0.0156 ? -0.5603 ? 
-0.0176 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 0 through 152 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 153 through 183 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 184 through 276 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 0 through 152 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 153 through 276 )
;
# 
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 -2 ? A GLY 1 
2 1 Y 1 A PRO -1 ? A PRO 2 
3 1 Y 1 B GLY -2 ? B GLY 1 
4 1 Y 1 B PRO -1 ? B PRO 2 
# 
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 
A1BA1 O1   O  N N 1   
A1BA1 C1   C  N N 2   
A1BA1 C2   C  N N 3   
A1BA1 C3   C  N N 4   
A1BA1 C4   C  Y N 5   
A1BA1 C5   C  Y N 6   
A1BA1 C6   C  Y N 7   
A1BA1 C7   C  Y N 8   
A1BA1 C8   C  Y N 9   
A1BA1 C9   C  Y N 10  
A1BA1 O2   O  N N 11  
A1BA1 N1   N  N N 12  
A1BA1 N2   N  N N 13  
A1BA1 O3   O  N N 14  
A1BA1 H3   H  N N 15  
A1BA1 H1   H  N N 16  
A1BA1 H2   H  N N 17  
A1BA1 H5   H  N N 18  
A1BA1 H6   H  N N 19  
A1BA1 H7   H  N N 20  
A1BA1 H8   H  N N 21  
A1BA1 H9   H  N N 22  
A1BA1 H10  H  N N 23  
A1BA1 H4   H  N N 24  
ALA   N    N  N N 25  
ALA   CA   C  N S 26  
ALA   C    C  N N 27  
ALA   O    O  N N 28  
ALA   CB   C  N N 29  
ALA   OXT  O  N N 30  
ALA   H    H  N N 31  
ALA   H2   H  N N 32  
ALA   HA   H  N N 33  
ALA   HB1  H  N N 34  
ALA   HB2  H  N N 35  
ALA   HB3  H  N N 36  
ALA   HXT  H  N N 37  
ARG   N    N  N N 38  
ARG   CA   C  N S 39  
ARG   C    C  N N 40  
ARG   O    O  N N 41  
ARG   CB   C  N N 42  
ARG   CG   C  N N 43  
ARG   CD   C  N N 44  
ARG   NE   N  N N 45  
ARG   CZ   C  N N 46  
ARG   NH1  N  N N 47  
ARG   NH2  N  N N 48  
ARG   OXT  O  N N 49  
ARG   H    H  N N 50  
ARG   H2   H  N N 51  
ARG   HA   H  N N 52  
ARG   HB2  H  N N 53  
ARG   HB3  H  N N 54  
ARG   HG2  H  N N 55  
ARG   HG3  H  N N 56  
ARG   HD2  H  N N 57  
ARG   HD3  H  N N 58  
ARG   HE   H  N N 59  
ARG   HH11 H  N N 60  
ARG   HH12 H  N N 61  
ARG   HH21 H  N N 62  
ARG   HH22 H  N N 63  
ARG   HXT  H  N N 64  
ASN   N    N  N N 65  
ASN   CA   C  N S 66  
ASN   C    C  N N 67  
ASN   O    O  N N 68  
ASN   CB   C  N N 69  
ASN   CG   C  N N 70  
ASN   OD1  O  N N 71  
ASN   ND2  N  N N 72  
ASN   OXT  O  N N 73  
ASN   H    H  N N 74  
ASN   H2   H  N N 75  
ASN   HA   H  N N 76  
ASN   HB2  H  N N 77  
ASN   HB3  H  N N 78  
ASN   HD21 H  N N 79  
ASN   HD22 H  N N 80  
ASN   HXT  H  N N 81  
ASP   N    N  N N 82  
ASP   CA   C  N S 83  
ASP   C    C  N N 84  
ASP   O    O  N N 85  
ASP   CB   C  N N 86  
ASP   CG   C  N N 87  
ASP   OD1  O  N N 88  
ASP   OD2  O  N N 89  
ASP   OXT  O  N N 90  
ASP   H    H  N N 91  
ASP   H2   H  N N 92  
ASP   HA   H  N N 93  
ASP   HB2  H  N N 94  
ASP   HB3  H  N N 95  
ASP   HD2  H  N N 96  
ASP   HXT  H  N N 97  
GLN   N    N  N N 98  
GLN   CA   C  N S 99  
GLN   C    C  N N 100 
GLN   O    O  N N 101 
GLN   CB   C  N N 102 
GLN   CG   C  N N 103 
GLN   CD   C  N N 104 
GLN   OE1  O  N N 105 
GLN   NE2  N  N N 106 
GLN   OXT  O  N N 107 
GLN   H    H  N N 108 
GLN   H2   H  N N 109 
GLN   HA   H  N N 110 
GLN   HB2  H  N N 111 
GLN   HB3  H  N N 112 
GLN   HG2  H  N N 113 
GLN   HG3  H  N N 114 
GLN   HE21 H  N N 115 
GLN   HE22 H  N N 116 
GLN   HXT  H  N N 117 
GLU   N    N  N N 118 
GLU   CA   C  N S 119 
GLU   C    C  N N 120 
GLU   O    O  N N 121 
GLU   CB   C  N N 122 
GLU   CG   C  N N 123 
GLU   CD   C  N N 124 
GLU   OE1  O  N N 125 
GLU   OE2  O  N N 126 
GLU   OXT  O  N N 127 
GLU   H    H  N N 128 
GLU   H2   H  N N 129 
GLU   HA   H  N N 130 
GLU   HB2  H  N N 131 
GLU   HB3  H  N N 132 
GLU   HG2  H  N N 133 
GLU   HG3  H  N N 134 
GLU   HE2  H  N N 135 
GLU   HXT  H  N N 136 
GLY   N    N  N N 137 
GLY   CA   C  N N 138 
GLY   C    C  N N 139 
GLY   O    O  N N 140 
GLY   OXT  O  N N 141 
GLY   H    H  N N 142 
GLY   H2   H  N N 143 
GLY   HA2  H  N N 144 
GLY   HA3  H  N N 145 
GLY   HXT  H  N N 146 
HIS   N    N  N N 147 
HIS   CA   C  N S 148 
HIS   C    C  N N 149 
HIS   O    O  N N 150 
HIS   CB   C  N N 151 
HIS   CG   C  Y N 152 
HIS   ND1  N  Y N 153 
HIS   CD2  C  Y N 154 
HIS   CE1  C  Y N 155 
HIS   NE2  N  Y N 156 
HIS   OXT  O  N N 157 
HIS   H    H  N N 158 
HIS   H2   H  N N 159 
HIS   HA   H  N N 160 
HIS   HB2  H  N N 161 
HIS   HB3  H  N N 162 
HIS   HD1  H  N N 163 
HIS   HD2  H  N N 164 
HIS   HE1  H  N N 165 
HIS   HE2  H  N N 166 
HIS   HXT  H  N N 167 
HOH   O    O  N N 168 
HOH   H1   H  N N 169 
HOH   H2   H  N N 170 
ILE   N    N  N N 171 
ILE   CA   C  N S 172 
ILE   C    C  N N 173 
ILE   O    O  N N 174 
ILE   CB   C  N S 175 
ILE   CG1  C  N N 176 
ILE   CG2  C  N N 177 
ILE   CD1  C  N N 178 
ILE   OXT  O  N N 179 
ILE   H    H  N N 180 
ILE   H2   H  N N 181 
ILE   HA   H  N N 182 
ILE   HB   H  N N 183 
ILE   HG12 H  N N 184 
ILE   HG13 H  N N 185 
ILE   HG21 H  N N 186 
ILE   HG22 H  N N 187 
ILE   HG23 H  N N 188 
ILE   HD11 H  N N 189 
ILE   HD12 H  N N 190 
ILE   HD13 H  N N 191 
ILE   HXT  H  N N 192 
LEU   N    N  N N 193 
LEU   CA   C  N S 194 
LEU   C    C  N N 195 
LEU   O    O  N N 196 
LEU   CB   C  N N 197 
LEU   CG   C  N N 198 
LEU   CD1  C  N N 199 
LEU   CD2  C  N N 200 
LEU   OXT  O  N N 201 
LEU   H    H  N N 202 
LEU   H2   H  N N 203 
LEU   HA   H  N N 204 
LEU   HB2  H  N N 205 
LEU   HB3  H  N N 206 
LEU   HG   H  N N 207 
LEU   HD11 H  N N 208 
LEU   HD12 H  N N 209 
LEU   HD13 H  N N 210 
LEU   HD21 H  N N 211 
LEU   HD22 H  N N 212 
LEU   HD23 H  N N 213 
LEU   HXT  H  N N 214 
LYS   N    N  N N 215 
LYS   CA   C  N S 216 
LYS   C    C  N N 217 
LYS   O    O  N N 218 
LYS   CB   C  N N 219 
LYS   CG   C  N N 220 
LYS   CD   C  N N 221 
LYS   CE   C  N N 222 
LYS   NZ   N  N N 223 
LYS   OXT  O  N N 224 
LYS   H    H  N N 225 
LYS   H2   H  N N 226 
LYS   HA   H  N N 227 
LYS   HB2  H  N N 228 
LYS   HB3  H  N N 229 
LYS   HG2  H  N N 230 
LYS   HG3  H  N N 231 
LYS   HD2  H  N N 232 
LYS   HD3  H  N N 233 
LYS   HE2  H  N N 234 
LYS   HE3  H  N N 235 
LYS   HZ1  H  N N 236 
LYS   HZ2  H  N N 237 
LYS   HZ3  H  N N 238 
LYS   HXT  H  N N 239 
MET   N    N  N N 240 
MET   CA   C  N S 241 
MET   C    C  N N 242 
MET   O    O  N N 243 
MET   CB   C  N N 244 
MET   CG   C  N N 245 
MET   SD   S  N N 246 
MET   CE   C  N N 247 
MET   OXT  O  N N 248 
MET   H    H  N N 249 
MET   H2   H  N N 250 
MET   HA   H  N N 251 
MET   HB2  H  N N 252 
MET   HB3  H  N N 253 
MET   HG2  H  N N 254 
MET   HG3  H  N N 255 
MET   HE1  H  N N 256 
MET   HE2  H  N N 257 
MET   HE3  H  N N 258 
MET   HXT  H  N N 259 
MG    MG   MG N N 260 
PHE   N    N  N N 261 
PHE   CA   C  N S 262 
PHE   C    C  N N 263 
PHE   O    O  N N 264 
PHE   CB   C  N N 265 
PHE   CG   C  Y N 266 
PHE   CD1  C  Y N 267 
PHE   CD2  C  Y N 268 
PHE   CE1  C  Y N 269 
PHE   CE2  C  Y N 270 
PHE   CZ   C  Y N 271 
PHE   OXT  O  N N 272 
PHE   H    H  N N 273 
PHE   H2   H  N N 274 
PHE   HA   H  N N 275 
PHE   HB2  H  N N 276 
PHE   HB3  H  N N 277 
PHE   HD1  H  N N 278 
PHE   HD2  H  N N 279 
PHE   HE1  H  N N 280 
PHE   HE2  H  N N 281 
PHE   HZ   H  N N 282 
PHE   HXT  H  N N 283 
PRO   N    N  N N 284 
PRO   CA   C  N S 285 
PRO   C    C  N N 286 
PRO   O    O  N N 287 
PRO   CB   C  N N 288 
PRO   CG   C  N N 289 
PRO   CD   C  N N 290 
PRO   OXT  O  N N 291 
PRO   H    H  N N 292 
PRO   HA   H  N N 293 
PRO   HB2  H  N N 294 
PRO   HB3  H  N N 295 
PRO   HG2  H  N N 296 
PRO   HG3  H  N N 297 
PRO   HD2  H  N N 298 
PRO   HD3  H  N N 299 
PRO   HXT  H  N N 300 
SER   N    N  N N 301 
SER   CA   C  N S 302 
SER   C    C  N N 303 
SER   O    O  N N 304 
SER   CB   C  N N 305 
SER   OG   O  N N 306 
SER   OXT  O  N N 307 
SER   H    H  N N 308 
SER   H2   H  N N 309 
SER   HA   H  N N 310 
SER   HB2  H  N N 311 
SER   HB3  H  N N 312 
SER   HG   H  N N 313 
SER   HXT  H  N N 314 
THR   N    N  N N 315 
THR   CA   C  N S 316 
THR   C    C  N N 317 
THR   O    O  N N 318 
THR   CB   C  N R 319 
THR   OG1  O  N N 320 
THR   CG2  C  N N 321 
THR   OXT  O  N N 322 
THR   H    H  N N 323 
THR   H2   H  N N 324 
THR   HA   H  N N 325 
THR   HB   H  N N 326 
THR   HG1  H  N N 327 
THR   HG21 H  N N 328 
THR   HG22 H  N N 329 
THR   HG23 H  N N 330 
THR   HXT  H  N N 331 
TRP   N    N  N N 332 
TRP   CA   C  N S 333 
TRP   C    C  N N 334 
TRP   O    O  N N 335 
TRP   CB   C  N N 336 
TRP   CG   C  Y N 337 
TRP   CD1  C  Y N 338 
TRP   CD2  C  Y N 339 
TRP   NE1  N  Y N 340 
TRP   CE2  C  Y N 341 
TRP   CE3  C  Y N 342 
TRP   CZ2  C  Y N 343 
TRP   CZ3  C  Y N 344 
TRP   CH2  C  Y N 345 
TRP   OXT  O  N N 346 
TRP   H    H  N N 347 
TRP   H2   H  N N 348 
TRP   HA   H  N N 349 
TRP   HB2  H  N N 350 
TRP   HB3  H  N N 351 
TRP   HD1  H  N N 352 
TRP   HE1  H  N N 353 
TRP   HE3  H  N N 354 
TRP   HZ2  H  N N 355 
TRP   HZ3  H  N N 356 
TRP   HH2  H  N N 357 
TRP   HXT  H  N N 358 
TYR   N    N  N N 359 
TYR   CA   C  N S 360 
TYR   C    C  N N 361 
TYR   O    O  N N 362 
TYR   CB   C  N N 363 
TYR   CG   C  Y N 364 
TYR   CD1  C  Y N 365 
TYR   CD2  C  Y N 366 
TYR   CE1  C  Y N 367 
TYR   CE2  C  Y N 368 
TYR   CZ   C  Y N 369 
TYR   OH   O  N N 370 
TYR   OXT  O  N N 371 
TYR   H    H  N N 372 
TYR   H2   H  N N 373 
TYR   HA   H  N N 374 
TYR   HB2  H  N N 375 
TYR   HB3  H  N N 376 
TYR   HD1  H  N N 377 
TYR   HD2  H  N N 378 
TYR   HE1  H  N N 379 
TYR   HE2  H  N N 380 
TYR   HH   H  N N 381 
TYR   HXT  H  N N 382 
VAL   N    N  N N 383 
VAL   CA   C  N S 384 
VAL   C    C  N N 385 
VAL   O    O  N N 386 
VAL   CB   C  N N 387 
VAL   CG1  C  N N 388 
VAL   CG2  C  N N 389 
VAL   OXT  O  N N 390 
VAL   H    H  N N 391 
VAL   H2   H  N N 392 
VAL   HA   H  N N 393 
VAL   HB   H  N N 394 
VAL   HG11 H  N N 395 
VAL   HG12 H  N N 396 
VAL   HG13 H  N N 397 
VAL   HG21 H  N N 398 
VAL   HG22 H  N N 399 
VAL   HG23 H  N N 400 
VAL   HXT  H  N N 401 
# 
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 
A1BA1 O3  C3   doub N N 1   
A1BA1 C3  N2   sing N N 2   
A1BA1 O2  C2   doub N N 3   
A1BA1 N2  N1   sing N N 4   
A1BA1 N2  C4   sing N N 5   
A1BA1 C9  C4   doub Y N 6   
A1BA1 C9  C8   sing Y N 7   
A1BA1 N1  C2   sing N N 8   
A1BA1 C2  O1   sing N N 9   
A1BA1 C4  C5   sing Y N 10  
A1BA1 C8  C7   doub Y N 11  
A1BA1 O1  C1   sing N N 12  
A1BA1 C5  C6   doub Y N 13  
A1BA1 C7  C6   sing Y N 14  
A1BA1 C1  H3   sing N N 15  
A1BA1 C1  H1   sing N N 16  
A1BA1 C1  H2   sing N N 17  
A1BA1 C3  H5   sing N N 18  
A1BA1 C5  H6   sing N N 19  
A1BA1 C6  H7   sing N N 20  
A1BA1 C7  H8   sing N N 21  
A1BA1 C8  H9   sing N N 22  
A1BA1 C9  H10  sing N N 23  
A1BA1 N1  H4   sing N N 24  
ALA   N   CA   sing N N 25  
ALA   N   H    sing N N 26  
ALA   N   H2   sing N N 27  
ALA   CA  C    sing N N 28  
ALA   CA  CB   sing N N 29  
ALA   CA  HA   sing N N 30  
ALA   C   O    doub N N 31  
ALA   C   OXT  sing N N 32  
ALA   CB  HB1  sing N N 33  
ALA   CB  HB2  sing N N 34  
ALA   CB  HB3  sing N N 35  
ALA   OXT HXT  sing N N 36  
ARG   N   CA   sing N N 37  
ARG   N   H    sing N N 38  
ARG   N   H2   sing N N 39  
ARG   CA  C    sing N N 40  
ARG   CA  CB   sing N N 41  
ARG   CA  HA   sing N N 42  
ARG   C   O    doub N N 43  
ARG   C   OXT  sing N N 44  
ARG   CB  CG   sing N N 45  
ARG   CB  HB2  sing N N 46  
ARG   CB  HB3  sing N N 47  
ARG   CG  CD   sing N N 48  
ARG   CG  HG2  sing N N 49  
ARG   CG  HG3  sing N N 50  
ARG   CD  NE   sing N N 51  
ARG   CD  HD2  sing N N 52  
ARG   CD  HD3  sing N N 53  
ARG   NE  CZ   sing N N 54  
ARG   NE  HE   sing N N 55  
ARG   CZ  NH1  sing N N 56  
ARG   CZ  NH2  doub N N 57  
ARG   NH1 HH11 sing N N 58  
ARG   NH1 HH12 sing N N 59  
ARG   NH2 HH21 sing N N 60  
ARG   NH2 HH22 sing N N 61  
ARG   OXT HXT  sing N N 62  
ASN   N   CA   sing N N 63  
ASN   N   H    sing N N 64  
ASN   N   H2   sing N N 65  
ASN   CA  C    sing N N 66  
ASN   CA  CB   sing N N 67  
ASN   CA  HA   sing N N 68  
ASN   C   O    doub N N 69  
ASN   C   OXT  sing N N 70  
ASN   CB  CG   sing N N 71  
ASN   CB  HB2  sing N N 72  
ASN   CB  HB3  sing N N 73  
ASN   CG  OD1  doub N N 74  
ASN   CG  ND2  sing N N 75  
ASN   ND2 HD21 sing N N 76  
ASN   ND2 HD22 sing N N 77  
ASN   OXT HXT  sing N N 78  
ASP   N   CA   sing N N 79  
ASP   N   H    sing N N 80  
ASP   N   H2   sing N N 81  
ASP   CA  C    sing N N 82  
ASP   CA  CB   sing N N 83  
ASP   CA  HA   sing N N 84  
ASP   C   O    doub N N 85  
ASP   C   OXT  sing N N 86  
ASP   CB  CG   sing N N 87  
ASP   CB  HB2  sing N N 88  
ASP   CB  HB3  sing N N 89  
ASP   CG  OD1  doub N N 90  
ASP   CG  OD2  sing N N 91  
ASP   OD2 HD2  sing N N 92  
ASP   OXT HXT  sing N N 93  
GLN   N   CA   sing N N 94  
GLN   N   H    sing N N 95  
GLN   N   H2   sing N N 96  
GLN   CA  C    sing N N 97  
GLN   CA  CB   sing N N 98  
GLN   CA  HA   sing N N 99  
GLN   C   O    doub N N 100 
GLN   C   OXT  sing N N 101 
GLN   CB  CG   sing N N 102 
GLN   CB  HB2  sing N N 103 
GLN   CB  HB3  sing N N 104 
GLN   CG  CD   sing N N 105 
GLN   CG  HG2  sing N N 106 
GLN   CG  HG3  sing N N 107 
GLN   CD  OE1  doub N N 108 
GLN   CD  NE2  sing N N 109 
GLN   NE2 HE21 sing N N 110 
GLN   NE2 HE22 sing N N 111 
GLN   OXT HXT  sing N N 112 
GLU   N   CA   sing N N 113 
GLU   N   H    sing N N 114 
GLU   N   H2   sing N N 115 
GLU   CA  C    sing N N 116 
GLU   CA  CB   sing N N 117 
GLU   CA  HA   sing N N 118 
GLU   C   O    doub N N 119 
GLU   C   OXT  sing N N 120 
GLU   CB  CG   sing N N 121 
GLU   CB  HB2  sing N N 122 
GLU   CB  HB3  sing N N 123 
GLU   CG  CD   sing N N 124 
GLU   CG  HG2  sing N N 125 
GLU   CG  HG3  sing N N 126 
GLU   CD  OE1  doub N N 127 
GLU   CD  OE2  sing N N 128 
GLU   OE2 HE2  sing N N 129 
GLU   OXT HXT  sing N N 130 
GLY   N   CA   sing N N 131 
GLY   N   H    sing N N 132 
GLY   N   H2   sing N N 133 
GLY   CA  C    sing N N 134 
GLY   CA  HA2  sing N N 135 
GLY   CA  HA3  sing N N 136 
GLY   C   O    doub N N 137 
GLY   C   OXT  sing N N 138 
GLY   OXT HXT  sing N N 139 
HIS   N   CA   sing N N 140 
HIS   N   H    sing N N 141 
HIS   N   H2   sing N N 142 
HIS   CA  C    sing N N 143 
HIS   CA  CB   sing N N 144 
HIS   CA  HA   sing N N 145 
HIS   C   O    doub N N 146 
HIS   C   OXT  sing N N 147 
HIS   CB  CG   sing N N 148 
HIS   CB  HB2  sing N N 149 
HIS   CB  HB3  sing N N 150 
HIS   CG  ND1  sing Y N 151 
HIS   CG  CD2  doub Y N 152 
HIS   ND1 CE1  doub Y N 153 
HIS   ND1 HD1  sing N N 154 
HIS   CD2 NE2  sing Y N 155 
HIS   CD2 HD2  sing N N 156 
HIS   CE1 NE2  sing Y N 157 
HIS   CE1 HE1  sing N N 158 
HIS   NE2 HE2  sing N N 159 
HIS   OXT HXT  sing N N 160 
HOH   O   H1   sing N N 161 
HOH   O   H2   sing N N 162 
ILE   N   CA   sing N N 163 
ILE   N   H    sing N N 164 
ILE   N   H2   sing N N 165 
ILE   CA  C    sing N N 166 
ILE   CA  CB   sing N N 167 
ILE   CA  HA   sing N N 168 
ILE   C   O    doub N N 169 
ILE   C   OXT  sing N N 170 
ILE   CB  CG1  sing N N 171 
ILE   CB  CG2  sing N N 172 
ILE   CB  HB   sing N N 173 
ILE   CG1 CD1  sing N N 174 
ILE   CG1 HG12 sing N N 175 
ILE   CG1 HG13 sing N N 176 
ILE   CG2 HG21 sing N N 177 
ILE   CG2 HG22 sing N N 178 
ILE   CG2 HG23 sing N N 179 
ILE   CD1 HD11 sing N N 180 
ILE   CD1 HD12 sing N N 181 
ILE   CD1 HD13 sing N N 182 
ILE   OXT HXT  sing N N 183 
LEU   N   CA   sing N N 184 
LEU   N   H    sing N N 185 
LEU   N   H2   sing N N 186 
LEU   CA  C    sing N N 187 
LEU   CA  CB   sing N N 188 
LEU   CA  HA   sing N N 189 
LEU   C   O    doub N N 190 
LEU   C   OXT  sing N N 191 
LEU   CB  CG   sing N N 192 
LEU   CB  HB2  sing N N 193 
LEU   CB  HB3  sing N N 194 
LEU   CG  CD1  sing N N 195 
LEU   CG  CD2  sing N N 196 
LEU   CG  HG   sing N N 197 
LEU   CD1 HD11 sing N N 198 
LEU   CD1 HD12 sing N N 199 
LEU   CD1 HD13 sing N N 200 
LEU   CD2 HD21 sing N N 201 
LEU   CD2 HD22 sing N N 202 
LEU   CD2 HD23 sing N N 203 
LEU   OXT HXT  sing N N 204 
LYS   N   CA   sing N N 205 
LYS   N   H    sing N N 206 
LYS   N   H2   sing N N 207 
LYS   CA  C    sing N N 208 
LYS   CA  CB   sing N N 209 
LYS   CA  HA   sing N N 210 
LYS   C   O    doub N N 211 
LYS   C   OXT  sing N N 212 
LYS   CB  CG   sing N N 213 
LYS   CB  HB2  sing N N 214 
LYS   CB  HB3  sing N N 215 
LYS   CG  CD   sing N N 216 
LYS   CG  HG2  sing N N 217 
LYS   CG  HG3  sing N N 218 
LYS   CD  CE   sing N N 219 
LYS   CD  HD2  sing N N 220 
LYS   CD  HD3  sing N N 221 
LYS   CE  NZ   sing N N 222 
LYS   CE  HE2  sing N N 223 
LYS   CE  HE3  sing N N 224 
LYS   NZ  HZ1  sing N N 225 
LYS   NZ  HZ2  sing N N 226 
LYS   NZ  HZ3  sing N N 227 
LYS   OXT HXT  sing N N 228 
MET   N   CA   sing N N 229 
MET   N   H    sing N N 230 
MET   N   H2   sing N N 231 
MET   CA  C    sing N N 232 
MET   CA  CB   sing N N 233 
MET   CA  HA   sing N N 234 
MET   C   O    doub N N 235 
MET   C   OXT  sing N N 236 
MET   CB  CG   sing N N 237 
MET   CB  HB2  sing N N 238 
MET   CB  HB3  sing N N 239 
MET   CG  SD   sing N N 240 
MET   CG  HG2  sing N N 241 
MET   CG  HG3  sing N N 242 
MET   SD  CE   sing N N 243 
MET   CE  HE1  sing N N 244 
MET   CE  HE2  sing N N 245 
MET   CE  HE3  sing N N 246 
MET   OXT HXT  sing N N 247 
PHE   N   CA   sing N N 248 
PHE   N   H    sing N N 249 
PHE   N   H2   sing N N 250 
PHE   CA  C    sing N N 251 
PHE   CA  CB   sing N N 252 
PHE   CA  HA   sing N N 253 
PHE   C   O    doub N N 254 
PHE   C   OXT  sing N N 255 
PHE   CB  CG   sing N N 256 
PHE   CB  HB2  sing N N 257 
PHE   CB  HB3  sing N N 258 
PHE   CG  CD1  doub Y N 259 
PHE   CG  CD2  sing Y N 260 
PHE   CD1 CE1  sing Y N 261 
PHE   CD1 HD1  sing N N 262 
PHE   CD2 CE2  doub Y N 263 
PHE   CD2 HD2  sing N N 264 
PHE   CE1 CZ   doub Y N 265 
PHE   CE1 HE1  sing N N 266 
PHE   CE2 CZ   sing Y N 267 
PHE   CE2 HE2  sing N N 268 
PHE   CZ  HZ   sing N N 269 
PHE   OXT HXT  sing N N 270 
PRO   N   CA   sing N N 271 
PRO   N   CD   sing N N 272 
PRO   N   H    sing N N 273 
PRO   CA  C    sing N N 274 
PRO   CA  CB   sing N N 275 
PRO   CA  HA   sing N N 276 
PRO   C   O    doub N N 277 
PRO   C   OXT  sing N N 278 
PRO   CB  CG   sing N N 279 
PRO   CB  HB2  sing N N 280 
PRO   CB  HB3  sing N N 281 
PRO   CG  CD   sing N N 282 
PRO   CG  HG2  sing N N 283 
PRO   CG  HG3  sing N N 284 
PRO   CD  HD2  sing N N 285 
PRO   CD  HD3  sing N N 286 
PRO   OXT HXT  sing N N 287 
SER   N   CA   sing N N 288 
SER   N   H    sing N N 289 
SER   N   H2   sing N N 290 
SER   CA  C    sing N N 291 
SER   CA  CB   sing N N 292 
SER   CA  HA   sing N N 293 
SER   C   O    doub N N 294 
SER   C   OXT  sing N N 295 
SER   CB  OG   sing N N 296 
SER   CB  HB2  sing N N 297 
SER   CB  HB3  sing N N 298 
SER   OG  HG   sing N N 299 
SER   OXT HXT  sing N N 300 
THR   N   CA   sing N N 301 
THR   N   H    sing N N 302 
THR   N   H2   sing N N 303 
THR   CA  C    sing N N 304 
THR   CA  CB   sing N N 305 
THR   CA  HA   sing N N 306 
THR   C   O    doub N N 307 
THR   C   OXT  sing N N 308 
THR   CB  OG1  sing N N 309 
THR   CB  CG2  sing N N 310 
THR   CB  HB   sing N N 311 
THR   OG1 HG1  sing N N 312 
THR   CG2 HG21 sing N N 313 
THR   CG2 HG22 sing N N 314 
THR   CG2 HG23 sing N N 315 
THR   OXT HXT  sing N N 316 
TRP   N   CA   sing N N 317 
TRP   N   H    sing N N 318 
TRP   N   H2   sing N N 319 
TRP   CA  C    sing N N 320 
TRP   CA  CB   sing N N 321 
TRP   CA  HA   sing N N 322 
TRP   C   O    doub N N 323 
TRP   C   OXT  sing N N 324 
TRP   CB  CG   sing N N 325 
TRP   CB  HB2  sing N N 326 
TRP   CB  HB3  sing N N 327 
TRP   CG  CD1  doub Y N 328 
TRP   CG  CD2  sing Y N 329 
TRP   CD1 NE1  sing Y N 330 
TRP   CD1 HD1  sing N N 331 
TRP   CD2 CE2  doub Y N 332 
TRP   CD2 CE3  sing Y N 333 
TRP   NE1 CE2  sing Y N 334 
TRP   NE1 HE1  sing N N 335 
TRP   CE2 CZ2  sing Y N 336 
TRP   CE3 CZ3  doub Y N 337 
TRP   CE3 HE3  sing N N 338 
TRP   CZ2 CH2  doub Y N 339 
TRP   CZ2 HZ2  sing N N 340 
TRP   CZ3 CH2  sing Y N 341 
TRP   CZ3 HZ3  sing N N 342 
TRP   CH2 HH2  sing N N 343 
TRP   OXT HXT  sing N N 344 
TYR   N   CA   sing N N 345 
TYR   N   H    sing N N 346 
TYR   N   H2   sing N N 347 
TYR   CA  C    sing N N 348 
TYR   CA  CB   sing N N 349 
TYR   CA  HA   sing N N 350 
TYR   C   O    doub N N 351 
TYR   C   OXT  sing N N 352 
TYR   CB  CG   sing N N 353 
TYR   CB  HB2  sing N N 354 
TYR   CB  HB3  sing N N 355 
TYR   CG  CD1  doub Y N 356 
TYR   CG  CD2  sing Y N 357 
TYR   CD1 CE1  sing Y N 358 
TYR   CD1 HD1  sing N N 359 
TYR   CD2 CE2  doub Y N 360 
TYR   CD2 HD2  sing N N 361 
TYR   CE1 CZ   doub Y N 362 
TYR   CE1 HE1  sing N N 363 
TYR   CE2 CZ   sing Y N 364 
TYR   CE2 HE2  sing N N 365 
TYR   CZ  OH   sing N N 366 
TYR   OH  HH   sing N N 367 
TYR   OXT HXT  sing N N 368 
VAL   N   CA   sing N N 369 
VAL   N   H    sing N N 370 
VAL   N   H2   sing N N 371 
VAL   CA  C    sing N N 372 
VAL   CA  CB   sing N N 373 
VAL   CA  HA   sing N N 374 
VAL   C   O    doub N N 375 
VAL   C   OXT  sing N N 376 
VAL   CB  CG1  sing N N 377 
VAL   CB  CG2  sing N N 378 
VAL   CB  HB   sing N N 379 
VAL   CG1 HG11 sing N N 380 
VAL   CG1 HG12 sing N N 381 
VAL   CG1 HG13 sing N N 382 
VAL   CG2 HG21 sing N N 383 
VAL   CG2 HG22 sing N N 384 
VAL   CG2 HG23 sing N N 385 
VAL   OXT HXT  sing N N 386 
# 
_pdbx_audit_support.funding_organization   'New Zealand Synchrotron Group Ltd' 
_pdbx_audit_support.country                'New Zealand' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8T87 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DRO 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.021228 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000352 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013408 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.013597 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
H  
MG 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . GLY   A 1 3   ? -7.833  10.218  6.129   1.00 66.34  ? 0   GLY   A N    1 
ATOM   2    C  CA   . GLY   A 1 3   ? -7.155  10.571  7.412   1.00 72.37  ? 0   GLY   A CA   1 
ATOM   3    C  C    . GLY   A 1 3   ? -6.400  9.398   8.008   1.00 65.03  ? 0   GLY   A C    1 
ATOM   4    O  O    . GLY   A 1 3   ? -5.695  9.536   9.008   1.00 71.94  ? 0   GLY   A O    1 
ATOM   5    H  H    . GLY   A 1 3   ? -8.259  10.933  5.812   1.00 79.65  ? 0   GLY   A H    1 
ATOM   6    H  HA2  . GLY   A 1 3   ? -6.525  11.292  7.255   1.00 86.88  ? 0   GLY   A HA2  1 
ATOM   7    H  HA3  . GLY   A 1 3   ? -7.819  10.866  8.055   1.00 86.88  ? 0   GLY   A HA3  1 
ATOM   8    N  N    . MET   A 1 4   ? -6.582  8.224   7.407   1.00 59.23  ? 1   MET   A N    1 
ATOM   9    C  CA   . MET   A 1 4   ? -5.711  7.090   7.663   1.00 44.96  ? 1   MET   A CA   1 
ATOM   10   C  C    . MET   A 1 4   ? -4.377  7.348   6.959   1.00 41.01  ? 1   MET   A C    1 
ATOM   11   O  O    . MET   A 1 4   ? -4.301  8.104   5.992   1.00 42.73  ? 1   MET   A O    1 
ATOM   12   C  CB   . MET   A 1 4   ? -6.344  5.797   7.131   1.00 43.41  ? 1   MET   A CB   1 
ATOM   13   C  CG   . MET   A 1 4   ? -7.535  5.296   7.929   1.00 37.28  ? 1   MET   A CG   1 
ATOM   14   S  SD   . MET   A 1 4   ? -8.049  3.632   7.513   1.00 38.11  ? 1   MET   A SD   1 
ATOM   15   C  CE   . MET   A 1 4   ? -6.636  2.694   8.077   1.00 31.20  ? 1   MET   A CE   1 
ATOM   16   H  H    . MET   A 1 4   ? -7.209  8.061   6.842   1.00 71.11  ? 1   MET   A H    1 
ATOM   17   H  HA   . MET   A 1 4   ? -5.575  6.969   8.616   1.00 53.99  ? 1   MET   A HA   1 
ATOM   18   H  HB2  . MET   A 1 4   ? -6.647  5.954   6.223   1.00 52.13  ? 1   MET   A HB2  1 
ATOM   19   H  HB3  . MET   A 1 4   ? -5.672  5.098   7.141   1.00 52.13  ? 1   MET   A HB3  1 
ATOM   20   H  HG2  . MET   A 1 4   ? -7.304  5.305   8.871   1.00 44.78  ? 1   MET   A HG2  1 
ATOM   21   H  HG3  . MET   A 1 4   ? -8.288  5.885   7.766   1.00 44.78  ? 1   MET   A HG3  1 
ATOM   22   H  HE1  . MET   A 1 4   ? -6.800  1.751   7.921   1.00 37.49  ? 1   MET   A HE1  1 
ATOM   23   H  HE2  . MET   A 1 4   ? -5.851  2.979   7.583   1.00 37.49  ? 1   MET   A HE2  1 
ATOM   24   H  HE3  . MET   A 1 4   ? -6.507  2.855   9.024   1.00 37.49  ? 1   MET   A HE3  1 
ATOM   25   N  N    . GLU   A 1 5   ? -3.317  6.737   7.463   1.00 31.87  ? 2   GLU   A N    1 
ATOM   26   C  CA   . GLU   A 1 5   ? -2.004  6.802   6.830   1.00 32.59  ? 2   GLU   A CA   1 
ATOM   27   C  C    . GLU   A 1 5   ? -1.921  5.804   5.673   1.00 32.76  ? 2   GLU   A C    1 
ATOM   28   O  O    . GLU   A 1 5   ? -2.655  4.833   5.626   1.00 30.09  ? 2   GLU   A O    1 
ATOM   29   C  CB   . GLU   A 1 5   ? -0.920  6.501   7.862   1.00 32.55  ? 2   GLU   A CB   1 
ATOM   30   C  CG   . GLU   A 1 5   ? -0.918  7.488   9.023   1.00 38.69  ? 2   GLU   A CG   1 
ATOM   31   C  CD   . GLU   A 1 5   ? -0.518  8.870   8.582   1.00 45.03  ? 2   GLU   A CD   1 
ATOM   32   O  OE1  . GLU   A 1 5   ? 0.606   9.022   8.060   1.00 48.53  ? 2   GLU   A OE1  1 
ATOM   33   O  OE2  . GLU   A 1 5   ? -1.337  9.795   8.731   1.00 58.38  ? 2   GLU   A OE2  1 
ATOM   34   H  H    . GLU   A 1 5   ? -3.328  6.268   8.184   1.00 38.29  ? 2   GLU   A H    1 
ATOM   35   H  HA   . GLU   A 1 5   ? -1.850  7.690   6.471   1.00 39.16  ? 2   GLU   A HA   1 
ATOM   36   H  HB2  . GLU   A 1 5   ? -1.068  5.613   8.224   1.00 39.11  ? 2   GLU   A HB2  1 
ATOM   37   H  HB3  . GLU   A 1 5   ? -0.053  6.544   7.430   1.00 39.11  ? 2   GLU   A HB3  1 
ATOM   38   H  HG2  . GLU   A 1 5   ? -1.809  7.536   9.404   1.00 46.47  ? 2   GLU   A HG2  1 
ATOM   39   H  HG3  . GLU   A 1 5   ? -0.286  7.189   9.695   1.00 46.47  ? 2   GLU   A HG3  1 
ATOM   40   N  N    . THR   A 1 6   ? -1.016  6.059   4.725   1.00 33.77  ? 3   THR   A N    1 
ATOM   41   C  CA   . THR   A 1 6   ? -0.901  5.232   3.529   1.00 28.77  ? 3   THR   A CA   1 
ATOM   42   C  C    . THR   A 1 6   ? 0.562   4.873   3.276   1.00 27.42  ? 3   THR   A C    1 
ATOM   43   O  O    . THR   A 1 6   ? 1.436   5.754   3.290   1.00 32.69  ? 3   THR   A O    1 
ATOM   44   C  CB   . THR   A 1 6   ? -1.476  5.941   2.283   1.00 33.91  ? 3   THR   A CB   1 
ATOM   45   O  OG1  . THR   A 1 6   ? -2.878  6.222   2.446   1.00 34.89  ? 3   THR   A OG1  1 
ATOM   46   C  CG2  . THR   A 1 6   ? -1.285  5.075   1.030   1.00 32.77  ? 3   THR   A CG2  1 
ATOM   47   H  H    . THR   A 1 6   ? -0.456  6.710   4.755   1.00 40.56  ? 3   THR   A H    1 
ATOM   48   H  HA   . THR   A 1 6   ? -1.398  4.413   3.681   1.00 34.57  ? 3   THR   A HA   1 
ATOM   49   H  HB   . THR   A 1 6   ? -1.001  6.778   2.165   1.00 40.73  ? 3   THR   A HB   1 
ATOM   50   H  HG1  . THR   A 1 6   ? -3.156  6.683   1.801   1.00 41.91  ? 3   THR   A HG1  1 
ATOM   51   H  HG21 . THR   A 1 6   ? -1.849  5.402   0.312   1.00 39.36  ? 3   THR   A HG21 1 
ATOM   52   H  HG22 . THR   A 1 6   ? -0.359  5.106   0.743   1.00 39.36  ? 3   THR   A HG22 1 
ATOM   53   H  HG23 . THR   A 1 6   ? -1.524  4.154   1.224   1.00 39.36  ? 3   THR   A HG23 1 
ATOM   54   N  N    . LEU   A 1 7   ? 0.825   3.587   3.047   1.00 24.39  ? 4   LEU   A N    1 
ATOM   55   C  CA   . LEU   A 1 7   ? 2.109   3.118   2.549   1.00 28.05  ? 4   LEU   A CA   1 
ATOM   56   C  C    . LEU   A 1 7   ? 1.855   2.441   1.211   1.00 24.84  ? 4   LEU   A C    1 
ATOM   57   O  O    . LEU   A 1 7   ? 1.086   1.470   1.140   1.00 25.32  ? 4   LEU   A O    1 
ATOM   58   C  CB   . LEU   A 1 7   ? 2.778   2.150   3.518   1.00 25.42  ? 4   LEU   A CB   1 
ATOM   59   C  CG   . LEU   A 1 7   ? 4.094   1.522   3.053   1.00 25.84  ? 4   LEU   A CG   1 
ATOM   60   C  CD1  . LEU   A 1 7   ? 5.129   2.590   2.857   1.00 32.08  ? 4   LEU   A CD1  1 
ATOM   61   C  CD2  . LEU   A 1 7   ? 4.532   0.503   4.084   1.00 27.56  ? 4   LEU   A CD2  1 
ATOM   62   H  H    . LEU   A 1 7   ? 0.258   2.954   3.178   1.00 29.31  ? 4   LEU   A H    1 
ATOM   63   H  HA   . LEU   A 1 7   ? 2.711   3.870   2.428   1.00 33.70  ? 4   LEU   A HA   1 
ATOM   64   H  HB2  . LEU   A 1 7   ? 2.965   2.629   4.341   1.00 30.55  ? 4   LEU   A HB2  1 
ATOM   65   H  HB3  . LEU   A 1 7   ? 2.160   1.423   3.691   1.00 30.55  ? 4   LEU   A HB3  1 
ATOM   66   H  HG   . LEU   A 1 7   ? 3.985   1.072   2.201   1.00 31.05  ? 4   LEU   A HG   1 
ATOM   67   H  HD11 . LEU   A 1 7   ? 5.989   2.170   2.699   1.00 38.54  ? 4   LEU   A HD11 1 
ATOM   68   H  HD12 . LEU   A 1 7   ? 4.880   3.134   2.093   1.00 38.54  ? 4   LEU   A HD12 1 
ATOM   69   H  HD13 . LEU   A 1 7   ? 5.170   3.139   3.655   1.00 38.54  ? 4   LEU   A HD13 1 
ATOM   70   H  HD21 . LEU   A 1 7   ? 5.346   0.073   3.777   1.00 33.11  ? 4   LEU   A HD21 1 
ATOM   71   H  HD22 . LEU   A 1 7   ? 4.695   0.955   4.926   1.00 33.11  ? 4   LEU   A HD22 1 
ATOM   72   H  HD23 . LEU   A 1 7   ? 3.830   -0.157  4.193   1.00 33.11  ? 4   LEU   A HD23 1 
ATOM   73   N  N    . GLU   A 1 8   ? 2.469   2.970   0.151   1.00 25.32  ? 5   GLU   A N    1 
ATOM   74   C  CA   . GLU   A 1 8   ? 2.298   2.410   -1.180  1.00 28.61  ? 5   GLU   A CA   1 
ATOM   75   C  C    . GLU   A 1 8   ? 3.276   1.263   -1.383  1.00 27.61  ? 5   GLU   A C    1 
ATOM   76   O  O    . GLU   A 1 8   ? 4.489   1.461   -1.277  1.00 32.06  ? 5   GLU   A O    1 
ATOM   77   C  CB   . GLU   A 1 8   ? 2.525   3.503   -2.221  1.00 30.46  ? 5   GLU   A CB   1 
ATOM   78   C  CG   . GLU   A 1 8   ? 1.363   4.488   -2.286  1.00 30.47  ? 5   GLU   A CG   1 
ATOM   79   C  CD   . GLU   A 1 8   ? 1.443   5.433   -3.480  1.00 38.14  ? 5   GLU   A CD   1 
ATOM   80   O  OE1  . GLU   A 1 8   ? 2.280   5.212   -4.372  1.00 53.48  ? 5   GLU   A OE1  1 
ATOM   81   O  OE2  . GLU   A 1 8   ? 0.646   6.380   -3.514  1.00 46.92  ? 5   GLU   A OE2  1 
ATOM   82   H  H    . GLU   A 1 8   ? 2.989   3.654   0.182   1.00 30.43  ? 5   GLU   A H    1 
ATOM   83   H  HA   . GLU   A 1 8   ? 1.399   2.059   -1.280  1.00 34.38  ? 5   GLU   A HA   1 
ATOM   84   H  HB2  . GLU   A 1 8   ? 3.328   3.997   -1.993  1.00 36.59  ? 5   GLU   A HB2  1 
ATOM   85   H  HB3  . GLU   A 1 8   ? 2.624   3.094   -3.095  1.00 36.59  ? 5   GLU   A HB3  1 
ATOM   86   H  HG2  . GLU   A 1 8   ? 0.533   3.991   -2.355  1.00 36.61  ? 5   GLU   A HG2  1 
ATOM   87   H  HG3  . GLU   A 1 8   ? 1.362   5.026   -1.479  1.00 36.61  ? 5   GLU   A HG3  1 
ATOM   88   N  N    . LEU   A 1 9   ? 2.749   0.073   -1.651  1.00 22.90  ? 6   LEU   A N    1 
ATOM   89   C  CA   . LEU   A 1 9   ? 3.508   -1.160  -1.763  1.00 26.90  ? 6   LEU   A CA   1 
ATOM   90   C  C    . LEU   A 1 9   ? 3.226   -1.760  -3.129  1.00 27.07  ? 6   LEU   A C    1 
ATOM   91   O  O    . LEU   A 1 9   ? 2.323   -1.307  -3.845  1.00 26.09  ? 6   LEU   A O    1 
ATOM   92   C  CB   . LEU   A 1 9   ? 3.153   -2.156  -0.645  1.00 28.62  ? 6   LEU   A CB   1 
ATOM   93   C  CG   . LEU   A 1 9   ? 3.392   -1.619  0.754   1.00 26.76  ? 6   LEU   A CG   1 
ATOM   94   C  CD1  . LEU   A 1 9   ? 2.894   -2.622  1.791   1.00 28.72  ? 6   LEU   A CD1  1 
ATOM   95   C  CD2  . LEU   A 1 9   ? 4.880   -1.356  0.927   1.00 32.80  ? 6   LEU   A CD2  1 
ATOM   96   H  H    . LEU   A 1 9   ? 1.907   -0.048  -1.778  1.00 27.53  ? 6   LEU   A H    1 
ATOM   97   H  HA   . LEU   A 1 9   ? 4.457   -0.975  -1.679  1.00 32.32  ? 6   LEU   A HA   1 
ATOM   98   H  HB2  . LEU   A 1 9   ? 2.213   -2.384  -0.719  1.00 34.38  ? 6   LEU   A HB2  1 
ATOM   99   H  HB3  . LEU   A 1 9   ? 3.697   -2.952  -0.754  1.00 34.38  ? 6   LEU   A HB3  1 
ATOM   100  H  HG   . LEU   A 1 9   ? 2.908   -0.789  0.889   1.00 32.16  ? 6   LEU   A HG   1 
ATOM   101  H  HD11 . LEU   A 1 9   ? 3.113   -2.295  2.677   1.00 34.51  ? 6   LEU   A HD11 1 
ATOM   102  H  HD12 . LEU   A 1 9   ? 1.932   -2.716  1.702   1.00 34.51  ? 6   LEU   A HD12 1 
ATOM   103  H  HD13 . LEU   A 1 9   ? 3.326   -3.477  1.637   1.00 34.51  ? 6   LEU   A HD13 1 
ATOM   104  H  HD21 . LEU   A 1 9   ? 5.060   -1.164  1.860   1.00 39.40  ? 6   LEU   A HD21 1 
ATOM   105  H  HD22 . LEU   A 1 9   ? 5.374   -2.143  0.649   1.00 39.40  ? 6   LEU   A HD22 1 
ATOM   106  H  HD23 . LEU   A 1 9   ? 5.132   -0.596  0.378   1.00 39.40  ? 6   LEU   A HD23 1 
ATOM   107  N  N    . GLN   A 1 10  ? 3.978   -2.804  -3.481  1.00 25.55  ? 7   GLN   A N    1 
ATOM   108  C  CA   . GLN   A 1 10  ? 3.753   -3.465  -4.764  1.00 24.44  ? 7   GLN   A CA   1 
ATOM   109  C  C    . GLN   A 1 10  ? 2.344   -4.045  -4.789  1.00 22.00  ? 7   GLN   A C    1 
ATOM   110  O  O    . GLN   A 1 10  ? 1.998   -4.891  -3.960  1.00 23.13  ? 7   GLN   A O    1 
ATOM   111  C  CB   . GLN   A 1 10  ? 4.801   -4.560  -4.999  1.00 29.58  ? 7   GLN   A CB   1 
ATOM   112  C  CG   . GLN   A 1 10  ? 4.543   -5.402  -6.240  1.00 29.85  ? 7   GLN   A CG   1 
ATOM   113  C  CD   . GLN   A 1 10  ? 4.847   -4.687  -7.528  1.00 30.82  ? 7   GLN   A CD   1 
ATOM   114  O  OE1  . GLN   A 1 10  ? 5.704   -3.790  -7.589  1.00 33.56  ? 7   GLN   A OE1  1 
ATOM   115  N  NE2  . GLN   A 1 10  ? 4.088   -5.022  -8.577  1.00 36.03  ? 7   GLN   A NE2  1 
ATOM   116  H  H    . GLN   A 1 10  ? 4.610   -3.140  -3.005  1.00 30.70  ? 7   GLN   A H    1 
ATOM   117  H  HA   . GLN   A 1 10  ? 3.844   -2.822  -5.485  1.00 29.37  ? 7   GLN   A HA   1 
ATOM   118  H  HB2  . GLN   A 1 10  ? 5.671   -4.142  -5.101  1.00 35.53  ? 7   GLN   A HB2  1 
ATOM   119  H  HB3  . GLN   A 1 10  ? 4.807   -5.156  -4.233  1.00 35.53  ? 7   GLN   A HB3  1 
ATOM   120  H  HG2  . GLN   A 1 10  ? 5.101   -6.195  -6.202  1.00 35.86  ? 7   GLN   A HG2  1 
ATOM   121  H  HG3  . GLN   A 1 10  ? 3.607   -5.656  -6.256  1.00 35.86  ? 7   GLN   A HG3  1 
ATOM   122  H  HE21 . GLN   A 1 10  ? 3.470   -5.614  -8.490  1.00 43.28  ? 7   GLN   A HE21 1 
ATOM   123  H  HE22 . GLN   A 1 10  ? 4.218   -4.645  -9.340  1.00 43.28  ? 7   GLN   A HE22 1 
ATOM   124  N  N    . GLY   A 1 11  ? 1.523   -3.548  -5.706  1.00 25.51  ? 8   GLY   A N    1 
ATOM   125  C  CA   . GLY   A 1 11  ? 0.185   -4.061  -5.884  1.00 26.48  ? 8   GLY   A CA   1 
ATOM   126  C  C    . GLY   A 1 11  ? -0.872  -3.544  -4.929  1.00 26.45  ? 8   GLY   A C    1 
ATOM   127  O  O    . GLY   A 1 11  ? -2.032  -3.983  -5.029  1.00 23.92  ? 8   GLY   A O    1 
ATOM   128  H  H    . GLY   A 1 11  ? 1.725   -2.906  -6.240  1.00 30.66  ? 8   GLY   A H    1 
ATOM   129  H  HA2  . GLY   A 1 11  ? -0.106  -3.842  -6.783  1.00 31.82  ? 8   GLY   A HA2  1 
ATOM   130  H  HA3  . GLY   A 1 11  ? 0.214   -5.025  -5.787  1.00 31.82  ? 8   GLY   A HA3  1 
ATOM   131  N  N    . ALA   A 1 12  ? -0.539  -2.623  -4.021  1.00 23.92  ? 9   ALA   A N    1 
ATOM   132  C  CA   . ALA   A 1 12  ? -1.563  -2.136  -3.109  1.00 22.54  ? 9   ALA   A CA   1 
ATOM   133  C  C    . ALA   A 1 12  ? -1.148  -0.825  -2.468  1.00 26.98  ? 9   ALA   A C    1 
ATOM   134  O  O    . ALA   A 1 12  ? 0.037   -0.532  -2.309  1.00 28.76  ? 9   ALA   A O    1 
ATOM   135  C  CB   . ALA   A 1 12  ? -1.885  -3.146  -1.988  1.00 22.34  ? 9   ALA   A CB   1 
ATOM   136  H  H    . ALA   A 1 12  ? 0.244   -2.282  -3.921  1.00 28.75  ? 9   ALA   A H    1 
ATOM   137  H  HA   . ALA   A 1 12  ? -2.355  -1.978  -3.646  1.00 27.09  ? 9   ALA   A HA   1 
ATOM   138  H  HB1  . ALA   A 1 12  ? -2.591  -2.784  -1.430  1.00 26.86  ? 9   ALA   A HB1  1 
ATOM   139  H  HB2  . ALA   A 1 12  ? -2.174  -3.981  -2.388  1.00 26.86  ? 9   ALA   A HB2  1 
ATOM   140  H  HB3  . ALA   A 1 12  ? -1.087  -3.293  -1.456  1.00 26.86  ? 9   ALA   A HB3  1 
ATOM   141  N  N    . LYS   A 1 13  ? -2.159  -0.063  -2.068  1.00 25.66  ? 10  LYS   A N    1 
ATOM   142  C  CA   . LYS   A 1 13  ? -2.007  1.034   -1.115  1.00 27.94  ? 10  LYS   A CA   1 
ATOM   143  C  C    . LYS   A 1 13  ? -2.508  0.534   0.233   1.00 24.57  ? 10  LYS   A C    1 
ATOM   144  O  O    . LYS   A 1 13  ? -3.710  0.285   0.417   1.00 25.61  ? 10  LYS   A O    1 
ATOM   145  C  CB   . LYS   A 1 13  ? -2.772  2.271   -1.557  1.00 30.13  ? 10  LYS   A CB   1 
ATOM   146  C  CG   . LYS   A 1 13  ? -2.373  2.793   -2.897  1.00 29.83  ? 10  LYS   A CG   1 
ATOM   147  C  CD   . LYS   A 1 13  ? -3.056  4.145   -3.137  1.00 37.61  ? 10  LYS   A CD   1 
ATOM   148  C  CE   . LYS   A 1 13  ? -3.438  4.307   -4.587  1.00 47.54  ? 10  LYS   A CE   1 
ATOM   149  N  NZ   . LYS   A 1 13  ? -2.231  4.638   -5.381  1.00 55.74  ? 10  LYS   A NZ   1 
ATOM   150  H  H    . LYS   A 1 13  ? -2.968  -0.164  -2.341  1.00 30.84  ? 10  LYS   A H    1 
ATOM   151  H  HA   . LYS   A 1 13  ? -1.071  1.279   -1.047  1.00 33.57  ? 10  LYS   A HA   1 
ATOM   152  H  HB2  . LYS   A 1 13  ? -3.716  2.054   -1.595  1.00 36.20  ? 10  LYS   A HB2  1 
ATOM   153  H  HB3  . LYS   A 1 13  ? -2.619  2.976   -0.909  1.00 36.20  ? 10  LYS   A HB3  1 
ATOM   154  H  HG2  . LYS   A 1 13  ? -1.411  2.917   -2.930  1.00 35.84  ? 10  LYS   A HG2  1 
ATOM   155  H  HG3  . LYS   A 1 13  ? -2.651  2.173   -3.589  1.00 35.84  ? 10  LYS   A HG3  1 
ATOM   156  H  HD2  . LYS   A 1 13  ? -3.862  4.200   -2.600  1.00 45.17  ? 10  LYS   A HD2  1 
ATOM   157  H  HD3  . LYS   A 1 13  ? -2.448  4.862   -2.898  1.00 45.17  ? 10  LYS   A HD3  1 
ATOM   158  H  HE2  . LYS   A 1 13  ? -3.816  3.480   -4.922  1.00 57.09  ? 10  LYS   A HE2  1 
ATOM   159  H  HE3  . LYS   A 1 13  ? -4.081  5.028   -4.679  1.00 57.09  ? 10  LYS   A HE3  1 
ATOM   160  H  HZ1  . LYS   A 1 13  ? -2.446  4.724   -6.240  1.00 66.92  ? 10  LYS   A HZ1  1 
ATOM   161  H  HZ2  . LYS   A 1 13  ? -1.878  5.403   -5.093  1.00 66.92  ? 10  LYS   A HZ2  1 
ATOM   162  H  HZ3  . LYS   A 1 13  ? -1.625  3.991   -5.298  1.00 66.92  ? 10  LYS   A HZ3  1 
ATOM   163  N  N    . LEU   A 1 14  ? -1.577  0.369   1.172   1.00 22.91  ? 11  LEU   A N    1 
ATOM   164  C  CA   . LEU   A 1 14  ? -1.876  -0.167  2.492   1.00 23.25  ? 11  LEU   A CA   1 
ATOM   165  C  C    . LEU   A 1 14  ? -2.243  1.006   3.402   1.00 25.60  ? 11  LEU   A C    1 
ATOM   166  O  O    . LEU   A 1 14  ? -1.449  1.927   3.572   1.00 25.13  ? 11  LEU   A O    1 
ATOM   167  C  CB   . LEU   A 1 14  ? -0.671  -0.910  3.049   1.00 23.02  ? 11  LEU   A CB   1 
ATOM   168  C  CG   . LEU   A 1 14  ? -0.927  -1.726  4.319   1.00 24.89  ? 11  LEU   A CG   1 
ATOM   169  C  CD1  . LEU   A 1 14  ? -1.564  -3.026  3.942   1.00 25.10  ? 11  LEU   A CD1  1 
ATOM   170  C  CD2  . LEU   A 1 14  ? 0.410   -1.949  5.048   1.00 26.81  ? 11  LEU   A CD2  1 
ATOM   171  H  H    . LEU   A 1 14  ? -0.747  0.565   1.063   1.00 27.54  ? 11  LEU   A H    1 
ATOM   172  H  HA   . LEU   A 1 14  ? -2.621  -0.787  2.443   1.00 27.94  ? 11  LEU   A HA   1 
ATOM   173  H  HB2  . LEU   A 1 14  ? -0.352  -1.524  2.370   1.00 27.66  ? 11  LEU   A HB2  1 
ATOM   174  H  HB3  . LEU   A 1 14  ? 0.017   -0.259  3.258   1.00 27.66  ? 11  LEU   A HB3  1 
ATOM   175  H  HG   . LEU   A 1 14  ? -1.526  -1.261  4.923   1.00 29.91  ? 11  LEU   A HG   1 
ATOM   176  H  HD11 . LEU   A 1 14  ? -1.723  -3.545  4.747   1.00 30.16  ? 11  LEU   A HD11 1 
ATOM   177  H  HD12 . LEU   A 1 14  ? -2.404  -2.848  3.492   1.00 30.16  ? 11  LEU   A HD12 1 
ATOM   178  H  HD13 . LEU   A 1 14  ? -0.967  -3.510  3.350   1.00 30.16  ? 11  LEU   A HD13 1 
ATOM   179  H  HD21 . LEU   A 1 14  ? 0.259   -2.525  5.814   1.00 32.21  ? 11  LEU   A HD21 1 
ATOM   180  H  HD22 . LEU   A 1 14  ? 1.036   -2.368  4.437   1.00 32.21  ? 11  LEU   A HD22 1 
ATOM   181  H  HD23 . LEU   A 1 14  ? 0.756   -1.092  5.341   1.00 32.21  ? 11  LEU   A HD23 1 
ATOM   182  N  N    . ARG   A 1 15  ? -3.440  0.980   3.960   1.00 24.16  ? 12  ARG   A N    1 
ATOM   183  C  CA   . ARG   A 1 15  ? -3.896  2.023   4.869   1.00 22.68  ? 12  ARG   A CA   1 
ATOM   184  C  C    . ARG   A 1 15  ? -3.818  1.516   6.303   1.00 26.71  ? 12  ARG   A C    1 
ATOM   185  O  O    . ARG   A 1 15  ? -4.028  0.315   6.568   1.00 24.20  ? 12  ARG   A O    1 
ATOM   186  C  CB   . ARG   A 1 15  ? -5.321  2.458   4.523   1.00 27.26  ? 12  ARG   A CB   1 
ATOM   187  C  CG   . ARG   A 1 15  ? -5.419  3.592   3.511   1.00 30.46  ? 12  ARG   A CG   1 
ATOM   188  C  CD   . ARG   A 1 15  ? -4.633  3.326   2.235   1.00 29.27  ? 12  ARG   A CD   1 
ATOM   189  N  NE   . ARG   A 1 15  ? -4.687  4.455   1.296   1.00 30.67  ? 12  ARG   A NE   1 
ATOM   190  C  CZ   . ARG   A 1 15  ? -5.497  4.540   0.250   1.00 33.29  ? 12  ARG   A CZ   1 
ATOM   191  N  NH1  . ARG   A 1 15  ? -6.405  3.612   -0.007  1.00 31.88  ? 12  ARG   A NH1  1 
ATOM   192  N  NH2  . ARG   A 1 15  ? -5.374  5.568   -0.585  1.00 37.58  ? 12  ARG   A NH2  1 
ATOM   193  H  H    . ARG   A 1 15  ? -4.019  0.358   3.827   1.00 29.04  ? 12  ARG   A H    1 
ATOM   194  H  HA   . ARG   A 1 15  ? -3.326  2.804   4.795   1.00 27.26  ? 12  ARG   A HA   1 
ATOM   195  H  HB2  . ARG   A 1 15  ? -5.794  1.696   4.154   1.00 32.75  ? 12  ARG   A HB2  1 
ATOM   196  H  HB3  . ARG   A 1 15  ? -5.757  2.756   5.337   1.00 32.75  ? 12  ARG   A HB3  1 
ATOM   197  H  HG2  . ARG   A 1 15  ? -6.349  3.716   3.267   1.00 36.59  ? 12  ARG   A HG2  1 
ATOM   198  H  HG3  . ARG   A 1 15  ? -5.069  4.403   3.912   1.00 36.59  ? 12  ARG   A HG3  1 
ATOM   199  H  HD2  . ARG   A 1 15  ? -3.704  3.167   2.462   1.00 35.16  ? 12  ARG   A HD2  1 
ATOM   200  H  HD3  . ARG   A 1 15  ? -5.004  2.547   1.791   1.00 35.16  ? 12  ARG   A HD3  1 
ATOM   201  H  HE   . ARG   A 1 15  ? -4.151  5.112   1.436   1.00 36.85  ? 12  ARG   A HE   1 
ATOM   202  H  HH11 . ARG   A 1 15  ? -6.481  2.930   0.511   1.00 38.29  ? 12  ARG   A HH11 1 
ATOM   203  H  HH12 . ARG   A 1 15  ? -6.919  3.691   -0.692  1.00 38.29  ? 12  ARG   A HH12 1 
ATOM   204  H  HH21 . ARG   A 1 15  ? -4.773  6.168   -0.443  1.00 45.13  ? 12  ARG   A HH21 1 
ATOM   205  H  HH22 . ARG   A 1 15  ? -5.894  5.634   -1.266  1.00 45.13  ? 12  ARG   A HH22 1 
ATOM   206  N  N    . TYR   A 1 16  ? -3.450  2.417   7.218   1.00 26.21  ? 13  TYR   A N    1 
ATOM   207  C  CA   . TYR   A 1 16  ? -3.316  2.058   8.629   1.00 25.63  ? 13  TYR   A CA   1 
ATOM   208  C  C    . TYR   A 1 16  ? -3.615  3.262   9.507   1.00 26.26  ? 13  TYR   A C    1 
ATOM   209  O  O    . TYR   A 1 16  ? -3.512  4.417   9.081   1.00 29.47  ? 13  TYR   A O    1 
ATOM   210  C  CB   . TYR   A 1 16  ? -1.914  1.514   8.947   1.00 25.63  ? 13  TYR   A CB   1 
ATOM   211  C  CG   . TYR   A 1 16  ? -0.750  2.434   8.637   1.00 24.95  ? 13  TYR   A CG   1 
ATOM   212  C  CD1  . TYR   A 1 16  ? -0.260  2.547   7.341   1.00 27.34  ? 13  TYR   A CD1  1 
ATOM   213  C  CD2  . TYR   A 1 16  ? -0.141  3.180   9.632   1.00 27.92  ? 13  TYR   A CD2  1 
ATOM   214  C  CE1  . TYR   A 1 16  ? 0.815   3.371   7.060   1.00 28.10  ? 13  TYR   A CE1  1 
ATOM   215  C  CE2  . TYR   A 1 16  ? 0.919   4.026   9.352   1.00 31.37  ? 13  TYR   A CE2  1 
ATOM   216  C  CZ   . TYR   A 1 16  ? 1.398   4.103   8.059   1.00 29.52  ? 13  TYR   A CZ   1 
ATOM   217  O  OH   . TYR   A 1 16  ? 2.469   4.925   7.779   1.00 31.54  ? 13  TYR   A OH   1 
ATOM   218  H  H    . TYR   A 1 16  ? -3.273  3.240   7.045   1.00 31.50  ? 13  TYR   A H    1 
ATOM   219  H  HA   . TYR   A 1 16  ? -3.973  1.373   8.830   1.00 30.80  ? 13  TYR   A HA   1 
ATOM   220  H  HB2  . TYR   A 1 16  ? -1.876  1.316   9.896   1.00 30.80  ? 13  TYR   A HB2  1 
ATOM   221  H  HB3  . TYR   A 1 16  ? -1.781  0.703   8.433   1.00 30.80  ? 13  TYR   A HB3  1 
ATOM   222  H  HD1  . TYR   A 1 16  ? -0.659  2.064   6.654   1.00 32.85  ? 13  TYR   A HD1  1 
ATOM   223  H  HD2  . TYR   A 1 16  ? -0.451  3.111   10.506  1.00 33.54  ? 13  TYR   A HD2  1 
ATOM   224  H  HE1  . TYR   A 1 16  ? 1.143   3.427   6.191   1.00 33.76  ? 13  TYR   A HE1  1 
ATOM   225  H  HE2  . TYR   A 1 16  ? 1.305   4.537   10.027  1.00 37.69  ? 13  TYR   A HE2  1 
ATOM   226  H  HH   . TYR   A 1 16  ? 2.774   5.251   8.490   1.00 37.89  ? 13  TYR   A HH   1 
ATOM   227  N  N    . HIS   A 1 17  ? -4.023  2.969   10.741  1.00 27.85  ? 14  HIS   A N    1 
ATOM   228  C  CA   . HIS   A 1 17  ? -4.156  3.958   11.795  1.00 29.46  ? 14  HIS   A CA   1 
ATOM   229  C  C    . HIS   A 1 17  ? -2.853  4.041   12.570  1.00 29.21  ? 14  HIS   A C    1 
ATOM   230  O  O    . HIS   A 1 17  ? -2.193  3.023   12.786  1.00 26.45  ? 14  HIS   A O    1 
ATOM   231  C  CB   . HIS   A 1 17  ? -5.278  3.589   12.763  1.00 29.58  ? 14  HIS   A CB   1 
ATOM   232  C  CG   . HIS   A 1 17  ? -6.589  3.308   12.106  1.00 28.44  ? 14  HIS   A CG   1 
ATOM   233  N  ND1  . HIS   A 1 17  ? -7.447  4.307   11.709  1.00 32.22  ? 14  HIS   A ND1  1 
ATOM   234  C  CD2  . HIS   A 1 17  ? -7.199  2.138   11.793  1.00 33.35  ? 14  HIS   A CD2  1 
ATOM   235  C  CE1  . HIS   A 1 17  ? -8.526  3.770   11.168  1.00 31.98  ? 14  HIS   A CE1  1 
ATOM   236  N  NE2  . HIS   A 1 17  ? -8.406  2.456   11.217  1.00 32.76  ? 14  HIS   A NE2  1 
ATOM   237  H  H    . HIS   A 1 17  ? -4.235  2.175   10.996  1.00 33.47  ? 14  HIS   A H    1 
ATOM   238  H  HA   . HIS   A 1 17  ? -4.366  4.819   11.400  1.00 35.39  ? 14  HIS   A HA   1 
ATOM   239  H  HB2  . HIS   A 1 17  ? -5.017  2.791   13.250  1.00 35.54  ? 14  HIS   A HB2  1 
ATOM   240  H  HB3  . HIS   A 1 17  ? -5.410  4.325   13.380  1.00 35.54  ? 14  HIS   A HB3  1 
ATOM   241  H  HD2  . HIS   A 1 17  ? -6.865  1.283   11.940  1.00 40.07  ? 14  HIS   A HD2  1 
ATOM   242  H  HE1  . HIS   A 1 17  ? -9.247  4.238   10.813  1.00 38.42  ? 14  HIS   A HE1  1 
ATOM   243  H  HE2  . HIS   A 1 17  ? -8.989  1.890   10.934  1.00 39.35  ? 14  HIS   A HE2  1 
ATOM   244  N  N    . GLN   A 1 18  ? -2.516  5.254   13.028  1.00 28.05  ? 15  GLN   A N    1 
ATOM   245  C  CA   . GLN   A 1 18  ? -1.319  5.492   13.834  1.00 31.96  ? 15  GLN   A CA   1 
ATOM   246  C  C    . GLN   A 1 18  ? -1.656  6.452   14.962  1.00 32.76  ? 15  GLN   A C    1 
ATOM   247  O  O    . GLN   A 1 18  ? -2.096  7.574   14.701  1.00 34.07  ? 15  GLN   A O    1 
ATOM   248  C  CB   . GLN   A 1 18  ? -0.189  6.081   12.993  1.00 35.14  ? 15  GLN   A CB   1 
ATOM   249  C  CG   . GLN   A 1 18  ? 1.155   6.103   13.703  1.00 35.10  ? 15  GLN   A CG   1 
ATOM   250  C  CD   . GLN   A 1 18  ? 2.270   6.623   12.822  1.00 40.72  ? 15  GLN   A CD   1 
ATOM   251  O  OE1  . GLN   A 1 18  ? 2.393   6.239   11.659  1.00 43.91  ? 15  GLN   A OE1  1 
ATOM   252  N  NE2  . GLN   A 1 18  ? 3.124   7.460   13.388  1.00 39.86  ? 15  GLN   A NE2  1 
ATOM   253  H  H    . GLN   A 1 18  ? -2.976  5.965   12.882  1.00 33.70  ? 15  GLN   A H    1 
ATOM   254  H  HA   . GLN   A 1 18  ? -1.032  4.647   14.213  1.00 38.39  ? 15  GLN   A HA   1 
ATOM   255  H  HB2  . GLN   A 1 18  ? -0.090  5.548   12.188  1.00 42.21  ? 15  GLN   A HB2  1 
ATOM   256  H  HB3  . GLN   A 1 18  ? -0.417  6.994   12.760  1.00 42.21  ? 15  GLN   A HB3  1 
ATOM   257  H  HG2  . GLN   A 1 18  ? 1.093   6.680   14.481  1.00 42.16  ? 15  GLN   A HG2  1 
ATOM   258  H  HG3  . GLN   A 1 18  ? 1.384   5.201   13.977  1.00 42.16  ? 15  GLN   A HG3  1 
ATOM   259  H  HE21 . GLN   A 1 18  ? 3.027   7.679   14.214  1.00 47.87  ? 15  GLN   A HE21 1 
ATOM   260  H  HE22 . GLN   A 1 18  ? 3.776   7.784   12.931  1.00 47.87  ? 15  GLN   A HE22 1 
ATOM   261  N  N    . VAL   A 1 19  ? -1.419  6.024   16.202  1.00 30.34  ? 16  VAL   A N    1 
ATOM   262  C  CA   . VAL   A 1 19  ? -1.623  6.874   17.368  1.00 39.94  ? 16  VAL   A CA   1 
ATOM   263  C  C    . VAL   A 1 19  ? -0.477  6.652   18.342  1.00 33.71  ? 16  VAL   A C    1 
ATOM   264  O  O    . VAL   A 1 19  ? 0.072   5.547   18.444  1.00 39.08  ? 16  VAL   A O    1 
ATOM   265  C  CB   . VAL   A 1 19  ? -2.966  6.586   18.082  1.00 46.85  ? 16  VAL   A CB   1 
ATOM   266  C  CG1  . VAL   A 1 19  ? -4.129  6.627   17.113  1.00 53.82  ? 16  VAL   A CG1  1 
ATOM   267  C  CG2  . VAL   A 1 19  ? -2.906  5.239   18.769  1.00 45.34  ? 16  VAL   A CG2  1 
ATOM   268  H  H    . VAL   A 1 19  ? -1.135  5.235   16.392  1.00 36.45  ? 16  VAL   A H    1 
ATOM   269  H  HA   . VAL   A 1 19  ? -1.621  7.798   17.074  1.00 47.96  ? 16  VAL   A HA   1 
ATOM   270  H  HB   . VAL   A 1 19  ? -3.114  7.277   18.747  1.00 56.26  ? 16  VAL   A HB   1 
ATOM   271  H  HG11 . VAL   A 1 19  ? -4.949  6.440   17.595  1.00 64.63  ? 16  VAL   A HG11 1 
ATOM   272  H  HG12 . VAL   A 1 19  ? -4.175  7.509   16.712  1.00 64.63  ? 16  VAL   A HG12 1 
ATOM   273  H  HG13 . VAL   A 1 19  ? -3.990  5.958   16.425  1.00 64.63  ? 16  VAL   A HG13 1 
ATOM   274  H  HG21 . VAL   A 1 19  ? -3.758  5.066   19.199  1.00 54.45  ? 16  VAL   A HG21 1 
ATOM   275  H  HG22 . VAL   A 1 19  ? -2.724  4.555   18.107  1.00 54.45  ? 16  VAL   A HG22 1 
ATOM   276  H  HG23 . VAL   A 1 19  ? -2.198  5.254   19.433  1.00 54.45  ? 16  VAL   A HG23 1 
ATOM   277  N  N    . GLY   A 1 20  ? -0.172  7.682   19.102  1.00 35.19  ? 17  GLY   A N    1 
ATOM   278  C  CA   . GLY   A 1 20  ? 0.709   7.540   20.229  1.00 38.74  ? 17  GLY   A CA   1 
ATOM   279  C  C    . GLY   A 1 20  ? 2.145   7.865   19.899  1.00 39.71  ? 17  GLY   A C    1 
ATOM   280  O  O    . GLY   A 1 20  ? 2.496   8.389   18.841  1.00 40.38  ? 17  GLY   A O    1 
ATOM   281  H  H    . GLY   A 1 20  ? -0.467  8.481   18.982  1.00 42.27  ? 17  GLY   A H    1 
ATOM   282  H  HA2  . GLY   A 1 20  ? 0.419   8.135   20.937  1.00 46.52  ? 17  GLY   A HA2  1 
ATOM   283  H  HA3  . GLY   A 1 20  ? 0.672   6.625   20.549  1.00 46.52  ? 17  GLY   A HA3  1 
ATOM   284  N  N    . GLN   A 1 21  ? 2.995   7.551   20.867  1.00 38.25  ? 18  GLN   A N    1 
ATOM   285  C  CA   . GLN   A 1 21  ? 4.416   7.837   20.761  1.00 43.91  ? 18  GLN   A CA   1 
ATOM   286  C  C    . GLN   A 1 21  ? 5.160   6.736   21.498  1.00 38.95  ? 18  GLN   A C    1 
ATOM   287  O  O    . GLN   A 1 21  ? 4.608   6.075   22.388  1.00 39.34  ? 18  GLN   A O    1 
ATOM   288  C  CB   . GLN   A 1 21  ? 4.781   9.220   21.329  1.00 45.40  ? 18  GLN   A CB   1 
ATOM   289  C  CG   . GLN   A 1 21  ? 4.154   9.575   22.669  1.00 62.75  ? 18  GLN   A CG   1 
ATOM   290  C  CD   . GLN   A 1 21  ? 2.673   9.945   22.579  1.00 76.55  ? 18  GLN   A CD   1 
ATOM   291  O  OE1  . GLN   A 1 21  ? 1.795   9.084   22.683  1.00 74.48  ? 18  GLN   A OE1  1 
ATOM   292  N  NE2  . GLN   A 1 21  ? 2.396   11.231  22.346  1.00 63.49  ? 18  GLN   A NE2  1 
ATOM   293  H  H    . GLN   A 1 21  ? 2.770   7.167   21.603  1.00 45.94  ? 18  GLN   A H    1 
ATOM   294  H  HA   . GLN   A 1 21  ? 4.687   7.837   19.830  1.00 52.73  ? 18  GLN   A HA   1 
ATOM   295  H  HB2  . GLN   A 1 21  ? 5.744   9.257   21.444  1.00 54.52  ? 18  GLN   A HB2  1 
ATOM   296  H  HB3  . GLN   A 1 21  ? 4.497   9.895   20.692  1.00 54.52  ? 18  GLN   A HB3  1 
ATOM   297  H  HG2  . GLN   A 1 21  ? 4.232   8.811   23.262  1.00 75.34  ? 18  GLN   A HG2  1 
ATOM   298  H  HG3  . GLN   A 1 21  ? 4.626   10.335  23.043  1.00 75.34  ? 18  GLN   A HG3  1 
ATOM   299  H  HE21 . GLN   A 1 21  ? 3.035   11.799  22.256  1.00 76.23  ? 18  GLN   A HE21 1 
ATOM   300  H  HE22 . GLN   A 1 21  ? 1.578   11.491  22.287  1.00 76.23  ? 18  GLN   A HE22 1 
ATOM   301  N  N    . GLY   A 1 22  ? 6.399   6.507   21.077  1.00 40.00  ? 19  GLY   A N    1 
ATOM   302  C  CA   . GLY   A 1 22  ? 7.190   5.430   21.613  1.00 40.59  ? 19  GLY   A CA   1 
ATOM   303  C  C    . GLY   A 1 22  ? 7.447   4.349   20.583  1.00 35.84  ? 19  GLY   A C    1 
ATOM   304  O  O    . GLY   A 1 22  ? 7.212   4.522   19.395  1.00 35.76  ? 19  GLY   A O    1 
ATOM   305  H  H    . GLY   A 1 22  ? 6.801   6.973   20.475  1.00 48.05  ? 19  GLY   A H    1 
ATOM   306  H  HA2  . GLY   A 1 22  ? 8.044   5.776   21.915  1.00 48.75  ? 19  GLY   A HA2  1 
ATOM   307  H  HA3  . GLY   A 1 22  ? 6.725   5.033   22.366  1.00 48.75  ? 19  GLY   A HA3  1 
ATOM   308  N  N    . PRO   A 1 23  ? 7.953   3.213   21.039  1.00 34.33  ? 20  PRO   A N    1 
ATOM   309  C  CA   . PRO   A 1 23  ? 8.244   2.112   20.116  1.00 32.64  ? 20  PRO   A CA   1 
ATOM   310  C  C    . PRO   A 1 23  ? 7.001   1.696   19.342  1.00 31.53  ? 20  PRO   A C    1 
ATOM   311  O  O    . PRO   A 1 23  ? 5.872   1.769   19.839  1.00 30.38  ? 20  PRO   A O    1 
ATOM   312  C  CB   . PRO   A 1 23  ? 8.737   0.982   21.027  1.00 32.64  ? 20  PRO   A CB   1 
ATOM   313  C  CG   . PRO   A 1 23  ? 8.773   1.535   22.421  1.00 39.81  ? 20  PRO   A CG   1 
ATOM   314  C  CD   . PRO   A 1 23  ? 8.133   2.860   22.457  1.00 36.02  ? 20  PRO   A CD   1 
ATOM   315  H  HA   . PRO   A 1 23  ? 8.950   2.363   19.500  1.00 39.21  ? 20  PRO   A HA   1 
ATOM   316  H  HB2  . PRO   A 1 23  ? 8.123   0.233   20.974  1.00 39.21  ? 20  PRO   A HB2  1 
ATOM   317  H  HB3  . PRO   A 1 23  ? 9.623   0.705   20.748  1.00 39.21  ? 20  PRO   A HB3  1 
ATOM   318  H  HG2  . PRO   A 1 23  ? 8.299   0.926   23.008  1.00 47.82  ? 20  PRO   A HG2  1 
ATOM   319  H  HG3  . PRO   A 1 23  ? 9.699   1.611   22.700  1.00 47.82  ? 20  PRO   A HG3  1 
ATOM   320  H  HD2  . PRO   A 1 23  ? 7.276   2.813   22.908  1.00 43.27  ? 20  PRO   A HD2  1 
ATOM   321  H  HD3  . PRO   A 1 23  ? 8.707   3.505   22.899  1.00 43.27  ? 20  PRO   A HD3  1 
ATOM   322  N  N    . VAL   A 1 24  ? 7.221   1.212   18.115  1.00 28.60  ? 21  VAL   A N    1 
ATOM   323  C  CA   . VAL   A 1 24  ? 6.096   0.822   17.282  1.00 28.44  ? 21  VAL   A CA   1 
ATOM   324  C  C    . VAL   A 1 24  ? 5.513   -0.505  17.753  1.00 27.06  ? 21  VAL   A C    1 
ATOM   325  O  O    . VAL   A 1 24  ? 6.237   -1.471  18.049  1.00 27.21  ? 21  VAL   A O    1 
ATOM   326  C  CB   . VAL   A 1 24  ? 6.542   0.737   15.816  1.00 26.75  ? 21  VAL   A CB   1 
ATOM   327  C  CG1  . VAL   A 1 24  ? 5.502   0.020   14.958  1.00 28.39  ? 21  VAL   A CG1  1 
ATOM   328  C  CG2  . VAL   A 1 24  ? 6.802   2.131   15.289  1.00 30.22  ? 21  VAL   A CG2  1 
ATOM   329  H  H    . VAL   A 1 24  ? 7.995   1.104   17.756  1.00 34.37  ? 21  VAL   A H    1 
ATOM   330  H  HA   . VAL   A 1 24  ? 5.401   1.494   17.364  1.00 34.17  ? 21  VAL   A HA   1 
ATOM   331  H  HB   . VAL   A 1 24  ? 7.361   0.219   15.764  1.00 32.14  ? 21  VAL   A HB   1 
ATOM   332  H  HG11 . VAL   A 1 24  ? 5.681   0.207   14.023  1.00 34.11  ? 21  VAL   A HG11 1 
ATOM   333  H  HG12 . VAL   A 1 24  ? 5.561   -0.935  15.121  1.00 34.11  ? 21  VAL   A HG12 1 
ATOM   334  H  HG13 . VAL   A 1 24  ? 4.619   0.342   15.196  1.00 34.11  ? 21  VAL   A HG13 1 
ATOM   335  H  HG21 . VAL   A 1 24  ? 7.092   2.070   14.365  1.00 36.30  ? 21  VAL   A HG21 1 
ATOM   336  H  HG22 . VAL   A 1 24  ? 5.983   2.647   15.345  1.00 36.30  ? 21  VAL   A HG22 1 
ATOM   337  H  HG23 . VAL   A 1 24  ? 7.493   2.548   15.826  1.00 36.30  ? 21  VAL   A HG23 1 
ATOM   338  N  N    . LEU   A 1 25  ? 4.182   -0.570  17.790  1.00 22.69  ? 22  LEU   A N    1 
ATOM   339  C  CA   . LEU   A 1 25  ? 3.421   -1.779  18.097  1.00 21.11  ? 22  LEU   A CA   1 
ATOM   340  C  C    . LEU   A 1 25  ? 2.401   -1.928  16.980  1.00 23.62  ? 22  LEU   A C    1 
ATOM   341  O  O    . LEU   A 1 25  ? 1.512   -1.078  16.838  1.00 25.79  ? 22  LEU   A O    1 
ATOM   342  C  CB   . LEU   A 1 25  ? 2.737   -1.664  19.457  1.00 24.92  ? 22  LEU   A CB   1 
ATOM   343  C  CG   . LEU   A 1 25  ? 1.659   -2.690  19.804  1.00 25.57  ? 22  LEU   A CG   1 
ATOM   344  C  CD1  . LEU   A 1 25  ? 2.123   -4.113  19.515  1.00 32.09  ? 22  LEU   A CD1  1 
ATOM   345  C  CD2  . LEU   A 1 25  ? 1.202   -2.533  21.238  1.00 28.55  ? 22  LEU   A CD2  1 
ATOM   346  H  H    . LEU   A 1 25  ? 3.674   0.106   17.632  1.00 27.27  ? 22  LEU   A H    1 
ATOM   347  H  HA   . LEU   A 1 25  ? 3.997   -2.559  18.123  1.00 25.37  ? 22  LEU   A HA   1 
ATOM   348  H  HB2  . LEU   A 1 25  ? 3.422   -1.738  20.140  1.00 29.95  ? 22  LEU   A HB2  1 
ATOM   349  H  HB3  . LEU   A 1 25  ? 2.316   -0.791  19.503  1.00 29.95  ? 22  LEU   A HB3  1 
ATOM   350  H  HG   . LEU   A 1 25  ? 0.890   -2.527  19.235  1.00 30.73  ? 22  LEU   A HG   1 
ATOM   351  H  HD11 . LEU   A 1 25  ? 1.458   -4.736  19.849  1.00 38.55  ? 22  LEU   A HD11 1 
ATOM   352  H  HD12 . LEU   A 1 25  ? 2.228   -4.223  18.557  1.00 38.55  ? 22  LEU   A HD12 1 
ATOM   353  H  HD13 . LEU   A 1 25  ? 2.971   -4.265  19.961  1.00 38.55  ? 22  LEU   A HD13 1 
ATOM   354  H  HD21 . LEU   A 1 25  ? 0.425   -3.094  21.385  1.00 34.30  ? 22  LEU   A HD21 1 
ATOM   355  H  HD22 . LEU   A 1 25  ? 1.922   -2.804  21.830  1.00 34.30  ? 22  LEU   A HD22 1 
ATOM   356  H  HD23 . LEU   A 1 25  ? 0.975   -1.604  21.398  1.00 34.30  ? 22  LEU   A HD23 1 
ATOM   357  N  N    . ILE   A 1 26  ? 2.567   -2.950  16.145  1.00 19.76  ? 23  ILE   A N    1 
ATOM   358  C  CA   . ILE   A 1 26  ? 1.674   -3.204  15.013  1.00 20.03  ? 23  ILE   A CA   1 
ATOM   359  C  C    . ILE   A 1 26  ? 0.648   -4.249  15.394  1.00 18.69  ? 23  ILE   A C    1 
ATOM   360  O  O    . ILE   A 1 26  ? 1.020   -5.357  15.787  1.00 20.11  ? 23  ILE   A O    1 
ATOM   361  C  CB   . ILE   A 1 26  ? 2.441   -3.665  13.763  1.00 20.25  ? 23  ILE   A CB   1 
ATOM   362  C  CG1  . ILE   A 1 26  ? 3.460   -2.600  13.358  1.00 21.91  ? 23  ILE   A CG1  1 
ATOM   363  C  CG2  . ILE   A 1 26  ? 1.459   -3.963  12.605  1.00 20.99  ? 23  ILE   A CG2  1 
ATOM   364  C  CD1  . ILE   A 1 26  ? 4.329   -2.966  12.162  1.00 23.30  ? 23  ILE   A CD1  1 
ATOM   365  H  H    . ILE   A 1 26  ? 3.204   -3.524  16.213  1.00 23.76  ? 23  ILE   A H    1 
ATOM   366  H  HA   . ILE   A 1 26  ? 1.214   -2.373  14.815  1.00 24.08  ? 23  ILE   A HA   1 
ATOM   367  H  HB   . ILE   A 1 26  ? 2.917   -4.485  13.970  1.00 24.34  ? 23  ILE   A HB   1 
ATOM   368  H  HG12 . ILE   A 1 26  ? 2.981   -1.787  13.132  1.00 26.33  ? 23  ILE   A HG12 1 
ATOM   369  H  HG13 . ILE   A 1 26  ? 4.051   -2.440  14.110  1.00 26.33  ? 23  ILE   A HG13 1 
ATOM   370  H  HG21 . ILE   A 1 26  ? 1.964   -4.252  11.829  1.00 25.23  ? 23  ILE   A HG21 1 
ATOM   371  H  HG22 . ILE   A 1 26  ? 0.848   -4.663  12.881  1.00 25.23  ? 23  ILE   A HG22 1 
ATOM   372  H  HG23 . ILE   A 1 26  ? 0.964   -3.155  12.396  1.00 25.23  ? 23  ILE   A HG23 1 
ATOM   373  H  HD11 . ILE   A 1 26  ? 5.075   -2.349  12.113  1.00 28.01  ? 23  ILE   A HD11 1 
ATOM   374  H  HD12 . ILE   A 1 26  ? 4.656   -3.873  12.275  1.00 28.01  ? 23  ILE   A HD12 1 
ATOM   375  H  HD13 . ILE   A 1 26  ? 3.796   -2.906  11.354  1.00 28.01  ? 23  ILE   A HD13 1 
ATOM   376  N  N    . PHE   A 1 27  ? -0.629  -3.922  15.189  1.00 19.24  ? 24  PHE   A N    1 
ATOM   377  C  CA   . PHE   A 1 27  ? -1.741  -4.851  15.371  1.00 19.20  ? 24  PHE   A CA   1 
ATOM   378  C  C    . PHE   A 1 27  ? -2.246  -5.331  14.022  1.00 17.82  ? 24  PHE   A C    1 
ATOM   379  O  O    . PHE   A 1 27  ? -2.547  -4.499  13.147  1.00 19.75  ? 24  PHE   A O    1 
ATOM   380  C  CB   . PHE   A 1 27  ? -2.912  -4.186  16.113  1.00 21.21  ? 24  PHE   A CB   1 
ATOM   381  C  CG   . PHE   A 1 27  ? -2.690  -4.006  17.604  1.00 21.01  ? 24  PHE   A CG   1 
ATOM   382  C  CD1  . PHE   A 1 27  ? -2.531  -5.094  18.443  1.00 25.05  ? 24  PHE   A CD1  1 
ATOM   383  C  CD2  . PHE   A 1 27  ? -2.642  -2.759  18.145  1.00 24.62  ? 24  PHE   A CD2  1 
ATOM   384  C  CE1  . PHE   A 1 27  ? -2.316  -4.894  19.832  1.00 23.62  ? 24  PHE   A CE1  1 
ATOM   385  C  CE2  . PHE   A 1 27  ? -2.427  -2.559  19.516  1.00 25.47  ? 24  PHE   A CE2  1 
ATOM   386  C  CZ   . PHE   A 1 27  ? -2.264  -3.643  20.343  1.00 25.58  ? 24  PHE   A CZ   1 
ATOM   387  H  H    . PHE   A 1 27  ? -0.883  -3.141  14.934  1.00 23.12  ? 24  PHE   A H    1 
ATOM   388  H  HA   . PHE   A 1 27  ? -1.419  -5.607  15.887  1.00 23.08  ? 24  PHE   A HA   1 
ATOM   389  H  HB2  . PHE   A 1 27  ? -3.061  -3.307  15.730  1.00 25.49  ? 24  PHE   A HB2  1 
ATOM   390  H  HB3  . PHE   A 1 27  ? -3.702  -4.736  15.999  1.00 25.49  ? 24  PHE   A HB3  1 
ATOM   391  H  HD1  . PHE   A 1 27  ? -2.565  -5.957  18.097  1.00 30.10  ? 24  PHE   A HD1  1 
ATOM   392  H  HD2  . PHE   A 1 27  ? -2.754  -2.020  17.592  1.00 29.58  ? 24  PHE   A HD2  1 
ATOM   393  H  HE1  . PHE   A 1 27  ? -2.210  -5.628  20.394  1.00 28.38  ? 24  PHE   A HE1  1 
ATOM   394  H  HE2  . PHE   A 1 27  ? -2.396  -1.697  19.863  1.00 30.61  ? 24  PHE   A HE2  1 
ATOM   395  H  HZ   . PHE   A 1 27  ? -2.117  -3.517  21.253  1.00 30.74  ? 24  PHE   A HZ   1 
ATOM   396  N  N    . ILE   A 1 28  ? -2.348  -6.644  13.859  1.00 16.97  ? 25  ILE   A N    1 
ATOM   397  C  CA   . ILE   A 1 28  ? -2.768  -7.288  12.611  1.00 16.94  ? 25  ILE   A CA   1 
ATOM   398  C  C    . ILE   A 1 28  ? -4.135  -7.916  12.830  1.00 17.57  ? 25  ILE   A C    1 
ATOM   399  O  O    . ILE   A 1 28  ? -4.274  -8.833  13.653  1.00 17.92  ? 25  ILE   A O    1 
ATOM   400  C  CB   . ILE   A 1 28  ? -1.789  -8.366  12.152  1.00 14.90  ? 25  ILE   A CB   1 
ATOM   401  C  CG1  . ILE   A 1 28  ? -0.362  -7.862  12.167  1.00 17.06  ? 25  ILE   A CG1  1 
ATOM   402  C  CG2  . ILE   A 1 28  ? -2.210  -8.897  10.771  1.00 16.32  ? 25  ILE   A CG2  1 
ATOM   403  C  CD1  . ILE   A 1 28  ? 0.632   -8.929  11.898  1.00 18.37  ? 25  ILE   A CD1  1 
ATOM   404  H  H    . ILE   A 1 28  ? -2.173  -7.210  14.482  1.00 20.41  ? 25  ILE   A H    1 
ATOM   405  H  HA   . ILE   A 1 28  ? -2.829  -6.601  11.929  1.00 20.37  ? 25  ILE   A HA   1 
ATOM   406  H  HB   . ILE   A 1 28  ? -1.819  -9.104  12.781  1.00 17.92  ? 25  ILE   A HB   1 
ATOM   407  H  HG12 . ILE   A 1 28  ? -0.262  -7.181  11.483  1.00 20.51  ? 25  ILE   A HG12 1 
ATOM   408  H  HG13 . ILE   A 1 28  ? -0.169  -7.487  13.040  1.00 20.51  ? 25  ILE   A HG13 1 
ATOM   409  H  HG21 . ILE   A 1 28  ? -1.541  -9.524  10.456  1.00 19.62  ? 25  ILE   A HG21 1 
ATOM   410  H  HG22 . ILE   A 1 28  ? -3.068  -9.342  10.852  1.00 19.62  ? 25  ILE   A HG22 1 
ATOM   411  H  HG23 . ILE   A 1 28  ? -2.282  -8.151  10.155  1.00 19.62  ? 25  ILE   A HG23 1 
ATOM   412  H  HD11 . ILE   A 1 28  ? 1.521   -8.586  12.082  1.00 22.08  ? 25  ILE   A HD11 1 
ATOM   413  H  HD12 . ILE   A 1 28  ? 0.444   -9.687  12.473  1.00 22.08  ? 25  ILE   A HD12 1 
ATOM   414  H  HD13 . ILE   A 1 28  ? 0.566   -9.195  10.967  1.00 22.08  ? 25  ILE   A HD13 1 
ATOM   415  N  N    . PRO   A 1 29  ? -5.155  -7.470  12.126  1.00 17.26  ? 26  PRO   A N    1 
ATOM   416  C  CA   . PRO   A 1 29  ? -6.497  -7.990  12.339  1.00 18.24  ? 26  PRO   A CA   1 
ATOM   417  C  C    . PRO   A 1 29  ? -6.695  -9.364  11.727  1.00 18.28  ? 26  PRO   A C    1 
ATOM   418  O  O    . PRO   A 1 29  ? -6.004  -9.785  10.783  1.00 18.32  ? 26  PRO   A O    1 
ATOM   419  C  CB   . PRO   A 1 29  ? -7.370  -6.954  11.631  1.00 19.23  ? 26  PRO   A CB   1 
ATOM   420  C  CG   . PRO   A 1 29  ? -6.540  -6.485  10.522  1.00 22.24  ? 26  PRO   A CG   1 
ATOM   421  C  CD   . PRO   A 1 29  ? -5.113  -6.444  11.060  1.00 20.10  ? 26  PRO   A CD   1 
ATOM   422  H  HA   . PRO   A 1 29  ? -6.706  -8.029  13.285  1.00 21.94  ? 26  PRO   A HA   1 
ATOM   423  H  HB2  . PRO   A 1 29  ? -8.184  -7.370  11.307  1.00 23.12  ? 26  PRO   A HB2  1 
ATOM   424  H  HB3  . PRO   A 1 29  ? -7.586  -6.229  12.237  1.00 23.12  ? 26  PRO   A HB3  1 
ATOM   425  H  HG2  . PRO   A 1 29  ? -6.609  -7.103  9.778   1.00 26.73  ? 26  PRO   A HG2  1 
ATOM   426  H  HG3  . PRO   A 1 29  ? -6.830  -5.602  10.248  1.00 26.73  ? 26  PRO   A HG3  1 
ATOM   427  H  HD2  . PRO   A 1 29  ? -4.472  -6.680  10.372  1.00 24.17  ? 26  PRO   A HD2  1 
ATOM   428  H  HD3  . PRO   A 1 29  ? -4.902  -5.570  11.424  1.00 24.17  ? 26  PRO   A HD3  1 
ATOM   429  N  N    . GLY   A 1 30  ? -7.676  -10.052 12.307  1.00 20.48  ? 27  GLY   A N    1 
ATOM   430  C  CA   . GLY   A 1 30  ? -8.199  -11.307 11.769  1.00 20.34  ? 27  GLY   A CA   1 
ATOM   431  C  C    . GLY   A 1 30  ? -9.197  -11.142 10.642  1.00 23.37  ? 27  GLY   A C    1 
ATOM   432  O  O    . GLY   A 1 30  ? -9.023  -10.314 9.750   1.00 21.65  ? 27  GLY   A O    1 
ATOM   433  H  H    . GLY   A 1 30  ? -8.068  -9.808  13.032  1.00 24.62  ? 27  GLY   A H    1 
ATOM   434  H  HA2  . GLY   A 1 30  ? -7.458  -11.836 11.434  1.00 24.45  ? 27  GLY   A HA2  1 
ATOM   435  H  HA3  . GLY   A 1 30  ? -8.637  -11.795 12.484  1.00 24.45  ? 27  GLY   A HA3  1 
ATOM   436  N  N    . ALA   A 1 31  ? -10.253 -11.949 10.670  1.00 22.97  ? 28  ALA   A N    1 
ATOM   437  C  CA   . ALA   A 1 31  ? -11.122 -12.075 9.508   1.00 25.07  ? 28  ALA   A CA   1 
ATOM   438  C  C    . ALA   A 1 31  ? -11.845 -10.777 9.158   1.00 24.82  ? 28  ALA   A C    1 
ATOM   439  O  O    . ALA   A 1 31  ? -12.239 -10.591 7.992   1.00 28.55  ? 28  ALA   A O    1 
ATOM   440  C  CB   . ALA   A 1 31  ? -12.144 -13.195 9.740   1.00 31.11  ? 28  ALA   A CB   1 
ATOM   441  H  H    . ALA   A 1 31  ? -10.486 -12.430 11.344  1.00 27.61  ? 28  ALA   A H    1 
ATOM   442  H  HA   . ALA   A 1 31  ? -10.566 -12.307 8.748   1.00 30.13  ? 28  ALA   A HA   1 
ATOM   443  H  HB1  . ALA   A 1 31  ? -12.720 -13.263 8.962   1.00 37.37  ? 28  ALA   A HB1  1 
ATOM   444  H  HB2  . ALA   A 1 31  ? -11.671 -14.031 9.875   1.00 37.37  ? 28  ALA   A HB2  1 
ATOM   445  H  HB3  . ALA   A 1 31  ? -12.673 -12.983 10.525  1.00 37.37  ? 28  ALA   A HB3  1 
ATOM   446  N  N    . ASN   A 1 32  ? -12.097 -9.890  10.127  1.00 24.87  ? 29  ASN   A N    1 
ATOM   447  C  CA   . ASN   A 1 32  ? -12.723 -8.610  9.781   1.00 24.99  ? 29  ASN   A CA   1 
ATOM   448  C  C    . ASN   A 1 32  ? -11.813 -7.768  8.886   1.00 26.59  ? 29  ASN   A C    1 
ATOM   449  O  O    . ASN   A 1 32  ? -12.283 -6.880  8.159   1.00 26.23  ? 29  ASN   A O    1 
ATOM   450  C  CB   . ASN   A 1 32  ? -13.081 -7.840  11.059  1.00 26.17  ? 29  ASN   A CB   1 
ATOM   451  C  CG   . ASN   A 1 32  ? -11.849 -7.424  11.847  1.00 28.27  ? 29  ASN   A CG   1 
ATOM   452  O  OD1  . ASN   A 1 32  ? -11.158 -8.265  12.424  1.00 27.90  ? 29  ASN   A OD1  1 
ATOM   453  N  ND2  . ASN   A 1 32  ? -11.550 -6.120  11.849  1.00 30.17  ? 29  ASN   A ND2  1 
ATOM   454  H  H    . ASN   A 1 32  ? -11.923 -10.001 10.962  1.00 29.89  ? 29  ASN   A H    1 
ATOM   455  H  HA   . ASN   A 1 32  ? -13.546 -8.780  9.295   1.00 30.03  ? 29  ASN   A HA   1 
ATOM   456  H  HB2  . ASN   A 1 32  ? -13.571 -7.037  10.820  1.00 31.45  ? 29  ASN   A HB2  1 
ATOM   457  H  HB3  . ASN   A 1 32  ? -13.627 -8.405  11.628  1.00 31.45  ? 29  ASN   A HB3  1 
ATOM   458  H  HD21 . ASN   A 1 32  ? -10.862 -5.837  12.281  1.00 36.24  ? 29  ASN   A HD21 1 
ATOM   459  H  HD22 . ASN   A 1 32  ? -12.045 -5.565  11.417  1.00 36.24  ? 29  ASN   A HD22 1 
ATOM   460  N  N    . GLY   A 1 33  ? -10.519 -7.991  8.977   1.00 21.87  ? 30  GLY   A N    1 
ATOM   461  C  CA   . GLY   A 1 33  ? -9.553  -7.443  8.046   1.00 22.67  ? 30  GLY   A CA   1 
ATOM   462  C  C    . GLY   A 1 33  ? -9.109  -6.019  8.312   1.00 23.93  ? 30  GLY   A C    1 
ATOM   463  O  O    . GLY   A 1 33  ? -8.166  -5.562  7.648   1.00 22.05  ? 30  GLY   A O    1 
ATOM   464  H  H    . GLY   A 1 33  ? -10.160 -8.474  9.592   1.00 26.28  ? 30  GLY   A H    1 
ATOM   465  H  HA2  . GLY   A 1 33  ? -8.761  -8.003  8.062   1.00 27.24  ? 30  GLY   A HA2  1 
ATOM   466  H  HA3  . GLY   A 1 33  ? -9.939  -7.466  7.156   1.00 27.24  ? 30  GLY   A HA3  1 
ATOM   467  N  N    . THR   A 1 34  ? -9.698  -5.319  9.290   1.00 22.98  ? 31  THR   A N    1 
ATOM   468  C  CA   . THR   A 1 34  ? -9.514  -3.874  9.421   1.00 24.55  ? 31  THR   A CA   1 
ATOM   469  C  C    . THR   A 1 34  ? -9.004  -3.483  10.799  1.00 24.54  ? 31  THR   A C    1 
ATOM   470  O  O    . THR   A 1 34  ? -9.326  -4.113  11.810  1.00 24.74  ? 31  THR   A O    1 
ATOM   471  C  CB   . THR   A 1 34  ? -10.809 -3.125  9.102   1.00 25.99  ? 31  THR   A CB   1 
ATOM   472  O  OG1  . THR   A 1 34  ? -11.886 -3.554  9.955   1.00 26.47  ? 31  THR   A OG1  1 
ATOM   473  C  CG2  . THR   A 1 34  ? -11.204 -3.395  7.655   1.00 30.02  ? 31  THR   A CG2  1 
ATOM   474  H  H    . THR   A 1 34  ? -10.210 -5.663  9.889   1.00 27.62  ? 31  THR   A H    1 
ATOM   475  H  HA   . THR   A 1 34  ? -8.825  -3.598  8.797   1.00 29.50  ? 31  THR   A HA   1 
ATOM   476  H  HB   . THR   A 1 34  ? -10.664 -2.176  9.243   1.00 31.23  ? 31  THR   A HB   1 
ATOM   477  H  HG1  . THR   A 1 34  ? -11.689 -3.412  10.759  1.00 31.81  ? 31  THR   A HG1  1 
ATOM   478  H  HG21 . THR   A 1 34  ? -11.969 -2.850  7.413   1.00 36.07  ? 31  THR   A HG21 1 
ATOM   479  H  HG22 . THR   A 1 34  ? -10.465 -3.181  7.064   1.00 36.07  ? 31  THR   A HG22 1 
ATOM   480  H  HG23 . THR   A 1 34  ? -11.436 -4.330  7.543   1.00 36.07  ? 31  THR   A HG23 1 
ATOM   481  N  N    . GLY   A 1 35  ? -8.192  -2.429  10.823  1.00 24.72  ? 32  GLY   A N    1 
ATOM   482  C  CA   . GLY   A 1 35  ? -7.551  -2.024  12.066  1.00 22.01  ? 32  GLY   A CA   1 
ATOM   483  C  C    . GLY   A 1 35  ? -8.418  -1.264  13.037  1.00 24.89  ? 32  GLY   A C    1 
ATOM   484  O  O    . GLY   A 1 35  ? -8.024  -1.120  14.204  1.00 25.69  ? 32  GLY   A O    1 
ATOM   485  H  H    . GLY   A 1 35  ? -8.000  -1.940  10.143  1.00 29.70  ? 32  GLY   A H    1 
ATOM   486  H  HA2  . GLY   A 1 35  ? -7.233  -2.821  12.520  1.00 26.45  ? 32  GLY   A HA2  1 
ATOM   487  H  HA3  . GLY   A 1 35  ? -6.792  -1.460  11.849  1.00 26.45  ? 32  GLY   A HA3  1 
ATOM   488  N  N    . ASP   A 1 36  ? -9.598  -0.779  12.609  1.00 23.87  ? 33  ASP   A N    1 
ATOM   489  C  CA   . ASP   A 1 36  ? -10.439 0.000   13.501  1.00 27.59  ? 33  ASP   A CA   1 
ATOM   490  C  C    . ASP   A 1 36  ? -10.812 -0.768  14.768  1.00 27.51  ? 33  ASP   A C    1 
ATOM   491  O  O    . ASP   A 1 36  ? -11.053 -0.151  15.814  1.00 29.14  ? 33  ASP   A O    1 
ATOM   492  C  CB   . ASP   A 1 36  ? -11.718 0.466   12.796  1.00 29.34  ? 33  ASP   A CB   1 
ATOM   493  C  CG   . ASP   A 1 36  ? -12.372 -0.601  11.929  1.00 39.27  ? 33  ASP   A CG   1 
ATOM   494  O  OD1  . ASP   A 1 36  ? -12.009 -1.800  11.970  1.00 35.71  ? 33  ASP   A OD1  1 
ATOM   495  O  OD2  . ASP   A 1 36  ? -13.313 -0.202  11.204  1.00 49.27  ? 33  ASP   A OD2  1 
ATOM   496  H  H    . ASP   A 1 36  ? -9.920  -0.891  11.819  1.00 28.69  ? 33  ASP   A H    1 
ATOM   497  H  HA   . ASP   A 1 36  ? -9.930  0.786   13.754  1.00 33.15  ? 33  ASP   A HA   1 
ATOM   498  H  HB2  . ASP   A 1 36  ? -12.363 0.735   13.468  1.00 35.25  ? 33  ASP   A HB2  1 
ATOM   499  H  HB3  . ASP   A 1 36  ? -11.501 1.218   12.223  1.00 35.25  ? 33  ASP   A HB3  1 
ATOM   500  N  N    . ILE   A 1 37  ? -10.851 -2.097  14.688  1.00 26.89  ? 34  ILE   A N    1 
ATOM   501  C  CA   . ILE   A 1 37  ? -11.207 -2.932  15.826  1.00 25.96  ? 34  ILE   A CA   1 
ATOM   502  C  C    . ILE   A 1 37  ? -10.207 -2.806  16.974  1.00 25.95  ? 34  ILE   A C    1 
ATOM   503  O  O    . ILE   A 1 37  ? -10.535 -3.129  18.120  1.00 28.21  ? 34  ILE   A O    1 
ATOM   504  C  CB   . ILE   A 1 37  ? -11.344 -4.397  15.333  1.00 22.29  ? 34  ILE   A CB   1 
ATOM   505  C  CG1  . ILE   A 1 37  ? -12.221 -5.195  16.315  1.00 28.15  ? 34  ILE   A CG1  1 
ATOM   506  C  CG2  . ILE   A 1 37  ? -10.001 -5.031  15.117  1.00 23.91  ? 34  ILE   A CG2  1 
ATOM   507  C  CD1  . ILE   A 1 37  ? -12.656 -6.551  15.760  1.00 29.81  ? 34  ILE   A CD1  1 
ATOM   508  H  H    . ILE   A 1 37  ? -10.671 -2.544  13.975  1.00 32.32  ? 34  ILE   A H    1 
ATOM   509  H  HA   . ILE   A 1 37  ? -12.060 -2.642  16.185  1.00 31.19  ? 34  ILE   A HA   1 
ATOM   510  H  HB   . ILE   A 1 37  ? -11.785 -4.396  14.469  1.00 26.79  ? 34  ILE   A HB   1 
ATOM   511  H  HG12 . ILE   A 1 37  ? -11.718 -5.352  17.130  1.00 33.82  ? 34  ILE   A HG12 1 
ATOM   512  H  HG13 . ILE   A 1 37  ? -13.020 -4.682  16.513  1.00 33.82  ? 34  ILE   A HG13 1 
ATOM   513  H  HG21 . ILE   A 1 37  ? -10.122 -5.877  14.657  1.00 28.73  ? 34  ILE   A HG21 1 
ATOM   514  H  HG22 . ILE   A 1 37  ? -9.454  -4.438  14.580  1.00 28.73  ? 34  ILE   A HG22 1 
ATOM   515  H  HG23 . ILE   A 1 37  ? -9.580  -5.181  15.979  1.00 28.73  ? 34  ILE   A HG23 1 
ATOM   516  H  HD11 . ILE   A 1 37  ? -13.175 -7.016  16.434  1.00 35.81  ? 34  ILE   A HD11 1 
ATOM   517  H  HD12 . ILE   A 1 37  ? -13.195 -6.409  14.967  1.00 35.81  ? 34  ILE   A HD12 1 
ATOM   518  H  HD13 . ILE   A 1 37  ? -11.867 -7.068  15.535  1.00 35.81  ? 34  ILE   A HD13 1 
ATOM   519  N  N    . PHE   A 1 38  ? -9.017  -2.298  16.702  1.00 24.04  ? 35  PHE   A N    1 
ATOM   520  C  CA   . PHE   A 1 38  ? -7.997  -2.106  17.720  1.00 24.90  ? 35  PHE   A CA   1 
ATOM   521  C  C    . PHE   A 1 38  ? -7.945  -0.689  18.280  1.00 26.55  ? 35  PHE   A C    1 
ATOM   522  O  O    . PHE   A 1 38  ? -7.116  -0.421  19.161  1.00 27.17  ? 35  PHE   A O    1 
ATOM   523  C  CB   . PHE   A 1 38  ? -6.638  -2.468  17.119  1.00 22.05  ? 35  PHE   A CB   1 
ATOM   524  C  CG   . PHE   A 1 38  ? -6.482  -3.917  16.764  1.00 21.96  ? 35  PHE   A CG   1 
ATOM   525  C  CD1  . PHE   A 1 38  ? -6.377  -4.893  17.746  1.00 23.72  ? 35  PHE   A CD1  1 
ATOM   526  C  CD2  . PHE   A 1 38  ? -6.459  -4.311  15.452  1.00 23.86  ? 35  PHE   A CD2  1 
ATOM   527  C  CE1  . PHE   A 1 38  ? -6.224  -6.212  17.418  1.00 25.51  ? 35  PHE   A CE1  1 
ATOM   528  C  CE2  . PHE   A 1 38  ? -6.301  -5.635  15.113  1.00 25.90  ? 35  PHE   A CE2  1 
ATOM   529  C  CZ   . PHE   A 1 38  ? -6.205  -6.589  16.086  1.00 24.05  ? 35  PHE   A CZ   1 
ATOM   530  H  H    . PHE   A 1 38  ? -8.770  -2.051  15.917  1.00 28.89  ? 35  PHE   A H    1 
ATOM   531  H  HA   . PHE   A 1 38  ? -8.185  -2.692  18.470  1.00 29.92  ? 35  PHE   A HA   1 
ATOM   532  H  HB2  . PHE   A 1 38  ? -6.511  -1.952  16.307  1.00 26.50  ? 35  PHE   A HB2  1 
ATOM   533  H  HB3  . PHE   A 1 38  ? -5.946  -2.248  17.763  1.00 26.50  ? 35  PHE   A HB3  1 
ATOM   534  H  HD1  . PHE   A 1 38  ? -6.411  -4.646  18.642  1.00 28.51  ? 35  PHE   A HD1  1 
ATOM   535  H  HD2  . PHE   A 1 38  ? -6.551  -3.674  14.781  1.00 28.67  ? 35  PHE   A HD2  1 
ATOM   536  H  HE1  . PHE   A 1 38  ? -6.133  -6.852  18.087  1.00 30.66  ? 35  PHE   A HE1  1 
ATOM   537  H  HE2  . PHE   A 1 38  ? -6.260  -5.882  14.218  1.00 31.12  ? 35  PHE   A HE2  1 
ATOM   538  H  HZ   . PHE   A 1 38  ? -6.127  -7.486  15.855  1.00 28.90  ? 35  PHE   A HZ   1 
ATOM   539  N  N    . LEU   A 1 39  ? -8.803  0.245   17.828  1.00 26.93  ? 36  LEU   A N    1 
ATOM   540  C  CA   . LEU   A 1 39  ? -8.599  1.636   18.227  1.00 26.82  ? 36  LEU   A CA   1 
ATOM   541  C  C    . LEU   A 1 39  ? -8.895  1.883   19.710  1.00 31.83  ? 36  LEU   A C    1 
ATOM   542  O  O    . LEU   A 1 39  ? -8.149  2.629   20.361  1.00 32.80  ? 36  LEU   A O    1 
ATOM   543  C  CB   . LEU   A 1 39  ? -9.436  2.583   17.336  1.00 30.03  ? 36  LEU   A CB   1 
ATOM   544  C  CG   . LEU   A 1 39  ? -8.899  2.580   15.904  1.00 32.99  ? 36  LEU   A CG   1 
ATOM   545  C  CD1  . LEU   A 1 39  ? -9.690  3.498   14.982  1.00 31.76  ? 36  LEU   A CD1  1 
ATOM   546  C  CD2  . LEU   A 1 39  ? -7.439  3.000   15.832  1.00 34.25  ? 36  LEU   A CD2  1 
ATOM   547  H  H    . LEU   A 1 39  ? -9.477  0.097   17.314  1.00 32.36  ? 36  LEU   A H    1 
ATOM   548  H  HA   . LEU   A 1 39  ? -7.658  1.837   18.109  1.00 32.22  ? 36  LEU   A HA   1 
ATOM   549  H  HB2  . LEU   A 1 39  ? -10.359 2.285   17.322  1.00 36.08  ? 36  LEU   A HB2  1 
ATOM   550  H  HB3  . LEU   A 1 39  ? -9.385  3.487   17.685  1.00 36.08  ? 36  LEU   A HB3  1 
ATOM   551  H  HG   . LEU   A 1 39  ? -8.988  1.664   15.599  1.00 39.63  ? 36  LEU   A HG   1 
ATOM   552  H  HD11 . LEU   A 1 39  ? -9.345  3.412   14.079  1.00 38.15  ? 36  LEU   A HD11 1 
ATOM   553  H  HD12 . LEU   A 1 39  ? -10.624 3.239   15.005  1.00 38.15  ? 36  LEU   A HD12 1 
ATOM   554  H  HD13 . LEU   A 1 39  ? -9.592  4.413   15.287  1.00 38.15  ? 36  LEU   A HD13 1 
ATOM   555  H  HD21 . LEU   A 1 39  ? -7.228  3.256   14.920  1.00 41.14  ? 36  LEU   A HD21 1 
ATOM   556  H  HD22 . LEU   A 1 39  ? -7.297  3.752   16.428  1.00 41.14  ? 36  LEU   A HD22 1 
ATOM   557  H  HD23 . LEU   A 1 39  ? -6.882  2.254   16.103  1.00 41.14  ? 36  LEU   A HD23 1 
ATOM   558  N  N    . PRO   A 1 40  ? -9.946  1.299   20.297  1.00 33.26  ? 37  PRO   A N    1 
ATOM   559  C  CA   . PRO   A 1 40  ? -10.120 1.473   21.755  1.00 35.87  ? 37  PRO   A CA   1 
ATOM   560  C  C    . PRO   A 1 40  ? -8.934  0.934   22.542  1.00 28.69  ? 37  PRO   A C    1 
ATOM   561  O  O    . PRO   A 1 40  ? -8.529  1.535   23.544  1.00 32.84  ? 37  PRO   A O    1 
ATOM   562  C  CB   . PRO   A 1 40  ? -11.428 0.724   22.045  1.00 37.82  ? 37  PRO   A CB   1 
ATOM   563  C  CG   . PRO   A 1 40  ? -12.193 0.779   20.715  1.00 34.10  ? 37  PRO   A CG   1 
ATOM   564  C  CD   . PRO   A 1 40  ? -11.101 0.628   19.664  1.00 32.81  ? 37  PRO   A CD   1 
ATOM   565  H  HA   . PRO   A 1 40  ? -10.254 2.407   21.979  1.00 43.09  ? 37  PRO   A HA   1 
ATOM   566  H  HB2  . PRO   A 1 40  ? -11.238 -0.192  22.302  1.00 45.43  ? 37  PRO   A HB2  1 
ATOM   567  H  HB3  . PRO   A 1 40  ? -11.919 1.172   22.751  1.00 45.43  ? 37  PRO   A HB3  1 
ATOM   568  H  HG2  . PRO   A 1 40  ? -12.832 0.051   20.665  1.00 40.97  ? 37  PRO   A HG2  1 
ATOM   569  H  HG3  . PRO   A 1 40  ? -12.652 1.629   20.626  1.00 40.97  ? 37  PRO   A HG3  1 
ATOM   570  H  HD2  . PRO   A 1 40  ? -10.909 -0.308  19.493  1.00 39.42  ? 37  PRO   A HD2  1 
ATOM   571  H  HD3  . PRO   A 1 40  ? -11.350 1.071   18.838  1.00 39.42  ? 37  PRO   A HD3  1 
ATOM   572  N  N    . LEU   A 1 41  ? -8.341  -0.163  22.081  1.00 28.22  ? 38  LEU   A N    1 
ATOM   573  C  CA   . LEU   A 1 41  ? -7.147  -0.691  22.744  1.00 26.51  ? 38  LEU   A CA   1 
ATOM   574  C  C    . LEU   A 1 41  ? -5.968  0.258   22.557  1.00 27.94  ? 38  LEU   A C    1 
ATOM   575  O  O    . LEU   A 1 41  ? -5.210  0.519   23.503  1.00 28.53  ? 38  LEU   A O    1 
ATOM   576  C  CB   . LEU   A 1 41  ? -6.833  -2.082  22.193  1.00 26.07  ? 38  LEU   A CB   1 
ATOM   577  C  CG   . LEU   A 1 41  ? -5.530  -2.739  22.656  1.00 25.58  ? 38  LEU   A CG   1 
ATOM   578  C  CD1  . LEU   A 1 41  ? -5.540  -2.829  24.144  1.00 28.12  ? 38  LEU   A CD1  1 
ATOM   579  C  CD2  . LEU   A 1 41  ? -5.359  -4.116  22.062  1.00 27.22  ? 38  LEU   A CD2  1 
ATOM   580  H  H    . LEU   A 1 41  ? -8.603  -0.615  21.398  1.00 33.90  ? 38  LEU   A H    1 
ATOM   581  H  HA   . LEU   A 1 41  ? -7.308  -0.781  23.696  1.00 31.85  ? 38  LEU   A HA   1 
ATOM   582  H  HB2  . LEU   A 1 41  ? -7.556  -2.675  22.451  1.00 31.33  ? 38  LEU   A HB2  1 
ATOM   583  H  HB3  . LEU   A 1 41  ? -6.788  -2.016  21.226  1.00 31.33  ? 38  LEU   A HB3  1 
ATOM   584  H  HG   . LEU   A 1 41  ? -4.779  -2.202  22.358  1.00 30.74  ? 38  LEU   A HG   1 
ATOM   585  H  HD11 . LEU   A 1 41  ? -4.809  -3.399  24.431  1.00 33.79  ? 38  LEU   A HD11 1 
ATOM   586  H  HD12 . LEU   A 1 41  ? -5.430  -1.939  24.514  1.00 33.79  ? 38  LEU   A HD12 1 
ATOM   587  H  HD13 . LEU   A 1 41  ? -6.386  -3.205  24.432  1.00 33.79  ? 38  LEU   A HD13 1 
ATOM   588  H  HD21 . LEU   A 1 41  ? -4.520  -4.492  22.371  1.00 32.70  ? 38  LEU   A HD21 1 
ATOM   589  H  HD22 . LEU   A 1 41  ? -6.097  -4.677  22.347  1.00 32.70  ? 38  LEU   A HD22 1 
ATOM   590  H  HD23 . LEU   A 1 41  ? -5.353  -4.044  21.094  1.00 32.70  ? 38  LEU   A HD23 1 
ATOM   591  N  N    . ALA   A 1 42  ? -5.810  0.810   21.353  1.00 29.61  ? 39  ALA   A N    1 
ATOM   592  C  CA   . ALA   A 1 42  ? -4.687  1.713   21.114  1.00 30.51  ? 39  ALA   A CA   1 
ATOM   593  C  C    . ALA   A 1 42  ? -4.727  2.915   22.035  1.00 30.87  ? 39  ALA   A C    1 
ATOM   594  O  O    . ALA   A 1 42  ? -3.672  3.415   22.446  1.00 31.70  ? 39  ALA   A O    1 
ATOM   595  C  CB   . ALA   A 1 42  ? -4.677  2.166   19.656  1.00 29.95  ? 39  ALA   A CB   1 
ATOM   596  H  H    . ALA   A 1 42  ? -6.326  0.682   20.677  1.00 35.57  ? 39  ALA   A H    1 
ATOM   597  H  HA   . ALA   A 1 42  ? -3.863  1.231   21.285  1.00 36.65  ? 39  ALA   A HA   1 
ATOM   598  H  HB1  . ALA   A 1 42  ? -3.920  2.755   19.514  1.00 35.98  ? 39  ALA   A HB1  1 
ATOM   599  H  HB2  . ALA   A 1 42  ? -4.602  1.386   19.084  1.00 35.98  ? 39  ALA   A HB2  1 
ATOM   600  H  HB3  . ALA   A 1 42  ? -5.503  2.637   19.466  1.00 35.98  ? 39  ALA   A HB3  1 
ATOM   601  N  N    . GLU   A 1 43  ? -5.937  3.370   22.395  1.00 31.81  ? 40  GLU   A N    1 
ATOM   602  C  CA   . GLU   A 1 43  ? -6.102  4.483   23.330  1.00 39.93  ? 40  GLU   A CA   1 
ATOM   603  C  C    . GLU   A 1 43  ? -5.490  4.181   24.694  1.00 35.51  ? 40  GLU   A C    1 
ATOM   604  O  O    . GLU   A 1 43  ? -4.918  5.066   25.343  1.00 37.01  ? 40  GLU   A O    1 
ATOM   605  C  CB   . GLU   A 1 43  ? -7.591  4.771   23.498  1.00 42.05  ? 40  GLU   A CB   1 
ATOM   606  C  CG   . GLU   A 1 43  ? -8.195  5.732   22.491  1.00 51.97  ? 40  GLU   A CG   1 
ATOM   607  C  CD   . GLU   A 1 43  ? -7.350  6.970   22.223  1.00 57.09  ? 40  GLU   A CD   1 
ATOM   608  O  OE1  . GLU   A 1 43  ? -7.281  7.846   23.111  1.00 51.33  ? 40  GLU   A OE1  1 
ATOM   609  O  OE2  . GLU   A 1 43  ? -6.771  7.066   21.110  1.00 47.68  ? 40  GLU   A OE2  1 
ATOM   610  H  H    . GLU   A 1 43  ? -6.681  3.047   22.109  1.00 38.22  ? 40  GLU   A H    1 
ATOM   611  H  HA   . GLU   A 1 43  ? -5.653  5.261   22.966  1.00 47.96  ? 40  GLU   A HA   1 
ATOM   612  H  HB2  . GLU   A 1 43  ? -8.073  3.933   23.422  1.00 50.50  ? 40  GLU   A HB2  1 
ATOM   613  H  HB3  . GLU   A 1 43  ? -7.728  5.154   24.379  1.00 50.50  ? 40  GLU   A HB3  1 
ATOM   614  H  HG2  . GLU   A 1 43  ? -8.310  5.267   21.648  1.00 62.41  ? 40  GLU   A HG2  1 
ATOM   615  H  HG3  . GLU   A 1 43  ? -9.055  6.031   22.825  1.00 62.41  ? 40  GLU   A HG3  1 
ATOM   616  N  N    . GLN   A 1 44  ? -5.627  2.934   25.156  1.00 31.80  ? 41  GLN   A N    1 
ATOM   617  C  CA   . GLN   A 1 44  ? -5.057  2.519   26.434  1.00 40.21  ? 41  GLN   A CA   1 
ATOM   618  C  C    . GLN   A 1 44  ? -3.543  2.401   26.365  1.00 36.51  ? 41  GLN   A C    1 
ATOM   619  O  O    . GLN   A 1 44  ? -2.884  2.427   27.405  1.00 39.36  ? 41  GLN   A O    1 
ATOM   620  C  CB   . GLN   A 1 44  ? -5.664  1.168   26.845  1.00 35.15  ? 41  GLN   A CB   1 
ATOM   621  C  CG   . GLN   A 1 44  ? -7.182  1.177   26.954  1.00 38.83  ? 41  GLN   A CG   1 
ATOM   622  C  CD   . GLN   A 1 44  ? -7.670  1.981   28.139  1.00 45.47  ? 41  GLN   A CD   1 
ATOM   623  O  OE1  . GLN   A 1 44  ? -7.080  1.944   29.219  1.00 52.65  ? 41  GLN   A OE1  1 
ATOM   624  N  NE2  . GLN   A 1 44  ? -8.736  2.737   27.935  1.00 47.03  ? 41  GLN   A NE2  1 
ATOM   625  H  H    . GLN   A 1 44  ? -6.049  2.308   24.745  1.00 38.21  ? 41  GLN   A H    1 
ATOM   626  H  HA   . GLN   A 1 44  ? -5.276  3.175   27.114  1.00 48.29  ? 41  GLN   A HA   1 
ATOM   627  H  HB2  . GLN   A 1 44  ? -5.420  0.503   26.183  1.00 42.22  ? 41  GLN   A HB2  1 
ATOM   628  H  HB3  . GLN   A 1 44  ? -5.308  0.920   27.713  1.00 42.22  ? 41  GLN   A HB3  1 
ATOM   629  H  HG2  . GLN   A 1 44  ? -7.556  1.569   26.149  1.00 46.64  ? 41  GLN   A HG2  1 
ATOM   630  H  HG3  . GLN   A 1 44  ? -7.499  0.266   27.057  1.00 46.64  ? 41  GLN   A HG3  1 
ATOM   631  H  HE21 . GLN   A 1 44  ? -9.111  2.751   27.161  1.00 56.48  ? 41  GLN   A HE21 1 
ATOM   632  H  HE22 . GLN   A 1 44  ? -9.054  3.214   28.576  1.00 56.48  ? 41  GLN   A HE22 1 
ATOM   633  N  N    . LEU   A 1 45  ? -2.976  2.280   25.171  1.00 34.26  ? 42  LEU   A N    1 
ATOM   634  C  CA   . LEU   A 1 45  ? -1.561  2.016   25.021  1.00 31.82  ? 42  LEU   A CA   1 
ATOM   635  C  C    . LEU   A 1 45  ? -0.780  3.196   24.471  1.00 39.35  ? 42  LEU   A C    1 
ATOM   636  O  O    . LEU   A 1 45  ? 0.456   3.131   24.451  1.00 32.14  ? 42  LEU   A O    1 
ATOM   637  C  CB   . LEU   A 1 45  ? -1.356  0.822   24.085  1.00 29.31  ? 42  LEU   A CB   1 
ATOM   638  C  CG   . LEU   A 1 45  ? -1.954  -0.497  24.573  1.00 29.99  ? 42  LEU   A CG   1 
ATOM   639  C  CD1  . LEU   A 1 45  ? -1.843  -1.542  23.460  1.00 28.93  ? 42  LEU   A CD1  1 
ATOM   640  C  CD2  . LEU   A 1 45  ? -1.257  -0.940  25.822  1.00 32.95  ? 42  LEU   A CD2  1 
ATOM   641  H  H    . LEU   A 1 45  ? -3.400  2.349   24.425  1.00 41.15  ? 42  LEU   A H    1 
ATOM   642  H  HA   . LEU   A 1 45  ? -1.194  1.796   25.891  1.00 38.22  ? 42  LEU   A HA   1 
ATOM   643  H  HB2  . LEU   A 1 45  ? -1.767  1.029   23.231  1.00 35.21  ? 42  LEU   A HB2  1 
ATOM   644  H  HB3  . LEU   A 1 45  ? -0.403  0.684   23.969  1.00 35.21  ? 42  LEU   A HB3  1 
ATOM   645  H  HG   . LEU   A 1 45  ? -2.894  -0.390  24.790  1.00 36.03  ? 42  LEU   A HG   1 
ATOM   646  H  HD11 . LEU   A 1 45  ? -2.133  -2.402  23.804  1.00 34.76  ? 42  LEU   A HD11 1 
ATOM   647  H  HD12 . LEU   A 1 45  ? -2.407  -1.275  22.718  1.00 34.76  ? 42  LEU   A HD12 1 
ATOM   648  H  HD13 . LEU   A 1 45  ? -0.919  -1.597  23.170  1.00 34.76  ? 42  LEU   A HD13 1 
ATOM   649  H  HD21 . LEU   A 1 45  ? -1.596  -1.812  26.081  1.00 39.58  ? 42  LEU   A HD21 1 
ATOM   650  H  HD22 . LEU   A 1 45  ? -0.304  -0.993  25.650  1.00 39.58  ? 42  LEU   A HD22 1 
ATOM   651  H  HD23 . LEU   A 1 45  ? -1.431  -0.296  26.526  1.00 39.58  ? 42  LEU   A HD23 1 
ATOM   652  N  N    . LYS   A 1 46  ? -1.464  4.261   24.023  1.00 33.97  ? 43  LYS   A N    1 
ATOM   653  C  CA   . LYS   A 1 46  ? -0.829  5.306   23.229  1.00 37.44  ? 43  LYS   A CA   1 
ATOM   654  C  C    . LYS   A 1 46  ? 0.186   6.107   24.026  1.00 40.83  ? 43  LYS   A C    1 
ATOM   655  O  O    . LYS   A 1 46  ? 0.992   6.820   23.425  1.00 41.25  ? 43  LYS   A O    1 
ATOM   656  C  CB   . LYS   A 1 46  ? -1.886  6.242   22.631  1.00 38.14  ? 43  LYS   A CB   1 
ATOM   657  C  CG   . LYS   A 1 46  ? -2.704  7.034   23.635  1.00 39.77  ? 43  LYS   A CG   1 
ATOM   658  C  CD   . LYS   A 1 46  ? -3.653  8.027   22.948  1.00 48.30  ? 43  LYS   A CD   1 
ATOM   659  C  CE   . LYS   A 1 46  ? -4.425  8.869   23.972  1.00 46.86  ? 43  LYS   A CE   1 
ATOM   660  N  NZ   . LYS   A 1 46  ? -5.636  9.560   23.437  1.00 57.66  ? 43  LYS   A NZ   1 
ATOM   661  H  H    . LYS   A 1 46  ? -2.300  4.396   24.170  1.00 40.81  ? 43  LYS   A H    1 
ATOM   662  H  HA   . LYS   A 1 46  ? -0.363  4.889   22.488  1.00 44.97  ? 43  LYS   A HA   1 
ATOM   663  H  HB2  . LYS   A 1 46  ? -1.436  6.882   22.057  1.00 45.81  ? 43  LYS   A HB2  1 
ATOM   664  H  HB3  . LYS   A 1 46  ? -2.506  5.709   22.110  1.00 45.81  ? 43  LYS   A HB3  1 
ATOM   665  H  HG2  . LYS   A 1 46  ? -3.239  6.422   24.165  1.00 47.77  ? 43  LYS   A HG2  1 
ATOM   666  H  HG3  . LYS   A 1 46  ? -2.106  7.535   24.211  1.00 47.77  ? 43  LYS   A HG3  1 
ATOM   667  H  HD2  . LYS   A 1 46  ? -3.138  8.627   22.386  1.00 58.00  ? 43  LYS   A HD2  1 
ATOM   668  H  HD3  . LYS   A 1 46  ? -4.295  7.538   22.409  1.00 58.00  ? 43  LYS   A HD3  1 
ATOM   669  H  HE2  . LYS   A 1 46  ? -4.717  8.287   24.691  1.00 56.27  ? 43  LYS   A HE2  1 
ATOM   670  H  HE3  . LYS   A 1 46  ? -3.831  9.552   24.319  1.00 56.27  ? 43  LYS   A HE3  1 
ATOM   671  H  HZ1  . LYS   A 1 46  ? -6.020  10.041  24.080  1.00 69.24  ? 43  LYS   A HZ1  1 
ATOM   672  H  HZ2  . LYS   A 1 46  ? -5.407  10.101  22.769  1.00 69.24  ? 43  LYS   A HZ2  1 
ATOM   673  H  HZ3  . LYS   A 1 46  ? -6.220  8.960   23.136  1.00 69.24  ? 43  LYS   A HZ3  1 
ATOM   674  N  N    . ASP   A 1 47  ? 0.182   5.994   25.351  1.00 39.67  ? 44  ASP   A N    1 
ATOM   675  C  CA   . ASP   A 1 47  ? 1.184   6.653   26.163  1.00 46.76  ? 44  ASP   A CA   1 
ATOM   676  C  C    . ASP   A 1 47  ? 2.510   5.902   26.142  1.00 44.65  ? 44  ASP   A C    1 
ATOM   677  O  O    . ASP   A 1 47  ? 3.547   6.482   26.472  1.00 45.03  ? 44  ASP   A O    1 
ATOM   678  C  CB   . ASP   A 1 47  ? 0.645   6.771   27.591  1.00 47.58  ? 44  ASP   A CB   1 
ATOM   679  C  CG   . ASP   A 1 47  ? 0.014   8.112   27.857  1.00 63.89  ? 44  ASP   A CG   1 
ATOM   680  O  OD1  . ASP   A 1 47  ? 0.306   9.070   27.113  1.00 68.89  ? 44  ASP   A OD1  1 
ATOM   681  O  OD2  . ASP   A 1 47  ? -0.805  8.203   28.796  1.00 86.58  ? 44  ASP   A OD2  1 
ATOM   682  H  H    . ASP   A 1 47  ? -0.393  5.539   25.800  1.00 47.65  ? 44  ASP   A H    1 
ATOM   683  H  HA   . ASP   A 1 47  ? 1.360   7.548   25.834  1.00 56.16  ? 44  ASP   A HA   1 
ATOM   684  H  HB2  . ASP   A 1 47  ? -0.029  6.087   27.734  1.00 57.14  ? 44  ASP   A HB2  1 
ATOM   685  H  HB3  . ASP   A 1 47  ? 1.376   6.652   28.218  1.00 57.14  ? 44  ASP   A HB3  1 
ATOM   686  N  N    . HIS   A 1 48  ? 2.505   4.637   25.743  1.00 36.03  ? 45  HIS   A N    1 
ATOM   687  C  CA   . HIS   A 1 48  ? 3.689   3.792   25.809  1.00 38.48  ? 45  HIS   A CA   1 
ATOM   688  C  C    . HIS   A 1 48  ? 4.206   3.351   24.452  1.00 37.41  ? 45  HIS   A C    1 
ATOM   689  O  O    . HIS   A 1 48  ? 5.397   3.091   24.317  1.00 39.90  ? 45  HIS   A O    1 
ATOM   690  C  CB   . HIS   A 1 48  ? 3.402   2.536   26.647  1.00 35.51  ? 45  HIS   A CB   1 
ATOM   691  C  CG   . HIS   A 1 48  ? 3.067   2.827   28.078  1.00 43.28  ? 45  HIS   A CG   1 
ATOM   692  N  ND1  . HIS   A 1 48  ? 1.788   3.122   28.500  1.00 45.89  ? 45  HIS   A ND1  1 
ATOM   693  C  CD2  . HIS   A 1 48  ? 3.845   2.862   29.185  1.00 56.05  ? 45  HIS   A CD2  1 
ATOM   694  C  CE1  . HIS   A 1 48  ? 1.793   3.325   29.805  1.00 49.96  ? 45  HIS   A CE1  1 
ATOM   695  N  NE2  . HIS   A 1 48  ? 3.030   3.184   30.243  1.00 54.98  ? 45  HIS   A NE2  1 
ATOM   696  H  H    . HIS   A 1 48  ? 1.814   4.238   25.423  1.00 43.28  ? 45  HIS   A H    1 
ATOM   697  H  HA   . HIS   A 1 48  ? 4.394   4.293   26.248  1.00 46.22  ? 45  HIS   A HA   1 
ATOM   698  H  HB2  . HIS   A 1 48  ? 2.648   2.066   26.256  1.00 42.66  ? 45  HIS   A HB2  1 
ATOM   699  H  HB3  . HIS   A 1 48  ? 4.188   1.968   26.637  1.00 42.66  ? 45  HIS   A HB3  1 
ATOM   700  H  HD2  . HIS   A 1 48  ? 4.760   2.699   29.222  1.00 67.30  ? 45  HIS   A HD2  1 
ATOM   701  H  HE1  . HIS   A 1 48  ? 1.051   3.531   30.326  1.00 59.99  ? 45  HIS   A HE1  1 
ATOM   702  H  HE2  . HIS   A 1 48  ? 3.285   3.278   31.059  1.00 66.02  ? 45  HIS   A HE2  1 
ATOM   703  N  N    . PHE   A 1 49  ? 3.337   3.264   23.452  1.00 33.67  ? 46  PHE   A N    1 
ATOM   704  C  CA   . PHE   A 1 49  ? 3.696   2.777   22.129  1.00 32.69  ? 46  PHE   A CA   1 
ATOM   705  C  C    . PHE   A 1 49  ? 3.177   3.728   21.055  1.00 30.52  ? 46  PHE   A C    1 
ATOM   706  O  O    . PHE   A 1 49  ? 2.155   4.396   21.231  1.00 32.70  ? 46  PHE   A O    1 
ATOM   707  C  CB   . PHE   A 1 49  ? 3.106   1.382   21.826  1.00 30.18  ? 46  PHE   A CB   1 
ATOM   708  C  CG   . PHE   A 1 49  ? 3.571   0.294   22.738  1.00 31.20  ? 46  PHE   A CG   1 
ATOM   709  C  CD1  . PHE   A 1 49  ? 4.718   -0.438  22.445  1.00 30.67  ? 46  PHE   A CD1  1 
ATOM   710  C  CD2  . PHE   A 1 49  ? 2.854   -0.011  23.894  1.00 32.41  ? 46  PHE   A CD2  1 
ATOM   711  C  CE1  . PHE   A 1 49  ? 5.142   -1.463  23.278  1.00 31.77  ? 46  PHE   A CE1  1 
ATOM   712  C  CE2  . PHE   A 1 49  ? 3.260   -1.051  24.733  1.00 35.80  ? 46  PHE   A CE2  1 
ATOM   713  C  CZ   . PHE   A 1 49  ? 4.422   -1.761  24.439  1.00 38.25  ? 46  PHE   A CZ   1 
ATOM   714  H  H    . PHE   A 1 49  ? 2.509   3.487   23.518  1.00 40.44  ? 46  PHE   A H    1 
ATOM   715  H  HA   . PHE   A 1 49  ? 4.665   2.732   22.092  1.00 39.27  ? 46  PHE   A HA   1 
ATOM   716  H  HB2  . PHE   A 1 49  ? 2.140   1.434   21.901  1.00 36.26  ? 46  PHE   A HB2  1 
ATOM   717  H  HB3  . PHE   A 1 49  ? 3.355   1.132   20.922  1.00 36.26  ? 46  PHE   A HB3  1 
ATOM   718  H  HD1  . PHE   A 1 49  ? 5.208   -0.236  21.680  1.00 36.85  ? 46  PHE   A HD1  1 
ATOM   719  H  HD2  . PHE   A 1 49  ? 2.096   0.483   24.109  1.00 38.93  ? 46  PHE   A HD2  1 
ATOM   720  H  HE1  . PHE   A 1 49  ? 5.903   -1.952  23.064  1.00 38.17  ? 46  PHE   A HE1  1 
ATOM   721  H  HE2  . PHE   A 1 49  ? 2.758   -1.268  25.485  1.00 43.00  ? 46  PHE   A HE2  1 
ATOM   722  H  HZ   . PHE   A 1 49  ? 4.718   -2.430  25.013  1.00 45.94  ? 46  PHE   A HZ   1 
ATOM   723  N  N    . THR   A 1 50  ? 3.870   3.750   19.919  1.00 31.92  ? 47  THR   A N    1 
ATOM   724  C  CA   . THR   A 1 50  ? 3.267   4.206   18.673  1.00 33.42  ? 47  THR   A CA   1 
ATOM   725  C  C    . THR   A 1 50  ? 2.459   3.028   18.129  1.00 28.93  ? 47  THR   A C    1 
ATOM   726  O  O    . THR   A 1 50  ? 3.023   2.071   17.610  1.00 28.33  ? 47  THR   A O    1 
ATOM   727  C  CB   . THR   A 1 50  ? 4.343   4.633   17.692  1.00 34.31  ? 47  THR   A CB   1 
ATOM   728  O  OG1  . THR   A 1 50  ? 5.030   5.774   18.211  1.00 36.89  ? 47  THR   A OG1  1 
ATOM   729  C  CG2  . THR   A 1 50  ? 3.720   5.045   16.361  1.00 35.27  ? 47  THR   A CG2  1 
ATOM   730  H  H    . THR   A 1 50  ? 4.691   3.506   19.845  1.00 38.35  ? 47  THR   A H    1 
ATOM   731  H  HA   . THR   A 1 50  ? 2.683   4.966   18.827  1.00 40.14  ? 47  THR   A HA   1 
ATOM   732  H  HB   . THR   A 1 50  ? 4.953   3.892   17.553  1.00 41.21  ? 47  THR   A HB   1 
ATOM   733  H  HG1  . THR   A 1 50  ? 5.592   5.534   18.788  1.00 44.30  ? 47  THR   A HG1  1 
ATOM   734  H  HG21 . THR   A 1 50  ? 4.344   5.593   15.859  1.00 42.36  ? 47  THR   A HG21 1 
ATOM   735  H  HG22 . THR   A 1 50  ? 3.502   4.258   15.839  1.00 42.36  ? 47  THR   A HG22 1 
ATOM   736  H  HG23 . THR   A 1 50  ? 2.910   5.554   16.518  1.00 42.36  ? 47  THR   A HG23 1 
ATOM   737  N  N    . VAL   A 1 51  ? 1.141   3.064   18.296  1.00 28.08  ? 48  VAL   A N    1 
ATOM   738  C  CA   . VAL   A 1 51  ? 0.276   1.952   17.921  1.00 26.17  ? 48  VAL   A CA   1 
ATOM   739  C  C    . VAL   A 1 51  ? -0.135  2.134   16.473  1.00 24.02  ? 48  VAL   A C    1 
ATOM   740  O  O    . VAL   A 1 51  ? -0.572  3.223   16.063  1.00 27.54  ? 48  VAL   A O    1 
ATOM   741  C  CB   . VAL   A 1 51  ? -0.954  1.867   18.839  1.00 28.84  ? 48  VAL   A CB   1 
ATOM   742  C  CG1  . VAL   A 1 51  ? -1.769  0.631   18.480  1.00 28.14  ? 48  VAL   A CG1  1 
ATOM   743  C  CG2  . VAL   A 1 51  ? -0.532  1.822   20.300  1.00 30.37  ? 48  VAL   A CG2  1 
ATOM   744  H  H    . VAL   A 1 51  ? 0.718   3.733   18.630  1.00 33.74  ? 48  VAL   A H    1 
ATOM   745  H  HA   . VAL   A 1 51  ? 0.768   1.121   18.004  1.00 31.44  ? 48  VAL   A HA   1 
ATOM   746  H  HB   . VAL   A 1 51  ? -1.504  2.656   18.715  1.00 34.65  ? 48  VAL   A HB   1 
ATOM   747  H  HG11 . VAL   A 1 51  ? -2.311  0.378   19.243  1.00 33.81  ? 48  VAL   A HG11 1 
ATOM   748  H  HG12 . VAL   A 1 51  ? -2.340  0.839   17.723  1.00 33.81  ? 48  VAL   A HG12 1 
ATOM   749  H  HG13 . VAL   A 1 51  ? -1.164  -0.091  18.249  1.00 33.81  ? 48  VAL   A HG13 1 
ATOM   750  H  HG21 . VAL   A 1 51  ? -1.291  1.549   20.839  1.00 36.49  ? 48  VAL   A HG21 1 
ATOM   751  H  HG22 . VAL   A 1 51  ? 0.191   1.183   20.400  1.00 36.49  ? 48  VAL   A HG22 1 
ATOM   752  H  HG23 . VAL   A 1 51  ? -0.234  2.704   20.570  1.00 36.49  ? 48  VAL   A HG23 1 
ATOM   753  N  N    . VAL   A 1 52  ? 0.049   1.075   15.702  1.00 23.85  ? 49  VAL   A N    1 
ATOM   754  C  CA   . VAL   A 1 52  ? -0.207  1.022   14.271  1.00 23.88  ? 49  VAL   A CA   1 
ATOM   755  C  C    . VAL   A 1 52  ? -1.202  -0.104  14.062  1.00 24.87  ? 49  VAL   A C    1 
ATOM   756  O  O    . VAL   A 1 52  ? -0.892  -1.256  14.373  1.00 25.21  ? 49  VAL   A O    1 
ATOM   757  C  CB   . VAL   A 1 52  ? 1.096   0.777   13.500  1.00 24.45  ? 49  VAL   A CB   1 
ATOM   758  C  CG1  . VAL   A 1 52  ? 0.814   0.527   12.031  1.00 27.63  ? 49  VAL   A CG1  1 
ATOM   759  C  CG2  . VAL   A 1 52  ? 2.035   1.923   13.736  1.00 27.52  ? 49  VAL   A CG2  1 
ATOM   760  H  H    . VAL   A 1 52  ? 0.341   0.325   16.005  1.00 28.67  ? 49  VAL   A H    1 
ATOM   761  H  HA   . VAL   A 1 52  ? -0.599  1.848   13.947  1.00 28.70  ? 49  VAL   A HA   1 
ATOM   762  H  HB   . VAL   A 1 52  ? 1.535   -0.026  13.822  1.00 29.38  ? 49  VAL   A HB   1 
ATOM   763  H  HG11 . VAL   A 1 52  ? 1.651   0.542   11.542  1.00 33.20  ? 49  VAL   A HG11 1 
ATOM   764  H  HG12 . VAL   A 1 52  ? 0.390   -0.340  11.934  1.00 33.20  ? 49  VAL   A HG12 1 
ATOM   765  H  HG13 . VAL   A 1 52  ? 0.225   1.222   11.700  1.00 33.20  ? 49  VAL   A HG13 1 
ATOM   766  H  HG21 . VAL   A 1 52  ? 2.853   1.770   13.237  1.00 33.07  ? 49  VAL   A HG21 1 
ATOM   767  H  HG22 . VAL   A 1 52  ? 1.614   2.744   13.437  1.00 33.07  ? 49  VAL   A HG22 1 
ATOM   768  H  HG23 . VAL   A 1 52  ? 2.233   1.980   14.684  1.00 33.07  ? 49  VAL   A HG23 1 
ATOM   769  N  N    . ALA   A 1 53  ? -2.396  0.229   13.561  1.00 24.56  ? 50  ALA   A N    1 
ATOM   770  C  CA   . ALA   A 1 53  ? -3.458  -0.740  13.338  1.00 22.72  ? 50  ALA   A CA   1 
ATOM   771  C  C    . ALA   A 1 53  ? -3.761  -0.771  11.850  1.00 22.25  ? 50  ALA   A C    1 
ATOM   772  O  O    . ALA   A 1 53  ? -4.215  0.231   11.293  1.00 24.59  ? 50  ALA   A O    1 
ATOM   773  C  CB   . ALA   A 1 53  ? -4.699  -0.392  14.148  1.00 27.64  ? 50  ALA   A CB   1 
ATOM   774  H  H    . ALA   A 1 53  ? -2.613  1.031   13.338  1.00 29.51  ? 50  ALA   A H    1 
ATOM   775  H  HA   . ALA   A 1 53  ? -3.167  -1.624  13.611  1.00 27.30  ? 50  ALA   A HA   1 
ATOM   776  H  HB1  . ALA   A 1 53  ? -5.430  -0.965  13.868  1.00 33.21  ? 50  ALA   A HB1  1 
ATOM   777  H  HB2  . ALA   A 1 53  ? -4.512  -0.532  15.089  1.00 33.21  ? 50  ALA   A HB2  1 
ATOM   778  H  HB3  . ALA   A 1 53  ? -4.929  0.537   13.991  1.00 33.21  ? 50  ALA   A HB3  1 
ATOM   779  N  N    A VAL   A 1 54  ? -3.506  -1.909  11.214  0.46 22.00  ? 51  VAL   A N    1 
ATOM   780  N  N    B VAL   A 1 54  ? -3.517  -1.919  11.222  0.54 22.00  ? 51  VAL   A N    1 
ATOM   781  C  CA   A VAL   A 1 54  ? -3.472  -2.006  9.757   0.46 23.20  ? 51  VAL   A CA   1 
ATOM   782  C  CA   B VAL   A 1 54  ? -3.482  -2.047  9.767   0.54 23.20  ? 51  VAL   A CA   1 
ATOM   783  C  C    A VAL   A 1 54  ? -4.793  -2.539  9.218   0.46 22.87  ? 51  VAL   A C    1 
ATOM   784  C  C    B VAL   A 1 54  ? -4.818  -2.536  9.227   0.54 22.86  ? 51  VAL   A C    1 
ATOM   785  O  O    A VAL   A 1 54  ? -5.417  -3.427  9.815   0.46 23.53  ? 51  VAL   A O    1 
ATOM   786  O  O    B VAL   A 1 54  ? -5.472  -3.403  9.823   0.54 23.53  ? 51  VAL   A O    1 
ATOM   787  C  CB   A VAL   A 1 54  ? -2.302  -2.904  9.309   0.46 23.38  ? 51  VAL   A CB   1 
ATOM   788  C  CB   B VAL   A 1 54  ? -2.349  -3.006  9.353   0.54 23.40  ? 51  VAL   A CB   1 
ATOM   789  C  CG1  A VAL   A 1 54  ? -2.609  -4.362  9.625   0.46 19.66  ? 51  VAL   A CG1  1 
ATOM   790  C  CG1  B VAL   A 1 54  ? -2.310  -3.185  7.844   0.54 26.95  ? 51  VAL   A CG1  1 
ATOM   791  C  CG2  A VAL   A 1 54  ? -2.034  -2.734  7.821   0.46 29.48  ? 51  VAL   A CG2  1 
ATOM   792  C  CG2  B VAL   A 1 54  ? -1.022  -2.513  9.871   0.54 21.52  ? 51  VAL   A CG2  1 
ATOM   793  H  H    A VAL   A 1 54  ? -3.345  -2.654  11.613  0.46 26.45  ? 51  VAL   A H    1 
ATOM   794  H  H    B VAL   A 1 54  ? -3.363  -2.661  11.630  0.54 26.44  ? 51  VAL   A H    1 
ATOM   795  H  HA   A VAL   A 1 54  ? -3.359  -1.113  9.396   0.46 27.89  ? 51  VAL   A HA   1 
ATOM   796  H  HA   B VAL   A 1 54  ? -3.334  -1.167  9.388   0.54 27.88  ? 51  VAL   A HA   1 
ATOM   797  H  HB   A VAL   A 1 54  ? -1.503  -2.642  9.792   0.46 28.10  ? 51  VAL   A HB   1 
ATOM   798  H  HB   B VAL   A 1 54  ? -2.522  -3.876  9.746   0.54 28.12  ? 51  VAL   A HB   1 
ATOM   799  H  HG11 A VAL   A 1 54  ? -1.774  -4.843  9.734   0.46 23.63  ? 51  VAL   A HG11 1 
ATOM   800  H  HG11 B VAL   A 1 54  ? -1.402  -3.395  7.574   0.54 32.38  ? 51  VAL   A HG11 1 
ATOM   801  H  HG12 A VAL   A 1 54  ? -3.125  -4.405  10.445  0.46 23.63  ? 51  VAL   A HG12 1 
ATOM   802  H  HG12 B VAL   A 1 54  ? -2.905  -3.909  7.596   0.54 32.38  ? 51  VAL   A HG12 1 
ATOM   803  H  HG13 A VAL   A 1 54  ? -3.117  -4.743  8.892   0.46 23.63  ? 51  VAL   A HG13 1 
ATOM   804  H  HG13 B VAL   A 1 54  ? -2.598  -2.361  7.421   0.54 32.38  ? 51  VAL   A HG13 1 
ATOM   805  H  HG21 A VAL   A 1 54  ? -1.117  -2.988  7.634   0.46 35.42  ? 51  VAL   A HG21 1 
ATOM   806  H  HG21 B VAL   A 1 54  ? -0.310  -3.001  9.429   0.54 25.87  ? 51  VAL   A HG21 1 
ATOM   807  H  HG22 A VAL   A 1 54  ? -2.642  -3.302  7.323   0.46 35.42  ? 51  VAL   A HG22 1 
ATOM   808  H  HG22 B VAL   A 1 54  ? -0.942  -1.565  9.682   0.54 25.87  ? 51  VAL   A HG22 1 
ATOM   809  H  HG23 A VAL   A 1 54  ? -2.176  -1.805  7.579   0.46 35.42  ? 51  VAL   A HG23 1 
ATOM   810  H  HG23 B VAL   A 1 54  ? -0.982  -2.664  10.828  0.54 25.87  ? 51  VAL   A HG23 1 
ATOM   811  N  N    . ASP   A 1 55  ? -5.213  -1.995  8.078   1.00 22.71  ? 52  ASP   A N    1 
ATOM   812  C  CA   . ASP   A 1 55  ? -6.216  -2.614  7.206   1.00 23.61  ? 52  ASP   A CA   1 
ATOM   813  C  C    . ASP   A 1 55  ? -5.434  -3.525  6.258   1.00 20.33  ? 52  ASP   A C    1 
ATOM   814  O  O    . ASP   A 1 55  ? -4.676  -3.029  5.430   1.00 22.02  ? 52  ASP   A O    1 
ATOM   815  C  CB   . ASP   A 1 55  ? -6.974  -1.564  6.398   1.00 23.63  ? 52  ASP   A CB   1 
ATOM   816  C  CG   . ASP   A 1 55  ? -8.075  -0.844  7.186   1.00 26.04  ? 52  ASP   A CG   1 
ATOM   817  O  OD1  . ASP   A 1 55  ? -8.167  -1.027  8.419   1.00 27.07  ? 52  ASP   A OD1  1 
ATOM   818  O  OD2  . ASP   A 1 55  ? -8.872  -0.111  6.550   1.00 27.49  ? 52  ASP   A OD2  1 
ATOM   819  H  H    A ASP   A 1 55  ? -4.925  -1.243  7.776   0.46 27.30  ? 52  ASP   A H    1 
ATOM   820  H  H    B ASP   A 1 55  ? -4.909  -1.251  7.772   0.54 27.30  ? 52  ASP   A H    1 
ATOM   821  H  HA   . ASP   A 1 55  ? -6.861  -3.112  7.732   1.00 28.37  ? 52  ASP   A HA   1 
ATOM   822  H  HB2  . ASP   A 1 55  ? -6.344  -0.893  6.091   1.00 28.40  ? 52  ASP   A HB2  1 
ATOM   823  H  HB3  . ASP   A 1 55  ? -7.392  -1.998  5.638   1.00 28.40  ? 52  ASP   A HB3  1 
ATOM   824  N  N    . ARG   A 1 56  ? -5.539  -4.853  6.399   1.00 18.79  ? 53  ARG   A N    1 
ATOM   825  C  CA   . ARG   A 1 56  ? -4.815  -5.709  5.455   1.00 17.95  ? 53  ARG   A CA   1 
ATOM   826  C  C    . ARG   A 1 56  ? -5.264  -5.394  4.011   1.00 18.63  ? 53  ARG   A C    1 
ATOM   827  O  O    . ARG   A 1 56  ? -6.376  -4.911  3.769   1.00 21.45  ? 53  ARG   A O    1 
ATOM   828  C  CB   . ARG   A 1 56  ? -4.990  -7.170  5.836   1.00 17.78  ? 53  ARG   A CB   1 
ATOM   829  C  CG   . ARG   A 1 56  ? -4.224  -7.512  7.115   1.00 19.52  ? 53  ARG   A CG   1 
ATOM   830  C  CD   . ARG   A 1 56  ? -4.045  -8.980  7.386   1.00 16.79  ? 53  ARG   A CD   1 
ATOM   831  N  NE   . ARG   A 1 56  ? -5.287  -9.575  7.871   1.00 18.94  ? 53  ARG   A NE   1 
ATOM   832  C  CZ   . ARG   A 1 56  ? -5.998  -10.505 7.245   1.00 19.98  ? 53  ARG   A CZ   1 
ATOM   833  N  NH1  . ARG   A 1 56  ? -5.631  -11.002 6.063   1.00 19.44  ? 53  ARG   A NH1  1 
ATOM   834  N  NH2  . ARG   A 1 56  ? -7.104  -10.951 7.820   1.00 21.20  ? 53  ARG   A NH2  1 
ATOM   835  H  H    . ARG   A 1 56  ? -5.999  -5.260  7.001   1.00 22.59  ? 53  ARG   A H    1 
ATOM   836  H  HA   . ARG   A 1 56  ? -3.861  -5.540  5.487   1.00 21.59  ? 53  ARG   A HA   1 
ATOM   837  H  HB2  . ARG   A 1 56  ? -5.931  -7.352  5.986   1.00 21.38  ? 53  ARG   A HB2  1 
ATOM   838  H  HB3  . ARG   A 1 56  ? -4.654  -7.731  5.119   1.00 21.38  ? 53  ARG   A HB3  1 
ATOM   839  H  HG2  . ARG   A 1 56  ? -3.338  -7.120  7.055   1.00 23.47  ? 53  ARG   A HG2  1 
ATOM   840  H  HG3  . ARG   A 1 56  ? -4.703  -7.135  7.869   1.00 23.47  ? 53  ARG   A HG3  1 
ATOM   841  H  HD2  . ARG   A 1 56  ? -3.787  -9.432  6.567   1.00 20.19  ? 53  ARG   A HD2  1 
ATOM   842  H  HD3  . ARG   A 1 56  ? -3.360  -9.103  8.062   1.00 20.19  ? 53  ARG   A HD3  1 
ATOM   843  H  HE   . ARG   A 1 56  ? -5.585  -9.297  8.629   1.00 22.77  ? 53  ARG   A HE   1 
ATOM   844  H  HH11 . ARG   A 1 56  ? -4.913  -10.720 5.682   1.00 23.37  ? 53  ARG   A HH11 1 
ATOM   845  H  HH12 . ARG   A 1 56  ? -6.112  -11.604 5.681   1.00 23.37  ? 53  ARG   A HH12 1 
ATOM   846  H  HH21 . ARG   A 1 56  ? -7.348  -10.638 8.583   1.00 25.48  ? 53  ARG   A HH21 1 
ATOM   847  H  HH22 . ARG   A 1 56  ? -7.579  -11.554 7.431   1.00 25.48  ? 53  ARG   A HH22 1 
ATOM   848  N  N    . ARG   A 1 57  ? -4.378  -5.666  3.029   1.00 18.39  ? 54  ARG   A N    1 
ATOM   849  C  CA   . ARG   A 1 57  ? -4.518  -4.999  1.731   1.00 20.05  ? 54  ARG   A CA   1 
ATOM   850  C  C    . ARG   A 1 57  ? -5.802  -5.348  0.985   1.00 20.68  ? 54  ARG   A C    1 
ATOM   851  O  O    . ARG   A 1 57  ? -6.240  -4.566  0.139   1.00 22.12  ? 54  ARG   A O    1 
ATOM   852  C  CB   . ARG   A 1 57  ? -3.309  -5.290  0.840   1.00 19.91  ? 54  ARG   A CB   1 
ATOM   853  C  CG   . ARG   A 1 57  ? -3.073  -6.785  0.524   1.00 20.09  ? 54  ARG   A CG   1 
ATOM   854  C  CD   . ARG   A 1 57  ? -2.135  -6.937  -0.688  1.00 20.01  ? 54  ARG   A CD   1 
ATOM   855  N  NE   . ARG   A 1 57  ? -0.851  -6.268  -0.510  1.00 19.89  ? 54  ARG   A NE   1 
ATOM   856  C  CZ   . ARG   A 1 57  ? -0.016  -5.963  -1.501  1.00 20.25  ? 54  ARG   A CZ   1 
ATOM   857  N  NH1  . ARG   A 1 57  ? -0.294  -6.267  -2.761  1.00 21.35  ? 54  ARG   A NH1  1 
ATOM   858  N  NH2  . ARG   A 1 57  ? 1.091   -5.276  -1.226  1.00 21.30  ? 54  ARG   A NH2  1 
ATOM   859  H  H    . ARG   A 1 57  ? -3.717  -6.212  3.093   1.00 22.11  ? 54  ARG   A H    1 
ATOM   860  H  HA   . ARG   A 1 57  ? -4.546  -4.046  1.908   1.00 24.10  ? 54  ARG   A HA   1 
ATOM   861  H  HB2  . ARG   A 1 57  ? -3.434  -4.831  -0.006  1.00 23.94  ? 54  ARG   A HB2  1 
ATOM   862  H  HB3  . ARG   A 1 57  ? -2.514  -4.958  1.284   1.00 23.94  ? 54  ARG   A HB3  1 
ATOM   863  H  HG2  . ARG   A 1 57  ? -2.662  -7.218  1.289   1.00 24.15  ? 54  ARG   A HG2  1 
ATOM   864  H  HG3  . ARG   A 1 57  ? -3.919  -7.212  0.317   1.00 24.15  ? 54  ARG   A HG3  1 
ATOM   865  H  HD2  . ARG   A 1 57  ? -1.962  -7.879  -0.836  1.00 24.05  ? 54  ARG   A HD2  1 
ATOM   866  H  HD3  . ARG   A 1 57  ? -2.565  -6.552  -1.468  1.00 24.05  ? 54  ARG   A HD3  1 
ATOM   867  H  HE   . ARG   A 1 57  ? -0.618  -6.055  0.290   1.00 23.90  ? 54  ARG   A HE   1 
ATOM   868  H  HH11 . ARG   A 1 57  ? -1.029  -6.670  -2.954  1.00 25.67  ? 54  ARG   A HH11 1 
ATOM   869  H  HH12 . ARG   A 1 57  ? 0.260   -6.061  -3.386  1.00 25.67  ? 54  ARG   A HH12 1 
ATOM   870  H  HH21 . ARG   A 1 57  ? 1.258   -5.035  -0.417  1.00 25.60  ? 54  ARG   A HH21 1 
ATOM   871  H  HH22 . ARG   A 1 57  ? 1.639   -5.073  -1.857  1.00 25.60  ? 54  ARG   A HH22 1 
ATOM   872  N  N    . ASP   A 1 58  ? -6.421  -6.476  1.273   1.00 18.32  ? 55  ASP   A N    1 
ATOM   873  C  CA   . ASP   A 1 58  ? -7.676  -6.858  0.635   1.00 20.93  ? 55  ASP   A CA   1 
ATOM   874  C  C    . ASP   A 1 58  ? -8.925  -6.291  1.324   1.00 24.77  ? 55  ASP   A C    1 
ATOM   875  O  O    . ASP   A 1 58  ? -10.036 -6.540  0.831   1.00 25.12  ? 55  ASP   A O    1 
ATOM   876  C  CB   . ASP   A 1 58  ? -7.783  -8.393  0.535   1.00 20.40  ? 55  ASP   A CB   1 
ATOM   877  C  CG   . ASP   A 1 58  ? -6.809  -8.959  -0.490  1.00 22.14  ? 55  ASP   A CG   1 
ATOM   878  O  OD1  . ASP   A 1 58  ? -7.100  -8.824  -1.713  1.00 26.01  ? 55  ASP   A OD1  1 
ATOM   879  O  OD2  . ASP   A 1 58  ? -5.766  -9.501  -0.092  1.00 22.90  ? 55  ASP   A OD2  1 
ATOM   880  H  H    . ASP   A 1 58  ? -6.133  -7.051  1.844   1.00 22.02  ? 55  ASP   A H    1 
ATOM   881  H  HA   . ASP   A 1 58  ? -7.667  -6.502  -0.267  1.00 25.16  ? 55  ASP   A HA   1 
ATOM   882  H  HB2  . ASP   A 1 58  ? -7.579  -8.785  1.398   1.00 24.53  ? 55  ASP   A HB2  1 
ATOM   883  H  HB3  . ASP   A 1 58  ? -8.683  -8.634  0.265   1.00 24.53  ? 55  ASP   A HB3  1 
ATOM   884  N  N    . TYR   A 1 59  ? -8.779  -5.484  2.377   1.00 21.48  ? 56  TYR   A N    1 
ATOM   885  C  CA   . TYR   A 1 59  ? -9.904  -5.093  3.207   1.00 20.68  ? 56  TYR   A CA   1 
ATOM   886  C  C    . TYR   A 1 59  ? -9.934  -3.599  3.515   1.00 22.86  ? 56  TYR   A C    1 
ATOM   887  O  O    . TYR   A 1 59  ? -8.907  -2.904  3.480   1.00 24.70  ? 56  TYR   A O    1 
ATOM   888  C  CB   . TYR   A 1 59  ? -9.860  -5.836  4.538   1.00 22.61  ? 56  TYR   A CB   1 
ATOM   889  C  CG   . TYR   A 1 59  ? -9.827  -7.344  4.492   1.00 21.25  ? 56  TYR   A CG   1 
ATOM   890  C  CD1  . TYR   A 1 59  ? -8.628  -8.051  4.445   1.00 20.06  ? 56  TYR   A CD1  1 
ATOM   891  C  CD2  . TYR   A 1 59  ? -11.013 -8.079  4.560   1.00 22.78  ? 56  TYR   A CD2  1 
ATOM   892  C  CE1  . TYR   A 1 59  ? -8.605  -9.459  4.461   1.00 21.37  ? 56  TYR   A CE1  1 
ATOM   893  C  CE2  . TYR   A 1 59  ? -10.996 -9.470  4.563   1.00 23.47  ? 56  TYR   A CE2  1 
ATOM   894  C  CZ   . TYR   A 1 59  ? -9.794  -10.144 4.501   1.00 22.00  ? 56  TYR   A CZ   1 
ATOM   895  O  OH   . TYR   A 1 59  ? -9.794  -11.528 4.519   1.00 25.71  ? 56  TYR   A OH   1 
ATOM   896  H  H    . TYR   A 1 59  ? -8.027  -5.150  2.628   1.00 25.82  ? 56  TYR   A H    1 
ATOM   897  H  HA   . TYR   A 1 59  ? -10.709 -5.293  2.704   1.00 24.85  ? 56  TYR   A HA   1 
ATOM   898  H  HB2  . TYR   A 1 59  ? -9.062  -5.552  5.011   1.00 27.18  ? 56  TYR   A HB2  1 
ATOM   899  H  HB3  . TYR   A 1 59  ? -10.650 -5.588  5.043   1.00 27.18  ? 56  TYR   A HB3  1 
ATOM   900  H  HD1  . TYR   A 1 59  ? -7.826  -7.584  4.401   1.00 24.12  ? 56  TYR   A HD1  1 
ATOM   901  H  HD2  . TYR   A 1 59  ? -11.827 -7.631  4.603   1.00 27.37  ? 56  TYR   A HD2  1 
ATOM   902  H  HE1  . TYR   A 1 59  ? -7.796  -9.917  4.446   1.00 25.68  ? 56  TYR   A HE1  1 
ATOM   903  H  HE2  . TYR   A 1 59  ? -11.794 -9.945  4.606   1.00 28.21  ? 56  TYR   A HE2  1 
ATOM   904  H  HH   . TYR   A 1 59  ? -9.017  -11.813 4.664   1.00 30.90  ? 56  TYR   A HH   1 
ATOM   905  N  N    . GLY   A 1 60  ? -11.140 -3.124  3.892   1.00 24.91  ? 57  GLY   A N    1 
ATOM   906  C  CA   . GLY   A 1 60  ? -11.246 -1.783  4.447   1.00 26.93  ? 57  GLY   A CA   1 
ATOM   907  C  C    . GLY   A 1 60  ? -10.879 -0.685  3.471   1.00 24.57  ? 57  GLY   A C    1 
ATOM   908  O  O    . GLY   A 1 60  ? -11.350 -0.641  2.335   1.00 29.33  ? 57  GLY   A O    1 
ATOM   909  H  H    . GLY   A 1 60  ? -11.883 -3.553  3.833   1.00 29.93  ? 57  GLY   A H    1 
ATOM   910  H  HA2  . GLY   A 1 60  ? -12.159 -1.633  4.737   1.00 32.36  ? 57  GLY   A HA2  1 
ATOM   911  H  HA3  . GLY   A 1 60  ? -10.655 -1.711  5.213   1.00 32.36  ? 57  GLY   A HA3  1 
ATOM   912  N  N    . GLU   A 1 61  ? -10.019 0.229   3.926   1.00 26.13  ? 58  GLU   A N    1 
ATOM   913  C  CA   . GLU   A 1 61  ? -9.569  1.372   3.148   1.00 26.85  ? 58  GLU   A CA   1 
ATOM   914  C  C    . GLU   A 1 61  ? -8.286  1.103   2.375   1.00 27.84  ? 58  GLU   A C    1 
ATOM   915  O  O    . GLU   A 1 61  ? -7.848  1.969   1.608   1.00 29.67  ? 58  GLU   A O    1 
ATOM   916  C  CB   . GLU   A 1 61  ? -9.379  2.574   4.074   1.00 34.59  ? 58  GLU   A CB   1 
ATOM   917  C  CG   . GLU   A 1 61  ? -10.669 2.996   4.807   1.00 41.07  ? 58  GLU   A CG   1 
ATOM   918  C  CD   . GLU   A 1 61  ? -11.780 3.371   3.842   1.00 54.49  ? 58  GLU   A CD   1 
ATOM   919  O  OE1  . GLU   A 1 61  ? -11.572 4.319   3.057   1.00 55.33  ? 58  GLU   A OE1  1 
ATOM   920  O  OE2  . GLU   A 1 61  ? -12.850 2.720   3.857   1.00 65.77  ? 58  GLU   A OE2  1 
ATOM   921  H  H    . GLU   A 1 61  ? -9.671  0.204   4.713   1.00 31.40  ? 58  GLU   A H    1 
ATOM   922  H  HA   . GLU   A 1 61  ? -10.249 1.601   2.495   1.00 32.26  ? 58  GLU   A HA   1 
ATOM   923  H  HB2  . GLU   A 1 61  ? -8.715  2.349   4.746   1.00 41.55  ? 58  GLU   A HB2  1 
ATOM   924  H  HB3  . GLU   A 1 61  ? -9.075  3.330   3.548   1.00 41.55  ? 58  GLU   A HB3  1 
ATOM   925  H  HG2  . GLU   A 1 61  ? -10.980 2.258   5.354   1.00 49.32  ? 58  GLU   A HG2  1 
ATOM   926  H  HG3  . GLU   A 1 61  ? -10.481 3.767   5.365   1.00 49.32  ? 58  GLU   A HG3  1 
ATOM   927  N  N    . SER   A 1 62  ? -7.680  -0.056  2.558   1.00 23.54  ? 59  SER   A N    1 
ATOM   928  C  CA   . SER   A 1 62  ? -6.581  -0.462  1.696   1.00 23.85  ? 59  SER   A CA   1 
ATOM   929  C  C    . SER   A 1 62  ? -7.160  -0.763  0.319   1.00 25.71  ? 59  SER   A C    1 
ATOM   930  O  O    . SER   A 1 62  ? -8.341  -1.104  0.175   1.00 27.41  ? 59  SER   A O    1 
ATOM   931  C  CB   . SER   A 1 62  ? -5.849  -1.659  2.297   1.00 24.62  ? 59  SER   A CB   1 
ATOM   932  O  OG   . SER   A 1 62  ? -5.129  -1.249  3.459   1.00 23.51  ? 59  SER   A OG   1 
ATOM   933  H  H    . SER   A 1 62  ? -7.883  -0.625  3.171   1.00 28.29  ? 59  SER   A H    1 
ATOM   934  H  HA   . SER   A 1 62  ? -5.909  0.231   1.603   1.00 28.66  ? 59  SER   A HA   1 
ATOM   935  H  HB2  . SER   A 1 62  ? -6.496  -2.339  2.545   1.00 29.59  ? 59  SER   A HB2  1 
ATOM   936  H  HB3  . SER   A 1 62  ? -5.227  -2.015  1.644   1.00 29.59  ? 59  SER   A HB3  1 
ATOM   937  H  HG   . SER   A 1 62  ? -4.829  -1.921  3.863   1.00 28.25  ? 59  SER   A HG   1 
ATOM   938  N  N    . GLU   A 1 63  ? -6.336  -0.586  -0.708  1.00 27.46  ? 60  GLU   A N    1 
ATOM   939  C  CA   . GLU   A 1 63  ? -6.802  -0.769  -2.073  1.00 27.17  ? 60  GLU   A CA   1 
ATOM   940  C  C    . GLU   A 1 63  ? -5.759  -1.498  -2.893  1.00 28.69  ? 60  GLU   A C    1 
ATOM   941  O  O    . GLU   A 1 63  ? -4.596  -1.069  -2.943  1.00 30.13  ? 60  GLU   A O    1 
ATOM   942  C  CB   . GLU   A 1 63  ? -7.108  0.560   -2.758  1.00 34.07  ? 60  GLU   A CB   1 
ATOM   943  C  CG   . GLU   A 1 63  ? -8.055  1.458   -2.011  1.00 40.08  ? 60  GLU   A CG   1 
ATOM   944  C  CD   . GLU   A 1 63  ? -8.403  2.701   -2.808  1.00 55.82  ? 60  GLU   A CD   1 
ATOM   945  O  OE1  . GLU   A 1 63  ? -9.608  3.012   -2.926  1.00 65.39  ? 60  GLU   A OE1  1 
ATOM   946  O  OE2  . GLU   A 1 63  ? -7.471  3.360   -3.317  1.00 52.90  ? 60  GLU   A OE2  1 
ATOM   947  H  H    . GLU   A 1 63  ? -5.509  -0.361  -0.638  1.00 32.99  ? 60  GLU   A H    1 
ATOM   948  H  HA   . GLU   A 1 63  ? -7.608  -1.308  -2.036  1.00 32.65  ? 60  GLU   A HA   1 
ATOM   949  H  HB2  . GLU   A 1 63  ? -6.276  1.046   -2.871  1.00 40.93  ? 60  GLU   A HB2  1 
ATOM   950  H  HB3  . GLU   A 1 63  ? -7.505  0.376   -3.624  1.00 40.93  ? 60  GLU   A HB3  1 
ATOM   951  H  HG2  . GLU   A 1 63  ? -8.876  0.974   -1.828  1.00 48.14  ? 60  GLU   A HG2  1 
ATOM   952  H  HG3  . GLU   A 1 63  ? -7.642  1.736   -1.178  1.00 48.14  ? 60  GLU   A HG3  1 
ATOM   953  N  N    . LEU   A 1 64  ? -6.196  -2.562  -3.567  1.00 25.45  ? 61  LEU   A N    1 
ATOM   954  C  CA   . LEU   A 1 64  ? -5.349  -3.190  -4.570  1.00 26.67  ? 61  LEU   A CA   1 
ATOM   955  C  C    . LEU   A 1 64  ? -5.213  -2.300  -5.787  1.00 29.49  ? 61  LEU   A C    1 
ATOM   956  O  O    . LEU   A 1 64  ? -6.175  -1.652  -6.233  1.00 29.09  ? 61  LEU   A O    1 
ATOM   957  C  CB   . LEU   A 1 64  ? -5.905  -4.543  -4.999  1.00 26.33  ? 61  LEU   A CB   1 
ATOM   958  C  CG   . LEU   A 1 64  ? -6.133  -5.600  -3.926  1.00 24.60  ? 61  LEU   A CG   1 
ATOM   959  C  CD1  . LEU   A 1 64  ? -6.544  -6.904  -4.635  1.00 28.20  ? 61  LEU   A CD1  1 
ATOM   960  C  CD2  . LEU   A 1 64  ? -4.943  -5.880  -3.011  1.00 25.56  ? 61  LEU   A CD2  1 
ATOM   961  H  H    . LEU   A 1 64  ? -6.966  -2.931  -3.462  1.00 30.58  ? 61  LEU   A H    1 
ATOM   962  H  HA   . LEU   A 1 64  ? -4.472  -3.334  -4.180  1.00 32.05  ? 61  LEU   A HA   1 
ATOM   963  H  HB2  . LEU   A 1 64  ? -6.764  -4.387  -5.422  1.00 31.64  ? 61  LEU   A HB2  1 
ATOM   964  H  HB3  . LEU   A 1 64  ? -5.285  -4.925  -5.639  1.00 31.64  ? 61  LEU   A HB3  1 
ATOM   965  H  HG   . LEU   A 1 64  ? -6.820  -5.260  -3.332  1.00 29.56  ? 61  LEU   A HG   1 
ATOM   966  H  HD11 . LEU   A 1 64  ? -6.791  -7.563  -3.967  1.00 33.88  ? 61  LEU   A HD11 1 
ATOM   967  H  HD12 . LEU   A 1 64  ? -7.300  -6.723  -5.215  1.00 33.88  ? 61  LEU   A HD12 1 
ATOM   968  H  HD13 . LEU   A 1 64  ? -5.795  -7.229  -5.159  1.00 33.88  ? 61  LEU   A HD13 1 
ATOM   969  H  HD21 . LEU   A 1 64  ? -5.212  -6.514  -2.328  1.00 30.71  ? 61  LEU   A HD21 1 
ATOM   970  H  HD22 . LEU   A 1 64  ? -4.218  -6.249  -3.539  1.00 30.71  ? 61  LEU   A HD22 1 
ATOM   971  H  HD23 . LEU   A 1 64  ? -4.661  -5.049  -2.597  1.00 30.71  ? 61  LEU   A HD23 1 
ATOM   972  N  N    . THR   A 1 65  ? -4.005  -2.281  -6.342  1.00 25.10  ? 62  THR   A N    1 
ATOM   973  C  CA   . THR   A 1 65  ? -3.728  -1.559  -7.573  1.00 27.46  ? 62  THR   A CA   1 
ATOM   974  C  C    . THR   A 1 65  ? -3.617  -2.504  -8.761  1.00 30.52  ? 62  THR   A C    1 
ATOM   975  O  O    . THR   A 1 65  ? -3.434  -2.045  -9.889  1.00 32.78  ? 62  THR   A O    1 
ATOM   976  C  CB   . THR   A 1 65  ? -2.448  -0.738  -7.422  1.00 33.47  ? 62  THR   A CB   1 
ATOM   977  O  OG1  . THR   A 1 65  ? -1.353  -1.631  -7.175  1.00 30.85  ? 62  THR   A OG1  1 
ATOM   978  C  CG2  . THR   A 1 65  ? -2.580  0.256   -6.249  1.00 30.15  ? 62  THR   A CG2  1 
ATOM   979  H  H    . THR   A 1 65  ? -3.321  -2.687  -6.016  1.00 30.16  ? 62  THR   A H    1 
ATOM   980  H  HA   . THR   A 1 65  ? -4.445  -0.931  -7.753  1.00 33.00  ? 62  THR   A HA   1 
ATOM   981  H  HB   . THR   A 1 65  ? -2.281  -0.228  -8.229  1.00 40.21  ? 62  THR   A HB   1 
ATOM   982  H  HG1  . THR   A 1 65  ? -0.641  -1.195  -7.087  1.00 37.06  ? 62  THR   A HG1  1 
ATOM   983  H  HG21 . THR   A 1 65  ? -1.798  0.829   -6.211  1.00 36.22  ? 62  THR   A HG21 1 
ATOM   984  H  HG22 . THR   A 1 65  ? -3.369  0.807   -6.369  1.00 36.22  ? 62  THR   A HG22 1 
ATOM   985  H  HG23 . THR   A 1 65  ? -2.657  -0.228  -5.412  1.00 36.22  ? 62  THR   A HG23 1 
ATOM   986  N  N    . GLU   A 1 66  ? -3.731  -3.807  -8.531  1.00 28.81  ? 63  GLU   A N    1 
ATOM   987  C  CA   . GLU   A 1 66  ? -3.894  -4.779  -9.599  1.00 31.15  ? 63  GLU   A CA   1 
ATOM   988  C  C    . GLU   A 1 66  ? -4.656  -5.968  -9.044  1.00 25.64  ? 63  GLU   A C    1 
ATOM   989  O  O    . GLU   A 1 66  ? -4.690  -6.170  -7.825  1.00 27.66  ? 63  GLU   A O    1 
ATOM   990  C  CB   . GLU   A 1 66  ? -2.543  -5.181  -10.200 1.00 40.03  ? 63  GLU   A CB   1 
ATOM   991  C  CG   . GLU   A 1 66  ? -1.877  -6.304  -9.547  1.00 31.64  ? 63  GLU   A CG   1 
ATOM   992  C  CD   . GLU   A 1 66  ? -0.401  -6.427  -9.937  1.00 32.56  ? 63  GLU   A CD   1 
ATOM   993  O  OE1  . GLU   A 1 66  ? 0.075   -5.680  -10.819 1.00 46.81  ? 63  GLU   A OE1  1 
ATOM   994  O  OE2  . GLU   A 1 66  ? 0.246   -7.327  -9.360  1.00 32.15  ? 63  GLU   A OE2  1 
ATOM   995  H  H    . GLU   A 1 66  ? -3.715  -4.158  -7.746  1.00 34.61  ? 63  GLU   A H    1 
ATOM   996  H  HA   . GLU   A 1 66  ? -4.427  -4.408  -10.320 1.00 37.43  ? 63  GLU   A HA   1 
ATOM   997  H  HB2  . GLU   A 1 66  ? -2.682  -5.428  -11.127 1.00 48.07  ? 63  GLU   A HB2  1 
ATOM   998  H  HB3  . GLU   A 1 66  ? -1.945  -4.419  -10.145 1.00 48.07  ? 63  GLU   A HB3  1 
ATOM   999  H  HG2  . GLU   A 1 66  ? -1.924  -6.183  -8.586  1.00 38.01  ? 63  GLU   A HG2  1 
ATOM   1000 H  HG3  . GLU   A 1 66  ? -2.324  -7.127  -9.800  1.00 38.01  ? 63  GLU   A HG3  1 
ATOM   1001 N  N    . PRO   A 1 67  ? -5.339  -6.733  -9.900  1.00 26.87  ? 64  PRO   A N    1 
ATOM   1002 C  CA   . PRO   A 1 67  ? -6.190  -7.805  -9.379  1.00 28.19  ? 64  PRO   A CA   1 
ATOM   1003 C  C    . PRO   A 1 67  ? -5.369  -8.884  -8.696  1.00 28.14  ? 64  PRO   A C    1 
ATOM   1004 O  O    . PRO   A 1 67  ? -4.185  -9.068  -8.971  1.00 27.81  ? 64  PRO   A O    1 
ATOM   1005 C  CB   . PRO   A 1 67  ? -6.898  -8.370  -10.619 1.00 34.59  ? 64  PRO   A CB   1 
ATOM   1006 C  CG   . PRO   A 1 67  ? -6.483  -7.528  -11.764 1.00 41.79  ? 64  PRO   A CG   1 
ATOM   1007 C  CD   . PRO   A 1 67  ? -5.248  -6.756  -11.370 1.00 31.06  ? 64  PRO   A CD   1 
ATOM   1008 H  HA   . PRO   A 1 67  ? -6.849  -7.441  -8.768  1.00 33.87  ? 64  PRO   A HA   1 
ATOM   1009 H  HB2  . PRO   A 1 67  ? -6.626  -9.291  -10.756 1.00 41.55  ? 64  PRO   A HB2  1 
ATOM   1010 H  HB3  . PRO   A 1 67  ? -7.859  -8.324  -10.492 1.00 41.55  ? 64  PRO   A HB3  1 
ATOM   1011 H  HG2  . PRO   A 1 67  ? -6.291  -8.100  -12.523 1.00 50.19  ? 64  PRO   A HG2  1 
ATOM   1012 H  HG3  . PRO   A 1 67  ? -7.203  -6.916  -11.983 1.00 50.19  ? 64  PRO   A HG3  1 
ATOM   1013 H  HD2  . PRO   A 1 67  ? -4.444  -7.214  -11.661 1.00 37.31  ? 64  PRO   A HD2  1 
ATOM   1014 H  HD3  . PRO   A 1 67  ? -5.269  -5.858  -11.734 1.00 37.31  ? 64  PRO   A HD3  1 
ATOM   1015 N  N    . LEU   A 1 68  ? -6.021  -9.621  -7.807  1.00 28.79  ? 65  LEU   A N    1 
ATOM   1016 C  CA   . LEU   A 1 68  ? -5.416  -10.851 -7.287  1.00 25.50  ? 65  LEU   A CA   1 
ATOM   1017 C  C    . LEU   A 1 68  ? -5.017  -11.789 -8.419  1.00 28.67  ? 65  LEU   A C    1 
ATOM   1018 O  O    . LEU   A 1 68  ? -5.684  -11.836 -9.467  1.00 29.44  ? 65  LEU   A O    1 
ATOM   1019 C  CB   . LEU   A 1 68  ? -6.374  -11.595 -6.361  1.00 28.09  ? 65  LEU   A CB   1 
ATOM   1020 C  CG   . LEU   A 1 68  ? -6.639  -11.013 -4.983  1.00 30.78  ? 65  LEU   A CG   1 
ATOM   1021 C  CD1  . LEU   A 1 68  ? -7.642  -11.886 -4.268  1.00 35.23  ? 65  LEU   A CD1  1 
ATOM   1022 C  CD2  . LEU   A 1 68  ? -5.373  -10.909 -4.148  1.00 26.42  ? 65  LEU   A CD2  1 
ATOM   1023 H  H    . LEU   A 1 68  ? -6.800  -9.438  -7.492  1.00 34.59  ? 65  LEU   A H    1 
ATOM   1024 H  HA   . LEU   A 1 68  ? -4.622  -10.594 -6.793  1.00 30.64  ? 65  LEU   A HA   1 
ATOM   1025 H  HB2  . LEU   A 1 68  ? -7.232  -11.649 -6.809  1.00 33.75  ? 65  LEU   A HB2  1 
ATOM   1026 H  HB3  . LEU   A 1 68  ? -6.015  -12.485 -6.222  1.00 33.75  ? 65  LEU   A HB3  1 
ATOM   1027 H  HG   . LEU   A 1 68  ? -6.985  -10.114 -5.091  1.00 36.98  ? 65  LEU   A HG   1 
ATOM   1028 H  HD11 . LEU   A 1 68  ? -7.798  -11.525 -3.382  1.00 42.32  ? 65  LEU   A HD11 1 
ATOM   1029 H  HD12 . LEU   A 1 68  ? -8.470  -11.894 -4.773  1.00 42.32  ? 65  LEU   A HD12 1 
ATOM   1030 H  HD13 . LEU   A 1 68  ? -7.286  -12.786 -4.202  1.00 42.32  ? 65  LEU   A HD13 1 
ATOM   1031 H  HD21 . LEU   A 1 68  ? -5.591  -10.508 -3.292  1.00 31.75  ? 65  LEU   A HD21 1 
ATOM   1032 H  HD22 . LEU   A 1 68  ? -5.010  -11.799 -4.014  1.00 31.75  ? 65  LEU   A HD22 1 
ATOM   1033 H  HD23 . LEU   A 1 68  ? -4.729  -10.357 -4.618  1.00 31.75  ? 65  LEU   A HD23 1 
ATOM   1034 N  N    . PRO   A 1 69  ? -3.917  -12.523 -8.271  1.00 25.61  ? 66  PRO   A N    1 
ATOM   1035 C  CA   . PRO   A 1 69  ? -3.565  -13.543 -9.265  1.00 27.76  ? 66  PRO   A CA   1 
ATOM   1036 C  C    . PRO   A 1 69  ? -4.632  -14.623 -9.294  1.00 31.29  ? 66  PRO   A C    1 
ATOM   1037 O  O    . PRO   A 1 69  ? -5.289  -14.888 -8.289  1.00 28.68  ? 66  PRO   A O    1 
ATOM   1038 C  CB   . PRO   A 1 69  ? -2.229  -14.088 -8.764  1.00 29.38  ? 66  PRO   A CB   1 
ATOM   1039 C  CG   . PRO   A 1 69  ? -2.211  -13.782 -7.318  1.00 31.26  ? 66  PRO   A CG   1 
ATOM   1040 C  CD   . PRO   A 1 69  ? -2.983  -12.497 -7.142  1.00 28.23  ? 66  PRO   A CD   1 
ATOM   1041 H  HA   . PRO   A 1 69  ? -3.441  -13.160 -10.148 1.00 33.35  ? 66  PRO   A HA   1 
ATOM   1042 H  HB2  . PRO   A 1 69  ? -2.184  -15.045 -8.917  1.00 35.30  ? 66  PRO   A HB2  1 
ATOM   1043 H  HB3  . PRO   A 1 69  ? -1.498  -13.644 -9.222  1.00 35.30  ? 66  PRO   A HB3  1 
ATOM   1044 H  HG2  . PRO   A 1 69  ? -2.634  -14.504 -6.828  1.00 37.55  ? 66  PRO   A HG2  1 
ATOM   1045 H  HG3  . PRO   A 1 69  ? -1.294  -13.672 -7.021  1.00 37.55  ? 66  PRO   A HG3  1 
ATOM   1046 H  HD2  . PRO   A 1 69  ? -3.460  -12.491 -6.297  1.00 33.92  ? 66  PRO   A HD2  1 
ATOM   1047 H  HD3  . PRO   A 1 69  ? -2.395  -11.728 -7.196  1.00 33.92  ? 66  PRO   A HD3  1 
ATOM   1048 N  N    . ASP   A 1 70  ? -4.811  -15.257 -10.460 1.00 31.31  ? 67  ASP   A N    1 
ATOM   1049 C  CA   . ASP   A 1 70  ? -5.855  -16.271 -10.540 1.00 36.60  ? 67  ASP   A CA   1 
ATOM   1050 C  C    . ASP   A 1 70  ? -5.608  -17.414 -9.559  1.00 34.01  ? 67  ASP   A C    1 
ATOM   1051 O  O    . ASP   A 1 70  ? -6.562  -17.993 -9.023  1.00 35.43  ? 67  ASP   A O    1 
ATOM   1052 C  CB   . ASP   A 1 70  ? -5.976  -16.822 -11.959 1.00 41.59  ? 67  ASP   A CB   1 
ATOM   1053 C  CG   . ASP   A 1 70  ? -6.498  -15.796 -12.941 1.00 52.01  ? 67  ASP   A CG   1 
ATOM   1054 O  OD1  . ASP   A 1 70  ? -7.460  -15.067 -12.589 1.00 45.22  ? 67  ASP   A OD1  1 
ATOM   1055 O  OD2  . ASP   A 1 70  ? -5.978  -15.758 -14.075 1.00 57.46  ? 67  ASP   A OD2  1 
ATOM   1056 H  H    . ASP   A 1 70  ? -4.362  -15.123 -11.181 1.00 37.61  ? 67  ASP   A H    1 
ATOM   1057 H  HA   . ASP   A 1 70  ? -6.698  -15.848 -10.315 1.00 43.96  ? 67  ASP   A HA   1 
ATOM   1058 H  HB2  . ASP   A 1 70  ? -5.101  -17.110 -12.262 1.00 49.95  ? 67  ASP   A HB2  1 
ATOM   1059 H  HB3  . ASP   A 1 70  ? -6.590  -17.573 -11.956 1.00 49.95  ? 67  ASP   A HB3  1 
ATOM   1060 N  N    . SER   A 1 71  ? -4.342  -17.729 -9.293  1.00 30.60  ? 68  SER   A N    1 
ATOM   1061 C  CA   . SER   A 1 71  ? -4.017  -18.841 -8.412  1.00 29.60  ? 68  SER   A CA   1 
ATOM   1062 C  C    . SER   A 1 71  ? -4.452  -18.604 -6.971  1.00 31.95  ? 68  SER   A C    1 
ATOM   1063 O  O    . SER   A 1 71  ? -4.473  -19.564 -6.195  1.00 26.60  ? 68  SER   A O    1 
ATOM   1064 C  CB   . SER   A 1 71  ? -2.516  -19.106 -8.451  1.00 31.54  ? 68  SER   A CB   1 
ATOM   1065 O  OG   . SER   A 1 71  ? -1.791  -17.993 -7.983  1.00 35.92  ? 68  SER   A OG   1 
ATOM   1066 H  H    . SER   A 1 71  ? -3.658  -17.316 -9.609  1.00 36.76  ? 68  SER   A H    1 
ATOM   1067 H  HA   . SER   A 1 71  ? -4.477  -19.632 -8.732  1.00 35.56  ? 68  SER   A HA   1 
ATOM   1068 H  HB2  . SER   A 1 71  ? -2.317  -19.870 -7.888  1.00 37.89  ? 68  SER   A HB2  1 
ATOM   1069 H  HB3  . SER   A 1 71  ? -2.254  -19.290 -9.367  1.00 37.89  ? 68  SER   A HB3  1 
ATOM   1070 H  HG   . SER   A 1 71  ? -1.029  -18.235 -7.724  1.00 43.14  ? 68  SER   A HG   1 
ATOM   1071 N  N    . ALA   A 1 72  ? -4.805  -17.372 -6.589  1.00 24.07  ? 69  ALA   A N    1 
ATOM   1072 C  CA   . ALA   A 1 72  ? -5.165  -17.137 -5.200  1.00 23.47  ? 69  ALA   A CA   1 
ATOM   1073 C  C    . ALA   A 1 72  ? -6.437  -17.882 -4.783  1.00 22.32  ? 69  ALA   A C    1 
ATOM   1074 O  O    . ALA   A 1 72  ? -6.635  -18.123 -3.580  1.00 22.93  ? 69  ALA   A O    1 
ATOM   1075 C  CB   . ALA   A 1 72  ? -5.333  -15.632 -4.940  1.00 22.79  ? 69  ALA   A CB   1 
ATOM   1076 H  H    . ALA   A 1 72  ? -4.842  -16.683 -7.102  1.00 28.92  ? 69  ALA   A H    1 
ATOM   1077 H  HA   . ALA   A 1 72  ? -4.439  -17.458 -4.641  1.00 28.21  ? 69  ALA   A HA   1 
ATOM   1078 H  HB1  . ALA   A 1 72  ? -5.531  -15.494 -4.001  1.00 27.39  ? 69  ALA   A HB1  1 
ATOM   1079 H  HB2  . ALA   A 1 72  ? -4.509  -15.177 -5.175  1.00 27.39  ? 69  ALA   A HB2  1 
ATOM   1080 H  HB3  . ALA   A 1 72  ? -6.062  -15.297 -5.485  1.00 27.39  ? 69  ALA   A HB3  1 
ATOM   1081 N  N    . SER   A 1 73  ? -7.296  -18.267 -5.729  1.00 25.71  ? 70  SER   A N    1 
ATOM   1082 C  CA   . SER   A 1 73  ? -8.475  -19.037 -5.355  1.00 28.07  ? 70  SER   A CA   1 
ATOM   1083 C  C    . SER   A 1 73  ? -8.140  -20.483 -4.984  1.00 29.08  ? 70  SER   A C    1 
ATOM   1084 O  O    . SER   A 1 73  ? -8.965  -21.150 -4.346  1.00 33.57  ? 70  SER   A O    1 
ATOM   1085 C  CB   . SER   A 1 73  ? -9.488  -19.018 -6.502  1.00 32.60  ? 70  SER   A CB   1 
ATOM   1086 O  OG   . SER   A 1 73  ? -8.823  -19.296 -7.696  1.00 41.04  ? 70  SER   A OG   1 
ATOM   1087 H  H    . SER   A 1 73  ? -7.218  -18.099 -6.569  1.00 30.89  ? 70  SER   A H    1 
ATOM   1088 H  HA   . SER   A 1 73  ? -8.883  -18.622 -4.579  1.00 33.72  ? 70  SER   A HA   1 
ATOM   1089 H  HB2  . SER   A 1 73  ? -10.168 -19.692 -6.345  1.00 39.16  ? 70  SER   A HB2  1 
ATOM   1090 H  HB3  . SER   A 1 73  ? -9.898  -18.140 -6.557  1.00 39.16  ? 70  SER   A HB3  1 
ATOM   1091 H  HG   . SER   A 1 73  ? -9.339  -19.174 -8.348  1.00 49.28  ? 70  SER   A HG   1 
ATOM   1092 N  N    . ASN   A 1 74  ? -6.961  -20.978 -5.344  1.00 25.18  ? 71  ASN   A N    1 
ATOM   1093 C  CA   . ASN   A 1 74  ? -6.580  -22.346 -4.984  1.00 25.98  ? 71  ASN   A CA   1 
ATOM   1094 C  C    . ASN   A 1 74  ? -6.449  -22.460 -3.477  1.00 24.18  ? 71  ASN   A C    1 
ATOM   1095 O  O    . ASN   A 1 74  ? -5.782  -21.627 -2.855  1.00 23.21  ? 71  ASN   A O    1 
ATOM   1096 C  CB   . ASN   A 1 74  ? -5.250  -22.741 -5.639  1.00 25.16  ? 71  ASN   A CB   1 
ATOM   1097 C  CG   . ASN   A 1 74  ? -5.309  -22.744 -7.146  1.00 47.72  ? 71  ASN   A CG   1 
ATOM   1098 O  OD1  . ASN   A 1 74  ? -6.381  -22.731 -7.746  1.00 49.91  ? 71  ASN   A OD1  1 
ATOM   1099 N  ND2  . ASN   A 1 74  ? -4.138  -22.747 -7.770  1.00 55.31  ? 71  ASN   A ND2  1 
ATOM   1100 H  H    . ASN   A 1 74  ? -6.366  -20.549 -5.794  1.00 30.25  ? 71  ASN   A H    1 
ATOM   1101 H  HA   . ASN   A 1 74  ? -7.268  -22.954 -5.299  1.00 31.21  ? 71  ASN   A HA   1 
ATOM   1102 H  HB2  . ASN   A 1 74  ? -4.567  -22.109 -5.369  1.00 30.23  ? 71  ASN   A HB2  1 
ATOM   1103 H  HB3  . ASN   A 1 74  ? -5.010  -23.635 -5.349  1.00 30.23  ? 71  ASN   A HB3  1 
ATOM   1104 H  HD21 . ASN   A 1 74  ? -3.408  -22.747 -7.315  1.00 66.41  ? 71  ASN   A HD21 1 
ATOM   1105 H  HD22 . ASN   A 1 74  ? -4.108  -22.749 -8.630  1.00 66.41  ? 71  ASN   A HD22 1 
ATOM   1106 N  N    . PRO   A 1 75  ? -6.989  -23.501 -2.853  1.00 22.99  ? 72  PRO   A N    1 
ATOM   1107 C  CA   . PRO   A 1 75  ? -6.879  -23.594 -1.394  1.00 23.82  ? 72  PRO   A CA   1 
ATOM   1108 C  C    . PRO   A 1 75  ? -5.469  -23.827 -0.882  1.00 22.36  ? 72  PRO   A C    1 
ATOM   1109 O  O    . PRO   A 1 75  ? -5.215  -23.604 0.314   1.00 22.90  ? 72  PRO   A O    1 
ATOM   1110 C  CB   . PRO   A 1 75  ? -7.820  -24.757 -1.045  1.00 28.75  ? 72  PRO   A CB   1 
ATOM   1111 C  CG   . PRO   A 1 75  ? -7.920  -25.538 -2.245  1.00 31.20  ? 72  PRO   A CG   1 
ATOM   1112 C  CD   . PRO   A 1 75  ? -7.810  -24.587 -3.411  1.00 28.98  ? 72  PRO   A CD   1 
ATOM   1113 H  HA   . PRO   A 1 75  ? -7.217  -22.781 -0.988  1.00 28.63  ? 72  PRO   A HA   1 
ATOM   1114 H  HB2  . PRO   A 1 75  ? -7.441  -25.280 -0.321  1.00 34.54  ? 72  PRO   A HB2  1 
ATOM   1115 H  HB3  . PRO   A 1 75  ? -8.688  -24.410 -0.784  1.00 34.54  ? 72  PRO   A HB3  1 
ATOM   1116 H  HG2  . PRO   A 1 75  ? -7.199  -26.186 -2.267  1.00 37.48  ? 72  PRO   A HG2  1 
ATOM   1117 H  HG3  . PRO   A 1 75  ? -8.776  -25.994 -2.260  1.00 37.48  ? 72  PRO   A HG3  1 
ATOM   1118 H  HD2  . PRO   A 1 75  ? -7.366  -25.009 -4.164  1.00 34.81  ? 72  PRO   A HD2  1 
ATOM   1119 H  HD3  . PRO   A 1 75  ? -8.683  -24.262 -3.680  1.00 34.81  ? 72  PRO   A HD3  1 
ATOM   1120 N  N    . ASP   A 1 76  ? -4.523  -24.241 -1.723  1.00 24.48  ? 73  ASP   A N    1 
ATOM   1121 C  CA   . ASP   A 1 76  ? -3.139  -24.375 -1.266  1.00 24.48  ? 73  ASP   A CA   1 
ATOM   1122 C  C    . ASP   A 1 76  ? -2.249  -23.199 -1.677  1.00 26.90  ? 73  ASP   A C    1 
ATOM   1123 O  O    . ASP   A 1 76  ? -1.022  -23.268 -1.497  1.00 28.12  ? 73  ASP   A O    1 
ATOM   1124 C  CB   . ASP   A 1 76  ? -2.552  -25.698 -1.774  1.00 31.60  ? 73  ASP   A CB   1 
ATOM   1125 C  CG   . ASP   A 1 76  ? -2.518  -25.753 -3.270  1.00 44.64  ? 73  ASP   A CG   1 
ATOM   1126 O  OD1  . ASP   A 1 76  ? -3.318  -25.028 -3.903  1.00 49.49  ? 73  ASP   A OD1  1 
ATOM   1127 O  OD2  . ASP   A 1 76  ? -1.709  -26.535 -3.822  1.00 81.64  ? 73  ASP   A OD2  1 
ATOM   1128 H  H    . ASP   A 1 76  ? -4.655  -24.445 -2.548  1.00 29.42  ? 73  ASP   A H    1 
ATOM   1129 H  HA   . ASP   A 1 76  ? -3.138  -24.400 -0.297  1.00 29.41  ? 73  ASP   A HA   1 
ATOM   1130 H  HB2  . ASP   A 1 76  ? -1.644  -25.791 -1.446  1.00 37.97  ? 73  ASP   A HB2  1 
ATOM   1131 H  HB3  . ASP   A 1 76  ? -3.097  -26.434 -1.455  1.00 37.97  ? 73  ASP   A HB3  1 
ATOM   1132 N  N    . SER   A 1 77  ? -2.835  -22.113 -2.172  1.00 21.78  ? 74  SER   A N    1 
ATOM   1133 C  CA   . SER   A 1 77  ? -2.060  -20.930 -2.524  1.00 19.48  ? 74  SER   A CA   1 
ATOM   1134 C  C    . SER   A 1 77  ? -1.431  -20.284 -1.284  1.00 20.07  ? 74  SER   A C    1 
ATOM   1135 O  O    . SER   A 1 77  ? -2.095  -20.100 -0.261  1.00 21.55  ? 74  SER   A O    1 
ATOM   1136 C  CB   . SER   A 1 77  ? -2.965  -19.915 -3.225  1.00 20.43  ? 74  SER   A CB   1 
ATOM   1137 O  OG   . SER   A 1 77  ? -2.261  -18.687 -3.451  1.00 21.72  ? 74  SER   A OG   1 
ATOM   1138 H  H    . SER   A 1 77  ? -3.680  -22.036 -2.314  1.00 26.18  ? 74  SER   A H    1 
ATOM   1139 H  HA   . SER   A 1 77  ? -1.341  -21.194 -3.119  1.00 23.42  ? 74  SER   A HA   1 
ATOM   1140 H  HB2  . SER   A 1 77  ? -3.250  -20.279 -4.078  1.00 24.55  ? 74  SER   A HB2  1 
ATOM   1141 H  HB3  . SER   A 1 77  ? -3.738  -19.739 -2.665  1.00 24.55  ? 74  SER   A HB3  1 
ATOM   1142 H  HG   . SER   A 1 77  ? -2.772  -18.125 -3.810  1.00 26.11  ? 74  SER   A HG   1 
ATOM   1143 N  N    . ASP   A 1 78  ? -0.147  -19.913 -1.381  1.00 19.74  ? 75  ASP   A N    1 
ATOM   1144 C  CA   . ASP   A 1 78  ? 0.499   -19.143 -0.329  1.00 22.44  ? 75  ASP   A CA   1 
ATOM   1145 C  C    . ASP   A 1 78  ? 0.659   -17.664 -0.687  1.00 19.74  ? 75  ASP   A C    1 
ATOM   1146 O  O    . ASP   A 1 78  ? 1.289   -16.923 0.066   1.00 19.58  ? 75  ASP   A O    1 
ATOM   1147 C  CB   . ASP   A 1 78  ? 1.872   -19.729 0.031   1.00 25.85  ? 75  ASP   A CB   1 
ATOM   1148 C  CG   . ASP   A 1 78  ? 2.905   -19.639 -1.071  1.00 34.32  ? 75  ASP   A CG   1 
ATOM   1149 O  OD1  . ASP   A 1 78  ? 2.589   -19.275 -2.222  1.00 31.18  ? 75  ASP   A OD1  1 
ATOM   1150 O  OD2  . ASP   A 1 78  ? 4.071   -19.968 -0.773  1.00 44.21  ? 75  ASP   A OD2  1 
ATOM   1151 H  H    . ASP   A 1 78  ? 0.363   -20.098 -2.048  1.00 23.73  ? 75  ASP   A H    1 
ATOM   1152 H  HA   . ASP   A 1 78  ? -0.063  -19.208 0.459   1.00 26.97  ? 75  ASP   A HA   1 
ATOM   1153 H  HB2  . ASP   A 1 78  ? 2.221   -19.250 0.799   1.00 31.07  ? 75  ASP   A HB2  1 
ATOM   1154 H  HB3  . ASP   A 1 78  ? 1.759   -20.668 0.250   1.00 31.07  ? 75  ASP   A HB3  1 
ATOM   1155 N  N    . TYR   A 1 79  ? 0.081   -17.203 -1.800  1.00 18.62  ? 76  TYR   A N    1 
ATOM   1156 C  CA   . TYR   A 1 79  ? 0.321   -15.834 -2.242  1.00 17.64  ? 76  TYR   A CA   1 
ATOM   1157 C  C    . TYR   A 1 79  ? -0.139  -14.822 -1.196  1.00 19.09  ? 76  TYR   A C    1 
ATOM   1158 O  O    . TYR   A 1 79  ? 0.606   -13.907 -0.821  1.00 17.97  ? 76  TYR   A O    1 
ATOM   1159 C  CB   . TYR   A 1 79  ? -0.379  -15.573 -3.589  1.00 19.90  ? 76  TYR   A CB   1 
ATOM   1160 C  CG   . TYR   A 1 79  ? -0.363  -14.110 -3.938  1.00 17.53  ? 76  TYR   A CG   1 
ATOM   1161 C  CD1  . TYR   A 1 79  ? 0.761   -13.525 -4.470  1.00 23.34  ? 76  TYR   A CD1  1 
ATOM   1162 C  CD2  . TYR   A 1 79  ? -1.437  -13.291 -3.658  1.00 17.67  ? 76  TYR   A CD2  1 
ATOM   1163 C  CE1  . TYR   A 1 79  ? 0.811   -12.186 -4.741  1.00 25.63  ? 76  TYR   A CE1  1 
ATOM   1164 C  CE2  . TYR   A 1 79  ? -1.396  -11.936 -3.917  1.00 19.88  ? 76  TYR   A CE2  1 
ATOM   1165 C  CZ   . TYR   A 1 79  ? -0.263  -11.386 -4.441  1.00 27.00  ? 76  TYR   A CZ   1 
ATOM   1166 O  OH   . TYR   A 1 79  ? -0.219  -10.038 -4.695  1.00 25.22  ? 76  TYR   A OH   1 
ATOM   1167 H  H    . TYR   A 1 79  ? -0.446  -17.657 -2.306  1.00 22.39  ? 76  TYR   A H    1 
ATOM   1168 H  HA   . TYR   A 1 79  ? 1.276   -15.721 -2.373  1.00 21.21  ? 76  TYR   A HA   1 
ATOM   1169 H  HB2  . TYR   A 1 79  ? 0.081   -16.060 -4.291  1.00 23.92  ? 76  TYR   A HB2  1 
ATOM   1170 H  HB3  . TYR   A 1 79  ? -1.302  -15.865 -3.533  1.00 23.92  ? 76  TYR   A HB3  1 
ATOM   1171 H  HD1  . TYR   A 1 79  ? 1.506   -14.052 -4.650  1.00 28.05  ? 76  TYR   A HD1  1 
ATOM   1172 H  HD2  . TYR   A 1 79  ? -2.206  -13.660 -3.288  1.00 21.24  ? 76  TYR   A HD2  1 
ATOM   1173 H  HE1  . TYR   A 1 79  ? 1.573   -11.817 -5.127  1.00 30.79  ? 76  TYR   A HE1  1 
ATOM   1174 H  HE2  . TYR   A 1 79  ? -2.135  -11.402 -3.734  1.00 23.90  ? 76  TYR   A HE2  1 
ATOM   1175 H  HH   . TYR   A 1 79  ? -0.920  -9.670  -4.416  1.00 30.31  ? 76  TYR   A HH   1 
ATOM   1176 N  N    . ARG   A 1 80  ? -1.394  -14.921 -0.756  1.00 17.55  ? 77  ARG   A N    1 
ATOM   1177 C  CA   . ARG   A 1 80  ? -1.916  -13.856 0.096   1.00 18.62  ? 77  ARG   A CA   1 
ATOM   1178 C  C    . ARG   A 1 80  ? -1.234  -13.804 1.452   1.00 16.53  ? 77  ARG   A C    1 
ATOM   1179 O  O    . ARG   A 1 80  ? -0.990  -12.696 1.968   1.00 16.16  ? 77  ARG   A O    1 
ATOM   1180 C  CB   . ARG   A 1 80  ? -3.440  -13.996 0.277   1.00 16.64  ? 77  ARG   A CB   1 
ATOM   1181 C  CG   . ARG   A 1 80  ? -4.235  -13.503 -0.936  1.00 17.72  ? 77  ARG   A CG   1 
ATOM   1182 C  CD   . ARG   A 1 80  ? -5.759  -13.325 -0.644  1.00 19.42  ? 77  ARG   A CD   1 
ATOM   1183 N  NE   . ARG   A 1 80  ? -5.966  -12.328 0.400   1.00 17.25  ? 77  ARG   A NE   1 
ATOM   1184 C  CZ   . ARG   A 1 80  ? -6.313  -12.595 1.658   1.00 18.28  ? 77  ARG   A CZ   1 
ATOM   1185 N  NH1  . ARG   A 1 80  ? -6.599  -13.830 2.061   1.00 18.77  ? 77  ARG   A NH1  1 
ATOM   1186 N  NH2  . ARG   A 1 80  ? -6.391  -11.600 2.539   1.00 19.03  ? 77  ARG   A NH2  1 
ATOM   1187 H  H    . ARG   A 1 80  ? -1.938  -15.564 -0.929  1.00 21.11  ? 77  ARG   A H    1 
ATOM   1188 H  HA   . ARG   A 1 80  ? -1.737  -13.016 -0.355  1.00 22.39  ? 77  ARG   A HA   1 
ATOM   1189 H  HB2  . ARG   A 1 80  ? -3.655  -14.932 0.415   1.00 20.01  ? 77  ARG   A HB2  1 
ATOM   1190 H  HB3  . ARG   A 1 80  ? -3.715  -13.475 1.047   1.00 20.01  ? 77  ARG   A HB3  1 
ATOM   1191 H  HG2  . ARG   A 1 80  ? -3.883  -12.642 -1.214  1.00 21.31  ? 77  ARG   A HG2  1 
ATOM   1192 H  HG3  . ARG   A 1 80  ? -4.143  -14.147 -1.656  1.00 21.31  ? 77  ARG   A HG3  1 
ATOM   1193 H  HD2  . ARG   A 1 80  ? -6.212  -13.028 -1.449  1.00 23.34  ? 77  ARG   A HD2  1 
ATOM   1194 H  HD3  . ARG   A 1 80  ? -6.133  -14.169 -0.345  1.00 23.34  ? 77  ARG   A HD3  1 
ATOM   1195 H  HE   . ARG   A 1 80  ? -5.855  -11.503 0.187   1.00 20.74  ? 77  ARG   A HE   1 
ATOM   1196 H  HH11 . ARG   A 1 80  ? -6.563  -14.484 1.503   1.00 22.57  ? 77  ARG   A HH11 1 
ATOM   1197 H  HH12 . ARG   A 1 80  ? -6.821  -13.975 2.879   1.00 22.57  ? 77  ARG   A HH12 1 
ATOM   1198 H  HH21 . ARG   A 1 80  ? -6.218  -10.794 2.293   1.00 22.87  ? 77  ARG   A HH21 1 
ATOM   1199 H  HH22 . ARG   A 1 80  ? -6.615  -11.763 3.353   1.00 22.87  ? 77  ARG   A HH22 1 
ATOM   1200 N  N    . VAL   A 1 81  ? -1.011  -14.959 2.093   1.00 16.90  ? 78  VAL   A N    1 
ATOM   1201 C  CA   . VAL   A 1 81  ? -0.466  -14.908 3.443   1.00 16.88  ? 78  VAL   A CA   1 
ATOM   1202 C  C    . VAL   A 1 81  ? 0.972   -14.371 3.410   1.00 16.80  ? 78  VAL   A C    1 
ATOM   1203 O  O    . VAL   A 1 81  ? 1.367   -13.575 4.270   1.00 17.19  ? 78  VAL   A O    1 
ATOM   1204 C  CB   . VAL   A 1 81  ? -0.561  -16.273 4.142   1.00 17.57  ? 78  VAL   A CB   1 
ATOM   1205 C  CG1  . VAL   A 1 81  ? 0.377   -17.279 3.543   1.00 18.91  ? 78  VAL   A CG1  1 
ATOM   1206 C  CG2  . VAL   A 1 81  ? -0.312  -16.087 5.634   1.00 18.82  ? 78  VAL   A CG2  1 
ATOM   1207 H  H    . VAL   A 1 81  ? -1.161  -15.746 1.779   1.00 20.32  ? 78  VAL   A H    1 
ATOM   1208 H  HA   . VAL   A 1 81  ? -1.007  -14.294 3.964   1.00 20.30  ? 78  VAL   A HA   1 
ATOM   1209 H  HB   . VAL   A 1 81  ? -1.452  -16.636 4.014   1.00 21.13  ? 78  VAL   A HB   1 
ATOM   1210 H  HG11 . VAL   A 1 81  ? 0.165   -18.157 3.895   1.00 22.74  ? 78  VAL   A HG11 1 
ATOM   1211 H  HG12 . VAL   A 1 81  ? 0.271   -17.274 2.579   1.00 22.74  ? 78  VAL   A HG12 1 
ATOM   1212 H  HG13 . VAL   A 1 81  ? 1.288   -17.040 3.777   1.00 22.74  ? 78  VAL   A HG13 1 
ATOM   1213 H  HG21 . VAL   A 1 81  ? -0.466  -16.930 6.088   1.00 22.63  ? 78  VAL   A HG21 1 
ATOM   1214 H  HG22 . VAL   A 1 81  ? 0.606   -15.801 5.768   1.00 22.63  ? 78  VAL   A HG22 1 
ATOM   1215 H  HG23 . VAL   A 1 81  ? -0.921  -15.412 5.974   1.00 22.63  ? 78  VAL   A HG23 1 
ATOM   1216 N  N    . LYS   A 1 82  ? 1.735   -14.709 2.381   1.00 15.70  ? 79  LYS   A N    1 
ATOM   1217 C  CA   . LYS   A 1 82  ? 3.098   -14.206 2.255   1.00 16.20  ? 79  LYS   A CA   1 
ATOM   1218 C  C    . LYS   A 1 82  ? 3.114   -12.717 1.934   1.00 17.27  ? 79  LYS   A C    1 
ATOM   1219 O  O    . LYS   A 1 82  ? 3.960   -11.972 2.452   1.00 18.80  ? 79  LYS   A O    1 
ATOM   1220 C  CB   . LYS   A 1 82  ? 3.889   -14.995 1.217   1.00 17.43  ? 79  LYS   A CB   1 
ATOM   1221 C  CG   . LYS   A 1 82  ? 4.116   -16.449 1.646   1.00 21.34  ? 79  LYS   A CG   1 
ATOM   1222 C  CD   . LYS   A 1 82  ? 5.064   -16.538 2.818   1.00 25.24  ? 79  LYS   A CD   1 
ATOM   1223 C  CE   . LYS   A 1 82  ? 5.518   -17.977 3.135   1.00 25.63  ? 79  LYS   A CE   1 
ATOM   1224 N  NZ   . LYS   A 1 82  ? 6.166   -18.058 4.493   1.00 22.44  ? 79  LYS   A NZ   1 
ATOM   1225 H  H    . LYS   A 1 82  ? 1.491   -15.228 1.740   1.00 18.88  ? 79  LYS   A H    1 
ATOM   1226 H  HA   . LYS   A 1 82  ? 3.542   -14.337 3.108   1.00 19.48  ? 79  LYS   A HA   1 
ATOM   1227 H  HB2  . LYS   A 1 82  ? 3.400   -14.999 0.380   1.00 20.95  ? 79  LYS   A HB2  1 
ATOM   1228 H  HB3  . LYS   A 1 82  ? 4.756   -14.577 1.092   1.00 20.95  ? 79  LYS   A HB3  1 
ATOM   1229 H  HG2  . LYS   A 1 82  ? 3.269   -16.843 1.908   1.00 25.65  ? 79  LYS   A HG2  1 
ATOM   1230 H  HG3  . LYS   A 1 82  ? 4.499   -16.947 0.906   1.00 25.65  ? 79  LYS   A HG3  1 
ATOM   1231 H  HD2  . LYS   A 1 82  ? 5.856   -16.014 2.621   1.00 30.33  ? 79  LYS   A HD2  1 
ATOM   1232 H  HD3  . LYS   A 1 82  ? 4.621   -16.187 3.607   1.00 30.33  ? 79  LYS   A HD3  1 
ATOM   1233 H  HE2  . LYS   A 1 82  ? 4.748   -18.567 3.127   1.00 30.79  ? 79  LYS   A HE2  1 
ATOM   1234 H  HE3  . LYS   A 1 82  ? 6.163   -18.265 2.471   1.00 30.79  ? 79  LYS   A HE3  1 
ATOM   1235 H  HZ1  . LYS   A 1 82  ? 7.049   -17.990 4.413   1.00 26.97  ? 79  LYS   A HZ1  1 
ATOM   1236 H  HZ2  . LYS   A 1 82  ? 5.870   -17.397 5.011   1.00 26.97  ? 79  LYS   A HZ2  1 
ATOM   1237 H  HZ3  . LYS   A 1 82  ? 5.970   -18.836 4.878   1.00 26.97  ? 79  LYS   A HZ3  1 
ATOM   1238 N  N    . ARG   A 1 83  ? 2.178   -12.262 1.092   1.00 16.60  ? 80  ARG   A N    1 
ATOM   1239 C  CA   . ARG   A 1 83  ? 2.077   -10.854 0.755   1.00 17.30  ? 80  ARG   A CA   1 
ATOM   1240 C  C    . ARG   A 1 83  ? 1.641   -10.024 1.952   1.00 17.85  ? 80  ARG   A C    1 
ATOM   1241 O  O    . ARG   A 1 83  ? 2.140   -8.909  2.132   1.00 17.91  ? 80  ARG   A O    1 
ATOM   1242 C  CB   . ARG   A 1 83  ? 1.119   -10.681 -0.429  1.00 17.63  ? 80  ARG   A CB   1 
ATOM   1243 C  CG   . ARG   A 1 83  ? 1.074   -9.294  -1.049  1.00 20.21  ? 80  ARG   A CG   1 
ATOM   1244 C  CD   . ARG   A 1 83  ? 2.415   -8.821  -1.552  1.00 20.50  ? 80  ARG   A CD   1 
ATOM   1245 N  NE   . ARG   A 1 83  ? 3.088   -7.996  -0.541  1.00 19.01  ? 80  ARG   A NE   1 
ATOM   1246 C  CZ   . ARG   A 1 83  ? 4.078   -7.161  -0.816  1.00 22.95  ? 80  ARG   A CZ   1 
ATOM   1247 N  NH1  . ARG   A 1 83  ? 4.692   -7.186  -1.987  1.00 24.99  ? 80  ARG   A NH1  1 
ATOM   1248 N  NH2  . ARG   A 1 83  ? 4.487   -6.300  0.116   1.00 23.76  ? 80  ARG   A NH2  1 
ATOM   1249 H  H    . ARG   A 1 83  ? 1.590   -12.756 0.704   1.00 19.97  ? 80  ARG   A H    1 
ATOM   1250 H  HA   . ARG   A 1 83  ? 2.949   -10.525 0.485   1.00 20.80  ? 80  ARG   A HA   1 
ATOM   1251 H  HB2  . ARG   A 1 83  ? 1.385   -11.299 -1.128  1.00 21.20  ? 80  ARG   A HB2  1 
ATOM   1252 H  HB3  . ARG   A 1 83  ? 0.221   -10.889 -0.126  1.00 21.20  ? 80  ARG   A HB3  1 
ATOM   1253 H  HG2  . ARG   A 1 83  ? 0.461   -9.305  -1.800  1.00 24.30  ? 80  ARG   A HG2  1 
ATOM   1254 H  HG3  . ARG   A 1 83  ? 0.768   -8.661  -0.380  1.00 24.30  ? 80  ARG   A HG3  1 
ATOM   1255 H  HD2  . ARG   A 1 83  ? 2.976   -9.587  -1.749  1.00 24.64  ? 80  ARG   A HD2  1 
ATOM   1256 H  HD3  . ARG   A 1 83  ? 2.291   -8.287  -2.353  1.00 24.64  ? 80  ARG   A HD3  1 
ATOM   1257 H  HE   . ARG   A 1 83  ? 2.824   -8.059  0.275   1.00 22.86  ? 80  ARG   A HE   1 
ATOM   1258 H  HH11 . ARG   A 1 83  ? 4.451   -7.752  -2.588  1.00 30.03  ? 80  ARG   A HH11 1 
ATOM   1259 H  HH12 . ARG   A 1 83  ? 5.334   -6.636  -2.148  1.00 30.03  ? 80  ARG   A HH12 1 
ATOM   1260 H  HH21 . ARG   A 1 83  ? 4.109   -6.290  0.888   1.00 28.55  ? 80  ARG   A HH21 1 
ATOM   1261 H  HH22 . ARG   A 1 83  ? 5.130   -5.755  -0.056  1.00 28.55  ? 80  ARG   A HH22 1 
ATOM   1262 N  N    . ASP   A 1 84  ? 0.710   -10.541 2.769   1.00 16.34  ? 81  ASP   A N    1 
ATOM   1263 C  CA   . ASP   A 1 84  ? 0.300   -9.855  3.983   1.00 15.61  ? 81  ASP   A CA   1 
ATOM   1264 C  C    . ASP   A 1 84  ? 1.485   -9.724  4.952   1.00 17.33  ? 81  ASP   A C    1 
ATOM   1265 O  O    . ASP   A 1 84  ? 1.695   -8.666  5.561   1.00 17.20  ? 81  ASP   A O    1 
ATOM   1266 C  CB   . ASP   A 1 84  ? -0.817  -10.643 4.687   1.00 17.32  ? 81  ASP   A CB   1 
ATOM   1267 C  CG   . ASP   A 1 84  ? -2.226  -10.280 4.230   1.00 20.84  ? 81  ASP   A CG   1 
ATOM   1268 O  OD1  . ASP   A 1 84  ? -2.454  -9.315  3.445   1.00 18.40  ? 81  ASP   A OD1  1 
ATOM   1269 O  OD2  . ASP   A 1 84  ? -3.168  -10.984 4.689   1.00 18.92  ? 81  ASP   A OD2  1 
ATOM   1270 H  H    . ASP   A 1 84  ? 0.306   -11.288 2.637   1.00 19.65  ? 81  ASP   A H    1 
ATOM   1271 H  HA   . ASP   A 1 84  ? -0.032  -8.976  3.743   1.00 18.78  ? 81  ASP   A HA   1 
ATOM   1272 H  HB2  . ASP   A 1 84  ? -0.687  -11.589 4.513   1.00 20.83  ? 81  ASP   A HB2  1 
ATOM   1273 H  HB3  . ASP   A 1 84  ? -0.765  -10.471 5.640   1.00 20.83  ? 81  ASP   A HB3  1 
ATOM   1274 N  N    . ALA   A 1 85  ? 2.260   -10.800 5.112   1.00 16.15  ? 82  ALA   A N    1 
ATOM   1275 C  CA   . ALA   A 1 85  ? 3.426   -10.752 6.000   1.00 16.22  ? 82  ALA   A CA   1 
ATOM   1276 C  C    . ALA   A 1 85  ? 4.444   -9.746  5.492   1.00 18.13  ? 82  ALA   A C    1 
ATOM   1277 O  O    . ALA   A 1 85  ? 5.017   -8.968  6.273   1.00 17.83  ? 82  ALA   A O    1 
ATOM   1278 C  CB   . ALA   A 1 85  ? 4.067   -12.127 6.143   1.00 16.69  ? 82  ALA   A CB   1 
ATOM   1279 H  H    . ALA   A 1 85  ? 2.136   -11.558 4.725   1.00 19.42  ? 82  ALA   A H    1 
ATOM   1280 H  HA   . ALA   A 1 85  ? 3.126   -10.481 6.882   1.00 19.50  ? 82  ALA   A HA   1 
ATOM   1281 H  HB1  . ALA   A 1 85  ? 4.744   -12.089 6.837   1.00 20.07  ? 82  ALA   A HB1  1 
ATOM   1282 H  HB2  . ALA   A 1 85  ? 3.382   -12.771 6.384   1.00 20.07  ? 82  ALA   A HB2  1 
ATOM   1283 H  HB3  . ALA   A 1 85  ? 4.472   -12.376 5.298   1.00 20.07  ? 82  ALA   A HB3  1 
ATOM   1284 N  N    . GLN   A 1 86  ? 4.710   -9.740  4.171   1.00 17.24  ? 83  GLN   A N    1 
ATOM   1285 C  CA   . GLN   A 1 86  ? 5.663   -8.778  3.646   1.00 17.47  ? 83  GLN   A CA   1 
ATOM   1286 C  C    . GLN   A 1 86  ? 5.162   -7.341  3.838   1.00 18.02  ? 83  GLN   A C    1 
ATOM   1287 O  O    . GLN   A 1 86  ? 5.972   -6.426  4.060   1.00 20.55  ? 83  GLN   A O    1 
ATOM   1288 C  CB   . GLN   A 1 86  ? 5.953   -9.068  2.157   1.00 20.31  ? 83  GLN   A CB   1 
ATOM   1289 C  CG   . GLN   A 1 86  ? 7.151   -8.306  1.639   1.00 22.78  ? 83  GLN   A CG   1 
ATOM   1290 C  CD   . GLN   A 1 86  ? 7.574   -8.723  0.258   1.00 30.50  ? 83  GLN   A CD   1 
ATOM   1291 O  OE1  . GLN   A 1 86  ? 7.572   -9.914  -0.061  1.00 31.15  ? 83  GLN   A OE1  1 
ATOM   1292 N  NE2  . GLN   A 1 86  ? 7.994   -7.754  -0.551  1.00 27.45  ? 83  GLN   A NE2  1 
ATOM   1293 H  H    . GLN   A 1 86  ? 4.360   -10.267 3.589   1.00 20.73  ? 83  GLN   A H    1 
ATOM   1294 H  HA   . GLN   A 1 86  ? 6.499   -8.869  4.130   1.00 21.01  ? 83  GLN   A HA   1 
ATOM   1295 H  HB2  . GLN   A 1 86  ? 6.130   -10.016 2.048   1.00 24.41  ? 83  GLN   A HB2  1 
ATOM   1296 H  HB3  . GLN   A 1 86  ? 5.182   -8.812  1.628   1.00 24.41  ? 83  GLN   A HB3  1 
ATOM   1297 H  HG2  . GLN   A 1 86  ? 6.932   -7.361  1.611   1.00 27.37  ? 83  GLN   A HG2  1 
ATOM   1298 H  HG3  . GLN   A 1 86  ? 7.900   -8.455  2.237   1.00 27.37  ? 83  GLN   A HG3  1 
ATOM   1299 H  HE21 . GLN   A 1 86  ? 8.013   -6.940  -0.274  1.00 32.98  ? 83  GLN   A HE21 1 
ATOM   1300 H  HE22 . GLN   A 1 86  ? 8.247   -7.942  -1.352  1.00 32.98  ? 83  GLN   A HE22 1 
ATOM   1301 N  N    . ASP   A 1 87  ? 3.843   -7.122  3.705   1.00 18.47  ? 84  ASP   A N    1 
ATOM   1302 C  CA   . ASP   A 1 87  ? 3.278   -5.796  3.949   1.00 18.92  ? 84  ASP   A CA   1 
ATOM   1303 C  C    . ASP   A 1 87  ? 3.615   -5.330  5.363   1.00 18.75  ? 84  ASP   A C    1 
ATOM   1304 O  O    . ASP   A 1 87  ? 3.985   -4.178  5.571   1.00 18.54  ? 84  ASP   A O    1 
ATOM   1305 C  CB   . ASP   A 1 87  ? 1.754   -5.800  3.797   1.00 18.59  ? 84  ASP   A CB   1 
ATOM   1306 C  CG   . ASP   A 1 87  ? 1.270   -5.827  2.374   1.00 22.24  ? 84  ASP   A CG   1 
ATOM   1307 O  OD1  . ASP   A 1 87  ? 2.069   -5.788  1.410   1.00 21.93  ? 84  ASP   A OD1  1 
ATOM   1308 O  OD2  . ASP   A 1 87  ? 0.024   -5.965  2.209   1.00 20.97  ? 84  ASP   A OD2  1 
ATOM   1309 H  H    . ASP   A 1 87  ? 3.266   -7.718  3.477   1.00 22.21  ? 84  ASP   A H    1 
ATOM   1310 H  HA   . ASP   A 1 87  ? 3.653   -5.193  3.288   1.00 22.75  ? 84  ASP   A HA   1 
ATOM   1311 H  HB2  . ASP   A 1 87  ? 1.401   -6.586  4.242   1.00 22.35  ? 84  ASP   A HB2  1 
ATOM   1312 H  HB3  . ASP   A 1 87  ? 1.400   -4.997  4.211   1.00 22.35  ? 84  ASP   A HB3  1 
ATOM   1313 N  N    . ILE   A 1 88  ? 3.417   -6.202  6.359   1.00 16.78  ? 85  ILE   A N    1 
ATOM   1314 C  CA   . ILE   A 1 88  ? 3.758   -5.844  7.743   1.00 17.59  ? 85  ILE   A CA   1 
ATOM   1315 C  C    . ILE   A 1 88  ? 5.243   -5.526  7.881   1.00 18.85  ? 85  ILE   A C    1 
ATOM   1316 O  O    . ILE   A 1 88  ? 5.624   -4.573  8.566   1.00 19.95  ? 85  ILE   A O    1 
ATOM   1317 C  CB   . ILE   A 1 88  ? 3.357   -6.954  8.730   1.00 17.56  ? 85  ILE   A CB   1 
ATOM   1318 C  CG1  . ILE   A 1 88  ? 1.854   -7.212  8.663   1.00 17.76  ? 85  ILE   A CG1  1 
ATOM   1319 C  CG2  . ILE   A 1 88  ? 3.810   -6.590  10.165  1.00 19.60  ? 85  ILE   A CG2  1 
ATOM   1320 C  CD1  . ILE   A 1 88  ? 0.989   -6.016  8.923   1.00 20.12  ? 85  ILE   A CD1  1 
ATOM   1321 H  H    . ILE   A 1 88  ? 3.094   -6.993  6.264   1.00 20.18  ? 85  ILE   A H    1 
ATOM   1322 H  HA   . ILE   A 1 88  ? 3.247   -5.048  7.957   1.00 21.14  ? 85  ILE   A HA   1 
ATOM   1323 H  HB   . ILE   A 1 88  ? 3.808   -7.775  8.475   1.00 21.12  ? 85  ILE   A HB   1 
ATOM   1324 H  HG12 . ILE   A 1 88  ? 1.638   -7.538  7.775   1.00 21.36  ? 85  ILE   A HG12 1 
ATOM   1325 H  HG13 . ILE   A 1 88  ? 1.628   -7.882  9.326   1.00 21.36  ? 85  ILE   A HG13 1 
ATOM   1326 H  HG21 . ILE   A 1 88  ? 3.312   -7.129  10.800  1.00 23.56  ? 85  ILE   A HG21 1 
ATOM   1327 H  HG22 . ILE   A 1 88  ? 4.760   -6.771  10.252  1.00 23.56  ? 85  ILE   A HG22 1 
ATOM   1328 H  HG23 . ILE   A 1 88  ? 3.637   -5.649  10.322  1.00 23.56  ? 85  ILE   A HG23 1 
ATOM   1329 H  HD11 . ILE   A 1 88  ? 0.061   -6.296  8.946   1.00 24.19  ? 85  ILE   A HD11 1 
ATOM   1330 H  HD12 . ILE   A 1 88  ? 1.238   -5.626  9.775   1.00 24.19  ? 85  ILE   A HD12 1 
ATOM   1331 H  HD13 . ILE   A 1 88  ? 1.122   -5.369  8.212   1.00 24.19  ? 85  ILE   A HD13 1 
ATOM   1332 N  N    . ALA   A 1 89  ? 6.105   -6.333  7.264   1.00 18.77  ? 86  ALA   A N    1 
ATOM   1333 C  CA   . ALA   A 1 89  ? 7.545   -6.096  7.381   1.00 21.07  ? 86  ALA   A CA   1 
ATOM   1334 C  C    . ALA   A 1 89  ? 7.933   -4.770  6.748   1.00 22.14  ? 86  ALA   A C    1 
ATOM   1335 O  O    . ALA   A 1 89  ? 8.759   -4.021  7.297   1.00 22.97  ? 86  ALA   A O    1 
ATOM   1336 C  CB   . ALA   A 1 89  ? 8.318   -7.232  6.717   1.00 22.98  ? 86  ALA   A CB   1 
ATOM   1337 H  H    . ALA   A 1 89  ? 5.889   -7.011  6.782   1.00 22.57  ? 86  ALA   A H    1 
ATOM   1338 H  HA   . ALA   A 1 89  ? 7.781   -6.071  8.321   1.00 25.32  ? 86  ALA   A HA   1 
ATOM   1339 H  HB1  . ALA   A 1 89  ? 9.268   -7.088  6.850   1.00 27.62  ? 86  ALA   A HB1  1 
ATOM   1340 H  HB2  . ALA   A 1 89  ? 8.051   -8.073  7.120   1.00 27.62  ? 86  ALA   A HB2  1 
ATOM   1341 H  HB3  . ALA   A 1 89  ? 8.114   -7.240  5.769   1.00 27.62  ? 86  ALA   A HB3  1 
ATOM   1342 N  N    . GLU   A 1 90  ? 7.386   -4.480  5.558   1.00 20.54  ? 87  GLU   A N    1 
ATOM   1343 C  CA   . GLU   A 1 90  ? 7.674   -3.222  4.896   1.00 20.45  ? 87  GLU   A CA   1 
ATOM   1344 C  C    . GLU   A 1 90  ? 7.131   -2.056  5.697   1.00 22.35  ? 87  GLU   A C    1 
ATOM   1345 O  O    . GLU   A 1 90  ? 7.771   -1.003  5.797   1.00 25.61  ? 87  GLU   A O    1 
ATOM   1346 C  CB   . GLU   A 1 90  ? 7.073   -3.245  3.500   1.00 24.97  ? 87  GLU   A CB   1 
ATOM   1347 C  CG   . GLU   A 1 90  ? 7.859   -4.069  2.507   1.00 29.89  ? 87  GLU   A CG   1 
ATOM   1348 C  CD   . GLU   A 1 90  ? 9.291   -3.608  2.334   1.00 41.60  ? 87  GLU   A CD   1 
ATOM   1349 O  OE1  . GLU   A 1 90  ? 10.187  -4.479  2.227   1.00 52.64  ? 87  GLU   A OE1  1 
ATOM   1350 O  OE2  . GLU   A 1 90  ? 9.522   -2.381  2.306   1.00 53.50  ? 87  GLU   A OE2  1 
ATOM   1351 H  H    . GLU   A 1 90  ? 6.851   -4.996  5.125   1.00 24.69  ? 87  GLU   A H    1 
ATOM   1352 H  HA   . GLU   A 1 90  ? 8.634   -3.105  4.814   1.00 24.59  ? 87  GLU   A HA   1 
ATOM   1353 H  HB2  . GLU   A 1 90  ? 6.180   -3.619  3.552   1.00 30.01  ? 87  GLU   A HB2  1 
ATOM   1354 H  HB3  . GLU   A 1 90  ? 7.033   -2.336  3.163   1.00 30.01  ? 87  GLU   A HB3  1 
ATOM   1355 H  HG2  . GLU   A 1 90  ? 7.879   -4.989  2.811   1.00 35.91  ? 87  GLU   A HG2  1 
ATOM   1356 H  HG3  . GLU   A 1 90  ? 7.424   -4.014  1.642   1.00 35.91  ? 87  GLU   A HG3  1 
ATOM   1357 N  N    . LEU   A 1 91  ? 5.970   -2.236  6.308   1.00 21.22  ? 88  LEU   A N    1 
ATOM   1358 C  CA   . LEU   A 1 91  ? 5.427   -1.199  7.166   1.00 22.86  ? 88  LEU   A CA   1 
ATOM   1359 C  C    . LEU   A 1 91  ? 6.355   -0.937  8.346   1.00 24.50  ? 88  LEU   A C    1 
ATOM   1360 O  O    . LEU   A 1 91  ? 6.704   0.214   8.632   1.00 26.57  ? 88  LEU   A O    1 
ATOM   1361 C  CB   . LEU   A 1 91  ? 4.037   -1.596  7.656   1.00 23.52  ? 88  LEU   A CB   1 
ATOM   1362 C  CG   . LEU   A 1 91  ? 3.274   -0.593  8.529   1.00 21.95  ? 88  LEU   A CG   1 
ATOM   1363 C  CD1  . LEU   A 1 91  ? 3.160   0.767   7.911   1.00 28.68  ? 88  LEU   A CD1  1 
ATOM   1364 C  CD2  . LEU   A 1 91  ? 1.889   -1.184  8.827   1.00 26.02  ? 88  LEU   A CD2  1 
ATOM   1365 H  H    . LEU   A 1 91  ? 5.483   -2.941  6.244   1.00 25.51  ? 88  LEU   A H    1 
ATOM   1366 H  HA   . LEU   A 1 91  ? 5.339   -0.380  6.653   1.00 27.47  ? 88  LEU   A HA   1 
ATOM   1367 H  HB2  . LEU   A 1 91  ? 3.485   -1.764  6.877   1.00 28.26  ? 88  LEU   A HB2  1 
ATOM   1368 H  HB3  . LEU   A 1 91  ? 4.129   -2.408  8.179   1.00 28.26  ? 88  LEU   A HB3  1 
ATOM   1369 H  HG   . LEU   A 1 91  ? 3.768   -0.450  9.352   1.00 26.38  ? 88  LEU   A HG   1 
ATOM   1370 H  HD11 . LEU   A 1 91  ? 2.603   1.325   8.476   1.00 34.45  ? 88  LEU   A HD11 1 
ATOM   1371 H  HD12 . LEU   A 1 91  ? 4.046   1.155   7.834   1.00 34.45  ? 88  LEU   A HD12 1 
ATOM   1372 H  HD13 . LEU   A 1 91  ? 2.759   0.682   7.032   1.00 34.45  ? 88  LEU   A HD13 1 
ATOM   1373 H  HD21 . LEU   A 1 91  ? 1.396   -0.567  9.390   1.00 31.27  ? 88  LEU   A HD21 1 
ATOM   1374 H  HD22 . LEU   A 1 91  ? 1.416   -1.317  7.990   1.00 31.27  ? 88  LEU   A HD22 1 
ATOM   1375 H  HD23 . LEU   A 1 91  ? 1.998   -2.033  9.283   1.00 31.27  ? 88  LEU   A HD23 1 
ATOM   1376 N  N    . ALA   A 1 92  ? 6.779   -2.000  9.036   1.00 23.48  ? 89  ALA   A N    1 
ATOM   1377 C  CA   . ALA   A 1 92  ? 7.701   -1.848  10.154  1.00 23.05  ? 89  ALA   A CA   1 
ATOM   1378 C  C    . ALA   A 1 92  ? 8.959   -1.106  9.737   1.00 24.03  ? 89  ALA   A C    1 
ATOM   1379 O  O    . ALA   A 1 92  ? 9.413   -0.197  10.439  1.00 27.11  ? 89  ALA   A O    1 
ATOM   1380 C  CB   . ALA   A 1 92  ? 8.028   -3.224  10.724  1.00 22.11  ? 89  ALA   A CB   1 
ATOM   1381 H  H    . ALA   A 1 92  ? 6.547   -2.812  8.876   1.00 28.21  ? 89  ALA   A H    1 
ATOM   1382 H  HA   . ALA   A 1 92  ? 7.280   -1.323  10.853  1.00 27.70  ? 89  ALA   A HA   1 
ATOM   1383 H  HB1  . ALA   A 1 92  ? 8.705   -3.128  11.412  1.00 26.57  ? 89  ALA   A HB1  1 
ATOM   1384 H  HB2  . ALA   A 1 92  ? 7.222   -3.607  11.104  1.00 26.57  ? 89  ALA   A HB2  1 
ATOM   1385 H  HB3  . ALA   A 1 92  ? 8.359   -3.791  10.010  1.00 26.57  ? 89  ALA   A HB3  1 
ATOM   1386 N  N    . LYS   A 1 93  ? 9.545   -1.478  8.592   1.00 24.38  ? 90  LYS   A N    1 
ATOM   1387 C  CA   . LYS   A 1 93  ? 10.780  -0.843  8.152   1.00 27.34  ? 90  LYS   A CA   1 
ATOM   1388 C  C    . LYS   A 1 93  ? 10.561  0.617   7.802   1.00 31.38  ? 90  LYS   A C    1 
ATOM   1389 O  O    . LYS   A 1 93  ? 11.495  1.425   7.896   1.00 30.50  ? 90  LYS   A O    1 
ATOM   1390 C  CB   . LYS   A 1 93  ? 11.341  -1.592  6.940   1.00 25.70  ? 90  LYS   A CB   1 
ATOM   1391 C  CG   . LYS   A 1 93  ? 11.930  -2.975  7.266   1.00 32.81  ? 90  LYS   A CG   1 
ATOM   1392 C  CD   . LYS   A 1 93  ? 12.313  -3.694  5.967   1.00 44.76  ? 90  LYS   A CD   1 
ATOM   1393 C  CE   . LYS   A 1 93  ? 13.069  -4.981  6.237   1.00 49.58  ? 90  LYS   A CE   1 
ATOM   1394 N  NZ   . LYS   A 1 93  ? 13.101  -5.859  5.028   1.00 62.88  ? 90  LYS   A NZ   1 
ATOM   1395 H  H    . LYS   A 1 93  ? 9.248   -2.088  8.063   1.00 29.30  ? 90  LYS   A H    1 
ATOM   1396 H  HA   . LYS   A 1 93  ? 11.431  -0.887  8.870   1.00 32.85  ? 90  LYS   A HA   1 
ATOM   1397 H  HB2  . LYS   A 1 93  ? 10.626  -1.722  6.298   1.00 30.88  ? 90  LYS   A HB2  1 
ATOM   1398 H  HB3  . LYS   A 1 93  ? 12.048  -1.058  6.545   1.00 30.88  ? 90  LYS   A HB3  1 
ATOM   1399 H  HG2  . LYS   A 1 93  ? 12.725  -2.872  7.812   1.00 39.41  ? 90  LYS   A HG2  1 
ATOM   1400 H  HG3  . LYS   A 1 93  ? 11.271  -3.509  7.736   1.00 39.41  ? 90  LYS   A HG3  1 
ATOM   1401 H  HD2  . LYS   A 1 93  ? 11.508  -3.913  5.473   1.00 53.75  ? 90  LYS   A HD2  1 
ATOM   1402 H  HD3  . LYS   A 1 93  ? 12.881  -3.115  5.435   1.00 53.75  ? 90  LYS   A HD3  1 
ATOM   1403 H  HE2  . LYS   A 1 93  ? 13.982  -4.771  6.486   1.00 59.53  ? 90  LYS   A HE2  1 
ATOM   1404 H  HE3  . LYS   A 1 93  ? 12.632  -5.466  6.954   1.00 59.53  ? 90  LYS   A HE3  1 
ATOM   1405 H  HZ1  . LYS   A 1 93  ? 13.545  -6.609  5.208   1.00 75.50  ? 90  LYS   A HZ1  1 
ATOM   1406 H  HZ2  . LYS   A 1 93  ? 12.272  -6.066  4.780   1.00 75.50  ? 90  LYS   A HZ2  1 
ATOM   1407 H  HZ3  . LYS   A 1 93  ? 13.506  -5.437  4.357   1.00 75.50  ? 90  LYS   A HZ3  1 
ATOM   1408 N  N    . SER   A 1 94  ? 9.339   0.974   7.392   1.00 26.60  ? 91  SER   A N    1 
ATOM   1409 C  CA   . SER   A 1 94  ? 9.049   2.355   7.013   1.00 31.41  ? 91  SER   A CA   1 
ATOM   1410 C  C    . SER   A 1 94  ? 8.824   3.247   8.222   1.00 36.80  ? 91  SER   A C    1 
ATOM   1411 O  O    . SER   A 1 94  ? 8.871   4.471   8.089   1.00 36.12  ? 91  SER   A O    1 
ATOM   1412 C  CB   . SER   A 1 94  ? 7.804   2.441   6.115   1.00 32.83  ? 91  SER   A CB   1 
ATOM   1413 O  OG   . SER   A 1 94  ? 6.578   2.295   6.845   1.00 30.29  ? 91  SER   A OG   1 
ATOM   1414 H  H    . SER   A 1 94  ? 8.669   0.439   7.327   1.00 31.97  ? 91  SER   A H    1 
ATOM   1415 H  HA   . SER   A 1 94  ? 9.806   2.683   6.503   1.00 37.73  ? 91  SER   A HA   1 
ATOM   1416 H  HB2  . SER   A 1 94  ? 7.800   3.307   5.677   1.00 39.43  ? 91  SER   A HB2  1 
ATOM   1417 H  HB3  . SER   A 1 94  ? 7.853   1.734   5.452   1.00 39.43  ? 91  SER   A HB3  1 
ATOM   1418 H  HG   . SER   A 1 94  ? 6.554   1.543   7.218   1.00 36.39  ? 91  SER   A HG   1 
ATOM   1419 N  N    . LEU   A 1 95  ? 8.552   2.662   9.386   1.00 32.05  ? 92  LEU   A N    1 
ATOM   1420 C  CA   . LEU   A 1 95  ? 8.238   3.436   10.572  1.00 30.45  ? 92  LEU   A CA   1 
ATOM   1421 C  C    . LEU   A 1 95  ? 9.329   3.412   11.622  1.00 38.78  ? 92  LEU   A C    1 
ATOM   1422 O  O    . LEU   A 1 95  ? 9.335   4.283   12.496  1.00 37.74  ? 92  LEU   A O    1 
ATOM   1423 C  CB   . LEU   A 1 95  ? 6.947   2.907   11.226  1.00 33.58  ? 92  LEU   A CB   1 
ATOM   1424 C  CG   . LEU   A 1 95  ? 5.647   3.034   10.434  1.00 33.44  ? 92  LEU   A CG   1 
ATOM   1425 C  CD1  . LEU   A 1 95  ? 4.577   2.178   11.109  1.00 37.77  ? 92  LEU   A CD1  1 
ATOM   1426 C  CD2  . LEU   A 1 95  ? 5.211   4.472   10.292  1.00 45.66  ? 92  LEU   A CD2  1 
ATOM   1427 H  H    . LEU   A 1 95  ? 8.543   1.811   9.511   1.00 38.51  ? 92  LEU   A H    1 
ATOM   1428 H  HA   . LEU   A 1 95  ? 8.094   4.357   10.304  1.00 36.58  ? 92  LEU   A HA   1 
ATOM   1429 H  HB2  . LEU   A 1 95  ? 7.073   1.963   11.408  1.00 40.34  ? 92  LEU   A HB2  1 
ATOM   1430 H  HB3  . LEU   A 1 95  ? 6.817   3.391   12.057  1.00 40.34  ? 92  LEU   A HB3  1 
ATOM   1431 H  HG   . LEU   A 1 95  ? 5.782   2.714   9.528   1.00 40.17  ? 92  LEU   A HG   1 
ATOM   1432 H  HD11 . LEU   A 1 95  ? 3.748   2.259   10.612  1.00 45.37  ? 92  LEU   A HD11 1 
ATOM   1433 H  HD12 . LEU   A 1 95  ? 4.870   1.253   11.115  1.00 45.37  ? 92  LEU   A HD12 1 
ATOM   1434 H  HD13 . LEU   A 1 95  ? 4.450   2.491   12.018  1.00 45.37  ? 92  LEU   A HD13 1 
ATOM   1435 H  HD21 . LEU   A 1 95  ? 4.390   4.504   9.776   1.00 54.83  ? 92  LEU   A HD21 1 
ATOM   1436 H  HD22 . LEU   A 1 95  ? 5.062   4.845   11.175  1.00 54.83  ? 92  LEU   A HD22 1 
ATOM   1437 H  HD23 . LEU   A 1 95  ? 5.908   4.970   9.836   1.00 54.83  ? 92  LEU   A HD23 1 
ATOM   1438 N  N    . SER   A 1 96  ? 10.264  2.469   11.535  1.00 34.56  ? 93  SER   A N    1 
ATOM   1439 C  CA   . SER   A 1 96  ? 11.186  2.212   12.632  1.00 31.37  ? 93  SER   A CA   1 
ATOM   1440 C  C    . SER   A 1 96  ? 12.514  1.684   12.119  1.00 34.67  ? 93  SER   A C    1 
ATOM   1441 O  O    . SER   A 1 96  ? 12.551  0.769   11.291  1.00 39.50  ? 93  SER   A O    1 
ATOM   1442 C  CB   . SER   A 1 96  ? 10.540  1.191   13.595  1.00 33.47  ? 93  SER   A CB   1 
ATOM   1443 O  OG   . SER   A 1 96  ? 11.348  0.931   14.720  1.00 39.56  ? 93  SER   A OG   1 
ATOM   1444 H  H    . SER   A 1 96  ? 10.383  1.965   10.849  1.00 41.52  ? 93  SER   A H    1 
ATOM   1445 H  HA   . SER   A 1 96  ? 11.386  3.042   13.092  1.00 37.69  ? 93  SER   A HA   1 
ATOM   1446 H  HB2  . SER   A 1 96  ? 9.691   1.548   13.900  1.00 40.20  ? 93  SER   A HB2  1 
ATOM   1447 H  HB3  . SER   A 1 96  ? 10.397  0.360   13.116  1.00 40.20  ? 93  SER   A HB3  1 
ATOM   1448 H  HG   . SER   A 1 96  ? 11.892  0.315   14.545  1.00 47.52  ? 93  SER   A HG   1 
ATOM   1449 N  N    . ASP   A 1 97  ? 13.601  2.234   12.657  1.00 34.59  ? 94  ASP   A N    1 
ATOM   1450 C  CA   . ASP   A 1 97  ? 14.932  1.717   12.399  1.00 43.25  ? 94  ASP   A CA   1 
ATOM   1451 C  C    . ASP   A 1 97  ? 15.295  0.567   13.322  1.00 42.20  ? 94  ASP   A C    1 
ATOM   1452 O  O    . ASP   A 1 97  ? 16.359  -0.039  13.151  1.00 53.59  ? 94  ASP   A O    1 
ATOM   1453 C  CB   . ASP   A 1 97  ? 15.947  2.860   12.559  1.00 47.43  ? 94  ASP   A CB   1 
ATOM   1454 C  CG   . ASP   A 1 97  ? 15.921  3.454   13.954  1.00 66.77  ? 94  ASP   A CG   1 
ATOM   1455 O  OD1  . ASP   A 1 97  ? 14.816  3.847   14.400  1.00 61.77  ? 94  ASP   A OD1  1 
ATOM   1456 O  OD2  . ASP   A 1 97  ? 16.990  3.544   14.594  1.00 79.41  ? 94  ASP   A OD2  1 
ATOM   1457 H  H    . ASP   A 1 97  ? 13.589  2.916   13.181  1.00 41.55  ? 94  ASP   A H    1 
ATOM   1458 H  HA   . ASP   A 1 97  ? 14.988  1.386   11.489  1.00 51.94  ? 94  ASP   A HA   1 
ATOM   1459 H  HB2  . ASP   A 1 97  ? 16.840  2.520   12.391  1.00 56.95  ? 94  ASP   A HB2  1 
ATOM   1460 H  HB3  . ASP   A 1 97  ? 15.736  3.564   11.926  1.00 56.95  ? 94  ASP   A HB3  1 
ATOM   1461 N  N    . GLU   A 1 98  ? 14.440  0.257   14.284  1.00 35.47  ? 95  GLU   A N    1 
ATOM   1462 C  CA   . GLU   A 1 98  ? 14.626  -0.858  15.195  1.00 35.48  ? 95  GLU   A CA   1 
ATOM   1463 C  C    . GLU   A 1 98  ? 13.501  -1.867  15.030  1.00 32.47  ? 95  GLU   A C    1 
ATOM   1464 O  O    . GLU   A 1 98  ? 12.429  -1.532  14.512  1.00 29.84  ? 95  GLU   A O    1 
ATOM   1465 C  CB   . GLU   A 1 98  ? 14.649  -0.381  16.647  1.00 36.06  ? 95  GLU   A CB   1 
ATOM   1466 C  CG   . GLU   A 1 98  ? 13.306  0.024   17.181  1.00 45.71  ? 95  GLU   A CG   1 
ATOM   1467 C  CD   . GLU   A 1 98  ? 13.408  1.025   18.317  1.00 70.07  ? 95  GLU   A CD   1 
ATOM   1468 O  OE1  . GLU   A 1 98  ? 12.858  0.747   19.407  1.00 71.07  ? 95  GLU   A OE1  1 
ATOM   1469 O  OE2  . GLU   A 1 98  ? 14.052  2.081   18.125  1.00 74.70  ? 95  GLU   A OE2  1 
ATOM   1470 H  H    . GLU   A 1 98  ? 13.716  0.697   14.433  1.00 42.61  ? 95  GLU   A H    1 
ATOM   1471 H  HA   . GLU   A 1 98  ? 15.471  -1.291  14.995  1.00 42.62  ? 95  GLU   A HA   1 
ATOM   1472 H  HB2  . GLU   A 1 98  ? 14.982  -1.102  17.205  1.00 43.32  ? 95  GLU   A HB2  1 
ATOM   1473 H  HB3  . GLU   A 1 98  ? 15.236  0.388   16.712  1.00 43.32  ? 95  GLU   A HB3  1 
ATOM   1474 H  HG2  . GLU   A 1 98  ? 12.792  0.432   16.467  1.00 54.89  ? 95  GLU   A HG2  1 
ATOM   1475 H  HG3  . GLU   A 1 98  ? 12.847  -0.763  17.513  1.00 54.89  ? 95  GLU   A HG3  1 
ATOM   1476 N  N    . PRO   A 1 99  ? 13.719  -3.121  15.449  1.00 27.93  ? 96  PRO   A N    1 
ATOM   1477 C  CA   . PRO   A 1 99  ? 12.636  -4.118  15.411  1.00 25.26  ? 96  PRO   A CA   1 
ATOM   1478 C  C    . PRO   A 1 99  ? 11.504  -3.673  16.326  1.00 27.49  ? 96  PRO   A C    1 
ATOM   1479 O  O    . PRO   A 1 99  ? 11.735  -2.952  17.320  1.00 29.35  ? 96  PRO   A O    1 
ATOM   1480 C  CB   . PRO   A 1 99  ? 13.308  -5.406  15.904  1.00 28.58  ? 96  PRO   A CB   1 
ATOM   1481 C  CG   . PRO   A 1 99  ? 14.811  -5.170  15.720  1.00 33.44  ? 96  PRO   A CG   1 
ATOM   1482 C  CD   . PRO   A 1 99  ? 15.006  -3.690  15.910  1.00 29.59  ? 96  PRO   A CD   1 
ATOM   1483 H  HA   . PRO   A 1 99  ? 12.307  -4.268  14.511  1.00 30.35  ? 96  PRO   A HA   1 
ATOM   1484 H  HB2  . PRO   A 1 99  ? 13.092  -5.554  16.838  1.00 34.34  ? 96  PRO   A HB2  1 
ATOM   1485 H  HB3  . PRO   A 1 99  ? 13.008  -6.159  15.370  1.00 34.34  ? 96  PRO   A HB3  1 
ATOM   1486 H  HG2  . PRO   A 1 99  ? 15.307  -5.672  16.386  1.00 40.17  ? 96  PRO   A HG2  1 
ATOM   1487 H  HG3  . PRO   A 1 99  ? 15.081  -5.443  14.829  1.00 40.17  ? 96  PRO   A HG3  1 
ATOM   1488 H  HD2  . PRO   A 1 99  ? 15.163  -3.478  16.843  1.00 35.56  ? 96  PRO   A HD2  1 
ATOM   1489 H  HD3  . PRO   A 1 99  ? 15.742  -3.365  15.367  1.00 35.56  ? 96  PRO   A HD3  1 
ATOM   1490 N  N    . VAL   A 1 100 ? 10.299  -4.089  15.944  1.00 25.80  ? 97  VAL   A N    1 
ATOM   1491 C  CA   . VAL   A 1 100 ? 9.064   -3.576  16.509  1.00 26.38  ? 97  VAL   A CA   1 
ATOM   1492 C  C    . VAL   A 1 100 ? 8.316   -4.673  17.269  1.00 24.47  ? 97  VAL   A C    1 
ATOM   1493 O  O    . VAL   A 1 100 ? 8.618   -5.861  17.173  1.00 23.62  ? 97  VAL   A O    1 
ATOM   1494 C  CB   . VAL   A 1 100 ? 8.155   -2.955  15.435  1.00 24.71  ? 97  VAL   A CB   1 
ATOM   1495 C  CG1  . VAL   A 1 100 ? 8.884   -1.846  14.665  1.00 26.89  ? 97  VAL   A CG1  1 
ATOM   1496 C  CG2  . VAL   A 1 100 ? 7.631   -4.019  14.462  1.00 25.46  ? 97  VAL   A CG2  1 
ATOM   1497 H  H    . VAL   A 1 100 ? 10.172  -4.687  15.340  1.00 31.01  ? 97  VAL   A H    1 
ATOM   1498 H  HA   . VAL   A 1 100 ? 9.308   -2.895  17.155  1.00 31.70  ? 97  VAL   A HA   1 
ATOM   1499 H  HB   . VAL   A 1 100 ? 7.394   -2.560  15.889  1.00 29.70  ? 97  VAL   A HB   1 
ATOM   1500 H  HG11 . VAL   A 1 100 ? 8.257   -1.418  14.061  1.00 32.31  ? 97  VAL   A HG11 1 
ATOM   1501 H  HG12 . VAL   A 1 100 ? 9.231   -1.198  15.297  1.00 32.31  ? 97  VAL   A HG12 1 
ATOM   1502 H  HG13 . VAL   A 1 100 ? 9.613   -2.240  14.160  1.00 32.31  ? 97  VAL   A HG13 1 
ATOM   1503 H  HG21 . VAL   A 1 100 ? 7.191   -3.578  13.718  1.00 30.60  ? 97  VAL   A HG21 1 
ATOM   1504 H  HG22 . VAL   A 1 100 ? 8.378   -4.546  14.138  1.00 30.60  ? 97  VAL   A HG22 1 
ATOM   1505 H  HG23 . VAL   A 1 100 ? 7.000   -4.590  14.927  1.00 30.60  ? 97  VAL   A HG23 1 
ATOM   1506 N  N    . TYR   A 1 101 ? 7.278   -4.258  17.987  1.00 23.54  ? 98  TYR   A N    1 
ATOM   1507 C  CA   . TYR   A 1 101 ? 6.341   -5.153  18.670  1.00 20.97  ? 98  TYR   A CA   1 
ATOM   1508 C  C    . TYR   A 1 101 ? 5.187   -5.460  17.728  1.00 19.89  ? 98  TYR   A C    1 
ATOM   1509 O  O    . TYR   A 1 101 ? 4.709   -4.563  17.036  1.00 21.53  ? 98  TYR   A O    1 
ATOM   1510 C  CB   . TYR   A 1 101 ? 5.822   -4.465  19.950  1.00 24.04  ? 98  TYR   A CB   1 
ATOM   1511 C  CG   . TYR   A 1 101 ? 6.896   -4.172  20.971  1.00 24.12  ? 98  TYR   A CG   1 
ATOM   1512 C  CD1  . TYR   A 1 101 ? 7.675   -3.015  20.892  1.00 26.54  ? 98  TYR   A CD1  1 
ATOM   1513 C  CD2  . TYR   A 1 101 ? 7.121   -5.057  22.021  1.00 25.87  ? 98  TYR   A CD2  1 
ATOM   1514 C  CE1  . TYR   A 1 101 ? 8.655   -2.758  21.835  1.00 28.48  ? 98  TYR   A CE1  1 
ATOM   1515 C  CE2  . TYR   A 1 101 ? 8.110   -4.806  22.961  1.00 25.93  ? 98  TYR   A CE2  1 
ATOM   1516 C  CZ   . TYR   A 1 101 ? 8.864   -3.672  22.856  1.00 26.17  ? 98  TYR   A CZ   1 
ATOM   1517 O  OH   . TYR   A 1 101 ? 9.866   -3.373  23.780  1.00 31.52  ? 98  TYR   A OH   1 
ATOM   1518 H  H    . TYR   A 1 101 ? 7.084   -3.427  18.100  1.00 28.29  ? 98  TYR   A H    1 
ATOM   1519 H  HA   . TYR   A 1 101 ? 6.766   -5.987  18.922  1.00 25.21  ? 98  TYR   A HA   1 
ATOM   1520 H  HB2  . TYR   A 1 101 ? 5.411   -3.622  19.705  1.00 28.89  ? 98  TYR   A HB2  1 
ATOM   1521 H  HB3  . TYR   A 1 101 ? 5.167   -5.045  20.370  1.00 28.89  ? 98  TYR   A HB3  1 
ATOM   1522 H  HD1  . TYR   A 1 101 ? 7.534   -2.411  20.199  1.00 31.89  ? 98  TYR   A HD1  1 
ATOM   1523 H  HD2  . TYR   A 1 101 ? 6.603   -5.826  22.093  1.00 31.08  ? 98  TYR   A HD2  1 
ATOM   1524 H  HE1  . TYR   A 1 101 ? 9.167   -1.984  21.783  1.00 34.22  ? 98  TYR   A HE1  1 
ATOM   1525 H  HE2  . TYR   A 1 101 ? 8.258   -5.405  23.657  1.00 31.16  ? 98  TYR   A HE2  1 
ATOM   1526 H  HH   . TYR   A 1 101 ? 9.849   -3.926  24.411  1.00 37.86  ? 98  TYR   A HH   1 
ATOM   1527 N  N    . ILE   A 1 102 ? 4.752   -6.723  17.696  1.00 19.29  ? 99  ILE   A N    1 
ATOM   1528 C  CA   . ILE   A 1 102 ? 3.692   -7.151  16.787  1.00 18.63  ? 99  ILE   A CA   1 
ATOM   1529 C  C    . ILE   A 1 102 ? 2.715   -8.042  17.541  1.00 19.00  ? 99  ILE   A C    1 
ATOM   1530 O  O    . ILE   A 1 102 ? 3.127   -8.958  18.270  1.00 19.09  ? 99  ILE   A O    1 
ATOM   1531 C  CB   . ILE   A 1 102 ? 4.259   -7.899  15.573  1.00 18.96  ? 99  ILE   A CB   1 
ATOM   1532 C  CG1  . ILE   A 1 102 ? 5.138   -6.957  14.741  1.00 22.80  ? 99  ILE   A CG1  1 
ATOM   1533 C  CG2  . ILE   A 1 102 ? 3.111   -8.455  14.729  1.00 20.86  ? 99  ILE   A CG2  1 
ATOM   1534 C  CD1  . ILE   A 1 102 ? 5.902   -7.665  13.602  1.00 21.78  ? 99  ILE   A CD1  1 
ATOM   1535 H  H    . ILE   A 1 102 ? 5.060   -7.352  18.196  1.00 23.20  ? 99  ILE   A H    1 
ATOM   1536 H  HA   . ILE   A 1 102 ? 3.207   -6.368  16.480  1.00 22.40  ? 99  ILE   A HA   1 
ATOM   1537 H  HB   . ILE   A 1 102 ? 4.809   -8.637  15.880  1.00 22.80  ? 99  ILE   A HB   1 
ATOM   1538 H  HG12 . ILE   A 1 102 ? 4.575   -6.276  14.341  1.00 27.40  ? 99  ILE   A HG12 1 
ATOM   1539 H  HG13 . ILE   A 1 102 ? 5.793   -6.544  15.325  1.00 27.40  ? 99  ILE   A HG13 1 
ATOM   1540 H  HG21 . ILE   A 1 102 ? 3.452   -8.702  13.856  1.00 25.07  ? 99  ILE   A HG21 1 
ATOM   1541 H  HG22 . ILE   A 1 102 ? 2.742   -9.235  15.173  1.00 25.07  ? 99  ILE   A HG22 1 
ATOM   1542 H  HG23 . ILE   A 1 102 ? 2.428   -7.773  14.637  1.00 25.07  ? 99  ILE   A HG23 1 
ATOM   1543 H  HD11 . ILE   A 1 102 ? 6.566   -7.056  13.241  1.00 26.18  ? 99  ILE   A HD11 1 
ATOM   1544 H  HD12 . ILE   A 1 102 ? 6.338   -8.455  13.957  1.00 26.18  ? 99  ILE   A HD12 1 
ATOM   1545 H  HD13 . ILE   A 1 102 ? 5.273   -7.917  12.909  1.00 26.18  ? 99  ILE   A HD13 1 
ATOM   1546 N  N    . LEU   A 1 103 ? 1.414   -7.793  17.356  1.00 19.20  ? 100 LEU   A N    1 
ATOM   1547 C  CA   . LEU   A 1 103 ? 0.388   -8.700  17.866  1.00 19.37  ? 100 LEU   A CA   1 
ATOM   1548 C  C    . LEU   A 1 103 ? -0.605  -8.977  16.754  1.00 17.92  ? 100 LEU   A C    1 
ATOM   1549 O  O    . LEU   A 1 103 ? -1.109  -8.038  16.128  1.00 18.13  ? 100 LEU   A O    1 
ATOM   1550 C  CB   . LEU   A 1 103 ? -0.341  -8.104  19.084  1.00 18.08  ? 100 LEU   A CB   1 
ATOM   1551 C  CG   . LEU   A 1 103 ? -1.371  -9.015  19.745  1.00 19.70  ? 100 LEU   A CG   1 
ATOM   1552 C  CD1  . LEU   A 1 103 ? -1.476  -8.695  21.232  1.00 23.31  ? 100 LEU   A CD1  1 
ATOM   1553 C  CD2  . LEU   A 1 103 ? -2.737  -8.885  19.103  1.00 22.88  ? 100 LEU   A CD2  1 
ATOM   1554 H  H    . LEU   A 1 103 ? 1.105   -7.106  16.940  1.00 23.09  ? 100 LEU   A H    1 
ATOM   1555 H  HA   . LEU   A 1 103 ? 0.800   -9.534  18.140  1.00 23.29  ? 100 LEU   A HA   1 
ATOM   1556 H  HB2  . LEU   A 1 103 ? 0.322   -7.882  19.757  1.00 21.73  ? 100 LEU   A HB2  1 
ATOM   1557 H  HB3  . LEU   A 1 103 ? -0.805  -7.302  18.798  1.00 21.73  ? 100 LEU   A HB3  1 
ATOM   1558 H  HG   . LEU   A 1 103 ? -1.076  -9.931  19.628  1.00 23.69  ? 100 LEU   A HG   1 
ATOM   1559 H  HD11 . LEU   A 1 103 ? -2.123  -9.293  21.638  1.00 28.01  ? 100 LEU   A HD11 1 
ATOM   1560 H  HD12 . LEU   A 1 103 ? -0.606  -8.820  21.644  1.00 28.01  ? 100 LEU   A HD12 1 
ATOM   1561 H  HD13 . LEU   A 1 103 ? -1.764  -7.775  21.338  1.00 28.01  ? 100 LEU   A HD13 1 
ATOM   1562 H  HD21 . LEU   A 1 103 ? -3.399  -9.287  19.686  1.00 27.50  ? 100 LEU   A HD21 1 
ATOM   1563 H  HD22 . LEU   A 1 103 ? -2.937  -7.944  18.974  1.00 27.50  ? 100 LEU   A HD22 1 
ATOM   1564 H  HD23 . LEU   A 1 103 ? -2.728  -9.341  18.247  1.00 27.50  ? 100 LEU   A HD23 1 
ATOM   1565 N  N    . GLY   A 1 104 ? -0.879  -10.253 16.497  1.00 16.73  ? 101 GLY   A N    1 
ATOM   1566 C  CA   . GLY   A 1 104 ? -1.935  -10.641 15.582  1.00 17.95  ? 101 GLY   A CA   1 
ATOM   1567 C  C    . GLY   A 1 104 ? -2.960  -11.494 16.294  1.00 19.24  ? 101 GLY   A C    1 
ATOM   1568 O  O    . GLY   A 1 104 ? -2.615  -12.242 17.200  1.00 20.85  ? 101 GLY   A O    1 
ATOM   1569 H  H    . GLY   A 1 104 ? -0.460  -10.918 16.847  1.00 20.12  ? 101 GLY   A H    1 
ATOM   1570 H  HA2  . GLY   A 1 104 ? -2.373  -9.850  15.231  1.00 21.58  ? 101 GLY   A HA2  1 
ATOM   1571 H  HA3  . GLY   A 1 104 ? -1.561  -11.149 14.845  1.00 21.58  ? 101 GLY   A HA3  1 
ATOM   1572 N  N    . SER   A 1 105 ? -4.224  -11.391 15.860  1.00 17.63  ? 102 SER   A N    1 
ATOM   1573 C  CA   . SER   A 1 105 ? -5.293  -12.239 16.368  1.00 18.93  ? 102 SER   A CA   1 
ATOM   1574 C  C    . SER   A 1 105 ? -5.915  -13.053 15.238  1.00 15.85  ? 102 SER   A C    1 
ATOM   1575 O  O    . SER   A 1 105 ? -6.124  -12.535 14.137  1.00 18.51  ? 102 SER   A O    1 
ATOM   1576 C  CB   . SER   A 1 105 ? -6.392  -11.419 17.017  1.00 26.29  ? 102 SER   A CB   1 
ATOM   1577 O  OG   . SER   A 1 105 ? -7.367  -12.284 17.578  1.00 28.22  ? 102 SER   A OG   1 
ATOM   1578 H  H    . SER   A 1 105 ? -4.482  -10.828 15.263  1.00 21.20  ? 102 SER   A H    1 
ATOM   1579 H  HA   . SER   A 1 105 ? -4.911  -12.845 17.022  1.00 22.76  ? 102 SER   A HA   1 
ATOM   1580 H  HB2  . SER   A 1 105 ? -6.010  -10.869 17.719  1.00 31.59  ? 102 SER   A HB2  1 
ATOM   1581 H  HB3  . SER   A 1 105 ? -6.811  -10.856 16.347  1.00 31.59  ? 102 SER   A HB3  1 
ATOM   1582 H  HG   . SER   A 1 105 ? -6.993  -12.876 18.042  1.00 33.91  ? 102 SER   A HG   1 
ATOM   1583 N  N    . SER   A 1 106 ? -6.254  -14.306 15.514  1.00 18.06  ? 103 SER   A N    1 
ATOM   1584 C  CA   . SER   A 1 106 ? -7.032  -15.144 14.575  1.00 17.17  ? 103 SER   A CA   1 
ATOM   1585 C  C    . SER   A 1 106 ? -6.208  -15.299 13.299  1.00 17.71  ? 103 SER   A C    1 
ATOM   1586 O  O    . SER   A 1 106 ? -5.011  -15.615 13.393  1.00 18.01  ? 103 SER   A O    1 
ATOM   1587 C  CB   . SER   A 1 106 ? -8.430  -14.585 14.384  1.00 21.32  ? 103 SER   A CB   1 
ATOM   1588 O  OG   . SER   A 1 106 ? -9.275  -15.583 13.796  1.00 23.78  ? 103 SER   A OG   1 
ATOM   1589 H  H    . SER   A 1 106 ? -6.048  -14.709 16.246  1.00 21.71  ? 103 SER   A H    1 
ATOM   1590 H  HA   . SER   A 1 106 ? -7.121  -16.023 14.975  1.00 20.65  ? 103 SER   A HA   1 
ATOM   1591 H  HB2  . SER   A 1 106 ? -8.792  -14.327 15.246  1.00 25.63  ? 103 SER   A HB2  1 
ATOM   1592 H  HB3  . SER   A 1 106 ? -8.389  -13.814 13.797  1.00 25.63  ? 103 SER   A HB3  1 
ATOM   1593 N  N    . SER   A 1 107 ? -6.776  -15.095 12.092  1.00 20.02  ? 104 SER   A N    1 
ATOM   1594 C  CA   . SER   A 1 107 ? -5.917  -15.225 10.921  1.00 18.63  ? 104 SER   A CA   1 
ATOM   1595 C  C    . SER   A 1 107 ? -4.814  -14.162 10.886  1.00 17.00  ? 104 SER   A C    1 
ATOM   1596 O  O    . SER   A 1 107 ? -3.772  -14.394 10.257  1.00 17.74  ? 104 SER   A O    1 
ATOM   1597 C  CB   . SER   A 1 107 ? -6.705  -15.199 9.628   1.00 26.05  ? 104 SER   A CB   1 
ATOM   1598 O  OG   . SER   A 1 107 ? -7.443  -14.029 9.549   1.00 26.08  ? 104 SER   A OG   1 
ATOM   1599 H  H    . SER   A 1 107 ? -7.600  -14.896 11.945  1.00 24.07  ? 104 SER   A H    1 
ATOM   1600 H  HA   . SER   A 1 107 ? -5.498  -16.099 10.968  1.00 22.40  ? 104 SER   A HA   1 
ATOM   1601 H  HB2  . SER   A 1 107 ? -6.091  -15.241 8.878   1.00 31.30  ? 104 SER   A HB2  1 
ATOM   1602 H  HB3  . SER   A 1 107 ? -7.308  -15.959 9.606   1.00 31.30  ? 104 SER   A HB3  1 
ATOM   1603 H  HG   . SER   A 1 107 ? -8.001  -14.083 8.923   1.00 31.34  ? 104 SER   A HG   1 
ATOM   1604 N  N    . GLY   A 1 108 ? -4.953  -13.058 11.627  1.00 16.79  ? 105 GLY   A N    1 
ATOM   1605 C  CA   . GLY   A 1 108 ? -3.866  -12.109 11.735  1.00 18.40  ? 105 GLY   A CA   1 
ATOM   1606 C  C    . GLY   A 1 108 ? -2.686  -12.666 12.537  1.00 17.20  ? 105 GLY   A C    1 
ATOM   1607 O  O    . GLY   A 1 108 ? -1.537  -12.239 12.362  1.00 17.19  ? 105 GLY   A O    1 
ATOM   1608 H  H    . GLY   A 1 108 ? -5.660  -12.845 12.067  1.00 20.19  ? 105 GLY   A H    1 
ATOM   1609 H  HA2  . GLY   A 1 108 ? -3.550  -11.879 10.847  1.00 22.12  ? 105 GLY   A HA2  1 
ATOM   1610 H  HA3  . GLY   A 1 108 ? -4.183  -11.305 12.175  1.00 22.12  ? 105 GLY   A HA3  1 
ATOM   1611 N  N    A SER   A 1 109 ? -2.951  -13.595 13.465  0.72 16.20  ? 106 SER   A N    1 
ATOM   1612 N  N    B SER   A 1 109 ? -2.957  -13.598 13.454  0.28 16.29  ? 106 SER   A N    1 
ATOM   1613 C  CA   A SER   A 1 109 ? -1.838  -14.255 14.150  0.72 16.64  ? 106 SER   A CA   1 
ATOM   1614 C  CA   B SER   A 1 109 ? -1.854  -14.250 14.148  0.28 16.69  ? 106 SER   A CA   1 
ATOM   1615 C  C    A SER   A 1 109 ? -1.065  -15.159 13.207  0.72 16.44  ? 106 SER   A C    1 
ATOM   1616 C  C    B SER   A 1 109 ? -1.068  -15.147 13.204  0.28 16.41  ? 106 SER   A C    1 
ATOM   1617 O  O    A SER   A 1 109 ? 0.135   -15.385 13.403  0.72 16.15  ? 106 SER   A O    1 
ATOM   1618 O  O    B SER   A 1 109 ? 0.138   -15.343 13.394  0.28 16.23  ? 106 SER   A O    1 
ATOM   1619 C  CB   A SER   A 1 109 ? -2.342  -15.050 15.358  0.72 18.64  ? 106 SER   A CB   1 
ATOM   1620 C  CB   B SER   A 1 109 ? -2.366  -15.064 15.334  0.28 18.55  ? 106 SER   A CB   1 
ATOM   1621 O  OG   A SER   A 1 109 ? -3.000  -16.210 14.976  0.72 20.26  ? 106 SER   A OG   1 
ATOM   1622 O  OG   B SER   A 1 109 ? -1.256  -15.595 16.038  0.28 18.47  ? 106 SER   A OG   1 
ATOM   1623 H  H    A SER   A 1 109 ? -3.736  -13.850 13.706  0.72 19.48  ? 106 SER   A H    1 
ATOM   1624 H  H    B SER   A 1 109 ? -3.743  -13.860 13.682  0.28 19.59  ? 106 SER   A H    1 
ATOM   1625 H  HA   A SER   A 1 109 ? -1.233  -13.574 14.482  0.72 20.01  ? 106 SER   A HA   1 
ATOM   1626 H  HA   B SER   A 1 109 ? -1.262  -13.566 14.497  0.28 20.07  ? 106 SER   A HA   1 
ATOM   1627 H  HB2  A SER   A 1 109 ? -1.583  -15.290 15.911  0.72 22.41  ? 106 SER   A HB2  1 
ATOM   1628 H  HB2  B SER   A 1 109 ? -2.878  -14.490 15.924  0.28 22.30  ? 106 SER   A HB2  1 
ATOM   1629 H  HB3  A SER   A 1 109 ? -2.957  -14.494 15.861  0.72 22.41  ? 106 SER   A HB3  1 
ATOM   1630 H  HB3  B SER   A 1 109 ? -2.922  -15.791 15.012  0.28 22.30  ? 106 SER   A HB3  1 
ATOM   1631 H  HG   A SER   A 1 109 ? -3.786  -16.030 14.741  0.72 24.36  ? 106 SER   A HG   1 
ATOM   1632 H  HG   B SER   A 1 109 ? -0.858  -16.162 15.562  0.28 22.20  ? 106 SER   A HG   1 
ATOM   1633 N  N    . ILE   A 1 110 ? -1.730  -15.708 12.190  1.00 17.04  ? 107 ILE   A N    1 
ATOM   1634 C  CA   . ILE   A 1 110 ? -1.017  -16.491 11.181  1.00 15.09  ? 107 ILE   A CA   1 
ATOM   1635 C  C    . ILE   A 1 110 ? -0.161  -15.576 10.321  1.00 14.44  ? 107 ILE   A C    1 
ATOM   1636 O  O    . ILE   A 1 110 ? 0.998   -15.899 10.028  1.00 15.06  ? 107 ILE   A O    1 
ATOM   1637 C  CB   . ILE   A 1 110 ? -2.012  -17.303 10.350  1.00 14.27  ? 107 ILE   A CB   1 
ATOM   1638 C  CG1  . ILE   A 1 110 ? -2.793  -18.251 11.275  1.00 17.27  ? 107 ILE   A CG1  1 
ATOM   1639 C  CG2  . ILE   A 1 110 ? -1.273  -18.021 9.218   1.00 17.39  ? 107 ILE   A CG2  1 
ATOM   1640 C  CD1  . ILE   A 1 110 ? -3.864  -19.077 10.564  1.00 19.36  ? 107 ILE   A CD1  1 
ATOM   1641 H  H    . ILE   A 1 110 ? -2.579  -15.642 12.066  1.00 20.49  ? 107 ILE   A H    1 
ATOM   1642 H  HA   . ILE   A 1 110 ? -0.424  -17.118 11.624  1.00 18.15  ? 107 ILE   A HA   1 
ATOM   1643 H  HB   . ILE   A 1 110 ? -2.664  -16.722 9.928   1.00 17.16  ? 107 ILE   A HB   1 
ATOM   1644 H  HG12 . ILE   A 1 110 ? -2.168  -18.869 11.686  1.00 20.77  ? 107 ILE   A HG12 1 
ATOM   1645 H  HG13 . ILE   A 1 110 ? -3.234  -17.723 11.959  1.00 20.77  ? 107 ILE   A HG13 1 
ATOM   1646 H  HG21 . ILE   A 1 110 ? -1.912  -18.539 8.703   1.00 20.92  ? 107 ILE   A HG21 1 
ATOM   1647 H  HG22 . ILE   A 1 110 ? -0.848  -17.361 8.650   1.00 20.92  ? 107 ILE   A HG22 1 
ATOM   1648 H  HG23 . ILE   A 1 110 ? -0.603  -18.609 9.601   1.00 20.92  ? 107 ILE   A HG23 1 
ATOM   1649 H  HD11 . ILE   A 1 110 ? -4.257  -19.697 11.197  1.00 23.28  ? 107 ILE   A HD11 1 
ATOM   1650 H  HD12 . ILE   A 1 110 ? -4.546  -18.480 10.218  1.00 23.28  ? 107 ILE   A HD12 1 
ATOM   1651 H  HD13 . ILE   A 1 110 ? -3.452  -19.566 9.834   1.00 23.28  ? 107 ILE   A HD13 1 
ATOM   1652 N  N    . VAL   A 1 111 ? -0.694  -14.420 9.919   1.00 15.26  ? 108 VAL   A N    1 
ATOM   1653 C  CA   . VAL   A 1 111 ? 0.181   -13.451 9.250   1.00 15.87  ? 108 VAL   A CA   1 
ATOM   1654 C  C    . VAL   A 1 111 ? 1.407   -13.170 10.109  1.00 14.61  ? 108 VAL   A C    1 
ATOM   1655 O  O    . VAL   A 1 111 ? 2.526   -13.123 9.612   1.00 15.85  ? 108 VAL   A O    1 
ATOM   1656 C  CB   . VAL   A 1 111 ? -0.579  -12.161 8.929   1.00 13.80  ? 108 VAL   A CB   1 
ATOM   1657 C  CG1  . VAL   A 1 111 ? 0.354   -11.098 8.345   1.00 16.05  ? 108 VAL   A CG1  1 
ATOM   1658 C  CG2  . VAL   A 1 111 ? -1.729  -12.420 7.992   1.00 15.40  ? 108 VAL   A CG2  1 
ATOM   1659 H  H    . VAL   A 1 111 ? -1.515  -14.183 10.016  1.00 18.35  ? 108 VAL   A H    1 
ATOM   1660 H  HA   . VAL   A 1 111 ? 0.475   -13.837 8.410   1.00 19.08  ? 108 VAL   A HA   1 
ATOM   1661 H  HB   . VAL   A 1 111 ? -0.942  -11.820 9.762   1.00 16.60  ? 108 VAL   A HB   1 
ATOM   1662 H  HG11 . VAL   A 1 111 ? -0.155  -10.289 8.179   1.00 19.31  ? 108 VAL   A HG11 1 
ATOM   1663 H  HG12 . VAL   A 1 111 ? 1.064   -10.917 8.980   1.00 19.31  ? 108 VAL   A HG12 1 
ATOM   1664 H  HG13 . VAL   A 1 111 ? 0.729   -11.429 7.514   1.00 19.31  ? 108 VAL   A HG13 1 
ATOM   1665 H  HG21 . VAL   A 1 111 ? -2.160  -11.578 7.781   1.00 18.53  ? 108 VAL   A HG21 1 
ATOM   1666 H  HG22 . VAL   A 1 111 ? -1.389  -12.830 7.181   1.00 18.53  ? 108 VAL   A HG22 1 
ATOM   1667 H  HG23 . VAL   A 1 111 ? -2.360  -13.016 8.424   1.00 18.53  ? 108 VAL   A HG23 1 
ATOM   1668 N  N    . ALA   A 1 112 ? 1.205   -12.955 11.415  1.00 15.65  ? 109 ALA   A N    1 
ATOM   1669 C  CA   . ALA   A 1 112 ? 2.302   -12.656 12.333  1.00 15.71  ? 109 ALA   A CA   1 
ATOM   1670 C  C    . ALA   A 1 112 ? 3.325   -13.779 12.358  1.00 15.58  ? 109 ALA   A C    1 
ATOM   1671 O  O    . ALA   A 1 112 ? 4.537   -13.522 12.390  1.00 17.71  ? 109 ALA   A O    1 
ATOM   1672 C  CB   . ALA   A 1 112 ? 1.764   -12.444 13.738  1.00 16.38  ? 109 ALA   A CB   1 
ATOM   1673 H  H    . ALA   A 1 112 ? 0.434   -12.977 11.796  1.00 18.82  ? 109 ALA   A H    1 
ATOM   1674 H  HA   . ALA   A 1 112 ? 2.735   -11.842 12.032  1.00 18.89  ? 109 ALA   A HA   1 
ATOM   1675 H  HB1  . ALA   A 1 112 ? 2.492   -12.169 14.317  1.00 19.70  ? 109 ALA   A HB1  1 
ATOM   1676 H  HB2  . ALA   A 1 112 ? 1.082   -11.754 13.714  1.00 19.70  ? 109 ALA   A HB2  1 
ATOM   1677 H  HB3  . ALA   A 1 112 ? 1.382   -13.276 14.059  1.00 19.70  ? 109 ALA   A HB3  1 
ATOM   1678 N  N    . MET   A 1 113 ? 2.856   -15.037 12.320  1.00 15.45  ? 110 MET   A N    1 
ATOM   1679 C  CA   . MET   A 1 113 ? 3.775   -16.192 12.251  1.00 16.00  ? 110 MET   A CA   1 
ATOM   1680 C  C    . MET   A 1 113 ? 4.657   -16.116 11.026  1.00 17.31  ? 110 MET   A C    1 
ATOM   1681 O  O    . MET   A 1 113 ? 5.861   -16.370 11.105  1.00 17.78  ? 110 MET   A O    1 
ATOM   1682 C  CB   . MET   A 1 113 ? 2.871   -17.410 12.249  1.00 16.37  ? 110 MET   A CB   1 
ATOM   1683 C  CG   . MET   A 1 113 ? 2.387   -17.789 13.615  1.00 15.55  ? 110 MET   A CG   1 
ATOM   1684 S  SD   . MET   A 1 113 ? 1.217   -19.144 13.482  1.00 18.55  ? 110 MET   A SD   1 
ATOM   1685 C  CE   . MET   A 1 113 ? 0.485   -19.076 15.125  1.00 21.32  ? 110 MET   A CE   1 
ATOM   1686 H  H    . MET   A 1 113 ? 2.023   -15.249 12.332  1.00 18.59  ? 110 MET   A H    1 
ATOM   1687 H  HA   . MET   A 1 113 ? 4.381   -16.235 13.007  1.00 19.25  ? 110 MET   A HA   1 
ATOM   1688 H  HB2  . MET   A 1 113 ? 2.095   -17.223 11.699  1.00 19.69  ? 110 MET   A HB2  1 
ATOM   1689 H  HB3  . MET   A 1 113 ? 3.362   -18.164 11.887  1.00 19.69  ? 110 MET   A HB3  1 
ATOM   1690 H  HG2  . MET   A 1 113 ? 3.136   -18.074 14.162  1.00 18.70  ? 110 MET   A HG2  1 
ATOM   1691 H  HG3  . MET   A 1 113 ? 1.944   -17.032 14.028  1.00 18.70  ? 110 MET   A HG3  1 
ATOM   1692 H  HE1  . MET   A 1 113 ? -0.161  -19.795 15.213  1.00 25.63  ? 110 MET   A HE1  1 
ATOM   1693 H  HE2  . MET   A 1 113 ? 1.186   -19.179 15.787  1.00 25.63  ? 110 MET   A HE2  1 
ATOM   1694 H  HE3  . MET   A 1 113 ? 0.045   -18.220 15.239  1.00 25.63  ? 110 MET   A HE3  1 
ATOM   1695 N  N    . HIS   A 1 114 ? 4.082   -15.714 9.882   1.00 15.65  ? 111 HIS   A N    1 
ATOM   1696 C  CA   . HIS   A 1 114 ? 4.886   -15.593 8.672   1.00 16.51  ? 111 HIS   A CA   1 
ATOM   1697 C  C    . HIS   A 1 114 ? 5.817   -14.383 8.680   1.00 17.61  ? 111 HIS   A C    1 
ATOM   1698 O  O    . HIS   A 1 114 ? 6.848   -14.423 8.027   1.00 18.01  ? 111 HIS   A O    1 
ATOM   1699 C  CB   . HIS   A 1 114 ? 3.972   -15.559 7.456   1.00 15.67  ? 111 HIS   A CB   1 
ATOM   1700 C  CG   . HIS   A 1 114 ? 3.373   -16.893 7.143   1.00 17.16  ? 111 HIS   A CG   1 
ATOM   1701 N  ND1  . HIS   A 1 114 ? 3.972   -17.803 6.295   1.00 19.54  ? 111 HIS   A ND1  1 
ATOM   1702 C  CD2  . HIS   A 1 114 ? 2.242   -17.478 7.593   1.00 16.78  ? 111 HIS   A CD2  1 
ATOM   1703 C  CE1  . HIS   A 1 114 ? 3.227   -18.896 6.238   1.00 19.96  ? 111 HIS   A CE1  1 
ATOM   1704 N  NE2  . HIS   A 1 114 ? 2.185   -18.735 7.028   1.00 17.97  ? 111 HIS   A NE2  1 
ATOM   1705 H  H    . HIS   A 1 114 ? 3.251   -15.512 9.789   1.00 18.82  ? 111 HIS   A H    1 
ATOM   1706 H  HA   . HIS   A 1 114 ? 5.457   -16.375 8.611   1.00 19.85  ? 111 HIS   A HA   1 
ATOM   1707 H  HB2  . HIS   A 1 114 ? 3.247   -14.937 7.623   1.00 18.85  ? 111 HIS   A HB2  1 
ATOM   1708 H  HB3  . HIS   A 1 114 ? 4.484   -15.272 6.684   1.00 18.85  ? 111 HIS   A HB3  1 
ATOM   1709 H  HD2  . HIS   A 1 114 ? 1.620   -17.104 8.173   1.00 20.18  ? 111 HIS   A HD2  1 
ATOM   1710 H  HE1  . HIS   A 1 114 ? 3.409   -19.651 5.726   1.00 24.00  ? 111 HIS   A HE1  1 
ATOM   1711 H  HE2  . HIS   A 1 114 ? 1.569   -19.319 7.168   1.00 21.60  ? 111 HIS   A HE2  1 
ATOM   1712 N  N    . VAL   A 1 115 ? 5.459   -13.296 9.376   1.00 18.52  ? 112 VAL   A N    1 
ATOM   1713 C  CA   . VAL   A 1 115 ? 6.405   -12.195 9.549   1.00 16.97  ? 112 VAL   A CA   1 
ATOM   1714 C  C    . VAL   A 1 115 ? 7.631   -12.680 10.287  1.00 19.00  ? 112 VAL   A C    1 
ATOM   1715 O  O    . VAL   A 1 115 ? 8.764   -12.346 9.931   1.00 20.08  ? 112 VAL   A O    1 
ATOM   1716 C  CB   . VAL   A 1 115 ? 5.749   -11.011 10.283  1.00 17.19  ? 112 VAL   A CB   1 
ATOM   1717 C  CG1  . VAL   A 1 115 ? 6.786   -9.920  10.557  1.00 19.64  ? 112 VAL   A CG1  1 
ATOM   1718 C  CG2  . VAL   A 1 115 ? 4.600   -10.459 9.522   1.00 16.04  ? 112 VAL   A CG2  1 
ATOM   1719 H  H    . VAL   A 1 115 ? 4.692   -13.178 9.747   1.00 22.27  ? 112 VAL   A H    1 
ATOM   1720 H  HA   . VAL   A 1 115 ? 6.672   -11.884 8.670   1.00 20.40  ? 112 VAL   A HA   1 
ATOM   1721 H  HB   . VAL   A 1 115 ? 5.402   -11.334 11.129  1.00 20.67  ? 112 VAL   A HB   1 
ATOM   1722 H  HG11 . VAL   A 1 115 ? 6.332   -9.124  10.873  1.00 23.61  ? 112 VAL   A HG11 1 
ATOM   1723 H  HG12 . VAL   A 1 115 ? 7.407   -10.237 11.232  1.00 23.61  ? 112 VAL   A HG12 1 
ATOM   1724 H  HG13 . VAL   A 1 115 ? 7.263   -9.724  9.735   1.00 23.61  ? 112 VAL   A HG13 1 
ATOM   1725 H  HG21 . VAL   A 1 115 ? 4.189   -9.751  10.042  1.00 19.29  ? 112 VAL   A HG21 1 
ATOM   1726 H  HG22 . VAL   A 1 115 ? 4.921   -10.106 8.678   1.00 19.29  ? 112 VAL   A HG22 1 
ATOM   1727 H  HG23 . VAL   A 1 115 ? 3.958   -11.168 9.361   1.00 19.29  ? 112 VAL   A HG23 1 
ATOM   1728 N  N    . LEU   A 1 116 ? 7.424   -13.418 11.384  1.00 19.44  ? 113 LEU   A N    1 
ATOM   1729 C  CA   . LEU   A 1 116 ? 8.561   -13.915 12.142  1.00 20.50  ? 113 LEU   A CA   1 
ATOM   1730 C  C    . LEU   A 1 116 ? 9.392   -14.891 11.308  1.00 23.04  ? 113 LEU   A C    1 
ATOM   1731 O  O    . LEU   A 1 116 ? 10.632  -14.856 11.356  1.00 24.60  ? 113 LEU   A O    1 
ATOM   1732 C  CB   . LEU   A 1 116 ? 8.069   -14.557 13.446  1.00 20.32  ? 113 LEU   A CB   1 
ATOM   1733 C  CG   . LEU   A 1 116 ? 9.177   -15.107 14.332  1.00 22.62  ? 113 LEU   A CG   1 
ATOM   1734 C  CD1  . LEU   A 1 116 ? 10.081  -14.016 14.850  1.00 28.60  ? 113 LEU   A CD1  1 
ATOM   1735 C  CD2  . LEU   A 1 116 ? 8.502   -15.857 15.476  1.00 25.35  ? 113 LEU   A CD2  1 
ATOM   1736 H  H    . LEU   A 1 116 ? 6.653   -13.637 11.698  1.00 23.37  ? 113 LEU   A H    1 
ATOM   1737 H  HA   . LEU   A 1 116 ? 9.142   -13.177 12.383  1.00 24.64  ? 113 LEU   A HA   1 
ATOM   1738 H  HB2  . LEU   A 1 116 ? 7.588   -13.888 13.957  1.00 24.42  ? 113 LEU   A HB2  1 
ATOM   1739 H  HB3  . LEU   A 1 116 ? 7.477   -15.293 13.223  1.00 24.42  ? 113 LEU   A HB3  1 
ATOM   1740 H  HG   . LEU   A 1 116 ? 9.754   -15.702 13.828  1.00 27.19  ? 113 LEU   A HG   1 
ATOM   1741 H  HD11 . LEU   A 1 116 ? 10.727  -14.404 15.462  1.00 34.37  ? 113 LEU   A HD11 1 
ATOM   1742 H  HD12 . LEU   A 1 116 ? 10.541  -13.604 14.102  1.00 34.37  ? 113 LEU   A HD12 1 
ATOM   1743 H  HD13 . LEU   A 1 116 ? 9.544   -13.354 15.313  1.00 34.37  ? 113 LEU   A HD13 1 
ATOM   1744 H  HD21 . LEU   A 1 116 ? 9.182   -16.174 16.090  1.00 30.46  ? 113 LEU   A HD21 1 
ATOM   1745 H  HD22 . LEU   A 1 116 ? 7.897   -15.254 15.935  1.00 30.46  ? 113 LEU   A HD22 1 
ATOM   1746 H  HD23 . LEU   A 1 116 ? 8.008   -16.608 15.112  1.00 30.46  ? 113 LEU   A HD23 1 
ATOM   1747 N  N    . LYS   A 1 117 ? 8.731   -15.725 10.499  1.00 20.25  ? 114 LYS   A N    1 
ATOM   1748 C  CA   . LYS   A 1 117 ? 9.455   -16.703 9.688   1.00 20.95  ? 114 LYS   A CA   1 
ATOM   1749 C  C    . LYS   A 1 117 ? 10.262  -16.032 8.582   1.00 21.45  ? 114 LYS   A C    1 
ATOM   1750 O  O    . LYS   A 1 117 ? 11.437  -16.386 8.367   1.00 26.92  ? 114 LYS   A O    1 
ATOM   1751 C  CB   . LYS   A 1 117 ? 8.483   -17.735 9.101   1.00 21.42  ? 114 LYS   A CB   1 
ATOM   1752 C  CG   . LYS   A 1 117 ? 9.184   -18.879 8.331   1.00 24.77  ? 114 LYS   A CG   1 
ATOM   1753 C  CD   . LYS   A 1 117 ? 8.195   -19.908 7.818   1.00 29.63  ? 114 LYS   A CD   1 
ATOM   1754 C  CE   . LYS   A 1 117 ? 8.892   -21.131 7.210   1.00 35.31  ? 114 LYS   A CE   1 
ATOM   1755 N  NZ   . LYS   A 1 117 ? 8.223   -22.454 7.548   1.00 34.05  ? 114 LYS   A NZ   1 
ATOM   1756 H  H    . LYS   A 1 117 ? 7.877   -15.745 10.404  1.00 24.34  ? 114 LYS   A H    1 
ATOM   1757 H  HA   . LYS   A 1 117 ? 10.078  -17.173 10.264  1.00 25.18  ? 114 LYS   A HA   1 
ATOM   1758 H  HB2  . LYS   A 1 117 ? 7.975   -18.132 9.826   1.00 25.75  ? 114 LYS   A HB2  1 
ATOM   1759 H  HB3  . LYS   A 1 117 ? 7.885   -17.285 8.485   1.00 25.75  ? 114 LYS   A HB3  1 
ATOM   1760 H  HG2  . LYS   A 1 117 ? 9.657   -18.508 7.570   1.00 29.76  ? 114 LYS   A HG2  1 
ATOM   1761 H  HG3  . LYS   A 1 117 ? 9.807   -19.328 8.923   1.00 29.76  ? 114 LYS   A HG3  1 
ATOM   1762 H  HD2  . LYS   A 1 117 ? 7.641   -20.211 8.554   1.00 35.60  ? 114 LYS   A HD2  1 
ATOM   1763 H  HD3  . LYS   A 1 117 ? 7.643   -19.503 7.131   1.00 35.60  ? 114 LYS   A HD3  1 
ATOM   1764 H  HE2  . LYS   A 1 117 ? 8.895   -21.041 6.244   1.00 42.42  ? 114 LYS   A HE2  1 
ATOM   1765 H  HE3  . LYS   A 1 117 ? 9.803   -21.168 7.542   1.00 42.42  ? 114 LYS   A HE3  1 
ATOM   1766 H  HZ1  . LYS   A 1 117 ? 8.694   -23.129 7.210   1.00 40.90  ? 114 LYS   A HZ1  1 
ATOM   1767 H  HZ2  . LYS   A 1 117 ? 8.172   -22.553 8.432   1.00 40.90  ? 114 LYS   A HZ2  1 
ATOM   1768 H  HZ3  . LYS   A 1 117 ? 7.401   -22.476 7.207   1.00 40.90  ? 114 LYS   A HZ3  1 
ATOM   1769 N  N    . ASP   A 1 118 ? 9.658   -15.083 7.869   1.00 20.69  ? 115 ASP   A N    1 
ATOM   1770 C  CA   . ASP   A 1 118 ? 10.285  -14.518 6.677   1.00 22.01  ? 115 ASP   A CA   1 
ATOM   1771 C  C    . ASP   A 1 118 ? 11.081  -13.236 6.930   1.00 26.87  ? 115 ASP   A C    1 
ATOM   1772 O  O    . ASP   A 1 118 ? 11.986  -12.923 6.144   1.00 24.08  ? 115 ASP   A O    1 
ATOM   1773 C  CB   . ASP   A 1 118 ? 9.205   -14.228 5.629   1.00 24.57  ? 115 ASP   A CB   1 
ATOM   1774 C  CG   . ASP   A 1 118 ? 8.573   -15.494 5.048   1.00 27.50  ? 115 ASP   A CG   1 
ATOM   1775 O  OD1  . ASP   A 1 118 ? 9.129   -16.577 5.207   1.00 34.35  ? 115 ASP   A OD1  1 
ATOM   1776 O  OD2  . ASP   A 1 118 ? 7.534   -15.344 4.376   1.00 34.68  ? 115 ASP   A OD2  1 
ATOM   1777 H  H    . ASP   A 1 118 ? 8.887   -14.751 8.055   1.00 24.87  ? 115 ASP   A H    1 
ATOM   1778 H  HA   . ASP   A 1 118 ? 10.909  -15.169 6.320   1.00 26.45  ? 115 ASP   A HA   1 
ATOM   1779 H  HB2  . ASP   A 1 118 ? 8.499   -13.705 6.041   1.00 29.53  ? 115 ASP   A HB2  1 
ATOM   1780 H  HB3  . ASP   A 1 118 ? 9.602   -13.731 4.897   1.00 29.53  ? 115 ASP   A HB3  1 
ATOM   1781 N  N    . TYR   A 1 119 ? 10.771  -12.496 7.986   1.00 22.75  ? 116 TYR   A N    1 
ATOM   1782 C  CA   . TYR   A 1 119 ? 11.395  -11.216 8.288   1.00 24.27  ? 116 TYR   A CA   1 
ATOM   1783 C  C    . TYR   A 1 119 ? 11.677  -11.126 9.782   1.00 28.07  ? 116 TYR   A C    1 
ATOM   1784 O  O    . TYR   A 1 119 ? 11.291  -10.152 10.432  1.00 23.34  ? 116 TYR   A O    1 
ATOM   1785 C  CB   . TYR   A 1 119 ? 10.481  -10.068 7.840   1.00 22.57  ? 116 TYR   A CB   1 
ATOM   1786 C  CG   . TYR   A 1 119 ? 10.362  -9.948  6.328   1.00 25.45  ? 116 TYR   A CG   1 
ATOM   1787 C  CD1  . TYR   A 1 119 ? 11.294  -9.211  5.626   1.00 32.44  ? 116 TYR   A CD1  1 
ATOM   1788 C  CD2  . TYR   A 1 119 ? 9.317   -10.538 5.630   1.00 34.76  ? 116 TYR   A CD2  1 
ATOM   1789 C  CE1  . TYR   A 1 119 ? 11.222  -9.063  4.255   1.00 35.52  ? 116 TYR   A CE1  1 
ATOM   1790 C  CE2  . TYR   A 1 119 ? 9.228   -10.398 4.226   1.00 31.73  ? 116 TYR   A CE2  1 
ATOM   1791 C  CZ   . TYR   A 1 119 ? 10.197  -9.660  3.565   1.00 39.22  ? 116 TYR   A CZ   1 
ATOM   1792 O  OH   . TYR   A 1 119 ? 10.162  -9.485  2.191   1.00 47.07  ? 116 TYR   A OH   1 
ATOM   1793 H  H    . TYR   A 1 119 ? 10.179  -12.723 8.567   1.00 27.35  ? 116 TYR   A H    1 
ATOM   1794 H  HA   . TYR   A 1 119 ? 12.238  -11.137 7.814   1.00 29.16  ? 116 TYR   A HA   1 
ATOM   1795 H  HB2  . TYR   A 1 119 ? 9.591   -10.217 8.198   1.00 27.13  ? 116 TYR   A HB2  1 
ATOM   1796 H  HB3  . TYR   A 1 119 ? 10.838  -9.232  8.179   1.00 27.13  ? 116 TYR   A HB3  1 
ATOM   1797 H  HD1  . TYR   A 1 119 ? 11.990  -8.803  6.089   1.00 38.97  ? 116 TYR   A HD1  1 
ATOM   1798 H  HD2  . TYR   A 1 119 ? 8.673   -11.028 6.088   1.00 41.76  ? 116 TYR   A HD2  1 
ATOM   1799 H  HE1  . TYR   A 1 119 ? 11.863  -8.563  3.803   1.00 42.67  ? 116 TYR   A HE1  1 
ATOM   1800 H  HE2  . TYR   A 1 119 ? 8.532   -10.794 3.754   1.00 38.11  ? 116 TYR   A HE2  1 
ATOM   1801 H  HH   . TYR   A 1 119 ? 9.542   -9.944  1.859   1.00 56.52  ? 116 TYR   A HH   1 
ATOM   1802 N  N    . PRO   A 1 120 ? 12.390  -12.096 10.351  1.00 22.89  ? 117 PRO   A N    1 
ATOM   1803 C  CA   . PRO   A 1 120 ? 12.630  -12.043 11.801  1.00 26.07  ? 117 PRO   A CA   1 
ATOM   1804 C  C    . PRO   A 1 120 ? 13.339  -10.780 12.236  1.00 28.69  ? 117 PRO   A C    1 
ATOM   1805 O  O    . PRO   A 1 120 ? 13.187  -10.360 13.393  1.00 27.54  ? 117 PRO   A O    1 
ATOM   1806 C  CB   . PRO   A 1 120 ? 13.470  -13.296 12.067  1.00 26.23  ? 117 PRO   A CB   1 
ATOM   1807 C  CG   . PRO   A 1 120 ? 14.107  -13.630 10.696  1.00 28.53  ? 117 PRO   A CG   1 
ATOM   1808 C  CD   . PRO   A 1 120 ? 13.104  -13.197 9.676   1.00 25.66  ? 117 PRO   A CD   1 
ATOM   1809 H  HA   . PRO   A 1 120 ? 11.792  -12.123 12.282  1.00 31.33  ? 117 PRO   A HA   1 
ATOM   1810 H  HB2  . PRO   A 1 120 ? 14.151  -13.105 12.731  1.00 31.52  ? 117 PRO   A HB2  1 
ATOM   1811 H  HB3  . PRO   A 1 120 ? 12.901  -14.019 12.374  1.00 31.52  ? 117 PRO   A HB3  1 
ATOM   1812 H  HG2  . PRO   A 1 120 ? 14.939  -13.142 10.591  1.00 34.28  ? 117 PRO   A HG2  1 
ATOM   1813 H  HG3  . PRO   A 1 120 ? 14.272  -14.584 10.634  1.00 34.28  ? 117 PRO   A HG3  1 
ATOM   1814 H  HD2  . PRO   A 1 120 ? 13.544  -12.882 8.871   1.00 30.83  ? 117 PRO   A HD2  1 
ATOM   1815 H  HD3  . PRO   A 1 120 ? 12.496  -13.921 9.461   1.00 30.83  ? 117 PRO   A HD3  1 
ATOM   1816 N  N    . GLU   A 1 121 ? 14.144  -10.169 11.354  1.00 26.41  ? 118 GLU   A N    1 
ATOM   1817 C  CA   . GLU   A 1 121 ? 14.887  -8.968  11.697  1.00 29.15  ? 118 GLU   A CA   1 
ATOM   1818 C  C    . GLU   A 1 121 ? 13.996  -7.783  12.053  1.00 27.89  ? 118 GLU   A C    1 
ATOM   1819 O  O    . GLU   A 1 121 ? 14.486  -6.847  12.696  1.00 30.65  ? 118 GLU   A O    1 
ATOM   1820 C  CB   . GLU   A 1 121 ? 15.818  -8.602  10.528  1.00 30.00  ? 118 GLU   A CB   1 
ATOM   1821 C  CG   . GLU   A 1 121 ? 15.105  -8.102  9.267   1.00 31.45  ? 118 GLU   A CG   1 
ATOM   1822 C  CD   . GLU   A 1 121 ? 14.698  -9.225  8.307   1.00 30.37  ? 118 GLU   A CD   1 
ATOM   1823 O  OE1  . GLU   A 1 121 ? 14.709  -10.429 8.706   1.00 32.64  ? 118 GLU   A OE1  1 
ATOM   1824 O  OE2  . GLU   A 1 121 ? 14.398  -8.912  7.130   1.00 41.49  ? 118 GLU   A OE2  1 
ATOM   1825 H  H    . GLU   A 1 121 ? 14.273  -10.438 10.548  1.00 31.73  ? 118 GLU   A H    1 
ATOM   1826 H  HA   . GLU   A 1 121 ? 15.425  -9.152  12.482  1.00 35.03  ? 118 GLU   A HA   1 
ATOM   1827 H  HB2  . GLU   A 1 121 ? 16.417  -7.898  10.822  1.00 36.04  ? 118 GLU   A HB2  1 
ATOM   1828 H  HB3  . GLU   A 1 121 ? 16.327  -9.390  10.282  1.00 36.04  ? 118 GLU   A HB3  1 
ATOM   1829 H  HG2  . GLU   A 1 121 ? 14.300  -7.629  9.529   1.00 37.78  ? 118 GLU   A HG2  1 
ATOM   1830 H  HG3  . GLU   A 1 121 ? 15.700  -7.504  8.787   1.00 37.78  ? 118 GLU   A HG3  1 
ATOM   1831 N  N    . VAL   A 1 122 ? 12.718  -7.782  11.654  1.00 24.05  ? 119 VAL   A N    1 
ATOM   1832 C  CA   . VAL   A 1 122 ? 11.838  -6.676  12.017  1.00 25.64  ? 119 VAL   A CA   1 
ATOM   1833 C  C    . VAL   A 1 122 ? 11.118  -6.909  13.350  1.00 26.68  ? 119 VAL   A C    1 
ATOM   1834 O  O    . VAL   A 1 122 ? 10.423  -6.005  13.822  1.00 24.93  ? 119 VAL   A O    1 
ATOM   1835 C  CB   . VAL   A 1 122 ? 10.756  -6.320  10.962  1.00 27.71  ? 119 VAL   A CB   1 
ATOM   1836 C  CG1  . VAL   A 1 122 ? 11.377  -6.148  9.553   1.00 27.11  ? 119 VAL   A CG1  1 
ATOM   1837 C  CG2  . VAL   A 1 122 ? 9.631   -7.326  10.943  1.00 22.36  ? 119 VAL   A CG2  1 
ATOM   1838 H  H    . VAL   A 1 122 ? 12.349  -8.399  11.183  1.00 28.90  ? 119 VAL   A H    1 
ATOM   1839 H  HA   . VAL   A 1 122 ? 12.437  -5.916  12.076  1.00 30.82  ? 119 VAL   A HA   1 
ATOM   1840 H  HB   . VAL   A 1 122 ? 10.369  -5.468  11.220  1.00 33.30  ? 119 VAL   A HB   1 
ATOM   1841 H  HG11 . VAL   A 1 122 ? 10.698  -5.815  8.946   1.00 32.58  ? 119 VAL   A HG11 1 
ATOM   1842 H  HG12 . VAL   A 1 122 ? 12.111  -5.516  9.606   1.00 32.58  ? 119 VAL   A HG12 1 
ATOM   1843 H  HG13 . VAL   A 1 122 ? 11.703  -7.008  9.244   1.00 32.58  ? 119 VAL   A HG13 1 
ATOM   1844 H  HG21 . VAL   A 1 122 ? 9.138   -7.233  10.113  1.00 26.87  ? 119 VAL   A HG21 1 
ATOM   1845 H  HG22 . VAL   A 1 122 ? 10.005  -8.219  11.007  1.00 26.87  ? 119 VAL   A HG22 1 
ATOM   1846 H  HG23 . VAL   A 1 122 ? 9.045   -7.159  11.697  1.00 26.87  ? 119 VAL   A HG23 1 
ATOM   1847 N  N    . VAL   A 1 123 ? 11.281  -8.074  13.981  1.00 20.88  ? 120 VAL   A N    1 
ATOM   1848 C  CA   . VAL   A 1 123 ? 10.477  -8.458  15.149  1.00 20.65  ? 120 VAL   A CA   1 
ATOM   1849 C  C    . VAL   A 1 123 ? 11.313  -8.330  16.428  1.00 23.23  ? 120 VAL   A C    1 
ATOM   1850 O  O    . VAL   A 1 123 ? 12.311  -9.035  16.597  1.00 27.34  ? 120 VAL   A O    1 
ATOM   1851 C  CB   . VAL   A 1 123 ? 9.920   -9.883  15.015  1.00 20.18  ? 120 VAL   A CB   1 
ATOM   1852 C  CG1  . VAL   A 1 123 ? 9.059   -10.228 16.232  1.00 23.84  ? 120 VAL   A CG1  1 
ATOM   1853 C  CG2  . VAL   A 1 123 ? 9.149   -10.016 13.730  1.00 20.85  ? 120 VAL   A CG2  1 
ATOM   1854 H  H    . VAL   A 1 123 ? 11.859  -8.667  13.750  1.00 25.09  ? 120 VAL   A H    1 
ATOM   1855 H  HA   . VAL   A 1 123 ? 9.741   -7.829  15.216  1.00 24.82  ? 120 VAL   A HA   1 
ATOM   1856 H  HB   . VAL   A 1 123 ? 10.650  -10.521 14.986  1.00 24.26  ? 120 VAL   A HB   1 
ATOM   1857 H  HG11 . VAL   A 1 123 ? 8.651   -11.097 16.095  1.00 28.65  ? 120 VAL   A HG11 1 
ATOM   1858 H  HG12 . VAL   A 1 123 ? 9.622   -10.247 17.022  1.00 28.65  ? 120 VAL   A HG12 1 
ATOM   1859 H  HG13 . VAL   A 1 123 ? 8.370   -9.552  16.334  1.00 28.65  ? 120 VAL   A HG13 1 
ATOM   1860 H  HG21 . VAL   A 1 123 ? 8.675   -10.863 13.732  1.00 25.06  ? 120 VAL   A HG21 1 
ATOM   1861 H  HG22 . VAL   A 1 123 ? 8.516   -9.284  13.663  1.00 25.06  ? 120 VAL   A HG22 1 
ATOM   1862 H  HG23 . VAL   A 1 123 ? 9.769   -9.986  12.985  1.00 25.06  ? 120 VAL   A HG23 1 
ATOM   1863 N  N    . LYS   A 1 124 ? 10.898  -7.430  17.325  1.00 23.18  ? 121 LYS   A N    1 
ATOM   1864 C  CA   . LYS   A 1 124 ? 11.459  -7.365  18.663  1.00 21.49  ? 121 LYS   A CA   1 
ATOM   1865 C  C    . LYS   A 1 124 ? 10.780  -8.388  19.559  1.00 25.35  ? 121 LYS   A C    1 
ATOM   1866 O  O    . LYS   A 1 124 ? 11.432  -9.229  20.189  1.00 26.63  ? 121 LYS   A O    1 
ATOM   1867 C  CB   . LYS   A 1 124 ? 11.292  -5.958  19.246  1.00 25.92  ? 121 LYS   A CB   1 
ATOM   1868 C  CG   . LYS   A 1 124 ? 11.790  -5.789  20.729  1.00 31.52  ? 121 LYS   A CG   1 
ATOM   1869 C  CD   . LYS   A 1 124 ? 12.336  -4.406  20.988  1.00 37.92  ? 121 LYS   A CD   1 
ATOM   1870 C  CE   . LYS   A 1 124 ? 12.986  -4.259  22.375  1.00 43.66  ? 121 LYS   A CE   1 
ATOM   1871 N  NZ   . LYS   A 1 124 ? 12.474  -3.050  23.099  1.00 53.78  ? 121 LYS   A NZ   1 
ATOM   1872 H  H    . LYS   A 1 124 ? 10.287  -6.844  17.177  1.00 27.86  ? 121 LYS   A H    1 
ATOM   1873 H  HA   . LYS   A 1 124 ? 12.409  -7.553  18.620  1.00 25.83  ? 121 LYS   A HA   1 
ATOM   1874 H  HB2  . LYS   A 1 124 ? 11.796  -5.336  18.698  1.00 31.15  ? 121 LYS   A HB2  1 
ATOM   1875 H  HB3  . LYS   A 1 124 ? 10.350  -5.728  19.228  1.00 31.15  ? 121 LYS   A HB3  1 
ATOM   1876 H  HG2  . LYS   A 1 124 ? 11.048  -5.940  21.335  1.00 37.87  ? 121 LYS   A HG2  1 
ATOM   1877 H  HG3  . LYS   A 1 124 ? 12.497  -6.431  20.903  1.00 37.87  ? 121 LYS   A HG3  1 
ATOM   1878 H  HD2  . LYS   A 1 124 ? 13.010  -4.203  20.320  1.00 45.55  ? 121 LYS   A HD2  1 
ATOM   1879 H  HD3  . LYS   A 1 124 ? 11.610  -3.765  20.930  1.00 45.55  ? 121 LYS   A HD3  1 
ATOM   1880 H  HE2  . LYS   A 1 124 ? 12.784  -5.042  22.909  1.00 52.44  ? 121 LYS   A HE2  1 
ATOM   1881 H  HE3  . LYS   A 1 124 ? 13.946  -4.167  22.271  1.00 52.44  ? 121 LYS   A HE3  1 
ATOM   1882 H  HZ1  . LYS   A 1 124 ? 12.853  -2.993  23.902  1.00 64.58  ? 121 LYS   A HZ1  1 
ATOM   1883 H  HZ2  . LYS   A 1 124 ? 12.665  -2.315  22.636  1.00 64.58  ? 121 LYS   A HZ2  1 
ATOM   1884 H  HZ3  . LYS   A 1 124 ? 11.591  -3.107  23.199  1.00 64.58  ? 121 LYS   A HZ3  1 
ATOM   1885 N  N    . LYS   A 1 125 ? 9.468   -8.291  19.651  1.00 22.84  ? 122 LYS   A N    1 
ATOM   1886 C  CA   . LYS   A 1 125 ? 8.618   -9.222  20.370  1.00 21.26  ? 122 LYS   A CA   1 
ATOM   1887 C  C    . LYS   A 1 125 ? 7.343   -9.409  19.569  1.00 19.95  ? 122 LYS   A C    1 
ATOM   1888 O  O    . LYS   A 1 125 ? 6.922   -8.500  18.842  1.00 21.66  ? 122 LYS   A O    1 
ATOM   1889 C  CB   . LYS   A 1 125 ? 8.236   -8.697  21.756  1.00 24.47  ? 122 LYS   A CB   1 
ATOM   1890 C  CG   . LYS   A 1 125 ? 9.377   -8.520  22.726  1.00 29.00  ? 122 LYS   A CG   1 
ATOM   1891 C  CD   . LYS   A 1 125 ? 9.845   -9.859  23.181  1.00 27.78  ? 122 LYS   A CD   1 
ATOM   1892 C  CE   . LYS   A 1 125 ? 10.583  -9.809  24.527  1.00 37.28  ? 122 LYS   A CE   1 
ATOM   1893 N  NZ   . LYS   A 1 125 ? 11.514  -10.957 24.620  1.00 38.42  ? 122 LYS   A NZ   1 
ATOM   1894 H  H    . LYS   A 1 125 ? 9.018   -7.657  19.283  1.00 27.44  ? 122 LYS   A H    1 
ATOM   1895 H  HA   . LYS   A 1 125 ? 9.081   -10.068 20.474  1.00 25.55  ? 122 LYS   A HA   1 
ATOM   1896 H  HB2  . LYS   A 1 125 ? 7.814   -7.831  21.647  1.00 29.41  ? 122 LYS   A HB2  1 
ATOM   1897 H  HB3  . LYS   A 1 125 ? 7.612   -9.322  22.156  1.00 29.41  ? 122 LYS   A HB3  1 
ATOM   1898 H  HG2  . LYS   A 1 125 ? 10.112  -8.061  22.291  1.00 34.84  ? 122 LYS   A HG2  1 
ATOM   1899 H  HG3  . LYS   A 1 125 ? 9.078   -8.013  23.497  1.00 34.84  ? 122 LYS   A HG3  1 
ATOM   1900 H  HD2  . LYS   A 1 125 ? 9.078   -10.444 23.282  1.00 33.38  ? 122 LYS   A HD2  1 
ATOM   1901 H  HD3  . LYS   A 1 125 ? 10.454  -10.222 22.519  1.00 33.38  ? 122 LYS   A HD3  1 
ATOM   1902 H  HE2  . LYS   A 1 125 ? 11.092  -8.985  24.593  1.00 44.78  ? 122 LYS   A HE2  1 
ATOM   1903 H  HE3  . LYS   A 1 125 ? 9.944   -9.863  25.255  1.00 44.78  ? 122 LYS   A HE3  1 
ATOM   1904 H  HZ1  . LYS   A 1 125 ? 11.879  -10.988 25.431  1.00 46.14  ? 122 LYS   A HZ1  1 
ATOM   1905 H  HZ2  . LYS   A 1 125 ? 11.075  -11.717 24.472  1.00 46.14  ? 122 LYS   A HZ2  1 
ATOM   1906 H  HZ3  . LYS   A 1 125 ? 12.161  -10.874 24.014  1.00 46.14  ? 122 LYS   A HZ3  1 
ATOM   1907 N  N    . ILE   A 1 126 ? 6.700   -10.553 19.745  1.00 19.62  ? 123 ILE   A N    1 
ATOM   1908 C  CA   . ILE   A 1 126 ? 5.500   -10.881 18.995  1.00 18.42  ? 123 ILE   A CA   1 
ATOM   1909 C  C    . ILE   A 1 126 ? 4.566   -11.699 19.875  1.00 18.47  ? 123 ILE   A C    1 
ATOM   1910 O  O    . ILE   A 1 126 ? 4.995   -12.507 20.698  1.00 20.21  ? 123 ILE   A O    1 
ATOM   1911 C  CB   . ILE   A 1 126 ? 5.895   -11.575 17.663  1.00 18.09  ? 123 ILE   A CB   1 
ATOM   1912 C  CG1  . ILE   A 1 126 ? 4.742   -11.640 16.661  1.00 19.08  ? 123 ILE   A CG1  1 
ATOM   1913 C  CG2  . ILE   A 1 126 ? 6.448   -12.975 17.913  1.00 21.10  ? 123 ILE   A CG2  1 
ATOM   1914 C  CD1  . ILE   A 1 126 ? 5.300   -11.806 15.213  1.00 19.99  ? 123 ILE   A CD1  1 
ATOM   1915 H  H    . ILE   A 1 126 ? 6.942   -11.164 20.300  1.00 23.59  ? 123 ILE   A H    1 
ATOM   1916 H  HA   . ILE   A 1 126 ? 4.993   -10.084 18.776  1.00 22.14  ? 123 ILE   A HA   1 
ATOM   1917 H  HB   . ILE   A 1 126 ? 6.587   -11.020 17.271  1.00 21.75  ? 123 ILE   A HB   1 
ATOM   1918 H  HG12 . ILE   A 1 126 ? 4.175   -12.401 16.865  1.00 22.93  ? 123 ILE   A HG12 1 
ATOM   1919 H  HG13 . ILE   A 1 126 ? 4.225   -10.821 16.704  1.00 22.93  ? 123 ILE   A HG13 1 
ATOM   1920 H  HG21 . ILE   A 1 126 ? 6.824   -13.319 17.087  1.00 25.36  ? 123 ILE   A HG21 1 
ATOM   1921 H  HG22 . ILE   A 1 126 ? 7.137   -12.926 18.594  1.00 25.36  ? 123 ILE   A HG22 1 
ATOM   1922 H  HG23 . ILE   A 1 126 ? 5.727   -13.551 18.213  1.00 25.36  ? 123 ILE   A HG23 1 
ATOM   1923 H  HD11 . ILE   A 1 126 ? 4.585   -11.641 14.578  1.00 24.03  ? 123 ILE   A HD11 1 
ATOM   1924 H  HD12 . ILE   A 1 126 ? 6.017   -11.167 15.076  1.00 24.03  ? 123 ILE   A HD12 1 
ATOM   1925 H  HD13 . ILE   A 1 126 ? 5.636   -12.709 15.105  1.00 24.03  ? 123 ILE   A HD13 1 
ATOM   1926 N  N    . ALA   A 1 127 ? 3.258   -11.514 19.650  1.00 17.39  ? 124 ALA   A N    1 
ATOM   1927 C  CA   . ALA   A 1 127 ? 2.229   -12.248 20.367  1.00 18.56  ? 124 ALA   A CA   1 
ATOM   1928 C  C    . ALA   A 1 127 ? 1.223   -12.814 19.384  1.00 17.15  ? 124 ALA   A C    1 
ATOM   1929 O  O    . ALA   A 1 127 ? 0.820   -12.142 18.414  1.00 18.31  ? 124 ALA   A O    1 
ATOM   1930 C  CB   . ALA   A 1 127 ? 1.524   -11.359 21.384  1.00 21.13  ? 124 ALA   A CB   1 
ATOM   1931 H  H    . ALA   A 1 127 ? 2.945   -10.957 19.075  1.00 20.91  ? 124 ALA   A H    1 
ATOM   1932 H  HA   . ALA   A 1 127 ? 2.633   -12.992 20.842  1.00 22.32  ? 124 ALA   A HA   1 
ATOM   1933 H  HB1  . ALA   A 1 127 ? 0.857   -11.885 21.854  1.00 25.40  ? 124 ALA   A HB1  1 
ATOM   1934 H  HB2  . ALA   A 1 127 ? 2.179   -11.018 22.013  1.00 25.40  ? 124 ALA   A HB2  1 
ATOM   1935 H  HB3  . ALA   A 1 127 ? 1.097   -10.623 20.918  1.00 25.40  ? 124 ALA   A HB3  1 
ATOM   1936 N  N    . PHE   A 1 128 ? 0.870   -14.062 19.605  1.00 18.41  ? 125 PHE   A N    1 
ATOM   1937 C  CA   . PHE   A 1 128 ? -0.074  -14.804 18.779  1.00 17.37  ? 125 PHE   A CA   1 
ATOM   1938 C  C    . PHE   A 1 128 ? -1.330  -15.010 19.644  1.00 19.08  ? 125 PHE   A C    1 
ATOM   1939 O  O    . PHE   A 1 128 ? -1.356  -15.836 20.568  1.00 19.73  ? 125 PHE   A O    1 
ATOM   1940 C  CB   . PHE   A 1 128 ? 0.476   -16.156 18.299  1.00 17.56  ? 125 PHE   A CB   1 
ATOM   1941 C  CG   . PHE   A 1 128 ? 1.805   -16.101 17.571  1.00 18.26  ? 125 PHE   A CG   1 
ATOM   1942 C  CD1  . PHE   A 1 128 ? 2.101   -15.105 16.645  1.00 18.29  ? 125 PHE   A CD1  1 
ATOM   1943 C  CD2  . PHE   A 1 128 ? 2.753   -17.079 17.803  1.00 19.64  ? 125 PHE   A CD2  1 
ATOM   1944 C  CE1  . PHE   A 1 128 ? 3.300   -15.089 15.988  1.00 18.72  ? 125 PHE   A CE1  1 
ATOM   1945 C  CE2  . PHE   A 1 128 ? 3.978   -17.056 17.119  1.00 21.09  ? 125 PHE   A CE2  1 
ATOM   1946 C  CZ   . PHE   A 1 128 ? 4.237   -16.041 16.224  1.00 19.65  ? 125 PHE   A CZ   1 
ATOM   1947 H  H    . PHE   A 1 128 ? 1.177   -14.529 20.259  1.00 22.14  ? 125 PHE   A H    1 
ATOM   1948 H  HA   . PHE   A 1 128 ? -0.274  -14.280 17.987  1.00 20.89  ? 125 PHE   A HA   1 
ATOM   1949 H  HB2  . PHE   A 1 128 ? 0.595   -16.729 19.073  1.00 21.12  ? 125 PHE   A HB2  1 
ATOM   1950 H  HB3  . PHE   A 1 128 ? -0.169  -16.550 17.692  1.00 21.12  ? 125 PHE   A HB3  1 
ATOM   1951 H  HD1  . PHE   A 1 128 ? 1.475   -14.440 16.471  1.00 21.99  ? 125 PHE   A HD1  1 
ATOM   1952 H  HD2  . PHE   A 1 128 ? 2.579   -17.756 18.416  1.00 23.61  ? 125 PHE   A HD2  1 
ATOM   1953 H  HE1  . PHE   A 1 128 ? 3.475   -14.417 15.369  1.00 22.50  ? 125 PHE   A HE1  1 
ATOM   1954 H  HE2  . PHE   A 1 128 ? 4.611   -17.722 17.268  1.00 25.35  ? 125 PHE   A HE2  1 
ATOM   1955 H  HZ   . PHE   A 1 128 ? 5.054   -16.008 15.783  1.00 23.62  ? 125 PHE   A HZ   1 
ATOM   1956 N  N    . HIS   A 1 129 ? -2.365  -14.244 19.357  1.00 17.02  ? 126 HIS   A N    1 
ATOM   1957 C  CA   . HIS   A 1 129 ? -3.637  -14.313 20.086  1.00 16.24  ? 126 HIS   A CA   1 
ATOM   1958 C  C    . HIS   A 1 129 ? -4.563  -15.272 19.352  1.00 19.77  ? 126 HIS   A C    1 
ATOM   1959 O  O    . HIS   A 1 129 ? -4.962  -15.017 18.207  1.00 20.58  ? 126 HIS   A O    1 
ATOM   1960 C  CB   . HIS   A 1 129 ? -4.239  -12.913 20.192  1.00 17.61  ? 126 HIS   A CB   1 
ATOM   1961 C  CG   . HIS   A 1 129 ? -5.504  -12.858 20.976  1.00 18.91  ? 126 HIS   A CG   1 
ATOM   1962 N  ND1  . HIS   A 1 129 ? -6.742  -12.831 20.374  1.00 23.05  ? 126 HIS   A ND1  1 
ATOM   1963 C  CD2  . HIS   A 1 129 ? -5.728  -12.828 22.312  1.00 21.62  ? 126 HIS   A CD2  1 
ATOM   1964 C  CE1  . HIS   A 1 129 ? -7.675  -12.787 21.308  1.00 23.91  ? 126 HIS   A CE1  1 
ATOM   1965 N  NE2  . HIS   A 1 129 ? -7.089  -12.771 22.493  1.00 25.66  ? 126 HIS   A NE2  1 
ATOM   1966 H  H    . HIS   A 1 129 ? -2.364  -13.657 18.728  1.00 20.47  ? 126 HIS   A H    1 
ATOM   1967 H  HA   . HIS   A 1 129 ? -3.499  -14.661 20.981  1.00 19.52  ? 126 HIS   A HA   1 
ATOM   1968 H  HB2  . HIS   A 1 129 ? -3.596  -12.330 20.626  1.00 21.18  ? 126 HIS   A HB2  1 
ATOM   1969 H  HB3  . HIS   A 1 129 ? -4.430  -12.588 19.298  1.00 21.18  ? 126 HIS   A HB3  1 
ATOM   1970 H  HD2  . HIS   A 1 129 ? -5.082  -12.844 22.980  1.00 25.99  ? 126 HIS   A HD2  1 
ATOM   1971 H  HE1  . HIS   A 1 129 ? -8.593  -12.771 21.156  1.00 28.73  ? 126 HIS   A HE1  1 
ATOM   1972 H  HE2  . HIS   A 1 129 ? -7.493  -12.730 23.251  1.00 30.83  ? 126 HIS   A HE2  1 
ATOM   1973 N  N    . GLU   A 1 130 ? -4.845  -16.401 19.981  1.00 21.40  ? 127 GLU   A N    1 
ATOM   1974 C  CA   . GLU   A 1 130 ? -5.834  -17.387 19.538  1.00 20.36  ? 127 GLU   A CA   1 
ATOM   1975 C  C    . GLU   A 1 130 ? -5.683  -17.737 18.067  1.00 19.03  ? 127 GLU   A C    1 
ATOM   1976 O  O    . GLU   A 1 130 ? -6.559  -17.441 17.234  1.00 20.14  ? 127 GLU   A O    1 
ATOM   1977 C  CB   . GLU   A 1 130 ? -7.244  -16.877 19.875  1.00 23.00  ? 127 GLU   A CB   1 
ATOM   1978 C  CG   . GLU   A 1 130 ? -7.389  -16.675 21.401  1.00 27.96  ? 127 GLU   A CG   1 
ATOM   1979 C  CD   . GLU   A 1 130 ? -8.769  -16.938 21.958  1.00 27.63  ? 127 GLU   A CD   1 
ATOM   1980 O  OE1  . GLU   A 1 130 ? -9.733  -17.008 21.184  1.00 27.55  ? 127 GLU   A OE1  1 
ATOM   1981 O  OE2  . GLU   A 1 130 ? -8.907  -17.034 23.186  1.00 26.41  ? 127 GLU   A OE2  1 
ATOM   1982 H  H    . GLU   A 1 130 ? -4.457  -16.640 20.711  1.00 25.73  ? 127 GLU   A H    1 
ATOM   1983 H  HA   . GLU   A 1 130 ? -5.685  -18.223 20.007  1.00 24.48  ? 127 GLU   A HA   1 
ATOM   1984 H  HB2  . GLU   A 1 130 ? -7.397  -16.027 19.433  1.00 27.64  ? 127 GLU   A HB2  1 
ATOM   1985 H  HB3  . GLU   A 1 130 ? -7.903  -17.526 19.583  1.00 27.64  ? 127 GLU   A HB3  1 
ATOM   1986 H  HG2  . GLU   A 1 130 ? -6.776  -17.280 21.850  1.00 33.60  ? 127 GLU   A HG2  1 
ATOM   1987 H  HG3  . GLU   A 1 130 ? -7.161  -15.756 21.612  1.00 33.60  ? 127 GLU   A HG3  1 
ATOM   1988 N  N    . PRO   A 1 131 ? -4.587  -18.414 17.734  1.00 18.33  ? 128 PRO   A N    1 
ATOM   1989 C  CA   . PRO   A 1 131 ? -4.303  -18.773 16.329  1.00 19.22  ? 128 PRO   A CA   1 
ATOM   1990 C  C    . PRO   A 1 131 ? -5.092  -20.001 15.905  1.00 20.95  ? 128 PRO   A C    1 
ATOM   1991 O  O    . PRO   A 1 131 ? -5.222  -20.956 16.691  1.00 21.68  ? 128 PRO   A O    1 
ATOM   1992 C  CB   . PRO   A 1 131 ? -2.790  -19.046 16.344  1.00 23.68  ? 128 PRO   A CB   1 
ATOM   1993 C  CG   . PRO   A 1 131 ? -2.494  -19.519 17.771  1.00 25.38  ? 128 PRO   A CG   1 
ATOM   1994 C  CD   . PRO   A 1 131 ? -3.465  -18.745 18.654  1.00 22.44  ? 128 PRO   A CD   1 
ATOM   1995 H  HA   . PRO   A 1 131 ? -4.502  -18.038 15.729  1.00 23.11  ? 128 PRO   A HA   1 
ATOM   1996 H  HB2  . PRO   A 1 131 ? -2.572  -19.735 15.697  1.00 28.46  ? 128 PRO   A HB2  1 
ATOM   1997 H  HB3  . PRO   A 1 131 ? -2.304  -18.232 16.138  1.00 28.46  ? 128 PRO   A HB3  1 
ATOM   1998 H  HG2  . PRO   A 1 131 ? -2.647  -20.474 17.842  1.00 30.50  ? 128 PRO   A HG2  1 
ATOM   1999 H  HG3  . PRO   A 1 131 ? -1.575  -19.312 18.004  1.00 30.50  ? 128 PRO   A HG3  1 
ATOM   2000 H  HD2  . PRO   A 1 131 ? -3.775  -19.296 19.389  1.00 26.97  ? 128 PRO   A HD2  1 
ATOM   2001 H  HD3  . PRO   A 1 131 ? -3.051  -17.937 18.995  1.00 26.97  ? 128 PRO   A HD3  1 
ATOM   2002 N  N    . PRO   A 1 132 ? -5.643  -20.003 14.690  1.00 17.86  ? 129 PRO   A N    1 
ATOM   2003 C  CA   . PRO   A 1 132 ? -6.420  -21.159 14.222  1.00 18.37  ? 129 PRO   A CA   1 
ATOM   2004 C  C    . PRO   A 1 132 ? -5.660  -22.012 13.211  1.00 19.51  ? 129 PRO   A C    1 
ATOM   2005 O  O    . PRO   A 1 132 ? -6.274  -22.807 12.501  1.00 21.14  ? 129 PRO   A O    1 
ATOM   2006 C  CB   . PRO   A 1 132 ? -7.645  -20.499 13.588  1.00 23.12  ? 129 PRO   A CB   1 
ATOM   2007 C  CG   . PRO   A 1 132 ? -7.070  -19.235 12.955  1.00 22.02  ? 129 PRO   A CG   1 
ATOM   2008 C  CD   . PRO   A 1 132 ? -5.966  -18.793 13.902  1.00 21.13  ? 129 PRO   A CD   1 
ATOM   2009 H  HA   . PRO   A 1 132 ? -6.690  -21.716 14.969  1.00 22.08  ? 129 PRO   A HA   1 
ATOM   2010 H  HB2  . PRO   A 1 132 ? -8.035  -21.084 12.920  1.00 27.79  ? 129 PRO   A HB2  1 
ATOM   2011 H  HB3  . PRO   A 1 132 ? -8.304  -20.286 14.268  1.00 27.79  ? 129 PRO   A HB3  1 
ATOM   2012 H  HG2  . PRO   A 1 132 ? -6.713  -19.438 12.076  1.00 26.47  ? 129 PRO   A HG2  1 
ATOM   2013 H  HG3  . PRO   A 1 132 ? -7.759  -18.557 12.884  1.00 26.47  ? 129 PRO   A HG3  1 
ATOM   2014 H  HD2  . PRO   A 1 132 ? -5.189  -18.494 13.404  1.00 25.40  ? 129 PRO   A HD2  1 
ATOM   2015 H  HD3  . PRO   A 1 132 ? -6.280  -18.083 14.483  1.00 25.40  ? 129 PRO   A HD3  1 
ATOM   2016 N  N    . ILE   A 1 133 ? -4.353  -21.838 13.129  1.00 17.28  ? 130 ILE   A N    1 
ATOM   2017 C  CA   . ILE   A 1 133 ? -3.542  -22.654 12.236  1.00 18.13  ? 130 ILE   A CA   1 
ATOM   2018 C  C    . ILE   A 1 133 ? -3.531  -24.110 12.708  1.00 17.83  ? 130 ILE   A C    1 
ATOM   2019 O  O    . ILE   A 1 133 ? -3.504  -24.414 13.907  1.00 19.97  ? 130 ILE   A O    1 
ATOM   2020 C  CB   . ILE   A 1 133 ? -2.127  -22.065 12.148  1.00 21.26  ? 130 ILE   A CB   1 
ATOM   2021 C  CG1  . ILE   A 1 133 ? -1.327  -22.798 11.073  1.00 22.88  ? 130 ILE   A CG1  1 
ATOM   2022 C  CG2  . ILE   A 1 133 ? -1.423  -22.062 13.522  1.00 19.75  ? 130 ILE   A CG2  1 
ATOM   2023 C  CD1  . ILE   A 1 133 ? -0.162  -22.008 10.572  1.00 22.08  ? 130 ILE   A CD1  1 
ATOM   2024 H  H    . ILE   A 1 133 ? -3.908  -21.256 13.578  1.00 20.78  ? 130 ILE   A H    1 
ATOM   2025 H  HA   . ILE   A 1 133 ? -3.934  -22.647 11.349  1.00 21.80  ? 130 ILE   A HA   1 
ATOM   2026 H  HB   . ILE   A 1 133 ? -2.193  -21.134 11.884  1.00 25.56  ? 130 ILE   A HB   1 
ATOM   2027 H  HG12 . ILE   A 1 133 ? -0.989  -23.629 11.443  1.00 27.49  ? 130 ILE   A HG12 1 
ATOM   2028 H  HG13 . ILE   A 1 133 ? -1.909  -22.984 10.319  1.00 27.49  ? 130 ILE   A HG13 1 
ATOM   2029 H  HG21 . ILE   A 1 133 ? -0.597  -21.558 13.452  1.00 23.74  ? 130 ILE   A HG21 1 
ATOM   2030 H  HG22 . ILE   A 1 133 ? -2.008  -21.649 14.176  1.00 23.74  ? 130 ILE   A HG22 1 
ATOM   2031 H  HG23 . ILE   A 1 133 ? -1.231  -22.977 13.781  1.00 23.74  ? 130 ILE   A HG23 1 
ATOM   2032 H  HD11 . ILE   A 1 133 ? 0.212   -22.453 9.795   1.00 26.54  ? 130 ILE   A HD11 1 
ATOM   2033 H  HD12 . ILE   A 1 133 ? -0.464  -21.118 10.330  1.00 26.54  ? 130 ILE   A HD12 1 
ATOM   2034 H  HD13 . ILE   A 1 133 ? 0.506   -21.951 11.273  1.00 26.54  ? 130 ILE   A HD13 1 
ATOM   2035 N  N    . ASN   A 1 134 ? -3.558  -25.030 11.747  1.00 16.72  ? 131 ASN   A N    1 
ATOM   2036 C  CA   . ASN   A 1 134 ? -3.602  -26.447 12.049  1.00 18.22  ? 131 ASN   A CA   1 
ATOM   2037 C  C    . ASN   A 1 134 ? -2.423  -27.242 11.500  1.00 18.98  ? 131 ASN   A C    1 
ATOM   2038 O  O    . ASN   A 1 134 ? -2.299  -28.430 11.835  1.00 18.91  ? 131 ASN   A O    1 
ATOM   2039 C  CB   . ASN   A 1 134 ? -4.933  -27.048 11.538  1.00 17.44  ? 131 ASN   A CB   1 
ATOM   2040 C  CG   . ASN   A 1 134 ? -5.029  -27.098 10.032  1.00 19.18  ? 131 ASN   A CG   1 
ATOM   2041 O  OD1  . ASN   A 1 134 ? -4.137  -27.663 9.358   1.00 20.68  ? 131 ASN   A OD1  1 
ATOM   2042 N  ND2  . ASN   A 1 134 ? -6.100  -26.517 9.469   1.00 19.32  ? 131 ASN   A ND2  1 
ATOM   2043 H  H    . ASN   A 1 134 ? -3.552  -24.851 10.905  1.00 20.10  ? 131 ASN   A H    1 
ATOM   2044 H  HA   . ASN   A 1 134 ? -3.578  -26.564 13.012  1.00 21.91  ? 131 ASN   A HA   1 
ATOM   2045 H  HB2  . ASN   A 1 134 ? -5.016  -27.956 11.871  1.00 20.97  ? 131 ASN   A HB2  1 
ATOM   2046 H  HB3  . ASN   A 1 134 ? -5.668  -26.506 11.865  1.00 20.97  ? 131 ASN   A HB3  1 
ATOM   2047 H  HD21 . ASN   A 1 134 ? -6.193  -26.523 8.614   1.00 23.23  ? 131 ASN   A HD21 1 
ATOM   2048 H  HD22 . ASN   A 1 134 ? -6.694  -26.139 9.963   1.00 23.23  ? 131 ASN   A HD22 1 
ATOM   2049 N  N    . THR   A 1 135 ? -1.525  -26.622 10.715  1.00 18.09  ? 132 THR   A N    1 
ATOM   2050 C  CA   . THR   A 1 135 ? -0.627  -27.422 9.880   1.00 17.81  ? 132 THR   A CA   1 
ATOM   2051 C  C    . THR   A 1 135 ? 0.271   -28.359 10.685  1.00 19.36  ? 132 THR   A C    1 
ATOM   2052 O  O    . THR   A 1 135 ? 0.542   -29.484 10.254  1.00 21.97  ? 132 THR   A O    1 
ATOM   2053 C  CB   . THR   A 1 135 ? 0.245   -26.490 9.046   1.00 19.95  ? 132 THR   A CB   1 
ATOM   2054 O  OG1  . THR   A 1 135 ? -0.568  -25.434 8.562   1.00 19.97  ? 132 THR   A OG1  1 
ATOM   2055 C  CG2  . THR   A 1 135 ? 0.901   -27.234 7.895   1.00 21.71  ? 132 THR   A CG2  1 
ATOM   2056 H  H    . THR   A 1 135 ? -1.422  -25.770 10.652  1.00 21.75  ? 132 THR   A H    1 
ATOM   2057 H  HA   . THR   A 1 135 ? -1.179  -27.975 9.305   1.00 21.41  ? 132 THR   A HA   1 
ATOM   2058 H  HB   . THR   A 1 135 ? 0.965   -26.127 9.587   1.00 23.98  ? 132 THR   A HB   1 
ATOM   2059 H  HG1  . THR   A 1 135 ? -0.089  -24.836 8.218   1.00 24.00  ? 132 THR   A HG1  1 
ATOM   2060 H  HG21 . THR   A 1 135 ? 1.374   -26.609 7.323   1.00 26.10  ? 132 THR   A HG21 1 
ATOM   2061 H  HG22 . THR   A 1 135 ? 1.532   -27.886 8.238   1.00 26.10  ? 132 THR   A HG22 1 
ATOM   2062 H  HG23 . THR   A 1 135 ? 0.227   -27.693 7.370   1.00 26.10  ? 132 THR   A HG23 1 
ATOM   2063 N  N    . PHE   A 1 136 ? 0.769   -27.901 11.844  1.00 18.37  ? 133 PHE   A N    1 
ATOM   2064 C  CA   . PHE   A 1 136 ? 1.730   -28.629 12.661  1.00 22.44  ? 133 PHE   A CA   1 
ATOM   2065 C  C    . PHE   A 1 136 ? 1.071   -29.465 13.757  1.00 22.94  ? 133 PHE   A C    1 
ATOM   2066 O  O    . PHE   A 1 136 ? 1.780   -30.060 14.574  1.00 24.32  ? 133 PHE   A O    1 
ATOM   2067 C  CB   . PHE   A 1 136 ? 2.757   -27.643 13.282  1.00 21.02  ? 133 PHE   A CB   1 
ATOM   2068 C  CG   . PHE   A 1 136 ? 2.140   -26.489 13.990  1.00 20.60  ? 133 PHE   A CG   1 
ATOM   2069 C  CD1  . PHE   A 1 136 ? 1.534   -26.668 15.245  1.00 21.80  ? 133 PHE   A CD1  1 
ATOM   2070 C  CD2  . PHE   A 1 136 ? 2.105   -25.222 13.421  1.00 21.65  ? 133 PHE   A CD2  1 
ATOM   2071 C  CE1  . PHE   A 1 136 ? 0.899   -25.608 15.877  1.00 21.41  ? 133 PHE   A CE1  1 
ATOM   2072 C  CE2  . PHE   A 1 136 ? 1.487   -24.141 14.075  1.00 24.89  ? 133 PHE   A CE2  1 
ATOM   2073 C  CZ   . PHE   A 1 136 ? 0.879   -24.346 15.314  1.00 23.16  ? 133 PHE   A CZ   1 
ATOM   2074 H  H    . PHE   A 1 136 ? 0.552   -27.141 12.183  1.00 22.08  ? 133 PHE   A H    1 
ATOM   2075 H  HA   . PHE   A 1 136 ? 2.218   -29.240 12.087  1.00 26.97  ? 133 PHE   A HA   1 
ATOM   2076 H  HB2  . PHE   A 1 136 ? 3.302   -28.126 13.923  1.00 25.27  ? 133 PHE   A HB2  1 
ATOM   2077 H  HB3  . PHE   A 1 136 ? 3.316   -27.289 12.572  1.00 25.27  ? 133 PHE   A HB3  1 
ATOM   2078 H  HD1  . PHE   A 1 136 ? 1.559   -27.502 15.655  1.00 26.20  ? 133 PHE   A HD1  1 
ATOM   2079 H  HD2  . PHE   A 1 136 ? 2.499   -25.085 12.590  1.00 26.02  ? 133 PHE   A HD2  1 
ATOM   2080 H  HE1  . PHE   A 1 136 ? 0.479   -25.750 16.695  1.00 25.73  ? 133 PHE   A HE1  1 
ATOM   2081 H  HE2  . PHE   A 1 136 ? 1.483   -23.297 13.685  1.00 29.91  ? 133 PHE   A HE2  1 
ATOM   2082 H  HZ   . PHE   A 1 136 ? 0.464   -23.641 15.757  1.00 27.83  ? 133 PHE   A HZ   1 
ATOM   2083 N  N    . LEU   A 1 137 ? -0.244  -29.535 13.779  1.00 19.79  ? 134 LEU   A N    1 
ATOM   2084 C  CA   . LEU   A 1 137 ? -0.929  -30.301 14.814  1.00 21.25  ? 134 LEU   A CA   1 
ATOM   2085 C  C    . LEU   A 1 137 ? -0.886  -31.792 14.492  1.00 20.88  ? 134 LEU   A C    1 
ATOM   2086 O  O    . LEU   A 1 137 ? -0.857  -32.198 13.313  1.00 23.70  ? 134 LEU   A O    1 
ATOM   2087 C  CB   . LEU   A 1 137 ? -2.386  -29.874 14.937  1.00 21.29  ? 134 LEU   A CB   1 
ATOM   2088 C  CG   . LEU   A 1 137 ? -2.647  -28.425 15.284  1.00 19.30  ? 134 LEU   A CG   1 
ATOM   2089 C  CD1  . LEU   A 1 137 ? -4.146  -28.142 15.258  1.00 22.47  ? 134 LEU   A CD1  1 
ATOM   2090 C  CD2  . LEU   A 1 137 ? -2.010  -28.067 16.648  1.00 21.71  ? 134 LEU   A CD2  1 
ATOM   2091 H  H    . LEU   A 1 137 ? -0.766  -29.152 13.212  1.00 23.79  ? 134 LEU   A H    1 
ATOM   2092 H  HA   . LEU   A 1 137 ? -0.489  -30.143 15.664  1.00 25.54  ? 134 LEU   A HA   1 
ATOM   2093 H  HB2  . LEU   A 1 137 ? -2.819  -30.044 14.086  1.00 25.58  ? 134 LEU   A HB2  1 
ATOM   2094 H  HB3  . LEU   A 1 137 ? -2.797  -30.410 15.632  1.00 25.58  ? 134 LEU   A HB3  1 
ATOM   2095 H  HG   . LEU   A 1 137 ? -2.233  -27.849 14.622  1.00 23.20  ? 134 LEU   A HG   1 
ATOM   2096 H  HD11 . LEU   A 1 137 ? -4.289  -27.187 15.352  1.00 27.01  ? 134 LEU   A HD11 1 
ATOM   2097 H  HD12 . LEU   A 1 137 ? -4.510  -28.448 14.413  1.00 27.01  ? 134 LEU   A HD12 1 
ATOM   2098 H  HD13 . LEU   A 1 137 ? -4.569  -28.614 15.992  1.00 27.01  ? 134 LEU   A HD13 1 
ATOM   2099 H  HD21 . LEU   A 1 137 ? -2.297  -27.178 16.908  1.00 26.09  ? 134 LEU   A HD21 1 
ATOM   2100 H  HD22 . LEU   A 1 137 ? -2.297  -28.714 17.311  1.00 26.09  ? 134 LEU   A HD22 1 
ATOM   2101 H  HD23 . LEU   A 1 137 ? -1.044  -28.090 16.561  1.00 26.09  ? 134 LEU   A HD23 1 
ATOM   2102 N  N    A PRO   A 1 138 ? -0.885  -32.640 15.510  0.58 22.82  ? 135 PRO   A N    1 
ATOM   2103 N  N    B PRO   A 1 138 ? -0.950  -32.638 15.514  0.42 22.86  ? 135 PRO   A N    1 
ATOM   2104 C  CA   A PRO   A 1 138 ? -1.002  -34.085 15.247  0.58 27.14  ? 135 PRO   A CA   1 
ATOM   2105 C  CA   B PRO   A 1 138 ? -1.014  -34.086 15.253  0.42 27.14  ? 135 PRO   A CA   1 
ATOM   2106 C  C    A PRO   A 1 138 ? -2.259  -34.451 14.478  0.58 26.28  ? 135 PRO   A C    1 
ATOM   2107 C  C    B PRO   A 1 138 ? -2.284  -34.497 14.534  0.42 26.31  ? 135 PRO   A C    1 
ATOM   2108 O  O    A PRO   A 1 138 ? -2.227  -35.393 13.667  0.58 29.44  ? 135 PRO   A O    1 
ATOM   2109 O  O    B PRO   A 1 138 ? -2.298  -35.533 13.850  0.42 29.29  ? 135 PRO   A O    1 
ATOM   2110 C  CB   A PRO   A 1 138 ? -0.996  -34.700 16.655  0.58 27.22  ? 135 PRO   A CB   1 
ATOM   2111 C  CB   B PRO   A 1 138 ? -0.947  -34.694 16.661  0.42 27.24  ? 135 PRO   A CB   1 
ATOM   2112 C  CG   A PRO   A 1 138 ? -0.289  -33.701 17.504  0.58 28.24  ? 135 PRO   A CG   1 
ATOM   2113 C  CG   B PRO   A 1 138 ? -1.582  -33.665 17.526  0.42 21.40  ? 135 PRO   A CG   1 
ATOM   2114 C  CD   A PRO   A 1 138 ? -0.593  -32.347 16.924  0.58 23.71  ? 135 PRO   A CD   1 
ATOM   2115 C  CD   B PRO   A 1 138 ? -1.143  -32.321 16.940  0.42 26.19  ? 135 PRO   A CD   1 
ATOM   2116 H  HA   A PRO   A 1 138 ? -0.224  -34.399 14.760  0.58 32.61  ? 135 PRO   A HA   1 
ATOM   2117 H  HA   B PRO   A 1 138 ? -0.240  -34.371 14.743  0.42 32.61  ? 135 PRO   A HA   1 
ATOM   2118 H  HB2  A PRO   A 1 138 ? -1.906  -34.835 16.961  0.58 32.71  ? 135 PRO   A HB2  1 
ATOM   2119 H  HB2  B PRO   A 1 138 ? -1.441  -35.529 16.688  0.42 32.73  ? 135 PRO   A HB2  1 
ATOM   2120 H  HB3  A PRO   A 1 138 ? -0.521  -35.545 16.645  0.58 32.71  ? 135 PRO   A HB3  1 
ATOM   2121 H  HB3  B PRO   A 1 138 ? -0.024  -34.847 16.916  0.42 32.73  ? 135 PRO   A HB3  1 
ATOM   2122 H  HG2  A PRO   A 1 138 ? -0.616  -33.761 18.416  0.58 33.92  ? 135 PRO   A HG2  1 
ATOM   2123 H  HG2  B PRO   A 1 138 ? -2.547  -33.758 17.495  0.42 25.72  ? 135 PRO   A HG2  1 
ATOM   2124 H  HG3  A PRO   A 1 138 ? 0.665   -33.874 17.482  0.58 33.92  ? 135 PRO   A HG3  1 
ATOM   2125 H  HG3  B PRO   A 1 138 ? -1.268  -33.763 18.439  0.42 25.72  ? 135 PRO   A HG3  1 
ATOM   2126 H  HD2  A PRO   A 1 138 ? -1.362  -31.949 17.361  0.58 28.49  ? 135 PRO   A HD2  1 
ATOM   2127 H  HD2  B PRO   A 1 138 ? -1.833  -31.650 17.057  0.42 31.47  ? 135 PRO   A HD2  1 
ATOM   2128 H  HD3  A PRO   A 1 138 ? 0.174   -31.758 17.003  0.58 28.49  ? 135 PRO   A HD3  1 
ATOM   2129 H  HD3  B PRO   A 1 138 ? -0.315  -32.020 17.345  0.42 31.47  ? 135 PRO   A HD3  1 
ATOM   2130 N  N    . ASP   A 1 139 ? -3.366  -33.736 14.719  1.00 23.40  ? 136 ASP   A N    1 
ATOM   2131 C  CA   . ASP   A 1 139 ? -4.649  -33.961 14.055  1.00 23.82  ? 136 ASP   A CA   1 
ATOM   2132 C  C    . ASP   A 1 139 ? -4.924  -32.894 13.003  1.00 22.20  ? 136 ASP   A C    1 
ATOM   2133 O  O    . ASP   A 1 139 ? -6.073  -32.502 12.766  1.00 21.81  ? 136 ASP   A O    1 
ATOM   2134 C  CB   . ASP   A 1 139 ? -5.779  -34.017 15.091  1.00 25.51  ? 136 ASP   A CB   1 
ATOM   2135 C  CG   . ASP   A 1 139 ? -5.837  -32.776 16.024  1.00 25.05  ? 136 ASP   A CG   1 
ATOM   2136 O  OD1  . ASP   A 1 139 ? -4.853  -32.001 16.124  1.00 28.01  ? 136 ASP   A OD1  1 
ATOM   2137 O  OD2  . ASP   A 1 139 ? -6.867  -32.633 16.718  1.00 26.47  ? 136 ASP   A OD2  1 
ATOM   2138 H  H    . ASP   A 1 139 ? -3.399  -33.090 15.286  1.00 28.12  ? 136 ASP   A H    1 
ATOM   2139 H  HA   . ASP   A 1 139 ? -4.628  -34.817 13.601  1.00 28.63  ? 136 ASP   A HA   1 
ATOM   2140 H  HB2  . ASP   A 1 139 ? -6.627  -34.076 14.624  1.00 30.65  ? 136 ASP   A HB2  1 
ATOM   2141 H  HB3  . ASP   A 1 139 ? -5.652  -34.801 15.649  1.00 30.65  ? 136 ASP   A HB3  1 
ATOM   2142 N  N    A SER   A 1 140 ? -3.862  -32.409 12.360  0.68 22.14  ? 137 SER   A N    1 
ATOM   2143 N  N    B SER   A 1 140 ? -3.867  -32.433 12.332  0.32 22.31  ? 137 SER   A N    1 
ATOM   2144 C  CA   A SER   A 1 140 ? -4.027  -31.414 11.311  0.68 19.62  ? 137 SER   A CA   1 
ATOM   2145 C  CA   B SER   A 1 140 ? -4.031  -31.411 11.307  0.32 19.74  ? 137 SER   A CA   1 
ATOM   2146 C  C    A SER   A 1 140 ? -5.066  -31.835 10.273  0.68 20.66  ? 137 SER   A C    1 
ATOM   2147 C  C    B SER   A 1 140 ? -5.043  -31.828 10.243  0.32 20.85  ? 137 SER   A C    1 
ATOM   2148 O  O    A SER   A 1 140 ? -5.903  -31.020 9.859   0.68 22.33  ? 137 SER   A O    1 
ATOM   2149 O  O    B SER   A 1 140 ? -5.853  -31.005 9.799   0.32 22.33  ? 137 SER   A O    1 
ATOM   2150 C  CB   A SER   A 1 140 ? -2.678  -31.166 10.631  0.68 19.44  ? 137 SER   A CB   1 
ATOM   2151 C  CB   B SER   A 1 140 ? -2.674  -31.112 10.661  0.32 19.67  ? 137 SER   A CB   1 
ATOM   2152 O  OG   A SER   A 1 140 ? -2.865  -30.340 9.484   0.68 17.42  ? 137 SER   A OG   1 
ATOM   2153 O  OG   B SER   A 1 140 ? -2.162  -32.239 9.971   0.32 28.16  ? 137 SER   A OG   1 
ATOM   2154 H  H    A SER   A 1 140 ? -3.047  -32.639 12.511  0.68 26.61  ? 137 SER   A H    1 
ATOM   2155 H  H    B SER   A 1 140 ? -3.056  -32.693 12.452  0.32 26.81  ? 137 SER   A H    1 
ATOM   2156 H  HA   A SER   A 1 140 ? -4.337  -30.590 11.718  0.68 23.59  ? 137 SER   A HA   1 
ATOM   2157 H  HA   B SER   A 1 140 ? -4.363  -30.602 11.725  0.32 23.73  ? 137 SER   A HA   1 
ATOM   2158 H  HB2  A SER   A 1 140 ? -2.082  -30.721 11.253  0.68 23.36  ? 137 SER   A HB2  1 
ATOM   2159 H  HB2  B SER   A 1 140 ? -2.782  -30.383 10.032  0.32 23.65  ? 137 SER   A HB2  1 
ATOM   2160 H  HB3  A SER   A 1 140 ? -2.296  -32.015 10.356  0.68 23.36  ? 137 SER   A HB3  1 
ATOM   2161 H  HB3  B SER   A 1 140 ? -2.046  -30.860 11.357  0.32 23.65  ? 137 SER   A HB3  1 
ATOM   2162 H  HG   A SER   A 1 140 ? -3.251  -29.627 9.704   0.68 20.94  ? 137 SER   A HG   1 
ATOM   2163 H  HG   B SER   A 1 140 ? -2.698  -32.475 9.369   0.32 33.83  ? 137 SER   A HG   1 
ATOM   2164 N  N    . THR   A 1 141 ? -4.997  -33.090 9.795   1.00 19.79  ? 138 THR   A N    1 
ATOM   2165 C  CA   . THR   A 1 141 ? -5.914  -33.538 8.750   1.00 21.23  ? 138 THR   A CA   1 
ATOM   2166 C  C    . THR   A 1 141 ? -7.378  -33.353 9.136   1.00 23.62  ? 138 THR   A C    1 
ATOM   2167 O  O    . THR   A 1 141 ? -8.188  -32.965 8.303   1.00 24.56  ? 138 THR   A O    1 
ATOM   2168 C  CB   . THR   A 1 141 ? -5.621  -34.993 8.414   1.00 27.01  ? 138 THR   A CB   1 
ATOM   2169 O  OG1  . THR   A 1 141 ? -4.318  -35.053 7.822   1.00 30.76  ? 138 THR   A OG1  1 
ATOM   2170 C  CG2  . THR   A 1 141 ? -6.655  -35.573 7.428   1.00 31.00  ? 138 THR   A CG2  1 
ATOM   2171 H  H    . THR   A 1 141 ? -4.434  -33.684 10.060  1.00 23.79  ? 138 THR   A H    1 
ATOM   2172 H  HA   . THR   A 1 141 ? -5.767  -32.997 7.958   1.00 25.52  ? 138 THR   A HA   1 
ATOM   2173 H  HB   . THR   A 1 141 ? -5.665  -35.531 9.221   1.00 32.45  ? 138 THR   A HB   1 
ATOM   2174 H  HG1  . THR   A 1 141 ? -4.038  -35.845 7.824   1.00 36.95  ? 138 THR   A HG1  1 
ATOM   2175 H  HG21 . THR   A 1 141 ? -6.317  -36.394 7.037   1.00 37.24  ? 138 THR   A HG21 1 
ATOM   2176 H  HG22 . THR   A 1 141 ? -7.486  -35.763 7.892   1.00 37.24  ? 138 THR   A HG22 1 
ATOM   2177 H  HG23 . THR   A 1 141 ? -6.830  -34.935 6.718   1.00 37.24  ? 138 THR   A HG23 1 
ATOM   2178 N  N    . TYR   A 1 142 ? -7.742  -33.653 10.377  1.00 21.35  ? 139 TYR   A N    1 
ATOM   2179 C  CA   . TYR   A 1 142 ? -9.140  -33.494 10.770  1.00 23.46  ? 139 TYR   A CA   1 
ATOM   2180 C  C    . TYR   A 1 142 ? -9.599  -32.056 10.589  1.00 22.40  ? 139 TYR   A C    1 
ATOM   2181 O  O    . TYR   A 1 142 ? -10.675 -31.804 10.034  1.00 22.93  ? 139 TYR   A O    1 
ATOM   2182 C  CB   . TYR   A 1 142 ? -9.301  -33.888 12.225  1.00 24.24  ? 139 TYR   A CB   1 
ATOM   2183 C  CG   . TYR   A 1 142 ? -10.651 -33.543 12.823  1.00 25.69  ? 139 TYR   A CG   1 
ATOM   2184 C  CD1  . TYR   A 1 142 ? -11.744 -34.340 12.607  1.00 25.68  ? 139 TYR   A CD1  1 
ATOM   2185 C  CD2  . TYR   A 1 142 ? -10.808 -32.380 13.567  1.00 24.98  ? 139 TYR   A CD2  1 
ATOM   2186 C  CE1  . TYR   A 1 142 ? -12.991 -34.039 13.165  1.00 26.08  ? 139 TYR   A CE1  1 
ATOM   2187 C  CE2  . TYR   A 1 142 ? -12.032 -32.055 14.122  1.00 27.47  ? 139 TYR   A CE2  1 
ATOM   2188 C  CZ   . TYR   A 1 142 ? -13.104 -32.868 13.914  1.00 26.18  ? 139 TYR   A CZ   1 
ATOM   2189 O  OH   . TYR   A 1 142 ? -14.336 -32.547 14.458  1.00 33.15  ? 139 TYR   A OH   1 
ATOM   2190 H  H    . TYR   A 1 142 ? -7.218  -33.943 10.994  1.00 25.67  ? 139 TYR   A H    1 
ATOM   2191 H  HA   . TYR   A 1 142 ? -9.687  -34.070 10.214  1.00 28.19  ? 139 TYR   A HA   1 
ATOM   2192 H  HB2  . TYR   A 1 142 ? -9.184  -34.848 12.300  1.00 29.13  ? 139 TYR   A HB2  1 
ATOM   2193 H  HB3  . TYR   A 1 142 ? -8.624  -33.429 12.746  1.00 29.13  ? 139 TYR   A HB3  1 
ATOM   2194 H  HD1  . TYR   A 1 142 ? -11.655 -35.099 12.078  1.00 30.85  ? 139 TYR   A HD1  1 
ATOM   2195 H  HD2  . TYR   A 1 142 ? -10.082 -31.814 13.693  1.00 30.01  ? 139 TYR   A HD2  1 
ATOM   2196 H  HE1  . TYR   A 1 142 ? -13.721 -34.601 13.039  1.00 31.33  ? 139 TYR   A HE1  1 
ATOM   2197 H  HE2  . TYR   A 1 142 ? -12.123 -31.285 14.635  1.00 33.00  ? 139 TYR   A HE2  1 
ATOM   2198 H  HH   . TYR   A 1 142 ? -14.248 -31.936 15.028  1.00 39.82  ? 139 TYR   A HH   1 
ATOM   2199 N  N    . TRP   A 1 143 ? -8.779  -31.104 11.054  1.00 21.70  ? 140 TRP   A N    1 
ATOM   2200 C  CA   . TRP   A 1 143 ? -9.134  -29.676 11.025  1.00 18.98  ? 140 TRP   A CA   1 
ATOM   2201 C  C    . TRP   A 1 143 ? -9.096  -29.143 9.597   1.00 20.28  ? 140 TRP   A C    1 
ATOM   2202 O  O    . TRP   A 1 143 ? -9.982  -28.384 9.195   1.00 22.26  ? 140 TRP   A O    1 
ATOM   2203 C  CB   . TRP   A 1 143 ? -8.226  -28.886 11.976  1.00 19.42  ? 140 TRP   A CB   1 
ATOM   2204 C  CG   . TRP   A 1 143 ? -8.507  -29.294 13.397  1.00 22.29  ? 140 TRP   A CG   1 
ATOM   2205 C  CD1  . TRP   A 1 143 ? -7.726  -30.088 14.194  1.00 22.70  ? 140 TRP   A CD1  1 
ATOM   2206 C  CD2  . TRP   A 1 143 ? -9.663  -28.960 14.173  1.00 24.82  ? 140 TRP   A CD2  1 
ATOM   2207 N  NE1  . TRP   A 1 143 ? -8.347  -30.293 15.409  1.00 23.93  ? 140 TRP   A NE1  1 
ATOM   2208 C  CE2  . TRP   A 1 143 ? -9.536  -29.610 15.418  1.00 25.38  ? 140 TRP   A CE2  1 
ATOM   2209 C  CE3  . TRP   A 1 143 ? -10.795 -28.182 13.931  1.00 31.71  ? 140 TRP   A CE3  1 
ATOM   2210 C  CZ2  . TRP   A 1 143 ? -10.491 -29.478 16.427  1.00 31.35  ? 140 TRP   A CZ2  1 
ATOM   2211 C  CZ3  . TRP   A 1 143 ? -11.747 -28.074 14.929  1.00 30.54  ? 140 TRP   A CZ3  1 
ATOM   2212 C  CH2  . TRP   A 1 143 ? -11.587 -28.715 16.153  1.00 30.75  ? 140 TRP   A CH2  1 
ATOM   2213 H  H    . TRP   A 1 143 ? -8.004  -31.257 11.394  1.00 26.09  ? 140 TRP   A H    1 
ATOM   2214 H  HA   . TRP   A 1 143 ? -10.039 -29.554 11.351  1.00 22.82  ? 140 TRP   A HA   1 
ATOM   2215 H  HB2  . TRP   A 1 143 ? -7.296  -29.074 11.774  1.00 23.35  ? 140 TRP   A HB2  1 
ATOM   2216 H  HB3  . TRP   A 1 143 ? -8.400  -27.936 11.882  1.00 23.35  ? 140 TRP   A HB3  1 
ATOM   2217 H  HD1  . TRP   A 1 143 ? -6.899  -30.437 13.951  1.00 27.28  ? 140 TRP   A HD1  1 
ATOM   2218 H  HE1  . TRP   A 1 143 ? -8.038  -30.770 16.054  1.00 28.76  ? 140 TRP   A HE1  1 
ATOM   2219 H  HE3  . TRP   A 1 143 ? -10.907 -27.746 13.118  1.00 38.09  ? 140 TRP   A HE3  1 
ATOM   2220 H  HZ2  . TRP   A 1 143 ? -10.384 -29.893 17.253  1.00 37.66  ? 140 TRP   A HZ2  1 
ATOM   2221 H  HZ3  . TRP   A 1 143 ? -12.509 -27.563 14.778  1.00 36.70  ? 140 TRP   A HZ3  1 
ATOM   2222 H  HH2  . TRP   A 1 143 ? -12.246 -28.620 16.802  1.00 36.94  ? 140 TRP   A HH2  1 
ATOM   2223 N  N    . LYS   A 1 144 ? -8.101  -29.573 8.811   1.00 20.17  ? 141 LYS   A N    1 
ATOM   2224 C  CA   . LYS   A 1 144 ? -8.035  -29.189 7.406   1.00 22.43  ? 141 LYS   A CA   1 
ATOM   2225 C  C    . LYS   A 1 144 ? -9.280  -29.665 6.671   1.00 23.08  ? 141 LYS   A C    1 
ATOM   2226 O  O    . LYS   A 1 144 ? -9.918  -28.904 5.930   1.00 22.52  ? 141 LYS   A O    1 
ATOM   2227 C  CB   . LYS   A 1 144 ? -6.771  -29.759 6.764   1.00 23.22  ? 141 LYS   A CB   1 
ATOM   2228 C  CG   . LYS   A 1 144 ? -6.652  -29.495 5.272   1.00 28.02  ? 141 LYS   A CG   1 
ATOM   2229 C  CD   . LYS   A 1 144 ? -5.590  -30.356 4.645   1.00 30.55  ? 141 LYS   A CD   1 
ATOM   2230 C  CE   . LYS   A 1 144 ? -5.317  -29.912 3.205   1.00 40.73  ? 141 LYS   A CE   1 
ATOM   2231 N  NZ   . LYS   A 1 144 ? -6.284  -30.535 2.263   1.00 54.41  ? 141 LYS   A NZ   1 
ATOM   2232 H  H    . LYS   A 1 144 ? -7.459  -30.084 9.069   1.00 24.24  ? 141 LYS   A H    1 
ATOM   2233 H  HA   . LYS   A 1 144 ? -7.987  -28.222 7.337   1.00 26.95  ? 141 LYS   A HA   1 
ATOM   2234 H  HB2  . LYS   A 1 144 ? -5.999  -29.362 7.196   1.00 27.91  ? 141 LYS   A HB2  1 
ATOM   2235 H  HB3  . LYS   A 1 144 ? -6.766  -30.720 6.894   1.00 27.91  ? 141 LYS   A HB3  1 
ATOM   2236 H  HG2  . LYS   A 1 144 ? -7.498  -29.692 4.842   1.00 33.67  ? 141 LYS   A HG2  1 
ATOM   2237 H  HG3  . LYS   A 1 144 ? -6.415  -28.565 5.128   1.00 33.67  ? 141 LYS   A HG3  1 
ATOM   2238 H  HD2  . LYS   A 1 144 ? -4.768  -30.279 5.153   1.00 36.70  ? 141 LYS   A HD2  1 
ATOM   2239 H  HD3  . LYS   A 1 144 ? -5.887  -31.280 4.632   1.00 36.70  ? 141 LYS   A HD3  1 
ATOM   2240 H  HE2  . LYS   A 1 144 ? -5.405  -28.948 3.142   1.00 48.91  ? 141 LYS   A HE2  1 
ATOM   2241 H  HE3  . LYS   A 1 144 ? -4.421  -30.182 2.949   1.00 48.91  ? 141 LYS   A HE3  1 
ATOM   2242 H  HZ1  . LYS   A 1 144 ? -6.092  -30.297 1.428   1.00 65.33  ? 141 LYS   A HZ1  1 
ATOM   2243 H  HZ2  . LYS   A 1 144 ? -6.243  -31.422 2.327   1.00 65.33  ? 141 LYS   A HZ2  1 
ATOM   2244 H  HZ3  . LYS   A 1 144 ? -7.111  -30.270 2.457   1.00 65.33  ? 141 LYS   A HZ3  1 
ATOM   2245 N  N    . ASP   A 1 145 ? -9.639  -30.935 6.849   1.00 21.60  ? 142 ASP   A N    1 
ATOM   2246 C  CA   . ASP   A 1 145 ? -10.799 -31.469 6.157   1.00 23.57  ? 142 ASP   A CA   1 
ATOM   2247 C  C    . ASP   A 1 145 ? -12.084 -30.756 6.567   1.00 24.74  ? 142 ASP   A C    1 
ATOM   2248 O  O    . ASP   A 1 145 ? -12.988 -30.572 5.739   1.00 25.35  ? 142 ASP   A O    1 
ATOM   2249 C  CB   . ASP   A 1 145 ? -10.913 -32.974 6.435   1.00 26.19  ? 142 ASP   A CB   1 
ATOM   2250 C  CG   . ASP   A 1 145 ? -9.867  -33.799 5.677   1.00 32.64  ? 142 ASP   A CG   1 
ATOM   2251 O  OD1  . ASP   A 1 145 ? -9.150  -33.232 4.824   1.00 34.71  ? 142 ASP   A OD1  1 
ATOM   2252 O  OD2  . ASP   A 1 145 ? -9.783  -35.016 5.936   1.00 34.14  ? 142 ASP   A OD2  1 
ATOM   2253 H  H    . ASP   A 1 145 ? -9.232  -31.497 7.357   1.00 25.97  ? 142 ASP   A H    1 
ATOM   2254 H  HA   . ASP   A 1 145 ? -10.681 -31.334 5.204   1.00 28.32  ? 142 ASP   A HA   1 
ATOM   2255 H  HB2  . ASP   A 1 145 ? -10.788 -33.130 7.384   1.00 31.47  ? 142 ASP   A HB2  1 
ATOM   2256 H  HB3  . ASP   A 1 145 ? -11.792 -33.280 6.161   1.00 31.47  ? 142 ASP   A HB3  1 
ATOM   2257 N  N    . LYS   A 1 146 ? -12.206 -30.399 7.851   1.00 23.29  ? 143 LYS   A N    1 
ATOM   2258 C  CA   . LYS   A 1 146 ? -13.373 -29.661 8.295   1.00 23.66  ? 143 LYS   A CA   1 
ATOM   2259 C  C    . LYS   A 1 146 ? -13.451 -28.296 7.624   1.00 24.54  ? 143 LYS   A C    1 
ATOM   2260 O  O    . LYS   A 1 146 ? -14.524 -27.886 7.153   1.00 23.73  ? 143 LYS   A O    1 
ATOM   2261 C  CB   . LYS   A 1 146 ? -13.344 -29.499 9.809   1.00 24.24  ? 143 LYS   A CB   1 
ATOM   2262 C  CG   . LYS   A 1 146 ? -13.657 -30.762 10.567  1.00 27.34  ? 143 LYS   A CG   1 
ATOM   2263 C  CD   . LYS   A 1 146 ? -15.155 -31.065 10.545  1.00 29.35  ? 143 LYS   A CD   1 
ATOM   2264 C  CE   . LYS   A 1 146 ? -15.494 -32.260 11.418  1.00 32.32  ? 143 LYS   A CE   1 
ATOM   2265 N  NZ   . LYS   A 1 146 ? -16.937 -32.643 11.314  1.00 39.84  ? 143 LYS   A NZ   1 
ATOM   2266 H  H    . LYS   A 1 146 ? -11.632 -30.572 8.468   1.00 27.99  ? 143 LYS   A H    1 
ATOM   2267 H  HA   . LYS   A 1 146 ? -14.167 -30.165 8.057   1.00 28.43  ? 143 LYS   A HA   1 
ATOM   2268 H  HB2  . LYS   A 1 146 ? -12.458 -29.208 10.073  1.00 29.13  ? 143 LYS   A HB2  1 
ATOM   2269 H  HB3  . LYS   A 1 146 ? -14.002 -28.832 10.062  1.00 29.13  ? 143 LYS   A HB3  1 
ATOM   2270 H  HG2  . LYS   A 1 146 ? -13.188 -31.507 10.160  1.00 32.85  ? 143 LYS   A HG2  1 
ATOM   2271 H  HG3  . LYS   A 1 146 ? -13.380 -30.661 11.491  1.00 32.85  ? 143 LYS   A HG3  1 
ATOM   2272 H  HD2  . LYS   A 1 146 ? -15.643 -30.296 10.877  1.00 35.27  ? 143 LYS   A HD2  1 
ATOM   2273 H  HD3  . LYS   A 1 146 ? -15.429 -31.265 9.636   1.00 35.27  ? 143 LYS   A HD3  1 
ATOM   2274 H  HE2  . LYS   A 1 146 ? -14.959 -33.019 11.140  1.00 38.82  ? 143 LYS   A HE2  1 
ATOM   2275 H  HE3  . LYS   A 1 146 ? -15.305 -32.041 12.344  1.00 38.82  ? 143 LYS   A HE3  1 
ATOM   2276 H  HZ1  . LYS   A 1 146 ? -17.096 -33.365 11.810  1.00 47.85  ? 143 LYS   A HZ1  1 
ATOM   2277 H  HZ2  . LYS   A 1 146 ? -17.450 -31.975 11.603  1.00 47.85  ? 143 LYS   A HZ2  1 
ATOM   2278 H  HZ3  . LYS   A 1 146 ? -17.144 -32.822 10.468  1.00 47.85  ? 143 LYS   A HZ3  1 
ATOM   2279 N  N    . ASN   A 1 147 ? -12.318 -27.607 7.509   1.00 22.73  ? 144 ASN   A N    1 
ATOM   2280 C  CA   . ASN   A 1 147 ? -12.323 -26.334 6.795   1.00 21.97  ? 144 ASN   A CA   1 
ATOM   2281 C  C    . ASN   A 1 147 ? -12.686 -26.524 5.326   1.00 24.45  ? 144 ASN   A C    1 
ATOM   2282 O  O    . ASN   A 1 147 ? -13.511 -25.780 4.774   1.00 23.53  ? 144 ASN   A O    1 
ATOM   2283 C  CB   . ASN   A 1 147 ? -10.966 -25.673 6.873   1.00 20.15  ? 144 ASN   A CB   1 
ATOM   2284 C  CG   . ASN   A 1 147 ? -10.631 -25.147 8.244   1.00 20.81  ? 144 ASN   A CG   1 
ATOM   2285 O  OD1  . ASN   A 1 147 ? -11.510 -24.898 9.063   1.00 24.35  ? 144 ASN   A OD1  1 
ATOM   2286 N  ND2  . ASN   A 1 147 ? -9.346  -24.979 8.490   1.00 22.06  ? 144 ASN   A ND2  1 
ATOM   2287 H  H    . ASN   A 1 147 ? -11.555 -27.846 7.826   1.00 27.32  ? 144 ASN   A H    1 
ATOM   2288 H  HA   . ASN   A 1 147 ? -12.980 -25.763 7.223   1.00 26.41  ? 144 ASN   A HA   1 
ATOM   2289 H  HB2  . ASN   A 1 147 ? -10.287 -26.322 6.630   1.00 24.22  ? 144 ASN   A HB2  1 
ATOM   2290 H  HB3  . ASN   A 1 147 ? -10.947 -24.925 6.256   1.00 24.22  ? 144 ASN   A HB3  1 
ATOM   2291 H  HD21 . ASN   A 1 147 ? -9.090  -24.682 9.255   1.00 26.51  ? 144 ASN   A HD21 1 
ATOM   2292 H  HD22 . ASN   A 1 147 ? -8.764  -25.167 7.885   1.00 26.51  ? 144 ASN   A HD22 1 
ATOM   2293 N  N    . ASP   A 1 148 ? -12.083 -27.533 4.676   1.00 21.68  ? 145 ASP   A N    1 
ATOM   2294 C  CA   . ASP   A 1 148 ? -12.339 -27.745 3.265   1.00 26.38  ? 145 ASP   A CA   1 
ATOM   2295 C  C    . ASP   A 1 148 ? -13.804 -28.061 3.048   1.00 25.70  ? 145 ASP   A C    1 
ATOM   2296 O  O    . ASP   A 1 148 ? -14.415 -27.626 2.063   1.00 26.52  ? 145 ASP   A O    1 
ATOM   2297 C  CB   . ASP   A 1 148 ? -11.483 -28.885 2.718   1.00 25.52  ? 145 ASP   A CB   1 
ATOM   2298 C  CG   . ASP   A 1 148 ? -10.003 -28.549 2.633   1.00 31.91  ? 145 ASP   A CG   1 
ATOM   2299 O  OD1  . ASP   A 1 148 ? -9.621  -27.353 2.641   1.00 31.98  ? 145 ASP   A OD1  1 
ATOM   2300 O  OD2  . ASP   A 1 148 ? -9.198  -29.500 2.525   1.00 34.30  ? 145 ASP   A OD2  1 
ATOM   2301 H  H    . ASP   A 1 148 ? -11.534 -28.092 5.031   1.00 26.05  ? 145 ASP   A H    1 
ATOM   2302 H  HA   . ASP   A 1 148 ? -12.099 -26.940 2.780   1.00 31.69  ? 145 ASP   A HA   1 
ATOM   2303 H  HB2  . ASP   A 1 148 ? -11.579 -29.655 3.301   1.00 30.67  ? 145 ASP   A HB2  1 
ATOM   2304 H  HB3  . ASP   A 1 148 ? -11.789 -29.105 1.825   1.00 30.67  ? 145 ASP   A HB3  1 
ATOM   2305 N  N    . ASP   A 1 149 ? -14.384 -28.853 3.947   1.00 24.78  ? 146 ASP   A N    1 
ATOM   2306 C  CA   . ASP   A 1 149 ? -15.754 -29.294 3.755   1.00 25.93  ? 146 ASP   A CA   1 
ATOM   2307 C  C    . ASP   A 1 149 ? -16.756 -28.172 3.990   1.00 27.47  ? 146 ASP   A C    1 
ATOM   2308 O  O    . ASP   A 1 149 ? -17.752 -28.073 3.250   1.00 28.26  ? 146 ASP   A O    1 
ATOM   2309 C  CB   . ASP   A 1 149 ? -16.041 -30.497 4.660   1.00 30.42  ? 146 ASP   A CB   1 
ATOM   2310 C  CG   . ASP   A 1 149 ? -15.251 -31.751 4.245   1.00 42.23  ? 146 ASP   A CG   1 
ATOM   2311 O  OD1  . ASP   A 1 149 ? -14.726 -31.781 3.111   1.00 52.00  ? 146 ASP   A OD1  1 
ATOM   2312 O  OD2  . ASP   A 1 149 ? -15.165 -32.715 5.053   1.00 46.72  ? 146 ASP   A OD2  1 
ATOM   2313 H  H    . ASP   A 1 149 ? -14.009 -29.144 4.664   1.00 29.78  ? 146 ASP   A H    1 
ATOM   2314 H  HA   . ASP   A 1 149 ? -15.864 -29.577 2.834   1.00 31.16  ? 146 ASP   A HA   1 
ATOM   2315 H  HB2  . ASP   A 1 149 ? -15.793 -30.275 5.571   1.00 36.55  ? 146 ASP   A HB2  1 
ATOM   2316 H  HB3  . ASP   A 1 149 ? -16.986 -30.710 4.615   1.00 36.55  ? 146 ASP   A HB3  1 
ATOM   2317 N  N    . ILE   A 1 150 ? -16.503 -27.292 4.973   1.00 25.73  ? 147 ILE   A N    1 
ATOM   2318 C  CA   . ILE   A 1 150 ? -17.431 -26.196 5.215   1.00 31.87  ? 147 ILE   A CA   1 
ATOM   2319 C  C    . ILE   A 1 150 ? -17.380 -25.201 4.058   1.00 27.56  ? 147 ILE   A C    1 
ATOM   2320 O  O    . ILE   A 1 150 ? -18.409 -24.717 3.595   1.00 29.91  ? 147 ILE   A O    1 
ATOM   2321 C  CB   . ILE   A 1 150 ? -17.133 -25.528 6.572   1.00 30.57  ? 147 ILE   A CB   1 
ATOM   2322 C  CG1  . ILE   A 1 150 ? -17.608 -26.432 7.706   1.00 42.82  ? 147 ILE   A CG1  1 
ATOM   2323 C  CG2  . ILE   A 1 150 ? -17.825 -24.181 6.667   1.00 42.65  ? 147 ILE   A CG2  1 
ATOM   2324 C  CD1  . ILE   A 1 150 ? -16.726 -26.462 8.942   1.00 43.17  ? 147 ILE   A CD1  1 
ATOM   2325 H  H    . ILE   A 1 150 ? -15.819 -27.313 5.494   1.00 30.92  ? 147 ILE   A H    1 
ATOM   2326 H  HA   . ILE   A 1 150 ? -18.332 -26.551 5.261   1.00 38.28  ? 147 ILE   A HA   1 
ATOM   2327 H  HB   . ILE   A 1 150 ? -16.175 -25.392 6.645   1.00 36.73  ? 147 ILE   A HB   1 
ATOM   2328 H  HG12 . ILE   A 1 150 ? -18.486 -26.130 7.988   1.00 51.43  ? 147 ILE   A HG12 1 
ATOM   2329 H  HG13 . ILE   A 1 150 ? -17.662 -27.340 7.369   1.00 51.43  ? 147 ILE   A HG13 1 
ATOM   2330 H  HG21 . ILE   A 1 150 ? -17.637 -23.789 7.534   1.00 51.22  ? 147 ILE   A HG21 1 
ATOM   2331 H  HG22 . ILE   A 1 150 ? -17.489 -23.603 5.963   1.00 51.22  ? 147 ILE   A HG22 1 
ATOM   2332 H  HG23 . ILE   A 1 150 ? -18.781 -24.308 6.562   1.00 51.22  ? 147 ILE   A HG23 1 
ATOM   2333 H  HD11 . ILE   A 1 150 ? -17.118 -27.061 9.596   1.00 51.84  ? 147 ILE   A HD11 1 
ATOM   2334 H  HD12 . ILE   A 1 150 ? -15.843 -26.778 8.691   1.00 51.84  ? 147 ILE   A HD12 1 
ATOM   2335 H  HD13 . ILE   A 1 150 ? -16.665 -25.566 9.308   1.00 51.84  ? 147 ILE   A HD13 1 
ATOM   2336 N  N    . VAL   A 1 151 ? -16.186 -24.909 3.545   1.00 26.36  ? 148 VAL   A N    1 
ATOM   2337 C  CA   . VAL   A 1 151 ? -16.091 -24.012 2.396   1.00 27.96  ? 148 VAL   A CA   1 
ATOM   2338 C  C    . VAL   A 1 151 ? -16.757 -24.635 1.185   1.00 27.17  ? 148 VAL   A C    1 
ATOM   2339 O  O    . VAL   A 1 151 ? -17.487 -23.970 0.454   1.00 30.71  ? 148 VAL   A O    1 
ATOM   2340 C  CB   . VAL   A 1 151 ? -14.618 -23.652 2.097   1.00 27.24  ? 148 VAL   A CB   1 
ATOM   2341 C  CG1  . VAL   A 1 151 ? -14.534 -22.872 0.774   1.00 26.89  ? 148 VAL   A CG1  1 
ATOM   2342 C  CG2  . VAL   A 1 151 ? -13.994 -22.867 3.232   1.00 26.42  ? 148 VAL   A CG2  1 
ATOM   2343 H  H    . VAL   A 1 151 ? -15.435 -25.209 3.836   1.00 31.67  ? 148 VAL   A H    1 
ATOM   2344 H  HA   . VAL   A 1 151 ? -16.559 -23.192 2.618   1.00 33.59  ? 148 VAL   A HA   1 
ATOM   2345 H  HB   . VAL   A 1 151 ? -14.106 -24.472 2.010   1.00 32.72  ? 148 VAL   A HB   1 
ATOM   2346 H  HG11 . VAL   A 1 151 ? -13.667 -22.443 0.715   1.00 32.32  ? 148 VAL   A HG11 1 
ATOM   2347 H  HG12 . VAL   A 1 151 ? -14.649 -23.491 0.036   1.00 32.32  ? 148 VAL   A HG12 1 
ATOM   2348 H  HG13 . VAL   A 1 151 ? -15.236 -22.203 0.757   1.00 32.32  ? 148 VAL   A HG13 1 
ATOM   2349 H  HG21 . VAL   A 1 151 ? -13.069 -22.673 3.012   1.00 31.75  ? 148 VAL   A HG21 1 
ATOM   2350 H  HG22 . VAL   A 1 151 ? -14.486 -22.039 3.351   1.00 31.75  ? 148 VAL   A HG22 1 
ATOM   2351 H  HG23 . VAL   A 1 151 ? -14.037 -23.396 4.044   1.00 31.75  ? 148 VAL   A HG23 1 
ATOM   2352 N  N    . HIS   A 1 152 ? -16.515 -25.920 0.947   1.00 30.79  ? 149 HIS   A N    1 
ATOM   2353 C  CA   . HIS   A 1 152 ? -17.140 -26.565 -0.195  1.00 32.87  ? 149 HIS   A CA   1 
ATOM   2354 C  C    . HIS   A 1 152 ? -18.656 -26.493 -0.098  1.00 32.57  ? 149 HIS   A C    1 
ATOM   2355 O  O    . HIS   A 1 152 ? -19.356 -26.252 -1.095  1.00 36.79  ? 149 HIS   A O    1 
ATOM   2356 C  CB   . HIS   A 1 152 ? -16.709 -28.026 -0.286  1.00 36.16  ? 149 HIS   A CB   1 
ATOM   2357 C  CG   . HIS   A 1 152 ? -17.264 -28.727 -1.486  1.00 43.69  ? 149 HIS   A CG   1 
ATOM   2358 N  ND1  . HIS   A 1 152 ? -18.369 -29.549 -1.429  1.00 47.07  ? 149 HIS   A ND1  1 
ATOM   2359 C  CD2  . HIS   A 1 152 ? -16.868 -28.712 -2.778  1.00 42.08  ? 149 HIS   A CD2  1 
ATOM   2360 C  CE1  . HIS   A 1 152 ? -18.630 -30.013 -2.641  1.00 37.79  ? 149 HIS   A CE1  1 
ATOM   2361 N  NE2  . HIS   A 1 152 ? -17.725 -29.526 -3.472  1.00 42.04  ? 149 HIS   A NE2  1 
ATOM   2362 H  H    . HIS   A 1 152 ? -16.005 -26.426 1.419   1.00 36.99  ? 149 HIS   A H    1 
ATOM   2363 H  HA   . HIS   A 1 152 ? -16.849 -26.107 -0.999  1.00 39.49  ? 149 HIS   A HA   1 
ATOM   2364 H  HB2  . HIS   A 1 152 ? -15.741 -28.065 -0.338  1.00 43.44  ? 149 HIS   A HB2  1 
ATOM   2365 H  HB3  . HIS   A 1 152 ? -17.019 -28.495 0.504   1.00 43.44  ? 149 HIS   A HB3  1 
ATOM   2366 H  HD2  . HIS   A 1 152 ? -16.149 -28.238 -3.130  1.00 50.54  ? 149 HIS   A HD2  1 
ATOM   2367 H  HE1  . HIS   A 1 152 ? -19.329 -30.583 -2.868  1.00 45.39  ? 149 HIS   A HE1  1 
ATOM   2368 H  HE2  . HIS   A 1 152 ? -17.680 -29.694 -4.315  1.00 50.48  ? 149 HIS   A HE2  1 
ATOM   2369 N  N    . GLN   A 1 153 ? -19.194 -26.740 1.094   1.00 32.35  ? 150 GLN   A N    1 
ATOM   2370 C  CA   . GLN   A 1 153 ? -20.638 -26.758 1.247   1.00 33.04  ? 150 GLN   A CA   1 
ATOM   2371 C  C    . GLN   A 1 153 ? -21.222 -25.378 0.977   1.00 37.36  ? 150 GLN   A C    1 
ATOM   2372 O  O    . GLN   A 1 153 ? -22.241 -25.253 0.291   1.00 38.81  ? 150 GLN   A O    1 
ATOM   2373 C  CB   . GLN   A 1 153 ? -20.990 -27.236 2.659   1.00 41.65  ? 150 GLN   A CB   1 
ATOM   2374 C  CG   . GLN   A 1 153 ? -22.291 -26.650 3.185   1.00 53.30  ? 150 GLN   A CG   1 
ATOM   2375 C  CD   . GLN   A 1 153 ? -22.524 -26.950 4.649   1.00 62.46  ? 150 GLN   A CD   1 
ATOM   2376 O  OE1  . GLN   A 1 153 ? -23.098 -26.138 5.362   1.00 61.86  ? 150 GLN   A OE1  1 
ATOM   2377 N  NE2  . GLN   A 1 153 ? -22.094 -28.123 5.098   1.00 72.53  ? 150 GLN   A NE2  1 
ATOM   2378 H  H    . GLN   A 1 153 ? -18.751 -26.897 1.815   1.00 38.86  ? 150 GLN   A H    1 
ATOM   2379 H  HA   . GLN   A 1 153 ? -21.030 -27.378 0.613   1.00 39.69  ? 150 GLN   A HA   1 
ATOM   2380 H  HB2  . GLN   A 1 153 ? -21.080 -28.202 2.650   1.00 50.02  ? 150 GLN   A HB2  1 
ATOM   2381 H  HB3  . GLN   A 1 153 ? -20.279 -26.975 3.265   1.00 50.02  ? 150 GLN   A HB3  1 
ATOM   2382 H  HG2  . GLN   A 1 153 ? -22.269 -25.686 3.077   1.00 64.01  ? 150 GLN   A HG2  1 
ATOM   2383 H  HG3  . GLN   A 1 153 ? -23.031 -27.023 2.682   1.00 64.01  ? 150 GLN   A HG3  1 
ATOM   2384 H  HE21 . GLN   A 1 153 ? -21.703 -28.671 4.563   1.00 87.08  ? 150 GLN   A HE21 1 
ATOM   2385 H  HE22 . GLN   A 1 153 ? -22.206 -28.334 5.924   1.00 87.08  ? 150 GLN   A HE22 1 
ATOM   2386 N  N    . ILE   A 1 154 ? -20.593 -24.339 1.525   1.00 33.26  ? 151 ILE   A N    1 
ATOM   2387 C  CA   . ILE   A 1 154 ? -21.099 -22.986 1.375   1.00 35.74  ? 151 ILE   A CA   1 
ATOM   2388 C  C    . ILE   A 1 154 ? -20.987 -22.535 -0.076  1.00 32.63  ? 151 ILE   A C    1 
ATOM   2389 O  O    . ILE   A 1 154 ? -21.952 -22.034 -0.666  1.00 38.78  ? 151 ILE   A O    1 
ATOM   2390 C  CB   . ILE   A 1 154 ? -20.354 -22.027 2.329   1.00 37.23  ? 151 ILE   A CB   1 
ATOM   2391 C  CG1  . ILE   A 1 154 ? -20.573 -22.440 3.794   1.00 36.27  ? 151 ILE   A CG1  1 
ATOM   2392 C  CG2  . ILE   A 1 154 ? -20.795 -20.598 2.035   1.00 41.50  ? 151 ILE   A CG2  1 
ATOM   2393 C  CD1  . ILE   A 1 154 ? -19.634 -21.740 4.804   1.00 37.15  ? 151 ILE   A CD1  1 
ATOM   2394 H  H    . ILE   A 1 154 ? -19.871 -24.394 1.989   1.00 39.96  ? 151 ILE   A H    1 
ATOM   2395 H  HA   . ILE   A 1 154 ? -22.039 -22.978 1.617   1.00 42.93  ? 151 ILE   A HA   1 
ATOM   2396 H  HB   . ILE   A 1 154 ? -19.397 -22.081 2.178   1.00 44.72  ? 151 ILE   A HB   1 
ATOM   2397 H  HG12 . ILE   A 1 154 ? -21.485 -22.222 4.043   1.00 43.56  ? 151 ILE   A HG12 1 
ATOM   2398 H  HG13 . ILE   A 1 154 ? -20.426 -23.395 3.871   1.00 43.56  ? 151 ILE   A HG13 1 
ATOM   2399 H  HG21 . ILE   A 1 154 ? -20.559 -20.034 2.788   1.00 49.84  ? 151 ILE   A HG21 1 
ATOM   2400 H  HG22 . ILE   A 1 154 ? -20.344 -20.287 1.235   1.00 49.84  ? 151 ILE   A HG22 1 
ATOM   2401 H  HG23 . ILE   A 1 154 ? -21.755 -20.586 1.900   1.00 49.84  ? 151 ILE   A HG23 1 
ATOM   2402 H  HD11 . ILE   A 1 154 ? -19.741 -22.155 5.674   1.00 44.62  ? 151 ILE   A HD11 1 
ATOM   2403 H  HD12 . ILE   A 1 154 ? -18.717 -21.838 4.502   1.00 44.62  ? 151 ILE   A HD12 1 
ATOM   2404 H  HD13 . ILE   A 1 154 ? -19.868 -20.800 4.854   1.00 44.62  ? 151 ILE   A HD13 1 
ATOM   2405 N  N    . LEU   A 1 155 ? -19.799 -22.695 -0.673  1.00 35.74  ? 152 LEU   A N    1 
ATOM   2406 C  CA   . LEU   A 1 155 ? -19.554 -22.128 -1.994  1.00 31.88  ? 152 LEU   A CA   1 
ATOM   2407 C  C    . LEU   A 1 155 ? -20.173 -22.944 -3.111  1.00 36.58  ? 152 LEU   A C    1 
ATOM   2408 O  O    . LEU   A 1 155 ? -20.689 -22.381 -4.079  1.00 47.23  ? 152 LEU   A O    1 
ATOM   2409 C  CB   . LEU   A 1 155 ? -18.042 -22.017 -2.257  1.00 33.78  ? 152 LEU   A CB   1 
ATOM   2410 C  CG   . LEU   A 1 155 ? -17.212 -21.120 -1.367  1.00 46.93  ? 152 LEU   A CG   1 
ATOM   2411 C  CD1  . LEU   A 1 155 ? -15.802 -20.916 -1.914  1.00 44.74  ? 152 LEU   A CD1  1 
ATOM   2412 C  CD2  . LEU   A 1 155 ? -17.931 -19.822 -1.223  1.00 42.90  ? 152 LEU   A CD2  1 
ATOM   2413 H  H    . LEU   A 1 155 ? -19.132 -23.122 -0.336  1.00 42.93  ? 152 LEU   A H    1 
ATOM   2414 H  HA   . LEU   A 1 155 ? -19.954 -21.244 -1.999  1.00 38.30  ? 152 LEU   A HA   1 
ATOM   2415 H  HB2  . LEU   A 1 155 ? -17.666 -22.908 -2.177  1.00 40.58  ? 152 LEU   A HB2  1 
ATOM   2416 H  HB3  . LEU   A 1 155 ? -17.927 -21.689 -3.163  1.00 40.58  ? 152 LEU   A HB3  1 
ATOM   2417 H  HG   . LEU   A 1 155 ? -17.098 -21.531 -0.497  1.00 56.35  ? 152 LEU   A HG   1 
ATOM   2418 H  HD11 . LEU   A 1 155 ? -15.307 -20.345 -1.306  1.00 53.73  ? 152 LEU   A HD11 1 
ATOM   2419 H  HD12 . LEU   A 1 155 ? -15.364 -21.778 -1.988  1.00 53.73  ? 152 LEU   A HD12 1 
ATOM   2420 H  HD13 . LEU   A 1 155 ? -15.859 -20.498 -2.788  1.00 53.73  ? 152 LEU   A HD13 1 
ATOM   2421 H  HD21 . LEU   A 1 155 ? -17.324 -19.164 -0.849  1.00 51.52  ? 152 LEU   A HD21 1 
ATOM   2422 H  HD22 . LEU   A 1 155 ? -18.236 -19.531 -2.097  1.00 51.52  ? 152 LEU   A HD22 1 
ATOM   2423 H  HD23 . LEU   A 1 155 ? -18.690 -19.945 -0.632  1.00 51.52  ? 152 LEU   A HD23 1 
ATOM   2424 N  N    . THR   A 1 156 ? -20.088 -24.264 -3.025  1.00 50.62  ? 153 THR   A N    1 
ATOM   2425 C  CA   . THR   A 1 156 ? -20.453 -25.137 -4.133  1.00 50.08  ? 153 THR   A CA   1 
ATOM   2426 C  C    . THR   A 1 156 ? -21.883 -25.645 -4.003  1.00 50.09  ? 153 THR   A C    1 
ATOM   2427 O  O    . THR   A 1 156 ? -22.702 -25.440 -4.898  1.00 48.38  ? 153 THR   A O    1 
ATOM   2428 C  CB   . THR   A 1 156 ? -19.465 -26.312 -4.209  1.00 60.48  ? 153 THR   A CB   1 
ATOM   2429 O  OG1  . THR   A 1 156 ? -18.175 -25.820 -4.592  1.00 58.80  ? 153 THR   A OG1  1 
ATOM   2430 C  CG2  . THR   A 1 156 ? -19.936 -27.356 -5.206  1.00 59.06  ? 153 THR   A CG2  1 
ATOM   2431 H  H    . THR   A 1 156 ? -19.817 -24.685 -2.326  1.00 60.54  ? 153 THR   A H    1 
ATOM   2432 H  HA   . THR   A 1 156 ? -20.394 -24.638 -4.962  1.00 60.14  ? 153 THR   A HA   1 
ATOM   2433 H  HB   . THR   A 1 156 ? -19.403 -26.742 -3.341  1.00 72.61  ? 153 THR   A HB   1 
ATOM   2434 H  HG1  . THR   A 1 156 ? -17.620 -26.451 -4.610  1.00 70.60  ? 153 THR   A HG1  1 
ATOM   2435 H  HG21 . THR   A 1 156 ? -19.297 -28.085 -5.250  1.00 70.91  ? 153 THR   A HG21 1 
ATOM   2436 H  HG22 . THR   A 1 156 ? -20.798 -27.709 -4.934  1.00 70.91  ? 153 THR   A HG22 1 
ATOM   2437 H  HG23 . THR   A 1 156 ? -20.022 -26.959 -6.086  1.00 70.91  ? 153 THR   A HG23 1 
ATOM   2438 N  N    . GLU   A 1 157 ? -22.190 -26.320 -2.901  1.00 52.23  ? 154 GLU   A N    1 
ATOM   2439 C  CA   . GLU   A 1 157 ? -23.504 -26.930 -2.751  1.00 52.77  ? 154 GLU   A CA   1 
ATOM   2440 C  C    . GLU   A 1 157 ? -24.592 -25.874 -2.751  1.00 53.20  ? 154 GLU   A C    1 
ATOM   2441 O  O    . GLU   A 1 157 ? -25.618 -26.031 -3.419  1.00 50.61  ? 154 GLU   A O    1 
ATOM   2442 C  CB   . GLU   A 1 157 ? -23.547 -27.755 -1.468  1.00 55.84  ? 154 GLU   A CB   1 
ATOM   2443 C  CG   . GLU   A 1 157 ? -22.721 -29.020 -1.516  1.00 62.31  ? 154 GLU   A CG   1 
ATOM   2444 C  CD   . GLU   A 1 157 ? -22.887 -29.853 -0.264  1.00 67.11  ? 154 GLU   A CD   1 
ATOM   2445 O  OE1  . GLU   A 1 157 ? -22.907 -31.098 -0.367  1.00 85.72  ? 154 GLU   A OE1  1 
ATOM   2446 O  OE2  . GLU   A 1 157 ? -23.011 -29.257 0.824   1.00 82.36  ? 154 GLU   A OE2  1 
ATOM   2447 H  H    . GLU   A 1 157 ? -21.662 -26.439 -2.233  1.00 62.46  ? 154 GLU   A H    1 
ATOM   2448 H  HA   . GLU   A 1 157 ? -23.667 -27.529 -3.496  1.00 63.11  ? 154 GLU   A HA   1 
ATOM   2449 H  HB2  . GLU   A 1 157 ? -23.211 -27.212 -0.738  1.00 66.80  ? 154 GLU   A HB2  1 
ATOM   2450 H  HB3  . GLU   A 1 157 ? -24.467 -28.010 -1.295  1.00 66.80  ? 154 GLU   A HB3  1 
ATOM   2451 H  HG2  . GLU   A 1 157 ? -23.001 -29.555 -2.275  1.00 74.81  ? 154 GLU   A HG2  1 
ATOM   2452 H  HG3  . GLU   A 1 157 ? -21.784 -28.786 -1.602  1.00 74.81  ? 154 GLU   A HG3  1 
ATOM   2453 N  N    . GLY   A 1 158 ? -24.378 -24.775 -2.031  1.00 52.96  ? 155 GLY   A N    1 
ATOM   2454 C  CA   . GLY   A 1 158 ? -25.377 -23.723 -2.019  1.00 49.63  ? 155 GLY   A CA   1 
ATOM   2455 C  C    . GLY   A 1 158 ? -25.628 -23.158 -3.400  1.00 49.80  ? 155 GLY   A C    1 
ATOM   2456 O  O    . GLY   A 1 158 ? -26.771 -22.914 -3.785  1.00 47.08  ? 155 GLY   A O    1 
ATOM   2457 H  H    . GLY   A 1 158 ? -23.680 -24.621 -1.553  1.00 63.59  ? 155 GLY   A H    1 
ATOM   2458 H  HA2  . GLY   A 1 158 ? -26.213 -24.076 -1.676  1.00 59.35  ? 155 GLY   A HA2  1 
ATOM   2459 H  HA3  . GLY   A 1 158 ? -25.079 -23.002 -1.443  1.00 59.35  ? 155 GLY   A HA3  1 
ATOM   2460 N  N    . LEU   A 1 159 ? -24.564 -22.967 -4.177  1.00 48.66  ? 156 LEU   A N    1 
ATOM   2461 C  CA   . LEU   A 1 159 ? -24.726 -22.477 -5.543  1.00 46.64  ? 156 LEU   A CA   1 
ATOM   2462 C  C    . LEU   A 1 159 ? -25.472 -23.494 -6.396  1.00 45.07  ? 156 LEU   A C    1 
ATOM   2463 O  O    . LEU   A 1 159 ? -26.448 -23.154 -7.078  1.00 44.38  ? 156 LEU   A O    1 
ATOM   2464 C  CB   . LEU   A 1 159 ? -23.350 -22.164 -6.138  1.00 55.52  ? 156 LEU   A CB   1 
ATOM   2465 C  CG   . LEU   A 1 159 ? -23.228 -21.686 -7.589  1.00 45.77  ? 156 LEU   A CG   1 
ATOM   2466 C  CD1  . LEU   A 1 159 ? -23.606 -22.726 -8.616  1.00 60.86  ? 156 LEU   A CD1  1 
ATOM   2467 C  CD2  . LEU   A 1 159 ? -24.090 -20.440 -7.737  1.00 51.20  ? 156 LEU   A CD2  1 
ATOM   2468 H  H    . LEU   A 1 159 ? -23.750 -23.112 -3.941  1.00 58.43  ? 156 LEU   A H    1 
ATOM   2469 H  HA   . LEU   A 1 159 ? -25.245 -21.658 -5.536  1.00 56.02  ? 156 LEU   A HA   1 
ATOM   2470 H  HB2  . LEU   A 1 159 ? -22.954 -21.467 -5.592  1.00 66.66  ? 156 LEU   A HB2  1 
ATOM   2471 H  HB3  . LEU   A 1 159 ? -22.821 -22.975 -6.077  1.00 66.66  ? 156 LEU   A HB3  1 
ATOM   2472 H  HG   . LEU   A 1 159 ? -22.296 -21.494 -7.775  1.00 54.97  ? 156 LEU   A HG   1 
ATOM   2473 H  HD11 . LEU   A 1 159 ? -23.464 -22.359 -9.503  1.00 73.07  ? 156 LEU   A HD11 1 
ATOM   2474 H  HD12 . LEU   A 1 159 ? -23.050 -23.511 -8.490  1.00 73.07  ? 156 LEU   A HD12 1 
ATOM   2475 H  HD13 . LEU   A 1 159 ? -24.540 -22.959 -8.501  1.00 73.07  ? 156 LEU   A HD13 1 
ATOM   2476 H  HD21 . LEU   A 1 159 ? -24.021 -20.115 -8.648  1.00 61.48  ? 156 LEU   A HD21 1 
ATOM   2477 H  HD22 . LEU   A 1 159 ? -25.011 -20.667 -7.535  1.00 61.48  ? 156 LEU   A HD22 1 
ATOM   2478 H  HD23 . LEU   A 1 159 ? -23.774 -19.762 -7.119  1.00 61.48  ? 156 LEU   A HD23 1 
ATOM   2479 N  N    . GLU   A 1 160 ? -24.990 -24.737 -6.411  1.00 49.67  ? 157 GLU   A N    1 
ATOM   2480 C  CA   . GLU   A 1 160 ? -25.607 -25.794 -7.207  1.00 49.28  ? 157 GLU   A CA   1 
ATOM   2481 C  C    . GLU   A 1 160 ? -27.110 -25.885 -6.944  1.00 47.32  ? 157 GLU   A C    1 
ATOM   2482 O  O    . GLU   A 1 160 ? -27.918 -25.936 -7.880  1.00 46.89  ? 157 GLU   A O    1 
ATOM   2483 C  CB   . GLU   A 1 160 ? -24.901 -27.125 -6.914  1.00 50.62  ? 157 GLU   A CB   1 
ATOM   2484 C  CG   . GLU   A 1 160 ? -23.804 -27.569 -7.920  1.00 63.92  ? 157 GLU   A CG   1 
ATOM   2485 C  CD   . GLU   A 1 160 ? -22.755 -26.507 -8.264  1.00 70.02  ? 157 GLU   A CD   1 
ATOM   2486 O  OE1  . GLU   A 1 160 ? -22.843 -25.924 -9.362  1.00 73.65  ? 157 GLU   A OE1  1 
ATOM   2487 O  OE2  . GLU   A 1 160 ? -21.813 -26.291 -7.468  1.00 76.09  ? 157 GLU   A OE2  1 
ATOM   2488 H  H    . GLU   A 1 160 ? -24.301 -24.996 -5.967  1.00 59.64  ? 157 GLU   A H    1 
ATOM   2489 H  HA   . GLU   A 1 160 ? -25.496 -25.597 -8.150  1.00 59.18  ? 157 GLU   A HA   1 
ATOM   2490 H  HB2  . GLU   A 1 160 ? -24.477 -27.055 -6.045  1.00 60.78  ? 157 GLU   A HB2  1 
ATOM   2491 H  HB3  . GLU   A 1 160 ? -25.572 -27.825 -6.900  1.00 60.78  ? 157 GLU   A HB3  1 
ATOM   2492 H  HG2  . GLU   A 1 160 ? -23.332 -28.328 -7.543  1.00 76.74  ? 157 GLU   A HG2  1 
ATOM   2493 H  HG3  . GLU   A 1 160 ? -24.236 -27.826 -8.750  1.00 76.74  ? 157 GLU   A HG3  1 
ATOM   2494 N  N    . LYS   A 1 161 ? -27.513 -25.845 -5.674  1.00 46.26  ? 158 LYS   A N    1 
ATOM   2495 C  CA   . LYS   A 1 161 ? -28.922 -26.075 -5.354  1.00 46.71  ? 158 LYS   A CA   1 
ATOM   2496 C  C    . LYS   A 1 161 ? -29.779 -24.870 -5.734  1.00 48.28  ? 158 LYS   A C    1 
ATOM   2497 O  O    . LYS   A 1 161 ? -30.920 -25.021 -6.184  1.00 46.13  ? 158 LYS   A O    1 
ATOM   2498 C  CB   . LYS   A 1 161 ? -29.072 -26.419 -3.868  1.00 53.32  ? 158 LYS   A CB   1 
ATOM   2499 C  CG   . LYS   A 1 161 ? -28.201 -27.611 -3.432  1.00 67.18  ? 158 LYS   A CG   1 
ATOM   2500 C  CD   . LYS   A 1 161 ? -28.247 -27.896 -1.919  1.00 73.64  ? 158 LYS   A CD   1 
ATOM   2501 C  CE   . LYS   A 1 161 ? -27.523 -29.207 -1.569  1.00 75.81  ? 158 LYS   A CE   1 
ATOM   2502 N  NZ   . LYS   A 1 161 ? -27.417 -29.459 -0.100  1.00 82.20  ? 158 LYS   A NZ   1 
ATOM   2503 H  H    . LYS   A 1 161 ? -27.006 -25.691 -4.997  1.00 55.30  ? 158 LYS   A H    1 
ATOM   2504 H  HA   . LYS   A 1 161 ? -29.245 -26.834 -5.864  1.00 55.85  ? 158 LYS   A HA   1 
ATOM   2505 H  HB2  . LYS   A 1 161 ? -28.810 -25.649 -3.339  1.00 64.02  ? 158 LYS   A HB2  1 
ATOM   2506 H  HB3  . LYS   A 1 161 ? -29.998 -26.645 -3.689  1.00 64.02  ? 158 LYS   A HB3  1 
ATOM   2507 H  HG2  . LYS   A 1 161 ? -28.510 -28.408 -3.891  1.00 80.66  ? 158 LYS   A HG2  1 
ATOM   2508 H  HG3  . LYS   A 1 161 ? -27.279 -27.428 -3.670  1.00 80.66  ? 158 LYS   A HG3  1 
ATOM   2509 H  HD2  . LYS   A 1 161 ? -27.812 -27.171 -1.443  1.00 88.41  ? 158 LYS   A HD2  1 
ATOM   2510 H  HD3  . LYS   A 1 161 ? -29.171 -27.972 -1.634  1.00 88.41  ? 158 LYS   A HD3  1 
ATOM   2511 H  HE2  . LYS   A 1 161 ? -28.010 -29.948 -1.962  1.00 91.02  ? 158 LYS   A HE2  1 
ATOM   2512 H  HE3  . LYS   A 1 161 ? -26.623 -29.174 -1.929  1.00 91.02  ? 158 LYS   A HE3  1 
ATOM   2513 H  HZ1  . LYS   A 1 161 ? -26.978 -30.219 0.048   1.00 98.69  ? 158 LYS   A HZ1  1 
ATOM   2514 H  HZ2  . LYS   A 1 161 ? -26.979 -28.791 0.293   1.00 98.69  ? 158 LYS   A HZ2  1 
ATOM   2515 H  HZ3  . LYS   A 1 161 ? -28.230 -29.521 0.258   1.00 98.69  ? 158 LYS   A HZ3  1 
ATOM   2516 N  N    . GLY   A 1 162 ? -29.251 -23.662 -5.554  1.00 45.80  ? 159 GLY   A N    1 
ATOM   2517 C  CA   . GLY   A 1 162 ? -30.015 -22.482 -5.920  1.00 51.58  ? 159 GLY   A CA   1 
ATOM   2518 C  C    . GLY   A 1 162 ? -30.132 -22.297 -7.418  1.00 43.81  ? 159 GLY   A C    1 
ATOM   2519 O  O    . GLY   A 1 162 ? -31.115 -21.732 -7.904  1.00 43.90  ? 159 GLY   A O    1 
ATOM   2520 H  H    . GLY   A 1 162 ? -28.471 -23.505 -5.230  1.00 55.00  ? 159 GLY   A H    1 
ATOM   2521 H  HA2  . GLY   A 1 162 ? -30.909 -22.555 -5.552  1.00 61.93  ? 159 GLY   A HA2  1 
ATOM   2522 H  HA3  . GLY   A 1 162 ? -29.584 -21.696 -5.549  1.00 61.93  ? 159 GLY   A HA3  1 
ATOM   2523 N  N    . MET   A 1 163 ? -29.128 -22.750 -8.172  1.00 45.19  ? 160 MET   A N    1 
ATOM   2524 C  CA   . MET   A 1 163 ? -29.257 -22.697 -9.626  1.00 45.68  ? 160 MET   A CA   1 
ATOM   2525 C  C    . MET   A 1 163 ? -30.308 -23.690 -10.104 1.00 41.56  ? 160 MET   A C    1 
ATOM   2526 O  O    . MET   A 1 163 ? -31.040 -23.410 -11.058 1.00 38.81  ? 160 MET   A O    1 
ATOM   2527 C  CB   . MET   A 1 163 ? -27.927 -22.984 -10.313 1.00 44.06  ? 160 MET   A CB   1 
ATOM   2528 C  CG   . MET   A 1 163 ? -26.930 -21.831 -10.371 1.00 46.21  ? 160 MET   A CG   1 
ATOM   2529 S  SD   . MET   A 1 163 ? -27.627 -20.200 -10.672 1.00 46.67  ? 160 MET   A SD   1 
ATOM   2530 C  CE   . MET   A 1 163 ? -27.630 -20.160 -12.466 1.00 53.31  ? 160 MET   A CE   1 
ATOM   2531 H  H    . MET   A 1 163 ? -28.391 -23.080 -7.877  1.00 54.27  ? 160 MET   A H    1 
ATOM   2532 H  HA   . MET   A 1 163 ? -29.515 -21.794 -9.867  1.00 54.86  ? 160 MET   A HA   1 
ATOM   2533 H  HB2  . MET   A 1 163 ? -27.494 -23.712 -9.840  1.00 52.92  ? 160 MET   A HB2  1 
ATOM   2534 H  HB3  . MET   A 1 163 ? -28.112 -23.247 -11.229 1.00 52.92  ? 160 MET   A HB3  1 
ATOM   2535 H  HG2  . MET   A 1 163 ? -26.463 -21.791 -9.522  1.00 55.49  ? 160 MET   A HG2  1 
ATOM   2536 H  HG3  . MET   A 1 163 ? -26.300 -22.010 -11.087 1.00 55.49  ? 160 MET   A HG3  1 
ATOM   2537 H  HE1  . MET   A 1 163 ? -28.037 -19.332 -12.763 1.00 64.01  ? 160 MET   A HE1  1 
ATOM   2538 H  HE2  . MET   A 1 163 ? -26.715 -20.211 -12.785 1.00 64.01  ? 160 MET   A HE2  1 
ATOM   2539 H  HE3  . MET   A 1 163 ? -28.138 -20.917 -12.798 1.00 64.01  ? 160 MET   A HE3  1 
ATOM   2540 N  N    . LYS   A 1 164 ? -30.390 -24.864 -9.472  1.00 43.02  ? 161 LYS   A N    1 
ATOM   2541 C  CA   . LYS   A 1 164 ? -31.460 -25.798 -9.827  1.00 40.55  ? 161 LYS   A CA   1 
ATOM   2542 C  C    . LYS   A 1 164 ? -32.821 -25.175 -9.528  1.00 45.55  ? 161 LYS   A C    1 
ATOM   2543 O  O    . LYS   A 1 164 ? -33.721 -25.213 -10.359 1.00 41.38  ? 161 LYS   A O    1 
ATOM   2544 C  CB   . LYS   A 1 164 ? -31.273 -27.128 -9.091  1.00 51.83  ? 161 LYS   A CB   1 
ATOM   2545 C  CG   . LYS   A 1 164 ? -32.018 -28.337 -9.703  1.00 65.47  ? 161 LYS   A CG   1 
ATOM   2546 C  CD   . LYS   A 1 164 ? -31.869 -28.490 -11.236 1.00 68.02  ? 161 LYS   A CD   1 
ATOM   2547 C  CE   . LYS   A 1 164 ? -30.434 -28.779 -11.688 1.00 73.78  ? 161 LYS   A CE   1 
ATOM   2548 N  NZ   . LYS   A 1 164 ? -30.137 -30.239 -11.846 1.00 70.54  ? 161 LYS   A NZ   1 
ATOM   2549 H  H    . LYS   A 1 164 ? -29.857 -25.134 -8.854  1.00 51.66  ? 161 LYS   A H    1 
ATOM   2550 H  HA   . LYS   A 1 164 ? -31.418 -25.995 -10.776 1.00 48.45  ? 161 LYS   A HA   1 
ATOM   2551 H  HB2  . LYS   A 1 164 ? -30.327 -27.344 -9.087  1.00 62.24  ? 161 LYS   A HB2  1 
ATOM   2552 H  HB3  . LYS   A 1 164 ? -31.593 -27.022 -8.182  1.00 62.24  ? 161 LYS   A HB3  1 
ATOM   2553 H  HG2  . LYS   A 1 164 ? -31.675 -29.148 -9.297  1.00 78.61  ? 161 LYS   A HG2  1 
ATOM   2554 H  HG3  . LYS   A 1 164 ? -32.964 -28.244 -9.512  1.00 78.61  ? 161 LYS   A HG3  1 
ATOM   2555 H  HD2  . LYS   A 1 164 ? -32.427 -29.226 -11.533 1.00 81.67  ? 161 LYS   A HD2  1 
ATOM   2556 H  HD3  . LYS   A 1 164 ? -32.153 -27.665 -11.662 1.00 81.67  ? 161 LYS   A HD3  1 
ATOM   2557 H  HE2  . LYS   A 1 164 ? -30.285 -28.352 -12.546 1.00 88.57  ? 161 LYS   A HE2  1 
ATOM   2558 H  HE3  . LYS   A 1 164 ? -29.820 -28.421 -11.028 1.00 88.57  ? 161 LYS   A HE3  1 
ATOM   2559 H  HZ1  . LYS   A 1 164 ? -29.293 -30.351 -12.106 1.00 84.69  ? 161 LYS   A HZ1  1 
ATOM   2560 H  HZ2  . LYS   A 1 164 ? -30.259 -30.660 -11.071 1.00 84.69  ? 161 LYS   A HZ2  1 
ATOM   2561 H  HZ3  . LYS   A 1 164 ? -30.677 -30.596 -12.457 1.00 84.69  ? 161 LYS   A HZ3  1 
ATOM   2562 N  N    . THR   A 1 165 ? -32.972 -24.553 -8.357  1.00 43.21  ? 162 THR   A N    1 
ATOM   2563 C  CA   . THR   A 1 165 ? -34.219 -23.854 -8.055  1.00 44.60  ? 162 THR   A CA   1 
ATOM   2564 C  C    . THR   A 1 165 ? -34.516 -22.777 -9.090  1.00 40.05  ? 162 THR   A C    1 
ATOM   2565 O  O    . THR   A 1 165 ? -35.659 -22.616 -9.521  1.00 37.17  ? 162 THR   A O    1 
ATOM   2566 C  CB   . THR   A 1 165 ? -34.163 -23.222 -6.664  1.00 41.53  ? 162 THR   A CB   1 
ATOM   2567 O  OG1  . THR   A 1 165 ? -33.891 -24.236 -5.688  1.00 49.06  ? 162 THR   A OG1  1 
ATOM   2568 C  CG2  . THR   A 1 165 ? -35.477 -22.499 -6.348  1.00 48.07  ? 162 THR   A CG2  1 
ATOM   2569 H  H    . THR   A 1 165 ? -32.381 -24.522 -7.734  1.00 51.89  ? 162 THR   A H    1 
ATOM   2570 H  HA   . THR   A 1 165 ? -34.936 -24.508 -8.065  1.00 53.56  ? 162 THR   A HA   1 
ATOM   2571 H  HB   . THR   A 1 165 ? -33.454 -22.561 -6.627  1.00 49.63  ? 162 THR   A HB   1 
ATOM   2572 H  HG1  . THR   A 1 165 ? -33.098 -24.502 -5.763  1.00 58.92  ? 162 THR   A HG1  1 
ATOM   2573 H  HG21 . THR   A 1 165 ? -35.477 -22.197 -5.426  1.00 57.73  ? 162 THR   A HG21 1 
ATOM   2574 H  HG22 . THR   A 1 165 ? -35.582 -21.731 -6.930  1.00 57.73  ? 162 THR   A HG22 1 
ATOM   2575 H  HG23 . THR   A 1 165 ? -36.227 -23.100 -6.481  1.00 57.73  ? 162 THR   A HG23 1 
ATOM   2576 N  N    . PHE   A 1 166 ? -33.506 -21.993 -9.468  1.00 36.83  ? 163 PHE   A N    1 
ATOM   2577 C  CA   . PHE   A 1 166 ? -33.743 -20.969 -10.473 1.00 34.78  ? 163 PHE   A CA   1 
ATOM   2578 C  C    . PHE   A 1 166 ? -34.242 -21.604 -11.764 1.00 36.78  ? 163 PHE   A C    1 
ATOM   2579 O  O    . PHE   A 1 166 ? -35.217 -21.134 -12.371 1.00 32.87  ? 163 PHE   A O    1 
ATOM   2580 C  CB   . PHE   A 1 166 ? -32.470 -20.162 -10.694 1.00 38.16  ? 163 PHE   A CB   1 
ATOM   2581 C  CG   . PHE   A 1 166 ? -32.593 -19.118 -11.743 1.00 41.09  ? 163 PHE   A CG   1 
ATOM   2582 C  CD1  . PHE   A 1 166 ? -32.074 -19.332 -13.000 1.00 43.97  ? 163 PHE   A CD1  1 
ATOM   2583 C  CD2  . PHE   A 1 166 ? -33.215 -17.910 -11.465 1.00 48.45  ? 163 PHE   A CD2  1 
ATOM   2584 C  CE1  . PHE   A 1 166 ? -32.185 -18.365 -13.985 1.00 44.37  ? 163 PHE   A CE1  1 
ATOM   2585 C  CE2  . PHE   A 1 166 ? -33.329 -16.934 -12.443 1.00 52.90  ? 163 PHE   A CE2  1 
ATOM   2586 C  CZ   . PHE   A 1 166 ? -32.806 -17.158 -13.698 1.00 42.12  ? 163 PHE   A CZ   1 
ATOM   2587 H  H    . PHE   A 1 166 ? -32.702 -22.035 -9.166  1.00 44.24  ? 163 PHE   A H    1 
ATOM   2588 H  HA   . PHE   A 1 166 ? -34.424 -20.350 -10.165 1.00 41.52  ? 163 PHE   A HA   1 
ATOM   2589 H  HB2  . PHE   A 1 166 ? -32.233 -19.720 -9.864  1.00 45.84  ? 163 PHE   A HB2  1 
ATOM   2590 H  HB3  . PHE   A 1 166 ? -31.760 -20.767 -10.962 1.00 45.84  ? 163 PHE   A HB3  1 
ATOM   2591 H  HD1  . PHE   A 1 166 ? -31.645 -20.135 -13.190 1.00 52.81  ? 163 PHE   A HD1  1 
ATOM   2592 H  HD2  . PHE   A 1 166 ? -33.558 -17.753 -10.615 1.00 58.18  ? 163 PHE   A HD2  1 
ATOM   2593 H  HE1  . PHE   A 1 166 ? -31.843 -18.524 -14.835 1.00 53.29  ? 163 PHE   A HE1  1 
ATOM   2594 H  HE2  . PHE   A 1 166 ? -33.757 -16.131 -12.253 1.00 63.52  ? 163 PHE   A HE2  1 
ATOM   2595 H  HZ   . PHE   A 1 166 ? -32.871 -16.501 -14.353 1.00 50.58  ? 163 PHE   A HZ   1 
ATOM   2596 N  N    . GLY   A 1 167 ? -33.617 -22.704 -12.178 1.00 34.57  ? 164 GLY   A N    1 
ATOM   2597 C  CA   . GLY   A 1 167 ? -34.084 -23.395 -13.370 1.00 35.74  ? 164 GLY   A CA   1 
ATOM   2598 C  C    . GLY   A 1 167 ? -35.528 -23.850 -13.260 1.00 38.27  ? 164 GLY   A C    1 
ATOM   2599 O  O    . GLY   A 1 167 ? -36.327 -23.634 -14.172 1.00 35.49  ? 164 GLY   A O    1 
ATOM   2600 H  H    . GLY   A 1 167 ? -32.935 -23.062 -11.795 1.00 41.28  ? 164 GLY   A H    1 
ATOM   2601 H  HA2  . GLY   A 1 167 ? -34.009 -22.802 -14.134 1.00 42.93  ? 164 GLY   A HA2  1 
ATOM   2602 H  HA3  . GLY   A 1 167 ? -33.530 -24.177 -13.523 1.00 42.93  ? 164 GLY   A HA3  1 
ATOM   2603 N  N    . GLU   A 1 168 ? -35.884 -24.470 -12.128 1.00 36.15  ? 165 GLU   A N    1 
ATOM   2604 C  CA   . GLU   A 1 168 ? -37.262 -24.930 -11.927 1.00 36.86  ? 165 GLU   A CA   1 
ATOM   2605 C  C    . GLU   A 1 168 ? -38.242 -23.758 -11.865 1.00 38.19  ? 165 GLU   A C    1 
ATOM   2606 O  O    . GLU   A 1 168 ? -39.366 -23.855 -12.360 1.00 39.44  ? 165 GLU   A O    1 
ATOM   2607 C  CB   . GLU   A 1 168 ? -37.377 -25.764 -10.642 1.00 44.32  ? 165 GLU   A CB   1 
ATOM   2608 C  CG   . GLU   A 1 168 ? -36.283 -26.806 -10.464 1.00 56.86  ? 165 GLU   A CG   1 
ATOM   2609 C  CD   . GLU   A 1 168 ? -36.404 -27.598 -9.153  1.00 76.35  ? 165 GLU   A CD   1 
ATOM   2610 O  OE1  . GLU   A 1 168 ? -37.438 -27.492 -8.468  1.00 73.52  ? 165 GLU   A OE1  1 
ATOM   2611 O  OE2  . GLU   A 1 168 ? -35.448 -28.323 -8.806  1.00 80.72  ? 165 GLU   A OE2  1 
ATOM   2612 H  H    . GLU   A 1 168 ? -35.354 -24.636 -11.471 1.00 43.17  ? 165 GLU   A H    1 
ATOM   2613 H  HA   . GLU   A 1 168 ? -37.498 -25.494 -12.679 1.00 44.02  ? 165 GLU   A HA   1 
ATOM   2614 H  HB2  . GLU   A 1 168 ? -37.338 -25.165 -9.880  1.00 53.23  ? 165 GLU   A HB2  1 
ATOM   2615 H  HB3  . GLU   A 1 168 ? -38.227 -26.232 -10.653 1.00 53.23  ? 165 GLU   A HB3  1 
ATOM   2616 H  HG2  . GLU   A 1 168 ? -36.328 -27.438 -11.198 1.00 68.27  ? 165 GLU   A HG2  1 
ATOM   2617 H  HG3  . GLU   A 1 168 ? -35.421 -26.360 -10.463 1.00 68.27  ? 165 GLU   A HG3  1 
ATOM   2618 N  N    . THR   A 1 169 ? -37.849 -22.654 -11.220 1.00 35.32  ? 166 THR   A N    1 
ATOM   2619 C  CA   . THR   A 1 169 ? -38.751 -21.506 -11.102 1.00 35.12  ? 166 THR   A CA   1 
ATOM   2620 C  C    . THR   A 1 169 ? -39.124 -20.952 -12.475 1.00 38.25  ? 166 THR   A C    1 
ATOM   2621 O  O    . THR   A 1 169 ? -40.276 -20.577 -12.711 1.00 37.04  ? 166 THR   A O    1 
ATOM   2622 C  CB   . THR   A 1 169 ? -38.095 -20.420 -10.241 1.00 38.94  ? 166 THR   A CB   1 
ATOM   2623 O  OG1  . THR   A 1 169 ? -37.908 -20.911 -8.903  1.00 38.49  ? 166 THR   A OG1  1 
ATOM   2624 C  CG2  . THR   A 1 169 ? -38.950 -19.146 -10.190 1.00 43.47  ? 166 THR   A CG2  1 
ATOM   2625 H  H    . THR   A 1 169 ? -37.080 -22.546 -10.850 1.00 42.17  ? 166 THR   A H    1 
ATOM   2626 H  HA   . THR   A 1 169 ? -39.569 -21.790 -10.665 1.00 42.19  ? 166 THR   A HA   1 
ATOM   2627 H  HB   . THR   A 1 169 ? -37.239 -20.189 -10.633 1.00 46.77  ? 166 THR   A HB   1 
ATOM   2628 H  HG1  . THR   A 1 169 ? -37.418 -21.593 -8.913  1.00 46.23  ? 166 THR   A HG1  1 
ATOM   2629 H  HG21 . THR   A 1 169 ? -38.590 -18.531 -9.532  1.00 52.21  ? 166 THR   A HG21 1 
ATOM   2630 H  HG22 . THR   A 1 169 ? -38.951 -18.712 -11.058 1.00 52.21  ? 166 THR   A HG22 1 
ATOM   2631 H  HG23 . THR   A 1 169 ? -39.863 -19.368 -9.948  1.00 52.21  ? 166 THR   A HG23 1 
ATOM   2632 N  N    . LEU   A 1 170 ? -38.179 -20.921 -13.401 1.00 31.63  ? 167 LEU   A N    1 
ATOM   2633 C  CA   . LEU   A 1 170 ? -38.418 -20.406 -14.745 1.00 30.10  ? 167 LEU   A CA   1 
ATOM   2634 C  C    . LEU   A 1 170 ? -38.963 -21.466 -15.706 1.00 31.29  ? 167 LEU   A C    1 
ATOM   2635 O  O    . LEU   A 1 170 ? -39.219 -21.155 -16.871 1.00 29.09  ? 167 LEU   A O    1 
ATOM   2636 C  CB   . LEU   A 1 170 ? -37.114 -19.807 -15.286 1.00 29.40  ? 167 LEU   A CB   1 
ATOM   2637 C  CG   . LEU   A 1 170 ? -36.917 -18.346 -14.869 1.00 33.21  ? 167 LEU   A CG   1 
ATOM   2638 C  CD1  . LEU   A 1 170 ? -36.643 -18.264 -13.357 1.00 42.22  ? 167 LEU   A CD1  1 
ATOM   2639 C  CD2  . LEU   A 1 170 ? -35.811 -17.650 -15.663 1.00 40.00  ? 167 LEU   A CD2  1 
ATOM   2640 H  H    . LEU   A 1 170 ? -37.374 -21.197 -13.275 1.00 37.75  ? 167 LEU   A H    1 
ATOM   2641 H  HA   . LEU   A 1 170 ? -39.082 -19.700 -14.710 1.00 35.94  ? 167 LEU   A HA   1 
ATOM   2642 H  HB2  . LEU   A 1 170 ? -36.365 -20.321 -14.946 1.00 35.07  ? 167 LEU   A HB2  1 
ATOM   2643 H  HB3  . LEU   A 1 170 ? -37.128 -19.844 -16.256 1.00 35.07  ? 167 LEU   A HB3  1 
ATOM   2644 H  HG   . LEU   A 1 170 ? -37.734 -17.864 -15.068 1.00 39.89  ? 167 LEU   A HG   1 
ATOM   2645 H  HD11 . LEU   A 1 170 ? -36.474 -17.340 -13.116 1.00 50.71  ? 167 LEU   A HD11 1 
ATOM   2646 H  HD12 . LEU   A 1 170 ? -37.419 -18.594 -12.877 1.00 50.71  ? 167 LEU   A HD12 1 
ATOM   2647 H  HD13 . LEU   A 1 170 ? -35.868 -18.808 -13.146 1.00 50.71  ? 167 LEU   A HD13 1 
ATOM   2648 H  HD21 . LEU   A 1 170 ? -35.742 -16.729 -15.367 1.00 48.04  ? 167 LEU   A HD21 1 
ATOM   2649 H  HD22 . LEU   A 1 170 ? -34.972 -18.111 -15.508 1.00 48.04  ? 167 LEU   A HD22 1 
ATOM   2650 H  HD23 . LEU   A 1 170 ? -36.035 -17.678 -16.607 1.00 48.04  ? 167 LEU   A HD23 1 
ATOM   2651 N  N    . ASN   A 1 171 ? -39.170 -22.698 -15.237 1.00 33.12  ? 168 ASN   A N    1 
ATOM   2652 C  CA   . ASN   A 1 171 ? -39.608 -23.830 -16.073 1.00 32.02  ? 168 ASN   A CA   1 
ATOM   2653 C  C    . ASN   A 1 171 ? -38.736 -24.013 -17.317 1.00 31.52  ? 168 ASN   A C    1 
ATOM   2654 O  O    . ASN   A 1 171 ? -39.221 -24.182 -18.443 1.00 31.10  ? 168 ASN   A O    1 
ATOM   2655 C  CB   . ASN   A 1 171 ? -41.079 -23.696 -16.477 1.00 37.68  ? 168 ASN   A CB   1 
ATOM   2656 C  CG   . ASN   A 1 171 ? -41.745 -25.050 -16.703 1.00 59.62  ? 168 ASN   A CG   1 
ATOM   2657 O  OD1  . ASN   A 1 171 ? -41.439 -26.027 -16.013 1.00 61.50  ? 168 ASN   A OD1  1 
ATOM   2658 N  ND2  . ASN   A 1 171 ? -42.660 -25.110 -17.668 1.00 56.42  ? 168 ASN   A ND2  1 
ATOM   2659 H  H    . ASN   A 1 171 ? -39.062 -22.915 -14.412 1.00 39.79  ? 168 ASN   A H    1 
ATOM   2660 H  HA   . ASN   A 1 171 ? -39.506 -24.626 -15.528 1.00 38.22  ? 168 ASN   A HA   1 
ATOM   2661 H  HB2  . ASN   A 1 171 ? -41.562 -23.237 -15.772 1.00 45.26  ? 168 ASN   A HB2  1 
ATOM   2662 H  HB3  . ASN   A 1 171 ? -41.137 -23.190 -17.302 1.00 45.26  ? 168 ASN   A HB3  1 
ATOM   2663 H  HD21 . ASN   A 1 171 ? -42.849 -24.407 -18.126 1.00 67.75  ? 168 ASN   A HD21 1 
ATOM   2664 H  HD22 . ASN   A 1 171 ? -43.063 -25.851 -17.833 1.00 67.75  ? 168 ASN   A HD22 1 
ATOM   2665 N  N    . ILE   A 1 172 ? -37.424 -24.048 -17.096 1.00 32.19  ? 169 ILE   A N    1 
ATOM   2666 C  CA   . ILE   A 1 172 ? -36.483 -24.262 -18.192 1.00 32.81  ? 169 ILE   A CA   1 
ATOM   2667 C  C    . ILE   A 1 172 ? -36.625 -25.685 -18.722 1.00 33.37  ? 169 ILE   A C    1 
ATOM   2668 O  O    . ILE   A 1 172 ? -36.866 -26.640 -17.964 1.00 34.81  ? 169 ILE   A O    1 
ATOM   2669 C  CB   . ILE   A 1 172 ? -35.047 -23.978 -17.711 1.00 40.41  ? 169 ILE   A CB   1 
ATOM   2670 C  CG1  . ILE   A 1 172 ? -34.851 -22.473 -17.493 1.00 43.79  ? 169 ILE   A CG1  1 
ATOM   2671 C  CG2  . ILE   A 1 172 ? -34.023 -24.531 -18.696 1.00 45.72  ? 169 ILE   A CG2  1 
ATOM   2672 C  CD1  . ILE   A 1 172 ? -34.740 -21.643 -18.790 1.00 51.21  ? 169 ILE   A CD1  1 
ATOM   2673 H  H    . ILE   A 1 172 ? -37.055 -23.950 -16.326 1.00 38.67  ? 169 ILE   A H    1 
ATOM   2674 H  HA   . ILE   A 1 172 ? -36.687 -23.653 -18.918 1.00 39.41  ? 169 ILE   A HA   1 
ATOM   2675 H  HB   . ILE   A 1 172 ? -34.912 -24.429 -16.863 1.00 48.53  ? 169 ILE   A HB   1 
ATOM   2676 H  HG12 . ILE   A 1 172 ? -35.610 -22.133 -16.993 1.00 52.58  ? 169 ILE   A HG12 1 
ATOM   2677 H  HG13 . ILE   A 1 172 ? -34.034 -22.338 -16.989 1.00 52.58  ? 169 ILE   A HG13 1 
ATOM   2678 H  HG21 . ILE   A 1 172 ? -33.131 -24.322 -18.376 1.00 54.90  ? 169 ILE   A HG21 1 
ATOM   2679 H  HG22 . ILE   A 1 172 ? -34.134 -25.492 -18.761 1.00 54.90  ? 169 ILE   A HG22 1 
ATOM   2680 H  HG23 . ILE   A 1 172 ? -34.166 -24.122 -19.564 1.00 54.90  ? 169 ILE   A HG23 1 
ATOM   2681 H  HD11 . ILE   A 1 172 ? -34.638 -20.707 -18.558 1.00 61.50  ? 169 ILE   A HD11 1 
ATOM   2682 H  HD12 . ILE   A 1 172 ? -33.967 -21.945 -19.292 1.00 61.50  ? 169 ILE   A HD12 1 
ATOM   2683 H  HD13 . ILE   A 1 172 ? -35.546 -21.768 -19.315 1.00 61.50  ? 169 ILE   A HD13 1 
ATOM   2684 N  N    . ALA   A 1 173 ? -36.443 -25.844 -20.036 1.00 33.37  ? 170 ALA   A N    1 
ATOM   2685 C  CA   . ALA   A 1 173 ? -36.594 -27.160 -20.656 1.00 35.05  ? 170 ALA   A CA   1 
ATOM   2686 C  C    . ALA   A 1 173 ? -35.378 -28.058 -20.404 1.00 36.91  ? 170 ALA   A C    1 
ATOM   2687 O  O    . ALA   A 1 173 ? -34.255 -27.567 -20.238 1.00 36.70  ? 170 ALA   A O    1 
ATOM   2688 C  CB   . ALA   A 1 173 ? -36.811 -26.995 -22.159 1.00 43.57  ? 170 ALA   A CB   1 
ATOM   2689 H  H    . ALA   A 1 173 ? -36.235 -25.213 -20.583 1.00 39.84  ? 170 ALA   A H    1 
ATOM   2690 H  HA   . ALA   A 1 173 ? -37.361 -27.608 -20.267 1.00 41.86  ? 170 ALA   A HA   1 
ATOM   2691 H  HB1  . ALA   A 1 173 ? -36.853 -27.873 -22.570 1.00 52.32  ? 170 ALA   A HB1  1 
ATOM   2692 H  HB2  . ALA   A 1 173 ? -37.643 -26.519 -22.308 1.00 52.32  ? 170 ALA   A HB2  1 
ATOM   2693 H  HB3  . ALA   A 1 173 ? -36.071 -26.491 -22.532 1.00 52.32  ? 170 ALA   A HB3  1 
ATOM   2694 N  N    . PRO   A 1 174 ? -35.572 -29.383 -20.388 1.00 38.95  ? 171 PRO   A N    1 
ATOM   2695 C  CA   . PRO   A 1 174 ? -34.443 -30.282 -20.088 1.00 41.04  ? 171 PRO   A CA   1 
ATOM   2696 C  C    . PRO   A 1 174 ? -33.219 -30.084 -20.973 1.00 41.40  ? 171 PRO   A C    1 
ATOM   2697 O  O    . PRO   A 1 174 ? -32.090 -30.146 -20.467 1.00 45.40  ? 171 PRO   A O    1 
ATOM   2698 C  CB   . PRO   A 1 174 ? -35.048 -31.679 -20.297 1.00 47.95  ? 171 PRO   A CB   1 
ATOM   2699 C  CG   . PRO   A 1 174 ? -36.495 -31.508 -19.975 1.00 45.79  ? 171 PRO   A CG   1 
ATOM   2700 C  CD   . PRO   A 1 174 ? -36.873 -30.079 -20.338 1.00 51.06  ? 171 PRO   A CD   1 
ATOM   2701 H  HA   . PRO   A 1 174 ? -34.189 -30.158 -19.160 1.00 49.03  ? 171 PRO   A HA   1 
ATOM   2702 H  HB2  . PRO   A 1 174 ? -34.925 -31.961 -21.217 1.00 57.58  ? 171 PRO   A HB2  1 
ATOM   2703 H  HB3  . PRO   A 1 174 ? -34.630 -32.316 -19.696 1.00 57.58  ? 171 PRO   A HB3  1 
ATOM   2704 H  HG2  . PRO   A 1 174 ? -37.016 -32.138 -20.496 1.00 54.99  ? 171 PRO   A HG2  1 
ATOM   2705 H  HG3  . PRO   A 1 174 ? -36.634 -31.664 -19.028 1.00 54.99  ? 171 PRO   A HG3  1 
ATOM   2706 H  HD2  . PRO   A 1 174 ? -37.314 -30.048 -21.201 1.00 61.32  ? 171 PRO   A HD2  1 
ATOM   2707 H  HD3  . PRO   A 1 174 ? -37.446 -29.691 -19.658 1.00 61.32  ? 171 PRO   A HD3  1 
ATOM   2708 N  N    . ILE   A 1 175 ? -33.409 -29.837 -22.270 1.00 45.81  ? 172 ILE   A N    1 
ATOM   2709 C  CA   . ILE   A 1 175 ? -32.261 -29.678 -23.159 1.00 53.91  ? 172 ILE   A CA   1 
ATOM   2710 C  C    . ILE   A 1 175 ? -31.430 -28.471 -22.744 1.00 44.41  ? 172 ILE   A C    1 
ATOM   2711 O  O    . ILE   A 1 175 ? -30.203 -28.474 -22.868 1.00 42.54  ? 172 ILE   A O    1 
ATOM   2712 C  CB   . ILE   A 1 175 ? -32.714 -29.553 -24.625 1.00 49.02  ? 172 ILE   A CB   1 
ATOM   2713 C  CG1  . ILE   A 1 175 ? -33.733 -28.421 -24.765 1.00 57.20  ? 172 ILE   A CG1  1 
ATOM   2714 C  CG2  . ILE   A 1 175 ? -33.253 -30.888 -25.130 1.00 72.43  ? 172 ILE   A CG2  1 
ATOM   2715 C  CD1  . ILE   A 1 175 ? -34.043 -28.042 -26.195 1.00 64.27  ? 172 ILE   A CD1  1 
ATOM   2716 H  H    . ILE   A 1 175 ? -34.176 -29.758 -22.651 1.00 55.01  ? 172 ILE   A H    1 
ATOM   2717 H  HA   . ILE   A 1 175 ? -31.713 -30.475 -23.080 1.00 64.73  ? 172 ILE   A HA   1 
ATOM   2718 H  HB   . ILE   A 1 175 ? -31.951 -29.325 -25.178 1.00 58.87  ? 172 ILE   A HB   1 
ATOM   2719 H  HG12 . ILE   A 1 175 ? -34.563 -28.697 -24.347 1.00 68.69  ? 172 ILE   A HG12 1 
ATOM   2720 H  HG13 . ILE   A 1 175 ? -33.383 -27.632 -24.321 1.00 68.69  ? 172 ILE   A HG13 1 
ATOM   2721 H  HG21 . ILE   A 1 175 ? -34.124 -30.745 -25.533 1.00 86.96  ? 172 ILE   A HG21 1 
ATOM   2722 H  HG22 . ILE   A 1 175 ? -32.639 -31.248 -25.788 1.00 86.96  ? 172 ILE   A HG22 1 
ATOM   2723 H  HG23 . ILE   A 1 175 ? -33.332 -31.500 -24.382 1.00 86.96  ? 172 ILE   A HG23 1 
ATOM   2724 H  HD11 . ILE   A 1 175 ? -34.647 -27.283 -26.197 1.00 77.17  ? 172 ILE   A HD11 1 
ATOM   2725 H  HD12 . ILE   A 1 175 ? -33.216 -27.809 -26.646 1.00 77.17  ? 172 ILE   A HD12 1 
ATOM   2726 H  HD13 . ILE   A 1 175 ? -34.459 -28.798 -26.638 1.00 77.17  ? 172 ILE   A HD13 1 
ATOM   2727 N  N    . ASP   A 1 176 ? -32.085 -27.404 -22.283 1.00 40.28  ? 173 ASP   A N    1 
ATOM   2728 C  CA   . ASP   A 1 176 ? -31.326 -26.247 -21.821 1.00 37.11  ? 173 ASP   A CA   1 
ATOM   2729 C  C    . ASP   A 1 176 ? -30.720 -26.486 -20.444 1.00 43.27  ? 173 ASP   A C    1 
ATOM   2730 O  O    . ASP   A 1 176 ? -29.555 -26.148 -20.212 1.00 42.03  ? 173 ASP   A O    1 
ATOM   2731 C  CB   . ASP   A 1 176 ? -32.197 -24.989 -21.789 1.00 34.66  ? 173 ASP   A CB   1 
ATOM   2732 C  CG   . ASP   A 1 176 ? -32.681 -24.577 -23.158 1.00 36.43  ? 173 ASP   A CG   1 
ATOM   2733 O  OD1  . ASP   A 1 176 ? -31.833 -24.418 -24.055 1.00 35.13  ? 173 ASP   A OD1  1 
ATOM   2734 O  OD2  . ASP   A 1 176 ? -33.895 -24.334 -23.336 1.00 33.22  ? 173 ASP   A OD2  1 
ATOM   2735 H  H    . ASP   A 1 176 ? -32.940 -27.329 -22.230 1.00 48.38  ? 173 ASP   A H    1 
ATOM   2736 H  HA   . ASP   A 1 176 ? -30.609 -26.093 -22.456 1.00 44.57  ? 173 ASP   A HA   1 
ATOM   2737 H  HB2  . ASP   A 1 176 ? -32.975 -25.157 -21.234 1.00 41.38  ? 173 ASP   A HB2  1 
ATOM   2738 H  HB3  . ASP   A 1 176 ? -31.679 -24.256 -21.421 1.00 41.38  ? 173 ASP   A HB3  1 
ATOM   2739 N  N    . ALA   A 1 177 ? -31.501 -27.056 -19.518 1.00 44.66  ? 174 ALA   A N    1 
ATOM   2740 C  CA   . ALA   A 1 177 ? -30.970 -27.400 -18.202 1.00 49.31  ? 174 ALA   A CA   1 
ATOM   2741 C  C    . ALA   A 1 177 ? -29.720 -28.265 -18.313 1.00 49.13  ? 174 ALA   A C    1 
ATOM   2742 O  O    . ALA   A 1 177 ? -28.731 -28.041 -17.606 1.00 57.45  ? 174 ALA   A O    1 
ATOM   2743 C  CB   . ALA   A 1 177 ? -32.047 -28.124 -17.390 1.00 45.41  ? 174 ALA   A CB   1 
ATOM   2744 H  H    . ALA   A 1 177 ? -32.332 -27.250 -19.628 1.00 53.63  ? 174 ALA   A H    1 
ATOM   2745 H  HA   . ALA   A 1 177 ? -30.727 -26.585 -17.737 1.00 59.21  ? 174 ALA   A HA   1 
ATOM   2746 H  HB1  . ALA   A 1 177 ? -31.695 -28.328 -16.510 1.00 54.53  ? 174 ALA   A HB1  1 
ATOM   2747 H  HB2  . ALA   A 1 177 ? -32.823 -27.548 -17.311 1.00 54.53  ? 174 ALA   A HB2  1 
ATOM   2748 H  HB3  . ALA   A 1 177 ? -32.289 -28.944 -17.848 1.00 54.53  ? 174 ALA   A HB3  1 
ATOM   2749 N  N    . LYS   A 1 178 ? -29.751 -29.269 -19.185 1.00 47.06  ? 175 LYS   A N    1 
ATOM   2750 C  CA   . LYS   A 1 178 ? -28.623 -30.184 -19.294 1.00 57.82  ? 175 LYS   A CA   1 
ATOM   2751 C  C    . LYS   A 1 178 ? -27.379 -29.485 -19.818 1.00 61.84  ? 175 LYS   A C    1 
ATOM   2752 O  O    . LYS   A 1 178 ? -26.260 -29.855 -19.451 1.00 67.61  ? 175 LYS   A O    1 
ATOM   2753 C  CB   . LYS   A 1 178 ? -28.991 -31.349 -20.205 1.00 55.88  ? 175 LYS   A CB   1 
ATOM   2754 C  CG   . LYS   A 1 178 ? -27.900 -32.402 -20.315 1.00 70.97  ? 175 LYS   A CG   1 
ATOM   2755 C  CD   . LYS   A 1 178 ? -28.362 -33.602 -21.125 1.00 68.01  ? 175 LYS   A CD   1 
ATOM   2756 C  CE   . LYS   A 1 178 ? -27.333 -34.732 -21.073 1.00 81.56  ? 175 LYS   A CE   1 
ATOM   2757 N  NZ   . LYS   A 1 178 ? -27.772 -35.936 -21.839 1.00 98.00  ? 175 LYS   A NZ   1 
ATOM   2758 H  H    . LYS   A 1 178 ? -30.405 -29.440 -19.718 1.00 56.52  ? 175 LYS   A H    1 
ATOM   2759 H  HA   . LYS   A 1 178 ? -28.420 -30.535 -18.413 1.00 69.43  ? 175 LYS   A HA   1 
ATOM   2760 H  HB2  . LYS   A 1 178 ? -29.786 -31.781 -19.855 1.00 67.09  ? 175 LYS   A HB2  1 
ATOM   2761 H  HB3  . LYS   A 1 178 ? -29.164 -31.007 -21.096 1.00 67.09  ? 175 LYS   A HB3  1 
ATOM   2762 H  HG2  . LYS   A 1 178 ? -27.125 -32.017 -20.755 1.00 85.20  ? 175 LYS   A HG2  1 
ATOM   2763 H  HG3  . LYS   A 1 178 ? -27.658 -32.708 -19.427 1.00 85.20  ? 175 LYS   A HG3  1 
ATOM   2764 H  HD2  . LYS   A 1 178 ? -29.199 -33.933 -20.763 1.00 81.66  ? 175 LYS   A HD2  1 
ATOM   2765 H  HD3  . LYS   A 1 178 ? -28.482 -33.340 -22.051 1.00 81.66  ? 175 LYS   A HD3  1 
ATOM   2766 H  HE2  . LYS   A 1 178 ? -26.498 -34.420 -21.456 1.00 97.91  ? 175 LYS   A HE2  1 
ATOM   2767 H  HE3  . LYS   A 1 178 ? -27.196 -34.996 -20.150 1.00 97.91  ? 175 LYS   A HE3  1 
ATOM   2768 H  HZ1  . LYS   A 1 178 ? -27.162 -36.581 -21.769 1.00 117.64 ? 175 LYS   A HZ1  1 
ATOM   2769 H  HZ2  . LYS   A 1 178 ? -28.547 -36.235 -21.518 1.00 117.64 ? 175 LYS   A HZ2  1 
ATOM   2770 H  HZ3  . LYS   A 1 178 ? -27.877 -35.729 -22.698 1.00 117.64 ? 175 LYS   A HZ3  1 
ATOM   2771 N  N    . MET   A 1 179 ? -27.551 -28.481 -20.673 1.00 52.85  ? 176 MET   A N    1 
ATOM   2772 C  CA   . MET   A 1 179 ? -26.431 -27.805 -21.315 1.00 58.03  ? 176 MET   A CA   1 
ATOM   2773 C  C    . MET   A 1 179 ? -25.903 -26.649 -20.474 1.00 58.03  ? 176 MET   A C    1 
ATOM   2774 O  O    . MET   A 1 179 ? -24.688 -26.434 -20.418 1.00 63.80  ? 176 MET   A O    1 
ATOM   2775 C  CB   . MET   A 1 179 ? -26.866 -27.320 -22.702 1.00 51.39  ? 176 MET   A CB   1 
ATOM   2776 C  CG   . MET   A 1 179 ? -25.744 -26.840 -23.593 1.00 64.64  ? 176 MET   A CG   1 
ATOM   2777 S  SD   . MET   A 1 179 ? -26.390 -26.129 -25.134 1.00 58.35  ? 176 MET   A SD   1 
ATOM   2778 C  CE   . MET   A 1 179 ? -27.087 -27.604 -25.871 1.00 48.13  ? 176 MET   A CE   1 
ATOM   2779 H  H    . MET   A 1 179 ? -28.320 -28.169 -20.901 1.00 63.46  ? 176 MET   A H    1 
ATOM   2780 H  HA   . MET   A 1 179 ? -25.702 -28.431 -21.443 1.00 69.68  ? 176 MET   A HA   1 
ATOM   2781 H  HB2  . MET   A 1 179 ? -27.306 -28.054 -23.159 1.00 61.71  ? 176 MET   A HB2  1 
ATOM   2782 H  HB3  . MET   A 1 179 ? -27.484 -26.581 -22.589 1.00 61.71  ? 176 MET   A HB3  1 
ATOM   2783 H  HG2  . MET   A 1 179 ? -25.234 -26.157 -23.130 1.00 77.61  ? 176 MET   A HG2  1 
ATOM   2784 H  HG3  . MET   A 1 179 ? -25.168 -27.588 -23.818 1.00 77.61  ? 176 MET   A HG3  1 
ATOM   2785 H  HE1  . MET   A 1 179 ? -27.449 -27.382 -26.743 1.00 57.80  ? 176 MET   A HE1  1 
ATOM   2786 H  HE2  . MET   A 1 179 ? -26.389 -28.272 -25.963 1.00 57.80  ? 176 MET   A HE2  1 
ATOM   2787 H  HE3  . MET   A 1 179 ? -27.792 -27.941 -25.296 1.00 57.80  ? 176 MET   A HE3  1 
ATOM   2788 N  N    . MET   A 1 180 ? -26.788 -25.925 -19.785 1.00 60.50  ? 177 MET   A N    1 
ATOM   2789 C  CA   . MET   A 1 180 ? -26.363 -24.795 -18.969 1.00 60.16  ? 177 MET   A CA   1 
ATOM   2790 C  C    . MET   A 1 180 ? -25.546 -25.219 -17.757 1.00 70.96  ? 177 MET   A C    1 
ATOM   2791 O  O    . MET   A 1 180 ? -24.795 -24.403 -17.214 1.00 76.31  ? 177 MET   A O    1 
ATOM   2792 C  CB   . MET   A 1 180 ? -27.581 -24.012 -18.485 1.00 64.30  ? 177 MET   A CB   1 
ATOM   2793 C  CG   . MET   A 1 180 ? -28.464 -23.499 -19.589 1.00 60.62  ? 177 MET   A CG   1 
ATOM   2794 S  SD   . MET   A 1 180 ? -30.094 -23.053 -18.973 1.00 64.21  ? 177 MET   A SD   1 
ATOM   2795 C  CE   . MET   A 1 180 ? -30.224 -21.376 -19.555 1.00 57.88  ? 177 MET   A CE   1 
ATOM   2796 H  H    . MET   A 1 180 ? -27.636 -26.068 -19.776 1.00 72.64  ? 177 MET   A H    1 
ATOM   2797 H  HA   . MET   A 1 180 ? -25.821 -24.216 -19.528 1.00 72.23  ? 177 MET   A HA   1 
ATOM   2798 H  HB2  . MET   A 1 180 ? -28.119 -24.591 -17.923 1.00 77.20  ? 177 MET   A HB2  1 
ATOM   2799 H  HB3  . MET   A 1 180 ? -27.274 -23.246 -17.974 1.00 77.20  ? 177 MET   A HB3  1 
ATOM   2800 H  HG2  . MET   A 1 180 ? -28.060 -22.710 -19.983 1.00 72.78  ? 177 MET   A HG2  1 
ATOM   2801 H  HG3  . MET   A 1 180 ? -28.570 -24.189 -20.262 1.00 72.78  ? 177 MET   A HG3  1 
ATOM   2802 H  HE1  . MET   A 1 180 ? -31.080 -21.011 -19.279 1.00 69.49  ? 177 MET   A HE1  1 
ATOM   2803 H  HE2  . MET   A 1 180 ? -29.503 -20.852 -19.173 1.00 69.49  ? 177 MET   A HE2  1 
ATOM   2804 H  HE3  . MET   A 1 180 ? -30.160 -21.371 -20.523 1.00 69.49  ? 177 MET   A HE3  1 
ATOM   2805 N  N    . SER   A 1 181 ? -25.691 -26.465 -17.318 1.00 66.71  ? 178 SER   A N    1 
ATOM   2806 C  CA   . SER   A 1 181 ? -25.016 -26.970 -16.136 1.00 76.38  ? 178 SER   A CA   1 
ATOM   2807 C  C    . SER   A 1 181 ? -23.859 -27.906 -16.460 1.00 81.97  ? 178 SER   A C    1 
ATOM   2808 O  O    . SER   A 1 181 ? -23.163 -28.349 -15.537 1.00 84.00  ? 178 SER   A O    1 
ATOM   2809 C  CB   . SER   A 1 181 ? -26.029 -27.690 -15.239 1.00 71.26  ? 178 SER   A CB   1 
ATOM   2810 O  OG   . SER   A 1 181 ? -26.484 -28.875 -15.868 1.00 65.27  ? 178 SER   A OG   1 
ATOM   2811 H  H    . SER   A 1 181 ? -26.190 -27.052 -17.702 1.00 80.09  ? 178 SER   A H    1 
ATOM   2812 H  HA   . SER   A 1 181 ? -24.648 -26.221 -15.641 1.00 91.70  ? 178 SER   A HA   1 
ATOM   2813 H  HB2  . SER   A 1 181 ? -25.603 -27.919 -14.398 1.00 85.56  ? 178 SER   A HB2  1 
ATOM   2814 H  HB3  . SER   A 1 181 ? -26.785 -27.104 -15.079 1.00 85.56  ? 178 SER   A HB3  1 
ATOM   2815 H  HG   . SER   A 1 181 ? -26.763 -28.701 -16.641 1.00 78.37  ? 178 SER   A HG   1 
ATOM   2816 N  N    . GLN   A 1 182 ? -23.641 -28.227 -17.734 1.00 77.19  ? 179 GLN   A N    1 
ATOM   2817 C  CA   . GLN   A 1 182 ? -22.496 -29.030 -18.145 1.00 74.95  ? 179 GLN   A CA   1 
ATOM   2818 C  C    . GLN   A 1 182 ? -21.215 -28.428 -17.558 1.00 75.55  ? 179 GLN   A C    1 
ATOM   2819 O  O    . GLN   A 1 182 ? -20.854 -27.295 -17.915 1.00 68.10  ? 179 GLN   A O    1 
ATOM   2820 C  CB   . GLN   A 1 182 ? -22.375 -29.062 -19.671 1.00 70.18  ? 179 GLN   A CB   1 
ATOM   2821 C  CG   . GLN   A 1 182 ? -23.236 -30.078 -20.438 1.00 81.37  ? 179 GLN   A CG   1 
ATOM   2822 C  CD   . GLN   A 1 182 ? -23.343 -31.434 -19.770 1.00 91.37  ? 179 GLN   A CD   1 
ATOM   2823 O  OE1  . GLN   A 1 182 ? -24.055 -31.596 -18.784 1.00 96.08  ? 179 GLN   A OE1  1 
ATOM   2824 N  NE2  . GLN   A 1 182 ? -22.643 -32.424 -20.319 1.00 92.28  ? 179 GLN   A NE2  1 
ATOM   2825 H  H    . GLN   A 1 182 ? -24.149 -27.988 -18.386 1.00 92.66  ? 179 GLN   A H    1 
ATOM   2826 H  HA   . GLN   A 1 182 ? -22.615 -29.939 -17.828 1.00 89.99  ? 179 GLN   A HA   1 
ATOM   2827 H  HB2  . GLN   A 1 182 ? -22.617 -28.184 -20.005 1.00 84.25  ? 179 GLN   A HB2  1 
ATOM   2828 H  HB3  . GLN   A 1 182 ? -21.451 -29.258 -19.890 1.00 84.25  ? 179 GLN   A HB3  1 
ATOM   2829 H  HG2  . GLN   A 1 182 ? -24.134 -29.722 -20.524 1.00 97.68  ? 179 GLN   A HG2  1 
ATOM   2830 H  HG3  . GLN   A 1 182 ? -22.847 -30.213 -21.317 1.00 97.68  ? 179 GLN   A HG3  1 
ATOM   2831 H  HE21 . GLN   A 1 182 ? -22.162 -32.275 -21.017 1.00 110.78 ? 179 GLN   A HE21 1 
ATOM   2832 H  HE22 . GLN   A 1 182 ? -22.671 -33.212 -19.977 1.00 110.78 ? 179 GLN   A HE22 1 
ATOM   2833 N  N    . PRO   A 1 183 ? -20.506 -29.136 -16.672 1.00 78.26  ? 180 PRO   A N    1 
ATOM   2834 C  CA   . PRO   A 1 183 ? -19.188 -28.640 -16.247 1.00 78.57  ? 180 PRO   A CA   1 
ATOM   2835 C  C    . PRO   A 1 183 ? -18.244 -28.505 -17.434 1.00 74.39  ? 180 PRO   A C    1 
ATOM   2836 O  O    . PRO   A 1 183 ? -18.244 -29.331 -18.351 1.00 69.00  ? 180 PRO   A O    1 
ATOM   2837 C  CB   . PRO   A 1 183 ? -18.706 -29.701 -15.247 1.00 74.28  ? 180 PRO   A CB   1 
ATOM   2838 C  CG   . PRO   A 1 183 ? -19.960 -30.361 -14.753 1.00 72.13  ? 180 PRO   A CG   1 
ATOM   2839 C  CD   . PRO   A 1 183 ? -20.893 -30.361 -15.941 1.00 78.02  ? 180 PRO   A CD   1 
ATOM   2840 H  HA   . PRO   A 1 183 ? -19.269 -27.786 -15.794 1.00 94.33  ? 180 PRO   A HA   1 
ATOM   2841 H  HB2  . PRO   A 1 183 ? -18.130 -30.340 -15.694 1.00 89.18  ? 180 PRO   A HB2  1 
ATOM   2842 H  HB3  . PRO   A 1 183 ? -18.227 -29.276 -14.518 1.00 89.18  ? 180 PRO   A HB3  1 
ATOM   2843 H  HG2  . PRO   A 1 183 ? -19.766 -31.266 -14.464 1.00 86.59  ? 180 PRO   A HG2  1 
ATOM   2844 H  HG3  . PRO   A 1 183 ? -20.335 -29.851 -14.018 1.00 86.59  ? 180 PRO   A HG3  1 
ATOM   2845 H  HD2  . PRO   A 1 183 ? -20.756 -31.150 -16.489 1.00 93.66  ? 180 PRO   A HD2  1 
ATOM   2846 H  HD3  . PRO   A 1 183 ? -21.819 -30.315 -15.654 1.00 93.66  ? 180 PRO   A HD3  1 
ATOM   2847 N  N    . ALA   A 1 184 ? -17.444 -27.440 -17.416 1.00 70.70  ? 181 ALA   A N    1 
ATOM   2848 C  CA   . ALA   A 1 184 ? -16.446 -27.228 -18.455 1.00 71.30  ? 181 ALA   A CA   1 
ATOM   2849 C  C    . ALA   A 1 184 ? -15.431 -28.371 -18.467 1.00 75.28  ? 181 ALA   A C    1 
ATOM   2850 O  O    . ALA   A 1 184 ? -15.232 -29.076 -17.471 1.00 72.03  ? 181 ALA   A O    1 
ATOM   2851 C  CB   . ALA   A 1 184 ? -15.723 -25.899 -18.244 1.00 64.92  ? 181 ALA   A CB   1 
ATOM   2852 H  H    . ALA   A 1 184 ? -17.461 -26.827 -16.813 1.00 84.88  ? 181 ALA   A H    1 
ATOM   2853 H  HA   . ALA   A 1 184 ? -16.887 -27.201 -19.319 1.00 85.60  ? 181 ALA   A HA   1 
ATOM   2854 H  HB1  . ALA   A 1 184 ? -15.091 -25.765 -18.968 1.00 77.95  ? 181 ALA   A HB1  1 
ATOM   2855 H  HB2  . ALA   A 1 184 ? -16.375 -25.182 -18.237 1.00 77.95  ? 181 ALA   A HB2  1 
ATOM   2856 H  HB3  . ALA   A 1 184 ? -15.253 -25.926 -17.396 1.00 77.95  ? 181 ALA   A HB3  1 
ATOM   2857 N  N    . ASP   A 1 185 ? -14.767 -28.534 -19.614 1.00 70.91  ? 182 ASP   A N    1 
ATOM   2858 C  CA   . ASP   A 1 185 ? -13.830 -29.644 -19.779 1.00 89.07  ? 182 ASP   A CA   1 
ATOM   2859 C  C    . ASP   A 1 185 ? -12.562 -29.440 -18.953 1.00 84.10  ? 182 ASP   A C    1 
ATOM   2860 O  O    . ASP   A 1 185 ? -12.153 -30.333 -18.201 1.00 78.26  ? 182 ASP   A O    1 
ATOM   2861 C  CB   . ASP   A 1 185 ? -13.497 -29.830 -21.264 1.00 81.00  ? 182 ASP   A CB   1 
ATOM   2862 C  CG   . ASP   A 1 185 ? -13.015 -28.550 -21.927 1.00 92.71  ? 182 ASP   A CG   1 
ATOM   2863 O  OD1  . ASP   A 1 185 ? -12.974 -27.500 -21.251 1.00 98.60  ? 182 ASP   A OD1  1 
ATOM   2864 O  OD2  . ASP   A 1 185 ? -12.688 -28.594 -23.131 1.00 98.72  ? 182 ASP   A OD2  1 
ATOM   2865 H  H    . ASP   A 1 185 ? -14.840 -28.022 -20.302 1.00 85.14  ? 182 ASP   A H    1 
ATOM   2866 H  HA   . ASP   A 1 185 ? -14.254 -30.457 -19.462 1.00 106.92 ? 182 ASP   A HA   1 
ATOM   2867 H  HB2  . ASP   A 1 185 ? -12.794 -30.493 -21.349 1.00 97.25  ? 182 ASP   A HB2  1 
ATOM   2868 H  HB3  . ASP   A 1 185 ? -14.293 -30.128 -21.731 1.00 97.25  ? 182 ASP   A HB3  1 
ATOM   2869 N  N    . THR   A 1 186 ? -11.923 -28.279 -19.079 1.00 81.24  ? 183 THR   A N    1 
ATOM   2870 C  CA   . THR   A 1 186 ? -10.692 -28.028 -18.345 1.00 77.14  ? 183 THR   A CA   1 
ATOM   2871 C  C    . THR   A 1 186 ? -10.993 -27.663 -16.891 1.00 75.42  ? 183 THR   A C    1 
ATOM   2872 O  O    . THR   A 1 186 ? -12.146 -27.451 -16.491 1.00 71.61  ? 183 THR   A O    1 
ATOM   2873 C  CB   . THR   A 1 186 ? -9.892  -26.898 -18.993 1.00 74.01  ? 183 THR   A CB   1 
ATOM   2874 O  OG1  . THR   A 1 186 ? -10.732 -25.750 -19.160 1.00 75.98  ? 183 THR   A OG1  1 
ATOM   2875 C  CG2  . THR   A 1 186 ? -9.351  -27.323 -20.350 1.00 76.53  ? 183 THR   A CG2  1 
ATOM   2876 H  H    . THR   A 1 186 ? -12.181 -27.628 -19.578 1.00 97.52  ? 183 THR   A H    1 
ATOM   2877 H  HA   . THR   A 1 186 ? -10.158 -28.838 -18.363 1.00 92.62  ? 183 THR   A HA   1 
ATOM   2878 H  HB   . THR   A 1 186 ? -9.140  -26.673 -18.423 1.00 88.85  ? 183 THR   A HB   1 
ATOM   2879 H  HG1  . THR   A 1 186 ? -10.320 -25.151 -19.580 1.00 91.22  ? 183 THR   A HG1  1 
ATOM   2880 H  HG21 . THR   A 1 186 ? -8.876  -26.586 -20.764 1.00 91.88  ? 183 THR   A HG21 1 
ATOM   2881 H  HG22 . THR   A 1 186 ? -8.743  -28.072 -20.245 1.00 91.88  ? 183 THR   A HG22 1 
ATOM   2882 H  HG23 . THR   A 1 186 ? -10.082 -27.591 -20.929 1.00 91.88  ? 183 THR   A HG23 1 
ATOM   2883 N  N    . GLU   A 1 187 ? -9.927  -27.570 -16.094 1.00 68.48  ? 184 GLU   A N    1 
ATOM   2884 C  CA   . GLU   A 1 187 ? -10.065 -27.058 -14.735 1.00 70.53  ? 184 GLU   A CA   1 
ATOM   2885 C  C    . GLU   A 1 187 ? -10.065 -25.534 -14.723 1.00 70.74  ? 184 GLU   A C    1 
ATOM   2886 O  O    . GLU   A 1 187 ? -10.672 -24.923 -13.835 1.00 73.79  ? 184 GLU   A O    1 
ATOM   2887 C  CB   . GLU   A 1 187 ? -8.947  -27.609 -13.853 1.00 68.75  ? 184 GLU   A CB   1 
ATOM   2888 C  CG   . GLU   A 1 187 ? -8.870  -27.005 -12.456 1.00 78.07  ? 184 GLU   A CG   1 
ATOM   2889 C  CD   . GLU   A 1 187 ? -10.121 -27.268 -11.635 1.00 87.32  ? 184 GLU   A CD   1 
ATOM   2890 O  OE1  . GLU   A 1 187 ? -11.028 -27.967 -12.138 1.00 83.57  ? 184 GLU   A OE1  1 
ATOM   2891 O  OE2  . GLU   A 1 187 ? -10.194 -26.785 -10.484 1.00 92.15  ? 184 GLU   A OE2  1 
ATOM   2892 H  H    . GLU   A 1 187 ? -9.126  -27.793 -16.315 1.00 82.22  ? 184 GLU   A H    1 
ATOM   2893 H  HA   . GLU   A 1 187 ? -10.903 -27.361 -14.353 1.00 84.68  ? 184 GLU   A HA   1 
ATOM   2894 H  HB2  . GLU   A 1 187 ? -9.080  -28.564 -13.749 1.00 82.54  ? 184 GLU   A HB2  1 
ATOM   2895 H  HB3  . GLU   A 1 187 ? -8.098  -27.437 -14.290 1.00 82.54  ? 184 GLU   A HB3  1 
ATOM   2896 H  HG2  . GLU   A 1 187 ? -8.115  -27.392 -11.985 1.00 93.73  ? 184 GLU   A HG2  1 
ATOM   2897 H  HG3  . GLU   A 1 187 ? -8.757  -26.045 -12.532 1.00 93.73  ? 184 GLU   A HG3  1 
ATOM   2898 N  N    . GLU   A 1 188 ? -9.403  -24.911 -15.703 1.00 63.61  ? 185 GLU   A N    1 
ATOM   2899 C  CA   . GLU   A 1 188 ? -9.496  -23.463 -15.854 1.00 67.80  ? 185 GLU   A CA   1 
ATOM   2900 C  C    . GLU   A 1 188 ? -10.926 -23.042 -16.168 1.00 69.46  ? 185 GLU   A C    1 
ATOM   2901 O  O    . GLU   A 1 188 ? -11.413 -22.027 -15.655 1.00 65.50  ? 185 GLU   A O    1 
ATOM   2902 C  CB   . GLU   A 1 188 ? -8.554  -22.989 -16.962 1.00 65.67  ? 185 GLU   A CB   1 
ATOM   2903 C  CG   . GLU   A 1 188 ? -7.083  -22.959 -16.583 1.00 85.73  ? 185 GLU   A CG   1 
ATOM   2904 C  CD   . GLU   A 1 188 ? -6.236  -22.223 -17.608 1.00 95.18  ? 185 GLU   A CD   1 
ATOM   2905 O  OE1  . GLU   A 1 188 ? -6.808  -21.741 -18.613 1.00 78.86  ? 185 GLU   A OE1  1 
ATOM   2906 O  OE2  . GLU   A 1 188 ? -4.998  -22.146 -17.418 1.00 89.86  ? 185 GLU   A OE2  1 
ATOM   2907 H  H    . GLU   A 1 188 ? -8.901  -25.300 -16.283 1.00 76.37  ? 185 GLU   A H    1 
ATOM   2908 H  HA   . GLU   A 1 188 ? -9.224  -23.042 -15.024 1.00 81.40  ? 185 GLU   A HA   1 
ATOM   2909 H  HB2  . GLU   A 1 188 ? -8.647  -23.585 -17.721 1.00 78.85  ? 185 GLU   A HB2  1 
ATOM   2910 H  HB3  . GLU   A 1 188 ? -8.808  -22.087 -17.216 1.00 78.85  ? 185 GLU   A HB3  1 
ATOM   2911 H  HG2  . GLU   A 1 188 ? -6.984  -22.507 -15.730 1.00 102.92 ? 185 GLU   A HG2  1 
ATOM   2912 H  HG3  . GLU   A 1 188 ? -6.754  -23.869 -16.517 1.00 102.92 ? 185 GLU   A HG3  1 
ATOM   2913 N  N    . GLY   A 1 189 ? -11.614 -23.812 -17.015 1.00 72.05  ? 186 GLY   A N    1 
ATOM   2914 C  CA   . GLY   A 1 189 ? -12.971 -23.453 -17.397 1.00 60.15  ? 186 GLY   A CA   1 
ATOM   2915 C  C    . GLY   A 1 189 ? -13.983 -23.697 -16.299 1.00 62.00  ? 186 GLY   A C    1 
ATOM   2916 O  O    . GLY   A 1 189 ? -14.993 -22.982 -16.210 1.00 49.72  ? 186 GLY   A O    1 
ATOM   2917 H  H    . GLY   A 1 189 ? -11.320 -24.535 -17.375 1.00 86.50  ? 186 GLY   A H    1 
ATOM   2918 H  HA2  . GLY   A 1 189 ? -12.997 -22.511 -17.629 1.00 72.22  ? 186 GLY   A HA2  1 
ATOM   2919 H  HA3  . GLY   A 1 189 ? -13.232 -23.976 -18.171 1.00 72.22  ? 186 GLY   A HA3  1 
ATOM   2920 N  N    . ARG   A 1 190 ? -13.739 -24.708 -15.457 1.00 62.29  ? 187 ARG   A N    1 
ATOM   2921 C  CA   . ARG   A 1 190 ? -14.627 -24.960 -14.331 1.00 63.55  ? 187 ARG   A CA   1 
ATOM   2922 C  C    . ARG   A 1 190 ? -14.590 -23.804 -13.342 1.00 53.77  ? 187 ARG   A C    1 
ATOM   2923 O  O    . ARG   A 1 190 ? -15.633 -23.381 -12.838 1.00 45.04  ? 187 ARG   A O    1 
ATOM   2924 C  CB   . ARG   A 1 190 ? -14.246 -26.263 -13.630 1.00 58.32  ? 187 ARG   A CB   1 
ATOM   2925 C  CG   . ARG   A 1 190 ? -15.428 -27.188 -13.367 1.00 65.31  ? 187 ARG   A CG   1 
ATOM   2926 C  CD   . ARG   A 1 190 ? -15.146 -28.614 -13.845 1.00 68.24  ? 187 ARG   A CD   1 
ATOM   2927 N  NE   . ARG   A 1 190 ? -13.766 -29.010 -13.575 1.00 72.87  ? 187 ARG   A NE   1 
ATOM   2928 C  CZ   . ARG   A 1 190 ? -13.059 -29.853 -14.317 1.00 68.17  ? 187 ARG   A CZ   1 
ATOM   2929 N  NH1  . ARG   A 1 190 ? -13.561 -30.405 -15.410 1.00 67.25  ? 187 ARG   A NH1  1 
ATOM   2930 N  NH2  . ARG   A 1 190 ? -11.815 -30.148 -13.952 1.00 71.40  ? 187 ARG   A NH2  1 
ATOM   2931 H  H    . ARG   A 1 190 ? -13.075 -25.251 -15.519 1.00 74.79  ? 187 ARG   A H    1 
ATOM   2932 H  HA   . ARG   A 1 190 ? -15.532 -25.055 -14.666 1.00 76.30  ? 187 ARG   A HA   1 
ATOM   2933 H  HB2  . ARG   A 1 190 ? -13.613 -26.742 -14.188 1.00 70.02  ? 187 ARG   A HB2  1 
ATOM   2934 H  HB3  . ARG   A 1 190 ? -13.840 -26.050 -12.776 1.00 70.02  ? 187 ARG   A HB3  1 
ATOM   2935 H  HG2  . ARG   A 1 190 ? -15.606 -27.216 -12.414 1.00 78.42  ? 187 ARG   A HG2  1 
ATOM   2936 H  HG3  . ARG   A 1 190 ? -16.206 -26.856 -13.840 1.00 78.42  ? 187 ARG   A HG3  1 
ATOM   2937 H  HD2  . ARG   A 1 190 ? -15.736 -29.230 -13.383 1.00 81.93  ? 187 ARG   A HD2  1 
ATOM   2938 H  HD3  . ARG   A 1 190 ? -15.296 -28.666 -14.802 1.00 81.93  ? 187 ARG   A HD3  1 
ATOM   2939 H  HE   . ARG   A 1 190 ? -13.383 -28.671 -12.883 1.00 87.49  ? 187 ARG   A HE   1 
ATOM   2940 H  HH11 . ARG   A 1 190 ? -14.365 -30.221 -15.655 1.00 80.75  ? 187 ARG   A HH11 1 
ATOM   2941 H  HH12 . ARG   A 1 190 ? -13.084 -30.949 -15.875 1.00 80.75  ? 187 ARG   A HH12 1 
ATOM   2942 H  HH21 . ARG   A 1 190 ? -11.478 -29.794 -13.244 1.00 85.73  ? 187 ARG   A HH21 1 
ATOM   2943 H  HH22 . ARG   A 1 190 ? -11.346 -30.693 -14.424 1.00 85.73  ? 187 ARG   A HH22 1 
ATOM   2944 N  N    . ILE   A 1 191 ? -13.396 -23.280 -13.060 1.00 52.10  ? 188 ILE   A N    1 
ATOM   2945 C  CA   . ILE   A 1 191 ? -13.275 -22.204 -12.082 1.00 48.10  ? 188 ILE   A CA   1 
ATOM   2946 C  C    . ILE   A 1 191 ? -13.819 -20.895 -12.644 1.00 48.44  ? 188 ILE   A C    1 
ATOM   2947 O  O    . ILE   A 1 191 ? -14.537 -20.156 -11.953 1.00 49.82  ? 188 ILE   A O    1 
ATOM   2948 C  CB   . ILE   A 1 191 ? -11.809 -22.060 -11.635 1.00 56.55  ? 188 ILE   A CB   1 
ATOM   2949 C  CG1  . ILE   A 1 191 ? -11.332 -23.369 -10.992 1.00 62.47  ? 188 ILE   A CG1  1 
ATOM   2950 C  CG2  . ILE   A 1 191 ? -11.661 -20.874 -10.690 1.00 53.21  ? 188 ILE   A CG2  1 
ATOM   2951 C  CD1  . ILE   A 1 191 ? -12.072 -23.736 -9.721  1.00 70.18  ? 188 ILE   A CD1  1 
ATOM   2952 H  H    . ILE   A 1 191 ? -12.653 -23.527 -13.416 1.00 62.56  ? 188 ILE   A H    1 
ATOM   2953 H  HA   . ILE   A 1 191 ? -13.809 -22.435 -11.305 1.00 57.76  ? 188 ILE   A HA   1 
ATOM   2954 H  HB   . ILE   A 1 191 ? -11.251 -21.888 -12.409 1.00 67.90  ? 188 ILE   A HB   1 
ATOM   2955 H  HG12 . ILE   A 1 191 ? -11.459 -24.092 -11.626 1.00 75.01  ? 188 ILE   A HG12 1 
ATOM   2956 H  HG13 . ILE   A 1 191 ? -10.392 -23.282 -10.771 1.00 75.01  ? 188 ILE   A HG13 1 
ATOM   2957 H  HG21 . ILE   A 1 191 ? -10.806 -20.937 -10.235 1.00 63.89  ? 188 ILE   A HG21 1 
ATOM   2958 H  HG22 . ILE   A 1 191 ? -11.702 -20.053 -11.205 1.00 63.89  ? 188 ILE   A HG22 1 
ATOM   2959 H  HG23 . ILE   A 1 191 ? -12.383 -20.894 -10.042 1.00 63.89  ? 188 ILE   A HG23 1 
ATOM   2960 H  HD11 . ILE   A 1 191 ? -11.660 -24.523 -9.332  1.00 84.25  ? 188 ILE   A HD11 1 
ATOM   2961 H  HD12 . ILE   A 1 191 ? -12.020 -22.994 -9.099  1.00 84.25  ? 188 ILE   A HD12 1 
ATOM   2962 H  HD13 . ILE   A 1 191 ? -12.999 -23.922 -9.938  1.00 84.25  ? 188 ILE   A HD13 1 
ATOM   2963 N  N    . GLU   A 1 192 ? -13.496 -20.579 -13.901 1.00 45.54  ? 189 GLU   A N    1 
ATOM   2964 C  CA   . GLU   A 1 192 ? -14.072 -19.376 -14.509 1.00 50.42  ? 189 GLU   A CA   1 
ATOM   2965 C  C    . GLU   A 1 192 ? -15.590 -19.460 -14.545 1.00 49.65  ? 189 GLU   A C    1 
ATOM   2966 O  O    . GLU   A 1 192 ? -16.282 -18.466 -14.305 1.00 43.72  ? 189 GLU   A O    1 
ATOM   2967 C  CB   . GLU   A 1 192 ? -13.525 -19.173 -15.921 1.00 66.09  ? 189 GLU   A CB   1 
ATOM   2968 C  CG   . GLU   A 1 192 ? -12.519 -18.036 -16.049 1.00 75.03  ? 189 GLU   A CG   1 
ATOM   2969 C  CD   . GLU   A 1 192 ? -13.150 -16.671 -15.868 1.00 71.46  ? 189 GLU   A CD   1 
ATOM   2970 O  OE1  . GLU   A 1 192 ? -13.996 -16.281 -16.709 1.00 64.99  ? 189 GLU   A OE1  1 
ATOM   2971 O  OE2  . GLU   A 1 192 ? -12.792 -15.987 -14.884 1.00 80.33  ? 189 GLU   A OE2  1 
ATOM   2972 H  H    . GLU   A 1 192 ? -12.965 -21.028 -14.407 1.00 54.69  ? 189 GLU   A H    1 
ATOM   2973 H  HA   . GLU   A 1 192 ? -13.813 -18.608 -13.976 1.00 60.55  ? 189 GLU   A HA   1 
ATOM   2974 H  HB2  . GLU   A 1 192 ? -13.083 -19.990 -16.201 1.00 79.34  ? 189 GLU   A HB2  1 
ATOM   2975 H  HB3  . GLU   A 1 192 ? -14.267 -18.977 -16.515 1.00 79.34  ? 189 GLU   A HB3  1 
ATOM   2976 H  HG2  . GLU   A 1 192 ? -11.834 -18.143 -15.370 1.00 90.07  ? 189 GLU   A HG2  1 
ATOM   2977 H  HG3  . GLU   A 1 192 ? -12.119 -18.066 -16.932 1.00 90.07  ? 189 GLU   A HG3  1 
ATOM   2978 N  N    . GLN   A 1 193 ? -16.125 -20.641 -14.847 1.00 42.15  ? 190 GLN   A N    1 
ATOM   2979 C  CA   . GLN   A 1 193 ? -17.574 -20.815 -14.875 1.00 44.92  ? 190 GLN   A CA   1 
ATOM   2980 C  C    . GLN   A 1 193 ? -18.182 -20.532 -13.504 1.00 42.37  ? 190 GLN   A C    1 
ATOM   2981 O  O    . GLN   A 1 193 ? -19.238 -19.889 -13.406 1.00 38.84  ? 190 GLN   A O    1 
ATOM   2982 C  CB   . GLN   A 1 193 ? -17.898 -22.229 -15.354 1.00 53.14  ? 190 GLN   A CB   1 
ATOM   2983 C  CG   . GLN   A 1 193 ? -19.353 -22.603 -15.324 1.00 54.38  ? 190 GLN   A CG   1 
ATOM   2984 C  CD   . GLN   A 1 193 ? -19.591 -23.991 -15.886 1.00 74.35  ? 190 GLN   A CD   1 
ATOM   2985 O  OE1  . GLN   A 1 193 ? -18.948 -24.398 -16.856 1.00 75.72  ? 190 GLN   A OE1  1 
ATOM   2986 N  NE2  . GLN   A 1 193 ? -20.514 -24.726 -15.276 1.00 83.14  ? 190 GLN   A NE2  1 
ATOM   2987 H  H    . GLN   A 1 193 ? -15.677 -21.350 -15.038 1.00 50.62  ? 190 GLN   A H    1 
ATOM   2988 H  HA   . GLN   A 1 193 ? -17.972 -20.190 -15.500 1.00 53.94  ? 190 GLN   A HA   1 
ATOM   2989 H  HB2  . GLN   A 1 193 ? -17.596 -22.316 -16.272 1.00 63.81  ? 190 GLN   A HB2  1 
ATOM   2990 H  HB3  . GLN   A 1 193 ? -17.426 -22.859 -14.788 1.00 63.81  ? 190 GLN   A HB3  1 
ATOM   2991 H  HG2  . GLN   A 1 193 ? -19.669 -22.588 -14.407 1.00 65.30  ? 190 GLN   A HG2  1 
ATOM   2992 H  HG3  . GLN   A 1 193 ? -19.857 -21.969 -15.858 1.00 65.30  ? 190 GLN   A HG3  1 
ATOM   2993 H  HE21 . GLN   A 1 193 ? -20.940 -24.407 -14.601 1.00 99.81  ? 190 GLN   A HE21 1 
ATOM   2994 H  HE22 . GLN   A 1 193 ? -20.685 -25.520 -15.557 1.00 99.81  ? 190 GLN   A HE22 1 
ATOM   2995 N  N    . TYR   A 1 194 ? -17.530 -20.989 -12.437 1.00 41.38  ? 191 TYR   A N    1 
ATOM   2996 C  CA   . TYR   A 1 194 ? -17.996 -20.654 -11.095 1.00 40.86  ? 191 TYR   A CA   1 
ATOM   2997 C  C    . TYR   A 1 194 ? -17.956 -19.141 -10.868 1.00 40.52  ? 191 TYR   A C    1 
ATOM   2998 O  O    . TYR   A 1 194 ? -18.940 -18.545 -10.407 1.00 37.23  ? 191 TYR   A O    1 
ATOM   2999 C  CB   . TYR   A 1 194 ? -17.158 -21.390 -10.048 1.00 42.40  ? 191 TYR   A CB   1 
ATOM   3000 C  CG   . TYR   A 1 194 ? -17.357 -20.829 -8.664  1.00 37.83  ? 191 TYR   A CG   1 
ATOM   3001 C  CD1  . TYR   A 1 194 ? -18.401 -21.263 -7.864  1.00 48.30  ? 191 TYR   A CD1  1 
ATOM   3002 C  CD2  . TYR   A 1 194 ? -16.506 -19.854 -8.165  1.00 41.24  ? 191 TYR   A CD2  1 
ATOM   3003 C  CE1  . TYR   A 1 194 ? -18.591 -20.740 -6.609  1.00 41.52  ? 191 TYR   A CE1  1 
ATOM   3004 C  CE2  . TYR   A 1 194 ? -16.695 -19.315 -6.919  1.00 47.19  ? 191 TYR   A CE2  1 
ATOM   3005 C  CZ   . TYR   A 1 194 ? -17.736 -19.762 -6.141  1.00 42.32  ? 191 TYR   A CZ   1 
ATOM   3006 O  OH   . TYR   A 1 194 ? -17.924 -19.216 -4.898  1.00 53.31  ? 191 TYR   A OH   1 
ATOM   3007 H  H    . TYR   A 1 194 ? -16.828 -21.486 -12.462 1.00 49.70  ? 191 TYR   A H    1 
ATOM   3008 H  HA   . TYR   A 1 194 ? -18.914 -20.949 -10.995 1.00 49.07  ? 191 TYR   A HA   1 
ATOM   3009 H  HB2  . TYR   A 1 194 ? -17.415 -22.325 -10.036 1.00 50.92  ? 191 TYR   A HB2  1 
ATOM   3010 H  HB3  . TYR   A 1 194 ? -16.219 -21.307 -10.277 1.00 50.92  ? 191 TYR   A HB3  1 
ATOM   3011 H  HD1  . TYR   A 1 194 ? -18.980 -21.917 -8.181  1.00 58.00  ? 191 TYR   A HD1  1 
ATOM   3012 H  HD2  . TYR   A 1 194 ? -15.793 -19.560 -8.686  1.00 49.53  ? 191 TYR   A HD2  1 
ATOM   3013 H  HE1  . TYR   A 1 194 ? -19.291 -21.042 -6.077  1.00 49.87  ? 191 TYR   A HE1  1 
ATOM   3014 H  HE2  . TYR   A 1 194 ? -16.124 -18.653 -6.602  1.00 56.67  ? 191 TYR   A HE2  1 
ATOM   3015 H  HH   . TYR   A 1 194 ? -18.651 -19.485 -4.574  1.00 64.01  ? 191 TYR   A HH   1 
ATOM   3016 N  N    . LYS   A 1 195 ? -16.836 -18.495 -11.219 1.00 41.29  ? 192 LYS   A N    1 
ATOM   3017 C  CA   . LYS   A 1 195 ? -16.726 -17.056 -11.004 1.00 40.75  ? 192 LYS   A CA   1 
ATOM   3018 C  C    . LYS   A 1 195 ? -17.787 -16.293 -11.796 1.00 31.91  ? 192 LYS   A C    1 
ATOM   3019 O  O    . LYS   A 1 195 ? -18.329 -15.282 -11.314 1.00 33.72  ? 192 LYS   A O    1 
ATOM   3020 C  CB   . LYS   A 1 195 ? -15.339 -16.531 -11.382 1.00 42.59  ? 192 LYS   A CB   1 
ATOM   3021 C  CG   . LYS   A 1 195 ? -14.162 -17.088 -10.568 1.00 46.27  ? 192 LYS   A CG   1 
ATOM   3022 C  CD   . LYS   A 1 195 ? -12.941 -16.165 -10.738 1.00 60.30  ? 192 LYS   A CD   1 
ATOM   3023 C  CE   . LYS   A 1 195 ? -11.633 -16.805 -10.308 1.00 67.16  ? 192 LYS   A CE   1 
ATOM   3024 N  NZ   . LYS   A 1 195 ? -10.616 -16.802 -11.411 1.00 65.60  ? 192 LYS   A NZ   1 
ATOM   3025 H  H    . LYS   A 1 195 ? -16.144 -18.861 -11.575 1.00 49.59  ? 192 LYS   A H    1 
ATOM   3026 H  HA   . LYS   A 1 195 ? -16.856 -16.898 -10.055 1.00 48.94  ? 192 LYS   A HA   1 
ATOM   3027 H  HB2  . LYS   A 1 195 ? -15.174 -16.753 -12.311 1.00 51.14  ? 192 LYS   A HB2  1 
ATOM   3028 H  HB3  . LYS   A 1 195 ? -15.337 -15.568 -11.265 1.00 51.14  ? 192 LYS   A HB3  1 
ATOM   3029 H  HG2  . LYS   A 1 195 ? -14.399 -17.125 -9.628  1.00 55.57  ? 192 LYS   A HG2  1 
ATOM   3030 H  HG3  . LYS   A 1 195 ? -13.931 -17.975 -10.887 1.00 55.57  ? 192 LYS   A HG3  1 
ATOM   3031 H  HD2  . LYS   A 1 195 ? -12.859 -15.922 -11.673 1.00 72.40  ? 192 LYS   A HD2  1 
ATOM   3032 H  HD3  . LYS   A 1 195 ? -13.072 -15.369 -10.199 1.00 72.40  ? 192 LYS   A HD3  1 
ATOM   3033 H  HE2  . LYS   A 1 195 ? -11.268 -16.311 -9.558  1.00 80.64  ? 192 LYS   A HE2  1 
ATOM   3034 H  HE3  . LYS   A 1 195 ? -11.798 -17.725 -10.051 1.00 80.64  ? 192 LYS   A HE3  1 
ATOM   3035 H  HZ1  . LYS   A 1 195 ? -9.863  -17.185 -11.132 1.00 78.76  ? 192 LYS   A HZ1  1 
ATOM   3036 H  HZ2  . LYS   A 1 195 ? -10.926 -17.252 -12.113 1.00 78.76  ? 192 LYS   A HZ2  1 
ATOM   3037 H  HZ3  . LYS   A 1 195 ? -10.439 -15.965 -11.659 1.00 78.76  ? 192 LYS   A HZ3  1 
ATOM   3038 N  N    . ARG   A 1 196 ? -18.071 -16.722 -13.044 1.00 33.03  ? 193 ARG   A N    1 
ATOM   3039 C  CA   . ARG   A 1 196 ? -19.052 -16.023 -13.865 1.00 34.10  ? 193 ARG   A CA   1 
ATOM   3040 C  C    . ARG   A 1 196 ? -20.454 -16.190 -13.301 1.00 29.35  ? 193 ARG   A C    1 
ATOM   3041 O  O    . ARG   A 1 196 ? -21.268 -15.255 -13.320 1.00 29.37  ? 193 ARG   A O    1 
ATOM   3042 C  CB   . ARG   A 1 196 ? -19.013 -16.546 -15.297 1.00 41.60  ? 193 ARG   A CB   1 
ATOM   3043 C  CG   . ARG   A 1 196 ? -17.924 -15.922 -16.120 1.00 44.22  ? 193 ARG   A CG   1 
ATOM   3044 C  CD   . ARG   A 1 196 ? -18.151 -16.115 -17.604 1.00 46.07  ? 193 ARG   A CD   1 
ATOM   3045 N  NE   . ARG   A 1 196 ? -16.872 -16.343 -18.270 1.00 42.33  ? 193 ARG   A NE   1 
ATOM   3046 C  CZ   . ARG   A 1 196 ? -16.722 -16.907 -19.460 1.00 51.49  ? 193 ARG   A CZ   1 
ATOM   3047 N  NH1  . ARG   A 1 196 ? -17.768 -17.289 -20.182 1.00 46.35  ? 193 ARG   A NH1  1 
ATOM   3048 N  NH2  . ARG   A 1 196 ? -15.493 -17.084 -19.941 1.00 42.95  ? 193 ARG   A NH2  1 
ATOM   3049 H  H    . ARG   A 1 196 ? -17.711 -17.405 -13.423 1.00 39.68  ? 193 ARG   A H    1 
ATOM   3050 H  HA   . ARG   A 1 196 ? -18.827 -15.080 -13.875 1.00 40.96  ? 193 ARG   A HA   1 
ATOM   3051 H  HB2  . ARG   A 1 196 ? -18.862 -17.504 -15.278 1.00 49.96  ? 193 ARG   A HB2  1 
ATOM   3052 H  HB3  . ARG   A 1 196 ? -19.861 -16.352 -15.726 1.00 49.96  ? 193 ARG   A HB3  1 
ATOM   3053 H  HG2  . ARG   A 1 196 ? -17.894 -14.969 -15.940 1.00 53.11  ? 193 ARG   A HG2  1 
ATOM   3054 H  HG3  . ARG   A 1 196 ? -17.075 -16.330 -15.888 1.00 53.11  ? 193 ARG   A HG3  1 
ATOM   3055 H  HD2  . ARG   A 1 196 ? -18.722 -16.886 -17.752 1.00 55.32  ? 193 ARG   A HD2  1 
ATOM   3056 H  HD3  . ARG   A 1 196 ? -18.563 -15.321 -17.980 1.00 55.32  ? 193 ARG   A HD3  1 
ATOM   3057 H  HE   . ARG   A 1 196 ? -16.160 -16.091 -17.859 1.00 50.83  ? 193 ARG   A HE   1 
ATOM   3058 H  HH11 . ARG   A 1 196 ? -18.565 -17.171 -19.880 1.00 55.66  ? 193 ARG   A HH11 1 
ATOM   3059 H  HH12 . ARG   A 1 196 ? -17.649 -17.653 -20.952 1.00 55.66  ? 193 ARG   A HH12 1 
ATOM   3060 H  HH21 . ARG   A 1 196 ? -14.811 -16.834 -19.481 1.00 51.58  ? 193 ARG   A HH21 1 
ATOM   3061 H  HH22 . ARG   A 1 196 ? -15.382 -17.449 -20.712 1.00 51.58  ? 193 ARG   A HH22 1 
ATOM   3062 N  N    . THR   A 1 197 ? -20.747 -17.379 -12.779 1.00 32.15  ? 194 THR   A N    1 
ATOM   3063 C  CA   . THR   A 1 197 ? -22.066 -17.605 -12.198 1.00 29.99  ? 194 THR   A CA   1 
ATOM   3064 C  C    . THR   A 1 197 ? -22.262 -16.743 -10.958 1.00 28.61  ? 194 THR   A C    1 
ATOM   3065 O  O    . THR   A 1 197 ? -23.315 -16.109 -10.816 1.00 27.68  ? 194 THR   A O    1 
ATOM   3066 C  CB   . THR   A 1 197 ? -22.245 -19.089 -11.870 1.00 36.71  ? 194 THR   A CB   1 
ATOM   3067 O  OG1  . THR   A 1 197 ? -22.093 -19.830 -13.090 1.00 35.81  ? 194 THR   A OG1  1 
ATOM   3068 C  CG2  . THR   A 1 197 ? -23.613 -19.349 -11.276 1.00 39.06  ? 194 THR   A CG2  1 
ATOM   3069 H  H    . THR   A 1 197 ? -20.214 -18.053 -12.750 1.00 38.62  ? 194 THR   A H    1 
ATOM   3070 H  HA   . THR   A 1 197 ? -22.747 -17.360 -12.844 1.00 36.03  ? 194 THR   A HA   1 
ATOM   3071 H  HB   . THR   A 1 197 ? -21.588 -19.376 -11.217 1.00 44.10  ? 194 THR   A HB   1 
ATOM   3072 H  HG1  . THR   A 1 197 ? -21.303 -19.769 -13.368 1.00 43.01  ? 194 THR   A HG1  1 
ATOM   3073 H  HG21 . THR   A 1 197 ? -23.736 -20.300 -11.131 1.00 46.92  ? 194 THR   A HG21 1 
ATOM   3074 H  HG22 . THR   A 1 197 ? -23.698 -18.887 -10.427 1.00 46.92  ? 194 THR   A HG22 1 
ATOM   3075 H  HG23 . THR   A 1 197 ? -24.302 -19.030 -11.879 1.00 46.92  ? 194 THR   A HG23 1 
ATOM   3076 N  N    . MET   A 1 198 ? -21.268 -16.706 -10.064 1.00 30.34  ? 195 MET   A N    1 
ATOM   3077 C  CA   . MET   A 1 198 ? -21.359 -15.865 -8.867  1.00 28.38  ? 195 MET   A CA   1 
ATOM   3078 C  C    . MET   A 1 198 ? -21.453 -14.397 -9.233  1.00 29.87  ? 195 MET   A C    1 
ATOM   3079 O  O    . MET   A 1 198 ? -22.168 -13.623 -8.585  1.00 30.09  ? 195 MET   A O    1 
ATOM   3080 C  CB   . MET   A 1 198 ? -20.162 -16.095 -7.942  1.00 32.01  ? 195 MET   A CB   1 
ATOM   3081 C  CG   . MET   A 1 198 ? -20.061 -17.517 -7.429  1.00 37.17  ? 195 MET   A CG   1 
ATOM   3082 S  SD   . MET   A 1 198 ? -21.581 -17.890 -6.499  1.00 46.35  ? 195 MET   A SD   1 
ATOM   3083 C  CE   . MET   A 1 198 ? -21.431 -16.789 -5.113  1.00 55.52  ? 195 MET   A CE   1 
ATOM   3084 H  H    . MET   A 1 198 ? -20.537 -17.154 -10.127 1.00 36.45  ? 195 MET   A H    1 
ATOM   3085 H  HA   . MET   A 1 198 ? -22.157 -16.130 -8.383  1.00 34.09  ? 195 MET   A HA   1 
ATOM   3086 H  HB2  . MET   A 1 198 ? -19.348 -15.895 -8.429  1.00 38.46  ? 195 MET   A HB2  1 
ATOM   3087 H  HB3  . MET   A 1 198 ? -20.242 -15.507 -7.175  1.00 38.46  ? 195 MET   A HB3  1 
ATOM   3088 H  HG2  . MET   A 1 198 ? -19.980 -18.135 -8.172  1.00 44.65  ? 195 MET   A HG2  1 
ATOM   3089 H  HG3  . MET   A 1 198 ? -19.296 -17.605 -6.839  1.00 44.65  ? 195 MET   A HG3  1 
ATOM   3090 H  HE1  . MET   A 1 198 ? -22.193 -16.915 -4.526  1.00 66.67  ? 195 MET   A HE1  1 
ATOM   3091 H  HE2  . MET   A 1 198 ? -20.611 -16.991 -4.637  1.00 66.67  ? 195 MET   A HE2  1 
ATOM   3092 H  HE3  . MET   A 1 198 ? -21.410 -15.875 -5.436  1.00 66.67  ? 195 MET   A HE3  1 
ATOM   3093 N  N    . PHE   A 1 199 ? -20.749 -13.986 -10.279 1.00 27.46  ? 196 PHE   A N    1 
ATOM   3094 C  CA   . PHE   A 1 199 ? -20.862 -12.594 -10.698 1.00 26.52  ? 196 PHE   A CA   1 
ATOM   3095 C  C    . PHE   A 1 199 ? -22.257 -12.276 -11.229 1.00 26.42  ? 196 PHE   A C    1 
ATOM   3096 O  O    . PHE   A 1 199 ? -22.865 -11.278 -10.850 1.00 24.75  ? 196 PHE   A O    1 
ATOM   3097 C  CB   . PHE   A 1 199 ? -19.828 -12.281 -11.767 1.00 28.44  ? 196 PHE   A CB   1 
ATOM   3098 C  CG   . PHE   A 1 199 ? -19.910 -10.863 -12.240 1.00 26.41  ? 196 PHE   A CG   1 
ATOM   3099 C  CD1  . PHE   A 1 199 ? -19.276 -9.862  -11.499 1.00 29.80  ? 196 PHE   A CD1  1 
ATOM   3100 C  CD2  . PHE   A 1 199 ? -20.617 -10.528 -13.369 1.00 23.49  ? 196 PHE   A CD2  1 
ATOM   3101 C  CE1  . PHE   A 1 199 ? -19.336 -8.563  -11.892 1.00 26.99  ? 196 PHE   A CE1  1 
ATOM   3102 C  CE2  . PHE   A 1 199 ? -20.712 -9.214  -13.760 1.00 24.42  ? 196 PHE   A CE2  1 
ATOM   3103 C  CZ   . PHE   A 1 199 ? -20.039 -8.251  -13.040 1.00 23.17  ? 196 PHE   A CZ   1 
ATOM   3104 H  H    . PHE   A 1 199 ? -20.217 -14.474 -10.747 1.00 32.99  ? 196 PHE   A H    1 
ATOM   3105 H  HA   . PHE   A 1 199 ? -20.692 -12.036 -9.923  1.00 31.86  ? 196 PHE   A HA   1 
ATOM   3106 H  HB2  . PHE   A 1 199 ? -18.940 -12.426 -11.403 1.00 34.17  ? 196 PHE   A HB2  1 
ATOM   3107 H  HB3  . PHE   A 1 199 ? -19.973 -12.862 -12.529 1.00 34.17  ? 196 PHE   A HB3  1 
ATOM   3108 H  HD1  . PHE   A 1 199 ? -18.807 -10.088 -10.729 1.00 35.80  ? 196 PHE   A HD1  1 
ATOM   3109 H  HD2  . PHE   A 1 199 ? -21.032 -11.192 -13.870 1.00 28.23  ? 196 PHE   A HD2  1 
ATOM   3110 H  HE1  . PHE   A 1 199 ? -18.913 -7.898  -11.398 1.00 32.43  ? 196 PHE   A HE1  1 
ATOM   3111 H  HE2  . PHE   A 1 199 ? -21.224 -8.978  -14.500 1.00 29.34  ? 196 PHE   A HE2  1 
ATOM   3112 H  HZ   . PHE   A 1 199 ? -20.058 -7.369  -13.334 1.00 27.85  ? 196 PHE   A HZ   1 
ATOM   3113 N  N    . TRP   A 1 200 ? -22.751 -13.080 -12.164 1.00 23.39  ? 197 TRP   A N    1 
ATOM   3114 C  CA   . TRP   A 1 200 ? -24.091 -12.890 -12.682 1.00 22.60  ? 197 TRP   A CA   1 
ATOM   3115 C  C    . TRP   A 1 200 ? -25.110 -12.855 -11.564 1.00 24.54  ? 197 TRP   A C    1 
ATOM   3116 O  O    . TRP   A 1 200 ? -26.033 -12.016 -11.580 1.00 22.75  ? 197 TRP   A O    1 
ATOM   3117 C  CB   . TRP   A 1 200 ? -24.369 -14.015 -13.684 1.00 27.67  ? 197 TRP   A CB   1 
ATOM   3118 C  CG   . TRP   A 1 200 ? -25.784 -14.170 -14.101 1.00 27.76  ? 197 TRP   A CG   1 
ATOM   3119 C  CD1  . TRP   A 1 200 ? -26.438 -13.499 -15.061 1.00 28.78  ? 197 TRP   A CD1  1 
ATOM   3120 C  CD2  . TRP   A 1 200 ? -26.720 -15.092 -13.536 1.00 26.09  ? 197 TRP   A CD2  1 
ATOM   3121 N  NE1  . TRP   A 1 200 ? -27.733 -13.940 -15.152 1.00 28.36  ? 197 TRP   A NE1  1 
ATOM   3122 C  CE2  . TRP   A 1 200 ? -27.928 -14.926 -14.226 1.00 28.63  ? 197 TRP   A CE2  1 
ATOM   3123 C  CE3  . TRP   A 1 200 ? -26.644 -16.039 -12.519 1.00 32.12  ? 197 TRP   A CE3  1 
ATOM   3124 C  CZ2  . TRP   A 1 200 ? -29.065 -15.658 -13.918 1.00 33.50  ? 197 TRP   A CZ2  1 
ATOM   3125 C  CZ3  . TRP   A 1 200 ? -27.765 -16.776 -12.223 1.00 39.56  ? 197 TRP   A CZ3  1 
ATOM   3126 C  CH2  . TRP   A 1 200 ? -28.958 -16.587 -12.930 1.00 35.03  ? 197 TRP   A CH2  1 
ATOM   3127 H  H    . TRP   A 1 200 ? -22.328 -13.742 -12.513 1.00 28.11  ? 197 TRP   A H    1 
ATOM   3128 H  HA   . TRP   A 1 200 ? -24.169 -12.042 -13.146 1.00 27.16  ? 197 TRP   A HA   1 
ATOM   3129 H  HB2  . TRP   A 1 200 ? -23.850 -13.844 -14.486 1.00 33.25  ? 197 TRP   A HB2  1 
ATOM   3130 H  HB3  . TRP   A 1 200 ? -24.094 -14.854 -13.284 1.00 33.25  ? 197 TRP   A HB3  1 
ATOM   3131 H  HD1  . TRP   A 1 200 ? -26.066 -12.830 -15.590 1.00 34.58  ? 197 TRP   A HD1  1 
ATOM   3132 H  HE1  . TRP   A 1 200 ? -28.325 -13.645 -15.702 1.00 34.07  ? 197 TRP   A HE1  1 
ATOM   3133 H  HE3  . TRP   A 1 200 ? -25.852 -16.170 -12.049 1.00 38.59  ? 197 TRP   A HE3  1 
ATOM   3134 H  HZ2  . TRP   A 1 200 ? -29.867 -15.519 -14.368 1.00 40.24  ? 197 TRP   A HZ2  1 
ATOM   3135 H  HZ3  . TRP   A 1 200 ? -27.731 -17.410 -11.544 1.00 47.52  ? 197 TRP   A HZ3  1 
ATOM   3136 H  HH2  . TRP   A 1 200 ? -29.697 -17.110 -12.718 1.00 42.07  ? 197 TRP   A HH2  1 
ATOM   3137 N  N    . LEU   A 1 201 ? -24.926 -13.714 -10.560 1.00 26.66  ? 198 LEU   A N    1 
ATOM   3138 C  CA   . LEU   A 1 201 ? -25.878 -13.821 -9.460  1.00 29.13  ? 198 LEU   A CA   1 
ATOM   3139 C  C    . LEU   A 1 201 ? -25.953 -12.524 -8.676  1.00 25.81  ? 198 LEU   A C    1 
ATOM   3140 O  O    . LEU   A 1 201 ? -27.054 -11.989 -8.439  1.00 30.03  ? 198 LEU   A O    1 
ATOM   3141 C  CB   . LEU   A 1 201 ? -25.453 -14.981 -8.578  1.00 31.22  ? 198 LEU   A CB   1 
ATOM   3142 C  CG   . LEU   A 1 201 ? -26.373 -16.166 -8.395  1.00 47.50  ? 198 LEU   A CG   1 
ATOM   3143 C  CD1  . LEU   A 1 201 ? -25.760 -17.020 -7.275  1.00 47.40  ? 198 LEU   A CD1  1 
ATOM   3144 C  CD2  . LEU   A 1 201 ? -27.744 -15.766 -8.041  1.00 40.12  ? 198 LEU   A CD2  1 
ATOM   3145 H  H    . LEU   A 1 201 ? -24.256 -14.249 -10.494 1.00 32.03  ? 198 LEU   A H    1 
ATOM   3146 H  HA   . LEU   A 1 201 ? -26.769 -13.996 -9.800  1.00 35.00  ? 198 LEU   A HA   1 
ATOM   3147 H  HB2  . LEU   A 1 201 ? -24.628 -15.334 -8.946  1.00 37.51  ? 198 LEU   A HB2  1 
ATOM   3148 H  HB3  . LEU   A 1 201 ? -25.295 -14.624 -7.690  1.00 37.51  ? 198 LEU   A HB3  1 
ATOM   3149 H  HG   . LEU   A 1 201 ? -26.454 -16.663 -9.225  1.00 57.04  ? 198 LEU   A HG   1 
ATOM   3150 H  HD11 . LEU   A 1 201 ? -26.323 -17.795 -7.125  1.00 56.92  ? 198 LEU   A HD11 1 
ATOM   3151 H  HD12 . LEU   A 1 201 ? -24.872 -17.303 -7.544  1.00 56.92  ? 198 LEU   A HD12 1 
ATOM   3152 H  HD13 . LEU   A 1 201 ? -25.707 -16.488 -6.466  1.00 56.92  ? 198 LEU   A HD13 1 
ATOM   3153 H  HD21 . LEU   A 1 201 ? -28.287 -16.563 -7.932  1.00 48.18  ? 198 LEU   A HD21 1 
ATOM   3154 H  HD22 . LEU   A 1 201 ? -27.722 -15.265 -7.211  1.00 48.18  ? 198 LEU   A HD22 1 
ATOM   3155 H  HD23 . LEU   A 1 201 ? -28.105 -15.214 -8.752  1.00 48.18  ? 198 LEU   A HD23 1 
ATOM   3156 N  N    . GLU   A 1 202 ? -24.805 -11.971 -8.324  1.00 27.25  ? 199 GLU   A N    1 
ATOM   3157 C  CA   . GLU   A 1 202 ? -24.765 -10.791 -7.464  1.00 28.51  ? 199 GLU   A CA   1 
ATOM   3158 C  C    . GLU   A 1 202 ? -25.006 -9.509  -8.251  1.00 28.38  ? 199 GLU   A C    1 
ATOM   3159 O  O    . GLU   A 1 202 ? -25.658 -8.573  -7.764  1.00 26.55  ? 199 GLU   A O    1 
ATOM   3160 C  CB   . GLU   A 1 202 ? -23.426 -10.699 -6.743  1.00 31.43  ? 199 GLU   A CB   1 
ATOM   3161 C  CG   . GLU   A 1 202 ? -23.293 -9.426  -5.925  1.00 36.94  ? 199 GLU   A CG   1 
ATOM   3162 C  CD   . GLU   A 1 202 ? -22.130 -9.472  -4.970  1.00 53.47  ? 199 GLU   A CD   1 
ATOM   3163 O  OE1  . GLU   A 1 202 ? -21.943 -8.491  -4.219  1.00 51.46  ? 199 GLU   A OE1  1 
ATOM   3164 O  OE2  . GLU   A 1 202 ? -21.385 -10.482 -5.009  1.00 50.07  ? 199 GLU   A OE2  1 
ATOM   3165 H  H    . GLU   A 1 202 ? -24.031 -12.256 -8.567  1.00 32.74  ? 199 GLU   A H    1 
ATOM   3166 H  HA   . GLU   A 1 202 ? -25.465 -10.883 -6.799  1.00 34.26  ? 199 GLU   A HA   1 
ATOM   3167 H  HB2  . GLU   A 1 202 ? -23.338 -11.455 -6.141  1.00 37.76  ? 199 GLU   A HB2  1 
ATOM   3168 H  HB3  . GLU   A 1 202 ? -22.711 -10.712 -7.398  1.00 37.76  ? 199 GLU   A HB3  1 
ATOM   3169 H  HG2  . GLU   A 1 202 ? -23.159 -8.676  -6.525  1.00 44.36  ? 199 GLU   A HG2  1 
ATOM   3170 H  HG3  . GLU   A 1 202 ? -24.102 -9.297  -5.407  1.00 44.36  ? 199 GLU   A HG3  1 
ATOM   3171 N  N    . PHE   A 1 203 ? -24.499 -9.447  -9.480  1.00 24.62  ? 200 PHE   A N    1 
ATOM   3172 C  CA   . PHE   A 1 203 ? -24.410 -8.182  -10.205 1.00 21.80  ? 200 PHE   A CA   1 
ATOM   3173 C  C    . PHE   A 1 203 ? -25.276 -8.067  -11.453 1.00 20.36  ? 200 PHE   A C    1 
ATOM   3174 O  O    . PHE   A 1 203 ? -25.330 -6.973  -12.043 1.00 20.54  ? 200 PHE   A O    1 
ATOM   3175 C  CB   . PHE   A 1 203 ? -22.934 -7.956  -10.632 1.00 23.58  ? 200 PHE   A CB   1 
ATOM   3176 C  CG   . PHE   A 1 203 ? -22.029 -7.675  -9.488  1.00 24.32  ? 200 PHE   A CG   1 
ATOM   3177 C  CD1  . PHE   A 1 203 ? -21.860 -6.375  -9.027  1.00 29.46  ? 200 PHE   A CD1  1 
ATOM   3178 C  CD2  . PHE   A 1 203 ? -21.336 -8.695  -8.862  1.00 29.03  ? 200 PHE   A CD2  1 
ATOM   3179 C  CE1  . PHE   A 1 203 ? -21.037 -6.095  -7.958  1.00 31.15  ? 200 PHE   A CE1  1 
ATOM   3180 C  CE2  . PHE   A 1 203 ? -20.517 -8.420  -7.765  1.00 33.12  ? 200 PHE   A CE2  1 
ATOM   3181 C  CZ   . PHE   A 1 203 ? -20.363 -7.109  -7.329  1.00 33.55  ? 200 PHE   A CZ   1 
ATOM   3182 H  H    . PHE   A 1 203 ? -24.199 -10.125 -9.915  1.00 29.58  ? 200 PHE   A H    1 
ATOM   3183 H  HA   . PHE   A 1 203 ? -24.706 -7.481  -9.603  1.00 26.21  ? 200 PHE   A HA   1 
ATOM   3184 H  HB2  . PHE   A 1 203 ? -22.611 -8.754  -11.079 1.00 28.33  ? 200 PHE   A HB2  1 
ATOM   3185 H  HB3  . PHE   A 1 203 ? -22.894 -7.198  -11.237 1.00 28.33  ? 200 PHE   A HB3  1 
ATOM   3186 H  HD1  . PHE   A 1 203 ? -22.312 -5.680  -9.448  1.00 35.39  ? 200 PHE   A HD1  1 
ATOM   3187 H  HD2  . PHE   A 1 203 ? -21.415 -9.568  -9.173  1.00 34.88  ? 200 PHE   A HD2  1 
ATOM   3188 H  HE1  . PHE   A 1 203 ? -20.939 -5.218  -7.663  1.00 37.43  ? 200 PHE   A HE1  1 
ATOM   3189 H  HE2  . PHE   A 1 203 ? -20.076 -9.112  -7.327  1.00 39.78  ? 200 PHE   A HE2  1 
ATOM   3190 H  HZ   . PHE   A 1 203 ? -19.802 -6.921  -6.611  1.00 40.30  ? 200 PHE   A HZ   1 
ATOM   3191 N  N    . GLU   A 1 204 ? -25.969 -9.123  -11.893 1.00 19.19  ? 201 GLU   A N    1 
ATOM   3192 C  CA   . GLU   A 1 204 ? -26.742 -9.071  -13.126 1.00 17.61  ? 201 GLU   A CA   1 
ATOM   3193 C  C    . GLU   A 1 204 ? -28.206 -9.441  -12.957 1.00 18.57  ? 201 GLU   A C    1 
ATOM   3194 O  O    . GLU   A 1 204 ? -29.075 -8.706  -13.430 1.00 20.42  ? 201 GLU   A O    1 
ATOM   3195 C  CB   . GLU   A 1 204 ? -26.091 -9.957  -14.210 1.00 18.67  ? 201 GLU   A CB   1 
ATOM   3196 C  CG   . GLU   A 1 204 ? -26.702 -9.766  -15.585 1.00 18.64  ? 201 GLU   A CG   1 
ATOM   3197 C  CD   . GLU   A 1 204 ? -25.691 -10.012 -16.695 1.00 20.01  ? 201 GLU   A CD   1 
ATOM   3198 O  OE1  . GLU   A 1 204 ? -24.604 -9.399  -16.668 1.00 20.38  ? 201 GLU   A OE1  1 
ATOM   3199 O  OE2  . GLU   A 1 204 ? -26.030 -10.832 -17.585 1.00 24.39  ? 201 GLU   A OE2  1 
ATOM   3200 H  H    . GLU   A 1 204 ? -26.004 -9.882  -11.489 1.00 23.06  ? 201 GLU   A H    1 
ATOM   3201 H  HA   . GLU   A 1 204 ? -26.723 -8.152  -13.439 1.00 21.18  ? 201 GLU   A HA   1 
ATOM   3202 H  HB2  . GLU   A 1 204 ? -25.148 -9.739  -14.270 1.00 22.45  ? 201 GLU   A HB2  1 
ATOM   3203 H  HB3  . GLU   A 1 204 ? -26.201 -10.889 -13.962 1.00 22.45  ? 201 GLU   A HB3  1 
ATOM   3204 H  HG2  . GLU   A 1 204 ? -27.435 -10.391 -15.698 1.00 22.41  ? 201 GLU   A HG2  1 
ATOM   3205 H  HG3  . GLU   A 1 204 ? -27.026 -8.855  -15.666 1.00 22.41  ? 201 GLU   A HG3  1 
ATOM   3206 N  N    . ILE   A 1 205 ? -28.524 -10.590 -12.387 1.00 20.16  ? 202 ILE   A N    1 
ATOM   3207 C  CA   . ILE   A 1 205 ? -29.878 -11.110 -12.519 1.00 22.67  ? 202 ILE   A CA   1 
ATOM   3208 C  C    . ILE   A 1 205 ? -30.913 -10.127 -11.943 1.00 20.09  ? 202 ILE   A C    1 
ATOM   3209 O  O    . ILE   A 1 205 ? -31.877 -9.749  -12.630 1.00 22.31  ? 202 ILE   A O    1 
ATOM   3210 C  CB   . ILE   A 1 205 ? -29.947 -12.520 -11.909 1.00 26.14  ? 202 ILE   A CB   1 
ATOM   3211 C  CG1  . ILE   A 1 205 ? -31.262 -13.218 -12.322 1.00 36.37  ? 202 ILE   A CG1  1 
ATOM   3212 C  CG2  . ILE   A 1 205 ? -29.723 -12.491 -10.433 1.00 28.72  ? 202 ILE   A CG2  1 
ATOM   3213 C  CD1  . ILE   A 1 205 ? -32.440 -12.774 -11.609 1.00 37.85  ? 202 ILE   A CD1  1 
ATOM   3214 H  H    . ILE   A 1 205 ? -27.988 -11.081 -11.927 1.00 24.23  ? 202 ILE   A H    1 
ATOM   3215 H  HA   . ILE   A 1 205 ? -30.103 -11.191 -13.459 1.00 27.25  ? 202 ILE   A HA   1 
ATOM   3216 H  HB   . ILE   A 1 205 ? -29.222 -13.054 -12.270 1.00 31.41  ? 202 ILE   A HB   1 
ATOM   3217 H  HG12 . ILE   A 1 205 ? -31.414 -13.054 -13.265 1.00 43.69  ? 202 ILE   A HG12 1 
ATOM   3218 H  HG13 . ILE   A 1 205 ? -31.167 -14.170 -12.162 1.00 43.69  ? 202 ILE   A HG13 1 
ATOM   3219 H  HG21 . ILE   A 1 205 ? -29.665 -13.401 -10.104 1.00 34.51  ? 202 ILE   A HG21 1 
ATOM   3220 H  HG22 . ILE   A 1 205 ? -28.895 -12.019 -10.249 1.00 34.51  ? 202 ILE   A HG22 1 
ATOM   3221 H  HG23 . ILE   A 1 205 ? -30.465 -12.032 -10.010 1.00 34.51  ? 202 ILE   A HG23 1 
ATOM   3222 H  HD11 . ILE   A 1 205 ? -33.149 -13.424 -11.736 1.00 45.46  ? 202 ILE   A HD11 1 
ATOM   3223 H  HD12 . ILE   A 1 205 ? -32.227 -12.696 -10.666 1.00 45.46  ? 202 ILE   A HD12 1 
ATOM   3224 H  HD13 . ILE   A 1 205 ? -32.714 -11.912 -11.959 1.00 45.46  ? 202 ILE   A HD13 1 
ATOM   3225 N  N    . ARG   A 1 206 ? -30.733 -9.676  -10.702 1.00 20.74  ? 203 ARG   A N    1 
ATOM   3226 C  CA   . ARG   A 1 206 ? -31.745 -8.777  -10.124 1.00 22.79  ? 203 ARG   A CA   1 
ATOM   3227 C  C    . ARG   A 1 206 ? -31.766 -7.430  -10.835 1.00 22.68  ? 203 ARG   A C    1 
ATOM   3228 O  O    . ARG   A 1 206 ? -32.854 -6.905  -11.149 1.00 22.22  ? 203 ARG   A O    1 
ATOM   3229 C  CB   . ARG   A 1 206 ? -31.495 -8.565  -8.620  1.00 21.95  ? 203 ARG   A CB   1 
ATOM   3230 C  CG   . ARG   A 1 206 ? -31.615 -9.832  -7.775  1.00 23.94  ? 203 ARG   A CG   1 
ATOM   3231 C  CD   . ARG   A 1 206 ? -31.068 -9.669  -6.365  1.00 26.95  ? 203 ARG   A CD   1 
ATOM   3232 N  NE   . ARG   A 1 206 ? -29.621 -9.456  -6.405  1.00 25.00  ? 203 ARG   A NE   1 
ATOM   3233 C  CZ   . ARG   A 1 206 ? -28.884 -9.180  -5.340  1.00 25.11  ? 203 ARG   A CZ   1 
ATOM   3234 N  NH1  . ARG   A 1 206 ? -29.418 -9.082  -4.129  1.00 29.98  ? 203 ARG   A NH1  1 
ATOM   3235 N  NH2  . ARG   A 1 206 ? -27.577 -8.985  -5.489  1.00 28.80  ? 203 ARG   A NH2  1 
ATOM   3236 H  H    . ARG   A 1 206 ? -30.066 -9.864  -10.192 1.00 24.93  ? 203 ARG   A H    1 
ATOM   3237 H  HA   . ARG   A 1 206 ? -32.612 -9.199  -10.230 1.00 27.39  ? 203 ARG   A HA   1 
ATOM   3238 H  HB2  . ARG   A 1 206 ? -30.597 -8.218  -8.501  1.00 26.38  ? 203 ARG   A HB2  1 
ATOM   3239 H  HB3  . ARG   A 1 206 ? -32.144 -7.927  -8.285  1.00 26.38  ? 203 ARG   A HB3  1 
ATOM   3240 H  HG2  . ARG   A 1 206 ? -32.551 -10.075 -7.704  1.00 28.76  ? 203 ARG   A HG2  1 
ATOM   3241 H  HG3  . ARG   A 1 206 ? -31.118 -10.545 -8.205  1.00 28.76  ? 203 ARG   A HG3  1 
ATOM   3242 H  HD2  . ARG   A 1 206 ? -31.484 -8.902  -5.941  1.00 32.38  ? 203 ARG   A HD2  1 
ATOM   3243 H  HD3  . ARG   A 1 206 ? -31.250 -10.471 -5.851  1.00 32.38  ? 203 ARG   A HD3  1 
ATOM   3244 H  HE   . ARG   A 1 206 ? -29.226 -9.514  -7.166  1.00 30.04  ? 203 ARG   A HE   1 
ATOM   3245 H  HH11 . ARG   A 1 206 ? -30.264 -9.198  -4.022  1.00 36.02  ? 203 ARG   A HH11 1 
ATOM   3246 H  HH12 . ARG   A 1 206 ? -28.920 -8.902  -3.452  1.00 36.02  ? 203 ARG   A HH12 1 
ATOM   3247 H  HH21 . ARG   A 1 206 ? -27.221 -9.039  -6.270  1.00 34.60  ? 203 ARG   A HH21 1 
ATOM   3248 H  HH22 . ARG   A 1 206 ? -27.088 -8.805  -4.805  1.00 34.60  ? 203 ARG   A HH22 1 
ATOM   3249 N  N    . GLN   A 1 207 ? -30.574 -6.883  -11.116 1.00 20.57  ? 204 GLN   A N    1 
ATOM   3250 C  CA   . GLN   A 1 207 ? -30.439 -5.557  -11.690 1.00 19.11  ? 204 GLN   A CA   1 
ATOM   3251 C  C    . GLN   A 1 207 ? -31.014 -5.517  -13.096 1.00 19.80  ? 204 GLN   A C    1 
ATOM   3252 O  O    . GLN   A 1 207 ? -31.715 -4.564  -13.460 1.00 25.17  ? 204 GLN   A O    1 
ATOM   3253 C  CB   . GLN   A 1 207 ? -28.972 -5.163  -11.701 1.00 21.31  ? 204 GLN   A CB   1 
ATOM   3254 C  CG   . GLN   A 1 207 ? -28.338 -4.973  -10.313 1.00 22.90  ? 204 GLN   A CG   1 
ATOM   3255 C  CD   . GLN   A 1 207 ? -27.765 -6.236  -9.681  1.00 20.70  ? 204 GLN   A CD   1 
ATOM   3256 O  OE1  . GLN   A 1 207 ? -28.032 -7.379  -10.120 1.00 21.43  ? 204 GLN   A OE1  1 
ATOM   3257 N  NE2  . GLN   A 1 207 ? -27.004 -6.043  -8.619  1.00 21.52  ? 204 GLN   A NE2  1 
ATOM   3258 H  H    . GLN   A 1 207 ? -29.820 -7.272  -10.977 1.00 24.72  ? 204 GLN   A H    1 
ATOM   3259 H  HA   . GLN   A 1 207 ? -30.925 -4.915  -11.149 1.00 22.98  ? 204 GLN   A HA   1 
ATOM   3260 H  HB2  . GLN   A 1 207 ? -28.471 -5.857  -12.156 1.00 25.61  ? 204 GLN   A HB2  1 
ATOM   3261 H  HB3  . GLN   A 1 207 ? -28.883 -4.323  -12.178 1.00 25.61  ? 204 GLN   A HB3  1 
ATOM   3262 H  HG2  . GLN   A 1 207 ? -27.612 -4.334  -10.393 1.00 27.53  ? 204 GLN   A HG2  1 
ATOM   3263 H  HG3  . GLN   A 1 207 ? -29.017 -4.631  -9.711  1.00 27.53  ? 204 GLN   A HG3  1 
ATOM   3264 H  HE21 . GLN   A 1 207 ? -26.862 -5.245  -8.331  1.00 25.86  ? 204 GLN   A HE21 1 
ATOM   3265 H  HE22 . GLN   A 1 207 ? -26.650 -6.715  -8.216  1.00 25.86  ? 204 GLN   A HE22 1 
ATOM   3266 N  N    . TYR   A 1 208 ? -30.797 -6.563  -13.869 1.00 17.33  ? 205 TYR   A N    1 
ATOM   3267 C  CA   . TYR   A 1 208 ? -31.222 -6.467  -15.261 1.00 15.65  ? 205 TYR   A CA   1 
ATOM   3268 C  C    . TYR   A 1 208 ? -32.702 -6.826  -15.426 1.00 16.93  ? 205 TYR   A C    1 
ATOM   3269 O  O    . TYR   A 1 208 ? -33.439 -6.161  -16.188 1.00 17.62  ? 205 TYR   A O    1 
ATOM   3270 C  CB   . TYR   A 1 208 ? -30.384 -7.385  -16.163 1.00 16.87  ? 205 TYR   A CB   1 
ATOM   3271 C  CG   . TYR   A 1 208 ? -28.991 -6.925  -16.493 1.00 15.73  ? 205 TYR   A CG   1 
ATOM   3272 C  CD1  . TYR   A 1 208 ? -28.203 -6.251  -15.554 1.00 17.16  ? 205 TYR   A CD1  1 
ATOM   3273 C  CD2  . TYR   A 1 208 ? -28.444 -7.162  -17.744 1.00 16.21  ? 205 TYR   A CD2  1 
ATOM   3274 C  CE1  . TYR   A 1 208 ? -26.912 -5.825  -15.830 1.00 19.30  ? 205 TYR   A CE1  1 
ATOM   3275 C  CE2  . TYR   A 1 208 ? -27.132 -6.744  -18.033 1.00 17.82  ? 205 TYR   A CE2  1 
ATOM   3276 C  CZ   . TYR   A 1 208 ? -26.372 -6.080  -17.062 1.00 17.37  ? 205 TYR   A CZ   1 
ATOM   3277 O  OH   . TYR   A 1 208 ? -25.081 -5.674  -17.323 1.00 19.36  ? 205 TYR   A OH   1 
ATOM   3278 H  H    . TYR   A 1 208 ? -30.426 -7.301  -13.632 1.00 20.84  ? 205 TYR   A H    1 
ATOM   3279 H  HA   . TYR   A 1 208 ? -31.080 -5.550  -15.544 1.00 18.82  ? 205 TYR   A HA   1 
ATOM   3280 H  HB2  . TYR   A 1 208 ? -30.301 -8.245  -15.721 1.00 20.28  ? 205 TYR   A HB2  1 
ATOM   3281 H  HB3  . TYR   A 1 208 ? -30.855 -7.489  -17.005 1.00 20.28  ? 205 TYR   A HB3  1 
ATOM   3282 H  HD1  . TYR   A 1 208 ? -28.559 -6.083  -14.711 1.00 20.63  ? 205 TYR   A HD1  1 
ATOM   3283 H  HD2  . TYR   A 1 208 ? -28.945 -7.599  -18.394 1.00 19.49  ? 205 TYR   A HD2  1 
ATOM   3284 H  HE1  . TYR   A 1 208 ? -26.418 -5.371  -15.185 1.00 23.20  ? 205 TYR   A HE1  1 
ATOM   3285 H  HE2  . TYR   A 1 208 ? -26.768 -6.908  -18.873 1.00 21.42  ? 205 TYR   A HE2  1 
ATOM   3286 H  HH   . TYR   A 1 208 ? -24.799 -6.044  -18.023 1.00 23.28  ? 205 TYR   A HH   1 
ATOM   3287 N  N    . THR   A 1 209 ? -33.157 -7.877  -14.722 1.00 17.86  ? 206 THR   A N    1 
ATOM   3288 C  CA   . THR   A 1 209 ? -34.533 -8.321  -14.900 1.00 17.72  ? 206 THR   A CA   1 
ATOM   3289 C  C    . THR   A 1 209 ? -35.570 -7.364  -14.296 1.00 19.29  ? 206 THR   A C    1 
ATOM   3290 O  O    . THR   A 1 209 ? -36.766 -7.472  -14.639 1.00 19.17  ? 206 THR   A O    1 
ATOM   3291 C  CB   . THR   A 1 209 ? -34.777 -9.712  -14.316 1.00 18.95  ? 206 THR   A CB   1 
ATOM   3292 O  OG1  . THR   A 1 209 ? -34.536 -9.722  -12.893 1.00 21.89  ? 206 THR   A OG1  1 
ATOM   3293 C  CG2  . THR   A 1 209 ? -33.877 -10.760 -15.000 1.00 21.83  ? 206 THR   A CG2  1 
ATOM   3294 H  H    . THR   A 1 209 ? -32.696 -8.330  -14.154 1.00 21.47  ? 206 THR   A H    1 
ATOM   3295 H  HA   . THR   A 1 209 ? -34.667 -8.370  -15.860 1.00 21.30  ? 206 THR   A HA   1 
ATOM   3296 H  HB   . THR   A 1 209 ? -35.704 -9.954  -14.473 1.00 22.79  ? 206 THR   A HB   1 
ATOM   3297 H  HG1  . THR   A 1 209 ? -33.782 -9.389  -12.727 1.00 26.31  ? 206 THR   A HG1  1 
ATOM   3298 H  HG21 . THR   A 1 209 ? -33.999 -11.627 -14.582 1.00 26.24  ? 206 THR   A HG21 1 
ATOM   3299 H  HG22 . THR   A 1 209 ? -34.104 -10.830 -15.941 1.00 26.24  ? 206 THR   A HG22 1 
ATOM   3300 H  HG23 . THR   A 1 209 ? -32.945 -10.500 -14.920 1.00 26.24  ? 206 THR   A HG23 1 
ATOM   3301 N  N    . HIS   A 1 210 ? -35.178 -6.458  -13.404 1.00 17.61  ? 207 HIS   A N    1 
ATOM   3302 C  CA   . HIS   A 1 210 ? -36.089 -5.424  -12.927 1.00 17.07  ? 207 HIS   A CA   1 
ATOM   3303 C  C    . HIS   A 1 210 ? -35.676 -4.029  -13.389 1.00 21.30  ? 207 HIS   A C    1 
ATOM   3304 O  O    . HIS   A 1 210 ? -35.955 -3.024  -12.731 1.00 21.46  ? 207 HIS   A O    1 
ATOM   3305 C  CB   . HIS   A 1 210 ? -36.254 -5.473  -11.409 1.00 19.64  ? 207 HIS   A CB   1 
ATOM   3306 C  CG   . HIS   A 1 210 ? -37.557 -4.878  -10.935 1.00 22.06  ? 207 HIS   A CG   1 
ATOM   3307 N  ND1  . HIS   A 1 210 ? -38.781 -5.448  -11.198 1.00 23.88  ? 207 HIS   A ND1  1 
ATOM   3308 C  CD2  . HIS   A 1 210 ? -37.825 -3.738  -10.247 1.00 22.40  ? 207 HIS   A CD2  1 
ATOM   3309 C  CE1  . HIS   A 1 210 ? -39.748 -4.692  -10.697 1.00 24.78  ? 207 HIS   A CE1  1 
ATOM   3310 N  NE2  . HIS   A 1 210 ? -39.197 -3.648  -10.113 1.00 26.49  ? 207 HIS   A NE2  1 
ATOM   3311 H  H    . HIS   A 1 210 ? -34.390 -6.424  -13.061 1.00 21.17  ? 207 HIS   A H    1 
ATOM   3312 H  HA   . HIS   A 1 210 ? -36.961 -5.607  -13.309 1.00 20.52  ? 207 HIS   A HA   1 
ATOM   3313 H  HB2  . HIS   A 1 210 ? -36.225 -6.398  -11.119 1.00 23.61  ? 207 HIS   A HB2  1 
ATOM   3314 H  HB3  . HIS   A 1 210 ? -35.531 -4.974  -10.998 1.00 23.61  ? 207 HIS   A HB3  1 
ATOM   3315 H  HD1  . HIS   A 1 210 ? -38.902 -6.185  -11.624 1.00 28.70  ? 207 HIS   A HD1  1 
ATOM   3316 H  HD2  . HIS   A 1 210 ? -37.200 -3.129  -9.927  1.00 26.92  ? 207 HIS   A HD2  1 
ATOM   3317 H  HE1  . HIS   A 1 210 ? -40.660 -4.868  -10.749 1.00 29.77  ? 207 HIS   A HE1  1 
ATOM   3318 N  N    . SER   A 1 211 ? -35.070 -3.949  -14.568 1.00 19.09  ? 208 SER   A N    1 
ATOM   3319 C  CA   . SER   A 1 211 ? -34.603 -2.659  -15.044 1.00 18.69  ? 208 SER   A CA   1 
ATOM   3320 C  C    . SER   A 1 211 ? -35.713 -1.889  -15.744 1.00 18.69  ? 208 SER   A C    1 
ATOM   3321 O  O    . SER   A 1 211 ? -36.824 -2.382  -15.937 1.00 19.84  ? 208 SER   A O    1 
ATOM   3322 C  CB   . SER   A 1 211 ? -33.391 -2.856  -15.963 1.00 17.10  ? 208 SER   A CB   1 
ATOM   3323 O  OG   . SER   A 1 211 ? -33.735 -3.548  -17.143 1.00 18.53  ? 208 SER   A OG   1 
ATOM   3324 H  H    . SER   A 1 211 ? -34.923 -4.612  -15.097 1.00 22.94  ? 208 SER   A H    1 
ATOM   3325 H  HA   . SER   A 1 211 ? -34.328 -2.118  -14.287 1.00 22.47  ? 208 SER   A HA   1 
ATOM   3326 H  HB2  . SER   A 1 211 ? -33.038 -1.985  -16.204 1.00 20.56  ? 208 SER   A HB2  1 
ATOM   3327 H  HB3  . SER   A 1 211 ? -32.718 -3.366  -15.486 1.00 20.56  ? 208 SER   A HB3  1 
ATOM   3328 H  HG   . SER   A 1 211 ? -33.987 -4.327  -16.955 1.00 22.28  ? 208 SER   A HG   1 
ATOM   3329 N  N    . ASN   A 1 212 ? -35.419 -0.626  -16.070 1.00 18.65  ? 209 ASN   A N    1 
ATOM   3330 C  CA   . ASN   A 1 212 ? -36.458 0.333   -16.445 1.00 19.42  ? 209 ASN   A CA   1 
ATOM   3331 C  C    . ASN   A 1 212 ? -36.763 0.241   -17.936 1.00 23.33  ? 209 ASN   A C    1 
ATOM   3332 O  O    . ASN   A 1 212 ? -36.326 1.064   -18.737 1.00 22.64  ? 209 ASN   A O    1 
ATOM   3333 C  CB   . ASN   A 1 212 ? -36.015 1.744   -16.060 1.00 23.08  ? 209 ASN   A CB   1 
ATOM   3334 C  CG   . ASN   A 1 212 ? -36.987 2.805   -16.450 1.00 29.31  ? 209 ASN   A CG   1 
ATOM   3335 O  OD1  . ASN   A 1 212 ? -38.200 2.752   -16.145 1.00 26.19  ? 209 ASN   A OD1  1 
ATOM   3336 N  ND2  . ASN   A 1 212 ? -36.479 3.791   -17.168 1.00 27.52  ? 209 ASN   A ND2  1 
ATOM   3337 H  H    . ASN   A 1 212 ? -34.623 -0.302  -16.081 1.00 22.42  ? 209 ASN   A H    1 
ATOM   3338 H  HA   . ASN   A 1 212 ? -37.271 0.096   -15.973 1.00 23.34  ? 209 ASN   A HA   1 
ATOM   3339 H  HB2  . ASN   A 1 212 ? -35.904 1.785   -15.097 1.00 27.74  ? 209 ASN   A HB2  1 
ATOM   3340 H  HB3  . ASN   A 1 212 ? -35.173 1.938   -16.500 1.00 27.74  ? 209 ASN   A HB3  1 
ATOM   3341 H  HD21 . ASN   A 1 212 ? -36.983 4.437   -17.428 1.00 33.07  ? 209 ASN   A HD21 1 
ATOM   3342 H  HD22 . ASN   A 1 212 ? -35.644 3.786   -17.376 1.00 33.07  ? 209 ASN   A HD22 1 
ATOM   3343 N  N    . ILE   A 1 213 ? -37.607 -0.740  -18.286 1.00 18.25  ? 210 ILE   A N    1 
ATOM   3344 C  CA   . ILE   A 1 213 ? -38.205 -0.916  -19.602 1.00 17.89  ? 210 ILE   A CA   1 
ATOM   3345 C  C    . ILE   A 1 213 ? -39.716 -0.941  -19.390 1.00 19.98  ? 210 ILE   A C    1 
ATOM   3346 O  O    . ILE   A 1 213 ? -40.186 -1.641  -18.492 1.00 21.97  ? 210 ILE   A O    1 
ATOM   3347 C  CB   . ILE   A 1 213 ? -37.765 -2.207  -20.293 1.00 21.62  ? 210 ILE   A CB   1 
ATOM   3348 C  CG1  . ILE   A 1 213 ? -36.239 -2.279  -20.474 1.00 18.72  ? 210 ILE   A CG1  1 
ATOM   3349 C  CG2  . ILE   A 1 213 ? -38.469 -2.354  -21.629 1.00 21.72  ? 210 ILE   A CG2  1 
ATOM   3350 C  CD1  . ILE   A 1 213 ? -35.663 -1.217  -21.317 1.00 19.66  ? 210 ILE   A CD1  1 
ATOM   3351 H  H    . ILE   A 1 213 ? -37.860 -1.351  -17.737 1.00 21.94  ? 210 ILE   A H    1 
ATOM   3352 H  HA   . ILE   A 1 213 ? -37.944 -0.176  -20.172 1.00 21.51  ? 210 ILE   A HA   1 
ATOM   3353 H  HB   . ILE   A 1 213 ? -38.019 -2.944  -19.715 1.00 25.98  ? 210 ILE   A HB   1 
ATOM   3354 H  HG12 . ILE   A 1 213 ? -35.823 -2.216  -19.600 1.00 22.50  ? 210 ILE   A HG12 1 
ATOM   3355 H  HG13 . ILE   A 1 213 ? -36.018 -3.130  -20.885 1.00 22.50  ? 210 ILE   A HG13 1 
ATOM   3356 H  HG21 . ILE   A 1 213 ? -38.055 -3.076  -22.127 1.00 26.11  ? 210 ILE   A HG21 1 
ATOM   3357 H  HG22 . ILE   A 1 213 ? -39.406 -2.554  -21.472 1.00 26.11  ? 210 ILE   A HG22 1 
ATOM   3358 H  HG23 . ILE   A 1 213 ? -38.387 -1.523  -22.122 1.00 26.11  ? 210 ILE   A HG23 1 
ATOM   3359 H  HD11 . ILE   A 1 213 ? -34.715 -1.385  -21.433 1.00 23.63  ? 210 ILE   A HD11 1 
ATOM   3360 H  HD12 . ILE   A 1 213 ? -36.107 -1.222  -22.179 1.00 23.63  ? 210 ILE   A HD12 1 
ATOM   3361 H  HD13 . ILE   A 1 213 ? -35.796 -0.361  -20.882 1.00 23.63  ? 210 ILE   A HD13 1 
ATOM   3362 N  N    . THR   A 1 214 ? -40.454 -0.152  -20.174 1.00 20.55  ? 211 THR   A N    1 
ATOM   3363 C  CA   . THR   A 1 214 ? -41.913 -0.080  -20.121 1.00 19.85  ? 211 THR   A CA   1 
ATOM   3364 C  C    . THR   A 1 214 ? -42.481 -0.584  -21.442 1.00 21.22  ? 211 THR   A C    1 
ATOM   3365 O  O    . THR   A 1 214 ? -41.778 -0.629  -22.446 1.00 22.38  ? 211 THR   A O    1 
ATOM   3366 C  CB   . THR   A 1 214 ? -42.416 1.345   -19.883 1.00 27.86  ? 211 THR   A CB   1 
ATOM   3367 O  OG1  . THR   A 1 214 ? -42.146 2.132   -21.049 1.00 29.78  ? 211 THR   A OG1  1 
ATOM   3368 C  CG2  . THR   A 1 214 ? -41.745 1.985   -18.682 1.00 29.68  ? 211 THR   A CG2  1 
ATOM   3369 H  H    . THR   A 1 214 ? -40.117 0.372   -20.768 1.00 24.71  ? 211 THR   A H    1 
ATOM   3370 H  HA   . THR   A 1 214 ? -42.227 -0.635  -19.391 1.00 23.86  ? 211 THR   A HA   1 
ATOM   3371 H  HB   . THR   A 1 214 ? -43.369 1.320   -19.703 1.00 33.47  ? 211 THR   A HB   1 
ATOM   3372 H  HG1  . THR   A 1 214 ? -42.503 2.889   -20.973 1.00 35.78  ? 211 THR   A HG1  1 
ATOM   3373 H  HG21 . THR   A 1 214 ? -42.160 2.840   -18.487 1.00 35.65  ? 211 THR   A HG21 1 
ATOM   3374 H  HG22 . THR   A 1 214 ? -41.833 1.409   -17.907 1.00 35.65  ? 211 THR   A HG22 1 
ATOM   3375 H  HG23 . THR   A 1 214 ? -40.803 2.126   -18.864 1.00 35.65  ? 211 THR   A HG23 1 
ATOM   3376 N  N    . LEU   A 1 215 ? -43.767 -0.960  -21.431 1.00 21.92  ? 212 LEU   A N    1 
ATOM   3377 C  CA   . LEU   A 1 215 ? -44.440 -1.326  -22.676 1.00 22.34  ? 212 LEU   A CA   1 
ATOM   3378 C  C    . LEU   A 1 215 ? -44.373 -0.194  -23.700 1.00 27.76  ? 212 LEU   A C    1 
ATOM   3379 O  O    . LEU   A 1 215 ? -44.218 -0.440  -24.909 1.00 26.68  ? 212 LEU   A O    1 
ATOM   3380 C  CB   . LEU   A 1 215 ? -45.895 -1.686  -22.370 1.00 29.85  ? 212 LEU   A CB   1 
ATOM   3381 C  CG   . LEU   A 1 215 ? -46.081 -2.984  -21.573 1.00 29.78  ? 212 LEU   A CG   1 
ATOM   3382 C  CD1  . LEU   A 1 215 ? -47.548 -3.144  -21.186 1.00 30.72  ? 212 LEU   A CD1  1 
ATOM   3383 C  CD2  . LEU   A 1 215 ? -45.564 -4.166  -22.341 1.00 28.65  ? 212 LEU   A CD2  1 
ATOM   3384 H  H    . LEU   A 1 215 ? -44.260 -1.010  -20.728 1.00 26.34  ? 212 LEU   A H    1 
ATOM   3385 H  HA   . LEU   A 1 215 ? -44.001 -2.099  -23.063 1.00 26.85  ? 212 LEU   A HA   1 
ATOM   3386 H  HB2  . LEU   A 1 215 ? -46.288 -0.966  -21.853 1.00 35.86  ? 212 LEU   A HB2  1 
ATOM   3387 H  HB3  . LEU   A 1 215 ? -46.369 -1.788  -23.210 1.00 35.86  ? 212 LEU   A HB3  1 
ATOM   3388 H  HG   . LEU   A 1 215 ? -45.563 -2.945  -20.754 1.00 35.78  ? 212 LEU   A HG   1 
ATOM   3389 H  HD11 . LEU   A 1 215 ? -47.650 -3.954  -20.661 1.00 36.91  ? 212 LEU   A HD11 1 
ATOM   3390 H  HD12 . LEU   A 1 215 ? -47.823 -2.375  -20.664 1.00 36.91  ? 212 LEU   A HD12 1 
ATOM   3391 H  HD13 . LEU   A 1 215 ? -48.083 -3.205  -21.993 1.00 36.91  ? 212 LEU   A HD13 1 
ATOM   3392 H  HD21 . LEU   A 1 215 ? -45.770 -4.976  -21.850 1.00 34.42  ? 212 LEU   A HD21 1 
ATOM   3393 H  HD22 . LEU   A 1 215 ? -45.991 -4.188  -23.212 1.00 34.42  ? 212 LEU   A HD22 1 
ATOM   3394 H  HD23 . LEU   A 1 215 ? -44.604 -4.078  -22.446 1.00 34.42  ? 212 LEU   A HD23 1 
ATOM   3395 N  N    . ASP   A 1 216 ? -44.441 1.037   -23.236 1.00 25.25  ? 213 ASP   A N    1 
ATOM   3396 C  CA   . ASP   A 1 216 ? -44.412 2.186   -24.129 1.00 32.08  ? 213 ASP   A CA   1 
ATOM   3397 C  C    . ASP   A 1 216 ? -43.078 2.288   -24.860 1.00 26.39  ? 213 ASP   A C    1 
ATOM   3398 O  O    . ASP   A 1 216 ? -43.037 2.777   -25.995 1.00 35.29  ? 213 ASP   A O    1 
ATOM   3399 C  CB   . ASP   A 1 216 ? -44.685 3.452   -23.320 1.00 33.67  ? 213 ASP   A CB   1 
ATOM   3400 C  CG   . ASP   A 1 216 ? -46.155 3.760   -23.195 1.00 45.75  ? 213 ASP   A CG   1 
ATOM   3401 O  OD1  . ASP   A 1 216 ? -46.500 4.808   -22.591 1.00 49.66  ? 213 ASP   A OD1  1 
ATOM   3402 O  OD2  . ASP   A 1 216 ? -46.980 2.985   -23.710 1.00 50.34  ? 213 ASP   A OD2  1 
ATOM   3403 H  H    . ASP   A 1 216 ? -44.504 1.241   -22.404 1.00 30.34  ? 213 ASP   A H    1 
ATOM   3404 H  HA   . ASP   A 1 216 ? -45.106 2.097   -24.800 1.00 38.54  ? 213 ASP   A HA   1 
ATOM   3405 H  HB2  . ASP   A 1 216 ? -44.326 3.340   -22.427 1.00 40.45  ? 213 ASP   A HB2  1 
ATOM   3406 H  HB3  . ASP   A 1 216 ? -44.258 4.204   -23.758 1.00 40.45  ? 213 ASP   A HB3  1 
ATOM   3407 N  N    . ASP   A 1 217 ? -41.983 1.807   -24.261 1.00 26.14  ? 214 ASP   A N    1 
ATOM   3408 C  CA   . ASP   A 1 217 ? -40.713 1.783   -24.984 1.00 27.69  ? 214 ASP   A CA   1 
ATOM   3409 C  C    . ASP   A 1 217 ? -40.791 0.900   -26.230 1.00 30.01  ? 214 ASP   A C    1 
ATOM   3410 O  O    . ASP   A 1 217 ? -40.165 1.205   -27.247 1.00 37.78  ? 214 ASP   A O    1 
ATOM   3411 C  CB   . ASP   A 1 217 ? -39.574 1.302   -24.075 1.00 31.07  ? 214 ASP   A CB   1 
ATOM   3412 C  CG   . ASP   A 1 217 ? -39.280 2.261   -22.914 1.00 33.47  ? 214 ASP   A CG   1 
ATOM   3413 O  OD1  . ASP   A 1 217 ? -39.299 3.496   -23.107 1.00 34.06  ? 214 ASP   A OD1  1 
ATOM   3414 O  OD2  . ASP   A 1 217 ? -39.020 1.780   -21.783 1.00 29.12  ? 214 ASP   A OD2  1 
ATOM   3415 H  H    . ASP   A 1 217 ? -41.951 1.498   -23.459 1.00 31.41  ? 214 ASP   A H    1 
ATOM   3416 H  HA   . ASP   A 1 217 ? -40.515 2.692   -25.260 1.00 33.27  ? 214 ASP   A HA   1 
ATOM   3417 H  HB2  . ASP   A 1 217 ? -39.816 0.442   -23.697 1.00 37.32  ? 214 ASP   A HB2  1 
ATOM   3418 H  HB3  . ASP   A 1 217 ? -38.765 1.217   -24.603 1.00 37.32  ? 214 ASP   A HB3  1 
ATOM   3419 N  N    . PHE   A 1 218 ? -41.503 -0.231  -26.151 1.00 25.47  ? 215 PHE   A N    1 
ATOM   3420 C  CA   . PHE   A 1 218 ? -41.639 -1.128  -27.302 1.00 23.44  ? 215 PHE   A CA   1 
ATOM   3421 C  C    . PHE   A 1 218 ? -42.495 -0.481  -28.377 1.00 29.42  ? 215 PHE   A C    1 
ATOM   3422 O  O    . PHE   A 1 218 ? -42.207 -0.601  -29.576 1.00 25.47  ? 215 PHE   A O    1 
ATOM   3423 C  CB   . PHE   A 1 218 ? -42.275 -2.477  -26.915 1.00 23.72  ? 215 PHE   A CB   1 
ATOM   3424 C  CG   . PHE   A 1 218 ? -41.468 -3.284  -25.958 1.00 24.29  ? 215 PHE   A CG   1 
ATOM   3425 C  CD1  . PHE   A 1 218 ? -40.348 -3.933  -26.389 1.00 34.49  ? 215 PHE   A CD1  1 
ATOM   3426 C  CD2  . PHE   A 1 218 ? -41.888 -3.445  -24.669 1.00 29.79  ? 215 PHE   A CD2  1 
ATOM   3427 C  CE1  . PHE   A 1 218 ? -39.601 -4.672  -25.511 1.00 35.99  ? 215 PHE   A CE1  1 
ATOM   3428 C  CE2  . PHE   A 1 218 ? -41.141 -4.181  -23.780 1.00 30.31  ? 215 PHE   A CE2  1 
ATOM   3429 C  CZ   . PHE   A 1 218 ? -40.002 -4.781  -24.206 1.00 24.92  ? 215 PHE   A CZ   1 
ATOM   3430 H  H    . PHE   A 1 218 ? -41.916 -0.501  -25.446 1.00 30.61  ? 215 PHE   A H    1 
ATOM   3431 H  HA   . PHE   A 1 218 ? -40.746 -1.308  -27.635 1.00 28.17  ? 215 PHE   A HA   1 
ATOM   3432 H  HB2  . PHE   A 1 218 ? -43.136 -2.307  -26.502 1.00 28.51  ? 215 PHE   A HB2  1 
ATOM   3433 H  HB3  . PHE   A 1 218 ? -42.392 -3.007  -27.720 1.00 28.51  ? 215 PHE   A HB3  1 
ATOM   3434 H  HD1  . PHE   A 1 218 ? -40.091 -3.873  -27.280 1.00 41.43  ? 215 PHE   A HD1  1 
ATOM   3435 H  HD2  . PHE   A 1 218 ? -42.685 -3.055  -24.390 1.00 35.79  ? 215 PHE   A HD2  1 
ATOM   3436 H  HE1  . PHE   A 1 218 ? -38.825 -5.096  -25.799 1.00 43.22  ? 215 PHE   A HE1  1 
ATOM   3437 H  HE2  . PHE   A 1 218 ? -41.414 -4.267  -22.895 1.00 36.41  ? 215 PHE   A HE2  1 
ATOM   3438 H  HZ   . PHE   A 1 218 ? -39.489 -5.273  -23.607 1.00 29.94  ? 215 PHE   A HZ   1 
ATOM   3439 N  N    . THR   A 1 219 ? -43.562 0.210   -27.970 1.00 26.47  ? 216 THR   A N    1 
ATOM   3440 C  CA   . THR   A 1 219 ? -44.494 0.740   -28.955 1.00 27.05  ? 216 THR   A CA   1 
ATOM   3441 C  C    . THR   A 1 219 ? -43.872 1.850   -29.791 1.00 29.66  ? 216 THR   A C    1 
ATOM   3442 O  O    . THR   A 1 219 ? -44.182 1.954   -30.985 1.00 29.09  ? 216 THR   A O    1 
ATOM   3443 C  CB   . THR   A 1 219 ? -45.764 1.212   -28.244 1.00 29.46  ? 216 THR   A CB   1 
ATOM   3444 O  OG1  . THR   A 1 219 ? -46.384 0.061   -27.645 1.00 37.18  ? 216 THR   A OG1  1 
ATOM   3445 C  CG2  . THR   A 1 219 ? -46.740 1.861   -29.211 1.00 34.79  ? 216 THR   A CG2  1 
ATOM   3446 H  H    . THR   A 1 219 ? -43.762 0.378   -27.151 1.00 31.80  ? 216 THR   A H    1 
ATOM   3447 H  HA   . THR   A 1 219 ? -44.745 0.037   -29.575 1.00 32.50  ? 216 THR   A HA   1 
ATOM   3448 H  HB   . THR   A 1 219 ? -45.541 1.878   -27.576 1.00 35.39  ? 216 THR   A HB   1 
ATOM   3449 H  HG1  . THR   A 1 219 ? -47.087 0.288   -27.246 1.00 44.66  ? 216 THR   A HG1  1 
ATOM   3450 H  HG21 . THR   A 1 219 ? -47.542 2.134   -28.739 1.00 41.78  ? 216 THR   A HG21 1 
ATOM   3451 H  HG22 . THR   A 1 219 ? -46.334 2.641   -29.620 1.00 41.78  ? 216 THR   A HG22 1 
ATOM   3452 H  HG23 . THR   A 1 219 ? -46.984 1.232   -29.908 1.00 41.78  ? 216 THR   A HG23 1 
ATOM   3453 N  N    . LYS   A 1 220 ? -42.963 2.635   -29.211 1.00 28.94  ? 217 LYS   A N    1 
ATOM   3454 C  CA   . LYS   A 1 220 ? -42.370 3.750   -29.939 1.00 31.07  ? 217 LYS   A CA   1 
ATOM   3455 C  C    . LYS   A 1 220 ? -41.613 3.283   -31.174 1.00 27.84  ? 217 LYS   A C    1 
ATOM   3456 O  O    . LYS   A 1 220 ? -41.550 4.016   -32.170 1.00 35.90  ? 217 LYS   A O    1 
ATOM   3457 C  CB   . LYS   A 1 220 ? -41.413 4.531   -29.032 1.00 37.44  ? 217 LYS   A CB   1 
ATOM   3458 C  CG   . LYS   A 1 220 ? -41.198 5.973   -29.458 1.00 48.75  ? 217 LYS   A CG   1 
ATOM   3459 C  CD   . LYS   A 1 220 ? -40.345 6.768   -28.462 1.00 57.84  ? 217 LYS   A CD   1 
ATOM   3460 C  CE   . LYS   A 1 220 ? -39.802 8.058   -29.099 1.00 70.26  ? 217 LYS   A CE   1 
ATOM   3461 N  NZ   . LYS   A 1 220 ? -40.191 9.300   -28.353 1.00 60.38  ? 217 LYS   A NZ   1 
ATOM   3462 H  H    . LYS   A 1 220 ? -42.677 2.543   -28.405 1.00 34.77  ? 217 LYS   A H    1 
ATOM   3463 H  HA   . LYS   A 1 220 ? -43.087 4.340   -30.217 1.00 37.32  ? 217 LYS   A HA   1 
ATOM   3464 H  HB2  . LYS   A 1 220 ? -41.776 4.540   -28.132 1.00 44.97  ? 217 LYS   A HB2  1 
ATOM   3465 H  HB3  . LYS   A 1 220 ? -40.550 4.090   -29.037 1.00 44.97  ? 217 LYS   A HB3  1 
ATOM   3466 H  HG2  . LYS   A 1 220 ? -40.745 5.985   -30.315 1.00 58.54  ? 217 LYS   A HG2  1 
ATOM   3467 H  HG3  . LYS   A 1 220 ? -42.060 6.413   -29.531 1.00 58.54  ? 217 LYS   A HG3  1 
ATOM   3468 H  HD2  . LYS   A 1 220 ? -40.887 7.011   -27.695 1.00 69.45  ? 217 LYS   A HD2  1 
ATOM   3469 H  HD3  . LYS   A 1 220 ? -39.592 6.227   -28.178 1.00 69.45  ? 217 LYS   A HD3  1 
ATOM   3470 H  HE2  . LYS   A 1 220 ? -38.833 8.014   -29.119 1.00 84.35  ? 217 LYS   A HE2  1 
ATOM   3471 H  HE3  . LYS   A 1 220 ? -40.150 8.133   -30.001 1.00 84.35  ? 217 LYS   A HE3  1 
ATOM   3472 H  HZ1  . LYS   A 1 220 ? -39.857 10.017  -28.761 1.00 72.49  ? 217 LYS   A HZ1  1 
ATOM   3473 H  HZ2  . LYS   A 1 220 ? -41.077 9.371   -28.322 1.00 72.49  ? 217 LYS   A HZ2  1 
ATOM   3474 H  HZ3  . LYS   A 1 220 ? -39.874 9.267   -27.522 1.00 72.49  ? 217 LYS   A HZ3  1 
ATOM   3475 N  N    . TYR   A 1 221 ? -40.977 2.119   -31.095 1.00 27.38  ? 218 TYR   A N    1 
ATOM   3476 C  CA   . TYR   A 1 221 ? -40.131 1.599   -32.168 1.00 29.92  ? 218 TYR   A CA   1 
ATOM   3477 C  C    . TYR   A 1 221 ? -40.600 0.233   -32.624 1.00 24.33  ? 218 TYR   A C    1 
ATOM   3478 O  O    . TYR   A 1 221 ? -39.800 -0.613  -33.013 1.00 24.98  ? 218 TYR   A O    1 
ATOM   3479 C  CB   . TYR   A 1 221 ? -38.670 1.520   -31.720 1.00 32.04  ? 218 TYR   A CB   1 
ATOM   3480 C  CG   . TYR   A 1 221 ? -38.174 2.824   -31.166 1.00 30.24  ? 218 TYR   A CG   1 
ATOM   3481 C  CD1  . TYR   A 1 221 ? -37.866 3.884   -31.994 1.00 34.96  ? 218 TYR   A CD1  1 
ATOM   3482 C  CD2  . TYR   A 1 221 ? -37.984 2.967   -29.798 1.00 32.95  ? 218 TYR   A CD2  1 
ATOM   3483 C  CE1  . TYR   A 1 221 ? -37.400 5.088   -31.473 1.00 45.06  ? 218 TYR   A CE1  1 
ATOM   3484 C  CE2  . TYR   A 1 221 ? -37.514 4.158   -29.264 1.00 37.75  ? 218 TYR   A CE2  1 
ATOM   3485 C  CZ   . TYR   A 1 221 ? -37.216 5.203   -30.100 1.00 37.83  ? 218 TYR   A CZ   1 
ATOM   3486 O  OH   . TYR   A 1 221 ? -36.756 6.376   -29.546 1.00 46.24  ? 218 TYR   A OH   1 
ATOM   3487 H  H    . TYR   A 1 221 ? -41.020 1.598   -30.412 1.00 32.90  ? 218 TYR   A H    1 
ATOM   3488 H  HA   . TYR   A 1 221 ? -40.188 2.210   -32.920 1.00 35.94  ? 218 TYR   A HA   1 
ATOM   3489 H  HB2  . TYR   A 1 221 ? -38.586 0.846   -31.028 1.00 38.49  ? 218 TYR   A HB2  1 
ATOM   3490 H  HB3  . TYR   A 1 221 ? -38.117 1.285   -32.481 1.00 38.49  ? 218 TYR   A HB3  1 
ATOM   3491 H  HD1  . TYR   A 1 221 ? -37.971 3.793   -32.914 1.00 41.99  ? 218 TYR   A HD1  1 
ATOM   3492 H  HD2  . TYR   A 1 221 ? -38.175 2.254   -29.232 1.00 39.59  ? 218 TYR   A HD2  1 
ATOM   3493 H  HE1  . TYR   A 1 221 ? -37.214 5.805   -32.035 1.00 54.11  ? 218 TYR   A HE1  1 
ATOM   3494 H  HE2  . TYR   A 1 221 ? -37.402 4.247   -28.345 1.00 45.34  ? 218 TYR   A HE2  1 
ATOM   3495 H  HH   . TYR   A 1 221 ? -36.545 6.917   -30.152 1.00 55.53  ? 218 TYR   A HH   1 
ATOM   3496 N  N    . SER   A 1 222 ? -41.915 0.011   -32.603 1.00 27.86  ? 219 SER   A N    1 
ATOM   3497 C  CA   . SER   A 1 222 ? -42.404 -1.349  -32.789 1.00 23.38  ? 219 SER   A CA   1 
ATOM   3498 C  C    . SER   A 1 222 ? -42.051 -1.912  -34.162 1.00 21.23  ? 219 SER   A C    1 
ATOM   3499 O  O    . SER   A 1 222 ? -41.818 -3.134  -34.267 1.00 26.89  ? 219 SER   A O    1 
ATOM   3500 C  CB   . SER   A 1 222 ? -43.915 -1.393  -32.559 1.00 29.45  ? 219 SER   A CB   1 
ATOM   3501 O  OG   . SER   A 1 222 ? -44.570 -0.629  -33.553 1.00 30.83  ? 219 SER   A OG   1 
ATOM   3502 H  H    . SER   A 1 222 ? -42.521 0.610   -32.488 1.00 33.48  ? 219 SER   A H    1 
ATOM   3503 H  HA   . SER   A 1 222 ? -41.980 -1.920  -32.130 1.00 28.10  ? 219 SER   A HA   1 
ATOM   3504 H  HB2  . SER   A 1 222 ? -44.220 -2.313  -32.610 1.00 35.38  ? 219 SER   A HB2  1 
ATOM   3505 H  HB3  . SER   A 1 222 ? -44.118 -1.024  -31.686 1.00 35.38  ? 219 SER   A HB3  1 
ATOM   3506 H  HG   . SER   A 1 222 ? -45.402 -0.690  -33.460 1.00 37.03  ? 219 SER   A HG   1 
ATOM   3507 N  N    . ASP   A 1 223 ? -41.939 -1.053  -35.181 1.00 23.12  ? 220 ASP   A N    1 
ATOM   3508 C  CA   . ASP   A 1 223 ? -41.584 -1.499  -36.518 1.00 23.65  ? 220 ASP   A CA   1 
ATOM   3509 C  C    . ASP   A 1 223 ? -40.205 -2.148  -36.574 1.00 27.24  ? 220 ASP   A C    1 
ATOM   3510 O  O    . ASP   A 1 223 ? -39.903 -2.857  -37.543 1.00 26.98  ? 220 ASP   A O    1 
ATOM   3511 C  CB   . ASP   A 1 223 ? -41.619 -0.306  -37.489 1.00 31.21  ? 220 ASP   A CB   1 
ATOM   3512 C  CG   . ASP   A 1 223 ? -40.723 0.843   -37.026 1.00 47.85  ? 220 ASP   A CG   1 
ATOM   3513 O  OD1  . ASP   A 1 223 ? -41.059 1.520   -36.015 1.00 47.70  ? 220 ASP   A OD1  1 
ATOM   3514 O  OD2  . ASP   A 1 223 ? -39.666 1.052   -37.664 1.00 52.52  ? 220 ASP   A OD2  1 
ATOM   3515 H  H    . ASP   A 1 223 ? -42.066 -0.205  -35.118 1.00 27.78  ? 220 ASP   A H    1 
ATOM   3516 H  HA   . ASP   A 1 223 ? -42.236 -2.158  -36.803 1.00 28.42  ? 220 ASP   A HA   1 
ATOM   3517 H  HB2  . ASP   A 1 223 ? -41.310 -0.596  -38.362 1.00 37.49  ? 220 ASP   A HB2  1 
ATOM   3518 H  HB3  . ASP   A 1 223 ? -42.528 0.027   -37.552 1.00 37.49  ? 220 ASP   A HB3  1 
ATOM   3519 N  N    . LYS   A 1 224 ? -39.359 -1.908  -35.581 1.00 20.61  ? 221 LYS   A N    1 
ATOM   3520 C  CA   . LYS   A 1 224 ? -38.005 -2.430  -35.621 1.00 20.22  ? 221 LYS   A CA   1 
ATOM   3521 C  C    . LYS   A 1 224 ? -37.869 -3.807  -34.974 1.00 19.18  ? 221 LYS   A C    1 
ATOM   3522 O  O    . LYS   A 1 224 ? -36.816 -4.454  -35.114 1.00 19.80  ? 221 LYS   A O    1 
ATOM   3523 C  CB   . LYS   A 1 224 ? -37.051 -1.487  -34.856 1.00 20.64  ? 221 LYS   A CB   1 
ATOM   3524 C  CG   . LYS   A 1 224 ? -36.765 -0.150  -35.538 1.00 23.25  ? 221 LYS   A CG   1 
ATOM   3525 C  CD   . LYS   A 1 224 ? -35.908 0.728   -34.572 1.00 24.29  ? 221 LYS   A CD   1 
ATOM   3526 C  CE   . LYS   A 1 224 ? -35.457 2.106   -35.113 1.00 33.15  ? 221 LYS   A CE   1 
ATOM   3527 N  NZ   . LYS   A 1 224 ? -35.461 2.217   -36.554 1.00 37.95  ? 221 LYS   A NZ   1 
ATOM   3528 H  H    . LYS   A 1 224 ? -39.546 -1.449  -34.878 1.00 24.77  ? 221 LYS   A H    1 
ATOM   3529 H  HA   . LYS   A 1 224 ? -37.741 -2.485  -36.552 1.00 24.30  ? 221 LYS   A HA   1 
ATOM   3530 H  HB2  . LYS   A 1 224 ? -37.444 -1.291  -33.991 1.00 24.81  ? 221 LYS   A HB2  1 
ATOM   3531 H  HB3  . LYS   A 1 224 ? -36.202 -1.940  -34.739 1.00 24.81  ? 221 LYS   A HB3  1 
ATOM   3532 H  HG2  . LYS   A 1 224 ? -36.268 -0.295  -36.359 1.00 27.94  ? 221 LYS   A HG2  1 
ATOM   3533 H  HG3  . LYS   A 1 224 ? -37.596 0.310   -35.731 1.00 27.94  ? 221 LYS   A HG3  1 
ATOM   3534 H  HD2  . LYS   A 1 224 ? -36.430 0.894   -33.772 1.00 29.19  ? 221 LYS   A HD2  1 
ATOM   3535 H  HD3  . LYS   A 1 224 ? -35.104 0.234   -34.347 1.00 29.19  ? 221 LYS   A HD3  1 
ATOM   3536 H  HE2  . LYS   A 1 224 ? -36.056 2.786   -34.766 1.00 39.82  ? 221 LYS   A HE2  1 
ATOM   3537 H  HE3  . LYS   A 1 224 ? -34.551 2.276   -34.810 1.00 39.82  ? 221 LYS   A HE3  1 
ATOM   3538 H  HZ1  . LYS   A 1 224 ? -35.106 2.995   -36.801 1.00 45.59  ? 221 LYS   A HZ1  1 
ATOM   3539 H  HZ2  . LYS   A 1 224 ? -34.984 1.556   -36.912 1.00 45.59  ? 221 LYS   A HZ2  1 
ATOM   3540 H  HZ3  . LYS   A 1 224 ? -36.295 2.170   -36.861 1.00 45.59  ? 221 LYS   A HZ3  1 
ATOM   3541 N  N    . ILE   A 1 225 ? -38.860 -4.262  -34.210 1.00 19.26  ? 222 ILE   A N    1 
ATOM   3542 C  CA   . ILE   A 1 225 ? -38.665 -5.327  -33.236 1.00 17.62  ? 222 ILE   A CA   1 
ATOM   3543 C  C    . ILE   A 1 225 ? -39.266 -6.648  -33.705 1.00 18.25  ? 222 ILE   A C    1 
ATOM   3544 O  O    . ILE   A 1 225 ? -40.415 -6.688  -34.187 1.00 18.93  ? 222 ILE   A O    1 
ATOM   3545 C  CB   . ILE   A 1 225 ? -39.310 -4.932  -31.886 1.00 18.85  ? 222 ILE   A CB   1 
ATOM   3546 C  CG1  . ILE   A 1 225 ? -38.744 -3.616  -31.352 1.00 19.15  ? 222 ILE   A CG1  1 
ATOM   3547 C  CG2  . ILE   A 1 225 ? -39.227 -6.057  -30.889 1.00 17.75  ? 222 ILE   A CG2  1 
ATOM   3548 C  CD1  . ILE   A 1 225 ? -39.518 -3.047  -30.116 1.00 21.37  ? 222 ILE   A CD1  1 
ATOM   3549 H  H    . ILE   A 1 225 ? -39.665 -3.962  -34.240 1.00 23.15  ? 222 ILE   A H    1 
ATOM   3550 H  HA   . ILE   A 1 225 ? -37.709 -5.469  -33.151 1.00 21.19  ? 222 ILE   A HA   1 
ATOM   3551 H  HB   . ILE   A 1 225 ? -40.253 -4.772  -32.046 1.00 22.66  ? 222 ILE   A HB   1 
ATOM   3552 H  HG12 . ILE   A 1 225 ? -37.823 -3.759  -31.083 1.00 23.02  ? 222 ILE   A HG12 1 
ATOM   3553 H  HG13 . ILE   A 1 225 ? -38.783 -2.951  -32.057 1.00 23.02  ? 222 ILE   A HG13 1 
ATOM   3554 H  HG21 . ILE   A 1 225 ? -39.461 -5.719  -30.011 1.00 21.35  ? 222 ILE   A HG21 1 
ATOM   3555 H  HG22 . ILE   A 1 225 ? -39.846 -6.757  -31.150 1.00 21.35  ? 222 ILE   A HG22 1 
ATOM   3556 H  HG23 . ILE   A 1 225 ? -38.321 -6.404  -30.879 1.00 21.35  ? 222 ILE   A HG23 1 
ATOM   3557 H  HD11 . ILE   A 1 225 ? -39.199 -2.150  -29.930 1.00 25.69  ? 222 ILE   A HD11 1 
ATOM   3558 H  HD12 . ILE   A 1 225 ? -40.466 -3.024  -30.320 1.00 25.69  ? 222 ILE   A HD12 1 
ATOM   3559 H  HD13 . ILE   A 1 225 ? -39.357 -3.621  -29.351 1.00 25.69  ? 222 ILE   A HD13 1 
ATOM   3560 N  N    . THR   A 1 226 ? -38.521 -7.731  -33.495 1.00 18.20  ? 223 THR   A N    1 
ATOM   3561 C  CA   . THR   A 1 226 ? -39.019 -9.105  -33.564 1.00 16.58  ? 223 THR   A CA   1 
ATOM   3562 C  C    . THR   A 1 226 ? -38.809 -9.776  -32.211 1.00 16.78  ? 223 THR   A C    1 
ATOM   3563 O  O    . THR   A 1 226 ? -37.721 -9.654  -31.615 1.00 17.29  ? 223 THR   A O    1 
ATOM   3564 C  CB   . THR   A 1 226 ? -38.298 -9.924  -34.645 1.00 18.37  ? 223 THR   A CB   1 
ATOM   3565 O  OG1  . THR   A 1 226 ? -38.450 -9.258  -35.913 1.00 22.60  ? 223 THR   A OG1  1 
ATOM   3566 C  CG2  . THR   A 1 226 ? -38.840 -11.372 -34.723 1.00 20.75  ? 223 THR   A CG2  1 
ATOM   3567 H  H    . THR   A 1 226 ? -37.684 -7.695  -33.301 1.00 21.88  ? 223 THR   A H    1 
ATOM   3568 H  HA   . THR   A 1 226 ? -39.965 -9.082  -33.776 1.00 19.94  ? 223 THR   A HA   1 
ATOM   3569 H  HB   . THR   A 1 226 ? -37.356 -9.995  -34.426 1.00 22.08  ? 223 THR   A HB   1 
ATOM   3570 H  HG1  . THR   A 1 226 ? -37.959 -9.622  -36.490 1.00 27.16  ? 223 THR   A HG1  1 
ATOM   3571 H  HG21 . THR   A 1 226 ? -38.474 -11.822 -35.501 1.00 24.95  ? 223 THR   A HG21 1 
ATOM   3572 H  HG22 . THR   A 1 226 ? -38.587 -11.864 -33.927 1.00 24.95  ? 223 THR   A HG22 1 
ATOM   3573 H  HG23 . THR   A 1 226 ? -39.808 -11.361 -34.792 1.00 24.95  ? 223 THR   A HG23 1 
ATOM   3574 N  N    . LEU   A 1 227 ? -39.844 -10.452 -31.708 1.00 15.89  ? 224 LEU   A N    1 
ATOM   3575 C  CA   . LEU   A 1 227 ? -39.753 -11.283 -30.516 1.00 16.99  ? 224 LEU   A CA   1 
ATOM   3576 C  C    . LEU   A 1 227 ? -39.511 -12.710 -30.991 1.00 17.13  ? 224 LEU   A C    1 
ATOM   3577 O  O    . LEU   A 1 227 ? -40.206 -13.179 -31.908 1.00 19.87  ? 224 LEU   A O    1 
ATOM   3578 C  CB   . LEU   A 1 227 ? -41.030 -11.170 -29.678 1.00 19.03  ? 224 LEU   A CB   1 
ATOM   3579 C  CG   . LEU   A 1 227 ? -41.532 -9.770  -29.316 1.00 17.65  ? 224 LEU   A CG   1 
ATOM   3580 C  CD1  . LEU   A 1 227 ? -42.890 -9.854  -28.677 1.00 20.08  ? 224 LEU   A CD1  1 
ATOM   3581 C  CD2  . LEU   A 1 227 ? -40.510 -9.078  -28.453 1.00 19.31  ? 224 LEU   A CD2  1 
ATOM   3582 H  H    . LEU   A 1 227 ? -40.631 -10.443 -32.054 1.00 19.11  ? 224 LEU   A H    1 
ATOM   3583 H  HA   . LEU   A 1 227 ? -39.022 -11.011 -29.939 1.00 20.43  ? 224 LEU   A HA   1 
ATOM   3584 H  HB2  . LEU   A 1 227 ? -41.744 -11.603 -30.170 1.00 22.87  ? 224 LEU   A HB2  1 
ATOM   3585 H  HB3  . LEU   A 1 227 ? -40.874 -11.634 -28.841 1.00 22.87  ? 224 LEU   A HB3  1 
ATOM   3586 H  HG   . LEU   A 1 227 ? -41.644 -9.226  -30.111 1.00 21.22  ? 224 LEU   A HG   1 
ATOM   3587 H  HD11 . LEU   A 1 227 ? -43.216 -8.956  -28.508 1.00 24.14  ? 224 LEU   A HD11 1 
ATOM   3588 H  HD12 . LEU   A 1 227 ? -43.494 -10.317 -29.279 1.00 24.14  ? 224 LEU   A HD12 1 
ATOM   3589 H  HD13 . LEU   A 1 227 ? -42.817 -10.342 -27.842 1.00 24.14  ? 224 LEU   A HD13 1 
ATOM   3590 H  HD21 . LEU   A 1 227 ? -40.824 -8.184  -28.247 1.00 23.21  ? 224 LEU   A HD21 1 
ATOM   3591 H  HD22 . LEU   A 1 227 ? -40.394 -9.584  -27.634 1.00 23.21  ? 224 LEU   A HD22 1 
ATOM   3592 H  HD23 . LEU   A 1 227 ? -39.670 -9.031  -28.935 1.00 23.21  ? 224 LEU   A HD23 1 
ATOM   3593 N  N    . LEU   A 1 228 ? -38.533 -13.393 -30.389 1.00 16.31  ? 225 LEU   A N    1 
ATOM   3594 C  CA   . LEU   A 1 228 ? -38.188 -14.762 -30.765 1.00 17.27  ? 225 LEU   A CA   1 
ATOM   3595 C  C    . LEU   A 1 228 ? -38.443 -15.727 -29.613 1.00 18.98  ? 225 LEU   A C    1 
ATOM   3596 O  O    . LEU   A 1 228 ? -37.959 -15.522 -28.483 1.00 18.61  ? 225 LEU   A O    1 
ATOM   3597 C  CB   . LEU   A 1 228 ? -36.718 -14.860 -31.195 1.00 16.85  ? 225 LEU   A CB   1 
ATOM   3598 C  CG   . LEU   A 1 228 ? -36.315 -14.141 -32.490 1.00 16.52  ? 225 LEU   A CG   1 
ATOM   3599 C  CD1  . LEU   A 1 228 ? -34.799 -14.130 -32.667 1.00 18.32  ? 225 LEU   A CD1  1 
ATOM   3600 C  CD2  . LEU   A 1 228 ? -37.048 -14.768 -33.692 1.00 20.43  ? 225 LEU   A CD2  1 
ATOM   3601 H  H    . LEU   A 1 228 ? -38.050 -13.077 -29.751 1.00 19.61  ? 225 LEU   A H    1 
ATOM   3602 H  HA   . LEU   A 1 228 ? -38.761 -15.026 -31.503 1.00 20.77  ? 225 LEU   A HA   1 
ATOM   3603 H  HB2  . LEU   A 1 228 ? -36.175 -14.485 -30.484 1.00 20.26  ? 225 LEU   A HB2  1 
ATOM   3604 H  HB3  . LEU   A 1 228 ? -36.505 -15.799 -31.315 1.00 20.26  ? 225 LEU   A HB3  1 
ATOM   3605 H  HG   . LEU   A 1 228 ? -36.584 -13.211 -32.444 1.00 19.86  ? 225 LEU   A HG   1 
ATOM   3606 H  HD11 . LEU   A 1 228 ? -34.571 -13.550 -33.411 1.00 22.03  ? 225 LEU   A HD11 1 
ATOM   3607 H  HD12 . LEU   A 1 228 ? -34.388 -13.800 -31.852 1.00 22.03  ? 225 LEU   A HD12 1 
ATOM   3608 H  HD13 . LEU   A 1 228 ? -34.495 -15.033 -32.848 1.00 22.03  ? 225 LEU   A HD13 1 
ATOM   3609 H  HD21 . LEU   A 1 228 ? -36.769 -14.316 -34.503 1.00 24.55  ? 225 LEU   A HD21 1 
ATOM   3610 H  HD22 . LEU   A 1 228 ? -36.822 -15.710 -33.743 1.00 24.55  ? 225 LEU   A HD22 1 
ATOM   3611 H  HD23 . LEU   A 1 228 ? -38.005 -14.664 -33.567 1.00 24.55  ? 225 LEU   A HD23 1 
ATOM   3612 N  N    . ASN   A 1 229 ? -39.155 -16.810 -29.925 1.00 18.10  ? 226 ASN   A N    1 
ATOM   3613 C  CA   . ASN   A 1 229 ? -39.447 -17.904 -29.014 1.00 18.26  ? 226 ASN   A CA   1 
ATOM   3614 C  C    . ASN   A 1 229 ? -38.872 -19.182 -29.616 1.00 19.59  ? 226 ASN   A C    1 
ATOM   3615 O  O    . ASN   A 1 229 ? -39.122 -19.485 -30.789 1.00 22.12  ? 226 ASN   A O    1 
ATOM   3616 C  CB   . ASN   A 1 229 ? -40.954 -18.089 -28.787 1.00 19.06  ? 226 ASN   A CB   1 
ATOM   3617 C  CG   . ASN   A 1 229 ? -41.545 -17.174 -27.706 1.00 20.70  ? 226 ASN   A CG   1 
ATOM   3618 O  OD1  . ASN   A 1 229 ? -40.835 -16.494 -26.977 1.00 21.98  ? 226 ASN   A OD1  1 
ATOM   3619 N  ND2  . ASN   A 1 229 ? -42.872 -17.211 -27.590 1.00 23.34  ? 226 ASN   A ND2  1 
ATOM   3620 H  H    . ASN   A 1 229 ? -39.496 -16.937 -30.705 1.00 21.76  ? 226 ASN   A H    1 
ATOM   3621 H  HA   . ASN   A 1 229 ? -39.038 -17.721 -28.154 1.00 21.96  ? 226 ASN   A HA   1 
ATOM   3622 H  HB2  . ASN   A 1 229 ? -41.418 -17.899 -29.617 1.00 22.91  ? 226 ASN   A HB2  1 
ATOM   3623 H  HB3  . ASN   A 1 229 ? -41.117 -19.006 -28.517 1.00 22.91  ? 226 ASN   A HB3  1 
ATOM   3624 H  HD21 . ASN   A 1 229 ? -43.266 -16.721 -27.003 1.00 28.05  ? 226 ASN   A HD21 1 
ATOM   3625 H  HD22 . ASN   A 1 229 ? -43.335 -17.723 -28.103 1.00 28.05  ? 226 ASN   A HD22 1 
ATOM   3626 N  N    . GLY   A 1 230 ? -38.136 -19.950 -28.820 1.00 19.37  ? 227 GLY   A N    1 
ATOM   3627 C  CA   . GLY   A 1 230 ? -37.633 -21.204 -29.309 1.00 18.98  ? 227 GLY   A CA   1 
ATOM   3628 C  C    . GLY   A 1 230 ? -38.731 -22.238 -29.435 1.00 22.71  ? 227 GLY   A C    1 
ATOM   3629 O  O    . GLY   A 1 230 ? -39.682 -22.270 -28.653 1.00 24.50  ? 227 GLY   A O    1 
ATOM   3630 H  H    . GLY   A 1 230 ? -37.923 -19.763 -28.008 1.00 23.28  ? 227 GLY   A H    1 
ATOM   3631 H  HA2  . GLY   A 1 230 ? -37.230 -21.073 -30.182 1.00 22.82  ? 227 GLY   A HA2  1 
ATOM   3632 H  HA3  . GLY   A 1 230 ? -36.959 -21.542 -28.699 1.00 22.82  ? 227 GLY   A HA3  1 
ATOM   3633 N  N    . THR   A 1 231 ? -38.591 -23.122 -30.415 1.00 23.07  ? 228 THR   A N    1 
ATOM   3634 C  CA   . THR   A 1 231 ? -39.554 -24.207 -30.564 1.00 25.60  ? 228 THR   A CA   1 
ATOM   3635 C  C    . THR   A 1 231 ? -39.383 -25.295 -29.508 1.00 24.72  ? 228 THR   A C    1 
ATOM   3636 O  O    . THR   A 1 231 ? -40.322 -26.060 -29.269 1.00 30.16  ? 228 THR   A O    1 
ATOM   3637 C  CB   . THR   A 1 231 ? -39.430 -24.842 -31.948 1.00 30.12  ? 228 THR   A CB   1 
ATOM   3638 O  OG1  . THR   A 1 231 ? -38.108 -25.368 -32.095 1.00 31.32  ? 228 THR   A OG1  1 
ATOM   3639 C  CG2  . THR   A 1 231 ? -39.697 -23.829 -33.022 1.00 27.10  ? 228 THR   A CG2  1 
ATOM   3640 H  H    . THR   A 1 231 ? -37.959 -23.117 -30.998 1.00 27.73  ? 228 THR   A H    1 
ATOM   3641 H  HA   . THR   A 1 231 ? -40.443 -23.829 -30.474 1.00 30.76  ? 228 THR   A HA   1 
ATOM   3642 H  HB   . THR   A 1 231 ? -40.081 -25.554 -32.048 1.00 36.19  ? 228 THR   A HB   1 
ATOM   3643 H  HG1  . THR   A 1 231 ? -38.055 -25.818 -32.803 1.00 37.62  ? 228 THR   A HG1  1 
ATOM   3644 H  HG21 . THR   A 1 231 ? -39.656 -24.251 -33.894 1.00 32.56  ? 228 THR   A HG21 1 
ATOM   3645 H  HG22 . THR   A 1 231 ? -40.578 -23.441 -32.901 1.00 32.56  ? 228 THR   A HG22 1 
ATOM   3646 H  HG23 . THR   A 1 231 ? -39.034 -23.122 -32.983 1.00 32.56  ? 228 THR   A HG23 1 
ATOM   3647 N  N    . ASP   A 1 232 ? -38.223 -25.376 -28.855 1.00 26.67  ? 229 ASP   A N    1 
ATOM   3648 C  CA   . ASP   A 1 232 ? -37.945 -26.448 -27.907 1.00 26.64  ? 229 ASP   A CA   1 
ATOM   3649 C  C    . ASP   A 1 232 ? -37.956 -25.980 -26.460 1.00 28.46  ? 229 ASP   A C    1 
ATOM   3650 O  O    . ASP   A 1 232 ? -37.602 -26.763 -25.563 1.00 36.23  ? 229 ASP   A O    1 
ATOM   3651 C  CB   . ASP   A 1 232 ? -36.588 -27.087 -28.220 1.00 32.77  ? 229 ASP   A CB   1 
ATOM   3652 C  CG   . ASP   A 1 232 ? -36.572 -27.800 -29.564 1.00 43.01  ? 229 ASP   A CG   1 
ATOM   3653 O  OD1  . ASP   A 1 232 ? -37.621 -28.348 -29.997 1.00 45.52  ? 229 ASP   A OD1  1 
ATOM   3654 O  OD2  . ASP   A 1 232 ? -35.507 -27.765 -30.206 1.00 43.96  ? 229 ASP   A OD2  1 
ATOM   3655 H  H    . ASP   A 1 232 ? -37.577 -24.816 -28.947 1.00 32.04  ? 229 ASP   A H    1 
ATOM   3656 H  HA   . ASP   A 1 232 ? -38.637 -27.121 -28.006 1.00 32.01  ? 229 ASP   A HA   1 
ATOM   3657 H  HB2  . ASP   A 1 232 ? -35.909 -26.394 -28.239 1.00 39.37  ? 229 ASP   A HB2  1 
ATOM   3658 H  HB3  . ASP   A 1 232 ? -36.378 -27.738 -27.532 1.00 39.37  ? 229 ASP   A HB3  1 
ATOM   3659 N  N    . SER   A 1 233 ? -38.380 -24.745 -26.205 1.00 25.39  ? 230 SER   A N    1 
ATOM   3660 C  CA   . SER   A 1 233 ? -38.452 -24.180 -24.862 1.00 27.46  ? 230 SER   A CA   1 
ATOM   3661 C  C    . SER   A 1 233 ? -39.867 -23.709 -24.523 1.00 28.60  ? 230 SER   A C    1 
ATOM   3662 O  O    . SER   A 1 233 ? -40.055 -22.816 -23.686 1.00 27.17  ? 230 SER   A O    1 
ATOM   3663 C  CB   . SER   A 1 233 ? -37.444 -23.046 -24.725 1.00 28.15  ? 230 SER   A CB   1 
ATOM   3664 O  OG   . SER   A 1 233 ? -37.345 -22.337 -25.947 1.00 26.79  ? 230 SER   A OG   1 
ATOM   3665 H  H    . SER   A 1 233 ? -38.640 -24.197 -26.814 1.00 30.51  ? 230 SER   A H    1 
ATOM   3666 H  HA   . SER   A 1 233 ? -38.224 -24.866 -24.215 1.00 33.00  ? 230 SER   A HA   1 
ATOM   3667 H  HB2  . SER   A 1 233 ? -37.739 -22.440 -24.027 1.00 33.83  ? 230 SER   A HB2  1 
ATOM   3668 H  HB3  . SER   A 1 233 ? -36.576 -23.415 -24.499 1.00 33.83  ? 230 SER   A HB3  1 
ATOM   3669 H  HG   . SER   A 1 233 ? -36.713 -21.785 -25.909 1.00 32.19  ? 230 SER   A HG   1 
ATOM   3670 N  N    . ARG   A 1 234 ? -40.876 -24.291 -25.161 1.00 29.32  ? 231 ARG   A N    1 
ATOM   3671 C  CA   . ARG   A 1 234 ? -42.245 -23.885 -24.865 1.00 28.48  ? 231 ARG   A CA   1 
ATOM   3672 C  C    . ARG   A 1 234 ? -42.575 -24.147 -23.392 1.00 28.93  ? 231 ARG   A C    1 
ATOM   3673 O  O    . ARG   A 1 234 ? -42.121 -25.123 -22.783 1.00 30.54  ? 231 ARG   A O    1 
ATOM   3674 C  CB   . ARG   A 1 234 ? -43.257 -24.612 -25.761 1.00 35.45  ? 231 ARG   A CB   1 
ATOM   3675 C  CG   . ARG   A 1 234 ? -42.838 -24.738 -27.218 1.00 45.51  ? 231 ARG   A CG   1 
ATOM   3676 C  CD   . ARG   A 1 234 ? -43.058 -23.470 -28.009 1.00 44.12  ? 231 ARG   A CD   1 
ATOM   3677 N  NE   . ARG   A 1 234 ? -44.464 -23.087 -28.091 1.00 68.03  ? 231 ARG   A NE   1 
ATOM   3678 C  CZ   . ARG   A 1 234 ? -44.893 -21.863 -28.376 1.00 65.12  ? 231 ARG   A CZ   1 
ATOM   3679 N  NH1  . ARG   A 1 234 ? -44.045 -20.860 -28.565 1.00 42.61  ? 231 ARG   A NH1  1 
ATOM   3680 N  NH2  . ARG   A 1 234 ? -46.204 -21.640 -28.470 1.00 53.62  ? 231 ARG   A NH2  1 
ATOM   3681 H  H    . ARG   A 1 234 ? -40.798 -24.908 -25.755 1.00 35.23  ? 231 ARG   A H    1 
ATOM   3682 H  HA   . ARG   A 1 234 ? -42.329 -22.935 -25.043 1.00 34.22  ? 231 ARG   A HA   1 
ATOM   3683 H  HB2  . ARG   A 1 234 ? -43.387 -25.509 -25.415 1.00 42.58  ? 231 ARG   A HB2  1 
ATOM   3684 H  HB3  . ARG   A 1 234 ? -44.095 -24.123 -25.738 1.00 42.58  ? 231 ARG   A HB3  1 
ATOM   3685 H  HG2  . ARG   A 1 234 ? -41.894 -24.953 -27.257 1.00 54.65  ? 231 ARG   A HG2  1 
ATOM   3686 H  HG3  . ARG   A 1 234 ? -43.357 -25.443 -27.635 1.00 54.65  ? 231 ARG   A HG3  1 
ATOM   3687 H  HD2  . ARG   A 1 234 ? -42.574 -22.745 -27.584 1.00 52.98  ? 231 ARG   A HD2  1 
ATOM   3688 H  HD3  . ARG   A 1 234 ? -42.730 -23.602 -28.913 1.00 52.98  ? 231 ARG   A HD3  1 
ATOM   3689 H  HE   . ARG   A 1 234 ? -45.055 -23.695 -27.945 1.00 81.68  ? 231 ARG   A HE   1 
ATOM   3690 H  HH11 . ARG   A 1 234 ? -43.198 -20.995 -28.504 1.00 51.18  ? 231 ARG   A HH11 1 
ATOM   3691 H  HH12 . ARG   A 1 234 ? -44.342 -20.074 -28.749 1.00 51.18  ? 231 ARG   A HH12 1 
ATOM   3692 H  HH21 . ARG   A 1 234 ? -46.759 -22.285 -28.346 1.00 64.38  ? 231 ARG   A HH21 1 
ATOM   3693 H  HH22 . ARG   A 1 234 ? -46.494 -20.851 -28.654 1.00 64.38  ? 231 ARG   A HH22 1 
ATOM   3694 N  N    . GLY   A 1 235 ? -43.390 -23.249 -22.823 1.00 28.68  ? 232 GLY   A N    1 
ATOM   3695 C  CA   . GLY   A 1 235 ? -43.794 -23.319 -21.437 1.00 31.08  ? 232 GLY   A CA   1 
ATOM   3696 C  C    . GLY   A 1 235 ? -42.871 -22.615 -20.469 1.00 29.81  ? 232 GLY   A C    1 
ATOM   3697 O  O    . GLY   A 1 235 ? -43.164 -22.560 -19.269 1.00 29.89  ? 232 GLY   A O    1 
ATOM   3698 H  H    . GLY   A 1 235 ? -43.726 -22.576 -23.241 1.00 34.46  ? 232 GLY   A H    1 
ATOM   3699 H  HA2  . GLY   A 1 235 ? -44.674 -22.921 -21.349 1.00 37.34  ? 232 GLY   A HA2  1 
ATOM   3700 H  HA3  . GLY   A 1 235 ? -43.841 -24.251 -21.174 1.00 37.34  ? 232 GLY   A HA3  1 
ATOM   3701 N  N    . SER   A 1 236 ? -41.746 -22.103 -20.930 1.00 28.31  ? 233 SER   A N    1 
ATOM   3702 C  CA   . SER   A 1 236 ? -40.825 -21.453 -20.023 1.00 26.15  ? 233 SER   A CA   1 
ATOM   3703 C  C    . SER   A 1 236 ? -41.219 -19.993 -19.813 1.00 26.44  ? 233 SER   A C    1 
ATOM   3704 O  O    . SER   A 1 236 ? -41.936 -19.378 -20.616 1.00 24.43  ? 233 SER   A O    1 
ATOM   3705 C  CB   . SER   A 1 236 ? -39.396 -21.554 -20.556 1.00 26.43  ? 233 SER   A CB   1 
ATOM   3706 O  OG   . SER   A 1 236 ? -39.265 -20.881 -21.774 1.00 27.94  ? 233 SER   A OG   1 
ATOM   3707 H  H    . SER   A 1 236 ? -41.497 -22.118 -21.753 1.00 34.02  ? 233 SER   A H    1 
ATOM   3708 H  HA   . SER   A 1 236 ? -40.852 -21.893 -19.158 1.00 31.42  ? 233 SER   A HA   1 
ATOM   3709 H  HB2  . SER   A 1 236 ? -38.791 -21.158 -19.910 1.00 31.76  ? 233 SER   A HB2  1 
ATOM   3710 H  HB3  . SER   A 1 236 ? -39.175 -22.490 -20.687 1.00 31.76  ? 233 SER   A HB3  1 
ATOM   3711 H  HG   . SER   A 1 236 ? -39.812 -21.189 -22.333 1.00 33.57  ? 233 SER   A HG   1 
ATOM   3712 N  N    . PHE   A 1 237 ? -40.728 -19.438 -18.703 1.00 24.72  ? 234 PHE   A N    1 
ATOM   3713 C  CA   . PHE   A 1 237 ? -41.070 -18.064 -18.346 1.00 23.93  ? 234 PHE   A CA   1 
ATOM   3714 C  C    . PHE   A 1 237 ? -40.717 -17.041 -19.425 1.00 21.85  ? 234 PHE   A C    1 
ATOM   3715 O  O    . PHE   A 1 237 ? -41.578 -16.194 -19.735 1.00 20.86  ? 234 PHE   A O    1 
ATOM   3716 C  CB   . PHE   A 1 237 ? -40.409 -17.720 -16.997 1.00 24.27  ? 234 PHE   A CB   1 
ATOM   3717 C  CG   . PHE   A 1 237 ? -40.382 -16.262 -16.702 1.00 21.48  ? 234 PHE   A CG   1 
ATOM   3718 C  CD1  . PHE   A 1 237 ? -41.531 -15.634 -16.292 1.00 21.31  ? 234 PHE   A CD1  1 
ATOM   3719 C  CD2  . PHE   A 1 237 ? -39.243 -15.520 -16.871 1.00 21.30  ? 234 PHE   A CD2  1 
ATOM   3720 C  CE1  . PHE   A 1 237 ? -41.537 -14.251 -16.064 1.00 21.49  ? 234 PHE   A CE1  1 
ATOM   3721 C  CE2  . PHE   A 1 237 ? -39.235 -14.131 -16.622 1.00 23.38  ? 234 PHE   A CE2  1 
ATOM   3722 C  CZ   . PHE   A 1 237 ? -40.407 -13.512 -16.200 1.00 21.26  ? 234 PHE   A CZ   1 
ATOM   3723 H  H    . PHE   A 1 237 ? -40.202 -19.830 -18.147 1.00 29.71  ? 234 PHE   A H    1 
ATOM   3724 H  HA   . PHE   A 1 237 ? -42.033 -18.013 -18.236 1.00 28.76  ? 234 PHE   A HA   1 
ATOM   3725 H  HB2  . PHE   A 1 237 ? -40.903 -18.158 -16.286 1.00 29.17  ? 234 PHE   A HB2  1 
ATOM   3726 H  HB3  . PHE   A 1 237 ? -39.492 -18.037 -17.008 1.00 29.17  ? 234 PHE   A HB3  1 
ATOM   3727 H  HD1  . PHE   A 1 237 ? -42.309 -16.128 -16.165 1.00 25.61  ? 234 PHE   A HD1  1 
ATOM   3728 H  HD2  . PHE   A 1 237 ? -38.463 -15.938 -17.155 1.00 25.60  ? 234 PHE   A HD2  1 
ATOM   3729 H  HE1  . PHE   A 1 237 ? -42.329 -13.833 -15.815 1.00 25.83  ? 234 PHE   A HE1  1 
ATOM   3730 H  HE2  . PHE   A 1 237 ? -38.456 -13.636 -16.737 1.00 28.10  ? 234 PHE   A HE2  1 
ATOM   3731 H  HZ   . PHE   A 1 237 ? -40.417 -12.601 -16.014 1.00 25.55  ? 234 PHE   A HZ   1 
ATOM   3732 N  N    . PRO   A 1 238 ? -39.553 -17.073 -20.066 1.00 19.57  ? 235 PRO   A N    1 
ATOM   3733 C  CA   . PRO   A 1 238 ? -39.274 -16.048 -21.075 1.00 20.63  ? 235 PRO   A CA   1 
ATOM   3734 C  C    . PRO   A 1 238 ? -40.267 -16.053 -22.214 1.00 20.33  ? 235 PRO   A C    1 
ATOM   3735 O  O    . PRO   A 1 238 ? -40.552 -14.994 -22.795 1.00 19.79  ? 235 PRO   A O    1 
ATOM   3736 C  CB   . PRO   A 1 238 ? -37.850 -16.386 -21.532 1.00 23.03  ? 235 PRO   A CB   1 
ATOM   3737 C  CG   . PRO   A 1 238 ? -37.253 -17.145 -20.361 1.00 25.41  ? 235 PRO   A CG   1 
ATOM   3738 C  CD   . PRO   A 1 238 ? -38.375 -17.923 -19.792 1.00 23.74  ? 235 PRO   A CD   1 
ATOM   3739 H  HA   . PRO   A 1 238 ? -39.266 -15.167 -20.669 1.00 24.80  ? 235 PRO   A HA   1 
ATOM   3740 H  HB2  . PRO   A 1 238 ? -37.877 -16.938 -22.329 1.00 27.67  ? 235 PRO   A HB2  1 
ATOM   3741 H  HB3  . PRO   A 1 238 ? -37.354 -15.571 -21.710 1.00 27.67  ? 235 PRO   A HB3  1 
ATOM   3742 H  HG2  . PRO   A 1 238 ? -36.548 -17.733 -20.673 1.00 30.54  ? 235 PRO   A HG2  1 
ATOM   3743 H  HG3  . PRO   A 1 238 ? -36.900 -16.520 -19.709 1.00 30.54  ? 235 PRO   A HG3  1 
ATOM   3744 H  HD2  . PRO   A 1 238 ? -38.459 -18.782 -20.236 1.00 28.53  ? 235 PRO   A HD2  1 
ATOM   3745 H  HD3  . PRO   A 1 238 ? -38.257 -18.052 -18.838 1.00 28.53  ? 235 PRO   A HD3  1 
ATOM   3746 N  N    . GLN   A 1 239 ? -40.817 -17.208 -22.561 1.00 21.36  ? 236 GLN   A N    1 
ATOM   3747 C  CA   . GLN   A 1 239 ? -41.824 -17.206 -23.612 1.00 20.28  ? 236 GLN   A CA   1 
ATOM   3748 C  C    . GLN   A 1 239 ? -43.074 -16.468 -23.170 1.00 21.19  ? 236 GLN   A C    1 
ATOM   3749 O  O    . GLN   A 1 239 ? -43.690 -15.757 -23.979 1.00 22.69  ? 236 GLN   A O    1 
ATOM   3750 C  CB   . GLN   A 1 239 ? -42.165 -18.619 -24.060 1.00 20.92  ? 236 GLN   A CB   1 
ATOM   3751 C  CG   . GLN   A 1 239 ? -40.934 -19.311 -24.629 1.00 23.33  ? 236 GLN   A CG   1 
ATOM   3752 C  CD   . GLN   A 1 239 ? -41.239 -20.259 -25.754 1.00 21.58  ? 236 GLN   A CD   1 
ATOM   3753 O  OE1  . GLN   A 1 239 ? -42.396 -20.579 -26.051 1.00 25.26  ? 236 GLN   A OE1  1 
ATOM   3754 N  NE2  . GLN   A 1 239 ? -40.165 -20.717 -26.418 1.00 23.36  ? 236 GLN   A NE2  1 
ATOM   3755 H  H    . GLN   A 1 239 ? -40.634 -17.975 -22.218 1.00 25.67  ? 236 GLN   A H    1 
ATOM   3756 H  HA   . GLN   A 1 239 ? -41.450 -16.749 -24.382 1.00 24.38  ? 236 GLN   A HA   1 
ATOM   3757 H  HB2  . GLN   A 1 239 ? -42.486 -19.131 -23.301 1.00 25.15  ? 236 GLN   A HB2  1 
ATOM   3758 H  HB3  . GLN   A 1 239 ? -42.848 -18.585 -24.749 1.00 25.15  ? 236 GLN   A HB3  1 
ATOM   3759 H  HG2  . GLN   A 1 239 ? -40.325 -18.636 -24.968 1.00 28.04  ? 236 GLN   A HG2  1 
ATOM   3760 H  HG3  . GLN   A 1 239 ? -40.507 -19.819 -23.922 1.00 28.04  ? 236 GLN   A HG3  1 
ATOM   3761 H  HE21 . GLN   A 1 239 ? -39.376 -20.463 -26.187 1.00 28.08  ? 236 GLN   A HE21 1 
ATOM   3762 H  HE22 . GLN   A 1 239 ? -40.266 -21.263 -27.074 1.00 28.08  ? 236 GLN   A HE22 1 
ATOM   3763 N  N    . ASP   A 1 240 ? -43.441 -16.595 -21.885 1.00 21.68  ? 237 ASP   A N    1 
ATOM   3764 C  CA   . ASP   A 1 240 ? -44.585 -15.865 -21.345 1.00 20.80  ? 237 ASP   A CA   1 
ATOM   3765 C  C    . ASP   A 1 240 ? -44.330 -14.364 -21.357 1.00 21.38  ? 237 ASP   A C    1 
ATOM   3766 O  O    . ASP   A 1 240 ? -45.281 -13.589 -21.523 1.00 21.47  ? 237 ASP   A O    1 
ATOM   3767 C  CB   . ASP   A 1 240 ? -44.919 -16.338 -19.928 1.00 24.36  ? 237 ASP   A CB   1 
ATOM   3768 C  CG   . ASP   A 1 240 ? -45.538 -17.719 -19.911 1.00 29.73  ? 237 ASP   A CG   1 
ATOM   3769 O  OD1  . ASP   A 1 240 ? -46.114 -18.111 -20.945 1.00 32.32  ? 237 ASP   A OD1  1 
ATOM   3770 O  OD2  . ASP   A 1 240 ? -45.465 -18.403 -18.863 1.00 36.05  ? 237 ASP   A OD2  1 
ATOM   3771 H  H    . ASP   A 1 240 ? -43.043 -17.096 -21.311 1.00 26.06  ? 237 ASP   A H    1 
ATOM   3772 H  HA   . ASP   A 1 240 ? -45.359 -16.053 -21.898 1.00 25.00  ? 237 ASP   A HA   1 
ATOM   3773 H  HB2  . ASP   A 1 240 ? -44.104 -16.366 -19.403 1.00 29.28  ? 237 ASP   A HB2  1 
ATOM   3774 H  HB3  . ASP   A 1 240 ? -45.550 -15.720 -19.528 1.00 29.28  ? 237 ASP   A HB3  1 
ATOM   3775 N  N    . VAL   A 1 241 ? -43.071 -13.935 -21.161 1.00 19.65  ? 238 VAL   A N    1 
ATOM   3776 C  CA   . VAL   A 1 241 ? -42.751 -12.518 -21.316 1.00 16.57  ? 238 VAL   A CA   1 
ATOM   3777 C  C    . VAL   A 1 241 ? -43.034 -12.066 -22.738 1.00 18.92  ? 238 VAL   A C    1 
ATOM   3778 O  O    . VAL   A 1 241 ? -43.701 -11.043 -22.962 1.00 20.41  ? 238 VAL   A O    1 
ATOM   3779 C  CB   . VAL   A 1 241 ? -41.295 -12.232 -20.921 1.00 17.12  ? 238 VAL   A CB   1 
ATOM   3780 C  CG1  . VAL   A 1 241 ? -40.942 -10.766 -21.171 1.00 18.69  ? 238 VAL   A CG1  1 
ATOM   3781 C  CG2  . VAL   A 1 241 ? -41.056 -12.654 -19.495 1.00 20.81  ? 238 VAL   A CG2  1 
ATOM   3782 H  H    . VAL   A 1 241 ? -42.406 -14.436 -20.945 1.00 23.62  ? 238 VAL   A H    1 
ATOM   3783 H  HA   . VAL   A 1 241 ? -43.324 -12.016 -20.715 1.00 19.93  ? 238 VAL   A HA   1 
ATOM   3784 H  HB   . VAL   A 1 241 ? -40.695 -12.754 -21.476 1.00 20.58  ? 238 VAL   A HB   1 
ATOM   3785 H  HG11 . VAL   A 1 241 ? -40.093 -10.568 -20.745 1.00 22.47  ? 238 VAL   A HG11 1 
ATOM   3786 H  HG12 . VAL   A 1 241 ? -40.876 -10.616 -22.127 1.00 22.47  ? 238 VAL   A HG12 1 
ATOM   3787 H  HG13 . VAL   A 1 241 ? -41.639 -10.205 -20.795 1.00 22.47  ? 238 VAL   A HG13 1 
ATOM   3788 H  HG21 . VAL   A 1 241 ? -40.167 -12.375 -19.228 1.00 25.01  ? 238 VAL   A HG21 1 
ATOM   3789 H  HG22 . VAL   A 1 241 ? -41.720 -12.234 -18.927 1.00 25.01  ? 238 VAL   A HG22 1 
ATOM   3790 H  HG23 . VAL   A 1 241 ? -41.132 -13.619 -19.435 1.00 25.01  ? 238 VAL   A HG23 1 
ATOM   3791 N  N    . ASN   A 1 242 ? -42.557 -12.831 -23.737 1.00 18.59  ? 239 ASN   A N    1 
ATOM   3792 C  CA   . ASN   A 1 242 ? -42.834 -12.443 -25.119 1.00 18.94  ? 239 ASN   A CA   1 
ATOM   3793 C  C    . ASN   A 1 242 ? -44.343 -12.463 -25.430 1.00 18.39  ? 239 ASN   A C    1 
ATOM   3794 O  O    . ASN   A 1 242 ? -44.841 -11.572 -26.131 1.00 19.99  ? 239 ASN   A O    1 
ATOM   3795 C  CB   . ASN   A 1 242 ? -42.099 -13.371 -26.074 1.00 17.27  ? 239 ASN   A CB   1 
ATOM   3796 C  CG   . ASN   A 1 242 ? -40.674 -12.913 -26.320 1.00 19.59  ? 239 ASN   A CG   1 
ATOM   3797 O  OD1  . ASN   A 1 242 ? -40.332 -11.765 -26.060 1.00 18.91  ? 239 ASN   A OD1  1 
ATOM   3798 N  ND2  . ASN   A 1 242 ? -39.858 -13.786 -26.894 1.00 19.74  ? 239 ASN   A ND2  1 
ATOM   3799 H  H    . ASN   A 1 242 ? -42.092 -13.548 -23.639 1.00 22.35  ? 239 ASN   A H    1 
ATOM   3800 H  HA   . ASN   A 1 242 ? -42.513 -11.537 -25.248 1.00 22.77  ? 239 ASN   A HA   1 
ATOM   3801 H  HB2  . ASN   A 1 242 ? -42.070 -14.263 -25.694 1.00 20.77  ? 239 ASN   A HB2  1 
ATOM   3802 H  HB3  . ASN   A 1 242 ? -42.564 -13.387 -26.925 1.00 20.77  ? 239 ASN   A HB3  1 
ATOM   3803 H  HD21 . ASN   A 1 242 ? -39.041 -13.570 -27.053 1.00 23.73  ? 239 ASN   A HD21 1 
ATOM   3804 H  HD22 . ASN   A 1 242 ? -40.146 -14.567 -27.108 1.00 23.73  ? 239 ASN   A HD22 1 
ATOM   3805 N  N    . PHE   A 1 243 ? -45.100 -13.433 -24.902 1.00 18.52  ? 240 PHE   A N    1 
ATOM   3806 C  CA   . PHE   A 1 243 ? -46.556 -13.431 -25.123 1.00 20.41  ? 240 PHE   A CA   1 
ATOM   3807 C  C    . PHE   A 1 243 ? -47.220 -12.185 -24.526 1.00 20.15  ? 240 PHE   A C    1 
ATOM   3808 O  O    . PHE   A 1 243 ? -48.170 -11.630 -25.112 1.00 23.01  ? 240 PHE   A O    1 
ATOM   3809 C  CB   . PHE   A 1 243 ? -47.208 -14.685 -24.539 1.00 23.52  ? 240 PHE   A CB   1 
ATOM   3810 C  CG   . PHE   A 1 243 ? -46.854 -15.944 -25.287 1.00 24.11  ? 240 PHE   A CG   1 
ATOM   3811 C  CD1  . PHE   A 1 243 ? -46.821 -15.938 -26.665 1.00 32.15  ? 240 PHE   A CD1  1 
ATOM   3812 C  CD2  . PHE   A 1 243 ? -46.577 -17.105 -24.615 1.00 30.01  ? 240 PHE   A CD2  1 
ATOM   3813 C  CE1  . PHE   A 1 243 ? -46.485 -17.083 -27.366 1.00 40.85  ? 240 PHE   A CE1  1 
ATOM   3814 C  CE2  . PHE   A 1 243 ? -46.232 -18.256 -25.320 1.00 38.23  ? 240 PHE   A CE2  1 
ATOM   3815 C  CZ   . PHE   A 1 243 ? -46.187 -18.232 -26.682 1.00 31.43  ? 240 PHE   A CZ   1 
ATOM   3816 H  H    . PHE   A 1 243 ? -44.807 -14.086 -24.425 1.00 22.26  ? 240 PHE   A H    1 
ATOM   3817 H  HA   . PHE   A 1 243 ? -46.700 -13.435 -26.083 1.00 24.53  ? 240 PHE   A HA   1 
ATOM   3818 H  HB2  . PHE   A 1 243 ? -46.916 -14.791 -23.621 1.00 28.27  ? 240 PHE   A HB2  1 
ATOM   3819 H  HB3  . PHE   A 1 243 ? -48.172 -14.581 -24.571 1.00 28.27  ? 240 PHE   A HB3  1 
ATOM   3820 H  HD1  . PHE   A 1 243 ? -47.025 -15.157 -27.127 1.00 38.62  ? 240 PHE   A HD1  1 
ATOM   3821 H  HD2  . PHE   A 1 243 ? -46.619 -17.125 -23.687 1.00 36.06  ? 240 PHE   A HD2  1 
ATOM   3822 H  HE1  . PHE   A 1 243 ? -46.462 -17.072 -28.295 1.00 49.06  ? 240 PHE   A HE1  1 
ATOM   3823 H  HE2  . PHE   A 1 243 ? -46.033 -19.040 -24.861 1.00 45.91  ? 240 PHE   A HE2  1 
ATOM   3824 H  HZ   . PHE   A 1 243 ? -45.953 -19.000 -27.150 1.00 37.75  ? 240 PHE   A HZ   1 
ATOM   3825 N  N    . TYR   A 1 244 ? -46.726 -11.721 -23.375 1.00 20.25  ? 241 TYR   A N    1 
ATOM   3826 C  CA   . TYR   A 1 244 ? -47.310 -10.511 -22.793 1.00 20.90  ? 241 TYR   A CA   1 
ATOM   3827 C  C    . TYR   A 1 244 ? -46.972 -9.279  -23.636 1.00 21.00  ? 241 TYR   A C    1 
ATOM   3828 O  O    . TYR   A 1 244 ? -47.854 -8.438  -23.886 1.00 22.19  ? 241 TYR   A O    1 
ATOM   3829 C  CB   . TYR   A 1 244 ? -46.839 -10.324 -21.347 1.00 20.14  ? 241 TYR   A CB   1 
ATOM   3830 C  CG   . TYR   A 1 244 ? -47.565 -9.177  -20.665 1.00 21.86  ? 241 TYR   A CG   1 
ATOM   3831 C  CD1  . TYR   A 1 244 ? -48.902 -9.287  -20.322 1.00 22.97  ? 241 TYR   A CD1  1 
ATOM   3832 C  CD2  . TYR   A 1 244 ? -46.927 -7.972  -20.420 1.00 20.67  ? 241 TYR   A CD2  1 
ATOM   3833 C  CE1  . TYR   A 1 244 ? -49.591 -8.233  -19.754 1.00 24.98  ? 241 TYR   A CE1  1 
ATOM   3834 C  CE2  . TYR   A 1 244 ? -47.604 -6.910  -19.846 1.00 22.18  ? 241 TYR   A CE2  1 
ATOM   3835 C  CZ   . TYR   A 1 244 ? -48.917 -7.040  -19.506 1.00 24.22  ? 241 TYR   A CZ   1 
ATOM   3836 O  OH   . TYR   A 1 244 ? -49.655 -6.019  -18.923 1.00 28.58  ? 241 TYR   A OH   1 
ATOM   3837 H  H    . TYR   A 1 244 ? -46.080 -12.073 -22.930 1.00 24.34  ? 241 TYR   A H    1 
ATOM   3838 H  HA   . TYR   A 1 244 ? -48.275 -10.613 -22.772 1.00 25.13  ? 241 TYR   A HA   1 
ATOM   3839 H  HB2  . TYR   A 1 244 ? -47.012 -11.136 -20.846 1.00 24.22  ? 241 TYR   A HB2  1 
ATOM   3840 H  HB3  . TYR   A 1 244 ? -45.888 -10.128 -21.343 1.00 24.22  ? 241 TYR   A HB3  1 
ATOM   3841 H  HD1  . TYR   A 1 244 ? -49.346 -10.089 -20.478 1.00 27.60  ? 241 TYR   A HD1  1 
ATOM   3842 H  HD2  . TYR   A 1 244 ? -46.030 -7.874  -20.645 1.00 24.84  ? 241 TYR   A HD2  1 
ATOM   3843 H  HE1  . TYR   A 1 244 ? -50.492 -8.319  -19.541 1.00 30.02  ? 241 TYR   A HE1  1 
ATOM   3844 H  HE2  . TYR   A 1 244 ? -47.162 -6.106  -19.693 1.00 26.66  ? 241 TYR   A HE2  1 
ATOM   3845 H  HH   . TYR   A 1 244 ? -49.291 -5.277  -19.076 1.00 34.33  ? 241 TYR   A HH   1 
ATOM   3846 N  N    . ILE   A 1 245 ? -45.709 -9.147  -24.065 1.00 19.26  ? 242 ILE   A N    1 
ATOM   3847 C  CA   . ILE   A 1 245 ? -45.368 -8.038  -24.952 1.00 19.24  ? 242 ILE   A CA   1 
ATOM   3848 C  C    . ILE   A 1 245 ? -46.266 -8.068  -26.185 1.00 18.44  ? 242 ILE   A C    1 
ATOM   3849 O  O    . ILE   A 1 245 ? -46.805 -7.047  -26.604 1.00 21.95  ? 242 ILE   A O    1 
ATOM   3850 C  CB   . ILE   A 1 245 ? -43.883 -8.080  -25.341 1.00 17.38  ? 242 ILE   A CB   1 
ATOM   3851 C  CG1  . ILE   A 1 245 ? -42.969 -7.942  -24.124 1.00 19.43  ? 242 ILE   A CG1  1 
ATOM   3852 C  CG2  . ILE   A 1 245 ? -43.597 -6.995  -26.385 1.00 19.54  ? 242 ILE   A CG2  1 
ATOM   3853 C  CD1  . ILE   A 1 245 ? -41.503 -8.252  -24.414 1.00 18.83  ? 242 ILE   A CD1  1 
ATOM   3854 H  H    . ILE   A 1 245 ? -45.057 -9.671  -23.863 1.00 23.16  ? 242 ILE   A H    1 
ATOM   3855 H  HA   . ILE   A 1 245 ? -45.521 -7.207  -24.477 1.00 23.13  ? 242 ILE   A HA   1 
ATOM   3856 H  HB   . ILE   A 1 245 ? -43.694 -8.950  -25.727 1.00 20.89  ? 242 ILE   A HB   1 
ATOM   3857 H  HG12 . ILE   A 1 245 ? -43.019 -7.029  -23.799 1.00 23.36  ? 242 ILE   A HG12 1 
ATOM   3858 H  HG13 . ILE   A 1 245 ? -43.271 -8.556  -23.437 1.00 23.36  ? 242 ILE   A HG13 1 
ATOM   3859 H  HG21 . ILE   A 1 245 ? -42.637 -6.908  -26.495 1.00 23.49  ? 242 ILE   A HG21 1 
ATOM   3860 H  HG22 . ILE   A 1 245 ? -44.005 -7.251  -27.227 1.00 23.49  ? 242 ILE   A HG22 1 
ATOM   3861 H  HG23 . ILE   A 1 245 ? -43.972 -6.155  -26.078 1.00 23.49  ? 242 ILE   A HG23 1 
ATOM   3862 H  HD11 . ILE   A 1 245 ? -41.000 -8.204  -23.586 1.00 22.64  ? 242 ILE   A HD11 1 
ATOM   3863 H  HD12 . ILE   A 1 245 ? -41.437 -9.144  -24.790 1.00 22.64  ? 242 ILE   A HD12 1 
ATOM   3864 H  HD13 . ILE   A 1 245 ? -41.161 -7.601  -25.047 1.00 22.64  ? 242 ILE   A HD13 1 
ATOM   3865 N  N    . ASN   A 1 246 ? -46.366 -9.239  -26.836 1.00 19.04  ? 243 ASN   A N    1 
ATOM   3866 C  CA   . ASN   A 1 246 ? -47.226 -9.336  -28.015 1.00 21.86  ? 243 ASN   A CA   1 
ATOM   3867 C  C    . ASN   A 1 246 ? -48.664 -8.936  -27.706 1.00 21.83  ? 243 ASN   A C    1 
ATOM   3868 O  O    . ASN   A 1 246 ? -49.306 -8.199  -28.475 1.00 23.04  ? 243 ASN   A O    1 
ATOM   3869 C  CB   . ASN   A 1 246 ? -47.161 -10.773 -28.562 1.00 20.18  ? 243 ASN   A CB   1 
ATOM   3870 C  CG   . ASN   A 1 246 ? -48.184 -11.034 -29.610 1.00 23.12  ? 243 ASN   A CG   1 
ATOM   3871 O  OD1  . ASN   A 1 246 ? -49.249 -11.592 -29.344 1.00 26.78  ? 243 ASN   A OD1  1 
ATOM   3872 N  ND2  . ASN   A 1 246 ? -47.860 -10.646 -30.847 1.00 25.08  ? 243 ASN   A ND2  1 
ATOM   3873 H  H    . ASN   A 1 246 ? -45.959 -9.965  -26.620 1.00 22.89  ? 243 ASN   A H    1 
ATOM   3874 H  HA   . ASN   A 1 246 ? -46.903 -8.725  -28.696 1.00 26.27  ? 243 ASN   A HA   1 
ATOM   3875 H  HB2  . ASN   A 1 246 ? -46.286 -10.925 -28.952 1.00 24.26  ? 243 ASN   A HB2  1 
ATOM   3876 H  HB3  . ASN   A 1 246 ? -47.312 -11.396 -27.834 1.00 24.26  ? 243 ASN   A HB3  1 
ATOM   3877 H  HD21 . ASN   A 1 246 ? -48.411 -10.770 -31.495 1.00 30.13  ? 243 ASN   A HD21 1 
ATOM   3878 H  HD22 . ASN   A 1 246 ? -47.100 -10.271 -30.995 1.00 30.13  ? 243 ASN   A HD22 1 
ATOM   3879 N  N    . LYS   A 1 247 ? -49.197 -9.400  -26.577 1.00 21.45  ? 244 LYS   A N    1 
ATOM   3880 C  CA   . LYS   A 1 247 ? -50.586 -9.107  -26.252 1.00 22.45  ? 244 LYS   A CA   1 
ATOM   3881 C  C    . LYS   A 1 247 ? -50.825 -7.608  -26.165 1.00 23.38  ? 244 LYS   A C    1 
ATOM   3882 O  O    . LYS   A 1 247 ? -51.845 -7.102  -26.634 1.00 25.73  ? 244 LYS   A O    1 
ATOM   3883 C  CB   . LYS   A 1 247 ? -50.981 -9.788  -24.930 1.00 25.77  ? 244 LYS   A CB   1 
ATOM   3884 C  CG   . LYS   A 1 247 ? -52.402 -9.486  -24.442 1.00 26.65  ? 244 LYS   A CG   1 
ATOM   3885 C  CD   . LYS   A 1 247 ? -52.697 -10.034 -23.051 1.00 26.00  ? 244 LYS   A CD   1 
ATOM   3886 C  CE   . LYS   A 1 247 ? -54.179 -9.814  -22.652 1.00 35.24  ? 244 LYS   A CE   1 
ATOM   3887 N  NZ   . LYS   A 1 247 ? -54.617 -10.739 -21.567 1.00 45.32  ? 244 LYS   A NZ   1 
ATOM   3888 H  H    . LYS   A 1 247 ? -48.782 -9.878  -25.994 1.00 25.78  ? 244 LYS   A H    1 
ATOM   3889 H  HA   . LYS   A 1 247 ? -51.150 -9.466  -26.955 1.00 26.99  ? 244 LYS   A HA   1 
ATOM   3890 H  HB2  . LYS   A 1 247 ? -50.913 -10.749 -25.048 1.00 30.97  ? 244 LYS   A HB2  1 
ATOM   3891 H  HB3  . LYS   A 1 247 ? -50.368 -9.494  -24.239 1.00 30.97  ? 244 LYS   A HB3  1 
ATOM   3892 H  HG2  . LYS   A 1 247 ? -52.526 -8.524  -24.414 1.00 32.02  ? 244 LYS   A HG2  1 
ATOM   3893 H  HG3  . LYS   A 1 247 ? -53.037 -9.884  -25.058 1.00 32.02  ? 244 LYS   A HG3  1 
ATOM   3894 H  HD2  . LYS   A 1 247 ? -52.516 -10.987 -23.037 1.00 31.24  ? 244 LYS   A HD2  1 
ATOM   3895 H  HD3  . LYS   A 1 247 ? -52.136 -9.581  -22.402 1.00 31.24  ? 244 LYS   A HD3  1 
ATOM   3896 H  HE2  . LYS   A 1 247 ? -54.291 -8.904  -22.336 1.00 42.33  ? 244 LYS   A HE2  1 
ATOM   3897 H  HE3  . LYS   A 1 247 ? -54.743 -9.968  -23.426 1.00 42.33  ? 244 LYS   A HE3  1 
ATOM   3898 H  HZ1  . LYS   A 1 247 ? -55.467 -10.580 -21.357 1.00 54.42  ? 244 LYS   A HZ1  1 
ATOM   3899 H  HZ2  . LYS   A 1 247 ? -54.540 -11.584 -21.837 1.00 54.42  ? 244 LYS   A HZ2  1 
ATOM   3900 H  HZ3  . LYS   A 1 247 ? -54.113 -10.620 -20.844 1.00 54.42  ? 244 LYS   A HZ3  1 
ATOM   3901 N  N    . GLU   A 1 248 ? -49.900 -6.886  -25.577 1.00 23.25  ? 245 GLU   A N    1 
ATOM   3902 C  CA   . GLU   A 1 248 ? -50.120 -5.483  -25.270 1.00 23.63  ? 245 GLU   A CA   1 
ATOM   3903 C  C    . GLU   A 1 248 ? -49.597 -4.531  -26.338 1.00 25.49  ? 245 GLU   A C    1 
ATOM   3904 O  O    . GLU   A 1 248 ? -49.975 -3.344  -26.325 1.00 31.27  ? 245 GLU   A O    1 
ATOM   3905 C  CB   . GLU   A 1 248 ? -49.438 -5.144  -23.944 1.00 24.23  ? 245 GLU   A CB   1 
ATOM   3906 C  CG   . GLU   A 1 248 ? -49.953 -5.845  -22.685 1.00 24.06  ? 245 GLU   A CG   1 
ATOM   3907 C  CD   . GLU   A 1 248 ? -51.435 -5.791  -22.497 1.00 26.99  ? 245 GLU   A CD   1 
ATOM   3908 O  OE1  . GLU   A 1 248 ? -52.102 -4.881  -23.066 1.00 27.30  ? 245 GLU   A OE1  1 
ATOM   3909 O  OE2  . GLU   A 1 248 ? -51.925 -6.584  -21.650 1.00 30.34  ? 245 GLU   A OE2  1 
ATOM   3910 H  H    . GLU   A 1 248 ? -49.129 -7.183  -25.340 1.00 27.94  ? 245 GLU   A H    1 
ATOM   3911 H  HA   . GLU   A 1 248 ? -51.075 -5.335  -25.189 1.00 28.40  ? 245 GLU   A HA   1 
ATOM   3912 H  HB2  . GLU   A 1 248 ? -48.498 -5.372  -24.026 1.00 29.12  ? 245 GLU   A HB2  1 
ATOM   3913 H  HB3  . GLU   A 1 248 ? -49.536 -4.191  -23.794 1.00 29.12  ? 245 GLU   A HB3  1 
ATOM   3914 H  HG2  . GLU   A 1 248 ? -49.699 -6.780  -22.728 1.00 28.91  ? 245 GLU   A HG2  1 
ATOM   3915 H  HG3  . GLU   A 1 248 ? -49.546 -5.425  -21.911 1.00 28.91  ? 245 GLU   A HG3  1 
ATOM   3916 N  N    . THR   A 1 249 ? -48.784 -5.014  -27.279 1.00 25.01  ? 246 THR   A N    1 
ATOM   3917 C  CA   . THR   A 1 249 ? -48.201 -4.161  -28.297 1.00 24.86  ? 246 THR   A CA   1 
ATOM   3918 C  C    . THR   A 1 249 ? -48.485 -4.573  -29.718 1.00 27.36  ? 246 THR   A C    1 
ATOM   3919 O  O    . THR   A 1 249 ? -48.336 -3.736  -30.618 1.00 28.85  ? 246 THR   A O    1 
ATOM   3920 C  CB   . THR   A 1 249 ? -46.670 -4.105  -28.168 1.00 24.65  ? 246 THR   A CB   1 
ATOM   3921 O  OG1  . THR   A 1 249 ? -46.095 -5.365  -28.555 1.00 23.66  ? 246 THR   A OG1  1 
ATOM   3922 C  CG2  . THR   A 1 249 ? -46.247 -3.738  -26.750 1.00 28.27  ? 246 THR   A CG2  1 
ATOM   3923 H  H    . THR   A 1 249 ? -48.556 -5.841  -27.343 1.00 30.05  ? 246 THR   A H    1 
ATOM   3924 H  HA   . THR   A 1 249 ? -48.570 -3.276  -28.150 1.00 29.87  ? 246 THR   A HA   1 
ATOM   3925 H  HB   . THR   A 1 249 ? -46.329 -3.414  -28.758 1.00 29.62  ? 246 THR   A HB   1 
ATOM   3926 H  HG1  . THR   A 1 249 ? -46.483 -5.993  -28.155 1.00 28.44  ? 246 THR   A HG1  1 
ATOM   3927 H  HG21 . THR   A 1 249 ? -45.296 -3.548  -26.726 1.00 33.97  ? 246 THR   A HG21 1 
ATOM   3928 H  HG22 . THR   A 1 249 ? -46.732 -2.953  -26.451 1.00 33.97  ? 246 THR   A HG22 1 
ATOM   3929 H  HG23 . THR   A 1 249 ? -46.436 -4.474  -26.146 1.00 33.97  ? 246 THR   A HG23 1 
ATOM   3930 N  N    . GLY   A 1 250 ? -48.865 -5.821  -29.959 1.00 24.09  ? 247 GLY   A N    1 
ATOM   3931 C  CA   . GLY   A 1 250 ? -49.016 -6.310  -31.317 1.00 25.07  ? 247 GLY   A CA   1 
ATOM   3932 C  C    . GLY   A 1 250 ? -47.728 -6.653  -32.027 1.00 25.89  ? 247 GLY   A C    1 
ATOM   3933 O  O    . GLY   A 1 250 ? -47.770 -6.987  -33.216 1.00 28.57  ? 247 GLY   A O    1 
ATOM   3934 H  H    . GLY   A 1 250 ? -49.040 -6.403  -29.351 1.00 28.95  ? 247 GLY   A H    1 
ATOM   3935 H  HA2  . GLY   A 1 250 ? -49.564 -7.111  -31.297 1.00 30.13  ? 247 GLY   A HA2  1 
ATOM   3936 H  HA3  . GLY   A 1 250 ? -49.469 -5.631  -31.841 1.00 30.13  ? 247 GLY   A HA3  1 
ATOM   3937 N  N    . ILE   A 1 251 ? -46.589 -6.554  -31.360 1.00 24.82  ? 248 ILE   A N    1 
ATOM   3938 C  CA   . ILE   A 1 251 ? -45.313 -6.883  -32.003 1.00 23.25  ? 248 ILE   A CA   1 
ATOM   3939 C  C    . ILE   A 1 251 ? -45.273 -8.380  -32.270 1.00 24.24  ? 248 ILE   A C    1 
ATOM   3940 O  O    . ILE   A 1 251 ? -45.491 -9.171  -31.335 1.00 22.88  ? 248 ILE   A O    1 
ATOM   3941 C  CB   . ILE   A 1 251 ? -44.154 -6.462  -31.116 1.00 22.00  ? 248 ILE   A CB   1 
ATOM   3942 C  CG1  . ILE   A 1 251 ? -44.086 -4.936  -31.048 1.00 23.89  ? 248 ILE   A CG1  1 
ATOM   3943 C  CG2  . ILE   A 1 251 ? -42.818 -7.062  -31.593 1.00 23.14  ? 248 ILE   A CG2  1 
ATOM   3944 C  CD1  . ILE   A 1 251 ? -43.167 -4.429  -29.985 1.00 26.94  ? 248 ILE   A CD1  1 
ATOM   3945 H  H    . ILE   A 1 251 ? -46.521 -6.301  -30.541 1.00 29.82  ? 248 ILE   A H    1 
ATOM   3946 H  HA   . ILE   A 1 251 ? -45.242 -6.411  -32.847 1.00 27.94  ? 248 ILE   A HA   1 
ATOM   3947 H  HB   . ILE   A 1 251 ? -44.313 -6.810  -30.224 1.00 26.44  ? 248 ILE   A HB   1 
ATOM   3948 H  HG12 . ILE   A 1 251 ? -43.770 -4.598  -31.901 1.00 28.71  ? 248 ILE   A HG12 1 
ATOM   3949 H  HG13 . ILE   A 1 251 ? -44.974 -4.591  -30.863 1.00 28.71  ? 248 ILE   A HG13 1 
ATOM   3950 H  HG21 . ILE   A 1 251 ? -42.118 -6.811  -30.969 1.00 27.81  ? 248 ILE   A HG21 1 
ATOM   3951 H  HG22 . ILE   A 1 251 ? -42.900 -8.028  -31.628 1.00 27.81  ? 248 ILE   A HG22 1 
ATOM   3952 H  HG23 . ILE   A 1 251 ? -42.613 -6.715  -32.475 1.00 27.81  ? 248 ILE   A HG23 1 
ATOM   3953 H  HD11 . ILE   A 1 251 ? -43.286 -3.471  -29.896 1.00 32.37  ? 248 ILE   A HD11 1 
ATOM   3954 H  HD12 . ILE   A 1 251 ? -43.381 -4.869  -29.147 1.00 32.37  ? 248 ILE   A HD12 1 
ATOM   3955 H  HD13 . ILE   A 1 251 ? -42.252 -4.627  -30.239 1.00 32.37  ? 248 ILE   A HD13 1 
ATOM   3956 N  N    . PRO   A 1 252 ? -44.937 -8.811  -33.478 1.00 25.57  ? 249 PRO   A N    1 
ATOM   3957 C  CA   . PRO   A 1 252 ? -45.009 -10.245 -33.805 1.00 29.25  ? 249 PRO   A CA   1 
ATOM   3958 C  C    . PRO   A 1 252 ? -43.971 -11.084 -33.076 1.00 20.70  ? 249 PRO   A C    1 
ATOM   3959 O  O    . PRO   A 1 252 ? -42.862 -10.630 -32.802 1.00 21.46  ? 249 PRO   A O    1 
ATOM   3960 C  CB   . PRO   A 1 252 ? -44.727 -10.279 -35.315 1.00 32.88  ? 249 PRO   A CB   1 
ATOM   3961 C  CG   . PRO   A 1 252 ? -43.831 -9.064  -35.547 1.00 44.75  ? 249 PRO   A CG   1 
ATOM   3962 C  CD   . PRO   A 1 252 ? -44.325 -8.006  -34.564 1.00 33.71  ? 249 PRO   A CD   1 
ATOM   3963 H  HA   . PRO   A 1 252 ? -45.897 -10.575 -33.598 1.00 35.14  ? 249 PRO   A HA   1 
ATOM   3964 H  HB2  . PRO   A 1 252 ? -44.272 -11.101 -35.553 1.00 39.50  ? 249 PRO   A HB2  1 
ATOM   3965 H  HB3  . PRO   A 1 252 ? -45.556 -10.203 -35.813 1.00 39.50  ? 249 PRO   A HB3  1 
ATOM   3966 H  HG2  . PRO   A 1 252 ? -42.907 -9.298  -35.367 1.00 53.75  ? 249 PRO   A HG2  1 
ATOM   3967 H  HG3  . PRO   A 1 252 ? -43.924 -8.756  -36.462 1.00 53.75  ? 249 PRO   A HG3  1 
ATOM   3968 H  HD2  . PRO   A 1 252 ? -43.586 -7.476  -34.226 1.00 40.49  ? 249 PRO   A HD2  1 
ATOM   3969 H  HD3  . PRO   A 1 252 ? -44.984 -7.428  -34.980 1.00 40.49  ? 249 PRO   A HD3  1 
ATOM   3970 N  N    . ILE   A 1 253 ? -44.367 -12.340 -32.805 1.00 22.68  ? 250 ILE   A N    1 
ATOM   3971 C  CA   . ILE   A 1 253 ? -43.478 -13.391 -32.314 1.00 21.47  ? 250 ILE   A CA   1 
ATOM   3972 C  C    . ILE   A 1 253 ? -43.152 -14.288 -33.501 1.00 22.42  ? 250 ILE   A C    1 
ATOM   3973 O  O    . ILE   A 1 253 ? -44.058 -14.743 -34.198 1.00 22.23  ? 250 ILE   A O    1 
ATOM   3974 C  CB   . ILE   A 1 253 ? -44.139 -14.214 -31.197 1.00 20.94  ? 250 ILE   A CB   1 
ATOM   3975 C  CG1  . ILE   A 1 253 ? -44.376 -13.347 -29.976 1.00 20.25  ? 250 ILE   A CG1  1 
ATOM   3976 C  CG2  . ILE   A 1 253 ? -43.257 -15.413 -30.787 1.00 25.04  ? 250 ILE   A CG2  1 
ATOM   3977 C  CD1  . ILE   A 1 253 ? -45.314 -13.942 -28.952 1.00 26.30  ? 250 ILE   A CD1  1 
ATOM   3978 H  H    . ILE   A 1 253 ? -45.177 -12.611 -32.903 1.00 27.26  ? 250 ILE   A H    1 
ATOM   3979 H  HA   . ILE   A 1 253 ? -42.666 -12.996 -31.959 1.00 25.81  ? 250 ILE   A HA   1 
ATOM   3980 H  HB   . ILE   A 1 253 ? -44.984 -14.542 -31.543 1.00 25.17  ? 250 ILE   A HB   1 
ATOM   3981 H  HG12 . ILE   A 1 253 ? -43.524 -13.194 -29.537 1.00 24.34  ? 250 ILE   A HG12 1 
ATOM   3982 H  HG13 . ILE   A 1 253 ? -44.757 -12.504 -30.266 1.00 24.34  ? 250 ILE   A HG13 1 
ATOM   3983 H  HG21 . ILE   A 1 253 ? -43.592 -15.782 -29.955 1.00 30.10  ? 250 ILE   A HG21 1 
ATOM   3984 H  HG22 . ILE   A 1 253 ? -43.294 -16.086 -31.485 1.00 30.10  ? 250 ILE   A HG22 1 
ATOM   3985 H  HG23 . ILE   A 1 253 ? -42.344 -15.108 -30.670 1.00 30.10  ? 250 ILE   A HG23 1 
ATOM   3986 H  HD11 . ILE   A 1 253 ? -45.489 -13.281 -28.263 1.00 31.61  ? 250 ILE   A HD11 1 
ATOM   3987 H  HD12 . ILE   A 1 253 ? -46.143 -14.190 -29.390 1.00 31.61  ? 250 ILE   A HD12 1 
ATOM   3988 H  HD13 . ILE   A 1 253 ? -44.898 -14.726 -28.560 1.00 31.61  ? 250 ILE   A HD13 1 
ATOM   3989 N  N    . VAL   A 1 254 ? -41.867 -14.552 -33.710 1.00 19.30  ? 251 VAL   A N    1 
ATOM   3990 C  CA   . VAL   A 1 254 ? -41.369 -15.530 -34.667 1.00 18.76  ? 251 VAL   A CA   1 
ATOM   3991 C  C    . VAL   A 1 254 ? -40.809 -16.704 -33.866 1.00 18.98  ? 251 VAL   A C    1 
ATOM   3992 O  O    . VAL   A 1 254 ? -40.056 -16.514 -32.900 1.00 19.51  ? 251 VAL   A O    1 
ATOM   3993 C  CB   . VAL   A 1 254 ? -40.306 -14.898 -35.584 1.00 19.94  ? 251 VAL   A CB   1 
ATOM   3994 C  CG1  . VAL   A 1 254 ? -39.598 -15.900 -36.460 1.00 19.63  ? 251 VAL   A CG1  1 
ATOM   3995 C  CG2  . VAL   A 1 254 ? -40.972 -13.835 -36.431 1.00 25.00  ? 251 VAL   A CG2  1 
ATOM   3996 H  H    . VAL   A 1 254 ? -41.232 -14.156 -33.286 1.00 23.20  ? 251 VAL   A H    1 
ATOM   3997 H  HA   . VAL   A 1 254 ? -42.087 -15.862 -35.229 1.00 22.55  ? 251 VAL   A HA   1 
ATOM   3998 H  HB   . VAL   A 1 254 ? -39.617 -14.510 -35.023 1.00 23.97  ? 251 VAL   A HB   1 
ATOM   3999 H  HG11 . VAL   A 1 254 ? -39.059 -15.424 -37.112 1.00 23.60  ? 251 VAL   A HG11 1 
ATOM   4000 H  HG12 . VAL   A 1 254 ? -39.031 -16.459 -35.907 1.00 23.60  ? 251 VAL   A HG12 1 
ATOM   4001 H  HG13 . VAL   A 1 254 ? -40.259 -16.446 -36.914 1.00 23.60  ? 251 VAL   A HG13 1 
ATOM   4002 H  HG21 . VAL   A 1 254 ? -40.302 -13.411 -36.990 1.00 30.04  ? 251 VAL   A HG21 1 
ATOM   4003 H  HG22 . VAL   A 1 254 ? -41.650 -14.252 -36.986 1.00 30.04  ? 251 VAL   A HG22 1 
ATOM   4004 H  HG23 . VAL   A 1 254 ? -41.381 -13.177 -35.847 1.00 30.04  ? 251 VAL   A HG23 1 
ATOM   4005 N  N    . ASP   A 1 255 ? -41.197 -17.905 -34.243 1.00 21.20  ? 252 ASP   A N    1 
ATOM   4006 C  CA   . ASP   A 1 255 ? -40.676 -19.118 -33.635 1.00 22.65  ? 252 ASP   A CA   1 
ATOM   4007 C  C    . ASP   A 1 255 ? -39.395 -19.533 -34.344 1.00 24.84  ? 252 ASP   A C    1 
ATOM   4008 O  O    . ASP   A 1 255 ? -39.271 -19.399 -35.562 1.00 24.29  ? 252 ASP   A O    1 
ATOM   4009 C  CB   . ASP   A 1 255 ? -41.707 -20.237 -33.698 1.00 25.91  ? 252 ASP   A CB   1 
ATOM   4010 C  CG   . ASP   A 1 255 ? -42.947 -19.926 -32.863 1.00 35.35  ? 252 ASP   A CG   1 
ATOM   4011 O  OD1  . ASP   A 1 255 ? -42.807 -19.348 -31.755 1.00 31.44  ? 252 ASP   A OD1  1 
ATOM   4012 O  OD2  . ASP   A 1 255 ? -44.053 -20.285 -33.307 1.00 39.51  ? 252 ASP   A OD2  1 
ATOM   4013 H  H    . ASP   A 1 255 ? -41.774 -18.051 -34.863 1.00 25.48  ? 252 ASP   A H    1 
ATOM   4014 H  HA   . ASP   A 1 255 ? -40.473 -18.960 -32.700 1.00 27.22  ? 252 ASP   A HA   1 
ATOM   4015 H  HB2  . ASP   A 1 255 ? -41.985 -20.362 -34.619 1.00 31.13  ? 252 ASP   A HB2  1 
ATOM   4016 H  HB3  . ASP   A 1 255 ? -41.310 -21.054 -33.357 1.00 31.13  ? 252 ASP   A HB3  1 
ATOM   4017 N  N    . ILE   A 1 256 ? -38.424 -20.014 -33.577 1.00 22.28  ? 253 ILE   A N    1 
ATOM   4018 C  CA   . ILE   A 1 256 ? -37.079 -20.254 -34.127 1.00 21.25  ? 253 ILE   A CA   1 
ATOM   4019 C  C    . ILE   A 1 256 ? -36.553 -21.566 -33.529 1.00 22.47  ? 253 ILE   A C    1 
ATOM   4020 O  O    . ILE   A 1 256 ? -36.847 -21.875 -32.362 1.00 22.07  ? 253 ILE   A O    1 
ATOM   4021 C  CB   . ILE   A 1 256 ? -36.188 -19.020 -33.875 1.00 18.18  ? 253 ILE   A CB   1 
ATOM   4022 C  CG1  . ILE   A 1 256 ? -34.929 -19.078 -34.753 1.00 19.01  ? 253 ILE   A CG1  1 
ATOM   4023 C  CG2  . ILE   A 1 256 ? -35.829 -18.838 -32.373 1.00 20.14  ? 253 ILE   A CG2  1 
ATOM   4024 C  CD1  . ILE   A 1 256 ? -34.213 -17.757 -34.878 1.00 19.25  ? 253 ILE   A CD1  1 
ATOM   4025 H  H    . ILE   A 1 256 ? -38.511 -20.210 -32.744 1.00 26.78  ? 253 ILE   A H    1 
ATOM   4026 H  HA   . ILE   A 1 256 ? -37.093 -20.389 -35.088 1.00 25.54  ? 253 ILE   A HA   1 
ATOM   4027 H  HB   . ILE   A 1 256 ? -36.705 -18.239 -34.127 1.00 21.85  ? 253 ILE   A HB   1 
ATOM   4028 H  HG12 . ILE   A 1 256 ? -34.308 -19.715 -34.366 1.00 22.85  ? 253 ILE   A HG12 1 
ATOM   4029 H  HG13 . ILE   A 1 256 ? -35.184 -19.362 -35.645 1.00 22.85  ? 253 ILE   A HG13 1 
ATOM   4030 H  HG21 . ILE   A 1 256 ? -35.387 -17.983 -32.255 1.00 24.21  ? 253 ILE   A HG21 1 
ATOM   4031 H  HG22 . ILE   A 1 256 ? -36.644 -18.865 -31.848 1.00 24.21  ? 253 ILE   A HG22 1 
ATOM   4032 H  HG23 . ILE   A 1 256 ? -35.236 -19.557 -32.101 1.00 24.21  ? 253 ILE   A HG23 1 
ATOM   4033 H  HD11 . ILE   A 1 256 ? -33.537 -17.828 -35.570 1.00 23.14  ? 253 ILE   A HD11 1 
ATOM   4034 H  HD12 . ILE   A 1 256 ? -34.856 -17.070 -35.113 1.00 23.14  ? 253 ILE   A HD12 1 
ATOM   4035 H  HD13 . ILE   A 1 256 ? -33.796 -17.543 -34.029 1.00 23.14  ? 253 ILE   A HD13 1 
ATOM   4036 N  N    . PRO   A 1 257 ? -35.815 -22.384 -34.275 1.00 23.10  ? 254 PRO   A N    1 
ATOM   4037 C  CA   . PRO   A 1 257 ? -35.436 -23.706 -33.761 1.00 23.45  ? 254 PRO   A CA   1 
ATOM   4038 C  C    . PRO   A 1 257 ? -34.612 -23.660 -32.483 1.00 21.57  ? 254 PRO   A C    1 
ATOM   4039 O  O    . PRO   A 1 257 ? -33.920 -22.686 -32.195 1.00 24.96  ? 254 PRO   A O    1 
ATOM   4040 C  CB   . PRO   A 1 257 ? -34.617 -24.303 -34.908 1.00 23.12  ? 254 PRO   A CB   1 
ATOM   4041 C  CG   . PRO   A 1 257 ? -35.208 -23.662 -36.140 1.00 25.98  ? 254 PRO   A CG   1 
ATOM   4042 C  CD   . PRO   A 1 257 ? -35.564 -22.260 -35.729 1.00 22.52  ? 254 PRO   A CD   1 
ATOM   4043 H  HA   . PRO   A 1 257 ? -36.239 -24.223 -33.592 1.00 28.18  ? 254 PRO   A HA   1 
ATOM   4044 H  HB2  . PRO   A 1 257 ? -33.681 -24.073 -34.806 1.00 27.79  ? 254 PRO   A HB2  1 
ATOM   4045 H  HB3  . PRO   A 1 257 ? -34.722 -25.267 -34.928 1.00 27.79  ? 254 PRO   A HB3  1 
ATOM   4046 H  HG2  . PRO   A 1 257 ? -34.553 -23.656 -36.854 1.00 31.22  ? 254 PRO   A HG2  1 
ATOM   4047 H  HG3  . PRO   A 1 257 ? -35.998 -24.151 -36.418 1.00 31.22  ? 254 PRO   A HG3  1 
ATOM   4048 H  HD2  . PRO   A 1 257 ? -34.828 -21.652 -35.902 1.00 27.06  ? 254 PRO   A HD2  1 
ATOM   4049 H  HD3  . PRO   A 1 257 ? -36.361 -21.956 -36.192 1.00 27.06  ? 254 PRO   A HD3  1 
ATOM   4050 N  N    . GLY   A 1 258 ? -34.695 -24.761 -31.729 1.00 24.24  ? 255 GLY   A N    1 
ATOM   4051 C  CA   . GLY   A 1 258 ? -33.969 -24.877 -30.483 1.00 28.24  ? 255 GLY   A CA   1 
ATOM   4052 C  C    . GLY   A 1 258 ? -34.694 -24.293 -29.298 1.00 27.55  ? 255 GLY   A C    1 
ATOM   4053 O  O    . GLY   A 1 258 ? -35.832 -23.822 -29.371 1.00 25.48  ? 255 GLY   A O    1 
ATOM   4054 H  H    . GLY   A 1 258 ? -35.170 -25.451 -31.926 1.00 29.13  ? 255 GLY   A H    1 
ATOM   4055 H  HA2  . GLY   A 1 258 ? -33.805 -25.816 -30.300 1.00 33.93  ? 255 GLY   A HA2  1 
ATOM   4056 H  HA3  . GLY   A 1 258 ? -33.119 -24.419 -30.570 1.00 33.93  ? 255 GLY   A HA3  1 
ATOM   4057 N  N    . GLY   A 1 259 ? -34.023 -24.368 -28.164 1.00 24.59  ? 256 GLY   A N    1 
ATOM   4058 C  CA   . GLY   A 1 259 ? -34.590 -23.862 -26.917 1.00 27.89  ? 256 GLY   A CA   1 
ATOM   4059 C  C    . GLY   A 1 259 ? -34.019 -22.521 -26.536 1.00 27.85  ? 256 GLY   A C    1 
ATOM   4060 O  O    . GLY   A 1 259 ? -33.764 -21.665 -27.388 1.00 23.24  ? 256 GLY   A O    1 
ATOM   4061 H  H    . GLY   A 1 259 ? -33.237 -24.708 -28.086 1.00 29.55  ? 256 GLY   A H    1 
ATOM   4062 H  HA2  . GLY   A 1 259 ? -35.550 -23.770 -27.015 1.00 33.51  ? 256 GLY   A HA2  1 
ATOM   4063 H  HA3  . GLY   A 1 259 ? -34.403 -24.490 -26.201 1.00 33.51  ? 256 GLY   A HA3  1 
ATOM   4064 N  N    . HIS   A 1 260 ? -33.823 -22.319 -25.230 1.00 26.10  ? 257 HIS   A N    1 
ATOM   4065 C  CA   . HIS   A 1 260 ? -33.207 -21.079 -24.773 1.00 25.70  ? 257 HIS   A CA   1 
ATOM   4066 C  C    . HIS   A 1 260 ? -31.826 -20.870 -25.392 1.00 26.07  ? 257 HIS   A C    1 
ATOM   4067 O  O    . HIS   A 1 260 ? -31.429 -19.735 -25.652 1.00 25.40  ? 257 HIS   A O    1 
ATOM   4068 C  CB   . HIS   A 1 260 ? -33.061 -21.106 -23.241 1.00 27.83  ? 257 HIS   A CB   1 
ATOM   4069 C  CG   . HIS   A 1 260 ? -32.966 -19.757 -22.622 1.00 28.92  ? 257 HIS   A CG   1 
ATOM   4070 N  ND1  . HIS   A 1 260 ? -33.799 -18.723 -22.974 1.00 29.14  ? 257 HIS   A ND1  1 
ATOM   4071 C  CD2  . HIS   A 1 260 ? -32.107 -19.249 -21.704 1.00 36.59  ? 257 HIS   A CD2  1 
ATOM   4072 C  CE1  . HIS   A 1 260 ? -33.475 -17.635 -22.294 1.00 34.13  ? 257 HIS   A CE1  1 
ATOM   4073 N  NE2  . HIS   A 1 260 ? -32.451 -17.928 -21.513 1.00 40.19  ? 257 HIS   A NE2  1 
ATOM   4074 H  H    . HIS   A 1 260 ? -34.033 -22.872 -24.605 1.00 31.37  ? 257 HIS   A H    1 
ATOM   4075 H  HA   . HIS   A 1 260 ? -33.781 -20.340 -25.031 1.00 30.88  ? 257 HIS   A HA   1 
ATOM   4076 H  HB2  . HIS   A 1 260 ? -33.835 -21.552 -22.862 1.00 33.44  ? 257 HIS   A HB2  1 
ATOM   4077 H  HB3  . HIS   A 1 260 ? -32.254 -21.593 -23.013 1.00 33.44  ? 257 HIS   A HB3  1 
ATOM   4078 H  HD1  . HIS   A 1 260 ? -34.436 -18.774 -23.550 1.00 35.01  ? 257 HIS   A HD1  1 
ATOM   4079 H  HD2  . HIS   A 1 260 ? -31.415 -19.706 -21.283 1.00 43.95  ? 257 HIS   A HD2  1 
ATOM   4080 H  HE1  . HIS   A 1 260 ? -33.895 -16.808 -22.355 1.00 41.00  ? 257 HIS   A HE1  1 
ATOM   4081 N  N    . LEU   A 1 261 ? -31.091 -21.954 -25.633 1.00 25.37  ? 258 LEU   A N    1 
ATOM   4082 C  CA   . LEU   A 1 261 ? -29.770 -21.903 -26.254 1.00 26.14  ? 258 LEU   A CA   1 
ATOM   4083 C  C    . LEU   A 1 261 ? -29.813 -22.342 -27.727 1.00 22.82  ? 258 LEU   A C    1 
ATOM   4084 O  O    . LEU   A 1 261 ? -28.857 -22.936 -28.232 1.00 24.96  ? 258 LEU   A O    1 
ATOM   4085 C  CB   . LEU   A 1 261 ? -28.795 -22.771 -25.456 1.00 27.37  ? 258 LEU   A CB   1 
ATOM   4086 C  CG   . LEU   A 1 261 ? -28.028 -22.129 -24.303 1.00 38.09  ? 258 LEU   A CG   1 
ATOM   4087 C  CD1  . LEU   A 1 261 ? -28.880 -21.247 -23.459 1.00 41.23  ? 258 LEU   A CD1  1 
ATOM   4088 C  CD2  . LEU   A 1 261 ? -27.389 -23.215 -23.453 1.00 42.31  ? 258 LEU   A CD2  1 
ATOM   4089 H  H    . LEU   A 1 261 ? -31.344 -22.753 -25.441 1.00 30.48  ? 258 LEU   A H    1 
ATOM   4090 H  HA   . LEU   A 1 261 ? -29.441 -20.990 -26.235 1.00 31.40  ? 258 LEU   A HA   1 
ATOM   4091 H  HB2  . LEU   A 1 261 ? -29.301 -23.506 -25.077 1.00 32.89  ? 258 LEU   A HB2  1 
ATOM   4092 H  HB3  . LEU   A 1 261 ? -28.130 -23.110 -26.076 1.00 32.89  ? 258 LEU   A HB3  1 
ATOM   4093 H  HG   . LEU   A 1 261 ? -27.340 -21.559 -24.681 1.00 45.75  ? 258 LEU   A HG   1 
ATOM   4094 H  HD11 . LEU   A 1 261 ? -28.339 -20.873 -22.747 1.00 49.52  ? 258 LEU   A HD11 1 
ATOM   4095 H  HD12 . LEU   A 1 261 ? -29.240 -20.535 -24.011 1.00 49.52  ? 258 LEU   A HD12 1 
ATOM   4096 H  HD13 . LEU   A 1 261 ? -29.604 -21.773 -23.084 1.00 49.52  ? 258 LEU   A HD13 1 
ATOM   4097 H  HD21 . LEU   A 1 261 ? -26.975 -22.806 -22.677 1.00 50.82  ? 258 LEU   A HD21 1 
ATOM   4098 H  HD22 . LEU   A 1 261 ? -28.076 -23.840 -23.171 1.00 50.82  ? 258 LEU   A HD22 1 
ATOM   4099 H  HD23 . LEU   A 1 261 ? -26.719 -23.676 -23.981 1.00 50.82  ? 258 LEU   A HD23 1 
ATOM   4100 N  N    . GLY   A 1 262 ? -30.904 -22.014 -28.422 1.00 22.65  ? 259 GLY   A N    1 
ATOM   4101 C  CA   . GLY   A 1 262 ? -31.113 -22.560 -29.752 1.00 25.66  ? 259 GLY   A CA   1 
ATOM   4102 C  C    . GLY   A 1 262 ? -30.082 -22.133 -30.776 1.00 21.18  ? 259 GLY   A C    1 
ATOM   4103 O  O    . GLY   A 1 262 ? -29.822 -22.868 -31.727 1.00 22.45  ? 259 GLY   A O    1 
ATOM   4104 H  H    . GLY   A 1 262 ? -31.526 -21.487 -28.147 1.00 27.22  ? 259 GLY   A H    1 
ATOM   4105 H  HA2  . GLY   A 1 262 ? -31.095 -23.528 -29.699 1.00 30.84  ? 259 GLY   A HA2  1 
ATOM   4106 H  HA3  . GLY   A 1 262 ? -31.984 -22.278 -30.072 1.00 30.84  ? 259 GLY   A HA3  1 
ATOM   4107 N  N    . TYR   A 1 263 ? -29.472 -20.960 -30.587 1.00 23.98  ? 260 TYR   A N    1 
ATOM   4108 C  CA   . TYR   A 1 263 ? -28.451 -20.496 -31.509 1.00 24.28  ? 260 TYR   A CA   1 
ATOM   4109 C  C    . TYR   A 1 263 ? -27.197 -21.357 -31.491 1.00 24.63  ? 260 TYR   A C    1 
ATOM   4110 O  O    . TYR   A 1 263 ? -26.418 -21.328 -32.460 1.00 23.55  ? 260 TYR   A O    1 
ATOM   4111 C  CB   . TYR   A 1 263 ? -28.067 -19.033 -31.196 1.00 23.47  ? 260 TYR   A CB   1 
ATOM   4112 C  CG   . TYR   A 1 263 ? -27.944 -18.743 -29.705 1.00 20.06  ? 260 TYR   A CG   1 
ATOM   4113 C  CD1  . TYR   A 1 263 ? -26.745 -18.949 -29.042 1.00 20.82  ? 260 TYR   A CD1  1 
ATOM   4114 C  CD2  . TYR   A 1 263 ? -29.020 -18.289 -28.981 1.00 23.03  ? 260 TYR   A CD2  1 
ATOM   4115 C  CE1  . TYR   A 1 263 ? -26.633 -18.698 -27.665 1.00 24.60  ? 260 TYR   A CE1  1 
ATOM   4116 C  CE2  . TYR   A 1 263 ? -28.914 -18.055 -27.610 1.00 21.04  ? 260 TYR   A CE2  1 
ATOM   4117 C  CZ   . TYR   A 1 263 ? -27.719 -18.250 -26.969 1.00 25.47  ? 260 TYR   A CZ   1 
ATOM   4118 O  OH   . TYR   A 1 263 ? -27.629 -17.984 -25.608 1.00 27.89  ? 260 TYR   A OH   1 
ATOM   4119 H  H    . TYR   A 1 263 ? -29.634 -20.422 -29.936 1.00 28.81  ? 260 TYR   A H    1 
ATOM   4120 H  HA   . TYR   A 1 263 ? -28.825 -20.532 -32.404 1.00 29.18  ? 260 TYR   A HA   1 
ATOM   4121 H  HB2  . TYR   A 1 263 ? -27.211 -18.839 -31.608 1.00 28.21  ? 260 TYR   A HB2  1 
ATOM   4122 H  HB3  . TYR   A 1 263 ? -28.750 -18.447 -31.557 1.00 28.21  ? 260 TYR   A HB3  1 
ATOM   4123 H  HD1  . TYR   A 1 263 ? -26.005 -19.257 -29.515 1.00 25.03  ? 260 TYR   A HD1  1 
ATOM   4124 H  HD2  . TYR   A 1 263 ? -29.831 -18.137 -29.411 1.00 27.68  ? 260 TYR   A HD2  1 
ATOM   4125 H  HE1  . TYR   A 1 263 ? -25.823 -18.837 -27.229 1.00 29.56  ? 260 TYR   A HE1  1 
ATOM   4126 H  HE2  . TYR   A 1 263 ? -29.656 -17.765 -27.131 1.00 25.28  ? 260 TYR   A HE2  1 
ATOM   4127 H  HH   . TYR   A 1 263 ? -27.810 -18.676 -25.167 1.00 33.51  ? 260 TYR   A HH   1 
ATOM   4128 N  N    . ILE   A 1 264 ? -26.956 -22.143 -30.442 1.00 22.44  ? 261 ILE   A N    1 
ATOM   4129 C  CA   . ILE   A 1 264 ? -25.850 -23.099 -30.469 1.00 23.56  ? 261 ILE   A CA   1 
ATOM   4130 C  C    . ILE   A 1 264 ? -26.320 -24.555 -30.582 1.00 27.22  ? 261 ILE   A C    1 
ATOM   4131 O  O    . ILE   A 1 264 ? -25.582 -25.392 -31.120 1.00 30.74  ? 261 ILE   A O    1 
ATOM   4132 C  CB   . ILE   A 1 264 ? -24.918 -22.903 -29.248 1.00 30.28  ? 261 ILE   A CB   1 
ATOM   4133 C  CG1  . ILE   A 1 264 ? -23.625 -23.693 -29.441 1.00 33.41  ? 261 ILE   A CG1  1 
ATOM   4134 C  CG2  . ILE   A 1 264 ? -25.645 -23.207 -27.932 1.00 31.71  ? 261 ILE   A CG2  1 
ATOM   4135 C  CD1  . ILE   A 1 264 ? -22.467 -23.161 -28.642 1.00 39.98  ? 261 ILE   A CD1  1 
ATOM   4136 H  H    . ILE   A 1 264 ? -27.413 -22.142 -29.713 1.00 26.97  ? 261 ILE   A H    1 
ATOM   4137 H  HA   . ILE   A 1 264 ? -25.316 -22.930 -31.262 1.00 28.32  ? 261 ILE   A HA   1 
ATOM   4138 H  HB   . ILE   A 1 264 ? -24.664 -21.969 -29.188 1.00 36.38  ? 261 ILE   A HB   1 
ATOM   4139 H  HG12 . ILE   A 1 264 ? -23.776 -24.611 -29.169 1.00 40.14  ? 261 ILE   A HG12 1 
ATOM   4140 H  HG13 . ILE   A 1 264 ? -23.377 -23.661 -30.379 1.00 40.14  ? 261 ILE   A HG13 1 
ATOM   4141 H  HG21 . ILE   A 1 264 ? -25.016 -23.127 -27.198 1.00 38.10  ? 261 ILE   A HG21 1 
ATOM   4142 H  HG22 . ILE   A 1 264 ? -26.370 -22.572 -27.818 1.00 38.10  ? 261 ILE   A HG22 1 
ATOM   4143 H  HG23 . ILE   A 1 264 ? -25.999 -24.109 -27.968 1.00 38.10  ? 261 ILE   A HG23 1 
ATOM   4144 H  HD11 . ILE   A 1 264 ? -21.682 -23.700 -28.826 1.00 48.02  ? 261 ILE   A HD11 1 
ATOM   4145 H  HD12 . ILE   A 1 264 ? -22.303 -22.240 -28.898 1.00 48.02  ? 261 ILE   A HD12 1 
ATOM   4146 H  HD13 . ILE   A 1 264 ? -22.687 -23.208 -27.698 1.00 48.02  ? 261 ILE   A HD13 1 
ATOM   4147 N  N    . GLN   A 1 265 ? -27.555 -24.858 -30.180 1.00 27.78  ? 262 GLN   A N    1 
ATOM   4148 C  CA   . GLN   A 1 265 ? -28.116 -26.191 -30.338 1.00 28.95  ? 262 GLN   A CA   1 
ATOM   4149 C  C    . GLN   A 1 265 ? -28.420 -26.507 -31.803 1.00 25.21  ? 262 GLN   A C    1 
ATOM   4150 O  O    . GLN   A 1 265 ? -28.227 -27.632 -32.266 1.00 29.85  ? 262 GLN   A O    1 
ATOM   4151 C  CB   . GLN   A 1 265 ? -29.410 -26.259 -29.521 1.00 27.43  ? 262 GLN   A CB   1 
ATOM   4152 C  CG   . GLN   A 1 265 ? -29.206 -26.285 -28.021 1.00 30.04  ? 262 GLN   A CG   1 
ATOM   4153 C  CD   . GLN   A 1 265 ? -30.394 -25.791 -27.200 1.00 35.47  ? 262 GLN   A CD   1 
ATOM   4154 O  OE1  . GLN   A 1 265 ? -31.367 -25.250 -27.723 1.00 35.79  ? 262 GLN   A OE1  1 
ATOM   4155 N  NE2  . GLN   A 1 265 ? -30.306 -25.986 -25.885 1.00 39.24  ? 262 GLN   A NE2  1 
ATOM   4156 H  H    . GLN   A 1 265 ? -28.094 -24.299 -29.809 1.00 33.38  ? 262 GLN   A H    1 
ATOM   4157 H  HA   . GLN   A 1 265 ? -27.480 -26.850 -30.019 1.00 34.78  ? 262 GLN   A HA   1 
ATOM   4158 H  HB2  . GLN   A 1 265 ? -29.948 -25.480 -29.730 1.00 32.96  ? 262 GLN   A HB2  1 
ATOM   4159 H  HB3  . GLN   A 1 265 ? -29.888 -27.067 -29.766 1.00 32.96  ? 262 GLN   A HB3  1 
ATOM   4160 H  HG2  . GLN   A 1 265 ? -29.026 -27.200 -27.752 1.00 36.09  ? 262 GLN   A HG2  1 
ATOM   4161 H  HG3  . GLN   A 1 265 ? -28.447 -25.721 -27.805 1.00 36.09  ? 262 GLN   A HG3  1 
ATOM   4162 H  HE21 . GLN   A 1 265 ? -29.611 -26.368 -25.552 1.00 47.13  ? 262 GLN   A HE21 1 
ATOM   4163 H  HE22 . GLN   A 1 265 ? -30.944 -25.729 -25.369 1.00 47.13  ? 262 GLN   A HE22 1 
ATOM   4164 N  N    . LYS   A 1 266 ? -28.959 -25.519 -32.523 1.00 24.88  ? 263 LYS   A N    1 
ATOM   4165 C  CA   . LYS   A 1 266 ? -29.452 -25.722 -33.887 1.00 31.16  ? 263 LYS   A CA   1 
ATOM   4166 C  C    . LYS   A 1 266 ? -29.069 -24.531 -34.746 1.00 23.92  ? 263 LYS   A C    1 
ATOM   4167 O  O    . LYS   A 1 266 ? -29.921 -23.793 -35.232 1.00 23.38  ? 263 LYS   A O    1 
ATOM   4168 C  CB   . LYS   A 1 266 ? -30.969 -25.924 -33.884 1.00 27.18  ? 263 LYS   A CB   1 
ATOM   4169 C  CG   . LYS   A 1 266 ? -31.398 -27.103 -33.005 1.00 34.84  ? 263 LYS   A CG   1 
ATOM   4170 C  CD   . LYS   A 1 266 ? -32.874 -27.415 -33.137 1.00 37.07  ? 263 LYS   A CD   1 
ATOM   4171 C  CE   . LYS   A 1 266 ? -33.235 -28.656 -32.295 1.00 47.09  ? 263 LYS   A CE   1 
ATOM   4172 N  NZ   . LYS   A 1 266 ? -34.689 -29.034 -32.369 1.00 43.36  ? 263 LYS   A NZ   1 
ATOM   4173 H  H    . LYS   A 1 266 ? -29.052 -24.713 -32.239 1.00 29.89  ? 263 LYS   A H    1 
ATOM   4174 H  HA   . LYS   A 1 266 ? -29.032 -26.514 -34.258 1.00 37.43  ? 263 LYS   A HA   1 
ATOM   4175 H  HB2  . LYS   A 1 266 ? -31.395 -25.122 -33.544 1.00 32.66  ? 263 LYS   A HB2  1 
ATOM   4176 H  HB3  . LYS   A 1 266 ? -31.267 -26.099 -34.791 1.00 32.66  ? 263 LYS   A HB3  1 
ATOM   4177 H  HG2  . LYS   A 1 266 ? -30.900 -27.893 -33.267 1.00 41.85  ? 263 LYS   A HG2  1 
ATOM   4178 H  HG3  . LYS   A 1 266 ? -31.218 -26.889 -32.076 1.00 41.85  ? 263 LYS   A HG3  1 
ATOM   4179 H  HD2  . LYS   A 1 266 ? -33.396 -26.662 -32.819 1.00 44.52  ? 263 LYS   A HD2  1 
ATOM   4180 H  HD3  . LYS   A 1 266 ? -33.087 -27.597 -34.066 1.00 44.52  ? 263 LYS   A HD3  1 
ATOM   4181 H  HE2  . LYS   A 1 266 ? -32.717 -29.412 -32.614 1.00 56.54  ? 263 LYS   A HE2  1 
ATOM   4182 H  HE3  . LYS   A 1 266 ? -33.023 -28.477 -31.366 1.00 56.54  ? 263 LYS   A HE3  1 
ATOM   4183 H  HZ1  . LYS   A 1 266 ? -35.194 -28.356 -32.090 1.00 52.07  ? 263 LYS   A HZ1  1 
ATOM   4184 H  HZ2  . LYS   A 1 266 ? -34.909 -29.233 -33.208 1.00 52.07  ? 263 LYS   A HZ2  1 
ATOM   4185 H  HZ3  . LYS   A 1 266 ? -34.846 -29.742 -31.853 1.00 52.07  ? 263 LYS   A HZ3  1 
ATOM   4186 N  N    . PRO   A 1 267 ? -27.769 -24.297 -34.933 1.00 25.08  ? 264 PRO   A N    1 
ATOM   4187 C  CA   . PRO   A 1 267 ? -27.361 -23.044 -35.598 1.00 25.33  ? 264 PRO   A CA   1 
ATOM   4188 C  C    . PRO   A 1 267 ? -27.803 -22.946 -37.061 1.00 22.74  ? 264 PRO   A C    1 
ATOM   4189 O  O    . PRO   A 1 267 ? -28.115 -21.837 -37.506 1.00 24.32  ? 264 PRO   A O    1 
ATOM   4190 C  CB   . PRO   A 1 267 ? -25.823 -23.067 -35.469 1.00 29.18  ? 264 PRO   A CB   1 
ATOM   4191 C  CG   . PRO   A 1 267 ? -25.485 -24.482 -35.230 1.00 34.37  ? 264 PRO   A CG   1 
ATOM   4192 C  CD   . PRO   A 1 267 ? -26.617 -25.065 -34.446 1.00 26.63  ? 264 PRO   A CD   1 
ATOM   4193 H  HA   . PRO   A 1 267 ? -27.717 -22.284 -35.113 1.00 30.44  ? 264 PRO   A HA   1 
ATOM   4194 H  HB2  . PRO   A 1 267 ? -25.417 -22.746 -36.289 1.00 35.06  ? 264 PRO   A HB2  1 
ATOM   4195 H  HB3  . PRO   A 1 267 ? -25.545 -22.512 -34.723 1.00 35.06  ? 264 PRO   A HB3  1 
ATOM   4196 H  HG2  . PRO   A 1 267 ? -25.388 -24.939 -36.080 1.00 41.28  ? 264 PRO   A HG2  1 
ATOM   4197 H  HG3  . PRO   A 1 267 ? -24.658 -24.537 -34.727 1.00 41.28  ? 264 PRO   A HG3  1 
ATOM   4198 H  HD2  . PRO   A 1 267 ? -26.722 -26.010 -34.637 1.00 32.00  ? 264 PRO   A HD2  1 
ATOM   4199 H  HD3  . PRO   A 1 267 ? -26.486 -24.931 -33.494 1.00 32.00  ? 264 PRO   A HD3  1 
ATOM   4200 N  N    . GLU   A 1 268 ? -27.861 -24.057 -37.790 1.00 26.29  ? 265 GLU   A N    1 
ATOM   4201 C  CA   . GLU   A 1 268 ? -28.320 -24.005 -39.179 1.00 27.97  ? 265 GLU   A CA   1 
ATOM   4202 C  C    . GLU   A 1 268 ? -29.769 -23.536 -39.235 1.00 26.73  ? 265 GLU   A C    1 
ATOM   4203 O  O    . GLU   A 1 268 ? -30.113 -22.608 -39.973 1.00 25.63  ? 265 GLU   A O    1 
ATOM   4204 C  CB   . GLU   A 1 268 ? -28.160 -25.377 -39.831 1.00 30.08  ? 265 GLU   A CB   1 
ATOM   4205 C  CG   . GLU   A 1 268 ? -26.735 -25.851 -40.046 1.00 45.11  ? 265 GLU   A CG   1 
ATOM   4206 C  CD   . GLU   A 1 268 ? -26.278 -26.850 -38.979 1.00 59.75  ? 265 GLU   A CD   1 
ATOM   4207 O  OE1  . GLU   A 1 268 ? -25.297 -27.593 -39.227 1.00 49.66  ? 265 GLU   A OE1  1 
ATOM   4208 O  OE2  . GLU   A 1 268 ? -26.887 -26.857 -37.876 1.00 42.45  ? 265 GLU   A OE2  1 
ATOM   4209 H  H    . GLU   A 1 268 ? -27.644 -24.842 -37.512 1.00 31.59  ? 265 GLU   A H    1 
ATOM   4210 H  HA   . GLU   A 1 268 ? -27.775 -23.378 -39.681 1.00 33.61  ? 265 GLU   A HA   1 
ATOM   4211 H  HB2  . GLU   A 1 268 ? -28.598 -26.033 -39.266 1.00 36.13  ? 265 GLU   A HB2  1 
ATOM   4212 H  HB3  . GLU   A 1 268 ? -28.588 -25.350 -40.701 1.00 36.13  ? 265 GLU   A HB3  1 
ATOM   4213 H  HG2  . GLU   A 1 268 ? -26.673 -26.286 -40.910 1.00 54.17  ? 265 GLU   A HG2  1 
ATOM   4214 H  HG3  . GLU   A 1 268 ? -26.139 -25.086 -40.016 1.00 54.17  ? 265 GLU   A HG3  1 
ATOM   4215 N  N    . GLY   A 1 269 ? -30.635 -24.154 -38.435 1.00 25.01  ? 266 GLY   A N    1 
ATOM   4216 C  CA   . GLY   A 1 269 ? -32.042 -23.757 -38.436 1.00 25.50  ? 266 GLY   A CA   1 
ATOM   4217 C  C    . GLY   A 1 269 ? -32.298 -22.375 -37.855 1.00 22.74  ? 266 GLY   A C    1 
ATOM   4218 O  O    . GLY   A 1 269 ? -33.205 -21.655 -38.281 1.00 22.45  ? 266 GLY   A O    1 
ATOM   4219 H  H    . GLY   A 1 269 ? -30.439 -24.793 -37.894 1.00 30.06  ? 266 GLY   A H    1 
ATOM   4220 H  HA2  . GLY   A 1 269 ? -32.370 -23.761 -39.349 1.00 30.64  ? 266 GLY   A HA2  1 
ATOM   4221 H  HA3  . GLY   A 1 269 ? -32.550 -24.398 -37.915 1.00 30.64  ? 266 GLY   A HA3  1 
ATOM   4222 N  N    . PHE   A 1 270 ? -31.528 -22.002 -36.828 1.00 21.31  ? 267 PHE   A N    1 
ATOM   4223 C  CA   . PHE   A 1 270 ? -31.606 -20.668 -36.272 1.00 21.70  ? 267 PHE   A CA   1 
ATOM   4224 C  C    . PHE   A 1 270 ? -31.233 -19.631 -37.322 1.00 18.66  ? 267 PHE   A C    1 
ATOM   4225 O  O    . PHE   A 1 270 ? -31.949 -18.625 -37.485 1.00 18.94  ? 267 PHE   A O    1 
ATOM   4226 C  CB   . PHE   A 1 270 ? -30.705 -20.589 -35.029 1.00 20.59  ? 267 PHE   A CB   1 
ATOM   4227 C  CG   . PHE   A 1 270 ? -31.050 -19.493 -34.053 1.00 17.56  ? 267 PHE   A CG   1 
ATOM   4228 C  CD1  . PHE   A 1 270 ? -30.588 -18.191 -34.228 1.00 18.39  ? 267 PHE   A CD1  1 
ATOM   4229 C  CD2  . PHE   A 1 270 ? -31.789 -19.764 -32.894 1.00 19.00  ? 267 PHE   A CD2  1 
ATOM   4230 C  CE1  . PHE   A 1 270 ? -30.830 -17.193 -33.300 1.00 18.36  ? 267 PHE   A CE1  1 
ATOM   4231 C  CE2  . PHE   A 1 270 ? -32.040 -18.764 -31.957 1.00 18.29  ? 267 PHE   A CE2  1 
ATOM   4232 C  CZ   . PHE   A 1 270 ? -31.603 -17.464 -32.158 1.00 20.26  ? 267 PHE   A CZ   1 
ATOM   4233 H  H    . PHE   A 1 270 ? -30.953 -22.510 -36.441 1.00 25.62  ? 267 PHE   A H    1 
ATOM   4234 H  HA   . PHE   A 1 270 ? -32.512 -20.472 -35.986 1.00 26.09  ? 267 PHE   A HA   1 
ATOM   4235 H  HB2  . PHE   A 1 270 ? -30.767 -21.432 -34.552 1.00 24.75  ? 267 PHE   A HB2  1 
ATOM   4236 H  HB3  . PHE   A 1 270 ? -29.792 -20.440 -35.322 1.00 24.75  ? 267 PHE   A HB3  1 
ATOM   4237 H  HD1  . PHE   A 1 270 ? -30.101 -17.986 -34.993 1.00 22.11  ? 267 PHE   A HD1  1 
ATOM   4238 H  HD2  . PHE   A 1 270 ? -32.115 -20.622 -32.749 1.00 22.84  ? 267 PHE   A HD2  1 
ATOM   4239 H  HE1  . PHE   A 1 270 ? -30.480 -16.341 -33.433 1.00 22.08  ? 267 PHE   A HE1  1 
ATOM   4240 H  HE2  . PHE   A 1 270 ? -32.511 -18.973 -31.182 1.00 21.99  ? 267 PHE   A HE2  1 
ATOM   4241 H  HZ   . PHE   A 1 270 ? -31.815 -16.789 -31.553 1.00 24.36  ? 267 PHE   A HZ   1 
ATOM   4242 N  N    . ALA   A 1 271 ? -30.114 -19.873 -38.036 1.00 20.40  ? 268 ALA   A N    1 
ATOM   4243 C  CA   . ALA   A 1 271 ? -29.700 -18.963 -39.109 1.00 22.31  ? 268 ALA   A CA   1 
ATOM   4244 C  C    . ALA   A 1 271 ? -30.780 -18.856 -40.184 1.00 21.99  ? 268 ALA   A C    1 
ATOM   4245 O  O    . ALA   A 1 271 ? -31.053 -17.764 -40.703 1.00 22.51  ? 268 ALA   A O    1 
ATOM   4246 C  CB   . ALA   A 1 271 ? -28.401 -19.427 -39.730 1.00 23.48  ? 268 ALA   A CB   1 
ATOM   4247 H  H    . ALA   A 1 271 ? -29.590 -20.545 -37.917 1.00 24.52  ? 268 ALA   A H    1 
ATOM   4248 H  HA   . ALA   A 1 271 ? -29.554 -18.086 -38.723 1.00 26.81  ? 268 ALA   A HA   1 
ATOM   4249 H  HB1  . ALA   A 1 271 ? -28.147 -18.807 -40.431 1.00 28.21  ? 268 ALA   A HB1  1 
ATOM   4250 H  HB2  . ALA   A 1 271 ? -27.715 -19.452 -39.046 1.00 28.21  ? 268 ALA   A HB2  1 
ATOM   4251 H  HB3  . ALA   A 1 271 ? -28.528 -20.314 -40.103 1.00 28.21  ? 268 ALA   A HB3  1 
ATOM   4252 N  N    . ASP   A 1 272 ? -31.381 -19.982 -40.547 1.00 22.78  ? 269 ASP   A N    1 
ATOM   4253 C  CA   . ASP   A 1 272 ? -32.363 -19.974 -41.631 1.00 24.34  ? 269 ASP   A CA   1 
ATOM   4254 C  C    . ASP   A 1 272 ? -33.486 -18.993 -41.331 1.00 22.38  ? 269 ASP   A C    1 
ATOM   4255 O  O    . ASP   A 1 272 ? -33.935 -18.252 -42.221 1.00 22.63  ? 269 ASP   A O    1 
ATOM   4256 C  CB   . ASP   A 1 272 ? -32.911 -21.378 -41.857 1.00 26.06  ? 269 ASP   A CB   1 
ATOM   4257 C  CG   . ASP   A 1 272 ? -31.919 -22.280 -42.588 1.00 36.73  ? 269 ASP   A CG   1 
ATOM   4258 O  OD1  . ASP   A 1 272 ? -30.995 -21.747 -43.250 1.00 38.12  ? 269 ASP   A OD1  1 
ATOM   4259 O  OD2  . ASP   A 1 272 ? -32.089 -23.519 -42.562 1.00 42.01  ? 269 ASP   A OD2  1 
ATOM   4260 H  H    . ASP   A 1 272 ? -31.244 -20.752 -40.190 1.00 27.38  ? 269 ASP   A H    1 
ATOM   4261 H  HA   . ASP   A 1 272 ? -31.929 -19.697 -42.453 1.00 29.25  ? 269 ASP   A HA   1 
ATOM   4262 H  HB2  . ASP   A 1 272 ? -33.110 -21.783 -40.998 1.00 31.31  ? 269 ASP   A HB2  1 
ATOM   4263 H  HB3  . ASP   A 1 272 ? -33.718 -21.322 -42.392 1.00 31.31  ? 269 ASP   A HB3  1 
ATOM   4264 N  N    . VAL   A 1 273 ? -33.963 -18.970 -40.080 1.00 20.05  ? 270 VAL   A N    1 
ATOM   4265 C  CA   . VAL   A 1 273 ? -35.016 -18.040 -39.688 1.00 18.54  ? 270 VAL   A CA   1 
ATOM   4266 C  C    . VAL   A 1 273 ? -34.512 -16.611 -39.687 1.00 19.52  ? 270 VAL   A C    1 
ATOM   4267 O  O    . VAL   A 1 273 ? -35.214 -15.702 -40.151 1.00 19.34  ? 270 VAL   A O    1 
ATOM   4268 C  CB   . VAL   A 1 273 ? -35.629 -18.449 -38.333 1.00 20.15  ? 270 VAL   A CB   1 
ATOM   4269 C  CG1  . VAL   A 1 273 ? -36.586 -17.422 -37.830 1.00 20.69  ? 270 VAL   A CG1  1 
ATOM   4270 C  CG2  . VAL   A 1 273 ? -36.271 -19.792 -38.475 1.00 22.65  ? 270 VAL   A CG2  1 
ATOM   4271 H  H    . VAL   A 1 273 ? -33.693 -19.483 -39.445 1.00 24.11  ? 270 VAL   A H    1 
ATOM   4272 H  HA   . VAL   A 1 273 ? -35.721 -18.091 -40.352 1.00 22.29  ? 270 VAL   A HA   1 
ATOM   4273 H  HB   . VAL   A 1 273 ? -34.930 -18.509 -37.663 1.00 24.23  ? 270 VAL   A HB   1 
ATOM   4274 H  HG11 . VAL   A 1 273 ? -37.070 -17.785 -37.072 1.00 24.87  ? 270 VAL   A HG11 1 
ATOM   4275 H  HG12 . VAL   A 1 273 ? -36.090 -16.634 -37.559 1.00 24.87  ? 270 VAL   A HG12 1 
ATOM   4276 H  HG13 . VAL   A 1 273 ? -37.207 -17.195 -38.540 1.00 24.87  ? 270 VAL   A HG13 1 
ATOM   4277 H  HG21 . VAL   A 1 273 ? -36.747 -20.003 -37.656 1.00 27.23  ? 270 VAL   A HG21 1 
ATOM   4278 H  HG22 . VAL   A 1 273 ? -36.891 -19.769 -39.221 1.00 27.23  ? 270 VAL   A HG22 1 
ATOM   4279 H  HG23 . VAL   A 1 273 ? -35.582 -20.456 -38.638 1.00 27.23  ? 270 VAL   A HG23 1 
ATOM   4280 N  N    . LEU   A 1 274 ? -33.316 -16.362 -39.114 1.00 17.97  ? 271 LEU   A N    1 
ATOM   4281 C  CA   . LEU   A 1 274 ? -32.792 -15.002 -39.130 1.00 18.05  ? 271 LEU   A CA   1 
ATOM   4282 C  C    . LEU   A 1 274 ? -32.639 -14.482 -40.558 1.00 18.47  ? 271 LEU   A C    1 
ATOM   4283 O  O    . LEU   A 1 274 ? -32.877 -13.291 -40.806 1.00 20.53  ? 271 LEU   A O    1 
ATOM   4284 C  CB   . LEU   A 1 274 ? -31.454 -14.935 -38.409 1.00 20.53  ? 271 LEU   A CB   1 
ATOM   4285 C  CG   . LEU   A 1 274 ? -31.509 -15.191 -36.908 1.00 20.28  ? 271 LEU   A CG   1 
ATOM   4286 C  CD1  . LEU   A 1 274 ? -30.095 -15.034 -36.369 1.00 21.12  ? 271 LEU   A CD1  1 
ATOM   4287 C  CD2  . LEU   A 1 274 ? -32.473 -14.262 -36.172 1.00 20.16  ? 271 LEU   A CD2  1 
ATOM   4288 H  H    . LEU   A 1 274 ? -32.817 -16.945 -38.728 1.00 21.61  ? 271 LEU   A H    1 
ATOM   4289 H  HA   . LEU   A 1 274 ? -33.418 -14.432 -38.658 1.00 21.71  ? 271 LEU   A HA   1 
ATOM   4290 H  HB2  . LEU   A 1 274 ? -30.865 -15.602 -38.796 1.00 24.68  ? 271 LEU   A HB2  1 
ATOM   4291 H  HB3  . LEU   A 1 274 ? -31.082 -14.048 -38.539 1.00 24.68  ? 271 LEU   A HB3  1 
ATOM   4292 H  HG   . LEU   A 1 274 ? -31.848 -16.085 -36.746 1.00 24.38  ? 271 LEU   A HG   1 
ATOM   4293 H  HD11 . LEU   A 1 274 ? -30.100 -15.204 -35.414 1.00 25.38  ? 271 LEU   A HD11 1 
ATOM   4294 H  HD12 . LEU   A 1 274 ? -29.515 -15.671 -36.815 1.00 25.38  ? 271 LEU   A HD12 1 
ATOM   4295 H  HD13 . LEU   A 1 274 ? -29.789 -14.130 -36.542 1.00 25.38  ? 271 LEU   A HD13 1 
ATOM   4296 H  HD21 . LEU   A 1 274 ? -32.385 -14.406 -35.217 1.00 24.23  ? 271 LEU   A HD21 1 
ATOM   4297 H  HD22 . LEU   A 1 274 ? -32.254 -13.342 -36.389 1.00 24.23  ? 271 LEU   A HD22 1 
ATOM   4298 H  HD23 . LEU   A 1 274 ? -33.380 -14.461 -36.454 1.00 24.23  ? 271 LEU   A HD23 1 
ATOM   4299 N  N    . LEU   A 1 275 ? -32.232 -15.340 -41.504 1.00 20.19  ? 272 LEU   A N    1 
ATOM   4300 C  CA   . LEU   A 1 275 ? -32.083 -14.901 -42.890 1.00 20.10  ? 272 LEU   A CA   1 
ATOM   4301 C  C    . LEU   A 1 275 ? -33.454 -14.604 -43.509 1.00 22.08  ? 272 LEU   A C    1 
ATOM   4302 O  O    . LEU   A 1 275 ? -33.604 -13.656 -44.294 1.00 26.54  ? 272 LEU   A O    1 
ATOM   4303 C  CB   . LEU   A 1 275 ? -31.328 -15.956 -43.682 1.00 21.39  ? 272 LEU   A CB   1 
ATOM   4304 C  CG   . LEU   A 1 275 ? -29.850 -16.071 -43.337 1.00 26.95  ? 272 LEU   A CG   1 
ATOM   4305 C  CD1  . LEU   A 1 275 ? -29.230 -17.276 -43.958 1.00 30.98  ? 272 LEU   A CD1  1 
ATOM   4306 C  CD2  . LEU   A 1 275 ? -29.101 -14.813 -43.785 1.00 27.68  ? 272 LEU   A CD2  1 
ATOM   4307 H  H    . LEU   A 1 275 ? -32.040 -16.167 -41.369 1.00 24.27  ? 272 LEU   A H    1 
ATOM   4308 H  HA   . LEU   A 1 275 ? -31.561 -14.085 -42.925 1.00 24.16  ? 272 LEU   A HA   1 
ATOM   4309 H  HB2  . LEU   A 1 275 ? -31.736 -16.819 -43.513 1.00 25.71  ? 272 LEU   A HB2  1 
ATOM   4310 H  HB3  . LEU   A 1 275 ? -31.392 -15.738 -44.625 1.00 25.71  ? 272 LEU   A HB3  1 
ATOM   4311 H  HG   . LEU   A 1 275 ? -29.772 -16.163 -42.374 1.00 32.39  ? 272 LEU   A HG   1 
ATOM   4312 H  HD11 . LEU   A 1 275 ? -28.297 -17.321 -43.697 1.00 37.22  ? 272 LEU   A HD11 1 
ATOM   4313 H  HD12 . LEU   A 1 275 ? -29.698 -18.067 -43.648 1.00 37.22  ? 272 LEU   A HD12 1 
ATOM   4314 H  HD13 . LEU   A 1 275 ? -29.301 -17.206 -44.923 1.00 37.22  ? 272 LEU   A HD13 1 
ATOM   4315 H  HD21 . LEU   A 1 275 ? -28.155 -15.015 -43.850 1.00 33.26  ? 272 LEU   A HD21 1 
ATOM   4316 H  HD22 . LEU   A 1 275 ? -29.441 -14.534 -44.649 1.00 33.26  ? 272 LEU   A HD22 1 
ATOM   4317 H  HD23 . LEU   A 1 275 ? -29.245 -14.110 -43.131 1.00 33.26  ? 272 LEU   A HD23 1 
ATOM   4318 N  N    . ASN   A 1 276 ? -34.458 -15.404 -43.183 1.00 19.98  ? 273 ASN   A N    1 
ATOM   4319 C  CA   . ASN   A 1 276 ? -35.816 -15.085 -43.635 1.00 22.85  ? 273 ASN   A CA   1 
ATOM   4320 C  C    . ASN   A 1 276 ? -36.282 -13.734 -43.087 1.00 23.53  ? 273 ASN   A C    1 
ATOM   4321 O  O    . ASN   A 1 276 ? -37.032 -13.008 -43.768 1.00 26.52  ? 273 ASN   A O    1 
ATOM   4322 C  CB   . ASN   A 1 276 ? -36.762 -16.191 -43.192 1.00 21.07  ? 273 ASN   A CB   1 
ATOM   4323 C  CG   . ASN   A 1 276 ? -36.582 -17.442 -43.984 1.00 22.71  ? 273 ASN   A CG   1 
ATOM   4324 O  OD1  . ASN   A 1 276 ? -35.903 -17.465 -45.023 1.00 22.07  ? 273 ASN   A OD1  1 
ATOM   4325 N  ND2  . ASN   A 1 276 ? -37.146 -18.534 -43.479 1.00 28.63  ? 273 ASN   A ND2  1 
ATOM   4326 H  H    . ASN   A 1 276 ? -34.390 -16.121 -42.713 1.00 24.02  ? 273 ASN   A H    1 
ATOM   4327 H  HA   . ASN   A 1 276 ? -35.833 -15.035 -44.604 1.00 27.46  ? 273 ASN   A HA   1 
ATOM   4328 H  HB2  . ASN   A 1 276 ? -36.594 -16.398 -42.259 1.00 25.33  ? 273 ASN   A HB2  1 
ATOM   4329 H  HB3  . ASN   A 1 276 ? -37.677 -15.891 -43.305 1.00 25.33  ? 273 ASN   A HB3  1 
ATOM   4330 H  HD21 . ASN   A 1 276 ? -37.075 -19.285 -43.892 1.00 34.39  ? 273 ASN   A HD21 1 
ATOM   4331 H  HD22 . ASN   A 1 276 ? -37.580 -18.490 -42.738 1.00 34.39  ? 273 ASN   A HD22 1 
ATOM   4332 N  N    . MET   A 1 277 ? -35.882 -13.396 -41.858 1.00 21.25  ? 274 MET   A N    1 
ATOM   4333 C  CA   . MET   A 1 277 ? -36.285 -12.129 -41.260 1.00 19.67  ? 274 MET   A CA   1 
ATOM   4334 C  C    . MET   A 1 277 ? -35.572 -10.945 -41.875 1.00 22.93  ? 274 MET   A C    1 
ATOM   4335 O  O    . MET   A 1 277 ? -36.191 -9.917  -42.173 1.00 23.97  ? 274 MET   A O    1 
ATOM   4336 C  CB   . MET   A 1 277 ? -36.064 -12.076 -39.743 1.00 22.12  ? 274 MET   A CB   1 
ATOM   4337 C  CG   . MET   A 1 277 ? -36.858 -13.032 -38.919 1.00 18.96  ? 274 MET   A CG   1 
ATOM   4338 S  SD   . MET   A 1 277 ? -36.173 -13.387 -37.266 1.00 21.48  ? 274 MET   A SD   1 
ATOM   4339 C  CE   . MET   A 1 277 ? -35.594 -11.791 -36.673 1.00 21.52  ? 274 MET   A CE   1 
ATOM   4340 H  H    . MET   A 1 277 ? -35.380 -13.882 -41.356 1.00 25.54  ? 274 MET   A H    1 
ATOM   4341 H  HA   . MET   A 1 277 ? -37.240 -12.081 -41.425 1.00 23.64  ? 274 MET   A HA   1 
ATOM   4342 H  HB2  . MET   A 1 277 ? -35.128 -12.261 -39.569 1.00 26.58  ? 274 MET   A HB2  1 
ATOM   4343 H  HB3  . MET   A 1 277 ? -36.289 -11.184 -39.437 1.00 26.58  ? 274 MET   A HB3  1 
ATOM   4344 H  HG2  . MET   A 1 277 ? -37.746 -12.662 -38.792 1.00 22.80  ? 274 MET   A HG2  1 
ATOM   4345 H  HG3  . MET   A 1 277 ? -36.915 -13.874 -39.397 1.00 22.80  ? 274 MET   A HG3  1 
ATOM   4346 H  HE1  . MET   A 1 277 ? -35.214 -11.901 -35.788 1.00 25.87  ? 274 MET   A HE1  1 
ATOM   4347 H  HE2  . MET   A 1 277 ? -34.919 -11.453 -37.283 1.00 25.87  ? 274 MET   A HE2  1 
ATOM   4348 H  HE3  . MET   A 1 277 ? -36.344 -11.176 -36.637 1.00 25.87  ? 274 MET   A HE3  1 
ATOM   4349 N  N    . TRP   A 1 278 ? -34.259 -11.044 -42.008 1.00 21.55  ? 275 TRP   A N    1 
ATOM   4350 C  CA   . TRP   A 1 278 ? -33.389 -9.890  -42.196 1.00 22.27  ? 275 TRP   A CA   1 
ATOM   4351 C  C    . TRP   A 1 278 ? -32.482 -10.011 -43.406 1.00 24.93  ? 275 TRP   A C    1 
ATOM   4352 O  O    . TRP   A 1 278 ? -31.830 -9.030  -43.788 1.00 27.69  ? 275 TRP   A O    1 
ATOM   4353 C  CB   . TRP   A 1 278 ? -32.510 -9.730  -40.957 1.00 21.72  ? 275 TRP   A CB   1 
ATOM   4354 C  CG   . TRP   A 1 278 ? -33.201 -9.241  -39.712 1.00 19.72  ? 275 TRP   A CG   1 
ATOM   4355 C  CD1  . TRP   A 1 278 ? -34.440 -8.714  -39.601 1.00 20.28  ? 275 TRP   A CD1  1 
ATOM   4356 C  CD2  . TRP   A 1 278 ? -32.676 -9.308  -38.386 1.00 19.56  ? 275 TRP   A CD2  1 
ATOM   4357 N  NE1  . TRP   A 1 278 ? -34.721 -8.414  -38.288 1.00 22.23  ? 275 TRP   A NE1  1 
ATOM   4358 C  CE2  . TRP   A 1 278 ? -33.644 -8.776  -37.526 1.00 19.11  ? 275 TRP   A CE2  1 
ATOM   4359 C  CE3  . TRP   A 1 278 ? -31.472 -9.768  -37.851 1.00 22.73  ? 275 TRP   A CE3  1 
ATOM   4360 C  CZ2  . TRP   A 1 278 ? -33.441 -8.665  -36.129 1.00 20.99  ? 275 TRP   A CZ2  1 
ATOM   4361 C  CZ3  . TRP   A 1 278 ? -31.276 -9.660  -36.497 1.00 20.93  ? 275 TRP   A CZ3  1 
ATOM   4362 C  CH2  . TRP   A 1 278 ? -32.255 -9.106  -35.653 1.00 21.16  ? 275 TRP   A CH2  1 
ATOM   4363 H  H    . TRP   A 1 278 ? -33.832 -11.791 -41.992 1.00 25.90  ? 275 TRP   A H    1 
ATOM   4364 H  HA   . TRP   A 1 278 ? -33.928 -9.091  -42.310 1.00 26.77  ? 275 TRP   A HA   1 
ATOM   4365 H  HB2  . TRP   A 1 278 ? -32.123 -10.594 -40.747 1.00 26.10  ? 275 TRP   A HB2  1 
ATOM   4366 H  HB3  . TRP   A 1 278 ? -31.809 -9.093  -41.163 1.00 26.10  ? 275 TRP   A HB3  1 
ATOM   4367 H  HD1  . TRP   A 1 278 ? -35.023 -8.575  -40.313 1.00 24.38  ? 275 TRP   A HD1  1 
ATOM   4368 H  HE1  . TRP   A 1 278 ? -35.448 -8.060  -37.996 1.00 26.71  ? 275 TRP   A HE1  1 
ATOM   4369 H  HE3  . TRP   A 1 278 ? -30.819 -10.138 -38.398 1.00 27.32  ? 275 TRP   A HE3  1 
ATOM   4370 H  HZ2  . TRP   A 1 278 ? -34.091 -8.307  -35.568 1.00 25.23  ? 275 TRP   A HZ2  1 
ATOM   4371 H  HZ3  . TRP   A 1 278 ? -30.476 -9.960  -36.129 1.00 25.16  ? 275 TRP   A HZ3  1 
ATOM   4372 H  HH2  . TRP   A 1 278 ? -32.081 -9.042  -34.742 1.00 25.43  ? 275 TRP   A HH2  1 
ATOM   4373 N  N    . GLY   A 1 279 ? -32.373 -11.185 -43.999 1.00 24.64  ? 276 GLY   A N    1 
ATOM   4374 C  CA   . GLY   A 1 279 ? -31.463 -11.412 -45.119 1.00 27.32  ? 276 GLY   A CA   1 
ATOM   4375 C  C    . GLY   A 1 279 ? -32.053 -11.032 -46.450 1.00 34.20  ? 276 GLY   A C    1 
ATOM   4376 O  O    . GLY   A 1 279 ? -31.369 -11.047 -47.482 1.00 37.04  ? 276 GLY   A O    1 
ATOM   4377 O  OXT  . GLY   A 1 279 ? -33.236 -10.712 -46.521 1.00 33.80  ? 276 GLY   A OXT  1 
ATOM   4378 H  H    . GLY   A 1 279 ? -32.821 -11.883 -43.771 1.00 29.61  ? 276 GLY   A H    1 
ATOM   4379 H  HA2  . GLY   A 1 279 ? -30.657 -10.889 -44.985 1.00 32.83  ? 276 GLY   A HA2  1 
ATOM   4380 H  HA3  . GLY   A 1 279 ? -31.226 -12.353 -45.151 1.00 32.83  ? 276 GLY   A HA3  1 
ATOM   4381 N  N    . GLY   B 1 3   ? -7.605  -14.444 -31.593 1.00 65.15  ? 0   GLY   B N    1 
ATOM   4382 C  CA   . GLY   B 1 3   ? -7.515  -13.146 -32.326 1.00 58.55  ? 0   GLY   B CA   1 
ATOM   4383 C  C    . GLY   B 1 3   ? -8.831  -12.395 -32.336 1.00 44.66  ? 0   GLY   B C    1 
ATOM   4384 O  O    . GLY   B 1 3   ? -9.538  -12.353 -33.344 1.00 53.70  ? 0   GLY   B O    1 
ATOM   4385 H  H    . GLY   B 1 3   ? -6.817  -14.857 -31.623 1.00 78.22  ? 0   GLY   B H    1 
ATOM   4386 H  HA2  . GLY   B 1 3   ? -6.846  -12.585 -31.904 1.00 70.30  ? 0   GLY   B HA2  1 
ATOM   4387 H  HA3  . GLY   B 1 3   ? -7.252  -13.315 -33.244 1.00 70.30  ? 0   GLY   B HA3  1 
ATOM   4388 N  N    . MET   B 1 4   ? -9.165  -11.809 -31.194 1.00 36.96  ? 1   MET   B N    1 
ATOM   4389 C  CA   . MET   B 1 4   ? -10.365 -11.006 -31.039 1.00 28.44  ? 1   MET   B CA   1 
ATOM   4390 C  C    . MET   B 1 4   ? -10.036 -9.544  -31.339 1.00 29.95  ? 1   MET   B C    1 
ATOM   4391 O  O    . MET   B 1 4   ? -8.872  -9.113  -31.282 1.00 32.48  ? 1   MET   B O    1 
ATOM   4392 C  CB   . MET   B 1 4   ? -10.895 -11.175 -29.610 1.00 29.55  ? 1   MET   B CB   1 
ATOM   4393 C  CG   . MET   B 1 4   ? -11.606 -12.510 -29.430 1.00 28.21  ? 1   MET   B CG   1 
ATOM   4394 S  SD   . MET   B 1 4   ? -12.312 -12.740 -27.802 1.00 31.21  ? 1   MET   B SD   1 
ATOM   4395 C  CE   . MET   B 1 4   ? -13.885 -11.920 -28.068 1.00 30.30  ? 1   MET   B CE   1 
ATOM   4396 H  H    . MET   B 1 4   ? -8.697  -11.864 -30.474 1.00 44.39  ? 1   MET   B H    1 
ATOM   4397 H  HA   . MET   B 1 4   ? -11.064 -11.292 -31.648 1.00 34.17  ? 1   MET   B HA   1 
ATOM   4398 H  HB2  . MET   B 1 4   ? -10.153 -11.139 -28.987 1.00 35.50  ? 1   MET   B HB2  1 
ATOM   4399 H  HB3  . MET   B 1 4   ? -11.527 -10.465 -29.416 1.00 35.50  ? 1   MET   B HB3  1 
ATOM   4400 H  HG2  . MET   B 1 4   ? -12.328 -12.569 -30.076 1.00 33.90  ? 1   MET   B HG2  1 
ATOM   4401 H  HG3  . MET   B 1 4   ? -10.969 -13.226 -29.580 1.00 33.90  ? 1   MET   B HG3  1 
ATOM   4402 H  HE1  . MET   B 1 4   ? -14.412 -11.977 -27.255 1.00 36.41  ? 1   MET   B HE1  1 
ATOM   4403 H  HE2  . MET   B 1 4   ? -13.722 -10.990 -28.292 1.00 36.41  ? 1   MET   B HE2  1 
ATOM   4404 H  HE3  . MET   B 1 4   ? -14.351 -12.359 -28.796 1.00 36.41  ? 1   MET   B HE3  1 
ATOM   4405 N  N    . GLU   B 1 5   ? -11.057 -8.802  -31.723 1.00 26.41  ? 2   GLU   B N    1 
ATOM   4406 C  CA   . GLU   B 1 5   ? -10.936 -7.364  -31.922 1.00 27.86  ? 2   GLU   B CA   1 
ATOM   4407 C  C    . GLU   B 1 5   ? -11.152 -6.641  -30.598 1.00 27.36  ? 2   GLU   B C    1 
ATOM   4408 O  O    . GLU   B 1 5   ? -11.720 -7.194  -29.666 1.00 26.10  ? 2   GLU   B O    1 
ATOM   4409 C  CB   . GLU   B 1 5   ? -11.960 -6.849  -32.934 1.00 28.23  ? 2   GLU   B CB   1 
ATOM   4410 C  CG   . GLU   B 1 5   ? -11.933 -7.577  -34.270 1.00 33.31  ? 2   GLU   B CG   1 
ATOM   4411 C  CD   . GLU   B 1 5   ? -10.783 -7.077  -35.105 1.00 40.22  ? 2   GLU   B CD   1 
ATOM   4412 O  OE1  . GLU   B 1 5   ? -10.744 -5.857  -35.398 1.00 44.19  ? 2   GLU   B OE1  1 
ATOM   4413 O  OE2  . GLU   B 1 5   ? -9.896  -7.889  -35.423 1.00 53.82  ? 2   GLU   B OE2  1 
ATOM   4414 H  H    . GLU   B 1 5   ? -11.845 -9.110  -31.879 1.00 31.73  ? 2   GLU   B H    1 
ATOM   4415 H  HA   . GLU   B 1 5   ? -10.050 -7.171  -32.264 1.00 33.48  ? 2   GLU   B HA   1 
ATOM   4416 H  HB2  . GLU   B 1 5   ? -12.848 -6.956  -32.559 1.00 33.91  ? 2   GLU   B HB2  1 
ATOM   4417 H  HB3  . GLU   B 1 5   ? -11.783 -5.911  -33.106 1.00 33.91  ? 2   GLU   B HB3  1 
ATOM   4418 H  HG2  . GLU   B 1 5   ? -11.820 -8.529  -34.122 1.00 40.01  ? 2   GLU   B HG2  1 
ATOM   4419 H  HG3  . GLU   B 1 5   ? -12.760 -7.412  -34.749 1.00 40.01  ? 2   GLU   B HG3  1 
ATOM   4420 N  N    . THR   B 1 6   ? -10.674 -5.395  -30.525 1.00 28.05  ? 3   THR   B N    1 
ATOM   4421 C  CA   . THR   B 1 6   ? -10.799 -4.585  -29.314 1.00 25.06  ? 3   THR   B CA   1 
ATOM   4422 C  C    . THR   B 1 6   ? -11.325 -3.194  -29.637 1.00 30.76  ? 3   THR   B C    1 
ATOM   4423 O  O    . THR   B 1 6   ? -10.820 -2.524  -30.543 1.00 30.79  ? 3   THR   B O    1 
ATOM   4424 C  CB   . THR   B 1 6   ? -9.453  -4.445  -28.609 1.00 30.24  ? 3   THR   B CB   1 
ATOM   4425 O  OG1  . THR   B 1 6   ? -8.964  -5.739  -28.210 1.00 30.41  ? 3   THR   B OG1  1 
ATOM   4426 C  CG2  . THR   B 1 6   ? -9.530  -3.483  -27.376 1.00 30.14  ? 3   THR   B CG2  1 
ATOM   4427 H  H    . THR   B 1 6   ? -10.270 -4.996  -31.171 1.00 33.70  ? 3   THR   B H    1 
ATOM   4428 H  HA   . THR   B 1 6   ? -11.441 -5.020  -28.731 1.00 30.12  ? 3   THR   B HA   1 
ATOM   4429 H  HB   . THR   B 1 6   ? -8.821  -4.051  -29.231 1.00 36.33  ? 3   THR   B HB   1 
ATOM   4430 H  HG1  . THR   B 1 6   ? -8.141  -5.697  -28.047 1.00 36.53  ? 3   THR   B HG1  1 
ATOM   4431 H  HG21 . THR   B 1 6   ? -8.767  -3.626  -26.795 1.00 36.21  ? 3   THR   B HG21 1 
ATOM   4432 H  HG22 . THR   B 1 6   ? -9.530  -2.560  -27.674 1.00 36.21  ? 3   THR   B HG22 1 
ATOM   4433 H  HG23 . THR   B 1 6   ? -10.343 -3.651  -26.874 1.00 36.21  ? 3   THR   B HG23 1 
ATOM   4434 N  N    . LEU   B 1 7   ? -12.305 -2.741  -28.863 1.00 27.50  ? 4   LEU   B N    1 
ATOM   4435 C  CA   . LEU   B 1 7   ? -12.700 -1.337  -28.845 1.00 25.66  ? 4   LEU   B CA   1 
ATOM   4436 C  C    . LEU   B 1 7   ? -12.477 -0.792  -27.441 1.00 26.81  ? 4   LEU   B C    1 
ATOM   4437 O  O    . LEU   B 1 7   ? -13.054 -1.301  -26.470 1.00 26.87  ? 4   LEU   B O    1 
ATOM   4438 C  CB   . LEU   B 1 7   ? -14.157 -1.173  -29.266 1.00 26.59  ? 4   LEU   B CB   1 
ATOM   4439 C  CG   . LEU   B 1 7   ? -14.740 0.237   -29.252 1.00 25.67  ? 4   LEU   B CG   1 
ATOM   4440 C  CD1  . LEU   B 1 7   ? -14.048 1.146   -30.253 1.00 30.90  ? 4   LEU   B CD1  1 
ATOM   4441 C  CD2  . LEU   B 1 7   ? -16.219 0.198   -29.557 1.00 27.02  ? 4   LEU   B CD2  1 
ATOM   4442 H  H    . LEU   B 1 7   ? -12.763 -3.237  -28.331 1.00 33.04  ? 4   LEU   B H    1 
ATOM   4443 H  HA   . LEU   B 1 7   ? -12.148 -0.832  -29.463 1.00 30.83  ? 4   LEU   B HA   1 
ATOM   4444 H  HB2  . LEU   B 1 7   ? -14.243 -1.503  -30.174 1.00 31.95  ? 4   LEU   B HB2  1 
ATOM   4445 H  HB3  . LEU   B 1 7   ? -14.701 -1.707  -28.666 1.00 31.95  ? 4   LEU   B HB3  1 
ATOM   4446 H  HG   . LEU   B 1 7   ? -14.599 0.605   -28.366 1.00 30.85  ? 4   LEU   B HG   1 
ATOM   4447 H  HD11 . LEU   B 1 7   ? -14.448 2.029   -30.207 1.00 37.12  ? 4   LEU   B HD11 1 
ATOM   4448 H  HD12 . LEU   B 1 7   ? -13.105 1.199   -30.032 1.00 37.12  ? 4   LEU   B HD12 1 
ATOM   4449 H  HD13 . LEU   B 1 7   ? -14.159 0.778   -31.143 1.00 37.12  ? 4   LEU   B HD13 1 
ATOM   4450 H  HD21 . LEU   B 1 7   ? -16.573 1.100   -29.524 1.00 32.47  ? 4   LEU   B HD21 1 
ATOM   4451 H  HD22 . LEU   B 1 7   ? -16.349 -0.177  -30.443 1.00 32.47  ? 4   LEU   B HD22 1 
ATOM   4452 H  HD23 . LEU   B 1 7   ? -16.663 -0.356  -28.896 1.00 32.47  ? 4   LEU   B HD23 1 
ATOM   4453 N  N    . GLU   B 1 8   ? -11.685 0.258   -27.332 1.00 29.96  ? 5   GLU   B N    1 
ATOM   4454 C  CA   . GLU   B 1 8   ? -11.357 0.817   -26.024 1.00 28.29  ? 5   GLU   B CA   1 
ATOM   4455 C  C    . GLU   B 1 8   ? -12.415 1.863   -25.687 1.00 32.23  ? 5   GLU   B C    1 
ATOM   4456 O  O    . GLU   B 1 8   ? -12.639 2.804   -26.453 1.00 35.46  ? 5   GLU   B O    1 
ATOM   4457 C  CB   . GLU   B 1 8   ? -9.929  1.365   -26.002 1.00 36.75  ? 5   GLU   B CB   1 
ATOM   4458 C  CG   . GLU   B 1 8   ? -9.718  2.783   -26.419 1.00 56.19  ? 5   GLU   B CG   1 
ATOM   4459 C  CD   . GLU   B 1 8   ? -8.235  3.157   -26.377 1.00 70.53  ? 5   GLU   B CD   1 
ATOM   4460 O  OE1  . GLU   B 1 8   ? -7.931  4.366   -26.442 1.00 64.60  ? 5   GLU   B OE1  1 
ATOM   4461 O  OE2  . GLU   B 1 8   ? -7.381  2.239   -26.287 1.00 61.31  ? 5   GLU   B OE2  1 
ATOM   4462 H  H    . GLU   B 1 8   ? -11.324 0.668   -27.996 1.00 35.99  ? 5   GLU   B H    1 
ATOM   4463 H  HA   . GLU   B 1 8   ? -11.384 0.136   -25.334 1.00 33.98  ? 5   GLU   B HA   1 
ATOM   4464 H  HB2  . GLU   B 1 8   ? -9.597  1.290   -25.094 1.00 44.14  ? 5   GLU   B HB2  1 
ATOM   4465 H  HB3  . GLU   B 1 8   ? -9.393  0.818   -26.597 1.00 44.14  ? 5   GLU   B HB3  1 
ATOM   4466 H  HG2  . GLU   B 1 8   ? -10.039 2.903   -27.327 1.00 67.47  ? 5   GLU   B HG2  1 
ATOM   4467 H  HG3  . GLU   B 1 8   ? -10.200 3.371   -25.817 1.00 67.47  ? 5   GLU   B HG3  1 
ATOM   4468 N  N    . LEU   B 1 9   ? -13.104 1.663   -24.575 1.00 31.57  ? 6   LEU   B N    1 
ATOM   4469 C  CA   . LEU   B 1 9   ? -14.201 2.512   -24.146 1.00 27.29  ? 6   LEU   B CA   1 
ATOM   4470 C  C    . LEU   B 1 9   ? -13.902 3.083   -22.764 1.00 26.21  ? 6   LEU   B C    1 
ATOM   4471 O  O    . LEU   B 1 9   ? -12.908 2.752   -22.122 1.00 29.53  ? 6   LEU   B O    1 
ATOM   4472 C  CB   . LEU   B 1 9   ? -15.508 1.726   -24.133 1.00 29.10  ? 6   LEU   B CB   1 
ATOM   4473 C  CG   . LEU   B 1 9   ? -15.866 1.154   -25.500 1.00 29.13  ? 6   LEU   B CG   1 
ATOM   4474 C  CD1  . LEU   B 1 9   ? -17.089 0.296   -25.388 1.00 25.64  ? 6   LEU   B CD1  1 
ATOM   4475 C  CD2  . LEU   B 1 9   ? -16.053 2.276   -26.524 1.00 29.96  ? 6   LEU   B CD2  1 
ATOM   4476 H  H    . LEU   B 1 9   ? -12.947 1.015   -24.031 1.00 37.92  ? 6   LEU   B H    1 
ATOM   4477 H  HA   . LEU   B 1 9   ? -14.289 3.252   -24.766 1.00 32.79  ? 6   LEU   B HA   1 
ATOM   4478 H  HB2  . LEU   B 1 9   ? -15.426 0.987   -23.510 1.00 34.96  ? 6   LEU   B HB2  1 
ATOM   4479 H  HB3  . LEU   B 1 9   ? -16.227 2.315   -23.856 1.00 34.96  ? 6   LEU   B HB3  1 
ATOM   4480 H  HG   . LEU   B 1 9   ? -15.142 0.595   -25.823 1.00 35.00  ? 6   LEU   B HG   1 
ATOM   4481 H  HD11 . LEU   B 1 9   ? -17.160 -0.257  -26.181 1.00 30.81  ? 6   LEU   B HD11 1 
ATOM   4482 H  HD12 . LEU   B 1 9   ? -17.010 -0.264  -24.600 1.00 30.81  ? 6   LEU   B HD12 1 
ATOM   4483 H  HD13 . LEU   B 1 9   ? -17.869 0.867   -25.311 1.00 30.81  ? 6   LEU   B HD13 1 
ATOM   4484 H  HD21 . LEU   B 1 9   ? -16.774 2.037   -27.127 1.00 35.99  ? 6   LEU   B HD21 1 
ATOM   4485 H  HD22 . LEU   B 1 9   ? -16.273 3.097   -26.055 1.00 35.99  ? 6   LEU   B HD22 1 
ATOM   4486 H  HD23 . LEU   B 1 9   ? -15.229 2.390   -27.022 1.00 35.99  ? 6   LEU   B HD23 1 
ATOM   4487 N  N    . GLN   B 1 10  ? -14.797 3.957   -22.299 1.00 31.19  ? 7   GLN   B N    1 
ATOM   4488 C  CA   . GLN   B 1 10  ? -14.659 4.505   -20.963 1.00 34.10  ? 7   GLN   B CA   1 
ATOM   4489 C  C    . GLN   B 1 10  ? -14.775 3.381   -19.930 1.00 25.89  ? 7   GLN   B C    1 
ATOM   4490 O  O    . GLN   B 1 10  ? -15.814 2.723   -19.830 1.00 28.52  ? 7   GLN   B O    1 
ATOM   4491 C  CB   . GLN   B 1 10  ? -15.746 5.580   -20.731 1.00 33.65  ? 7   GLN   B CB   1 
ATOM   4492 C  CG   . GLN   B 1 10  ? -15.724 6.247   -19.375 1.00 63.89  ? 7   GLN   B CG   1 
ATOM   4493 C  CD   . GLN   B 1 10  ? -16.726 7.419   -19.166 1.00 64.03  ? 7   GLN   B CD   1 
ATOM   4494 O  OE1  . GLN   B 1 10  ? -16.970 8.255   -20.071 1.00 61.57  ? 7   GLN   B OE1  1 
ATOM   4495 N  NE2  . GLN   B 1 10  ? -17.329 7.449   -17.966 1.00 70.10  ? 7   GLN   B NE2  1 
ATOM   4496 H  H    . GLN   B 1 10  ? -15.481 4.241   -22.736 1.00 37.47  ? 7   GLN   B H    1 
ATOM   4497 H  HA   . GLN   B 1 10  ? -13.791 4.927   -20.863 1.00 40.96  ? 7   GLN   B HA   1 
ATOM   4498 H  HB2  . GLN   B 1 10  ? -15.634 6.276   -21.397 1.00 40.43  ? 7   GLN   B HB2  1 
ATOM   4499 H  HB3  . GLN   B 1 10  ? -16.615 5.161   -20.832 1.00 40.43  ? 7   GLN   B HB3  1 
ATOM   4500 H  HG2  . GLN   B 1 10  ? -15.927 5.576   -18.704 1.00 76.71  ? 7   GLN   B HG2  1 
ATOM   4501 H  HG3  . GLN   B 1 10  ? -14.834 6.604   -19.228 1.00 76.71  ? 7   GLN   B HG3  1 
ATOM   4502 H  HE21 . GLN   B 1 10  ? -17.149 6.846   -17.380 1.00 84.16  ? 7   GLN   B HE21 1 
ATOM   4503 H  HE22 . GLN   B 1 10  ? -17.894 8.071   -17.785 1.00 84.16  ? 7   GLN   B HE22 1 
ATOM   4504 N  N    . GLY   B 1 11  ? -13.680 3.151   -19.189 1.00 28.30  ? 8   GLY   B N    1 
ATOM   4505 C  CA   . GLY   B 1 11  ? -13.673 2.138   -18.149 1.00 30.96  ? 8   GLY   B CA   1 
ATOM   4506 C  C    . GLY   B 1 11  ? -13.512 0.690   -18.587 1.00 30.11  ? 8   GLY   B C    1 
ATOM   4507 O  O    . GLY   B 1 11  ? -13.571 -0.205  -17.726 1.00 29.55  ? 8   GLY   B O    1 
ATOM   4508 H  H    . GLY   B 1 11  ? -12.936 3.572   -19.278 1.00 34.00  ? 8   GLY   B H    1 
ATOM   4509 H  HA2  . GLY   B 1 11  ? -12.943 2.336   -17.542 1.00 37.20  ? 8   GLY   B HA2  1 
ATOM   4510 H  HA3  . GLY   B 1 11  ? -14.511 2.198   -17.665 1.00 37.20  ? 8   GLY   B HA3  1 
ATOM   4511 N  N    . ALA   B 1 12  ? -13.329 0.409   -19.876 1.00 25.80  ? 9   ALA   B N    1 
ATOM   4512 C  CA   . ALA   B 1 12  ? -13.169 -0.979  -20.277 1.00 24.28  ? 9   ALA   B CA   1 
ATOM   4513 C  C    . ALA   B 1 12  ? -12.559 -1.095  -21.661 1.00 30.49  ? 9   ALA   B C    1 
ATOM   4514 O  O    . ALA   B 1 12  ? -12.687 -0.195  -22.485 1.00 29.22  ? 9   ALA   B O    1 
ATOM   4515 C  CB   . ALA   B 1 12  ? -14.511 -1.723  -20.276 1.00 24.61  ? 9   ALA   B CB   1 
ATOM   4516 H  H    . ALA   B 1 12  ? -13.296 0.987   -20.512 1.00 31.00  ? 9   ALA   B H    1 
ATOM   4517 H  HA   . ALA   B 1 12  ? -12.553 -1.385  -19.647 1.00 29.18  ? 9   ALA   B HA   1 
ATOM   4518 H  HB1  . ALA   B 1 12  ? -14.364 -2.640  -20.557 1.00 29.58  ? 9   ALA   B HB1  1 
ATOM   4519 H  HB2  . ALA   B 1 12  ? -14.881 -1.706  -19.380 1.00 29.58  ? 9   ALA   B HB2  1 
ATOM   4520 H  HB3  . ALA   B 1 12  ? -15.117 -1.282  -20.892 1.00 29.58  ? 9   ALA   B HB3  1 
ATOM   4521 N  N    . LYS   B 1 13  ? -11.917 -2.234  -21.905 1.00 25.43  ? 10  LYS   B N    1 
ATOM   4522 C  CA   . LYS   B 1 13  ? -11.543 -2.670  -23.245 1.00 25.40  ? 10  LYS   B CA   1 
ATOM   4523 C  C    . LYS   B 1 13  ? -12.527 -3.763  -23.647 1.00 24.39  ? 10  LYS   B C    1 
ATOM   4524 O  O    . LYS   B 1 13  ? -12.627 -4.796  -22.978 1.00 24.28  ? 10  LYS   B O    1 
ATOM   4525 C  CB   . LYS   B 1 13  ? -10.094 -3.158  -23.279 1.00 26.47  ? 10  LYS   B CB   1 
ATOM   4526 C  CG   . LYS   B 1 13  ? -9.069  -2.009  -23.000 1.00 28.72  ? 10  LYS   B CG   1 
ATOM   4527 C  CD   . LYS   B 1 13  ? -7.603  -2.437  -23.154 1.00 31.87  ? 10  LYS   B CD   1 
ATOM   4528 C  CE   . LYS   B 1 13  ? -6.716  -1.592  -22.276 1.00 39.58  ? 10  LYS   B CE   1 
ATOM   4529 N  NZ   . LYS   B 1 13  ? -5.313  -2.132  -22.246 1.00 43.86  ? 10  LYS   B NZ   1 
ATOM   4530 H  H    . LYS   B 1 13  ? -11.681 -2.787  -21.291 1.00 30.56  ? 10  LYS   B H    1 
ATOM   4531 H  HA   . LYS   B 1 13  ? -11.604 -1.942  -23.882 1.00 30.52  ? 10  LYS   B HA   1 
ATOM   4532 H  HB2  . LYS   B 1 13  ? -9.973  -3.840  -22.600 1.00 31.80  ? 10  LYS   B HB2  1 
ATOM   4533 H  HB3  . LYS   B 1 13  ? -9.903  -3.525  -24.156 1.00 31.80  ? 10  LYS   B HB3  1 
ATOM   4534 H  HG2  . LYS   B 1 13  ? -9.233  -1.285  -23.625 1.00 34.50  ? 10  LYS   B HG2  1 
ATOM   4535 H  HG3  . LYS   B 1 13  ? -9.191  -1.695  -22.090 1.00 34.50  ? 10  LYS   B HG3  1 
ATOM   4536 H  HD2  . LYS   B 1 13  ? -7.506  -3.365  -22.891 1.00 38.29  ? 10  LYS   B HD2  1 
ATOM   4537 H  HD3  . LYS   B 1 13  ? -7.325  -2.322  -24.076 1.00 38.29  ? 10  LYS   B HD3  1 
ATOM   4538 H  HE2  . LYS   B 1 13  ? -6.689  -0.686  -22.621 1.00 47.54  ? 10  LYS   B HE2  1 
ATOM   4539 H  HE3  . LYS   B 1 13  ? -7.064  -1.592  -21.370 1.00 47.54  ? 10  LYS   B HE3  1 
ATOM   4540 H  HZ1  . LYS   B 1 13  ? -4.789  -1.593  -21.769 1.00 52.67  ? 10  LYS   B HZ1  1 
ATOM   4541 H  HZ2  . LYS   B 1 13  ? -5.306  -2.942  -21.878 1.00 52.67  ? 10  LYS   B HZ2  1 
ATOM   4542 H  HZ3  . LYS   B 1 13  ? -4.991  -2.189  -23.074 1.00 52.67  ? 10  LYS   B HZ3  1 
ATOM   4543 N  N    . LEU   B 1 14  ? -13.336 -3.490  -24.672 1.00 24.13  ? 11  LEU   B N    1 
ATOM   4544 C  CA   . LEU   B 1 14  ? -14.395 -4.388  -25.094 1.00 21.08  ? 11  LEU   B CA   1 
ATOM   4545 C  C    . LEU   B 1 14  ? -13.881 -5.284  -26.222 1.00 24.85  ? 11  LEU   B C    1 
ATOM   4546 O  O    . LEU   B 1 14  ? -13.453 -4.794  -27.274 1.00 25.82  ? 11  LEU   B O    1 
ATOM   4547 C  CB   . LEU   B 1 14  ? -15.606 -3.586  -25.576 1.00 20.79  ? 11  LEU   B CB   1 
ATOM   4548 C  CG   . LEU   B 1 14  ? -16.865 -4.379  -25.834 1.00 22.54  ? 11  LEU   B CG   1 
ATOM   4549 C  CD1  . LEU   B 1 14  ? -17.575 -4.744  -24.520 1.00 22.35  ? 11  LEU   B CD1  1 
ATOM   4550 C  CD2  . LEU   B 1 14  ? -17.813 -3.572  -26.736 1.00 24.00  ? 11  LEU   B CD2  1 
ATOM   4551 H  H    . LEU   B 1 14  ? -13.285 -2.773  -25.145 1.00 29.00  ? 11  LEU   B H    1 
ATOM   4552 H  HA   . LEU   B 1 14  ? -14.659 -4.947  -24.347 1.00 25.33  ? 11  LEU   B HA   1 
ATOM   4553 H  HB2  . LEU   B 1 14  ? -15.818 -2.923  -24.900 1.00 24.99  ? 11  LEU   B HB2  1 
ATOM   4554 H  HB3  . LEU   B 1 14  ? -15.367 -3.148  -26.408 1.00 24.99  ? 11  LEU   B HB3  1 
ATOM   4555 H  HG   . LEU   B 1 14  ? -16.626 -5.207  -26.280 1.00 27.09  ? 11  LEU   B HG   1 
ATOM   4556 H  HD11 . LEU   B 1 14  ? -18.361 -5.275  -24.722 1.00 26.86  ? 11  LEU   B HD11 1 
ATOM   4557 H  HD12 . LEU   B 1 14  ? -16.966 -5.254  -23.963 1.00 26.86  ? 11  LEU   B HD12 1 
ATOM   4558 H  HD13 . LEU   B 1 14  ? -17.835 -3.928  -24.064 1.00 26.86  ? 11  LEU   B HD13 1 
ATOM   4559 H  HD21 . LEU   B 1 14  ? -18.652 -4.051  -26.821 1.00 28.84  ? 11  LEU   B HD21 1 
ATOM   4560 H  HD22 . LEU   B 1 14  ? -17.967 -2.703  -26.333 1.00 28.84  ? 11  LEU   B HD22 1 
ATOM   4561 H  HD23 . LEU   B 1 14  ? -17.403 -3.464  -27.608 1.00 28.84  ? 11  LEU   B HD23 1 
ATOM   4562 N  N    . ARG   B 1 15  ? -13.891 -6.589  -26.001 1.00 20.70  ? 12  ARG   B N    1 
ATOM   4563 C  CA   . ARG   B 1 15  ? -13.390 -7.532  -26.993 1.00 21.89  ? 12  ARG   B CA   1 
ATOM   4564 C  C    . ARG   B 1 15  ? -14.560 -8.223  -27.680 1.00 20.88  ? 12  ARG   B C    1 
ATOM   4565 O  O    . ARG   B 1 15  ? -15.586 -8.517  -27.052 1.00 20.97  ? 12  ARG   B O    1 
ATOM   4566 C  CB   . ARG   B 1 15  ? -12.465 -8.589  -26.374 1.00 22.51  ? 12  ARG   B CB   1 
ATOM   4567 C  CG   . ARG   B 1 15  ? -11.013 -8.220  -26.349 1.00 29.69  ? 12  ARG   B CG   1 
ATOM   4568 C  CD   . ARG   B 1 15  ? -10.738 -6.898  -25.691 1.00 28.27  ? 12  ARG   B CD   1 
ATOM   4569 N  NE   . ARG   B 1 15  ? -9.300  -6.548  -25.649 1.00 30.29  ? 12  ARG   B NE   1 
ATOM   4570 C  CZ   . ARG   B 1 15  ? -8.542  -6.488  -24.550 1.00 27.78  ? 12  ARG   B CZ   1 
ATOM   4571 N  NH1  . ARG   B 1 15  ? -8.984  -6.919  -23.371 1.00 26.39  ? 12  ARG   B NH1  1 
ATOM   4572 N  NH2  . ARG   B 1 15  ? -7.339  -5.927  -24.618 1.00 29.04  ? 12  ARG   B NH2  1 
ATOM   4573 H  H    . ARG   B 1 15  ? -14.184 -6.957  -25.281 1.00 24.88  ? 12  ARG   B H    1 
ATOM   4574 H  HA   . ARG   B 1 15  ? -12.874 -7.042  -27.652 1.00 26.31  ? 12  ARG   B HA   1 
ATOM   4575 H  HB2  . ARG   B 1 15  ? -12.742 -8.742  -25.458 1.00 27.05  ? 12  ARG   B HB2  1 
ATOM   4576 H  HB3  . ARG   B 1 15  ? -12.548 -9.408  -26.887 1.00 27.05  ? 12  ARG   B HB3  1 
ATOM   4577 H  HG2  . ARG   B 1 15  ? -10.526 -8.901  -25.860 1.00 35.67  ? 12  ARG   B HG2  1 
ATOM   4578 H  HG3  . ARG   B 1 15  ? -10.687 -8.170  -27.261 1.00 35.67  ? 12  ARG   B HG3  1 
ATOM   4579 H  HD2  . ARG   B 1 15  ? -11.198 -6.201  -26.184 1.00 33.97  ? 12  ARG   B HD2  1 
ATOM   4580 H  HD3  . ARG   B 1 15  ? -11.062 -6.928  -24.778 1.00 33.97  ? 12  ARG   B HD3  1 
ATOM   4581 H  HE   . ARG   B 1 15  ? -8.919  -6.367  -26.398 1.00 36.39  ? 12  ARG   B HE   1 
ATOM   4582 H  HH11 . ARG   B 1 15  ? -9.776  -7.246  -23.302 1.00 31.71  ? 12  ARG   B HH11 1 
ATOM   4583 H  HH12 . ARG   B 1 15  ? -8.478  -6.869  -22.677 1.00 31.71  ? 12  ARG   B HH12 1 
ATOM   4584 H  HH21 . ARG   B 1 15  ? -7.056  -5.608  -25.364 1.00 34.89  ? 12  ARG   B HH21 1 
ATOM   4585 H  HH22 . ARG   B 1 15  ? -6.845  -5.884  -23.916 1.00 34.89  ? 12  ARG   B HH22 1 
ATOM   4586 N  N    . TYR   B 1 16  ? -14.409 -8.483  -28.976 1.00 20.79  ? 13  TYR   B N    1 
ATOM   4587 C  CA   . TYR   B 1 16  ? -15.465 -9.114  -29.743 1.00 20.85  ? 13  TYR   B CA   1 
ATOM   4588 C  C    . TYR   B 1 16  ? -14.882 -9.958  -30.879 1.00 20.83  ? 13  TYR   B C    1 
ATOM   4589 O  O    . TYR   B 1 16  ? -13.788 -9.713  -31.382 1.00 22.72  ? 13  TYR   B O    1 
ATOM   4590 C  CB   . TYR   B 1 16  ? -16.438 -8.066  -30.294 1.00 19.41  ? 13  TYR   B CB   1 
ATOM   4591 C  CG   . TYR   B 1 16  ? -15.810 -6.989  -31.149 1.00 21.12  ? 13  TYR   B CG   1 
ATOM   4592 C  CD1  . TYR   B 1 16  ? -15.233 -5.876  -30.570 1.00 22.16  ? 13  TYR   B CD1  1 
ATOM   4593 C  CD2  . TYR   B 1 16  ? -15.846 -7.074  -32.543 1.00 23.08  ? 13  TYR   B CD2  1 
ATOM   4594 C  CE1  . TYR   B 1 16  ? -14.624 -4.874  -31.347 1.00 24.84  ? 13  TYR   B CE1  1 
ATOM   4595 C  CE2  . TYR   B 1 16  ? -15.273 -6.059  -33.331 1.00 24.04  ? 13  TYR   B CE2  1 
ATOM   4596 C  CZ   . TYR   B 1 16  ? -14.676 -4.968  -32.729 1.00 28.42  ? 13  TYR   B CZ   1 
ATOM   4597 O  OH   . TYR   B 1 16  ? -14.082 -3.962  -33.485 1.00 29.01  ? 13  TYR   B OH   1 
ATOM   4598 H  H    . TYR   B 1 16  ? -13.702 -8.301  -29.430 1.00 24.99  ? 13  TYR   B H    1 
ATOM   4599 H  HA   . TYR   B 1 16  ? -15.946 -9.725  -29.164 1.00 25.06  ? 13  TYR   B HA   1 
ATOM   4600 H  HB2  . TYR   B 1 16  ? -17.100 -8.520  -30.839 1.00 23.33  ? 13  TYR   B HB2  1 
ATOM   4601 H  HB3  . TYR   B 1 16  ? -16.870 -7.626  -29.545 1.00 23.33  ? 13  TYR   B HB3  1 
ATOM   4602 H  HD1  . TYR   B 1 16  ? -15.247 -5.787  -29.645 1.00 26.63  ? 13  TYR   B HD1  1 
ATOM   4603 H  HD2  . TYR   B 1 16  ? -16.250 -7.805  -32.952 1.00 27.74  ? 13  TYR   B HD2  1 
ATOM   4604 H  HE1  . TYR   B 1 16  ? -14.193 -4.158  -30.939 1.00 29.85  ? 13  TYR   B HE1  1 
ATOM   4605 H  HE2  . TYR   B 1 16  ? -15.296 -6.122  -34.258 1.00 28.89  ? 13  TYR   B HE2  1 
ATOM   4606 H  HH   . TYR   B 1 16  ? -14.003 -4.211  -34.283 1.00 34.85  ? 13  TYR   B HH   1 
ATOM   4607 N  N    . HIS   B 1 17  ? -15.673 -10.950 -31.296 1.00 21.06  ? 14  HIS   B N    1 
ATOM   4608 C  CA   . HIS   B 1 17  ? -15.383 -11.717 -32.490 1.00 22.47  ? 14  HIS   B CA   1 
ATOM   4609 C  C    . HIS   B 1 17  ? -16.010 -10.995 -33.666 1.00 22.43  ? 14  HIS   B C    1 
ATOM   4610 O  O    . HIS   B 1 17  ? -17.123 -10.474 -33.558 1.00 24.25  ? 14  HIS   B O    1 
ATOM   4611 C  CB   . HIS   B 1 17  ? -15.960 -13.130 -32.412 1.00 25.66  ? 14  HIS   B CB   1 
ATOM   4612 C  CG   . HIS   B 1 17  ? -15.520 -13.905 -31.218 1.00 25.44  ? 14  HIS   B CG   1 
ATOM   4613 N  ND1  . HIS   B 1 17  ? -14.317 -14.577 -31.157 1.00 27.63  ? 14  HIS   B ND1  1 
ATOM   4614 C  CD2  . HIS   B 1 17  ? -16.122 -14.094 -30.015 1.00 27.81  ? 14  HIS   B CD2  1 
ATOM   4615 C  CE1  . HIS   B 1 17  ? -14.211 -15.164 -29.976 1.00 27.96  ? 14  HIS   B CE1  1 
ATOM   4616 N  NE2  . HIS   B 1 17  ? -15.282 -14.879 -29.262 1.00 28.24  ? 14  HIS   B NE2  1 
ATOM   4617 H  H    . HIS   B 1 17  ? -16.393 -11.195 -30.893 1.00 25.32  ? 14  HIS   B H    1 
ATOM   4618 H  HA   . HIS   B 1 17  ? -14.423 -11.802 -32.602 1.00 27.01  ? 14  HIS   B HA   1 
ATOM   4619 H  HB2  . HIS   B 1 17  ? -16.928 -13.069 -32.383 1.00 30.84  ? 14  HIS   B HB2  1 
ATOM   4620 H  HB3  . HIS   B 1 17  ? -15.683 -13.622 -33.201 1.00 30.84  ? 14  HIS   B HB3  1 
ATOM   4621 H  HD2  . HIS   B 1 17  ? -16.947 -13.755 -29.750 1.00 33.41  ? 14  HIS   B HD2  1 
ATOM   4622 H  HE1  . HIS   B 1 17  ? -13.498 -15.692 -29.696 1.00 33.60  ? 14  HIS   B HE1  1 
ATOM   4623 H  HE2  . HIS   B 1 17  ? -15.431 -15.142 -28.456 1.00 33.93  ? 14  HIS   B HE2  1 
ATOM   4624 N  N    . GLN   B 1 18  ? -15.317 -10.993 -34.804 1.00 25.37  ? 15  GLN   B N    1 
ATOM   4625 C  CA   . GLN   B 1 18  ? -15.890 -10.408 -36.010 1.00 27.19  ? 15  GLN   B CA   1 
ATOM   4626 C  C    . GLN   B 1 18  ? -15.631 -11.350 -37.171 1.00 28.53  ? 15  GLN   B C    1 
ATOM   4627 O  O    . GLN   B 1 18  ? -14.480 -11.652 -37.493 1.00 28.70  ? 15  GLN   B O    1 
ATOM   4628 C  CB   . GLN   B 1 18  ? -15.321 -9.016  -36.266 1.00 28.60  ? 15  GLN   B CB   1 
ATOM   4629 C  CG   . GLN   B 1 18  ? -15.643 -8.442  -37.639 1.00 29.37  ? 15  GLN   B CG   1 
ATOM   4630 C  CD   . GLN   B 1 18  ? -15.411 -6.931  -37.749 1.00 36.17  ? 15  GLN   B CD   1 
ATOM   4631 O  OE1  . GLN   B 1 18  ? -15.008 -6.282  -36.803 1.00 38.70  ? 15  GLN   B OE1  1 
ATOM   4632 N  NE2  . GLN   B 1 18  ? -15.499 -6.414  -38.975 1.00 40.04  ? 15  GLN   B NE2  1 
ATOM   4633 H  H    . GLN   B 1 18  ? -14.527 -11.319 -34.898 1.00 30.48  ? 15  GLN   B H    1 
ATOM   4634 H  HA   . GLN   B 1 18  ? -16.852 -10.318 -35.916 1.00 32.67  ? 15  GLN   B HA   1 
ATOM   4635 H  HB2  . GLN   B 1 18  ? -15.682 -8.408  -35.603 1.00 34.37  ? 15  GLN   B HB2  1 
ATOM   4636 H  HB3  . GLN   B 1 18  ? -14.355 -9.059  -36.186 1.00 34.37  ? 15  GLN   B HB3  1 
ATOM   4637 H  HG2  . GLN   B 1 18  ? -15.080 -8.876  -38.299 1.00 35.29  ? 15  GLN   B HG2  1 
ATOM   4638 H  HG3  . GLN   B 1 18  ? -16.577 -8.613  -37.837 1.00 35.29  ? 15  GLN   B HG3  1 
ATOM   4639 H  HE21 . GLN   B 1 18  ? -15.677 -6.923  -39.645 1.00 48.09  ? 15  GLN   B HE21 1 
ATOM   4640 H  HE22 . GLN   B 1 18  ? -15.378 -5.571  -39.096 1.00 48.09  ? 15  GLN   B HE22 1 
ATOM   4641 N  N    . VAL   B 1 19  ? -16.702 -11.819 -37.792 1.00 25.52  ? 16  VAL   B N    1 
ATOM   4642 C  CA   . VAL   B 1 19  ? -16.603 -12.807 -38.852 1.00 29.90  ? 16  VAL   B CA   1 
ATOM   4643 C  C    . VAL   B 1 19  ? -17.611 -12.459 -39.935 1.00 28.79  ? 16  VAL   B C    1 
ATOM   4644 O  O    . VAL   B 1 19  ? -18.794 -12.229 -39.657 1.00 28.28  ? 16  VAL   B O    1 
ATOM   4645 C  CB   . VAL   B 1 19  ? -16.838 -14.240 -38.330 1.00 37.63  ? 16  VAL   B CB   1 
ATOM   4646 C  CG1  . VAL   B 1 19  ? -15.933 -14.543 -37.116 1.00 47.01  ? 16  VAL   B CG1  1 
ATOM   4647 C  CG2  . VAL   B 1 19  ? -18.268 -14.433 -37.992 1.00 44.39  ? 16  VAL   B CG2  1 
ATOM   4648 H  H    . VAL   B 1 19  ? -17.508 -11.576 -37.615 1.00 30.67  ? 16  VAL   B H    1 
ATOM   4649 H  HA   . VAL   B 1 19  ? -15.715 -12.769 -39.241 1.00 35.92  ? 16  VAL   B HA   1 
ATOM   4650 H  HB   . VAL   B 1 19  ? -16.605 -14.870 -39.029 1.00 45.20  ? 16  VAL   B HB   1 
ATOM   4651 H  HG11 . VAL   B 1 19  ? -16.096 -15.452 -36.820 1.00 56.45  ? 16  VAL   B HG11 1 
ATOM   4652 H  HG12 . VAL   B 1 19  ? -15.005 -14.443 -37.381 1.00 56.45  ? 16  VAL   B HG12 1 
ATOM   4653 H  HG13 . VAL   B 1 19  ? -16.142 -13.920 -36.402 1.00 56.45  ? 16  VAL   B HG13 1 
ATOM   4654 H  HG21 . VAL   B 1 19  ? -18.392 -15.330 -37.644 1.00 53.31  ? 16  VAL   B HG21 1 
ATOM   4655 H  HG22 . VAL   B 1 19  ? -18.526 -13.780 -37.323 1.00 53.31  ? 16  VAL   B HG22 1 
ATOM   4656 H  HG23 . VAL   B 1 19  ? -18.801 -14.313 -38.794 1.00 53.31  ? 16  VAL   B HG23 1 
ATOM   4657 N  N    . GLY   B 1 20  ? -17.159 -12.471 -41.165 1.00 30.46  ? 17  GLY   B N    1 
ATOM   4658 C  CA   . GLY   B 1 20  ? -18.050 -12.338 -42.292 1.00 30.51  ? 17  GLY   B CA   1 
ATOM   4659 C  C    . GLY   B 1 20  ? -17.963 -10.972 -42.942 1.00 30.39  ? 17  GLY   B C    1 
ATOM   4660 O  O    . GLY   B 1 20  ? -17.070 -10.158 -42.656 1.00 33.62  ? 17  GLY   B O    1 
ATOM   4661 H  H    . GLY   B 1 20  ? -16.330 -12.557 -41.377 1.00 36.59  ? 17  GLY   B H    1 
ATOM   4662 H  HA2  . GLY   B 1 20  ? -17.827 -13.007 -42.958 1.00 36.65  ? 17  GLY   B HA2  1 
ATOM   4663 H  HA3  . GLY   B 1 20  ? -18.963 -12.477 -41.997 1.00 36.65  ? 17  GLY   B HA3  1 
ATOM   4664 N  N    . GLN   B 1 21  ? -18.905 -10.755 -43.857 1.00 27.94  ? 18  GLN   B N    1 
ATOM   4665 C  CA   . GLN   B 1 21  ? -19.035 -9.561  -44.672 1.00 33.00  ? 18  GLN   B CA   1 
ATOM   4666 C  C    . GLN   B 1 21  ? -20.501 -9.260  -44.919 1.00 32.36  ? 18  GLN   B C    1 
ATOM   4667 O  O    . GLN   B 1 21  ? -21.349 -10.158 -44.965 1.00 31.52  ? 18  GLN   B O    1 
ATOM   4668 C  CB   . GLN   B 1 21  ? -18.277 -9.716  -45.989 1.00 33.62  ? 18  GLN   B CB   1 
ATOM   4669 C  CG   . GLN   B 1 21  ? -16.811 -10.027 -45.736 1.00 40.99  ? 18  GLN   B CG   1 
ATOM   4670 C  CD   . GLN   B 1 21  ? -16.046 -10.115 -47.010 1.00 49.74  ? 18  GLN   B CD   1 
ATOM   4671 O  OE1  . GLN   B 1 21  ? -16.382 -9.436  -47.982 1.00 50.44  ? 18  GLN   B OE1  1 
ATOM   4672 N  NE2  . GLN   B 1 21  ? -14.997 -10.940 -47.028 1.00 49.30  ? 18  GLN   B NE2  1 
ATOM   4673 H  H    . GLN   B 1 21  ? -19.523 -11.327 -44.034 1.00 33.57  ? 18  GLN   B H    1 
ATOM   4674 H  HA   . GLN   B 1 21  ? -18.669 -8.799  -44.195 1.00 39.64  ? 18  GLN   B HA   1 
ATOM   4675 H  HB2  . GLN   B 1 21  ? -18.664 -10.445 -46.499 1.00 40.39  ? 18  GLN   B HB2  1 
ATOM   4676 H  HB3  . GLN   B 1 21  ? -18.335 -8.890  -46.494 1.00 40.39  ? 18  GLN   B HB3  1 
ATOM   4677 H  HG2  . GLN   B 1 21  ? -16.423 -9.323  -45.194 1.00 49.23  ? 18  GLN   B HG2  1 
ATOM   4678 H  HG3  . GLN   B 1 21  ? -16.738 -10.878 -45.277 1.00 49.23  ? 18  GLN   B HG3  1 
ATOM   4679 H  HE21 . GLN   B 1 21  ? -14.792 -11.390 -46.324 1.00 59.20  ? 18  GLN   B HE21 1 
ATOM   4680 H  HE22 . GLN   B 1 21  ? -14.526 -11.022 -47.743 1.00 59.20  ? 18  GLN   B HE22 1 
ATOM   4681 N  N    . GLY   B 1 22  ? -20.794 -7.969  -45.076 1.00 30.68  ? 19  GLY   B N    1 
ATOM   4682 C  CA   . GLY   B 1 22  ? -22.149 -7.510  -45.214 1.00 28.00  ? 19  GLY   B CA   1 
ATOM   4683 C  C    . GLY   B 1 22  ? -22.534 -6.558  -44.097 1.00 26.18  ? 19  GLY   B C    1 
ATOM   4684 O  O    . GLY   B 1 22  ? -21.696 -6.115  -43.313 1.00 28.86  ? 19  GLY   B O    1 
ATOM   4685 H  H    . GLY   B 1 22  ? -20.208 -7.340  -45.104 1.00 36.86  ? 19  GLY   B H    1 
ATOM   4686 H  HA2  . GLY   B 1 22  ? -22.250 -7.049  -46.062 1.00 33.65  ? 19  GLY   B HA2  1 
ATOM   4687 H  HA3  . GLY   B 1 22  ? -22.753 -8.269  -45.194 1.00 33.65  ? 19  GLY   B HA3  1 
ATOM   4688 N  N    . PRO   B 1 23  ? -23.821 -6.231  -43.991 1.00 26.99  ? 20  PRO   B N    1 
ATOM   4689 C  CA   . PRO   B 1 23  ? -24.253 -5.350  -42.897 1.00 27.03  ? 20  PRO   B CA   1 
ATOM   4690 C  C    . PRO   B 1 23  ? -23.915 -5.942  -41.540 1.00 23.59  ? 20  PRO   B C    1 
ATOM   4691 O  O    . PRO   B 1 23  ? -23.872 -7.161  -41.357 1.00 25.34  ? 20  PRO   B O    1 
ATOM   4692 C  CB   . PRO   B 1 23  ? -25.767 -5.226  -43.091 1.00 27.68  ? 20  PRO   B CB   1 
ATOM   4693 C  CG   . PRO   B 1 23  ? -26.114 -5.994  -44.306 1.00 40.01  ? 20  PRO   B CG   1 
ATOM   4694 C  CD   . PRO   B 1 23  ? -24.923 -6.634  -44.881 1.00 30.32  ? 20  PRO   B CD   1 
ATOM   4695 H  HA   . PRO   B 1 23  ? -23.843 -4.475  -42.987 1.00 32.48  ? 20  PRO   B HA   1 
ATOM   4696 H  HB2  . PRO   B 1 23  ? -26.221 -5.593  -42.316 1.00 33.25  ? 20  PRO   B HB2  1 
ATOM   4697 H  HB3  . PRO   B 1 23  ? -26.001 -4.291  -43.202 1.00 33.25  ? 20  PRO   B HB3  1 
ATOM   4698 H  HG2  . PRO   B 1 23  ? -26.763 -6.673  -44.064 1.00 48.05  ? 20  PRO   B HG2  1 
ATOM   4699 H  HG3  . PRO   B 1 23  ? -26.499 -5.383  -44.955 1.00 48.05  ? 20  PRO   B HG3  1 
ATOM   4700 H  HD2  . PRO   B 1 23  ? -25.024 -7.599  -44.884 1.00 36.43  ? 20  PRO   B HD2  1 
ATOM   4701 H  HD3  . PRO   B 1 23  ? -24.767 -6.314  -45.783 1.00 36.43  ? 20  PRO   B HD3  1 
ATOM   4702 N  N    . VAL   B 1 24  ? -23.698 -5.056  -40.565 1.00 23.48  ? 21  VAL   B N    1 
ATOM   4703 C  CA   . VAL   B 1 24  ? -23.291 -5.490  -39.239 1.00 21.68  ? 21  VAL   B CA   1 
ATOM   4704 C  C    . VAL   B 1 24  ? -24.477 -6.097  -38.486 1.00 21.21  ? 21  VAL   B C    1 
ATOM   4705 O  O    . VAL   B 1 24  ? -25.567 -5.513  -38.438 1.00 22.00  ? 21  VAL   B O    1 
ATOM   4706 C  CB   . VAL   B 1 24  ? -22.692 -4.318  -38.456 1.00 22.13  ? 21  VAL   B CB   1 
ATOM   4707 C  CG1  . VAL   B 1 24  ? -22.528 -4.699  -36.987 1.00 20.94  ? 21  VAL   B CG1  1 
ATOM   4708 C  CG2  . VAL   B 1 24  ? -21.352 -3.912  -39.025 1.00 27.40  ? 21  VAL   B CG2  1 
ATOM   4709 H  H    . VAL   B 1 24  ? -23.780 -4.204  -40.651 1.00 28.21  ? 21  VAL   B H    1 
ATOM   4710 H  HA   . VAL   B 1 24  ? -22.617 -6.181  -39.339 1.00 26.06  ? 21  VAL   B HA   1 
ATOM   4711 H  HB   . VAL   B 1 24  ? -23.297 -3.562  -38.528 1.00 26.60  ? 21  VAL   B HB   1 
ATOM   4712 H  HG11 . VAL   B 1 24  ? -21.978 -4.032  -36.547 1.00 25.17  ? 21  VAL   B HG11 1 
ATOM   4713 H  HG12 . VAL   B 1 24  ? -23.403 -4.734  -36.570 1.00 25.17  ? 21  VAL   B HG12 1 
ATOM   4714 H  HG13 . VAL   B 1 24  ? -22.100 -5.568  -36.932 1.00 25.17  ? 21  VAL   B HG13 1 
ATOM   4715 H  HG21 . VAL   B 1 24  ? -21.016 -3.149  -38.528 1.00 32.92  ? 21  VAL   B HG21 1 
ATOM   4716 H  HG22 . VAL   B 1 24  ? -20.736 -4.657  -38.943 1.00 32.92  ? 21  VAL   B HG22 1 
ATOM   4717 H  HG23 . VAL   B 1 24  ? -21.463 -3.675  -39.959 1.00 32.92  ? 21  VAL   B HG23 1 
ATOM   4718 N  N    . LEU   B 1 25  ? -24.257 -7.263  -37.889 1.00 19.23  ? 22  LEU   B N    1 
ATOM   4719 C  CA   . LEU   B 1 25  ? -25.209 -7.940  -37.018 1.00 19.55  ? 22  LEU   B CA   1 
ATOM   4720 C  C    . LEU   B 1 25  ? -24.483 -8.181  -35.689 1.00 20.51  ? 22  LEU   B C    1 
ATOM   4721 O  O    . LEU   B 1 25  ? -23.513 -8.955  -35.642 1.00 19.75  ? 22  LEU   B O    1 
ATOM   4722 C  CB   . LEU   B 1 25  ? -25.668 -9.244  -37.653 1.00 20.76  ? 22  LEU   B CB   1 
ATOM   4723 C  CG   . LEU   B 1 25  ? -26.492 -10.212 -36.831 1.00 23.66  ? 22  LEU   B CG   1 
ATOM   4724 C  CD1  . LEU   B 1 25  ? -27.645 -9.522  -36.199 1.00 29.08  ? 22  LEU   B CD1  1 
ATOM   4725 C  CD2  . LEU   B 1 25  ? -26.949 -11.354 -37.733 1.00 25.53  ? 22  LEU   B CD2  1 
ATOM   4726 H  H    . LEU   B 1 25  ? -23.524 -7.704  -37.978 1.00 23.12  ? 22  LEU   B H    1 
ATOM   4727 H  HA   . LEU   B 1 25  ? -25.995 -7.394  -36.857 1.00 23.50  ? 22  LEU   B HA   1 
ATOM   4728 H  HB2  . LEU   B 1 25  ? -26.206 -9.017  -38.428 1.00 24.96  ? 22  LEU   B HB2  1 
ATOM   4729 H  HB3  . LEU   B 1 25  ? -24.874 -9.727  -37.931 1.00 24.96  ? 22  LEU   B HB3  1 
ATOM   4730 H  HG   . LEU   B 1 25  ? -25.958 -10.577 -36.108 1.00 28.44  ? 22  LEU   B HG   1 
ATOM   4731 H  HD11 . LEU   B 1 25  ? -28.239 -10.187 -35.816 1.00 34.94  ? 22  LEU   B HD11 1 
ATOM   4732 H  HD12 . LEU   B 1 25  ? -27.318 -8.932  -35.503 1.00 34.94  ? 22  LEU   B HD12 1 
ATOM   4733 H  HD13 . LEU   B 1 25  ? -28.115 -9.009  -36.874 1.00 34.94  ? 22  LEU   B HD13 1 
ATOM   4734 H  HD21 . LEU   B 1 25  ? -27.386 -12.029 -37.191 1.00 30.68  ? 22  LEU   B HD21 1 
ATOM   4735 H  HD22 . LEU   B 1 25  ? -27.569 -11.006 -38.393 1.00 30.68  ? 22  LEU   B HD22 1 
ATOM   4736 H  HD23 . LEU   B 1 25  ? -26.175 -11.736 -38.176 1.00 30.68  ? 22  LEU   B HD23 1 
ATOM   4737 N  N    . ILE   B 1 26  ? -24.910 -7.495  -34.619 1.00 19.27  ? 23  ILE   B N    1 
ATOM   4738 C  CA   . ILE   B 1 26  ? -24.326 -7.649  -33.290 1.00 18.10  ? 23  ILE   B CA   1 
ATOM   4739 C  C    . ILE   B 1 26  ? -25.133 -8.647  -32.471 1.00 17.13  ? 23  ILE   B C    1 
ATOM   4740 O  O    . ILE   B 1 26  ? -26.338 -8.445  -32.262 1.00 18.65  ? 23  ILE   B O    1 
ATOM   4741 C  CB   . ILE   B 1 26  ? -24.257 -6.312  -32.550 1.00 18.12  ? 23  ILE   B CB   1 
ATOM   4742 C  CG1  . ILE   B 1 26  ? -23.426 -5.312  -33.337 1.00 20.13  ? 23  ILE   B CG1  1 
ATOM   4743 C  CG2  . ILE   B 1 26  ? -23.631 -6.502  -31.172 1.00 17.61  ? 23  ILE   B CG2  1 
ATOM   4744 C  CD1  . ILE   B 1 26  ? -23.447 -3.939  -32.779 1.00 22.52  ? 23  ILE   B CD1  1 
ATOM   4745 H  H    . ILE   B 1 26  ? -25.552 -6.923  -34.645 1.00 23.16  ? 23  ILE   B H    1 
ATOM   4746 H  HA   . ILE   B 1 26  ? -23.433 -8.011  -33.408 1.00 21.76  ? 23  ILE   B HA   1 
ATOM   4747 H  HB   . ILE   B 1 26  ? -25.162 -5.976  -32.455 1.00 21.79  ? 23  ILE   B HB   1 
ATOM   4748 H  HG12 . ILE   B 1 26  ? -22.504 -5.612  -33.346 1.00 24.20  ? 23  ILE   B HG12 1 
ATOM   4749 H  HG13 . ILE   B 1 26  ? -23.769 -5.267  -34.243 1.00 24.20  ? 23  ILE   B HG13 1 
ATOM   4750 H  HG21 . ILE   B 1 26  ? -23.597 -5.644  -30.720 1.00 21.17  ? 23  ILE   B HG21 1 
ATOM   4751 H  HG22 . ILE   B 1 26  ? -24.174 -7.123  -30.662 1.00 21.17  ? 23  ILE   B HG22 1 
ATOM   4752 H  HG23 . ILE   B 1 26  ? -22.735 -6.856  -31.278 1.00 21.17  ? 23  ILE   B HG23 1 
ATOM   4753 H  HD11 . ILE   B 1 26  ? -23.122 -3.320  -33.452 1.00 27.07  ? 23  ILE   B HD11 1 
ATOM   4754 H  HD12 . ILE   B 1 26  ? -24.357 -3.711  -32.533 1.00 27.07  ? 23  ILE   B HD12 1 
ATOM   4755 H  HD13 . ILE   B 1 26  ? -22.875 -3.907  -31.996 1.00 27.07  ? 23  ILE   B HD13 1 
ATOM   4756 N  N    . PHE   B 1 27  ? -24.451 -9.678  -31.971 1.00 16.04  ? 24  PHE   B N    1 
ATOM   4757 C  CA   . PHE   B 1 27  ? -25.013 -10.635 -31.019 1.00 16.98  ? 24  PHE   B CA   1 
ATOM   4758 C  C    . PHE   B 1 27  ? -24.562 -10.297 -29.598 1.00 17.08  ? 24  PHE   B C    1 
ATOM   4759 O  O    . PHE   B 1 27  ? -23.351 -10.198 -29.315 1.00 16.56  ? 24  PHE   B O    1 
ATOM   4760 C  CB   . PHE   B 1 27  ? -24.603 -12.069 -31.361 1.00 16.57  ? 24  PHE   B CB   1 
ATOM   4761 C  CG   . PHE   B 1 27  ? -25.279 -12.632 -32.574 1.00 19.21  ? 24  PHE   B CG   1 
ATOM   4762 C  CD1  . PHE   B 1 27  ? -26.629 -12.873 -32.586 1.00 21.03  ? 24  PHE   B CD1  1 
ATOM   4763 C  CD2  . PHE   B 1 27  ? -24.550 -12.944 -33.688 1.00 22.35  ? 24  PHE   B CD2  1 
ATOM   4764 C  CE1  . PHE   B 1 27  ? -27.252 -13.410 -33.711 1.00 21.31  ? 24  PHE   B CE1  1 
ATOM   4765 C  CE2  . PHE   B 1 27  ? -25.183 -13.493 -34.811 1.00 24.23  ? 24  PHE   B CE2  1 
ATOM   4766 C  CZ   . PHE   B 1 27  ? -26.539 -13.723 -34.792 1.00 21.33  ? 24  PHE   B CZ   1 
ATOM   4767 H  H    . PHE   B 1 27  ? -23.633 -9.849  -32.175 1.00 19.29  ? 24  PHE   B H    1 
ATOM   4768 H  HA   . PHE   B 1 27  ? -25.981 -10.573 -31.057 1.00 20.41  ? 24  PHE   B HA   1 
ATOM   4769 H  HB2  . PHE   B 1 27  ? -23.647 -12.086 -31.524 1.00 19.93  ? 24  PHE   B HB2  1 
ATOM   4770 H  HB3  . PHE   B 1 27  ? -24.823 -12.641 -30.610 1.00 19.93  ? 24  PHE   B HB3  1 
ATOM   4771 H  HD1  . PHE   B 1 27  ? -27.136 -12.675 -31.833 1.00 25.27  ? 24  PHE   B HD1  1 
ATOM   4772 H  HD2  . PHE   B 1 27  ? -23.632 -12.791 -33.701 1.00 26.86  ? 24  PHE   B HD2  1 
ATOM   4773 H  HE1  . PHE   B 1 27  ? -28.171 -13.551 -33.707 1.00 25.62  ? 24  PHE   B HE1  1 
ATOM   4774 H  HE2  . PHE   B 1 27  ? -24.687 -13.702 -35.569 1.00 29.12  ? 24  PHE   B HE2  1 
ATOM   4775 H  HZ   . PHE   B 1 27  ? -26.958 -14.097 -35.533 1.00 25.64  ? 24  PHE   B HZ   1 
ATOM   4776 N  N    . ILE   B 1 28  ? -25.540 -10.187 -28.708 1.00 16.52  ? 25  ILE   B N    1 
ATOM   4777 C  CA   . ILE   B 1 28  ? -25.295 -9.840  -27.314 1.00 17.97  ? 25  ILE   B CA   1 
ATOM   4778 C  C    . ILE   B 1 28  ? -25.586 -11.066 -26.451 1.00 15.53  ? 25  ILE   B C    1 
ATOM   4779 O  O    . ILE   B 1 28  ? -26.759 -11.497 -26.361 1.00 17.23  ? 25  ILE   B O    1 
ATOM   4780 C  CB   . ILE   B 1 28  ? -26.160 -8.653  -26.856 1.00 16.71  ? 25  ILE   B CB   1 
ATOM   4781 C  CG1  . ILE   B 1 28  ? -26.123 -7.481  -27.822 1.00 16.41  ? 25  ILE   B CG1  1 
ATOM   4782 C  CG2  . ILE   B 1 28  ? -25.704 -8.251  -25.419 1.00 17.00  ? 25  ILE   B CG2  1 
ATOM   4783 C  CD1  . ILE   B 1 28  ? -27.095 -6.367  -27.508 1.00 16.47  ? 25  ILE   B CD1  1 
ATOM   4784 H  H    . ILE   B 1 28  ? -26.371 -10.310 -28.892 1.00 19.86  ? 25  ILE   B H    1 
ATOM   4785 H  HA   . ILE   B 1 28  ? -24.359 -9.605  -27.215 1.00 21.61  ? 25  ILE   B HA   1 
ATOM   4786 H  HB   . ILE   B 1 28  ? -27.090 -8.927  -26.845 1.00 20.09  ? 25  ILE   B HB   1 
ATOM   4787 H  HG12 . ILE   B 1 28  ? -25.230 -7.102  -27.811 1.00 19.73  ? 25  ILE   B HG12 1 
ATOM   4788 H  HG13 . ILE   B 1 28  ? -26.333 -7.809  -28.711 1.00 19.73  ? 25  ILE   B HG13 1 
ATOM   4789 H  HG21 . ILE   B 1 28  ? -26.242 -7.503  -25.114 1.00 20.44  ? 25  ILE   B HG21 1 
ATOM   4790 H  HG22 . ILE   B 1 28  ? -25.826 -9.009  -24.825 1.00 20.44  ? 25  ILE   B HG22 1 
ATOM   4791 H  HG23 . ILE   B 1 28  ? -24.768 -7.997  -25.443 1.00 20.44  ? 25  ILE   B HG23 1 
ATOM   4792 H  HD11 . ILE   B 1 28  ? -27.123 -5.752  -28.257 1.00 19.81  ? 25  ILE   B HD11 1 
ATOM   4793 H  HD12 . ILE   B 1 28  ? -27.974 -6.747  -27.358 1.00 19.81  ? 25  ILE   B HD12 1 
ATOM   4794 H  HD13 . ILE   B 1 28  ? -26.795 -5.903  -26.710 1.00 19.81  ? 25  ILE   B HD13 1 
ATOM   4795 N  N    . PRO   B 1 29  ? -24.595 -11.611 -25.757 1.00 15.31  ? 26  PRO   B N    1 
ATOM   4796 C  CA   . PRO   B 1 29  ? -24.803 -12.837 -24.970 1.00 17.02  ? 26  PRO   B CA   1 
ATOM   4797 C  C    . PRO   B 1 29  ? -25.558 -12.582 -23.669 1.00 17.96  ? 26  PRO   B C    1 
ATOM   4798 O  O    . PRO   B 1 29  ? -25.534 -11.495 -23.095 1.00 17.72  ? 26  PRO   B O    1 
ATOM   4799 C  CB   . PRO   B 1 29  ? -23.366 -13.328 -24.664 1.00 19.14  ? 26  PRO   B CB   1 
ATOM   4800 C  CG   . PRO   B 1 29  ? -22.609 -12.036 -24.601 1.00 19.41  ? 26  PRO   B CG   1 
ATOM   4801 C  CD   . PRO   B 1 29  ? -23.177 -11.163 -25.681 1.00 18.13  ? 26  PRO   B CD   1 
ATOM   4802 H  HA   . PRO   B 1 29  ? -25.278 -13.493 -25.504 1.00 20.46  ? 26  PRO   B HA   1 
ATOM   4803 H  HB2  . PRO   B 1 29  ? -23.339 -13.801 -23.817 1.00 23.01  ? 26  PRO   B HB2  1 
ATOM   4804 H  HB3  . PRO   B 1 29  ? -23.040 -13.901 -25.375 1.00 23.01  ? 26  PRO   B HB3  1 
ATOM   4805 H  HG2  . PRO   B 1 29  ? -22.733 -11.627 -23.730 1.00 23.33  ? 26  PRO   B HG2  1 
ATOM   4806 H  HG3  . PRO   B 1 29  ? -21.666 -12.203 -24.758 1.00 23.33  ? 26  PRO   B HG3  1 
ATOM   4807 H  HD2  . PRO   B 1 29  ? -23.122 -10.227 -25.436 1.00 21.80  ? 26  PRO   B HD2  1 
ATOM   4808 H  HD3  . PRO   B 1 29  ? -22.721 -11.313 -26.524 1.00 21.80  ? 26  PRO   B HD3  1 
ATOM   4809 N  N    . GLY   B 1 30  ? -26.162 -13.661 -23.192 1.00 19.52  ? 27  GLY   B N    1 
ATOM   4810 C  CA   . GLY   B 1 30  ? -26.800 -13.704 -21.883 1.00 19.49  ? 27  GLY   B CA   1 
ATOM   4811 C  C    . GLY   B 1 30  ? -25.830 -14.036 -20.772 1.00 19.63  ? 27  GLY   B C    1 
ATOM   4812 O  O    . GLY   B 1 30  ? -24.712 -13.529 -20.733 1.00 21.28  ? 27  GLY   B O    1 
ATOM   4813 H  H    . GLY   B 1 30  ? -26.218 -14.406 -23.619 1.00 23.47  ? 27  GLY   B H    1 
ATOM   4814 H  HA2  . GLY   B 1 30  ? -27.197 -12.840 -21.693 1.00 23.42  ? 27  GLY   B HA2  1 
ATOM   4815 H  HA3  . GLY   B 1 30  ? -27.497 -14.379 -21.890 1.00 23.42  ? 27  GLY   B HA3  1 
ATOM   4816 N  N    . ALA   B 1 31  ? -26.255 -14.893 -19.847 1.00 23.34  ? 28  ALA   B N    1 
ATOM   4817 C  CA   . ALA   B 1 31  ? -25.528 -15.040 -18.595 1.00 23.93  ? 28  ALA   B CA   1 
ATOM   4818 C  C    . ALA   B 1 31  ? -24.117 -15.566 -18.784 1.00 26.62  ? 28  ALA   B C    1 
ATOM   4819 O  O    . ALA   B 1 31  ? -23.263 -15.349 -17.910 1.00 30.32  ? 28  ALA   B O    1 
ATOM   4820 C  CB   . ALA   B 1 31  ? -26.287 -15.976 -17.650 1.00 26.67  ? 28  ALA   B CB   1 
ATOM   4821 H  H    . ALA   B 1 31  ? -26.950 -15.393 -19.920 1.00 28.04  ? 28  ALA   B H    1 
ATOM   4822 H  HA   . ALA   B 1 31  ? -25.465 -14.159 -18.194 1.00 28.75  ? 28  ALA   B HA   1 
ATOM   4823 H  HB1  . ALA   B 1 31  ? -25.810 -16.029 -16.807 1.00 32.04  ? 28  ALA   B HB1  1 
ATOM   4824 H  HB2  . ALA   B 1 31  ? -27.178 -15.621 -17.504 1.00 32.04  ? 28  ALA   B HB2  1 
ATOM   4825 H  HB3  . ALA   B 1 31  ? -26.343 -16.855 -18.054 1.00 32.04  ? 28  ALA   B HB3  1 
ATOM   4826 N  N    . ASN   B 1 32  ? -23.849 -16.314 -19.861 1.00 25.04  ? 29  ASN   B N    1 
ATOM   4827 C  CA   . ASN   B 1 32  ? -22.480 -16.784 -20.070 1.00 24.72  ? 29  ASN   B CA   1 
ATOM   4828 C  C    . ASN   B 1 32  ? -21.534 -15.626 -20.350 1.00 23.99  ? 29  ASN   B C    1 
ATOM   4829 O  O    . ASN   B 1 32  ? -20.325 -15.768 -20.138 1.00 25.20  ? 29  ASN   B O    1 
ATOM   4830 C  CB   . ASN   B 1 32  ? -22.441 -17.800 -21.215 1.00 25.12  ? 29  ASN   B CB   1 
ATOM   4831 C  CG   . ASN   B 1 32  ? -22.723 -17.151 -22.554 1.00 28.33  ? 29  ASN   B CG   1 
ATOM   4832 O  OD1  . ASN   B 1 32  ? -23.852 -16.759 -22.832 1.00 29.94  ? 29  ASN   B OD1  1 
ATOM   4833 N  ND2  . ASN   B 1 32  ? -21.701 -17.043 -23.387 1.00 24.69  ? 29  ASN   B ND2  1 
ATOM   4834 H  H    . ASN   B 1 32  ? -24.419 -16.553 -20.459 1.00 30.09  ? 29  ASN   B H    1 
ATOM   4835 H  HA   . ASN   B 1 32  ? -22.168 -17.241 -19.272 1.00 29.71  ? 29  ASN   B HA   1 
ATOM   4836 H  HB2  . ASN   B 1 32  ? -21.561 -18.206 -21.253 1.00 30.19  ? 29  ASN   B HB2  1 
ATOM   4837 H  HB3  . ASN   B 1 32  ? -23.114 -18.482 -21.060 1.00 30.19  ? 29  ASN   B HB3  1 
ATOM   4838 H  HD21 . ASN   B 1 32  ? -21.813 -16.682 -24.160 1.00 29.67  ? 29  ASN   B HD21 1 
ATOM   4839 H  HD22 . ASN   B 1 32  ? -20.926 -17.335 -23.157 1.00 29.67  ? 29  ASN   B HD22 1 
ATOM   4840 N  N    . GLY   B 1 33  ? -22.056 -14.502 -20.835 1.00 21.69  ? 30  GLY   B N    1 
ATOM   4841 C  CA   . GLY   B 1 33  ? -21.327 -13.256 -20.958 1.00 22.79  ? 30  GLY   B CA   1 
ATOM   4842 C  C    . GLY   B 1 33  ? -20.412 -13.122 -22.158 1.00 20.73  ? 30  GLY   B C    1 
ATOM   4843 O  O    . GLY   B 1 33  ? -19.931 -12.006 -22.426 1.00 21.08  ? 30  GLY   B O    1 
ATOM   4844 H  H    . GLY   B 1 33  ? -22.867 -14.438 -21.112 1.00 26.08  ? 30  GLY   B H    1 
ATOM   4845 H  HA2  . GLY   B 1 33  ? -21.970 -12.531 -21.002 1.00 27.39  ? 30  GLY   B HA2  1 
ATOM   4846 H  HA3  . GLY   B 1 33  ? -20.780 -13.145 -20.164 1.00 27.39  ? 30  GLY   B HA3  1 
ATOM   4847 N  N    . THR   B 1 34  ? -20.209 -14.179 -22.925 1.00 21.96  ? 31  THR   B N    1 
ATOM   4848 C  CA   . THR   B 1 34  ? -19.163 -14.198 -23.945 1.00 22.41  ? 31  THR   B CA   1 
ATOM   4849 C  C    . THR   B 1 34  ? -19.704 -14.558 -25.322 1.00 22.05  ? 31  THR   B C    1 
ATOM   4850 O  O    . THR   B 1 34  ? -20.700 -15.286 -25.482 1.00 22.67  ? 31  THR   B O    1 
ATOM   4851 C  CB   . THR   B 1 34  ? -18.035 -15.146 -23.541 1.00 25.31  ? 31  THR   B CB   1 
ATOM   4852 O  OG1  . THR   B 1 34  ? -18.534 -16.478 -23.369 1.00 27.33  ? 31  THR   B OG1  1 
ATOM   4853 C  CG2  . THR   B 1 34  ? -17.420 -14.685 -22.200 1.00 28.92  ? 31  THR   B CG2  1 
ATOM   4854 H  H    . THR   B 1 34  ? -20.666 -14.906 -22.876 1.00 26.39  ? 31  THR   B H    1 
ATOM   4855 H  HA   . THR   B 1 34  ? -18.807 -13.301 -24.039 1.00 26.94  ? 31  THR   B HA   1 
ATOM   4856 H  HB   . THR   B 1 34  ? -17.358 -15.145 -24.235 1.00 30.42  ? 31  THR   B HB   1 
ATOM   4857 H  HG1  . THR   B 1 34  ? -18.930 -16.728 -24.067 1.00 32.84  ? 31  THR   B HG1  1 
ATOM   4858 H  HG21 . THR   B 1 34  ? -16.605 -15.179 -22.021 1.00 34.74  ? 31  THR   B HG21 1 
ATOM   4859 H  HG22 . THR   B 1 34  ? -17.211 -13.738 -22.239 1.00 34.74  ? 31  THR   B HG22 1 
ATOM   4860 H  HG23 . THR   B 1 34  ? -18.047 -14.839 -21.476 1.00 34.74  ? 31  THR   B HG23 1 
ATOM   4861 N  N    . GLY   B 1 35  ? -19.030 -14.005 -26.329 1.00 22.53  ? 32  GLY   B N    1 
ATOM   4862 C  CA   . GLY   B 1 35  ? -19.515 -14.111 -27.685 1.00 22.78  ? 32  GLY   B CA   1 
ATOM   4863 C  C    . GLY   B 1 35  ? -19.228 -15.432 -28.363 1.00 22.30  ? 32  GLY   B C    1 
ATOM   4864 O  O    . GLY   B 1 35  ? -19.847 -15.725 -29.397 1.00 21.83  ? 32  GLY   B O    1 
ATOM   4865 H  H    . GLY   B 1 35  ? -18.294 -13.568 -26.246 1.00 27.08  ? 32  GLY   B H    1 
ATOM   4866 H  HA2  . GLY   B 1 35  ? -20.477 -13.984 -27.682 1.00 27.38  ? 32  GLY   B HA2  1 
ATOM   4867 H  HA3  . GLY   B 1 35  ? -19.106 -13.411 -28.217 1.00 27.38  ? 32  GLY   B HA3  1 
ATOM   4868 N  N    . ASP   B 1 36  ? -18.307 -16.233 -27.820 1.00 23.09  ? 33  ASP   B N    1 
ATOM   4869 C  CA   . ASP   B 1 36  ? -17.977 -17.503 -28.445 1.00 23.44  ? 33  ASP   B CA   1 
ATOM   4870 C  C    . ASP   B 1 36  ? -19.184 -18.424 -28.606 1.00 23.97  ? 33  ASP   B C    1 
ATOM   4871 O  O    . ASP   B 1 36  ? -19.187 -19.254 -29.516 1.00 26.52  ? 33  ASP   B O    1 
ATOM   4872 C  CB   . ASP   B 1 36  ? -16.878 -18.234 -27.675 1.00 27.10  ? 33  ASP   B CB   1 
ATOM   4873 C  CG   . ASP   B 1 36  ? -17.100 -18.275 -26.177 1.00 32.10  ? 33  ASP   B CG   1 
ATOM   4874 O  OD1  . ASP   B 1 36  ? -16.129 -18.665 -25.480 1.00 39.21  ? 33  ASP   B OD1  1 
ATOM   4875 O  OD2  . ASP   B 1 36  ? -18.194 -17.905 -25.683 1.00 31.98  ? 33  ASP   B OD2  1 
ATOM   4876 H  H    . ASP   B 1 36  ? -17.869 -16.062 -27.101 1.00 27.76  ? 33  ASP   B H    1 
ATOM   4877 H  HA   . ASP   B 1 36  ? -17.634 -17.302 -29.329 1.00 28.17  ? 33  ASP   B HA   1 
ATOM   4878 H  HB2  . ASP   B 1 36  ? -16.832 -19.149 -27.992 1.00 32.57  ? 33  ASP   B HB2  1 
ATOM   4879 H  HB3  . ASP   B 1 36  ? -16.034 -17.784 -27.836 1.00 32.57  ? 33  ASP   B HB3  1 
ATOM   4880 N  N    . ILE   B 1 37  ? -20.228 -18.256 -27.787 1.00 25.05  ? 34  ILE   B N    1 
ATOM   4881 C  CA   . ILE   B 1 37  ? -21.421 -19.108 -27.881 1.00 22.55  ? 34  ILE   B CA   1 
ATOM   4882 C  C    . ILE   B 1 37  ? -22.144 -18.900 -29.210 1.00 24.97  ? 34  ILE   B C    1 
ATOM   4883 O  O    . ILE   B 1 37  ? -22.913 -19.769 -29.640 1.00 25.31  ? 34  ILE   B O    1 
ATOM   4884 C  CB   . ILE   B 1 37  ? -22.352 -18.836 -26.667 1.00 21.58  ? 34  ILE   B CB   1 
ATOM   4885 C  CG1  . ILE   B 1 37  ? -23.294 -20.054 -26.480 1.00 25.05  ? 34  ILE   B CG1  1 
ATOM   4886 C  CG2  . ILE   B 1 37  ? -23.063 -17.475 -26.760 1.00 23.95  ? 34  ILE   B CG2  1 
ATOM   4887 C  CD1  . ILE   B 1 37  ? -24.118 -20.003 -25.187 1.00 25.54  ? 34  ILE   B CD1  1 
ATOM   4888 H  H    . ILE   B 1 37  ? -20.273 -17.658 -27.170 1.00 30.10  ? 34  ILE   B H    1 
ATOM   4889 H  HA   . ILE   B 1 37  ? -21.156 -20.040 -27.845 1.00 27.10  ? 34  ILE   B HA   1 
ATOM   4890 H  HB   . ILE   B 1 37  ? -21.822 -18.753 -25.859 1.00 25.94  ? 34  ILE   B HB   1 
ATOM   4891 H  HG12 . ILE   B 1 37  ? -23.914 -20.088 -27.225 1.00 30.11  ? 34  ILE   B HG12 1 
ATOM   4892 H  HG13 . ILE   B 1 37  ? -22.758 -20.863 -26.458 1.00 30.11  ? 34  ILE   B HG13 1 
ATOM   4893 H  HG21 . ILE   B 1 37  ? -23.451 -17.263 -25.897 1.00 28.78  ? 34  ILE   B HG21 1 
ATOM   4894 H  HG22 . ILE   B 1 37  ? -22.415 -16.797 -27.008 1.00 28.78  ? 34  ILE   B HG22 1 
ATOM   4895 H  HG23 . ILE   B 1 37  ? -23.760 -17.528 -27.432 1.00 28.78  ? 34  ILE   B HG23 1 
ATOM   4896 H  HD11 . ILE   B 1 37  ? -24.669 -20.799 -25.132 1.00 30.69  ? 34  ILE   B HD11 1 
ATOM   4897 H  HD12 . ILE   B 1 37  ? -23.514 -19.966 -24.429 1.00 30.69  ? 34  ILE   B HD12 1 
ATOM   4898 H  HD13 . ILE   B 1 37  ? -24.679 -19.212 -25.202 1.00 30.69  ? 34  ILE   B HD13 1 
ATOM   4899 N  N    . PHE   B 1 38  ? -21.884 -17.783 -29.894 1.00 20.85  ? 35  PHE   B N    1 
ATOM   4900 C  CA   . PHE   B 1 38  ? -22.523 -17.476 -31.175 1.00 19.94  ? 35  PHE   B CA   1 
ATOM   4901 C  C    . PHE   B 1 38  ? -21.656 -17.866 -32.366 1.00 21.17  ? 35  PHE   B C    1 
ATOM   4902 O  O    . PHE   B 1 38  ? -22.063 -17.606 -33.505 1.00 22.06  ? 35  PHE   B O    1 
ATOM   4903 C  CB   . PHE   B 1 38  ? -22.807 -15.987 -31.256 1.00 18.94  ? 35  PHE   B CB   1 
ATOM   4904 C  CG   . PHE   B 1 38  ? -23.838 -15.495 -30.290 1.00 21.81  ? 35  PHE   B CG   1 
ATOM   4905 C  CD1  . PHE   B 1 38  ? -25.153 -15.878 -30.415 1.00 21.14  ? 35  PHE   B CD1  1 
ATOM   4906 C  CD2  . PHE   B 1 38  ? -23.477 -14.668 -29.232 1.00 22.59  ? 35  PHE   B CD2  1 
ATOM   4907 C  CE1  . PHE   B 1 38  ? -26.116 -15.433 -29.531 1.00 20.72  ? 35  PHE   B CE1  1 
ATOM   4908 C  CE2  . PHE   B 1 38  ? -24.440 -14.215 -28.338 1.00 22.44  ? 35  PHE   B CE2  1 
ATOM   4909 C  CZ   . PHE   B 1 38  ? -25.753 -14.603 -28.493 1.00 21.79  ? 35  PHE   B CZ   1 
ATOM   4910 H  H    . PHE   B 1 38  ? -21.332 -17.178 -29.631 1.00 25.06  ? 35  PHE   B H    1 
ATOM   4911 H  HA   . PHE   B 1 38  ? -23.361 -17.960 -31.229 1.00 23.97  ? 35  PHE   B HA   1 
ATOM   4912 H  HB2  . PHE   B 1 38  ? -21.985 -15.505 -31.076 1.00 22.77  ? 35  PHE   B HB2  1 
ATOM   4913 H  HB3  . PHE   B 1 38  ? -23.123 -15.782 -32.150 1.00 22.77  ? 35  PHE   B HB3  1 
ATOM   4914 H  HD1  . PHE   B 1 38  ? -25.398 -16.448 -31.108 1.00 25.41  ? 35  PHE   B HD1  1 
ATOM   4915 H  HD2  . PHE   B 1 38  ? -22.588 -14.417 -29.123 1.00 27.15  ? 35  PHE   B HD2  1 
ATOM   4916 H  HE1  . PHE   B 1 38  ? -27.004 -15.691 -29.636 1.00 24.91  ? 35  PHE   B HE1  1 
ATOM   4917 H  HE2  . PHE   B 1 38  ? -24.199 -13.652 -27.638 1.00 26.97  ? 35  PHE   B HE2  1 
ATOM   4918 H  HZ   . PHE   B 1 38  ? -26.398 -14.304 -27.893 1.00 26.20  ? 35  PHE   B HZ   1 
ATOM   4919 N  N    . LEU   B 1 39  ? -20.482 -18.454 -32.155 1.00 22.45  ? 36  LEU   B N    1 
ATOM   4920 C  CA   . LEU   B 1 39  ? -19.622 -18.648 -33.317 1.00 23.87  ? 36  LEU   B CA   1 
ATOM   4921 C  C    . LEU   B 1 39  ? -20.158 -19.713 -34.288 1.00 25.97  ? 36  LEU   B C    1 
ATOM   4922 O  O    . LEU   B 1 39  ? -20.028 -19.531 -35.501 1.00 27.71  ? 36  LEU   B O    1 
ATOM   4923 C  CB   . LEU   B 1 39  ? -18.191 -18.985 -32.879 1.00 24.50  ? 36  LEU   B CB   1 
ATOM   4924 C  CG   . LEU   B 1 39  ? -17.489 -17.756 -32.293 1.00 29.59  ? 36  LEU   B CG   1 
ATOM   4925 C  CD1  . LEU   B 1 39  ? -16.118 -18.083 -31.697 1.00 30.85  ? 36  LEU   B CD1  1 
ATOM   4926 C  CD2  . LEU   B 1 39  ? -17.352 -16.602 -33.288 1.00 32.82  ? 36  LEU   B CD2  1 
ATOM   4927 H  H    . LEU   B 1 39  ? -20.182 -18.730 -31.398 1.00 26.99  ? 36  LEU   B H    1 
ATOM   4928 H  HA   . LEU   B 1 39  ? -19.614 -17.815 -33.814 1.00 28.68  ? 36  LEU   B HA   1 
ATOM   4929 H  HB2  . LEU   B 1 39  ? -18.218 -19.677 -32.200 1.00 29.44  ? 36  LEU   B HB2  1 
ATOM   4930 H  HB3  . LEU   B 1 39  ? -17.684 -19.292 -33.647 1.00 29.44  ? 36  LEU   B HB3  1 
ATOM   4931 H  HG   . LEU   B 1 39  ? -18.069 -17.457 -31.575 1.00 35.55  ? 36  LEU   B HG   1 
ATOM   4932 H  HD11 . LEU   B 1 39  ? -15.721 -17.267 -31.354 1.00 37.06  ? 36  LEU   B HD11 1 
ATOM   4933 H  HD12 . LEU   B 1 39  ? -16.232 -18.723 -30.977 1.00 37.06  ? 36  LEU   B HD12 1 
ATOM   4934 H  HD13 . LEU   B 1 39  ? -15.554 -18.460 -32.390 1.00 37.06  ? 36  LEU   B HD13 1 
ATOM   4935 H  HD21 . LEU   B 1 39  ? -16.691 -15.975 -32.956 1.00 39.42  ? 36  LEU   B HD21 1 
ATOM   4936 H  HD22 . LEU   B 1 39  ? -17.070 -16.956 -34.146 1.00 39.42  ? 36  LEU   B HD22 1 
ATOM   4937 H  HD23 . LEU   B 1 39  ? -18.211 -16.159 -33.379 1.00 39.42  ? 36  LEU   B HD23 1 
ATOM   4938 N  N    . PRO   B 1 40  ? -20.761 -20.825 -33.838 1.00 24.19  ? 37  PRO   B N    1 
ATOM   4939 C  CA   . PRO   B 1 40  ? -21.369 -21.731 -34.835 1.00 25.68  ? 37  PRO   B CA   1 
ATOM   4940 C  C    . PRO   B 1 40  ? -22.462 -21.050 -35.642 1.00 23.01  ? 37  PRO   B C    1 
ATOM   4941 O  O    . PRO   B 1 40  ? -22.584 -21.330 -36.858 1.00 26.90  ? 37  PRO   B O    1 
ATOM   4942 C  CB   . PRO   B 1 40  ? -21.897 -22.898 -33.987 1.00 29.00  ? 37  PRO   B CB   1 
ATOM   4943 C  CG   . PRO   B 1 40  ? -20.965 -22.921 -32.789 1.00 26.20  ? 37  PRO   B CG   1 
ATOM   4944 C  CD   . PRO   B 1 40  ? -20.735 -21.437 -32.494 1.00 24.84  ? 37  PRO   B CD   1 
ATOM   4945 H  HA   . PRO   B 1 40  ? -20.692 -22.079 -35.436 1.00 30.85  ? 37  PRO   B HA   1 
ATOM   4946 H  HB2  . PRO   B 1 40  ? -22.813 -22.730 -33.717 1.00 34.84  ? 37  PRO   B HB2  1 
ATOM   4947 H  HB3  . PRO   B 1 40  ? -21.846 -23.727 -34.488 1.00 34.84  ? 37  PRO   B HB3  1 
ATOM   4948 H  HG2  . PRO   B 1 40  ? -21.389 -23.368 -32.040 1.00 31.48  ? 37  PRO   B HG2  1 
ATOM   4949 H  HG3  . PRO   B 1 40  ? -20.135 -23.369 -33.016 1.00 31.48  ? 37  PRO   B HG3  1 
ATOM   4950 H  HD2  . PRO   B 1 40  ? -21.444 -21.080 -31.937 1.00 29.85  ? 37  PRO   B HD2  1 
ATOM   4951 H  HD3  . PRO   B 1 40  ? -19.875 -21.298 -32.067 1.00 29.85  ? 37  PRO   B HD3  1 
ATOM   4952 N  N    . LEU   B 1 41  ? -23.253 -20.194 -34.996 1.00 22.18  ? 38  LEU   B N    1 
ATOM   4953 C  CA   . LEU   B 1 41  ? -24.262 -19.431 -35.740 1.00 23.10  ? 38  LEU   B CA   1 
ATOM   4954 C  C    . LEU   B 1 41  ? -23.598 -18.444 -36.705 1.00 24.23  ? 38  LEU   B C    1 
ATOM   4955 O  O    . LEU   B 1 41  ? -24.037 -18.302 -37.859 1.00 24.29  ? 38  LEU   B O    1 
ATOM   4956 C  CB   . LEU   B 1 41  ? -25.202 -18.718 -34.780 1.00 22.62  ? 38  LEU   B CB   1 
ATOM   4957 C  CG   . LEU   B 1 41  ? -26.247 -17.811 -35.409 1.00 20.40  ? 38  LEU   B CG   1 
ATOM   4958 C  CD1  . LEU   B 1 41  ? -27.136 -18.627 -36.332 1.00 23.06  ? 38  LEU   B CD1  1 
ATOM   4959 C  CD2  . LEU   B 1 41  ? -27.017 -17.154 -34.314 1.00 19.36  ? 38  LEU   B CD2  1 
ATOM   4960 H  H    . LEU   B 1 41  ? -23.230 -20.038 -34.151 1.00 26.66  ? 38  LEU   B H    1 
ATOM   4961 H  HA   . LEU   B 1 41  ? -24.801 -20.044 -36.265 1.00 27.77  ? 38  LEU   B HA   1 
ATOM   4962 H  HB2  . LEU   B 1 41  ? -25.678 -19.391 -34.268 1.00 27.19  ? 38  LEU   B HB2  1 
ATOM   4963 H  HB3  . LEU   B 1 41  ? -24.666 -18.168 -34.187 1.00 27.19  ? 38  LEU   B HB3  1 
ATOM   4964 H  HG   . LEU   B 1 41  ? -25.842 -17.117 -35.952 1.00 24.52  ? 38  LEU   B HG   1 
ATOM   4965 H  HD11 . LEU   B 1 41  ? -27.839 -18.056 -36.679 1.00 27.71  ? 38  LEU   B HD11 1 
ATOM   4966 H  HD12 . LEU   B 1 41  ? -26.600 -18.973 -37.062 1.00 27.71  ? 38  LEU   B HD12 1 
ATOM   4967 H  HD13 . LEU   B 1 41  ? -27.524 -19.361 -35.829 1.00 27.71  ? 38  LEU   B HD13 1 
ATOM   4968 H  HD21 . LEU   B 1 41  ? -27.697 -16.584 -34.704 1.00 23.27  ? 38  LEU   B HD21 1 
ATOM   4969 H  HD22 . LEU   B 1 41  ? -27.433 -17.838 -33.766 1.00 23.27  ? 38  LEU   B HD22 1 
ATOM   4970 H  HD23 . LEU   B 1 41  ? -26.409 -16.624 -33.775 1.00 23.27  ? 38  LEU   B HD23 1 
ATOM   4971 N  N    . ALA   B 1 42  ? -22.534 -17.768 -36.263 1.00 24.11  ? 39  ALA   B N    1 
ATOM   4972 C  CA   . ALA   B 1 42  ? -21.839 -16.824 -37.141 1.00 25.34  ? 39  ALA   B CA   1 
ATOM   4973 C  C    . ALA   B 1 42  ? -21.359 -17.502 -38.414 1.00 23.86  ? 39  ALA   B C    1 
ATOM   4974 O  O    . ALA   B 1 42  ? -21.384 -16.910 -39.494 1.00 28.56  ? 39  ALA   B O    1 
ATOM   4975 C  CB   . ALA   B 1 42  ? -20.633 -16.205 -36.422 1.00 24.26  ? 39  ALA   B CB   1 
ATOM   4976 H  H    . ALA   B 1 42  ? -22.201 -17.835 -35.473 1.00 28.98  ? 39  ALA   B H    1 
ATOM   4977 H  HA   . ALA   B 1 42  ? -22.463 -16.119 -37.371 1.00 30.45  ? 39  ALA   B HA   1 
ATOM   4978 H  HB1  . ALA   B 1 42  ? -20.350 -15.412 -36.904 1.00 29.15  ? 39  ALA   B HB1  1 
ATOM   4979 H  HB2  . ALA   B 1 42  ? -20.892 -15.967 -35.518 1.00 29.15  ? 39  ALA   B HB2  1 
ATOM   4980 H  HB3  . ALA   B 1 42  ? -19.911 -16.853 -36.399 1.00 29.15  ? 39  ALA   B HB3  1 
ATOM   4981 N  N    . GLU   B 1 43  ? -20.893 -18.745 -38.305 1.00 24.62  ? 40  GLU   B N    1 
ATOM   4982 C  CA   . GLU   B 1 43  ? -20.438 -19.486 -39.468 1.00 29.18  ? 40  GLU   B CA   1 
ATOM   4983 C  C    . GLU   B 1 43  ? -21.547 -19.666 -40.503 1.00 26.04  ? 40  GLU   B C    1 
ATOM   4984 O  O    . GLU   B 1 43  ? -21.279 -19.698 -41.704 1.00 33.01  ? 40  GLU   B O    1 
ATOM   4985 C  CB   . GLU   B 1 43  ? -19.898 -20.835 -38.986 1.00 31.00  ? 40  GLU   B CB   1 
ATOM   4986 C  CG   . GLU   B 1 43  ? -18.437 -20.772 -38.455 1.00 45.79  ? 40  GLU   B CG   1 
ATOM   4987 C  CD   . GLU   B 1 43  ? -17.445 -20.058 -39.394 1.00 50.76  ? 40  GLU   B CD   1 
ATOM   4988 O  OE1  . GLU   B 1 43  ? -17.343 -20.479 -40.565 1.00 47.75  ? 40  GLU   B OE1  1 
ATOM   4989 O  OE2  . GLU   B 1 43  ? -16.761 -19.100 -38.969 1.00 41.03  ? 40  GLU   B OE2  1 
ATOM   4990 H  H    . GLU   B 1 43  ? -20.832 -19.180 -37.566 1.00 29.59  ? 40  GLU   B H    1 
ATOM   4991 H  HA   . GLU   B 1 43  ? -19.725 -19.005 -39.916 1.00 35.05  ? 40  GLU   B HA   1 
ATOM   4992 H  HB2  . GLU   B 1 43  ? -20.461 -21.157 -38.265 1.00 37.24  ? 40  GLU   B HB2  1 
ATOM   4993 H  HB3  . GLU   B 1 43  ? -19.917 -21.461 -39.727 1.00 37.24  ? 40  GLU   B HB3  1 
ATOM   4994 H  HG2  . GLU   B 1 43  ? -18.435 -20.294 -37.611 1.00 54.99  ? 40  GLU   B HG2  1 
ATOM   4995 H  HG3  . GLU   B 1 43  ? -18.116 -21.678 -38.325 1.00 54.99  ? 40  GLU   B HG3  1 
ATOM   4996 N  N    . GLN   B 1 44  ? -22.793 -19.790 -40.063 1.00 26.62  ? 41  GLN   B N    1 
ATOM   4997 C  CA   . GLN   B 1 44  ? -23.924 -19.938 -40.963 1.00 25.82  ? 41  GLN   B CA   1 
ATOM   4998 C  C    . GLN   B 1 44  ? -24.374 -18.627 -41.585 1.00 27.90  ? 41  GLN   B C    1 
ATOM   4999 O  O    . GLN   B 1 44  ? -25.048 -18.650 -42.623 1.00 31.74  ? 41  GLN   B O    1 
ATOM   5000 C  CB   . GLN   B 1 44  ? -25.092 -20.561 -40.183 1.00 30.02  ? 41  GLN   B CB   1 
ATOM   5001 C  CG   . GLN   B 1 44  ? -24.711 -21.914 -39.605 1.00 27.43  ? 41  GLN   B CG   1 
ATOM   5002 C  CD   . GLN   B 1 44  ? -24.477 -22.949 -40.676 1.00 35.92  ? 41  GLN   B CD   1 
ATOM   5003 O  OE1  . GLN   B 1 44  ? -25.210 -23.009 -41.668 1.00 37.41  ? 41  GLN   B OE1  1 
ATOM   5004 N  NE2  . GLN   B 1 44  ? -23.416 -23.719 -40.522 1.00 40.52  ? 41  GLN   B NE2  1 
ATOM   5005 H  H    . GLN   B 1 44  ? -23.013 -19.792 -39.231 1.00 31.98  ? 41  GLN   B H    1 
ATOM   5006 H  HA   . GLN   B 1 44  ? -23.675 -20.525 -41.694 1.00 31.03  ? 41  GLN   B HA   1 
ATOM   5007 H  HB2  . GLN   B 1 44  ? -25.340 -19.974 -39.452 1.00 36.06  ? 41  GLN   B HB2  1 
ATOM   5008 H  HB3  . GLN   B 1 44  ? -25.847 -20.685 -40.780 1.00 36.06  ? 41  GLN   B HB3  1 
ATOM   5009 H  HG2  . GLN   B 1 44  ? -23.893 -21.821 -39.092 1.00 32.95  ? 41  GLN   B HG2  1 
ATOM   5010 H  HG3  . GLN   B 1 44  ? -25.428 -22.228 -39.033 1.00 32.95  ? 41  GLN   B HG3  1 
ATOM   5011 H  HE21 . GLN   B 1 44  ? -22.904 -23.614 -39.839 1.00 48.66  ? 41  GLN   B HE21 1 
ATOM   5012 H  HE22 . GLN   B 1 44  ? -23.237 -24.326 -41.104 1.00 48.66  ? 41  GLN   B HE22 1 
ATOM   5013 N  N    . LEU   B 1 45  ? -24.012 -17.505 -40.980 1.00 24.69  ? 42  LEU   B N    1 
ATOM   5014 C  CA   . LEU   B 1 45  ? -24.466 -16.182 -41.382 1.00 23.94  ? 42  LEU   B CA   1 
ATOM   5015 C  C    . LEU   B 1 45  ? -23.407 -15.360 -42.099 1.00 27.60  ? 42  LEU   B C    1 
ATOM   5016 O  O    . LEU   B 1 45  ? -23.731 -14.287 -42.610 1.00 25.58  ? 42  LEU   B O    1 
ATOM   5017 C  CB   . LEU   B 1 45  ? -24.948 -15.398 -40.150 1.00 23.14  ? 42  LEU   B CB   1 
ATOM   5018 C  CG   . LEU   B 1 45  ? -26.187 -15.979 -39.476 1.00 23.63  ? 42  LEU   B CG   1 
ATOM   5019 C  CD1  . LEU   B 1 45  ? -26.490 -15.214 -38.218 1.00 25.31  ? 42  LEU   B CD1  1 
ATOM   5020 C  CD2  . LEU   B 1 45  ? -27.327 -15.945 -40.467 1.00 25.92  ? 42  LEU   B CD2  1 
ATOM   5021 H  H    . LEU   B 1 45  ? -23.481 -17.483 -40.304 1.00 29.67  ? 42  LEU   B H    1 
ATOM   5022 H  HA   . LEU   B 1 45  ? -25.214 -16.289 -41.990 1.00 28.77  ? 42  LEU   B HA   1 
ATOM   5023 H  HB2  . LEU   B 1 45  ? -24.234 -15.387 -39.493 1.00 27.81  ? 42  LEU   B HB2  1 
ATOM   5024 H  HB3  . LEU   B 1 45  ? -25.160 -14.492 -40.424 1.00 27.81  ? 42  LEU   B HB3  1 
ATOM   5025 H  HG   . LEU   B 1 45  ? -26.051 -16.901 -39.209 1.00 28.39  ? 42  LEU   B HG   1 
ATOM   5026 H  HD11 . LEU   B 1 45  ? -27.322 -15.540 -37.842 1.00 30.41  ? 42  LEU   B HD11 1 
ATOM   5027 H  HD12 . LEU   B 1 45  ? -25.767 -15.347 -37.586 1.00 30.41  ? 42  LEU   B HD12 1 
ATOM   5028 H  HD13 . LEU   B 1 45  ? -26.571 -14.271 -38.434 1.00 30.41  ? 42  LEU   B HD13 1 
ATOM   5029 H  HD21 . LEU   B 1 45  ? -28.162 -16.081 -39.992 1.00 31.15  ? 42  LEU   B HD21 1 
ATOM   5030 H  HD22 . LEU   B 1 45  ? -27.335 -15.082 -40.910 1.00 31.15  ? 42  LEU   B HD22 1 
ATOM   5031 H  HD23 . LEU   B 1 45  ? -27.199 -16.651 -41.120 1.00 31.15  ? 42  LEU   B HD23 1 
ATOM   5032 N  N    . LYS   B 1 46  ? -22.163 -15.834 -42.147 1.00 26.74  ? 43  LYS   B N    1 
ATOM   5033 C  CA   . LYS   B 1 46  ? -21.035 -14.973 -42.503 1.00 30.24  ? 43  LYS   B CA   1 
ATOM   5034 C  C    . LYS   B 1 46  ? -21.030 -14.557 -43.966 1.00 31.12  ? 43  LYS   B C    1 
ATOM   5035 O  O    . LYS   B 1 46  ? -20.314 -13.609 -44.313 1.00 30.75  ? 43  LYS   B O    1 
ATOM   5036 C  CB   . LYS   B 1 46  ? -19.728 -15.677 -42.141 1.00 29.35  ? 43  LYS   B CB   1 
ATOM   5037 C  CG   . LYS   B 1 46  ? -19.471 -16.899 -42.898 1.00 32.24  ? 43  LYS   B CG   1 
ATOM   5038 C  CD   . LYS   B 1 46  ? -18.067 -17.427 -42.688 1.00 44.06  ? 43  LYS   B CD   1 
ATOM   5039 C  CE   . LYS   B 1 46  ? -17.972 -18.865 -43.145 1.00 40.78  ? 43  LYS   B CE   1 
ATOM   5040 N  NZ   . LYS   B 1 46  ? -16.698 -19.473 -42.671 1.00 56.16  ? 43  LYS   B NZ   1 
ATOM   5041 H  H    . LYS   B 1 46  ? -21.945 -16.649 -41.979 1.00 32.13  ? 43  LYS   B H    1 
ATOM   5042 H  HA   . LYS   B 1 46  ? -21.095 -14.155 -41.986 1.00 36.34  ? 43  LYS   B HA   1 
ATOM   5043 H  HB2  . LYS   B 1 46  ? -18.992 -15.068 -42.309 1.00 35.26  ? 43  LYS   B HB2  1 
ATOM   5044 H  HB3  . LYS   B 1 46  ? -19.754 -15.914 -41.201 1.00 35.26  ? 43  LYS   B HB3  1 
ATOM   5045 H  HG2  . LYS   B 1 46  ? -20.095 -17.585 -42.615 1.00 38.72  ? 43  LYS   B HG2  1 
ATOM   5046 H  HG3  . LYS   B 1 46  ? -19.584 -16.717 -43.844 1.00 38.72  ? 43  LYS   B HG3  1 
ATOM   5047 H  HD2  . LYS   B 1 46  ? -17.439 -16.896 -43.203 1.00 52.91  ? 43  LYS   B HD2  1 
ATOM   5048 H  HD3  . LYS   B 1 46  ? -17.841 -17.386 -41.746 1.00 52.91  ? 43  LYS   B HD3  1 
ATOM   5049 H  HE2  . LYS   B 1 46  ? -18.713 -19.372 -42.779 1.00 48.98  ? 43  LYS   B HE2  1 
ATOM   5050 H  HE3  . LYS   B 1 46  ? -17.992 -18.901 -44.114 1.00 48.98  ? 43  LYS   B HE3  1 
ATOM   5051 H  HZ1  . LYS   B 1 46  ? -16.664 -20.331 -42.905 1.00 67.43  ? 43  LYS   B HZ1  1 
ATOM   5052 H  HZ2  . LYS   B 1 46  ? -16.005 -19.047 -43.032 1.00 67.43  ? 43  LYS   B HZ2  1 
ATOM   5053 H  HZ3  . LYS   B 1 46  ? -16.643 -19.413 -41.785 1.00 67.43  ? 43  LYS   B HZ3  1 
ATOM   5054 N  N    . ASP   B 1 47  ? -21.795 -15.228 -44.830 1.00 33.66  ? 44  ASP   B N    1 
ATOM   5055 C  CA   . ASP   B 1 47  ? -21.917 -14.784 -46.208 1.00 33.76  ? 44  ASP   B CA   1 
ATOM   5056 C  C    . ASP   B 1 47  ? -22.917 -13.645 -46.385 1.00 30.66  ? 44  ASP   B C    1 
ATOM   5057 O  O    . ASP   B 1 47  ? -23.010 -13.091 -47.491 1.00 33.84  ? 44  ASP   B O    1 
ATOM   5058 C  CB   . ASP   B 1 47  ? -22.337 -15.970 -47.089 1.00 37.16  ? 44  ASP   B CB   1 
ATOM   5059 C  CG   . ASP   B 1 47  ? -21.358 -17.141 -46.978 1.00 51.56  ? 44  ASP   B CG   1 
ATOM   5060 O  OD1  . ASP   B 1 47  ? -21.818 -18.282 -46.731 1.00 60.82  ? 44  ASP   B OD1  1 
ATOM   5061 O  OD2  . ASP   B 1 47  ? -20.140 -16.913 -47.111 1.00 54.82  ? 44  ASP   B OD2  1 
ATOM   5062 H  H    . ASP   B 1 47  ? -22.246 -15.935 -44.639 1.00 40.43  ? 44  ASP   B H    1 
ATOM   5063 H  HA   . ASP   B 1 47  ? -21.054 -14.462 -46.510 1.00 40.55  ? 44  ASP   B HA   1 
ATOM   5064 H  HB2  . ASP   B 1 47  ? -23.213 -16.280 -46.811 1.00 44.63  ? 44  ASP   B HB2  1 
ATOM   5065 H  HB3  . ASP   B 1 47  ? -22.365 -15.686 -48.016 1.00 44.63  ? 44  ASP   B HB3  1 
ATOM   5066 N  N    . HIS   B 1 48  ? -23.668 -13.303 -45.356 1.00 27.28  ? 45  HIS   B N    1 
ATOM   5067 C  CA   . HIS   B 1 48  ? -24.729 -12.311 -45.474 1.00 29.40  ? 45  HIS   B CA   1 
ATOM   5068 C  C    . HIS   B 1 48  ? -24.562 -11.121 -44.551 1.00 26.06  ? 45  HIS   B C    1 
ATOM   5069 O  O    . HIS   B 1 48  ? -25.087 -10.044 -44.868 1.00 28.65  ? 45  HIS   B O    1 
ATOM   5070 C  CB   . HIS   B 1 48  ? -26.121 -12.926 -45.161 1.00 25.72  ? 45  HIS   B CB   1 
ATOM   5071 C  CG   . HIS   B 1 48  ? -26.511 -14.061 -46.056 1.00 29.82  ? 45  HIS   B CG   1 
ATOM   5072 N  ND1  . HIS   B 1 48  ? -26.115 -15.362 -45.833 1.00 39.10  ? 45  HIS   B ND1  1 
ATOM   5073 C  CD2  . HIS   B 1 48  ? -27.294 -14.092 -47.156 1.00 33.71  ? 45  HIS   B CD2  1 
ATOM   5074 C  CE1  . HIS   B 1 48  ? -26.624 -16.147 -46.766 1.00 38.85  ? 45  HIS   B CE1  1 
ATOM   5075 N  NE2  . HIS   B 1 48  ? -27.333 -15.400 -47.590 1.00 39.09  ? 45  HIS   B NE2  1 
ATOM   5076 H  H    . HIS   B 1 48  ? -23.585 -13.634 -44.567 1.00 32.78  ? 45  HIS   B H    1 
ATOM   5077 H  HA   . HIS   B 1 48  ? -24.729 -12.005 -46.395 1.00 35.32  ? 45  HIS   B HA   1 
ATOM   5078 H  HB2  . HIS   B 1 48  ? -26.114 -13.259 -44.250 1.00 30.90  ? 45  HIS   B HB2  1 
ATOM   5079 H  HB3  . HIS   B 1 48  ? -26.793 -12.233 -45.256 1.00 30.90  ? 45  HIS   B HB3  1 
ATOM   5080 H  HD2  . HIS   B 1 48  ? -27.726 -13.367 -47.548 1.00 40.49  ? 45  HIS   B HD2  1 
ATOM   5081 H  HE1  . HIS   B 1 48  ? -26.503 -17.067 -46.829 1.00 46.66  ? 45  HIS   B HE1  1 
ATOM   5082 H  HE2  . HIS   B 1 48  ? -27.752 -15.684 -48.286 1.00 46.95  ? 45  HIS   B HE2  1 
ATOM   5083 N  N    . PHE   B 1 49  ? -23.866 -11.288 -43.403 1.00 23.89  ? 46  PHE   B N    1 
ATOM   5084 C  CA   . PHE   B 1 49  ? -23.664 -10.238 -42.422 1.00 23.72  ? 46  PHE   B CA   1 
ATOM   5085 C  C    . PHE   B 1 49  ? -22.214 -10.204 -41.971 1.00 25.60  ? 46  PHE   B C    1 
ATOM   5086 O  O    . PHE   B 1 49  ? -21.531 -11.230 -41.974 1.00 24.58  ? 46  PHE   B O    1 
ATOM   5087 C  CB   . PHE   B 1 49  ? -24.509 -10.466 -41.162 1.00 22.64  ? 46  PHE   B CB   1 
ATOM   5088 C  CG   . PHE   B 1 49  ? -25.969 -10.452 -41.410 1.00 22.78  ? 46  PHE   B CG   1 
ATOM   5089 C  CD1  . PHE   B 1 49  ? -26.669 -9.252  -41.342 1.00 27.48  ? 46  PHE   B CD1  1 
ATOM   5090 C  CD2  . PHE   B 1 49  ? -26.670 -11.629 -41.660 1.00 24.29  ? 46  PHE   B CD2  1 
ATOM   5091 C  CE1  . PHE   B 1 49  ? -28.050 -9.222  -41.537 1.00 30.81  ? 46  PHE   B CE1  1 
ATOM   5092 C  CE2  . PHE   B 1 49  ? -28.051 -11.604 -41.873 1.00 27.88  ? 46  PHE   B CE2  1 
ATOM   5093 C  CZ   . PHE   B 1 49  ? -28.733 -10.399 -41.804 1.00 28.69  ? 46  PHE   B CZ   1 
ATOM   5094 H  H    . PHE   B 1 49  ? -23.497 -12.031 -43.178 1.00 28.71  ? 46  PHE   B H    1 
ATOM   5095 H  HA   . PHE   B 1 49  ? -23.900 -9.395  -42.840 1.00 28.51  ? 46  PHE   B HA   1 
ATOM   5096 H  HB2  . PHE   B 1 49  ? -24.282 -11.331 -40.786 1.00 27.21  ? 46  PHE   B HB2  1 
ATOM   5097 H  HB3  . PHE   B 1 49  ? -24.311 -9.764  -40.522 1.00 27.21  ? 46  PHE   B HB3  1 
ATOM   5098 H  HD1  . PHE   B 1 49  ? -26.212 -8.461  -41.166 1.00 33.02  ? 46  PHE   B HD1  1 
ATOM   5099 H  HD2  . PHE   B 1 49  ? -26.214 -12.439 -41.687 1.00 29.19  ? 46  PHE   B HD2  1 
ATOM   5100 H  HE1  . PHE   B 1 49  ? -28.511 -8.416  -41.488 1.00 37.01  ? 46  PHE   B HE1  1 
ATOM   5101 H  HE2  . PHE   B 1 49  ? -28.510 -12.391 -42.059 1.00 33.50  ? 46  PHE   B HE2  1 
ATOM   5102 H  HZ   . PHE   B 1 49  ? -29.653 -10.379 -41.937 1.00 34.47  ? 46  PHE   B HZ   1 
ATOM   5103 N  N    . THR   B 1 50  ? -21.755 -9.023  -41.555 1.00 24.25  ? 47  THR   B N    1 
ATOM   5104 C  CA   . THR   B 1 50  ? -20.570 -8.919  -40.711 1.00 24.26  ? 47  THR   B CA   1 
ATOM   5105 C  C    . THR   B 1 50  ? -21.034 -9.242  -39.300 1.00 24.55  ? 47  THR   B C    1 
ATOM   5106 O  O    . THR   B 1 50  ? -21.653 -8.408  -38.636 1.00 24.92  ? 47  THR   B O    1 
ATOM   5107 C  CB   . THR   B 1 50  ? -19.958 -7.535  -40.787 1.00 25.49  ? 47  THR   B CB   1 
ATOM   5108 O  OG1  . THR   B 1 50  ? -19.499 -7.304  -42.111 1.00 26.72  ? 47  THR   B OG1  1 
ATOM   5109 C  CG2  . THR   B 1 50  ? -18.796 -7.446  -39.840 1.00 28.86  ? 47  THR   B CG2  1 
ATOM   5110 H  H    . THR   B 1 50  ? -22.116 -8.267  -41.750 1.00 29.14  ? 47  THR   B H    1 
ATOM   5111 H  HA   . THR   B 1 50  ? -19.889 -9.547  -40.998 1.00 29.16  ? 47  THR   B HA   1 
ATOM   5112 H  HB   . THR   B 1 50  ? -20.613 -6.861  -40.546 1.00 30.63  ? 47  THR   B HB   1 
ATOM   5113 H  HG1  . THR   B 1 50  ? -20.132 -7.398  -42.655 1.00 32.11  ? 47  THR   B HG1  1 
ATOM   5114 H  HG21 . THR   B 1 50  ? -18.284 -6.641  -40.017 1.00 34.67  ? 47  THR   B HG21 1 
ATOM   5115 H  HG22 . THR   B 1 50  ? -19.115 -7.422  -38.924 1.00 34.67  ? 47  THR   B HG22 1 
ATOM   5116 H  HG23 . THR   B 1 50  ? -18.218 -8.217  -39.952 1.00 34.67  ? 47  THR   B HG23 1 
ATOM   5117 N  N    . VAL   B 1 51  ? -20.798 -10.456 -38.851 1.00 21.79  ? 48  VAL   B N    1 
ATOM   5118 C  CA   . VAL   B 1 51  ? -21.283 -10.889 -37.542 1.00 21.62  ? 48  VAL   B CA   1 
ATOM   5119 C  C    . VAL   B 1 51  ? -20.292 -10.453 -36.473 1.00 22.67  ? 48  VAL   B C    1 
ATOM   5120 O  O    . VAL   B 1 51  ? -19.089 -10.759 -36.544 1.00 22.79  ? 48  VAL   B O    1 
ATOM   5121 C  CB   . VAL   B 1 51  ? -21.492 -12.409 -37.505 1.00 21.23  ? 48  VAL   B CB   1 
ATOM   5122 C  CG1  . VAL   B 1 51  ? -22.028 -12.786 -36.155 1.00 24.19  ? 48  VAL   B CG1  1 
ATOM   5123 C  CG2  . VAL   B 1 51  ? -22.401 -12.857 -38.621 1.00 24.14  ? 48  VAL   B CG2  1 
ATOM   5124 H  H    . VAL   B 1 51  ? -20.358 -11.057 -39.282 1.00 26.19  ? 48  VAL   B H    1 
ATOM   5125 H  HA   . VAL   B 1 51  ? -22.133 -10.456 -37.366 1.00 25.99  ? 48  VAL   B HA   1 
ATOM   5126 H  HB   . VAL   B 1 51  ? -20.649 -12.868 -37.642 1.00 25.52  ? 48  VAL   B HB   1 
ATOM   5127 H  HG11 . VAL   B 1 51  ? -22.339 -13.704 -36.184 1.00 29.07  ? 48  VAL   B HG11 1 
ATOM   5128 H  HG12 . VAL   B 1 51  ? -21.320 -12.697 -35.498 1.00 29.07  ? 48  VAL   B HG12 1 
ATOM   5129 H  HG13 . VAL   B 1 51  ? -22.764 -12.195 -35.931 1.00 29.07  ? 48  VAL   B HG13 1 
ATOM   5130 H  HG21 . VAL   B 1 51  ? -22.496 -13.822 -38.583 1.00 29.01  ? 48  VAL   B HG21 1 
ATOM   5131 H  HG22 . VAL   B 1 51  ? -23.268 -12.435 -38.511 1.00 29.01  ? 48  VAL   B HG22 1 
ATOM   5132 H  HG23 . VAL   B 1 51  ? -22.011 -12.597 -39.470 1.00 29.01  ? 48  VAL   B HG23 1 
ATOM   5133 N  N    . VAL   B 1 52  ? -20.813 -9.793  -35.442 1.00 19.80  ? 49  VAL   B N    1 
ATOM   5134 C  CA   . VAL   B 1 52  ? -20.035 -9.271  -34.331 1.00 19.80  ? 49  VAL   B CA   1 
ATOM   5135 C  C    . VAL   B 1 52  ? -20.603 -9.896  -33.076 1.00 22.82  ? 49  VAL   B C    1 
ATOM   5136 O  O    . VAL   B 1 52  ? -21.776 -9.674  -32.746 1.00 22.97  ? 49  VAL   B O    1 
ATOM   5137 C  CB   . VAL   B 1 52  ? -20.117 -7.746  -34.275 1.00 21.87  ? 49  VAL   B CB   1 
ATOM   5138 C  CG1  . VAL   B 1 52  ? -19.521 -7.218  -33.012 1.00 21.09  ? 49  VAL   B CG1  1 
ATOM   5139 C  CG2  . VAL   B 1 52  ? -19.465 -7.142  -35.500 1.00 23.33  ? 49  VAL   B CG2  1 
ATOM   5140 H  H    . VAL   B 1 52  ? -21.654 -9.629  -35.364 1.00 23.80  ? 49  VAL   B H    1 
ATOM   5141 H  HA   . VAL   B 1 52  ? -19.103 -9.525  -34.412 1.00 23.80  ? 49  VAL   B HA   1 
ATOM   5142 H  HB   . VAL   B 1 52  ? -21.050 -7.480  -34.274 1.00 26.29  ? 49  VAL   B HB   1 
ATOM   5143 H  HG11 . VAL   B 1 52  ? -19.381 -6.263  -33.104 1.00 25.34  ? 49  VAL   B HG11 1 
ATOM   5144 H  HG12 . VAL   B 1 52  ? -20.129 -7.394  -32.277 1.00 25.34  ? 49  VAL   B HG12 1 
ATOM   5145 H  HG13 . VAL   B 1 52  ? -18.673 -7.663  -32.853 1.00 25.34  ? 49  VAL   B HG13 1 
ATOM   5146 H  HG21 . VAL   B 1 52  ? -19.571 -6.178  -35.472 1.00 28.04  ? 49  VAL   B HG21 1 
ATOM   5147 H  HG22 . VAL   B 1 52  ? -18.523 -7.372  -35.503 1.00 28.04  ? 49  VAL   B HG22 1 
ATOM   5148 H  HG23 . VAL   B 1 52  ? -19.895 -7.498  -36.294 1.00 28.04  ? 49  VAL   B HG23 1 
ATOM   5149 N  N    . ALA   B 1 53  ? -19.808 -10.697 -32.396 1.00 19.10  ? 50  ALA   B N    1 
ATOM   5150 C  CA   . ALA   B 1 53  ? -20.240 -11.419 -31.192 1.00 18.81  ? 50  ALA   B CA   1 
ATOM   5151 C  C    . ALA   B 1 53  ? -19.407 -10.941 -30.007 1.00 19.24  ? 50  ALA   B C    1 
ATOM   5152 O  O    . ALA   B 1 53  ? -18.194 -11.171 -29.956 1.00 21.58  ? 50  ALA   B O    1 
ATOM   5153 C  CB   . ALA   B 1 53  ? -20.092 -12.925 -31.356 1.00 20.92  ? 50  ALA   B CB   1 
ATOM   5154 H  H    . ALA   B 1 53  ? -18.989 -10.850 -32.610 1.00 22.96  ? 50  ALA   B H    1 
ATOM   5155 H  HA   . ALA   B 1 53  ? -21.174 -11.212 -31.031 1.00 22.61  ? 50  ALA   B HA   1 
ATOM   5156 H  HB1  . ALA   B 1 53  ? -20.405 -13.363 -30.549 1.00 25.14  ? 50  ALA   B HB1  1 
ATOM   5157 H  HB2  . ALA   B 1 53  ? -20.621 -13.214 -32.116 1.00 25.14  ? 50  ALA   B HB2  1 
ATOM   5158 H  HB3  . ALA   B 1 53  ? -19.157 -13.136 -31.505 1.00 25.14  ? 50  ALA   B HB3  1 
ATOM   5159 N  N    . VAL   B 1 54  ? -20.064 -10.238 -29.076 1.00 18.77  ? 51  VAL   B N    1 
ATOM   5160 C  CA   . VAL   B 1 54  ? -19.375 -9.444  -28.062 1.00 19.04  ? 51  VAL   B CA   1 
ATOM   5161 C  C    . VAL   B 1 54  ? -19.127 -10.266 -26.808 1.00 20.43  ? 51  VAL   B C    1 
ATOM   5162 O  O    . VAL   B 1 54  ? -20.017 -11.010 -26.373 1.00 21.14  ? 51  VAL   B O    1 
ATOM   5163 C  CB   . VAL   B 1 54  ? -20.234 -8.213  -27.723 1.00 23.70  ? 51  VAL   B CB   1 
ATOM   5164 C  CG1  . VAL   B 1 54  ? -19.594 -7.361  -26.649 1.00 27.48  ? 51  VAL   B CG1  1 
ATOM   5165 C  CG2  . VAL   B 1 54  ? -20.456 -7.390  -28.963 1.00 28.17  ? 51  VAL   B CG2  1 
ATOM   5166 H  H    . VAL   B 1 54  ? -20.921 -10.209 -29.013 1.00 22.57  ? 51  VAL   B H    1 
ATOM   5167 H  HA   . VAL   B 1 54  ? -18.509 -9.178  -28.409 1.00 22.89  ? 51  VAL   B HA   1 
ATOM   5168 H  HB   . VAL   B 1 54  ? -21.087 -8.524  -27.381 1.00 28.48  ? 51  VAL   B HB   1 
ATOM   5169 H  HG11 . VAL   B 1 54  ? -19.896 -6.445  -26.751 1.00 33.01  ? 51  VAL   B HG11 1 
ATOM   5170 H  HG12 . VAL   B 1 54  ? -19.856 -7.701  -25.779 1.00 33.01  ? 51  VAL   B HG12 1 
ATOM   5171 H  HG13 . VAL   B 1 54  ? -18.630 -7.404  -26.744 1.00 33.01  ? 51  VAL   B HG13 1 
ATOM   5172 H  HG21 . VAL   B 1 54  ? -20.807 -6.523  -28.708 1.00 33.84  ? 51  VAL   B HG21 1 
ATOM   5173 H  HG22 . VAL   B 1 54  ? -19.610 -7.282  -29.425 1.00 33.84  ? 51  VAL   B HG22 1 
ATOM   5174 H  HG23 . VAL   B 1 54  ? -21.090 -7.848  -29.537 1.00 33.84  ? 51  VAL   B HG23 1 
ATOM   5175 N  N    . ASP   B 1 55  ? -17.950 -10.081 -26.175 1.00 19.53  ? 52  ASP   B N    1 
ATOM   5176 C  CA   . ASP   B 1 55  ? -17.757 -10.377 -24.752 1.00 17.20  ? 52  ASP   B CA   1 
ATOM   5177 C  C    . ASP   B 1 55  ? -18.175 -9.132  -23.972 1.00 18.76  ? 52  ASP   B C    1 
ATOM   5178 O  O    . ASP   B 1 55  ? -17.499 -8.105  -24.041 1.00 20.85  ? 52  ASP   B O    1 
ATOM   5179 C  CB   . ASP   B 1 55  ? -16.297 -10.697 -24.437 1.00 19.88  ? 52  ASP   B CB   1 
ATOM   5180 C  CG   . ASP   B 1 55  ? -15.870 -12.104 -24.863 1.00 21.15  ? 52  ASP   B CG   1 
ATOM   5181 O  OD1  . ASP   B 1 55  ? -16.626 -12.796 -25.609 1.00 22.94  ? 52  ASP   B OD1  1 
ATOM   5182 O  OD2  . ASP   B 1 55  ? -14.731 -12.525 -24.517 1.00 23.89  ? 52  ASP   B OD2  1 
ATOM   5183 H  H    . ASP   B 1 55  ? -17.243 -9.780  -26.560 1.00 23.47  ? 52  ASP   B H    1 
ATOM   5184 H  HA   . ASP   B 1 55  ? -18.300 -11.144 -24.511 1.00 20.69  ? 52  ASP   B HA   1 
ATOM   5185 H  HB2  . ASP   B 1 55  ? -15.730 -10.063 -24.902 1.00 23.90  ? 52  ASP   B HB2  1 
ATOM   5186 H  HB3  . ASP   B 1 55  ? -16.161 -10.624 -23.479 1.00 23.90  ? 52  ASP   B HB3  1 
ATOM   5187 N  N    . ARG   B 1 56  ? -19.294 -9.181  -23.260 1.00 18.36  ? 53  ARG   B N    1 
ATOM   5188 C  CA   . ARG   B 1 56  ? -19.667 -8.003  -22.492 1.00 17.34  ? 53  ARG   B CA   1 
ATOM   5189 C  C    . ARG   B 1 56  ? -18.549 -7.675  -21.482 1.00 16.60  ? 53  ARG   B C    1 
ATOM   5190 O  O    . ARG   B 1 56  ? -17.706 -8.510  -21.135 1.00 20.23  ? 53  ARG   B O    1 
ATOM   5191 C  CB   . ARG   B 1 56  ? -21.031 -8.214  -21.839 1.00 18.10  ? 53  ARG   B CB   1 
ATOM   5192 C  CG   . ARG   B 1 56  ? -22.163 -8.212  -22.871 1.00 17.92  ? 53  ARG   B CG   1 
ATOM   5193 C  CD   . ARG   B 1 56  ? -23.567 -8.010  -22.311 1.00 17.24  ? 53  ARG   B CD   1 
ATOM   5194 N  NE   . ARG   B 1 56  ? -24.041 -9.261  -21.740 1.00 18.91  ? 53  ARG   B NE   1 
ATOM   5195 C  CZ   . ARG   B 1 56  ? -24.242 -9.497  -20.449 1.00 18.05  ? 53  ARG   B CZ   1 
ATOM   5196 N  NH1  . ARG   B 1 56  ? -24.085 -8.550  -19.558 1.00 18.06  ? 53  ARG   B NH1  1 
ATOM   5197 N  NH2  . ARG   B 1 56  ? -24.610 -10.714 -20.052 1.00 20.78  ? 53  ARG   B NH2  1 
ATOM   5198 H  H    . ARG   B 1 56  ? -19.829 -9.853  -23.208 1.00 22.07  ? 53  ARG   B H    1 
ATOM   5199 H  HA   . ARG   B 1 56  ? -19.766 -7.222  -23.059 1.00 20.85  ? 53  ARG   B HA   1 
ATOM   5200 H  HB2  . ARG   B 1 56  ? -21.037 -9.070  -21.382 1.00 21.76  ? 53  ARG   B HB2  1 
ATOM   5201 H  HB3  . ARG   B 1 56  ? -21.195 -7.499  -21.205 1.00 21.76  ? 53  ARG   B HB3  1 
ATOM   5202 H  HG2  . ARG   B 1 56  ? -22.000 -7.493  -23.502 1.00 21.55  ? 53  ARG   B HG2  1 
ATOM   5203 H  HG3  . ARG   B 1 56  ? -22.158 -9.065  -23.332 1.00 21.55  ? 53  ARG   B HG3  1 
ATOM   5204 H  HD2  . ARG   B 1 56  ? -23.551 -7.334  -21.615 1.00 20.73  ? 53  ARG   B HD2  1 
ATOM   5205 H  HD3  . ARG   B 1 56  ? -24.170 -7.741  -23.021 1.00 20.73  ? 53  ARG   B HD3  1 
ATOM   5206 H  HE   . ARG   B 1 56  ? -24.205 -9.904  -22.287 1.00 22.74  ? 53  ARG   B HE   1 
ATOM   5207 H  HH11 . ARG   B 1 56  ? -24.219 -8.718  -18.725 1.00 21.72  ? 53  ARG   B HH11 1 
ATOM   5208 H  HH12 . ARG   B 1 56  ? -23.849 -7.761  -19.805 1.00 21.72  ? 53  ARG   B HH12 1 
ATOM   5209 H  HH21 . ARG   B 1 56  ? -24.742 -10.873 -19.217 1.00 24.98  ? 53  ARG   B HH21 1 
ATOM   5210 H  HH22 . ARG   B 1 56  ? -24.717 -11.341 -20.631 1.00 24.98  ? 53  ARG   B HH22 1 
ATOM   5211 N  N    . ARG   B 1 57  ? -18.505 -6.397  -21.053 1.00 18.66  ? 54  ARG   B N    1 
ATOM   5212 C  CA   . ARG   B 1 57  ? -17.228 -5.873  -20.517 1.00 20.80  ? 54  ARG   B CA   1 
ATOM   5213 C  C    . ARG   B 1 57  ? -16.774 -6.552  -19.225 1.00 21.15  ? 54  ARG   B C    1 
ATOM   5214 O  O    . ARG   B 1 57  ? -15.566 -6.561  -18.912 1.00 22.91  ? 54  ARG   B O    1 
ATOM   5215 C  CB   . ARG   B 1 57  ? -17.280 -4.345  -20.325 1.00 20.33  ? 54  ARG   B CB   1 
ATOM   5216 C  CG   . ARG   B 1 57  ? -18.392 -3.848  -19.404 1.00 21.47  ? 54  ARG   B CG   1 
ATOM   5217 C  CD   . ARG   B 1 57  ? -18.134 -2.427  -18.931 1.00 20.66  ? 54  ARG   B CD   1 
ATOM   5218 N  NE   . ARG   B 1 57  ? -18.029 -1.474  -20.048 1.00 22.88  ? 54  ARG   B NE   1 
ATOM   5219 C  CZ   . ARG   B 1 57  ? -17.484 -0.271  -19.928 1.00 22.88  ? 54  ARG   B CZ   1 
ATOM   5220 N  NH1  . ARG   B 1 57  ? -17.043 0.169   -18.766 1.00 22.49  ? 54  ARG   B NH1  1 
ATOM   5221 N  NH2  . ARG   B 1 57  ? -17.389 0.518   -20.996 1.00 23.67  ? 54  ARG   B NH2  1 
ATOM   5222 H  H    . ARG   B 1 57  ? -19.162 -5.842  -21.062 1.00 22.43  ? 54  ARG   B H    1 
ATOM   5223 H  HA   . ARG   B 1 57  ? -16.551 -6.056  -21.186 1.00 25.00  ? 54  ARG   B HA   1 
ATOM   5224 H  HB2  . ARG   B 1 57  ? -16.436 -4.054  -19.945 1.00 24.44  ? 54  ARG   B HB2  1 
ATOM   5225 H  HB3  . ARG   B 1 57  ? -17.414 -3.931  -21.192 1.00 24.44  ? 54  ARG   B HB3  1 
ATOM   5226 H  HG2  . ARG   B 1 57  ? -19.235 -3.862  -19.882 1.00 25.80  ? 54  ARG   B HG2  1 
ATOM   5227 H  HG3  . ARG   B 1 57  ? -18.443 -4.423  -18.624 1.00 25.80  ? 54  ARG   B HG3  1 
ATOM   5228 H  HD2  . ARG   B 1 57  ? -18.867 -2.144  -18.362 1.00 24.83  ? 54  ARG   B HD2  1 
ATOM   5229 H  HD3  . ARG   B 1 57  ? -17.301 -2.403  -18.436 1.00 24.83  ? 54  ARG   B HD3  1 
ATOM   5230 H  HE   . ARG   B 1 57  ? -18.336 -1.710  -20.816 1.00 27.50  ? 54  ARG   B HE   1 
ATOM   5231 H  HH11 . ARG   B 1 57  ? -16.693 0.952   -18.707 1.00 27.03  ? 54  ARG   B HH11 1 
ATOM   5232 H  HH12 . ARG   B 1 57  ? -17.106 -0.328  -18.066 1.00 27.03  ? 54  ARG   B HH12 1 
ATOM   5233 H  HH21 . ARG   B 1 57  ? -17.680 0.246   -21.759 1.00 28.45  ? 54  ARG   B HH21 1 
ATOM   5234 H  HH22 . ARG   B 1 57  ? -17.037 1.299   -20.924 1.00 28.45  ? 54  ARG   B HH22 1 
ATOM   5235 N  N    . ASP   B 1 58  ? -17.695 -7.126  -18.473 1.00 21.44  ? 55  ASP   B N    1 
ATOM   5236 C  CA   . ASP   B 1 58  ? -17.325 -7.805  -17.246 1.00 21.54  ? 55  ASP   B CA   1 
ATOM   5237 C  C    . ASP   B 1 58  ? -16.931 -9.264  -17.455 1.00 21.01  ? 55  ASP   B C    1 
ATOM   5238 O  O    . ASP   B 1 58  ? -16.648 -9.971  -16.468 1.00 24.80  ? 55  ASP   B O    1 
ATOM   5239 C  CB   . ASP   B 1 58  ? -18.471 -7.710  -16.237 1.00 21.35  ? 55  ASP   B CB   1 
ATOM   5240 C  CG   . ASP   B 1 58  ? -18.650 -6.298  -15.701 1.00 23.35  ? 55  ASP   B CG   1 
ATOM   5241 O  OD1  . ASP   B 1 58  ? -17.808 -5.902  -14.854 1.00 27.99  ? 55  ASP   B OD1  1 
ATOM   5242 O  OD2  . ASP   B 1 58  ? -19.631 -5.622  -16.064 1.00 23.04  ? 55  ASP   B OD2  1 
ATOM   5243 H  H    . ASP   B 1 58  ? -18.537 -7.137  -18.652 1.00 25.77  ? 55  ASP   B H    1 
ATOM   5244 H  HA   . ASP   B 1 58  ? -16.552 -7.354  -16.871 1.00 25.90  ? 55  ASP   B HA   1 
ATOM   5245 H  HB2  . ASP   B 1 58  ? -19.298 -7.977  -16.669 1.00 25.66  ? 55  ASP   B HB2  1 
ATOM   5246 H  HB3  . ASP   B 1 58  ? -18.285 -8.297  -15.488 1.00 25.66  ? 55  ASP   B HB3  1 
ATOM   5247 N  N    . TYR   B 1 59  ? -16.856 -9.729  -18.711 1.00 21.39  ? 56  TYR   B N    1 
ATOM   5248 C  CA   . TYR   B 1 59  ? -16.648 -11.143 -18.969 1.00 21.38  ? 56  TYR   B CA   1 
ATOM   5249 C  C    . TYR   B 1 59  ? -15.601 -11.457 -20.042 1.00 25.21  ? 56  TYR   B C    1 
ATOM   5250 O  O    . TYR   B 1 59  ? -15.315 -10.648 -20.931 1.00 23.03  ? 56  TYR   B O    1 
ATOM   5251 C  CB   . TYR   B 1 59  ? -17.968 -11.751 -19.469 1.00 21.11  ? 56  TYR   B CB   1 
ATOM   5252 C  CG   . TYR   B 1 59  ? -19.193 -11.595 -18.580 1.00 17.95  ? 56  TYR   B CG   1 
ATOM   5253 C  CD1  . TYR   B 1 59  ? -19.427 -12.518 -17.576 1.00 22.13  ? 56  TYR   B CD1  1 
ATOM   5254 C  CD2  . TYR   B 1 59  ? -20.097 -10.552 -18.745 1.00 19.90  ? 56  TYR   B CD2  1 
ATOM   5255 C  CE1  . TYR   B 1 59  ? -20.570 -12.420 -16.776 1.00 23.73  ? 56  TYR   B CE1  1 
ATOM   5256 C  CE2  . TYR   B 1 59  ? -21.225 -10.433 -17.937 1.00 20.97  ? 56  TYR   B CE2  1 
ATOM   5257 C  CZ   . TYR   B 1 59  ? -21.442 -11.391 -16.980 1.00 22.93  ? 56  TYR   B CZ   1 
ATOM   5258 O  OH   . TYR   B 1 59  ? -22.551 -11.281 -16.156 1.00 22.88  ? 56  TYR   B OH   1 
ATOM   5259 H  H    . TYR   B 1 59  ? -16.922 -9.242  -19.417 1.00 25.71  ? 56  TYR   B H    1 
ATOM   5260 H  HA   . TYR   B 1 59  ? -16.314 -11.527 -18.144 1.00 25.70  ? 56  TYR   B HA   1 
ATOM   5261 H  HB2  . TYR   B 1 59  ? -18.184 -11.336 -20.319 1.00 25.37  ? 56  TYR   B HB2  1 
ATOM   5262 H  HB3  . TYR   B 1 59  ? -17.830 -12.703 -19.590 1.00 25.37  ? 56  TYR   B HB3  1 
ATOM   5263 H  HD1  . TYR   B 1 59  ? -18.821 -13.208 -17.432 1.00 26.60  ? 56  TYR   B HD1  1 
ATOM   5264 H  HD2  . TYR   B 1 59  ? -19.945 -9.919  -19.409 1.00 23.92  ? 56  TYR   B HD2  1 
ATOM   5265 H  HE1  . TYR   B 1 59  ? -20.734 -13.050 -16.111 1.00 28.52  ? 56  TYR   B HE1  1 
ATOM   5266 H  HE2  . TYR   B 1 59  ? -21.816 -9.723  -18.045 1.00 25.21  ? 56  TYR   B HE2  1 
ATOM   5267 H  HH   . TYR   B 1 59  ? -23.053 -10.666 -16.430 1.00 27.50  ? 56  TYR   B HH   1 
ATOM   5268 N  N    . GLY   B 1 60  ? -15.092 -12.693 -19.987 1.00 25.54  ? 57  GLY   B N    1 
ATOM   5269 C  CA   . GLY   B 1 60  ? -14.323 -13.228 -21.097 1.00 26.08  ? 57  GLY   B CA   1 
ATOM   5270 C  C    . GLY   B 1 60  ? -13.017 -12.472 -21.313 1.00 24.42  ? 57  GLY   B C    1 
ATOM   5271 O  O    . GLY   B 1 60  ? -12.278 -12.172 -20.379 1.00 27.13  ? 57  GLY   B O    1 
ATOM   5272 H  H    . GLY   B 1 60  ? -15.180 -13.231 -19.322 1.00 30.69  ? 57  GLY   B H    1 
ATOM   5273 H  HA2  . GLY   B 1 60  ? -14.112 -14.159 -20.923 1.00 31.34  ? 57  GLY   B HA2  1 
ATOM   5274 H  HA3  . GLY   B 1 60  ? -14.848 -13.170 -21.910 1.00 31.34  ? 57  GLY   B HA3  1 
ATOM   5275 N  N    . GLU   B 1 61  ? -12.736 -12.125 -22.571 1.00 23.35  ? 58  GLU   B N    1 
ATOM   5276 C  CA   . GLU   B 1 61  ? -11.504 -11.419 -22.898 1.00 25.51  ? 58  GLU   B CA   1 
ATOM   5277 C  C    . GLU   B 1 61  ? -11.634 -9.898  -22.805 1.00 22.24  ? 58  GLU   B C    1 
ATOM   5278 O  O    . GLU   B 1 61  ? -10.603 -9.208  -22.903 1.00 24.00  ? 58  GLU   B O    1 
ATOM   5279 C  CB   . GLU   B 1 61  ? -11.050 -11.806 -24.318 1.00 24.08  ? 58  GLU   B CB   1 
ATOM   5280 C  CG   . GLU   B 1 61  ? -10.660 -13.256 -24.451 1.00 26.15  ? 58  GLU   B CG   1 
ATOM   5281 C  CD   . GLU   B 1 61  ? -9.524  -13.632 -23.539 1.00 37.88  ? 58  GLU   B CD   1 
ATOM   5282 O  OE1  . GLU   B 1 61  ? -8.477  -12.951 -23.626 1.00 36.38  ? 58  GLU   B OE1  1 
ATOM   5283 O  OE2  . GLU   B 1 61  ? -9.682  -14.582 -22.736 1.00 51.66  ? 58  GLU   B OE2  1 
ATOM   5284 H  H    . GLU   B 1 61  ? -13.243 -12.289 -23.246 1.00 28.07  ? 58  GLU   B H    1 
ATOM   5285 H  HA   . GLU   B 1 61  ? -10.814 -11.689 -22.272 1.00 30.66  ? 58  GLU   B HA   1 
ATOM   5286 H  HB2  . GLU   B 1 61  ? -11.778 -11.635 -24.936 1.00 28.93  ? 58  GLU   B HB2  1 
ATOM   5287 H  HB3  . GLU   B 1 61  ? -10.279 -11.268 -24.557 1.00 28.93  ? 58  GLU   B HB3  1 
ATOM   5288 H  HG2  . GLU   B 1 61  ? -11.423 -13.812 -24.227 1.00 31.42  ? 58  GLU   B HG2  1 
ATOM   5289 H  HG3  . GLU   B 1 61  ? -10.382 -13.427 -25.364 1.00 31.42  ? 58  GLU   B HG3  1 
ATOM   5290 N  N    . SER   B 1 62  ? -12.838 -9.369  -22.562 1.00 23.64  ? 59  SER   B N    1 
ATOM   5291 C  CA   . SER   B 1 62  ? -12.986 -7.960  -22.203 1.00 23.07  ? 59  SER   B CA   1 
ATOM   5292 C  C    . SER   B 1 62  ? -12.356 -7.736  -20.836 1.00 24.63  ? 59  SER   B C    1 
ATOM   5293 O  O    . SER   B 1 62  ? -12.072 -8.684  -20.094 1.00 27.03  ? 59  SER   B O    1 
ATOM   5294 C  CB   . SER   B 1 62  ? -14.455 -7.539  -22.225 1.00 21.88  ? 59  SER   B CB   1 
ATOM   5295 O  OG   . SER   B 1 62  ? -14.904 -7.590  -23.584 1.00 21.26  ? 59  SER   B OG   1 
ATOM   5296 H  H    . SER   B 1 62  ? -13.579 -9.804  -22.599 1.00 28.41  ? 59  SER   B H    1 
ATOM   5297 H  HA   . SER   B 1 62  ? -12.537 -7.391  -22.848 1.00 27.73  ? 59  SER   B HA   1 
ATOM   5298 H  HB2  . SER   B 1 62  ? -14.979 -8.148  -21.682 1.00 26.30  ? 59  SER   B HB2  1 
ATOM   5299 H  HB3  . SER   B 1 62  ? -14.541 -6.634  -21.885 1.00 26.30  ? 59  SER   B HB3  1 
ATOM   5300 H  HG   . SER   B 1 62  ? -15.726 -7.422  -23.621 1.00 25.55  ? 59  SER   B HG   1 
ATOM   5301 N  N    . GLU   B 1 63  ? -12.011 -6.477  -20.547 1.00 23.29  ? 60  GLU   B N    1 
ATOM   5302 C  CA   . GLU   B 1 63  ? -11.408 -6.183  -19.253 1.00 25.12  ? 60  GLU   B CA   1 
ATOM   5303 C  C    . GLU   B 1 63  ? -11.823 -4.795  -18.797 1.00 28.29  ? 60  GLU   B C    1 
ATOM   5304 O  O    . GLU   B 1 63  ? -11.921 -3.869  -19.603 1.00 27.34  ? 60  GLU   B O    1 
ATOM   5305 C  CB   . GLU   B 1 63  ? -9.871  -6.281  -19.286 1.00 31.81  ? 60  GLU   B CB   1 
ATOM   5306 C  CG   . GLU   B 1 63  ? -9.190  -5.254  -20.132 1.00 31.20  ? 60  GLU   B CG   1 
ATOM   5307 C  CD   . GLU   B 1 63  ? -7.701  -5.510  -20.248 1.00 34.22  ? 60  GLU   B CD   1 
ATOM   5308 O  OE1  . GLU   B 1 63  ? -7.332  -6.285  -21.173 1.00 31.07  ? 60  GLU   B OE1  1 
ATOM   5309 O  OE2  . GLU   B 1 63  ? -6.912  -4.973  -19.420 1.00 36.31  ? 60  GLU   B OE2  1 
ATOM   5310 H  H    . GLU   B 1 63  ? -12.114 -5.802  -21.069 1.00 27.98  ? 60  GLU   B H    1 
ATOM   5311 H  HA   . GLU   B 1 63  ? -11.739 -6.830  -18.610 1.00 30.19  ? 60  GLU   B HA   1 
ATOM   5312 H  HB2  . GLU   B 1 63  ? -9.538  -6.179  -18.381 1.00 38.21  ? 60  GLU   B HB2  1 
ATOM   5313 H  HB3  . GLU   B 1 63  ? -9.627  -7.153  -19.633 1.00 38.21  ? 60  GLU   B HB3  1 
ATOM   5314 H  HG2  . GLU   B 1 63  ? -9.571  -5.271  -21.024 1.00 37.48  ? 60  GLU   B HG2  1 
ATOM   5315 H  HG3  . GLU   B 1 63  ? -9.316  -4.378  -19.735 1.00 37.48  ? 60  GLU   B HG3  1 
ATOM   5316 N  N    . LEU   B 1 64  ? -12.125 -4.680  -17.503 1.00 25.81  ? 61  LEU   B N    1 
ATOM   5317 C  CA   . LEU   B 1 64  ? -12.309 -3.365  -16.914 1.00 26.12  ? 61  LEU   B CA   1 
ATOM   5318 C  C    . LEU   B 1 64  ? -10.964 -2.675  -16.749 1.00 30.78  ? 61  LEU   B C    1 
ATOM   5319 O  O    . LEU   B 1 64  ? -9.948  -3.306  -16.433 1.00 32.86  ? 61  LEU   B O    1 
ATOM   5320 C  CB   . LEU   B 1 64  ? -13.005 -3.495  -15.567 1.00 25.84  ? 61  LEU   B CB   1 
ATOM   5321 C  CG   . LEU   B 1 64  ? -14.352 -4.210  -15.557 1.00 24.98  ? 61  LEU   B CG   1 
ATOM   5322 C  CD1  . LEU   B 1 64  ? -15.004 -4.049  -14.150 1.00 29.51  ? 61  LEU   B CD1  1 
ATOM   5323 C  CD2  . LEU   B 1 64  ? -15.299 -3.684  -16.614 1.00 24.19  ? 61  LEU   B CD2  1 
ATOM   5324 H  H    . LEU   B 1 64  ? -12.225 -5.338  -16.959 1.00 31.01  ? 61  LEU   B H    1 
ATOM   5325 H  HA   . LEU   B 1 64  ? -12.864 -2.817  -17.490 1.00 31.39  ? 61  LEU   B HA   1 
ATOM   5326 H  HB2  . LEU   B 1 64  ? -12.418 -3.987  -14.972 1.00 31.05  ? 61  LEU   B HB2  1 
ATOM   5327 H  HB3  . LEU   B 1 64  ? -13.155 -2.601  -15.220 1.00 31.05  ? 61  LEU   B HB3  1 
ATOM   5328 H  HG   . LEU   B 1 64  ? -14.199 -5.146  -15.758 1.00 30.02  ? 61  LEU   B HG   1 
ATOM   5329 H  HD11 . LEU   B 1 64  ? -15.837 -4.545  -14.129 1.00 35.45  ? 61  LEU   B HD11 1 
ATOM   5330 H  HD12 . LEU   B 1 64  ? -14.395 -4.396  -13.479 1.00 35.45  ? 61  LEU   B HD12 1 
ATOM   5331 H  HD13 . LEU   B 1 64  ? -15.174 -3.108  -13.987 1.00 35.45  ? 61  LEU   B HD13 1 
ATOM   5332 H  HD21 . LEU   B 1 64  ? -16.161 -4.116  -16.508 1.00 29.07  ? 61  LEU   B HD21 1 
ATOM   5333 H  HD22 . LEU   B 1 64  ? -15.393 -2.725  -16.505 1.00 29.07  ? 61  LEU   B HD22 1 
ATOM   5334 H  HD23 . LEU   B 1 64  ? -14.935 -3.883  -17.491 1.00 29.07  ? 61  LEU   B HD23 1 
ATOM   5335 N  N    . THR   B 1 65  ? -10.955 -1.357  -16.948 1.00 27.98  ? 62  THR   B N    1 
ATOM   5336 C  CA   . THR   B 1 65  ? -9.767  -0.561  -16.703 1.00 30.32  ? 62  THR   B CA   1 
ATOM   5337 C  C    . THR   B 1 65  ? -9.929  0.306   -15.455 1.00 32.09  ? 62  THR   B C    1 
ATOM   5338 O  O    . THR   B 1 65  ? -8.985  0.981   -15.048 1.00 36.54  ? 62  THR   B O    1 
ATOM   5339 C  CB   . THR   B 1 65  ? -9.425  0.306   -17.921 1.00 31.39  ? 62  THR   B CB   1 
ATOM   5340 O  OG1  . THR   B 1 65  ? -10.535 1.155   -18.227 1.00 35.37  ? 62  THR   B OG1  1 
ATOM   5341 C  CG2  . THR   B 1 65  ? -9.098  -0.561  -19.141 1.00 32.58  ? 62  THR   B CG2  1 
ATOM   5342 H  H    . THR   B 1 65  ? -11.632 -0.904  -17.225 1.00 33.62  ? 62  THR   B H    1 
ATOM   5343 H  HA   . THR   B 1 65  ? -9.006  -1.149  -16.573 1.00 36.43  ? 62  THR   B HA   1 
ATOM   5344 H  HB   . THR   B 1 65  ? -8.645  0.846   -17.720 1.00 37.71  ? 62  THR   B HB   1 
ATOM   5345 H  HG1  . THR   B 1 65  ? -10.485 1.419   -19.023 1.00 42.48  ? 62  THR   B HG1  1 
ATOM   5346 H  HG21 . THR   B 1 65  ? -8.808  -0.001  -19.879 1.00 39.13  ? 62  THR   B HG21 1 
ATOM   5347 H  HG22 . THR   B 1 65  ? -8.389  -1.186  -18.923 1.00 39.13  ? 62  THR   B HG22 1 
ATOM   5348 H  HG23 . THR   B 1 65  ? -9.884  -1.059  -19.415 1.00 39.13  ? 62  THR   B HG23 1 
ATOM   5349 N  N    . GLU   B 1 66  ? -11.115 0.304   -14.858 1.00 33.36  ? 63  GLU   B N    1 
ATOM   5350 C  CA   . GLU   B 1 66  ? -11.463 0.991   -13.619 1.00 37.19  ? 63  GLU   B CA   1 
ATOM   5351 C  C    . GLU   B 1 66  ? -12.399 0.056   -12.870 1.00 33.09  ? 63  GLU   B C    1 
ATOM   5352 O  O    . GLU   B 1 66  ? -13.163 -0.680  -13.501 1.00 32.22  ? 63  GLU   B O    1 
ATOM   5353 C  CB   . GLU   B 1 66  ? -12.188 2.328   -13.874 1.00 42.79  ? 63  GLU   B CB   1 
ATOM   5354 C  CG   . GLU   B 1 66  ? -11.443 3.326   -14.771 1.00 60.84  ? 63  GLU   B CG   1 
ATOM   5355 C  CD   . GLU   B 1 66  ? -10.396 4.145   -14.017 1.00 83.68  ? 63  GLU   B CD   1 
ATOM   5356 O  OE1  . GLU   B 1 66  ? -10.646 4.512   -12.847 1.00 81.45  ? 63  GLU   B OE1  1 
ATOM   5357 O  OE2  . GLU   B 1 66  ? -9.323  4.431   -14.602 1.00 86.02  ? 63  GLU   B OE2  1 
ATOM   5358 H  H    . GLU   B 1 66  ? -11.789 -0.124  -15.176 1.00 40.08  ? 63  GLU   B H    1 
ATOM   5359 H  HA   . GLU   B 1 66  ? -10.670 1.188   -13.095 1.00 44.68  ? 63  GLU   B HA   1 
ATOM   5360 H  HB2  . GLU   B 1 66  ? -13.038 2.137   -14.300 1.00 51.39  ? 63  GLU   B HB2  1 
ATOM   5361 H  HB3  . GLU   B 1 66  ? -12.336 2.763   -13.019 1.00 51.39  ? 63  GLU   B HB3  1 
ATOM   5362 H  HG2  . GLU   B 1 66  ? -10.989 2.838   -15.475 1.00 73.04  ? 63  GLU   B HG2  1 
ATOM   5363 H  HG3  . GLU   B 1 66  ? -12.084 3.944   -15.155 1.00 73.04  ? 63  GLU   B HG3  1 
ATOM   5364 N  N    . PRO   B 1 67  ? -12.391 0.086   -11.540 1.00 35.40  ? 64  PRO   B N    1 
ATOM   5365 C  CA   . PRO   B 1 67  ? -13.279 -0.807  -10.779 1.00 35.17  ? 64  PRO   B CA   1 
ATOM   5366 C  C    . PRO   B 1 67  ? -14.742 -0.478  -11.003 1.00 33.90  ? 64  PRO   B C    1 
ATOM   5367 O  O    . PRO   B 1 67  ? -15.105 0.658   -11.312 1.00 32.74  ? 64  PRO   B O    1 
ATOM   5368 C  CB   . PRO   B 1 67  ? -12.869 -0.537  -9.317  1.00 40.40  ? 64  PRO   B CB   1 
ATOM   5369 C  CG   . PRO   B 1 67  ? -11.477 -0.025  -9.444  1.00 43.98  ? 64  PRO   B CG   1 
ATOM   5370 C  CD   . PRO   B 1 67  ? -11.590 0.908   -10.618 1.00 43.01  ? 64  PRO   B CD   1 
ATOM   5371 H  HA   . PRO   B 1 67  ? -13.117 -1.733  -11.015 1.00 42.25  ? 64  PRO   B HA   1 
ATOM   5372 H  HB2  . PRO   B 1 67  ? -13.455 0.125   -8.919  1.00 48.52  ? 64  PRO   B HB2  1 
ATOM   5373 H  HB3  . PRO   B 1 67  ? -12.898 -1.359  -8.802  1.00 48.52  ? 64  PRO   B HB3  1 
ATOM   5374 H  HG2  . PRO   B 1 67  ? -11.212 0.446   -8.638  1.00 52.82  ? 64  PRO   B HG2  1 
ATOM   5375 H  HG3  . PRO   B 1 67  ? -10.860 -0.751  -9.622  1.00 52.82  ? 64  PRO   B HG3  1 
ATOM   5376 H  HD2  . PRO   B 1 67  ? -12.051 1.727   -10.379 1.00 51.66  ? 64  PRO   B HD2  1 
ATOM   5377 H  HD3  . PRO   B 1 67  ? -10.719 1.115   -10.992 1.00 51.66  ? 64  PRO   B HD3  1 
ATOM   5378 N  N    . LEU   B 1 68  ? -15.597 -1.490  -10.848 1.00 35.66  ? 65  LEU   B N    1 
ATOM   5379 C  CA   . LEU   B 1 68  ? -17.017 -1.219  -10.808 1.00 32.32  ? 65  LEU   B CA   1 
ATOM   5380 C  C    . LEU   B 1 68  ? -17.327 -0.237  -9.679  1.00 31.51  ? 65  LEU   B C    1 
ATOM   5381 O  O    . LEU   B 1 68  ? -16.662 -0.246  -8.643  1.00 35.11  ? 65  LEU   B O    1 
ATOM   5382 C  CB   . LEU   B 1 68  ? -17.836 -2.476  -10.557 1.00 35.18  ? 65  LEU   B CB   1 
ATOM   5383 C  CG   . LEU   B 1 68  ? -17.964 -3.539  -11.624 1.00 36.06  ? 65  LEU   B CG   1 
ATOM   5384 C  CD1  . LEU   B 1 68  ? -18.719 -4.710  -11.038 1.00 31.47  ? 65  LEU   B CD1  1 
ATOM   5385 C  CD2  . LEU   B 1 68  ? -18.697 -2.944  -12.808 1.00 31.20  ? 65  LEU   B CD2  1 
ATOM   5386 H  H    . LEU   B 1 68  ? -15.378 -2.318  -10.767 1.00 42.83  ? 65  LEU   B H    1 
ATOM   5387 H  HA   . LEU   B 1 68  ? -17.270 -0.849  -11.668 1.00 38.82  ? 65  LEU   B HA   1 
ATOM   5388 H  HB2  . LEU   B 1 68  ? -17.449 -2.918  -9.785  1.00 42.25  ? 65  LEU   B HB2  1 
ATOM   5389 H  HB3  . LEU   B 1 68  ? -18.741 -2.190  -10.356 1.00 42.25  ? 65  LEU   B HB3  1 
ATOM   5390 H  HG   . LEU   B 1 68  ? -17.100 -3.854  -11.931 1.00 43.31  ? 65  LEU   B HG   1 
ATOM   5391 H  HD11 . LEU   B 1 68  ? -18.743 -5.428  -11.690 1.00 37.80  ? 65  LEU   B HD11 1 
ATOM   5392 H  HD12 . LEU   B 1 68  ? -18.265 -5.007  -10.234 1.00 37.80  ? 65  LEU   B HD12 1 
ATOM   5393 H  HD13 . LEU   B 1 68  ? -19.622 -4.428  -10.824 1.00 37.80  ? 65  LEU   B HD13 1 
ATOM   5394 H  HD21 . LEU   B 1 68  ? -18.801 -3.626  -13.490 1.00 37.49  ? 65  LEU   B HD21 1 
ATOM   5395 H  HD22 . LEU   B 1 68  ? -19.568 -2.632  -12.516 1.00 37.49  ? 65  LEU   B HD22 1 
ATOM   5396 H  HD23 . LEU   B 1 68  ? -18.181 -2.202  -13.159 1.00 37.49  ? 65  LEU   B HD23 1 
ATOM   5397 N  N    . PRO   B 1 69  ? -18.380 0.568   -9.802  1.00 31.53  ? 66  PRO   B N    1 
ATOM   5398 C  CA   . PRO   B 1 69  ? -18.820 1.343   -8.636  1.00 35.68  ? 66  PRO   B CA   1 
ATOM   5399 C  C    . PRO   B 1 69  ? -19.231 0.417   -7.498  1.00 33.33  ? 66  PRO   B C    1 
ATOM   5400 O  O    . PRO   B 1 69  ? -19.711 -0.700  -7.724  1.00 37.82  ? 66  PRO   B O    1 
ATOM   5401 C  CB   . PRO   B 1 69  ? -20.006 2.165   -9.163  1.00 42.03  ? 66  PRO   B CB   1 
ATOM   5402 C  CG   . PRO   B 1 69  ? -20.357 1.572   -10.474 1.00 40.97  ? 66  PRO   B CG   1 
ATOM   5403 C  CD   . PRO   B 1 69  ? -19.132 0.918   -11.020 1.00 34.99  ? 66  PRO   B CD   1 
ATOM   5404 H  HA   . PRO   B 1 69  ? -18.126 1.951   -8.336  1.00 42.86  ? 66  PRO   B HA   1 
ATOM   5405 H  HB2  . PRO   B 1 69  ? -20.750 2.098   -8.545  1.00 50.48  ? 66  PRO   B HB2  1 
ATOM   5406 H  HB3  . PRO   B 1 69  ? -19.741 3.092   -9.265  1.00 50.48  ? 66  PRO   B HB3  1 
ATOM   5407 H  HG2  . PRO   B 1 69  ? -21.061 0.917   -10.349 1.00 49.21  ? 66  PRO   B HG2  1 
ATOM   5408 H  HG3  . PRO   B 1 69  ? -20.658 2.274   -11.071 1.00 49.21  ? 66  PRO   B HG3  1 
ATOM   5409 H  HD2  . PRO   B 1 69  ? -19.359 0.124   -11.528 1.00 42.03  ? 66  PRO   B HD2  1 
ATOM   5410 H  HD3  . PRO   B 1 69  ? -18.628 1.534   -11.574 1.00 42.03  ? 66  PRO   B HD3  1 
ATOM   5411 N  N    . ASP   B 1 70  ? -19.026 0.888   -6.258  1.00 36.48  ? 67  ASP   B N    1 
ATOM   5412 C  CA   . ASP   B 1 70  ? -19.411 0.081   -5.106  1.00 40.70  ? 67  ASP   B CA   1 
ATOM   5413 C  C    . ASP   B 1 70  ? -20.897 -0.248  -5.151  1.00 37.79  ? 67  ASP   B C    1 
ATOM   5414 O  O    . ASP   B 1 70  ? -21.317 -1.335  -4.737  1.00 40.22  ? 67  ASP   B O    1 
ATOM   5415 C  CB   . ASP   B 1 70  ? -19.085 0.797   -3.796  1.00 47.82  ? 67  ASP   B CB   1 
ATOM   5416 C  CG   . ASP   B 1 70  ? -17.596 0.885   -3.538  1.00 56.91  ? 67  ASP   B CG   1 
ATOM   5417 O  OD1  . ASP   B 1 70  ? -16.860 -0.034  -3.966  1.00 54.18  ? 67  ASP   B OD1  1 
ATOM   5418 O  OD2  . ASP   B 1 70  ? -17.166 1.862   -2.892  1.00 66.88  ? 67  ASP   B OD2  1 
ATOM   5419 H  H    . ASP   B 1 70  ? -18.675 1.650   -6.069  1.00 43.82  ? 67  ASP   B H    1 
ATOM   5420 H  HA   . ASP   B 1 70  ? -18.896 -0.741  -5.124  1.00 48.88  ? 67  ASP   B HA   1 
ATOM   5421 H  HB2  . ASP   B 1 70  ? -19.438 1.700   -3.832  1.00 57.42  ? 67  ASP   B HB2  1 
ATOM   5422 H  HB3  . ASP   B 1 70  ? -19.489 0.312   -3.060  1.00 57.42  ? 67  ASP   B HB3  1 
ATOM   5423 N  N    . SER   B 1 71  ? -21.696 0.661   -5.703  1.00 34.87  ? 68  SER   B N    1 
ATOM   5424 C  CA   . SER   B 1 71  ? -23.140 0.508   -5.700  1.00 35.03  ? 68  SER   B CA   1 
ATOM   5425 C  C    . SER   B 1 71  ? -23.619 -0.558  -6.666  1.00 31.99  ? 68  SER   B C    1 
ATOM   5426 O  O    . SER   B 1 71  ? -24.816 -0.865  -6.688  1.00 30.88  ? 68  SER   B O    1 
ATOM   5427 C  CB   . SER   B 1 71  ? -23.788 1.844   -6.048  1.00 40.44  ? 68  SER   B CB   1 
ATOM   5428 O  OG   . SER   B 1 71  ? -23.376 2.283   -7.331  1.00 45.23  ? 68  SER   B OG   1 
ATOM   5429 H  H    . SER   B 1 71  ? -21.421 1.379   -6.088  1.00 41.88  ? 68  SER   B H    1 
ATOM   5430 H  HA   . SER   B 1 71  ? -23.430 0.247   -4.812  1.00 42.08  ? 68  SER   B HA   1 
ATOM   5431 H  HB2  . SER   B 1 71  ? -24.752 1.739   -6.045  1.00 48.57  ? 68  SER   B HB2  1 
ATOM   5432 H  HB3  . SER   B 1 71  ? -23.524 2.505   -5.389  1.00 48.57  ? 68  SER   B HB3  1 
ATOM   5433 H  HG   . SER   B 1 71  ? -23.582 3.090   -7.438  1.00 54.32  ? 68  SER   B HG   1 
ATOM   5434 N  N    . ALA   B 1 72  ? -22.731 -1.112  -7.487  1.00 30.05  ? 69  ALA   B N    1 
ATOM   5435 C  CA   . ALA   B 1 72  ? -23.212 -2.088  -8.446  1.00 26.53  ? 69  ALA   B CA   1 
ATOM   5436 C  C    . ALA   B 1 72  ? -23.737 -3.345  -7.773  1.00 26.94  ? 69  ALA   B C    1 
ATOM   5437 O  O    . ALA   B 1 72  ? -24.550 -4.058  -8.385  1.00 27.11  ? 69  ALA   B O    1 
ATOM   5438 C  CB   . ALA   B 1 72  ? -22.114 -2.451  -9.455  1.00 27.79  ? 69  ALA   B CB   1 
ATOM   5439 H  H    . ALA   B 1 72  ? -21.887 -0.945  -7.505  1.00 36.10  ? 69  ALA   B H    1 
ATOM   5440 H  HA   . ALA   B 1 72  ? -23.940 -1.688  -8.947  1.00 31.87  ? 69  ALA   B HA   1 
ATOM   5441 H  HB1  . ALA   B 1 72  ? -22.457 -3.119  -10.068 1.00 33.39  ? 69  ALA   B HB1  1 
ATOM   5442 H  HB2  . ALA   B 1 72  ? -21.858 -1.653  -9.943  1.00 33.39  ? 69  ALA   B HB2  1 
ATOM   5443 H  HB3  . ALA   B 1 72  ? -21.349 -2.805  -8.974  1.00 33.39  ? 69  ALA   B HB3  1 
ATOM   5444 N  N    A SER   B 1 73  ? -23.302 -3.629  -6.538  0.69 28.25  ? 70  SER   B N    1 
ATOM   5445 N  N    B SER   B 1 73  ? -23.295 -3.631  -6.544  0.31 28.29  ? 70  SER   B N    1 
ATOM   5446 C  CA   A SER   B 1 73  ? -23.844 -4.763  -5.800  0.69 31.26  ? 70  SER   B CA   1 
ATOM   5447 C  CA   B SER   B 1 73  ? -23.850 -4.760  -5.808  0.31 31.28  ? 70  SER   B CA   1 
ATOM   5448 C  C    A SER   B 1 73  ? -25.257 -4.515  -5.291  0.69 31.16  ? 70  SER   B C    1 
ATOM   5449 C  C    B SER   B 1 73  ? -25.322 -4.532  -5.482  0.31 31.31  ? 70  SER   B C    1 
ATOM   5450 O  O    A SER   B 1 73  ? -25.905 -5.461  -4.812  0.69 33.28  ? 70  SER   B O    1 
ATOM   5451 O  O    B SER   B 1 73  ? -26.095 -5.498  -5.382  0.31 29.95  ? 70  SER   B O    1 
ATOM   5452 C  CB   A SER   B 1 73  ? -22.957 -5.080  -4.605  0.69 30.46  ? 70  SER   B CB   1 
ATOM   5453 C  CB   B SER   B 1 73  ? -23.043 -4.988  -4.530  0.31 30.35  ? 70  SER   B CB   1 
ATOM   5454 O  OG   A SER   B 1 73  ? -22.670 -3.880  -3.917  0.69 35.43  ? 70  SER   B OG   1 
ATOM   5455 O  OG   B SER   B 1 73  ? -21.714 -5.388  -4.837  0.31 32.73  ? 70  SER   B OG   1 
ATOM   5456 H  H    A SER   B 1 73  ? -22.700 -3.183  -6.115  0.69 33.94  ? 70  SER   B H    1 
ATOM   5457 H  H    B SER   B 1 73  ? -22.686 -3.193  -6.124  0.31 33.99  ? 70  SER   B H    1 
ATOM   5458 H  HA   A SER   B 1 73  ? -23.857 -5.529  -6.394  0.69 37.56  ? 70  SER   B HA   1 
ATOM   5459 H  HA   B SER   B 1 73  ? -23.784 -5.563  -6.349  0.31 37.57  ? 70  SER   B HA   1 
ATOM   5460 H  HB2  A SER   B 1 73  ? -23.421 -5.690  -4.011  0.69 36.59  ? 70  SER   B HB2  1 
ATOM   5461 H  HB2  B SER   B 1 73  ? -23.016 -4.162  -4.022  0.31 36.46  ? 70  SER   B HB2  1 
ATOM   5462 H  HB3  A SER   B 1 73  ? -22.130 -5.482  -4.913  0.69 36.59  ? 70  SER   B HB3  1 
ATOM   5463 H  HB3  B SER   B 1 73  ? -23.470 -5.685  -4.007  0.31 36.46  ? 70  SER   B HB3  1 
ATOM   5464 H  HG   A SER   B 1 73  ? -22.178 -4.039  -3.255  0.69 42.56  ? 70  SER   B HG   1 
ATOM   5465 H  HG   B SER   B 1 73  ? -21.719 -6.145  -5.201  0.31 39.31  ? 70  SER   B HG   1 
ATOM   5466 N  N    . ASN   B 1 74  ? -25.731 -3.272  -5.342  1.00 27.37  ? 71  ASN   B N    1 
ATOM   5467 C  CA   . ASN   B 1 74  ? -27.093 -2.975  -4.936  1.00 32.07  ? 71  ASN   B CA   1 
ATOM   5468 C  C    . ASN   B 1 74  ? -28.067 -3.602  -5.922  1.00 28.63  ? 71  ASN   B C    1 
ATOM   5469 O  O    . ASN   B 1 74  ? -27.897 -3.434  -7.132  1.00 28.34  ? 71  ASN   B O    1 
ATOM   5470 C  CB   . ASN   B 1 74  ? -27.317 -1.465  -4.885  1.00 31.44  ? 71  ASN   B CB   1 
ATOM   5471 C  CG   . ASN   B 1 74  ? -28.500 -1.091  -4.037  1.00 49.82  ? 71  ASN   B CG   1 
ATOM   5472 O  OD1  . ASN   B 1 74  ? -29.650 -1.313  -4.429  1.00 42.77  ? 71  ASN   B OD1  1 
ATOM   5473 N  ND2  . ASN   B 1 74  ? -28.232 -0.521  -2.859  1.00 65.67  ? 71  ASN   B ND2  1 
ATOM   5474 H  H    A ASN   B 1 74  ? -25.283 -2.588  -5.608  0.69 32.89  ? 71  ASN   B H    1 
ATOM   5475 H  H    B ASN   B 1 74  ? -25.240 -2.579  -5.477  0.31 32.89  ? 71  ASN   B H    1 
ATOM   5476 H  HA   . ASN   B 1 74  ? -27.254 -3.341  -4.052  1.00 38.53  ? 71  ASN   B HA   1 
ATOM   5477 H  HB2  . ASN   B 1 74  ? -26.530 -1.040  -4.509  1.00 37.76  ? 71  ASN   B HB2  1 
ATOM   5478 H  HB3  . ASN   B 1 74  ? -27.474 -1.136  -5.784  1.00 37.76  ? 71  ASN   B HB3  1 
ATOM   5479 H  HD21 . ASN   B 1 74  ? -28.875 -0.289  -2.338  1.00 78.85  ? 71  ASN   B HD21 1 
ATOM   5480 H  HD22 . ASN   B 1 74  ? -27.416 -0.386  -2.623  1.00 78.85  ? 71  ASN   B HD22 1 
ATOM   5481 N  N    . PRO   B 1 75  ? -29.100 -4.323  -5.460  1.00 27.26  ? 72  PRO   B N    1 
ATOM   5482 C  CA   . PRO   B 1 75  ? -29.998 -4.985  -6.422  1.00 27.53  ? 72  PRO   B CA   1 
ATOM   5483 C  C    . PRO   B 1 75  ? -30.789 -4.012  -7.288  1.00 29.48  ? 72  PRO   B C    1 
ATOM   5484 O  O    . PRO   B 1 75  ? -31.291 -4.426  -8.344  1.00 29.47  ? 72  PRO   B O    1 
ATOM   5485 C  CB   . PRO   B 1 75  ? -30.911 -5.840  -5.528  1.00 33.51  ? 72  PRO   B CB   1 
ATOM   5486 C  CG   . PRO   B 1 75  ? -30.860 -5.177  -4.203  1.00 32.37  ? 72  PRO   B CG   1 
ATOM   5487 C  CD   . PRO   B 1 75  ? -29.440 -4.676  -4.065  1.00 31.50  ? 72  PRO   B CD   1 
ATOM   5488 H  HA   . PRO   B 1 75  ? -29.493 -5.577  -7.001  1.00 33.08  ? 72  PRO   B HA   1 
ATOM   5489 H  HB2  . PRO   B 1 75  ? -31.814 -5.843  -5.882  1.00 40.25  ? 72  PRO   B HB2  1 
ATOM   5490 H  HB3  . PRO   B 1 75  ? -30.571 -6.747  -5.478  1.00 40.25  ? 72  PRO   B HB3  1 
ATOM   5491 H  HG2  . PRO   B 1 75  ? -31.491 -4.440  -4.178  1.00 38.88  ? 72  PRO   B HG2  1 
ATOM   5492 H  HG3  . PRO   B 1 75  ? -31.070 -5.817  -3.505  1.00 38.88  ? 72  PRO   B HG3  1 
ATOM   5493 H  HD2  . PRO   B 1 75  ? -29.398 -3.898  -3.487  1.00 37.85  ? 72  PRO   B HD2  1 
ATOM   5494 H  HD3  . PRO   B 1 75  ? -28.854 -5.372  -3.727  1.00 37.85  ? 72  PRO   B HD3  1 
ATOM   5495 N  N    . ASP   B 1 76  ? -30.868 -2.733  -6.898  1.00 27.76  ? 73  ASP   B N    1 
ATOM   5496 C  CA   . ASP   B 1 76  ? -31.588 -1.708  -7.640  1.00 33.91  ? 73  ASP   B CA   1 
ATOM   5497 C  C    . ASP   B 1 76  ? -30.695 -0.888  -8.551  1.00 32.83  ? 73  ASP   B C    1 
ATOM   5498 O  O    . ASP   B 1 76  ? -31.181 0.073   -9.172  1.00 30.99  ? 73  ASP   B O    1 
ATOM   5499 C  CB   . ASP   B 1 76  ? -32.287 -0.749  -6.654  1.00 41.36  ? 73  ASP   B CB   1 
ATOM   5500 C  CG   . ASP   B 1 76  ? -33.253 -1.455  -5.727  1.00 57.95  ? 73  ASP   B CG   1 
ATOM   5501 O  OD1  . ASP   B 1 76  ? -33.463 -0.936  -4.609  1.00 64.11  ? 73  ASP   B OD1  1 
ATOM   5502 O  OD2  . ASP   B 1 76  ? -33.818 -2.497  -6.125  1.00 64.33  ? 73  ASP   B OD2  1 
ATOM   5503 H  H    . ASP   B 1 76  ? -30.498 -2.431  -6.183  1.00 33.35  ? 73  ASP   B H    1 
ATOM   5504 H  HA   . ASP   B 1 76  ? -32.257 -2.146  -8.188  1.00 40.74  ? 73  ASP   B HA   1 
ATOM   5505 H  HB2  . ASP   B 1 76  ? -31.614 -0.312  -6.109  1.00 49.67  ? 73  ASP   B HB2  1 
ATOM   5506 H  HB3  . ASP   B 1 76  ? -32.786 -0.087  -7.158  1.00 49.67  ? 73  ASP   B HB3  1 
ATOM   5507 N  N    . SER   B 1 77  ? -29.409 -1.233  -8.650  1.00 27.11  ? 74  SER   B N    1 
ATOM   5508 C  CA   . SER   B 1 77  ? -28.493 -0.478  -9.494  1.00 23.96  ? 74  SER   B CA   1 
ATOM   5509 C  C    . SER   B 1 77  ? -28.826 -0.707  -10.956 1.00 23.25  ? 74  SER   B C    1 
ATOM   5510 O  O    . SER   B 1 77  ? -29.101 -1.835  -11.365 1.00 25.69  ? 74  SER   B O    1 
ATOM   5511 C  CB   . SER   B 1 77  ? -27.057 -0.930  -9.240  1.00 25.20  ? 74  SER   B CB   1 
ATOM   5512 O  OG   . SER   B 1 77  ? -26.166 -0.343  -10.181 1.00 26.18  ? 74  SER   B OG   1 
ATOM   5513 H  H    . SER   B 1 77  ? -29.048 -1.896  -8.240  1.00 32.57  ? 74  SER   B H    1 
ATOM   5514 H  HA   . SER   B 1 77  ? -28.569 0.467   -9.291  1.00 28.80  ? 74  SER   B HA   1 
ATOM   5515 H  HB2  . SER   B 1 77  ? -26.795 -0.659  -8.346  1.00 30.29  ? 74  SER   B HB2  1 
ATOM   5516 H  HB3  . SER   B 1 77  ? -27.011 -1.895  -9.321  1.00 30.29  ? 74  SER   B HB3  1 
ATOM   5517 H  HG   . SER   B 1 77  ? -25.371 -0.473  -9.944  1.00 31.45  ? 74  SER   B HG   1 
ATOM   5518 N  N    . ASP   B 1 78  ? -28.756 0.352   -11.769 1.00 22.92  ? 75  ASP   B N    1 
ATOM   5519 C  CA   . ASP   B 1 78  ? -28.808 0.121   -13.210 1.00 22.04  ? 75  ASP   B CA   1 
ATOM   5520 C  C    . ASP   B 1 78  ? -27.553 0.602   -13.932 1.00 20.79  ? 75  ASP   B C    1 
ATOM   5521 O  O    . ASP   B 1 78  ? -27.553 0.679   -15.163 1.00 20.61  ? 75  ASP   B O    1 
ATOM   5522 C  CB   . ASP   B 1 78  ? -30.076 0.714   -13.826 1.00 29.79  ? 75  ASP   B CB   1 
ATOM   5523 C  CG   . ASP   B 1 78  ? -30.132 2.200   -13.796 1.00 26.97  ? 75  ASP   B CG   1 
ATOM   5524 O  OD1  . ASP   B 1 78  ? -29.415 2.876   -13.053 1.00 33.39  ? 75  ASP   B OD1  1 
ATOM   5525 O  OD2  . ASP   B 1 78  ? -31.023 2.700   -14.554 1.00 41.04  ? 75  ASP   B OD2  1 
ATOM   5526 H  H    . ASP   B 1 78  ? -28.681 1.171   -11.519 1.00 27.55  ? 75  ASP   B H    1 
ATOM   5527 H  HA   . ASP   B 1 78  ? -28.855 -0.837  -13.353 1.00 26.49  ? 75  ASP   B HA   1 
ATOM   5528 H  HB2  . ASP   B 1 78  ? -30.129 0.437   -14.754 1.00 35.79  ? 75  ASP   B HB2  1 
ATOM   5529 H  HB3  . ASP   B 1 78  ? -30.844 0.381   -13.336 1.00 35.79  ? 75  ASP   B HB3  1 
ATOM   5530 N  N    . TYR   B 1 79  ? -26.446 0.750   -13.205 1.00 22.98  ? 76  TYR   B N    1 
ATOM   5531 C  CA   . TYR   B 1 79  ? -25.175 1.118   -13.815 1.00 19.86  ? 76  TYR   B CA   1 
ATOM   5532 C  C    . TYR   B 1 79  ? -24.775 0.134   -14.922 1.00 21.59  ? 76  TYR   B C    1 
ATOM   5533 O  O    . TYR   B 1 79  ? -24.412 0.544   -16.035 1.00 20.15  ? 76  TYR   B O    1 
ATOM   5534 C  CB   . TYR   B 1 79  ? -24.067 1.179   -12.762 1.00 22.92  ? 76  TYR   B CB   1 
ATOM   5535 C  CG   . TYR   B 1 79  ? -22.713 1.297   -13.450 1.00 22.42  ? 76  TYR   B CG   1 
ATOM   5536 C  CD1  . TYR   B 1 79  ? -22.301 2.497   -14.010 1.00 27.08  ? 76  TYR   B CD1  1 
ATOM   5537 C  CD2  . TYR   B 1 79  ? -21.905 0.183   -13.618 1.00 22.53  ? 76  TYR   B CD2  1 
ATOM   5538 C  CE1  . TYR   B 1 79  ? -21.100 2.603   -14.702 1.00 27.53  ? 76  TYR   B CE1  1 
ATOM   5539 C  CE2  . TYR   B 1 79  ? -20.702 0.276   -14.317 1.00 23.45  ? 76  TYR   B CE2  1 
ATOM   5540 C  CZ   . TYR   B 1 79  ? -20.306 1.475   -14.850 1.00 26.90  ? 76  TYR   B CZ   1 
ATOM   5541 O  OH   . TYR   B 1 79  ? -19.112 1.557   -15.564 1.00 26.93  ? 76  TYR   B OH   1 
ATOM   5542 H  H    . TYR   B 1 79  ? -26.405 0.642   -12.353 1.00 27.62  ? 76  TYR   B H    1 
ATOM   5543 H  HA   . TYR   B 1 79  ? -25.281 2.000   -14.204 1.00 23.87  ? 76  TYR   B HA   1 
ATOM   5544 H  HB2  . TYR   B 1 79  ? -24.198 1.953   -12.193 1.00 27.55  ? 76  TYR   B HB2  1 
ATOM   5545 H  HB3  . TYR   B 1 79  ? -24.078 0.369   -12.228 1.00 27.55  ? 76  TYR   B HB3  1 
ATOM   5546 H  HD1  . TYR   B 1 79  ? -22.841 3.248   -13.921 1.00 32.54  ? 76  TYR   B HD1  1 
ATOM   5547 H  HD2  . TYR   B 1 79  ? -22.167 -0.635  -13.260 1.00 27.08  ? 76  TYR   B HD2  1 
ATOM   5548 H  HE1  . TYR   B 1 79  ? -20.832 3.418   -15.060 1.00 33.08  ? 76  TYR   B HE1  1 
ATOM   5549 H  HE2  . TYR   B 1 79  ? -20.167 -0.478  -14.422 1.00 28.18  ? 76  TYR   B HE2  1 
ATOM   5550 H  HH   . TYR   B 1 79  ? -18.770 0.793   -15.641 1.00 32.35  ? 76  TYR   B HH   1 
ATOM   5551 N  N    . ARG   B 1 80  ? -24.775 -1.164  -14.612 1.00 19.93  ? 77  ARG   B N    1 
ATOM   5552 C  CA   . ARG   B 1 80  ? -24.190 -2.120  -15.545 1.00 17.40  ? 77  ARG   B CA   1 
ATOM   5553 C  C    . ARG   B 1 80  ? -25.011 -2.266  -16.808 1.00 19.39  ? 77  ARG   B C    1 
ATOM   5554 O  O    . ARG   B 1 80  ? -24.440 -2.358  -17.902 1.00 19.42  ? 77  ARG   B O    1 
ATOM   5555 C  CB   . ARG   B 1 80  ? -23.991 -3.497  -14.880 1.00 18.61  ? 77  ARG   B CB   1 
ATOM   5556 C  CG   . ARG   B 1 80  ? -22.764 -3.593  -13.932 1.00 19.03  ? 77  ARG   B CG   1 
ATOM   5557 C  CD   . ARG   B 1 80  ? -22.385 -5.061  -13.586 1.00 17.97  ? 77  ARG   B CD   1 
ATOM   5558 N  NE   . ARG   B 1 80  ? -22.090 -5.838  -14.779 1.00 19.40  ? 77  ARG   B NE   1 
ATOM   5559 C  CZ   . ARG   B 1 80  ? -22.831 -6.819  -15.266 1.00 19.58  ? 77  ARG   B CZ   1 
ATOM   5560 N  NH1  . ARG   B 1 80  ? -23.971 -7.186  -14.699 1.00 21.35  ? 77  ARG   B NH1  1 
ATOM   5561 N  NH2  . ARG   B 1 80  ? -22.470 -7.401  -16.403 1.00 19.66  ? 77  ARG   B NH2  1 
ATOM   5562 H  H    . ARG   B 1 80  ? -25.097 -1.504  -13.891 1.00 23.96  ? 77  ARG   B H    1 
ATOM   5563 H  HA   . ARG   B 1 80  ? -23.317 -1.779  -15.792 1.00 20.92  ? 77  ARG   B HA   1 
ATOM   5564 H  HB2  . ARG   B 1 80  ? -24.781 -3.702  -14.356 1.00 22.37  ? 77  ARG   B HB2  1 
ATOM   5565 H  HB3  . ARG   B 1 80  ? -23.873 -4.161  -15.577 1.00 22.37  ? 77  ARG   B HB3  1 
ATOM   5566 H  HG2  . ARG   B 1 80  ? -21.999 -3.180  -14.361 1.00 22.88  ? 77  ARG   B HG2  1 
ATOM   5567 H  HG3  . ARG   B 1 80  ? -22.968 -3.133  -13.102 1.00 22.88  ? 77  ARG   B HG3  1 
ATOM   5568 H  HD2  . ARG   B 1 80  ? -21.598 -5.064  -13.019 1.00 21.60  ? 77  ARG   B HD2  1 
ATOM   5569 H  HD3  . ARG   B 1 80  ? -23.127 -5.483  -13.125 1.00 21.60  ? 77  ARG   B HD3  1 
ATOM   5570 H  HE   . ARG   B 1 80  ? -21.369 -5.643  -15.206 1.00 23.32  ? 77  ARG   B HE   1 
ATOM   5571 H  HH11 . ARG   B 1 80  ? -24.249 -6.782  -13.992 1.00 25.67  ? 77  ARG   B HH11 1 
ATOM   5572 H  HH12 . ARG   B 1 80  ? -24.433 -7.827  -15.037 1.00 25.67  ? 77  ARG   B HH12 1 
ATOM   5573 H  HH21 . ARG   B 1 80  ? -21.762 -7.140  -16.814 1.00 23.63  ? 77  ARG   B HH21 1 
ATOM   5574 H  HH22 . ARG   B 1 80  ? -22.945 -8.040  -16.729 1.00 23.63  ? 77  ARG   B HH22 1 
ATOM   5575 N  N    . VAL   B 1 81  ? -26.342 -2.373  -16.697 1.00 18.44  ? 78  VAL   B N    1 
ATOM   5576 C  CA   . VAL   B 1 81  ? -27.135 -2.585  -17.912 1.00 17.51  ? 78  VAL   B CA   1 
ATOM   5577 C  C    . VAL   B 1 81  ? -27.047 -1.354  -18.822 1.00 19.36  ? 78  VAL   B C    1 
ATOM   5578 O  O    . VAL   B 1 81  ? -26.949 -1.495  -20.057 1.00 17.62  ? 78  VAL   B O    1 
ATOM   5579 C  CB   . VAL   B 1 81  ? -28.586 -2.975  -17.554 1.00 17.03  ? 78  VAL   B CB   1 
ATOM   5580 C  CG1  . VAL   B 1 81  ? -29.371 -1.811  -16.956 1.00 22.65  ? 78  VAL   B CG1  1 
ATOM   5581 C  CG2  . VAL   B 1 81  ? -29.292 -3.534  -18.804 1.00 17.85  ? 78  VAL   B CG2  1 
ATOM   5582 H  H    . VAL   B 1 81  ? -26.789 -2.329  -15.963 1.00 22.17  ? 78  VAL   B H    1 
ATOM   5583 H  HA   . VAL   B 1 81  ? -26.762 -3.332  -18.406 1.00 21.05  ? 78  VAL   B HA   1 
ATOM   5584 H  HB   . VAL   B 1 81  ? -28.557 -3.661  -16.868 1.00 20.48  ? 78  VAL   B HB   1 
ATOM   5585 H  HG11 . VAL   B 1 81  ? -30.225 -2.139  -16.632 1.00 27.22  ? 78  VAL   B HG11 1 
ATOM   5586 H  HG12 . VAL   B 1 81  ? -28.863 -1.430  -16.223 1.00 27.22  ? 78  VAL   B HG12 1 
ATOM   5587 H  HG13 . VAL   B 1 81  ? -29.514 -1.141  -17.643 1.00 27.22  ? 78  VAL   B HG13 1 
ATOM   5588 H  HG21 . VAL   B 1 81  ? -30.176 -3.846  -18.555 1.00 21.46  ? 78  VAL   B HG21 1 
ATOM   5589 H  HG22 . VAL   B 1 81  ? -29.365 -2.830  -19.467 1.00 21.46  ? 78  VAL   B HG22 1 
ATOM   5590 H  HG23 . VAL   B 1 81  ? -28.770 -4.270  -19.160 1.00 21.46  ? 78  VAL   B HG23 1 
ATOM   5591 N  N    . LYS   B 1 82  ? -27.018 -0.143  -18.244 1.00 18.22  ? 79  LYS   B N    1 
ATOM   5592 C  CA   . LYS   B 1 82  ? -26.889 1.067   -19.042 1.00 20.02  ? 79  LYS   B CA   1 
ATOM   5593 C  C    . LYS   B 1 82  ? -25.523 1.150   -19.705 1.00 18.15  ? 79  LYS   B C    1 
ATOM   5594 O  O    . LYS   B 1 82  ? -25.412 1.533   -20.879 1.00 20.96  ? 79  LYS   B O    1 
ATOM   5595 C  CB   . LYS   B 1 82  ? -27.143 2.307   -18.182 1.00 21.18  ? 79  LYS   B CB   1 
ATOM   5596 C  CG   . LYS   B 1 82  ? -28.598 2.455   -17.716 1.00 24.16  ? 79  LYS   B CG   1 
ATOM   5597 C  CD   . LYS   B 1 82  ? -29.562 2.356   -18.854 1.00 29.43  ? 79  LYS   B CD   1 
ATOM   5598 C  CE   . LYS   B 1 82  ? -30.946 2.871   -18.499 1.00 36.29  ? 79  LYS   B CE   1 
ATOM   5599 N  NZ   . LYS   B 1 82  ? -31.833 2.815   -19.693 1.00 29.36  ? 79  LYS   B NZ   1 
ATOM   5600 H  H    . LYS   B 1 82  ? -27.071 -0.004  -17.397 1.00 21.90  ? 79  LYS   B H    1 
ATOM   5601 H  HA   . LYS   B 1 82  ? -27.564 1.047   -19.738 1.00 24.06  ? 79  LYS   B HA   1 
ATOM   5602 H  HB2  . LYS   B 1 82  ? -26.583 2.257   -17.392 1.00 25.46  ? 79  LYS   B HB2  1 
ATOM   5603 H  HB3  . LYS   B 1 82  ? -26.917 3.096   -18.700 1.00 25.46  ? 79  LYS   B HB3  1 
ATOM   5604 H  HG2  . LYS   B 1 82  ? -28.804 1.749   -17.082 1.00 29.03  ? 79  LYS   B HG2  1 
ATOM   5605 H  HG3  . LYS   B 1 82  ? -28.713 3.321   -17.296 1.00 29.03  ? 79  LYS   B HG3  1 
ATOM   5606 H  HD2  . LYS   B 1 82  ? -29.229 2.882   -19.598 1.00 35.36  ? 79  LYS   B HD2  1 
ATOM   5607 H  HD3  . LYS   B 1 82  ? -29.648 1.426   -19.117 1.00 35.36  ? 79  LYS   B HD3  1 
ATOM   5608 H  HE2  . LYS   B 1 82  ? -31.330 2.320   -17.799 1.00 43.59  ? 79  LYS   B HE2  1 
ATOM   5609 H  HE3  . LYS   B 1 82  ? -30.885 3.792   -18.200 1.00 43.59  ? 79  LYS   B HE3  1 
ATOM   5610 H  HZ1  . LYS   B 1 82  ? -32.686 2.855   -19.440 1.00 35.27  ? 79  LYS   B HZ1  1 
ATOM   5611 H  HZ2  . LYS   B 1 82  ? -31.659 3.499   -20.234 1.00 35.27  ? 79  LYS   B HZ2  1 
ATOM   5612 H  HZ3  . LYS   B 1 82  ? -31.699 2.054   -20.136 1.00 35.27  ? 79  LYS   B HZ3  1 
ATOM   5613 N  N    . ARG   B 1 83  ? -24.467 0.777   -18.975 1.00 18.73  ? 80  ARG   B N    1 
ATOM   5614 C  CA   . ARG   B 1 83  ? -23.123 0.771   -19.549 1.00 18.29  ? 80  ARG   B CA   1 
ATOM   5615 C  C    . ARG   B 1 83  ? -22.966 -0.297  -20.634 1.00 17.16  ? 80  ARG   B C    1 
ATOM   5616 O  O    . ARG   B 1 83  ? -22.244 -0.081  -21.625 1.00 19.55  ? 80  ARG   B O    1 
ATOM   5617 C  CB   . ARG   B 1 83  ? -22.105 0.562   -18.423 1.00 19.40  ? 80  ARG   B CB   1 
ATOM   5618 C  CG   . ARG   B 1 83  ? -20.639 0.683   -18.834 1.00 20.46  ? 80  ARG   B CG   1 
ATOM   5619 C  CD   . ARG   B 1 83  ? -20.249 2.073   -19.384 1.00 24.65  ? 80  ARG   B CD   1 
ATOM   5620 N  NE   . ARG   B 1 83  ? -20.342 2.101   -20.829 1.00 23.06  ? 80  ARG   B NE   1 
ATOM   5621 C  CZ   . ARG   B 1 83  ? -19.768 2.998   -21.612 1.00 26.43  ? 80  ARG   B CZ   1 
ATOM   5622 N  NH1  . ARG   B 1 83  ? -19.166 4.076   -21.124 1.00 28.35  ? 80  ARG   B NH1  1 
ATOM   5623 N  NH2  . ARG   B 1 83  ? -19.789 2.801   -22.929 1.00 24.89  ? 80  ARG   B NH2  1 
ATOM   5624 H  H    . ARG   B 1 83  ? -24.503 0.526   -18.153 1.00 22.52  ? 80  ARG   B H    1 
ATOM   5625 H  HA   . ARG   B 1 83  ? -22.952 1.627   -19.972 1.00 21.99  ? 80  ARG   B HA   1 
ATOM   5626 H  HB2  . ARG   B 1 83  ? -22.269 1.227   -17.736 1.00 23.32  ? 80  ARG   B HB2  1 
ATOM   5627 H  HB3  . ARG   B 1 83  ? -22.231 -0.329  -18.059 1.00 23.32  ? 80  ARG   B HB3  1 
ATOM   5628 H  HG2  . ARG   B 1 83  ? -20.084 0.508   -18.058 1.00 24.60  ? 80  ARG   B HG2  1 
ATOM   5629 H  HG3  . ARG   B 1 83  ? -20.456 0.030   -19.527 1.00 24.60  ? 80  ARG   B HG3  1 
ATOM   5630 H  HD2  . ARG   B 1 83  ? -20.850 2.744   -19.024 1.00 29.62  ? 80  ARG   B HD2  1 
ATOM   5631 H  HD3  . ARG   B 1 83  ? -19.335 2.276   -19.131 1.00 29.62  ? 80  ARG   B HD3  1 
ATOM   5632 H  HE   . ARG   B 1 83  ? -20.807 1.485   -21.208 1.00 27.71  ? 80  ARG   B HE   1 
ATOM   5633 H  HH11 . ARG   B 1 83  ? -19.142 4.207   -20.275 1.00 34.06  ? 80  ARG   B HH11 1 
ATOM   5634 H  HH12 . ARG   B 1 83  ? -18.801 4.643   -21.658 1.00 34.06  ? 80  ARG   B HH12 1 
ATOM   5635 H  HH21 . ARG   B 1 83  ? -20.170 2.102   -23.253 1.00 29.91  ? 80  ARG   B HH21 1 
ATOM   5636 H  HH22 . ARG   B 1 83  ? -19.421 3.373   -23.455 1.00 29.91  ? 80  ARG   B HH22 1 
ATOM   5637 N  N    . ASP   B 1 84  ? -23.584 -1.474  -20.447 1.00 16.69  ? 81  ASP   B N    1 
ATOM   5638 C  CA   . ASP   B 1 84  ? -23.570 -2.505  -21.490 1.00 16.79  ? 81  ASP   B CA   1 
ATOM   5639 C  C    . ASP   B 1 84  ? -24.246 -1.962  -22.751 1.00 17.66  ? 81  ASP   B C    1 
ATOM   5640 O  O    . ASP   B 1 84  ? -23.770 -2.156  -23.874 1.00 17.80  ? 81  ASP   B O    1 
ATOM   5641 C  CB   . ASP   B 1 84  ? -24.291 -3.775  -21.000 1.00 18.01  ? 81  ASP   B CB   1 
ATOM   5642 C  CG   . ASP   B 1 84  ? -23.407 -4.779  -20.222 1.00 21.56  ? 81  ASP   B CG   1 
ATOM   5643 O  OD1  . ASP   B 1 84  ? -22.177 -4.617  -20.107 1.00 19.81  ? 81  ASP   B OD1  1 
ATOM   5644 O  OD2  . ASP   B 1 84  ? -23.983 -5.807  -19.718 1.00 19.65  ? 81  ASP   B OD2  1 
ATOM   5645 H  H    . ASP   B 1 84  ? -24.013 -1.696  -19.735 1.00 20.07  ? 81  ASP   B H    1 
ATOM   5646 H  HA   . ASP   B 1 84  ? -22.654 -2.751  -21.693 1.00 20.19  ? 81  ASP   B HA   1 
ATOM   5647 H  HB2  . ASP   B 1 84  ? -25.013 -3.508  -20.409 1.00 21.66  ? 81  ASP   B HB2  1 
ATOM   5648 H  HB3  . ASP   B 1 84  ? -24.649 -4.242  -21.771 1.00 21.66  ? 81  ASP   B HB3  1 
ATOM   5649 N  N    . ALA   B 1 85  ? -25.399 -1.297  -22.580 1.00 18.66  ? 82  ALA   B N    1 
ATOM   5650 C  CA   . ALA   B 1 85  ? -26.109 -0.754  -23.747 1.00 18.39  ? 82  ALA   B CA   1 
ATOM   5651 C  C    . ALA   B 1 85  ? -25.285 0.323   -24.450 1.00 19.26  ? 82  ALA   B C    1 
ATOM   5652 O  O    . ALA   B 1 85  ? -25.171 0.325   -25.678 1.00 18.60  ? 82  ALA   B O    1 
ATOM   5653 C  CB   . ALA   B 1 85  ? -27.477 -0.203  -23.324 1.00 18.48  ? 82  ALA   B CB   1 
ATOM   5654 H  H    . ALA   B 1 85  ? -25.780 -1.150  -21.823 1.00 22.43  ? 82  ALA   B H    1 
ATOM   5655 H  HA   . ALA   B 1 85  ? -26.259 -1.473  -24.380 1.00 22.11  ? 82  ALA   B HA   1 
ATOM   5656 H  HB1  . ALA   B 1 85  ? -27.910 0.193   -24.097 1.00 22.22  ? 82  ALA   B HB1  1 
ATOM   5657 H  HB2  . ALA   B 1 85  ? -28.018 -0.930  -22.979 1.00 22.22  ? 82  ALA   B HB2  1 
ATOM   5658 H  HB3  . ALA   B 1 85  ? -27.348 0.469   -22.637 1.00 22.22  ? 82  ALA   B HB3  1 
ATOM   5659 N  N    . GLN   B 1 86  ? -24.641 1.215   -23.691 1.00 17.81  ? 83  GLN   B N    1 
ATOM   5660 C  CA   . GLN   B 1 86  ? -23.783 2.213   -24.302 1.00 17.47  ? 83  GLN   B CA   1 
ATOM   5661 C  C    . GLN   B 1 86  ? -22.622 1.542   -25.036 1.00 20.58  ? 83  GLN   B C    1 
ATOM   5662 O  O    . GLN   B 1 86  ? -22.203 2.024   -26.097 1.00 20.55  ? 83  GLN   B O    1 
ATOM   5663 C  CB   . GLN   B 1 86  ? -23.292 3.222   -23.253 1.00 21.65  ? 83  GLN   B CB   1 
ATOM   5664 C  CG   . GLN   B 1 86  ? -22.633 4.439   -23.876 1.00 24.94  ? 83  GLN   B CG   1 
ATOM   5665 C  CD   . GLN   B 1 86  ? -22.042 5.382   -22.837 1.00 28.47  ? 83  GLN   B CD   1 
ATOM   5666 O  OE1  . GLN   B 1 86  ? -22.307 5.268   -21.645 1.00 33.13  ? 83  GLN   B OE1  1 
ATOM   5667 N  NE2  . GLN   B 1 86  ? -21.187 6.278   -23.301 1.00 37.40  ? 83  GLN   B NE2  1 
ATOM   5668 H  H    . GLN   B 1 86  ? -24.688 1.258   -22.833 1.00 21.42  ? 83  GLN   B H    1 
ATOM   5669 H  HA   . GLN   B 1 86  ? -24.292 2.721   -24.952 1.00 21.01  ? 83  GLN   B HA   1 
ATOM   5670 H  HB2  . GLN   B 1 86  ? -24.048 3.526   -22.728 1.00 26.02  ? 83  GLN   B HB2  1 
ATOM   5671 H  HB3  . GLN   B 1 86  ? -22.641 2.789   -22.678 1.00 26.02  ? 83  GLN   B HB3  1 
ATOM   5672 H  HG2  . GLN   B 1 86  ? -21.915 4.147   -24.459 1.00 29.97  ? 83  GLN   B HG2  1 
ATOM   5673 H  HG3  . GLN   B 1 86  ? -23.295 4.931   -24.386 1.00 29.97  ? 83  GLN   B HG3  1 
ATOM   5674 H  HE21 . GLN   B 1 86  ? -21.000 6.299   -24.140 1.00 44.92  ? 83  GLN   B HE21 1 
ATOM   5675 H  HE22 . GLN   B 1 86  ? -20.819 6.840   -22.764 1.00 44.92  ? 83  GLN   B HE22 1 
ATOM   5676 N  N    . ASP   B 1 87  ? -22.078 0.443   -24.491 1.00 19.00  ? 84  ASP   B N    1 
ATOM   5677 C  CA   . ASP   B 1 87  ? -20.997 -0.268  -25.183 1.00 19.96  ? 84  ASP   B CA   1 
ATOM   5678 C  C    . ASP   B 1 87  ? -21.447 -0.736  -26.570 1.00 20.84  ? 84  ASP   B C    1 
ATOM   5679 O  O    . ASP   B 1 87  ? -20.692 -0.604  -27.555 1.00 20.61  ? 84  ASP   B O    1 
ATOM   5680 C  CB   . ASP   B 1 87  ? -20.522 -1.495  -24.377 1.00 19.81  ? 84  ASP   B CB   1 
ATOM   5681 C  CG   . ASP   B 1 87  ? -19.716 -1.159  -23.151 1.00 23.99  ? 84  ASP   B CG   1 
ATOM   5682 O  OD1  . ASP   B 1 87  ? -19.376 0.022   -22.944 1.00 24.15  ? 84  ASP   B OD1  1 
ATOM   5683 O  OD2  . ASP   B 1 87  ? -19.392 -2.111  -22.390 1.00 23.73  ? 84  ASP   B OD2  1 
ATOM   5684 H  H    . ASP   B 1 87  ? -22.312 0.098   -23.739 1.00 22.84  ? 84  ASP   B H    1 
ATOM   5685 H  HA   . ASP   B 1 87  ? -20.253 0.349   -25.266 1.00 23.99  ? 84  ASP   B HA   1 
ATOM   5686 H  HB2  . ASP   B 1 87  ? -21.300 -1.996  -24.088 1.00 23.82  ? 84  ASP   B HB2  1 
ATOM   5687 H  HB3  . ASP   B 1 87  ? -19.966 -2.046  -24.951 1.00 23.82  ? 84  ASP   B HB3  1 
ATOM   5688 N  N    . ILE   B 1 88  ? -22.661 -1.284  -26.668 1.00 18.74  ? 85  ILE   B N    1 
ATOM   5689 C  CA   . ILE   B 1 88  ? -23.144 -1.793  -27.944 1.00 17.26  ? 85  ILE   B CA   1 
ATOM   5690 C  C    . ILE   B 1 88  ? -23.342 -0.639  -28.916 1.00 19.11  ? 85  ILE   B C    1 
ATOM   5691 O  O    . ILE   B 1 88  ? -23.016 -0.757  -30.106 1.00 20.15  ? 85  ILE   B O    1 
ATOM   5692 C  CB   . ILE   B 1 88  ? -24.449 -2.607  -27.755 1.00 17.35  ? 85  ILE   B CB   1 
ATOM   5693 C  CG1  . ILE   B 1 88  ? -24.232 -3.814  -26.855 1.00 18.60  ? 85  ILE   B CG1  1 
ATOM   5694 C  CG2  . ILE   B 1 88  ? -25.044 -3.016  -29.104 1.00 18.94  ? 85  ILE   B CG2  1 
ATOM   5695 C  CD1  . ILE   B 1 88  ? -23.282 -4.823  -27.399 1.00 21.88  ? 85  ILE   B CD1  1 
ATOM   5696 H  H    . ILE   B 1 88  ? -23.215 -1.371  -26.016 1.00 22.53  ? 85  ILE   B H    1 
ATOM   5697 H  HA   . ILE   B 1 88  ? -22.476 -2.396  -28.309 1.00 20.76  ? 85  ILE   B HA   1 
ATOM   5698 H  HB   . ILE   B 1 88  ? -25.089 -2.029  -27.310 1.00 20.87  ? 85  ILE   B HB   1 
ATOM   5699 H  HG12 . ILE   B 1 88  ? -23.880 -3.507  -26.005 1.00 22.36  ? 85  ILE   B HG12 1 
ATOM   5700 H  HG13 . ILE   B 1 88  ? -25.085 -4.256  -26.720 1.00 22.36  ? 85  ILE   B HG13 1 
ATOM   5701 H  HG21 . ILE   B 1 88  ? -25.722 -3.694  -28.958 1.00 22.77  ? 85  ILE   B HG21 1 
ATOM   5702 H  HG22 . ILE   B 1 88  ? -25.442 -2.236  -29.523 1.00 22.77  ? 85  ILE   B HG22 1 
ATOM   5703 H  HG23 . ILE   B 1 88  ? -24.338 -3.369  -29.667 1.00 22.77  ? 85  ILE   B HG23 1 
ATOM   5704 H  HD11 . ILE   B 1 88  ? -23.299 -5.611  -26.833 1.00 26.30  ? 85  ILE   B HD11 1 
ATOM   5705 H  HD12 . ILE   B 1 88  ? -23.553 -5.058  -28.301 1.00 26.30  ? 85  ILE   B HD12 1 
ATOM   5706 H  HD13 . ILE   B 1 88  ? -22.390 -4.443  -27.410 1.00 26.30  ? 85  ILE   B HD13 1 
ATOM   5707 N  N    . ALA   B 1 89  ? -23.889 0.494   -28.440 1.00 18.39  ? 86  ALA   B N    1 
ATOM   5708 C  CA   . ALA   B 1 89  ? -24.055 1.660   -29.304 1.00 19.61  ? 86  ALA   B CA   1 
ATOM   5709 C  C    . ALA   B 1 89  ? -22.726 2.183   -29.818 1.00 22.51  ? 86  ALA   B C    1 
ATOM   5710 O  O    . ALA   B 1 89  ? -22.608 2.539   -31.001 1.00 23.28  ? 86  ALA   B O    1 
ATOM   5711 C  CB   . ALA   B 1 89  ? -24.819 2.760   -28.557 1.00 24.33  ? 86  ALA   B CB   1 
ATOM   5712 H  H    . ALA   B 1 89  ? -24.165 0.606   -27.633 1.00 22.11  ? 86  ALA   B H    1 
ATOM   5713 H  HA   . ALA   B 1 89  ? -24.577 1.395   -30.077 1.00 23.58  ? 86  ALA   B HA   1 
ATOM   5714 H  HB1  . ALA   B 1 89  ? -24.864 3.550   -29.117 1.00 29.24  ? 86  ALA   B HB1  1 
ATOM   5715 H  HB2  . ALA   B 1 89  ? -25.715 2.443   -28.360 1.00 29.24  ? 86  ALA   B HB2  1 
ATOM   5716 H  HB3  . ALA   B 1 89  ? -24.352 2.964   -27.732 1.00 29.24  ? 86  ALA   B HB3  1 
ATOM   5717 N  N    . GLU   B 1 90  ? -21.710 2.255   -28.953 1.00 23.06  ? 87  GLU   B N    1 
ATOM   5718 C  CA   . GLU   B 1 90  ? -20.419 2.740   -29.425 1.00 22.76  ? 87  GLU   B CA   1 
ATOM   5719 C  C    . GLU   B 1 90  ? -19.781 1.742   -30.375 1.00 22.89  ? 87  GLU   B C    1 
ATOM   5720 O  O    . GLU   B 1 90  ? -19.107 2.138   -31.339 1.00 24.45  ? 87  GLU   B O    1 
ATOM   5721 C  CB   . GLU   B 1 90  ? -19.499 3.061   -28.253 1.00 25.18  ? 87  GLU   B CB   1 
ATOM   5722 C  CG   . GLU   B 1 90  ? -20.171 4.073   -27.342 1.00 31.46  ? 87  GLU   B CG   1 
ATOM   5723 C  CD   . GLU   B 1 90  ? -19.258 4.887   -26.511 1.00 52.68  ? 87  GLU   B CD   1 
ATOM   5724 O  OE1  . GLU   B 1 90  ? -18.832 5.959   -26.983 1.00 64.19  ? 87  GLU   B OE1  1 
ATOM   5725 O  OE2  . GLU   B 1 90  ? -19.011 4.474   -25.367 1.00 44.87  ? 87  GLU   B OE2  1 
ATOM   5726 H  H    . GLU   B 1 90  ? -21.744 2.037   -28.122 1.00 27.71  ? 87  GLU   B H    1 
ATOM   5727 H  HA   . GLU   B 1 90  ? -20.553 3.570   -29.909 1.00 27.35  ? 87  GLU   B HA   1 
ATOM   5728 H  HB2  . GLU   B 1 90  ? -19.319 2.254   -27.747 1.00 30.26  ? 87  GLU   B HB2  1 
ATOM   5729 H  HB3  . GLU   B 1 90  ? -18.668 3.439   -28.583 1.00 30.26  ? 87  GLU   B HB3  1 
ATOM   5730 H  HG2  . GLU   B 1 90  ? -20.684 4.685   -27.892 1.00 37.79  ? 87  GLU   B HG2  1 
ATOM   5731 H  HG3  . GLU   B 1 90  ? -20.761 3.595   -26.738 1.00 37.79  ? 87  GLU   B HG3  1 
ATOM   5732 N  N    . LEU   B 1 91  ? -19.984 0.456   -30.117 1.00 21.92  ? 88  LEU   B N    1 
ATOM   5733 C  CA   . LEU   B 1 91  ? -19.490 -0.572  -31.029 1.00 20.92  ? 88  LEU   B CA   1 
ATOM   5734 C  C    . LEU   B 1 91  ? -20.133 -0.430  -32.399 1.00 24.18  ? 88  LEU   B C    1 
ATOM   5735 O  O    . LEU   B 1 91  ? -19.444 -0.433  -33.436 1.00 23.58  ? 88  LEU   B O    1 
ATOM   5736 C  CB   . LEU   B 1 91  ? -19.752 -1.947  -30.421 1.00 20.51  ? 88  LEU   B CB   1 
ATOM   5737 C  CG   . LEU   B 1 91  ? -19.276 -3.151  -31.243 1.00 23.09  ? 88  LEU   B CG   1 
ATOM   5738 C  CD1  . LEU   B 1 91  ? -17.772 -3.085  -31.518 1.00 26.08  ? 88  LEU   B CD1  1 
ATOM   5739 C  CD2  . LEU   B 1 91  ? -19.634 -4.389  -30.476 1.00 24.04  ? 88  LEU   B CD2  1 
ATOM   5740 H  H    . LEU   B 1 91  ? -20.400 0.153   -29.428 1.00 26.34  ? 88  LEU   B H    1 
ATOM   5741 H  HA   . LEU   B 1 91  ? -18.532 -0.478  -31.149 1.00 25.14  ? 88  LEU   B HA   1 
ATOM   5742 H  HB2  . LEU   B 1 91  ? -19.300 -1.988  -29.563 1.00 24.66  ? 88  LEU   B HB2  1 
ATOM   5743 H  HB3  . LEU   B 1 91  ? -20.709 -2.044  -30.296 1.00 24.66  ? 88  LEU   B HB3  1 
ATOM   5744 H  HG   . LEU   B 1 91  ? -19.705 -3.161  -32.113 1.00 27.75  ? 88  LEU   B HG   1 
ATOM   5745 H  HD11 . LEU   B 1 91  ? -17.493 -3.910  -31.945 1.00 31.34  ? 88  LEU   B HD11 1 
ATOM   5746 H  HD12 . LEU   B 1 91  ? -17.590 -2.332  -32.102 1.00 31.34  ? 88  LEU   B HD12 1 
ATOM   5747 H  HD13 . LEU   B 1 91  ? -17.302 -2.972  -30.677 1.00 31.34  ? 88  LEU   B HD13 1 
ATOM   5748 H  HD21 . LEU   B 1 91  ? -19.266 -5.161  -30.934 1.00 28.88  ? 88  LEU   B HD21 1 
ATOM   5749 H  HD22 . LEU   B 1 91  ? -19.261 -4.326  -29.583 1.00 28.88  ? 88  LEU   B HD22 1 
ATOM   5750 H  HD23 . LEU   B 1 91  ? -20.600 -4.463  -30.427 1.00 28.88  ? 88  LEU   B HD23 1 
ATOM   5751 N  N    . ALA   B 1 92  ? -21.454 -0.245  -32.430 1.00 20.94  ? 89  ALA   B N    1 
ATOM   5752 C  CA   . ALA   B 1 92  ? -22.139 -0.074  -33.716 1.00 22.46  ? 89  ALA   B CA   1 
ATOM   5753 C  C    . ALA   B 1 92  ? -21.584 1.125   -34.477 1.00 24.62  ? 89  ALA   B C    1 
ATOM   5754 O  O    . ALA   B 1 92  ? -21.323 1.047   -35.688 1.00 25.73  ? 89  ALA   B O    1 
ATOM   5755 C  CB   . ALA   B 1 92  ? -23.658 0.051   -33.497 1.00 21.33  ? 89  ALA   B CB   1 
ATOM   5756 H  H    . ALA   B 1 92  ? -21.965 -0.214  -31.740 1.00 25.17  ? 89  ALA   B H    1 
ATOM   5757 H  HA   . ALA   B 1 92  ? -21.990 -0.863  -34.261 1.00 26.99  ? 89  ALA   B HA   1 
ATOM   5758 H  HB1  . ALA   B 1 92  ? -24.096 0.122   -34.359 1.00 25.63  ? 89  ALA   B HB1  1 
ATOM   5759 H  HB2  . ALA   B 1 92  ? -23.975 -0.738  -33.029 1.00 25.63  ? 89  ALA   B HB2  1 
ATOM   5760 H  HB3  . ALA   B 1 92  ? -23.836 0.844   -32.968 1.00 25.63  ? 89  ALA   B HB3  1 
ATOM   5761 N  N    . LYS   B 1 93  ? -21.424 2.262   -33.798 1.00 22.95  ? 90  LYS   B N    1 
ATOM   5762 C  CA   . LYS   B 1 93  ? -20.939 3.464   -34.475 1.00 24.42  ? 90  LYS   B CA   1 
ATOM   5763 C  C    . LYS   B 1 93  ? -19.502 3.294   -34.955 1.00 25.22  ? 90  LYS   B C    1 
ATOM   5764 O  O    . LYS   B 1 93  ? -19.111 3.876   -35.974 1.00 27.66  ? 90  LYS   B O    1 
ATOM   5765 C  CB   . LYS   B 1 93  ? -21.078 4.660   -33.540 1.00 26.34  ? 90  LYS   B CB   1 
ATOM   5766 C  CG   . LYS   B 1 93  ? -22.545 4.974   -33.234 1.00 32.06  ? 90  LYS   B CG   1 
ATOM   5767 C  CD   . LYS   B 1 93  ? -22.709 6.385   -32.719 1.00 40.31  ? 90  LYS   B CD   1 
ATOM   5768 C  CE   . LYS   B 1 93  ? -23.219 6.454   -31.299 1.00 48.04  ? 90  LYS   B CE   1 
ATOM   5769 N  NZ   . LYS   B 1 93  ? -24.531 7.167   -31.193 1.00 54.79  ? 90  LYS   B NZ   1 
ATOM   5770 H  H    . LYS   B 1 93  ? -21.585 2.362   -32.960 1.00 27.58  ? 90  LYS   B H    1 
ATOM   5771 H  HA   . LYS   B 1 93  ? -21.482 3.639   -35.260 1.00 29.34  ? 90  LYS   B HA   1 
ATOM   5772 H  HB2  . LYS   B 1 93  ? -20.626 4.466   -32.704 1.00 31.65  ? 90  LYS   B HB2  1 
ATOM   5773 H  HB3  . LYS   B 1 93  ? -20.680 5.440   -33.958 1.00 31.65  ? 90  LYS   B HB3  1 
ATOM   5774 H  HG2  . LYS   B 1 93  ? -23.071 4.881   -34.044 1.00 38.51  ? 90  LYS   B HG2  1 
ATOM   5775 H  HG3  . LYS   B 1 93  ? -22.871 4.362   -32.555 1.00 38.51  ? 90  LYS   B HG3  1 
ATOM   5776 H  HD2  . LYS   B 1 93  ? -21.848 6.831   -32.747 1.00 48.41  ? 90  LYS   B HD2  1 
ATOM   5777 H  HD3  . LYS   B 1 93  ? -23.344 6.853   -33.285 1.00 48.41  ? 90  LYS   B HD3  1 
ATOM   5778 H  HE2  . LYS   B 1 93  ? -23.338 5.553   -30.961 1.00 57.69  ? 90  LYS   B HE2  1 
ATOM   5779 H  HE3  . LYS   B 1 93  ? -22.573 6.931   -30.754 1.00 57.69  ? 90  LYS   B HE3  1 
ATOM   5780 H  HZ1  . LYS   B 1 93  ? -24.775 7.230   -30.339 1.00 65.80  ? 90  LYS   B HZ1  1 
ATOM   5781 H  HZ2  . LYS   B 1 93  ? -24.461 7.986   -31.534 1.00 65.80  ? 90  LYS   B HZ2  1 
ATOM   5782 H  HZ3  . LYS   B 1 93  ? -25.157 6.720   -31.640 1.00 65.80  ? 90  LYS   B HZ3  1 
ATOM   5783 N  N    . SER   B 1 94  ? -18.700 2.506   -34.236 1.00 26.25  ? 91  SER   B N    1 
ATOM   5784 C  CA   . SER   B 1 94  ? -17.315 2.271   -34.649 1.00 27.30  ? 91  SER   B CA   1 
ATOM   5785 C  C    . SER   B 1 94  ? -17.203 1.380   -35.881 1.00 25.47  ? 91  SER   B C    1 
ATOM   5786 O  O    . SER   B 1 94  ? -16.200 1.463   -36.600 1.00 30.74  ? 91  SER   B O    1 
ATOM   5787 C  CB   . SER   B 1 94  ? -16.526 1.678   -33.469 1.00 28.32  ? 91  SER   B CB   1 
ATOM   5788 O  OG   . SER   B 1 94  ? -16.687 0.264   -33.360 1.00 29.78  ? 91  SER   B OG   1 
ATOM   5789 H  H    . SER   B 1 94  ? -18.929 2.101   -33.513 1.00 31.54  ? 91  SER   B H    1 
ATOM   5790 H  HA   . SER   B 1 94  ? -16.908 3.118   -34.887 1.00 32.81  ? 91  SER   B HA   1 
ATOM   5791 H  HB2  . SER   B 1 94  ? -15.584 1.874   -33.598 1.00 34.02  ? 91  SER   B HB2  1 
ATOM   5792 H  HB3  . SER   B 1 94  ? -16.841 2.089   -32.649 1.00 34.02  ? 91  SER   B HB3  1 
ATOM   5793 H  HG   . SER   B 1 94  ? -17.442 0.085   -33.040 1.00 35.77  ? 91  SER   B HG   1 
ATOM   5794 N  N    . LEU   B 1 95  ? -18.202 0.552   -36.153 1.00 25.33  ? 92  LEU   B N    1 
ATOM   5795 C  CA   . LEU   B 1 95  ? -18.128 -0.446  -37.210 1.00 28.37  ? 92  LEU   B CA   1 
ATOM   5796 C  C    . LEU   B 1 95  ? -18.982 -0.121  -38.420 1.00 31.74  ? 92  LEU   B C    1 
ATOM   5797 O  O    . LEU   B 1 95  ? -18.759 -0.713  -39.480 1.00 32.55  ? 92  LEU   B O    1 
ATOM   5798 C  CB   . LEU   B 1 95  ? -18.584 -1.817  -36.680 1.00 26.07  ? 92  LEU   B CB   1 
ATOM   5799 C  CG   . LEU   B 1 95  ? -17.662 -2.479  -35.656 1.00 28.20  ? 92  LEU   B CG   1 
ATOM   5800 C  CD1  . LEU   B 1 95  ? -18.329 -3.732  -35.148 1.00 34.94  ? 92  LEU   B CD1  1 
ATOM   5801 C  CD2  . LEU   B 1 95  ? -16.320 -2.808  -36.260 1.00 34.16  ? 92  LEU   B CD2  1 
ATOM   5802 H  H    . LEU   B 1 95  ? -18.951 0.548   -35.730 1.00 30.44  ? 92  LEU   B H    1 
ATOM   5803 H  HA   . LEU   B 1 95  ? -17.203 -0.512  -37.495 1.00 34.09  ? 92  LEU   B HA   1 
ATOM   5804 H  HB2  . LEU   B 1 95  ? -19.450 -1.705  -36.258 1.00 31.32  ? 92  LEU   B HB2  1 
ATOM   5805 H  HB3  . LEU   B 1 95  ? -18.659 -2.422  -37.434 1.00 31.32  ? 92  LEU   B HB3  1 
ATOM   5806 H  HG   . LEU   B 1 95  ? -17.501 -1.871  -34.918 1.00 33.88  ? 92  LEU   B HG   1 
ATOM   5807 H  HD11 . LEU   B 1 95  ? -17.766 -4.137  -34.470 1.00 41.98  ? 92  LEU   B HD11 1 
ATOM   5808 H  HD12 . LEU   B 1 95  ? -19.191 -3.499  -34.767 1.00 41.98  ? 92  LEU   B HD12 1 
ATOM   5809 H  HD13 . LEU   B 1 95  ? -18.450 -4.347  -35.888 1.00 41.98  ? 92  LEU   B HD13 1 
ATOM   5810 H  HD21 . LEU   B 1 95  ? -15.795 -3.303  -35.612 1.00 41.04  ? 92  LEU   B HD21 1 
ATOM   5811 H  HD22 . LEU   B 1 95  ? -16.456 -3.345  -37.056 1.00 41.04  ? 92  LEU   B HD22 1 
ATOM   5812 H  HD23 . LEU   B 1 95  ? -15.868 -1.982  -36.492 1.00 41.04  ? 92  LEU   B HD23 1 
ATOM   5813 N  N    . SER   B 1 96  ? -19.933 0.805   -38.305 1.00 28.99  ? 93  SER   B N    1 
ATOM   5814 C  CA   . SER   B 1 96  ? -20.937 1.017   -39.345 1.00 29.80  ? 93  SER   B CA   1 
ATOM   5815 C  C    . SER   B 1 96  ? -21.379 2.471   -39.363 1.00 26.62  ? 93  SER   B C    1 
ATOM   5816 O  O    . SER   B 1 96  ? -21.567 3.072   -38.304 1.00 33.89  ? 93  SER   B O    1 
ATOM   5817 C  CB   . SER   B 1 96  ? -22.146 0.104   -39.099 1.00 27.98  ? 93  SER   B CB   1 
ATOM   5818 O  OG   . SER   B 1 96  ? -23.173 0.312   -40.048 1.00 33.03  ? 93  SER   B OG   1 
ATOM   5819 H  H    . SER   B 1 96  ? -20.017 1.328   -37.627 1.00 34.84  ? 93  SER   B H    1 
ATOM   5820 H  HA   . SER   B 1 96  ? -20.552 0.826   -40.214 1.00 35.80  ? 93  SER   B HA   1 
ATOM   5821 H  HB2  . SER   B 1 96  ? -21.854 -0.819  -39.155 1.00 33.62  ? 93  SER   B HB2  1 
ATOM   5822 H  HB3  . SER   B 1 96  ? -22.498 0.287   -38.214 1.00 33.62  ? 93  SER   B HB3  1 
ATOM   5823 H  HG   . SER   B 1 96  ? -23.548 1.051   -39.909 1.00 39.68  ? 93  SER   B HG   1 
ATOM   5824 N  N    . ASP   B 1 97  ? -21.543 3.037   -40.561 1.00 31.06  ? 94  ASP   B N    1 
ATOM   5825 C  CA   . ASP   B 1 97  ? -22.183 4.344   -40.676 1.00 35.44  ? 94  ASP   B CA   1 
ATOM   5826 C  C    . ASP   B 1 97  ? -23.703 4.266   -40.838 1.00 40.76  ? 94  ASP   B C    1 
ATOM   5827 O  O    . ASP   B 1 97  ? -24.368 5.307   -40.775 1.00 48.83  ? 94  ASP   B O    1 
ATOM   5828 C  CB   . ASP   B 1 97  ? -21.572 5.131   -41.842 1.00 45.75  ? 94  ASP   B CB   1 
ATOM   5829 C  CG   . ASP   B 1 97  ? -20.051 5.197   -41.753 1.00 57.06  ? 94  ASP   B CG   1 
ATOM   5830 O  OD1  . ASP   B 1 97  ? -19.529 5.595   -40.677 1.00 59.26  ? 94  ASP   B OD1  1 
ATOM   5831 O  OD2  . ASP   B 1 97  ? -19.380 4.859   -42.746 1.00 58.93  ? 94  ASP   B OD2  1 
ATOM   5832 H  H    . ASP   B 1 97  ? -21.296 2.688   -41.307 1.00 37.31  ? 94  ASP   B H    1 
ATOM   5833 H  HA   . ASP   B 1 97  ? -22.009 4.845   -39.864 1.00 42.58  ? 94  ASP   B HA   1 
ATOM   5834 H  HB2  . ASP   B 1 97  ? -21.807 4.698   -42.678 1.00 54.94  ? 94  ASP   B HB2  1 
ATOM   5835 H  HB3  . ASP   B 1 97  ? -21.915 6.038   -41.830 1.00 54.94  ? 94  ASP   B HB3  1 
ATOM   5836 N  N    . GLU   B 1 98  ? -24.266 3.070   -41.037 1.00 35.32  ? 95  GLU   B N    1 
ATOM   5837 C  CA   . GLU   B 1 98  ? -25.710 2.854   -41.022 1.00 33.48  ? 95  GLU   B CA   1 
ATOM   5838 C  C    . GLU   B 1 98  ? -26.140 2.224   -39.704 1.00 26.80  ? 95  GLU   B C    1 
ATOM   5839 O  O    . GLU   B 1 98  ? -25.339 1.587   -39.010 1.00 27.77  ? 95  GLU   B O    1 
ATOM   5840 C  CB   . GLU   B 1 98  ? -26.129 1.910   -42.160 1.00 35.48  ? 95  GLU   B CB   1 
ATOM   5841 C  CG   . GLU   B 1 98  ? -26.117 2.496   -43.573 1.00 46.19  ? 95  GLU   B CG   1 
ATOM   5842 C  CD   . GLU   B 1 98  ? -26.787 3.857   -43.651 1.00 67.81  ? 95  GLU   B CD   1 
ATOM   5843 O  OE1  . GLU   B 1 98  ? -28.036 3.908   -43.688 1.00 66.57  ? 95  GLU   B OE1  1 
ATOM   5844 O  OE2  . GLU   B 1 98  ? -26.061 4.874   -43.668 1.00 74.23  ? 95  GLU   B OE2  1 
ATOM   5845 H  H    . GLU   B 1 98  ? -23.817 2.352   -41.186 1.00 42.42  ? 95  GLU   B H    1 
ATOM   5846 H  HA   . GLU   B 1 98  ? -26.156 3.707   -41.140 1.00 40.22  ? 95  GLU   B HA   1 
ATOM   5847 H  HB2  . GLU   B 1 98  ? -25.523 1.153   -42.162 1.00 42.61  ? 95  GLU   B HB2  1 
ATOM   5848 H  HB3  . GLU   B 1 98  ? -27.034 1.610   -41.984 1.00 42.61  ? 95  GLU   B HB3  1 
ATOM   5849 H  HG2  . GLU   B 1 98  ? -25.198 2.597   -43.865 1.00 55.47  ? 95  GLU   B HG2  1 
ATOM   5850 H  HG3  . GLU   B 1 98  ? -26.591 1.894   -44.168 1.00 55.47  ? 95  GLU   B HG3  1 
ATOM   5851 N  N    . PRO   B 1 99  ? -27.403 2.376   -39.317 1.00 26.31  ? 96  PRO   B N    1 
ATOM   5852 C  CA   . PRO   B 1 99  ? -27.911 1.583   -38.190 1.00 23.70  ? 96  PRO   B CA   1 
ATOM   5853 C  C    . PRO   B 1 99  ? -27.727 0.101   -38.494 1.00 25.85  ? 96  PRO   B C    1 
ATOM   5854 O  O    . PRO   B 1 99  ? -27.703 -0.302  -39.659 1.00 27.01  ? 96  PRO   B O    1 
ATOM   5855 C  CB   . PRO   B 1 99  ? -29.393 1.970   -38.099 1.00 25.54  ? 96  PRO   B CB   1 
ATOM   5856 C  CG   . PRO   B 1 99  ? -29.592 3.125   -39.010 1.00 34.95  ? 96  PRO   B CG   1 
ATOM   5857 C  CD   . PRO   B 1 99  ? -28.399 3.296   -39.886 1.00 34.16  ? 96  PRO   B CD   1 
ATOM   5858 H  HA   . PRO   B 1 99  ? -27.480 1.822   -37.354 1.00 28.49  ? 96  PRO   B HA   1 
ATOM   5859 H  HB2  . PRO   B 1 99  ? -29.940 1.219   -38.377 1.00 30.69  ? 96  PRO   B HB2  1 
ATOM   5860 H  HB3  . PRO   B 1 99  ? -29.606 2.216   -37.185 1.00 30.69  ? 96  PRO   B HB3  1 
ATOM   5861 H  HG2  . PRO   B 1 99  ? -30.377 2.959   -39.555 1.00 41.98  ? 96  PRO   B HG2  1 
ATOM   5862 H  HG3  . PRO   B 1 99  ? -29.722 3.923   -38.475 1.00 41.98  ? 96  PRO   B HG3  1 
ATOM   5863 H  HD2  . PRO   B 1 99  ? -28.608 3.051   -40.801 1.00 41.03  ? 96  PRO   B HD2  1 
ATOM   5864 H  HD3  . PRO   B 1 99  ? -28.078 4.211   -39.852 1.00 41.03  ? 96  PRO   B HD3  1 
ATOM   5865 N  N    . VAL   B 1 100 ? -27.610 -0.711  -37.434 1.00 23.01  ? 97  VAL   B N    1 
ATOM   5866 C  CA   . VAL   B 1 100 ? -27.179 -2.099  -37.554 1.00 21.49  ? 97  VAL   B CA   1 
ATOM   5867 C  C    . VAL   B 1 100 ? -28.284 -3.044  -37.069 1.00 20.54  ? 97  VAL   B C    1 
ATOM   5868 O  O    . VAL   B 1 100 ? -29.317 -2.645  -36.504 1.00 20.98  ? 97  VAL   B O    1 
ATOM   5869 C  CB   . VAL   B 1 100 ? -25.871 -2.388  -36.787 1.00 18.84  ? 97  VAL   B CB   1 
ATOM   5870 C  CG1  . VAL   B 1 100 ? -24.717 -1.409  -37.231 1.00 22.71  ? 97  VAL   B CG1  1 
ATOM   5871 C  CG2  . VAL   B 1 100 ? -26.109 -2.317  -35.265 1.00 22.03  ? 97  VAL   B CG2  1 
ATOM   5872 H  H    . VAL   B 1 100 ? -27.778 -0.471  -36.625 1.00 27.65  ? 97  VAL   B H    1 
ATOM   5873 H  HA   . VAL   B 1 100 ? -27.035 -2.271  -38.498 1.00 25.83  ? 97  VAL   B HA   1 
ATOM   5874 H  HB   . VAL   B 1 100 ? -25.581 -3.288  -37.002 1.00 22.65  ? 97  VAL   B HB   1 
ATOM   5875 H  HG11 . VAL   B 1 100 ? -23.885 -1.695  -36.823 1.00 27.30  ? 97  VAL   B HG11 1 
ATOM   5876 H  HG12 . VAL   B 1 100 ? -24.636 -1.433  -38.198 1.00 27.30  ? 97  VAL   B HG12 1 
ATOM   5877 H  HG13 . VAL   B 1 100 ? -24.936 -0.510  -36.941 1.00 27.30  ? 97  VAL   B HG13 1 
ATOM   5878 H  HG21 . VAL   B 1 100 ? -25.253 -2.347  -34.809 1.00 26.48  ? 97  VAL   B HG21 1 
ATOM   5879 H  HG22 . VAL   B 1 100 ? -26.567 -1.488  -35.055 1.00 26.48  ? 97  VAL   B HG22 1 
ATOM   5880 H  HG23 . VAL   B 1 100 ? -26.654 -3.073  -34.995 1.00 26.48  ? 97  VAL   B HG23 1 
ATOM   5881 N  N    . TYR   B 1 101 ? -28.056 -4.334  -37.322 1.00 18.98  ? 98  TYR   B N    1 
ATOM   5882 C  CA   . TYR   B 1 101 ? -28.937 -5.383  -36.815 1.00 19.35  ? 98  TYR   B CA   1 
ATOM   5883 C  C    . TYR   B 1 101 ? -28.420 -5.861  -35.475 1.00 18.63  ? 98  TYR   B C    1 
ATOM   5884 O  O    . TYR   B 1 101 ? -27.215 -6.013  -35.297 1.00 17.86  ? 98  TYR   B O    1 
ATOM   5885 C  CB   . TYR   B 1 101 ? -28.987 -6.546  -37.799 1.00 18.09  ? 98  TYR   B CB   1 
ATOM   5886 C  CG   . TYR   B 1 101 ? -29.566 -6.207  -39.161 1.00 24.17  ? 98  TYR   B CG   1 
ATOM   5887 C  CD1  . TYR   B 1 101 ? -28.766 -5.675  -40.163 1.00 24.21  ? 98  TYR   B CD1  1 
ATOM   5888 C  CD2  . TYR   B 1 101 ? -30.901 -6.392  -39.433 1.00 21.32  ? 98  TYR   B CD2  1 
ATOM   5889 C  CE1  . TYR   B 1 101 ? -29.286 -5.373  -41.412 1.00 25.56  ? 98  TYR   B CE1  1 
ATOM   5890 C  CE2  . TYR   B 1 101 ? -31.447 -6.106  -40.684 1.00 24.63  ? 98  TYR   B CE2  1 
ATOM   5891 C  CZ   . TYR   B 1 101 ? -30.623 -5.582  -41.668 1.00 23.66  ? 98  TYR   B CZ   1 
ATOM   5892 O  OH   . TYR   B 1 101 ? -31.157 -5.265  -42.903 1.00 27.92  ? 98  TYR   B OH   1 
ATOM   5893 H  H    . TYR   B 1 101 ? -27.394 -4.627  -37.786 1.00 22.82  ? 98  TYR   B H    1 
ATOM   5894 H  HA   . TYR   B 1 101 ? -29.839 -5.043  -36.702 1.00 23.26  ? 98  TYR   B HA   1 
ATOM   5895 H  HB2  . TYR   B 1 101 ? -28.083 -6.868  -37.939 1.00 21.75  ? 98  TYR   B HB2  1 
ATOM   5896 H  HB3  . TYR   B 1 101 ? -29.534 -7.249  -37.416 1.00 21.75  ? 98  TYR   B HB3  1 
ATOM   5897 H  HD1  . TYR   B 1 101 ? -27.865 -5.520  -39.993 1.00 29.10  ? 98  TYR   B HD1  1 
ATOM   5898 H  HD2  . TYR   B 1 101 ? -31.456 -6.719  -38.763 1.00 25.63  ? 98  TYR   B HD2  1 
ATOM   5899 H  HE1  . TYR   B 1 101 ? -28.733 -5.030  -42.077 1.00 30.71  ? 98  TYR   B HE1  1 
ATOM   5900 H  HE2  . TYR   B 1 101 ? -32.347 -6.264  -40.855 1.00 29.60  ? 98  TYR   B HE2  1 
ATOM   5901 H  HH   . TYR   B 1 101 ? -30.540 -5.089  -43.446 1.00 33.55  ? 98  TYR   B HH   1 
ATOM   5902 N  N    . ILE   B 1 102 ? -29.323 -6.101  -34.528 1.00 16.62  ? 99  ILE   B N    1 
ATOM   5903 C  CA   . ILE   B 1 102 ? -28.940 -6.528  -33.197 1.00 15.75  ? 99  ILE   B CA   1 
ATOM   5904 C  C    . ILE   B 1 102 ? -29.829 -7.661  -32.714 1.00 16.49  ? 99  ILE   B C    1 
ATOM   5905 O  O    . ILE   B 1 102 ? -31.050 -7.585  -32.829 1.00 16.22  ? 99  ILE   B O    1 
ATOM   5906 C  CB   . ILE   B 1 102 ? -29.017 -5.340  -32.205 1.00 15.32  ? 99  ILE   B CB   1 
ATOM   5907 C  CG1  . ILE   B 1 102 ? -28.084 -4.203  -32.616 1.00 19.64  ? 99  ILE   B CG1  1 
ATOM   5908 C  CG2  . ILE   B 1 102 ? -28.689 -5.790  -30.783 1.00 15.81  ? 99  ILE   B CG2  1 
ATOM   5909 C  CD1  . ILE   B 1 102 ? -28.150 -2.909  -31.753 1.00 18.89  ? 99  ILE   B CD1  1 
ATOM   5910 H  H    . ILE   B 1 102 ? -30.172 -6.022  -34.639 1.00 19.99  ? 99  ILE   B H    1 
ATOM   5911 H  HA   . ILE   B 1 102 ? -28.036 -6.877  -33.241 1.00 18.94  ? 99  ILE   B HA   1 
ATOM   5912 H  HB   . ILE   B 1 102 ? -29.930 -5.012  -32.231 1.00 18.42  ? 99  ILE   B HB   1 
ATOM   5913 H  HG12 . ILE   B 1 102 ? -27.172 -4.530  -32.570 1.00 23.61  ? 99  ILE   B HG12 1 
ATOM   5914 H  HG13 . ILE   B 1 102 ? -28.300 -3.950  -33.527 1.00 23.61  ? 99  ILE   B HG13 1 
ATOM   5915 H  HG21 . ILE   B 1 102 ? -28.806 -5.039  -30.179 1.00 19.02  ? 99  ILE   B HG21 1 
ATOM   5916 H  HG22 . ILE   B 1 102 ? -29.287 -6.511  -30.534 1.00 19.02  ? 99  ILE   B HG22 1 
ATOM   5917 H  HG23 . ILE   B 1 102 ? -27.769 -6.097  -30.753 1.00 19.02  ? 99  ILE   B HG23 1 
ATOM   5918 H  HD11 . ILE   B 1 102 ? -27.663 -2.203  -32.205 1.00 22.71  ? 99  ILE   B HD11 1 
ATOM   5919 H  HD12 . ILE   B 1 102 ? -29.079 -2.651  -31.641 1.00 22.71  ? 99  ILE   B HD12 1 
ATOM   5920 H  HD13 . ILE   B 1 102 ? -27.749 -3.086  -30.887 1.00 22.71  ? 99  ILE   B HD13 1 
ATOM   5921 N  N    . LEU   B 1 103 ? -29.213 -8.695  -32.121 1.00 16.89  ? 100 LEU   B N    1 
ATOM   5922 C  CA   . LEU   B 1 103 ? -29.970 -9.780  -31.483 1.00 15.91  ? 100 LEU   B CA   1 
ATOM   5923 C  C    . LEU   B 1 103 ? -29.366 -10.045 -30.117 1.00 17.30  ? 100 LEU   B C    1 
ATOM   5924 O  O    . LEU   B 1 103 ? -28.151 -10.167 -29.985 1.00 16.23  ? 100 LEU   B O    1 
ATOM   5925 C  CB   . LEU   B 1 103 ? -29.964 -11.049 -32.316 1.00 15.85  ? 100 LEU   B CB   1 
ATOM   5926 C  CG   . LEU   B 1 103 ? -30.816 -12.230 -31.765 1.00 17.78  ? 100 LEU   B CG   1 
ATOM   5927 C  CD1  . LEU   B 1 103 ? -31.307 -13.087 -32.885 1.00 18.91  ? 100 LEU   B CD1  1 
ATOM   5928 C  CD2  . LEU   B 1 103 ? -30.001 -13.033 -30.783 1.00 21.09  ? 100 LEU   B CD2  1 
ATOM   5929 H  H    . LEU   B 1 103 ? -28.359 -8.788  -32.077 1.00 20.31  ? 100 LEU   B H    1 
ATOM   5930 H  HA   . LEU   B 1 103 ? -30.895 -9.509  -31.376 1.00 19.13  ? 100 LEU   B HA   1 
ATOM   5931 H  HB2  . LEU   B 1 103 ? -30.307 -10.834 -33.197 1.00 19.06  ? 100 LEU   B HB2  1 
ATOM   5932 H  HB3  . LEU   B 1 103 ? -29.049 -11.363 -32.384 1.00 19.06  ? 100 LEU   B HB3  1 
ATOM   5933 H  HG   . LEU   B 1 103 ? -31.594 -11.883 -31.301 1.00 21.37  ? 100 LEU   B HG   1 
ATOM   5934 H  HD11 . LEU   B 1 103 ? -31.742 -13.871 -32.515 1.00 22.73  ? 100 LEU   B HD11 1 
ATOM   5935 H  HD12 . LEU   B 1 103 ? -31.939 -12.579 -33.418 1.00 22.73  ? 100 LEU   B HD12 1 
ATOM   5936 H  HD13 . LEU   B 1 103 ? -30.552 -13.354 -33.432 1.00 22.73  ? 100 LEU   B HD13 1 
ATOM   5937 H  HD21 . LEU   B 1 103 ? -30.489 -13.839 -30.554 1.00 25.35  ? 100 LEU   B HD21 1 
ATOM   5938 H  HD22 . LEU   B 1 103 ? -29.153 -13.265 -31.192 1.00 25.35  ? 100 LEU   B HD22 1 
ATOM   5939 H  HD23 . LEU   B 1 103 ? -29.850 -12.500 -29.988 1.00 25.35  ? 100 LEU   B HD23 1 
ATOM   5940 N  N    . GLY   B 1 104 ? -30.209 -10.058 -29.088 1.00 15.93  ? 101 GLY   B N    1 
ATOM   5941 C  CA   . GLY   B 1 104 ? -29.787 -10.416 -27.752 1.00 15.63  ? 101 GLY   B CA   1 
ATOM   5942 C  C    . GLY   B 1 104 ? -30.603 -11.582 -27.258 1.00 16.83  ? 101 GLY   B C    1 
ATOM   5943 O  O    . GLY   B 1 104 ? -31.766 -11.757 -27.650 1.00 20.59  ? 101 GLY   B O    1 
ATOM   5944 H  H    . GLY   B 1 104 ? -31.043 -9.859  -29.147 1.00 19.16  ? 101 GLY   B H    1 
ATOM   5945 H  HA2  . GLY   B 1 104 ? -28.849 -10.664 -27.755 1.00 18.80  ? 101 GLY   B HA2  1 
ATOM   5946 H  HA3  . GLY   B 1 104 ? -29.913 -9.664  -27.152 1.00 18.80  ? 101 GLY   B HA3  1 
ATOM   5947 N  N    A SER   B 1 105 ? -29.976 -12.433 -26.463 0.73 16.73  ? 102 SER   B N    1 
ATOM   5948 N  N    B SER   B 1 105 ? -29.991 -12.384 -26.396 0.27 16.81  ? 102 SER   B N    1 
ATOM   5949 C  CA   A SER   B 1 105 ? -30.689 -13.538 -25.821 0.73 17.65  ? 102 SER   B CA   1 
ATOM   5950 C  CA   B SER   B 1 105 ? -30.628 -13.553 -25.802 0.27 17.65  ? 102 SER   B CA   1 
ATOM   5951 C  C    A SER   B 1 105 ? -30.558 -13.439 -24.306 0.73 18.49  ? 102 SER   B C    1 
ATOM   5952 C  C    B SER   B 1 105 ? -30.525 -13.487 -24.284 0.27 18.48  ? 102 SER   B C    1 
ATOM   5953 O  O    A SER   B 1 105 ? -29.511 -13.026 -23.800 0.73 17.72  ? 102 SER   B O    1 
ATOM   5954 O  O    B SER   B 1 105 ? -29.464 -13.152 -23.749 0.27 17.81  ? 102 SER   B O    1 
ATOM   5955 C  CB   A SER   B 1 105 ? -30.181 -14.904 -26.269 0.73 22.74  ? 102 SER   B CB   1 
ATOM   5956 C  CB   B SER   B 1 105 ? -29.972 -14.838 -26.293 0.27 22.35  ? 102 SER   B CB   1 
ATOM   5957 O  OG   A SER   B 1 105 ? -30.950 -15.970 -25.697 0.73 23.50  ? 102 SER   B OG   1 
ATOM   5958 O  OG   B SER   B 1 105 ? -28.618 -14.904 -25.877 0.27 28.95  ? 102 SER   B OG   1 
ATOM   5959 H  H    A SER   B 1 105 ? -29.138 -12.396 -26.276 0.73 20.12  ? 102 SER   B H    1 
ATOM   5960 H  H    B SER   B 1 105 ? -29.181 -12.269 -26.132 0.27 20.22  ? 102 SER   B H    1 
ATOM   5961 H  HA   A SER   B 1 105 ? -31.625 -13.468 -26.067 0.73 21.22  ? 102 SER   B HA   1 
ATOM   5962 H  HA   B SER   B 1 105 ? -31.567 -13.562 -26.044 0.27 21.22  ? 102 SER   B HA   1 
ATOM   5963 H  HB2  A SER   B 1 105 ? -30.241 -14.959 -27.235 0.73 27.32  ? 102 SER   B HB2  1 
ATOM   5964 H  HB2  B SER   B 1 105 ? -30.453 -15.597 -25.927 0.27 26.86  ? 102 SER   B HB2  1 
ATOM   5965 H  HB3  A SER   B 1 105 ? -29.257 -15.001 -25.988 0.73 27.32  ? 102 SER   B HB3  1 
ATOM   5966 H  HB3  B SER   B 1 105 ? -30.006 -14.860 -27.262 0.27 26.86  ? 102 SER   B HB3  1 
ATOM   5967 H  HG   A SER   B 1 105 ? -31.770 -15.796 -25.754 0.73 28.24  ? 102 SER   B HG   1 
ATOM   5968 H  HG   B SER   B 1 105 ? -28.578 -14.995 -25.042 0.27 34.78  ? 102 SER   B HG   1 
ATOM   5969 N  N    . SER   B 1 106 ? -31.607 -13.849 -23.594 1.00 19.63  ? 103 SER   B N    1 
ATOM   5970 C  CA   . SER   B 1 106 ? -31.592 -13.927 -22.112 1.00 20.40  ? 103 SER   B CA   1 
ATOM   5971 C  C    . SER   B 1 106 ? -31.256 -12.534 -21.577 1.00 17.21  ? 103 SER   B C    1 
ATOM   5972 O  O    . SER   B 1 106 ? -31.842 -11.537 -22.028 1.00 18.65  ? 103 SER   B O    1 
ATOM   5973 C  CB   . SER   B 1 106 ? -30.673 -15.048 -21.692 1.00 22.67  ? 103 SER   B CB   1 
ATOM   5974 O  OG   . SER   B 1 106 ? -30.968 -15.388 -20.325 1.00 26.50  ? 103 SER   B OG   1 
ATOM   5975 H  H    . SER   B 1 106 ? -32.356 -14.094 -23.939 1.00 23.59  ? 103 SER   B H    1 
ATOM   5976 H  HA   . SER   B 1 106 ? -32.484 -14.132 -21.790 1.00 24.52  ? 103 SER   B HA   1 
ATOM   5977 H  HB2  . SER   B 1 106 ? -30.822 -15.820 -22.259 1.00 27.25  ? 103 SER   B HB2  1 
ATOM   5978 H  HB3  . SER   B 1 106 ? -29.751 -14.757 -21.763 1.00 27.25  ? 103 SER   B HB3  1 
ATOM   5979 N  N    . SER   B 1 107 ? -30.312 -12.372 -20.635 1.00 18.60  ? 104 SER   B N    1 
ATOM   5980 C  CA   . SER   B 1 107 ? -30.052 -11.007 -20.190 1.00 19.28  ? 104 SER   B CA   1 
ATOM   5981 C  C    . SER   B 1 107 ? -29.445 -10.126 -21.285 1.00 18.04  ? 104 SER   B C    1 
ATOM   5982 O  O    . SER   B 1 107 ? -29.529 -8.891  -21.198 1.00 17.91  ? 104 SER   B O    1 
ATOM   5983 C  CB   . SER   B 1 107 ? -29.174 -11.018 -18.952 1.00 26.26  ? 104 SER   B CB   1 
ATOM   5984 O  OG   . SER   B 1 107 ? -27.966 -11.671 -19.260 1.00 25.50  ? 104 SER   B OG   1 
ATOM   5985 H  H    . SER   B 1 107 ? -29.846 -12.995 -20.268 1.00 22.36  ? 104 SER   B H    1 
ATOM   5986 H  HA   . SER   B 1 107 ? -30.896 -10.598 -19.943 1.00 23.18  ? 104 SER   B HA   1 
ATOM   5987 H  HB2  . SER   B 1 107 ? -28.989 -10.106 -18.677 1.00 31.56  ? 104 SER   B HB2  1 
ATOM   5988 H  HB3  . SER   B 1 107 ? -29.627 -11.494 -18.238 1.00 31.56  ? 104 SER   B HB3  1 
ATOM   5989 H  HG   . SER   B 1 107 ? -27.574 -11.899 -18.553 1.00 30.65  ? 104 SER   B HG   1 
ATOM   5990 N  N    . GLY   B 1 108 ? -28.878 -10.735 -22.334 1.00 17.23  ? 105 GLY   B N    1 
ATOM   5991 C  CA   . GLY   B 1 108 ? -28.446 -9.948  -23.483 1.00 17.52  ? 105 GLY   B CA   1 
ATOM   5992 C  C    . GLY   B 1 108 ? -29.603 -9.326  -24.242 1.00 15.26  ? 105 GLY   B C    1 
ATOM   5993 O  O    . GLY   B 1 108 ? -29.434 -8.312  -24.912 1.00 15.82  ? 105 GLY   B O    1 
ATOM   5994 H  H    . GLY   B 1 108 ? -28.737 -11.581 -22.400 1.00 20.71  ? 105 GLY   B H    1 
ATOM   5995 H  HA2  . GLY   B 1 108 ? -27.863 -9.235  -23.179 1.00 21.06  ? 105 GLY   B HA2  1 
ATOM   5996 H  HA3  . GLY   B 1 108 ? -27.954 -10.520 -24.093 1.00 21.06  ? 105 GLY   B HA3  1 
ATOM   5997 N  N    A SER   B 1 109 ? -30.781 -9.959  -24.202 0.76 17.04  ? 106 SER   B N    1 
ATOM   5998 N  N    B SER   B 1 109 ? -30.781 -9.943  -24.186 0.24 17.07  ? 106 SER   B N    1 
ATOM   5999 C  CA   A SER   B 1 109 ? -31.970 -9.320  -24.776 0.76 15.84  ? 106 SER   B CA   1 
ATOM   6000 C  CA   B SER   B 1 109 ? -31.951 -9.300  -24.777 0.24 15.91  ? 106 SER   B CA   1 
ATOM   6001 C  C    A SER   B 1 109 ? -32.399 -8.084  -23.973 0.76 14.97  ? 106 SER   B C    1 
ATOM   6002 C  C    B SER   B 1 109 ? -32.365 -8.065  -23.977 0.24 14.99  ? 106 SER   B C    1 
ATOM   6003 O  O    A SER   B 1 109 ? -32.970 -7.140  -24.540 0.76 16.02  ? 106 SER   B O    1 
ATOM   6004 O  O    B SER   B 1 109 ? -32.877 -7.096  -24.551 0.24 16.12  ? 106 SER   B O    1 
ATOM   6005 C  CB   A SER   B 1 109 ? -33.110 -10.324 -24.883 0.76 17.16  ? 106 SER   B CB   1 
ATOM   6006 C  CB   B SER   B 1 109 ? -33.098 -10.296 -24.884 0.24 17.11  ? 106 SER   B CB   1 
ATOM   6007 O  OG   A SER   B 1 109 ? -33.787 -10.499 -23.649 0.76 21.47  ? 106 SER   B OG   1 
ATOM   6008 O  OG   B SER   B 1 109 ? -34.239 -9.686  -25.450 0.24 20.91  ? 106 SER   B OG   1 
ATOM   6009 H  H    A SER   B 1 109 ? -30.915 -10.735 -23.859 0.76 20.48  ? 106 SER   B H    1 
ATOM   6010 H  H    B SER   B 1 109 ? -30.925 -10.709 -23.823 0.24 20.53  ? 106 SER   B H    1 
ATOM   6011 H  HA   A SER   B 1 109 ? -31.759 -9.023  -25.675 0.76 19.05  ? 106 SER   B HA   1 
ATOM   6012 H  HA   B SER   B 1 109 ? -31.737 -9.010  -25.678 0.24 19.14  ? 106 SER   B HA   1 
ATOM   6013 H  HB2  A SER   B 1 109 ? -33.745 -10.003 -25.543 0.76 20.63  ? 106 SER   B HB2  1 
ATOM   6014 H  HB2  B SER   B 1 109 ? -32.823 -11.036 -25.448 0.24 20.58  ? 106 SER   B HB2  1 
ATOM   6015 H  HB3  A SER   B 1 109 ? -32.745 -11.179 -25.162 0.76 20.63  ? 106 SER   B HB3  1 
ATOM   6016 H  HB3  B SER   B 1 109 ? -33.320 -10.619 -23.997 0.24 20.58  ? 106 SER   B HB3  1 
ATOM   6017 H  HG   A SER   B 1 109 ? -33.333 -10.989 -23.139 0.76 25.80  ? 106 SER   B HG   1 
ATOM   6018 H  HG   B SER   B 1 109 ? -34.509 -9.066  -24.952 0.24 25.13  ? 106 SER   B HG   1 
ATOM   6019 N  N    . ILE   B 1 110 ? -32.116 -8.060  -22.664 1.00 15.09  ? 107 ILE   B N    1 
ATOM   6020 C  CA   . ILE   B 1 110 ? -32.389 -6.881  -21.857 1.00 14.62  ? 107 ILE   B CA   1 
ATOM   6021 C  C    . ILE   B 1 110 ? -31.414 -5.760  -22.199 1.00 14.51  ? 107 ILE   B C    1 
ATOM   6022 O  O    . ILE   B 1 110 ? -31.804 -4.601  -22.342 1.00 16.10  ? 107 ILE   B O    1 
ATOM   6023 C  CB   . ILE   B 1 110 ? -32.359 -7.273  -20.367 1.00 16.55  ? 107 ILE   B CB   1 
ATOM   6024 C  CG1  . ILE   B 1 110 ? -33.403 -8.337  -20.110 1.00 16.62  ? 107 ILE   B CG1  1 
ATOM   6025 C  CG2  . ILE   B 1 110 ? -32.508 -6.047  -19.507 1.00 16.26  ? 107 ILE   B CG2  1 
ATOM   6026 C  CD1  . ILE   B 1 110 ? -33.440 -8.870  -18.692 1.00 20.39  ? 107 ILE   B CD1  1 
ATOM   6027 H  H    . ILE   B 1 110 ? -31.768 -8.715  -22.230 1.00 18.15  ? 107 ILE   B H    1 
ATOM   6028 H  HA   . ILE   B 1 110 ? -33.276 -6.543  -22.058 1.00 17.58  ? 107 ILE   B HA   1 
ATOM   6029 H  HB   . ILE   B 1 110 ? -31.502 -7.660  -20.130 1.00 19.90  ? 107 ILE   B HB   1 
ATOM   6030 H  HG12 . ILE   B 1 110 ? -34.277 -7.963  -20.303 1.00 19.99  ? 107 ILE   B HG12 1 
ATOM   6031 H  HG13 . ILE   B 1 110 ? -33.226 -9.088  -20.698 1.00 19.99  ? 107 ILE   B HG13 1 
ATOM   6032 H  HG21 . ILE   B 1 110 ? -32.516 -6.315  -18.574 1.00 19.55  ? 107 ILE   B HG21 1 
ATOM   6033 H  HG22 . ILE   B 1 110 ? -31.760 -5.452  -19.673 1.00 19.55  ? 107 ILE   B HG22 1 
ATOM   6034 H  HG23 . ILE   B 1 110 ? -33.340 -5.603  -19.731 1.00 19.55  ? 107 ILE   B HG23 1 
ATOM   6035 H  HD11 . ILE   B 1 110 ? -34.069 -9.608  -18.648 1.00 24.51  ? 107 ILE   B HD11 1 
ATOM   6036 H  HD12 . ILE   B 1 110 ? -32.553 -9.177  -18.446 1.00 24.51  ? 107 ILE   B HD12 1 
ATOM   6037 H  HD13 . ILE   B 1 110 ? -33.722 -8.160  -18.094 1.00 24.51  ? 107 ILE   B HD13 1 
ATOM   6038 N  N    . VAL   B 1 111 ? -30.128 -6.098  -22.365 1.00 15.79  ? 108 VAL   B N    1 
ATOM   6039 C  CA   . VAL   B 1 111 ? -29.199 -5.104  -22.875 1.00 17.17  ? 108 VAL   B CA   1 
ATOM   6040 C  C    . VAL   B 1 111 ? -29.738 -4.527  -24.181 1.00 16.41  ? 108 VAL   B C    1 
ATOM   6041 O  O    . VAL   B 1 111 ? -29.759 -3.314  -24.364 1.00 16.31  ? 108 VAL   B O    1 
ATOM   6042 C  CB   . VAL   B 1 111 ? -27.789 -5.687  -23.049 1.00 15.48  ? 108 VAL   B CB   1 
ATOM   6043 C  CG1  . VAL   B 1 111 ? -26.922 -4.656  -23.715 1.00 17.04  ? 108 VAL   B CG1  1 
ATOM   6044 C  CG2  . VAL   B 1 111 ? -27.190 -6.115  -21.702 1.00 16.51  ? 108 VAL   B CG2  1 
ATOM   6045 H  H    . VAL   B 1 111 ? -29.788 -6.869  -22.194 1.00 18.99  ? 108 VAL   B H    1 
ATOM   6046 H  HA   . VAL   B 1 111 ? -29.127 -4.388  -22.225 1.00 20.64  ? 108 VAL   B HA   1 
ATOM   6047 H  HB   . VAL   B 1 111 ? -27.832 -6.483  -23.601 1.00 18.62  ? 108 VAL   B HB   1 
ATOM   6048 H  HG11 . VAL   B 1 111 ? -26.007 -4.975  -23.729 1.00 20.49  ? 108 VAL   B HG11 1 
ATOM   6049 H  HG12 . VAL   B 1 111 ? -27.238 -4.516  -24.621 1.00 20.49  ? 108 VAL   B HG12 1 
ATOM   6050 H  HG13 . VAL   B 1 111 ? -26.976 -3.827  -23.214 1.00 20.49  ? 108 VAL   B HG13 1 
ATOM   6051 H  HG21 . VAL   B 1 111 ? -26.328 -6.531  -21.858 1.00 19.85  ? 108 VAL   B HG21 1 
ATOM   6052 H  HG22 . VAL   B 1 111 ? -27.082 -5.331  -21.141 1.00 19.85  ? 108 VAL   B HG22 1 
ATOM   6053 H  HG23 . VAL   B 1 111 ? -27.790 -6.747  -21.276 1.00 19.85  ? 108 VAL   B HG23 1 
ATOM   6054 N  N    . ALA   B 1 112 ? -30.176 -5.410  -25.105 1.00 15.87  ? 109 ALA   B N    1 
ATOM   6055 C  CA   . ALA   B 1 112 ? -30.715 -4.960  -26.388 1.00 15.76  ? 109 ALA   B CA   1 
ATOM   6056 C  C    . ALA   B 1 112 ? -31.895 -3.993  -26.228 1.00 15.23  ? 109 ALA   B C    1 
ATOM   6057 O  O    . ALA   B 1 112 ? -32.005 -3.001  -26.953 1.00 17.10  ? 109 ALA   B O    1 
ATOM   6058 C  CB   . ALA   B 1 112 ? -31.134 -6.185  -27.222 1.00 16.34  ? 109 ALA   B CB   1 
ATOM   6059 H  H    . ALA   B 1 112 ? -30.168 -6.264  -25.007 1.00 19.09  ? 109 ALA   B H    1 
ATOM   6060 H  HA   . ALA   B 1 112 ? -30.017 -4.478  -26.858 1.00 18.95  ? 109 ALA   B HA   1 
ATOM   6061 H  HB1  . ALA   B 1 112 ? -31.524 -5.881  -28.057 1.00 19.65  ? 109 ALA   B HB1  1 
ATOM   6062 H  HB2  . ALA   B 1 112 ? -30.350 -6.727  -27.403 1.00 19.65  ? 109 ALA   B HB2  1 
ATOM   6063 H  HB3  . ALA   B 1 112 ? -31.784 -6.701  -26.721 1.00 19.65  ? 109 ALA   B HB3  1 
ATOM   6064 N  N    . MET   B 1 113 ? -32.775 -4.262  -25.267 1.00 16.57  ? 110 MET   B N    1 
ATOM   6065 C  CA   . MET   B 1 113 ? -33.895 -3.374  -25.028 1.00 17.69  ? 110 MET   B CA   1 
ATOM   6066 C  C    . MET   B 1 113 ? -33.419 -1.975  -24.611 1.00 17.22  ? 110 MET   B C    1 
ATOM   6067 O  O    . MET   B 1 113 ? -33.981 -0.964  -25.052 1.00 18.55  ? 110 MET   B O    1 
ATOM   6068 C  CB   . MET   B 1 113 ? -34.775 -3.972  -23.941 1.00 16.67  ? 110 MET   B CB   1 
ATOM   6069 C  CG   . MET   B 1 113 ? -35.604 -5.160  -24.356 1.00 18.07  ? 110 MET   B CG   1 
ATOM   6070 S  SD   . MET   B 1 113 ? -36.419 -5.919  -22.913 1.00 17.86  ? 110 MET   B SD   1 
ATOM   6071 C  CE   . MET   B 1 113 ? -37.045 -7.364  -23.760 1.00 22.41  ? 110 MET   B CE   1 
ATOM   6072 H  H    . MET   B 1 113 ? -32.744 -4.947  -24.748 1.00 19.93  ? 110 MET   B H    1 
ATOM   6073 H  HA   . MET   B 1 113 ? -34.413 -3.292  -25.844 1.00 21.27  ? 110 MET   B HA   1 
ATOM   6074 H  HB2  . MET   B 1 113 ? -34.205 -4.259  -23.210 1.00 20.05  ? 110 MET   B HB2  1 
ATOM   6075 H  HB3  . MET   B 1 113 ? -35.388 -3.286  -23.633 1.00 20.05  ? 110 MET   B HB3  1 
ATOM   6076 H  HG2  . MET   B 1 113 ? -36.288 -4.875  -24.981 1.00 21.72  ? 110 MET   B HG2  1 
ATOM   6077 H  HG3  . MET   B 1 113 ? -35.031 -5.825  -24.770 1.00 21.72  ? 110 MET   B HG3  1 
ATOM   6078 H  HE1  . MET   B 1 113 ? -37.564 -7.896  -23.137 1.00 26.94  ? 110 MET   B HE1  1 
ATOM   6079 H  HE2  . MET   B 1 113 ? -37.607 -7.078  -24.498 1.00 26.94  ? 110 MET   B HE2  1 
ATOM   6080 H  HE3  . MET   B 1 113 ? -36.297 -7.882  -24.095 1.00 26.94  ? 110 MET   B HE3  1 
ATOM   6081 N  N    . HIS   B 1 114 ? -32.356 -1.900  -23.765 1.00 16.30  ? 111 HIS   B N    1 
ATOM   6082 C  CA   . HIS   B 1 114 ? -31.804 -0.609  -23.389 1.00 17.47  ? 111 HIS   B CA   1 
ATOM   6083 C  C    . HIS   B 1 114 ? -31.063 0.067   -24.531 1.00 16.65  ? 111 HIS   B C    1 
ATOM   6084 O  O    . HIS   B 1 114 ? -30.991 1.303   -24.550 1.00 20.73  ? 111 HIS   B O    1 
ATOM   6085 C  CB   . HIS   B 1 114 ? -30.911 -0.770  -22.154 1.00 16.94  ? 111 HIS   B CB   1 
ATOM   6086 C  CG   . HIS   B 1 114 ? -31.682 -1.040  -20.893 1.00 18.04  ? 111 HIS   B CG   1 
ATOM   6087 N  ND1  . HIS   B 1 114 ? -32.133 -0.030  -20.087 1.00 20.11  ? 111 HIS   B ND1  1 
ATOM   6088 C  CD2  . HIS   B 1 114 ? -32.148 -2.193  -20.361 1.00 18.18  ? 111 HIS   B CD2  1 
ATOM   6089 C  CE1  . HIS   B 1 114 ? -32.796 -0.556  -19.075 1.00 20.96  ? 111 HIS   B CE1  1 
ATOM   6090 N  NE2  . HIS   B 1 114 ? -32.855 -1.858  -19.235 1.00 18.50  ? 111 HIS   B NE2  1 
ATOM   6091 H  H    . HIS   B 1 114 ? -31.959 -2.576  -23.413 1.00 19.60  ? 111 HIS   B H    1 
ATOM   6092 H  HA   . HIS   B 1 114 ? -32.534 -0.016  -23.151 1.00 21.00  ? 111 HIS   B HA   1 
ATOM   6093 H  HB2  . HIS   B 1 114 ? -30.306 -1.514  -22.299 1.00 20.37  ? 111 HIS   B HB2  1 
ATOM   6094 H  HB3  . HIS   B 1 114 ? -30.405 0.048   -22.024 1.00 20.37  ? 111 HIS   B HB3  1 
ATOM   6095 H  HD2  . HIS   B 1 114 ? -32.013 -3.050  -20.695 1.00 21.85  ? 111 HIS   B HD2  1 
ATOM   6096 H  HE1  . HIS   B 1 114 ? -33.161 -0.082  -18.363 1.00 25.19  ? 111 HIS   B HE1  1 
ATOM   6097 H  HE2  . HIS   B 1 114 ? -33.269 -2.409  -18.721 1.00 22.24  ? 111 HIS   B HE2  1 
ATOM   6098 N  N    . VAL   B 1 115 ? -30.475 -0.703  -25.462 1.00 17.09  ? 112 VAL   B N    1 
ATOM   6099 C  CA   . VAL   B 1 115 ? -29.875 -0.070  -26.639 1.00 17.60  ? 112 VAL   B CA   1 
ATOM   6100 C  C    . VAL   B 1 115 ? -30.957 0.651   -27.431 1.00 18.23  ? 112 VAL   B C    1 
ATOM   6101 O  O    . VAL   B 1 115 ? -30.798 1.800   -27.824 1.00 20.44  ? 112 VAL   B O    1 
ATOM   6102 C  CB   . VAL   B 1 115 ? -29.146 -1.115  -27.504 1.00 19.00  ? 112 VAL   B CB   1 
ATOM   6103 C  CG1  . VAL   B 1 115 ? -28.621 -0.443  -28.820 1.00 19.07  ? 112 VAL   B CG1  1 
ATOM   6104 C  CG2  . VAL   B 1 115 ? -27.974 -1.695  -26.755 1.00 17.24  ? 112 VAL   B CG2  1 
ATOM   6105 H  H    . VAL   B 1 115 ? -30.415 -1.561  -25.433 1.00 20.55  ? 112 VAL   B H    1 
ATOM   6106 H  HA   . VAL   B 1 115 ? -29.217 0.581   -26.347 1.00 21.16  ? 112 VAL   B HA   1 
ATOM   6107 H  HB   . VAL   B 1 115 ? -29.767 -1.827  -27.723 1.00 22.84  ? 112 VAL   B HB   1 
ATOM   6108 H  HG11 . VAL   B 1 115 ? -28.049 -1.071  -29.289 1.00 22.93  ? 112 VAL   B HG11 1 
ATOM   6109 H  HG12 . VAL   B 1 115 ? -29.379 -0.206  -29.377 1.00 22.93  ? 112 VAL   B HG12 1 
ATOM   6110 H  HG13 . VAL   B 1 115 ? -28.119 0.354   -28.589 1.00 22.93  ? 112 VAL   B HG13 1 
ATOM   6111 H  HG21 . VAL   B 1 115 ? -27.558 -2.381  -27.301 1.00 20.73  ? 112 VAL   B HG21 1 
ATOM   6112 H  HG22 . VAL   B 1 115 ? -27.337 -0.988  -26.569 1.00 20.73  ? 112 VAL   B HG22 1 
ATOM   6113 H  HG23 . VAL   B 1 115 ? -28.291 -2.082  -25.923 1.00 20.73  ? 112 VAL   B HG23 1 
ATOM   6114 N  N    . LEU   B 1 116 ? -32.081 -0.020  -27.656 1.00 18.78  ? 113 LEU   B N    1 
ATOM   6115 C  CA   . LEU   B 1 116 ? -33.155 0.590   -28.428 1.00 21.42  ? 113 LEU   B CA   1 
ATOM   6116 C  C    . LEU   B 1 116 ? -33.710 1.818   -27.717 1.00 23.72  ? 113 LEU   B C    1 
ATOM   6117 O  O    . LEU   B 1 116 ? -33.934 2.852   -28.348 1.00 26.15  ? 113 LEU   B O    1 
ATOM   6118 C  CB   . LEU   B 1 116 ? -34.249 -0.441  -28.675 1.00 21.34  ? 113 LEU   B CB   1 
ATOM   6119 C  CG   . LEU   B 1 116 ? -35.459 0.090   -29.460 1.00 23.92  ? 113 LEU   B CG   1 
ATOM   6120 C  CD1  . LEU   B 1 116 ? -35.091 0.551   -30.836 1.00 26.21  ? 113 LEU   B CD1  1 
ATOM   6121 C  CD2  . LEU   B 1 116 ? -36.460 -1.032  -29.506 1.00 27.67  ? 113 LEU   B CD2  1 
ATOM   6122 H  H    . LEU   B 1 116 ? -32.245 -0.817  -27.377 1.00 22.58  ? 113 LEU   B H    1 
ATOM   6123 H  HA   . LEU   B 1 116 ? -32.814 0.880   -29.288 1.00 25.75  ? 113 LEU   B HA   1 
ATOM   6124 H  HB2  . LEU   B 1 116 ? -33.870 -1.177  -29.181 1.00 25.65  ? 113 LEU   B HB2  1 
ATOM   6125 H  HB3  . LEU   B 1 116 ? -34.572 -0.760  -27.818 1.00 25.65  ? 113 LEU   B HB3  1 
ATOM   6126 H  HG   . LEU   B 1 116 ? -35.833 0.874   -29.028 1.00 28.75  ? 113 LEU   B HG   1 
ATOM   6127 H  HD11 . LEU   B 1 116 ? -35.895 0.833   -31.300 1.00 31.49  ? 113 LEU   B HD11 1 
ATOM   6128 H  HD12 . LEU   B 1 116 ? -34.473 1.295   -30.765 1.00 31.49  ? 113 LEU   B HD12 1 
ATOM   6129 H  HD13 . LEU   B 1 116 ? -34.674 -0.182  -31.314 1.00 31.49  ? 113 LEU   B HD13 1 
ATOM   6130 H  HD21 . LEU   B 1 116 ? -37.229 -0.748  -30.024 1.00 33.25  ? 113 LEU   B HD21 1 
ATOM   6131 H  HD22 . LEU   B 1 116 ? -36.048 -1.805  -29.922 1.00 33.25  ? 113 LEU   B HD22 1 
ATOM   6132 H  HD23 . LEU   B 1 116 ? -36.732 -1.249  -28.601 1.00 33.25  ? 113 LEU   B HD23 1 
ATOM   6133 N  N    . LYS   B 1 117 ? -33.883 1.727   -26.397 1.00 20.24  ? 114 LYS   B N    1 
ATOM   6134 C  CA   . LYS   B 1 117 ? -34.452 2.821   -25.623 1.00 20.53  ? 114 LYS   B CA   1 
ATOM   6135 C  C    . LYS   B 1 117 ? -33.568 4.061   -25.619 1.00 23.03  ? 114 LYS   B C    1 
ATOM   6136 O  O    . LYS   B 1 117 ? -34.058 5.183   -25.780 1.00 24.72  ? 114 LYS   B O    1 
ATOM   6137 C  CB   . LYS   B 1 117 ? -34.657 2.352   -24.175 1.00 25.30  ? 114 LYS   B CB   1 
ATOM   6138 C  CG   . LYS   B 1 117 ? -35.414 3.377   -23.338 1.00 30.30  ? 114 LYS   B CG   1 
ATOM   6139 C  CD   . LYS   B 1 117 ? -35.800 2.833   -21.998 1.00 29.92  ? 114 LYS   B CD   1 
ATOM   6140 C  CE   . LYS   B 1 117 ? -36.587 3.903   -21.208 1.00 44.08  ? 114 LYS   B CE   1 
ATOM   6141 N  NZ   . LYS   B 1 117 ? -37.447 3.346   -20.106 1.00 39.80  ? 114 LYS   B NZ   1 
ATOM   6142 H  H    . LYS   B 1 117 ? -33.677 1.038   -25.926 1.00 24.33  ? 114 LYS   B H    1 
ATOM   6143 H  HA   . LYS   B 1 117 ? -35.300 3.062   -26.028 1.00 24.68  ? 114 LYS   B HA   1 
ATOM   6144 H  HB2  . LYS   B 1 117 ? -35.168 1.527   -24.177 1.00 30.41  ? 114 LYS   B HB2  1 
ATOM   6145 H  HB3  . LYS   B 1 117 ? -33.791 2.204   -23.763 1.00 30.41  ? 114 LYS   B HB3  1 
ATOM   6146 H  HG2  . LYS   B 1 117 ? -34.850 4.154   -23.199 1.00 36.40  ? 114 LYS   B HG2  1 
ATOM   6147 H  HG3  . LYS   B 1 117 ? -36.224 3.635   -23.805 1.00 36.40  ? 114 LYS   B HG3  1 
ATOM   6148 H  HD2  . LYS   B 1 117 ? -36.363 2.052   -22.110 1.00 35.94  ? 114 LYS   B HD2  1 
ATOM   6149 H  HD3  . LYS   B 1 117 ? -35.004 2.599   -21.497 1.00 35.94  ? 114 LYS   B HD3  1 
ATOM   6150 H  HE2  . LYS   B 1 117 ? -35.956 4.520   -20.805 1.00 52.93  ? 114 LYS   B HE2  1 
ATOM   6151 H  HE3  . LYS   B 1 117 ? -37.169 4.378   -21.823 1.00 52.93  ? 114 LYS   B HE3  1 
ATOM   6152 H  HZ1  . LYS   B 1 117 ? -37.869 4.007   -19.686 1.00 47.80  ? 114 LYS   B HZ1  1 
ATOM   6153 H  HZ2  . LYS   B 1 117 ? -38.050 2.786   -20.445 1.00 47.80  ? 114 LYS   B HZ2  1 
ATOM   6154 H  HZ3  . LYS   B 1 117 ? -36.942 2.906   -19.520 1.00 47.80  ? 114 LYS   B HZ3  1 
ATOM   6155 N  N    . ASP   B 1 118 ? -32.264 3.883   -25.403 1.00 24.21  ? 115 ASP   B N    1 
ATOM   6156 C  CA   . ASP   B 1 118 ? -31.359 5.007   -25.201 1.00 26.33  ? 115 ASP   B CA   1 
ATOM   6157 C  C    . ASP   B 1 118 ? -30.607 5.419   -26.462 1.00 22.31  ? 115 ASP   B C    1 
ATOM   6158 O  O    . ASP   B 1 118 ? -30.151 6.573   -26.554 1.00 26.26  ? 115 ASP   B O    1 
ATOM   6159 C  CB   . ASP   B 1 118 ? -30.325 4.662   -24.107 1.00 24.14  ? 115 ASP   B CB   1 
ATOM   6160 C  CG   . ASP   B 1 118 ? -30.937 4.528   -22.708 1.00 31.54  ? 115 ASP   B CG   1 
ATOM   6161 O  OD1  . ASP   B 1 118 ? -32.035 5.059   -22.480 1.00 38.95  ? 115 ASP   B OD1  1 
ATOM   6162 O  OD2  . ASP   B 1 118 ? -30.264 3.915   -21.844 1.00 40.26  ? 115 ASP   B OD2  1 
ATOM   6163 H  H    . ASP   B 1 118 ? -31.879 3.115   -25.369 1.00 29.09  ? 115 ASP   B H    1 
ATOM   6164 H  HA   . ASP   B 1 118 ? -31.880 5.769   -24.903 1.00 31.63  ? 115 ASP   B HA   1 
ATOM   6165 H  HB2  . ASP   B 1 118 ? -29.904 3.816   -24.329 1.00 29.01  ? 115 ASP   B HB2  1 
ATOM   6166 H  HB3  . ASP   B 1 118 ? -29.658 5.365   -24.074 1.00 29.01  ? 115 ASP   B HB3  1 
ATOM   6167 N  N    . TYR   B 1 119 ? -30.440 4.501   -27.421 1.00 24.16  ? 116 TYR   B N    1 
ATOM   6168 C  CA   . TYR   B 1 119 ? -29.670 4.768   -28.627 1.00 24.85  ? 116 TYR   B CA   1 
ATOM   6169 C  C    . TYR   B 1 119 ? -30.406 4.235   -29.856 1.00 24.50  ? 116 TYR   B C    1 
ATOM   6170 O  O    . TYR   B 1 119 ? -29.816 3.519   -30.692 1.00 22.87  ? 116 TYR   B O    1 
ATOM   6171 C  CB   . TYR   B 1 119 ? -28.270 4.152   -28.507 1.00 24.33  ? 116 TYR   B CB   1 
ATOM   6172 C  CG   . TYR   B 1 119 ? -27.572 4.533   -27.215 1.00 27.72  ? 116 TYR   B CG   1 
ATOM   6173 C  CD1  . TYR   B 1 119 ? -27.036 5.791   -27.035 1.00 33.55  ? 116 TYR   B CD1  1 
ATOM   6174 C  CD2  . TYR   B 1 119 ? -27.514 3.635   -26.168 1.00 26.39  ? 116 TYR   B CD2  1 
ATOM   6175 C  CE1  . TYR   B 1 119 ? -26.421 6.130   -25.829 1.00 29.74  ? 116 TYR   B CE1  1 
ATOM   6176 C  CE2  . TYR   B 1 119 ? -26.936 3.965   -24.979 1.00 28.83  ? 116 TYR   B CE2  1 
ATOM   6177 C  CZ   . TYR   B 1 119 ? -26.394 5.191   -24.814 1.00 27.15  ? 116 TYR   B CZ   1 
ATOM   6178 O  OH   . TYR   B 1 119 ? -25.800 5.515   -23.593 1.00 38.10  ? 116 TYR   B OH   1 
ATOM   6179 H  H    . TYR   B 1 119 ? -30.770 3.708   -27.391 1.00 29.03  ? 116 TYR   B H    1 
ATOM   6180 H  HA   . TYR   B 1 119 ? -29.569 5.725   -28.744 1.00 29.87  ? 116 TYR   B HA   1 
ATOM   6181 H  HB2  . TYR   B 1 119 ? -28.346 3.186   -28.535 1.00 29.24  ? 116 TYR   B HB2  1 
ATOM   6182 H  HB3  . TYR   B 1 119 ? -27.724 4.463   -29.246 1.00 29.24  ? 116 TYR   B HB3  1 
ATOM   6183 H  HD1  . TYR   B 1 119 ? -27.085 6.417   -27.720 1.00 40.31  ? 116 TYR   B HD1  1 
ATOM   6184 H  HD2  . TYR   B 1 119 ? -27.876 2.786   -26.277 1.00 31.71  ? 116 TYR   B HD2  1 
ATOM   6185 H  HE1  . TYR   B 1 119 ? -26.037 6.969   -25.710 1.00 35.73  ? 116 TYR   B HE1  1 
ATOM   6186 H  HE2  . TYR   B 1 119 ? -26.915 3.348   -24.284 1.00 34.63  ? 116 TYR   B HE2  1 
ATOM   6187 H  HH   . TYR   B 1 119 ? -25.590 6.328   -23.582 1.00 45.76  ? 116 TYR   B HH   1 
ATOM   6188 N  N    . PRO   B 1 120 ? -31.667 4.621   -30.045 1.00 24.02  ? 117 PRO   B N    1 
ATOM   6189 C  CA   . PRO   B 1 120 ? -32.423 4.080   -31.190 1.00 24.87  ? 117 PRO   B CA   1 
ATOM   6190 C  C    . PRO   B 1 120 ? -31.785 4.393   -32.537 1.00 25.82  ? 117 PRO   B C    1 
ATOM   6191 O  O    . PRO   B 1 120 ? -32.019 3.656   -33.507 1.00 24.69  ? 117 PRO   B O    1 
ATOM   6192 C  CB   . PRO   B 1 120 ? -33.797 4.757   -31.059 1.00 26.84  ? 117 PRO   B CB   1 
ATOM   6193 C  CG   . PRO   B 1 120 ? -33.545 5.974   -30.214 1.00 28.64  ? 117 PRO   B CG   1 
ATOM   6194 C  CD   . PRO   B 1 120 ? -32.454 5.619   -29.283 1.00 27.61  ? 117 PRO   B CD   1 
ATOM   6195 H  HA   . PRO   B 1 120 ? -32.528 3.121   -31.095 1.00 29.88  ? 117 PRO   B HA   1 
ATOM   6196 H  HB2  . PRO   B 1 120 ? -34.129 5.004   -31.936 1.00 32.25  ? 117 PRO   B HB2  1 
ATOM   6197 H  HB3  . PRO   B 1 120 ? -34.422 4.155   -30.625 1.00 32.25  ? 117 PRO   B HB3  1 
ATOM   6198 H  HG2  . PRO   B 1 120 ? -33.282 6.714   -30.782 1.00 34.41  ? 117 PRO   B HG2  1 
ATOM   6199 H  HG3  . PRO   B 1 120 ? -34.351 6.201   -29.724 1.00 34.41  ? 117 PRO   B HG3  1 
ATOM   6200 H  HD2  . PRO   B 1 120 ? -31.914 6.396   -29.072 1.00 33.18  ? 117 PRO   B HD2  1 
ATOM   6201 H  HD3  . PRO   B 1 120 ? -32.808 5.230   -28.468 1.00 33.18  ? 117 PRO   B HD3  1 
ATOM   6202 N  N    . GLU   B 1 121 ? -30.963 5.430   -32.624 1.00 24.94  ? 118 GLU   B N    1 
ATOM   6203 C  CA   . GLU   B 1 121 ? -30.348 5.806   -33.890 1.00 27.36  ? 118 GLU   B CA   1 
ATOM   6204 C  C    . GLU   B 1 121 ? -29.362 4.764   -34.408 1.00 26.48  ? 118 GLU   B C    1 
ATOM   6205 O  O    . GLU   B 1 121 ? -29.047 4.792   -35.611 1.00 29.15  ? 118 GLU   B O    1 
ATOM   6206 C  CB   . GLU   B 1 121 ? -29.701 7.185   -33.708 1.00 32.61  ? 118 GLU   B CB   1 
ATOM   6207 C  CG   . GLU   B 1 121 ? -28.476 7.189   -32.825 1.00 34.03  ? 118 GLU   B CG   1 
ATOM   6208 C  CD   . GLU   B 1 121 ? -28.779 7.359   -31.335 1.00 44.44  ? 118 GLU   B CD   1 
ATOM   6209 O  OE1  . GLU   B 1 121 ? -29.977 7.431   -30.957 1.00 35.02  ? 118 GLU   B OE1  1 
ATOM   6210 O  OE2  . GLU   B 1 121 ? -27.795 7.431   -30.551 1.00 41.33  ? 118 GLU   B OE2  1 
ATOM   6211 H  H    . GLU   B 1 121 ? -30.743 5.935   -31.964 1.00 29.97  ? 118 GLU   B H    1 
ATOM   6212 H  HA   . GLU   B 1 121 ? -31.019 5.878   -34.586 1.00 32.88  ? 118 GLU   B HA   1 
ATOM   6213 H  HB2  . GLU   B 1 121 ? -29.436 7.519   -34.579 1.00 39.18  ? 118 GLU   B HB2  1 
ATOM   6214 H  HB3  . GLU   B 1 121 ? -30.353 7.782   -33.307 1.00 39.18  ? 118 GLU   B HB3  1 
ATOM   6215 H  HG2  . GLU   B 1 121 ? -28.010 6.346   -32.936 1.00 40.88  ? 118 GLU   B HG2  1 
ATOM   6216 H  HG3  . GLU   B 1 121 ? -27.902 7.923   -33.094 1.00 40.88  ? 118 GLU   B HG3  1 
ATOM   6217 N  N    . VAL   B 1 122 ? -28.876 3.852   -33.563 1.00 24.07  ? 119 VAL   B N    1 
ATOM   6218 C  CA   . VAL   B 1 122 ? -27.979 2.828   -34.068 1.00 23.59  ? 119 VAL   B CA   1 
ATOM   6219 C  C    . VAL   B 1 122 ? -28.717 1.560   -34.488 1.00 22.70  ? 119 VAL   B C    1 
ATOM   6220 O  O    . VAL   B 1 122 ? -28.070 0.615   -34.953 1.00 24.76  ? 119 VAL   B O    1 
ATOM   6221 C  CB   . VAL   B 1 122 ? -26.869 2.430   -33.074 1.00 20.95  ? 119 VAL   B CB   1 
ATOM   6222 C  CG1  . VAL   B 1 122 ? -26.170 3.674   -32.549 1.00 24.88  ? 119 VAL   B CG1  1 
ATOM   6223 C  CG2  . VAL   B 1 122 ? -27.414 1.646   -31.901 1.00 24.35  ? 119 VAL   B CG2  1 
ATOM   6224 H  H    . VAL   B 1 122 ? -29.049 3.811   -32.721 1.00 28.93  ? 119 VAL   B H    1 
ATOM   6225 H  HA   . VAL   B 1 122 ? -27.549 3.229   -34.839 1.00 28.35  ? 119 VAL   B HA   1 
ATOM   6226 H  HB   . VAL   B 1 122 ? -26.240 1.865   -33.549 1.00 25.18  ? 119 VAL   B HB   1 
ATOM   6227 H  HG11 . VAL   B 1 122 ? -25.404 3.406   -32.019 1.00 29.90  ? 119 VAL   B HG11 1 
ATOM   6228 H  HG12 . VAL   B 1 122 ? -25.880 4.214   -33.301 1.00 29.90  ? 119 VAL   B HG12 1 
ATOM   6229 H  HG13 . VAL   B 1 122 ? -26.792 4.178   -32.001 1.00 29.90  ? 119 VAL   B HG13 1 
ATOM   6230 H  HG21 . VAL   B 1 122 ? -26.759 1.653   -31.185 1.00 29.27  ? 119 VAL   B HG21 1 
ATOM   6231 H  HG22 . VAL   B 1 122 ? -28.238 2.059   -31.599 1.00 29.27  ? 119 VAL   B HG22 1 
ATOM   6232 H  HG23 . VAL   B 1 122 ? -27.586 0.734   -32.183 1.00 29.27  ? 119 VAL   B HG23 1 
ATOM   6233 N  N    . VAL   B 1 123 ? -30.041 1.504   -34.340 1.00 22.12  ? 120 VAL   B N    1 
ATOM   6234 C  CA   . VAL   B 1 123 ? -30.788 0.257   -34.521 1.00 19.49  ? 120 VAL   B CA   1 
ATOM   6235 C  C    . VAL   B 1 123 ? -31.556 0.290   -35.832 1.00 21.29  ? 120 VAL   B C    1 
ATOM   6236 O  O    . VAL   B 1 123 ? -32.467 1.110   -36.001 1.00 23.66  ? 120 VAL   B O    1 
ATOM   6237 C  CB   . VAL   B 1 123 ? -31.758 0.003   -33.360 1.00 19.47  ? 120 VAL   B CB   1 
ATOM   6238 C  CG1  . VAL   B 1 123 ? -32.477 -1.319  -33.561 1.00 21.76  ? 120 VAL   B CG1  1 
ATOM   6239 C  CG2  . VAL   B 1 123 ? -31.018 0.028   -32.033 1.00 22.01  ? 120 VAL   B CG2  1 
ATOM   6240 H  H    . VAL   B 1 123 ? -30.532 2.179   -34.134 1.00 26.59  ? 120 VAL   B H    1 
ATOM   6241 H  HA   . VAL   B 1 123 ? -30.139 -0.462  -34.576 1.00 23.42  ? 120 VAL   B HA   1 
ATOM   6242 H  HB   . VAL   B 1 123 ? -32.425 0.708   -33.338 1.00 23.40  ? 120 VAL   B HB   1 
ATOM   6243 H  HG11 . VAL   B 1 123 ? -32.927 -1.562  -32.737 1.00 26.16  ? 120 VAL   B HG11 1 
ATOM   6244 H  HG12 . VAL   B 1 123 ? -33.126 -1.220  -34.276 1.00 26.16  ? 120 VAL   B HG12 1 
ATOM   6245 H  HG13 . VAL   B 1 123 ? -31.827 -1.999  -33.796 1.00 26.16  ? 120 VAL   B HG13 1 
ATOM   6246 H  HG21 . VAL   B 1 123 ? -31.596 -0.331  -31.342 1.00 26.45  ? 120 VAL   B HG21 1 
ATOM   6247 H  HG22 . VAL   B 1 123 ? -30.217 -0.513  -32.109 1.00 26.45  ? 120 VAL   B HG22 1 
ATOM   6248 H  HG23 . VAL   B 1 123 ? -30.780 0.945   -31.822 1.00 26.45  ? 120 VAL   B HG23 1 
ATOM   6249 N  N    . LYS   B 1 124 ? -31.199 -0.616  -36.756 1.00 20.79  ? 121 LYS   B N    1 
ATOM   6250 C  CA   . LYS   B 1 124 ? -32.026 -0.843  -37.944 1.00 20.49  ? 121 LYS   B CA   1 
ATOM   6251 C  C    . LYS   B 1 124 ? -33.171 -1.792  -37.632 1.00 22.04  ? 121 LYS   B C    1 
ATOM   6252 O  O    . LYS   B 1 124 ? -34.351 -1.465  -37.830 1.00 23.50  ? 121 LYS   B O    1 
ATOM   6253 C  CB   . LYS   B 1 124 ? -31.169 -1.419  -39.077 1.00 24.37  ? 121 LYS   B CB   1 
ATOM   6254 C  CG   . LYS   B 1 124 ? -31.868 -1.585  -40.416 1.00 27.52  ? 121 LYS   B CG   1 
ATOM   6255 C  CD   . LYS   B 1 124 ? -30.813 -1.838  -41.481 1.00 33.61  ? 121 LYS   B CD   1 
ATOM   6256 C  CE   . LYS   B 1 124 ? -31.276 -1.540  -42.900 1.00 52.55  ? 121 LYS   B CE   1 
ATOM   6257 N  NZ   . LYS   B 1 124 ? -31.180 -2.759  -43.749 1.00 53.44  ? 121 LYS   B NZ   1 
ATOM   6258 H  H    . LYS   B 1 124 ? -30.492 -1.104  -36.716 1.00 24.98  ? 121 LYS   B H    1 
ATOM   6259 H  HA   . LYS   B 1 124 ? -32.393 0.007   -38.235 1.00 24.63  ? 121 LYS   B HA   1 
ATOM   6260 H  HB2  . LYS   B 1 124 ? -30.414 -0.826  -39.218 1.00 29.29  ? 121 LYS   B HB2  1 
ATOM   6261 H  HB3  . LYS   B 1 124 ? -30.856 -2.296  -38.805 1.00 29.29  ? 121 LYS   B HB3  1 
ATOM   6262 H  HG2  . LYS   B 1 124 ? -32.474 -2.342  -40.383 1.00 33.07  ? 121 LYS   B HG2  1 
ATOM   6263 H  HG3  . LYS   B 1 124 ? -32.357 -0.778  -40.639 1.00 33.07  ? 121 LYS   B HG3  1 
ATOM   6264 H  HD2  . LYS   B 1 124 ? -30.045 -1.275  -41.298 1.00 40.38  ? 121 LYS   B HD2  1 
ATOM   6265 H  HD3  . LYS   B 1 124 ? -30.555 -2.773  -41.447 1.00 40.38  ? 121 LYS   B HD3  1 
ATOM   6266 H  HE2  . LYS   B 1 124 ? -32.201 -1.246  -42.885 1.00 63.10  ? 121 LYS   B HE2  1 
ATOM   6267 H  HE3  . LYS   B 1 124 ? -30.715 -0.849  -43.287 1.00 63.10  ? 121 LYS   B HE3  1 
ATOM   6268 H  HZ1  . LYS   B 1 124 ? -31.446 -2.574  -44.578 1.00 64.17  ? 121 LYS   B HZ1  1 
ATOM   6269 H  HZ2  . LYS   B 1 124 ? -30.338 -3.047  -43.773 1.00 64.17  ? 121 LYS   B HZ2  1 
ATOM   6270 H  HZ3  . LYS   B 1 124 ? -31.697 -3.403  -43.417 1.00 64.17  ? 121 LYS   B HZ3  1 
ATOM   6271 N  N    . LYS   B 1 125 ? -32.817 -2.979  -37.131 1.00 19.90  ? 122 LYS   B N    1 
ATOM   6272 C  CA   . LYS   B 1 125 ? -33.765 -3.996  -36.687 1.00 20.69  ? 122 LYS   B CA   1 
ATOM   6273 C  C    . LYS   B 1 125 ? -33.191 -4.668  -35.456 1.00 16.71  ? 122 LYS   B C    1 
ATOM   6274 O  O    . LYS   B 1 125 ? -31.955 -4.766  -35.294 1.00 18.87  ? 122 LYS   B O    1 
ATOM   6275 C  CB   . LYS   B 1 125 ? -34.043 -5.065  -37.771 1.00 22.78  ? 122 LYS   B CB   1 
ATOM   6276 C  CG   . LYS   B 1 125 ? -34.638 -4.524  -39.069 1.00 24.11  ? 122 LYS   B CG   1 
ATOM   6277 C  CD   . LYS   B 1 125 ? -36.108 -4.251  -38.908 1.00 26.03  ? 122 LYS   B CD   1 
ATOM   6278 C  CE   . LYS   B 1 125 ? -36.768 -3.951  -40.242 1.00 33.22  ? 122 LYS   B CE   1 
ATOM   6279 N  NZ   . LYS   B 1 125 ? -38.151 -3.411  -40.008 1.00 36.28  ? 122 LYS   B NZ   1 
ATOM   6280 H  H    . LYS   B 1 125 ? -31.999 -3.226  -37.035 1.00 23.92  ? 122 LYS   B H    1 
ATOM   6281 H  HA   . LYS   B 1 125 ? -34.611 -3.574  -36.468 1.00 24.87  ? 122 LYS   B HA   1 
ATOM   6282 H  HB2  . LYS   B 1 125 ? -33.206 -5.502  -37.994 1.00 27.38  ? 122 LYS   B HB2  1 
ATOM   6283 H  HB3  . LYS   B 1 125 ? -34.670 -5.713  -37.411 1.00 27.38  ? 122 LYS   B HB3  1 
ATOM   6284 H  HG2  . LYS   B 1 125 ? -34.194 -3.695  -39.308 1.00 28.97  ? 122 LYS   B HG2  1 
ATOM   6285 H  HG3  . LYS   B 1 125 ? -34.521 -5.178  -39.777 1.00 28.97  ? 122 LYS   B HG3  1 
ATOM   6286 H  HD2  . LYS   B 1 125 ? -36.539 -5.030  -38.523 1.00 31.28  ? 122 LYS   B HD2  1 
ATOM   6287 H  HD3  . LYS   B 1 125 ? -36.230 -3.483  -38.328 1.00 31.28  ? 122 LYS   B HD3  1 
ATOM   6288 H  HE2  . LYS   B 1 125 ? -36.249 -3.287  -40.723 1.00 39.90  ? 122 LYS   B HE2  1 
ATOM   6289 H  HE3  . LYS   B 1 125 ? -36.833 -4.764  -40.767 1.00 39.90  ? 122 LYS   B HE3  1 
ATOM   6290 H  HZ1  . LYS   B 1 125 ? -38.565 -3.285  -40.786 1.00 43.58  ? 122 LYS   B HZ1  1 
ATOM   6291 H  HZ2  . LYS   B 1 125 ? -38.624 -3.985  -39.519 1.00 43.58  ? 122 LYS   B HZ2  1 
ATOM   6292 H  HZ3  . LYS   B 1 125 ? -38.106 -2.634  -39.576 1.00 43.58  ? 122 LYS   B HZ3  1 
ATOM   6293 N  N    . ILE   B 1 126 ? -34.081 -5.150  -34.591 1.00 16.90  ? 123 ILE   B N    1 
ATOM   6294 C  CA   . ILE   B 1 126 ? -33.619 -5.772  -33.359 1.00 16.43  ? 123 ILE   B CA   1 
ATOM   6295 C  C    . ILE   B 1 126 ? -34.509 -6.929  -32.990 1.00 16.68  ? 123 ILE   B C    1 
ATOM   6296 O  O    . ILE   B 1 126 ? -35.703 -6.941  -33.288 1.00 18.20  ? 123 ILE   B O    1 
ATOM   6297 C  CB   . ILE   B 1 126 ? -33.552 -4.733  -32.215 1.00 17.18  ? 123 ILE   B CB   1 
ATOM   6298 C  CG1  . ILE   B 1 126 ? -32.767 -5.178  -31.004 1.00 17.64  ? 123 ILE   B CG1  1 
ATOM   6299 C  CG2  . ILE   B 1 126 ? -34.955 -4.268  -31.838 1.00 20.28  ? 123 ILE   B CG2  1 
ATOM   6300 C  CD1  . ILE   B 1 126 ? -32.231 -3.955  -30.175 1.00 20.05  ? 123 ILE   B CD1  1 
ATOM   6301 H  H    . ILE   B 1 126 ? -34.935 -5.127  -34.695 1.00 20.32  ? 123 ILE   B H    1 
ATOM   6302 H  HA   . ILE   B 1 126 ? -32.735 -6.146  -33.506 1.00 19.75  ? 123 ILE   B HA   1 
ATOM   6303 H  HB   . ILE   B 1 126 ? -33.047 -3.984  -32.569 1.00 20.66  ? 123 ILE   B HB   1 
ATOM   6304 H  HG12 . ILE   B 1 126 ? -33.340 -5.707  -30.428 1.00 21.21  ? 123 ILE   B HG12 1 
ATOM   6305 H  HG13 . ILE   B 1 126 ? -32.007 -5.707  -31.292 1.00 21.21  ? 123 ILE   B HG13 1 
ATOM   6306 H  HG21 . ILE   B 1 126 ? -34.886 -3.472  -31.288 1.00 24.37  ? 123 ILE   B HG21 1 
ATOM   6307 H  HG22 . ILE   B 1 126 ? -35.449 -4.068  -32.648 1.00 24.37  ? 123 ILE   B HG22 1 
ATOM   6308 H  HG23 . ILE   B 1 126 ? -35.400 -4.975  -31.345 1.00 24.37  ? 123 ILE   B HG23 1 
ATOM   6309 H  HD11 . ILE   B 1 126 ? -31.587 -4.274  -29.523 1.00 24.10  ? 123 ILE   B HD11 1 
ATOM   6310 H  HD12 . ILE   B 1 126 ? -31.806 -3.326  -30.779 1.00 24.10  ? 123 ILE   B HD12 1 
ATOM   6311 H  HD13 . ILE   B 1 126 ? -32.976 -3.529  -29.724 1.00 24.10  ? 123 ILE   B HD13 1 
ATOM   6312 N  N    . ALA   B 1 127 ? -33.889 -7.947  -32.397 1.00 15.27  ? 124 ALA   B N    1 
ATOM   6313 C  CA   . ALA   B 1 127 ? -34.595 -9.135  -31.969 1.00 16.36  ? 124 ALA   B CA   1 
ATOM   6314 C  C    . ALA   B 1 127 ? -34.315 -9.407  -30.518 1.00 14.98  ? 124 ALA   B C    1 
ATOM   6315 O  O    . ALA   B 1 127 ? -33.159 -9.353  -30.064 1.00 16.94  ? 124 ALA   B O    1 
ATOM   6316 C  CB   . ALA   B 1 127 ? -34.224 -10.338 -32.824 1.00 19.08  ? 124 ALA   B CB   1 
ATOM   6317 H  H    . ALA   B 1 127 ? -33.045 -7.967  -32.234 1.00 18.36  ? 124 ALA   B H    1 
ATOM   6318 H  HA   . ALA   B 1 127 ? -35.551 -8.991  -32.055 1.00 19.68  ? 124 ALA   B HA   1 
ATOM   6319 H  HB1  . ALA   B 1 127 ? -34.737 -11.106 -32.529 1.00 22.93  ? 124 ALA   B HB1  1 
ATOM   6320 H  HB2  . ALA   B 1 127 ? -34.428 -10.141 -33.752 1.00 22.93  ? 124 ALA   B HB2  1 
ATOM   6321 H  HB3  . ALA   B 1 127 ? -33.275 -10.515 -32.725 1.00 22.93  ? 124 ALA   B HB3  1 
ATOM   6322 N  N    . PHE   B 1 128 ? -35.388 -9.731  -29.795 1.00 16.39  ? 125 PHE   B N    1 
ATOM   6323 C  CA   . PHE   B 1 128 ? -35.323 -10.094 -28.392 1.00 14.66  ? 125 PHE   B CA   1 
ATOM   6324 C  C    . PHE   B 1 128 ? -35.626 -11.585 -28.270 1.00 16.25  ? 125 PHE   B C    1 
ATOM   6325 O  O    . PHE   B 1 128 ? -36.781 -12.022 -28.390 1.00 17.11  ? 125 PHE   B O    1 
ATOM   6326 C  CB   . PHE   B 1 128 ? -36.300 -9.279  -27.527 1.00 17.32  ? 125 PHE   B CB   1 
ATOM   6327 C  CG   . PHE   B 1 128 ? -36.158 -7.783  -27.670 1.00 17.22  ? 125 PHE   B CG   1 
ATOM   6328 C  CD1  . PHE   B 1 128 ? -34.912 -7.177  -27.746 1.00 15.87  ? 125 PHE   B CD1  1 
ATOM   6329 C  CD2  . PHE   B 1 128 ? -37.273 -6.981  -27.723 1.00 19.72  ? 125 PHE   B CD2  1 
ATOM   6330 C  CE1  . PHE   B 1 128 ? -34.826 -5.763  -27.896 1.00 16.66  ? 125 PHE   B CE1  1 
ATOM   6331 C  CE2  . PHE   B 1 128 ? -37.143 -5.584  -27.863 1.00 20.43  ? 125 PHE   B CE2  1 
ATOM   6332 C  CZ   . PHE   B 1 128 ? -35.911 -5.005  -27.963 1.00 17.99  ? 125 PHE   B CZ   1 
ATOM   6333 H  H    . PHE   B 1 128 ? -36.188 -9.746  -30.113 1.00 19.71  ? 125 PHE   B H    1 
ATOM   6334 H  HA   . PHE   B 1 128 ? -34.421 -9.916  -28.083 1.00 17.63  ? 125 PHE   B HA   1 
ATOM   6335 H  HB2  . PHE   B 1 128 ? -37.207 -9.513  -27.780 1.00 20.83  ? 125 PHE   B HB2  1 
ATOM   6336 H  HB3  . PHE   B 1 128 ? -36.148 -9.501  -26.595 1.00 20.83  ? 125 PHE   B HB3  1 
ATOM   6337 H  HD1  . PHE   B 1 128 ? -34.138 -7.691  -27.699 1.00 19.08  ? 125 PHE   B HD1  1 
ATOM   6338 H  HD2  . PHE   B 1 128 ? -38.119 -7.362  -27.666 1.00 23.70  ? 125 PHE   B HD2  1 
ATOM   6339 H  HE1  . PHE   B 1 128 ? -33.989 -5.362  -27.947 1.00 20.03  ? 125 PHE   B HE1  1 
ATOM   6340 H  HE2  . PHE   B 1 128 ? -37.905 -5.051  -27.886 1.00 24.56  ? 125 PHE   B HE2  1 
ATOM   6341 H  HZ   . PHE   B 1 128 ? -35.833 -4.086  -28.079 1.00 21.62  ? 125 PHE   B HZ   1 
ATOM   6342 N  N    . HIS   B 1 129 ? -34.571 -12.391 -28.088 1.00 16.15  ? 126 HIS   B N    1 
ATOM   6343 C  CA   . HIS   B 1 129 ? -34.734 -13.820 -27.938 1.00 17.05  ? 126 HIS   B CA   1 
ATOM   6344 C  C    . HIS   B 1 129 ? -34.893 -14.160 -26.464 1.00 20.30  ? 126 HIS   B C    1 
ATOM   6345 O  O    . HIS   B 1 129 ? -33.974 -13.962 -25.660 1.00 19.58  ? 126 HIS   B O    1 
ATOM   6346 C  CB   . HIS   B 1 129 ? -33.538 -14.534 -28.573 1.00 16.32  ? 126 HIS   B CB   1 
ATOM   6347 C  CG   . HIS   B 1 129 ? -33.626 -16.031 -28.511 1.00 16.77  ? 126 HIS   B CG   1 
ATOM   6348 N  ND1  . HIS   B 1 129 ? -33.024 -16.759 -27.506 1.00 23.46  ? 126 HIS   B ND1  1 
ATOM   6349 C  CD2  . HIS   B 1 129 ? -34.220 -16.937 -29.329 1.00 18.22  ? 126 HIS   B CD2  1 
ATOM   6350 C  CE1  . HIS   B 1 129 ? -33.266 -18.047 -27.696 1.00 25.04  ? 126 HIS   B CE1  1 
ATOM   6351 N  NE2  . HIS   B 1 129 ? -33.992 -18.187 -28.795 1.00 22.76  ? 126 HIS   B NE2  1 
ATOM   6352 H  H    . HIS   B 1 129 ? -33.755 -12.122 -28.050 1.00 19.42  ? 126 HIS   B H    1 
ATOM   6353 H  HA   . HIS   B 1 129 ? -35.545 -14.113 -28.382 1.00 20.50  ? 126 HIS   B HA   1 
ATOM   6354 H  HB2  . HIS   B 1 129 ? -33.482 -14.279 -29.507 1.00 19.63  ? 126 HIS   B HB2  1 
ATOM   6355 H  HB3  . HIS   B 1 129 ? -32.731 -14.266 -28.106 1.00 19.63  ? 126 HIS   B HB3  1 
ATOM   6356 H  HD2  . HIS   B 1 129 ? -34.694 -16.749 -30.107 1.00 21.91  ? 126 HIS   B HD2  1 
ATOM   6357 H  HE1  . HIS   B 1 129 ? -32.974 -18.740 -27.149 1.00 30.09  ? 126 HIS   B HE1  1 
ATOM   6358 H  HE2  . HIS   B 1 129 ? -34.274 -18.932 -29.120 1.00 27.36  ? 126 HIS   B HE2  1 
ATOM   6359 N  N    . GLU   B 1 130 ? -36.078 -14.654 -26.113 1.00 18.89  ? 127 GLU   B N    1 
ATOM   6360 C  CA   . GLU   B 1 130 ? -36.390 -15.186 -24.784 1.00 21.98  ? 127 GLU   B CA   1 
ATOM   6361 C  C    . GLU   B 1 130 ? -35.913 -14.274 -23.664 1.00 19.15  ? 127 GLU   B C    1 
ATOM   6362 O  O    . GLU   B 1 130 ? -35.064 -14.666 -22.840 1.00 18.95  ? 127 GLU   B O    1 
ATOM   6363 C  CB   . GLU   B 1 130 ? -35.818 -16.592 -24.712 1.00 22.16  ? 127 GLU   B CB   1 
ATOM   6364 C  CG   . GLU   B 1 130 ? -36.696 -17.490 -25.655 1.00 25.47  ? 127 GLU   B CG   1 
ATOM   6365 C  CD   . GLU   B 1 130 ? -36.722 -18.945 -25.313 1.00 25.26  ? 127 GLU   B CD   1 
ATOM   6366 O  OE1  . GLU   B 1 130 ? -37.352 -19.703 -26.068 1.00 25.38  ? 127 GLU   B OE1  1 
ATOM   6367 O  OE2  . GLU   B 1 130 ? -36.041 -19.369 -24.368 1.00 29.49  ? 127 GLU   B OE2  1 
ATOM   6368 H  H    . GLU   B 1 130 ? -36.749 -14.695 -26.649 1.00 22.72  ? 127 GLU   B H    1 
ATOM   6369 H  HA   . GLU   B 1 130 ? -37.348 -15.224 -24.640 1.00 26.41  ? 127 GLU   B HA   1 
ATOM   6370 H  HB2  . GLU   B 1 130 ? -34.899 -16.599 -25.020 1.00 26.63  ? 127 GLU   B HB2  1 
ATOM   6371 H  HB3  . GLU   B 1 130 ? -35.867 -16.930 -23.804 1.00 26.63  ? 127 GLU   B HB3  1 
ATOM   6372 H  HG2  . GLU   B 1 130 ? -37.611 -17.169 -25.619 1.00 30.61  ? 127 GLU   B HG2  1 
ATOM   6373 H  HG3  . GLU   B 1 130 ? -36.353 -17.412 -26.559 1.00 30.61  ? 127 GLU   B HG3  1 
ATOM   6374 N  N    . PRO   B 1 131 ? -36.536 -13.093 -23.531 1.00 18.06  ? 128 PRO   B N    1 
ATOM   6375 C  CA   . PRO   B 1 131 ? -36.173 -12.150 -22.480 1.00 19.31  ? 128 PRO   B CA   1 
ATOM   6376 C  C    . PRO   B 1 131 ? -36.733 -12.557 -21.124 1.00 19.82  ? 128 PRO   B C    1 
ATOM   6377 O  O    . PRO   B 1 131 ? -37.887 -13.005 -21.025 1.00 22.34  ? 128 PRO   B O    1 
ATOM   6378 C  CB   . PRO   B 1 131 ? -36.798 -10.836 -22.963 1.00 19.88  ? 128 PRO   B CB   1 
ATOM   6379 C  CG   . PRO   B 1 131 ? -37.987 -11.246 -23.701 1.00 20.55  ? 128 PRO   B CG   1 
ATOM   6380 C  CD   . PRO   B 1 131 ? -37.621 -12.570 -24.379 1.00 24.36  ? 128 PRO   B CD   1 
ATOM   6381 H  HA   . PRO   B 1 131 ? -35.208 -12.068 -22.415 1.00 23.21  ? 128 PRO   B HA   1 
ATOM   6382 H  HB2  . PRO   B 1 131 ? -37.033 -10.281 -22.203 1.00 23.89  ? 128 PRO   B HB2  1 
ATOM   6383 H  HB3  . PRO   B 1 131 ? -36.176 -10.364 -23.539 1.00 23.89  ? 128 PRO   B HB3  1 
ATOM   6384 H  HG2  . PRO   B 1 131 ? -38.728 -11.367 -23.086 1.00 24.70  ? 128 PRO   B HG2  1 
ATOM   6385 H  HG3  . PRO   B 1 131 ? -38.211 -10.572 -24.362 1.00 24.70  ? 128 PRO   B HG3  1 
ATOM   6386 H  HD2  . PRO   B 1 131 ? -38.378 -13.177 -24.384 1.00 29.28  ? 128 PRO   B HD2  1 
ATOM   6387 H  HD3  . PRO   B 1 131 ? -37.311 -12.420 -25.285 1.00 29.28  ? 128 PRO   B HD3  1 
ATOM   6388 N  N    . PRO   B 1 132 ? -35.928 -12.415 -20.054 1.00 18.34  ? 129 PRO   B N    1 
ATOM   6389 C  CA   . PRO   B 1 132 ? -36.421 -12.726 -18.703 1.00 16.99  ? 129 PRO   B CA   1 
ATOM   6390 C  C    . PRO   B 1 132 ? -36.770 -11.492 -17.879 1.00 19.77  ? 129 PRO   B C    1 
ATOM   6391 O  O    . PRO   B 1 132 ? -36.889 -11.586 -16.648 1.00 22.48  ? 129 PRO   B O    1 
ATOM   6392 C  CB   . PRO   B 1 132 ? -35.244 -13.482 -18.077 1.00 22.31  ? 129 PRO   B CB   1 
ATOM   6393 C  CG   . PRO   B 1 132 ? -34.034 -12.770 -18.692 1.00 20.84  ? 129 PRO   B CG   1 
ATOM   6394 C  CD   . PRO   B 1 132 ? -34.449 -12.383 -20.105 1.00 20.61  ? 129 PRO   B CD   1 
ATOM   6395 H  HA   . PRO   B 1 132 ? -37.202 -13.298 -18.765 1.00 20.43  ? 129 PRO   B HA   1 
ATOM   6396 H  HB2  . PRO   B 1 132 ? -35.258 -13.394 -17.111 1.00 26.81  ? 129 PRO   B HB2  1 
ATOM   6397 H  HB3  . PRO   B 1 132 ? -35.270 -14.420 -18.325 1.00 26.81  ? 129 PRO   B HB3  1 
ATOM   6398 H  HG2  . PRO   B 1 132 ? -33.820 -11.981 -18.169 1.00 25.05  ? 129 PRO   B HG2  1 
ATOM   6399 H  HG3  . PRO   B 1 132 ? -33.274 -13.372 -18.710 1.00 25.05  ? 129 PRO   B HG3  1 
ATOM   6400 H  HD2  . PRO   B 1 132 ? -34.131 -11.493 -20.326 1.00 24.77  ? 129 PRO   B HD2  1 
ATOM   6401 H  HD3  . PRO   B 1 132 ? -34.112 -13.025 -20.750 1.00 24.77  ? 129 PRO   B HD3  1 
ATOM   6402 N  N    . ILE   B 1 133 ? -36.967 -10.349 -18.525 1.00 19.72  ? 130 ILE   B N    1 
ATOM   6403 C  CA   . ILE   B 1 133 ? -37.309 -9.122  -17.810 1.00 18.60  ? 130 ILE   B CA   1 
ATOM   6404 C  C    . ILE   B 1 133 ? -38.719 -9.241  -17.252 1.00 18.50  ? 130 ILE   B C    1 
ATOM   6405 O  O    . ILE   B 1 133 ? -39.610 -9.810  -17.886 1.00 20.45  ? 130 ILE   B O    1 
ATOM   6406 C  CB   . ILE   B 1 133 ? -37.130 -7.919  -18.748 1.00 19.86  ? 130 ILE   B CB   1 
ATOM   6407 C  CG1  . ILE   B 1 133 ? -37.393 -6.606  -17.972 1.00 19.35  ? 130 ILE   B CG1  1 
ATOM   6408 C  CG2  . ILE   B 1 133 ? -37.981 -8.036  -19.985 1.00 20.37  ? 130 ILE   B CG2  1 
ATOM   6409 C  CD1  . ILE   B 1 133 ? -36.709 -5.384  -18.522 1.00 23.30  ? 130 ILE   B CD1  1 
ATOM   6410 H  H    . ILE   B 1 133 ? -36.909 -10.254 -19.378 1.00 23.70  ? 130 ILE   B H    1 
ATOM   6411 H  HA   . ILE   B 1 133 ? -36.716 -8.990  -17.053 1.00 22.37  ? 130 ILE   B HA   1 
ATOM   6412 H  HB   . ILE   B 1 133 ? -36.212 -7.907  -19.060 1.00 23.87  ? 130 ILE   B HB   1 
ATOM   6413 H  HG12 . ILE   B 1 133 ? -38.348 -6.432  -17.980 1.00 23.26  ? 130 ILE   B HG12 1 
ATOM   6414 H  HG13 . ILE   B 1 133 ? -37.086 -6.724  -17.059 1.00 23.26  ? 130 ILE   B HG13 1 
ATOM   6415 H  HG21 . ILE   B 1 133 ? -37.919 -7.210  -20.490 1.00 24.49  ? 130 ILE   B HG21 1 
ATOM   6416 H  HG22 . ILE   B 1 133 ? -37.658 -8.777  -20.521 1.00 24.49  ? 130 ILE   B HG22 1 
ATOM   6417 H  HG23 . ILE   B 1 133 ? -38.901 -8.194  -19.722 1.00 24.49  ? 130 ILE   B HG23 1 
ATOM   6418 H  HD11 . ILE   B 1 133 ? -36.947 -4.617  -17.977 1.00 28.00  ? 130 ILE   B HD11 1 
ATOM   6419 H  HD12 . ILE   B 1 133 ? -35.749 -5.522  -18.498 1.00 28.00  ? 130 ILE   B HD12 1 
ATOM   6420 H  HD13 . ILE   B 1 133 ? -37.001 -5.243  -19.436 1.00 28.00  ? 130 ILE   B HD13 1 
ATOM   6421 N  N    . ASN   B 1 134 ? -38.936 -8.711  -16.048 1.00 17.56  ? 131 ASN   B N    1 
ATOM   6422 C  CA   . ASN   B 1 134 ? -40.243 -8.800  -15.411 1.00 19.12  ? 131 ASN   B CA   1 
ATOM   6423 C  C    . ASN   B 1 134 ? -40.878 -7.450  -15.082 1.00 19.12  ? 131 ASN   B C    1 
ATOM   6424 O  O    . ASN   B 1 134 ? -42.031 -7.425  -14.665 1.00 18.85  ? 131 ASN   B O    1 
ATOM   6425 C  CB   . ASN   B 1 134 ? -40.162 -9.650  -14.124 1.00 19.14  ? 131 ASN   B CB   1 
ATOM   6426 C  CG   . ASN   B 1 134 ? -39.324 -8.996  -13.027 1.00 20.27  ? 131 ASN   B CG   1 
ATOM   6427 O  OD1  . ASN   B 1 134 ? -39.565 -7.845  -12.628 1.00 20.60  ? 131 ASN   B OD1  1 
ATOM   6428 N  ND2  . ASN   B 1 134 ? -38.326 -9.748  -12.512 1.00 20.94  ? 131 ASN   B ND2  1 
ATOM   6429 H  H    . ASN   B 1 134 ? -38.342 -8.296  -15.585 1.00 21.12  ? 131 ASN   B H    1 
ATOM   6430 H  HA   . ASN   B 1 134 ? -40.837 -9.248  -16.033 1.00 22.98  ? 131 ASN   B HA   1 
ATOM   6431 H  HB2  . ASN   B 1 134 ? -41.058 -9.782  -13.777 1.00 23.01  ? 131 ASN   B HB2  1 
ATOM   6432 H  HB3  . ASN   B 1 134 ? -39.759 -10.506 -14.337 1.00 23.01  ? 131 ASN   B HB3  1 
ATOM   6433 H  HD21 . ASN   B 1 134 ? -37.823 -9.429  -11.892 1.00 25.17  ? 131 ASN   B HD21 1 
ATOM   6434 H  HD22 . ASN   B 1 134 ? -38.193 -10.546 -12.806 1.00 25.17  ? 131 ASN   B HD22 1 
ATOM   6435 N  N    . THR   B 1 135 ? -40.198 -6.330  -15.321 1.00 17.24  ? 132 THR   B N    1 
ATOM   6436 C  CA   . THR   B 1 135 ? -40.599 -5.080  -14.662 1.00 17.11  ? 132 THR   B CA   1 
ATOM   6437 C  C    . THR   B 1 135 ? -42.008 -4.671  -15.040 1.00 18.97  ? 132 THR   B C    1 
ATOM   6438 O  O    . THR   B 1 135 ? -42.767 -4.188  -14.199 1.00 21.30  ? 132 THR   B O    1 
ATOM   6439 C  CB   . THR   B 1 135 ? -39.629 -3.963  -15.037 1.00 21.50  ? 132 THR   B CB   1 
ATOM   6440 O  OG1  . THR   B 1 135 ? -38.308 -4.514  -15.100 1.00 19.19  ? 132 THR   B OG1  1 
ATOM   6441 C  CG2  . THR   B 1 135 ? -39.679 -2.845  -14.030 1.00 22.58  ? 132 THR   B CG2  1 
ATOM   6442 H  H    . THR   B 1 135 ? -39.520 -6.264  -15.845 1.00 20.73  ? 132 THR   B H    1 
ATOM   6443 H  HA   . THR   B 1 135 ? -40.569 -5.221  -13.703 1.00 20.58  ? 132 THR   B HA   1 
ATOM   6444 H  HB   . THR   B 1 135 ? -39.869 -3.584  -15.897 1.00 25.84  ? 132 THR   B HB   1 
ATOM   6445 H  HG1  . THR   B 1 135 ? -37.739 -3.896  -15.103 1.00 23.07  ? 132 THR   B HG1  1 
ATOM   6446 H  HG21 . THR   B 1 135 ? -39.092 -2.124  -14.305 1.00 27.14  ? 132 THR   B HG21 1 
ATOM   6447 H  HG22 . THR   B 1 135 ? -40.584 -2.505  -13.957 1.00 27.14  ? 132 THR   B HG22 1 
ATOM   6448 H  HG23 . THR   B 1 135 ? -39.394 -3.169  -13.161 1.00 27.14  ? 132 THR   B HG23 1 
ATOM   6449 N  N    . PHE   B 1 136 ? -42.359 -4.814  -16.313 1.00 20.83  ? 133 PHE   B N    1 
ATOM   6450 C  CA   . PHE   B 1 136 ? -43.636 -4.377  -16.832 1.00 21.23  ? 133 PHE   B CA   1 
ATOM   6451 C  C    . PHE   B 1 136 ? -44.722 -5.460  -16.806 1.00 21.97  ? 133 PHE   B C    1 
ATOM   6452 O  O    . PHE   B 1 136 ? -45.834 -5.219  -17.310 1.00 23.56  ? 133 PHE   B O    1 
ATOM   6453 C  CB   . PHE   B 1 136 ? -43.438 -3.867  -18.290 1.00 22.07  ? 133 PHE   B CB   1 
ATOM   6454 C  CG   . PHE   B 1 136 ? -42.723 -4.854  -19.174 1.00 20.04  ? 133 PHE   B CG   1 
ATOM   6455 C  CD1  . PHE   B 1 136 ? -43.392 -5.963  -19.661 1.00 20.08  ? 133 PHE   B CD1  1 
ATOM   6456 C  CD2  . PHE   B 1 136 ? -41.381 -4.676  -19.501 1.00 20.53  ? 133 PHE   B CD2  1 
ATOM   6457 C  CE1  . PHE   B 1 136 ? -42.727 -6.895  -20.442 1.00 20.56  ? 133 PHE   B CE1  1 
ATOM   6458 C  CE2  . PHE   B 1 136 ? -40.704 -5.626  -20.279 1.00 20.75  ? 133 PHE   B CE2  1 
ATOM   6459 C  CZ   . PHE   B 1 136 ? -41.401 -6.721  -20.754 1.00 19.98  ? 133 PHE   B CZ   1 
ATOM   6460 H  H    . PHE   B 1 136 ? -41.854 -5.173  -16.909 1.00 25.03  ? 133 PHE   B H    1 
ATOM   6461 H  HA   . PHE   B 1 136 ? -43.959 -3.648  -16.279 1.00 25.52  ? 133 PHE   B HA   1 
ATOM   6462 H  HB2  . PHE   B 1 136 ? -44.307 -3.692  -18.682 1.00 26.53  ? 133 PHE   B HB2  1 
ATOM   6463 H  HB3  . PHE   B 1 136 ? -42.913 -3.052  -18.269 1.00 26.53  ? 133 PHE   B HB3  1 
ATOM   6464 H  HD1  . PHE   B 1 136 ? -44.292 -6.084  -19.463 1.00 24.14  ? 133 PHE   B HD1  1 
ATOM   6465 H  HD2  . PHE   B 1 136 ? -40.930 -3.920  -19.201 1.00 24.68  ? 133 PHE   B HD2  1 
ATOM   6466 H  HE1  . PHE   B 1 136 ? -43.181 -7.643  -20.757 1.00 24.71  ? 133 PHE   B HE1  1 
ATOM   6467 H  HE2  . PHE   B 1 136 ? -39.801 -5.521  -20.471 1.00 24.94  ? 133 PHE   B HE2  1 
ATOM   6468 H  HZ   . PHE   B 1 136 ? -40.968 -7.345  -21.291 1.00 24.02  ? 133 PHE   B HZ   1 
ATOM   6469 N  N    . LEU   B 1 137 ? -44.451 -6.629  -16.222 1.00 20.64  ? 134 LEU   B N    1 
ATOM   6470 C  CA   . LEU   B 1 137 ? -45.452 -7.688  -16.193 1.00 21.25  ? 134 LEU   B CA   1 
ATOM   6471 C  C    . LEU   B 1 137 ? -46.545 -7.393  -15.163 1.00 23.46  ? 134 LEU   B C    1 
ATOM   6472 O  O    . LEU   B 1 137 ? -46.306 -6.700  -14.167 1.00 24.19  ? 134 LEU   B O    1 
ATOM   6473 C  CB   . LEU   B 1 137 ? -44.773 -9.026  -15.868 1.00 20.96  ? 134 LEU   B CB   1 
ATOM   6474 C  CG   . LEU   B 1 137 ? -43.691 -9.559  -16.821 1.00 19.49  ? 134 LEU   B CG   1 
ATOM   6475 C  CD1  . LEU   B 1 137 ? -43.068 -10.824 -16.255 1.00 22.16  ? 134 LEU   B CD1  1 
ATOM   6476 C  CD2  . LEU   B 1 137 ? -44.282 -9.789  -18.202 1.00 22.93  ? 134 LEU   B CD2  1 
ATOM   6477 H  H    . LEU   B 1 137 ? -43.706 -6.829  -15.843 1.00 24.81  ? 134 LEU   B H    1 
ATOM   6478 H  HA   . LEU   B 1 137 ? -45.884 -7.755  -17.059 1.00 25.54  ? 134 LEU   B HA   1 
ATOM   6479 H  HB2  . LEU   B 1 137 ? -44.353 -8.936  -14.999 1.00 25.19  ? 134 LEU   B HB2  1 
ATOM   6480 H  HB3  . LEU   B 1 137 ? -45.466 -9.703  -15.834 1.00 25.19  ? 134 LEU   B HB3  1 
ATOM   6481 H  HG   . LEU   B 1 137 ? -42.980 -8.906  -16.914 1.00 23.43  ? 134 LEU   B HG   1 
ATOM   6482 H  HD11 . LEU   B 1 137 ? -42.367 -11.125 -16.852 1.00 26.64  ? 134 LEU   B HD11 1 
ATOM   6483 H  HD12 . LEU   B 1 137 ? -42.697 -10.628 -15.380 1.00 26.64  ? 134 LEU   B HD12 1 
ATOM   6484 H  HD13 . LEU   B 1 137 ? -43.754 -11.506 -16.178 1.00 26.64  ? 134 LEU   B HD13 1 
ATOM   6485 H  HD21 . LEU   B 1 137 ? -43.643 -10.282 -18.741 1.00 27.56  ? 134 LEU   B HD21 1 
ATOM   6486 H  HD22 . LEU   B 1 137 ? -45.103 -10.298 -18.114 1.00 27.56  ? 134 LEU   B HD22 1 
ATOM   6487 H  HD23 . LEU   B 1 137 ? -44.468 -8.930  -18.613 1.00 27.56  ? 134 LEU   B HD23 1 
ATOM   6488 N  N    . PRO   B 1 138 ? -47.740 -7.951  -15.358 1.00 23.52  ? 135 PRO   B N    1 
ATOM   6489 C  CA   . PRO   B 1 138 ? -48.796 -7.799  -14.345 1.00 26.75  ? 135 PRO   B CA   1 
ATOM   6490 C  C    . PRO   B 1 138 ? -48.513 -8.551  -13.048 1.00 28.80  ? 135 PRO   B C    1 
ATOM   6491 O  O    . PRO   B 1 138 ? -49.170 -8.271  -12.039 1.00 31.77  ? 135 PRO   B O    1 
ATOM   6492 C  CB   . PRO   B 1 138 ? -50.047 -8.350  -15.037 1.00 27.19  ? 135 PRO   B CB   1 
ATOM   6493 C  CG   . PRO   B 1 138 ? -49.634 -8.850  -16.357 1.00 30.10  ? 135 PRO   B CG   1 
ATOM   6494 C  CD   . PRO   B 1 138 ? -48.144 -8.762  -16.520 1.00 24.43  ? 135 PRO   B CD   1 
ATOM   6495 H  HA   . PRO   B 1 138 ? -48.928 -6.857  -14.151 1.00 32.14  ? 135 PRO   B HA   1 
ATOM   6496 H  HB2  . PRO   B 1 138 ? -50.417 -9.070  -14.503 1.00 32.67  ? 135 PRO   B HB2  1 
ATOM   6497 H  HB3  . PRO   B 1 138 ? -50.700 -7.639  -15.133 1.00 32.67  ? 135 PRO   B HB3  1 
ATOM   6498 H  HG2  . PRO   B 1 138 ? -49.916 -9.774  -16.436 1.00 36.17  ? 135 PRO   B HG2  1 
ATOM   6499 H  HG3  . PRO   B 1 138 ? -50.067 -8.311  -17.037 1.00 36.17  ? 135 PRO   B HG3  1 
ATOM   6500 H  HD2  . PRO   B 1 138 ? -47.738 -9.643  -16.487 1.00 29.36  ? 135 PRO   B HD2  1 
ATOM   6501 H  HD3  . PRO   B 1 138 ? -47.910 -8.320  -17.351 1.00 29.36  ? 135 PRO   B HD3  1 
ATOM   6502 N  N    . ASP   B 1 139 ? -47.628 -9.537  -13.070 1.00 23.14  ? 136 ASP   B N    1 
ATOM   6503 C  CA   . ASP   B 1 139 ? -47.206 -10.283 -11.887 1.00 26.50  ? 136 ASP   B CA   1 
ATOM   6504 C  C    . ASP   B 1 139 ? -45.725 -10.035 -11.615 1.00 24.69  ? 136 ASP   B C    1 
ATOM   6505 O  O    . ASP   B 1 139 ? -45.003 -10.912 -11.123 1.00 24.37  ? 136 ASP   B O    1 
ATOM   6506 C  CB   . ASP   B 1 139 ? -47.537 -11.768 -12.038 1.00 26.93  ? 136 ASP   B CB   1 
ATOM   6507 C  CG   . ASP   B 1 139 ? -46.955 -12.409 -13.303 1.00 30.65  ? 136 ASP   B CG   1 
ATOM   6508 O  OD1  . ASP   B 1 139 ? -46.338 -11.739 -14.150 1.00 27.94  ? 136 ASP   B OD1  1 
ATOM   6509 O  OD2  . ASP   B 1 139 ? -47.175 -13.627 -13.484 1.00 36.29  ? 136 ASP   B OD2  1 
ATOM   6510 H  H    . ASP   B 1 139 ? -47.239 -9.806  -13.788 1.00 27.81  ? 136 ASP   B H    1 
ATOM   6511 H  HA   . ASP   B 1 139 ? -47.694 -9.976  -11.107 1.00 31.84  ? 136 ASP   B HA   1 
ATOM   6512 H  HB2  . ASP   B 1 139 ? -47.179 -12.246 -11.274 1.00 32.36  ? 136 ASP   B HB2  1 
ATOM   6513 H  HB3  . ASP   B 1 139 ? -48.501 -11.870 -12.073 1.00 32.36  ? 136 ASP   B HB3  1 
ATOM   6514 N  N    A SER   B 1 140 ? -45.256 -8.816  -11.895 0.33 21.82  ? 137 SER   B N    1 
ATOM   6515 N  N    B SER   B 1 140 ? -45.273 -8.810  -11.907 0.67 21.68  ? 137 SER   B N    1 
ATOM   6516 C  CA   A SER   B 1 140 ? -43.842 -8.501  -11.685 0.33 22.81  ? 137 SER   B CA   1 
ATOM   6517 C  CA   B SER   B 1 140 ? -43.872 -8.434  -11.683 0.67 22.75  ? 137 SER   B CA   1 
ATOM   6518 C  C    A SER   B 1 140 ? -43.407 -8.758  -10.246 0.33 22.82  ? 137 SER   B C    1 
ATOM   6519 C  C    B SER   B 1 140 ? -43.414 -8.722  -10.259 0.67 22.67  ? 137 SER   B C    1 
ATOM   6520 O  O    A SER   B 1 140 ? -42.277 -9.198  -10.006 0.33 23.26  ? 137 SER   B O    1 
ATOM   6521 O  O    B SER   B 1 140 ? -42.273 -9.145  -10.042 0.67 23.25  ? 137 SER   B O    1 
ATOM   6522 C  CB   A SER   B 1 140 ? -43.551 -7.041  -12.057 0.33 21.26  ? 137 SER   B CB   1 
ATOM   6523 C  CB   B SER   B 1 140 ? -43.653 -6.939  -12.008 0.67 21.05  ? 137 SER   B CB   1 
ATOM   6524 O  OG   A SER   B 1 140 ? -42.214 -6.697  -11.728 0.33 19.10  ? 137 SER   B OG   1 
ATOM   6525 O  OG   B SER   B 1 140 ? -44.348 -6.064  -11.121 0.67 24.94  ? 137 SER   B OG   1 
ATOM   6526 H  H    A SER   B 1 140 ? -45.727 -8.166  -12.203 0.33 26.23  ? 137 SER   B H    1 
ATOM   6527 H  H    B SER   B 1 140 ? -45.755 -8.178  -12.235 0.67 26.05  ? 137 SER   B H    1 
ATOM   6528 H  HA   A SER   B 1 140 ? -43.325 -9.077  -12.270 0.33 27.41  ? 137 SER   B HA   1 
ATOM   6529 H  HA   B SER   B 1 140 ? -43.329 -8.965  -12.286 0.67 27.35  ? 137 SER   B HA   1 
ATOM   6530 H  HB2  A SER   B 1 140 ? -43.682 -6.925  -13.011 0.33 25.55  ? 137 SER   B HB2  1 
ATOM   6531 H  HB2  B SER   B 1 140 ? -42.704 -6.748  -11.947 0.67 25.30  ? 137 SER   B HB2  1 
ATOM   6532 H  HB3  A SER   B 1 140 ? -44.156 -6.463  -11.566 0.33 25.55  ? 137 SER   B HB3  1 
ATOM   6533 H  HB3  B SER   B 1 140 ? -43.967 -6.773  -12.911 0.67 25.30  ? 137 SER   B HB3  1 
ATOM   6534 H  HG   A SER   B 1 140 ? -41.679 -7.148  -12.193 0.33 22.96  ? 137 SER   B HG   1 
ATOM   6535 H  HG   B SER   B 1 140 ? -44.316 -5.276  -11.412 0.67 29.97  ? 137 SER   B HG   1 
ATOM   6536 N  N    . THR   B 1 141 ? -44.272 -8.455  -9.271  1.00 23.70  ? 138 THR   B N    1 
ATOM   6537 C  CA   . THR   B 1 141 ? -43.883 -8.634  -7.871  1.00 26.54  ? 138 THR   B CA   1 
ATOM   6538 C  C    . THR   B 1 141 ? -43.519 -10.084 -7.589  1.00 27.61  ? 138 THR   B C    1 
ATOM   6539 O  O    . THR   B 1 141 ? -42.525 -10.369 -6.907  1.00 25.33  ? 138 THR   B O    1 
ATOM   6540 C  CB   . THR   B 1 141 ? -45.004 -8.183  -6.940  1.00 27.04  ? 138 THR   B CB   1 
ATOM   6541 O  OG1  . THR   B 1 141 ? -45.376 -6.828  -7.244  1.00 29.07  ? 138 THR   B OG1  1 
ATOM   6542 C  CG2  . THR   B 1 141 ? -44.595 -8.307  -5.482  1.00 26.04  ? 138 THR   B CG2  1 
ATOM   6543 H  H    A THR   B 1 141 ? -45.068 -8.153  -9.391  0.33 28.48  ? 138 THR   B H    1 
ATOM   6544 H  H    B THR   B 1 141 ? -45.076 -8.172  -9.383  0.67 28.48  ? 138 THR   B H    1 
ATOM   6545 H  HA   . THR   B 1 141 ? -43.108 -8.078  -7.694  1.00 31.89  ? 138 THR   B HA   1 
ATOM   6546 H  HB   . THR   B 1 141 ? -45.777 -8.755  -7.069  1.00 32.49  ? 138 THR   B HB   1 
ATOM   6547 H  HG1  . THR   B 1 141 ? -46.119 -6.649  -6.896  1.00 34.92  ? 138 THR   B HG1  1 
ATOM   6548 H  HG21 . THR   B 1 141 ? -45.246 -7.865  -4.916  1.00 31.29  ? 138 THR   B HG21 1 
ATOM   6549 H  HG22 . THR   B 1 141 ? -44.542 -9.242  -5.231  1.00 31.29  ? 138 THR   B HG22 1 
ATOM   6550 H  HG23 . THR   B 1 141 ? -43.727 -7.895  -5.345  1.00 31.29  ? 138 THR   B HG23 1 
ATOM   6551 N  N    . TYR   B 1 142 ? -44.320 -11.021 -8.099  1.00 26.24  ? 139 TYR   B N    1 
ATOM   6552 C  CA   . TYR   B 1 142 ? -44.001 -12.425 -7.897  1.00 29.50  ? 139 TYR   B CA   1 
ATOM   6553 C  C    . TYR   B 1 142 ? -42.611 -12.757 -8.430  1.00 25.23  ? 139 TYR   B C    1 
ATOM   6554 O  O    . TYR   B 1 142 ? -41.821 -13.414 -7.755  1.00 28.31  ? 139 TYR   B O    1 
ATOM   6555 C  CB   . TYR   B 1 142 ? -45.070 -13.296 -8.565  1.00 26.99  ? 139 TYR   B CB   1 
ATOM   6556 C  CG   . TYR   B 1 142 ? -44.697 -14.763 -8.641  1.00 29.52  ? 139 TYR   B CG   1 
ATOM   6557 C  CD1  . TYR   B 1 142 ? -43.855 -15.242 -9.634  1.00 33.07  ? 139 TYR   B CD1  1 
ATOM   6558 C  CD2  . TYR   B 1 142 ? -45.213 -15.672 -7.716  1.00 37.00  ? 139 TYR   B CD2  1 
ATOM   6559 C  CE1  . TYR   B 1 142 ? -43.506 -16.588 -9.707  1.00 37.74  ? 139 TYR   B CE1  1 
ATOM   6560 C  CE2  . TYR   B 1 142 ? -44.866 -17.020 -7.775  1.00 41.34  ? 139 TYR   B CE2  1 
ATOM   6561 C  CZ   . TYR   B 1 142 ? -44.016 -17.468 -8.777  1.00 44.61  ? 139 TYR   B CZ   1 
ATOM   6562 O  OH   . TYR   B 1 142 ? -43.678 -18.809 -8.840  1.00 47.38  ? 139 TYR   B OH   1 
ATOM   6563 H  H    . TYR   B 1 142 ? -45.034 -10.870 -8.554  1.00 31.53  ? 139 TYR   B H    1 
ATOM   6564 H  HA   . TYR   B 1 142 ? -44.005 -12.619 -6.947  1.00 35.44  ? 139 TYR   B HA   1 
ATOM   6565 H  HB2  . TYR   B 1 142 ? -45.893 -13.225 -8.057  1.00 32.43  ? 139 TYR   B HB2  1 
ATOM   6566 H  HB3  . TYR   B 1 142 ? -45.211 -12.978 -9.470  1.00 32.43  ? 139 TYR   B HB3  1 
ATOM   6567 H  HD1  . TYR   B 1 142 ? -43.515 -14.650 -10.266 1.00 39.72  ? 139 TYR   B HD1  1 
ATOM   6568 H  HD2  . TYR   B 1 142 ? -45.795 -15.375 -7.054  1.00 44.44  ? 139 TYR   B HD2  1 
ATOM   6569 H  HE1  . TYR   B 1 142 ? -42.936 -16.890 -10.377 1.00 45.33  ? 139 TYR   B HE1  1 
ATOM   6570 H  HE2  . TYR   B 1 142 ? -45.202 -17.617 -7.147  1.00 49.65  ? 139 TYR   B HE2  1 
ATOM   6571 H  HH   . TYR   B 1 142 ? -44.065 -19.232 -8.226  1.00 56.90  ? 139 TYR   B HH   1 
ATOM   6572 N  N    . TRP   B 1 143 ? -42.291 -12.331 -9.663  1.00 23.59  ? 140 TRP   B N    1 
ATOM   6573 C  CA   . TRP   B 1 143 ? -41.041 -12.748 -10.283 1.00 22.48  ? 140 TRP   B CA   1 
ATOM   6574 C  C    . TRP   B 1 143 ? -39.855 -12.006 -9.678  1.00 24.16  ? 140 TRP   B C    1 
ATOM   6575 O  O    . TRP   B 1 143 ? -38.779 -12.585 -9.471  1.00 25.44  ? 140 TRP   B O    1 
ATOM   6576 C  CB   . TRP   B 1 143 ? -41.102 -12.530 -11.813 1.00 21.67  ? 140 TRP   B CB   1 
ATOM   6577 C  CG   . TRP   B 1 143 ? -42.086 -13.478 -12.445 1.00 26.20  ? 140 TRP   B CG   1 
ATOM   6578 C  CD1  . TRP   B 1 143 ? -43.354 -13.203 -12.898 1.00 26.27  ? 140 TRP   B CD1  1 
ATOM   6579 C  CD2  . TRP   B 1 143 ? -41.896 -14.884 -12.635 1.00 27.35  ? 140 TRP   B CD2  1 
ATOM   6580 N  NE1  . TRP   B 1 143 ? -43.954 -14.354 -13.348 1.00 25.60  ? 140 TRP   B NE1  1 
ATOM   6581 C  CE2  . TRP   B 1 143 ? -43.074 -15.396 -13.208 1.00 28.20  ? 140 TRP   B CE2  1 
ATOM   6582 C  CE3  . TRP   B 1 143 ? -40.826 -15.761 -12.381 1.00 29.78  ? 140 TRP   B CE3  1 
ATOM   6583 C  CZ2  . TRP   B 1 143 ? -43.222 -16.749 -13.536 1.00 31.65  ? 140 TRP   B CZ2  1 
ATOM   6584 C  CZ3  . TRP   B 1 143 ? -40.971 -17.102 -12.718 1.00 30.00  ? 140 TRP   B CZ3  1 
ATOM   6585 C  CH2  . TRP   B 1 143 ? -42.166 -17.582 -13.279 1.00 35.28  ? 140 TRP   B CH2  1 
ATOM   6586 H  H    . TRP   B 1 143 ? -42.775 -11.811 -10.146 1.00 28.35  ? 140 TRP   B H    1 
ATOM   6587 H  HA   . TRP   B 1 143 ? -40.914 -13.697 -10.125 1.00 27.02  ? 140 TRP   B HA   1 
ATOM   6588 H  HB2  . TRP   B 1 143 ? -41.385 -11.621 -12.000 1.00 26.05  ? 140 TRP   B HB2  1 
ATOM   6589 H  HB3  . TRP   B 1 143 ? -40.227 -12.691 -12.199 1.00 26.05  ? 140 TRP   B HB3  1 
ATOM   6590 H  HD1  . TRP   B 1 143 ? -43.748 -12.361 -12.899 1.00 31.57  ? 140 TRP   B HD1  1 
ATOM   6591 H  HE1  . TRP   B 1 143 ? -44.751 -14.412 -13.665 1.00 30.76  ? 140 TRP   B HE1  1 
ATOM   6592 H  HE3  . TRP   B 1 143 ? -40.038 -15.450 -11.996 1.00 35.78  ? 140 TRP   B HE3  1 
ATOM   6593 H  HZ2  . TRP   B 1 143 ? -44.008 -17.070 -13.914 1.00 38.03  ? 140 TRP   B HZ2  1 
ATOM   6594 H  HZ3  . TRP   B 1 143 ? -40.266 -17.690 -12.569 1.00 36.04  ? 140 TRP   B HZ3  1 
ATOM   6595 H  HH2  . TRP   B 1 143 ? -42.242 -18.487 -13.480 1.00 42.38  ? 140 TRP   B HH2  1 
ATOM   6596 N  N    . LYS   B 1 144 ? -40.021 -10.711 -9.412  1.00 21.80  ? 141 LYS   B N    1 
ATOM   6597 C  CA   . LYS   B 1 144 ? -38.963 -9.948  -8.763  1.00 24.18  ? 141 LYS   B CA   1 
ATOM   6598 C  C    . LYS   B 1 144 ? -38.636 -10.541 -7.404  1.00 25.26  ? 141 LYS   B C    1 
ATOM   6599 O  O    . LYS   B 1 144 ? -37.460 -10.735 -7.059  1.00 27.46  ? 141 LYS   B O    1 
ATOM   6600 C  CB   . LYS   B 1 144 ? -39.385 -8.482  -8.607  1.00 23.48  ? 141 LYS   B CB   1 
ATOM   6601 C  CG   . LYS   B 1 144 ? -38.311 -7.642  -7.929  1.00 29.14  ? 141 LYS   B CG   1 
ATOM   6602 C  CD   . LYS   B 1 144 ? -38.810 -6.286  -7.480  1.00 32.26  ? 141 LYS   B CD   1 
ATOM   6603 C  CE   . LYS   B 1 144 ? -37.626 -5.419  -7.074  1.00 39.79  ? 141 LYS   B CE   1 
ATOM   6604 N  NZ   . LYS   B 1 144 ? -37.247 -5.746  -5.684  1.00 41.38  ? 141 LYS   B NZ   1 
ATOM   6605 H  H    . LYS   B 1 144 ? -40.728 -10.258 -9.596  1.00 26.20  ? 141 LYS   B H    1 
ATOM   6606 H  HA   . LYS   B 1 144 ? -38.170 -9.978  -9.321  1.00 29.06  ? 141 LYS   B HA   1 
ATOM   6607 H  HB2  . LYS   B 1 144 ? -39.555 -8.105  -9.484  1.00 28.21  ? 141 LYS   B HB2  1 
ATOM   6608 H  HB3  . LYS   B 1 144 ? -40.189 -8.439  -8.066  1.00 28.21  ? 141 LYS   B HB3  1 
ATOM   6609 H  HG2  . LYS   B 1 144 ? -37.989 -8.116  -7.146  1.00 35.00  ? 141 LYS   B HG2  1 
ATOM   6610 H  HG3  . LYS   B 1 144 ? -37.583 -7.500  -8.554  1.00 35.00  ? 141 LYS   B HG3  1 
ATOM   6611 H  HD2  . LYS   B 1 144 ? -39.281 -5.852  -8.208  1.00 38.75  ? 141 LYS   B HD2  1 
ATOM   6612 H  HD3  . LYS   B 1 144 ? -39.400 -6.389  -6.717  1.00 38.75  ? 141 LYS   B HD3  1 
ATOM   6613 H  HE2  . LYS   B 1 144 ? -36.871 -5.595  -7.657  1.00 47.79  ? 141 LYS   B HE2  1 
ATOM   6614 H  HE3  . LYS   B 1 144 ? -37.871 -4.481  -7.122  1.00 47.79  ? 141 LYS   B HE3  1 
ATOM   6615 H  HZ1  . LYS   B 1 144 ? -36.482 -5.342  -5.474  1.00 49.70  ? 141 LYS   B HZ1  1 
ATOM   6616 H  HZ2  . LYS   B 1 144 ? -37.881 -5.472  -5.123  1.00 49.70  ? 141 LYS   B HZ2  1 
ATOM   6617 H  HZ3  . LYS   B 1 144 ? -37.143 -6.625  -5.596  1.00 49.70  ? 141 LYS   B HZ3  1 
ATOM   6618 N  N    . ASP   B 1 145 ? -39.668 -10.839 -6.625  1.00 24.35  ? 142 ASP   B N    1 
ATOM   6619 C  CA   . ASP   B 1 145 ? -39.426 -11.355 -5.290  1.00 26.28  ? 142 ASP   B CA   1 
ATOM   6620 C  C    . ASP   B 1 145 ? -38.822 -12.756 -5.327  1.00 29.59  ? 142 ASP   B C    1 
ATOM   6621 O  O    . ASP   B 1 145 ? -38.042 -13.110 -4.429  1.00 31.66  ? 142 ASP   B O    1 
ATOM   6622 C  CB   . ASP   B 1 145 ? -40.718 -11.357 -4.484  1.00 27.06  ? 142 ASP   B CB   1 
ATOM   6623 C  CG   . ASP   B 1 145 ? -41.116 -9.970  -4.007  1.00 33.38  ? 142 ASP   B CG   1 
ATOM   6624 O  OD1  . ASP   B 1 145 ? -40.369 -8.988  -4.262  1.00 35.18  ? 142 ASP   B OD1  1 
ATOM   6625 O  OD2  . ASP   B 1 145 ? -42.161 -9.869  -3.360  1.00 32.46  ? 142 ASP   B OD2  1 
ATOM   6626 H  H    . ASP   B 1 145 ? -40.496 -10.754 -6.841  1.00 29.27  ? 142 ASP   B H    1 
ATOM   6627 H  HA   . ASP   B 1 145 ? -38.797 -10.768 -4.841  1.00 31.58  ? 142 ASP   B HA   1 
ATOM   6628 H  HB2  . ASP   B 1 145 ? -41.436 -11.701 -5.038  1.00 32.51  ? 142 ASP   B HB2  1 
ATOM   6629 H  HB3  . ASP   B 1 145 ? -40.602 -11.921 -3.703  1.00 32.51  ? 142 ASP   B HB3  1 
ATOM   6630 N  N    . LYS   B 1 146 ? -39.147 -13.560 -6.351  1.00 29.54  ? 143 LYS   B N    1 
ATOM   6631 C  CA   . LYS   B 1 146 ? -38.506 -14.866 -6.487  1.00 29.31  ? 143 LYS   B CA   1 
ATOM   6632 C  C    . LYS   B 1 146 ? -37.023 -14.698 -6.753  1.00 29.18  ? 143 LYS   B C    1 
ATOM   6633 O  O    . LYS   B 1 146 ? -36.189 -15.383 -6.148  1.00 32.26  ? 143 LYS   B O    1 
ATOM   6634 C  CB   . LYS   B 1 146 ? -39.113 -15.666 -7.649  1.00 33.83  ? 143 LYS   B CB   1 
ATOM   6635 C  CG   . LYS   B 1 146 ? -40.430 -16.341 -7.375  1.00 37.99  ? 143 LYS   B CG   1 
ATOM   6636 C  CD   . LYS   B 1 146 ? -40.305 -17.530 -6.464  1.00 43.93  ? 143 LYS   B CD   1 
ATOM   6637 C  CE   . LYS   B 1 146 ? -41.599 -18.341 -6.494  1.00 55.61  ? 143 LYS   B CE   1 
ATOM   6638 N  NZ   . LYS   B 1 146 ? -41.624 -19.467 -5.524  1.00 71.68  ? 143 LYS   B NZ   1 
ATOM   6639 H  H    . LYS   B 1 146 ? -39.722 -13.374 -6.963  1.00 35.49  ? 143 LYS   B H    1 
ATOM   6640 H  HA   . LYS   B 1 146 ? -38.655 -15.355 -5.663  1.00 35.22  ? 143 LYS   B HA   1 
ATOM   6641 H  HB2  . LYS   B 1 146 ? -39.252 -15.060 -8.393  1.00 40.63  ? 143 LYS   B HB2  1 
ATOM   6642 H  HB3  . LYS   B 1 146 ? -38.483 -16.360 -7.899  1.00 40.63  ? 143 LYS   B HB3  1 
ATOM   6643 H  HG2  . LYS   B 1 146 ? -41.028 -15.704 -6.954  1.00 45.63  ? 143 LYS   B HG2  1 
ATOM   6644 H  HG3  . LYS   B 1 146 ? -40.808 -16.646 -8.214  1.00 45.63  ? 143 LYS   B HG3  1 
ATOM   6645 H  HD2  . LYS   B 1 146 ? -39.575 -18.095 -6.762  1.00 52.76  ? 143 LYS   B HD2  1 
ATOM   6646 H  HD3  . LYS   B 1 146 ? -40.144 -17.231 -5.556  1.00 52.76  ? 143 LYS   B HD3  1 
ATOM   6647 H  HE2  . LYS   B 1 146 ? -42.341 -17.753 -6.282  1.00 66.77  ? 143 LYS   B HE2  1 
ATOM   6648 H  HE3  . LYS   B 1 146 ? -41.714 -18.714 -7.382  1.00 66.77  ? 143 LYS   B HE3  1 
ATOM   6649 H  HZ1  . LYS   B 1 146 ? -42.367 -19.945 -5.631  1.00 86.06  ? 143 LYS   B HZ1  1 
ATOM   6650 H  HZ2  . LYS   B 1 146 ? -40.920 -19.995 -5.652  1.00 86.06  ? 143 LYS   B HZ2  1 
ATOM   6651 H  HZ3  . LYS   B 1 146 ? -41.601 -19.152 -4.692  1.00 86.06  ? 143 LYS   B HZ3  1 
ATOM   6652 N  N    . ASN   B 1 147 ? -36.681 -13.823 -7.705  1.00 27.44  ? 144 ASN   B N    1 
ATOM   6653 C  CA   . ASN   B 1 147 ? -35.280 -13.586 -8.035  1.00 27.34  ? 144 ASN   B CA   1 
ATOM   6654 C  C    . ASN   B 1 147 ? -34.509 -13.138 -6.803  1.00 26.14  ? 144 ASN   B C    1 
ATOM   6655 O  O    . ASN   B 1 147 ? -33.425 -13.650 -6.505  1.00 28.98  ? 144 ASN   B O    1 
ATOM   6656 C  CB   . ASN   B 1 147 ? -35.142 -12.508 -9.111  1.00 25.29  ? 144 ASN   B CB   1 
ATOM   6657 C  CG   . ASN   B 1 147 ? -35.513 -12.996 -10.487 1.00 26.69  ? 144 ASN   B CG   1 
ATOM   6658 O  OD1  . ASN   B 1 147 ? -35.505 -14.194 -10.759 1.00 29.04  ? 144 ASN   B OD1  1 
ATOM   6659 N  ND2  . ASN   B 1 147 ? -35.847 -12.058 -11.364 1.00 26.32  ? 144 ASN   B ND2  1 
ATOM   6660 H  H    . ASN   B 1 147 ? -37.238 -13.360 -8.168  1.00 32.97  ? 144 ASN   B H    1 
ATOM   6661 H  HA   . ASN   B 1 147 ? -34.915 -14.416 -8.379  1.00 32.85  ? 144 ASN   B HA   1 
ATOM   6662 H  HB2  . ASN   B 1 147 ? -35.725 -11.766 -8.890  1.00 30.38  ? 144 ASN   B HB2  1 
ATOM   6663 H  HB3  . ASN   B 1 147 ? -34.219 -12.209 -9.140  1.00 30.38  ? 144 ASN   B HB3  1 
ATOM   6664 H  HD21 . ASN   B 1 147 ? -36.069 -12.278 -12.166 1.00 31.62  ? 144 ASN   B HD21 1 
ATOM   6665 H  HD22 . ASN   B 1 147 ? -35.843 -11.230 -11.131 1.00 31.62  ? 144 ASN   B HD22 1 
ATOM   6666 N  N    . ASP   B 1 148 ? -35.068 -12.165 -6.064  1.00 27.06  ? 145 ASP   B N    1 
ATOM   6667 C  CA   . ASP   B 1 148 ? -34.399 -11.676 -4.870  1.00 28.37  ? 145 ASP   B CA   1 
ATOM   6668 C  C    . ASP   B 1 148 ? -34.236 -12.784 -3.836  1.00 26.77  ? 145 ASP   B C    1 
ATOM   6669 O  O    . ASP   B 1 148 ? -33.231 -12.832 -3.117  1.00 29.73  ? 145 ASP   B O    1 
ATOM   6670 C  CB   . ASP   B 1 148 ? -35.173 -10.512 -4.244  1.00 30.81  ? 145 ASP   B CB   1 
ATOM   6671 C  CG   . ASP   B 1 148 ? -35.274 -9.283  -5.148  1.00 37.62  ? 145 ASP   B CG   1 
ATOM   6672 O  OD1  . ASP   B 1 148 ? -34.540 -9.178  -6.154  1.00 34.83  ? 145 ASP   B OD1  1 
ATOM   6673 O  OD2  . ASP   B 1 148 ? -36.076 -8.382  -4.807  1.00 33.09  ? 145 ASP   B OD2  1 
ATOM   6674 H  H    . ASP   B 1 148 ? -35.820 -11.785 -6.237  1.00 32.51  ? 145 ASP   B H    1 
ATOM   6675 H  HA   . ASP   B 1 148 ? -33.524 -11.352 -5.135  1.00 34.09  ? 145 ASP   B HA   1 
ATOM   6676 H  HB2  . ASP   B 1 148 ? -36.075 -10.807 -4.045  1.00 37.02  ? 145 ASP   B HB2  1 
ATOM   6677 H  HB3  . ASP   B 1 148 ? -34.724 -10.242 -3.428  1.00 37.02  ? 145 ASP   B HB3  1 
ATOM   6678 N  N    . ASP   B 1 149 ? -35.241 -13.651 -3.715  1.00 29.01  ? 146 ASP   B N    1 
ATOM   6679 C  CA   . ASP   B 1 149 ? -35.201 -14.715 -2.723  1.00 28.31  ? 146 ASP   B CA   1 
ATOM   6680 C  C    . ASP   B 1 149 ? -34.148 -15.766 -3.078  1.00 33.88  ? 146 ASP   B C    1 
ATOM   6681 O  O    . ASP   B 1 149 ? -33.375 -16.191 -2.214  1.00 35.16  ? 146 ASP   B O    1 
ATOM   6682 C  CB   . ASP   B 1 149 ? -36.596 -15.330 -2.557  1.00 35.18  ? 146 ASP   B CB   1 
ATOM   6683 C  CG   . ASP   B 1 149 ? -37.580 -14.411 -1.787  1.00 45.36  ? 146 ASP   B CG   1 
ATOM   6684 O  OD1  . ASP   B 1 149 ? -37.138 -13.459 -1.093  1.00 47.92  ? 146 ASP   B OD1  1 
ATOM   6685 O  OD2  . ASP   B 1 149 ? -38.812 -14.657 -1.831  1.00 49.77  ? 146 ASP   B OD2  1 
ATOM   6686 H  H    . ASP   B 1 149 ? -35.955 -13.642 -4.194  1.00 34.86  ? 146 ASP   B H    1 
ATOM   6687 H  HA   . ASP   B 1 149 ? -34.948 -14.342 -1.864  1.00 33.76  ? 146 ASP   B HA   1 
ATOM   6688 H  HB2  . ASP   B 1 149 ? -36.971 -15.499 -3.436  1.00 42.25  ? 146 ASP   B HB2  1 
ATOM   6689 H  HB3  . ASP   B 1 149 ? -36.517 -16.162 -2.065  1.00 42.25  ? 146 ASP   B HB3  1 
ATOM   6690 N  N    . ILE   B 1 150 ? -34.085 -16.195 -4.343  1.00 34.14  ? 147 ILE   B N    1 
ATOM   6691 C  CA   . ILE   B 1 150 ? -33.082 -17.195 -4.719  1.00 39.84  ? 147 ILE   B CA   1 
ATOM   6692 C  C    . ILE   B 1 150 ? -31.667 -16.641 -4.554  1.00 35.12  ? 147 ILE   B C    1 
ATOM   6693 O  O    . ILE   B 1 150 ? -30.769 -17.329 -4.049  1.00 37.93  ? 147 ILE   B O    1 
ATOM   6694 C  CB   . ILE   B 1 150 ? -33.331 -17.709 -6.155  1.00 40.00  ? 147 ILE   B CB   1 
ATOM   6695 C  CG1  . ILE   B 1 150 ? -34.553 -18.630 -6.198  1.00 41.69  ? 147 ILE   B CG1  1 
ATOM   6696 C  CG2  . ILE   B 1 150 ? -32.110 -18.461 -6.676  1.00 47.80  ? 147 ILE   B CG2  1 
ATOM   6697 C  CD1  . ILE   B 1 150 ? -35.608 -18.280 -7.219  1.00 51.21  ? 147 ILE   B CD1  1 
ATOM   6698 H  H    . ILE   B 1 150 ? -34.596 -15.931 -4.983  1.00 41.01  ? 147 ILE   B H    1 
ATOM   6699 H  HA   . ILE   B 1 150 ? -33.174 -17.949 -4.116  1.00 47.86  ? 147 ILE   B HA   1 
ATOM   6700 H  HB   . ILE   B 1 150 ? -33.497 -16.937 -6.719  1.00 48.05  ? 147 ILE   B HB   1 
ATOM   6701 H  HG12 . ILE   B 1 150 ? -34.248 -19.529 -6.397  1.00 50.07  ? 147 ILE   B HG12 1 
ATOM   6702 H  HG13 . ILE   B 1 150 ? -34.979 -18.609 -5.327  1.00 50.07  ? 147 ILE   B HG13 1 
ATOM   6703 H  HG21 . ILE   B 1 150 ? -32.291 -18.773 -7.577  1.00 57.40  ? 147 ILE   B HG21 1 
ATOM   6704 H  HG22 . ILE   B 1 150 ? -31.347 -17.861 -6.681  1.00 57.40  ? 147 ILE   B HG22 1 
ATOM   6705 H  HG23 . ILE   B 1 150 ? -31.932 -19.217 -6.095  1.00 57.40  ? 147 ILE   B HG23 1 
ATOM   6706 H  HD11 . ILE   B 1 150 ? -36.331 -18.924 -7.160  1.00 61.49  ? 147 ILE   B HD11 1 
ATOM   6707 H  HD12 . ILE   B 1 150 ? -35.943 -17.389 -7.035  1.00 61.49  ? 147 ILE   B HD12 1 
ATOM   6708 H  HD13 . ILE   B 1 150 ? -35.212 -18.309 -8.105  1.00 61.49  ? 147 ILE   B HD13 1 
ATOM   6709 N  N    . VAL   B 1 151 ? -31.426 -15.403 -4.997  1.00 31.06  ? 148 VAL   B N    1 
ATOM   6710 C  CA   . VAL   B 1 151 ? -30.106 -14.807 -4.809  1.00 33.44  ? 148 VAL   B CA   1 
ATOM   6711 C  C    . VAL   B 1 151 ? -29.745 -14.738 -3.324  1.00 33.65  ? 148 VAL   B C    1 
ATOM   6712 O  O    . VAL   B 1 151 ? -28.660 -15.155 -2.906  1.00 38.36  ? 148 VAL   B O    1 
ATOM   6713 C  CB   . VAL   B 1 151 ? -30.037 -13.417 -5.467  1.00 32.66  ? 148 VAL   B CB   1 
ATOM   6714 C  CG1  . VAL   B 1 151 ? -28.741 -12.735 -5.103  1.00 39.08  ? 148 VAL   B CG1  1 
ATOM   6715 C  CG2  . VAL   B 1 151 ? -30.168 -13.545 -6.958  1.00 32.64  ? 148 VAL   B CG2  1 
ATOM   6716 H  H    . VAL   B 1 151 ? -31.997 -14.901 -5.399  1.00 37.31  ? 148 VAL   B H    1 
ATOM   6717 H  HA   . VAL   B 1 151 ? -29.456 -15.379 -5.245  1.00 40.17  ? 148 VAL   B HA   1 
ATOM   6718 H  HB   . VAL   B 1 151 ? -30.770 -12.871 -5.144  1.00 39.24  ? 148 VAL   B HB   1 
ATOM   6719 H  HG11 . VAL   B 1 151 ? -28.597 -11.989 -5.706  1.00 46.94  ? 148 VAL   B HG11 1 
ATOM   6720 H  HG12 . VAL   B 1 151 ? -28.798 -12.416 -4.189  1.00 46.94  ? 148 VAL   B HG12 1 
ATOM   6721 H  HG13 . VAL   B 1 151 ? -28.015 -13.372 -5.187  1.00 46.94  ? 148 VAL   B HG13 1 
ATOM   6722 H  HG21 . VAL   B 1 151 ? -30.129 -12.661 -7.355  1.00 39.21  ? 148 VAL   B HG21 1 
ATOM   6723 H  HG22 . VAL   B 1 151 ? -29.440 -14.091 -7.293  1.00 39.21  ? 148 VAL   B HG22 1 
ATOM   6724 H  HG23 . VAL   B 1 151 ? -31.018 -13.963 -7.165  1.00 39.21  ? 148 VAL   B HG23 1 
ATOM   6725 N  N    . HIS   B 1 152 ? -30.647 -14.203 -2.502  1.00 35.41  ? 149 HIS   B N    1 
ATOM   6726 C  CA   . HIS   B 1 152 ? -30.399 -14.144 -1.064  1.00 36.22  ? 149 HIS   B CA   1 
ATOM   6727 C  C    . HIS   B 1 152 ? -30.099 -15.532 -0.491  1.00 35.98  ? 149 HIS   B C    1 
ATOM   6728 O  O    . HIS   B 1 152 ? -29.184 -15.693 0.324   1.00 40.85  ? 149 HIS   B O    1 
ATOM   6729 C  CB   . HIS   B 1 152 ? -31.608 -13.531 -0.350  1.00 34.37  ? 149 HIS   B CB   1 
ATOM   6730 C  CG   . HIS   B 1 152 ? -31.345 -13.120 1.075   1.00 40.97  ? 149 HIS   B CG   1 
ATOM   6731 N  ND1  . HIS   B 1 152 ? -30.612 -12.001 1.407   1.00 46.70  ? 149 HIS   B ND1  1 
ATOM   6732 C  CD2  . HIS   B 1 152 ? -31.730 -13.674 2.253   1.00 40.10  ? 149 HIS   B CD2  1 
ATOM   6733 C  CE1  . HIS   B 1 152 ? -30.567 -11.877 2.726   1.00 44.90  ? 149 HIS   B CE1  1 
ATOM   6734 N  NE2  . HIS   B 1 152 ? -31.227 -12.886 3.269   1.00 41.13  ? 149 HIS   B NE2  1 
ATOM   6735 H  H    . HIS   B 1 152 ? -31.402 -13.872 -2.748  1.00 42.53  ? 149 HIS   B H    1 
ATOM   6736 H  HA   . HIS   B 1 152 ? -29.626 -13.579 -0.907  1.00 43.50  ? 149 HIS   B HA   1 
ATOM   6737 H  HB2  . HIS   B 1 152 ? -31.887 -12.740 -0.838  1.00 41.28  ? 149 HIS   B HB2  1 
ATOM   6738 H  HB3  . HIS   B 1 152 ? -32.326 -14.184 -0.340  1.00 41.28  ? 149 HIS   B HB3  1 
ATOM   6739 H  HD2  . HIS   B 1 152 ? -32.240 -14.445 2.358   1.00 48.16  ? 149 HIS   B HD2  1 
ATOM   6740 H  HE1  . HIS   B 1 152 ? -30.142 -11.194 3.192   1.00 53.92  ? 149 HIS   B HE1  1 
ATOM   6741 N  N    . GLN   B 1 153 ? -30.881 -16.537 -0.898  1.00 37.08  ? 150 GLN   B N    1 
ATOM   6742 C  CA   . GLN   B 1 153 ? -30.672 -17.918 -0.450  1.00 38.43  ? 150 GLN   B CA   1 
ATOM   6743 C  C    . GLN   B 1 153 ? -29.266 -18.417 -0.771  1.00 38.17  ? 150 GLN   B C    1 
ATOM   6744 O  O    . GLN   B 1 153 ? -28.576 -18.971 0.095   1.00 40.63  ? 150 GLN   B O    1 
ATOM   6745 C  CB   . GLN   B 1 153 ? -31.731 -18.791 -1.122  1.00 45.19  ? 150 GLN   B CB   1 
ATOM   6746 C  CG   . GLN   B 1 153 ? -31.841 -20.211 -0.662  1.00 53.43  ? 150 GLN   B CG   1 
ATOM   6747 C  CD   . GLN   B 1 153 ? -32.324 -21.115 -1.789  1.00 71.42  ? 150 GLN   B CD   1 
ATOM   6748 O  OE1  . GLN   B 1 153 ? -31.589 -21.988 -2.264  1.00 61.87  ? 150 GLN   B OE1  1 
ATOM   6749 N  NE2  . GLN   B 1 153 ? -33.559 -20.890 -2.240  1.00 65.28  ? 150 GLN   B NE2  1 
ATOM   6750 H  H    . GLN   B 1 153 ? -31.544 -16.447 -1.438  1.00 44.54  ? 150 GLN   B H    1 
ATOM   6751 H  HA   . GLN   B 1 153 ? -30.769 -17.971 0.514   1.00 46.16  ? 150 GLN   B HA   1 
ATOM   6752 H  HB2  . GLN   B 1 153 ? -32.596 -18.380 -0.971  1.00 54.27  ? 150 GLN   B HB2  1 
ATOM   6753 H  HB3  . GLN   B 1 153 ? -31.537 -18.817 -2.072  1.00 54.27  ? 150 GLN   B HB3  1 
ATOM   6754 H  HG2  . GLN   B 1 153 ? -30.970 -20.523 -0.370  1.00 64.16  ? 150 GLN   B HG2  1 
ATOM   6755 H  HG3  . GLN   B 1 153 ? -32.475 -20.265 0.069   1.00 64.16  ? 150 GLN   B HG3  1 
ATOM   6756 H  HE21 . GLN   B 1 153 ? -34.035 -20.262 -1.897  1.00 78.38  ? 150 GLN   B HE21 1 
ATOM   6757 H  HE22 . GLN   B 1 153 ? -33.879 -21.374 -2.876  1.00 78.38  ? 150 GLN   B HE22 1 
ATOM   6758 N  N    . ILE   B 1 154 ? -28.826 -18.241 -2.021  1.00 45.82  ? 151 ILE   B N    1 
ATOM   6759 C  CA   . ILE   B 1 154 ? -27.512 -18.743 -2.418  1.00 44.03  ? 151 ILE   B CA   1 
ATOM   6760 C  C    . ILE   B 1 154 ? -26.420 -17.969 -1.703  1.00 43.30  ? 151 ILE   B C    1 
ATOM   6761 O  O    . ILE   B 1 154 ? -25.478 -18.541 -1.150  1.00 46.57  ? 151 ILE   B O    1 
ATOM   6762 C  CB   . ILE   B 1 154 ? -27.332 -18.645 -3.943  1.00 40.58  ? 151 ILE   B CB   1 
ATOM   6763 C  CG1  . ILE   B 1 154 ? -28.350 -19.524 -4.655  1.00 43.42  ? 151 ILE   B CG1  1 
ATOM   6764 C  CG2  . ILE   B 1 154 ? -25.902 -19.017 -4.329  1.00 50.90  ? 151 ILE   B CG2  1 
ATOM   6765 C  CD1  . ILE   B 1 154 ? -28.166 -19.553 -6.160  1.00 53.85  ? 151 ILE   B CD1  1 
ATOM   6766 H  H    . ILE   B 1 154 ? -29.262 -17.842 -2.645  1.00 55.03  ? 151 ILE   B H    1 
ATOM   6767 H  HA   . ILE   B 1 154 ? -27.454 -19.677 -2.162  1.00 52.88  ? 151 ILE   B HA   1 
ATOM   6768 H  HB   . ILE   B 1 154 ? -27.489 -17.729 -4.220  1.00 48.74  ? 151 ILE   B HB   1 
ATOM   6769 H  HG12 . ILE   B 1 154 ? -28.264 -20.432 -4.326  1.00 52.15  ? 151 ILE   B HG12 1 
ATOM   6770 H  HG13 . ILE   B 1 154 ? -29.240 -19.186 -4.470  1.00 52.15  ? 151 ILE   B HG13 1 
ATOM   6771 H  HG21 . ILE   B 1 154 ? -25.808 -18.950 -5.292  1.00 61.12  ? 151 ILE   B HG21 1 
ATOM   6772 H  HG22 . ILE   B 1 154 ? -25.288 -18.406 -3.893  1.00 61.12  ? 151 ILE   B HG22 1 
ATOM   6773 H  HG23 . ILE   B 1 154 ? -25.724 -19.926 -4.041  1.00 61.12  ? 151 ILE   B HG23 1 
ATOM   6774 H  HD11 . ILE   B 1 154 ? -28.863 -20.101 -6.553  1.00 64.66  ? 151 ILE   B HD11 1 
ATOM   6775 H  HD12 . ILE   B 1 154 ? -28.223 -18.648 -6.503  1.00 64.66  ? 151 ILE   B HD12 1 
ATOM   6776 H  HD13 . ILE   B 1 154 ? -27.295 -19.929 -6.365  1.00 64.66  ? 151 ILE   B HD13 1 
ATOM   6777 N  N    . LEU   B 1 155 ? -26.504 -16.651 -1.750  1.00 42.32  ? 152 LEU   B N    1 
ATOM   6778 C  CA   . LEU   B 1 155 ? -25.622 -15.793 -0.985  1.00 46.94  ? 152 LEU   B CA   1 
ATOM   6779 C  C    . LEU   B 1 155 ? -26.111 -15.855 0.463   1.00 53.98  ? 152 LEU   B C    1 
ATOM   6780 O  O    . LEU   B 1 155 ? -26.727 -16.848 0.871   1.00 59.16  ? 152 LEU   B O    1 
ATOM   6781 C  CB   . LEU   B 1 155 ? -25.628 -14.391 -1.575  1.00 49.59  ? 152 LEU   B CB   1 
ATOM   6782 C  CG   . LEU   B 1 155 ? -25.544 -14.338 -3.107  1.00 51.14  ? 152 LEU   B CG   1 
ATOM   6783 C  CD1  . LEU   B 1 155 ? -25.387 -12.881 -3.576  1.00 52.41  ? 152 LEU   B CD1  1 
ATOM   6784 C  CD2  . LEU   B 1 155 ? -24.453 -15.200 -3.728  1.00 56.00  ? 152 LEU   B CD2  1 
ATOM   6785 H  H    . LEU   B 1 155 ? -27.075 -16.220 -2.228  1.00 50.82  ? 152 LEU   B H    1 
ATOM   6786 H  HA   . LEU   B 1 155 ? -24.692 -16.069 -1.010  1.00 56.37  ? 152 LEU   B HA   1 
ATOM   6787 H  HB2  . LEU   B 1 155 ? -26.451 -13.950 -1.312  1.00 59.55  ? 152 LEU   B HB2  1 
ATOM   6788 H  HB3  . LEU   B 1 155 ? -24.865 -13.906 -1.224  1.00 59.55  ? 152 LEU   B HB3  1 
ATOM   6789 H  HG   . LEU   B 1 155 ? -26.377 -14.715 -3.428  1.00 61.41  ? 152 LEU   B HG   1 
ATOM   6790 H  HD11 . LEU   B 1 155 ? -25.348 -12.864 -4.545  1.00 62.93  ? 152 LEU   B HD11 1 
ATOM   6791 H  HD12 . LEU   B 1 155 ? -26.148 -12.366 -3.266  1.00 62.93  ? 152 LEU   B HD12 1 
ATOM   6792 H  HD13 . LEU   B 1 155 ? -24.568 -12.517 -3.206  1.00 62.93  ? 152 LEU   B HD13 1 
ATOM   6793 H  HD21 . LEU   B 1 155 ? -24.460 -15.073 -4.690  1.00 67.24  ? 152 LEU   B HD21 1 
ATOM   6794 H  HD22 . LEU   B 1 155 ? -23.594 -14.931 -3.366  1.00 67.24  ? 152 LEU   B HD22 1 
ATOM   6795 H  HD23 . LEU   B 1 155 ? -24.625 -16.130 -3.515  1.00 67.24  ? 152 LEU   B HD23 1 
ATOM   6796 N  N    . THR   B 1 156 ? -25.864 -14.798 1.226   1.00 66.59  ? 153 THR   B N    1 
ATOM   6797 C  CA   . THR   B 1 156 ? -26.176 -14.692 2.646   1.00 63.16  ? 153 THR   B CA   1 
ATOM   6798 C  C    . THR   B 1 156 ? -26.542 -15.963 3.408   1.00 57.99  ? 153 THR   B C    1 
ATOM   6799 O  O    . THR   B 1 156 ? -25.895 -16.270 4.415   1.00 54.52  ? 153 THR   B O    1 
ATOM   6800 C  CB   . THR   B 1 156 ? -27.323 -13.678 2.835   1.00 48.52  ? 153 THR   B CB   1 
ATOM   6801 O  OG1  . THR   B 1 156 ? -28.587 -14.347 2.696   1.00 55.06  ? 153 THR   B OG1  1 
ATOM   6802 C  CG2  . THR   B 1 156 ? -27.205 -12.547 1.815   1.00 63.13  ? 153 THR   B CG2  1 
ATOM   6803 H  H    . THR   B 1 156 ? -25.491 -14.082 0.927   1.00 79.95  ? 153 THR   B H    1 
ATOM   6804 H  HA   . THR   B 1 156 ? -25.337 -14.416 3.047   1.00 75.84  ? 153 THR   B HA   1 
ATOM   6805 H  HB   . THR   B 1 156 ? -27.275 -13.286 3.721   1.00 58.27  ? 153 THR   B HB   1 
ATOM   6806 H  HG1  . THR   B 1 156 ? -28.914 -14.505 3.453   1.00 66.11  ? 153 THR   B HG1  1 
ATOM   6807 H  HG21 . THR   B 1 156 ? -27.774 -11.805 2.075   1.00 75.80  ? 153 THR   B HG21 1 
ATOM   6808 H  HG22 . THR   B 1 156 ? -26.287 -12.238 1.767   1.00 75.80  ? 153 THR   B HG22 1 
ATOM   6809 H  HG23 . THR   B 1 156 ? -27.478 -12.861 0.939   1.00 75.80  ? 153 THR   B HG23 1 
ATOM   6810 N  N    . GLU   B 1 157 ? -27.558 -16.705 2.980   1.00 46.59  ? 154 GLU   B N    1 
ATOM   6811 C  CA   . GLU   B 1 157 ? -28.142 -17.699 3.882   1.00 56.66  ? 154 GLU   B CA   1 
ATOM   6812 C  C    . GLU   B 1 157 ? -27.296 -18.967 3.979   1.00 55.59  ? 154 GLU   B C    1 
ATOM   6813 O  O    . GLU   B 1 157 ? -27.090 -19.488 5.081   1.00 47.39  ? 154 GLU   B O    1 
ATOM   6814 C  CB   . GLU   B 1 157 ? -29.587 -18.048 3.485   1.00 57.47  ? 154 GLU   B CB   1 
ATOM   6815 C  CG   . GLU   B 1 157 ? -30.632 -16.998 3.902   1.00 58.00  ? 154 GLU   B CG   1 
ATOM   6816 C  CD   . GLU   B 1 157 ? -32.072 -17.386 3.559   1.00 64.64  ? 154 GLU   B CD   1 
ATOM   6817 O  OE1  . GLU   B 1 157 ? -32.283 -18.440 2.916   1.00 65.88  ? 154 GLU   B OE1  1 
ATOM   6818 O  OE2  . GLU   B 1 157 ? -32.997 -16.634 3.949   1.00 67.71  ? 154 GLU   B OE2  1 
ATOM   6819 H  H    . GLU   B 1 157 ? -27.917 -16.657 2.200   1.00 55.95  ? 154 GLU   B H    1 
ATOM   6820 H  HA   . GLU   B 1 157 ? -28.174 -17.294 4.762   1.00 68.04  ? 154 GLU   B HA   1 
ATOM   6821 H  HB2  . GLU   B 1 157 ? -29.630 -18.138 2.520   1.00 69.01  ? 154 GLU   B HB2  1 
ATOM   6822 H  HB3  . GLU   B 1 157 ? -29.830 -18.887 3.907   1.00 69.01  ? 154 GLU   B HB3  1 
ATOM   6823 H  HG2  . GLU   B 1 157 ? -30.581 -16.871 4.862   1.00 69.64  ? 154 GLU   B HG2  1 
ATOM   6824 H  HG3  . GLU   B 1 157 ? -30.434 -16.164 3.446   1.00 69.64  ? 154 GLU   B HG3  1 
ATOM   6825 N  N    . GLY   B 1 158 ? -26.821 -19.506 2.852   1.00 56.42  ? 155 GLY   B N    1 
ATOM   6826 C  CA   . GLY   B 1 158 ? -25.931 -20.659 2.926   1.00 48.16  ? 155 GLY   B CA   1 
ATOM   6827 C  C    . GLY   B 1 158 ? -24.665 -20.360 3.709   1.00 50.80  ? 155 GLY   B C    1 
ATOM   6828 O  O    . GLY   B 1 158 ? -24.111 -21.234 4.391   1.00 42.74  ? 155 GLY   B O    1 
ATOM   6829 H  H    . GLY   B 1 158 ? -26.995 -19.229 2.057   1.00 67.74  ? 155 GLY   B H    1 
ATOM   6830 H  HA2  . GLY   B 1 158 ? -26.392 -21.394 3.359   1.00 57.83  ? 155 GLY   B HA2  1 
ATOM   6831 H  HA3  . GLY   B 1 158 ? -25.679 -20.929 2.029   1.00 57.83  ? 155 GLY   B HA3  1 
ATOM   6832 N  N    . LEU   B 1 159 ? -24.185 -19.127 3.619   1.00 49.14  ? 156 LEU   B N    1 
ATOM   6833 C  CA   . LEU   B 1 159 ? -23.097 -18.689 4.472   1.00 47.28  ? 156 LEU   B CA   1 
ATOM   6834 C  C    . LEU   B 1 159 ? -23.507 -18.714 5.939   1.00 44.79  ? 156 LEU   B C    1 
ATOM   6835 O  O    . LEU   B 1 159 ? -22.703 -19.081 6.806   1.00 42.48  ? 156 LEU   B O    1 
ATOM   6836 C  CB   . LEU   B 1 159 ? -22.681 -17.296 4.040   1.00 50.81  ? 156 LEU   B CB   1 
ATOM   6837 C  CG   . LEU   B 1 159 ? -21.602 -16.596 4.829   1.00 53.12  ? 156 LEU   B CG   1 
ATOM   6838 C  CD1  . LEU   B 1 159 ? -20.289 -17.306 4.563   1.00 49.21  ? 156 LEU   B CD1  1 
ATOM   6839 C  CD2  . LEU   B 1 159 ? -21.603 -15.146 4.371   1.00 54.04  ? 156 LEU   B CD2  1 
ATOM   6840 H  H    . LEU   B 1 159 ? -24.472 -18.527 3.073   1.00 59.01  ? 156 LEU   B H    1 
ATOM   6841 H  HA   . LEU   B 1 159 ? -22.336 -19.284 4.378   1.00 56.78  ? 156 LEU   B HA   1 
ATOM   6842 H  HB2  . LEU   B 1 159 ? -22.362 -17.355 3.126   1.00 61.01  ? 156 LEU   B HB2  1 
ATOM   6843 H  HB3  . LEU   B 1 159 ? -23.467 -16.729 4.082   1.00 61.01  ? 156 LEU   B HB3  1 
ATOM   6844 H  HG   . LEU   B 1 159 ? -21.738 -16.613 5.790   1.00 63.78  ? 156 LEU   B HG   1 
ATOM   6845 H  HD11 . LEU   B 1 159 ? -19.615 -16.962 5.170   1.00 59.10  ? 156 LEU   B HD11 1 
ATOM   6846 H  HD12 . LEU   B 1 159 ? -20.409 -18.257 4.706   1.00 59.10  ? 156 LEU   B HD12 1 
ATOM   6847 H  HD13 . LEU   B 1 159 ? -20.022 -17.140 3.645   1.00 59.10  ? 156 LEU   B HD13 1 
ATOM   6848 H  HD21 . LEU   B 1 159 ? -20.944 -14.652 4.884   1.00 64.89  ? 156 LEU   B HD21 1 
ATOM   6849 H  HD22 . LEU   B 1 159 ? -21.380 -15.113 3.427   1.00 64.89  ? 156 LEU   B HD22 1 
ATOM   6850 H  HD23 . LEU   B 1 159 ? -22.485 -14.769 4.515   1.00 64.89  ? 156 LEU   B HD23 1 
ATOM   6851 N  N    . GLU   B 1 160 ? -24.748 -18.326 6.236   1.00 43.04  ? 157 GLU   B N    1 
ATOM   6852 C  CA   . GLU   B 1 160 ? -25.196 -18.266 7.627   1.00 47.03  ? 157 GLU   B CA   1 
ATOM   6853 C  C    . GLU   B 1 160 ? -25.164 -19.641 8.271   1.00 44.84  ? 157 GLU   B C    1 
ATOM   6854 O  O    . GLU   B 1 160 ? -24.730 -19.792 9.423   1.00 44.79  ? 157 GLU   B O    1 
ATOM   6855 C  CB   . GLU   B 1 160 ? -26.609 -17.687 7.701   1.00 51.09  ? 157 GLU   B CB   1 
ATOM   6856 C  CG   . GLU   B 1 160 ? -26.660 -16.177 7.603   1.00 56.16  ? 157 GLU   B CG   1 
ATOM   6857 C  CD   . GLU   B 1 160 ? -28.068 -15.651 7.320   1.00 56.97  ? 157 GLU   B CD   1 
ATOM   6858 O  OE1  . GLU   B 1 160 ? -29.030 -16.453 7.283   1.00 62.48  ? 157 GLU   B OE1  1 
ATOM   6859 O  OE2  . GLU   B 1 160 ? -28.201 -14.421 7.140   1.00 66.58  ? 157 GLU   B OE2  1 
ATOM   6860 H  H    . GLU   B 1 160 ? -25.343 -18.095 5.659   1.00 51.69  ? 157 GLU   B H    1 
ATOM   6861 H  HA   . GLU   B 1 160 ? -24.600 -17.681 8.119   1.00 56.47  ? 157 GLU   B HA   1 
ATOM   6862 H  HB2  . GLU   B 1 160 ? -27.132 -18.049 6.968   1.00 61.36  ? 157 GLU   B HB2  1 
ATOM   6863 H  HB3  . GLU   B 1 160 ? -27.006 -17.942 8.548   1.00 61.36  ? 157 GLU   B HB3  1 
ATOM   6864 H  HG2  . GLU   B 1 160 ? -26.360 -15.796 8.443   1.00 67.44  ? 157 GLU   B HG2  1 
ATOM   6865 H  HG3  . GLU   B 1 160 ? -26.080 -15.887 6.881   1.00 67.44  ? 157 GLU   B HG3  1 
ATOM   6866 N  N    . LYS   B 1 161 ? -25.607 -20.659 7.535   1.00 44.54  ? 158 LYS   B N    1 
ATOM   6867 C  CA   . LYS   B 1 161 ? -25.677 -22.004 8.093   1.00 37.73  ? 158 LYS   B CA   1 
ATOM   6868 C  C    . LYS   B 1 161 ? -24.283 -22.588 8.271   1.00 47.29  ? 158 LYS   B C    1 
ATOM   6869 O  O    . LYS   B 1 161 ? -23.982 -23.195 9.305   1.00 42.34  ? 158 LYS   B O    1 
ATOM   6870 C  CB   . LYS   B 1 161 ? -26.548 -22.869 7.193   1.00 57.11  ? 158 LYS   B CB   1 
ATOM   6871 C  CG   . LYS   B 1 161 ? -26.414 -24.358 7.395   1.00 67.73  ? 158 LYS   B CG   1 
ATOM   6872 C  CD   . LYS   B 1 161 ? -25.397 -24.997 6.482   1.00 63.46  ? 158 LYS   B CD   1 
ATOM   6873 C  CE   . LYS   B 1 161 ? -25.278 -26.481 6.817   1.00 69.93  ? 158 LYS   B CE   1 
ATOM   6874 N  NZ   . LYS   B 1 161 ? -24.334 -26.701 7.953   1.00 61.54  ? 158 LYS   B NZ   1 
ATOM   6875 H  H    . LYS   B 1 161 ? -25.871 -20.597 6.719   1.00 53.49  ? 158 LYS   B H    1 
ATOM   6876 H  HA   . LYS   B 1 161 ? -26.090 -21.983 8.970   1.00 45.31  ? 158 LYS   B HA   1 
ATOM   6877 H  HB2  . LYS   B 1 161 ? -27.476 -22.638 7.355   1.00 68.57  ? 158 LYS   B HB2  1 
ATOM   6878 H  HB3  . LYS   B 1 161 ? -26.315 -22.681 6.271   1.00 68.57  ? 158 LYS   B HB3  1 
ATOM   6879 H  HG2  . LYS   B 1 161 ? -26.139 -24.527 8.310   1.00 81.31  ? 158 LYS   B HG2  1 
ATOM   6880 H  HG3  . LYS   B 1 161 ? -27.272 -24.777 7.224   1.00 81.31  ? 158 LYS   B HG3  1 
ATOM   6881 H  HD2  . LYS   B 1 161 ? -25.680 -24.906 5.559   1.00 76.19  ? 158 LYS   B HD2  1 
ATOM   6882 H  HD3  . LYS   B 1 161 ? -24.532 -24.577 6.608   1.00 76.19  ? 158 LYS   B HD3  1 
ATOM   6883 H  HE2  . LYS   B 1 161 ? -26.149 -26.826 7.071   1.00 83.95  ? 158 LYS   B HE2  1 
ATOM   6884 H  HE3  . LYS   B 1 161 ? -24.945 -26.962 6.043   1.00 83.95  ? 158 LYS   B HE3  1 
ATOM   6885 H  HZ1  . LYS   B 1 161 ? -24.222 -27.573 8.091   1.00 73.88  ? 158 LYS   B HZ1  1 
ATOM   6886 H  HZ2  . LYS   B 1 161 ? -23.545 -26.334 7.767   1.00 73.88  ? 158 LYS   B HZ2  1 
ATOM   6887 H  HZ3  . LYS   B 1 161 ? -24.658 -26.331 8.694   1.00 73.88  ? 158 LYS   B HZ3  1 
ATOM   6888 N  N    . GLY   B 1 162 ? -23.405 -22.388 7.295   1.00 40.30  ? 159 GLY   B N    1 
ATOM   6889 C  CA   . GLY   B 1 162 ? -22.071 -22.946 7.403   1.00 41.27  ? 159 GLY   B CA   1 
ATOM   6890 C  C    . GLY   B 1 162 ? -21.277 -22.347 8.548   1.00 35.00  ? 159 GLY   B C    1 
ATOM   6891 O  O    . GLY   B 1 162 ? -20.477 -23.037 9.191   1.00 37.93  ? 159 GLY   B O    1 
ATOM   6892 H  H    . GLY   B 1 162 ? -23.555 -21.942 6.575   1.00 48.40  ? 159 GLY   B H    1 
ATOM   6893 H  HA2  . GLY   B 1 162 ? -22.135 -23.903 7.545   1.00 49.57  ? 159 GLY   B HA2  1 
ATOM   6894 H  HA3  . GLY   B 1 162 ? -21.587 -22.781 6.578   1.00 49.57  ? 159 GLY   B HA3  1 
ATOM   6895 N  N    . MET   B 1 163 ? -21.441 -21.044 8.781   1.00 35.77  ? 160 MET   B N    1 
ATOM   6896 C  CA   . MET   B 1 163 ? -20.737 -20.407 9.884   1.00 33.67  ? 160 MET   B CA   1 
ATOM   6897 C  C    . MET   B 1 163 ? -21.237 -20.919 11.229  1.00 40.34  ? 160 MET   B C    1 
ATOM   6898 O  O    . MET   B 1 163 ? -20.480 -20.913 12.208  1.00 32.77  ? 160 MET   B O    1 
ATOM   6899 C  CB   . MET   B 1 163 ? -20.895 -18.897 9.812   1.00 36.83  ? 160 MET   B CB   1 
ATOM   6900 C  CG   . MET   B 1 163 ? -20.023 -18.174 8.801   1.00 36.25  ? 160 MET   B CG   1 
ATOM   6901 S  SD   . MET   B 1 163 ? -18.386 -18.893 8.458   1.00 37.10  ? 160 MET   B SD   1 
ATOM   6902 C  CE   . MET   B 1 163 ? -17.428 -18.265 9.815   1.00 44.72  ? 160 MET   B CE   1 
ATOM   6903 H  H    . MET   B 1 163 ? -21.946 -20.519 8.323   1.00 42.96  ? 160 MET   B H    1 
ATOM   6904 H  HA   . MET   B 1 163 ? -19.792 -20.608 9.797   1.00 40.45  ? 160 MET   B HA   1 
ATOM   6905 H  HB2  . MET   B 1 163 ? -21.818 -18.700 9.585   1.00 44.24  ? 160 MET   B HB2  1 
ATOM   6906 H  HB3  . MET   B 1 163 ? -20.684 -18.530 10.685  1.00 44.24  ? 160 MET   B HB3  1 
ATOM   6907 H  HG2  . MET   B 1 163 ? -20.502 -18.147 7.958   1.00 43.54  ? 160 MET   B HG2  1 
ATOM   6908 H  HG3  . MET   B 1 163 ? -19.872 -17.272 9.126   1.00 43.54  ? 160 MET   B HG3  1 
ATOM   6909 H  HE1  . MET   B 1 163 ? -16.518 -18.590 9.736   1.00 53.70  ? 160 MET   B HE1  1 
ATOM   6910 H  HE2  . MET   B 1 163 ? -17.437 -17.295 9.785   1.00 53.70  ? 160 MET   B HE2  1 
ATOM   6911 H  HE3  . MET   B 1 163 ? -17.819 -18.574 10.647  1.00 53.70  ? 160 MET   B HE3  1 
ATOM   6912 N  N    . LYS   B 1 164 ? -22.496 -21.350 11.317  1.00 39.54  ? 161 LYS   B N    1 
ATOM   6913 C  CA   . LYS   B 1 164 ? -22.955 -21.941 12.575  1.00 37.88  ? 161 LYS   B CA   1 
ATOM   6914 C  C    . LYS   B 1 164 ? -22.245 -23.267 12.823  1.00 42.95  ? 161 LYS   B C    1 
ATOM   6915 O  O    . LYS   B 1 164 ? -21.735 -23.513 13.920  1.00 39.78  ? 161 LYS   B O    1 
ATOM   6916 C  CB   . LYS   B 1 164 ? -24.473 -22.099 12.589  1.00 46.03  ? 161 LYS   B CB   1 
ATOM   6917 C  CG   . LYS   B 1 164 ? -25.250 -20.790 12.895  1.00 63.70  ? 161 LYS   B CG   1 
ATOM   6918 C  CD   . LYS   B 1 164 ? -24.534 -19.835 13.871  1.00 71.00  ? 161 LYS   B CD   1 
ATOM   6919 C  CE   . LYS   B 1 164 ? -24.016 -18.589 13.136  1.00 70.80  ? 161 LYS   B CE   1 
ATOM   6920 N  NZ   . LYS   B 1 164 ? -23.243 -17.644 13.996  1.00 55.17  ? 161 LYS   B NZ   1 
ATOM   6921 H  H    . LYS   B 1 164 ? -23.082 -21.314 10.689  1.00 47.49  ? 161 LYS   B H    1 
ATOM   6922 H  HA   . LYS   B 1 164 ? -22.743 -21.339 13.306  1.00 45.50  ? 161 LYS   B HA   1 
ATOM   6923 H  HB2  . LYS   B 1 164 ? -24.759 -22.414 11.717  1.00 55.28  ? 161 LYS   B HB2  1 
ATOM   6924 H  HB3  . LYS   B 1 164 ? -24.710 -22.748 13.269  1.00 55.28  ? 161 LYS   B HB3  1 
ATOM   6925 H  HG2  . LYS   B 1 164 ? -25.387 -20.310 12.064  1.00 76.48  ? 161 LYS   B HG2  1 
ATOM   6926 H  HG3  . LYS   B 1 164 ? -26.105 -21.023 13.289  1.00 76.48  ? 161 LYS   B HG3  1 
ATOM   6927 H  HD2  . LYS   B 1 164 ? -25.156 -19.550 14.559  1.00 85.24  ? 161 LYS   B HD2  1 
ATOM   6928 H  HD3  . LYS   B 1 164 ? -23.779 -20.290 14.274  1.00 85.24  ? 161 LYS   B HD3  1 
ATOM   6929 H  HE2  . LYS   B 1 164 ? -23.432 -18.874 12.416  1.00 85.00  ? 161 LYS   B HE2  1 
ATOM   6930 H  HE3  . LYS   B 1 164 ? -24.775 -18.103 12.776  1.00 85.00  ? 161 LYS   B HE3  1 
ATOM   6931 H  HZ1  . LYS   B 1 164 ? -22.987 -16.938 13.519  1.00 66.25  ? 161 LYS   B HZ1  1 
ATOM   6932 H  HZ2  . LYS   B 1 164 ? -23.748 -17.367 14.674  1.00 66.25  ? 161 LYS   B HZ2  1 
ATOM   6933 H  HZ3  . LYS   B 1 164 ? -22.521 -18.050 14.321  1.00 66.25  ? 161 LYS   B HZ3  1 
ATOM   6934 N  N    . THR   B 1 165 ? -22.133 -24.103 11.794  1.00 38.55  ? 162 THR   B N    1 
ATOM   6935 C  CA   . THR   B 1 165 ? -21.357 -25.333 11.916  1.00 39.66  ? 162 THR   B CA   1 
ATOM   6936 C  C    . THR   B 1 165 ? -19.904 -25.038 12.267  1.00 37.37  ? 162 THR   B C    1 
ATOM   6937 O  O    . THR   B 1 165 ? -19.308 -25.715 13.110  1.00 39.49  ? 162 THR   B O    1 
ATOM   6938 C  CB   . THR   B 1 165 ? -21.436 -26.122 10.607  1.00 43.78  ? 162 THR   B CB   1 
ATOM   6939 O  OG1  . THR   B 1 165 ? -22.812 -26.389 10.307  1.00 50.39  ? 162 THR   B OG1  1 
ATOM   6940 C  CG2  . THR   B 1 165 ? -20.676 -27.422 10.724  1.00 49.75  ? 162 THR   B CG2  1 
ATOM   6941 H  H    . THR   B 1 165 ? -22.493 -23.983 11.022  1.00 46.31  ? 162 THR   B H    1 
ATOM   6942 H  HA   . THR   B 1 165 ? -21.735 -25.874 12.627  1.00 47.63  ? 162 THR   B HA   1 
ATOM   6943 H  HB   . THR   B 1 165 ? -21.039 -25.609 9.886   1.00 52.58  ? 162 THR   B HB   1 
ATOM   6944 H  HG1  . THR   B 1 165 ? -22.867 -26.982 9.714   1.00 60.51  ? 162 THR   B HG1  1 
ATOM   6945 H  HG21 . THR   B 1 165 ? -20.807 -27.957 9.925   1.00 59.74  ? 162 THR   B HG21 1 
ATOM   6946 H  HG22 . THR   B 1 165 ? -19.729 -27.244 10.832  1.00 59.74  ? 162 THR   B HG22 1 
ATOM   6947 H  HG23 . THR   B 1 165 ? -20.991 -27.923 11.493  1.00 59.74  ? 162 THR   B HG23 1 
ATOM   6948 N  N    . PHE   B 1 166 ? -19.313 -24.047 11.610  1.00 33.40  ? 163 PHE   B N    1 
ATOM   6949 C  CA   . PHE   B 1 166 ? -17.936 -23.666 11.898  1.00 32.79  ? 163 PHE   B CA   1 
ATOM   6950 C  C    . PHE   B 1 166 ? -17.780 -23.336 13.374  1.00 31.67  ? 163 PHE   B C    1 
ATOM   6951 O  O    . PHE   B 1 166 ? -16.865 -23.830 14.048  1.00 29.85  ? 163 PHE   B O    1 
ATOM   6952 C  CB   . PHE   B 1 166 ? -17.579 -22.486 11.000  1.00 33.26  ? 163 PHE   B CB   1 
ATOM   6953 C  CG   . PHE   B 1 166 ? -16.202 -21.953 11.186  1.00 33.19  ? 163 PHE   B CG   1 
ATOM   6954 C  CD1  . PHE   B 1 166 ? -15.126 -22.588 10.599  1.00 35.82  ? 163 PHE   B CD1  1 
ATOM   6955 C  CD2  . PHE   B 1 166 ? -15.985 -20.774 11.890  1.00 32.37  ? 163 PHE   B CD2  1 
ATOM   6956 C  CE1  . PHE   B 1 166 ? -13.836 -22.080 10.747  1.00 37.12  ? 163 PHE   B CE1  1 
ATOM   6957 C  CE2  . PHE   B 1 166 ? -14.696 -20.254 12.050  1.00 34.78  ? 163 PHE   B CE2  1 
ATOM   6958 C  CZ   . PHE   B 1 166 ? -13.633 -20.896 11.465  1.00 30.39  ? 163 PHE   B CZ   1 
ATOM   6959 H  H    . PHE   B 1 166 ? -19.687 -23.578 10.993  1.00 40.12  ? 163 PHE   B H    1 
ATOM   6960 H  HA   . PHE   B 1 166 ? -17.321 -24.391 11.705  1.00 39.39  ? 163 PHE   B HA   1 
ATOM   6961 H  HB2  . PHE   B 1 166 ? -17.660 -22.767 10.075  1.00 39.95  ? 163 PHE   B HB2  1 
ATOM   6962 H  HB3  . PHE   B 1 166 ? -18.199 -21.762 11.182  1.00 39.95  ? 163 PHE   B HB3  1 
ATOM   6963 H  HD1  . PHE   B 1 166 ? -15.263 -23.360 10.100  1.00 43.03  ? 163 PHE   B HD1  1 
ATOM   6964 H  HD2  . PHE   B 1 166 ? -16.709 -20.324 12.262  1.00 38.88  ? 163 PHE   B HD2  1 
ATOM   6965 H  HE1  . PHE   B 1 166 ? -13.113 -22.527 10.370  1.00 44.59  ? 163 PHE   B HE1  1 
ATOM   6966 H  HE2  . PHE   B 1 166 ? -14.561 -19.480 12.547  1.00 41.77  ? 163 PHE   B HE2  1 
ATOM   6967 H  HZ   . PHE   B 1 166 ? -12.776 -20.543 11.546  1.00 36.51  ? 163 PHE   B HZ   1 
ATOM   6968 N  N    . GLY   B 1 167 ? -18.697 -22.534 13.907  1.00 33.98  ? 164 GLY   B N    1 
ATOM   6969 C  CA   . GLY   B 1 167 ? -18.575 -22.137 15.302  1.00 32.60  ? 164 GLY   B CA   1 
ATOM   6970 C  C    . GLY   B 1 167 ? -18.741 -23.301 16.265  1.00 35.67  ? 164 GLY   B C    1 
ATOM   6971 O  O    . GLY   B 1 167 ? -18.039 -23.378 17.285  1.00 33.35  ? 164 GLY   B O    1 
ATOM   6972 H  H    . GLY   B 1 167 ? -19.380 -22.214 13.493  1.00 40.82  ? 164 GLY   B H    1 
ATOM   6973 H  HA2  . GLY   B 1 167 ? -17.699 -21.745 15.447  1.00 39.16  ? 164 GLY   B HA2  1 
ATOM   6974 H  HA3  . GLY   B 1 167 ? -19.254 -21.475 15.506  1.00 39.16  ? 164 GLY   B HA3  1 
ATOM   6975 N  N    . GLU   B 1 168 ? -19.625 -24.241 15.935  1.00 32.94  ? 165 GLU   B N    1 
ATOM   6976 C  CA   . GLU   B 1 168 ? -19.777 -25.447 16.749  1.00 33.64  ? 165 GLU   B CA   1 
ATOM   6977 C  C    . GLU   B 1 168 ? -18.559 -26.357 16.629  1.00 37.30  ? 165 GLU   B C    1 
ATOM   6978 O  O    . GLU   B 1 168 ? -18.098 -26.921 17.629  1.00 39.17  ? 165 GLU   B O    1 
ATOM   6979 C  CB   . GLU   B 1 168 ? -21.058 -26.197 16.366  1.00 39.00  ? 165 GLU   B CB   1 
ATOM   6980 C  CG   . GLU   B 1 168 ? -22.315 -25.365 16.539  1.00 45.03  ? 165 GLU   B CG   1 
ATOM   6981 C  CD   . GLU   B 1 168 ? -23.533 -26.019 15.929  1.00 63.74  ? 165 GLU   B CD   1 
ATOM   6982 O  OE1  . GLU   B 1 168 ? -23.376 -27.086 15.296  1.00 64.65  ? 165 GLU   B OE1  1 
ATOM   6983 O  OE2  . GLU   B 1 168 ? -24.646 -25.473 16.090  1.00 64.57  ? 165 GLU   B OE2  1 
ATOM   6984 H  H    . GLU   B 1 168 ? -20.145 -24.206 15.251  1.00 39.58  ? 165 GLU   B H    1 
ATOM   6985 H  HA   . GLU   B 1 168 ? -19.861 -25.181 17.678  1.00 40.41  ? 165 GLU   B HA   1 
ATOM   6986 H  HB2  . GLU   B 1 168 ? -21.000 -26.459 15.434  1.00 46.84  ? 165 GLU   B HB2  1 
ATOM   6987 H  HB3  . GLU   B 1 168 ? -21.141 -26.983 16.927  1.00 46.84  ? 165 GLU   B HB3  1 
ATOM   6988 H  HG2  . GLU   B 1 168 ? -22.484 -25.240 17.486  1.00 54.08  ? 165 GLU   B HG2  1 
ATOM   6989 H  HG3  . GLU   B 1 168 ? -22.188 -24.505 16.109  1.00 54.08  ? 165 GLU   B HG3  1 
ATOM   6990 N  N    . THR   B 1 169 ? -18.012 -26.497 15.423  1.00 33.47  ? 166 THR   B N    1 
ATOM   6991 C  CA   . THR   B 1 169 ? -16.873 -27.387 15.236  1.00 33.50  ? 166 THR   B CA   1 
ATOM   6992 C  C    . THR   B 1 169 ? -15.669 -26.910 16.041  1.00 36.17  ? 166 THR   B C    1 
ATOM   6993 O  O    . THR   B 1 169 ? -14.967 -27.715 16.664  1.00 35.83  ? 166 THR   B O    1 
ATOM   6994 C  CB   . THR   B 1 169 ? -16.555 -27.482 13.743  1.00 35.74  ? 166 THR   B CB   1 
ATOM   6995 O  OG1  . THR   B 1 169 ? -17.707 -28.008 13.068  1.00 38.93  ? 166 THR   B OG1  1 
ATOM   6996 C  CG2  . THR   B 1 169 ? -15.364 -28.373 13.491  1.00 38.59  ? 166 THR   B CG2  1 
ATOM   6997 H  H    . THR   B 1 169 ? -18.278 -26.096 14.710  1.00 40.21  ? 166 THR   B H    1 
ATOM   6998 H  HA   . THR   B 1 169 ? -17.091 -28.278 15.551  1.00 40.24  ? 166 THR   B HA   1 
ATOM   6999 H  HB   . THR   B 1 169 ? -16.333 -26.604 13.395  1.00 42.93  ? 166 THR   B HB   1 
ATOM   7000 H  HG1  . THR   B 1 169 ? -18.369 -27.507 13.197  1.00 46.75  ? 166 THR   B HG1  1 
ATOM   7001 H  HG21 . THR   B 1 169 ? -15.297 -28.578 12.546  1.00 46.35  ? 166 THR   B HG21 1 
ATOM   7002 H  HG22 . THR   B 1 169 ? -14.550 -27.928 13.775  1.00 46.35  ? 166 THR   B HG22 1 
ATOM   7003 H  HG23 . THR   B 1 169 ? -15.459 -29.201 13.987  1.00 46.35  ? 166 THR   B HG23 1 
ATOM   7004 N  N    . LEU   B 1 170 ? -15.432 -25.611 16.058  1.00 29.44  ? 167 LEU   B N    1 
ATOM   7005 C  CA   . LEU   B 1 170 ? -14.325 -25.024 16.802  1.00 29.44  ? 167 LEU   B CA   1 
ATOM   7006 C  C    . LEU   B 1 170 ? -14.664 -24.700 18.253  1.00 32.00  ? 167 LEU   B C    1 
ATOM   7007 O  O    . LEU   B 1 170 ? -13.778 -24.213 18.975  1.00 27.25  ? 167 LEU   B O    1 
ATOM   7008 C  CB   . LEU   B 1 170 ? -13.865 -23.751 16.086  1.00 27.07  ? 167 LEU   B CB   1 
ATOM   7009 C  CG   . LEU   B 1 170 ? -12.787 -23.912 14.991  1.00 26.05  ? 167 LEU   B CG   1 
ATOM   7010 C  CD1  . LEU   B 1 170 ? -13.430 -24.629 13.791  1.00 34.29  ? 167 LEU   B CD1  1 
ATOM   7011 C  CD2  . LEU   B 1 170 ? -12.167 -22.595 14.577  1.00 28.64  ? 167 LEU   B CD2  1 
ATOM   7012 H  H    . LEU   B 1 170 ? -15.908 -25.031 15.638  1.00 35.37  ? 167 LEU   B H    1 
ATOM   7013 H  HA   . LEU   B 1 170 ? -13.592 -25.659 16.821  1.00 35.37  ? 167 LEU   B HA   1 
ATOM   7014 H  HB2  . LEU   B 1 170 ? -14.640 -23.350 15.662  1.00 32.52  ? 167 LEU   B HB2  1 
ATOM   7015 H  HB3  . LEU   B 1 170 ? -13.503 -23.147 16.753  1.00 32.52  ? 167 LEU   B HB3  1 
ATOM   7016 H  HG   . LEU   B 1 170 ? -12.050 -24.439 15.340  1.00 31.30  ? 167 LEU   B HG   1 
ATOM   7017 H  HD11 . LEU   B 1 170 ? -12.754 -24.777 13.112  1.00 41.19  ? 167 LEU   B HD11 1 
ATOM   7018 H  HD12 . LEU   B 1 170 ? -13.793 -25.478 14.088  1.00 41.19  ? 167 LEU   B HD12 1 
ATOM   7019 H  HD13 . LEU   B 1 170 ? -14.140 -24.073 13.435  1.00 41.19  ? 167 LEU   B HD13 1 
ATOM   7020 H  HD21 . LEU   B 1 170 ? -11.494 -22.762 13.899  1.00 34.41  ? 167 LEU   B HD21 1 
ATOM   7021 H  HD22 . LEU   B 1 170 ? -12.861 -22.019 14.220  1.00 34.41  ? 167 LEU   B HD22 1 
ATOM   7022 H  HD23 . LEU   B 1 170 ? -11.759 -22.180 15.353  1.00 34.41  ? 167 LEU   B HD23 1 
ATOM   7023 N  N    . ASN   B 1 171 ? -15.898 -24.955 18.689  1.00 27.49  ? 168 ASN   B N    1 
ATOM   7024 C  CA   . ASN   B 1 171 ? -16.386 -24.599 20.031  1.00 28.50  ? 168 ASN   B CA   1 
ATOM   7025 C  C    . ASN   B 1 171 ? -16.090 -23.142 20.383  1.00 31.59  ? 168 ASN   B C    1 
ATOM   7026 O  O    . ASN   B 1 171 ? -15.613 -22.820 21.480  1.00 30.50  ? 168 ASN   B O    1 
ATOM   7027 C  CB   . ASN   B 1 171 ? -15.818 -25.524 21.106  1.00 29.87  ? 168 ASN   B CB   1 
ATOM   7028 C  CG   . ASN   B 1 171 ? -16.637 -25.494 22.368  1.00 38.28  ? 168 ASN   B CG   1 
ATOM   7029 O  OD1  . ASN   B 1 171 ? -17.873 -25.429 22.320  1.00 48.65  ? 168 ASN   B OD1  1 
ATOM   7030 N  ND2  . ASN   B 1 171 ? -15.966 -25.589 23.518  1.00 38.91  ? 168 ASN   B ND2  1 
ATOM   7031 H  H    . ASN   B 1 171 ? -16.496 -25.347 18.212  1.00 33.03  ? 168 ASN   B H    1 
ATOM   7032 H  HA   . ASN   B 1 171 ? -17.349 -24.709 20.011  1.00 34.25  ? 168 ASN   B HA   1 
ATOM   7033 H  HB2  . ASN   B 1 171 ? -15.810 -26.434 20.772  1.00 35.89  ? 168 ASN   B HB2  1 
ATOM   7034 H  HB3  . ASN   B 1 171 ? -14.916 -25.242 21.324  1.00 35.89  ? 168 ASN   B HB3  1 
ATOM   7035 H  HD21 . ASN   B 1 171 ? -16.391 -25.577 24.266  1.00 46.73  ? 168 ASN   B HD21 1 
ATOM   7036 H  HD22 . ASN   B 1 171 ? -15.109 -25.663 23.511  1.00 46.73  ? 168 ASN   B HD22 1 
ATOM   7037 N  N    . ILE   B 1 172 ? -16.433 -22.255 19.454  1.00 32.02  ? 169 ILE   B N    1 
ATOM   7038 C  CA   . ILE   B 1 172 ? -16.340 -20.818 19.670  1.00 31.66  ? 169 ILE   B CA   1 
ATOM   7039 C  C    . ILE   B 1 172 ? -17.333 -20.412 20.753  1.00 31.26  ? 169 ILE   B C    1 
ATOM   7040 O  O    . ILE   B 1 172 ? -18.461 -20.924 20.816  1.00 34.07  ? 169 ILE   B O    1 
ATOM   7041 C  CB   . ILE   B 1 172 ? -16.628 -20.074 18.354  1.00 33.52  ? 169 ILE   B CB   1 
ATOM   7042 C  CG1  . ILE   B 1 172 ? -15.619 -20.459 17.268  1.00 31.96  ? 169 ILE   B CG1  1 
ATOM   7043 C  CG2  . ILE   B 1 172 ? -16.585 -18.558 18.560  1.00 32.71  ? 169 ILE   B CG2  1 
ATOM   7044 C  CD1  . ILE   B 1 172 ? -14.162 -20.242 17.661  1.00 37.90  ? 169 ILE   B CD1  1 
ATOM   7045 H  H    . ILE   B 1 172 ? -16.729 -22.465 18.674  1.00 38.47  ? 169 ILE   B H    1 
ATOM   7046 H  HA   . ILE   B 1 172 ? -15.445 -20.588 19.966  1.00 38.03  ? 169 ILE   B HA   1 
ATOM   7047 H  HB   . ILE   B 1 172 ? -17.517 -20.337 18.069  1.00 40.26  ? 169 ILE   B HB   1 
ATOM   7048 H  HG12 . ILE   B 1 172 ? -15.730 -21.400 17.060  1.00 38.39  ? 169 ILE   B HG12 1 
ATOM   7049 H  HG13 . ILE   B 1 172 ? -15.793 -19.922 16.478  1.00 38.39  ? 169 ILE   B HG13 1 
ATOM   7050 H  HG21 . ILE   B 1 172 ? -16.570 -18.122 17.694  1.00 39.29  ? 169 ILE   B HG21 1 
ATOM   7051 H  HG22 . ILE   B 1 172 ? -17.373 -18.284 19.055  1.00 39.29  ? 169 ILE   B HG22 1 
ATOM   7052 H  HG23 . ILE   B 1 172 ? -15.786 -18.330 19.060  1.00 39.29  ? 169 ILE   B HG23 1 
ATOM   7053 H  HD11 . ILE   B 1 172 ? -13.608 -20.305 16.867  1.00 45.52  ? 169 ILE   B HD11 1 
ATOM   7054 H  HD12 . ILE   B 1 172 ? -14.069 -19.363 18.059  1.00 45.52  ? 169 ILE   B HD12 1 
ATOM   7055 H  HD13 . ILE   B 1 172 ? -13.902 -20.924 18.300  1.00 45.52  ? 169 ILE   B HD13 1 
ATOM   7056 N  N    . ALA   B 1 173 ? -16.906 -19.500 21.630  1.00 31.46  ? 170 ALA   B N    1 
ATOM   7057 C  CA   . ALA   B 1 173 ? -17.765 -19.043 22.705  1.00 29.40  ? 170 ALA   B CA   1 
ATOM   7058 C  C    . ALA   B 1 173 ? -18.971 -18.289 22.156  1.00 34.39  ? 170 ALA   B C    1 
ATOM   7059 O  O    . ALA   B 1 173 ? -18.844 -17.547 21.177  1.00 37.50  ? 170 ALA   B O    1 
ATOM   7060 C  CB   . ALA   B 1 173 ? -16.958 -18.144 23.644  1.00 35.06  ? 170 ALA   B CB   1 
ATOM   7061 H  H    . ALA   B 1 173 ? -16.127 -19.137 21.619  1.00 37.80  ? 170 ALA   B H    1 
ATOM   7062 H  HA   . ALA   B 1 173 ? -18.106 -19.802 23.204  1.00 35.32  ? 170 ALA   B HA   1 
ATOM   7063 H  HB1  . ALA   B 1 173 ? -17.542 -17.814 24.345  1.00 42.12  ? 170 ALA   B HB1  1 
ATOM   7064 H  HB2  . ALA   B 1 173 ? -16.235 -18.662 24.032  1.00 42.12  ? 170 ALA   B HB2  1 
ATOM   7065 H  HB3  . ALA   B 1 173 ? -16.596 -17.401 23.137  1.00 42.12  ? 170 ALA   B HB3  1 
ATOM   7066 N  N    . PRO   B 1 174 ? -20.150 -18.457 22.757  1.00 36.87  ? 171 PRO   B N    1 
ATOM   7067 C  CA   . PRO   B 1 174 ? -21.337 -17.739 22.248  1.00 42.26  ? 171 PRO   B CA   1 
ATOM   7068 C  C    . PRO   B 1 174 ? -21.126 -16.243 22.135  1.00 43.67  ? 171 PRO   B C    1 
ATOM   7069 O  O    . PRO   B 1 174 ? -21.533 -15.628 21.141  1.00 46.62  ? 171 PRO   B O    1 
ATOM   7070 C  CB   . PRO   B 1 174 ? -22.422 -18.081 23.277  1.00 46.03  ? 171 PRO   B CB   1 
ATOM   7071 C  CG   . PRO   B 1 174 ? -21.991 -19.371 23.845  1.00 42.66  ? 171 PRO   B CG   1 
ATOM   7072 C  CD   . PRO   B 1 174 ? -20.496 -19.322 23.904  1.00 36.03  ? 171 PRO   B CD   1 
ATOM   7073 H  HA   . PRO   B 1 174 ? -21.591 -18.098 21.383  1.00 50.75  ? 171 PRO   B HA   1 
ATOM   7074 H  HB2  . PRO   B 1 174 ? -22.461 -17.394 23.960  1.00 55.28  ? 171 PRO   B HB2  1 
ATOM   7075 H  HB3  . PRO   B 1 174 ? -23.283 -18.162 22.838  1.00 55.28  ? 171 PRO   B HB3  1 
ATOM   7076 H  HG2  . PRO   B 1 174 ? -22.366 -19.477 24.733  1.00 51.24  ? 171 PRO   B HG2  1 
ATOM   7077 H  HG3  . PRO   B 1 174 ? -22.288 -20.095 23.271  1.00 51.24  ? 171 PRO   B HG3  1 
ATOM   7078 H  HD2  . PRO   B 1 174 ? -20.195 -18.928 24.738  1.00 43.28  ? 171 PRO   B HD2  1 
ATOM   7079 H  HD3  . PRO   B 1 174 ? -20.115 -20.207 23.798  1.00 43.28  ? 171 PRO   B HD3  1 
ATOM   7080 N  N    . ILE   B 1 175 ? -20.490 -15.643 23.145  1.00 44.26  ? 172 ILE   B N    1 
ATOM   7081 C  CA   . ILE   B 1 175 ? -20.223 -14.207 23.126  1.00 52.71  ? 172 ILE   B CA   1 
ATOM   7082 C  C    . ILE   B 1 175 ? -19.530 -13.827 21.828  1.00 53.06  ? 172 ILE   B C    1 
ATOM   7083 O  O    . ILE   B 1 175 ? -19.906 -12.847 21.168  1.00 53.90  ? 172 ILE   B O    1 
ATOM   7084 C  CB   . ILE   B 1 175 ? -19.396 -13.809 24.369  1.00 57.80  ? 172 ILE   B CB   1 
ATOM   7085 C  CG1  . ILE   B 1 175 ? -19.330 -12.281 24.511  1.00 59.91  ? 172 ILE   B CG1  1 
ATOM   7086 C  CG2  . ILE   B 1 175 ? -17.992 -14.433 24.339  1.00 54.20  ? 172 ILE   B CG2  1 
ATOM   7087 C  CD1  . ILE   B 1 175 ? -20.647 -11.565 24.232  1.00 69.71  ? 172 ILE   B CD1  1 
ATOM   7088 H  H    . ILE   B 1 175 ? -20.204 -16.045 23.850  1.00 53.16  ? 172 ILE   B H    1 
ATOM   7089 H  HA   . ILE   B 1 175 ? -21.063 -13.723 23.165  1.00 63.30  ? 172 ILE   B HA   1 
ATOM   7090 H  HB   . ILE   B 1 175 ? -19.849 -14.163 25.150  1.00 69.41  ? 172 ILE   B HB   1 
ATOM   7091 H  HG12 . ILE   B 1 175 ? -19.066 -12.066 25.420  1.00 71.94  ? 172 ILE   B HG12 1 
ATOM   7092 H  HG13 . ILE   B 1 175 ? -18.672 -11.940 23.885  1.00 71.94  ? 172 ILE   B HG13 1 
ATOM   7093 H  HG21 . ILE   B 1 175 ? -17.565 -14.293 25.198  1.00 65.08  ? 172 ILE   B HG21 1 
ATOM   7094 H  HG22 . ILE   B 1 175 ? -18.073 -15.384 24.161  1.00 65.08  ? 172 ILE   B HG22 1 
ATOM   7095 H  HG23 . ILE   B 1 175 ? -17.472 -14.009 23.638  1.00 65.08  ? 172 ILE   B HG23 1 
ATOM   7096 H  HD11 . ILE   B 1 175 ? -20.568 -10.640 24.512  1.00 83.69  ? 172 ILE   B HD11 1 
ATOM   7097 H  HD12 . ILE   B 1 175 ? -20.834 -11.609 23.281  1.00 83.69  ? 172 ILE   B HD12 1 
ATOM   7098 H  HD13 . ILE   B 1 175 ? -21.355 -12.002 24.729  1.00 83.69  ? 172 ILE   B HD13 1 
ATOM   7099 N  N    . ASP   B 1 176 ? -18.535 -14.618 21.423  1.00 43.79  ? 173 ASP   B N    1 
ATOM   7100 C  CA   . ASP   B 1 176 ? -17.797 -14.343 20.190  1.00 41.89  ? 173 ASP   B CA   1 
ATOM   7101 C  C    . ASP   B 1 176 ? -18.638 -14.640 18.958  1.00 39.88  ? 173 ASP   B C    1 
ATOM   7102 O  O    . ASP   B 1 176 ? -18.747 -13.799 18.057  1.00 48.31  ? 173 ASP   B O    1 
ATOM   7103 C  CB   . ASP   B 1 176 ? -16.515 -15.172 20.191  1.00 34.28  ? 173 ASP   B CB   1 
ATOM   7104 C  CG   . ASP   B 1 176 ? -15.497 -14.678 21.202  1.00 35.77  ? 173 ASP   B CG   1 
ATOM   7105 O  OD1  . ASP   B 1 176 ? -15.397 -13.451 21.406  1.00 35.85  ? 173 ASP   B OD1  1 
ATOM   7106 O  OD2  . ASP   B 1 176 ? -14.828 -15.525 21.845  1.00 30.95  ? 173 ASP   B OD2  1 
ATOM   7107 H  H    . ASP   B 1 176 ? -18.267 -15.319 21.842  1.00 52.59  ? 173 ASP   B H    1 
ATOM   7108 H  HA   . ASP   B 1 176 ? -17.562 -13.403 20.156  1.00 50.31  ? 173 ASP   B HA   1 
ATOM   7109 H  HB2  . ASP   B 1 176 ? -16.733 -16.091 20.410  1.00 41.18  ? 173 ASP   B HB2  1 
ATOM   7110 H  HB3  . ASP   B 1 176 ? -16.109 -15.128 19.311  1.00 41.18  ? 173 ASP   B HB3  1 
ATOM   7111 N  N    . ALA   B 1 177 ? -19.237 -15.833 18.890  1.00 42.73  ? 174 ALA   B N    1 
ATOM   7112 C  CA   . ALA   B 1 177 ? -20.120 -16.135 17.768  1.00 52.04  ? 174 ALA   B CA   1 
ATOM   7113 C  C    . ALA   B 1 177 ? -21.240 -15.106 17.655  1.00 55.42  ? 174 ALA   B C    1 
ATOM   7114 O  O    . ALA   B 1 177 ? -21.712 -14.817 16.550  1.00 57.11  ? 174 ALA   B O    1 
ATOM   7115 C  CB   . ALA   B 1 177 ? -20.699 -17.542 17.919  1.00 49.23  ? 174 ALA   B CB   1 
ATOM   7116 H  H    . ALA   B 1 177 ? -19.149 -16.466 19.465  1.00 51.31  ? 174 ALA   B H    1 
ATOM   7117 H  HA   . ALA   B 1 177 ? -19.605 -16.114 16.946  1.00 62.49  ? 174 ALA   B HA   1 
ATOM   7118 H  HB1  . ALA   B 1 177 ? -21.238 -17.747 17.139  1.00 59.12  ? 174 ALA   B HB1  1 
ATOM   7119 H  HB2  . ALA   B 1 177 ? -19.969 -18.177 17.992  1.00 59.12  ? 174 ALA   B HB2  1 
ATOM   7120 H  HB3  . ALA   B 1 177 ? -21.247 -17.574 18.718  1.00 59.12  ? 174 ALA   B HB3  1 
ATOM   7121 N  N    . LYS   B 1 178 ? -21.672 -14.538 18.784  1.00 50.40  ? 175 LYS   B N    1 
ATOM   7122 C  CA   . LYS   B 1 178 ? -22.691 -13.491 18.742  1.00 62.77  ? 175 LYS   B CA   1 
ATOM   7123 C  C    . LYS   B 1 178 ? -22.157 -12.236 18.058  1.00 64.03  ? 175 LYS   B C    1 
ATOM   7124 O  O    . LYS   B 1 178 ? -22.781 -11.709 17.129  1.00 58.00  ? 175 LYS   B O    1 
ATOM   7125 C  CB   . LYS   B 1 178 ? -23.168 -13.179 20.164  1.00 62.79  ? 175 LYS   B CB   1 
ATOM   7126 C  CG   . LYS   B 1 178 ? -23.930 -11.870 20.337  1.00 76.78  ? 175 LYS   B CG   1 
ATOM   7127 C  CD   . LYS   B 1 178 ? -24.259 -11.654 21.819  1.00 74.65  ? 175 LYS   B CD   1 
ATOM   7128 C  CE   . LYS   B 1 178 ? -24.804 -10.263 22.111  1.00 67.38  ? 175 LYS   B CE   1 
ATOM   7129 N  NZ   . LYS   B 1 178 ? -24.962 -10.052 23.585  1.00 92.64  ? 175 LYS   B NZ   1 
ATOM   7130 H  H    . LYS   B 1 178 ? -21.395 -14.738 19.573  1.00 60.52  ? 175 LYS   B H    1 
ATOM   7131 H  HA   . LYS   B 1 178 ? -23.452 -13.806 18.231  1.00 75.37  ? 175 LYS   B HA   1 
ATOM   7132 H  HB2  . LYS   B 1 178 ? -23.757 -13.895 20.450  1.00 75.39  ? 175 LYS   B HB2  1 
ATOM   7133 H  HB3  . LYS   B 1 178 ? -22.390 -13.138 20.742  1.00 75.39  ? 175 LYS   B HB3  1 
ATOM   7134 H  HG2  . LYS   B 1 178 ? -23.385 -11.130 20.027  1.00 92.18  ? 175 LYS   B HG2  1 
ATOM   7135 H  HG3  . LYS   B 1 178 ? -24.759 -11.905 19.835  1.00 92.18  ? 175 LYS   B HG3  1 
ATOM   7136 H  HD2  . LYS   B 1 178 ? -24.929 -12.300 22.091  1.00 89.62  ? 175 LYS   B HD2  1 
ATOM   7137 H  HD3  . LYS   B 1 178 ? -23.451 -11.773 22.343  1.00 89.62  ? 175 LYS   B HD3  1 
ATOM   7138 H  HE2  . LYS   B 1 178 ? -24.189 -9.595  21.769  1.00 80.89  ? 175 LYS   B HE2  1 
ATOM   7139 H  HE3  . LYS   B 1 178 ? -25.673 -10.161 21.691  1.00 80.89  ? 175 LYS   B HE3  1 
ATOM   7140 H  HZ1  . LYS   B 1 178 ? -25.267 -9.231  23.744  1.00 111.21 ? 175 LYS   B HZ1  1 
ATOM   7141 H  HZ2  . LYS   B 1 178 ? -25.537 -10.644 23.918  1.00 111.21 ? 175 LYS   B HZ2  1 
ATOM   7142 H  HZ3  . LYS   B 1 178 ? -24.177 -10.152 23.993  1.00 111.21 ? 175 LYS   B HZ3  1 
ATOM   7143 N  N    . MET   B 1 179 ? -20.995 -11.747 18.498  1.00 51.14  ? 176 MET   B N    1 
ATOM   7144 C  CA   . MET   B 1 179 ? -20.448 -10.524 17.922  1.00 60.10  ? 176 MET   B CA   1 
ATOM   7145 C  C    . MET   B 1 179 ? -20.057 -10.727 16.462  1.00 58.95  ? 176 MET   B C    1 
ATOM   7146 O  O    . MET   B 1 179 ? -20.323 -9.864  15.619  1.00 62.05  ? 176 MET   B O    1 
ATOM   7147 C  CB   . MET   B 1 179 ? -19.251 -10.059 18.753  1.00 53.53  ? 176 MET   B CB   1 
ATOM   7148 C  CG   . MET   B 1 179 ? -19.651 -9.350  20.039  1.00 54.36  ? 176 MET   B CG   1 
ATOM   7149 S  SD   . MET   B 1 179 ? -18.264 -8.948  21.121  1.00 54.62  ? 176 MET   B SD   1 
ATOM   7150 C  CE   . MET   B 1 179 ? -17.579 -7.503  20.297  1.00 61.05  ? 176 MET   B CE   1 
ATOM   7151 H  H    . MET   B 1 179 ? -20.514 -12.100 19.117  1.00 61.41  ? 176 MET   B H    1 
ATOM   7152 H  HA   . MET   B 1 179 ? -21.122 -9.828  17.959  1.00 72.16  ? 176 MET   B HA   1 
ATOM   7153 H  HB2  . MET   B 1 179 ? -18.716 -10.832 18.993  1.00 64.27  ? 176 MET   B HB2  1 
ATOM   7154 H  HB3  . MET   B 1 179 ? -18.722 -9.442  18.224  1.00 64.27  ? 176 MET   B HB3  1 
ATOM   7155 H  HG2  . MET   B 1 179 ? -20.096 -8.519  19.810  1.00 65.27  ? 176 MET   B HG2  1 
ATOM   7156 H  HG3  . MET   B 1 179 ? -20.255 -9.924  20.536  1.00 65.27  ? 176 MET   B HG3  1 
ATOM   7157 H  HE1  . MET   B 1 179 ? -16.807 -7.192  20.794  1.00 73.30  ? 176 MET   B HE1  1 
ATOM   7158 H  HE2  . MET   B 1 179 ? -17.316 -7.749  19.396  1.00 73.30  ? 176 MET   B HE2  1 
ATOM   7159 H  HE3  . MET   B 1 179 ? -18.255 -6.808  20.266  1.00 73.30  ? 176 MET   B HE3  1 
ATOM   7160 N  N    . MET   B 1 180 ? -19.444 -11.867 16.144  1.00 54.09  ? 177 MET   B N    1 
ATOM   7161 C  CA   . MET   B 1 180 ? -19.013 -12.130 14.776  1.00 65.13  ? 177 MET   B CA   1 
ATOM   7162 C  C    . MET   B 1 180 ? -20.182 -12.148 13.794  1.00 60.11  ? 177 MET   B C    1 
ATOM   7163 O  O    . MET   B 1 180 ? -20.027 -11.740 12.638  1.00 55.18  ? 177 MET   B O    1 
ATOM   7164 C  CB   . MET   B 1 180 ? -18.281 -13.471 14.716  1.00 66.56  ? 177 MET   B CB   1 
ATOM   7165 C  CG   . MET   B 1 180 ? -16.865 -13.463 15.268  1.00 60.78  ? 177 MET   B CG   1 
ATOM   7166 S  SD   . MET   B 1 180 ? -16.460 -15.060 16.025  1.00 62.05  ? 177 MET   B SD   1 
ATOM   7167 C  CE   . MET   B 1 180 ? -16.047 -16.039 14.578  1.00 64.81  ? 177 MET   B CE   1 
ATOM   7168 H  H    . MET   B 1 180 ? -19.267 -12.500 16.699  1.00 64.95  ? 177 MET   B H    1 
ATOM   7169 H  HA   . MET   B 1 180 ? -18.400 -11.425 14.515  1.00 78.20  ? 177 MET   B HA   1 
ATOM   7170 H  HB2  . MET   B 1 180 ? -18.788 -14.120 15.228  1.00 79.91  ? 177 MET   B HB2  1 
ATOM   7171 H  HB3  . MET   B 1 180 ? -18.228 -13.750 13.788  1.00 79.91  ? 177 MET   B HB3  1 
ATOM   7172 H  HG2  . MET   B 1 180 ? -16.237 -13.296 14.547  1.00 72.98  ? 177 MET   B HG2  1 
ATOM   7173 H  HG3  . MET   B 1 180 ? -16.785 -12.772 15.944  1.00 72.98  ? 177 MET   B HG3  1 
ATOM   7174 H  HE1  . MET   B 1 180 ? -15.849 -16.947 14.857  1.00 77.81  ? 177 MET   B HE1  1 
ATOM   7175 H  HE2  . MET   B 1 180 ? -16.802 -16.037 13.969  1.00 77.81  ? 177 MET   B HE2  1 
ATOM   7176 H  HE3  . MET   B 1 180 ? -15.272 -15.650 14.144  1.00 77.81  ? 177 MET   B HE3  1 
ATOM   7177 N  N    . SER   B 1 181 ? -21.344 -12.623 14.222  1.00 63.41  ? 178 SER   B N    1 
ATOM   7178 C  CA   . SER   B 1 181 ? -22.482 -12.839 13.336  1.00 62.50  ? 178 SER   B CA   1 
ATOM   7179 C  C    . SER   B 1 181 ? -23.494 -11.701 13.358  1.00 63.81  ? 178 SER   B C    1 
ATOM   7180 O  O    . SER   B 1 181 ? -24.458 -11.730 12.577  1.00 61.00  ? 178 SER   B O    1 
ATOM   7181 C  CB   . SER   B 1 181 ? -23.164 -14.159 13.701  1.00 59.16  ? 178 SER   B CB   1 
ATOM   7182 O  OG   . SER   B 1 181 ? -23.795 -14.069 14.964  1.00 65.55  ? 178 SER   B OG   1 
ATOM   7183 H  H    . SER   B 1 181 ? -21.503 -12.834 15.041  1.00 76.14  ? 178 SER   B H    1 
ATOM   7184 H  HA   . SER   B 1 181 ? -22.160 -12.905 12.424  1.00 75.04  ? 178 SER   B HA   1 
ATOM   7185 H  HB2  . SER   B 1 181 ? -23.832 -14.365 13.029  1.00 71.03  ? 178 SER   B HB2  1 
ATOM   7186 H  HB3  . SER   B 1 181 ? -22.496 -14.861 13.732  1.00 71.03  ? 178 SER   B HB3  1 
ATOM   7187 H  HG   . SER   B 1 181 ? -23.235 -13.851 15.551  1.00 78.70  ? 178 SER   B HG   1 
ATOM   7188 N  N    . GLN   B 1 182 ? -23.301 -10.701 14.216  1.00 68.09  ? 179 GLN   B N    1 
ATOM   7189 C  CA   . GLN   B 1 182 ? -24.236 -9.587  14.336  1.00 66.52  ? 179 GLN   B CA   1 
ATOM   7190 C  C    . GLN   B 1 182 ? -24.435 -8.888  12.996  1.00 69.25  ? 179 GLN   B C    1 
ATOM   7191 O  O    . GLN   B 1 182 ? -23.456 -8.402  12.410  1.00 66.59  ? 179 GLN   B O    1 
ATOM   7192 C  CB   . GLN   B 1 182 ? -23.723 -8.573  15.363  1.00 74.44  ? 179 GLN   B CB   1 
ATOM   7193 C  CG   . GLN   B 1 182 ? -24.761 -7.559  15.841  1.00 79.74  ? 179 GLN   B CG   1 
ATOM   7194 C  CD   . GLN   B 1 182 ? -25.439 -7.971  17.137  1.00 82.34  ? 179 GLN   B CD   1 
ATOM   7195 O  OE1  . GLN   B 1 182 ? -24.775 -8.353  18.105  1.00 78.01  ? 179 GLN   B OE1  1 
ATOM   7196 N  NE2  . GLN   B 1 182 ? -26.765 -7.881  17.167  1.00 81.25  ? 179 GLN   B NE2  1 
ATOM   7197 H  H    . GLN   B 1 182 ? -22.627 -10.645 14.747  1.00 81.76  ? 179 GLN   B H    1 
ATOM   7198 H  HA   . GLN   B 1 182 ? -25.091 -9.937  14.631  1.00 79.86  ? 179 GLN   B HA   1 
ATOM   7199 H  HB2  . GLN   B 1 182 ? -23.409 -9.057  16.142  1.00 89.37  ? 179 GLN   B HB2  1 
ATOM   7200 H  HB3  . GLN   B 1 182 ? -22.993 -8.075  14.964  1.00 89.37  ? 179 GLN   B HB3  1 
ATOM   7201 H  HG2  . GLN   B 1 182 ? -24.324 -6.707  15.991  1.00 95.73  ? 179 GLN   B HG2  1 
ATOM   7202 H  HG3  . GLN   B 1 182 ? -25.447 -7.465  15.162  1.00 95.73  ? 179 GLN   B HG3  1 
ATOM   7203 H  HE21 . GLN   B 1 182 ? -27.192 -7.601  16.476  1.00 97.54  ? 179 GLN   B HE21 1 
ATOM   7204 H  HE22 . GLN   B 1 182 ? -27.195 -8.103  17.878  1.00 97.54  ? 179 GLN   B HE22 1 
ATOM   7205 N  N    . PRO   B 1 183 ? -25.659 -8.809  12.480  1.00 61.34  ? 180 PRO   B N    1 
ATOM   7206 C  CA   . PRO   B 1 183 ? -25.888 -8.004  11.276  1.00 59.18  ? 180 PRO   B CA   1 
ATOM   7207 C  C    . PRO   B 1 183 ? -25.547 -6.538  11.506  1.00 66.98  ? 180 PRO   B C    1 
ATOM   7208 O  O    . PRO   B 1 183 ? -25.785 -5.989  12.583  1.00 67.02  ? 180 PRO   B O    1 
ATOM   7209 C  CB   . PRO   B 1 183 ? -27.391 -8.191  11.014  1.00 58.74  ? 180 PRO   B CB   1 
ATOM   7210 C  CG   . PRO   B 1 183 ? -27.658 -9.572  11.538  1.00 62.31  ? 180 PRO   B CG   1 
ATOM   7211 C  CD   . PRO   B 1 183 ? -26.846 -9.627  12.819  1.00 53.74  ? 180 PRO   B CD   1 
ATOM   7212 H  HA   . PRO   B 1 183 ? -25.370 -8.346  10.531  1.00 71.06  ? 180 PRO   B HA   1 
ATOM   7213 H  HB2  . PRO   B 1 183 ? -27.904 -7.524  11.497  1.00 70.54  ? 180 PRO   B HB2  1 
ATOM   7214 H  HB3  . PRO   B 1 183 ? -27.579 -8.130  10.065  1.00 70.54  ? 180 PRO   B HB3  1 
ATOM   7215 H  HG2  . PRO   B 1 183 ? -28.605 -9.688  11.716  1.00 74.82  ? 180 PRO   B HG2  1 
ATOM   7216 H  HG3  . PRO   B 1 183 ? -27.357 -10.239 10.901  1.00 74.82  ? 180 PRO   B HG3  1 
ATOM   7217 H  HD2  . PRO   B 1 183 ? -27.337 -9.238  13.560  1.00 64.53  ? 180 PRO   B HD2  1 
ATOM   7218 H  HD3  . PRO   B 1 183 ? -26.591 -10.538 13.031  1.00 64.53  ? 180 PRO   B HD3  1 
ATOM   7219 N  N    . ALA   B 1 184 ? -24.982 -5.908  10.476  1.00 57.55  ? 181 ALA   B N    1 
ATOM   7220 C  CA   . ALA   B 1 184 ? -24.857 -4.455  10.461  1.00 62.60  ? 181 ALA   B CA   1 
ATOM   7221 C  C    . ALA   B 1 184 ? -26.240 -3.810  10.421  1.00 62.33  ? 181 ALA   B C    1 
ATOM   7222 O  O    . ALA   B 1 184 ? -27.205 -4.389  9.920   1.00 64.94  ? 181 ALA   B O    1 
ATOM   7223 C  CB   . ALA   B 1 184 ? -24.022 -4.005  9.258   1.00 62.87  ? 181 ALA   B CB   1 
ATOM   7224 H  H    . ALA   B 1 184 ? -24.664 -6.298  9.779   1.00 69.10  ? 181 ALA   B H    1 
ATOM   7225 H  HA   . ALA   B 1 184 ? -24.404 -4.156  11.265  1.00 75.16  ? 181 ALA   B HA   1 
ATOM   7226 H  HB1  . ALA   B 1 184 ? -24.324 -3.128  8.974   1.00 75.48  ? 181 ALA   B HB1  1 
ATOM   7227 H  HB2  . ALA   B 1 184 ? -23.088 -3.966  9.518   1.00 75.48  ? 181 ALA   B HB2  1 
ATOM   7228 H  HB3  . ALA   B 1 184 ? -24.138 -4.644  8.537   1.00 75.48  ? 181 ALA   B HB3  1 
ATOM   7229 N  N    . ASP   B 1 185 ? -26.332 -2.589  10.950  1.00 73.59  ? 182 ASP   B N    1 
ATOM   7230 C  CA   . ASP   B 1 185 ? -27.608 -1.889  11.068  1.00 75.83  ? 182 ASP   B CA   1 
ATOM   7231 C  C    . ASP   B 1 185 ? -28.046 -1.204  9.768   1.00 80.15  ? 182 ASP   B C    1 
ATOM   7232 O  O    . ASP   B 1 185 ? -28.977 -0.383  9.801   1.00 75.27  ? 182 ASP   B O    1 
ATOM   7233 C  CB   . ASP   B 1 185 ? -27.535 -0.881  12.228  1.00 85.57  ? 182 ASP   B CB   1 
ATOM   7234 C  CG   . ASP   B 1 185 ? -26.439 0.160   12.051  1.00 85.30  ? 182 ASP   B CG   1 
ATOM   7235 O  OD1  . ASP   B 1 185 ? -25.747 0.137   11.014  1.00 90.06  ? 182 ASP   B OD1  1 
ATOM   7236 O  OD2  . ASP   B 1 185 ? -26.261 0.994   12.966  1.00 92.26  ? 182 ASP   B OD2  1 
ATOM   7237 H  H    . ASP   B 1 185 ? -25.662 -2.142  11.250  1.00 88.36  ? 182 ASP   B H    1 
ATOM   7238 H  HA   . ASP   B 1 185 ? -28.301 -2.531  11.284  1.00 91.04  ? 182 ASP   B HA   1 
ATOM   7239 H  HB2  . ASP   B 1 185 ? -28.382 -0.414  12.292  1.00 102.72 ? 182 ASP   B HB2  1 
ATOM   7240 H  HB3  . ASP   B 1 185 ? -27.358 -1.362  13.051  1.00 102.72 ? 182 ASP   B HB3  1 
ATOM   7241 N  N    . THR   B 1 186 ? -27.432 -1.552  8.631   1.00 68.77  ? 183 THR   B N    1 
ATOM   7242 C  CA   . THR   B 1 186 ? -27.780 -1.002  7.325   1.00 68.92  ? 183 THR   B CA   1 
ATOM   7243 C  C    . THR   B 1 186 ? -27.816 -2.124  6.295   1.00 68.89  ? 183 THR   B C    1 
ATOM   7244 O  O    . THR   B 1 186 ? -26.966 -3.021  6.323   1.00 64.90  ? 183 THR   B O    1 
ATOM   7245 C  CB   . THR   B 1 186 ? -26.760 0.049   6.842   1.00 66.44  ? 183 THR   B CB   1 
ATOM   7246 O  OG1  . THR   B 1 186 ? -25.430 -0.431  7.097   1.00 73.85  ? 183 THR   B OG1  1 
ATOM   7247 C  CG2  . THR   B 1 186 ? -26.963 1.383   7.527   1.00 69.37  ? 183 THR   B CG2  1 
ATOM   7248 H  H    . THR   B 1 186 ? -26.790 -2.124  8.594   1.00 82.56  ? 183 THR   B H    1 
ATOM   7249 H  HA   . THR   B 1 186 ? -28.655 -0.589  7.395   1.00 82.74  ? 183 THR   B HA   1 
ATOM   7250 H  HB   . THR   B 1 186 ? -26.880 0.196   5.891   1.00 79.77  ? 183 THR   B HB   1 
ATOM   7251 H  HG1  . THR   B 1 186 ? -25.370 -1.240  6.877   1.00 88.66  ? 183 THR   B HG1  1 
ATOM   7252 H  HG21 . THR   B 1 186 ? -26.345 2.038   7.168   1.00 83.28  ? 183 THR   B HG21 1 
ATOM   7253 H  HG22 . THR   B 1 186 ? -27.871 1.694   7.384   1.00 83.28  ? 183 THR   B HG22 1 
ATOM   7254 H  HG23 . THR   B 1 186 ? -26.808 1.293   8.480   1.00 83.28  ? 183 THR   B HG23 1 
ATOM   7255 N  N    . GLU   B 1 187 ? -28.771 -2.047  5.362   1.00 57.21  ? 184 GLU   B N    1 
ATOM   7256 C  CA   . GLU   B 1 187 ? -28.785 -2.978  4.237   1.00 61.68  ? 184 GLU   B CA   1 
ATOM   7257 C  C    . GLU   B 1 187 ? -27.424 -3.046  3.549   1.00 62.76  ? 184 GLU   B C    1 
ATOM   7258 O  O    . GLU   B 1 187 ? -26.940 -4.126  3.191   1.00 59.85  ? 184 GLU   B O    1 
ATOM   7259 C  CB   . GLU   B 1 187 ? -29.839 -2.565  3.207   1.00 63.81  ? 184 GLU   B CB   1 
ATOM   7260 C  CG   . GLU   B 1 187 ? -29.442 -3.018  1.801   1.00 72.66  ? 184 GLU   B CG   1 
ATOM   7261 C  CD   . GLU   B 1 187 ? -30.573 -2.963  0.794   1.00 92.89  ? 184 GLU   B CD   1 
ATOM   7262 O  OE1  . GLU   B 1 187 ? -31.718 -2.636  1.184   1.00 92.13  ? 184 GLU   B OE1  1 
ATOM   7263 O  OE2  . GLU   B 1 187 ? -30.301 -3.248  -0.394  1.00 77.82  ? 184 GLU   B OE2  1 
ATOM   7264 H  H    . GLU   B 1 187 ? -29.411 -1.472  5.359   1.00 68.69  ? 184 GLU   B H    1 
ATOM   7265 H  HA   . GLU   B 1 187 ? -29.012 -3.854  4.587   1.00 74.06  ? 184 GLU   B HA   1 
ATOM   7266 H  HB2  . GLU   B 1 187 ? -30.689 -2.974  3.433   1.00 76.62  ? 184 GLU   B HB2  1 
ATOM   7267 H  HB3  . GLU   B 1 187 ? -29.926 -1.599  3.205   1.00 76.62  ? 184 GLU   B HB3  1 
ATOM   7268 H  HG2  . GLU   B 1 187 ? -28.731 -2.443  1.477   1.00 87.24  ? 184 GLU   B HG2  1 
ATOM   7269 H  HG3  . GLU   B 1 187 ? -29.131 -3.936  1.845   1.00 87.24  ? 184 GLU   B HG3  1 
ATOM   7270 N  N    . GLU   B 1 188 ? -26.820 -1.882  3.305   1.00 66.38  ? 185 GLU   B N    1 
ATOM   7271 C  CA   . GLU   B 1 188 ? -25.567 -1.826  2.556   1.00 64.36  ? 185 GLU   B CA   1 
ATOM   7272 C  C    . GLU   B 1 188 ? -24.399 -2.329  3.396   1.00 64.07  ? 185 GLU   B C    1 
ATOM   7273 O  O    . GLU   B 1 188 ? -23.525 -3.051  2.893   1.00 59.62  ? 185 GLU   B O    1 
ATOM   7274 C  CB   . GLU   B 1 188 ? -25.353 -0.388  2.078   1.00 67.07  ? 185 GLU   B CB   1 
ATOM   7275 C  CG   . GLU   B 1 188 ? -26.403 0.034   1.043   1.00 77.20  ? 185 GLU   B CG   1 
ATOM   7276 C  CD   . GLU   B 1 188 ? -26.884 1.470   1.201   1.00 80.97  ? 185 GLU   B CD   1 
ATOM   7277 O  OE1  . GLU   B 1 188 ? -26.427 2.169   2.133   1.00 76.64  ? 185 GLU   B OE1  1 
ATOM   7278 O  OE2  . GLU   B 1 188 ? -27.733 1.895   0.389   1.00 80.45  ? 185 GLU   B OE2  1 
ATOM   7279 H  H    . GLU   B 1 188 ? -27.113 -1.115  3.560   1.00 79.70  ? 185 GLU   B H    1 
ATOM   7280 H  HA   . GLU   B 1 188 ? -25.612 -2.400  1.776   1.00 77.27  ? 185 GLU   B HA   1 
ATOM   7281 H  HB2  . GLU   B 1 188 ? -25.416 0.213   2.837   1.00 80.53  ? 185 GLU   B HB2  1 
ATOM   7282 H  HB3  . GLU   B 1 188 ? -24.477 -0.316  1.669   1.00 80.53  ? 185 GLU   B HB3  1 
ATOM   7283 H  HG2  . GLU   B 1 188 ? -26.019 -0.053  0.157   1.00 92.69  ? 185 GLU   B HG2  1 
ATOM   7284 H  HG3  . GLU   B 1 188 ? -27.175 -0.547  1.128   1.00 92.69  ? 185 GLU   B HG3  1 
ATOM   7285 N  N    . GLY   B 1 189 ? -24.369 -1.974  4.680   1.00 59.12  ? 186 GLY   B N    1 
ATOM   7286 C  CA   . GLY   B 1 189 ? -23.377 -2.554  5.565   1.00 55.57  ? 186 GLY   B CA   1 
ATOM   7287 C  C    . GLY   B 1 189 ? -23.468 -4.065  5.630   1.00 53.90  ? 186 GLY   B C    1 
ATOM   7288 O  O    . GLY   B 1 189 ? -22.457 -4.745  5.791   1.00 56.10  ? 186 GLY   B O    1 
ATOM   7289 H  H    . GLY   B 1 189 ? -24.902 -1.411  5.052   1.00 70.99  ? 186 GLY   B H    1 
ATOM   7290 H  HA2  . GLY   B 1 189 ? -22.491 -2.316  5.252   1.00 66.73  ? 186 GLY   B HA2  1 
ATOM   7291 H  HA3  . GLY   B 1 189 ? -23.502 -2.202  6.460   1.00 66.73  ? 186 GLY   B HA3  1 
ATOM   7292 N  N    . ARG   B 1 190 ? -24.682 -4.607  5.514   1.00 51.04  ? 187 ARG   B N    1 
ATOM   7293 C  CA   . ARG   B 1 190 ? -24.845 -6.055  5.475   1.00 50.48  ? 187 ARG   B CA   1 
ATOM   7294 C  C    . ARG   B 1 190 ? -24.308 -6.634  4.170   1.00 43.33  ? 187 ARG   B C    1 
ATOM   7295 O  O    . ARG   B 1 190 ? -23.710 -7.717  4.173   1.00 49.87  ? 187 ARG   B O    1 
ATOM   7296 C  CB   . ARG   B 1 190 ? -26.323 -6.428  5.664   1.00 48.54  ? 187 ARG   B CB   1 
ATOM   7297 C  CG   . ARG   B 1 190 ? -26.868 -6.157  7.067   1.00 57.76  ? 187 ARG   B CG   1 
ATOM   7298 C  CD   . ARG   B 1 190 ? -28.135 -6.973  7.361   1.00 57.39  ? 187 ARG   B CD   1 
ATOM   7299 N  NE   . ARG   B 1 190 ? -29.305 -6.232  6.910   1.00 53.95  ? 187 ARG   B NE   1 
ATOM   7300 C  CZ   . ARG   B 1 190 ? -29.875 -5.233  7.572   1.00 55.39  ? 187 ARG   B CZ   1 
ATOM   7301 N  NH1  . ARG   B 1 190 ? -29.506 -4.917  8.803   1.00 60.93  ? 187 ARG   B NH1  1 
ATOM   7302 N  NH2  . ARG   B 1 190 ? -30.847 -4.537  6.985   1.00 58.51  ? 187 ARG   B NH2  1 
ATOM   7303 H  H    . ARG   B 1 190 ? -25.416 -4.163  5.457   1.00 61.29  ? 187 ARG   B H    1 
ATOM   7304 H  HA   . ARG   B 1 190 ? -24.343 -6.445  6.208   1.00 60.62  ? 187 ARG   B HA   1 
ATOM   7305 H  HB2  . ARG   B 1 190 ? -26.854 -5.912  5.038   1.00 58.29  ? 187 ARG   B HB2  1 
ATOM   7306 H  HB3  . ARG   B 1 190 ? -26.428 -7.375  5.486   1.00 58.29  ? 187 ARG   B HB3  1 
ATOM   7307 H  HG2  . ARG   B 1 190 ? -26.195 -6.397  7.723   1.00 69.36  ? 187 ARG   B HG2  1 
ATOM   7308 H  HG3  . ARG   B 1 190 ? -27.089 -5.216  7.148   1.00 69.36  ? 187 ARG   B HG3  1 
ATOM   7309 H  HD2  . ARG   B 1 190 ? -28.099 -7.819  6.888   1.00 68.91  ? 187 ARG   B HD2  1 
ATOM   7310 H  HD3  . ARG   B 1 190 ? -28.212 -7.129  8.315   1.00 68.91  ? 187 ARG   B HD3  1 
ATOM   7311 H  HE   . ARG   B 1 190 ? -29.653 -6.459  6.157   1.00 64.78  ? 187 ARG   B HE   1 
ATOM   7312 H  HH11 . ARG   B 1 190 ? -28.883 -5.363  9.194   1.00 73.16  ? 187 ARG   B HH11 1 
ATOM   7313 H  HH12 . ARG   B 1 190 ? -29.890 -4.265  9.213   1.00 73.16  ? 187 ARG   B HH12 1 
ATOM   7314 H  HH21 . ARG   B 1 190 ? -31.097 -4.737  6.187   1.00 70.26  ? 187 ARG   B HH21 1 
ATOM   7315 H  HH22 . ARG   B 1 190 ? -31.224 -3.887  7.403   1.00 70.26  ? 187 ARG   B HH22 1 
ATOM   7316 N  N    . ILE   B 1 191 ? -24.543 -5.950  3.043   1.00 54.46  ? 188 ILE   B N    1 
ATOM   7317 C  CA   . ILE   B 1 191 ? -23.949 -6.387  1.781   1.00 46.62  ? 188 ILE   B CA   1 
ATOM   7318 C  C    . ILE   B 1 191 ? -22.428 -6.464  1.922   1.00 53.24  ? 188 ILE   B C    1 
ATOM   7319 O  O    . ILE   B 1 191 ? -21.797 -7.451  1.527   1.00 48.06  ? 188 ILE   B O    1 
ATOM   7320 C  CB   . ILE   B 1 191 ? -24.357 -5.457  0.622   1.00 49.11  ? 188 ILE   B CB   1 
ATOM   7321 C  CG1  . ILE   B 1 191 ? -25.818 -5.644  0.268   1.00 51.72  ? 188 ILE   B CG1  1 
ATOM   7322 C  CG2  . ILE   B 1 191 ? -23.518 -5.762  -0.625  1.00 50.20  ? 188 ILE   B CG2  1 
ATOM   7323 C  CD1  . ILE   B 1 191 ? -26.386 -4.563  -0.683  1.00 49.96  ? 188 ILE   B CD1  1 
ATOM   7324 H  H    . ILE   B 1 191 ? -25.033 -5.246  2.986   1.00 65.39  ? 188 ILE   B H    1 
ATOM   7325 H  HA   . ILE   B 1 191 ? -24.287 -7.273  1.575   1.00 55.98  ? 188 ILE   B HA   1 
ATOM   7326 H  HB   . ILE   B 1 191 ? -24.207 -4.545  0.916   1.00 58.98  ? 188 ILE   B HB   1 
ATOM   7327 H  HG12 . ILE   B 1 191 ? -25.924 -6.503  -0.169  1.00 62.10  ? 188 ILE   B HG12 1 
ATOM   7328 H  HG13 . ILE   B 1 191 ? -26.341 -5.620  1.084   1.00 62.10  ? 188 ILE   B HG13 1 
ATOM   7329 H  HG21 . ILE   B 1 191 ? -23.903 -5.300  -1.386  1.00 60.29  ? 188 ILE   B HG21 1 
ATOM   7330 H  HG22 . ILE   B 1 191 ? -22.609 -5.456  -0.477  1.00 60.29  ? 188 ILE   B HG22 1 
ATOM   7331 H  HG23 . ILE   B 1 191 ? -23.522 -6.720  -0.782  1.00 60.29  ? 188 ILE   B HG23 1 
ATOM   7332 H  HD11 . ILE   B 1 191 ? -27.345 -4.682  -0.760  1.00 59.99  ? 188 ILE   B HD11 1 
ATOM   7333 H  HD12 . ILE   B 1 191 ? -26.190 -3.686  -0.317  1.00 59.99  ? 188 ILE   B HD12 1 
ATOM   7334 H  HD13 . ILE   B 1 191 ? -25.970 -4.658  -1.554  1.00 59.99  ? 188 ILE   B HD13 1 
ATOM   7335 N  N    . GLU   B 1 192 ? -21.820 -5.420  2.493   1.00 53.83  ? 189 GLU   B N    1 
ATOM   7336 C  CA   . GLU   B 1 192 ? -20.375 -5.405  2.691   1.00 55.10  ? 189 GLU   B CA   1 
ATOM   7337 C  C    . GLU   B 1 192 ? -19.925 -6.539  3.604   1.00 45.12  ? 189 GLU   B C    1 
ATOM   7338 O  O    . GLU   B 1 192 ? -18.877 -7.157  3.374   1.00 40.09  ? 189 GLU   B O    1 
ATOM   7339 C  CB   . GLU   B 1 192 ? -19.952 -4.049  3.268   1.00 50.70  ? 189 GLU   B CB   1 
ATOM   7340 C  CG   . GLU   B 1 192 ? -18.457 -3.888  3.576   1.00 60.90  ? 189 GLU   B CG   1 
ATOM   7341 C  CD   . GLU   B 1 192 ? -17.586 -3.719  2.339   1.00 72.93  ? 189 GLU   B CD   1 
ATOM   7342 O  OE1  . GLU   B 1 192 ? -16.355 -3.556  2.505   1.00 74.02  ? 189 GLU   B OE1  1 
ATOM   7343 O  OE2  . GLU   B 1 192 ? -18.124 -3.742  1.212   1.00 79.14  ? 189 GLU   B OE2  1 
ATOM   7344 H  H    . GLU   B 1 192 ? -22.222 -4.713  2.773   1.00 64.63  ? 189 GLU   B H    1 
ATOM   7345 H  HA   . GLU   B 1 192 ? -19.936 -5.524  1.833   1.00 66.16  ? 189 GLU   B HA   1 
ATOM   7346 H  HB2  . GLU   B 1 192 ? -20.189 -3.360  2.628   1.00 60.88  ? 189 GLU   B HB2  1 
ATOM   7347 H  HB3  . GLU   B 1 192 ? -20.433 -3.910  4.099   1.00 60.88  ? 189 GLU   B HB3  1 
ATOM   7348 H  HG2  . GLU   B 1 192 ? -18.336 -3.101  4.131   1.00 73.12  ? 189 GLU   B HG2  1 
ATOM   7349 H  HG3  . GLU   B 1 192 ? -18.149 -4.677  4.048   1.00 73.12  ? 189 GLU   B HG3  1 
ATOM   7350 N  N    . GLN   B 1 193 ? -20.698 -6.826  4.655   1.00 49.09  ? 190 GLN   B N    1 
ATOM   7351 C  CA   . GLN   B 1 193 ? -20.258 -7.823  5.632   1.00 45.79  ? 190 GLN   B CA   1 
ATOM   7352 C  C    . GLN   B 1 193 ? -20.340 -9.230  5.040   1.00 42.22  ? 190 GLN   B C    1 
ATOM   7353 O  O    . GLN   B 1 193 ? -19.440 -10.061 5.263   1.00 39.57  ? 190 GLN   B O    1 
ATOM   7354 C  CB   . GLN   B 1 193 ? -21.080 -7.670  6.919   1.00 56.08  ? 190 GLN   B CB   1 
ATOM   7355 C  CG   . GLN   B 1 193 ? -21.378 -8.930  7.725   1.00 65.50  ? 190 GLN   B CG   1 
ATOM   7356 C  CD   . GLN   B 1 193 ? -22.628 -8.776  8.606   1.00 85.33  ? 190 GLN   B CD   1 
ATOM   7357 O  OE1  . GLN   B 1 193 ? -23.150 -7.665  8.790   1.00 72.77  ? 190 GLN   B OE1  1 
ATOM   7358 N  NE2  . GLN   B 1 193 ? -23.104 -9.890  9.156   1.00 82.85  ? 190 GLN   B NE2  1 
ATOM   7359 H  H    . GLN   B 1 193 ? -21.462 -6.467  4.821   1.00 58.95  ? 190 GLN   B H    1 
ATOM   7360 H  HA   . GLN   B 1 193 ? -19.330 -7.677  5.874   1.00 54.99  ? 190 GLN   B HA   1 
ATOM   7361 H  HB2  . GLN   B 1 193 ? -20.598 -7.069  7.508   1.00 67.34  ? 190 GLN   B HB2  1 
ATOM   7362 H  HB3  . GLN   B 1 193 ? -21.937 -7.283  6.679   1.00 67.34  ? 190 GLN   B HB3  1 
ATOM   7363 H  HG2  . GLN   B 1 193 ? -21.527 -9.670  7.115   1.00 78.65  ? 190 GLN   B HG2  1 
ATOM   7364 H  HG3  . GLN   B 1 193 ? -20.623 -9.124  8.303   1.00 78.65  ? 190 GLN   B HG3  1 
ATOM   7365 H  HE21 . GLN   B 1 193 ? -22.714 -10.642 9.011   1.00 99.46  ? 190 GLN   B HE21 1 
ATOM   7366 H  HE22 . GLN   B 1 193 ? -23.802 -9.857  9.658   1.00 99.46  ? 190 GLN   B HE22 1 
ATOM   7367 N  N    . TYR   B 1 194 ? -21.384 -9.497  4.250   1.00 40.71  ? 191 TYR   B N    1 
ATOM   7368 C  CA   . TYR   B 1 194 ? -21.461 -10.745 3.503   1.00 40.03  ? 191 TYR   B CA   1 
ATOM   7369 C  C    . TYR   B 1 194 ? -20.294 -10.879 2.522   1.00 42.38  ? 191 TYR   B C    1 
ATOM   7370 O  O    . TYR   B 1 194 ? -19.714 -11.959 2.379   1.00 35.30  ? 191 TYR   B O    1 
ATOM   7371 C  CB   . TYR   B 1 194 ? -22.805 -10.824 2.772   1.00 41.76  ? 191 TYR   B CB   1 
ATOM   7372 C  CG   . TYR   B 1 194 ? -22.740 -11.741 1.582   1.00 41.34  ? 191 TYR   B CG   1 
ATOM   7373 C  CD1  . TYR   B 1 194 ? -22.254 -11.292 0.358   1.00 46.49  ? 191 TYR   B CD1  1 
ATOM   7374 C  CD2  . TYR   B 1 194 ? -23.110 -13.075 1.695   1.00 60.07  ? 191 TYR   B CD2  1 
ATOM   7375 C  CE1  . TYR   B 1 194 ? -22.155 -12.125 -0.710  1.00 45.48  ? 191 TYR   B CE1  1 
ATOM   7376 C  CE2  . TYR   B 1 194 ? -23.022 -13.924 0.621   1.00 55.70  ? 191 TYR   B CE2  1 
ATOM   7377 C  CZ   . TYR   B 1 194 ? -22.538 -13.437 -0.583  1.00 58.77  ? 191 TYR   B CZ   1 
ATOM   7378 O  OH   . TYR   B 1 194 ? -22.433 -14.265 -1.672  1.00 65.31  ? 191 TYR   B OH   1 
ATOM   7379 H  H    . TYR   B 1 194 ? -22.055 -8.973  4.132   1.00 48.89  ? 191 TYR   B H    1 
ATOM   7380 H  HA   . TYR   B 1 194 ? -21.411 -11.492 4.121   1.00 48.07  ? 191 TYR   B HA   1 
ATOM   7381 H  HB2  . TYR   B 1 194 ? -23.480 -11.164 3.381   1.00 50.16  ? 191 TYR   B HB2  1 
ATOM   7382 H  HB3  . TYR   B 1 194 ? -23.053 -9.939  2.462   1.00 50.16  ? 191 TYR   B HB3  1 
ATOM   7383 H  HD1  . TYR   B 1 194 ? -21.992 -10.404 0.269   1.00 55.82  ? 191 TYR   B HD1  1 
ATOM   7384 H  HD2  . TYR   B 1 194 ? -23.421 -13.397 2.510   1.00 72.13  ? 191 TYR   B HD2  1 
ATOM   7385 H  HE1  . TYR   B 1 194 ? -21.830 -11.809 -1.522  1.00 54.62  ? 191 TYR   B HE1  1 
ATOM   7386 H  HE2  . TYR   B 1 194 ? -23.282 -14.814 0.699   1.00 66.89  ? 191 TYR   B HE2  1 
ATOM   7387 H  HH   . TYR   B 1 194 ? -22.659 -15.046 -1.461  1.00 78.41  ? 191 TYR   B HH   1 
ATOM   7388 N  N    . LYS   B 1 195 ? -19.956 -9.795  1.814   1.00 39.75  ? 192 LYS   B N    1 
ATOM   7389 C  CA   . LYS   B 1 195 ? -18.848 -9.829  0.856   1.00 44.12  ? 192 LYS   B CA   1 
ATOM   7390 C  C    . LYS   B 1 195 ? -17.530 -10.185 1.547   1.00 41.95  ? 192 LYS   B C    1 
ATOM   7391 O  O    . LYS   B 1 195 ? -16.728 -10.971 1.028   1.00 34.31  ? 192 LYS   B O    1 
ATOM   7392 C  CB   . LYS   B 1 195 ? -18.731 -8.464  0.169   1.00 47.72  ? 192 LYS   B CB   1 
ATOM   7393 C  CG   . LYS   B 1 195 ? -19.926 -8.039  -0.708  1.00 56.09  ? 192 LYS   B CG   1 
ATOM   7394 C  CD   . LYS   B 1 195 ? -19.639 -8.132  -2.209  1.00 72.24  ? 192 LYS   B CD   1 
ATOM   7395 C  CE   . LYS   B 1 195 ? -19.602 -9.577  -2.701  1.00 69.95  ? 192 LYS   B CE   1 
ATOM   7396 N  NZ   . LYS   B 1 195 ? -18.811 -9.716  -3.963  1.00 60.32  ? 192 LYS   B NZ   1 
ATOM   7397 H  H    . LYS   B 1 195 ? -20.349 -9.032  1.870   1.00 47.74  ? 192 LYS   B H    1 
ATOM   7398 H  HA   . LYS   B 1 195 ? -19.028 -10.505 0.184   1.00 52.99  ? 192 LYS   B HA   1 
ATOM   7399 H  HB2  . LYS   B 1 195 ? -18.626 -7.788  0.856   1.00 57.31  ? 192 LYS   B HB2  1 
ATOM   7400 H  HB3  . LYS   B 1 195 ? -17.948 -8.480  -0.404  1.00 57.31  ? 192 LYS   B HB3  1 
ATOM   7401 H  HG2  . LYS   B 1 195 ? -20.680 -8.617  -0.514  1.00 67.35  ? 192 LYS   B HG2  1 
ATOM   7402 H  HG3  . LYS   B 1 195 ? -20.152 -7.118  -0.505  1.00 67.35  ? 192 LYS   B HG3  1 
ATOM   7403 H  HD2  . LYS   B 1 195 ? -20.337 -7.665  -2.695  1.00 86.73  ? 192 LYS   B HD2  1 
ATOM   7404 H  HD3  . LYS   B 1 195 ? -18.778 -7.727  -2.394  1.00 86.73  ? 192 LYS   B HD3  1 
ATOM   7405 H  HE2  . LYS   B 1 195 ? -19.191 -10.135 -2.022  1.00 83.98  ? 192 LYS   B HE2  1 
ATOM   7406 H  HE3  . LYS   B 1 195 ? -20.508 -9.879  -2.875  1.00 83.98  ? 192 LYS   B HE3  1 
ATOM   7407 H  HZ1  . LYS   B 1 195 ? -18.797 -10.568 -4.222  1.00 72.42  ? 192 LYS   B HZ1  1 
ATOM   7408 H  HZ2  . LYS   B 1 195 ? -19.178 -9.225  -4.608  1.00 72.42  ? 192 LYS   B HZ2  1 
ATOM   7409 H  HZ3  . LYS   B 1 195 ? -17.975 -9.441  -3.831  1.00 72.42  ? 192 LYS   B HZ3  1 
ATOM   7410 N  N    . ARG   B 1 196 ? -17.289 -9.592  2.716   1.00 35.38  ? 193 ARG   B N    1 
ATOM   7411 C  CA   . ARG   B 1 196 ? -16.081 -9.854  3.485   1.00 39.96  ? 193 ARG   B CA   1 
ATOM   7412 C  C    . ARG   B 1 196 ? -16.015 -11.298 3.964   1.00 30.32  ? 193 ARG   B C    1 
ATOM   7413 O  O    . ARG   B 1 196 ? -14.956 -11.944 3.895   1.00 28.35  ? 193 ARG   B O    1 
ATOM   7414 C  CB   . ARG   B 1 196 ? -16.057 -8.888  4.660   1.00 42.93  ? 193 ARG   B CB   1 
ATOM   7415 C  CG   . ARG   B 1 196 ? -14.762 -8.806  5.382   1.00 42.00  ? 193 ARG   B CG   1 
ATOM   7416 C  CD   . ARG   B 1 196 ? -14.879 -7.741  6.474   1.00 46.97  ? 193 ARG   B CD   1 
ATOM   7417 N  NE   . ARG   B 1 196 ? -15.987 -7.969  7.405   1.00 58.73  ? 193 ARG   B NE   1 
ATOM   7418 C  CZ   . ARG   B 1 196 ? -16.359 -9.139  7.913   1.00 64.84  ? 193 ARG   B CZ   1 
ATOM   7419 N  NH1  . ARG   B 1 196 ? -15.586 -10.212 7.829   1.00 63.79  ? 193 ARG   B NH1  1 
ATOM   7420 N  NH2  . ARG   B 1 196 ? -17.528 -9.232  8.539   1.00 68.00  ? 193 ARG   B NH2  1 
ATOM   7421 H  H    . ARG   B 1 196 ? -17.818 -9.026  3.090   1.00 42.50  ? 193 ARG   B H    1 
ATOM   7422 H  HA   . ARG   B 1 196 ? -15.298 -9.711  2.932   1.00 48.00  ? 193 ARG   B HA   1 
ATOM   7423 H  HB2  . ARG   B 1 196 ? -16.262 -8.000  4.330   1.00 51.56  ? 193 ARG   B HB2  1 
ATOM   7424 H  HB3  . ARG   B 1 196 ? -16.729 -9.168  5.301   1.00 51.56  ? 193 ARG   B HB3  1 
ATOM   7425 H  HG2  . ARG   B 1 196 ? -14.556 -9.661  5.793   1.00 50.44  ? 193 ARG   B HG2  1 
ATOM   7426 H  HG3  . ARG   B 1 196 ? -14.055 -8.555  4.768   1.00 50.44  ? 193 ARG   B HG3  1 
ATOM   7427 H  HD2  . ARG   B 1 196 ? -14.058 -7.731  6.990   1.00 56.40  ? 193 ARG   B HD2  1 
ATOM   7428 H  HD3  . ARG   B 1 196 ? -15.018 -6.878  6.055   1.00 56.40  ? 193 ARG   B HD3  1 
ATOM   7429 H  HE   . ARG   B 1 196 ? -16.440 -7.279  7.645   1.00 70.51  ? 193 ARG   B HE   1 
ATOM   7430 H  HH11 . ARG   B 1 196 ? -14.822 -10.162 7.438   1.00 76.59  ? 193 ARG   B HH11 1 
ATOM   7431 H  HH12 . ARG   B 1 196 ? -15.849 -10.958 8.166   1.00 76.59  ? 193 ARG   B HH12 1 
ATOM   7432 H  HH21 . ARG   B 1 196 ? -18.034 -8.540  8.612   1.00 81.64  ? 193 ARG   B HH21 1 
ATOM   7433 H  HH22 . ARG   B 1 196 ? -17.779 -9.984  8.872   1.00 81.64  ? 193 ARG   B HH22 1 
ATOM   7434 N  N    . THR   B 1 197 ? -17.145 -11.836 4.441   1.00 31.30  ? 194 THR   B N    1 
ATOM   7435 C  CA   . THR   B 1 197 ? -17.138 -13.229 4.870   1.00 32.35  ? 194 THR   B CA   1 
ATOM   7436 C  C    . THR   B 1 197 ? -16.911 -14.152 3.688   1.00 25.46  ? 194 THR   B C    1 
ATOM   7437 O  O    . THR   B 1 197 ? -16.148 -15.131 3.798   1.00 25.08  ? 194 THR   B O    1 
ATOM   7438 C  CB   . THR   B 1 197 ? -18.459 -13.585 5.568   1.00 30.12  ? 194 THR   B CB   1 
ATOM   7439 O  OG1  . THR   B 1 197 ? -18.654 -12.686 6.655   1.00 41.28  ? 194 THR   B OG1  1 
ATOM   7440 C  CG2  . THR   B 1 197 ? -18.385 -14.985 6.114   1.00 38.41  ? 194 THR   B CG2  1 
ATOM   7441 H  H    . THR   B 1 197 ? -17.898 -11.428 4.521   1.00 37.60  ? 194 THR   B H    1 
ATOM   7442 H  HA   . THR   B 1 197 ? -16.419 -13.354 5.510   1.00 38.86  ? 194 THR   B HA   1 
ATOM   7443 H  HB   . THR   B 1 197 ? -19.197 -13.525 4.942   1.00 36.18  ? 194 THR   B HB   1 
ATOM   7444 H  HG1  . THR   B 1 197 ? -18.837 -11.919 6.365   1.00 49.58  ? 194 THR   B HG1  1 
ATOM   7445 H  HG21 . THR   B 1 197 ? -19.253 -15.257 6.451   1.00 46.13  ? 194 THR   B HG21 1 
ATOM   7446 H  HG22 . THR   B 1 197 ? -18.112 -15.600 5.415   1.00 46.13  ? 194 THR   B HG22 1 
ATOM   7447 H  HG23 . THR   B 1 197 ? -17.740 -15.026 6.838   1.00 46.13  ? 194 THR   B HG23 1 
ATOM   7448 N  N    . MET   B 1 198 ? -17.563 -13.855 2.566   1.00 27.26  ? 195 MET   B N    1 
ATOM   7449 C  CA   . MET   B 1 198 ? -17.397 -14.653 1.351   1.00 25.42  ? 195 MET   B CA   1 
ATOM   7450 C  C    . MET   B 1 198 ? -15.944 -14.608 0.884   1.00 25.22  ? 195 MET   B C    1 
ATOM   7451 O  O    . MET   B 1 198 ? -15.387 -15.625 0.458   1.00 25.19  ? 195 MET   B O    1 
ATOM   7452 C  CB   . MET   B 1 198 ? -18.296 -14.137 0.240   1.00 30.56  ? 195 MET   B CB   1 
ATOM   7453 C  CG   . MET   B 1 198 ? -19.759 -14.559 0.364   1.00 40.26  ? 195 MET   B CG   1 
ATOM   7454 S  SD   . MET   B 1 198 ? -20.020 -16.309 0.789   1.00 45.79  ? 195 MET   B SD   1 
ATOM   7455 C  CE   . MET   B 1 198 ? -19.204 -17.011 -0.646  1.00 55.59  ? 195 MET   B CE   1 
ATOM   7456 H  H    . MET   B 1 198 ? -18.109 -13.196 2.479   1.00 32.75  ? 195 MET   B H    1 
ATOM   7457 H  HA   . MET   B 1 198 ? -17.662 -15.565 1.550   1.00 30.55  ? 195 MET   B HA   1 
ATOM   7458 H  HB2  . MET   B 1 198 ? -18.268 -13.168 0.245   1.00 36.71  ? 195 MET   B HB2  1 
ATOM   7459 H  HB3  . MET   B 1 198 ? -17.964 -14.474 -0.607  1.00 36.71  ? 195 MET   B HB3  1 
ATOM   7460 H  HG2  . MET   B 1 198 ? -20.175 -14.026 1.059   1.00 48.35  ? 195 MET   B HG2  1 
ATOM   7461 H  HG3  . MET   B 1 198 ? -20.199 -14.397 -0.486  1.00 48.35  ? 195 MET   B HG3  1 
ATOM   7462 H  HE1  . MET   B 1 198 ? -19.271 -17.978 -0.606  1.00 66.75  ? 195 MET   B HE1  1 
ATOM   7463 H  HE2  . MET   B 1 198 ? -19.638 -16.682 -1.449  1.00 66.75  ? 195 MET   B HE2  1 
ATOM   7464 H  HE3  . MET   B 1 198 ? -18.271 -16.743 -0.642  1.00 66.75  ? 195 MET   B HE3  1 
ATOM   7465 N  N    . PHE   B 1 199 ? -15.302 -13.439 0.993   1.00 25.62  ? 196 PHE   B N    1 
ATOM   7466 C  CA   . PHE   B 1 199 ? -13.888 -13.336 0.609   1.00 22.70  ? 196 PHE   B CA   1 
ATOM   7467 C  C    . PHE   B 1 199 ? -13.011 -14.181 1.520   1.00 23.97  ? 196 PHE   B C    1 
ATOM   7468 O  O    . PHE   B 1 199 ? -12.153 -14.946 1.061   1.00 22.83  ? 196 PHE   B O    1 
ATOM   7469 C  CB   . PHE   B 1 199 ? -13.446 -11.861 0.627   1.00 23.31  ? 196 PHE   B CB   1 
ATOM   7470 C  CG   . PHE   B 1 199 ? -12.018 -11.689 0.231   1.00 22.15  ? 196 PHE   B CG   1 
ATOM   7471 C  CD1  . PHE   B 1 199 ? -11.662 -11.679 -1.103  1.00 23.37  ? 196 PHE   B CD1  1 
ATOM   7472 C  CD2  . PHE   B 1 199 ? -11.035 -11.593 1.191   1.00 26.21  ? 196 PHE   B CD2  1 
ATOM   7473 C  CE1  . PHE   B 1 199 ? -10.296 -11.587 -1.453  1.00 27.81  ? 196 PHE   B CE1  1 
ATOM   7474 C  CE2  . PHE   B 1 199 ? -9.685  -11.500 0.836   1.00 24.07  ? 196 PHE   B CE2  1 
ATOM   7475 C  CZ   . PHE   B 1 199 ? -9.346  -11.480 -0.474  1.00 22.74  ? 196 PHE   B CZ   1 
ATOM   7476 H  H    . PHE   B 1 199 ? -15.653 -12.708 1.279   1.00 30.78  ? 196 PHE   B H    1 
ATOM   7477 H  HA   . PHE   B 1 199 ? -13.781 -13.668 -0.296  1.00 27.28  ? 196 PHE   B HA   1 
ATOM   7478 H  HB2  . PHE   B 1 199 ? -13.994 -11.358 0.004   1.00 28.02  ? 196 PHE   B HB2  1 
ATOM   7479 H  HB3  . PHE   B 1 199 ? -13.555 -11.508 1.524   1.00 28.02  ? 196 PHE   B HB3  1 
ATOM   7480 H  HD1  . PHE   B 1 199 ? -12.314 -11.731 -1.764  1.00 28.09  ? 196 PHE   B HD1  1 
ATOM   7481 H  HD2  . PHE   B 1 199 ? -11.273 -11.590 2.090   1.00 31.49  ? 196 PHE   B HD2  1 
ATOM   7482 H  HE1  . PHE   B 1 199 ? -10.043 -11.599 -2.348  1.00 33.42  ? 196 PHE   B HE1  1 
ATOM   7483 H  HE2  . PHE   B 1 199 ? -9.028  -11.453 1.493   1.00 28.92  ? 196 PHE   B HE2  1 
ATOM   7484 H  HZ   . PHE   B 1 199 ? -8.452  -11.392 -0.713  1.00 27.32  ? 196 PHE   B HZ   1 
ATOM   7485 N  N    . TRP   B 1 200 ? -13.206 -14.061 2.823   1.00 19.52  ? 197 TRP   B N    1 
ATOM   7486 C  CA   . TRP   B 1 200 ? -12.418 -14.821 3.776   1.00 19.79  ? 197 TRP   B CA   1 
ATOM   7487 C  C    . TRP   B 1 200 ? -12.614 -16.321 3.561   1.00 21.69  ? 197 TRP   B C    1 
ATOM   7488 O  O    . TRP   B 1 200 ? -11.648 -17.104 3.628   1.00 20.35  ? 197 TRP   B O    1 
ATOM   7489 C  CB   . TRP   B 1 200 ? -12.797 -14.374 5.199   1.00 23.55  ? 197 TRP   B CB   1 
ATOM   7490 C  CG   . TRP   B 1 200 ? -12.361 -15.275 6.300   1.00 23.88  ? 197 TRP   B CG   1 
ATOM   7491 C  CD1  . TRP   B 1 200 ? -11.152 -15.280 6.958   1.00 25.75  ? 197 TRP   B CD1  1 
ATOM   7492 C  CD2  . TRP   B 1 200 ? -13.160 -16.308 6.908   1.00 23.26  ? 197 TRP   B CD2  1 
ATOM   7493 N  NE1  . TRP   B 1 200 ? -11.162 -16.257 7.916   1.00 28.39  ? 197 TRP   B NE1  1 
ATOM   7494 C  CE2  . TRP   B 1 200 ? -12.371 -16.900 7.909   1.00 32.61  ? 197 TRP   B CE2  1 
ATOM   7495 C  CE3  . TRP   B 1 200 ? -14.457 -16.769 6.706   1.00 28.05  ? 197 TRP   B CE3  1 
ATOM   7496 C  CZ2  . TRP   B 1 200 ? -12.838 -17.943 8.699   1.00 28.74  ? 197 TRP   B CZ2  1 
ATOM   7497 C  CZ3  . TRP   B 1 200 ? -14.920 -17.815 7.486   1.00 35.47  ? 197 TRP   B CZ3  1 
ATOM   7498 C  CH2  . TRP   B 1 200 ? -14.099 -18.392 8.466   1.00 32.01  ? 197 TRP   B CH2  1 
ATOM   7499 H  H    . TRP   B 1 200 ? -13.791 -13.544 3.184   1.00 23.47  ? 197 TRP   B H    1 
ATOM   7500 H  HA   . TRP   B 1 200 ? -11.471 -14.644 3.659   1.00 23.79  ? 197 TRP   B HA   1 
ATOM   7501 H  HB2  . TRP   B 1 200 ? -12.395 -13.507 5.363   1.00 28.31  ? 197 TRP   B HB2  1 
ATOM   7502 H  HB3  . TRP   B 1 200 ? -13.763 -14.306 5.249   1.00 28.31  ? 197 TRP   B HB3  1 
ATOM   7503 H  HD1  . TRP   B 1 200 ? -10.440 -14.709 6.779   1.00 30.94  ? 197 TRP   B HD1  1 
ATOM   7504 H  HE1  . TRP   B 1 200 ? -10.508 -16.439 8.444   1.00 34.11  ? 197 TRP   B HE1  1 
ATOM   7505 H  HE3  . TRP   B 1 200 ? -15.003 -16.382 6.060   1.00 33.70  ? 197 TRP   B HE3  1 
ATOM   7506 H  HZ2  . TRP   B 1 200 ? -12.307 -18.319 9.363   1.00 34.53  ? 197 TRP   B HZ2  1 
ATOM   7507 H  HZ3  . TRP   B 1 200 ? -15.783 -18.138 7.359   1.00 42.60  ? 197 TRP   B HZ3  1 
ATOM   7508 H  HH2  . TRP   B 1 200 ? -14.426 -19.102 8.970   1.00 38.45  ? 197 TRP   B HH2  1 
ATOM   7509 N  N    . LEU   B 1 201 ? -13.859 -16.734 3.295   1.00 21.21  ? 198 LEU   B N    1 
ATOM   7510 C  CA   . LEU   B 1 201 ? -14.138 -18.147 3.053   1.00 21.69  ? 198 LEU   B CA   1 
ATOM   7511 C  C    . LEU   B 1 201 ? -13.360 -18.672 1.846   1.00 20.87  ? 198 LEU   B C    1 
ATOM   7512 O  O    . LEU   B 1 201 ? -12.760 -19.748 1.909   1.00 24.79  ? 198 LEU   B O    1 
ATOM   7513 C  CB   . LEU   B 1 201 ? -15.641 -18.349 2.822   1.00 24.85  ? 198 LEU   B CB   1 
ATOM   7514 C  CG   . LEU   B 1 201 ? -16.377 -19.522 3.435   1.00 41.64  ? 198 LEU   B CG   1 
ATOM   7515 C  CD1  . LEU   B 1 201 ? -16.142 -19.689 4.896   1.00 37.05  ? 198 LEU   B CD1  1 
ATOM   7516 C  CD2  . LEU   B 1 201 ? -17.867 -19.246 3.127   1.00 42.61  ? 198 LEU   B CD2  1 
ATOM   7517 H  H    . LEU   B 1 201 ? -14.548 -16.221 3.250   1.00 25.49  ? 198 LEU   B H    1 
ATOM   7518 H  HA   . LEU   B 1 201 ? -13.866 -18.649 3.837   1.00 26.07  ? 198 LEU   B HA   1 
ATOM   7519 H  HB2  . LEU   B 1 201 ? -16.086 -17.554 3.154   1.00 29.86  ? 198 LEU   B HB2  1 
ATOM   7520 H  HB3  . LEU   B 1 201 ? -15.771 -18.427 1.864   1.00 29.86  ? 198 LEU   B HB3  1 
ATOM   7521 H  HG   . LEU   B 1 201 ? -16.066 -20.363 3.066   1.00 50.01  ? 198 LEU   B HG   1 
ATOM   7522 H  HD11 . LEU   B 1 201 ? -16.687 -20.421 5.222   1.00 44.50  ? 198 LEU   B HD11 1 
ATOM   7523 H  HD12 . LEU   B 1 201 ? -15.203 -19.885 5.043   1.00 44.50  ? 198 LEU   B HD12 1 
ATOM   7524 H  HD13 . LEU   B 1 201 ? -16.384 -18.867 5.351   1.00 44.50  ? 198 LEU   B HD13 1 
ATOM   7525 H  HD21 . LEU   B 1 201 ? -18.393 -20.013 3.403   1.00 51.17  ? 198 LEU   B HD21 1 
ATOM   7526 H  HD22 . LEU   B 1 201 ? -18.150 -18.457 3.616   1.00 51.17  ? 198 LEU   B HD22 1 
ATOM   7527 H  HD23 . LEU   B 1 201 ? -17.970 -19.100 2.174   1.00 51.17  ? 198 LEU   B HD23 1 
ATOM   7528 N  N    . GLU   B 1 202 ? -13.343 -17.932 0.754   1.00 23.46  ? 199 GLU   B N    1 
ATOM   7529 C  CA   . GLU   B 1 202 ? -12.756 -18.467 -0.471  1.00 22.49  ? 199 GLU   B CA   1 
ATOM   7530 C  C    . GLU   B 1 202 ? -11.255 -18.255 -0.511  1.00 22.57  ? 199 GLU   B C    1 
ATOM   7531 O  O    . GLU   B 1 202 ? -10.521 -19.156 -0.958  1.00 23.68  ? 199 GLU   B O    1 
ATOM   7532 C  CB   . GLU   B 1 202 ? -13.422 -17.851 -1.691  1.00 25.53  ? 199 GLU   B CB   1 
ATOM   7533 C  CG   . GLU   B 1 202 ? -12.812 -18.257 -3.023  1.00 31.96  ? 199 GLU   B CG   1 
ATOM   7534 C  CD   . GLU   B 1 202 ? -13.494 -17.591 -4.226  1.00 44.18  ? 199 GLU   B CD   1 
ATOM   7535 O  OE1  . GLU   B 1 202 ? -13.111 -17.921 -5.378  1.00 46.23  ? 199 GLU   B OE1  1 
ATOM   7536 O  OE2  . GLU   B 1 202 ? -14.421 -16.770 -4.031  1.00 44.25  ? 199 GLU   B OE2  1 
ATOM   7537 H  H    . GLU   B 1 202 ? -13.656 -17.133 0.692   1.00 28.19  ? 199 GLU   B H    1 
ATOM   7538 H  HA   . GLU   B 1 202 ? -12.922 -19.422 -0.524  1.00 27.02  ? 199 GLU   B HA   1 
ATOM   7539 H  HB2  . GLU   B 1 202 ? -14.354 -18.119 -1.702  1.00 30.67  ? 199 GLU   B HB2  1 
ATOM   7540 H  HB3  . GLU   B 1 202 ? -13.356 -16.885 -1.622  1.00 30.67  ? 199 GLU   B HB3  1 
ATOM   7541 H  HG2  . GLU   B 1 202 ? -11.876 -18.003 -3.031  1.00 38.40  ? 199 GLU   B HG2  1 
ATOM   7542 H  HG3  . GLU   B 1 202 ? -12.896 -19.218 -3.127  1.00 38.40  ? 199 GLU   B HG3  1 
ATOM   7543 N  N    . PHE   B 1 203 ? -10.768 -17.141 0.058   1.00 19.92  ? 200 PHE   B N    1 
ATOM   7544 C  CA   . PHE   B 1 203 ? -9.396  -16.714 -0.173  1.00 17.32  ? 200 PHE   B CA   1 
ATOM   7545 C  C    . PHE   B 1 203 ? -8.513  -16.731 1.059   1.00 17.68  ? 200 PHE   B C    1 
ATOM   7546 O  O    . PHE   B 1 203 ? -7.296  -16.513 0.913   1.00 19.41  ? 200 PHE   B O    1 
ATOM   7547 C  CB   . PHE   B 1 203 ? -9.387  -15.296 -0.782  1.00 20.19  ? 200 PHE   B CB   1 
ATOM   7548 C  CG   . PHE   B 1 203 ? -9.938  -15.233 -2.162  1.00 23.47  ? 200 PHE   B CG   1 
ATOM   7549 C  CD1  . PHE   B 1 203 ? -9.123  -15.536 -3.237  1.00 22.80  ? 200 PHE   B CD1  1 
ATOM   7550 C  CD2  . PHE   B 1 203 ? -11.251 -14.921 -2.394  1.00 24.57  ? 200 PHE   B CD2  1 
ATOM   7551 C  CE1  . PHE   B 1 203 ? -9.628  -15.514 -4.521  1.00 28.75  ? 200 PHE   B CE1  1 
ATOM   7552 C  CE2  . PHE   B 1 203 ? -11.763 -14.917 -3.682  1.00 26.38  ? 200 PHE   B CE2  1 
ATOM   7553 C  CZ   . PHE   B 1 203 ? -10.942 -15.213 -4.732  1.00 30.06  ? 200 PHE   B CZ   1 
ATOM   7554 H  H    . PHE   B 1 203 ? -11.218 -16.623 0.578   1.00 23.95  ? 200 PHE   B H    1 
ATOM   7555 H  HA   . PHE   B 1 203 ? -8.995  -17.327 -0.809  1.00 20.82  ? 200 PHE   B HA   1 
ATOM   7556 H  HB2  . PHE   B 1 203 ? -9.923  -14.712 -0.222  1.00 24.26  ? 200 PHE   B HB2  1 
ATOM   7557 H  HB3  . PHE   B 1 203 ? -8.472  -14.975 -0.813  1.00 24.26  ? 200 PHE   B HB3  1 
ATOM   7558 H  HD1  . PHE   B 1 203 ? -8.230  -15.755 -3.094  1.00 27.40  ? 200 PHE   B HD1  1 
ATOM   7559 H  HD2  . PHE   B 1 203 ? -11.806 -14.709 -1.678  1.00 29.53  ? 200 PHE   B HD2  1 
ATOM   7560 H  HE1  . PHE   B 1 203 ? -9.073  -15.704 -5.242  1.00 34.54  ? 200 PHE   B HE1  1 
ATOM   7561 H  HE2  . PHE   B 1 203 ? -12.659 -14.715 -3.830  1.00 31.70  ? 200 PHE   B HE2  1 
ATOM   7562 H  HZ   . PHE   B 1 203 ? -11.280 -15.209 -5.598  1.00 36.11  ? 200 PHE   B HZ   1 
ATOM   7563 N  N    . GLU   B 1 204 ? -9.065  -16.971 2.258   1.00 17.40  ? 201 GLU   B N    1 
ATOM   7564 C  CA   . GLU   B 1 204 ? -8.256  -16.905 3.467   1.00 15.94  ? 201 GLU   B CA   1 
ATOM   7565 C  C    . GLU   B 1 204 ? -8.267  -18.151 4.344   1.00 17.22  ? 201 GLU   B C    1 
ATOM   7566 O  O    . GLU   B 1 204 ? -7.194  -18.628 4.714   1.00 18.35  ? 201 GLU   B O    1 
ATOM   7567 C  CB   . GLU   B 1 204 ? -8.679  -15.688 4.307   1.00 17.52  ? 201 GLU   B CB   1 
ATOM   7568 C  CG   . GLU   B 1 204 ? -7.765  -15.364 5.484   1.00 19.49  ? 201 GLU   B CG   1 
ATOM   7569 C  CD   . GLU   B 1 204 ? -7.693  -13.885 5.810   1.00 19.62  ? 201 GLU   B CD   1 
ATOM   7570 O  OE1  . GLU   B 1 204 ? -7.422  -13.060 4.926   1.00 19.37  ? 201 GLU   B OE1  1 
ATOM   7571 O  OE2  . GLU   B 1 204 ? -7.987  -13.537 6.986   1.00 22.45  ? 201 GLU   B OE2  1 
ATOM   7572 H  H    . GLU   B 1 204 ? -9.892  -17.170 2.386   1.00 20.92  ? 201 GLU   B H    1 
ATOM   7573 H  HA   . GLU   B 1 204 ? -7.338  -16.802 3.173   1.00 19.18  ? 201 GLU   B HA   1 
ATOM   7574 H  HB2  . GLU   B 1 204 ? -8.696  -14.908 3.730   1.00 21.07  ? 201 GLU   B HB2  1 
ATOM   7575 H  HB3  . GLU   B 1 204 ? -9.565  -15.855 4.665   1.00 21.07  ? 201 GLU   B HB3  1 
ATOM   7576 H  HG2  . GLU   B 1 204 ? -8.094  -15.825 6.271   1.00 23.43  ? 201 GLU   B HG2  1 
ATOM   7577 H  HG3  . GLU   B 1 204 ? -6.867  -15.664 5.275   1.00 23.43  ? 201 GLU   B HG3  1 
ATOM   7578 N  N    . ILE   B 1 205 ? -9.421  -18.692 4.710   1.00 16.82  ? 202 ILE   B N    1 
ATOM   7579 C  CA   . ILE   B 1 205 ? -9.429  -19.693 5.777   1.00 18.66  ? 202 ILE   B CA   1 
ATOM   7580 C  C    . ILE   B 1 205 ? -8.560  -20.902 5.420   1.00 18.52  ? 202 ILE   B C    1 
ATOM   7581 O  O    . ILE   B 1 205 ? -7.685  -21.288 6.201   1.00 19.47  ? 202 ILE   B O    1 
ATOM   7582 C  CB   . ILE   B 1 205 ? -10.858 -20.107 6.167   1.00 21.28  ? 202 ILE   B CB   1 
ATOM   7583 C  CG1  . ILE   B 1 205 ? -10.779 -21.134 7.310   1.00 21.23  ? 202 ILE   B CG1  1 
ATOM   7584 C  CG2  . ILE   B 1 205 ? -11.657 -20.662 5.012   1.00 24.41  ? 202 ILE   B CG2  1 
ATOM   7585 C  CD1  . ILE   B 1 205 ? -12.081 -21.523 7.880   1.00 32.97  ? 202 ILE   B CD1  1 
ATOM   7586 H  H    . ILE   B 1 205 ? -10.189 -18.506 4.371   1.00 20.23  ? 202 ILE   B H    1 
ATOM   7587 H  HA   . ILE   B 1 205 ? -9.033  -19.273 6.556   1.00 22.43  ? 202 ILE   B HA   1 
ATOM   7588 H  HB   . ILE   B 1 205 ? -11.326 -19.307 6.454   1.00 25.58  ? 202 ILE   B HB   1 
ATOM   7589 H  HG12 . ILE   B 1 205 ? -10.356 -21.939 6.973   1.00 25.52  ? 202 ILE   B HG12 1 
ATOM   7590 H  HG13 . ILE   B 1 205 ? -10.248 -20.755 8.028   1.00 25.52  ? 202 ILE   B HG13 1 
ATOM   7591 H  HG21 . ILE   B 1 205 ? -12.582 -20.759 5.287   1.00 29.33  ? 202 ILE   B HG21 1 
ATOM   7592 H  HG22 . ILE   B 1 205 ? -11.597 -20.048 4.263   1.00 29.33  ? 202 ILE   B HG22 1 
ATOM   7593 H  HG23 . ILE   B 1 205 ? -11.293 -21.525 4.763   1.00 29.33  ? 202 ILE   B HG23 1 
ATOM   7594 H  HD11 . ILE   B 1 205 ? -11.931 -22.068 8.668   1.00 39.60  ? 202 ILE   B HD11 1 
ATOM   7595 H  HD12 . ILE   B 1 205 ? -12.572 -20.722 8.121   1.00 39.60  ? 202 ILE   B HD12 1 
ATOM   7596 H  HD13 . ILE   B 1 205 ? -12.577 -22.029 7.218   1.00 39.60  ? 202 ILE   B HD13 1 
ATOM   7597 N  N    . ARG   B 1 206 ? -8.782  -21.507 4.241   1.00 17.95  ? 203 ARG   B N    1 
ATOM   7598 C  CA   . ARG   B 1 206 ? -8.017  -22.714 3.902   1.00 18.18  ? 203 ARG   B CA   1 
ATOM   7599 C  C    . ARG   B 1 206 ? -6.538  -22.377 3.722   1.00 18.85  ? 203 ARG   B C    1 
ATOM   7600 O  O    . ARG   B 1 206 ? -5.653  -23.061 4.245   1.00 18.71  ? 203 ARG   B O    1 
ATOM   7601 C  CB   . ARG   B 1 206 ? -8.577  -23.368 2.637   1.00 19.14  ? 203 ARG   B CB   1 
ATOM   7602 C  CG   . ARG   B 1 206 ? -9.974  -23.937 2.790   1.00 20.50  ? 203 ARG   B CG   1 
ATOM   7603 C  CD   . ARG   B 1 206 ? -10.611 -24.315 1.478   1.00 20.01  ? 203 ARG   B CD   1 
ATOM   7604 N  NE   . ARG   B 1 206 ? -10.752 -23.156 0.606   1.00 22.19  ? 203 ARG   B NE   1 
ATOM   7605 C  CZ   . ARG   B 1 206 ? -11.202 -23.184 -0.637  1.00 22.38  ? 203 ARG   B CZ   1 
ATOM   7606 N  NH1  . ARG   B 1 206 ? -11.584 -24.323 -1.223  1.00 24.81  ? 203 ARG   B NH1  1 
ATOM   7607 N  NH2  . ARG   B 1 206 ? -11.257 -22.049 -1.337  1.00 23.63  ? 203 ARG   B NH2  1 
ATOM   7608 H  H    . ARG   B 1 206 ? -9.347  -21.249 3.646   1.00 21.58  ? 203 ARG   B H    1 
ATOM   7609 H  HA   . ARG   B 1 206 ? -8.106  -23.354 4.626   1.00 21.86  ? 203 ARG   B HA   1 
ATOM   7610 H  HB2  . ARG   B 1 206 ? -8.606  -22.703 1.932   1.00 23.01  ? 203 ARG   B HB2  1 
ATOM   7611 H  HB3  . ARG   B 1 206 ? -7.990  -24.097 2.380   1.00 23.01  ? 203 ARG   B HB3  1 
ATOM   7612 H  HG2  . ARG   B 1 206 ? -9.931  -24.734 3.340   1.00 24.64  ? 203 ARG   B HG2  1 
ATOM   7613 H  HG3  . ARG   B 1 206 ? -10.539 -23.271 3.213   1.00 24.64  ? 203 ARG   B HG3  1 
ATOM   7614 H  HD2  . ARG   B 1 206 ? -10.056 -24.971 1.028   1.00 24.05  ? 203 ARG   B HD2  1 
ATOM   7615 H  HD3  . ARG   B 1 206 ? -11.493 -24.684 1.642   1.00 24.05  ? 203 ARG   B HD3  1 
ATOM   7616 H  HE   . ARG   B 1 206 ? -10.524 -22.391 0.926   1.00 26.67  ? 203 ARG   B HE   1 
ATOM   7617 H  HH11 . ARG   B 1 206 ? -11.541 -25.065 -0.789  1.00 29.82  ? 203 ARG   B HH11 1 
ATOM   7618 H  HH12 . ARG   B 1 206 ? -11.873 -24.315 -2.033  1.00 29.82  ? 203 ARG   B HH12 1 
ATOM   7619 H  HH21 . ARG   B 1 206 ? -11.001 -21.310 -0.980  1.00 28.40  ? 203 ARG   B HH21 1 
ATOM   7620 H  HH22 . ARG   B 1 206 ? -11.548 -22.057 -2.147  1.00 28.40  ? 203 ARG   B HH22 1 
ATOM   7621 N  N    . GLN   B 1 207 ? -6.260  -21.317 2.980   1.00 18.10  ? 204 GLN   B N    1 
ATOM   7622 C  CA   . GLN   B 1 207 ? -4.891  -20.969 2.617   1.00 17.48  ? 204 GLN   B CA   1 
ATOM   7623 C  C    . GLN   B 1 207 ? -4.067  -20.608 3.840   1.00 17.95  ? 204 GLN   B C    1 
ATOM   7624 O  O    . GLN   B 1 207 ? -2.866  -20.909 3.903   1.00 20.63  ? 204 GLN   B O    1 
ATOM   7625 C  CB   . GLN   B 1 207 ? -4.919  -19.801 1.630   1.00 18.78  ? 204 GLN   B CB   1 
ATOM   7626 C  CG   . GLN   B 1 207 ? -5.559  -20.078 0.254   1.00 17.48  ? 204 GLN   B CG   1 
ATOM   7627 C  CD   . GLN   B 1 207 ? -7.056  -19.884 0.200   1.00 18.34  ? 204 GLN   B CD   1 
ATOM   7628 O  OE1  . GLN   B 1 207 ? -7.716  -19.744 1.229   1.00 18.12  ? 204 GLN   B OE1  1 
ATOM   7629 N  NE2  . GLN   B 1 207 ? -7.611  -19.876 -0.998  1.00 20.45  ? 204 GLN   B NE2  1 
ATOM   7630 H  H    . GLN   B 1 207 ? -6.849  -20.773 2.669   1.00 21.76  ? 204 GLN   B H    1 
ATOM   7631 H  HA   . GLN   B 1 207 ? -4.468  -21.732 2.192   1.00 21.02  ? 204 GLN   B HA   1 
ATOM   7632 H  HB2  . GLN   B 1 207 ? -5.421  -19.076 2.036   1.00 22.58  ? 204 GLN   B HB2  1 
ATOM   7633 H  HB3  . GLN   B 1 207 ? -4.005  -19.521 1.468   1.00 22.58  ? 204 GLN   B HB3  1 
ATOM   7634 H  HG2  . GLN   B 1 207 ? -5.164  -19.476 -0.396  1.00 21.02  ? 204 GLN   B HG2  1 
ATOM   7635 H  HG3  . GLN   B 1 207 ? -5.375  -20.998 0.008   1.00 21.02  ? 204 GLN   B HG3  1 
ATOM   7636 H  HE21 . GLN   B 1 207 ? -7.123  -19.977 -1.699  1.00 24.59  ? 204 GLN   B HE21 1 
ATOM   7637 H  HE22 . GLN   B 1 207 ? -8.461  -19.769 -1.078  1.00 24.59  ? 204 GLN   B HE22 1 
ATOM   7638 N  N    . TYR   B 1 208 ? -4.675  -19.920 4.813   1.00 15.19  ? 205 TYR   B N    1 
ATOM   7639 C  CA   . TYR   B 1 208 ? -3.884  -19.465 5.947   1.00 15.00  ? 205 TYR   B CA   1 
ATOM   7640 C  C    . TYR   B 1 208 ? -3.765  -20.552 7.018   1.00 15.95  ? 205 TYR   B C    1 
ATOM   7641 O  O    . TYR   B 1 208 ? -2.674  -20.744 7.588   1.00 16.78  ? 205 TYR   B O    1 
ATOM   7642 C  CB   . TYR   B 1 208 ? -4.494  -18.200 6.571   1.00 17.24  ? 205 TYR   B CB   1 
ATOM   7643 C  CG   . TYR   B 1 208 ? -4.291  -16.896 5.820   1.00 14.81  ? 205 TYR   B CG   1 
ATOM   7644 C  CD1  . TYR   B 1 208 ? -4.327  -16.868 4.437   1.00 16.83  ? 205 TYR   B CD1  1 
ATOM   7645 C  CD2  . TYR   B 1 208 ? -4.068  -15.697 6.479   1.00 16.38  ? 205 TYR   B CD2  1 
ATOM   7646 C  CE1  . TYR   B 1 208 ? -4.165  -15.716 3.742   1.00 16.51  ? 205 TYR   B CE1  1 
ATOM   7647 C  CE2  . TYR   B 1 208 ? -3.886  -14.489 5.764   1.00 16.36  ? 205 TYR   B CE2  1 
ATOM   7648 C  CZ   . TYR   B 1 208 ? -3.944  -14.518 4.390   1.00 18.07  ? 205 TYR   B CZ   1 
ATOM   7649 O  OH   . TYR   B 1 208 ? -3.788  -13.364 3.639   1.00 19.26  ? 205 TYR   B OH   1 
ATOM   7650 H  H    . TYR   B 1 208 ? -5.509  -19.713 4.834   1.00 18.27  ? 205 TYR   B H    1 
ATOM   7651 H  HA   . TYR   B 1 208 ? -2.997  -19.243 5.622   1.00 18.05  ? 205 TYR   B HA   1 
ATOM   7652 H  HB2  . TYR   B 1 208 ? -5.452  -18.335 6.647   1.00 20.73  ? 205 TYR   B HB2  1 
ATOM   7653 H  HB3  . TYR   B 1 208 ? -4.105  -18.082 7.452   1.00 20.73  ? 205 TYR   B HB3  1 
ATOM   7654 H  HD1  . TYR   B 1 208 ? -4.467  -17.661 3.971   1.00 20.24  ? 205 TYR   B HD1  1 
ATOM   7655 H  HD2  . TYR   B 1 208 ? -4.038  -15.685 7.409   1.00 19.69  ? 205 TYR   B HD2  1 
ATOM   7656 H  HE1  . TYR   B 1 208 ? -4.202  -15.733 2.813   1.00 19.86  ? 205 TYR   B HE1  1 
ATOM   7657 H  HE2  . TYR   B 1 208 ? -3.730  -13.691 6.215   1.00 19.67  ? 205 TYR   B HE2  1 
ATOM   7658 H  HH   . TYR   B 1 208 ? -3.705  -12.700 4.147   1.00 23.16  ? 205 TYR   B HH   1 
ATOM   7659 N  N    . THR   B 1 209 ? -4.899  -21.237 7.332   1.00 17.21  ? 206 THR   B N    1 
ATOM   7660 C  CA   . THR   B 1 209 ? -4.858  -22.225 8.419   1.00 17.36  ? 206 THR   B CA   1 
ATOM   7661 C  C    . THR   B 1 209 ? -4.063  -23.469 8.059   1.00 17.57  ? 206 THR   B C    1 
ATOM   7662 O  O    . THR   B 1 209 ? -3.690  -24.217 8.958   1.00 18.86  ? 206 THR   B O    1 
ATOM   7663 C  CB   . THR   B 1 209 ? -6.254  -22.678 8.882   1.00 18.38  ? 206 THR   B CB   1 
ATOM   7664 O  OG1  . THR   B 1 209 ? -6.930  -23.336 7.795   1.00 18.49  ? 206 THR   B OG1  1 
ATOM   7665 C  CG2  . THR   B 1 209 ? -7.059  -21.464 9.382   1.00 19.88  ? 206 THR   B CG2  1 
ATOM   7666 H  H    . THR   B 1 209 ? -5.661  -21.144 6.944   1.00 20.69  ? 206 THR   B H    1 
ATOM   7667 H  HA   . THR   B 1 209 ? -4.439  -21.766 9.164   1.00 20.87  ? 206 THR   B HA   1 
ATOM   7668 H  HB   . THR   B 1 209 ? -6.183  -23.307 9.617   1.00 22.10  ? 206 THR   B HB   1 
ATOM   7669 H  HG1  . THR   B 1 209 ? -7.471  -22.807 7.432   1.00 22.23  ? 206 THR   B HG1  1 
ATOM   7670 H  HG21 . THR   B 1 209 ? -7.913  -21.756 9.738   1.00 23.90  ? 206 THR   B HG21 1 
ATOM   7671 H  HG22 . THR   B 1 209 ? -6.567  -21.005 10.081  1.00 23.90  ? 206 THR   B HG22 1 
ATOM   7672 H  HG23 . THR   B 1 209 ? -7.217  -20.847 8.650   1.00 23.90  ? 206 THR   B HG23 1 
ATOM   7673 N  N    . HIS   B 1 210 ? -3.780  -23.731 6.778   1.00 15.80  ? 207 HIS   B N    1 
ATOM   7674 C  CA   . HIS   B 1 210 ? -2.911  -24.854 6.428   1.00 16.81  ? 207 HIS   B CA   1 
ATOM   7675 C  C    . HIS   B 1 210 ? -1.620  -24.360 5.769   1.00 18.09  ? 207 HIS   B C    1 
ATOM   7676 O  O    . HIS   B 1 210 ? -1.029  -25.046 4.929   1.00 20.40  ? 207 HIS   B O    1 
ATOM   7677 C  CB   . HIS   B 1 210 ? -3.624  -25.868 5.530   1.00 18.48  ? 207 HIS   B CB   1 
ATOM   7678 C  CG   . HIS   B 1 210 ? -3.047  -27.250 5.615   1.00 20.25  ? 207 HIS   B CG   1 
ATOM   7679 N  ND1  . HIS   B 1 210 ? -3.060  -27.995 6.778   1.00 21.66  ? 207 HIS   B ND1  1 
ATOM   7680 C  CD2  . HIS   B 1 210 ? -2.393  -28.011 4.699   1.00 23.14  ? 207 HIS   B CD2  1 
ATOM   7681 C  CE1  . HIS   B 1 210 ? -2.473  -29.161 6.569   1.00 25.60  ? 207 HIS   B CE1  1 
ATOM   7682 N  NE2  . HIS   B 1 210 ? -2.072  -29.205 5.311   1.00 23.93  ? 207 HIS   B NE2  1 
ATOM   7683 H  H    . HIS   B 1 210 ? -4.075  -23.280 6.109   1.00 19.00  ? 207 HIS   B H    1 
ATOM   7684 H  HA   . HIS   B 1 210 ? -2.677  -25.320 7.246   1.00 20.21  ? 207 HIS   B HA   1 
ATOM   7685 H  HB2  . HIS   B 1 210 ? -4.556  -25.918 5.792   1.00 22.22  ? 207 HIS   B HB2  1 
ATOM   7686 H  HB3  . HIS   B 1 210 ? -3.554  -25.573 4.608   1.00 22.22  ? 207 HIS   B HB3  1 
ATOM   7687 H  HD1  . HIS   B 1 210 ? -3.398  -27.738 7.526   1.00 26.04  ? 207 HIS   B HD1  1 
ATOM   7688 H  HD2  . HIS   B 1 210 ? -2.197  -27.771 3.822   1.00 27.81  ? 207 HIS   B HD2  1 
ATOM   7689 H  HE1  . HIS   B 1 210 ? -2.362  -29.836 7.200   1.00 30.76  ? 207 HIS   B HE1  1 
ATOM   7690 N  N    . SER   B 1 211 ? -1.145  -23.165 6.154   1.00 16.55  ? 208 SER   B N    1 
ATOM   7691 C  CA   . SER   B 1 211 ? 0.061   -22.601 5.560   1.00 17.55  ? 208 SER   B CA   1 
ATOM   7692 C  C    . SER   B 1 211 ? 1.306   -23.177 6.247   1.00 18.38  ? 208 SER   B C    1 
ATOM   7693 O  O    . SER   B 1 211 ? 1.232   -23.877 7.280   1.00 19.22  ? 208 SER   B O    1 
ATOM   7694 C  CB   . SER   B 1 211 ? 0.027   -21.082 5.671   1.00 19.12  ? 208 SER   B CB   1 
ATOM   7695 O  OG   . SER   B 1 211 ? 0.035   -20.633 7.036   1.00 17.72  ? 208 SER   B OG   1 
ATOM   7696 H  H    . SER   B 1 211 ? -1.506  -22.668 6.755   1.00 19.90  ? 208 SER   B H    1 
ATOM   7697 H  HA   . SER   B 1 211 ? 0.110   -22.831 4.619   1.00 21.10  ? 208 SER   B HA   1 
ATOM   7698 H  HB2  . SER   B 1 211 ? 0.808   -20.721 5.222   1.00 22.98  ? 208 SER   B HB2  1 
ATOM   7699 H  HB3  . SER   B 1 211 ? -0.781  -20.758 5.244   1.00 22.98  ? 208 SER   B HB3  1 
ATOM   7700 H  HG   . SER   B 1 211 ? -0.742  -20.661 7.352   1.00 21.31  ? 208 SER   B HG   1 
ATOM   7701 N  N    . ASN   B 1 212 ? 2.479   -22.907 5.660   1.00 18.30  ? 209 ASN   B N    1 
ATOM   7702 C  CA   . ASN   B 1 212 ? 3.716   -23.625 5.994   1.00 20.38  ? 209 ASN   B CA   1 
ATOM   7703 C  C    . ASN   B 1 212 ? 4.431   -22.992 7.179   1.00 24.74  ? 209 ASN   B C    1 
ATOM   7704 O  O    . ASN   B 1 212 ? 5.409   -22.250 7.046   1.00 24.48  ? 209 ASN   B O    1 
ATOM   7705 C  CB   . ASN   B 1 212 ? 4.627   -23.667 4.770   1.00 22.97  ? 209 ASN   B CB   1 
ATOM   7706 C  CG   . ASN   B 1 212 ? 5.876   -24.481 4.997   1.00 34.47  ? 209 ASN   B CG   1 
ATOM   7707 O  OD1  . ASN   B 1 212 ? 5.909   -25.345 5.867   1.00 32.85  ? 209 ASN   B OD1  1 
ATOM   7708 N  ND2  . ASN   B 1 212 ? 6.929   -24.184 4.240   1.00 38.11  ? 209 ASN   B ND2  1 
ATOM   7709 H  H    . ASN   B 1 212 ? 2.585   -22.303 5.056   1.00 22.00  ? 209 ASN   B H    1 
ATOM   7710 H  HA   . ASN   B 1 212 ? 3.466   -24.521 6.268   1.00 24.50  ? 209 ASN   B HA   1 
ATOM   7711 H  HB2  . ASN   B 1 212 ? 4.142   -24.063 4.028   1.00 27.60  ? 209 ASN   B HB2  1 
ATOM   7712 H  HB3  . ASN   B 1 212 ? 4.896   -22.763 4.545   1.00 27.60  ? 209 ASN   B HB3  1 
ATOM   7713 H  HD21 . ASN   B 1 212 ? 7.663   -24.622 4.334   1.00 45.77  ? 209 ASN   B HD21 1 
ATOM   7714 H  HD22 . ASN   B 1 212 ? 6.875   -23.555 3.657   1.00 45.77  ? 209 ASN   B HD22 1 
ATOM   7715 N  N    . ILE   B 1 213 ? 3.947   -23.343 8.369   1.00 20.41  ? 210 ILE   B N    1 
ATOM   7716 C  CA   . ILE   B 1 213 ? 4.545   -22.985 9.646   1.00 20.30  ? 210 ILE   B CA   1 
ATOM   7717 C  C    . ILE   B 1 213 ? 4.795   -24.281 10.397  1.00 24.85  ? 210 ILE   B C    1 
ATOM   7718 O  O    . ILE   B 1 213 ? 3.889   -25.124 10.497  1.00 23.54  ? 210 ILE   B O    1 
ATOM   7719 C  CB   . ILE   B 1 213 ? 3.630   -22.060 10.477  1.00 21.59  ? 210 ILE   B CB   1 
ATOM   7720 C  CG1  . ILE   B 1 213 ? 3.330   -20.768 9.722   1.00 20.48  ? 210 ILE   B CG1  1 
ATOM   7721 C  CG2  . ILE   B 1 213 ? 4.213   -21.819 11.865  1.00 22.37  ? 210 ILE   B CG2  1 
ATOM   7722 C  CD1  . ILE   B 1 213 ? 4.519   -19.895 9.487   1.00 20.07  ? 210 ILE   B CD1  1 
ATOM   7723 H  H    . ILE   B 1 213 ? 3.234   -23.814 8.464   1.00 24.54  ? 210 ILE   B H    1 
ATOM   7724 H  HA   . ILE   B 1 213 ? 5.384   -22.522 9.494   1.00 24.41  ? 210 ILE   B HA   1 
ATOM   7725 H  HB   . ILE   B 1 213 ? 2.779   -22.506 10.608  1.00 25.95  ? 210 ILE   B HB   1 
ATOM   7726 H  HG12 . ILE   B 1 213 ? 2.958   -20.996 8.856   1.00 24.62  ? 210 ILE   B HG12 1 
ATOM   7727 H  HG13 . ILE   B 1 213 ? 2.686   -20.254 10.234  1.00 24.62  ? 210 ILE   B HG13 1 
ATOM   7728 H  HG21 . ILE   B 1 213 ? 3.714   -21.108 12.298  1.00 26.89  ? 210 ILE   B HG21 1 
ATOM   7729 H  HG22 . ILE   B 1 213 ? 4.143   -22.636 12.383  1.00 26.89  ? 210 ILE   B HG22 1 
ATOM   7730 H  HG23 . ILE   B 1 213 ? 5.144   -21.562 11.776  1.00 26.89  ? 210 ILE   B HG23 1 
ATOM   7731 H  HD11 . ILE   B 1 213 ? 4.250   -19.133 8.951   1.00 24.13  ? 210 ILE   B HD11 1 
ATOM   7732 H  HD12 . ILE   B 1 213 ? 4.863   -19.593 10.342  1.00 24.13  ? 210 ILE   B HD12 1 
ATOM   7733 H  HD13 . ILE   B 1 213 ? 5.198   -20.406 9.019   1.00 24.13  ? 210 ILE   B HD13 1 
ATOM   7734 N  N    . THR   B 1 214 ? 6.007   -24.432 10.941  1.00 23.85  ? 211 THR   B N    1 
ATOM   7735 C  CA   . THR   B 1 214 ? 6.347   -25.606 11.730  1.00 22.95  ? 211 THR   B CA   1 
ATOM   7736 C  C    . THR   B 1 214 ? 6.722   -25.176 13.143  1.00 24.45  ? 211 THR   B C    1 
ATOM   7737 O  O    . THR   B 1 214 ? 7.019   -24.008 13.400  1.00 25.72  ? 211 THR   B O    1 
ATOM   7738 C  CB   . THR   B 1 214 ? 7.526   -26.374 11.109  1.00 26.43  ? 211 THR   B CB   1 
ATOM   7739 O  OG1  . THR   B 1 214 ? 8.700   -25.563 11.215  1.00 30.30  ? 211 THR   B OG1  1 
ATOM   7740 C  CG2  . THR   B 1 214 ? 7.286   -26.708 9.644   1.00 29.27  ? 211 THR   B CG2  1 
ATOM   7741 H  H    . THR   B 1 214 ? 6.647   -23.863 10.862  1.00 28.67  ? 211 THR   B H    1 
ATOM   7742 H  HA   . THR   B 1 214 ? 5.580   -26.198 11.772  1.00 27.58  ? 211 THR   B HA   1 
ATOM   7743 H  HB   . THR   B 1 214 ? 7.640   -27.215 11.579  1.00 31.76  ? 211 THR   B HB   1 
ATOM   7744 H  HG1  . THR   B 1 214 ? 9.347   -25.943 10.835  1.00 36.40  ? 211 THR   B HG1  1 
ATOM   7745 H  HG21 . THR   B 1 214 ? 7.988   -27.292 9.317   1.00 35.16  ? 211 THR   B HG21 1 
ATOM   7746 H  HG22 . THR   B 1 214 ? 6.431   -27.155 9.541   1.00 35.16  ? 211 THR   B HG22 1 
ATOM   7747 H  HG23 . THR   B 1 214 ? 7.281   -25.894 9.115   1.00 35.16  ? 211 THR   B HG23 1 
ATOM   7748 N  N    . LEU   B 1 215 ? 6.698   -26.142 14.065  1.00 26.91  ? 212 LEU   B N    1 
ATOM   7749 C  CA   . LEU   B 1 215 ? 7.148   -25.840 15.422  1.00 30.56  ? 212 LEU   B CA   1 
ATOM   7750 C  C    . LEU   B 1 215 ? 8.589   -25.346 15.435  1.00 33.89  ? 212 LEU   B C    1 
ATOM   7751 O  O    . LEU   B 1 215 ? 8.957   -24.531 16.287  1.00 32.37  ? 212 LEU   B O    1 
ATOM   7752 C  CB   . LEU   B 1 215 ? 7.011   -27.089 16.285  1.00 36.66  ? 212 LEU   B CB   1 
ATOM   7753 C  CG   . LEU   B 1 215 ? 5.574   -27.459 16.646  1.00 42.45  ? 212 LEU   B CG   1 
ATOM   7754 C  CD1  . LEU   B 1 215 ? 5.600   -28.652 17.574  1.00 50.30  ? 212 LEU   B CD1  1 
ATOM   7755 C  CD2  . LEU   B 1 215 ? 4.832   -26.302 17.273  1.00 36.31  ? 212 LEU   B CD2  1 
ATOM   7756 H  H    . LEU   B 1 215 ? 6.436   -26.950 13.935  1.00 32.33  ? 212 LEU   B H    1 
ATOM   7757 H  HA   . LEU   B 1 215 ? 6.590   -25.140 15.796  1.00 36.72  ? 212 LEU   B HA   1 
ATOM   7758 H  HB2  . LEU   B 1 215 ? 7.395   -27.839 15.805  1.00 44.03  ? 212 LEU   B HB2  1 
ATOM   7759 H  HB3  . LEU   B 1 215 ? 7.493   -26.944 17.114  1.00 44.03  ? 212 LEU   B HB3  1 
ATOM   7760 H  HG   . LEU   B 1 215 ? 5.088   -27.686 15.838  1.00 50.99  ? 212 LEU   B HG   1 
ATOM   7761 H  HD11 . LEU   B 1 215 ? 4.688   -28.901 17.793  1.00 60.41  ? 212 LEU   B HD11 1 
ATOM   7762 H  HD12 . LEU   B 1 215 ? 6.046   -29.389 17.129  1.00 60.41  ? 212 LEU   B HD12 1 
ATOM   7763 H  HD13 . LEU   B 1 215 ? 6.081   -28.414 18.382  1.00 60.41  ? 212 LEU   B HD13 1 
ATOM   7764 H  HD21 . LEU   B 1 215 ? 3.988   -26.622 17.626  1.00 43.61  ? 212 LEU   B HD21 1 
ATOM   7765 H  HD22 . LEU   B 1 215 ? 5.371   -25.931 17.989  1.00 43.61  ? 212 LEU   B HD22 1 
ATOM   7766 H  HD23 . LEU   B 1 215 ? 4.672   -25.625 16.596  1.00 43.61  ? 212 LEU   B HD23 1 
ATOM   7767 N  N    . ASP   B 1 216 ? 9.413   -25.822 14.499  1.00 31.45  ? 213 ASP   B N    1 
ATOM   7768 C  CA   . ASP   B 1 216 ? 10.799  -25.365 14.410  1.00 33.75  ? 213 ASP   B CA   1 
ATOM   7769 C  C    . ASP   B 1 216 ? 10.864  -23.863 14.167  1.00 36.14  ? 213 ASP   B C    1 
ATOM   7770 O  O    . ASP   B 1 216 ? 11.778  -23.200 14.659  1.00 34.15  ? 213 ASP   B O    1 
ATOM   7771 C  CB   . ASP   B 1 216 ? 11.500  -26.123 13.280  1.00 34.32  ? 213 ASP   B CB   1 
ATOM   7772 C  CG   . ASP   B 1 216 ? 12.202  -27.367 13.752  1.00 52.51  ? 213 ASP   B CG   1 
ATOM   7773 O  OD1  . ASP   B 1 216 ? 12.178  -27.660 14.970  1.00 55.37  ? 213 ASP   B OD1  1 
ATOM   7774 O  OD2  . ASP   B 1 216 ? 12.754  -28.083 12.891  1.00 69.61  ? 213 ASP   B OD2  1 
ATOM   7775 H  H    . ASP   B 1 216 ? 9.196   -26.407 13.908  1.00 37.79  ? 213 ASP   B H    1 
ATOM   7776 H  HA   . ASP   B 1 216 ? 11.264  -25.552 15.240  1.00 40.55  ? 213 ASP   B HA   1 
ATOM   7777 H  HB2  . ASP   B 1 216 ? 10.839  -26.385 12.620  1.00 41.23  ? 213 ASP   B HB2  1 
ATOM   7778 H  HB3  . ASP   B 1 216 ? 12.162  -25.542 12.874  1.00 41.23  ? 213 ASP   B HB3  1 
ATOM   7779 N  N    . ASP   B 1 217 ? 9.893   -23.305 13.433  1.00 27.34  ? 214 ASP   B N    1 
ATOM   7780 C  CA   . ASP   B 1 217 ? 9.865   -21.870 13.189  1.00 31.32  ? 214 ASP   B CA   1 
ATOM   7781 C  C    . ASP   B 1 217 ? 9.679   -21.101 14.491  1.00 35.40  ? 214 ASP   B C    1 
ATOM   7782 O  O    . ASP   B 1 217 ? 10.179  -19.985 14.629  1.00 40.88  ? 214 ASP   B O    1 
ATOM   7783 C  CB   . ASP   B 1 217 ? 8.746   -21.540 12.197  1.00 30.49  ? 214 ASP   B CB   1 
ATOM   7784 C  CG   . ASP   B 1 217 ? 8.986   -22.137 10.808  1.00 35.52  ? 214 ASP   B CG   1 
ATOM   7785 O  OD1  . ASP   B 1 217 ? 10.143  -22.105 10.345  1.00 31.48  ? 214 ASP   B OD1  1 
ATOM   7786 O  OD2  . ASP   B 1 217 ? 8.027   -22.645 10.168  1.00 29.40  ? 214 ASP   B OD2  1 
ATOM   7787 H  H    . ASP   B 1 217 ? 9.245   -23.737 13.069  1.00 32.85  ? 214 ASP   B H    1 
ATOM   7788 H  HA   . ASP   B 1 217 ? 10.705  -21.588 12.793  1.00 37.62  ? 214 ASP   B HA   1 
ATOM   7789 H  HB2  . ASP   B 1 217 ? 7.909   -21.896 12.535  1.00 36.63  ? 214 ASP   B HB2  1 
ATOM   7790 H  HB3  . ASP   B 1 217 ? 8.681   -20.577 12.102  1.00 36.63  ? 214 ASP   B HB3  1 
ATOM   7791 N  N    . PHE   B 1 218 ? 8.962   -21.683 15.449  1.00 27.01  ? 215 PHE   B N    1 
ATOM   7792 C  CA   . PHE   B 1 218 ? 8.762   -21.021 16.735  1.00 30.13  ? 215 PHE   B CA   1 
ATOM   7793 C  C    . PHE   B 1 218 ? 9.987   -21.179 17.626  1.00 32.60  ? 215 PHE   B C    1 
ATOM   7794 O  O    . PHE   B 1 218 ? 10.437  -20.215 18.244  1.00 31.38  ? 215 PHE   B O    1 
ATOM   7795 C  CB   . PHE   B 1 218 ? 7.547   -21.599 17.447  1.00 29.79  ? 215 PHE   B CB   1 
ATOM   7796 C  CG   . PHE   B 1 218 ? 6.254   -21.420 16.704  1.00 26.63  ? 215 PHE   B CG   1 
ATOM   7797 C  CD1  . PHE   B 1 218 ? 6.038   -20.272 15.970  1.00 31.58  ? 215 PHE   B CD1  1 
ATOM   7798 C  CD2  . PHE   B 1 218 ? 5.304   -22.391 16.730  1.00 32.19  ? 215 PHE   B CD2  1 
ATOM   7799 C  CE1  . PHE   B 1 218 ? 4.847   -20.101 15.284  1.00 35.13  ? 215 PHE   B CE1  1 
ATOM   7800 C  CE2  . PHE   B 1 218 ? 4.108   -22.223 16.029  1.00 32.62  ? 215 PHE   B CE2  1 
ATOM   7801 C  CZ   . PHE   B 1 218 ? 3.898   -21.069 15.337  1.00 30.43  ? 215 PHE   B CZ   1 
ATOM   7802 H  H    . PHE   B 1 218 ? 8.585   -22.452 15.381  1.00 32.45  ? 215 PHE   B H    1 
ATOM   7803 H  HA   . PHE   B 1 218 ? 8.605   -20.078 16.571  1.00 36.20  ? 215 PHE   B HA   1 
ATOM   7804 H  HB2  . PHE   B 1 218 ? 7.685   -22.551 17.571  1.00 35.79  ? 215 PHE   B HB2  1 
ATOM   7805 H  HB3  . PHE   B 1 218 ? 7.455   -21.162 18.308  1.00 35.79  ? 215 PHE   B HB3  1 
ATOM   7806 H  HD1  . PHE   B 1 218 ? 6.693   -19.612 15.935  1.00 37.93  ? 215 PHE   B HD1  1 
ATOM   7807 H  HD2  . PHE   B 1 218 ? 5.451   -23.170 17.216  1.00 38.67  ? 215 PHE   B HD2  1 
ATOM   7808 H  HE1  . PHE   B 1 218 ? 4.698   -19.327 14.790  1.00 42.20  ? 215 PHE   B HE1  1 
ATOM   7809 H  HE2  . PHE   B 1 218 ? 3.462   -22.892 16.035  1.00 39.18  ? 215 PHE   B HE2  1 
ATOM   7810 H  HZ   . PHE   B 1 218 ? 3.091   -20.942 14.894  1.00 36.56  ? 215 PHE   B HZ   1 
ATOM   7811 N  N    . THR   B 1 219 ? 10.529  -22.399 17.716  1.00 29.04  ? 216 THR   B N    1 
ATOM   7812 C  CA   . THR   B 1 219 ? 11.646  -22.644 18.625  1.00 30.37  ? 216 THR   B CA   1 
ATOM   7813 C  C    . THR   B 1 219 ? 12.859  -21.806 18.267  1.00 32.65  ? 216 THR   B C    1 
ATOM   7814 O  O    . THR   B 1 219 ? 13.615  -21.411 19.170  1.00 32.03  ? 216 THR   B O    1 
ATOM   7815 C  CB   . THR   B 1 219 ? 12.008  -24.116 18.626  1.00 34.95  ? 216 THR   B CB   1 
ATOM   7816 O  OG1  . THR   B 1 219 ? 12.491  -24.478 17.327  1.00 38.22  ? 216 THR   B OG1  1 
ATOM   7817 C  CG2  . THR   B 1 219 ? 10.838  -24.961 19.024  1.00 33.94  ? 216 THR   B CG2  1 
ATOM   7818 H  H    . THR   B 1 219 ? 10.271  -23.087 17.269  1.00 34.89  ? 216 THR   B H    1 
ATOM   7819 H  HA   . THR   B 1 219 ? 11.371  -22.401 19.523  1.00 36.49  ? 216 THR   B HA   1 
ATOM   7820 H  HB   . THR   B 1 219 ? 12.706  -24.287 19.278  1.00 41.98  ? 216 THR   B HB   1 
ATOM   7821 H  HG1  . THR   B 1 219 ? 12.667  -25.299 17.305  1.00 45.90  ? 216 THR   B HG1  1 
ATOM   7822 H  HG21 . THR   B 1 219 ? 11.090  -25.898 19.023  1.00 40.77  ? 216 THR   B HG21 1 
ATOM   7823 H  HG22 . THR   B 1 219 ? 10.540  -24.716 19.913  1.00 40.77  ? 216 THR   B HG22 1 
ATOM   7824 H  HG23 . THR   B 1 219 ? 10.107  -24.831 18.399  1.00 40.77  ? 216 THR   B HG23 1 
ATOM   7825 N  N    . LYS   B 1 220 ? 13.067  -21.510 16.972  1.00 30.42  ? 217 LYS   B N    1 
ATOM   7826 C  CA   . LYS   B 1 220 ? 14.229  -20.699 16.616  1.00 29.66  ? 217 LYS   B CA   1 
ATOM   7827 C  C    . LYS   B 1 220 ? 14.188  -19.343 17.305  1.00 26.83  ? 217 LYS   B C    1 
ATOM   7828 O  O    . LYS   B 1 220 ? 15.237  -18.792 17.634  1.00 30.91  ? 217 LYS   B O    1 
ATOM   7829 C  CB   . LYS   B 1 220 ? 14.378  -20.449 15.101  1.00 36.20  ? 217 LYS   B CB   1 
ATOM   7830 C  CG   . LYS   B 1 220 ? 14.061  -21.576 14.168  1.00 52.26  ? 217 LYS   B CG   1 
ATOM   7831 C  CD   . LYS   B 1 220 ? 14.630  -21.285 12.764  1.00 59.99  ? 217 LYS   B CD   1 
ATOM   7832 C  CE   . LYS   B 1 220 ? 14.137  -22.308 11.735  1.00 60.35  ? 217 LYS   B CE   1 
ATOM   7833 N  NZ   . LYS   B 1 220 ? 14.623  -22.001 10.356  1.00 57.09  ? 217 LYS   B NZ   1 
ATOM   7834 H  H    . LYS   B 1 220 ? 12.571  -21.758 16.315  1.00 36.55  ? 217 LYS   B H    1 
ATOM   7835 H  HA   . LYS   B 1 220 ? 15.000  -21.217 16.896  1.00 35.64  ? 217 LYS   B HA   1 
ATOM   7836 H  HB2  . LYS   B 1 220 ? 13.788  -19.717 14.863  1.00 43.48  ? 217 LYS   B HB2  1 
ATOM   7837 H  HB3  . LYS   B 1 220 ? 15.300  -20.200 14.932  1.00 43.48  ? 217 LYS   B HB3  1 
ATOM   7838 H  HG2  . LYS   B 1 220 ? 14.460  -22.395 14.500  1.00 62.76  ? 217 LYS   B HG2  1 
ATOM   7839 H  HG3  . LYS   B 1 220 ? 13.100  -21.680 14.098  1.00 62.76  ? 217 LYS   B HG3  1 
ATOM   7840 H  HD2  . LYS   B 1 220 ? 14.344  -20.403 12.478  1.00 72.03  ? 217 LYS   B HD2  1 
ATOM   7841 H  HD3  . LYS   B 1 220 ? 15.599  -21.325 12.795  1.00 72.03  ? 217 LYS   B HD3  1 
ATOM   7842 H  HE2  . LYS   B 1 220 ? 14.462  -23.189 11.981  1.00 72.47  ? 217 LYS   B HE2  1 
ATOM   7843 H  HE3  . LYS   B 1 220 ? 13.167  -22.304 11.722  1.00 72.47  ? 217 LYS   B HE3  1 
ATOM   7844 H  HZ1  . LYS   B 1 220 ? 14.312  -22.606 9.782   1.00 68.55  ? 217 LYS   B HZ1  1 
ATOM   7845 H  HZ2  . LYS   B 1 220 ? 14.342  -21.194 10.106  1.00 68.55  ? 217 LYS   B HZ2  1 
ATOM   7846 H  HZ3  . LYS   B 1 220 ? 15.513  -22.015 10.336  1.00 68.55  ? 217 LYS   B HZ3  1 
ATOM   7847 N  N    . TYR   B 1 221 ? 12.985  -18.802 17.533  1.00 29.84  ? 218 TYR   B N    1 
ATOM   7848 C  CA   . TYR   B 1 221 ? 12.838  -17.473 18.106  1.00 31.90  ? 218 TYR   B CA   1 
ATOM   7849 C  C    . TYR   B 1 221 ? 11.971  -17.488 19.353  1.00 32.31  ? 218 TYR   B C    1 
ATOM   7850 O  O    . TYR   B 1 221 ? 11.220  -16.547 19.602  1.00 26.05  ? 218 TYR   B O    1 
ATOM   7851 C  CB   . TYR   B 1 221 ? 12.235  -16.502 17.092  1.00 34.47  ? 218 TYR   B CB   1 
ATOM   7852 C  CG   . TYR   B 1 221 ? 12.858  -16.592 15.714  1.00 34.20  ? 218 TYR   B CG   1 
ATOM   7853 C  CD1  . TYR   B 1 221 ? 14.038  -15.951 15.429  1.00 44.90  ? 218 TYR   B CD1  1 
ATOM   7854 C  CD2  . TYR   B 1 221 ? 12.226  -17.306 14.705  1.00 44.16  ? 218 TYR   B CD2  1 
ATOM   7855 C  CE1  . TYR   B 1 221 ? 14.598  -16.026 14.174  1.00 44.40  ? 218 TYR   B CE1  1 
ATOM   7856 C  CE2  . TYR   B 1 221 ? 12.778  -17.390 13.446  1.00 46.46  ? 218 TYR   B CE2  1 
ATOM   7857 C  CZ   . TYR   B 1 221 ? 13.961  -16.742 13.189  1.00 45.33  ? 218 TYR   B CZ   1 
ATOM   7858 O  OH   . TYR   B 1 221 ? 14.522  -16.823 11.925  1.00 58.51  ? 218 TYR   B OH   1 
ATOM   7859 H  H    . TYR   B 1 221 ? 12.240  -19.195 17.360  1.00 35.85  ? 218 TYR   B H    1 
ATOM   7860 H  HA   . TYR   B 1 221 ? 13.725  -17.172 18.358  1.00 38.32  ? 218 TYR   B HA   1 
ATOM   7861 H  HB2  . TYR   B 1 221 ? 11.289  -16.693 17.002  1.00 41.41  ? 218 TYR   B HB2  1 
ATOM   7862 H  HB3  . TYR   B 1 221 ? 12.362  -15.596 17.415  1.00 41.41  ? 218 TYR   B HB3  1 
ATOM   7863 H  HD1  . TYR   B 1 221 ? 14.465  -15.460 16.093  1.00 53.92  ? 218 TYR   B HD1  1 
ATOM   7864 H  HD2  . TYR   B 1 221 ? 11.420  -17.735 14.882  1.00 53.03  ? 218 TYR   B HD2  1 
ATOM   7865 H  HE1  . TYR   B 1 221 ? 15.402  -15.595 13.994  1.00 53.32  ? 218 TYR   B HE1  1 
ATOM   7866 H  HE2  . TYR   B 1 221 ? 12.354  -17.878 12.778  1.00 55.79  ? 218 TYR   B HE2  1 
ATOM   7867 H  HH   . TYR   B 1 221 ? 14.030  -17.281 11.421  1.00 70.25  ? 218 TYR   B HH   1 
ATOM   7868 N  N    . SER   B 1 222 ? 12.102  -18.517 20.192  1.00 29.66  ? 219 SER   B N    1 
ATOM   7869 C  CA   . SER   B 1 222 ? 11.144  -18.678 21.279  1.00 32.52  ? 219 SER   B CA   1 
ATOM   7870 C  C    . SER   B 1 222 ? 11.206  -17.523 22.261  1.00 26.39  ? 219 SER   B C    1 
ATOM   7871 O  O    . SER   B 1 222 ? 10.192  -17.207 22.907  1.00 26.68  ? 219 SER   B O    1 
ATOM   7872 C  CB   . SER   B 1 222 ? 11.393  -19.986 22.024  1.00 33.74  ? 219 SER   B CB   1 
ATOM   7873 O  OG   . SER   B 1 222 ? 12.608  -19.924 22.715  1.00 37.84  ? 219 SER   B OG   1 
ATOM   7874 H  H    . SER   B 1 222 ? 12.718  -19.116 20.154  1.00 35.64  ? 219 SER   B H    1 
ATOM   7875 H  HA   . SER   B 1 222 ? 10.256  -18.709 20.890  1.00 39.07  ? 219 SER   B HA   1 
ATOM   7876 H  HB2  . SER   B 1 222 ? 10.674  -20.133 22.658  1.00 40.53  ? 219 SER   B HB2  1 
ATOM   7877 H  HB3  . SER   B 1 222 ? 11.426  -20.715 21.386  1.00 40.53  ? 219 SER   B HB3  1 
ATOM   7878 H  HG   . SER   B 1 222 ? 12.718  -20.624 23.167  1.00 45.45  ? 219 SER   B HG   1 
ATOM   7879 N  N    . ASP   B 1 223 ? 12.375  -16.888 22.395  1.00 25.29  ? 220 ASP   B N    1 
ATOM   7880 C  CA   . ASP   B 1 223 ? 12.517  -15.788 23.334  1.00 26.26  ? 220 ASP   B CA   1 
ATOM   7881 C  C    . ASP   B 1 223 ? 11.628  -14.600 22.970  1.00 25.32  ? 220 ASP   B C    1 
ATOM   7882 O  O    . ASP   B 1 223 ? 11.345  -13.759 23.832  1.00 28.53  ? 220 ASP   B O    1 
ATOM   7883 C  CB   . ASP   B 1 223 ? 13.973  -15.315 23.374  1.00 26.65  ? 220 ASP   B CB   1 
ATOM   7884 C  CG   . ASP   B 1 223 ? 14.823  -16.118 24.291  1.00 39.37  ? 220 ASP   B CG   1 
ATOM   7885 O  OD1  . ASP   B 1 223 ? 14.277  -16.824 25.181  1.00 43.16  ? 220 ASP   B OD1  1 
ATOM   7886 O  OD2  . ASP   B 1 223 ? 16.071  -16.047 24.126  1.00 44.19  ? 220 ASP   B OD2  1 
ATOM   7887 H  H    . ASP   B 1 223 ? 13.090  -17.076 21.956  1.00 30.39  ? 220 ASP   B H    1 
ATOM   7888 H  HA   . ASP   B 1 223 ? 12.267  -16.108 24.215  1.00 31.55  ? 220 ASP   B HA   1 
ATOM   7889 H  HB2  . ASP   B 1 223 ? 14.350  -15.382 22.483  1.00 32.02  ? 220 ASP   B HB2  1 
ATOM   7890 H  HB3  . ASP   B 1 223 ? 13.996  -14.394 23.676  1.00 32.02  ? 220 ASP   B HB3  1 
ATOM   7891 N  N    . LYS   B 1 224 ? 11.231  -14.479 21.721  1.00 21.94  ? 221 LYS   B N    1 
ATOM   7892 C  CA   . LYS   B 1 224 ? 10.449  -13.339 21.281  1.00 22.69  ? 221 LYS   B CA   1 
ATOM   7893 C  C    . LYS   B 1 224 ? 8.956   -13.529 21.398  1.00 21.14  ? 221 LYS   B C    1 
ATOM   7894 O  O    . LYS   B 1 224 ? 8.237   -12.549 21.213  1.00 22.14  ? 221 LYS   B O    1 
ATOM   7895 C  CB   . LYS   B 1 224 ? 10.740  -12.962 19.820  1.00 22.93  ? 221 LYS   B CB   1 
ATOM   7896 C  CG   . LYS   B 1 224 ? 12.193  -12.703 19.535  1.00 30.10  ? 221 LYS   B CG   1 
ATOM   7897 C  CD   . LYS   B 1 224 ? 12.507  -13.018 18.084  1.00 49.51  ? 221 LYS   B CD   1 
ATOM   7898 C  CE   . LYS   B 1 224 ? 12.663  -11.764 17.297  1.00 51.28  ? 221 LYS   B CE   1 
ATOM   7899 N  NZ   . LYS   B 1 224 ? 14.013  -11.167 17.553  1.00 44.00  ? 221 LYS   B NZ   1 
ATOM   7900 H  H    . LYS   B 1 224 ? 11.403  -15.049 21.100  1.00 26.37  ? 221 LYS   B H    1 
ATOM   7901 H  HA   . LYS   B 1 224 ? 10.724  -12.602 21.848  1.00 27.27  ? 221 LYS   B HA   1 
ATOM   7902 H  HB2  . LYS   B 1 224 ? 10.451  -13.689 19.248  1.00 27.56  ? 221 LYS   B HB2  1 
ATOM   7903 H  HB3  . LYS   B 1 224 ? 10.248  -12.154 19.604  1.00 27.56  ? 221 LYS   B HB3  1 
ATOM   7904 H  HG2  . LYS   B 1 224 ? 12.397  -11.770 19.700  1.00 36.16  ? 221 LYS   B HG2  1 
ATOM   7905 H  HG3  . LYS   B 1 224 ? 12.742  -13.268 20.100  1.00 36.16  ? 221 LYS   B HG3  1 
ATOM   7906 H  HD2  . LYS   B 1 224 ? 13.335  -13.520 18.033  1.00 59.45  ? 221 LYS   B HD2  1 
ATOM   7907 H  HD3  . LYS   B 1 224 ? 11.782  -13.536 17.700  1.00 59.45  ? 221 LYS   B HD3  1 
ATOM   7908 H  HE2  . LYS   B 1 224 ? 12.583  -11.959 16.350  1.00 61.58  ? 221 LYS   B HE2  1 
ATOM   7909 H  HE3  . LYS   B 1 224 ? 11.983  -11.124 17.562  1.00 61.58  ? 221 LYS   B HE3  1 
ATOM   7910 H  HZ1  . LYS   B 1 224 ? 14.142  -10.466 17.020  1.00 52.84  ? 221 LYS   B HZ1  1 
ATOM   7911 H  HZ2  . LYS   B 1 224 ? 14.072  -10.900 18.400  1.00 52.84  ? 221 LYS   B HZ2  1 
ATOM   7912 H  HZ3  . LYS   B 1 224 ? 14.648  -11.770 17.395  1.00 52.84  ? 221 LYS   B HZ3  1 
ATOM   7913 N  N    . ILE   B 1 225 ? 8.467   -14.739 21.685  1.00 20.37  ? 222 ILE   B N    1 
ATOM   7914 C  CA   . ILE   B 1 225 ? 7.077   -15.110 21.438  1.00 18.90  ? 222 ILE   B CA   1 
ATOM   7915 C  C    . ILE   B 1 225 ? 6.293   -15.248 22.753  1.00 20.82  ? 222 ILE   B C    1 
ATOM   7916 O  O    . ILE   B 1 225 ? 6.749   -15.911 23.705  1.00 22.72  ? 222 ILE   B O    1 
ATOM   7917 C  CB   . ILE   B 1 225 ? 6.981   -16.421 20.656  1.00 19.65  ? 222 ILE   B CB   1 
ATOM   7918 C  CG1  . ILE   B 1 225 ? 7.698   -16.302 19.315  1.00 21.24  ? 222 ILE   B CG1  1 
ATOM   7919 C  CG2  . ILE   B 1 225 ? 5.547   -16.786 20.378  1.00 19.08  ? 222 ILE   B CG2  1 
ATOM   7920 C  CD1  . ILE   B 1 225 ? 7.830   -17.671 18.598  1.00 23.24  ? 222 ILE   B CD1  1 
ATOM   7921 H  H    . ILE   B 1 225 ? 8.934   -15.373 22.031  1.00 24.48  ? 222 ILE   B H    1 
ATOM   7922 H  HA   . ILE   B 1 225 ? 6.678   -14.381 20.937  1.00 22.72  ? 222 ILE   B HA   1 
ATOM   7923 H  HB   . ILE   B 1 225 ? 7.397   -17.104 21.204  1.00 23.62  ? 222 ILE   B HB   1 
ATOM   7924 H  HG12 . ILE   B 1 225 ? 7.197   -15.705 18.738  1.00 25.54  ? 222 ILE   B HG12 1 
ATOM   7925 H  HG13 . ILE   B 1 225 ? 8.590   -15.950 19.462  1.00 25.54  ? 222 ILE   B HG13 1 
ATOM   7926 H  HG21 . ILE   B 1 225 ? 5.525   -17.584 19.827  1.00 22.94  ? 222 ILE   B HG21 1 
ATOM   7927 H  HG22 . ILE   B 1 225 ? 5.095   -16.952 21.220  1.00 22.94  ? 222 ILE   B HG22 1 
ATOM   7928 H  HG23 . ILE   B 1 225 ? 5.119   -16.051 19.911  1.00 22.94  ? 222 ILE   B HG23 1 
ATOM   7929 H  HD11 . ILE   B 1 225 ? 8.512   -17.604 17.912  1.00 27.93  ? 222 ILE   B HD11 1 
ATOM   7930 H  HD12 . ILE   B 1 225 ? 8.080   -18.345 19.249  1.00 27.93  ? 222 ILE   B HD12 1 
ATOM   7931 H  HD13 . ILE   B 1 225 ? 6.978   -17.900 18.196  1.00 27.93  ? 222 ILE   B HD13 1 
ATOM   7932 N  N    . THR   B 1 226 ? 5.084   -14.677 22.759  1.00 20.38  ? 223 THR   B N    1 
ATOM   7933 C  CA   . THR   B 1 226 ? 4.057   -14.924 23.773  1.00 18.59  ? 223 THR   B CA   1 
ATOM   7934 C  C    . THR   B 1 226 ? 2.816   -15.456 23.069  1.00 18.95  ? 223 THR   B C    1 
ATOM   7935 O  O    . THR   B 1 226 ? 2.397   -14.905 22.047  1.00 20.07  ? 223 THR   B O    1 
ATOM   7936 C  CB   . THR   B 1 226 ? 3.729   -13.650 24.532  1.00 21.22  ? 223 THR   B CB   1 
ATOM   7937 O  OG1  . THR   B 1 226 ? 4.924   -13.138 25.154  1.00 23.31  ? 223 THR   B OG1  1 
ATOM   7938 C  CG2  . THR   B 1 226 ? 2.702   -13.912 25.654  1.00 23.35  ? 223 THR   B CG2  1 
ATOM   7939 H  H    . THR   B 1 226 ? 4.825   -14.118 22.158  1.00 24.50  ? 223 THR   B H    1 
ATOM   7940 H  HA   . THR   B 1 226 ? 4.360   -15.581 24.419  1.00 22.35  ? 223 THR   B HA   1 
ATOM   7941 H  HB   . THR   B 1 226 ? 3.359   -13.008 23.906  1.00 25.50  ? 223 THR   B HB   1 
ATOM   7942 H  HG1  . THR   B 1 226 ? 4.836   -12.318 25.314  1.00 28.01  ? 223 THR   B HG1  1 
ATOM   7943 H  HG21 . THR   B 1 226 ? 2.570   -13.106 26.177  1.00 28.06  ? 223 THR   B HG21 1 
ATOM   7944 H  HG22 . THR   B 1 226 ? 1.853   -14.181 25.270  1.00 28.06  ? 223 THR   B HG22 1 
ATOM   7945 H  HG23 . THR   B 1 226 ? 3.022   -14.618 26.238  1.00 28.06  ? 223 THR   B HG23 1 
ATOM   7946 N  N    . LEU   B 1 227 ? 2.212   -16.502 23.617  1.00 18.37  ? 224 LEU   B N    1 
ATOM   7947 C  CA   . LEU   B 1 227 ? 0.914   -17.010 23.190  1.00 18.65  ? 224 LEU   B CA   1 
ATOM   7948 C  C    . LEU   B 1 227 ? -0.164  -16.436 24.105  1.00 22.34  ? 224 LEU   B C    1 
ATOM   7949 O  O    . LEU   B 1 227 ? 0.006   -16.434 25.328  1.00 22.38  ? 224 LEU   B O    1 
ATOM   7950 C  CB   . LEU   B 1 227 ? 0.911   -18.538 23.257  1.00 19.62  ? 224 LEU   B CB   1 
ATOM   7951 C  CG   . LEU   B 1 227 ? 2.097   -19.207 22.571  1.00 18.51  ? 224 LEU   B CG   1 
ATOM   7952 C  CD1  . LEU   B 1 227 ? 2.099   -20.693 22.948  1.00 22.41  ? 224 LEU   B CD1  1 
ATOM   7953 C  CD2  . LEU   B 1 227 ? 2.061   -19.051 21.084  1.00 20.86  ? 224 LEU   B CD2  1 
ATOM   7954 H  H    . LEU   B 1 227 ? 2.549   -16.955 24.266  1.00 22.09  ? 224 LEU   B H    1 
ATOM   7955 H  HA   . LEU   B 1 227 ? 0.719   -16.738 22.279  1.00 22.42  ? 224 LEU   B HA   1 
ATOM   7956 H  HB2  . LEU   B 1 227 ? 0.924   -18.805 24.190  1.00 23.59  ? 224 LEU   B HB2  1 
ATOM   7957 H  HB3  . LEU   B 1 227 ? 0.104   -18.864 22.830  1.00 23.59  ? 224 LEU   B HB3  1 
ATOM   7958 H  HG   . LEU   B 1 227 ? 2.915   -18.780 22.868  1.00 22.25  ? 224 LEU   B HG   1 
ATOM   7959 H  HD11 . LEU   B 1 227 ? 2.907   -21.105 22.604  1.00 26.93  ? 224 LEU   B HD11 1 
ATOM   7960 H  HD12 . LEU   B 1 227 ? 2.072   -20.774 23.914  1.00 26.93  ? 224 LEU   B HD12 1 
ATOM   7961 H  HD13 . LEU   B 1 227 ? 1.320   -21.120 22.558  1.00 26.93  ? 224 LEU   B HD13 1 
ATOM   7962 H  HD21 . LEU   B 1 227 ? 2.859   -19.453 20.705  1.00 25.07  ? 224 LEU   B HD21 1 
ATOM   7963 H  HD22 . LEU   B 1 227 ? 1.271   -19.494 20.738  1.00 25.07  ? 224 LEU   B HD22 1 
ATOM   7964 H  HD23 . LEU   B 1 227 ? 2.032   -18.106 20.867  1.00 25.07  ? 224 LEU   B HD23 1 
ATOM   7965 N  N    . LEU   B 1 228 ? -1.264  -15.958 23.533  1.00 19.50  ? 225 LEU   B N    1 
ATOM   7966 C  CA   . LEU   B 1 228 ? -2.334  -15.340 24.307  1.00 19.31  ? 225 LEU   B CA   1 
ATOM   7967 C  C    . LEU   B 1 228 ? -3.632  -16.126 24.183  1.00 20.43  ? 225 LEU   B C    1 
ATOM   7968 O  O    . LEU   B 1 228 ? -4.112  -16.384 23.071  1.00 19.06  ? 225 LEU   B O    1 
ATOM   7969 C  CB   . LEU   B 1 228 ? -2.542  -13.889 23.862  1.00 20.55  ? 225 LEU   B CB   1 
ATOM   7970 C  CG   . LEU   B 1 228 ? -1.409  -12.924 24.148  1.00 20.27  ? 225 LEU   B CG   1 
ATOM   7971 C  CD1  . LEU   B 1 228 ? -1.697  -11.583 23.478  1.00 22.37  ? 225 LEU   B CD1  1 
ATOM   7972 C  CD2  . LEU   B 1 228 ? -1.138  -12.727 25.654  1.00 21.67  ? 225 LEU   B CD2  1 
ATOM   7973 H  H    . LEU   B 1 228 ? -1.415  -15.981 22.686  1.00 23.45  ? 225 LEU   B H    1 
ATOM   7974 H  HA   . LEU   B 1 228 ? -2.091  -15.358 25.246  1.00 23.21  ? 225 LEU   B HA   1 
ATOM   7975 H  HB2  . LEU   B 1 228 ? -2.683  -13.887 22.903  1.00 24.71  ? 225 LEU   B HB2  1 
ATOM   7976 H  HB3  . LEU   B 1 228 ? -3.329  -13.546 24.314  1.00 24.71  ? 225 LEU   B HB3  1 
ATOM   7977 H  HG   . LEU   B 1 228 ? -0.596  -13.308 23.783  1.00 24.37  ? 225 LEU   B HG   1 
ATOM   7978 H  HD11 . LEU   B 1 228 ? -1.019  -10.944 23.745  1.00 26.89  ? 225 LEU   B HD11 1 
ATOM   7979 H  HD12 . LEU   B 1 228 ? -1.679  -11.702 22.515  1.00 26.89  ? 225 LEU   B HD12 1 
ATOM   7980 H  HD13 . LEU   B 1 228 ? -2.573  -11.273 23.757  1.00 26.89  ? 225 LEU   B HD13 1 
ATOM   7981 H  HD21 . LEU   B 1 228 ? -0.427  -12.077 25.765  1.00 26.05  ? 225 LEU   B HD21 1 
ATOM   7982 H  HD22 . LEU   B 1 228 ? -1.948  -12.406 26.081  1.00 26.05  ? 225 LEU   B HD22 1 
ATOM   7983 H  HD23 . LEU   B 1 228 ? -0.874  -13.576 26.042  1.00 26.05  ? 225 LEU   B HD23 1 
ATOM   7984 N  N    . ASN   B 1 229 ? -4.212  -16.474 25.330  1.00 21.59  ? 226 ASN   B N    1 
ATOM   7985 C  CA   . ASN   B 1 229 ? -5.504  -17.151 25.428  1.00 22.09  ? 226 ASN   B CA   1 
ATOM   7986 C  C    . ASN   B 1 229 ? -6.468  -16.223 26.158  1.00 21.18  ? 226 ASN   B C    1 
ATOM   7987 O  O    . ASN   B 1 229 ? -6.149  -15.740 27.241  1.00 24.82  ? 226 ASN   B O    1 
ATOM   7988 C  CB   . ASN   B 1 229 ? -5.392  -18.463 26.214  1.00 21.18  ? 226 ASN   B CB   1 
ATOM   7989 C  CG   . ASN   B 1 229 ? -4.934  -19.619 25.369  1.00 24.25  ? 226 ASN   B CG   1 
ATOM   7990 O  OD1  . ASN   B 1 229 ? -4.928  -19.545 24.129  1.00 25.99  ? 226 ASN   B OD1  1 
ATOM   7991 N  ND2  . ASN   B 1 229 ? -4.602  -20.717 26.024  1.00 29.11  ? 226 ASN   B ND2  1 
ATOM   7992 H  H    . ASN   B 1 229 ? -3.860  -16.323 26.099  1.00 25.95  ? 226 ASN   B H    1 
ATOM   7993 H  HA   . ASN   B 1 229 ? -5.835  -17.350 24.539  1.00 26.54  ? 226 ASN   B HA   1 
ATOM   7994 H  HB2  . ASN   B 1 229 ? -4.751  -18.346 26.933  1.00 25.46  ? 226 ASN   B HB2  1 
ATOM   7995 H  HB3  . ASN   B 1 229 ? -6.263  -18.686 26.579  1.00 25.46  ? 226 ASN   B HB3  1 
ATOM   7996 H  HD21 . ASN   B 1 229 ? -4.333  -21.411 25.593  1.00 34.97  ? 226 ASN   B HD21 1 
ATOM   7997 H  HD22 . ASN   B 1 229 ? -4.655  -20.739 26.882  1.00 34.97  ? 226 ASN   B HD22 1 
ATOM   7998 N  N    . GLY   B 1 230 ? -7.658  -16.017 25.591  1.00 22.87  ? 227 GLY   B N    1 
ATOM   7999 C  CA   . GLY   B 1 230 ? -8.685  -15.259 26.285  1.00 23.94  ? 227 GLY   B CA   1 
ATOM   8000 C  C    . GLY   B 1 230 ? -9.290  -15.997 27.472  1.00 28.56  ? 227 GLY   B C    1 
ATOM   8001 O  O    . GLY   B 1 230 ? -9.438  -17.213 27.479  1.00 28.07  ? 227 GLY   B O    1 
ATOM   8002 H  H    . GLY   B 1 230 ? -7.890  -16.303 24.814  1.00 27.49  ? 227 GLY   B H    1 
ATOM   8003 H  HA2  . GLY   B 1 230 ? -8.300  -14.430 26.611  1.00 28.77  ? 227 GLY   B HA2  1 
ATOM   8004 H  HA3  . GLY   B 1 230 ? -9.400  -15.053 25.663  1.00 28.77  ? 227 GLY   B HA3  1 
ATOM   8005 N  N    . THR   B 1 231 ? -9.654  -15.244 28.509  1.00 27.72  ? 228 THR   B N    1 
ATOM   8006 C  CA   . THR   B 1 231 ? -10.302 -15.863 29.663  1.00 27.20  ? 228 THR   B CA   1 
ATOM   8007 C  C    . THR   B 1 231 ? -11.764 -16.193 29.390  1.00 34.64  ? 228 THR   B C    1 
ATOM   8008 O  O    . THR   B 1 231 ? -12.343 -17.002 30.122  1.00 33.98  ? 228 THR   B O    1 
ATOM   8009 C  CB   . THR   B 1 231 ? -10.169 -14.963 30.890  1.00 32.69  ? 228 THR   B CB   1 
ATOM   8010 O  OG1  . THR   B 1 231 ? -10.719 -13.671 30.603  1.00 39.10  ? 228 THR   B OG1  1 
ATOM   8011 C  CG2  . THR   B 1 231 ? -8.715  -14.805 31.278  1.00 39.38  ? 228 THR   B CG2  1 
ATOM   8012 H  H    . THR   B 1 231 ? -9.539  -14.394 28.567  1.00 33.30  ? 228 THR   B H    1 
ATOM   8013 H  HA   . THR   B 1 231 ? -9.851  -16.695 29.876  1.00 32.43  ? 228 THR   B HA   1 
ATOM   8014 H  HB   . THR   B 1 231 ? -10.646 -15.362 31.634  1.00 39.27  ? 228 THR   B HB   1 
ATOM   8015 H  HG1  . THR   B 1 231 ? -10.671 -13.181 31.283  1.00 46.96  ? 228 THR   B HG1  1 
ATOM   8016 H  HG21 . THR   B 1 231 ? -8.644  -14.286 32.094  1.00 47.30  ? 228 THR   B HG21 1 
ATOM   8017 H  HG22 . THR   B 1 231 ? -8.313  -15.676 31.422  1.00 47.30  ? 228 THR   B HG22 1 
ATOM   8018 H  HG23 . THR   B 1 231 ? -8.231  -14.348 30.572  1.00 47.30  ? 228 THR   B HG23 1 
ATOM   8019 N  N    . ASP   B 1 232 ? -12.370 -15.617 28.347  1.00 30.38  ? 229 ASP   B N    1 
ATOM   8020 C  CA   . ASP   B 1 232 ? -13.789 -15.841 28.064  1.00 33.14  ? 229 ASP   B CA   1 
ATOM   8021 C  C    . ASP   B 1 232 ? -14.009 -16.801 26.906  1.00 33.37  ? 229 ASP   B C    1 
ATOM   8022 O  O    . ASP   B 1 232 ? -15.159 -16.997 26.492  1.00 33.69  ? 229 ASP   B O    1 
ATOM   8023 C  CB   . ASP   B 1 232 ? -14.489 -14.510 27.755  1.00 34.38  ? 229 ASP   B CB   1 
ATOM   8024 C  CG   . ASP   B 1 232 ? -14.679 -13.649 28.965  1.00 41.53  ? 229 ASP   B CG   1 
ATOM   8025 O  OD1  . ASP   B 1 232 ? -14.766 -14.201 30.091  1.00 41.65  ? 229 ASP   B OD1  1 
ATOM   8026 O  OD2  . ASP   B 1 232 ? -14.698 -12.405 28.802  1.00 43.51  ? 229 ASP   B OD2  1 
ATOM   8027 H  H    . ASP   B 1 232 ? -11.979 -15.092 27.789  1.00 36.50  ? 229 ASP   B H    1 
ATOM   8028 H  HA   . ASP   B 1 232 ? -14.196 -16.221 28.859  1.00 39.81  ? 229 ASP   B HA   1 
ATOM   8029 H  HB2  . ASP   B 1 232 ? -13.953 -14.013 27.117  1.00 41.30  ? 229 ASP   B HB2  1 
ATOM   8030 H  HB3  . ASP   B 1 232 ? -15.364 -14.694 27.380  1.00 41.30  ? 229 ASP   B HB3  1 
ATOM   8031 N  N    . SER   B 1 233 ? -12.950 -17.409 26.384  1.00 29.72  ? 230 SER   B N    1 
ATOM   8032 C  CA   . SER   B 1 233 ? -13.048 -18.303 25.240  1.00 26.09  ? 230 SER   B CA   1 
ATOM   8033 C  C    . SER   B 1 233 ? -12.433 -19.662 25.546  1.00 28.34  ? 230 SER   B C    1 
ATOM   8034 O  O    . SER   B 1 233 ? -11.926 -20.336 24.650  1.00 27.07  ? 230 SER   B O    1 
ATOM   8035 C  CB   . SER   B 1 233 ? -12.387 -17.662 24.028  1.00 27.34  ? 230 SER   B CB   1 
ATOM   8036 O  OG   . SER   B 1 233 ? -11.224 -16.989 24.449  1.00 29.60  ? 230 SER   B OG   1 
ATOM   8037 H  H    . SER   B 1 233 ? -12.149 -17.316 26.682  1.00 35.71  ? 230 SER   B H    1 
ATOM   8038 H  HA   . SER   B 1 233 ? -13.983 -18.458 25.031  1.00 31.35  ? 230 SER   B HA   1 
ATOM   8039 H  HB2  . SER   B 1 233 ? -12.148 -18.351 23.387  1.00 32.85  ? 230 SER   B HB2  1 
ATOM   8040 H  HB3  . SER   B 1 233 ? -12.999 -17.029 23.621  1.00 32.85  ? 230 SER   B HB3  1 
ATOM   8041 H  HG   . SER   B 1 233 ? -10.912 -16.531 23.818  1.00 35.56  ? 230 SER   B HG   1 
ATOM   8042 N  N    . ARG   B 1 234 ? -12.478 -20.086 26.807  1.00 28.22  ? 231 ARG   B N    1 
ATOM   8043 C  CA   . ARG   B 1 234 ? -11.965 -21.401 27.165  1.00 30.20  ? 231 ARG   B CA   1 
ATOM   8044 C  C    . ARG   B 1 234 ? -12.713 -22.495 26.416  1.00 29.48  ? 231 ARG   B C    1 
ATOM   8045 O  O    . ARG   B 1 234 ? -13.913 -22.394 26.152  1.00 31.67  ? 231 ARG   B O    1 
ATOM   8046 C  CB   . ARG   B 1 234 ? -12.086 -21.657 28.670  1.00 31.06  ? 231 ARG   B CB   1 
ATOM   8047 C  CG   . ARG   B 1 234 ? -11.706 -20.496 29.552  1.00 41.40  ? 231 ARG   B CG   1 
ATOM   8048 C  CD   . ARG   B 1 234 ? -10.257 -20.149 29.324  1.00 40.49  ? 231 ARG   B CD   1 
ATOM   8049 N  NE   . ARG   B 1 234 ? -9.364  -20.723 30.323  1.00 62.34  ? 231 ARG   B NE   1 
ATOM   8050 C  CZ   . ARG   B 1 234 ? -8.043  -20.746 30.206  1.00 55.19  ? 231 ARG   B CZ   1 
ATOM   8051 N  NH1  . ARG   B 1 234 ? -7.444  -20.289 29.124  1.00 39.18  ? 231 ARG   B NH1  1 
ATOM   8052 N  NH2  . ARG   B 1 234 ? -7.310  -21.248 31.199  1.00 63.90  ? 231 ARG   B NH2  1 
ATOM   8053 H  H    . ARG   B 1 234 ? -12.797 -19.635 27.466  1.00 33.91  ? 231 ARG   B H    1 
ATOM   8054 H  HA   . ARG   B 1 234 ? -11.026 -21.435 26.925  1.00 36.28  ? 231 ARG   B HA   1 
ATOM   8055 H  HB2  . ARG   B 1 234 ? -13.009 -21.881 28.869  1.00 37.31  ? 231 ARG   B HB2  1 
ATOM   8056 H  HB3  . ARG   B 1 234 ? -11.507 -22.399 28.902  1.00 37.31  ? 231 ARG   B HB3  1 
ATOM   8057 H  HG2  . ARG   B 1 234 ? -12.252 -19.725 29.335  1.00 49.72  ? 231 ARG   B HG2  1 
ATOM   8058 H  HG3  . ARG   B 1 234 ? -11.827 -20.737 30.484  1.00 49.72  ? 231 ARG   B HG3  1 
ATOM   8059 H  HD2  . ARG   B 1 234 ? -9.987  -20.484 28.455  1.00 48.63  ? 231 ARG   B HD2  1 
ATOM   8060 H  HD3  . ARG   B 1 234 ? -10.157 -19.185 29.354  1.00 48.63  ? 231 ARG   B HD3  1 
ATOM   8061 H  HE   . ARG   B 1 234 ? -9.714  -21.066 31.029  1.00 74.85  ? 231 ARG   B HE   1 
ATOM   8062 H  HH11 . ARG   B 1 234 ? -7.911  -19.967 28.477  1.00 47.05  ? 231 ARG   B HH11 1 
ATOM   8063 H  HH12 . ARG   B 1 234 ? -6.586  -20.312 29.065  1.00 47.05  ? 231 ARG   B HH12 1 
ATOM   8064 H  HH21 . ARG   B 1 234 ? -7.693  -21.552 31.906  1.00 76.73  ? 231 ARG   B HH21 1 
ATOM   8065 H  HH22 . ARG   B 1 234 ? -6.453  -21.268 31.132  1.00 76.73  ? 231 ARG   B HH22 1 
ATOM   8066 N  N    . GLY   B 1 235 ? -11.989 -23.563 26.092  1.00 30.12  ? 232 GLY   B N    1 
ATOM   8067 C  CA   . GLY   B 1 235 ? -12.555 -24.699 25.395  1.00 30.96  ? 232 GLY   B CA   1 
ATOM   8068 C  C    . GLY   B 1 235 ? -12.582 -24.572 23.881  1.00 28.91  ? 232 GLY   B C    1 
ATOM   8069 O  O    . GLY   B 1 235 ? -12.984 -25.529 23.196  1.00 30.53  ? 232 GLY   B O    1 
ATOM   8070 H  H    . GLY   B 1 235 ? -11.153 -23.650 26.272  1.00 36.18  ? 232 GLY   B H    1 
ATOM   8071 H  HA2  . GLY   B 1 235 ? -12.036 -25.488 25.616  1.00 37.19  ? 232 GLY   B HA2  1 
ATOM   8072 H  HA3  . GLY   B 1 235 ? -13.468 -24.825 25.697  1.00 37.19  ? 232 GLY   B HA3  1 
ATOM   8073 N  N    . SER   B 1 236 ? -12.181 -23.433 23.332  1.00 26.64  ? 233 SER   B N    1 
ATOM   8074 C  CA   . SER   B 1 236 ? -12.249 -23.248 21.886  1.00 24.52  ? 233 SER   B CA   1 
ATOM   8075 C  C    . SER   B 1 236 ? -10.974 -23.767 21.224  1.00 23.70  ? 233 SER   B C    1 
ATOM   8076 O  O    . SER   B 1 236 ? -9.921  -23.900 21.850  1.00 26.03  ? 233 SER   B O    1 
ATOM   8077 C  CB   . SER   B 1 236 ? -12.450 -21.771 21.557  1.00 24.31  ? 233 SER   B CB   1 
ATOM   8078 O  OG   . SER   B 1 236 ? -11.305 -21.010 21.906  1.00 27.86  ? 233 SER   B OG   1 
ATOM   8079 H  H    . SER   B 1 236 ? -11.869 -22.761 23.769  1.00 32.01  ? 233 SER   B H    1 
ATOM   8080 H  HA   . SER   B 1 236 ? -13.000 -23.745 21.525  1.00 29.46  ? 233 SER   B HA   1 
ATOM   8081 H  HB2  . SER   B 1 236 ? -12.610 -21.680 20.605  1.00 29.21  ? 233 SER   B HB2  1 
ATOM   8082 H  HB3  . SER   B 1 236 ? -13.213 -21.439 22.055  1.00 29.21  ? 233 SER   B HB3  1 
ATOM   8083 H  HG   . SER   B 1 236 ? -11.249 -20.943 22.741  1.00 33.48  ? 233 SER   B HG   1 
ATOM   8084 N  N    . PHE   B 1 237 ? -11.077 -24.058 19.923  1.00 24.55  ? 234 PHE   B N    1 
ATOM   8085 C  CA   . PHE   B 1 237 ? -9.957  -24.667 19.212  1.00 22.37  ? 234 PHE   B CA   1 
ATOM   8086 C  C    . PHE   B 1 237 ? -8.694  -23.817 19.218  1.00 21.68  ? 234 PHE   B C    1 
ATOM   8087 O  O    . PHE   B 1 237 ? -7.608  -24.376 19.426  1.00 21.11  ? 234 PHE   B O    1 
ATOM   8088 C  CB   . PHE   B 1 237 ? -10.410 -25.005 17.776  1.00 23.59  ? 234 PHE   B CB   1 
ATOM   8089 C  CG   . PHE   B 1 237 ? -9.281  -25.341 16.834  1.00 20.02  ? 234 PHE   B CG   1 
ATOM   8090 C  CD1  . PHE   B 1 237 ? -8.667  -26.572 16.879  1.00 25.58  ? 234 PHE   B CD1  1 
ATOM   8091 C  CD2  . PHE   B 1 237 ? -8.840  -24.425 15.903  1.00 19.64  ? 234 PHE   B CD2  1 
ATOM   8092 C  CE1  . PHE   B 1 237 ? -7.628  -26.875 16.019  1.00 22.73  ? 234 PHE   B CE1  1 
ATOM   8093 C  CE2  . PHE   B 1 237 ? -7.799  -24.723 15.031  1.00 21.59  ? 234 PHE   B CE2  1 
ATOM   8094 C  CZ   . PHE   B 1 237 ? -7.188  -25.957 15.110  1.00 21.06  ? 234 PHE   B CZ   1 
ATOM   8095 H  H    . PHE   B 1 237 ? -11.773 -23.914 19.439  1.00 29.51  ? 234 PHE   B H    1 
ATOM   8096 H  HA   . PHE   B 1 237 ? -9.723  -25.493 19.663  1.00 26.89  ? 234 PHE   B HA   1 
ATOM   8097 H  HB2  . PHE   B 1 237 ? -11.003 -25.772 17.811  1.00 28.35  ? 234 PHE   B HB2  1 
ATOM   8098 H  HB3  . PHE   B 1 237 ? -10.880 -24.239 17.411  1.00 28.35  ? 234 PHE   B HB3  1 
ATOM   8099 H  HD1  . PHE   B 1 237 ? -8.954  -27.207 17.495  1.00 30.74  ? 234 PHE   B HD1  1 
ATOM   8100 H  HD2  . PHE   B 1 237 ? -9.247  -23.591 15.857  1.00 23.61  ? 234 PHE   B HD2  1 
ATOM   8101 H  HE1  . PHE   B 1 237 ? -7.225  -27.712 16.059  1.00 27.32  ? 234 PHE   B HE1  1 
ATOM   8102 H  HE2  . PHE   B 1 237 ? -7.518  -24.098 14.403  1.00 25.95  ? 234 PHE   B HE2  1 
ATOM   8103 H  HZ   . PHE   B 1 237 ? -6.478  -26.162 14.545  1.00 25.31  ? 234 PHE   B HZ   1 
ATOM   8104 N  N    . PRO   B 1 238 ? -8.743  -22.500 19.045  1.00 21.51  ? 235 PRO   B N    1 
ATOM   8105 C  CA   . PRO   B 1 238 ? -7.489  -21.727 19.062  1.00 21.05  ? 235 PRO   B CA   1 
ATOM   8106 C  C    . PRO   B 1 238 ? -6.721  -21.861 20.357  1.00 21.30  ? 235 PRO   B C    1 
ATOM   8107 O  O    . PRO   B 1 238 ? -5.482  -21.851 20.365  1.00 23.25  ? 235 PRO   B O    1 
ATOM   8108 C  CB   . PRO   B 1 238 ? -7.966  -20.288 18.784  1.00 23.83  ? 235 PRO   B CB   1 
ATOM   8109 C  CG   . PRO   B 1 238 ? -9.271  -20.457 18.031  1.00 24.81  ? 235 PRO   B CG   1 
ATOM   8110 C  CD   . PRO   B 1 238 ? -9.908  -21.687 18.654  1.00 24.64  ? 235 PRO   B CD   1 
ATOM   8111 H  HA   . PRO   B 1 238 ? -6.909  -22.001 18.334  1.00 25.31  ? 235 PRO   B HA   1 
ATOM   8112 H  HB2  . PRO   B 1 238 ? -8.104  -19.816 19.620  1.00 28.64  ? 235 PRO   B HB2  1 
ATOM   8113 H  HB3  . PRO   B 1 238 ? -7.310  -19.820 18.243  1.00 28.64  ? 235 PRO   B HB3  1 
ATOM   8114 H  HG2  . PRO   B 1 238 ? -9.831  -19.674 18.154  1.00 29.82  ? 235 PRO   B HG2  1 
ATOM   8115 H  HG3  . PRO   B 1 238 ? -9.096  -20.595 17.087  1.00 29.82  ? 235 PRO   B HG3  1 
ATOM   8116 H  HD2  . PRO   B 1 238 ? -10.439 -21.447 19.430  1.00 29.61  ? 235 PRO   B HD2  1 
ATOM   8117 H  HD3  . PRO   B 1 238 ? -10.458 -22.157 18.008  1.00 29.61  ? 235 PRO   B HD3  1 
ATOM   8118 N  N    . GLN   B 1 239 ? -7.411  -22.074 21.465  1.00 21.94  ? 236 GLN   B N    1 
ATOM   8119 C  CA   . GLN   B 1 239 ? -6.695  -22.279 22.715  1.00 23.85  ? 236 GLN   B CA   1 
ATOM   8120 C  C    . GLN   B 1 239 ? -5.976  -23.624 22.724  1.00 25.46  ? 236 GLN   B C    1 
ATOM   8121 O  O    . GLN   B 1 239 ? -4.867  -23.740 23.264  1.00 26.32  ? 236 GLN   B O    1 
ATOM   8122 C  CB   . GLN   B 1 239 ? -7.660  -22.177 23.900  1.00 24.97  ? 236 GLN   B CB   1 
ATOM   8123 C  CG   . GLN   B 1 239 ? -8.321  -20.799 23.964  1.00 27.29  ? 236 GLN   B CG   1 
ATOM   8124 C  CD   . GLN   B 1 239 ? -8.557  -20.267 25.360  1.00 24.52  ? 236 GLN   B CD   1 
ATOM   8125 O  OE1  . GLN   B 1 239 ? -8.441  -20.970 26.370  1.00 28.94  ? 236 GLN   B OE1  1 
ATOM   8126 N  NE2  . GLN   B 1 239 ? -8.926  -18.994 25.421  1.00 26.75  ? 236 GLN   B NE2  1 
ATOM   8127 H  H    . GLN   B 1 239 ? -8.268  -22.104 21.521  1.00 26.36  ? 236 GLN   B H    1 
ATOM   8128 H  HA   . GLN   B 1 239 ? -6.029  -21.580 22.812  1.00 28.67  ? 236 GLN   B HA   1 
ATOM   8129 H  HB2  . GLN   B 1 239 ? -8.356  -22.846 23.806  1.00 30.00  ? 236 GLN   B HB2  1 
ATOM   8130 H  HB3  . GLN   B 1 239 ? -7.171  -22.321 24.725  1.00 30.00  ? 236 GLN   B HB3  1 
ATOM   8131 H  HG2  . GLN   B 1 239 ? -7.751  -20.163 23.504  1.00 32.79  ? 236 GLN   B HG2  1 
ATOM   8132 H  HG3  . GLN   B 1 239 ? -9.183  -20.851 23.523  1.00 32.79  ? 236 GLN   B HG3  1 
ATOM   8133 H  HE21 . GLN   B 1 239 ? -9.013  -18.536 24.699  1.00 32.15  ? 236 GLN   B HE21 1 
ATOM   8134 H  HE22 . GLN   B 1 239 ? -9.077  -18.627 26.184  1.00 32.15  ? 236 GLN   B HE22 1 
ATOM   8135 N  N    . ASP   B 1 240 ? -6.580  -24.645 22.121  1.00 22.96  ? 237 ASP   B N    1 
ATOM   8136 C  CA   . ASP   B 1 240 ? -5.912  -25.938 21.992  1.00 26.20  ? 237 ASP   B CA   1 
ATOM   8137 C  C    . ASP   B 1 240 ? -4.662  -25.836 21.143  1.00 22.34  ? 237 ASP   B C    1 
ATOM   8138 O  O    . ASP   B 1 240 ? -3.673  -26.540 21.397  1.00 26.56  ? 237 ASP   B O    1 
ATOM   8139 C  CB   . ASP   B 1 240 ? -6.863  -26.957 21.391  1.00 28.55  ? 237 ASP   B CB   1 
ATOM   8140 C  CG   . ASP   B 1 240 ? -7.954  -27.362 22.353  1.00 33.44  ? 237 ASP   B CG   1 
ATOM   8141 O  OD1  . ASP   B 1 240 ? -7.795  -27.135 23.571  1.00 38.66  ? 237 ASP   B OD1  1 
ATOM   8142 O  OD2  . ASP   B 1 240 ? -8.970  -27.926 21.880  1.00 44.29  ? 237 ASP   B OD2  1 
ATOM   8143 H  H    . ASP   B 1 240 ? -7.370  -24.618 21.782  1.00 27.59  ? 237 ASP   B H    1 
ATOM   8144 H  HA   . ASP   B 1 240 ? -5.655  -26.244 22.876  1.00 31.48  ? 237 ASP   B HA   1 
ATOM   8145 H  HB2  . ASP   B 1 240 ? -7.281  -26.575 20.604  1.00 34.30  ? 237 ASP   B HB2  1 
ATOM   8146 H  HB3  . ASP   B 1 240 ? -6.364  -27.752 21.149  1.00 34.30  ? 237 ASP   B HB3  1 
ATOM   8147 N  N    . VAL   B 1 241 ? -4.674  -24.976 20.128  1.00 20.68  ? 238 VAL   B N    1 
ATOM   8148 C  CA   . VAL   B 1 241 ? -3.469  -24.765 19.322  1.00 18.33  ? 238 VAL   B CA   1 
ATOM   8149 C  C    . VAL   B 1 241 ? -2.361  -24.183 20.205  1.00 19.77  ? 238 VAL   B C    1 
ATOM   8150 O  O    . VAL   B 1 241 ? -1.219  -24.661 20.213  1.00 22.50  ? 238 VAL   B O    1 
ATOM   8151 C  CB   . VAL   B 1 241 ? -3.763  -23.849 18.126  1.00 20.55  ? 238 VAL   B CB   1 
ATOM   8152 C  CG1  . VAL   B 1 241 ? -2.526  -23.578 17.325  1.00 21.31  ? 238 VAL   B CG1  1 
ATOM   8153 C  CG2  . VAL   B 1 241 ? -4.812  -24.503 17.217  1.00 19.75  ? 238 VAL   B CG2  1 
ATOM   8154 H  H    . VAL   B 1 241 ? -5.354  -24.508 19.887  1.00 24.86  ? 238 VAL   B H    1 
ATOM   8155 H  HA   . VAL   B 1 241 ? -3.177  -25.621 18.971  1.00 22.04  ? 238 VAL   B HA   1 
ATOM   8156 H  HB   . VAL   B 1 241 ? -4.098  -23.004 18.467  1.00 24.71  ? 238 VAL   B HB   1 
ATOM   8157 H  HG11 . VAL   B 1 241 ? -2.762  -23.049 16.547  1.00 25.61  ? 238 VAL   B HG11 1 
ATOM   8158 H  HG12 . VAL   B 1 241 ? -1.893  -23.091 17.876  1.00 25.61  ? 238 VAL   B HG12 1 
ATOM   8159 H  HG13 . VAL   B 1 241 ? -2.140  -24.422 17.045  1.00 25.61  ? 238 VAL   B HG13 1 
ATOM   8160 H  HG21 . VAL   B 1 241 ? -5.008  -23.904 16.480  1.00 23.74  ? 238 VAL   B HG21 1 
ATOM   8161 H  HG22 . VAL   B 1 241 ? -4.458  -25.340 16.878  1.00 23.74  ? 238 VAL   B HG22 1 
ATOM   8162 H  HG23 . VAL   B 1 241 ? -5.617  -24.668 17.732  1.00 23.74  ? 238 VAL   B HG23 1 
ATOM   8163 N  N    . ASN   B 1 242 ? -2.682  -23.130 20.976  1.00 20.24  ? 239 ASN   B N    1 
ATOM   8164 C  CA   . ASN   B 1 242 ? -1.686  -22.558 21.896  1.00 19.74  ? 239 ASN   B CA   1 
ATOM   8165 C  C    . ASN   B 1 242 ? -1.201  -23.592 22.919  1.00 21.39  ? 239 ASN   B C    1 
ATOM   8166 O  O    . ASN   B 1 242 ? -0.004  -23.658 23.222  1.00 21.87  ? 239 ASN   B O    1 
ATOM   8167 C  CB   . ASN   B 1 242 ? -2.259  -21.315 22.582  1.00 20.93  ? 239 ASN   B CB   1 
ATOM   8168 C  CG   . ASN   B 1 242 ? -2.113  -20.058 21.731  1.00 20.61  ? 239 ASN   B CG   1 
ATOM   8169 O  OD1  . ASN   B 1 242 ? -1.345  -20.019 20.769  1.00 21.04  ? 239 ASN   B OD1  1 
ATOM   8170 N  ND2  . ASN   B 1 242 ? -2.850  -19.003 22.093  1.00 23.50  ? 239 ASN   B ND2  1 
ATOM   8171 H  H    . ASN   B 1 242 ? -3.449  -22.740 20.985  1.00 24.33  ? 239 ASN   B H    1 
ATOM   8172 H  HA   . ASN   B 1 242 ? -0.910  -22.278 21.385  1.00 23.72  ? 239 ASN   B HA   1 
ATOM   8173 H  HB2  . ASN   B 1 242 ? -3.204  -21.455 22.753  1.00 25.16  ? 239 ASN   B HB2  1 
ATOM   8174 H  HB3  . ASN   B 1 242 ? -1.789  -21.169 23.418  1.00 25.16  ? 239 ASN   B HB3  1 
ATOM   8175 H  HD21 . ASN   B 1 242 ? -2.803  -18.271 21.645  1.00 28.24  ? 239 ASN   B HD21 1 
ATOM   8176 H  HD22 . ASN   B 1 242 ? -3.372  -19.057 22.775  1.00 28.24  ? 239 ASN   B HD22 1 
ATOM   8177 N  N    . PHE   B 1 243 ? -2.102  -24.417 23.465  1.00 22.88  ? 240 PHE   B N    1 
ATOM   8178 C  CA   . PHE   B 1 243 ? -1.655  -25.427 24.418  1.00 25.29  ? 240 PHE   B CA   1 
ATOM   8179 C  C    . PHE   B 1 243 ? -0.666  -26.397 23.787  1.00 23.02  ? 240 PHE   B C    1 
ATOM   8180 O  O    . PHE   B 1 243 ? 0.291   -26.830 24.451  1.00 24.33  ? 240 PHE   B O    1 
ATOM   8181 C  CB   . PHE   B 1 243 ? -2.835  -26.211 25.009  1.00 27.81  ? 240 PHE   B CB   1 
ATOM   8182 C  CG   . PHE   B 1 243 ? -3.676  -25.399 25.961  1.00 36.39  ? 240 PHE   B CG   1 
ATOM   8183 C  CD1  . PHE   B 1 243 ? -3.084  -24.669 26.972  1.00 37.61  ? 240 PHE   B CD1  1 
ATOM   8184 C  CD2  . PHE   B 1 243 ? -5.062  -25.400 25.857  1.00 37.58  ? 240 PHE   B CD2  1 
ATOM   8185 C  CE1  . PHE   B 1 243 ? -3.852  -23.915 27.848  1.00 45.45  ? 240 PHE   B CE1  1 
ATOM   8186 C  CE2  . PHE   B 1 243 ? -5.835  -24.645 26.725  1.00 39.48  ? 240 PHE   B CE2  1 
ATOM   8187 C  CZ   . PHE   B 1 243 ? -5.234  -23.898 27.709  1.00 43.32  ? 240 PHE   B CZ   1 
ATOM   8188 H  H    . PHE   B 1 243 ? -2.947  -24.410 23.305  1.00 27.50  ? 240 PHE   B H    1 
ATOM   8189 H  HA   . PHE   B 1 243 ? -1.217  -24.956 25.145  1.00 30.40  ? 240 PHE   B HA   1 
ATOM   8190 H  HB2  . PHE   B 1 243 ? -3.408  -26.508 24.285  1.00 33.41  ? 240 PHE   B HB2  1 
ATOM   8191 H  HB3  . PHE   B 1 243 ? -2.491  -26.976 25.495  1.00 33.41  ? 240 PHE   B HB3  1 
ATOM   8192 H  HD1  . PHE   B 1 243 ? -2.159  -24.682 27.067  1.00 45.18  ? 240 PHE   B HD1  1 
ATOM   8193 H  HD2  . PHE   B 1 243 ? -5.474  -25.911 25.198  1.00 45.14  ? 240 PHE   B HD2  1 
ATOM   8194 H  HE1  . PHE   B 1 243 ? -3.443  -23.424 28.525  1.00 54.58  ? 240 PHE   B HE1  1 
ATOM   8195 H  HE2  . PHE   B 1 243 ? -6.761  -24.644 26.642  1.00 47.42  ? 240 PHE   B HE2  1 
ATOM   8196 H  HZ   . PHE   B 1 243 ? -5.752  -23.380 28.282  1.00 52.02  ? 240 PHE   B HZ   1 
ATOM   8197 N  N    . TYR   B 1 244 ? -0.906  -26.784 22.522  1.00 23.21  ? 241 TYR   B N    1 
ATOM   8198 C  CA   . TYR   B 1 244 ? 0.024   -27.675 21.829  1.00 25.77  ? 241 TYR   B CA   1 
ATOM   8199 C  C    . TYR   B 1 244 ? 1.387   -27.017 21.627  1.00 24.49  ? 241 TYR   B C    1 
ATOM   8200 O  O    . TYR   B 1 244 ? 2.434   -27.618 21.904  1.00 23.67  ? 241 TYR   B O    1 
ATOM   8201 C  CB   . TYR   B 1 244 ? -0.537  -28.093 20.480  1.00 23.84  ? 241 TYR   B CB   1 
ATOM   8202 C  CG   . TYR   B 1 244 ? 0.335   -29.101 19.804  1.00 25.42  ? 241 TYR   B CG   1 
ATOM   8203 C  CD1  . TYR   B 1 244 ? 0.383   -30.410 20.259  1.00 28.90  ? 241 TYR   B CD1  1 
ATOM   8204 C  CD2  . TYR   B 1 244 ? 1.156   -28.736 18.730  1.00 25.09  ? 241 TYR   B CD2  1 
ATOM   8205 C  CE1  . TYR   B 1 244 ? 1.181   -31.335 19.649  1.00 27.52  ? 241 TYR   B CE1  1 
ATOM   8206 C  CE2  . TYR   B 1 244 ? 1.964   -29.664 18.117  1.00 27.26  ? 241 TYR   B CE2  1 
ATOM   8207 C  CZ   . TYR   B 1 244 ? 1.982   -30.946 18.583  1.00 31.73  ? 241 TYR   B CZ   1 
ATOM   8208 O  OH   . TYR   B 1 244 ? 2.773   -31.902 17.992  1.00 34.86  ? 241 TYR   B OH   1 
ATOM   8209 H  H    . TYR   B 1 244 ? -1.589  -26.547 22.056  1.00 27.89  ? 241 TYR   B H    1 
ATOM   8210 H  HA   . TYR   B 1 244 ? 0.134   -28.467 22.379  1.00 30.97  ? 241 TYR   B HA   1 
ATOM   8211 H  HB2  . TYR   B 1 244 ? -1.414  -28.486 20.607  1.00 28.65  ? 241 TYR   B HB2  1 
ATOM   8212 H  HB3  . TYR   B 1 244 ? -0.602  -27.314 19.907  1.00 28.65  ? 241 TYR   B HB3  1 
ATOM   8213 H  HD1  . TYR   B 1 244 ? -0.135  -30.661 20.989  1.00 34.73  ? 241 TYR   B HD1  1 
ATOM   8214 H  HD2  . TYR   B 1 244 ? 1.154   -27.857 18.428  1.00 30.15  ? 241 TYR   B HD2  1 
ATOM   8215 H  HE1  . TYR   B 1 244 ? 1.188   -32.217 19.944  1.00 33.07  ? 241 TYR   B HE1  1 
ATOM   8216 H  HE2  . TYR   B 1 244 ? 2.494   -29.420 17.393  1.00 32.75  ? 241 TYR   B HE2  1 
ATOM   8217 H  HH   . TYR   B 1 244 ? 3.199   -31.566 17.351  1.00 41.88  ? 241 TYR   B HH   1 
ATOM   8218 N  N    . ILE   B 1 245 ? 1.392   -25.772 21.162  1.00 23.12  ? 242 ILE   B N    1 
ATOM   8219 C  CA   . ILE   B 1 245 ? 2.662   -25.069 20.964  1.00 21.98  ? 242 ILE   B CA   1 
ATOM   8220 C  C    . ILE   B 1 245 ? 3.441   -25.005 22.277  1.00 21.58  ? 242 ILE   B C    1 
ATOM   8221 O  O    . ILE   B 1 245 ? 4.634   -25.329 22.339  1.00 25.13  ? 242 ILE   B O    1 
ATOM   8222 C  CB   . ILE   B 1 245 ? 2.418   -23.655 20.416  1.00 20.14  ? 242 ILE   B CB   1 
ATOM   8223 C  CG1  . ILE   B 1 245 ? 1.772   -23.691 19.033  1.00 21.97  ? 242 ILE   B CG1  1 
ATOM   8224 C  CG2  . ILE   B 1 245 ? 3.723   -22.858 20.389  1.00 22.50  ? 242 ILE   B CG2  1 
ATOM   8225 C  CD1  . ILE   B 1 245 ? 1.311   -22.292 18.588  1.00 25.45  ? 242 ILE   B CD1  1 
ATOM   8226 H  H    . ILE   B 1 245 ? 0.691   -25.317 20.958  1.00 27.78  ? 242 ILE   B H    1 
ATOM   8227 H  HA   . ILE   B 1 245 ? 3.183   -25.566 20.314  1.00 26.42  ? 242 ILE   B HA   1 
ATOM   8228 H  HB   . ILE   B 1 245 ? 1.796   -23.211 21.014  1.00 24.21  ? 242 ILE   B HB   1 
ATOM   8229 H  HG12 . ILE   B 1 245 ? 2.417   -24.020 18.387  1.00 26.41  ? 242 ILE   B HG12 1 
ATOM   8230 H  HG13 . ILE   B 1 245 ? 0.998   -24.275 19.057  1.00 26.41  ? 242 ILE   B HG13 1 
ATOM   8231 H  HG21 . ILE   B 1 245 ? 3.588   -22.049 19.871  1.00 27.04  ? 242 ILE   B HG21 1 
ATOM   8232 H  HG22 . ILE   B 1 245 ? 3.974   -22.632 21.298  1.00 27.04  ? 242 ILE   B HG22 1 
ATOM   8233 H  HG23 . ILE   B 1 245 ? 4.416   -23.400 19.979  1.00 27.04  ? 242 ILE   B HG23 1 
ATOM   8234 H  HD11 . ILE   B 1 245 ? 0.709   -22.383 17.833  1.00 30.59  ? 242 ILE   B HD11 1 
ATOM   8235 H  HD12 . ILE   B 1 245 ? 0.853   -21.861 19.326  1.00 30.59  ? 242 ILE   B HD12 1 
ATOM   8236 H  HD13 . ILE   B 1 245 ? 2.087   -21.770 18.331  1.00 30.59  ? 242 ILE   B HD13 1 
ATOM   8237 N  N    . ASN   B 1 246 ? 2.756   -24.622 23.367  1.00 21.97  ? 243 ASN   B N    1 
ATOM   8238 C  CA   . ASN   B 1 246 ? 3.392   -24.549 24.671  1.00 23.57  ? 243 ASN   B CA   1 
ATOM   8239 C  C    . ASN   B 1 246 ? 3.917   -25.907 25.125  1.00 24.00  ? 243 ASN   B C    1 
ATOM   8240 O  O    . ASN   B 1 246 ? 5.029   -26.003 25.661  1.00 26.35  ? 243 ASN   B O    1 
ATOM   8241 C  CB   . ASN   B 1 246 ? 2.394   -23.984 25.683  1.00 23.86  ? 243 ASN   B CB   1 
ATOM   8242 C  CG   . ASN   B 1 246 ? 2.845   -24.140 27.109  1.00 27.91  ? 243 ASN   B CG   1 
ATOM   8243 O  OD1  . ASN   B 1 246 ? 2.440   -25.084 27.799  1.00 28.95  ? 243 ASN   B OD1  1 
ATOM   8244 N  ND2  . ASN   B 1 246 ? 3.684   -23.208 27.570  1.00 28.02  ? 243 ASN   B ND2  1 
ATOM   8245 H  H    . ASN   B 1 246 ? 1.924   -24.402 23.370  1.00 26.41  ? 243 ASN   B H    1 
ATOM   8246 H  HA   . ASN   B 1 246 ? 4.156   -23.953 24.620  1.00 28.32  ? 243 ASN   B HA   1 
ATOM   8247 H  HB2  . ASN   B 1 246 ? 2.273   -23.037 25.510  1.00 28.67  ? 243 ASN   B HB2  1 
ATOM   8248 H  HB3  . ASN   B 1 246 ? 1.549   -24.449 25.585  1.00 28.67  ? 243 ASN   B HB3  1 
ATOM   8249 H  HD21 . ASN   B 1 246 ? 3.972   -23.251 28.379  1.00 33.66  ? 243 ASN   B HD21 1 
ATOM   8250 H  HD22 . ASN   B 1 246 ? 3.936   -22.565 27.058  1.00 33.66  ? 243 ASN   B HD22 1 
ATOM   8251 N  N    . LYS   B 1 247 ? 3.122   -26.973 24.956  1.00 26.92  ? 244 LYS   B N    1 
ATOM   8252 C  CA   . LYS   B 1 247 ? 3.550   -28.314 25.364  1.00 30.94  ? 244 LYS   B CA   1 
ATOM   8253 C  C    . LYS   B 1 247 ? 4.857   -28.702 24.692  1.00 29.74  ? 244 LYS   B C    1 
ATOM   8254 O  O    . LYS   B 1 247 ? 5.753   -29.279 25.320  1.00 32.08  ? 244 LYS   B O    1 
ATOM   8255 C  CB   . LYS   B 1 247 ? 2.467   -29.328 24.992  1.00 31.86  ? 244 LYS   B CB   1 
ATOM   8256 C  CG   . LYS   B 1 247 ? 2.618   -30.710 25.593  1.00 45.53  ? 244 LYS   B CG   1 
ATOM   8257 C  CD   . LYS   B 1 247 ? 1.279   -31.457 25.543  1.00 57.33  ? 244 LYS   B CD   1 
ATOM   8258 C  CE   . LYS   B 1 247 ? 1.430   -32.934 25.902  1.00 69.90  ? 244 LYS   B CE   1 
ATOM   8259 N  NZ   . LYS   B 1 247 ? 2.491   -33.634 25.118  1.00 82.75  ? 244 LYS   B NZ   1 
ATOM   8260 H  H    . LYS   B 1 247 ? 2.336   -26.945 24.608  1.00 32.35  ? 244 LYS   B H    1 
ATOM   8261 H  HA   . LYS   B 1 247 ? 3.680   -28.323 26.326  1.00 37.18  ? 244 LYS   B HA   1 
ATOM   8262 H  HB2  . LYS   B 1 247 ? 1.611   -28.979 25.286  1.00 38.28  ? 244 LYS   B HB2  1 
ATOM   8263 H  HB3  . LYS   B 1 247 ? 2.469   -29.433 24.028  1.00 38.28  ? 244 LYS   B HB3  1 
ATOM   8264 H  HG2  . LYS   B 1 247 ? 3.275   -31.215 25.089  1.00 54.68  ? 244 LYS   B HG2  1 
ATOM   8265 H  HG3  . LYS   B 1 247 ? 2.897   -30.634 26.519  1.00 54.68  ? 244 LYS   B HG3  1 
ATOM   8266 H  HD2  . LYS   B 1 247 ? 0.665   -31.053 26.176  1.00 68.84  ? 244 LYS   B HD2  1 
ATOM   8267 H  HD3  . LYS   B 1 247 ? 0.916   -31.399 24.645  1.00 68.84  ? 244 LYS   B HD3  1 
ATOM   8268 H  HE2  . LYS   B 1 247 ? 1.660   -33.006 26.841  1.00 83.92  ? 244 LYS   B HE2  1 
ATOM   8269 H  HE3  . LYS   B 1 247 ? 0.589   -33.385 25.731  1.00 83.92  ? 244 LYS   B HE3  1 
ATOM   8270 H  HZ1  . LYS   B 1 247 ? 2.517   -34.495 25.342  1.00 99.34  ? 244 LYS   B HZ1  1 
ATOM   8271 H  HZ2  . LYS   B 1 247 ? 2.320   -33.568 24.247  1.00 99.34  ? 244 LYS   B HZ2  1 
ATOM   8272 H  HZ3  . LYS   B 1 247 ? 3.285   -33.268 25.285  1.00 99.34  ? 244 LYS   B HZ3  1 
ATOM   8273 N  N    . GLU   B 1 248 ? 4.980   -28.393 23.399  1.00 27.31  ? 245 GLU   B N    1 
ATOM   8274 C  CA   . GLU   B 1 248 ? 6.095   -28.885 22.610  1.00 32.56  ? 245 GLU   B CA   1 
ATOM   8275 C  C    . GLU   B 1 248 ? 7.309   -27.971 22.620  1.00 29.58  ? 245 GLU   B C    1 
ATOM   8276 O  O    . GLU   B 1 248 ? 8.422   -28.453 22.368  1.00 35.79  ? 245 GLU   B O    1 
ATOM   8277 C  CB   . GLU   B 1 248 ? 5.684   -29.082 21.151  1.00 31.31  ? 245 GLU   B CB   1 
ATOM   8278 C  CG   . GLU   B 1 248 ? 4.592   -30.143 20.939  1.00 30.38  ? 245 GLU   B CG   1 
ATOM   8279 C  CD   . GLU   B 1 248 ? 5.073   -31.539 21.240  1.00 41.16  ? 245 GLU   B CD   1 
ATOM   8280 O  OE1  . GLU   B 1 248 ? 6.238   -31.865 20.922  1.00 56.00  ? 245 GLU   B OE1  1 
ATOM   8281 O  OE2  . GLU   B 1 248 ? 4.291   -32.290 21.852  1.00 47.75  ? 245 GLU   B OE2  1 
ATOM   8282 H  H    . GLU   B 1 248 ? 4.427   -27.900 22.962  1.00 32.81  ? 245 GLU   B H    1 
ATOM   8283 H  HA   . GLU   B 1 248 ? 6.349   -29.743 22.985  1.00 39.12  ? 245 GLU   B HA   1 
ATOM   8284 H  HB2  . GLU   B 1 248 ? 5.346   -28.240 20.808  1.00 37.61  ? 245 GLU   B HB2  1 
ATOM   8285 H  HB3  . GLU   B 1 248 ? 6.464   -29.358 20.644  1.00 37.61  ? 245 GLU   B HB3  1 
ATOM   8286 H  HG2  . GLU   B 1 248 ? 3.844   -29.949 21.526  1.00 36.50  ? 245 GLU   B HG2  1 
ATOM   8287 H  HG3  . GLU   B 1 248 ? 4.302   -30.118 20.014  1.00 36.50  ? 245 GLU   B HG3  1 
ATOM   8288 N  N    . THR   B 1 249 ? 7.123   -26.675 22.901  1.00 27.94  ? 246 THR   B N    1 
ATOM   8289 C  CA   . THR   B 1 249 ? 8.200   -25.699 22.808  1.00 27.46  ? 246 THR   B CA   1 
ATOM   8290 C  C    . THR   B 1 249 ? 8.528   -24.984 24.113  1.00 28.09  ? 246 THR   B C    1 
ATOM   8291 O  O    . THR   B 1 249 ? 9.569   -24.334 24.181  1.00 29.04  ? 246 THR   B O    1 
ATOM   8292 C  CB   . THR   B 1 249 ? 7.883   -24.600 21.779  1.00 28.85  ? 246 THR   B CB   1 
ATOM   8293 O  OG1  . THR   B 1 249 ? 6.864   -23.740 22.297  1.00 24.70  ? 246 THR   B OG1  1 
ATOM   8294 C  CG2  . THR   B 1 249 ? 7.421   -25.156 20.432  1.00 28.11  ? 246 THR   B CG2  1 
ATOM   8295 H  H    . THR   B 1 249 ? 6.371   -26.339 23.150  1.00 33.57  ? 246 THR   B H    1 
ATOM   8296 H  HA   . THR   B 1 249 ? 8.984   -26.186 22.511  1.00 32.99  ? 246 THR   B HA   1 
ATOM   8297 H  HB   . THR   B 1 249 ? 8.701   -24.105 21.615  1.00 34.67  ? 246 THR   B HB   1 
ATOM   8298 H  HG1  . THR   B 1 249 ? 6.171   -24.183 22.463  1.00 29.68  ? 246 THR   B HG1  1 
ATOM   8299 H  HG21 . THR   B 1 249 ? 7.269   -24.430 19.808  1.00 33.77  ? 246 THR   B HG21 1 
ATOM   8300 H  HG22 . THR   B 1 249 ? 8.097   -25.748 20.068  1.00 33.77  ? 246 THR   B HG22 1 
ATOM   8301 H  HG23 . THR   B 1 249 ? 6.595   -25.653 20.544  1.00 33.77  ? 246 THR   B HG23 1 
ATOM   8302 N  N    . GLY   B 1 250 ? 7.650   -25.018 25.105  1.00 26.90  ? 247 GLY   B N    1 
ATOM   8303 C  CA   . GLY   B 1 250 ? 7.841   -24.250 26.319  1.00 25.98  ? 247 GLY   B CA   1 
ATOM   8304 C  C    . GLY   B 1 250 ? 7.530   -22.770 26.205  1.00 25.45  ? 247 GLY   B C    1 
ATOM   8305 O  O    . GLY   B 1 250 ? 7.676   -22.035 27.197  1.00 27.63  ? 247 GLY   B O    1 
ATOM   8306 H  H    . GLY   B 1 250 ? 6.928   -25.485 25.097  1.00 32.32  ? 247 GLY   B H    1 
ATOM   8307 H  HA2  . GLY   B 1 250 ? 7.269   -24.618 27.011  1.00 31.21  ? 247 GLY   B HA2  1 
ATOM   8308 H  HA3  . GLY   B 1 250 ? 8.767   -24.335 26.596  1.00 31.21  ? 247 GLY   B HA3  1 
ATOM   8309 N  N    . ILE   B 1 251 ? 7.138   -22.302 25.031  1.00 24.03  ? 248 ILE   B N    1 
ATOM   8310 C  CA   . ILE   B 1 251 ? 6.787   -20.885 24.856  1.00 24.07  ? 248 ILE   B CA   1 
ATOM   8311 C  C    . ILE   B 1 251 ? 5.610   -20.567 25.766  1.00 25.09  ? 248 ILE   B C    1 
ATOM   8312 O  O    . ILE   B 1 251 ? 4.618   -21.332 25.779  1.00 23.99  ? 248 ILE   B O    1 
ATOM   8313 C  CB   . ILE   B 1 251 ? 6.448   -20.598 23.374  1.00 24.74  ? 248 ILE   B CB   1 
ATOM   8314 C  CG1  . ILE   B 1 251 ? 7.750   -20.653 22.553  1.00 27.02  ? 248 ILE   B CG1  1 
ATOM   8315 C  CG2  . ILE   B 1 251 ? 5.764   -19.254 23.246  1.00 25.07  ? 248 ILE   B CG2  1 
ATOM   8316 C  CD1  . ILE   B 1 251 ? 7.531   -20.785 21.061  1.00 26.92  ? 248 ILE   B CD1  1 
ATOM   8317 H  H    . ILE   B 1 251 ? 7.065   -22.773 24.315  1.00 28.87  ? 248 ILE   B H    1 
ATOM   8318 H  HA   . ILE   B 1 251 ? 7.534   -20.320 25.108  1.00 28.92  ? 248 ILE   B HA   1 
ATOM   8319 H  HB   . ILE   B 1 251 ? 5.834   -21.268 23.036  1.00 29.73  ? 248 ILE   B HB   1 
ATOM   8320 H  HG12 . ILE   B 1 251 ? 8.250   -19.836 22.707  1.00 32.46  ? 248 ILE   B HG12 1 
ATOM   8321 H  HG13 . ILE   B 1 251 ? 8.269   -21.419 22.844  1.00 32.46  ? 248 ILE   B HG13 1 
ATOM   8322 H  HG21 . ILE   B 1 251 ? 5.545   -19.099 22.314  1.00 30.12  ? 248 ILE   B HG21 1 
ATOM   8323 H  HG22 . ILE   B 1 251 ? 4.953   -19.260 23.779  1.00 30.12  ? 248 ILE   B HG22 1 
ATOM   8324 H  HG23 . ILE   B 1 251 ? 6.364   -18.562 23.565  1.00 30.12  ? 248 ILE   B HG23 1 
ATOM   8325 H  HD11 . ILE   B 1 251 ? 8.389   -20.902 20.625  1.00 32.34  ? 248 ILE   B HD11 1 
ATOM   8326 H  HD12 . ILE   B 1 251 ? 6.965   -21.554 20.891  1.00 32.34  ? 248 ILE   B HD12 1 
ATOM   8327 H  HD13 . ILE   B 1 251 ? 7.101   -19.979 20.732  1.00 32.34  ? 248 ILE   B HD13 1 
ATOM   8328 N  N    . PRO   B 1 252 ? 5.658   -19.474 26.525  1.00 23.23  ? 249 PRO   B N    1 
ATOM   8329 C  CA   . PRO   B 1 252 ? 4.646   -19.242 27.559  1.00 23.82  ? 249 PRO   B CA   1 
ATOM   8330 C  C    . PRO   B 1 252 ? 3.302   -18.808 26.985  1.00 23.96  ? 249 PRO   B C    1 
ATOM   8331 O  O    . PRO   B 1 252 ? 3.217   -18.113 25.971  1.00 22.00  ? 249 PRO   B O    1 
ATOM   8332 C  CB   . PRO   B 1 252 ? 5.248   -18.125 28.411  1.00 24.33  ? 249 PRO   B CB   1 
ATOM   8333 C  CG   . PRO   B 1 252 ? 6.257   -17.429 27.489  1.00 25.50  ? 249 PRO   B CG   1 
ATOM   8334 C  CD   . PRO   B 1 252 ? 6.753   -18.477 26.562  1.00 22.39  ? 249 PRO   B CD   1 
ATOM   8335 H  HA   . PRO   B 1 252 ? 4.529   -20.048 28.086  1.00 28.62  ? 249 PRO   B HA   1 
ATOM   8336 H  HB2  . PRO   B 1 252 ? 4.552   -17.511 28.692  1.00 29.23  ? 249 PRO   B HB2  1 
ATOM   8337 H  HB3  . PRO   B 1 252 ? 5.690   -18.503 29.188  1.00 29.23  ? 249 PRO   B HB3  1 
ATOM   8338 H  HG2  . PRO   B 1 252 ? 5.815   -16.718 26.998  1.00 30.64  ? 249 PRO   B HG2  1 
ATOM   8339 H  HG3  . PRO   B 1 252 ? 6.985   -17.065 28.016  1.00 30.64  ? 249 PRO   B HG3  1 
ATOM   8340 H  HD2  . PRO   B 1 252 ? 6.909   -18.107 25.679  1.00 26.91  ? 249 PRO   B HD2  1 
ATOM   8341 H  HD3  . PRO   B 1 252 ? 7.569   -18.877 26.902  1.00 26.91  ? 249 PRO   B HD3  1 
ATOM   8342 N  N    . ILE   B 1 253 ? 2.251   -19.237 27.680  1.00 23.72  ? 250 ILE   B N    1 
ATOM   8343 C  CA   . ILE   B 1 253 ? 0.897   -18.740 27.485  1.00 23.45  ? 250 ILE   B CA   1 
ATOM   8344 C  C    . ILE   B 1 253 ? 0.598   -17.712 28.566  1.00 23.68  ? 250 ILE   B C    1 
ATOM   8345 O  O    . ILE   B 1 253 ? 0.794   -17.971 29.767  1.00 26.81  ? 250 ILE   B O    1 
ATOM   8346 C  CB   . ILE   B 1 253 ? -0.145  -19.862 27.562  1.00 24.00  ? 250 ILE   B CB   1 
ATOM   8347 C  CG1  . ILE   B 1 253 ? 0.076   -20.878 26.459  1.00 24.39  ? 250 ILE   B CG1  1 
ATOM   8348 C  CG2  . ILE   B 1 253 ? -1.564  -19.275 27.422  1.00 29.68  ? 250 ILE   B CG2  1 
ATOM   8349 C  CD1  . ILE   B 1 253 ? -0.782  -22.136 26.554  1.00 25.85  ? 250 ILE   B CD1  1 
ATOM   8350 H  H    . ILE   B 1 253 ? 2.302   -19.839 28.292  1.00 28.51  ? 250 ILE   B H    1 
ATOM   8351 H  HA   . ILE   B 1 253 ? 0.853   -18.325 26.610  1.00 28.18  ? 250 ILE   B HA   1 
ATOM   8352 H  HB   . ILE   B 1 253 ? -0.048  -20.299 28.423  1.00 28.84  ? 250 ILE   B HB   1 
ATOM   8353 H  HG12 . ILE   B 1 253 ? -0.122  -20.455 25.609  1.00 29.31  ? 250 ILE   B HG12 1 
ATOM   8354 H  HG13 . ILE   B 1 253 ? 1.004   -21.158 26.483  1.00 29.31  ? 250 ILE   B HG13 1 
ATOM   8355 H  HG21 . ILE   B 1 253 ? -2.192  -19.999 27.274  1.00 35.66  ? 250 ILE   B HG21 1 
ATOM   8356 H  HG22 . ILE   B 1 253 ? -1.792  -18.801 28.238  1.00 35.66  ? 250 ILE   B HG22 1 
ATOM   8357 H  HG23 . ILE   B 1 253 ? -1.580  -18.664 26.669  1.00 35.66  ? 250 ILE   B HG23 1 
ATOM   8358 H  HD11 . ILE   B 1 253 ? -0.468  -22.782 25.902  1.00 31.06  ? 250 ILE   B HD11 1 
ATOM   8359 H  HD12 . ILE   B 1 253 ? -0.706  -22.504 27.448  1.00 31.06  ? 250 ILE   B HD12 1 
ATOM   8360 H  HD13 . ILE   B 1 253 ? -1.706  -21.903 26.370  1.00 31.06  ? 250 ILE   B HD13 1 
ATOM   8361 N  N    . VAL   B 1 254 ? 0.089   -16.567 28.144  1.00 24.45  ? 251 VAL   B N    1 
ATOM   8362 C  CA   . VAL   B 1 254 ? -0.428  -15.538 29.030  1.00 20.99  ? 251 VAL   B CA   1 
ATOM   8363 C  C    . VAL   B 1 254 ? -1.934  -15.460 28.831  1.00 22.49  ? 251 VAL   B C    1 
ATOM   8364 O  O    . VAL   B 1 254 ? -2.417  -15.400 27.690  1.00 22.36  ? 251 VAL   B O    1 
ATOM   8365 C  CB   . VAL   B 1 254 ? 0.255   -14.190 28.755  1.00 23.36  ? 251 VAL   B CB   1 
ATOM   8366 C  CG1  . VAL   B 1 254 ? -0.477  -13.065 29.453  1.00 28.16  ? 251 VAL   B CG1  1 
ATOM   8367 C  CG2  . VAL   B 1 254 ? 1.731   -14.249 29.158  1.00 26.71  ? 251 VAL   B CG2  1 
ATOM   8368 H  H    . VAL   B 1 254 ? 0.029   -16.353 27.313  1.00 29.38  ? 251 VAL   B H    1 
ATOM   8369 H  HA   . VAL   B 1 254 ? -0.263  -15.776 29.956  1.00 25.23  ? 251 VAL   B HA   1 
ATOM   8370 H  HB   . VAL   B 1 254 ? 0.221   -14.003 27.803  1.00 28.07  ? 251 VAL   B HB   1 
ATOM   8371 H  HG11 . VAL   B 1 254 ? 0.108   -12.293 29.506  1.00 33.83  ? 251 VAL   B HG11 1 
ATOM   8372 H  HG12 . VAL   B 1 254 ? -1.273  -12.844 28.946  1.00 33.83  ? 251 VAL   B HG12 1 
ATOM   8373 H  HG13 . VAL   B 1 254 ? -0.723  -13.355 30.346  1.00 33.83  ? 251 VAL   B HG13 1 
ATOM   8374 H  HG21 . VAL   B 1 254 ? 2.124   -13.369 29.046  1.00 32.09  ? 251 VAL   B HG21 1 
ATOM   8375 H  HG22 . VAL   B 1 254 ? 1.794   -14.523 30.086  1.00 32.09  ? 251 VAL   B HG22 1 
ATOM   8376 H  HG23 . VAL   B 1 254 ? 2.188   -14.890 28.591  1.00 32.09  ? 251 VAL   B HG23 1 
ATOM   8377 N  N    . ASP   B 1 255 ? -2.679  -15.464 29.927  1.00 27.86  ? 252 ASP   B N    1 
ATOM   8378 C  CA   . ASP   B 1 255 ? -4.120  -15.300 29.863  1.00 27.36  ? 252 ASP   B CA   1 
ATOM   8379 C  C    . ASP   B 1 255 ? -4.461  -13.817 29.837  1.00 24.94  ? 252 ASP   B C    1 
ATOM   8380 O  O    . ASP   B 1 255 ? -3.831  -12.993 30.517  1.00 28.63  ? 252 ASP   B O    1 
ATOM   8381 C  CB   . ASP   B 1 255 ? -4.831  -15.973 31.035  1.00 30.39  ? 252 ASP   B CB   1 
ATOM   8382 C  CG   . ASP   B 1 255 ? -4.715  -17.496 30.981  1.00 35.10  ? 252 ASP   B CG   1 
ATOM   8383 O  OD1  . ASP   B 1 255 ? -4.721  -18.068 29.881  1.00 36.62  ? 252 ASP   B OD1  1 
ATOM   8384 O  OD2  . ASP   B 1 255 ? -4.657  -18.123 32.062  1.00 44.18  ? 252 ASP   B OD2  1 
ATOM   8385 H  H    . ASP   B 1 255 ? -2.369  -15.559 30.723  1.00 33.48  ? 252 ASP   B H    1 
ATOM   8386 H  HA   . ASP   B 1 255 ? -4.446  -15.724 29.054  1.00 32.88  ? 252 ASP   B HA   1 
ATOM   8387 H  HB2  . ASP   B 1 255 ? -4.435  -15.669 31.866  1.00 36.50  ? 252 ASP   B HB2  1 
ATOM   8388 H  HB3  . ASP   B 1 255 ? -5.773  -15.740 31.012  1.00 36.50  ? 252 ASP   B HB3  1 
ATOM   8389 N  N    . ILE   B 1 256 ? -5.454  -13.474 29.023  1.00 26.31  ? 253 ILE   B N    1 
ATOM   8390 C  CA   . ILE   B 1 256 ? -5.767  -12.061 28.807  1.00 27.03  ? 253 ILE   B CA   1 
ATOM   8391 C  C    . ILE   B 1 256 ? -7.280  -11.892 28.748  1.00 24.68  ? 253 ILE   B C    1 
ATOM   8392 O  O    . ILE   B 1 256 ? -8.024  -12.815 28.364  1.00 28.90  ? 253 ILE   B O    1 
ATOM   8393 C  CB   . ILE   B 1 256 ? -5.100  -11.567 27.476  1.00 22.22  ? 253 ILE   B CB   1 
ATOM   8394 C  CG1  . ILE   B 1 256 ? -5.009  -10.059 27.439  1.00 23.40  ? 253 ILE   B CG1  1 
ATOM   8395 C  CG2  . ILE   B 1 256 ? -5.707  -12.242 26.227  1.00 23.19  ? 253 ILE   B CG2  1 
ATOM   8396 C  CD1  . ILE   B 1 256 ? -3.977  -9.546  26.440  1.00 23.67  ? 253 ILE   B CD1  1 
ATOM   8397 H  H    . ILE   B 1 256 ? -5.952  -14.027 28.591  1.00 31.61  ? 253 ILE   B H    1 
ATOM   8398 H  HA   . ILE   B 1 256 ? -5.447  -11.512 29.540  1.00 32.48  ? 253 ILE   B HA   1 
ATOM   8399 H  HB   . ILE   B 1 256 ? -4.177  -11.867 27.461  1.00 26.71  ? 253 ILE   B HB   1 
ATOM   8400 H  HG12 . ILE   B 1 256 ? -5.874  -9.698  27.188  1.00 28.12  ? 253 ILE   B HG12 1 
ATOM   8401 H  HG13 . ILE   B 1 256 ? -4.758  -9.738  28.319  1.00 28.12  ? 253 ILE   B HG13 1 
ATOM   8402 H  HG21 . ILE   B 1 256 ? -5.208  -11.963 25.444  1.00 27.87  ? 253 ILE   B HG21 1 
ATOM   8403 H  HG22 . ILE   B 1 256 ? -5.650  -13.205 26.330  1.00 27.87  ? 253 ILE   B HG22 1 
ATOM   8404 H  HG23 . ILE   B 1 256 ? -6.635  -11.973 26.143  1.00 27.87  ? 253 ILE   B HG23 1 
ATOM   8405 H  HD11 . ILE   B 1 256 ? -3.968  -8.576  26.465  1.00 28.44  ? 253 ILE   B HD11 1 
ATOM   8406 H  HD12 . ILE   B 1 256 ? -3.104  -9.891  26.682  1.00 28.44  ? 253 ILE   B HD12 1 
ATOM   8407 H  HD13 . ILE   B 1 256 ? -4.219  -9.851  25.551  1.00 28.44  ? 253 ILE   B HD13 1 
ATOM   8408 N  N    . PRO   B 1 257 ? -7.784  -10.767 29.279  1.00 26.10  ? 254 PRO   B N    1 
ATOM   8409 C  CA   . PRO   B 1 257 ? -9.250  -10.621 29.386  1.00 28.31  ? 254 PRO   B CA   1 
ATOM   8410 C  C    . PRO   B 1 257 ? -9.969  -10.675 28.044  1.00 28.98  ? 254 PRO   B C    1 
ATOM   8411 O  O    . PRO   B 1 257 ? -9.412  -10.380 26.986  1.00 29.96  ? 254 PRO   B O    1 
ATOM   8412 C  CB   . PRO   B 1 257 ? -9.436  -9.253  30.056  1.00 31.78  ? 254 PRO   B CB   1 
ATOM   8413 C  CG   . PRO   B 1 257 ? -8.230  -9.140  30.916  1.00 33.38  ? 254 PRO   B CG   1 
ATOM   8414 C  CD   . PRO   B 1 257 ? -7.116  -9.677  30.033  1.00 27.41  ? 254 PRO   B CD   1 
ATOM   8415 H  HA   . PRO   B 1 257 ? -9.598  -11.326 29.954  1.00 34.02  ? 254 PRO   B HA   1 
ATOM   8416 H  HB2  . PRO   B 1 257 ? -9.464  -8.550  29.388  1.00 38.18  ? 254 PRO   B HB2  1 
ATOM   8417 H  HB3  . PRO   B 1 257 ? -10.250 -9.242  30.583  1.00 38.18  ? 254 PRO   B HB3  1 
ATOM   8418 H  HG2  . PRO   B 1 257 ? -8.073  -8.213  31.156  1.00 40.09  ? 254 PRO   B HG2  1 
ATOM   8419 H  HG3  . PRO   B 1 257 ? -8.335  -9.676  31.717  1.00 40.09  ? 254 PRO   B HG3  1 
ATOM   8420 H  HD2  . PRO   B 1 257 ? -6.789  -8.990  29.431  1.00 32.94  ? 254 PRO   B HD2  1 
ATOM   8421 H  HD3  . PRO   B 1 257 ? -6.386  -10.024 30.569  1.00 32.94  ? 254 PRO   B HD3  1 
ATOM   8422 N  N    . GLY   B 1 258 ? -11.250 -11.039 28.113  1.00 30.45  ? 255 GLY   B N    1 
ATOM   8423 C  CA   . GLY   B 1 258 ? -12.091 -11.144 26.939  1.00 31.59  ? 255 GLY   B CA   1 
ATOM   8424 C  C    . GLY   B 1 258 ? -12.033 -12.510 26.302  1.00 26.50  ? 255 GLY   B C    1 
ATOM   8425 O  O    . GLY   B 1 258 ? -11.332 -13.426 26.739  1.00 29.18  ? 255 GLY   B O    1 
ATOM   8426 H  H    . GLY   B 1 258 ? -11.657 -11.234 28.845  1.00 36.58  ? 255 GLY   B H    1 
ATOM   8427 H  HA2  . GLY   B 1 258 ? -13.011 -10.962 27.188  1.00 37.95  ? 255 GLY   B HA2  1 
ATOM   8428 H  HA3  . GLY   B 1 258 ? -11.806 -10.489 26.283  1.00 37.95  ? 255 GLY   B HA3  1 
ATOM   8429 N  N    . GLY   B 1 259 ? -12.764 -12.640 25.206  1.00 28.51  ? 256 GLY   B N    1 
ATOM   8430 C  CA   . GLY   B 1 259 ? -12.732 -13.863 24.432  1.00 29.00  ? 256 GLY   B CA   1 
ATOM   8431 C  C    . GLY   B 1 259 ? -11.901 -13.715 23.179  1.00 28.64  ? 256 GLY   B C    1 
ATOM   8432 O  O    . GLY   B 1 259 ? -10.848 -13.064 23.178  1.00 25.73  ? 256 GLY   B O    1 
ATOM   8433 H  H    . GLY   B 1 259 ? -13.284 -12.031 24.893  1.00 34.25  ? 256 GLY   B H    1 
ATOM   8434 H  HA2  . GLY   B 1 259 ? -12.353 -14.576 24.970  1.00 34.84  ? 256 GLY   B HA2  1 
ATOM   8435 H  HA3  . GLY   B 1 259 ? -13.635 -14.107 24.176  1.00 34.84  ? 256 GLY   B HA3  1 
ATOM   8436 N  N    . HIS   B 1 260 ? -12.367 -14.353 22.101  1.00 24.41  ? 257 HIS   B N    1 
ATOM   8437 C  CA   . HIS   B 1 260 ? -11.659 -14.291 20.834  1.00 25.92  ? 257 HIS   B CA   1 
ATOM   8438 C  C    . HIS   B 1 260 ? -11.497 -12.861 20.355  1.00 27.21  ? 257 HIS   B C    1 
ATOM   8439 O  O    . HIS   B 1 260 ? -10.499 -12.550 19.696  1.00 24.24  ? 257 HIS   B O    1 
ATOM   8440 C  CB   . HIS   B 1 260 ? -12.406 -15.143 19.821  1.00 26.33  ? 257 HIS   B CB   1 
ATOM   8441 C  CG   . HIS   B 1 260 ? -11.667 -15.347 18.555  1.00 26.74  ? 257 HIS   B CG   1 
ATOM   8442 N  ND1  . HIS   B 1 260 ? -10.471 -16.036 18.502  1.00 27.54  ? 257 HIS   B ND1  1 
ATOM   8443 C  CD2  . HIS   B 1 260 ? -11.970 -14.997 17.283  1.00 35.92  ? 257 HIS   B CD2  1 
ATOM   8444 C  CE1  . HIS   B 1 260 ? -10.065 -16.085 17.240  1.00 31.22  ? 257 HIS   B CE1  1 
ATOM   8445 N  NE2  . HIS   B 1 260 ? -10.951 -15.458 16.487  1.00 33.03  ? 257 HIS   B NE2  1 
ATOM   8446 H  H    . HIS   B 1 260 ? -13.085 -14.825 22.082  1.00 29.33  ? 257 HIS   B H    1 
ATOM   8447 H  HA   . HIS   B 1 260 ? -10.763 -14.651 20.931  1.00 31.15  ? 257 HIS   B HA   1 
ATOM   8448 H  HB2  . HIS   B 1 260 ? -12.574 -16.016 20.210  1.00 31.64  ? 257 HIS   B HB2  1 
ATOM   8449 H  HB3  . HIS   B 1 260 ? -13.247 -14.708 19.607  1.00 31.64  ? 257 HIS   B HB3  1 
ATOM   8450 H  HD1  . HIS   B 1 260 ? -10.058 -16.375 19.176  1.00 33.09  ? 257 HIS   B HD1  1 
ATOM   8451 H  HD2  . HIS   B 1 260 ? -12.726 -14.533 17.002  1.00 43.15  ? 257 HIS   B HD2  1 
ATOM   8452 H  HE1  . HIS   B 1 260 ? -9.287  -16.494 16.936  1.00 37.50  ? 257 HIS   B HE1  1 
ATOM   8453 N  N    . LEU   B 1 261 ? -12.449 -11.985 20.671  1.00 27.78  ? 258 LEU   B N    1 
ATOM   8454 C  CA   . LEU   B 1 261 ? -12.360 -10.562 20.348  1.00 30.96  ? 258 LEU   B CA   1 
ATOM   8455 C  C    . LEU   B 1 261 ? -12.074 -9.703  21.580  1.00 25.76  ? 258 LEU   B C    1 
ATOM   8456 O  O    . LEU   B 1 261 ? -12.564 -8.571  21.702  1.00 27.68  ? 258 LEU   B O    1 
ATOM   8457 C  CB   . LEU   B 1 261 ? -13.649 -10.082 19.691  1.00 30.39  ? 258 LEU   B CB   1 
ATOM   8458 C  CG   . LEU   B 1 261 ? -14.102 -10.948 18.513  1.00 35.53  ? 258 LEU   B CG   1 
ATOM   8459 C  CD1  . LEU   B 1 261 ? -15.503 -10.531 18.056  1.00 40.58  ? 258 LEU   B CD1  1 
ATOM   8460 C  CD2  . LEU   B 1 261 ? -13.129 -10.852 17.393  1.00 39.66  ? 258 LEU   B CD2  1 
ATOM   8461 H  H    . LEU   B 1 261 ? -13.173 -12.197 21.083  1.00 33.38  ? 258 LEU   B H    1 
ATOM   8462 H  HA   . LEU   B 1 261 ? -11.624 -10.448 19.727  1.00 37.20  ? 258 LEU   B HA   1 
ATOM   8463 H  HB2  . LEU   B 1 261 ? -14.357 -10.090 20.354  1.00 36.51  ? 258 LEU   B HB2  1 
ATOM   8464 H  HB3  . LEU   B 1 261 ? -13.513 -9.180  19.361  1.00 36.51  ? 258 LEU   B HB3  1 
ATOM   8465 H  HG   . LEU   B 1 261 ? -14.140 -11.876 18.793  1.00 42.67  ? 258 LEU   B HG   1 
ATOM   8466 H  HD11 . LEU   B 1 261 ? -15.765 -11.078 17.299  1.00 48.74  ? 258 LEU   B HD11 1 
ATOM   8467 H  HD12 . LEU   B 1 261 ? -16.126 -10.660 18.789  1.00 48.74  ? 258 LEU   B HD12 1 
ATOM   8468 H  HD13 . LEU   B 1 261 ? -15.486 -9.596  17.798  1.00 48.74  ? 258 LEU   B HD13 1 
ATOM   8469 H  HD21 . LEU   B 1 261 ? -13.478 -11.337 16.629  1.00 47.64  ? 258 LEU   B HD21 1 
ATOM   8470 H  HD22 . LEU   B 1 261 ? -13.005 -9.918  17.163  1.00 47.64  ? 258 LEU   B HD22 1 
ATOM   8471 H  HD23 . LEU   B 1 261 ? -12.285 -11.239 17.673  1.00 47.64  ? 258 LEU   B HD23 1 
ATOM   8472 N  N    . GLY   B 1 262 ? -11.216 -10.202 22.478  1.00 26.23  ? 259 GLY   B N    1 
ATOM   8473 C  CA   . GLY   B 1 262 ? -11.041 -9.558  23.780  1.00 27.09  ? 259 GLY   B CA   1 
ATOM   8474 C  C    . GLY   B 1 262 ? -10.470 -8.151  23.712  1.00 27.87  ? 259 GLY   B C    1 
ATOM   8475 O  O    . GLY   B 1 262 ? -10.702 -7.339  24.603  1.00 28.98  ? 259 GLY   B O    1 
ATOM   8476 H  H    . GLY   B 1 262 ? -10.731 -10.902 22.359  1.00 31.52  ? 259 GLY   B H    1 
ATOM   8477 H  HA2  . GLY   B 1 262 ? -11.902 -9.508  24.223  1.00 32.55  ? 259 GLY   B HA2  1 
ATOM   8478 H  HA3  . GLY   B 1 262 ? -10.440 -10.097 24.318  1.00 32.55  ? 259 GLY   B HA3  1 
ATOM   8479 N  N    . TYR   B 1 263 ? -9.716  -7.843  22.657  1.00 25.18  ? 260 TYR   B N    1 
ATOM   8480 C  CA   . TYR   B 1 263 ? -9.100  -6.523  22.521  1.00 24.62  ? 260 TYR   B CA   1 
ATOM   8481 C  C    . TYR   B 1 263 ? -10.115 -5.419  22.278  1.00 29.47  ? 260 TYR   B C    1 
ATOM   8482 O  O    . TYR   B 1 263 ? -9.802  -4.247  22.532  1.00 28.62  ? 260 TYR   B O    1 
ATOM   8483 C  CB   . TYR   B 1 263 ? -8.080  -6.543  21.350  1.00 24.98  ? 260 TYR   B CB   1 
ATOM   8484 C  CG   . TYR   B 1 263 ? -8.545  -7.354  20.162  1.00 25.99  ? 260 TYR   B CG   1 
ATOM   8485 C  CD1  . TYR   B 1 263 ? -9.352  -6.798  19.184  1.00 26.07  ? 260 TYR   B CD1  1 
ATOM   8486 C  CD2  . TYR   B 1 263 ? -8.198  -8.684  20.025  1.00 21.86  ? 260 TYR   B CD2  1 
ATOM   8487 C  CE1  . TYR   B 1 263 ? -9.788  -7.549  18.103  1.00 26.72  ? 260 TYR   B CE1  1 
ATOM   8488 C  CE2  . TYR   B 1 263 ? -8.639  -9.440  18.973  1.00 25.27  ? 260 TYR   B CE2  1 
ATOM   8489 C  CZ   . TYR   B 1 263 ? -9.430  -8.860  17.997  1.00 27.22  ? 260 TYR   B CZ   1 
ATOM   8490 O  OH   . TYR   B 1 263 ? -9.872  -9.603  16.914  1.00 29.60  ? 260 TYR   B OH   1 
ATOM   8491 H  H    . TYR   B 1 263 ? -9.545  -8.379  22.007  1.00 30.26  ? 260 TYR   B H    1 
ATOM   8492 H  HA   . TYR   B 1 263 ? -8.632  -6.318  23.345  1.00 29.58  ? 260 TYR   B HA   1 
ATOM   8493 H  HB2  . TYR   B 1 263 ? -7.931  -5.633  21.049  1.00 30.02  ? 260 TYR   B HB2  1 
ATOM   8494 H  HB3  . TYR   B 1 263 ? -7.248  -6.928  21.666  1.00 30.02  ? 260 TYR   B HB3  1 
ATOM   8495 H  HD1  . TYR   B 1 263 ? -9.605  -5.905  19.252  1.00 31.32  ? 260 TYR   B HD1  1 
ATOM   8496 H  HD2  . TYR   B 1 263 ? -7.648  -9.076  20.664  1.00 26.27  ? 260 TYR   B HD2  1 
ATOM   8497 H  HE1  . TYR   B 1 263 ? -10.325 -7.159  17.451  1.00 32.11  ? 260 TYR   B HE1  1 
ATOM   8498 H  HE2  . TYR   B 1 263 ? -8.409  -10.339 18.915  1.00 30.36  ? 260 TYR   B HE2  1 
ATOM   8499 H  HH   . TYR   B 1 263 ? -9.519  -10.365 16.926  1.00 35.56  ? 260 TYR   B HH   1 
ATOM   8500 N  N    . ILE   B 1 264 ? -11.327 -5.752  21.822  1.00 27.41  ? 261 ILE   B N    1 
ATOM   8501 C  CA   . ILE   B 1 264 ? -12.407 -4.788  21.701  1.00 28.81  ? 261 ILE   B CA   1 
ATOM   8502 C  C    . ILE   B 1 264 ? -13.479 -4.986  22.773  1.00 30.37  ? 261 ILE   B C    1 
ATOM   8503 O  O    . ILE   B 1 264 ? -14.116 -4.017  23.180  1.00 34.13  ? 261 ILE   B O    1 
ATOM   8504 C  CB   . ILE   B 1 264 ? -13.016 -4.854  20.279  1.00 33.07  ? 261 ILE   B CB   1 
ATOM   8505 C  CG1  . ILE   B 1 264 ? -14.042 -3.748  20.041  1.00 33.75  ? 261 ILE   B CG1  1 
ATOM   8506 C  CG2  . ILE   B 1 264 ? -13.648 -6.203  19.979  1.00 35.67  ? 261 ILE   B CG2  1 
ATOM   8507 C  CD1  . ILE   B 1 264 ? -13.606 -2.412  20.454  1.00 39.32  ? 261 ILE   B CD1  1 
ATOM   8508 H  H    . ILE   B 1 264 ? -11.547 -6.545  21.574  1.00 32.93  ? 261 ILE   B H    1 
ATOM   8509 H  HA   . ILE   B 1 264 ? -12.061 -3.892  21.837  1.00 34.62  ? 261 ILE   B HA   1 
ATOM   8510 H  HB   . ILE   B 1 264 ? -12.269 -4.723  19.674  1.00 39.72  ? 261 ILE   B HB   1 
ATOM   8511 H  HG12 . ILE   B 1 264 ? -14.241 -3.710  19.092  1.00 40.55  ? 261 ILE   B HG12 1 
ATOM   8512 H  HG13 . ILE   B 1 264 ? -14.846 -3.960  20.540  1.00 40.55  ? 261 ILE   B HG13 1 
ATOM   8513 H  HG21 . ILE   B 1 264 ? -14.046 -6.176  19.095  1.00 42.84  ? 261 ILE   B HG21 1 
ATOM   8514 H  HG22 . ILE   B 1 264 ? -12.961 -6.887  20.011  1.00 42.84  ? 261 ILE   B HG22 1 
ATOM   8515 H  HG23 . ILE   B 1 264 ? -14.330 -6.387  20.644  1.00 42.84  ? 261 ILE   B HG23 1 
ATOM   8516 H  HD11 . ILE   B 1 264 ? -14.163 -1.749  20.017  1.00 47.23  ? 261 ILE   B HD11 1 
ATOM   8517 H  HD12 . ILE   B 1 264 ? -13.693 -2.335  21.417  1.00 47.23  ? 261 ILE   B HD12 1 
ATOM   8518 H  HD13 . ILE   B 1 264 ? -12.679 -2.289  20.194  1.00 47.23  ? 261 ILE   B HD13 1 
ATOM   8519 N  N    . GLN   B 1 265 ? -13.626 -6.210  23.294  1.00 30.33  ? 262 GLN   B N    1 
ATOM   8520 C  CA   . GLN   B 1 265 ? -14.586 -6.487  24.365  1.00 31.73  ? 262 GLN   B CA   1 
ATOM   8521 C  C    . GLN   B 1 265 ? -14.125 -5.875  25.678  1.00 32.82  ? 262 GLN   B C    1 
ATOM   8522 O  O    . GLN   B 1 265 ? -14.924 -5.315  26.430  1.00 38.67  ? 262 GLN   B O    1 
ATOM   8523 C  CB   . GLN   B 1 265 ? -14.732 -8.002  24.511  1.00 33.83  ? 262 GLN   B CB   1 
ATOM   8524 C  CG   . GLN   B 1 265 ? -15.522 -8.679  23.383  1.00 34.44  ? 262 GLN   B CG   1 
ATOM   8525 C  CD   . GLN   B 1 265 ? -15.233 -10.171 23.273  1.00 34.14  ? 262 GLN   B CD   1 
ATOM   8526 O  OE1  . GLN   B 1 265 ? -14.311 -10.684 23.899  1.00 39.59  ? 262 GLN   B OE1  1 
ATOM   8527 N  NE2  . GLN   B 1 265 ? -16.050 -10.881 22.487  1.00 38.19  ? 262 GLN   B NE2  1 
ATOM   8528 H  H    . GLN   B 1 265 ? -13.180 -6.901  23.043  1.00 36.44  ? 262 GLN   B H    1 
ATOM   8529 H  HA   . GLN   B 1 265 ? -15.448 -6.104  24.141  1.00 37.86  ? 262 GLN   B HA   1 
ATOM   8530 H  HB2  . GLN   B 1 265 ? -13.846 -8.397  24.526  1.00 40.64  ? 262 GLN   B HB2  1 
ATOM   8531 H  HB3  . GLN   B 1 265 ? -15.192 -8.189  25.344  1.00 40.64  ? 262 GLN   B HB3  1 
ATOM   8532 H  HG2  . GLN   B 1 265 ? -16.471 -8.569  23.552  1.00 41.37  ? 262 GLN   B HG2  1 
ATOM   8533 H  HG3  . GLN   B 1 265 ? -15.286 -8.264  22.538  1.00 41.37  ? 262 GLN   B HG3  1 
ATOM   8534 H  HE21 . GLN   B 1 265 ? -16.698 -10.491 22.077  1.00 45.87  ? 262 GLN   B HE21 1 
ATOM   8535 H  HE22 . GLN   B 1 265 ? -15.928 -11.727 22.393  1.00 45.87  ? 262 GLN   B HE22 1 
ATOM   8536 N  N    . LYS   B 1 266 ? -12.821 -5.968  25.960  1.00 34.11  ? 263 LYS   B N    1 
ATOM   8537 C  CA   . LYS   B 1 266 ? -12.255 -5.539  27.242  1.00 33.23  ? 263 LYS   B CA   1 
ATOM   8538 C  C    . LYS   B 1 266 ? -10.926 -4.839  27.019  1.00 31.12  ? 263 LYS   B C    1 
ATOM   8539 O  O    . LYS   B 1 266 ? -9.861  -5.316  27.440  1.00 30.19  ? 263 LYS   B O    1 
ATOM   8540 C  CB   . LYS   B 1 266 ? -12.121 -6.735  28.187  1.00 36.37  ? 263 LYS   B CB   1 
ATOM   8541 C  CG   . LYS   B 1 266 ? -13.495 -7.249  28.605  1.00 52.06  ? 263 LYS   B CG   1 
ATOM   8542 C  CD   . LYS   B 1 266 ? -13.516 -8.660  29.158  1.00 53.78  ? 263 LYS   B CD   1 
ATOM   8543 C  CE   . LYS   B 1 266 ? -14.471 -8.717  30.367  1.00 58.31  ? 263 LYS   B CE   1 
ATOM   8544 N  NZ   . LYS   B 1 266 ? -14.544 -10.070 30.990  1.00 63.65  ? 263 LYS   B NZ   1 
ATOM   8545 H  H    . LYS   B 1 266 ? -12.235 -6.281  25.414  1.00 40.97  ? 263 LYS   B H    1 
ATOM   8546 H  HA   . LYS   B 1 266 ? -12.847 -4.887  27.648  1.00 39.91  ? 263 LYS   B HA   1 
ATOM   8547 H  HB2  . LYS   B 1 266 ? -11.647 -7.451  27.737  1.00 43.68  ? 263 LYS   B HB2  1 
ATOM   8548 H  HB3  . LYS   B 1 266 ? -11.637 -6.465  28.983  1.00 43.68  ? 263 LYS   B HB3  1 
ATOM   8549 H  HG2  . LYS   B 1 266 ? -13.846 -6.663  29.294  1.00 62.52  ? 263 LYS   B HG2  1 
ATOM   8550 H  HG3  . LYS   B 1 266 ? -14.077 -7.234  27.829  1.00 62.52  ? 263 LYS   B HG3  1 
ATOM   8551 H  HD2  . LYS   B 1 266 ? -13.832 -9.276  28.479  1.00 64.58  ? 263 LYS   B HD2  1 
ATOM   8552 H  HD3  . LYS   B 1 266 ? -12.626 -8.914  29.448  1.00 64.58  ? 263 LYS   B HD3  1 
ATOM   8553 H  HE2  . LYS   B 1 266 ? -14.162 -8.093  31.043  1.00 70.01  ? 263 LYS   B HE2  1 
ATOM   8554 H  HE3  . LYS   B 1 266 ? -15.364 -8.474  30.076  1.00 70.01  ? 263 LYS   B HE3  1 
ATOM   8555 H  HZ1  . LYS   B 1 266 ? -15.136 -10.068 31.654  1.00 76.42  ? 263 LYS   B HZ1  1 
ATOM   8556 H  HZ2  . LYS   B 1 266 ? -14.793 -10.671 30.383  1.00 76.42  ? 263 LYS   B HZ2  1 
ATOM   8557 H  HZ3  . LYS   B 1 266 ? -13.747 -10.299 31.313  1.00 76.42  ? 263 LYS   B HZ3  1 
ATOM   8558 N  N    . PRO   B 1 267 ? -10.960 -3.662  26.385  1.00 35.21  ? 264 PRO   B N    1 
ATOM   8559 C  CA   . PRO   B 1 267 ? -9.702  -3.018  25.973  1.00 32.23  ? 264 PRO   B CA   1 
ATOM   8560 C  C    . PRO   B 1 267 ? -8.826  -2.603  27.139  1.00 31.68  ? 264 PRO   B C    1 
ATOM   8561 O  O    . PRO   B 1 267 ? -7.600  -2.729  27.037  1.00 32.11  ? 264 PRO   B O    1 
ATOM   8562 C  CB   . PRO   B 1 267 ? -10.177 -1.813  25.138  1.00 33.61  ? 264 PRO   B CB   1 
ATOM   8563 C  CG   . PRO   B 1 267 ? -11.593 -1.604  25.508  1.00 40.23  ? 264 PRO   B CG   1 
ATOM   8564 C  CD   . PRO   B 1 267 ? -12.145 -2.949  25.870  1.00 35.50  ? 264 PRO   B CD   1 
ATOM   8565 H  HA   . PRO   B 1 267 ? -9.195  -3.614  25.400  1.00 38.71  ? 264 PRO   B HA   1 
ATOM   8566 H  HB2  . PRO   B 1 267 ? -9.645  -1.032  25.357  1.00 40.38  ? 264 PRO   B HB2  1 
ATOM   8567 H  HB3  . PRO   B 1 267 ? -10.095 -2.017  24.193  1.00 40.38  ? 264 PRO   B HB3  1 
ATOM   8568 H  HG2  . PRO   B 1 267 ? -11.645 -1.000  26.265  1.00 48.32  ? 264 PRO   B HG2  1 
ATOM   8569 H  HG3  . PRO   B 1 267 ? -12.074 -1.231  24.753  1.00 48.32  ? 264 PRO   B HG3  1 
ATOM   8570 H  HD2  . PRO   B 1 267 ? -12.828 -2.872  26.554  1.00 42.64  ? 264 PRO   B HD2  1 
ATOM   8571 H  HD3  . PRO   B 1 267 ? -12.507 -3.397  25.089  1.00 42.64  ? 264 PRO   B HD3  1 
ATOM   8572 N  N    . GLU   B 1 268 ? -9.408  -2.178  28.256  1.00 35.82  ? 265 GLU   B N    1 
ATOM   8573 C  CA   . GLU   B 1 268 ? -8.592  -1.747  29.390  1.00 34.52  ? 265 GLU   B CA   1 
ATOM   8574 C  C    . GLU   B 1 268 ? -7.865  -2.942  30.013  1.00 37.24  ? 265 GLU   B C    1 
ATOM   8575 O  O    . GLU   B 1 268 ? -6.657  -2.881  30.269  1.00 34.51  ? 265 GLU   B O    1 
ATOM   8576 C  CB   . GLU   B 1 268 ? -9.465  -1.008  30.400  1.00 37.78  ? 265 GLU   B CB   1 
ATOM   8577 C  CG   . GLU   B 1 268 ? -8.695  -0.471  31.553  1.00 49.04  ? 265 GLU   B CG   1 
ATOM   8578 C  CD   . GLU   B 1 268 ? -9.589  0.222   32.565  1.00 61.18  ? 265 GLU   B CD   1 
ATOM   8579 O  OE1  . GLU   B 1 268 ? -10.707 0.640   32.193  1.00 63.78  ? 265 GLU   B OE1  1 
ATOM   8580 O  OE2  . GLU   B 1 268 ? -9.170  0.328   33.727  1.00 65.78  ? 265 GLU   B OE2  1 
ATOM   8581 H  H    . GLU   B 1 268 ? -10.257 -2.130  28.383  1.00 43.02  ? 265 GLU   B H    1 
ATOM   8582 H  HA   . GLU   B 1 268 ? -7.912  -1.121  29.094  1.00 41.46  ? 265 GLU   B HA   1 
ATOM   8583 H  HB2  . GLU   B 1 268 ? -9.898  -0.263  29.956  1.00 45.38  ? 265 GLU   B HB2  1 
ATOM   8584 H  HB3  . GLU   B 1 268 ? -10.132 -1.621  30.746  1.00 45.38  ? 265 GLU   B HB3  1 
ATOM   8585 H  HG2  . GLU   B 1 268 ? -8.240  -1.201  32.000  1.00 58.89  ? 265 GLU   B HG2  1 
ATOM   8586 H  HG3  . GLU   B 1 268 ? -8.047  0.175   31.229  1.00 58.89  ? 265 GLU   B HG3  1 
ATOM   8587 N  N    . GLY   B 1 269 ? -8.557  -4.061  30.191  1.00 32.58  ? 266 GLY   B N    1 
ATOM   8588 C  CA   . GLY   B 1 269 ? -7.902  -5.234  30.754  1.00 32.43  ? 266 GLY   B CA   1 
ATOM   8589 C  C    . GLY   B 1 269 ? -6.903  -5.859  29.804  1.00 30.73  ? 266 GLY   B C    1 
ATOM   8590 O  O    . GLY   B 1 269 ? -5.861  -6.377  30.221  1.00 32.31  ? 266 GLY   B O    1 
ATOM   8591 H  H    . GLY   B 1 269 ? -9.389  -4.166  29.998  1.00 38.89  ? 266 GLY   B H    1 
ATOM   8592 H  HA2  . GLY   B 1 269 ? -7.434  -4.981  31.565  1.00 38.96  ? 266 GLY   B HA2  1 
ATOM   8593 H  HA3  . GLY   B 1 269 ? -8.572  -5.901  30.972  1.00 38.96  ? 266 GLY   B HA3  1 
ATOM   8594 N  N    . PHE   B 1 270 ? -7.228  -5.864  28.515  1.00 28.13  ? 267 PHE   B N    1 
ATOM   8595 C  CA   . PHE   B 1 270 ? -6.298  -6.365  27.511  1.00 26.02  ? 267 PHE   B CA   1 
ATOM   8596 C  C    . PHE   B 1 270 ? -5.014  -5.549  27.519  1.00 25.81  ? 267 PHE   B C    1 
ATOM   8597 O  O    . PHE   B 1 270 ? -3.906  -6.110  27.480  1.00 25.15  ? 267 PHE   B O    1 
ATOM   8598 C  CB   . PHE   B 1 270 ? -6.987  -6.315  26.142  1.00 26.31  ? 267 PHE   B CB   1 
ATOM   8599 C  CG   . PHE   B 1 270 ? -6.456  -7.260  25.114  1.00 23.42  ? 267 PHE   B CG   1 
ATOM   8600 C  CD1  . PHE   B 1 270 ? -5.370  -6.915  24.318  1.00 23.77  ? 267 PHE   B CD1  1 
ATOM   8601 C  CD2  . PHE   B 1 270 ? -7.099  -8.467  24.855  1.00 22.95  ? 267 PHE   B CD2  1 
ATOM   8602 C  CE1  . PHE   B 1 270 ? -4.912  -7.750  23.324  1.00 24.47  ? 267 PHE   B CE1  1 
ATOM   8603 C  CE2  . PHE   B 1 270 ? -6.621  -9.319  23.867  1.00 22.30  ? 267 PHE   B CE2  1 
ATOM   8604 C  CZ   . PHE   B 1 270 ? -5.532  -8.956  23.090  1.00 22.16  ? 267 PHE   B CZ   1 
ATOM   8605 H  H    . PHE   B 1 270 ? -7.976  -5.585  28.197  1.00 33.80  ? 267 PHE   B H    1 
ATOM   8606 H  HA   . PHE   B 1 270 ? -6.058  -7.285  27.700  1.00 31.01  ? 267 PHE   B HA   1 
ATOM   8607 H  HB2  . PHE   B 1 270 ? -7.926  -6.524  26.267  1.00 31.61  ? 267 PHE   B HB2  1 
ATOM   8608 H  HB3  . PHE   B 1 270 ? -6.892  -5.419  25.786  1.00 31.61  ? 267 PHE   B HB3  1 
ATOM   8609 H  HD1  . PHE   B 1 270 ? -4.943  -6.101  24.461  1.00 28.56  ? 267 PHE   B HD1  1 
ATOM   8610 H  HD2  . PHE   B 1 270 ? -7.852  -8.705  25.346  1.00 27.58  ? 267 PHE   B HD2  1 
ATOM   8611 H  HE1  . PHE   B 1 270 ? -4.181  -7.497  22.808  1.00 29.41  ? 267 PHE   B HE1  1 
ATOM   8612 H  HE2  . PHE   B 1 270 ? -7.035  -10.140 23.727  1.00 26.80  ? 267 PHE   B HE2  1 
ATOM   8613 H  HZ   . PHE   B 1 270 ? -5.224  -9.521  22.419  1.00 26.63  ? 267 PHE   B HZ   1 
ATOM   8614 N  N    . ALA   B 1 271 ? -5.142  -4.222  27.547  1.00 27.83  ? 268 ALA   B N    1 
ATOM   8615 C  CA   . ALA   B 1 271 ? -3.965  -3.358  27.557  1.00 27.19  ? 268 ALA   B CA   1 
ATOM   8616 C  C    . ALA   B 1 271 ? -3.113  -3.587  28.798  1.00 27.81  ? 268 ALA   B C    1 
ATOM   8617 O  O    . ALA   B 1 271 ? -1.875  -3.576  28.726  1.00 30.58  ? 268 ALA   B O    1 
ATOM   8618 C  CB   . ALA   B 1 271 ? -4.382  -1.891  27.475  1.00 30.00  ? 268 ALA   B CB   1 
ATOM   8619 H  H    . ALA   B 1 271 ? -5.892  -3.801  27.560  1.00 33.44  ? 268 ALA   B H    1 
ATOM   8620 H  HA   . ALA   B 1 271 ? -3.430  -3.569  26.776  1.00 32.42  ? 268 ALA   B HA   1 
ATOM   8621 H  HB1  . ALA   B 1 271 ? -3.593  -1.333  27.565  1.00 36.04  ? 268 ALA   B HB1  1 
ATOM   8622 H  HB2  . ALA   B 1 271 ? -4.805  -1.730  26.617  1.00 36.04  ? 268 ALA   B HB2  1 
ATOM   8623 H  HB3  . ALA   B 1 271 ? -5.006  -1.699  28.193  1.00 36.04  ? 268 ALA   B HB3  1 
ATOM   8624 N  N    . ASP   B 1 272 ? -3.758  -3.788  29.946  1.00 30.42  ? 269 ASP   B N    1 
ATOM   8625 C  CA   . ASP   B 1 272 ? -3.023  -3.985  31.195  1.00 30.94  ? 269 ASP   B CA   1 
ATOM   8626 C  C    . ASP   B 1 272 ? -2.088  -5.190  31.094  1.00 28.15  ? 269 ASP   B C    1 
ATOM   8627 O  O    . ASP   B 1 272 ? -0.941  -5.142  31.555  1.00 30.36  ? 269 ASP   B O    1 
ATOM   8628 C  CB   . ASP   B 1 272 ? -4.015  -4.179  32.341  1.00 32.50  ? 269 ASP   B CB   1 
ATOM   8629 C  CG   . ASP   B 1 272 ? -4.525  -2.878  32.902  1.00 47.52  ? 269 ASP   B CG   1 
ATOM   8630 O  OD1  . ASP   B 1 272 ? -4.085  -1.799  32.440  1.00 46.97  ? 269 ASP   B OD1  1 
ATOM   8631 O  OD2  . ASP   B 1 272 ? -5.393  -2.939  33.795  1.00 48.87  ? 269 ASP   B OD2  1 
ATOM   8632 H  H    . ASP   B 1 272 ? -4.614  -3.815  30.030  1.00 36.54  ? 269 ASP   B H    1 
ATOM   8633 H  HA   . ASP   B 1 272 ? -2.486  -3.199  31.379  1.00 37.17  ? 269 ASP   B HA   1 
ATOM   8634 H  HB2  . ASP   B 1 272 ? -4.777  -4.684  32.017  1.00 39.05  ? 269 ASP   B HB2  1 
ATOM   8635 H  HB3  . ASP   B 1 272 ? -3.577  -4.663  33.059  1.00 39.05  ? 269 ASP   B HB3  1 
ATOM   8636 N  N    . VAL   B 1 273 ? -2.561  -6.282  30.510  1.00 26.75  ? 270 VAL   B N    1 
ATOM   8637 C  CA   . VAL   B 1 273 ? -1.701  -7.447  30.318  1.00 25.37  ? 270 VAL   B CA   1 
ATOM   8638 C  C    . VAL   B 1 273 ? -0.573  -7.145  29.335  1.00 25.17  ? 270 VAL   B C    1 
ATOM   8639 O  O    . VAL   B 1 273 ? 0.583   -7.529  29.565  1.00 26.50  ? 270 VAL   B O    1 
ATOM   8640 C  CB   . VAL   B 1 273 ? -2.518  -8.671  29.864  1.00 29.35  ? 270 VAL   B CB   1 
ATOM   8641 C  CG1  . VAL   B 1 273 ? -1.567  -9.798  29.460  1.00 28.66  ? 270 VAL   B CG1  1 
ATOM   8642 C  CG2  . VAL   B 1 273 ? -3.456  -9.106  30.955  1.00 33.57  ? 270 VAL   B CG2  1 
ATOM   8643 H  H    . VAL   B 1 273 ? -3.365  -6.377  30.218  1.00 32.15  ? 270 VAL   B H    1 
ATOM   8644 H  HA   . VAL   B 1 273 ? -1.300  -7.654  31.176  1.00 30.39  ? 270 VAL   B HA   1 
ATOM   8645 H  HB   . VAL   B 1 273 ? -3.060  -8.442  29.093  1.00 35.26  ? 270 VAL   B HB   1 
ATOM   8646 H  HG11 . VAL   B 1 273 ? -2.051  -10.638 29.469  1.00 34.44  ? 270 VAL   B HG11 1 
ATOM   8647 H  HG12 . VAL   B 1 273 ? -1.228  -9.620  28.568  1.00 34.44  ? 270 VAL   B HG12 1 
ATOM   8648 H  HG13 . VAL   B 1 273 ? -0.833  -9.832  30.092  1.00 34.44  ? 270 VAL   B HG13 1 
ATOM   8649 H  HG21 . VAL   B 1 273 ? -3.893  -9.929  30.686  1.00 40.32  ? 270 VAL   B HG21 1 
ATOM   8650 H  HG22 . VAL   B 1 273 ? -2.949  -9.251  31.769  1.00 40.32  ? 270 VAL   B HG22 1 
ATOM   8651 H  HG23 . VAL   B 1 273 ? -4.119  -8.412  31.097  1.00 40.32  ? 270 VAL   B HG23 1 
ATOM   8652 N  N    . LEU   B 1 274 ? -0.885  -6.509  28.202  1.00 25.83  ? 271 LEU   B N    1 
ATOM   8653 C  CA   . LEU   B 1 274 ? 0.176   -6.190  27.249  1.00 25.89  ? 271 LEU   B CA   1 
ATOM   8654 C  C    . LEU   B 1 274 ? 1.235   -5.298  27.889  1.00 26.79  ? 271 LEU   B C    1 
ATOM   8655 O  O    . LEU   B 1 274 ? 2.433   -5.427  27.597  1.00 27.18  ? 271 LEU   B O    1 
ATOM   8656 C  CB   . LEU   B 1 274 ? -0.394  -5.496  26.011  1.00 25.52  ? 271 LEU   B CB   1 
ATOM   8657 C  CG   . LEU   B 1 274 ? -1.270  -6.354  25.099  1.00 26.07  ? 271 LEU   B CG   1 
ATOM   8658 C  CD1  . LEU   B 1 274 ? -1.664  -5.556  23.831  1.00 25.36  ? 271 LEU   B CD1  1 
ATOM   8659 C  CD2  . LEU   B 1 274 ? -0.603  -7.657  24.678  1.00 22.83  ? 271 LEU   B CD2  1 
ATOM   8660 H  H    . LEU   B 1 274 ? -1.675  -6.260  27.971  1.00 31.04  ? 271 LEU   B H    1 
ATOM   8661 H  HA   . LEU   B 1 274 ? 0.587   -7.022  26.967  1.00 31.11  ? 271 LEU   B HA   1 
ATOM   8662 H  HB2  . LEU   B 1 274 ? -0.937  -4.748  26.308  1.00 30.67  ? 271 LEU   B HB2  1 
ATOM   8663 H  HB3  . LEU   B 1 274 ? 0.349   -5.176  25.476  1.00 30.67  ? 271 LEU   B HB3  1 
ATOM   8664 H  HG   . LEU   B 1 274 ? -2.060  -6.589  25.609  1.00 31.33  ? 271 LEU   B HG   1 
ATOM   8665 H  HD11 . LEU   B 1 274 ? -2.244  -6.105  23.280  1.00 30.47  ? 271 LEU   B HD11 1 
ATOM   8666 H  HD12 . LEU   B 1 274 ? -2.129  -4.748  24.099  1.00 30.47  ? 271 LEU   B HD12 1 
ATOM   8667 H  HD13 . LEU   B 1 274 ? -0.859  -5.327  23.339  1.00 30.47  ? 271 LEU   B HD13 1 
ATOM   8668 H  HD21 . LEU   B 1 274 ? -1.150  -8.087  24.002  1.00 27.43  ? 271 LEU   B HD21 1 
ATOM   8669 H  HD22 . LEU   B 1 274 ? 0.275   -7.460  24.317  1.00 27.43  ? 271 LEU   B HD22 1 
ATOM   8670 H  HD23 . LEU   B 1 274 ? -0.521  -8.234  25.453  1.00 27.43  ? 271 LEU   B HD23 1 
ATOM   8671 N  N    . LEU   B 1 275 ? 0.812   -4.353  28.744  1.00 25.50  ? 272 LEU   B N    1 
ATOM   8672 C  CA   . LEU   B 1 275 ? 1.770   -3.487  29.409  1.00 27.65  ? 272 LEU   B CA   1 
ATOM   8673 C  C    . LEU   B 1 275 ? 2.604   -4.275  30.410  1.00 30.64  ? 272 LEU   B C    1 
ATOM   8674 O  O    . LEU   B 1 275 ? 3.800   -4.012  30.575  1.00 36.33  ? 272 LEU   B O    1 
ATOM   8675 C  CB   . LEU   B 1 275 ? 1.044   -2.334  30.100  1.00 29.33  ? 272 LEU   B CB   1 
ATOM   8676 C  CG   . LEU   B 1 275 ? 0.676   -1.216  29.100  1.00 32.66  ? 272 LEU   B CG   1 
ATOM   8677 C  CD1  . LEU   B 1 275 ? -0.391  -0.295  29.727  1.00 37.25  ? 272 LEU   B CD1  1 
ATOM   8678 C  CD2  . LEU   B 1 275 ? 1.884   -0.430  28.651  1.00 45.37  ? 272 LEU   B CD2  1 
ATOM   8679 H  H    . LEU   B 1 275 ? -0.010  -4.203  28.946  1.00 30.48  ? 272 LEU   B H    1 
ATOM   8680 H  HA   . LEU   B 1 275 ? 2.368   -3.106  28.746  1.00 33.23  ? 272 LEU   B HA   1 
ATOM   8681 H  HB2  . LEU   B 1 275 ? 0.227   -2.666  30.503  1.00 35.24  ? 272 LEU   B HB2  1 
ATOM   8682 H  HB3  . LEU   B 1 275 ? 1.621   -1.956  30.783  1.00 35.24  ? 272 LEU   B HB3  1 
ATOM   8683 H  HG   . LEU   B 1 275 ? 0.310   -1.622  28.299  1.00 39.24  ? 272 LEU   B HG   1 
ATOM   8684 H  HD11 . LEU   B 1 275 ? -0.575  0.436   29.118  1.00 44.74  ? 272 LEU   B HD11 1 
ATOM   8685 H  HD12 . LEU   B 1 275 ? -1.200  -0.808  29.882  1.00 44.74  ? 272 LEU   B HD12 1 
ATOM   8686 H  HD13 . LEU   B 1 275 ? -0.054  0.052   30.568  1.00 44.74  ? 272 LEU   B HD13 1 
ATOM   8687 H  HD21 . LEU   B 1 275 ? 1.673   0.026   27.822  1.00 54.48  ? 272 LEU   B HD21 1 
ATOM   8688 H  HD22 . LEU   B 1 275 ? 2.111   0.218   29.337  1.00 54.48  ? 272 LEU   B HD22 1 
ATOM   8689 H  HD23 . LEU   B 1 275 ? 2.625   -1.040  28.514  1.00 54.48  ? 272 LEU   B HD23 1 
ATOM   8690 N  N    . ASN   B 1 276 ? 1.992   -5.255  31.076  1.00 27.97  ? 273 ASN   B N    1 
ATOM   8691 C  CA   . ASN   B 1 276 ? 2.752   -6.116  31.976  1.00 30.92  ? 273 ASN   B CA   1 
ATOM   8692 C  C    . ASN   B 1 276 ? 3.794   -6.922  31.208  1.00 32.52  ? 273 ASN   B C    1 
ATOM   8693 O  O    . ASN   B 1 276 ? 4.928   -7.093  31.681  1.00 33.23  ? 273 ASN   B O    1 
ATOM   8694 C  CB   . ASN   B 1 276 ? 1.794   -7.037  32.711  1.00 32.88  ? 273 ASN   B CB   1 
ATOM   8695 C  CG   . ASN   B 1 276 ? 2.396   -7.630  33.960  1.00 51.65  ? 273 ASN   B CG   1 
ATOM   8696 O  OD1  . ASN   B 1 276 ? 2.446   -8.849  34.110  1.00 65.51  ? 273 ASN   B OD1  1 
ATOM   8697 N  ND2  . ASN   B 1 276 ? 2.882   -6.774  34.857  1.00 55.77  ? 273 ASN   B ND2  1 
ATOM   8698 H  H    . ASN   B 1 276 ? 1.153   -5.439  31.025  1.00 33.61  ? 273 ASN   B H    1 
ATOM   8699 H  HA   . ASN   B 1 276 ? 3.220   -5.573  32.630  1.00 37.15  ? 273 ASN   B HA   1 
ATOM   8700 H  HB2  . ASN   B 1 276 ? 1.006   -6.533  32.968  1.00 39.50  ? 273 ASN   B HB2  1 
ATOM   8701 H  HB3  . ASN   B 1 276 ? 1.543   -7.766  32.123  1.00 39.50  ? 273 ASN   B HB3  1 
ATOM   8702 H  HD21 . ASN   B 1 276 ? 2.843   -5.927  34.709  1.00 66.96  ? 273 ASN   B HD21 1 
ATOM   8703 H  HD22 . ASN   B 1 276 ? 3.235   -7.067  35.584  1.00 66.96  ? 273 ASN   B HD22 1 
ATOM   8704 N  N    . MET   B 1 277 ? 3.432   -7.387  30.014  1.00 28.14  ? 274 MET   B N    1 
ATOM   8705 C  CA   . MET   B 1 277 ? 4.340   -8.182  29.190  1.00 26.10  ? 274 MET   B CA   1 
ATOM   8706 C  C    . MET   B 1 277 ? 5.482   -7.341  28.648  1.00 29.78  ? 274 MET   B C    1 
ATOM   8707 O  O    . MET   B 1 277 ? 6.643   -7.766  28.647  1.00 31.12  ? 274 MET   B O    1 
ATOM   8708 C  CB   . MET   B 1 277 ? 3.596   -8.790  27.992  1.00 28.36  ? 274 MET   B CB   1 
ATOM   8709 C  CG   . MET   B 1 277 ? 2.442   -9.680  28.350  1.00 29.38  ? 274 MET   B CG   1 
ATOM   8710 S  SD   . MET   B 1 277 ? 1.437   -10.155 26.968  1.00 25.26  ? 274 MET   B SD   1 
ATOM   8711 C  CE   . MET   B 1 277 ? 2.536   -10.115 25.545  1.00 25.65  ? 274 MET   B CE   1 
ATOM   8712 H  H    . MET   B 1 277 ? 2.662   -7.257  29.655  1.00 33.82  ? 274 MET   B H    1 
ATOM   8713 H  HA   . MET   B 1 277 ? 4.680   -8.894  29.754  1.00 31.36  ? 274 MET   B HA   1 
ATOM   8714 H  HB2  . MET   B 1 277 ? 3.248   -8.067  27.447  1.00 34.08  ? 274 MET   B HB2  1 
ATOM   8715 H  HB3  . MET   B 1 277 ? 4.223   -9.321  27.477  1.00 34.08  ? 274 MET   B HB3  1 
ATOM   8716 H  HG2  . MET   B 1 277 ? 2.788   -10.490 28.754  1.00 35.30  ? 274 MET   B HG2  1 
ATOM   8717 H  HG3  . MET   B 1 277 ? 1.872   -9.211  28.980  1.00 35.30  ? 274 MET   B HG3  1 
ATOM   8718 H  HE1  . MET   B 1 277 ? 2.039   -10.378 24.755  1.00 30.83  ? 274 MET   B HE1  1 
ATOM   8719 H  HE2  . MET   B 1 277 ? 2.879   -9.214  25.436  1.00 30.83  ? 274 MET   B HE2  1 
ATOM   8720 H  HE3  . MET   B 1 277 ? 3.269   -10.732 25.695  1.00 30.83  ? 274 MET   B HE3  1 
ATOM   8721 N  N    . TRP   B 1 278 ? 5.153   -6.160  28.120  1.00 27.50  ? 275 TRP   B N    1 
ATOM   8722 C  CA   . TRP   B 1 278 ? 6.030   -5.439  27.204  1.00 27.01  ? 275 TRP   B CA   1 
ATOM   8723 C  C    . TRP   B 1 278 ? 6.320   -4.022  27.634  1.00 31.85  ? 275 TRP   B C    1 
ATOM   8724 O  O    . TRP   B 1 278 ? 7.168   -3.368  27.014  1.00 32.34  ? 275 TRP   B O    1 
ATOM   8725 C  CB   . TRP   B 1 278 ? 5.384   -5.407  25.815  1.00 25.96  ? 275 TRP   B CB   1 
ATOM   8726 C  CG   . TRP   B 1 278 ? 5.398   -6.714  25.074  1.00 24.82  ? 275 TRP   B CG   1 
ATOM   8727 C  CD1  . TRP   B 1 278 ? 6.092   -7.849  25.370  1.00 25.44  ? 275 TRP   B CD1  1 
ATOM   8728 C  CD2  . TRP   B 1 278 ? 4.622   -7.024  23.912  1.00 25.88  ? 275 TRP   B CD2  1 
ATOM   8729 N  NE1  . TRP   B 1 278 ? 5.822   -8.827  24.454  1.00 26.07  ? 275 TRP   B NE1  1 
ATOM   8730 C  CE2  . TRP   B 1 278 ? 4.925   -8.342  23.542  1.00 22.42  ? 275 TRP   B CE2  1 
ATOM   8731 C  CE3  . TRP   B 1 278 ? 3.716   -6.293  23.136  1.00 27.48  ? 275 TRP   B CE3  1 
ATOM   8732 C  CZ2  . TRP   B 1 278 ? 4.356   -8.956  22.424  1.00 23.70  ? 275 TRP   B CZ2  1 
ATOM   8733 C  CZ3  . TRP   B 1 278 ? 3.140   -6.907  22.053  1.00 23.73  ? 275 TRP   B CZ3  1 
ATOM   8734 C  CH2  . TRP   B 1 278 ? 3.482   -8.201  21.686  1.00 22.15  ? 275 TRP   B CH2  1 
ATOM   8735 H  H    . TRP   B 1 278 ? 4.414   -5.750  28.282  1.00 33.05  ? 275 TRP   B H    1 
ATOM   8736 H  HA   . TRP   B 1 278 ? 6.880   -5.902  27.139  1.00 32.46  ? 275 TRP   B HA   1 
ATOM   8737 H  HB2  . TRP   B 1 278 ? 4.456   -5.140  25.915  1.00 31.20  ? 275 TRP   B HB2  1 
ATOM   8738 H  HB3  . TRP   B 1 278 ? 5.858   -4.760  25.271  1.00 31.20  ? 275 TRP   B HB3  1 
ATOM   8739 H  HD1  . TRP   B 1 278 ? 6.668   -7.945  26.093  1.00 30.57  ? 275 TRP   B HD1  1 
ATOM   8740 H  HE1  . TRP   B 1 278 ? 6.161   -9.617  24.452  1.00 31.32  ? 275 TRP   B HE1  1 
ATOM   8741 H  HE3  . TRP   B 1 278 ? 3.509   -5.412  23.350  1.00 33.01  ? 275 TRP   B HE3  1 
ATOM   8742 H  HZ2  . TRP   B 1 278 ? 4.561   -9.833  22.193  1.00 28.48  ? 275 TRP   B HZ2  1 
ATOM   8743 H  HZ3  . TRP   B 1 278 ? 2.506   -6.445  21.553  1.00 28.52  ? 275 TRP   B HZ3  1 
ATOM   8744 H  HH2  . TRP   B 1 278 ? 3.108   -8.566  20.917  1.00 26.63  ? 275 TRP   B HH2  1 
ATOM   8745 N  N    . GLY   B 1 279 ? 5.654   -3.520  28.665  1.00 30.62  ? 276 GLY   B N    1 
ATOM   8746 C  CA   . GLY   B 1 279 ? 5.839   -2.144  29.090  1.00 34.33  ? 276 GLY   B CA   1 
ATOM   8747 C  C    . GLY   B 1 279 ? 6.915   -2.024  30.139  1.00 40.31  ? 276 GLY   B C    1 
ATOM   8748 O  O    . GLY   B 1 279 ? 7.248   -0.922  30.584  1.00 54.53  ? 276 GLY   B O    1 
ATOM   8749 O  OXT  . GLY   B 1 279 ? 7.465   -3.037  30.567  1.00 44.43  ? 276 GLY   B OXT  1 
ATOM   8750 H  H    . GLY   B 1 279 ? 5.086   -3.960  29.137  1.00 36.79  ? 276 GLY   B H    1 
ATOM   8751 H  HA2  . GLY   B 1 279 ? 6.089   -1.601  28.327  1.00 41.24  ? 276 GLY   B HA2  1 
ATOM   8752 H  HA3  . GLY   B 1 279 ? 5.008   -1.806  29.460  1.00 41.24  ? 276 GLY   B HA3  1 
HETATM 8753 O  O1   . A1BA1 C 2 .   ? -10.666 -19.629 13.224  1.00 54.91  ? 301 A1BA1 A O1   1 
HETATM 8754 C  C1   . A1BA1 C 2 .   ? -10.353 -19.843 11.861  1.00 46.86  ? 301 A1BA1 A C1   1 
HETATM 8755 C  C2   . A1BA1 C 2 .   ? -11.068 -18.339 13.612  1.00 45.98  ? 301 A1BA1 A C2   1 
HETATM 8756 C  C3   . A1BA1 C 2 .   ? -10.464 -15.006 13.421  1.00 36.31  ? 301 A1BA1 A C3   1 
HETATM 8757 C  C4   . A1BA1 C 2 .   ? -12.802 -15.479 12.498  1.00 43.12  ? 301 A1BA1 A C4   1 
HETATM 8758 C  C5   . A1BA1 C 2 .   ? -13.624 -16.365 11.565  1.00 49.41  ? 301 A1BA1 A C5   1 
HETATM 8759 C  C6   . A1BA1 C 2 .   ? -14.832 -15.992 11.169  1.00 55.69  ? 301 A1BA1 A C6   1 
HETATM 8760 C  C7   . A1BA1 C 2 .   ? -15.424 -14.660 11.622  1.00 62.93  ? 301 A1BA1 A C7   1 
HETATM 8761 C  C8   . A1BA1 C 2 .   ? -14.718 -13.878 12.411  1.00 61.63  ? 301 A1BA1 A C8   1 
HETATM 8762 C  C9   . A1BA1 C 2 .   ? -13.320 -14.317 12.880  1.00 51.14  ? 301 A1BA1 A C9   1 
HETATM 8763 O  O2   . A1BA1 C 2 .   ? -11.436 -18.136 14.728  1.00 52.27  ? 301 A1BA1 A O2   1 
HETATM 8764 N  N1   . A1BA1 C 2 .   ? -11.029 -17.268 12.645  1.00 42.08  ? 301 A1BA1 A N1   1 
HETATM 8765 N  N2   . A1BA1 C 2 .   ? -11.454 -15.930 12.901  1.00 32.94  ? 301 A1BA1 A N2   1 
HETATM 8766 O  O3   . A1BA1 C 2 .   ? -10.720 -13.868 13.630  1.00 49.00  ? 301 A1BA1 A O3   1 
HETATM 8767 H  H3   . A1BA1 C 2 .   ? -9.370  -19.432 11.647  1.00 56.28  ? 301 A1BA1 A H3   1 
HETATM 8768 H  H1   . A1BA1 C 2 .   ? -11.094 -19.351 11.238  1.00 56.28  ? 301 A1BA1 A H1   1 
HETATM 8769 H  H2   . A1BA1 C 2 .   ? -10.353 -20.908 11.652  1.00 56.28  ? 301 A1BA1 A H2   1 
HETATM 8770 H  H6   . A1BA1 C 2 .   ? -13.215 -17.309 11.224  1.00 59.33  ? 301 A1BA1 A H6   1 
HETATM 8771 H  H7   . A1BA1 C 2 .   ? -15.405 -16.639 10.517  1.00 66.87  ? 301 A1BA1 A H7   1 
HETATM 8772 H  H8   . A1BA1 C 2 .   ? -16.414 -14.362 11.297  1.00 75.55  ? 301 A1BA1 A H8   1 
HETATM 8773 H  H9   . A1BA1 C 2 .   ? -15.121 -12.925 12.731  1.00 74.00  ? 301 A1BA1 A H9   1 
HETATM 8774 H  H10  . A1BA1 C 2 .   ? -12.749 -13.667 13.532  1.00 61.41  ? 301 A1BA1 A H10  1 
HETATM 8775 H  H4   . A1BA1 C 2 .   ? -10.679 -17.480 11.731  1.00 50.54  ? 301 A1BA1 A H4   1 
HETATM 8776 MG MG   . MG    D 3 .   ? -34.835 -18.205 -46.506 0.83 23.82  ? 302 MG    A MG   1 
HETATM 8777 MG MG   . MG    E 3 .   ? -7.846  -32.369 18.673  0.72 32.91  ? 303 MG    A MG   1 
HETATM 8778 O  O1   . A1BA1 F 2 .   ? -33.713 -15.748 -17.004 1.00 62.52  ? 301 A1BA1 B O1   1 
HETATM 8779 C  C1   . A1BA1 F 2 .   ? -33.129 -14.841 -16.093 1.00 44.36  ? 301 A1BA1 B C1   1 
HETATM 8780 C  C2   . A1BA1 F 2 .   ? -32.837 -16.394 -17.897 1.00 51.08  ? 301 A1BA1 B C2   1 
HETATM 8781 C  C3   . A1BA1 F 2 .   ? -29.956 -16.198 -19.852 1.00 39.59  ? 301 A1BA1 B C3   1 
HETATM 8782 C  C4   . A1BA1 F 2 .   ? -29.642 -17.705 -17.790 1.00 45.97  ? 301 A1BA1 B C4   1 
HETATM 8783 C  C5   . A1BA1 F 2 .   ? -29.950 -17.881 -16.312 1.00 52.86  ? 301 A1BA1 B C5   1 
HETATM 8784 C  C6   . A1BA1 F 2 .   ? -29.328 -18.793 -15.593 1.00 56.92  ? 301 A1BA1 B C6   1 
HETATM 8785 C  C7   . A1BA1 F 2 .   ? -28.271 -19.685 -16.230 1.00 62.50  ? 301 A1BA1 B C7   1 
HETATM 8786 C  C8   . A1BA1 F 2 .   ? -27.987 -19.529 -17.505 1.00 68.29  ? 301 A1BA1 B C8   1 
HETATM 8787 C  C9   . A1BA1 F 2 .   ? -28.718 -18.466 -18.339 1.00 55.98  ? 301 A1BA1 B C9   1 
HETATM 8788 O  O2   . A1BA1 F 2 .   ? -33.251 -17.245 -18.620 1.00 53.39  ? 301 A1BA1 B O2   1 
HETATM 8789 N  N1   . A1BA1 F 2 .   ? -31.449 -15.979 -17.903 1.00 37.63  ? 301 A1BA1 B N1   1 
HETATM 8790 N  N2   . A1BA1 F 2 .   ? -30.363 -16.658 -18.530 1.00 40.63  ? 301 A1BA1 B N2   1 
HETATM 8791 O  O3   . A1BA1 F 2 .   ? -29.020 -16.673 -20.426 1.00 35.37  ? 301 A1BA1 B O3   1 
HETATM 8792 H  H3   . A1BA1 F 2 .   ? -33.816 -14.659 -15.272 1.00 53.27  ? 301 A1BA1 B H3   1 
HETATM 8793 H  H1   . A1BA1 F 2 .   ? -32.917 -13.905 -16.601 1.00 53.27  ? 301 A1BA1 B H1   1 
HETATM 8794 H  H2   . A1BA1 F 2 .   ? -32.205 -15.260 -15.706 1.00 53.27  ? 301 A1BA1 B H2   1 
HETATM 8795 H  H6   . A1BA1 F 2 .   ? -30.692 -17.247 -15.842 1.00 63.47  ? 301 A1BA1 B H6   1 
HETATM 8796 H  H7   . A1BA1 F 2 .   ? -29.570 -18.909 -14.544 1.00 68.35  ? 301 A1BA1 B H7   1 
HETATM 8797 H  H8   . A1BA1 F 2 .   ? -27.760 -20.436 -15.641 1.00 75.04  ? 301 A1BA1 B H8   1 
HETATM 8798 H  H9   . A1BA1 F 2 .   ? -27.233 -20.154 -17.970 1.00 81.99  ? 301 A1BA1 B H9   1 
HETATM 8799 H  H10  . A1BA1 F 2 .   ? -28.472 -18.342 -19.387 1.00 67.22  ? 301 A1BA1 B H10  1 
HETATM 8800 H  H4   . A1BA1 F 2 .   ? -31.231 -15.131 -17.420 1.00 45.20  ? 301 A1BA1 B H4   1 
HETATM 8801 MG MG   . MG    G 3 .   ? -31.216 -12.583 5.353   0.92 34.14  ? 302 MG    B MG   1 
HETATM 8802 MG MG   . MG    H 3 .   ? -38.368 -11.707 -0.177  0.89 31.44  ? 303 MG    B MG   1 
HETATM 8803 O  O    . HOH   I 4 .   ? 10.484  -10.716 0.249   0.89 33.65  ? 401 HOH   A O    1 
HETATM 8804 O  O    . HOH   I 4 .   ? 2.904   6.939   9.404   1.00 41.48  ? 402 HOH   A O    1 
HETATM 8805 O  O    . HOH   I 4 .   ? 12.305  -0.811  21.255  1.00 48.54  ? 403 HOH   A O    1 
HETATM 8806 O  O    . HOH   I 4 .   ? -44.314 -18.697 -29.799 1.00 29.48  ? 404 HOH   A O    1 
HETATM 8807 O  O    . HOH   I 4 .   ? -39.089 3.029   -35.626 1.00 43.54  ? 405 HOH   A O    1 
HETATM 8808 O  O    . HOH   I 4 .   ? 13.627  -11.422 23.342  1.00 44.16  ? 406 HOH   A O    1 
HETATM 8809 O  O    . HOH   I 4 .   ? -9.813  -12.181 16.993  1.00 29.60  ? 407 HOH   A O    1 
HETATM 8810 O  O    . HOH   I 4 .   ? -38.571 -9.723  -43.074 1.00 41.36  ? 408 HOH   A O    1 
HETATM 8811 O  O    . HOH   I 4 .   ? -42.362 -5.263  -35.580 1.00 39.59  ? 409 HOH   A O    1 
HETATM 8812 O  O    . HOH   I 4 .   ? 9.631   -4.361  26.132  1.00 38.07  ? 410 HOH   A O    1 
HETATM 8813 O  O    . HOH   I 4 .   ? -9.367  -8.056  -2.697  1.00 32.62  ? 411 HOH   A O    1 
HETATM 8814 O  O    . HOH   I 4 .   ? -20.725 -12.583 -6.370  1.00 38.24  ? 412 HOH   A O    1 
HETATM 8815 O  O    . HOH   I 4 .   ? -46.405 -20.684 -32.301 1.00 47.39  ? 413 HOH   A O    1 
HETATM 8816 O  O    . HOH   I 4 .   ? -37.592 5.677   -18.553 0.72 37.84  ? 414 HOH   A O    1 
HETATM 8817 O  O    . HOH   I 4 .   ? -14.566 -33.375 7.487   1.00 38.80  ? 415 HOH   A O    1 
HETATM 8818 O  O    . HOH   I 4 .   ? -9.862  -32.057 2.626   1.00 42.85  ? 416 HOH   A O    1 
HETATM 8819 O  O    . HOH   I 4 .   ? -11.647 -18.625 20.492  1.00 29.19  ? 417 HOH   A O    1 
HETATM 8820 O  O    . HOH   I 4 .   ? -15.224 -14.072 -17.347 1.00 42.01  ? 418 HOH   A O    1 
HETATM 8821 O  O    . HOH   I 4 .   ? 4.520   4.298   6.294   1.00 33.86  ? 419 HOH   A O    1 
HETATM 8822 O  O    . HOH   I 4 .   ? -3.125  8.509   3.678   1.00 40.83  ? 420 HOH   A O    1 
HETATM 8823 O  O    . HOH   I 4 .   ? -38.581 5.538   -24.566 1.00 43.77  ? 421 HOH   A O    1 
HETATM 8824 O  O    . HOH   I 4 .   ? -38.171 -30.112 -31.855 1.00 51.29  ? 422 HOH   A O    1 
HETATM 8825 O  O    . HOH   I 4 .   ? 0.899   -31.953 11.359  1.00 32.02  ? 423 HOH   A O    1 
HETATM 8826 O  O    . HOH   I 4 .   ? -36.771 -0.513  -12.725 1.00 29.71  ? 424 HOH   A O    1 
HETATM 8827 O  O    . HOH   I 4 .   ? -9.668  -15.846 10.881  1.00 48.85  ? 425 HOH   A O    1 
HETATM 8828 O  O    . HOH   I 4 .   ? -40.299 -1.403  -9.254  1.00 42.20  ? 426 HOH   A O    1 
HETATM 8829 O  O    . HOH   I 4 .   ? -49.733 -12.954 -27.125 1.00 28.98  ? 427 HOH   A O    1 
HETATM 8830 O  O    . HOH   I 4 .   ? -28.381 -9.755  -9.001  1.00 20.57  ? 428 HOH   A O    1 
HETATM 8831 O  O    . HOH   I 4 .   ? -9.273  -8.745  14.235  1.00 26.92  ? 429 HOH   A O    1 
HETATM 8832 O  O    . HOH   I 4 .   ? -9.886  0.434   9.831   1.00 29.13  ? 430 HOH   A O    1 
HETATM 8833 O  O    . HOH   I 4 .   ? -1.862  -6.737  3.923   1.00 19.52  ? 431 HOH   A O    1 
HETATM 8834 O  O    . HOH   I 4 .   ? -17.092 -13.824 -9.456  1.00 36.74  ? 432 HOH   A O    1 
HETATM 8835 O  O    . HOH   I 4 .   ? -36.837 -7.184  -36.384 1.00 23.61  ? 433 HOH   A O    1 
HETATM 8836 O  O    . HOH   I 4 .   ? -40.230 -25.957 -20.172 1.00 49.21  ? 434 HOH   A O    1 
HETATM 8837 O  O    . HOH   I 4 .   ? 10.783  -1.053  18.962  1.00 33.20  ? 435 HOH   A O    1 
HETATM 8838 O  O    . HOH   I 4 .   ? -3.239  -2.487  -12.531 1.00 44.43  ? 436 HOH   A O    1 
HETATM 8839 O  O    . HOH   I 4 .   ? 9.383   -0.147  3.791   1.00 33.25  ? 437 HOH   A O    1 
HETATM 8840 O  O    . HOH   I 4 .   ? 13.005  -17.903 9.941   1.00 37.04  ? 438 HOH   A O    1 
HETATM 8841 O  O    . HOH   I 4 .   ? -52.197 -6.563  -18.210 1.00 33.41  ? 439 HOH   A O    1 
HETATM 8842 O  O    . HOH   I 4 .   ? 6.840   -12.489 -0.393  0.89 36.67  ? 440 HOH   A O    1 
HETATM 8843 O  O    . HOH   I 4 .   ? 1.698   8.899   16.308  1.00 47.38  ? 441 HOH   A O    1 
HETATM 8844 O  O    . HOH   I 4 .   ? -36.921 -29.218 -24.649 1.00 42.99  ? 442 HOH   A O    1 
HETATM 8845 O  O    . HOH   I 4 .   ? -2.163  -8.425  -3.717  1.00 23.11  ? 443 HOH   A O    1 
HETATM 8846 O  O    . HOH   I 4 .   ? -8.592  -3.840  -1.006  1.00 31.09  ? 444 HOH   A O    1 
HETATM 8847 O  O    . HOH   I 4 .   ? -5.167  -8.975  2.504   1.00 20.49  ? 445 HOH   A O    1 
HETATM 8848 O  O    . HOH   I 4 .   ? -44.457 -21.197 -24.394 1.00 27.31  ? 446 HOH   A O    1 
HETATM 8849 O  O    . HOH   I 4 .   ? -34.244 -14.103 -46.896 1.00 34.81  ? 447 HOH   A O    1 
HETATM 8850 O  O    . HOH   I 4 .   ? -32.129 -2.232  -12.129 1.00 32.27  ? 448 HOH   A O    1 
HETATM 8851 O  O    . HOH   I 4 .   ? -34.166 4.354   -18.481 1.00 44.75  ? 449 HOH   A O    1 
HETATM 8852 O  O    . HOH   I 4 .   ? -34.213 -20.848 -29.948 1.00 21.68  ? 450 HOH   A O    1 
HETATM 8853 O  O    . HOH   I 4 .   ? -6.590  -30.698 18.627  0.72 32.53  ? 451 HOH   A O    1 
HETATM 8854 O  O    . HOH   I 4 .   ? -44.728 -14.124 -36.774 1.00 33.16  ? 452 HOH   A O    1 
HETATM 8855 O  O    . HOH   I 4 .   ? -35.723 -30.675 -23.465 1.00 45.67  ? 453 HOH   A O    1 
HETATM 8856 O  O    . HOH   I 4 .   ? -10.188 2.789   25.325  1.00 39.30  ? 454 HOH   A O    1 
HETATM 8857 O  O    . HOH   I 4 .   ? -0.959  -28.699 -5.325  1.00 39.24  ? 455 HOH   A O    1 
HETATM 8858 O  O    . HOH   I 4 .   ? 14.260  -14.227 5.346   0.92 42.68  ? 456 HOH   A O    1 
HETATM 8859 O  O    . HOH   I 4 .   ? -40.297 -19.092 -38.085 1.00 35.04  ? 457 HOH   A O    1 
HETATM 8860 O  O    . HOH   I 4 .   ? 11.111  -6.991  1.524   1.00 48.46  ? 458 HOH   A O    1 
HETATM 8861 O  O    . HOH   I 4 .   ? -3.527  -9.843  -1.666  1.00 23.55  ? 459 HOH   A O    1 
HETATM 8862 O  O    . HOH   I 4 .   ? -35.953 -9.049  -10.624 1.00 23.05  ? 460 HOH   A O    1 
HETATM 8863 O  O    . HOH   I 4 .   ? -48.426 -16.600 -21.028 1.00 45.70  ? 461 HOH   A O    1 
HETATM 8864 O  O    . HOH   I 4 .   ? -25.832 -16.092 -24.698 1.00 25.81  ? 462 HOH   A O    1 
HETATM 8865 O  O    . HOH   I 4 .   ? -47.894 -14.013 -20.728 1.00 27.36  ? 463 HOH   A O    1 
HETATM 8866 O  O    . HOH   I 4 .   ? -36.043 -23.588 -21.758 1.00 35.31  ? 464 HOH   A O    1 
HETATM 8867 O  O    . HOH   I 4 .   ? -39.018 -13.938 -45.469 1.00 29.63  ? 465 HOH   A O    1 
HETATM 8868 O  O    . HOH   I 4 .   ? -33.592 -19.007 -44.984 0.83 22.58  ? 466 HOH   A O    1 
HETATM 8869 O  O    . HOH   I 4 .   ? 1.268   1.050   -4.877  1.00 39.94  ? 467 HOH   A O    1 
HETATM 8870 O  O    . HOH   I 4 .   ? -7.542  -26.371 4.206   1.00 35.62  ? 468 HOH   A O    1 
HETATM 8871 O  O    . HOH   I 4 .   ? -52.461 -2.618  -25.305 1.00 44.63  ? 469 HOH   A O    1 
HETATM 8872 O  O    . HOH   I 4 .   ? -45.279 -2.276  -35.684 1.00 43.58  ? 470 HOH   A O    1 
HETATM 8873 O  O    . HOH   I 4 .   ? -3.226  -16.897 -1.485  1.00 21.16  ? 471 HOH   A O    1 
HETATM 8874 O  O    . HOH   I 4 .   ? -0.356  -18.891 -5.483  1.00 32.25  ? 472 HOH   A O    1 
HETATM 8875 O  O    . HOH   I 4 .   ? 6.800   -20.784 4.551   1.00 39.47  ? 473 HOH   A O    1 
HETATM 8876 O  O    . HOH   I 4 .   ? -5.180  -25.724 2.157   1.00 32.53  ? 474 HOH   A O    1 
HETATM 8877 O  O    . HOH   I 4 .   ? -44.398 -20.190 -21.753 1.00 31.26  ? 475 HOH   A O    1 
HETATM 8878 O  O    . HOH   I 4 .   ? -35.789 -10.901 -45.340 1.00 41.06  ? 476 HOH   A O    1 
HETATM 8879 O  O    . HOH   I 4 .   ? -7.784  -24.855 11.275  1.00 20.63  ? 477 HOH   A O    1 
HETATM 8880 O  O    . HOH   I 4 .   ? -10.323 -23.290 11.061  1.00 31.77  ? 478 HOH   A O    1 
HETATM 8881 O  O    . HOH   I 4 .   ? -40.969 -0.353  -16.100 1.00 30.91  ? 479 HOH   A O    1 
HETATM 8882 O  O    . HOH   I 4 .   ? -11.732 -21.724 -4.183  1.00 39.90  ? 480 HOH   A O    1 
HETATM 8883 O  O    . HOH   I 4 .   ? -14.814 -30.720 16.569  1.00 37.77  ? 481 HOH   A O    1 
HETATM 8884 O  O    . HOH   I 4 .   ? 6.566   -12.766 3.237   1.00 25.89  ? 482 HOH   A O    1 
HETATM 8885 O  O    . HOH   I 4 .   ? 10.116  1.240   17.255  1.00 28.62  ? 483 HOH   A O    1 
HETATM 8886 O  O    . HOH   I 4 .   ? -1.669  -32.661 7.206   1.00 45.12  ? 484 HOH   A O    1 
HETATM 8887 O  O    . HOH   I 4 .   ? -31.614 -10.413 -2.900  1.00 31.24  ? 485 HOH   A O    1 
HETATM 8888 O  O    . HOH   I 4 .   ? 0.142   -30.925 7.830   1.00 34.31  ? 486 HOH   A O    1 
HETATM 8889 O  O    . HOH   I 4 .   ? 14.221  -11.245 5.503   0.92 29.88  ? 487 HOH   A O    1 
HETATM 8890 O  O    . HOH   I 4 .   ? -2.200  -10.407 0.775   1.00 21.29  ? 488 HOH   A O    1 
HETATM 8891 O  O    . HOH   I 4 .   ? -11.479 0.578   7.497   1.00 39.01  ? 489 HOH   A O    1 
HETATM 8892 O  O    . HOH   I 4 .   ? -47.264 -1.081  -30.555 1.00 39.21  ? 490 HOH   A O    1 
HETATM 8893 O  O    . HOH   I 4 .   ? -2.736  -6.741  -5.809  1.00 33.48  ? 491 HOH   A O    1 
HETATM 8894 O  O    . HOH   I 4 .   ? 4.630   -21.467 1.612   1.00 36.44  ? 492 HOH   A O    1 
HETATM 8895 O  O    . HOH   I 4 .   ? -13.524 -4.732  3.849   1.00 40.90  ? 493 HOH   A O    1 
HETATM 8896 O  O    . HOH   I 4 .   ? -26.479 -28.894 -35.882 1.00 41.98  ? 494 HOH   A O    1 
HETATM 8897 O  O    . HOH   I 4 .   ? -37.956 -0.515  -39.379 1.00 40.07  ? 495 HOH   A O    1 
HETATM 8898 O  O    . HOH   I 4 .   ? -46.901 0.690   -32.464 1.00 44.64  ? 496 HOH   A O    1 
HETATM 8899 O  O    . HOH   I 4 .   ? -12.729 -26.776 -0.146  1.00 30.32  ? 497 HOH   A O    1 
HETATM 8900 O  O    . HOH   I 4 .   ? -31.357 -20.007 -45.554 1.00 43.61  ? 498 HOH   A O    1 
HETATM 8901 O  O    . HOH   I 4 .   ? 1.035   0.027   -7.037  1.00 47.51  ? 499 HOH   A O    1 
HETATM 8902 O  O    . HOH   I 4 .   ? -35.328 -22.972 -39.787 1.00 33.43  ? 500 HOH   A O    1 
HETATM 8903 O  O    . HOH   I 4 .   ? -45.402 7.260   -23.733 1.00 44.32  ? 501 HOH   A O    1 
HETATM 8904 O  O    . HOH   I 4 .   ? -51.885 -10.480 -29.928 1.00 45.07  ? 502 HOH   A O    1 
HETATM 8905 O  O    . HOH   I 4 .   ? -53.284 -4.578  -26.977 1.00 34.35  ? 503 HOH   A O    1 
HETATM 8906 O  O    . HOH   I 4 .   ? 9.578   -24.968 6.901   1.00 46.74  ? 504 HOH   A O    1 
HETATM 8907 O  O    . HOH   I 4 .   ? -32.752 0.352   -15.323 1.00 27.71  ? 505 HOH   A O    1 
HETATM 8908 O  O    . HOH   I 4 .   ? -8.888  -9.054  -7.495  1.00 35.74  ? 506 HOH   A O    1 
HETATM 8909 O  O    . HOH   I 4 .   ? -23.074 -25.900 -32.566 1.00 41.77  ? 507 HOH   A O    1 
HETATM 8910 O  O    . HOH   I 4 .   ? 15.811  -12.845 7.425   0.92 35.63  ? 508 HOH   A O    1 
HETATM 8911 O  O    . HOH   I 4 .   ? -39.068 0.676   -14.221 1.00 26.85  ? 509 HOH   A O    1 
HETATM 8912 O  O    . HOH   I 4 .   ? -2.238  -17.484 1.128   1.00 20.04  ? 510 HOH   A O    1 
HETATM 8913 O  O    . HOH   I 4 .   ? -0.909  -7.584  6.481   1.00 22.31  ? 511 HOH   A O    1 
HETATM 8914 O  O    . HOH   I 4 .   ? 0.246   3.026   -5.663  1.00 44.53  ? 512 HOH   A O    1 
HETATM 8915 O  O    . HOH   I 4 .   ? 11.702  -2.267  11.727  1.00 37.13  ? 513 HOH   A O    1 
HETATM 8916 O  O    . HOH   I 4 .   ? -27.981 -7.986  -1.761  1.00 39.04  ? 514 HOH   A O    1 
HETATM 8917 O  O    . HOH   I 4 .   ? -38.873 -18.329 -41.060 1.00 28.33  ? 515 HOH   A O    1 
HETATM 8918 O  O    . HOH   I 4 .   ? 11.498  -12.726 3.211   1.00 39.77  ? 516 HOH   A O    1 
HETATM 8919 O  O    . HOH   I 4 .   ? -3.034  -35.153 10.677  1.00 30.41  ? 517 HOH   A O    1 
HETATM 8920 O  O    . HOH   I 4 .   ? 3.254   -13.497 -2.130  1.00 31.10  ? 518 HOH   A O    1 
HETATM 8921 O  O    . HOH   I 4 .   ? -41.128 -27.066 -26.579 1.00 38.80  ? 519 HOH   A O    1 
HETATM 8922 O  O    . HOH   I 4 .   ? -12.683 -33.878 9.240   1.00 31.57  ? 520 HOH   A O    1 
HETATM 8923 O  O    . HOH   I 4 .   ? -28.377 -11.209 -47.280 1.00 45.25  ? 521 HOH   A O    1 
HETATM 8924 O  O    . HOH   I 4 .   ? -29.367 -7.805  -44.997 1.00 38.50  ? 522 HOH   A O    1 
HETATM 8925 O  O    . HOH   I 4 .   ? -47.195 -13.020 -33.576 1.00 31.97  ? 523 HOH   A O    1 
HETATM 8926 O  O    . HOH   I 4 .   ? -49.293 -11.474 -33.362 1.00 41.29  ? 524 HOH   A O    1 
HETATM 8927 O  O    . HOH   I 4 .   ? -29.797 -26.819 -37.100 1.00 31.09  ? 525 HOH   A O    1 
HETATM 8928 O  O    . HOH   I 4 .   ? -3.768  -30.861 18.707  1.00 38.23  ? 526 HOH   A O    1 
HETATM 8929 O  O    . HOH   I 4 .   ? -4.291  7.542   12.152  1.00 40.92  ? 527 HOH   A O    1 
HETATM 8930 O  O    . HOH   I 4 .   ? -42.703 -18.155 -36.858 1.00 32.64  ? 528 HOH   A O    1 
HETATM 8931 O  O    . HOH   I 4 .   ? -3.542  1.858   30.309  1.00 51.98  ? 529 HOH   A O    1 
HETATM 8932 O  O    . HOH   I 4 .   ? 8.831   -12.204 1.857   0.89 32.78  ? 530 HOH   A O    1 
HETATM 8933 O  O    . HOH   I 4 .   ? -3.330  -14.028 -12.838 1.00 45.23  ? 531 HOH   A O    1 
HETATM 8934 O  O    . HOH   I 4 .   ? 2.671   -1.453  -7.630  1.00 45.08  ? 532 HOH   A O    1 
HETATM 8935 O  O    . HOH   I 4 .   ? -35.768 -20.110 -46.589 0.83 26.29  ? 533 HOH   A O    1 
HETATM 8936 O  O    . HOH   I 4 .   ? 4.243   5.494   0.251   1.00 32.15  ? 534 HOH   A O    1 
HETATM 8937 O  O    . HOH   I 4 .   ? -9.306  -17.852 10.134  1.00 31.46  ? 535 HOH   A O    1 
HETATM 8938 O  O    . HOH   I 4 .   ? -45.377 -0.549  -18.805 1.00 21.11  ? 536 HOH   A O    1 
HETATM 8939 O  O    . HOH   I 4 .   ? -52.292 -7.790  -29.635 1.00 43.54  ? 537 HOH   A O    1 
HETATM 8940 O  O    . HOH   I 4 .   ? -39.131 -5.883  -37.705 1.00 35.10  ? 538 HOH   A O    1 
HETATM 8941 O  O    . HOH   I 4 .   ? -45.922 1.722   -20.563 1.00 35.46  ? 539 HOH   A O    1 
HETATM 8942 O  O    . HOH   I 4 .   ? -10.796 -36.194 8.679   1.00 43.71  ? 540 HOH   A O    1 
HETATM 8943 O  O    . HOH   I 4 .   ? -11.224 -2.892  0.121   1.00 47.46  ? 541 HOH   A O    1 
HETATM 8944 O  O    . HOH   I 4 .   ? -23.891 -29.727 -37.309 1.00 48.24  ? 542 HOH   A O    1 
HETATM 8945 O  O    . HOH   I 4 .   ? -6.382  -36.127 11.897  1.00 22.82  ? 543 HOH   A O    1 
HETATM 8946 O  O    . HOH   I 4 .   ? -53.897 -9.094  -28.170 1.00 51.00  ? 544 HOH   A O    1 
HETATM 8947 O  O    . HOH   I 4 .   ? 6.442   -4.338  -1.612  1.00 24.56  ? 545 HOH   A O    1 
HETATM 8948 O  O    . HOH   I 4 .   ? -34.803 -2.599  -9.692  1.00 43.00  ? 546 HOH   A O    1 
HETATM 8949 O  O    . HOH   I 4 .   ? -44.722 -27.002 -19.539 1.00 40.68  ? 547 HOH   A O    1 
HETATM 8950 O  O    . HOH   I 4 .   ? -3.248  -37.645 16.340  1.00 38.47  ? 548 HOH   A O    1 
HETATM 8951 O  O    . HOH   I 4 .   ? 3.495   -16.503 -4.049  1.00 44.60  ? 549 HOH   A O    1 
HETATM 8952 O  O    . HOH   I 4 .   ? -37.960 -7.800  -39.412 1.00 40.86  ? 550 HOH   A O    1 
HETATM 8953 O  O    . HOH   I 4 .   ? -0.948  -38.759 14.247  1.00 56.18  ? 551 HOH   A O    1 
HETATM 8954 O  O    . HOH   I 4 .   ? -9.383  -24.944 12.035  1.00 37.71  ? 552 HOH   A O    1 
HETATM 8955 O  O    . HOH   I 4 .   ? -51.701 -11.641 -19.737 1.00 51.20  ? 553 HOH   A O    1 
HETATM 8956 O  O    . HOH   I 4 .   ? -9.031  -37.048 10.421  1.00 36.96  ? 554 HOH   A O    1 
HETATM 8957 O  O    . HOH   I 4 .   ? -49.947 -12.612 -21.900 1.00 32.60  ? 555 HOH   A O    1 
HETATM 8958 O  O    . HOH   I 4 .   ? -7.622  -3.923  -9.349  1.00 40.92  ? 556 HOH   A O    1 
HETATM 8959 O  O    . HOH   I 4 .   ? -48.253 -14.361 -31.553 1.00 49.62  ? 557 HOH   A O    1 
HETATM 8960 O  O    . HOH   I 4 .   ? -5.004  -29.556 18.884  1.00 44.75  ? 558 HOH   A O    1 
HETATM 8961 O  O    . HOH   I 4 .   ? -33.569 -0.169  -12.474 1.00 33.36  ? 559 HOH   A O    1 
HETATM 8962 O  O    . HOH   I 4 .   ? -4.325  -37.838 11.648  1.00 40.40  ? 560 HOH   A O    1 
HETATM 8963 O  O    . HOH   I 4 .   ? -15.443 -13.501 -13.615 1.00 48.39  ? 561 HOH   A O    1 
HETATM 8964 O  O    . HOH   I 4 .   ? -22.702 -26.114 -36.754 1.00 50.63  ? 562 HOH   A O    1 
HETATM 8965 O  O    . HOH   I 4 .   ? -33.230 2.306   -39.783 1.00 45.22  ? 563 HOH   A O    1 
HETATM 8966 O  O    . HOH   I 4 .   ? -23.999 -27.690 -35.308 1.00 50.49  ? 564 HOH   A O    1 
HETATM 8967 O  O    . HOH   I 4 .   ? -46.604 -17.922 -30.949 1.00 47.13  ? 565 HOH   A O    1 
HETATM 8968 O  O    . HOH   I 4 .   ? -44.094 -16.355 -38.008 1.00 42.17  ? 566 HOH   A O    1 
HETATM 8969 O  O    . HOH   I 4 .   ? -40.719 -16.019 -41.829 1.00 43.81  ? 567 HOH   A O    1 
HETATM 8970 O  O    . HOH   J 4 .   ? -27.951 -17.364 -22.121 1.00 46.85  ? 401 HOH   B O    1 
HETATM 8971 O  O    . HOH   J 4 .   ? -29.739 -14.018 5.393   0.92 47.50  ? 402 HOH   B O    1 
HETATM 8972 O  O    . HOH   J 4 .   ? -4.861  -2.921  -20.012 1.00 47.70  ? 403 HOH   B O    1 
HETATM 8973 O  O    . HOH   J 4 .   ? -18.117 -8.244  -49.213 1.00 45.64  ? 404 HOH   B O    1 
HETATM 8974 O  O    . HOH   J 4 .   ? -25.136 1.812   -8.990  1.00 43.53  ? 405 HOH   B O    1 
HETATM 8975 O  O    . HOH   J 4 .   ? -12.562 -11.520 30.682  1.00 47.96  ? 406 HOH   B O    1 
HETATM 8976 O  O    . HOH   J 4 .   ? -14.484 -17.978 21.383  1.00 29.92  ? 407 HOH   B O    1 
HETATM 8977 O  O    . HOH   J 4 .   ? -24.612 -20.681 -0.130  1.00 42.14  ? 408 HOH   B O    1 
HETATM 8978 O  O    . HOH   J 4 .   ? -37.915 -8.709  -3.091  1.00 34.02  ? 409 HOH   B O    1 
HETATM 8979 O  O    . HOH   J 4 .   ? -4.626  -20.488 29.077  1.00 28.43  ? 410 HOH   B O    1 
HETATM 8980 O  O    . HOH   J 4 .   ? -14.125 -15.012 -24.517 1.00 36.27  ? 411 HOH   B O    1 
HETATM 8981 O  O    . HOH   J 4 .   ? -13.260 -4.549  -36.088 1.00 38.25  ? 412 HOH   B O    1 
HETATM 8982 O  O    . HOH   J 4 .   ? -46.232 -15.056 -15.403 1.00 38.50  ? 413 HOH   B O    1 
HETATM 8983 O  O    . HOH   J 4 .   ? -29.939 -17.846 -24.256 1.00 27.81  ? 414 HOH   B O    1 
HETATM 8984 O  O    . HOH   J 4 .   ? 9.226   -21.246 29.100  1.00 37.06  ? 415 HOH   B O    1 
HETATM 8985 O  O    . HOH   J 4 .   ? 1.266   -25.639 3.898   1.00 37.03  ? 416 HOH   B O    1 
HETATM 8986 O  O    . HOH   J 4 .   ? -38.224 -11.327 -2.156  0.89 34.70  ? 417 HOH   B O    1 
HETATM 8987 O  O    . HOH   J 4 .   ? -36.519 5.952   -26.260 1.00 37.03  ? 418 HOH   B O    1 
HETATM 8988 O  O    . HOH   J 4 .   ? -10.289 -20.630 1.923   1.00 19.42  ? 419 HOH   B O    1 
HETATM 8989 O  O    . HOH   J 4 .   ? -9.533  -25.299 24.274  1.00 35.25  ? 420 HOH   B O    1 
HETATM 8990 O  O    . HOH   J 4 .   ? -7.409  -3.507  -17.067 1.00 38.24  ? 421 HOH   B O    1 
HETATM 8991 O  O    . HOH   J 4 .   ? -25.935 -7.655  -3.361  1.00 37.31  ? 422 HOH   B O    1 
HETATM 8992 O  O    . HOH   J 4 .   ? -15.308 -9.265  -40.912 1.00 40.53  ? 423 HOH   B O    1 
HETATM 8993 O  O    . HOH   J 4 .   ? -10.509 2.177   -21.187 1.00 42.50  ? 424 HOH   B O    1 
HETATM 8994 O  O    . HOH   J 4 .   ? -15.589 -21.728 23.890  1.00 41.02  ? 425 HOH   B O    1 
HETATM 8995 O  O    . HOH   J 4 .   ? -46.466 -12.531 -16.673 1.00 31.87  ? 426 HOH   B O    1 
HETATM 8996 O  O    . HOH   J 4 .   ? -14.454 -1.375  -33.043 1.00 36.23  ? 427 HOH   B O    1 
HETATM 8997 O  O    . HOH   J 4 .   ? -8.905  -12.080 24.698  1.00 24.35  ? 428 HOH   B O    1 
HETATM 8998 O  O    . HOH   J 4 .   ? -15.334 -14.806 -2.493  1.00 40.45  ? 429 HOH   B O    1 
HETATM 8999 O  O    . HOH   J 4 .   ? -17.742 -0.679  -16.020 1.00 23.94  ? 430 HOH   B O    1 
HETATM 9000 O  O    . HOH   J 4 .   ? 12.374  -16.506 27.019  0.83 24.96  ? 431 HOH   B O    1 
HETATM 9001 O  O    . HOH   J 4 .   ? -36.482 -20.692 -22.097 1.00 32.19  ? 432 HOH   B O    1 
HETATM 9002 O  O    . HOH   J 4 .   ? -35.534 0.138   -39.602 1.00 37.98  ? 433 HOH   B O    1 
HETATM 9003 O  O    . HOH   J 4 .   ? -38.802 5.608   -20.517 0.72 39.03  ? 434 HOH   B O    1 
HETATM 9004 O  O    . HOH   J 4 .   ? 0.361   -26.664 27.219  1.00 33.34  ? 435 HOH   B O    1 
HETATM 9005 O  O    . HOH   J 4 .   ? -42.289 -11.545 -1.279  1.00 30.72  ? 436 HOH   B O    1 
HETATM 9006 O  O    . HOH   J 4 .   ? -7.036  -25.770 6.685   1.00 21.39  ? 437 HOH   B O    1 
HETATM 9007 O  O    . HOH   J 4 .   ? -16.674 -11.409 -1.614  1.00 40.48  ? 438 HOH   B O    1 
HETATM 9008 O  O    . HOH   J 4 .   ? -7.618  -7.022  -30.138 1.00 28.84  ? 439 HOH   B O    1 
HETATM 9009 O  O    . HOH   J 4 .   ? -26.858 -2.124  -41.436 1.00 31.66  ? 440 HOH   B O    1 
HETATM 9010 O  O    . HOH   J 4 .   ? 4.467   -27.271 7.055   1.00 34.84  ? 441 HOH   B O    1 
HETATM 9011 O  O    . HOH   J 4 .   ? -15.803 -15.199 -26.483 1.00 26.34  ? 442 HOH   B O    1 
HETATM 9012 O  O    . HOH   J 4 .   ? 3.793   -27.696 9.721   1.00 29.99  ? 443 HOH   B O    1 
HETATM 9013 O  O    . HOH   J 4 .   ? -20.419 -4.596  -22.281 1.00 19.78  ? 444 HOH   B O    1 
HETATM 9014 O  O    . HOH   J 4 .   ? -29.048 -14.040 -18.558 1.00 39.73  ? 445 HOH   B O    1 
HETATM 9015 O  O    . HOH   J 4 .   ? -18.652 -30.273 11.946  1.00 47.39  ? 446 HOH   B O    1 
HETATM 9016 O  O    . HOH   J 4 .   ? -5.879  -16.675 -1.389  1.00 20.73  ? 447 HOH   B O    1 
HETATM 9017 O  O    . HOH   J 4 .   ? -13.939 -8.106  -17.385 1.00 28.86  ? 448 HOH   B O    1 
HETATM 9018 O  O    . HOH   J 4 .   ? -9.749  -2.243  20.698  1.00 26.42  ? 449 HOH   B O    1 
HETATM 9019 O  O    . HOH   J 4 .   ? 8.304   -15.066 25.775  1.00 25.21  ? 450 HOH   B O    1 
HETATM 9020 O  O    . HOH   J 4 .   ? -24.627 -4.517  -11.069 1.00 22.95  ? 451 HOH   B O    1 
HETATM 9021 O  O    . HOH   J 4 .   ? -16.067 -7.486  -13.475 1.00 36.75  ? 452 HOH   B O    1 
HETATM 9022 O  O    . HOH   J 4 .   ? -45.519 -4.098  -13.934 1.00 28.76  ? 453 HOH   B O    1 
HETATM 9023 O  O    . HOH   J 4 .   ? -17.927 -21.660 -29.799 1.00 45.18  ? 454 HOH   B O    1 
HETATM 9024 O  O    . HOH   J 4 .   ? -14.469 -18.214 -40.164 1.00 51.11  ? 455 HOH   B O    1 
HETATM 9025 O  O    . HOH   J 4 .   ? -23.792 -20.425 -32.151 1.00 23.47  ? 456 HOH   B O    1 
HETATM 9026 O  O    . HOH   J 4 .   ? -17.977 3.669   -16.906 1.00 46.27  ? 457 HOH   B O    1 
HETATM 9027 O  O    . HOH   J 4 .   ? 9.778   -17.308 25.627  0.83 24.34  ? 458 HOH   B O    1 
HETATM 9028 O  O    . HOH   J 4 .   ? -16.391 -10.704 -13.826 1.00 48.55  ? 459 HOH   B O    1 
HETATM 9029 O  O    . HOH   J 4 .   ? -27.169 3.453   -21.793 1.00 31.31  ? 460 HOH   B O    1 
HETATM 9030 O  O    . HOH   J 4 .   ? -21.943 -23.799 -37.908 1.00 32.17  ? 461 HOH   B O    1 
HETATM 9031 O  O    . HOH   J 4 .   ? 6.579   -11.714 23.462  1.00 24.33  ? 462 HOH   B O    1 
HETATM 9032 O  O    . HOH   J 4 .   ? 2.744   -17.090 31.521  1.00 32.99  ? 463 HOH   B O    1 
HETATM 9033 O  O    . HOH   J 4 .   ? -17.617 4.471   -31.203 1.00 35.12  ? 464 HOH   B O    1 
HETATM 9034 O  O    . HOH   J 4 .   ? -15.181 -0.094  -15.311 1.00 31.18  ? 465 HOH   B O    1 
HETATM 9035 O  O    . HOH   J 4 .   ? -25.604 -2.260  -12.105 1.00 23.04  ? 466 HOH   B O    1 
HETATM 9036 O  O    . HOH   J 4 .   ? 5.386   -11.968 27.626  1.00 37.48  ? 467 HOH   B O    1 
HETATM 9037 O  O    . HOH   J 4 .   ? -20.711 -6.474  -18.474 1.00 20.38  ? 468 HOH   B O    1 
HETATM 9038 O  O    . HOH   J 4 .   ? -23.801 -17.209 -44.657 1.00 42.37  ? 469 HOH   B O    1 
HETATM 9039 O  O    . HOH   J 4 .   ? -19.608 -2.837  -15.950 1.00 24.09  ? 470 HOH   B O    1 
HETATM 9040 O  O    . HOH   J 4 .   ? -34.914 -7.729  -8.506  1.00 29.93  ? 471 HOH   B O    1 
HETATM 9041 O  O    . HOH   J 4 .   ? -12.108 -15.694 -21.928 1.00 42.75  ? 472 HOH   B O    1 
HETATM 9042 O  O    . HOH   J 4 .   ? -33.934 -5.317  -8.357  1.00 31.66  ? 473 HOH   B O    1 
HETATM 9043 O  O    . HOH   J 4 .   ? 13.878  -22.372 21.777  1.00 50.25  ? 474 HOH   B O    1 
HETATM 9044 O  O    . HOH   J 4 .   ? -21.622 -2.965  -17.915 1.00 21.08  ? 475 HOH   B O    1 
HETATM 9045 O  O    . HOH   J 4 .   ? -28.904 8.543   -28.106 1.00 41.44  ? 476 HOH   B O    1 
HETATM 9046 O  O    . HOH   J 4 .   ? -2.066  -12.465 32.649  1.00 40.80  ? 477 HOH   B O    1 
HETATM 9047 O  O    . HOH   J 4 .   ? 16.021  -18.845 26.083  1.00 44.58  ? 478 HOH   B O    1 
HETATM 9048 O  O    . HOH   J 4 .   ? -37.441 -12.050 -13.921 1.00 23.24  ? 479 HOH   B O    1 
HETATM 9049 O  O    . HOH   J 4 .   ? -1.509  -22.357 1.893   1.00 38.23  ? 480 HOH   B O    1 
HETATM 9050 O  O    . HOH   J 4 .   ? -11.740 -6.970  -15.880 1.00 35.01  ? 481 HOH   B O    1 
HETATM 9051 O  O    . HOH   J 4 .   ? -9.235  -23.677 26.751  1.00 28.22  ? 482 HOH   B O    1 
HETATM 9052 O  O    . HOH   J 4 .   ? -35.677 -14.283 -13.587 1.00 33.67  ? 483 HOH   B O    1 
HETATM 9053 O  O    . HOH   J 4 .   ? -39.651 -6.281  -3.771  1.00 39.86  ? 484 HOH   B O    1 
HETATM 9054 O  O    . HOH   J 4 .   ? -0.435  -3.130  33.500  1.00 37.75  ? 485 HOH   B O    1 
HETATM 9055 O  O    . HOH   J 4 .   ? -42.419 -14.331 -5.128  1.00 42.36  ? 486 HOH   B O    1 
HETATM 9056 O  O    . HOH   J 4 .   ? -9.830  -10.416 -19.773 1.00 34.54  ? 487 HOH   B O    1 
HETATM 9057 O  O    . HOH   J 4 .   ? 12.293  -18.922 25.366  0.83 28.90  ? 488 HOH   B O    1 
HETATM 9058 O  O    . HOH   J 4 .   ? -23.997 -2.105  -41.356 1.00 26.97  ? 489 HOH   B O    1 
HETATM 9059 O  O    . HOH   J 4 .   ? -1.070  -19.158 31.608  1.00 48.99  ? 490 HOH   B O    1 
HETATM 9060 O  O    . HOH   J 4 .   ? -19.233 5.081   -18.419 1.00 42.07  ? 491 HOH   B O    1 
HETATM 9061 O  O    . HOH   J 4 .   ? 4.829   -2.672  32.917  1.00 41.06  ? 492 HOH   B O    1 
HETATM 9062 O  O    . HOH   J 4 .   ? -11.258 -18.447 32.376  1.00 41.74  ? 493 HOH   B O    1 
HETATM 9063 O  O    . HOH   J 4 .   ? -3.676  -29.162 22.611  1.00 42.14  ? 494 HOH   B O    1 
HETATM 9064 O  O    . HOH   J 4 .   ? -30.677 -13.537 -16.556 1.00 34.99  ? 495 HOH   B O    1 
HETATM 9065 O  O    . HOH   J 4 .   ? 14.966  -17.131 21.128  1.00 38.39  ? 496 HOH   B O    1 
HETATM 9066 O  O    . HOH   J 4 .   ? -6.007  -7.121  33.015  1.00 40.81  ? 497 HOH   B O    1 
HETATM 9067 O  O    . HOH   J 4 .   ? 6.253   -28.942 13.469  1.00 32.25  ? 498 HOH   B O    1 
HETATM 9068 O  O    . HOH   J 4 .   ? -50.794 -10.617 -11.522 1.00 37.76  ? 499 HOH   B O    1 
HETATM 9069 O  O    . HOH   J 4 .   ? -10.122 1.309   -29.563 1.00 35.57  ? 500 HOH   B O    1 
HETATM 9070 O  O    . HOH   J 4 .   ? -27.571 -2.827  -14.084 1.00 21.16  ? 501 HOH   B O    1 
HETATM 9071 O  O    . HOH   J 4 .   ? 8.919   -12.493 24.893  1.00 30.02  ? 502 HOH   B O    1 
HETATM 9072 O  O    . HOH   J 4 .   ? -14.406 -4.066  -10.098 1.00 39.03  ? 503 HOH   B O    1 
HETATM 9073 O  O    . HOH   J 4 .   ? -19.543 -27.008 20.185  1.00 45.42  ? 504 HOH   B O    1 
HETATM 9074 O  O    . HOH   J 4 .   ? -42.583 -3.713  -11.236 1.00 29.62  ? 505 HOH   B O    1 
HETATM 9075 O  O    . HOH   J 4 .   ? -9.936  -30.525 22.882  1.00 46.82  ? 506 HOH   B O    1 
HETATM 9076 O  O    . HOH   J 4 .   ? 4.264   -10.075 36.096  1.00 43.31  ? 507 HOH   B O    1 
HETATM 9077 O  O    . HOH   J 4 .   ? -27.880 -9.356  -45.590 1.00 41.39  ? 508 HOH   B O    1 
HETATM 9078 O  O    . HOH   J 4 .   ? -20.357 8.021   -21.039 1.00 53.01  ? 509 HOH   B O    1 
HETATM 9079 O  O    . HOH   J 4 .   ? -9.132  -4.441  -32.896 1.00 39.07  ? 510 HOH   B O    1 
HETATM 9080 O  O    . HOH   J 4 .   ? -32.933 -15.937 6.851   1.00 47.01  ? 511 HOH   B O    1 
HETATM 9081 O  O    . HOH   J 4 .   ? -13.373 -20.896 -5.557  1.00 49.25  ? 512 HOH   B O    1 
HETATM 9082 O  O    . HOH   J 4 .   ? -1.394  -15.496 32.637  1.00 30.25  ? 513 HOH   B O    1 
HETATM 9083 O  O    . HOH   J 4 .   ? -12.512 -12.081 -34.612 1.00 35.56  ? 514 HOH   B O    1 
HETATM 9084 O  O    . HOH   J 4 .   ? 10.824  -21.811 25.260  1.00 37.30  ? 515 HOH   B O    1 
HETATM 9085 O  O    . HOH   J 4 .   ? -24.284 2.741   -36.429 1.00 39.40  ? 516 HOH   B O    1 
HETATM 9086 O  O    . HOH   J 4 .   ? 2.732   -20.927 30.141  1.00 30.54  ? 517 HOH   B O    1 
HETATM 9087 O  O    . HOH   J 4 .   ? -26.101 -18.317 -21.518 1.00 45.86  ? 518 HOH   B O    1 
HETATM 9088 O  O    . HOH   J 4 .   ? -20.446 6.077   -37.588 1.00 47.62  ? 519 HOH   B O    1 
HETATM 9089 O  O    . HOH   J 4 .   ? -12.268 -2.301  29.324  1.00 48.17  ? 520 HOH   B O    1 
HETATM 9090 O  O    . HOH   J 4 .   ? -17.502 -14.414 -45.244 1.00 41.08  ? 521 HOH   B O    1 
HETATM 9091 O  O    . HOH   J 4 .   ? 2.673   -20.928 3.309   1.00 21.58  ? 522 HOH   B O    1 
HETATM 9092 O  O    . HOH   J 4 .   ? 6.608   -27.087 28.090  1.00 48.69  ? 523 HOH   B O    1 
HETATM 9093 O  O    . HOH   J 4 .   ? -11.633 -4.031  30.519  1.00 35.02  ? 524 HOH   B O    1 
HETATM 9094 O  O    . HOH   J 4 .   ? 8.974   -28.719 13.493  1.00 38.39  ? 525 HOH   B O    1 
HETATM 9095 O  O    . HOH   J 4 .   ? -24.077 4.302   -19.293 1.00 48.07  ? 526 HOH   B O    1 
HETATM 9096 O  O    . HOH   J 4 .   ? -22.695 -5.067  -23.902 1.00 23.23  ? 527 HOH   B O    1 
HETATM 9097 O  O    . HOH   J 4 .   ? -18.408 -5.972  -45.079 1.00 43.94  ? 528 HOH   B O    1 
HETATM 9098 O  O    . HOH   J 4 .   ? 6.527   -21.528 2.644   1.00 46.35  ? 529 HOH   B O    1 
HETATM 9099 O  O    . HOH   J 4 .   ? -32.606 4.187   -36.606 1.00 45.96  ? 530 HOH   B O    1 
HETATM 9100 O  O    . HOH   J 4 .   ? -24.030 3.541   -16.941 1.00 38.00  ? 531 HOH   B O    1 
HETATM 9101 O  O    . HOH   J 4 .   ? -27.272 3.102   -10.698 1.00 43.56  ? 532 HOH   B O    1 
HETATM 9102 O  O    . HOH   J 4 .   ? -26.797 -21.624 0.157   1.00 40.20  ? 533 HOH   B O    1 
HETATM 9103 O  O    . HOH   J 4 .   ? -28.903 -11.009 -1.105  1.00 43.25  ? 534 HOH   B O    1 
HETATM 9104 O  O    . HOH   J 4 .   ? -23.627 7.296   -38.357 1.00 48.30  ? 535 HOH   B O    1 
HETATM 9105 O  O    . HOH   J 4 .   ? -21.002 7.674   -38.709 1.00 53.63  ? 536 HOH   B O    1 
HETATM 9106 O  O    . HOH   J 4 .   ? -14.741 -3.365  -39.755 1.00 48.01  ? 537 HOH   B O    1 
HETATM 9107 O  O    . HOH   J 4 .   ? 2.075   -11.887 35.201  1.00 37.84  ? 538 HOH   B O    1 
HETATM 9108 O  O    . HOH   J 4 .   ? -0.110  -10.689 33.240  1.00 49.00  ? 539 HOH   B O    1 
HETATM 9109 O  O    . HOH   J 4 .   ? -17.033 -12.535 -14.347 1.00 47.11  ? 540 HOH   B O    1 
HETATM 9110 O  O    . HOH   J 4 .   ? -29.991 -11.097 5.823   0.92 40.53  ? 541 HOH   B O    1 
HETATM 9111 O  O    . HOH   J 4 .   ? -37.786 -13.723 -13.552 1.00 37.83  ? 542 HOH   B O    1 
HETATM 9112 O  O    . HOH   J 4 .   ? -27.848 -2.130  -43.833 1.00 44.34  ? 543 HOH   B O    1 
HETATM 9113 O  O    . HOH   J 4 .   ? 7.757   -10.638 26.578  1.00 38.76  ? 544 HOH   B O    1 
HETATM 9114 O  O    . HOH   J 4 .   ? -2.307  -26.345 1.972   1.00 44.51  ? 545 HOH   B O    1 
HETATM 9115 O  O    . HOH   J 4 .   ? -14.394 -26.046 -2.628  1.00 44.10  ? 546 HOH   B O    1 
HETATM 9116 O  O    . HOH   J 4 .   ? -13.994 -7.961  -14.774 1.00 43.14  ? 547 HOH   B O    1 
HETATM 9117 O  O    . HOH   J 4 .   ? -45.651 -14.064 -17.054 1.00 43.97  ? 548 HOH   B O    1 
HETATM 9118 O  O    . HOH   J 4 .   ? -14.986 -12.826 -2.792  1.00 41.83  ? 549 HOH   B O    1 
HETATM 9119 O  O    . HOH   J 4 .   ? -25.140 4.981   -36.402 1.00 45.51  ? 550 HOH   B O    1 
HETATM 9120 O  O    . HOH   J 4 .   ? -27.937 1.934   -6.543  1.00 46.19  ? 551 HOH   B O    1 
HETATM 9121 O  O    . HOH   J 4 .   ? 15.241  -14.661 19.546  1.00 35.61  ? 552 HOH   B O    1 
HETATM 9122 O  O    . HOH   J 4 .   ? -50.814 -4.603  -13.494 1.00 55.73  ? 553 HOH   B O    1 
HETATM 9123 O  O    . HOH   J 4 .   ? -5.891  -6.380  -15.359 1.00 46.69  ? 554 HOH   B O    1 
HETATM 9124 O  O    . HOH   J 4 .   ? 5.152   -29.547 11.173  1.00 35.33  ? 555 HOH   B O    1 
HETATM 9125 O  O    . HOH   J 4 .   ? -48.656 -12.468 -18.270 1.00 42.62  ? 556 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLY A 3   ? 1.0257 0.6145 0.8803 0.1097  -0.0278 0.0297  0   GLY A N   
2    C CA  . GLY A 3   ? 1.1141 0.6820 0.9535 0.1007  -0.0242 0.0178  0   GLY A CA  
3    C C   . GLY A 3   ? 1.0147 0.6009 0.8554 0.0868  -0.0197 0.0130  0   GLY A C   
4    O O   . GLY A 3   ? 1.1108 0.6836 0.9391 0.0757  -0.0183 0.0046  0   GLY A O   
8    N N   . MET A 4   ? 0.9259 0.5430 0.7815 0.0878  -0.0180 0.0183  1   MET A N   
9    C CA  . MET A 4   ? 0.7341 0.3777 0.5963 0.0701  -0.0149 0.0170  1   MET A CA  
10   C C   . MET A 4   ? 0.6914 0.3230 0.5439 0.0470  -0.0211 0.0271  1   MET A C   
11   O O   . MET A 4   ? 0.7229 0.3339 0.5667 0.0456  -0.0272 0.0377  1   MET A O   
12   C CB  . MET A 4   ? 0.6893 0.3831 0.5769 0.0750  -0.0108 0.0196  1   MET A CB  
13   C CG  . MET A 4   ? 0.5999 0.3154 0.5012 0.0929  -0.0032 0.0100  1   MET A CG  
14   S SD  . MET A 4   ? 0.5822 0.3548 0.5109 0.0916  0.0008  0.0120  1   MET A SD  
15   C CE  . MET A 4   ? 0.4926 0.2755 0.4175 0.0683  0.0031  0.0089  1   MET A CE  
25   N N   . GLU A 5   ? 0.5706 0.2155 0.4249 0.0286  -0.0195 0.0245  2   GLU A N   
26   C CA  . GLU A 5   ? 0.5809 0.2252 0.4323 0.0060  -0.0234 0.0342  2   GLU A CA  
27   C C   . GLU A 5   ? 0.5641 0.2477 0.4329 0.0028  -0.0207 0.0430  2   GLU A C   
28   O O   . GLU A 5   ? 0.5148 0.2294 0.3989 0.0134  -0.0162 0.0396  2   GLU A O   
29   C CB  . GLU A 5   ? 0.5802 0.2271 0.4297 -0.0109 -0.0234 0.0280  2   GLU A CB  
30   C CG  . GLU A 5   ? 0.6793 0.2841 0.5068 -0.0101 -0.0269 0.0185  2   GLU A CG  
31   C CD  . GLU A 5   ? 0.7720 0.3509 0.5880 -0.0173 -0.0331 0.0243  2   GLU A CD  
32   O OE1 . GLU A 5   ? 0.8140 0.3978 0.6319 -0.0373 -0.0367 0.0333  2   GLU A OE1 
33   O OE2 . GLU A 5   ? 0.9523 0.5075 0.7585 -0.0025 -0.0338 0.0203  2   GLU A OE2 
40   N N   . THR A 6   ? 0.5790 0.2601 0.4438 -0.0129 -0.0232 0.0545  3   THR A N   
41   C CA  . THR A 6   ? 0.5015 0.2143 0.3773 -0.0160 -0.0201 0.0629  3   THR A CA  
42   C C   . THR A 6   ? 0.4776 0.2062 0.3580 -0.0376 -0.0176 0.0683  3   THR A C   
43   O O   . THR A 6   ? 0.5556 0.2614 0.4252 -0.0527 -0.0212 0.0739  3   THR A O   
44   C CB  . THR A 6   ? 0.5758 0.2719 0.4407 -0.0099 -0.0247 0.0741  3   THR A CB  
45   O OG1 . THR A 6   ? 0.5911 0.2781 0.4565 0.0123  -0.0274 0.0701  3   THR A OG1 
46   C CG2 . THR A 6   ? 0.5488 0.2757 0.4204 -0.0148 -0.0213 0.0822  3   THR A CG2 
54   N N   . LEU A 7   ? 0.4210 0.1882 0.3177 -0.0391 -0.0114 0.0668  4   LEU A N   
55   C CA  . LEU A 7   ? 0.4575 0.2463 0.3618 -0.0558 -0.0072 0.0730  4   LEU A CA  
56   C C   . LEU A 7   ? 0.4092 0.2191 0.3154 -0.0521 -0.0025 0.0792  4   LEU A C   
57   O O   . LEU A 7   ? 0.4062 0.2357 0.3202 -0.0401 -0.0002 0.0735  4   LEU A O   
58   C CB  . LEU A 7   ? 0.4104 0.2244 0.3310 -0.0603 -0.0041 0.0651  4   LEU A CB  
59   C CG  . LEU A 7   ? 0.4019 0.2444 0.3356 -0.0744 0.0013  0.0707  4   LEU A CG  
60   C CD1 . LEU A 7   ? 0.4881 0.3151 0.4157 -0.0928 -0.0015 0.0799  4   LEU A CD1 
61   C CD2 . LEU A 7   ? 0.4104 0.2761 0.3604 -0.0743 0.0026  0.0624  4   LEU A CD2 
73   N N   . GLU A 8   ? 0.4204 0.2245 0.3172 -0.0633 -0.0014 0.0909  5   GLU A N   
74   C CA  . GLU A 8   ? 0.4579 0.2783 0.3510 -0.0613 0.0031  0.0971  5   GLU A CA  
75   C C   . GLU A 8   ? 0.4285 0.2845 0.3360 -0.0685 0.0128  0.0955  5   GLU A C   
76   O O   . GLU A 8   ? 0.4804 0.3436 0.3940 -0.0832 0.0166  0.0997  5   GLU A O   
77   C CB  . GLU A 8   ? 0.4957 0.2926 0.3691 -0.0703 0.0007  0.1110  5   GLU A CB  
78   C CG  . GLU A 8   ? 0.5124 0.2749 0.3706 -0.0585 -0.0093 0.1135  5   GLU A CG  
79   C CD  . GLU A 8   ? 0.6248 0.3636 0.4609 -0.0656 -0.0127 0.1286  5   GLU A CD  
80   O OE1 . GLU A 8   ? 0.8147 0.5693 0.6478 -0.0783 -0.0056 0.1360  5   GLU A OE1 
81   O OE2 . GLU A 8   ? 0.7491 0.4590 0.5745 -0.0561 -0.0213 0.1309  5   GLU A OE2 
88   N N   . LEU A 9   ? 0.3596 0.2375 0.2732 -0.0580 0.0165  0.0895  6   LEU A N   
89   C CA  . LEU A 9   ? 0.3953 0.3046 0.3222 -0.0603 0.0254  0.0856  6   LEU A CA  
90   C C   . LEU A 9   ? 0.3981 0.3169 0.3136 -0.0569 0.0304  0.0889  6   LEU A C   
91   O O   . LEU A 9   ? 0.3964 0.2994 0.2957 -0.0520 0.0250  0.0934  6   LEU A O   
92   C CB  . LEU A 9   ? 0.4074 0.3301 0.3497 -0.0513 0.0245  0.0736  6   LEU A CB  
93   C CG  . LEU A 9   ? 0.3850 0.2971 0.3348 -0.0545 0.0193  0.0694  6   LEU A CG  
94   C CD1 . LEU A 9   ? 0.4023 0.3259 0.3631 -0.0451 0.0185  0.0584  6   LEU A CD1 
95   C CD2 . LEU A 9   ? 0.4554 0.3765 0.4141 -0.0698 0.0223  0.0743  6   LEU A CD2 
107  N N   . GLN A 10  ? 0.3680 0.3118 0.2910 -0.0586 0.0400  0.0863  7   GLN A N   
108  C CA  . GLN A 10  ? 0.3562 0.3074 0.2650 -0.0554 0.0455  0.0877  7   GLN A CA  
109  C C   . GLN A 10  ? 0.3289 0.2752 0.2320 -0.0427 0.0380  0.0811  7   GLN A C   
110  O O   . GLN A 10  ? 0.3355 0.2912 0.2521 -0.0357 0.0365  0.0716  7   GLN A O   
111  C CB  . GLN A 10  ? 0.4090 0.3869 0.3279 -0.0568 0.0581  0.0838  7   GLN A CB  
112  C CG  . GLN A 10  ? 0.4164 0.3998 0.3178 -0.0520 0.0643  0.0823  7   GLN A CG  
113  C CD  . GLN A 10  ? 0.4385 0.4147 0.3177 -0.0605 0.0694  0.0933  7   GLN A CD  
114  O OE1 . GLN A 10  ? 0.4724 0.4485 0.3541 -0.0720 0.0735  0.1025  7   GLN A OE1 
115  N NE2 . GLN A 10  ? 0.5153 0.4833 0.3704 -0.0561 0.0679  0.0933  7   GLN A NE2 
124  N N   . GLY A 11  ? 0.3847 0.3163 0.2685 -0.0406 0.0322  0.0872  8   GLY A N   
125  C CA  . GLY A 11  ? 0.3990 0.3290 0.2782 -0.0302 0.0241  0.0828  8   GLY A CA  
126  C C   . GLY A 11  ? 0.3985 0.3187 0.2879 -0.0218 0.0138  0.0802  8   GLY A C   
127  O O   . GLY A 11  ? 0.3653 0.2885 0.2550 -0.0132 0.0070  0.0770  8   GLY A O   
131  N N   . ALA A 12  ? 0.3676 0.2763 0.2650 -0.0240 0.0125  0.0814  9   ALA A N   
132  C CA  . ALA A 12  ? 0.3509 0.2494 0.2562 -0.0142 0.0045  0.0778  9   ALA A CA  
133  C C   . ALA A 12  ? 0.4152 0.2910 0.3189 -0.0181 0.0022  0.0815  9   ALA A C   
134  O O   . ALA A 12  ? 0.4383 0.3122 0.3422 -0.0298 0.0071  0.0840  9   ALA A O   
135  C CB  . ALA A 12  ? 0.3368 0.2521 0.2600 -0.0085 0.0062  0.0661  9   ALA A CB  
141  N N   . LYS A 13  ? 0.4044 0.2634 0.3073 -0.0078 -0.0054 0.0813  10  LYS A N   
142  C CA  . LYS A 13  ? 0.4415 0.2765 0.3436 -0.0077 -0.0081 0.0803  10  LYS A CA  
143  C C   . LYS A 13  ? 0.3907 0.2350 0.3078 0.0006  -0.0069 0.0682  10  LYS A C   
144  O O   . LYS A 13  ? 0.3995 0.2504 0.3232 0.0140  -0.0096 0.0643  10  LYS A O   
145  C CB  . LYS A 13  ? 0.4832 0.2895 0.3722 0.0000  -0.0165 0.0879  10  LYS A CB  
146  C CG  . LYS A 13  ? 0.4894 0.2839 0.3602 -0.0085 -0.0186 0.1011  10  LYS A CG  
147  C CD  . LYS A 13  ? 0.6040 0.3639 0.4611 -0.0005 -0.0283 0.1090  10  LYS A CD  
148  C CE  . LYS A 13  ? 0.7364 0.4923 0.5777 0.0000  -0.0338 0.1212  10  LYS A CE  
149  N NZ  . LYS A 13  ? 0.8486 0.5960 0.6730 -0.0189 -0.0294 0.1315  10  LYS A NZ  
163  N N   . LEU A 14  ? 0.3671 0.2137 0.2898 -0.0079 -0.0029 0.0629  11  LEU A N   
164  C CA  . LEU A 14  ? 0.3649 0.2199 0.2986 -0.0026 -0.0011 0.0519  11  LEU A CA  
165  C C   . LEU A 14  ? 0.4068 0.2328 0.3329 0.0028  -0.0049 0.0487  11  LEU A C   
166  O O   . LEU A 14  ? 0.4120 0.2150 0.3279 -0.0066 -0.0072 0.0518  11  LEU A O   
167  C CB  . LEU A 14  ? 0.3541 0.2245 0.2958 -0.0142 0.0034  0.0486  11  LEU A CB  
168  C CG  . LEU A 14  ? 0.3706 0.2530 0.3222 -0.0100 0.0052  0.0383  11  LEU A CG  
169  C CD1 . LEU A 14  ? 0.3619 0.2691 0.3225 -0.0038 0.0080  0.0357  11  LEU A CD1 
170  C CD2 . LEU A 14  ? 0.3918 0.2789 0.3480 -0.0224 0.0063  0.0368  11  LEU A CD2 
182  N N   . ARG A 15  ? 0.3870 0.2136 0.3175 0.0177  -0.0053 0.0424  12  ARG A N   
183  C CA  . ARG A 15  ? 0.3801 0.1792 0.3026 0.0261  -0.0071 0.0374  12  ARG A CA  
184  C C   . ARG A 15  ? 0.4276 0.2331 0.3541 0.0259  -0.0027 0.0261  12  ARG A C   
185  O O   . ARG A 15  ? 0.3821 0.2163 0.3212 0.0264  0.0014  0.0221  12  ARG A O   
186  C CB  . ARG A 15  ? 0.4384 0.2338 0.3634 0.0449  -0.0096 0.0385  12  ARG A CB  
187  C CG  . ARG A 15  ? 0.4920 0.2610 0.4042 0.0474  -0.0165 0.0489  12  ARG A CG  
188  C CD  . ARG A 15  ? 0.4761 0.2524 0.3836 0.0335  -0.0184 0.0597  12  ARG A CD  
189  N NE  . ARG A 15  ? 0.5085 0.2565 0.4005 0.0343  -0.0253 0.0709  12  ARG A NE  
190  C CZ  . ARG A 15  ? 0.5410 0.2922 0.4319 0.0432  -0.0308 0.0789  12  ARG A CZ  
191  N NH1 . ARG A 15  ? 0.5078 0.2898 0.4135 0.0524  -0.0307 0.0767  12  ARG A NH1 
192  N NH2 . ARG A 15  ? 0.6105 0.3331 0.4841 0.0414  -0.0375 0.0903  12  ARG A NH2 
206  N N   . TYR A 16  ? 0.4354 0.2119 0.3485 0.0235  -0.0041 0.0213  13  TYR A N   
207  C CA  . TYR A 16  ? 0.4282 0.2059 0.3397 0.0222  -0.0008 0.0107  13  TYR A CA  
208  C C   . TYR A 16  ? 0.4548 0.1949 0.3480 0.0290  -0.0020 0.0039  13  TYR A C   
209  O O   . TYR A 16  ? 0.5104 0.2190 0.3904 0.0295  -0.0069 0.0080  13  TYR A O   
210  C CB  . TYR A 16  ? 0.4248 0.2115 0.3377 0.0034  -0.0022 0.0116  13  TYR A CB  
211  C CG  . TYR A 16  ? 0.4273 0.1913 0.3296 -0.0119 -0.0080 0.0180  13  TYR A CG  
212  C CD1 . TYR A 16  ? 0.4543 0.2240 0.3604 -0.0191 -0.0093 0.0291  13  TYR A CD1 
213  C CD2 . TYR A 16  ? 0.4789 0.2157 0.3662 -0.0205 -0.0123 0.0131  13  TYR A CD2 
214  C CE1 . TYR A 16  ? 0.4728 0.2243 0.3705 -0.0350 -0.0138 0.0360  13  TYR A CE1 
215  C CE2 . TYR A 16  ? 0.5323 0.2489 0.4108 -0.0369 -0.0185 0.0197  13  TYR A CE2 
216  C CZ  . TYR A 16  ? 0.5036 0.2293 0.3887 -0.0444 -0.0188 0.0316  13  TYR A CZ  
217  O OH  . TYR A 16  ? 0.5376 0.2458 0.4151 -0.0625 -0.0242 0.0392  13  TYR A OH  
227  N N   . HIS A 17  ? 0.4754 0.2172 0.3657 0.0348  0.0028  -0.0069 14  HIS A N   
228  C CA  . HIS A 17  ? 0.5150 0.2205 0.3839 0.0396  0.0030  -0.0161 14  HIS A CA  
229  C C   . HIS A 17  ? 0.5214 0.2123 0.3764 0.0200  -0.0020 -0.0187 14  HIS A C   
230  O O   . HIS A 17  ? 0.4740 0.1914 0.3394 0.0086  -0.0021 -0.0175 14  HIS A O   
231  C CB  . HIS A 17  ? 0.5125 0.2285 0.3831 0.0555  0.0121  -0.0265 14  HIS A CB  
232  C CG  . HIS A 17  ? 0.4835 0.2237 0.3735 0.0735  0.0170  -0.0238 14  HIS A CG  
233  N ND1 . HIS A 17  ? 0.5384 0.2597 0.4261 0.0910  0.0168  -0.0231 14  HIS A ND1 
234  C CD2 . HIS A 17  ? 0.5246 0.3059 0.4368 0.0765  0.0212  -0.0212 14  HIS A CD2 
235  C CE1 . HIS A 17  ? 0.5174 0.2706 0.4273 0.1039  0.0202  -0.0197 14  HIS A CE1 
236  N NE2 . HIS A 17  ? 0.5103 0.2997 0.4346 0.0945  0.0229  -0.0188 14  HIS A NE2 
244  N N   . GLN A 18  ? 0.5290 0.1765 0.3602 0.0167  -0.0070 -0.0225 15  GLN A N   
245  C CA  . GLN A 18  ? 0.5899 0.2191 0.4052 -0.0028 -0.0138 -0.0254 15  GLN A CA  
246  C C   . GLN A 18  ? 0.6205 0.2141 0.4101 0.0034  -0.0137 -0.0370 15  GLN A C   
247  O O   . GLN A 18  ? 0.6470 0.2185 0.4290 0.0121  -0.0146 -0.0370 15  GLN A O   
248  C CB  . GLN A 18  ? 0.6344 0.2517 0.4490 -0.0213 -0.0229 -0.0143 15  GLN A CB  
249  C CG  . GLN A 18  ? 0.6365 0.2517 0.4454 -0.0439 -0.0308 -0.0145 15  GLN A CG  
250  C CD  . GLN A 18  ? 0.7045 0.3221 0.5206 -0.0620 -0.0377 -0.0022 15  GLN A CD  
251  O OE1 . GLN A 18  ? 0.7343 0.3689 0.5653 -0.0642 -0.0357 0.0082  15  GLN A OE1 
252  N NE2 . GLN A 18  ? 0.7022 0.3049 0.5074 -0.0759 -0.0453 -0.0031 15  GLN A NE2 
261  N N   . VAL A 19  ? 0.5925 0.1884 0.3718 -0.0018 -0.0128 -0.0459 16  VAL A N   
262  C CA  . VAL A 19  ? 0.7298 0.3013 0.4863 0.0018  -0.0123 -0.0563 16  VAL A CA  
263  C C   . VAL A 19  ? 0.6552 0.2254 0.4001 -0.0184 -0.0203 -0.0585 16  VAL A C   
264  O O   . VAL A 19  ? 0.7118 0.3060 0.4672 -0.0287 -0.0221 -0.0557 16  VAL A O   
265  C CB  . VAL A 19  ? 0.8161 0.3941 0.5698 0.0234  0.0005  -0.0668 16  VAL A CB  
266  C CG1 . VAL A 19  ? 0.8950 0.4836 0.6664 0.0441  0.0078  -0.0635 16  VAL A CG1 
267  C CG2 . VAL A 19  ? 0.7875 0.3908 0.5444 0.0193  0.0050  -0.0704 16  VAL A CG2 
277  N N   . GLY A 20  ? 0.6908 0.2329 0.4135 -0.0231 -0.0252 -0.0636 17  GLY A N   
278  C CA  . GLY A 20  ? 0.7416 0.2806 0.4496 -0.0389 -0.0324 -0.0672 17  GLY A CA  
279  C C   . GLY A 20  ? 0.7525 0.2913 0.4650 -0.0621 -0.0460 -0.0578 17  GLY A C   
280  O O   . GLY A 20  ? 0.7583 0.2946 0.4813 -0.0670 -0.0496 -0.0490 17  GLY A O   
284  N N   . GLN A 21  ? 0.7353 0.2785 0.4394 -0.0766 -0.0537 -0.0593 18  GLN A N   
285  C CA  . GLN A 21  ? 0.8040 0.3511 0.5133 -0.0990 -0.0670 -0.0508 18  GLN A CA  
286  C C   . GLN A 21  ? 0.7300 0.3035 0.4464 -0.1103 -0.0727 -0.0493 18  GLN A C   
287  O O   . GLN A 21  ? 0.7375 0.3138 0.4433 -0.1025 -0.0678 -0.0568 18  GLN A O   
288  C CB  . GLN A 21  ? 0.8440 0.3541 0.5268 -0.1062 -0.0747 -0.0543 18  GLN A CB  
289  C CG  . GLN A 21  ? 1.0832 0.5667 0.7344 -0.0974 -0.0716 -0.0675 18  GLN A CG  
290  C CD  . GLN A 21  ? 1.2666 0.7331 0.9089 -0.0728 -0.0579 -0.0763 18  GLN A CD  
291  O OE1 . GLN A 21  ? 1.2318 0.7164 0.8818 -0.0584 -0.0470 -0.0804 18  GLN A OE1 
292  N NE2 . GLN A 21  ? 1.1172 0.5503 0.7448 -0.0678 -0.0585 -0.0785 18  GLN A NE2 
301  N N   . GLY A 22  ? 0.7294 0.3249 0.4657 -0.1278 -0.0823 -0.0387 19  GLY A N   
302  C CA  . GLY A 22  ? 0.7228 0.3477 0.4717 -0.1378 -0.0887 -0.0350 19  GLY A CA  
303  C C   . GLY A 22  ? 0.6383 0.3017 0.4219 -0.1384 -0.0856 -0.0259 19  GLY A C   
304  O O   . GLY A 22  ? 0.6310 0.2987 0.4290 -0.1346 -0.0799 -0.0208 19  GLY A O   
308  N N   . PRO A 23  ? 0.6056 0.2968 0.4021 -0.1430 -0.0896 -0.0232 20  PRO A N   
309  C CA  . PRO A 23  ? 0.5606 0.2893 0.3904 -0.1433 -0.0868 -0.0147 20  PRO A CA  
310  C C   . PRO A 23  ? 0.5462 0.2730 0.3787 -0.1274 -0.0735 -0.0179 20  PRO A C   
311  O O   . PRO A 23  ? 0.5456 0.2516 0.3569 -0.1143 -0.0663 -0.0279 20  PRO A O   
312  C CB  . PRO A 23  ? 0.5514 0.3021 0.3866 -0.1470 -0.0933 -0.0141 20  PRO A CB  
313  C CG  . PRO A 23  ? 0.6613 0.3862 0.4652 -0.1504 -0.1001 -0.0213 20  PRO A CG  
314  C CD  . PRO A 23  ? 0.6345 0.3214 0.4127 -0.1460 -0.0960 -0.0285 20  PRO A CD  
322  N N   . VAL A 24  ? 0.4920 0.2432 0.3516 -0.1282 -0.0697 -0.0090 21  VAL A N   
323  C CA  . VAL A 24  ? 0.4846 0.2441 0.3519 -0.1097 -0.0560 -0.0098 21  VAL A CA  
324  C C   . VAL A 24  ? 0.4570 0.2402 0.3310 -0.0976 -0.0498 -0.0134 21  VAL A C   
325  O O   . VAL A 24  ? 0.4452 0.2545 0.3340 -0.1030 -0.0543 -0.0093 21  VAL A O   
326  C CB  . VAL A 24  ? 0.4464 0.2298 0.3402 -0.1118 -0.0522 0.0015  21  VAL A CB  
327  C CG1 . VAL A 24  ? 0.4572 0.2586 0.3627 -0.0932 -0.0396 0.0017  21  VAL A CG1 
328  C CG2 . VAL A 24  ? 0.5039 0.2579 0.3863 -0.1214 -0.0562 0.0050  21  VAL A CG2 
338  N N   . LEU A 25  ? 0.4077 0.1826 0.2719 -0.0809 -0.0394 -0.0202 22  LEU A N   
339  C CA  . LEU A 25  ? 0.3785 0.1747 0.2488 -0.0693 -0.0317 -0.0229 22  LEU A CA  
340  C C   . LEU A 25  ? 0.4021 0.2096 0.2856 -0.0547 -0.0208 -0.0212 22  LEU A C   
341  O O   . LEU A 25  ? 0.4405 0.2272 0.3121 -0.0453 -0.0158 -0.0257 22  LEU A O   
342  C CB  . LEU A 25  ? 0.4431 0.2181 0.2857 -0.0651 -0.0300 -0.0336 22  LEU A CB  
343  C CG  . LEU A 25  ? 0.4453 0.2368 0.2896 -0.0524 -0.0196 -0.0371 22  LEU A CG  
344  C CD1 . LEU A 25  ? 0.5087 0.3344 0.3762 -0.0549 -0.0211 -0.0296 22  LEU A CD1 
345  C CD2 . LEU A 25  ? 0.5001 0.2705 0.3142 -0.0515 -0.0181 -0.0470 22  LEU A CD2 
357  N N   . ILE A 26  ? 0.3349 0.1737 0.2423 -0.0527 -0.0179 -0.0144 23  ILE A N   
358  C CA  . ILE A 26  ? 0.3299 0.1815 0.2497 -0.0408 -0.0094 -0.0120 23  ILE A CA  
359  C C   . ILE A 26  ? 0.3073 0.1736 0.2294 -0.0306 -0.0025 -0.0160 23  ILE A C   
360  O O   . ILE A 26  ? 0.3174 0.2007 0.2462 -0.0339 -0.0039 -0.0147 23  ILE A O   
361  C CB  . ILE A 26  ? 0.3180 0.1922 0.2591 -0.0452 -0.0098 -0.0027 23  ILE A CB  
362  C CG1 . ILE A 26  ? 0.3437 0.2054 0.2834 -0.0573 -0.0158 0.0026  23  ILE A CG1 
363  C CG2 . ILE A 26  ? 0.3208 0.2061 0.2706 -0.0336 -0.0023 -0.0006 23  ILE A CG2 
364  C CD1 . ILE A 26  ? 0.3469 0.2319 0.3067 -0.0629 -0.0146 0.0120  23  ILE A CD1 
376  N N   . PHE A 27  ? 0.3168 0.1784 0.2356 -0.0182 0.0046  -0.0196 24  PHE A N   
377  C CA  . PHE A 27  ? 0.3087 0.1877 0.2331 -0.0090 0.0120  -0.0220 24  PHE A CA  
378  C C   . PHE A 27  ? 0.2786 0.1773 0.2212 -0.0032 0.0149  -0.0164 24  PHE A C   
379  O O   . PHE A 27  ? 0.3049 0.1962 0.2492 0.0017  0.0151  -0.0140 24  PHE A O   
380  C CB  . PHE A 27  ? 0.3435 0.2082 0.2541 0.0016  0.0187  -0.0299 24  PHE A CB  
381  C CG  . PHE A 27  ? 0.3542 0.2015 0.2426 -0.0028 0.0182  -0.0372 24  PHE A CG  
382  C CD1 . PHE A 27  ? 0.4021 0.2616 0.2879 -0.0084 0.0182  -0.0377 24  PHE A CD1 
383  C CD2 . PHE A 27  ? 0.4171 0.2335 0.2848 -0.0016 0.0171  -0.0434 24  PHE A CD2 
384  C CE1 . PHE A 27  ? 0.3983 0.2396 0.2595 -0.0132 0.0170  -0.0442 24  PHE A CE1 
385  C CE2 . PHE A 27  ? 0.4427 0.2399 0.2854 -0.0063 0.0162  -0.0510 24  PHE A CE2 
386  C CZ  . PHE A 27  ? 0.4404 0.2515 0.2800 -0.0123 0.0161  -0.0510 24  PHE A CZ  
396  N N   . ILE A 28  ? 0.2569 0.1775 0.2104 -0.0041 0.0163  -0.0143 25  ILE A N   
397  C CA  . ILE A 28  ? 0.2457 0.1842 0.2137 -0.0005 0.0180  -0.0097 25  ILE A CA  
398  C C   . ILE A 28  ? 0.2480 0.1994 0.2200 0.0066  0.0235  -0.0122 25  ILE A C   
399  O O   . ILE A 28  ? 0.2507 0.2092 0.2209 0.0037  0.0251  -0.0142 25  ILE A O   
400  C CB  . ILE A 28  ? 0.2125 0.1643 0.1892 -0.0073 0.0152  -0.0055 25  ILE A CB  
401  C CG1 . ILE A 28  ? 0.2425 0.1873 0.2185 -0.0156 0.0102  -0.0027 25  ILE A CG1 
402  C CG2 . ILE A 28  ? 0.2227 0.1880 0.2093 -0.0036 0.0168  -0.0017 25  ILE A CG2 
403  C CD1 . ILE A 28  ? 0.2506 0.2103 0.2370 -0.0202 0.0082  0.0008  25  ILE A CD1 
415  N N   . PRO A 29  ? 0.2407 0.1965 0.2187 0.0152  0.0258  -0.0113 26  PRO A N   
416  C CA  . PRO A 29  ? 0.2453 0.2173 0.2306 0.0213  0.0309  -0.0129 26  PRO A CA  
417  C C   . PRO A 29  ? 0.2359 0.2274 0.2313 0.0167  0.0295  -0.0094 26  PRO A C   
418  O O   . PRO A 29  ? 0.2351 0.2281 0.2330 0.0124  0.0253  -0.0057 26  PRO A O   
419  C CB  . PRO A 29  ? 0.2567 0.2268 0.2471 0.0324  0.0315  -0.0117 26  PRO A CB  
420  C CG  . PRO A 29  ? 0.2985 0.2590 0.2875 0.0294  0.0256  -0.0065 26  PRO A CG  
421  C CD  . PRO A 29  ? 0.2794 0.2261 0.2583 0.0192  0.0232  -0.0075 26  PRO A CD  
429  N N   . GLY A 30  ? 0.2576 0.2632 0.2574 0.0174  0.0339  -0.0110 27  GLY A N   
430  C CA  . GLY A 30  ? 0.2469 0.2700 0.2558 0.0129  0.0325  -0.0080 27  GLY A CA  
431  C C   . GLY A 30  ? 0.2765 0.3136 0.2979 0.0182  0.0306  -0.0047 27  GLY A C   
432  O O   . GLY A 30  ? 0.2567 0.2874 0.2787 0.0231  0.0272  -0.0025 27  GLY A O   
436  N N   . ALA A 31  ? 0.2617 0.3181 0.2930 0.0160  0.0318  -0.0035 28  ALA A N   
437  C CA  . ALA A 31  ? 0.2792 0.3509 0.3226 0.0178  0.0270  0.0006  28  ALA A CA  
438  C C   . ALA A 31  ? 0.2718 0.3475 0.3239 0.0304  0.0273  0.0018  28  ALA A C   
439  O O   . ALA A 31  ? 0.3149 0.3967 0.3732 0.0330  0.0208  0.0062  28  ALA A O   
440  C CB  . ALA A 31  ? 0.3452 0.4382 0.3985 0.0109  0.0277  0.0021  28  ALA A CB  
446  N N   . ASN A 32  ? 0.2739 0.3456 0.3256 0.0389  0.0344  -0.0019 29  ASN A N   
447  C CA  . ASN A 32  ? 0.2733 0.3442 0.3320 0.0530  0.0344  -0.0009 29  ASN A CA  
448  C C   . ASN A 32  ? 0.3051 0.3526 0.3528 0.0548  0.0278  0.0016  29  ASN A C   
449  O O   . ASN A 32  ? 0.2994 0.3451 0.3521 0.0646  0.0239  0.0051  29  ASN A O   
450  C CB  . ASN A 32  ? 0.2907 0.3568 0.3469 0.0625  0.0444  -0.0070 29  ASN A CB  
451  C CG  . ASN A 32  ? 0.3344 0.3711 0.3686 0.0587  0.0464  -0.0122 29  ASN A CG  
452  O OD1 . ASN A 32  ? 0.3338 0.3673 0.3588 0.0474  0.0470  -0.0137 29  ASN A OD1 
453  N ND2 . ASN A 32  ? 0.3692 0.3827 0.3942 0.0676  0.0460  -0.0143 29  ASN A ND2 
460  N N   . GLY A 33  ? 0.2559 0.2858 0.2891 0.0458  0.0267  0.0003  30  GLY A N   
461  C CA  . GLY A 33  ? 0.2750 0.2874 0.2988 0.0436  0.0211  0.0038  30  GLY A CA  
462  C C   . GLY A 33  ? 0.3026 0.2904 0.3164 0.0496  0.0216  0.0028  30  GLY A C   
463  O O   . GLY A 33  ? 0.2869 0.2591 0.2918 0.0451  0.0176  0.0062  30  GLY A O   
467  N N   . THR A 34  ? 0.2925 0.2748 0.3060 0.0589  0.0268  -0.0022 31  THR A N   
468  C CA  . THR A 34  ? 0.3248 0.2803 0.3277 0.0669  0.0263  -0.0034 31  THR A CA  
469  C C   . THR A 34  ? 0.3359 0.2724 0.3243 0.0653  0.0315  -0.0114 31  THR A C   
470  O O   . THR A 34  ? 0.3344 0.2820 0.3236 0.0643  0.0379  -0.0167 31  THR A O   
471  C CB  . THR A 34  ? 0.3376 0.2986 0.3514 0.0836  0.0266  -0.0018 31  THR A CB  
472  O OG1 . THR A 34  ? 0.3321 0.3153 0.3584 0.0909  0.0346  -0.0065 31  THR A OG1 
473  C CG2 . THR A 34  ? 0.3801 0.3559 0.4046 0.0838  0.0186  0.0072  31  THR A CG2 
481  N N   . GLY A 35  ? 0.3533 0.2596 0.3263 0.0637  0.0282  -0.0118 32  GLY A N   
482  C CA  . GLY A 35  ? 0.3321 0.2165 0.2875 0.0594  0.0306  -0.0192 32  GLY A CA  
483  C C   . GLY A 35  ? 0.3754 0.2472 0.3230 0.0732  0.0377  -0.0275 32  GLY A C   
484  O O   . GLY A 35  ? 0.3963 0.2525 0.3272 0.0694  0.0408  -0.0350 32  GLY A O   
488  N N   . ASP A 36  ? 0.3565 0.2351 0.3154 0.0898  0.0404  -0.0265 33  ASP A N   
489  C CA  . ASP A 36  ? 0.4097 0.2765 0.3621 0.1058  0.0487  -0.0349 33  ASP A CA  
490  C C   . ASP A 36  ? 0.4040 0.2869 0.3545 0.1045  0.0592  -0.0425 33  ASP A C   
491  O O   . ASP A 36  ? 0.4360 0.3006 0.3704 0.1125  0.0669  -0.0519 33  ASP A O   
492  C CB  . ASP A 36  ? 0.4211 0.3013 0.3924 0.1251  0.0500  -0.0313 33  ASP A CB  
493  C CG  . ASP A 36  ? 0.5239 0.4460 0.5220 0.1231  0.0478  -0.0232 33  ASP A CG  
494  O OD1 . ASP A 36  ? 0.4706 0.4129 0.4733 0.1085  0.0476  -0.0216 33  ASP A OD1 
495  O OD2 . ASP A 36  ? 0.6414 0.5749 0.6557 0.1372  0.0457  -0.0184 33  ASP A OD2 
500  N N   . ILE A 37  ? 0.3811 0.2955 0.3452 0.0942  0.0598  -0.0387 34  ILE A N   
501  C CA  . ILE A 37  ? 0.3645 0.2952 0.3265 0.0908  0.0691  -0.0439 34  ILE A CA  
502  C C   . ILE A 37  ? 0.3828 0.2865 0.3167 0.0807  0.0693  -0.0507 34  ILE A C   
503  O O   . ILE A 37  ? 0.4138 0.3207 0.3373 0.0806  0.0782  -0.0570 34  ILE A O   
504  C CB  . ILE A 37  ? 0.3005 0.2652 0.2812 0.0798  0.0669  -0.0368 34  ILE A CB  
505  C CG1 . ILE A 37  ? 0.3651 0.3539 0.3506 0.0801  0.0781  -0.0399 34  ILE A CG1 
506  C CG2 . ILE A 37  ? 0.3268 0.2826 0.2990 0.0629  0.0579  -0.0334 34  ILE A CG2 
507  C CD1 . ILE A 37  ? 0.3682 0.3904 0.3741 0.0711  0.0761  -0.0326 34  ILE A CD1 
519  N N   . PHE A 38  ? 0.3719 0.2490 0.2924 0.0718  0.0594  -0.0494 35  PHE A N   
520  C CA  . PHE A 38  ? 0.4001 0.2513 0.2946 0.0608  0.0566  -0.0550 35  PHE A CA  
521  C C   . PHE A 38  ? 0.4421 0.2542 0.3124 0.0685  0.0577  -0.0635 35  PHE A C   
522  O O   . PHE A 38  ? 0.4665 0.2536 0.3121 0.0587  0.0541  -0.0688 35  PHE A O   
523  C CB  . PHE A 38  ? 0.3641 0.2129 0.2607 0.0444  0.0445  -0.0479 35  PHE A CB  
524  C CG  . PHE A 38  ? 0.3469 0.2269 0.2608 0.0359  0.0431  -0.0414 35  PHE A CG  
525  C CD1 . PHE A 38  ? 0.3681 0.2575 0.2758 0.0286  0.0456  -0.0435 35  PHE A CD1 
526  C CD2 . PHE A 38  ? 0.3587 0.2557 0.2922 0.0352  0.0390  -0.0334 35  PHE A CD2 
527  C CE1 . PHE A 38  ? 0.3782 0.2915 0.2998 0.0213  0.0436  -0.0376 35  PHE A CE1 
528  C CE2 . PHE A 38  ? 0.3722 0.2933 0.3185 0.0279  0.0376  -0.0285 35  PHE A CE2 
529  C CZ  . PHE A 38  ? 0.3480 0.2766 0.2890 0.0214  0.0398  -0.0306 35  PHE A CZ  
539  N N   . LEU A 39  ? 0.4481 0.2519 0.3231 0.0860  0.0616  -0.0650 36  LEU A N   
540  C CA  . LEU A 39  ? 0.4701 0.2295 0.3195 0.0924  0.0605  -0.0726 36  LEU A CA  
541  C C   . LEU A 39  ? 0.5482 0.2899 0.3711 0.0972  0.0704  -0.0857 36  LEU A C   
542  O O   . LEU A 39  ? 0.5805 0.2885 0.3774 0.0890  0.0643  -0.0910 36  LEU A O   
543  C CB  . LEU A 39  ? 0.5094 0.2616 0.3700 0.1116  0.0613  -0.0703 36  LEU A CB  
544  C CG  . LEU A 39  ? 0.5400 0.2974 0.4161 0.1039  0.0494  -0.0577 36  LEU A CG  
545  C CD1 . LEU A 39  ? 0.5241 0.2730 0.4097 0.1220  0.0481  -0.0536 36  LEU A CD1 
546  C CD2 . LEU A 39  ? 0.5721 0.2997 0.4295 0.0850  0.0381  -0.0554 36  LEU A CD2 
558  N N   . PRO A 40  ? 0.5539 0.3237 0.3860 0.1068  0.0837  -0.0893 37  PRO A N   
559  C CA  . PRO A 40  ? 0.5971 0.3586 0.4074 0.1054  0.0906  -0.0990 37  PRO A CA  
560  C C   . PRO A 40  ? 0.5195 0.2661 0.3046 0.0850  0.0838  -0.1006 37  PRO A C   
561  O O   . PRO A 40  ? 0.5893 0.3104 0.3481 0.0797  0.0813  -0.1075 37  PRO A O   
562  C CB  . PRO A 40  ? 0.6009 0.4039 0.4322 0.1158  0.1053  -0.0992 37  PRO A CB  
563  C CG  . PRO A 40  ? 0.5348 0.3610 0.3999 0.1291  0.1052  -0.0914 37  PRO A CG  
564  C CD  . PRO A 40  ? 0.5228 0.3356 0.3883 0.1183  0.0916  -0.0835 37  PRO A CD  
572  N N   . LEU A 41  ? 0.5034 0.2688 0.2999 0.0721  0.0782  -0.0928 38  LEU A N   
573  C CA  . LEU A 41  ? 0.4909 0.2469 0.2695 0.0518  0.0684  -0.0919 38  LEU A CA  
574  C C   . LEU A 41  ? 0.5266 0.2461 0.2887 0.0418  0.0542  -0.0924 38  LEU A C   
575  O O   . LEU A 41  ? 0.5515 0.2465 0.2860 0.0305  0.0479  -0.0974 38  LEU A O   
576  C CB  . LEU A 41  ? 0.4643 0.2572 0.2690 0.0406  0.0636  -0.0806 38  LEU A CB  
577  C CG  . LEU A 41  ? 0.4628 0.2518 0.2572 0.0209  0.0514  -0.0769 38  LEU A CG  
578  C CD1 . LEU A 41  ? 0.5108 0.2845 0.2732 0.0168  0.0554  -0.0851 38  LEU A CD1 
579  C CD2 . LEU A 41  ? 0.4633 0.2871 0.2838 0.0139  0.0483  -0.0666 38  LEU A CD2 
591  N N   . ALA A 42  ? 0.5430 0.2598 0.3222 0.0447  0.0482  -0.0860 39  ALA A N   
592  C CA  . ALA A 42  ? 0.5701 0.2538 0.3353 0.0332  0.0348  -0.0848 39  ALA A CA  
593  C C   . ALA A 42  ? 0.5956 0.2445 0.3329 0.0360  0.0345  -0.0940 39  ALA A C   
594  O O   . ALA A 42  ? 0.6188 0.2460 0.3396 0.0206  0.0229  -0.0939 39  ALA A O   
595  C CB  . ALA A 42  ? 0.5545 0.2417 0.3417 0.0371  0.0303  -0.0757 39  ALA A CB  
601  N N   . GLU A 43  ? 0.6073 0.2575 0.3440 0.0546  0.0467  -0.1005 40  GLU A N   
602  C CA  . GLU A 43  ? 0.7273 0.3495 0.4403 0.0588  0.0479  -0.1093 40  GLU A CA  
603  C C   . GLU A 43  ? 0.6829 0.2965 0.3698 0.0451  0.0452  -0.1146 40  GLU A C   
604  O O   . GLU A 43  ? 0.7202 0.3032 0.3830 0.0380  0.0381  -0.1189 40  GLU A O   
605  C CB  . GLU A 43  ? 0.7473 0.3813 0.4691 0.0818  0.0633  -0.1151 40  GLU A CB  
606  C CG  . GLU A 43  ? 0.8707 0.4967 0.6073 0.0973  0.0634  -0.1126 40  GLU A CG  
607  C CD  . GLU A 43  ? 0.9547 0.5402 0.6743 0.0897  0.0506  -0.1116 40  GLU A CD  
608  O OE1 . GLU A 43  ? 0.8995 0.4565 0.5943 0.0902  0.0505  -0.1199 40  GLU A OE1 
609  O OE2 . GLU A 43  ? 0.8327 0.4152 0.5635 0.0830  0.0410  -0.1022 40  GLU A OE2 
616  N N   . GLN A 44  ? 0.6260 0.2659 0.3165 0.0412  0.0505  -0.1138 41  GLN A N   
617  C CA  . GLN A 44  ? 0.7424 0.3766 0.4088 0.0278  0.0470  -0.1170 41  GLN A CA  
618  C C   . GLN A 44  ? 0.7013 0.3246 0.3615 0.0060  0.0287  -0.1108 41  GLN A C   
619  O O   . GLN A 44  ? 0.7491 0.3596 0.3868 -0.0060 0.0216  -0.1130 41  GLN A O   
620  C CB  . GLN A 44  ? 0.6649 0.3319 0.3388 0.0294  0.0575  -0.1159 41  GLN A CB  
621  C CG  . GLN A 44  ? 0.7014 0.3876 0.3863 0.0493  0.0761  -0.1207 41  GLN A CG  
622  C CD  . GLN A 44  ? 0.7999 0.4677 0.4602 0.0563  0.0834  -0.1312 41  GLN A CD  
623  O OE1 . GLN A 44  ? 0.9053 0.5572 0.5381 0.0447  0.0786  -0.1344 41  GLN A OE1 
624  N NE2 . GLN A 44  ? 0.8160 0.4853 0.4858 0.0753  0.0944  -0.1364 41  GLN A NE2 
633  N N   . LEU A 45  ? 0.6636 0.2934 0.3445 0.0006  0.0208  -0.1027 42  LEU A N   
634  C CA  . LEU A 45  ? 0.6324 0.2614 0.3151 -0.0201 0.0043  -0.0953 42  LEU A CA  
635  C C   . LEU A 45  ? 0.7359 0.3418 0.4175 -0.0276 -0.0070 -0.0921 42  LEU A C   
636  O O   . LEU A 45  ? 0.6436 0.2502 0.3274 -0.0458 -0.0211 -0.0857 42  LEU A O   
637  C CB  . LEU A 45  ? 0.5823 0.2403 0.2909 -0.0238 0.0033  -0.0873 42  LEU A CB  
638  C CG  . LEU A 45  ? 0.5818 0.2651 0.2926 -0.0202 0.0124  -0.0882 42  LEU A CG  
639  C CD1 . LEU A 45  ? 0.5412 0.2657 0.2922 -0.0208 0.0115  -0.0757 42  LEU A CD1 
640  C CD2 . LEU A 45  ? 0.6267 0.3072 0.3179 -0.0338 0.0044  -0.0886 42  LEU A CD2 
652  N N   . LYS A 46  ? 0.6743 0.2621 0.3543 -0.0143 -0.0014 -0.0954 43  LYS A N   
653  C CA  . LYS A 46  ? 0.7237 0.2923 0.4065 -0.0207 -0.0110 -0.0903 43  LYS A CA  
654  C C   . LYS A 46  ? 0.7826 0.3261 0.4428 -0.0368 -0.0234 -0.0915 43  LYS A C   
655  O O   . LYS A 46  ? 0.7905 0.3227 0.4541 -0.0478 -0.0336 -0.0852 43  LYS A O   
656  C CB  . LYS A 46  ? 0.7367 0.2908 0.4215 -0.0012 -0.0024 -0.0933 43  LYS A CB  
657  C CG  . LYS A 46  ? 0.7725 0.3045 0.4342 0.0121  0.0057  -0.1048 43  LYS A CG  
658  C CD  . LYS A 46  ? 0.8834 0.4015 0.5504 0.0312  0.0121  -0.1064 43  LYS A CD  
659  C CE  . LYS A 46  ? 0.8804 0.3755 0.5246 0.0447  0.0202  -0.1185 43  LYS A CE  
660  N NZ  . LYS A 46  ? 1.0149 0.5066 0.6695 0.0682  0.0297  -0.1210 43  LYS A NZ  
674  N N   . ASP A 47  ? 0.7783 0.3139 0.4153 -0.0391 -0.0228 -0.0987 44  ASP A N   
675  C CA  . ASP A 47  ? 0.8829 0.3961 0.4977 -0.0554 -0.0357 -0.0994 44  ASP A CA  
676  C C   . ASP A 47  ? 0.8449 0.3791 0.4724 -0.0764 -0.0498 -0.0897 44  ASP A C   
677  O O   . ASP A 47  ? 0.8574 0.3784 0.4752 -0.0924 -0.0631 -0.0866 44  ASP A O   
678  C CB  . ASP A 47  ? 0.9089 0.4058 0.4931 -0.0495 -0.0295 -0.1105 44  ASP A CB  
679  C CG  . ASP A 47  ? 1.1347 0.5958 0.6969 -0.0380 -0.0242 -0.1197 44  ASP A CG  
680  O OD1 . ASP A 47  ? 1.2032 0.6462 0.7682 -0.0400 -0.0301 -0.1166 44  ASP A OD1 
681  O OD2 . ASP A 47  ? 1.4318 0.8835 0.9743 -0.0264 -0.0136 -0.1299 44  ASP A OD2 
686  N N   . HIS A 48  ? 0.7173 0.2844 0.3673 -0.0764 -0.0474 -0.0844 45  HIS A N   
687  C CA  . HIS A 48  ? 0.7356 0.3265 0.3999 -0.0937 -0.0599 -0.0753 45  HIS A CA  
688  C C   . HIS A 48  ? 0.7022 0.3185 0.4007 -0.0986 -0.0630 -0.0647 45  HIS A C   
689  O O   . HIS A 48  ? 0.7233 0.3560 0.4366 -0.1143 -0.0751 -0.0559 45  HIS A O   
690  C CB  . HIS A 48  ? 0.6934 0.3024 0.3535 -0.0916 -0.0562 -0.0773 45  HIS A CB  
691  C CG  . HIS A 48  ? 0.8103 0.3979 0.4364 -0.0899 -0.0541 -0.0860 45  HIS A CG  
692  N ND1 . HIS A 48  ? 0.8535 0.4275 0.4626 -0.0730 -0.0387 -0.0964 45  HIS A ND1 
693  C CD2 . HIS A 48  ? 0.9814 0.5601 0.5882 -0.1027 -0.0653 -0.0857 45  HIS A CD2 
694  C CE1 . HIS A 48  ? 0.9207 0.4775 0.5001 -0.0759 -0.0397 -0.1024 45  HIS A CE1 
695  N NE2 . HIS A 48  ? 0.9852 0.5427 0.5612 -0.0941 -0.0562 -0.0961 45  HIS A NE2 
703  N N   . PHE A 49  ? 0.6486 0.2698 0.3608 -0.0852 -0.0521 -0.0649 46  PHE A N   
704  C CA  . PHE A 49  ? 0.6182 0.2628 0.3611 -0.0886 -0.0532 -0.0551 46  PHE A CA  
705  C C   . PHE A 49  ? 0.5945 0.2237 0.3416 -0.0799 -0.0479 -0.0539 46  PHE A C   
706  O O   . PHE A 49  ? 0.6344 0.2420 0.3660 -0.0649 -0.0395 -0.0617 46  PHE A O   
707  C CB  . PHE A 49  ? 0.5725 0.2435 0.3308 -0.0806 -0.0451 -0.0547 46  PHE A CB  
708  C CG  . PHE A 49  ? 0.5799 0.2686 0.3368 -0.0882 -0.0504 -0.0541 46  PHE A CG  
709  C CD1 . PHE A 49  ? 0.5569 0.2719 0.3365 -0.1018 -0.0610 -0.0442 46  PHE A CD1 
710  C CD2 . PHE A 49  ? 0.6055 0.2866 0.3394 -0.0810 -0.0443 -0.0627 46  PHE A CD2 
711  C CE1 . PHE A 49  ? 0.5653 0.2970 0.3448 -0.1071 -0.0669 -0.0425 46  PHE A CE1 
712  C CE2 . PHE A 49  ? 0.6443 0.3407 0.3752 -0.0880 -0.0496 -0.0608 46  PHE A CE2 
713  C CZ  . PHE A 49  ? 0.6600 0.3802 0.4131 -0.1009 -0.0620 -0.0506 46  PHE A CZ  
723  N N   . THR A 50  ? 0.6002 0.2430 0.3697 -0.0887 -0.0524 -0.0432 47  THR A N   
724  C CA  . THR A 50  ? 0.6178 0.2551 0.3968 -0.0791 -0.0460 -0.0394 47  THR A CA  
725  C C   . THR A 50  ? 0.5465 0.2098 0.3431 -0.0663 -0.0359 -0.0386 47  THR A C   
726  O O   . THR A 50  ? 0.5179 0.2181 0.3405 -0.0718 -0.0367 -0.0301 47  THR A O   
727  C CB  . THR A 50  ? 0.6208 0.2663 0.4164 -0.0942 -0.0535 -0.0273 47  THR A CB  
728  O OG1 . THR A 50  ? 0.6662 0.2895 0.4458 -0.1052 -0.0623 -0.0279 47  THR A OG1 
729  C CG2 . THR A 50  ? 0.6320 0.2722 0.4358 -0.0847 -0.0473 -0.0218 47  THR A CG2 
737  N N   . VAL A 51  ? 0.5402 0.1973 0.3295 -0.0466 -0.0250 -0.0461 48  VAL A N   
738  C CA  . VAL A 51  ? 0.4964 0.1903 0.3075 -0.0328 -0.0145 -0.0444 48  VAL A CA  
739  C C   . VAL A 51  ? 0.4591 0.1638 0.2897 -0.0246 -0.0111 -0.0362 48  VAL A C   
740  O O   . VAL A 51  ? 0.5162 0.1935 0.3366 -0.0174 -0.0108 -0.0370 48  VAL A O   
741  C CB  . VAL A 51  ? 0.5376 0.2245 0.3338 -0.0167 -0.0040 -0.0556 48  VAL A CB  
742  C CG1 . VAL A 51  ? 0.5072 0.2347 0.3275 -0.0063 0.0054  -0.0525 48  VAL A CG1 
743  C CG2 . VAL A 51  ? 0.5715 0.2413 0.3413 -0.0256 -0.0078 -0.0641 48  VAL A CG2 
753  N N   . VAL A 52  ? 0.4360 0.1781 0.2923 -0.0262 -0.0093 -0.0283 49  VAL A N   
754  C CA  . VAL A 52  ? 0.4251 0.1824 0.2998 -0.0211 -0.0069 -0.0195 49  VAL A CA  
755  C C   . VAL A 52  ? 0.4220 0.2104 0.3127 -0.0085 0.0014  -0.0202 49  VAL A C   
756  O O   . VAL A 52  ? 0.4149 0.2276 0.3154 -0.0132 0.0021  -0.0197 49  VAL A O   
757  C CB  . VAL A 52  ? 0.4228 0.1951 0.3112 -0.0371 -0.0128 -0.0094 49  VAL A CB  
758  C CG1 . VAL A 52  ? 0.4514 0.2421 0.3563 -0.0318 -0.0091 -0.0008 49  VAL A CG1 
759  C CG2 . VAL A 52  ? 0.4767 0.2190 0.3500 -0.0516 -0.0216 -0.0080 49  VAL A CG2 
769  N N   . ALA A 53  ? 0.4176 0.2045 0.3110 0.0071  0.0068  -0.0210 50  ALA A N   
770  C CA  . ALA A 53  ? 0.3792 0.1955 0.2884 0.0182  0.0139  -0.0213 50  ALA A CA  
771  C C   . ALA A 53  ? 0.3642 0.1932 0.2879 0.0224  0.0129  -0.0125 50  ALA A C   
772  O O   . ALA A 53  ? 0.4013 0.2126 0.3205 0.0304  0.0116  -0.0104 50  ALA A O   
773  C CB  . ALA A 53  ? 0.4466 0.2553 0.3483 0.0335  0.0213  -0.0299 50  ALA A CB  
779  N N   A VAL A 54  ? 0.3467 0.2038 0.2855 0.0173  0.0131  -0.0075 51  VAL A N   
780  N N   B VAL A 54  ? 0.3465 0.2039 0.2855 0.0173  0.0132  -0.0076 51  VAL A N   
781  C CA  A VAL A 54  ? 0.3553 0.2228 0.3036 0.0170  0.0111  0.0012  51  VAL A CA  
782  C CA  B VAL A 54  ? 0.3548 0.2231 0.3034 0.0171  0.0112  0.0011  51  VAL A CA  
783  C C   A VAL A 54  ? 0.3405 0.2278 0.3005 0.0290  0.0142  0.0018  51  VAL A C   
784  C C   B VAL A 54  ? 0.3404 0.2277 0.3005 0.0293  0.0142  0.0018  51  VAL A C   
785  O O   A VAL A 54  ? 0.3405 0.2458 0.3077 0.0322  0.0183  -0.0025 51  VAL A O   
786  O O   B VAL A 54  ? 0.3405 0.2457 0.3077 0.0328  0.0184  -0.0026 51  VAL A O   
787  C CB  A VAL A 54  ? 0.3494 0.2338 0.3053 0.0042  0.0097  0.0058  51  VAL A CB  
788  C CB  B VAL A 54  ? 0.3487 0.2349 0.3053 0.0045  0.0100  0.0054  51  VAL A CB  
789  C CG1 A VAL A 54  ? 0.2903 0.2000 0.2565 0.0052  0.0130  0.0029  51  VAL A CG1 
790  C CG1 B VAL A 54  ? 0.3881 0.2849 0.3510 0.0042  0.0094  0.0134  51  VAL A CG1 
791  C CG2 A VAL A 54  ? 0.4243 0.3124 0.3834 0.0019  0.0082  0.0146  51  VAL A CG2 
792  C CG2 B VAL A 54  ? 0.3320 0.2043 0.2814 -0.0083 0.0060  0.0059  51  VAL A CG2 
811  N N   . ASP A 55  ? 0.3391 0.2231 0.3008 0.0345  0.0113  0.0082  52  ASP A N   
812  C CA  . ASP A 55  ? 0.3389 0.2452 0.3129 0.0417  0.0111  0.0118  52  ASP A CA  
813  C C   . ASP A 55  ? 0.2918 0.2123 0.2685 0.0309  0.0096  0.0169  52  ASP A C   
814  O O   . ASP A 55  ? 0.3190 0.2290 0.2888 0.0249  0.0069  0.0231  52  ASP A O   
815  C CB  . ASP A 55  ? 0.3438 0.2380 0.3161 0.0526  0.0069  0.0171  52  ASP A CB  
816  C CG  . ASP A 55  ? 0.3761 0.2629 0.3504 0.0685  0.0096  0.0117  52  ASP A CG  
817  O OD1 . ASP A 55  ? 0.3893 0.2765 0.3625 0.0697  0.0156  0.0033  52  ASP A OD1 
818  O OD2 . ASP A 55  ? 0.3955 0.2767 0.3724 0.0804  0.0059  0.0162  52  ASP A OD2 
824  N N   . ARG A 56  ? 0.2621 0.2047 0.2472 0.0277  0.0119  0.0144  53  ARG A N   
825  C CA  . ARG A 56  ? 0.2478 0.2010 0.2334 0.0196  0.0112  0.0182  53  ARG A CA  
826  C C   . ARG A 56  ? 0.2572 0.2106 0.2399 0.0225  0.0073  0.0252  53  ARG A C   
827  O O   . ARG A 56  ? 0.2920 0.2456 0.2775 0.0317  0.0042  0.0269  53  ARG A O   
828  C CB  . ARG A 56  ? 0.2369 0.2089 0.2298 0.0171  0.0135  0.0141  53  ARG A CB  
829  C CG  . ARG A 56  ? 0.2600 0.2295 0.2523 0.0120  0.0160  0.0092  53  ARG A CG  
830  C CD  . ARG A 56  ? 0.2193 0.2027 0.2161 0.0078  0.0173  0.0068  53  ARG A CD  
831  N NE  . ARG A 56  ? 0.2412 0.2353 0.2430 0.0117  0.0185  0.0039  53  ARG A NE  
832  C CZ  . ARG A 56  ? 0.2485 0.2557 0.2548 0.0116  0.0174  0.0048  53  ARG A CZ  
833  N NH1 . ARG A 56  ? 0.2419 0.2511 0.2457 0.0089  0.0151  0.0075  53  ARG A NH1 
834  N NH2 . ARG A 56  ? 0.2583 0.2765 0.2706 0.0133  0.0187  0.0028  53  ARG A NH2 
848  N N   . ARG A 57  ? 0.2559 0.2101 0.2326 0.0150  0.0076  0.0297  54  ARG A N   
849  C CA  . ARG A 57  ? 0.2826 0.2290 0.2502 0.0157  0.0038  0.0376  54  ARG A CA  
850  C C   . ARG A 57  ? 0.2864 0.2433 0.2561 0.0226  -0.0013 0.0396  54  ARG A C   
851  O O   . ARG A 57  ? 0.3098 0.2580 0.2727 0.0264  -0.0067 0.0464  54  ARG A O   
852  C CB  . ARG A 57  ? 0.2832 0.2306 0.2428 0.0060  0.0072  0.0417  54  ARG A CB  
853  C CG  . ARG A 57  ? 0.2787 0.2438 0.2409 0.0032  0.0107  0.0377  54  ARG A CG  
854  C CD  . ARG A 57  ? 0.2811 0.2468 0.2324 -0.0033 0.0146  0.0425  54  ARG A CD  
855  N NE  . ARG A 57  ? 0.2812 0.2416 0.2328 -0.0106 0.0191  0.0460  54  ARG A NE  
856  C CZ  . ARG A 57  ? 0.2892 0.2484 0.2317 -0.0170 0.0234  0.0524  54  ARG A CZ  
857  N NH1 . ARG A 57  ? 0.3074 0.2677 0.2362 -0.0165 0.0240  0.0555  54  ARG A NH1 
858  N NH2 . ARG A 57  ? 0.3024 0.2585 0.2483 -0.0251 0.0267  0.0564  54  ARG A NH2 
872  N N   . ASP A 58  ? 0.2475 0.2223 0.2262 0.0236  -0.0010 0.0346  55  ASP A N   
873  C CA  . ASP A 58  ? 0.2749 0.2625 0.2578 0.0282  -0.0072 0.0366  55  ASP A CA  
874  C C   . ASP A 58  ? 0.3170 0.3106 0.3138 0.0391  -0.0096 0.0359  55  ASP A C   
875  O O   . ASP A 58  ? 0.3140 0.3220 0.3184 0.0433  -0.0157 0.0385  55  ASP A O   
876  C CB  . ASP A 58  ? 0.2623 0.2655 0.2474 0.0222  -0.0065 0.0321  55  ASP A CB  
877  C CG  . ASP A 58  ? 0.2910 0.2893 0.2609 0.0147  -0.0048 0.0332  55  ASP A CG  
878  O OD1 . ASP A 58  ? 0.3446 0.3405 0.3031 0.0141  -0.0101 0.0383  55  ASP A OD1 
879  O OD2 . ASP A 58  ? 0.3016 0.2984 0.2702 0.0100  0.0017  0.0293  55  ASP A OD2 
884  N N   . TYR A 59  ? 0.2780 0.2607 0.2776 0.0441  -0.0054 0.0328  56  TYR A N   
885  C CA  . TYR A 59  ? 0.2608 0.2510 0.2738 0.0555  -0.0045 0.0300  56  TYR A CA  
886  C C   . TYR A 59  ? 0.2977 0.2652 0.3058 0.0654  -0.0046 0.0312  56  TYR A C   
887  O O   . TYR A 59  ? 0.3336 0.2774 0.3276 0.0605  -0.0042 0.0324  56  TYR A O   
888  C CB  . TYR A 59  ? 0.2800 0.2797 0.2995 0.0526  0.0031  0.0218  56  TYR A CB  
889  C CG  . TYR A 59  ? 0.2554 0.2732 0.2788 0.0430  0.0038  0.0197  56  TYR A CG  
890  C CD1 . TYR A 59  ? 0.2457 0.2572 0.2595 0.0326  0.0058  0.0180  56  TYR A CD1 
891  C CD2 . TYR A 59  ? 0.2622 0.3035 0.2996 0.0444  0.0025  0.0195  56  TYR A CD2 
892  C CE1 . TYR A 59  ? 0.2575 0.2813 0.2731 0.0251  0.0062  0.0156  56  TYR A CE1 
893  C CE2 . TYR A 59  ? 0.2666 0.3201 0.3051 0.0345  0.0024  0.0176  56  TYR A CE2 
894  C CZ  . TYR A 59  ? 0.2557 0.2981 0.2820 0.0256  0.0041  0.0154  56  TYR A CZ  
895  O OH  . TYR A 59  ? 0.3002 0.3507 0.3260 0.0171  0.0037  0.0133  56  TYR A OH  
905  N N   . GLY A 60  ? 0.3168 0.2921 0.3376 0.0794  -0.0049 0.0304  57  GLY A N   
906  C CA  . GLY A 60  ? 0.3520 0.3036 0.3678 0.0911  -0.0034 0.0289  57  GLY A CA  
907  C C   . GLY A 60  ? 0.3355 0.2606 0.3375 0.0931  -0.0109 0.0372  57  GLY A C   
908  O O   . GLY A 60  ? 0.3930 0.3244 0.3969 0.0957  -0.0191 0.0456  57  GLY A O   
912  N N   . GLU A 61  ? 0.3712 0.2645 0.3571 0.0908  -0.0090 0.0353  58  GLU A N   
913  C CA  . GLU A 61  ? 0.3960 0.2585 0.3658 0.0907  -0.0156 0.0434  58  GLU A CA  
914  C C   . GLU A 61  ? 0.4149 0.2714 0.3713 0.0722  -0.0170 0.0490  58  GLU A C   
915  O O   . GLU A 61  ? 0.4510 0.2838 0.3928 0.0691  -0.0221 0.0574  58  GLU A O   
916  C CB  . GLU A 61  ? 0.5092 0.3375 0.4675 0.0974  -0.0134 0.0383  58  GLU A CB  
917  C CG  . GLU A 61  ? 0.5862 0.4178 0.5563 0.1189  -0.0104 0.0325  58  GLU A CG  
918  C CD  . GLU A 61  ? 0.7499 0.5896 0.7309 0.1342  -0.0183 0.0412  58  GLU A CD  
919  O OE1 . GLU A 61  ? 0.7745 0.5861 0.7417 0.1362  -0.0264 0.0498  58  GLU A OE1 
920  O OE2 . GLU A 61  ? 0.8738 0.7480 0.8770 0.1434  -0.0172 0.0405  58  GLU A OE2 
927  N N   . SER A 62  ? 0.3522 0.2291 0.3131 0.0605  -0.0121 0.0451  59  SER A N   
928  C CA  . SER A 62  ? 0.3587 0.2369 0.3105 0.0455  -0.0120 0.0504  59  SER A CA  
929  C C   . SER A 62  ? 0.3791 0.2683 0.3294 0.0473  -0.0180 0.0585  59  SER A C   
930  O O   . SER A 62  ? 0.3915 0.2972 0.3529 0.0573  -0.0218 0.0582  59  SER A O   
931  C CB  . SER A 62  ? 0.3601 0.2570 0.3184 0.0355  -0.0054 0.0436  59  SER A CB  
932  O OG  . SER A 62  ? 0.3516 0.2346 0.3072 0.0313  -0.0019 0.0380  59  SER A OG  
938  N N   . GLU A 63  ? 0.4092 0.2894 0.3448 0.0372  -0.0192 0.0663  60  GLU A N   
939  C CA  . GLU A 63  ? 0.4062 0.2920 0.3342 0.0377  -0.0255 0.0745  60  GLU A CA  
940  C C   . GLU A 63  ? 0.4268 0.3197 0.3437 0.0237  -0.0206 0.0767  60  GLU A C   
941  O O   . GLU A 63  ? 0.4521 0.3328 0.3600 0.0136  -0.0157 0.0795  60  GLU A O   
942  C CB  . GLU A 63  ? 0.5066 0.3666 0.4214 0.0431  -0.0337 0.0852  60  GLU A CB  
943  C CG  . GLU A 63  ? 0.5839 0.4317 0.5075 0.0592  -0.0379 0.0835  60  GLU A CG  
944  C CD  . GLU A 63  ? 0.7969 0.6175 0.7065 0.0659  -0.0476 0.0951  60  GLU A CD  
945  O OE1 . GLU A 63  ? 0.9138 0.7380 0.8326 0.0818  -0.0552 0.0976  60  GLU A OE1 
946  O OE2 . GLU A 63  ? 0.7745 0.5710 0.6646 0.0550  -0.0477 0.1025  60  GLU A OE2 
953  N N   . LEU A 64  ? 0.3793 0.2914 0.2964 0.0230  -0.0222 0.0755  61  LEU A N   
954  C CA  . LEU A 64  ? 0.3984 0.3144 0.3006 0.0123  -0.0178 0.0780  61  LEU A CA  
955  C C   . LEU A 64  ? 0.4472 0.3454 0.3278 0.0091  -0.0225 0.0901  61  LEU A C   
956  O O   . LEU A 64  ? 0.4463 0.3360 0.3227 0.0168  -0.0330 0.0968  61  LEU A O   
957  C CB  . LEU A 64  ? 0.3870 0.3229 0.2906 0.0123  -0.0193 0.0729  61  LEU A CB  
958  C CG  . LEU A 64  ? 0.3530 0.3063 0.2753 0.0142  -0.0155 0.0620  61  LEU A CG  
959  C CD1 . LEU A 64  ? 0.3960 0.3627 0.3126 0.0112  -0.0179 0.0586  61  LEU A CD1 
960  C CD2 . LEU A 64  ? 0.3626 0.3168 0.2916 0.0089  -0.0052 0.0561  61  LEU A CD2 
972  N N   . THR A 65  ? 0.3976 0.2915 0.2646 -0.0023 -0.0145 0.0936  62  THR A N   
973  C CA  . THR A 65  ? 0.4409 0.3188 0.2837 -0.0083 -0.0168 0.1057  62  THR A CA  
974  C C   . THR A 65  ? 0.4819 0.3705 0.3072 -0.0133 -0.0142 0.1061  62  THR A C   
975  O O   . THR A 65  ? 0.5226 0.3992 0.3237 -0.0188 -0.0157 0.1160  62  THR A O   
976  C CB  . THR A 65  ? 0.5231 0.3878 0.3610 -0.0192 -0.0090 0.1111  62  THR A CB  
977  O OG1 . THR A 65  ? 0.4809 0.3645 0.3267 -0.0270 0.0036  0.1043  62  THR A OG1 
978  C CG2 . THR A 65  ? 0.4822 0.3306 0.3326 -0.0149 -0.0129 0.1100  62  THR A CG2 
986  N N   . GLU A 66  ? 0.4509 0.3588 0.2850 -0.0117 -0.0105 0.0954  63  GLU A N   
987  C CA  . GLU A 66  ? 0.4844 0.3991 0.3002 -0.0144 -0.0105 0.0937  63  GLU A CA  
988  C C   . GLU A 66  ? 0.4042 0.3350 0.2351 -0.0090 -0.0139 0.0826  63  GLU A C   
989  O O   . GLU A 66  ? 0.4191 0.3582 0.2737 -0.0052 -0.0116 0.0758  63  GLU A O   
990  C CB  . GLU A 66  ? 0.6007 0.5180 0.4022 -0.0236 0.0042  0.0931  63  GLU A CB  
991  C CG  . GLU A 66  ? 0.4842 0.4176 0.3004 -0.0235 0.0148  0.0815  63  GLU A CG  
992  C CD  . GLU A 66  ? 0.4963 0.4347 0.3059 -0.0309 0.0309  0.0824  63  GLU A CD  
993  O OE1 . GLU A 66  ? 0.6861 0.6158 0.4767 -0.0379 0.0345  0.0923  63  GLU A OE1 
994  O OE2 . GLU A 66  ? 0.4817 0.4341 0.3058 -0.0295 0.0398  0.0734  63  GLU A OE2 
1001 N N   . PRO A 67  ? 0.4236 0.3576 0.2398 -0.0095 -0.0206 0.0812  64  PRO A N   
1002 C CA  . PRO A 67  ? 0.4308 0.3789 0.2614 -0.0061 -0.0259 0.0720  64  PRO A CA  
1003 C C   . PRO A 67  ? 0.4245 0.3808 0.2640 -0.0082 -0.0137 0.0609  64  PRO A C   
1004 O O   . PRO A 67  ? 0.4243 0.3779 0.2543 -0.0122 -0.0017 0.0594  64  PRO A O   
1005 C CB  . PRO A 67  ? 0.5205 0.4665 0.3272 -0.0093 -0.0358 0.0736  64  PRO A CB  
1006 C CG  . PRO A 67  ? 0.6261 0.5566 0.4053 -0.0131 -0.0362 0.0840  64  PRO A CG  
1007 C CD  . PRO A 67  ? 0.4908 0.4152 0.2740 -0.0151 -0.0226 0.0871  64  PRO A CD  
1015 N N   . LEU A 68  ? 0.4226 0.3901 0.2813 -0.0052 -0.0170 0.0537  65  LEU A N   
1016 C CA  . LEU A 68  ? 0.3775 0.3505 0.2409 -0.0070 -0.0084 0.0434  65  LEU A CA  
1017 C C   . LEU A 68  ? 0.4287 0.3952 0.2654 -0.0114 -0.0051 0.0394  65  LEU A C   
1018 O O   . LEU A 68  ? 0.4471 0.4079 0.2635 -0.0140 -0.0138 0.0424  65  LEU A O   
1019 C CB  . LEU A 68  ? 0.4004 0.3842 0.2826 -0.0052 -0.0145 0.0375  65  LEU A CB  
1020 C CG  . LEU A 68  ? 0.4232 0.4145 0.3318 -0.0003 -0.0140 0.0376  65  LEU A CG  
1021 C CD1 . LEU A 68  ? 0.4707 0.4740 0.3938 -0.0002 -0.0192 0.0325  65  LEU A CD1 
1022 C CD2 . LEU A 68  ? 0.3662 0.3553 0.2825 -0.0004 -0.0024 0.0346  65  LEU A CD2 
1034 N N   . PRO A 69  ? 0.3907 0.3570 0.2255 -0.0118 0.0074  0.0326  66  PRO A N   
1035 C CA  . PRO A 69  ? 0.4292 0.3877 0.2379 -0.0140 0.0119  0.0265  66  PRO A CA  
1036 C C   . PRO A 69  ? 0.4764 0.4323 0.2801 -0.0158 0.0010  0.0200  66  PRO A C   
1037 O O   . PRO A 69  ? 0.4335 0.3974 0.2590 -0.0150 -0.0049 0.0180  66  PRO A O   
1038 C CB  . PRO A 69  ? 0.4455 0.4079 0.2629 -0.0111 0.0271  0.0205  66  PRO A CB  
1039 C CG  . PRO A 69  ? 0.4555 0.4279 0.3043 -0.0087 0.0261  0.0210  66  PRO A CG  
1040 C CD  . PRO A 69  ? 0.4141 0.3875 0.2708 -0.0095 0.0171  0.0299  66  PRO A CD  
1048 N N   . ASP A 70  ? 0.4910 0.4349 0.2638 -0.0194 -0.0017 0.0167  67  ASP A N   
1049 C CA  . ASP A 70  ? 0.5615 0.5014 0.3278 -0.0236 -0.0140 0.0110  67  ASP A CA  
1050 C C   . ASP A 70  ? 0.5241 0.4639 0.3042 -0.0221 -0.0094 0.0014  67  ASP A C   
1051 O O   . ASP A 70  ? 0.5375 0.4807 0.3281 -0.0259 -0.0197 -0.0006 67  ASP A O   
1052 C CB  . ASP A 70  ? 0.6438 0.5666 0.3698 -0.0286 -0.0175 0.0076  67  ASP A CB  
1053 C CG  . ASP A 70  ? 0.7815 0.7030 0.4914 -0.0318 -0.0268 0.0182  67  ASP A CG  
1054 O OD1 . ASP A 70  ? 0.6851 0.6184 0.4147 -0.0318 -0.0395 0.0264  67  ASP A OD1 
1055 O OD2 . ASP A 70  ? 0.8662 0.7744 0.5425 -0.0337 -0.0216 0.0182  67  ASP A OD2 
1060 N N   . SER A 71  ? 0.4813 0.4185 0.2628 -0.0167 0.0057  -0.0034 68  SER A N   
1061 C CA  . SER A 71  ? 0.4661 0.4004 0.2582 -0.0141 0.0096  -0.0118 68  SER A CA  
1062 C C   . SER A 71  ? 0.4801 0.4285 0.3055 -0.0138 0.0054  -0.0088 68  SER A C   
1063 O O   . SER A 71  ? 0.4110 0.3560 0.2438 -0.0137 0.0051  -0.0144 68  SER A O   
1064 C CB  . SER A 71  ? 0.4921 0.4242 0.2821 -0.0066 0.0265  -0.0161 68  SER A CB  
1065 O OG  . SER A 71  ? 0.5354 0.4830 0.3463 -0.0038 0.0339  -0.0087 68  SER A OG  
1071 N N   . ALA A 72  ? 0.3699 0.3317 0.2129 -0.0135 0.0023  -0.0002 69  ALA A N   
1072 C CA  . ALA A 72  ? 0.3489 0.3226 0.2203 -0.0124 0.0002  0.0015  69  ALA A CA  
1073 C C   . ALA A 72  ? 0.3314 0.3081 0.2085 -0.0177 -0.0108 -0.0005 69  ALA A C   
1074 O O   . ALA A 72  ? 0.3304 0.3141 0.2266 -0.0177 -0.0105 -0.0014 69  ALA A O   
1075 C CB  . ALA A 72  ? 0.3321 0.3158 0.2179 -0.0100 -0.0008 0.0102  69  ALA A CB  
1081 N N   . SER A 73  ? 0.3816 0.3534 0.2418 -0.0236 -0.0208 -0.0008 70  SER A N   
1082 C CA  . SER A 73  ? 0.4077 0.3841 0.2745 -0.0309 -0.0316 -0.0021 70  SER A CA  
1083 C C   . SER A 73  ? 0.4284 0.3900 0.2865 -0.0343 -0.0292 -0.0106 70  SER A C   
1084 O O   . SER A 73  ? 0.4807 0.4464 0.3483 -0.0412 -0.0359 -0.0112 70  SER A O   
1085 C CB  . SER A 73  ? 0.4704 0.4464 0.3217 -0.0376 -0.0451 0.0007  70  SER A CB  
1086 O OG  . SER A 73  ? 0.5943 0.5512 0.4136 -0.0379 -0.0424 -0.0031 70  SER A OG  
1092 N N   . ASN A 74  ? 0.3901 0.3351 0.2314 -0.0295 -0.0196 -0.0167 71  ASN A N   
1093 C CA  . ASN A 74  ? 0.4089 0.3366 0.2414 -0.0304 -0.0174 -0.0247 71  ASN A CA  
1094 C C   . ASN A 74  ? 0.3746 0.3114 0.2326 -0.0286 -0.0143 -0.0232 71  ASN A C   
1095 O O   . ASN A 74  ? 0.3526 0.3014 0.2279 -0.0218 -0.0067 -0.0196 71  ASN A O   
1096 C CB  . ASN A 74  ? 0.4107 0.3217 0.2234 -0.0220 -0.0057 -0.0313 71  ASN A CB  
1097 C CG  . ASN A 74  ? 0.7111 0.6094 0.4924 -0.0239 -0.0071 -0.0340 71  ASN A CG  
1098 O OD1 . ASN A 74  ? 0.7431 0.6400 0.5132 -0.0329 -0.0196 -0.0323 71  ASN A OD1 
1099 N ND2 . ASN A 74  ? 0.8146 0.7051 0.5816 -0.0155 0.0058  -0.0379 71  ASN A ND2 
1106 N N   . PRO A 75  ? 0.3619 0.2911 0.2205 -0.0354 -0.0200 -0.0257 72  PRO A N   
1107 C CA  . PRO A 75  ? 0.3627 0.2998 0.2427 -0.0345 -0.0171 -0.0234 72  PRO A CA  
1108 C C   . PRO A 75  ? 0.3462 0.2752 0.2281 -0.0243 -0.0069 -0.0263 72  PRO A C   
1109 O O   . PRO A 75  ? 0.3441 0.2821 0.2441 -0.0223 -0.0041 -0.0232 72  PRO A O   
1110 C CB  . PRO A 75  ? 0.4299 0.3577 0.3049 -0.0463 -0.0263 -0.0249 72  PRO A CB  
1111 C CG  . PRO A 75  ? 0.4775 0.3835 0.3245 -0.0504 -0.0315 -0.0308 72  PRO A CG  
1112 C CD  . PRO A 75  ? 0.4497 0.3626 0.2887 -0.0461 -0.0304 -0.0298 72  PRO A CD  
1120 N N   . ASP A 76  ? 0.3839 0.2977 0.2485 -0.0174 -0.0010 -0.0319 73  ASP A N   
1121 C CA  . ASP A 76  ? 0.3823 0.2940 0.2537 -0.0064 0.0089  -0.0336 73  ASP A CA  
1122 C C   . ASP A 76  ? 0.4049 0.3324 0.2846 0.0008  0.0180  -0.0304 73  ASP A C   
1123 O O   . ASP A 76  ? 0.4176 0.3470 0.3038 0.0097  0.0267  -0.0316 73  ASP A O   
1124 C CB  . ASP A 76  ? 0.4885 0.3739 0.3384 -0.0013 0.0112  -0.0421 73  ASP A CB  
1125 C CG  . ASP A 76  ? 0.6657 0.5401 0.4901 -0.0002 0.0136  -0.0473 73  ASP A CG  
1126 O OD1 . ASP A 76  ? 0.7258 0.6090 0.5457 -0.0075 0.0086  -0.0440 73  ASP A OD1 
1127 O OD2 . ASP A 76  ? 1.1462 1.0022 0.9536 0.0084  0.0204  -0.0548 73  ASP A OD2 
1132 N N   . SER A 77  ? 0.3355 0.2752 0.2168 -0.0033 0.0158  -0.0256 74  SER A N   
1133 C CA  . SER A 77  ? 0.2998 0.2525 0.1880 0.0012  0.0235  -0.0212 74  SER A CA  
1134 C C   . SER A 77  ? 0.2942 0.2608 0.2075 0.0040  0.0268  -0.0168 74  SER A C   
1135 O O   . SER A 77  ? 0.3069 0.2789 0.2330 0.0003  0.0211  -0.0143 74  SER A O   
1136 C CB  . SER A 77  ? 0.3110 0.2704 0.1947 -0.0040 0.0179  -0.0159 74  SER A CB  
1137 O OG  . SER A 77  ? 0.3218 0.2914 0.2122 -0.0011 0.0245  -0.0103 74  SER A OG  
1143 N N   . ASP A 78  ? 0.2855 0.2589 0.2055 0.0099  0.0361  -0.0157 75  ASP A N   
1144 C CA  . ASP A 78  ? 0.3079 0.2946 0.2500 0.0107  0.0379  -0.0109 75  ASP A CA  
1145 C C   . ASP A 78  ? 0.2688 0.2656 0.2155 0.0080  0.0402  -0.0043 75  ASP A C   
1146 O O   . ASP A 78  ? 0.2585 0.2645 0.2210 0.0074  0.0417  -0.0004 75  ASP A O   
1147 C CB  . ASP A 78  ? 0.3467 0.3370 0.2985 0.0179  0.0448  -0.0127 75  ASP A CB  
1148 C CG  . ASP A 78  ? 0.4540 0.4494 0.4008 0.0231  0.0558  -0.0133 75  ASP A CG  
1149 O OD1 . ASP A 78  ? 0.4208 0.4129 0.3510 0.0209  0.0585  -0.0132 75  ASP A OD1 
1150 O OD2 . ASP A 78  ? 0.5720 0.5760 0.5318 0.0298  0.0620  -0.0136 75  ASP A OD2 
1155 N N   . TYR A 79  ? 0.2609 0.2541 0.1925 0.0055  0.0393  -0.0027 76  TYR A N   
1156 C CA  . TYR A 79  ? 0.2462 0.2452 0.1790 0.0030  0.0416  0.0044  76  TYR A CA  
1157 C C   . TYR A 79  ? 0.2581 0.2611 0.2061 0.0004  0.0359  0.0088  76  TYR A C   
1158 O O   . TYR A 79  ? 0.2389 0.2469 0.1970 -0.0011 0.0389  0.0133  76  TYR A O   
1159 C CB  . TYR A 79  ? 0.2843 0.2761 0.1955 0.0006  0.0392  0.0061  76  TYR A CB  
1160 C CG  . TYR A 79  ? 0.2535 0.2476 0.1649 -0.0025 0.0389  0.0147  76  TYR A CG  
1161 C CD1 . TYR A 79  ? 0.3264 0.3245 0.2358 -0.0037 0.0482  0.0190  76  TYR A CD1 
1162 C CD2 . TYR A 79  ? 0.2545 0.2470 0.1697 -0.0039 0.0295  0.0190  76  TYR A CD2 
1163 C CE1 . TYR A 79  ? 0.3561 0.3531 0.2645 -0.0079 0.0474  0.0277  76  TYR A CE1 
1164 C CE2 . TYR A 79  ? 0.2835 0.2739 0.1981 -0.0057 0.0286  0.0270  76  TYR A CE2 
1165 C CZ  . TYR A 79  ? 0.3750 0.3659 0.2851 -0.0086 0.0371  0.0315  76  TYR A CZ  
1166 O OH  . TYR A 79  ? 0.3552 0.3406 0.2626 -0.0119 0.0354  0.0402  76  TYR A OH  
1176 N N   . ARG A 80  ? 0.2391 0.2397 0.1881 -0.0005 0.0277  0.0078  77  ARG A N   
1177 C CA  . ARG A 80  ? 0.2481 0.2511 0.2085 -0.0011 0.0236  0.0115  77  ARG A CA  
1178 C C   . ARG A 80  ? 0.2158 0.2219 0.1904 -0.0011 0.0256  0.0103  77  ARG A C   
1179 O O   . ARG A 80  ? 0.2091 0.2147 0.1900 -0.0022 0.0254  0.0137  77  ARG A O   
1180 C CB  . ARG A 80  ? 0.2223 0.2265 0.1834 -0.0011 0.0158  0.0108  77  ARG A CB  
1181 C CG  . ARG A 80  ? 0.2402 0.2427 0.1903 -0.0013 0.0108  0.0148  77  ARG A CG  
1182 C CD  . ARG A 80  ? 0.2570 0.2661 0.2147 -0.0003 0.0025  0.0161  77  ARG A CD  
1183 N NE  . ARG A 80  ? 0.2239 0.2357 0.1956 0.0034  0.0033  0.0179  77  ARG A NE  
1184 C CZ  . ARG A 80  ? 0.2312 0.2485 0.2149 0.0040  0.0044  0.0146  77  ARG A CZ  
1185 N NH1 . ARG A 80  ? 0.2353 0.2572 0.2207 0.0004  0.0039  0.0105  77  ARG A NH1 
1186 N NH2 . ARG A 80  ? 0.2383 0.2544 0.2302 0.0079  0.0061  0.0154  77  ARG A NH2 
1200 N N   . VAL A 81  ? 0.2191 0.2260 0.1971 -0.0003 0.0259  0.0057  78  VAL A N   
1201 C CA  . VAL A 81  ? 0.2142 0.2234 0.2039 -0.0008 0.0257  0.0053  78  VAL A CA  
1202 C C   . VAL A 81  ? 0.2092 0.2232 0.2058 -0.0015 0.0302  0.0083  78  VAL A C   
1203 O O   . VAL A 81  ? 0.2113 0.2261 0.2156 -0.0042 0.0287  0.0105  78  VAL A O   
1204 C CB  . VAL A 81  ? 0.2235 0.2304 0.2137 -0.0001 0.0239  0.0012  78  VAL A CB  
1205 C CG1 . VAL A 81  ? 0.2419 0.2475 0.2292 0.0034  0.0278  -0.0012 78  VAL A CG1 
1206 C CG2 . VAL A 81  ? 0.2362 0.2440 0.2350 -0.0017 0.0218  0.0016  78  VAL A CG2 
1216 N N   . LYS A 82  ? 0.1952 0.2127 0.1886 0.0003  0.0360  0.0087  79  LYS A N   
1217 C CA  . LYS A 82  ? 0.1952 0.2222 0.1981 -0.0011 0.0413  0.0125  79  LYS A CA  
1218 C C   . LYS A 82  ? 0.2098 0.2352 0.2112 -0.0068 0.0412  0.0186  79  LYS A C   
1219 O O   . LYS A 82  ? 0.2241 0.2544 0.2358 -0.0115 0.0413  0.0225  79  LYS A O   
1220 C CB  . LYS A 82  ? 0.2098 0.2427 0.2095 0.0034  0.0497  0.0110  79  LYS A CB  
1221 C CG  . LYS A 82  ? 0.2589 0.2906 0.2614 0.0101  0.0496  0.0053  79  LYS A CG  
1222 C CD  . LYS A 82  ? 0.2987 0.3401 0.3203 0.0107  0.0475  0.0071  79  LYS A CD  
1223 C CE  . LYS A 82  ? 0.3028 0.3429 0.3280 0.0192  0.0479  0.0027  79  LYS A CE  
1224 N NZ  . LYS A 82  ? 0.2547 0.3014 0.2965 0.0188  0.0418  0.0053  79  LYS A NZ  
1238 N N   . ARG A 83  ? 0.2085 0.2259 0.1964 -0.0069 0.0399  0.0200  80  ARG A N   
1239 C CA  . ARG A 83  ? 0.2207 0.2320 0.2045 -0.0114 0.0386  0.0263  80  ARG A CA  
1240 C C   . ARG A 83  ? 0.2283 0.2321 0.2180 -0.0128 0.0322  0.0264  80  ARG A C   
1241 O O   . ARG A 83  ? 0.2303 0.2289 0.2214 -0.0180 0.0315  0.0311  80  ARG A O   
1242 C CB  . ARG A 83  ? 0.2329 0.2369 0.2002 -0.0098 0.0369  0.0282  80  ARG A CB  
1243 C CG  . ARG A 83  ? 0.2711 0.2663 0.2305 -0.0137 0.0357  0.0362  80  ARG A CG  
1244 C CD  . ARG A 83  ? 0.2729 0.2732 0.2329 -0.0203 0.0434  0.0418  80  ARG A CD  
1245 N NE  . ARG A 83  ? 0.2500 0.2495 0.2229 -0.0258 0.0417  0.0444  80  ARG A NE  
1246 C CZ  . ARG A 83  ? 0.2988 0.2996 0.2735 -0.0345 0.0454  0.0515  80  ARG A CZ  
1247 N NH1 . ARG A 83  ? 0.3247 0.3325 0.2922 -0.0379 0.0535  0.0565  80  ARG A NH1 
1248 N NH2 . ARG A 83  ? 0.3083 0.3033 0.2911 -0.0408 0.0411  0.0537  80  ARG A NH2 
1262 N N   . ASP A 84  ? 0.2092 0.2111 0.2006 -0.0089 0.0280  0.0213  81  ASP A N   
1263 C CA  . ASP A 84  ? 0.2012 0.1959 0.1961 -0.0091 0.0237  0.0200  81  ASP A CA  
1264 C C   . ASP A 84  ? 0.2194 0.2163 0.2227 -0.0142 0.0237  0.0200  81  ASP A C   
1265 O O   . ASP A 84  ? 0.2212 0.2087 0.2237 -0.0181 0.0209  0.0215  81  ASP A O   
1266 C CB  . ASP A 84  ? 0.2219 0.2184 0.2178 -0.0048 0.0213  0.0147  81  ASP A CB  
1267 C CG  . ASP A 84  ? 0.2686 0.2628 0.2603 -0.0003 0.0185  0.0152  81  ASP A CG  
1268 O OD1 . ASP A 84  ? 0.2415 0.2295 0.2281 0.0009  0.0172  0.0197  81  ASP A OD1 
1269 O OD2 . ASP A 84  ? 0.2416 0.2412 0.2361 0.0020  0.0171  0.0118  81  ASP A OD2 
1274 N N   . ALA A 85  ? 0.1983 0.2063 0.2090 -0.0141 0.0257  0.0184  82  ALA A N   
1275 C CA  . ALA A 85  ? 0.1940 0.2073 0.2149 -0.0188 0.0241  0.0194  82  ALA A CA  
1276 C C   . ALA A 85  ? 0.2157 0.2321 0.2409 -0.0259 0.0259  0.0256  82  ALA A C   
1277 O O   . ALA A 85  ? 0.2120 0.2246 0.2408 -0.0330 0.0216  0.0275  82  ALA A O   
1278 C CB  . ALA A 85  ? 0.1932 0.2185 0.2226 -0.0151 0.0257  0.0174  82  ALA A CB  
1284 N N   . GLN A 86  ? 0.2031 0.2256 0.2264 -0.0256 0.0322  0.0292  83  GLN A N   
1285 C CA  . GLN A 86  ? 0.2036 0.2299 0.2305 -0.0341 0.0349  0.0363  83  GLN A CA  
1286 C C   . GLN A 86  ? 0.2207 0.2267 0.2371 -0.0398 0.0297  0.0393  83  GLN A C   
1287 O O   . GLN A 86  ? 0.2522 0.2560 0.2724 -0.0498 0.0278  0.0444  83  GLN A O   
1288 C CB  . GLN A 86  ? 0.2378 0.2732 0.2606 -0.0325 0.0441  0.0395  83  GLN A CB  
1289 C CG  . GLN A 86  ? 0.2632 0.3090 0.2932 -0.0423 0.0492  0.0477  83  GLN A CG  
1290 C CD  . GLN A 86  ? 0.3584 0.4163 0.3843 -0.0403 0.0604  0.0503  83  GLN A CD  
1291 O OE1 . GLN A 86  ? 0.3635 0.4301 0.3900 -0.0311 0.0656  0.0448  83  GLN A OE1 
1292 N NE2 . GLN A 86  ? 0.3218 0.3790 0.3420 -0.0494 0.0647  0.0587  83  GLN A NE2 
1301 N N   . ASP A 87  ? 0.2356 0.2268 0.2394 -0.0334 0.0271  0.0367  84  ASP A N   
1302 C CA  . ASP A 87  ? 0.2519 0.2215 0.2456 -0.0355 0.0221  0.0386  84  ASP A CA  
1303 C C   . ASP A 87  ? 0.2517 0.2126 0.2482 -0.0402 0.0166  0.0355  84  ASP A C   
1304 O O   . ASP A 87  ? 0.2560 0.2015 0.2471 -0.0479 0.0130  0.0389  84  ASP A O   
1305 C CB  . ASP A 87  ? 0.2538 0.2139 0.2385 -0.0253 0.0199  0.0353  84  ASP A CB  
1306 C CG  . ASP A 87  ? 0.3026 0.2635 0.2790 -0.0223 0.0219  0.0398  84  ASP A CG  
1307 O OD1 . ASP A 87  ? 0.2975 0.2641 0.2716 -0.0278 0.0264  0.0454  84  ASP A OD1 
1308 O OD2 . ASP A 87  ? 0.2890 0.2468 0.2611 -0.0141 0.0191  0.0376  84  ASP A OD2 
1313 N N   . ILE A 88  ? 0.2228 0.1903 0.2244 -0.0361 0.0151  0.0290  85  ILE A N   
1314 C CA  . ILE A 88  ? 0.2362 0.1949 0.2370 -0.0411 0.0094  0.0258  85  ILE A CA  
1315 C C   . ILE A 88  ? 0.2465 0.2129 0.2569 -0.0534 0.0069  0.0310  85  ILE A C   
1316 O O   . ILE A 88  ? 0.2673 0.2187 0.2721 -0.0621 0.0009  0.0315  85  ILE A O   
1317 C CB  . ILE A 88  ? 0.2327 0.1985 0.2360 -0.0355 0.0085  0.0193  85  ILE A CB  
1318 C CG1 . ILE A 88  ? 0.2394 0.2002 0.2354 -0.0253 0.0109  0.0149  85  ILE A CG1 
1319 C CG2 . ILE A 88  ? 0.2631 0.2192 0.2624 -0.0419 0.0020  0.0164  85  ILE A CG2 
1320 C CD1 . ILE A 88  ? 0.2800 0.2202 0.2643 -0.0221 0.0096  0.0130  85  ILE A CD1 
1332 N N   . ALA A 89  ? 0.2327 0.2229 0.2578 -0.0544 0.0113  0.0346  86  ALA A N   
1333 C CA  . ALA A 89  ? 0.2522 0.2565 0.2917 -0.0658 0.0094  0.0404  86  ALA A CA  
1334 C C   . ALA A 89  ? 0.2710 0.2648 0.3054 -0.0769 0.0094  0.0476  86  ALA A C   
1335 O O   . ALA A 89  ? 0.2815 0.2720 0.3194 -0.0899 0.0032  0.0511  86  ALA A O   
1336 C CB  . ALA A 89  ? 0.2609 0.2942 0.3181 -0.0616 0.0164  0.0428  86  ALA A CB  
1342 N N   . GLU A 90  ? 0.2558 0.2438 0.2810 -0.0734 0.0155  0.0506  87  GLU A N   
1343 C CA  . GLU A 90  ? 0.2618 0.2364 0.2790 -0.0840 0.0153  0.0585  87  GLU A CA  
1344 C C   . GLU A 90  ? 0.3024 0.2435 0.3032 -0.0876 0.0064  0.0561  87  GLU A C   
1345 O O   . GLU A 90  ? 0.3493 0.2773 0.3464 -0.1013 0.0019  0.0616  87  GLU A O   
1346 C CB  . GLU A 90  ? 0.3228 0.2959 0.3301 -0.0779 0.0226  0.0620  87  GLU A CB  
1347 C CG  . GLU A 90  ? 0.3717 0.3735 0.3906 -0.0780 0.0328  0.0660  87  GLU A CG  
1348 C CD  . GLU A 90  ? 0.5098 0.5281 0.5427 -0.0931 0.0356  0.0746  87  GLU A CD  
1349 O OE1 . GLU A 90  ? 0.6332 0.6816 0.6854 -0.0921 0.0420  0.0751  87  GLU A OE1 
1350 O OE2 . GLU A 90  ? 0.6687 0.6701 0.6940 -0.1058 0.0314  0.0813  87  GLU A OE2 
1357 N N   . LEU A 91  ? 0.2962 0.2231 0.2871 -0.0756 0.0041  0.0478  88  LEU A N   
1358 C CA  . LEU A 91  ? 0.3330 0.2279 0.3075 -0.0762 -0.0029 0.0437  88  LEU A CA  
1359 C C   . LEU A 91  ? 0.3542 0.2456 0.3310 -0.0886 -0.0104 0.0420  88  LEU A C   
1360 O O   . LEU A 91  ? 0.3923 0.2594 0.3579 -0.0996 -0.0166 0.0441  88  LEU A O   
1361 C CB  . LEU A 91  ? 0.3464 0.2337 0.3134 -0.0602 -0.0019 0.0349  88  LEU A CB  
1362 C CG  . LEU A 91  ? 0.3435 0.1979 0.2926 -0.0562 -0.0066 0.0288  88  LEU A CG  
1363 C CD1 . LEU A 91  ? 0.4428 0.2687 0.3780 -0.0592 -0.0093 0.0342  88  LEU A CD1 
1364 C CD2 . LEU A 91  ? 0.3945 0.2521 0.3421 -0.0394 -0.0027 0.0214  88  LEU A CD2 
1376 N N   . ALA A 92  ? 0.3294 0.2432 0.3194 -0.0876 -0.0109 0.0385  89  ALA A N   
1377 C CA  . ALA A 92  ? 0.3231 0.2366 0.3160 -0.0997 -0.0198 0.0377  89  ALA A CA  
1378 C C   . ALA A 92  ? 0.3308 0.2497 0.3326 -0.1178 -0.0232 0.0472  89  ALA A C   
1379 O O   . ALA A 92  ? 0.3795 0.2786 0.3720 -0.1311 -0.0326 0.0474  89  ALA A O   
1380 C CB  . ALA A 92  ? 0.2970 0.2376 0.3053 -0.0948 -0.0197 0.0350  89  ALA A CB  
1386 N N   . LYS A 93  ? 0.3206 0.2660 0.3397 -0.1194 -0.0155 0.0552  90  LYS A N   
1387 C CA  . LYS A 93  ? 0.3504 0.3070 0.3814 -0.1376 -0.0170 0.0655  90  LYS A CA  
1388 C C   . LYS A 93  ? 0.4200 0.3419 0.4305 -0.1478 -0.0203 0.0697  90  LYS A C   
1389 O O   . LYS A 93  ? 0.4084 0.3287 0.4217 -0.1634 -0.0256 0.0750  90  LYS A O   
1390 C CB  . LYS A 93  ? 0.3108 0.3033 0.3622 -0.1347 -0.0051 0.0724  90  LYS A CB  
1391 C CG  . LYS A 93  ? 0.3807 0.4094 0.4564 -0.1272 -0.0027 0.0703  90  LYS A CG  
1392 C CD  . LYS A 93  ? 0.5172 0.5757 0.6077 -0.1211 0.0112  0.0752  90  LYS A CD  
1393 C CE  . LYS A 93  ? 0.5579 0.6517 0.6741 -0.1137 0.0138  0.0740  90  LYS A CE  
1394 N NZ  . LYS A 93  ? 0.7173 0.8318 0.8402 -0.1020 0.0285  0.0746  90  LYS A NZ  
1408 N N   . SER A 94  ? 0.3750 0.2706 0.3653 -0.1356 -0.0173 0.0662  91  SER A N   
1409 C CA  . SER A 94  ? 0.4552 0.3139 0.4242 -0.1426 -0.0208 0.0705  91  SER A CA  
1410 C C   . SER A 94  ? 0.5422 0.3641 0.4918 -0.1463 -0.0317 0.0630  91  SER A C   
1411 O O   . SER A 94  ? 0.5474 0.3429 0.4822 -0.1509 -0.0356 0.0646  91  SER A O   
1412 C CB  . SER A 94  ? 0.4825 0.3269 0.4378 -0.1263 -0.0148 0.0699  91  SER A CB  
1413 O OG  . SER A 94  ? 0.4601 0.2869 0.4038 -0.1094 -0.0165 0.0588  91  SER A OG  
1419 N N   . LEU A 95  ? 0.4822 0.3047 0.4309 -0.1403 -0.0354 0.0532  92  LEU A N   
1420 C CA  . LEU A 95  ? 0.4811 0.2681 0.4076 -0.1412 -0.0442 0.0442  92  LEU A CA  
1421 C C   . LEU A 95  ? 0.5806 0.3792 0.5135 -0.1537 -0.0531 0.0423  92  LEU A C   
1422 O O   . LEU A 95  ? 0.5832 0.3540 0.4965 -0.1569 -0.0607 0.0362  92  LEU A O   
1423 C CB  . LEU A 95  ? 0.5278 0.3049 0.4431 -0.1214 -0.0407 0.0326  92  LEU A CB  
1424 C CG  . LEU A 95  ? 0.5319 0.2987 0.4400 -0.1028 -0.0328 0.0314  92  LEU A CG  
1425 C CD1 . LEU A 95  ? 0.5842 0.3592 0.4918 -0.0846 -0.0278 0.0210  92  LEU A CD1 
1426 C CD2 . LEU A 95  ? 0.7097 0.4312 0.5939 -0.1032 -0.0368 0.0317  92  LEU A CD2 
1438 N N   . SER A 96  ? 0.5049 0.3439 0.4644 -0.1600 -0.0526 0.0477  93  SER A N   
1439 C CA  . SER A 96  ? 0.4574 0.3102 0.4244 -0.1688 -0.0621 0.0457  93  SER A CA  
1440 C C   . SER A 96  ? 0.4736 0.3707 0.4730 -0.1779 -0.0610 0.0557  93  SER A C   
1441 O O   . SER A 96  ? 0.5180 0.4448 0.5381 -0.1721 -0.0518 0.0605  93  SER A O   
1442 C CB  . SER A 96  ? 0.4853 0.3387 0.4476 -0.1592 -0.0635 0.0371  93  SER A CB  
1443 O OG  . SER A 96  ? 0.5578 0.4217 0.5237 -0.1665 -0.0738 0.0353  93  SER A OG  
1449 N N   . ASP A 97  ? 0.4695 0.3716 0.4732 -0.1912 -0.0703 0.0585  94  ASP A N   
1450 C CA  . ASP A 97  ? 0.5540 0.4995 0.5897 -0.1989 -0.0707 0.0671  94  ASP A CA  
1451 C C   . ASP A 97  ? 0.5276 0.4975 0.5783 -0.1950 -0.0765 0.0648  94  ASP A C   
1452 O O   . ASP A 97  ? 0.6490 0.6579 0.7291 -0.1978 -0.0765 0.0715  94  ASP A O   
1453 C CB  . ASP A 97  ? 0.6094 0.5493 0.6433 -0.2160 -0.0789 0.0720  94  ASP A CB  
1454 C CG  . ASP A 97  ? 0.8722 0.7824 0.8823 -0.2219 -0.0932 0.0649  94  ASP A CG  
1455 O OD1 . ASP A 97  ? 0.8317 0.7034 0.8121 -0.2145 -0.0939 0.0559  94  ASP A OD1 
1456 O OD2 . ASP A 97  ? 1.0240 0.9490 1.0441 -0.2334 -0.1034 0.0683  94  ASP A OD2 
1461 N N   . GLU A 98  ? 0.4565 0.4041 0.4870 -0.1879 -0.0813 0.0556  95  GLU A N   
1462 C CA  . GLU A 98  ? 0.4476 0.4131 0.4873 -0.1832 -0.0873 0.0532  95  GLU A CA  
1463 C C   . GLU A 98  ? 0.4106 0.3753 0.4477 -0.1686 -0.0795 0.0483  95  GLU A C   
1464 O O   . GLU A 98  ? 0.3908 0.3318 0.4112 -0.1626 -0.0716 0.0444  95  GLU A O   
1465 C CB  . GLU A 98  ? 0.4723 0.4112 0.4867 -0.1890 -0.1009 0.0467  95  GLU A CB  
1466 C CG  . GLU A 98  ? 0.6209 0.5169 0.5991 -0.1817 -0.0993 0.0355  95  GLU A CG  
1467 C CD  . GLU A 98  ? 0.9503 0.8133 0.8988 -0.1897 -0.1100 0.0297  95  GLU A CD  
1468 O OE1 . GLU A 98  ? 0.9762 0.8215 0.9026 -0.1848 -0.1138 0.0215  95  GLU A OE1 
1469 O OE2 . GLU A 98  ? 1.0126 0.8671 0.9587 -0.2012 -0.1143 0.0336  95  GLU A OE2 
1476 N N   . PRO A 99  ? 0.3393 0.3292 0.3929 -0.1625 -0.0818 0.0489  96  PRO A N   
1477 C CA  . PRO A 99  ? 0.3084 0.2962 0.3551 -0.1435 -0.0728 0.0424  96  PRO A CA  
1478 C C   . PRO A 99  ? 0.3621 0.3098 0.3725 -0.1399 -0.0750 0.0317  96  PRO A C   
1479 O O   . PRO A 99  ? 0.3995 0.3245 0.3910 -0.1521 -0.0870 0.0287  96  PRO A O   
1480 C CB  . PRO A 99  ? 0.3330 0.3517 0.4012 -0.1385 -0.0777 0.0454  96  PRO A CB  
1481 C CG  . PRO A 99  ? 0.3744 0.4236 0.4725 -0.1532 -0.0855 0.0560  96  PRO A CG  
1482 C CD  . PRO A 99  ? 0.3410 0.3640 0.4195 -0.1664 -0.0902 0.0550  96  PRO A CD  
1490 N N   . VAL A 100 ? 0.3465 0.2865 0.3475 -0.1235 -0.0633 0.0261  97  VAL A N   
1491 C CA  . VAL A 100 ? 0.3756 0.2811 0.3457 -0.1170 -0.0607 0.0163  97  VAL A CA  
1492 C C   . VAL A 100 ? 0.3531 0.2612 0.3156 -0.1051 -0.0581 0.0105  97  VAL A C   
1493 O O   . VAL A 100 ? 0.3277 0.2615 0.3080 -0.0999 -0.0572 0.0140  97  VAL A O   
1494 C CB  . VAL A 100 ? 0.3606 0.2532 0.3252 -0.1088 -0.0497 0.0153  97  VAL A CB  
1495 C CG1 . VAL A 100 ? 0.3886 0.2754 0.3578 -0.1218 -0.0522 0.0223  97  VAL A CG1 
1496 C CG2 . VAL A 100 ? 0.3564 0.2734 0.3377 -0.0944 -0.0382 0.0172  97  VAL A CG2 
1506 N N   . TYR A 101 ? 0.3598 0.2399 0.2948 -0.1001 -0.0558 0.0015  98  TYR A N   
1507 C CA  . TYR A 101 ? 0.3310 0.2106 0.2552 -0.0892 -0.0507 -0.0042 98  TYR A CA  
1508 C C   . TYR A 101 ? 0.3132 0.1990 0.2436 -0.0746 -0.0371 -0.0056 98  TYR A C   
1509 O O   . TYR A 101 ? 0.3393 0.2126 0.2661 -0.0716 -0.0322 -0.0067 98  TYR A O   
1510 C CB  . TYR A 101 ? 0.3919 0.2391 0.2823 -0.0918 -0.0539 -0.0134 98  TYR A CB  
1511 C CG  . TYR A 101 ? 0.3996 0.2378 0.2791 -0.1074 -0.0693 -0.0127 98  TYR A CG  
1512 C CD1 . TYR A 101 ? 0.4369 0.2596 0.3120 -0.1212 -0.0783 -0.0113 98  TYR A CD1 
1513 C CD2 . TYR A 101 ? 0.4222 0.2661 0.2944 -0.1096 -0.0759 -0.0127 98  TYR A CD2 
1514 C CE1 . TYR A 101 ? 0.4673 0.2824 0.3324 -0.1372 -0.0942 -0.0103 98  TYR A CE1 
1515 C CE2 . TYR A 101 ? 0.4291 0.2654 0.2907 -0.1245 -0.0920 -0.0114 98  TYR A CE2 
1516 C CZ  . TYR A 101 ? 0.4373 0.2605 0.2964 -0.1383 -0.1012 -0.0104 98  TYR A CZ  
1517 O OH  . TYR A 101 ? 0.5073 0.3298 0.3604 -0.1488 -0.1144 -0.0071 98  TYR A OH  
1527 N N   . ILE A 102 ? 0.2969 0.2005 0.2358 -0.0664 -0.0322 -0.0051 99  ILE A N   
1528 C CA  . ILE A 102 ? 0.2832 0.1954 0.2294 -0.0543 -0.0211 -0.0058 99  ILE A CA  
1529 C C   . ILE A 102 ? 0.2907 0.2037 0.2274 -0.0476 -0.0166 -0.0101 99  ILE A C   
1530 O O   . ILE A 102 ? 0.2899 0.2096 0.2259 -0.0507 -0.0214 -0.0086 99  ILE A O   
1531 C CB  . ILE A 102 ? 0.2710 0.2079 0.2417 -0.0524 -0.0190 0.0012  99  ILE A CB  
1532 C CG1 . ILE A 102 ? 0.3162 0.2539 0.2960 -0.0597 -0.0211 0.0063  99  ILE A CG1 
1533 C CG2 . ILE A 102 ? 0.2913 0.2353 0.2659 -0.0413 -0.0094 0.0000  99  ILE A CG2 
1534 C CD1 . ILE A 102 ? 0.2869 0.2506 0.2902 -0.0587 -0.0181 0.0132  99  ILE A CD1 
1546 N N   . LEU A 103 ? 0.2973 0.2049 0.2275 -0.0386 -0.0076 -0.0146 100 LEU A N   
1547 C CA  . LEU A 103 ? 0.2988 0.2127 0.2245 -0.0329 -0.0014 -0.0173 100 LEU A CA  
1548 C C   . LEU A 103 ? 0.2717 0.1984 0.2106 -0.0239 0.0066  -0.0162 100 LEU A C   
1549 O O   . LEU A 103 ? 0.2762 0.1969 0.2159 -0.0186 0.0100  -0.0175 100 LEU A O   
1550 C CB  . LEU A 103 ? 0.2966 0.1919 0.1983 -0.0316 0.0021  -0.0249 100 LEU A CB  
1551 C CG  . LEU A 103 ? 0.3166 0.2197 0.2123 -0.0277 0.0094  -0.0270 100 LEU A CG  
1552 C CD1 . LEU A 103 ? 0.3774 0.2625 0.2457 -0.0313 0.0096  -0.0330 100 LEU A CD1 
1553 C CD2 . LEU A 103 ? 0.3508 0.2633 0.2553 -0.0171 0.0202  -0.0289 100 LEU A CD2 
1565 N N   . GLY A 104 ? 0.2483 0.1910 0.1965 -0.0225 0.0084  -0.0135 101 GLY A N   
1566 C CA  . GLY A 104 ? 0.2563 0.2112 0.2146 -0.0157 0.0147  -0.0128 101 GLY A CA  
1567 C C   . GLY A 104 ? 0.2721 0.2333 0.2258 -0.0147 0.0195  -0.0146 101 GLY A C   
1568 O O   . GLY A 104 ? 0.2958 0.2549 0.2416 -0.0199 0.0169  -0.0141 101 GLY A O   
1572 N N   . SER A 105 ? 0.2469 0.2168 0.2063 -0.0085 0.0261  -0.0158 102 SER A N   
1573 C CA  . SER A 105 ? 0.2598 0.2406 0.2189 -0.0088 0.0315  -0.0162 102 SER A CA  
1574 C C   . SER A 105 ? 0.2105 0.2073 0.1846 -0.0079 0.0316  -0.0125 102 SER A C   
1575 O O   . SER A 105 ? 0.2396 0.2406 0.2232 -0.0030 0.0310  -0.0115 102 SER A O   
1576 C CB  . SER A 105 ? 0.3548 0.3355 0.3086 -0.0025 0.0400  -0.0210 102 SER A CB  
1577 O OG  . SER A 105 ? 0.3745 0.3688 0.3289 -0.0047 0.0461  -0.0204 102 SER A OG  
1583 N N   . SER A 106 ? 0.2361 0.2400 0.2101 -0.0135 0.0317  -0.0104 103 SER A N   
1584 C CA  . SER A 106 ? 0.2165 0.2341 0.2018 -0.0146 0.0314  -0.0075 103 SER A CA  
1585 C C   . SER A 106 ? 0.2226 0.2370 0.2132 -0.0135 0.0255  -0.0058 103 SER A C   
1586 O O   . SER A 106 ? 0.2310 0.2360 0.2173 -0.0155 0.0214  -0.0051 103 SER A O   
1587 C CB  . SER A 106 ? 0.2607 0.2936 0.2558 -0.0096 0.0374  -0.0083 103 SER A CB  
1588 O OG  . SER A 106 ? 0.2838 0.3314 0.2882 -0.0143 0.0362  -0.0051 103 SER A OG  
1593 N N   . SER A 107 ? 0.2461 0.2689 0.2457 -0.0101 0.0249  -0.0047 104 SER A N   
1594 C CA  . SER A 107 ? 0.2296 0.2479 0.2303 -0.0093 0.0208  -0.0033 104 SER A CA  
1595 C C   . SER A 107 ? 0.2128 0.2218 0.2114 -0.0064 0.0203  -0.0035 104 SER A C   
1596 O O   . SER A 107 ? 0.2231 0.2288 0.2220 -0.0072 0.0181  -0.0022 104 SER A O   
1597 C CB  . SER A 107 ? 0.3187 0.3456 0.3254 -0.0073 0.0192  -0.0018 104 SER A CB  
1598 O OG  . SER A 107 ? 0.3154 0.3478 0.3276 -0.0013 0.0212  -0.0016 104 SER A OG  
1604 N N   . GLY A 108 ? 0.2126 0.2167 0.2085 -0.0038 0.0226  -0.0053 105 GLY A N   
1605 C CA  . GLY A 108 ? 0.2380 0.2308 0.2302 -0.0040 0.0208  -0.0053 105 GLY A CA  
1606 C C   . GLY A 108 ? 0.2259 0.2137 0.2140 -0.0096 0.0175  -0.0051 105 GLY A C   
1607 O O   . GLY A 108 ? 0.2267 0.2104 0.2162 -0.0119 0.0145  -0.0035 105 GLY A O   
1611 N N   A SER A 109 ? 0.2144 0.2032 0.1978 -0.0126 0.0175  -0.0060 106 SER A N   
1612 N N   B SER A 109 ? 0.2155 0.2044 0.1990 -0.0125 0.0175  -0.0060 106 SER A N   
1613 C CA  A SER A 109 ? 0.2226 0.2070 0.2028 -0.0171 0.0126  -0.0045 106 SER A CA  
1614 C CA  B SER A 109 ? 0.2231 0.2076 0.2033 -0.0171 0.0126  -0.0046 106 SER A CA  
1615 C C   A SER A 109 ? 0.2154 0.2050 0.2043 -0.0163 0.0100  -0.0017 106 SER A C   
1616 C C   B SER A 109 ? 0.2150 0.2046 0.2039 -0.0163 0.0101  -0.0017 106 SER A C   
1617 O O   A SER A 109 ? 0.2108 0.1998 0.2029 -0.0176 0.0058  0.0004  106 SER A O   
1618 O O   B SER A 109 ? 0.2119 0.2008 0.2040 -0.0176 0.0058  0.0003  106 SER A O   
1619 C CB  A SER A 109 ? 0.2520 0.2338 0.2223 -0.0208 0.0128  -0.0051 106 SER A CB  
1620 C CB  B SER A 109 ? 0.2507 0.2328 0.2213 -0.0207 0.0129  -0.0051 106 SER A CB  
1621 O OG  A SER A 109 ? 0.2698 0.2574 0.2428 -0.0215 0.0139  -0.0036 106 SER A OG  
1622 O OG  B SER A 109 ? 0.2529 0.2292 0.2194 -0.0244 0.0064  -0.0029 106 SER A OG  
1633 N N   . ILE A 110 ? 0.2200 0.2149 0.2126 -0.0140 0.0125  -0.0016 107 ILE A N   
1634 C CA  . ILE A 110 ? 0.1928 0.1900 0.1904 -0.0119 0.0115  -0.0003 107 ILE A CA  
1635 C C   . ILE A 110 ? 0.1815 0.1820 0.1853 -0.0099 0.0127  0.0011  107 ILE A C   
1636 O O   . ILE A 110 ? 0.1862 0.1899 0.1961 -0.0088 0.0120  0.0028  107 ILE A O   
1637 C CB  . ILE A 110 ? 0.1825 0.1814 0.1781 -0.0115 0.0128  -0.0013 107 ILE A CB  
1638 C CG1 . ILE A 110 ? 0.2237 0.2194 0.2133 -0.0159 0.0115  -0.0014 107 ILE A CG1 
1639 C CG2 . ILE A 110 ? 0.2221 0.2199 0.2189 -0.0083 0.0129  -0.0014 107 ILE A CG2 
1640 C CD1 . ILE A 110 ? 0.2502 0.2476 0.2379 -0.0183 0.0113  -0.0019 107 ILE A CD1 
1652 N N   . VAL A 111 ? 0.1920 0.1924 0.1953 -0.0093 0.0148  0.0011  108 VAL A N   
1653 C CA  . VAL A 111 ? 0.1982 0.1993 0.2054 -0.0097 0.0155  0.0037  108 VAL A CA  
1654 C C   . VAL A 111 ? 0.1812 0.1817 0.1923 -0.0137 0.0122  0.0051  108 VAL A C   
1655 O O   . VAL A 111 ? 0.1919 0.1991 0.2111 -0.0148 0.0125  0.0081  108 VAL A O   
1656 C CB  . VAL A 111 ? 0.1749 0.1709 0.1785 -0.0085 0.0166  0.0040  108 VAL A CB  
1657 C CG1 . VAL A 111 ? 0.2037 0.1971 0.2091 -0.0112 0.0168  0.0077  108 VAL A CG1 
1658 C CG2 . VAL A 111 ? 0.1945 0.1942 0.1966 -0.0047 0.0181  0.0038  108 VAL A CG2 
1668 N N   . ALA A 112 ? 0.1987 0.1922 0.2038 -0.0164 0.0090  0.0032  109 ALA A N   
1669 C CA  . ALA A 112 ? 0.1996 0.1913 0.2061 -0.0217 0.0036  0.0046  109 ALA A CA  
1670 C C   . ALA A 112 ? 0.1914 0.1929 0.2077 -0.0210 0.0007  0.0074  109 ALA A C   
1671 O O   . ALA A 112 ? 0.2126 0.2213 0.2390 -0.0241 -0.0027 0.0108  109 ALA A O   
1672 C CB  . ALA A 112 ? 0.2162 0.1967 0.2096 -0.0243 0.0010  0.0014  109 ALA A CB  
1678 N N   . MET A 113 ? 0.1902 0.1922 0.2047 -0.0168 0.0017  0.0063  110 MET A N   
1679 C CA  . MET A 113 ? 0.1922 0.2005 0.2154 -0.0134 -0.0008 0.0085  110 MET A CA  
1680 C C   . MET A 113 ? 0.2002 0.2207 0.2366 -0.0097 0.0036  0.0105  110 MET A C   
1681 O O   . MET A 113 ? 0.1983 0.2294 0.2479 -0.0083 0.0012  0.0137  110 MET A O   
1682 C CB  . MET A 113 ? 0.2020 0.2033 0.2168 -0.0103 0.0003  0.0064  110 MET A CB  
1683 C CG  . MET A 113 ? 0.1984 0.1904 0.2019 -0.0144 -0.0043 0.0064  110 MET A CG  
1684 S SD  . MET A 113 ? 0.2424 0.2262 0.2361 -0.0137 -0.0025 0.0050  110 MET A SD  
1685 C CE  . MET A 113 ? 0.2852 0.2609 0.2640 -0.0210 -0.0050 0.0055  110 MET A CE  
1695 N N   . HIS A 114 ? 0.1802 0.2009 0.2136 -0.0083 0.0100  0.0091  111 HIS A N   
1696 C CA  . HIS A 114 ? 0.1843 0.2159 0.2269 -0.0056 0.0157  0.0111  111 HIS A CA  
1697 C C   . HIS A 114 ? 0.1922 0.2324 0.2445 -0.0118 0.0152  0.0156  111 HIS A C   
1698 O O   . HIS A 114 ? 0.1883 0.2428 0.2531 -0.0107 0.0191  0.0187  111 HIS A O   
1699 C CB  . HIS A 114 ? 0.1785 0.2057 0.2113 -0.0032 0.0214  0.0089  111 HIS A CB  
1700 C CG  . HIS A 114 ? 0.2019 0.2229 0.2271 0.0020  0.0222  0.0050  111 HIS A CG  
1701 N ND1 . HIS A 114 ? 0.2308 0.2545 0.2572 0.0084  0.0267  0.0036  111 HIS A ND1 
1702 C CD2 . HIS A 114 ? 0.2036 0.2149 0.2192 0.0011  0.0190  0.0023  111 HIS A CD2 
1703 C CE1 . HIS A 114 ? 0.2435 0.2558 0.2593 0.0108  0.0250  -0.0002 111 HIS A CE1 
1704 N NE2 . HIS A 114 ? 0.2222 0.2281 0.2324 0.0055  0.0202  -0.0005 111 HIS A NE2 
1712 N N   . VAL A 115 ? 0.2088 0.2400 0.2548 -0.0187 0.0110  0.0158  112 VAL A N   
1713 C CA  . VAL A 115 ? 0.1851 0.2209 0.2387 -0.0269 0.0083  0.0202  112 VAL A CA  
1714 C C   . VAL A 115 ? 0.2014 0.2505 0.2701 -0.0288 0.0025  0.0232  112 VAL A C   
1715 O O   . VAL A 115 ? 0.2043 0.2697 0.2889 -0.0327 0.0031  0.0283  112 VAL A O   
1716 C CB  . VAL A 115 ? 0.1983 0.2162 0.2385 -0.0330 0.0039  0.0184  112 VAL A CB  
1717 C CG1 . VAL A 115 ? 0.2270 0.2461 0.2731 -0.0437 -0.0009 0.0229  112 VAL A CG1 
1718 C CG2 . VAL A 115 ? 0.1912 0.1983 0.2201 -0.0297 0.0088  0.0166  112 VAL A CG2 
1728 N N   . LEU A 116 ? 0.2104 0.2538 0.2745 -0.0269 -0.0039 0.0211  113 LEU A N   
1729 C CA  . LEU A 116 ? 0.2151 0.2706 0.2931 -0.0279 -0.0116 0.0248  113 LEU A CA  
1730 C C   . LEU A 116 ? 0.2346 0.3095 0.3313 -0.0188 -0.0064 0.0273  113 LEU A C   
1731 O O   . LEU A 116 ? 0.2408 0.3356 0.3582 -0.0201 -0.0091 0.0325  113 LEU A O   
1732 C CB  . LEU A 116 ? 0.2216 0.2637 0.2866 -0.0275 -0.0194 0.0226  113 LEU A CB  
1733 C CG  . LEU A 116 ? 0.2435 0.2958 0.3203 -0.0283 -0.0299 0.0273  113 LEU A CG  
1734 C CD1 . LEU A 116 ? 0.3145 0.3736 0.3987 -0.0399 -0.0380 0.0312  113 LEU A CD1 
1735 C CD2 . LEU A 116 ? 0.2896 0.3252 0.3484 -0.0275 -0.0360 0.0253  113 LEU A CD2 
1747 N N   . LYS A 117 ? 0.2032 0.2730 0.2932 -0.0096 0.0014  0.0234  114 LYS A N   
1748 C CA  . LYS A 117 ? 0.2029 0.2866 0.3064 0.0010  0.0075  0.0240  114 LYS A CA  
1749 C C   . LYS A 117 ? 0.1981 0.3011 0.3158 -0.0004 0.0163  0.0273  114 LYS A C   
1750 O O   . LYS A 117 ? 0.2529 0.3779 0.3921 0.0044  0.0187  0.0309  114 LYS A O   
1751 C CB  . LYS A 117 ? 0.2192 0.2877 0.3072 0.0095  0.0127  0.0182  114 LYS A CB  
1752 C CG  . LYS A 117 ? 0.2558 0.3324 0.3530 0.0223  0.0190  0.0170  114 LYS A CG  
1753 C CD  . LYS A 117 ? 0.3304 0.3870 0.4084 0.0286  0.0221  0.0107  114 LYS A CD  
1754 C CE  . LYS A 117 ? 0.4000 0.4583 0.4833 0.0426  0.0273  0.0083  114 LYS A CE  
1755 N NZ  . LYS A 117 ? 0.3974 0.4315 0.4648 0.0480  0.0225  0.0043  114 LYS A NZ  
1769 N N   . ASP A 118 ? 0.1945 0.2907 0.3010 -0.0065 0.0215  0.0268  115 ASP A N   
1770 C CA  . ASP A 118 ? 0.2034 0.3148 0.3181 -0.0082 0.0314  0.0302  115 ASP A CA  
1771 C C   . ASP A 118 ? 0.2571 0.3799 0.3838 -0.0213 0.0282  0.0372  115 ASP A C   
1772 O O   . ASP A 118 ? 0.2102 0.3534 0.3514 -0.0237 0.0358  0.0422  115 ASP A O   
1773 C CB  . ASP A 118 ? 0.2479 0.3440 0.3416 -0.0077 0.0382  0.0270  115 ASP A CB  
1774 C CG  . ASP A 118 ? 0.2917 0.3791 0.3739 0.0037  0.0428  0.0207  115 ASP A CG  
1775 O OD1 . ASP A 118 ? 0.3735 0.4673 0.4643 0.0126  0.0437  0.0189  115 ASP A OD1 
1776 O OD2 . ASP A 118 ? 0.3935 0.4669 0.4573 0.0034  0.0450  0.0179  115 ASP A OD2 
1781 N N   . TYR A 119 ? 0.2117 0.3212 0.3317 -0.0306 0.0176  0.0375  116 TYR A N   
1782 C CA  . TYR A 119 ? 0.2276 0.3407 0.3537 -0.0450 0.0126  0.0432  116 TYR A CA  
1783 C C   . TYR A 119 ? 0.2766 0.3854 0.4047 -0.0511 -0.0014 0.0434  116 TYR A C   
1784 O O   . TYR A 119 ? 0.2277 0.3176 0.3417 -0.0608 -0.0084 0.0425  116 TYR A O   
1785 C CB  . TYR A 119 ? 0.2206 0.3112 0.3259 -0.0513 0.0145  0.0424  116 TYR A CB  
1786 C CG  . TYR A 119 ? 0.2565 0.3518 0.3586 -0.0485 0.0266  0.0444  116 TYR A CG  
1787 C CD1 . TYR A 119 ? 0.3364 0.4466 0.4495 -0.0578 0.0316  0.0521  116 TYR A CD1 
1788 C CD2 . TYR A 119 ? 0.3832 0.4676 0.4700 -0.0383 0.0324  0.0393  116 TYR A CD2 
1789 C CE1 . TYR A 119 ? 0.3764 0.4900 0.4834 -0.0564 0.0430  0.0547  116 TYR A CE1 
1790 C CE2 . TYR A 119 ? 0.3460 0.4331 0.4263 -0.0368 0.0425  0.0414  116 TYR A CE2 
1791 C CZ  . TYR A 119 ? 0.4331 0.5343 0.5226 -0.0456 0.0481  0.0491  116 TYR A CZ  
1792 O OH  . TYR A 119 ? 0.5348 0.6383 0.6153 -0.0452 0.0586  0.0520  116 TYR A OH  
1802 N N   . PRO A 120 ? 0.2002 0.3252 0.3445 -0.0455 -0.0061 0.0447  117 PRO A N   
1803 C CA  . PRO A 120 ? 0.2428 0.3621 0.3856 -0.0518 -0.0208 0.0453  117 PRO A CA  
1804 C C   . PRO A 120 ? 0.2734 0.3954 0.4212 -0.0689 -0.0293 0.0503  117 PRO A C   
1805 O O   . PRO A 120 ? 0.2689 0.3744 0.4031 -0.0770 -0.0412 0.0487  117 PRO A O   
1806 C CB  . PRO A 120 ? 0.2305 0.3715 0.3947 -0.0417 -0.0239 0.0482  117 PRO A CB  
1807 C CG  . PRO A 120 ? 0.2444 0.4105 0.4292 -0.0338 -0.0100 0.0508  117 PRO A CG  
1808 C CD  . PRO A 120 ? 0.2204 0.3695 0.3851 -0.0333 0.0014  0.0463  117 PRO A CD  
1816 N N   . GLU A 121 ? 0.2320 0.3739 0.3974 -0.0757 -0.0236 0.0566  118 GLU A N   
1817 C CA  . GLU A 121 ? 0.2639 0.4087 0.4351 -0.0944 -0.0321 0.0624  118 GLU A CA  
1818 C C   . GLU A 121 ? 0.2705 0.3781 0.4111 -0.1042 -0.0362 0.0580  118 GLU A C   
1819 O O   . GLU A 121 ? 0.3087 0.4091 0.4467 -0.1203 -0.0472 0.0608  118 GLU A O   
1820 C CB  . GLU A 121 ? 0.2569 0.4308 0.4521 -0.0998 -0.0222 0.0705  118 GLU A CB  
1821 C CG  . GLU A 121 ? 0.2848 0.4456 0.4646 -0.0980 -0.0082 0.0693  118 GLU A CG  
1822 C CD  . GLU A 121 ? 0.2679 0.4372 0.4487 -0.0793 0.0060  0.0655  118 GLU A CD  
1823 O OE1 . GLU A 121 ? 0.2918 0.4687 0.4796 -0.0660 0.0048  0.0618  118 GLU A OE1 
1824 O OE2 . GLU A 121 ? 0.4122 0.5791 0.5852 -0.0785 0.0179  0.0664  118 GLU A OE2 
1831 N N   . VAL A 122 ? 0.2374 0.3212 0.3552 -0.0951 -0.0283 0.0513  119 VAL A N   
1832 C CA  . VAL A 122 ? 0.2785 0.3273 0.3686 -0.1013 -0.0316 0.0468  119 VAL A CA  
1833 C C   . VAL A 122 ? 0.3057 0.3325 0.3754 -0.0983 -0.0398 0.0392  119 VAL A C   
1834 O O   . VAL A 122 ? 0.3014 0.2985 0.3474 -0.1023 -0.0427 0.0343  119 VAL A O   
1835 C CB  . VAL A 122 ? 0.3151 0.3478 0.3901 -0.0939 -0.0204 0.0442  119 VAL A CB  
1836 C CG1 . VAL A 122 ? 0.2957 0.3484 0.3860 -0.0964 -0.0106 0.0518  119 VAL A CG1 
1837 C CG2 . VAL A 122 ? 0.2520 0.2796 0.3178 -0.0778 -0.0148 0.0373  119 VAL A CG2 
1847 N N   . VAL A 123 ? 0.2257 0.2649 0.3027 -0.0911 -0.0433 0.0382  120 VAL A N   
1848 C CA  . VAL A 123 ? 0.2366 0.2557 0.2921 -0.0871 -0.0485 0.0314  120 VAL A CA  
1849 C C   . VAL A 123 ? 0.2699 0.2885 0.3241 -0.0982 -0.0641 0.0333  120 VAL A C   
1850 O O   . VAL A 123 ? 0.3064 0.3498 0.3825 -0.0986 -0.0703 0.0393  120 VAL A O   
1851 C CB  . VAL A 123 ? 0.2270 0.2543 0.2855 -0.0722 -0.0425 0.0292  120 VAL A CB  
1852 C CG1 . VAL A 123 ? 0.2880 0.2948 0.3229 -0.0701 -0.0469 0.0232  120 VAL A CG1 
1853 C CG2 . VAL A 123 ? 0.2350 0.2631 0.2939 -0.0630 -0.0290 0.0274  120 VAL A CG2 
1863 N N   . LYS A 124 ? 0.2877 0.2776 0.3156 -0.1065 -0.0707 0.0282  121 LYS A N   
1864 C CA  . LYS A 124 ? 0.2720 0.2548 0.2897 -0.1167 -0.0861 0.0282  121 LYS A CA  
1865 C C   . LYS A 124 ? 0.3285 0.3039 0.3308 -0.1075 -0.0868 0.0240  121 LYS A C   
1866 O O   . LYS A 124 ? 0.3372 0.3263 0.3481 -0.1078 -0.0964 0.0284  121 LYS A O   
1867 C CB  . LYS A 124 ? 0.3477 0.2984 0.3388 -0.1297 -0.0924 0.0233  121 LYS A CB  
1868 C CG  . LYS A 124 ? 0.4295 0.3663 0.4018 -0.1419 -0.1097 0.0218  121 LYS A CG  
1869 C CD  . LYS A 124 ? 0.5208 0.4390 0.4810 -0.1570 -0.1176 0.0215  121 LYS A CD  
1870 C CE  . LYS A 124 ? 0.6018 0.5116 0.5456 -0.1646 -0.1317 0.0213  121 LYS A CE  
1871 N NZ  . LYS A 124 ? 0.7564 0.6252 0.6619 -0.1689 -0.1325 0.0125  121 LYS A NZ  
1885 N N   . LYS A 125 ? 0.3116 0.2653 0.2908 -0.0998 -0.0772 0.0161  122 LYS A N   
1886 C CA  . LYS A 125 ? 0.2993 0.2456 0.2627 -0.0914 -0.0745 0.0121  122 LYS A CA  
1887 C C   . LYS A 125 ? 0.2847 0.2278 0.2456 -0.0792 -0.0588 0.0076  122 LYS A C   
1888 O O   . LYS A 125 ? 0.3093 0.2446 0.2689 -0.0783 -0.0519 0.0052  122 LYS A O   
1889 C CB  . LYS A 125 ? 0.3609 0.2791 0.2899 -0.0984 -0.0811 0.0057  122 LYS A CB  
1890 C CG  . LYS A 125 ? 0.4199 0.3371 0.3447 -0.1120 -0.0990 0.0095  122 LYS A CG  
1891 C CD  . LYS A 125 ? 0.3952 0.3300 0.3305 -0.1085 -0.1062 0.0159  122 LYS A CD  
1892 C CE  . LYS A 125 ? 0.5240 0.4500 0.4425 -0.1207 -0.1249 0.0180  122 LYS A CE  
1893 N NZ  . LYS A 125 ? 0.5215 0.4736 0.4646 -0.1180 -0.1353 0.0281  122 LYS A NZ  
1907 N N   . ILE A 126 ? 0.2798 0.2271 0.2386 -0.0707 -0.0542 0.0070  123 ILE A N   
1908 C CA  . ILE A 126 ? 0.2643 0.2121 0.2232 -0.0603 -0.0409 0.0037  123 ILE A CA  
1909 C C   . ILE A 126 ? 0.2736 0.2134 0.2150 -0.0569 -0.0383 0.0007  123 ILE A C   
1910 O O   . ILE A 126 ? 0.2967 0.2374 0.2336 -0.0595 -0.0459 0.0038  123 ILE A O   
1911 C CB  . ILE A 126 ? 0.2441 0.2138 0.2293 -0.0540 -0.0364 0.0087  123 ILE A CB  
1912 C CG1 . ILE A 126 ? 0.2564 0.2262 0.2422 -0.0455 -0.0243 0.0057  123 ILE A CG1 
1913 C CG2 . ILE A 126 ? 0.2746 0.2569 0.2700 -0.0505 -0.0412 0.0132  123 ILE A CG2 
1914 C CD1 . ILE A 126 ? 0.2551 0.2421 0.2623 -0.0419 -0.0200 0.0099  123 ILE A CD1 
1926 N N   . ALA A 127 ? 0.2648 0.1984 0.1975 -0.0509 -0.0273 -0.0044 124 ALA A N   
1927 C CA  . ALA A 127 ? 0.2860 0.2153 0.2041 -0.0483 -0.0221 -0.0068 124 ALA A CA  
1928 C C   . ALA A 127 ? 0.2604 0.2009 0.1901 -0.0404 -0.0120 -0.0069 124 ALA A C   
1929 O O   . ALA A 127 ? 0.2713 0.2148 0.2098 -0.0358 -0.0063 -0.0086 124 ALA A O   
1930 C CB  . ALA A 127 ? 0.3334 0.2439 0.2257 -0.0502 -0.0187 -0.0139 124 ALA A CB  
1936 N N   . PHE A 128 ? 0.2751 0.2204 0.2042 -0.0397 -0.0113 -0.0044 125 PHE A N   
1937 C CA  . PHE A 128 ? 0.2557 0.2106 0.1938 -0.0347 -0.0038 -0.0040 125 PHE A CA  
1938 C C   . PHE A 128 ? 0.2837 0.2349 0.2063 -0.0359 0.0031  -0.0066 125 PHE A C   
1939 O O   . PHE A 128 ? 0.2976 0.2440 0.2079 -0.0406 0.0007  -0.0043 125 PHE A O   
1940 C CB  . PHE A 128 ? 0.2524 0.2137 0.2012 -0.0336 -0.0082 0.0012  125 PHE A CB  
1941 C CG  . PHE A 128 ? 0.2535 0.2217 0.2186 -0.0316 -0.0139 0.0042  125 PHE A CG  
1942 C CD1 . PHE A 128 ? 0.2485 0.2222 0.2243 -0.0298 -0.0113 0.0031  125 PHE A CD1 
1943 C CD2 . PHE A 128 ? 0.2687 0.2387 0.2390 -0.0312 -0.0215 0.0089  125 PHE A CD2 
1944 C CE1 . PHE A 128 ? 0.2455 0.2286 0.2370 -0.0289 -0.0147 0.0066  125 PHE A CE1 
1945 C CE2 . PHE A 128 ? 0.2773 0.2581 0.2659 -0.0281 -0.0252 0.0119  125 PHE A CE2 
1946 C CZ  . PHE A 128 ? 0.2530 0.2414 0.2522 -0.0277 -0.0211 0.0107  125 PHE A CZ  
1956 N N   . HIS A 129 ? 0.2565 0.2105 0.1798 -0.0316 0.0120  -0.0109 126 HIS A N   
1957 C CA  . HIS A 129 ? 0.2496 0.2052 0.1622 -0.0314 0.0211  -0.0137 126 HIS A CA  
1958 C C   . HIS A 129 ? 0.2849 0.2557 0.2106 -0.0307 0.0254  -0.0106 126 HIS A C   
1959 O O   . HIS A 129 ? 0.2867 0.2673 0.2281 -0.0255 0.0275  -0.0108 126 HIS A O   
1960 C CB  . HIS A 129 ? 0.2700 0.2212 0.1780 -0.0253 0.0282  -0.0201 126 HIS A CB  
1961 C CG  . HIS A 129 ? 0.2883 0.2435 0.1867 -0.0233 0.0394  -0.0236 126 HIS A CG  
1962 N ND1 . HIS A 129 ? 0.3301 0.3025 0.2433 -0.0171 0.0482  -0.0240 126 HIS A ND1 
1963 C CD2 . HIS A 129 ? 0.3332 0.2794 0.2090 -0.0268 0.0437  -0.0266 126 HIS A CD2 
1964 C CE1 . HIS A 129 ? 0.3431 0.3194 0.2459 -0.0163 0.0585  -0.0269 126 HIS A CE1 
1965 N NE2 . HIS A 129 ? 0.3791 0.3384 0.2574 -0.0221 0.0567  -0.0290 126 HIS A NE2 
1973 N N   . GLU A 130 ? 0.3080 0.2791 0.2261 -0.0370 0.0254  -0.0072 127 GLU A N   
1974 C CA  . GLU A 130 ? 0.2881 0.2713 0.2143 -0.0396 0.0292  -0.0041 127 GLU A CA  
1975 C C   . GLU A 130 ? 0.2631 0.2527 0.2070 -0.0364 0.0253  -0.0026 127 GLU A C   
1976 O O   . GLU A 130 ? 0.2687 0.2712 0.2251 -0.0330 0.0296  -0.0036 127 GLU A O   
1977 C CB  . GLU A 130 ? 0.3168 0.3130 0.2441 -0.0379 0.0410  -0.0069 127 GLU A CB  
1978 C CG  . GLU A 130 ? 0.3898 0.3779 0.2948 -0.0417 0.0464  -0.0087 127 GLU A CG  
1979 C CD  . GLU A 130 ? 0.3809 0.3843 0.2848 -0.0447 0.0585  -0.0082 127 GLU A CD  
1980 O OE1 . GLU A 130 ? 0.3668 0.3898 0.2901 -0.0423 0.0633  -0.0073 127 GLU A OE1 
1981 O OE2 . GLU A 130 ? 0.3744 0.3714 0.2576 -0.0497 0.0635  -0.0085 127 GLU A OE2 
1988 N N   . PRO A 131 ? 0.2569 0.2381 0.2016 -0.0371 0.0170  0.0001  128 PRO A N   
1989 C CA  . PRO A 131 ? 0.2626 0.2474 0.2204 -0.0334 0.0141  0.0007  128 PRO A CA  
1990 C C   . PRO A 131 ? 0.2836 0.2703 0.2422 -0.0382 0.0139  0.0030  128 PRO A C   
1991 O O   . PRO A 131 ? 0.2987 0.2780 0.2470 -0.0448 0.0121  0.0062  128 PRO A O   
1992 C CB  . PRO A 131 ? 0.3223 0.2978 0.2798 -0.0315 0.0065  0.0024  128 PRO A CB  
1993 C CG  . PRO A 131 ? 0.3520 0.3174 0.2948 -0.0370 0.0027  0.0051  128 PRO A CG  
1994 C CD  . PRO A 131 ? 0.3172 0.2852 0.2503 -0.0399 0.0098  0.0024  128 PRO A CD  
2002 N N   . PRO A 132 ? 0.2383 0.2333 0.2069 -0.0361 0.0149  0.0020  129 PRO A N   
2003 C CA  . PRO A 132 ? 0.2448 0.2402 0.2129 -0.0425 0.0133  0.0039  129 PRO A CA  
2004 C C   . PRO A 132 ? 0.2635 0.2473 0.2303 -0.0403 0.0075  0.0035  129 PRO A C   
2005 O O   . PRO A 132 ? 0.2852 0.2671 0.2508 -0.0447 0.0053  0.0037  129 PRO A O   
2006 C CB  . PRO A 132 ? 0.2951 0.3089 0.2746 -0.0419 0.0175  0.0029  129 PRO A CB  
2007 C CG  . PRO A 132 ? 0.2782 0.2944 0.2641 -0.0321 0.0184  0.0002  129 PRO A CG  
2008 C CD  . PRO A 132 ? 0.2728 0.2785 0.2516 -0.0298 0.0183  -0.0006 129 PRO A CD  
2016 N N   . ILE A 133 ? 0.2378 0.2141 0.2047 -0.0336 0.0052  0.0028  130 ILE A N   
2017 C CA  . ILE A 133 ? 0.2524 0.2183 0.2182 -0.0294 0.0016  0.0019  130 ILE A CA  
2018 C C   . ILE A 133 ? 0.2581 0.2068 0.2126 -0.0340 -0.0033 0.0042  130 ILE A C   
2019 O O   . ILE A 133 ? 0.2893 0.2322 0.2371 -0.0384 -0.0052 0.0077  130 ILE A O   
2020 C CB  . ILE A 133 ? 0.2896 0.2565 0.2618 -0.0211 0.0013  0.0015  130 ILE A CB  
2021 C CG1 . ILE A 133 ? 0.3121 0.2721 0.2850 -0.0145 0.0003  -0.0003 130 ILE A CG1 
2022 C CG2 . ILE A 133 ? 0.2728 0.2354 0.2421 -0.0222 -0.0023 0.0045  130 ILE A CG2 
2023 C CD1 . ILE A 133 ? 0.2955 0.2644 0.2790 -0.0071 0.0027  -0.0007 130 ILE A CD1 
2035 N N   . ASN A 134 ? 0.2493 0.1868 0.1990 -0.0333 -0.0056 0.0022  131 ASN A N   
2036 C CA  . ASN A 134 ? 0.2798 0.1960 0.2166 -0.0377 -0.0109 0.0041  131 ASN A CA  
2037 C C   . ASN A 134 ? 0.2964 0.1952 0.2295 -0.0274 -0.0139 0.0019  131 ASN A C   
2038 O O   . ASN A 134 ? 0.3069 0.1836 0.2281 -0.0290 -0.0192 0.0037  131 ASN A O   
2039 C CB  . ASN A 134 ? 0.2729 0.1864 0.2034 -0.0489 -0.0122 0.0037  131 ASN A CB  
2040 C CG  . ASN A 134 ? 0.2956 0.2077 0.2254 -0.0455 -0.0123 -0.0015 131 ASN A CG  
2041 O OD1 . ASN A 134 ? 0.3222 0.2182 0.2455 -0.0371 -0.0136 -0.0051 131 ASN A OD1 
2042 N ND2 . ASN A 134 ? 0.2899 0.2187 0.2256 -0.0513 -0.0109 -0.0021 131 ASN A ND2 
2049 N N   . THR A 135 ? 0.2790 0.1867 0.2217 -0.0166 -0.0103 -0.0014 132 THR A N   
2050 C CA  . THR A 135 ? 0.2814 0.1748 0.2204 -0.0061 -0.0106 -0.0050 132 THR A CA  
2051 C C   . THR A 135 ? 0.3076 0.1845 0.2437 0.0000  -0.0160 -0.0019 132 THR A C   
2052 O O   . THR A 135 ? 0.3515 0.2060 0.2771 0.0054  -0.0184 -0.0043 132 THR A O   
2053 C CB  . THR A 135 ? 0.2985 0.2090 0.2504 0.0036  -0.0043 -0.0077 132 THR A CB  
2054 O OG1 . THR A 135 ? 0.2923 0.2186 0.2477 -0.0023 -0.0007 -0.0085 132 THR A OG1 
2055 C CG2 . THR A 135 ? 0.3269 0.2252 0.2729 0.0140  -0.0014 -0.0131 132 THR A CG2 
2063 N N   . PHE A 136 ? 0.2893 0.1753 0.2332 -0.0002 -0.0187 0.0035  133 PHE A N   
2064 C CA  . PHE A 136 ? 0.3449 0.2191 0.2887 0.0066  -0.0254 0.0080  133 PHE A CA  
2065 C C   . PHE A 136 ? 0.3634 0.2178 0.2905 -0.0036 -0.0325 0.0135  133 PHE A C   
2066 O O   . PHE A 136 ? 0.3857 0.2283 0.3101 0.0008  -0.0398 0.0187  133 PHE A O   
2067 C CB  . PHE A 136 ? 0.3140 0.2097 0.2751 0.0113  -0.0262 0.0114  133 PHE A CB  
2068 C CG  . PHE A 136 ? 0.3034 0.2140 0.2653 0.0006  -0.0247 0.0130  133 PHE A CG  
2069 C CD1 . PHE A 136 ? 0.3256 0.2279 0.2747 -0.0095 -0.0293 0.0176  133 PHE A CD1 
2070 C CD2 . PHE A 136 ? 0.3063 0.2370 0.2793 0.0003  -0.0182 0.0100  133 PHE A CD2 
2071 C CE1 . PHE A 136 ? 0.3170 0.2316 0.2648 -0.0181 -0.0261 0.0178  133 PHE A CE1 
2072 C CE2 . PHE A 136 ? 0.3443 0.2851 0.3163 -0.0082 -0.0165 0.0106  133 PHE A CE2 
2073 C CZ  . PHE A 136 ? 0.3293 0.2622 0.2885 -0.0167 -0.0200 0.0139  133 PHE A CZ  
2083 N N   . LEU A 137 ? 0.3281 0.1794 0.2445 -0.0170 -0.0309 0.0132  134 LEU A N   
2084 C CA  . LEU A 137 ? 0.3576 0.1920 0.2579 -0.0289 -0.0362 0.0194  134 LEU A CA  
2085 C C   . LEU A 137 ? 0.3693 0.1704 0.2538 -0.0277 -0.0423 0.0197  134 LEU A C   
2086 O O   . LEU A 137 ? 0.4087 0.2005 0.2914 -0.0221 -0.0406 0.0132  134 LEU A O   
2087 C CB  . LEU A 137 ? 0.3551 0.2014 0.2522 -0.0442 -0.0314 0.0196  134 LEU A CB  
2088 C CG  . LEU A 137 ? 0.3163 0.1913 0.2256 -0.0456 -0.0248 0.0188  134 LEU A CG  
2089 C CD1 . LEU A 137 ? 0.3525 0.2400 0.2612 -0.0584 -0.0195 0.0187  134 LEU A CD1 
2090 C CD2 . LEU A 137 ? 0.3473 0.2236 0.2539 -0.0453 -0.0278 0.0238  134 LEU A CD2 
2102 N N   A PRO A 138 ? 0.4057 0.1854 0.2758 -0.0330 -0.0498 0.0270  135 PRO A N   
2103 N N   B PRO A 138 ? 0.4064 0.1862 0.2761 -0.0338 -0.0496 0.0270  135 PRO A N   
2104 C CA  A PRO A 138 ? 0.4790 0.2218 0.3305 -0.0340 -0.0563 0.0277  135 PRO A CA  
2105 C CA  B PRO A 138 ? 0.4790 0.2218 0.3304 -0.0342 -0.0563 0.0278  135 PRO A CA  
2106 C C   A PRO A 138 ? 0.4737 0.2094 0.3154 -0.0479 -0.0541 0.0240  135 PRO A C   
2107 C C   B PRO A 138 ? 0.4749 0.2093 0.3155 -0.0485 -0.0544 0.0245  135 PRO A C   
2108 O O   A PRO A 138 ? 0.5270 0.2352 0.3564 -0.0449 -0.0574 0.0197  135 PRO A O   
2109 O O   B PRO A 138 ? 0.5272 0.2317 0.3539 -0.0470 -0.0586 0.0212  135 PRO A O   
2110 C CB  A PRO A 138 ? 0.4909 0.2158 0.3276 -0.0417 -0.0644 0.0384  135 PRO A CB  
2111 C CB  B PRO A 138 ? 0.4910 0.2159 0.3280 -0.0411 -0.0645 0.0384  135 PRO A CB  
2112 C CG  A PRO A 138 ? 0.4913 0.2406 0.3409 -0.0363 -0.0640 0.0417  135 PRO A CG  
2113 C CG  B PRO A 138 ? 0.4064 0.1588 0.2479 -0.0531 -0.0594 0.0419  135 PRO A CG  
2114 C CD  A PRO A 138 ? 0.4162 0.2006 0.2841 -0.0364 -0.0537 0.0349  135 PRO A CD  
2115 C CD  B PRO A 138 ? 0.4482 0.2340 0.3128 -0.0430 -0.0519 0.0350  135 PRO A CD  
2130 N N   . ASP A 139 ? 0.4277 0.1871 0.2741 -0.0626 -0.0489 0.0255  136 ASP A N   
2131 C CA  . ASP A 139 ? 0.4344 0.1947 0.2760 -0.0775 -0.0476 0.0233  136 ASP A CA  
2132 C C   . ASP A 139 ? 0.3986 0.1879 0.2570 -0.0732 -0.0405 0.0159  136 ASP A C   
2133 O O   . ASP A 139 ? 0.3858 0.1935 0.2493 -0.0854 -0.0376 0.0160  136 ASP A O   
2134 C CB  . ASP A 139 ? 0.4549 0.2229 0.2913 -0.0974 -0.0468 0.0316  136 ASP A CB  
2135 C CG  . ASP A 139 ? 0.4338 0.2346 0.2835 -0.0969 -0.0395 0.0344  136 ASP A CG  
2136 O OD1 . ASP A 139 ? 0.4643 0.2757 0.3242 -0.0823 -0.0377 0.0318  136 ASP A OD1 
2137 O OD2 . ASP A 139 ? 0.4478 0.2618 0.2961 -0.1119 -0.0355 0.0394  136 ASP A OD2 
2142 N N   A SER A 140 ? 0.3930 0.1876 0.2607 -0.0557 -0.0378 0.0102  137 SER A N   
2143 N N   B SER A 140 ? 0.3955 0.1894 0.2628 -0.0558 -0.0378 0.0101  137 SER A N   
2144 C CA  A SER A 140 ? 0.3488 0.1673 0.2295 -0.0513 -0.0315 0.0040  137 SER A CA  
2145 C CA  B SER A 140 ? 0.3502 0.1688 0.2310 -0.0514 -0.0315 0.0040  137 SER A CA  
2146 C C   A SER A 140 ? 0.3669 0.1791 0.2390 -0.0616 -0.0334 0.0001  137 SER A C   
2147 C C   B SER A 140 ? 0.3693 0.1814 0.2414 -0.0612 -0.0334 -0.0001 137 SER A C   
2148 O O   A SER A 140 ? 0.3765 0.2133 0.2587 -0.0676 -0.0303 -0.0006 137 SER A O   
2149 O O   B SER A 140 ? 0.3766 0.2132 0.2588 -0.0668 -0.0301 -0.0010 137 SER A O   
2150 C CB  A SER A 140 ? 0.3443 0.1624 0.2317 -0.0324 -0.0287 -0.0012 137 SER A CB  
2151 C CB  B SER A 140 ? 0.3466 0.1660 0.2347 -0.0324 -0.0285 -0.0010 137 SER A CB  
2152 O OG  A SER A 140 ? 0.3103 0.1462 0.2053 -0.0294 -0.0231 -0.0068 137 SER A OG  
2153 O OG  B SER A 140 ? 0.4688 0.2583 0.3428 -0.0249 -0.0318 -0.0055 137 SER A OG  
2164 N N   . THR A 141 ? 0.3737 0.1518 0.2264 -0.0631 -0.0395 -0.0026 138 THR A N   
2165 C CA  . THR A 141 ? 0.3989 0.1676 0.2402 -0.0737 -0.0431 -0.0069 138 THR A CA  
2166 C C   . THR A 141 ? 0.4209 0.2086 0.2679 -0.0943 -0.0450 -0.0011 138 THR A C   
2167 O O   . THR A 141 ? 0.4263 0.2294 0.2777 -0.1010 -0.0455 -0.0036 138 THR A O   
2168 C CB  . THR A 141 ? 0.4957 0.2189 0.3116 -0.0736 -0.0503 -0.0103 138 THR A CB  
2169 O OG1 . THR A 141 ? 0.5479 0.2592 0.3616 -0.0521 -0.0465 -0.0172 138 THR A OG1 
2170 C CG2 . THR A 141 ? 0.5565 0.2651 0.3563 -0.0886 -0.0565 -0.0145 138 THR A CG2 
2178 N N   . TYR A 142 ? 0.3924 0.1799 0.2391 -0.1046 -0.0460 0.0070  139 TYR A N   
2179 C CA  . TYR A 142 ? 0.4092 0.2186 0.2635 -0.1241 -0.0459 0.0130  139 TYR A CA  
2180 C C   . TYR A 142 ? 0.3735 0.2258 0.2517 -0.1202 -0.0384 0.0122  139 TYR A C   
2181 O O   . TYR A 142 ? 0.3708 0.2427 0.2576 -0.1303 -0.0395 0.0125  139 TYR A O   
2182 C CB  . TYR A 142 ? 0.4220 0.2272 0.2719 -0.1335 -0.0455 0.0222  139 TYR A CB  
2183 C CG  . TYR A 142 ? 0.4262 0.2618 0.2881 -0.1513 -0.0415 0.0290  139 TYR A CG  
2184 C CD1 . TYR A 142 ? 0.4273 0.2628 0.2854 -0.1673 -0.0462 0.0320  139 TYR A CD1 
2185 C CD2 . TYR A 142 ? 0.3999 0.2697 0.2793 -0.1466 -0.0319 0.0311  139 TYR A CD2 
2186 C CE1 . TYR A 142 ? 0.4160 0.2857 0.2891 -0.1799 -0.0412 0.0382  139 TYR A CE1 
2187 C CE2 . TYR A 142 ? 0.4176 0.3170 0.3091 -0.1606 -0.0264 0.0368  139 TYR A CE2 
2188 C CZ  . TYR A 142 ? 0.4013 0.3024 0.2912 -0.1768 -0.0308 0.0405  139 TYR A CZ  
2189 O OH  . TYR A 142 ? 0.4724 0.4088 0.3784 -0.1864 -0.0242 0.0456  139 TYR A OH  
2199 N N   . TRP A 143 ? 0.3565 0.2227 0.2454 -0.1054 -0.0316 0.0115  140 TRP A N   
2200 C CA  . TRP A 143 ? 0.3030 0.2055 0.2127 -0.1004 -0.0243 0.0110  140 TRP A CA  
2201 C C   . TRP A 143 ? 0.3155 0.2252 0.2301 -0.0931 -0.0250 0.0047  140 TRP A C   
2202 O O   . TRP A 143 ? 0.3274 0.2628 0.2555 -0.0963 -0.0235 0.0052  140 TRP A O   
2203 C CB  . TRP A 143 ? 0.3043 0.2139 0.2199 -0.0889 -0.0185 0.0120  140 TRP A CB  
2204 C CG  . TRP A 143 ? 0.3439 0.2502 0.2530 -0.0985 -0.0176 0.0188  140 TRP A CG  
2205 C CD1 . TRP A 143 ? 0.3623 0.2435 0.2568 -0.0978 -0.0216 0.0222  140 TRP A CD1 
2206 C CD2 . TRP A 143 ? 0.3660 0.2949 0.2822 -0.1101 -0.0122 0.0237  140 TRP A CD2 
2207 N NE1 . TRP A 143 ? 0.3787 0.2632 0.2675 -0.1099 -0.0195 0.0293  140 TRP A NE1 
2208 C CE2 . TRP A 143 ? 0.3825 0.2971 0.2847 -0.1176 -0.0127 0.0299  140 TRP A CE2 
2209 C CE3 . TRP A 143 ? 0.4371 0.3975 0.3702 -0.1142 -0.0067 0.0237  140 TRP A CE3 
2210 C CZ2 . TRP A 143 ? 0.4520 0.3836 0.3554 -0.1296 -0.0062 0.0357  140 TRP A CZ2 
2211 C CZ3 . TRP A 143 ? 0.4147 0.3937 0.3521 -0.1248 -0.0003 0.0291  140 TRP A CZ3 
2212 C CH2 . TRP A 143 ? 0.4273 0.3920 0.3492 -0.1327 0.0007  0.0348  140 TRP A CH2 
2223 N N   . LYS A 144 ? 0.3255 0.2123 0.2284 -0.0831 -0.0273 -0.0009 141 LYS A N   
2224 C CA  . LYS A 144 ? 0.3535 0.2430 0.2555 -0.0773 -0.0278 -0.0067 141 LYS A CA  
2225 C C   . LYS A 144 ? 0.3635 0.2534 0.2600 -0.0922 -0.0349 -0.0068 141 LYS A C   
2226 O O   . LYS A 144 ? 0.3463 0.2573 0.2521 -0.0932 -0.0354 -0.0072 141 LYS A O   
2227 C CB  . LYS A 144 ? 0.3773 0.2401 0.2649 -0.0646 -0.0277 -0.0129 141 LYS A CB  
2228 C CG  . LYS A 144 ? 0.4408 0.3023 0.3217 -0.0592 -0.0273 -0.0193 141 LYS A CG  
2229 C CD  . LYS A 144 ? 0.4890 0.3202 0.3517 -0.0486 -0.0268 -0.0261 141 LYS A CD  
2230 C CE  . LYS A 144 ? 0.6198 0.4526 0.4750 -0.0415 -0.0236 -0.0325 141 LYS A CE  
2231 N NZ  . LYS A 144 ? 0.8046 0.6223 0.6404 -0.0536 -0.0317 -0.0362 141 LYS A NZ  
2245 N N   . ASP A 145 ? 0.3582 0.2236 0.2390 -0.1045 -0.0417 -0.0058 142 ASP A N   
2246 C CA  . ASP A 145 ? 0.3855 0.2497 0.2602 -0.1212 -0.0503 -0.0055 142 ASP A CA  
2247 C C   . ASP A 145 ? 0.3794 0.2830 0.2774 -0.1323 -0.0494 0.0014  142 ASP A C   
2248 O O   . ASP A 145 ? 0.3805 0.2990 0.2837 -0.1405 -0.0552 0.0015  142 ASP A O   
2249 C CB  . ASP A 145 ? 0.4383 0.2659 0.2908 -0.1340 -0.0580 -0.0048 142 ASP A CB  
2250 C CG  . ASP A 145 ? 0.5427 0.3283 0.3693 -0.1233 -0.0607 -0.0135 142 ASP A CG  
2251 O OD1 . ASP A 145 ? 0.5684 0.3562 0.3942 -0.1080 -0.0563 -0.0200 142 ASP A OD1 
2252 O OD2 . ASP A 145 ? 0.5798 0.3307 0.3868 -0.1297 -0.0664 -0.0133 142 ASP A OD2 
2257 N N   . LYS A 146 ? 0.3508 0.2715 0.2625 -0.1329 -0.0425 0.0073  143 LYS A N   
2258 C CA  . LYS A 146 ? 0.3345 0.2945 0.2697 -0.1403 -0.0390 0.0133  143 LYS A CA  
2259 C C   . LYS A 146 ? 0.3310 0.3181 0.2834 -0.1275 -0.0355 0.0109  143 LYS A C   
2260 O O   . LYS A 146 ? 0.3067 0.3205 0.2745 -0.1336 -0.0386 0.0136  143 LYS A O   
2261 C CB  . LYS A 146 ? 0.3366 0.3060 0.2783 -0.1411 -0.0304 0.0187  143 LYS A CB  
2262 C CG  . LYS A 146 ? 0.3869 0.3371 0.3148 -0.1583 -0.0340 0.0242  143 LYS A CG  
2263 C CD  . LYS A 146 ? 0.4004 0.3744 0.3405 -0.1788 -0.0370 0.0304  143 LYS A CD  
2264 C CE  . LYS A 146 ? 0.4478 0.4057 0.3745 -0.1901 -0.0383 0.0363  143 LYS A CE  
2265 N NZ  . LYS A 146 ? 0.5312 0.5127 0.4698 -0.2039 -0.0407 0.0416  143 LYS A NZ  
2279 N N   . ASN A 147 ? 0.3112 0.2912 0.2612 -0.1101 -0.0302 0.0066  144 ASN A N   
2280 C CA  . ASN A 147 ? 0.2907 0.2908 0.2532 -0.0986 -0.0277 0.0049  144 ASN A CA  
2281 C C   . ASN A 147 ? 0.3260 0.3220 0.2809 -0.1021 -0.0367 0.0022  144 ASN A C   
2282 O O   . ASN A 147 ? 0.3015 0.3220 0.2705 -0.1024 -0.0393 0.0045  144 ASN A O   
2283 C CB  . ASN A 147 ? 0.2721 0.2624 0.2312 -0.0822 -0.0213 0.0012  144 ASN A CB  
2284 C CG  . ASN A 147 ? 0.2750 0.2732 0.2424 -0.0776 -0.0133 0.0036  144 ASN A CG  
2285 O OD1 . ASN A 147 ? 0.3095 0.3271 0.2885 -0.0834 -0.0100 0.0077  144 ASN A OD1 
2286 N ND2 . ASN A 147 ? 0.2975 0.2817 0.2588 -0.0672 -0.0101 0.0011  144 ASN A ND2 
2293 N N   . ASP A 148 ? 0.3096 0.2732 0.2408 -0.1041 -0.0418 -0.0029 145 ASP A N   
2294 C CA  . ASP A 148 ? 0.3764 0.3313 0.2944 -0.1074 -0.0502 -0.0066 145 ASP A CA  
2295 C C   . ASP A 148 ? 0.3595 0.3314 0.2855 -0.1251 -0.0601 -0.0020 145 ASP A C   
2296 O O   . ASP A 148 ? 0.3646 0.3497 0.2933 -0.1272 -0.0670 -0.0015 145 ASP A O   
2297 C CB  . ASP A 148 ? 0.3891 0.3031 0.2776 -0.1066 -0.0531 -0.0138 145 ASP A CB  
2298 C CG  . ASP A 148 ? 0.4763 0.3774 0.3586 -0.0880 -0.0440 -0.0186 145 ASP A CG  
2299 O OD1 . ASP A 148 ? 0.4656 0.3871 0.3624 -0.0769 -0.0371 -0.0172 145 ASP A OD1 
2300 O OD2 . ASP A 148 ? 0.5237 0.3933 0.3864 -0.0844 -0.0438 -0.0238 145 ASP A OD2 
2305 N N   . ASP A 149 ? 0.3467 0.3187 0.2761 -0.1391 -0.0616 0.0023  146 ASP A N   
2306 C CA  . ASP A 149 ? 0.3530 0.3415 0.2907 -0.1587 -0.0715 0.0074  146 ASP A CA  
2307 C C   . ASP A 149 ? 0.3453 0.3820 0.3165 -0.1573 -0.0688 0.0141  146 ASP A C   
2308 O O   . ASP A 149 ? 0.3455 0.4021 0.3264 -0.1665 -0.0787 0.0172  146 ASP A O   
2309 C CB  . ASP A 149 ? 0.4174 0.3906 0.3478 -0.1755 -0.0733 0.0109  146 ASP A CB  
2310 C CG  . ASP A 149 ? 0.5954 0.5180 0.4913 -0.1762 -0.0782 0.0045  146 ASP A CG  
2311 O OD1 . ASP A 149 ? 0.7321 0.6343 0.6095 -0.1697 -0.0827 -0.0031 146 ASP A OD1 
2312 O OD2 . ASP A 149 ? 0.6618 0.5651 0.5483 -0.1814 -0.0769 0.0073  146 ASP A OD2 
2317 N N   . ILE A 150 ? 0.3113 0.3665 0.2998 -0.1450 -0.0562 0.0163  147 ILE A N   
2318 C CA  . ILE A 150 ? 0.3643 0.4628 0.3838 -0.1407 -0.0524 0.0217  147 ILE A CA  
2319 C C   . ILE A 150 ? 0.3059 0.4126 0.3289 -0.1284 -0.0568 0.0199  147 ILE A C   
2320 O O   . ILE A 150 ? 0.3191 0.4557 0.3617 -0.1309 -0.0628 0.0246  147 ILE A O   
2321 C CB  . ILE A 150 ? 0.3399 0.4502 0.3715 -0.1305 -0.0375 0.0230  147 ILE A CB  
2322 C CG1 . ILE A 150 ? 0.4939 0.6066 0.5266 -0.1460 -0.0341 0.0277  147 ILE A CG1 
2323 C CG2 . ILE A 150 ? 0.4709 0.6190 0.5304 -0.1192 -0.0321 0.0261  147 ILE A CG2 
2324 C CD1 . ILE A 150 ? 0.5071 0.6035 0.5295 -0.1398 -0.0233 0.0265  147 ILE A CD1 
2336 N N   . VAL A 151 ? 0.3055 0.3864 0.3096 -0.1156 -0.0544 0.0139  148 VAL A N   
2337 C CA  . VAL A 151 ? 0.3247 0.4098 0.3278 -0.1056 -0.0587 0.0130  148 VAL A CA  
2338 C C   . VAL A 151 ? 0.3197 0.4009 0.3117 -0.1183 -0.0738 0.0132  148 VAL A C   
2339 O O   . VAL A 151 ? 0.3536 0.4560 0.3571 -0.1171 -0.0814 0.0172  148 VAL A O   
2340 C CB  . VAL A 151 ? 0.3307 0.3892 0.3149 -0.0912 -0.0519 0.0070  148 VAL A CB  
2341 C CG1 . VAL A 151 ? 0.3285 0.3874 0.3060 -0.0841 -0.0572 0.0068  148 VAL A CG1 
2342 C CG2 . VAL A 151 ? 0.3145 0.3789 0.3105 -0.0793 -0.0391 0.0074  148 VAL A CG2 
2352 N N   . HIS A 152 ? 0.3834 0.4353 0.3514 -0.1305 -0.0795 0.0090  149 HIS A N   
2353 C CA  . HIS A 152 ? 0.4174 0.4613 0.3704 -0.1443 -0.0950 0.0082  149 HIS A CA  
2354 C C   . HIS A 152 ? 0.3917 0.4738 0.3722 -0.1581 -0.1044 0.0168  149 HIS A C   
2355 O O   . HIS A 152 ? 0.4406 0.5345 0.4229 -0.1616 -0.1162 0.0194  149 HIS A O   
2356 C CB  . HIS A 152 ? 0.4826 0.4861 0.4052 -0.1561 -0.0992 0.0020  149 HIS A CB  
2357 C CG  . HIS A 152 ? 0.5898 0.5781 0.4921 -0.1679 -0.1133 0.0000  149 HIS A CG  
2358 N ND1 . HIS A 152 ? 0.6284 0.6228 0.5372 -0.1824 -0.1201 0.0051  149 HIS A ND1 
2359 C CD2 . HIS A 152 ? 0.5854 0.5523 0.4613 -0.1635 -0.1187 -0.0058 149 HIS A CD2 
2360 C CE1 . HIS A 152 ? 0.5238 0.5007 0.4113 -0.1872 -0.1302 0.0022  149 HIS A CE1 
2361 N NE2 . HIS A 152 ? 0.5903 0.5498 0.4571 -0.1756 -0.1290 -0.0045 149 HIS A NE2 
2369 N N   . GLN A 153 ? 0.3752 0.4768 0.3770 -0.1653 -0.0985 0.0218  150 GLN A N   
2370 C CA  . GLN A 153 ? 0.3634 0.4997 0.3922 -0.1730 -0.1020 0.0299  150 GLN A CA  
2371 C C   . GLN A 153 ? 0.3952 0.5712 0.4531 -0.1609 -0.1026 0.0350  150 GLN A C   
2372 O O   . GLN A 153 ? 0.4030 0.5985 0.4732 -0.1639 -0.1120 0.0396  150 GLN A O   
2373 C CB  . GLN A 153 ? 0.4643 0.6112 0.5070 -0.1793 -0.0914 0.0339  150 GLN A CB  
2374 C CG  . GLN A 153 ? 0.5834 0.7782 0.6637 -0.1785 -0.0875 0.0420  150 GLN A CG  
2375 C CD  . GLN A 153 ? 0.6921 0.8976 0.7837 -0.1822 -0.0742 0.0453  150 GLN A CD  
2376 O OE1 . GLN A 153 ? 0.6634 0.9039 0.7829 -0.1741 -0.0645 0.0493  150 GLN A OE1 
2377 N NE2 . GLN A 153 ? 0.8382 1.0116 0.9061 -0.1934 -0.0738 0.0437  150 GLN A NE2 
2386 N N   . ILE A 154 ? 0.3368 0.5219 0.4051 -0.1446 -0.0915 0.0342  151 ILE A N   
2387 C CA  . ILE A 154 ? 0.3484 0.5664 0.4432 -0.1293 -0.0900 0.0389  151 ILE A CA  
2388 C C   . ILE A 154 ? 0.3167 0.5254 0.3976 -0.1244 -0.1028 0.0385  151 ILE A C   
2389 O O   . ILE A 154 ? 0.3787 0.6159 0.4790 -0.1242 -0.1133 0.0450  151 ILE A O   
2390 C CB  . ILE A 154 ? 0.3658 0.5822 0.4666 -0.1096 -0.0723 0.0364  151 ILE A CB  
2391 C CG1 . ILE A 154 ? 0.3456 0.5734 0.4589 -0.1151 -0.0599 0.0375  151 ILE A CG1 
2392 C CG2 . ILE A 154 ? 0.4038 0.6460 0.5268 -0.0922 -0.0719 0.0405  151 ILE A CG2 
2393 C CD1 . ILE A 154 ? 0.3622 0.5779 0.4714 -0.0990 -0.0435 0.0333  151 ILE A CD1 
2405 N N   . LEU A 155 ? 0.3809 0.5496 0.4277 -0.1197 -0.1017 0.0313  152 LEU A N   
2406 C CA  . LEU A 155 ? 0.3410 0.4990 0.3713 -0.1131 -0.1108 0.0309  152 LEU A CA  
2407 C C   . LEU A 155 ? 0.4080 0.5598 0.4219 -0.1304 -0.1296 0.0315  152 LEU A C   
2408 O O   . LEU A 155 ? 0.5387 0.7016 0.5540 -0.1283 -0.1414 0.0360  152 LEU A O   
2409 C CB  . LEU A 155 ? 0.3881 0.5079 0.3877 -0.1023 -0.1013 0.0231  152 LEU A CB  
2410 C CG  . LEU A 155 ? 0.5514 0.6709 0.5606 -0.0854 -0.0848 0.0220  152 LEU A CG  
2411 C CD1 . LEU A 155 ? 0.5437 0.6311 0.5250 -0.0762 -0.0783 0.0161  152 LEU A CD1 
2412 C CD2 . LEU A 155 ? 0.4806 0.6312 0.5181 -0.0740 -0.0846 0.0291  152 LEU A CD2 
2424 N N   . THR A 156 ? 0.7966 0.4748 0.6519 0.1362  -0.2393 0.1865  153 THR A N   
2425 C CA  . THR A 156 ? 0.7889 0.4529 0.6611 0.1365  -0.2270 0.1850  153 THR A CA  
2426 C C   . THR A 156 ? 0.8082 0.4538 0.6411 0.1247  -0.2213 0.1934  153 THR A C   
2427 O O   . THR A 156 ? 0.7875 0.4332 0.6176 0.1233  -0.2094 0.1842  153 THR A O   
2428 C CB  . THR A 156 ? 0.9154 0.5640 0.8184 0.1421  -0.2321 0.1910  153 THR A CB  
2429 O OG1 . THR A 156 ? 0.8743 0.5440 0.8157 0.1533  -0.2337 0.1820  153 THR A OG1 
2430 C CG2 . THR A 156 ? 0.8988 0.5281 0.8170 0.1431  -0.2237 0.1876  153 THR A CG2 
2438 N N   . GLU A 157 ? 0.8500 0.4821 0.6524 0.1148  -0.2295 0.2126  154 GLU A N   
2439 C CA  . GLU A 157 ? 0.8729 0.4914 0.6406 0.0999  -0.2232 0.2257  154 GLU A CA  
2440 C C   . GLU A 157 ? 0.8850 0.5216 0.6147 0.0958  -0.2146 0.2165  154 GLU A C   
2441 O O   . GLU A 157 ? 0.8509 0.4935 0.5787 0.0865  -0.1945 0.2086  154 GLU A O   
2442 C CB  . GLU A 157 ? 0.9224 0.5336 0.6656 0.0880  -0.2343 0.2518  154 GLU A CB  
2443 C CG  . GLU A 157 ? 1.0000 0.5876 0.7800 0.0895  -0.2433 0.2616  154 GLU A CG  
2444 C CD  . GLU A 157 ? 1.0708 0.6522 0.8268 0.0749  -0.2550 0.2905  154 GLU A CD  
2445 O OE1 . GLU A 157 ? 1.3076 0.8653 1.0841 0.0677  -0.2605 0.3033  154 GLU A OE1 
2446 O OE2 . GLU A 157 ? 1.2699 0.8723 0.9872 0.0706  -0.2599 0.2997  154 GLU A OE2 
2453 N N   . GLY A 158 ? 0.8809 0.5396 0.5916 0.1015  -0.2234 0.2090  155 GLY A N   
2454 C CA  . GLY A 158 ? 0.8351 0.5265 0.5243 0.0980  -0.2097 0.1894  155 GLY A CA  
2455 C C   . GLY A 158 ? 0.8228 0.5235 0.5459 0.1015  -0.1937 0.1673  155 GLY A C   
2456 O O   . GLY A 158 ? 0.7866 0.5032 0.4989 0.0928  -0.1753 0.1563  155 GLY A O   
2460 N N   . LEU A 159 ? 0.7964 0.4906 0.5617 0.1135  -0.2006 0.1624  156 LEU A N   
2461 C CA  . LEU A 159 ? 0.7553 0.4636 0.5535 0.1155  -0.1860 0.1454  156 LEU A CA  
2462 C C   . LEU A 159 ? 0.7378 0.4350 0.5397 0.1069  -0.1659 0.1455  156 LEU A C   
2463 O O   . LEU A 159 ? 0.7248 0.4367 0.5247 0.0996  -0.1485 0.1328  156 LEU A O   
2464 C CB  . LEU A 159 ? 0.8518 0.5628 0.6947 0.1293  -0.1978 0.1445  156 LEU A CB  
2465 C CG  . LEU A 159 ? 0.7081 0.4410 0.5900 0.1319  -0.1855 0.1321  156 LEU A CG  
2466 C CD1 . LEU A 159 ? 0.8979 0.6241 0.7904 0.1293  -0.1661 0.1285  156 LEU A CD1 
2467 C CD2 . LEU A 159 ? 0.7713 0.5280 0.6461 0.1254  -0.1812 0.1187  156 LEU A CD2 
2479 N N   . GLU A 160 ? 0.8018 0.4717 0.6137 0.1086  -0.1708 0.1585  157 GLU A N   
2480 C CA  . GLU A 160 ? 0.7991 0.4536 0.6198 0.1024  -0.1573 0.1572  157 GLU A CA  
2481 C C   . GLU A 160 ? 0.7839 0.4431 0.5709 0.0847  -0.1427 0.1594  157 GLU A C   
2482 O O   . GLU A 160 ? 0.7739 0.4394 0.5681 0.0791  -0.1256 0.1469  157 GLU A O   
2483 C CB  . GLU A 160 ? 0.8230 0.4428 0.6574 0.1064  -0.1727 0.1732  157 GLU A CB  
2484 C CG  . GLU A 160 ? 0.9771 0.5919 0.8596 0.1241  -0.1767 0.1616  157 GLU A CG  
2485 C CD  . GLU A 160 ? 1.0368 0.6802 0.9435 0.1381  -0.1798 0.1519  157 GLU A CD  
2486 O OE1 . GLU A 160 ? 1.0672 0.7387 0.9926 0.1414  -0.1650 0.1350  157 GLU A OE1 
2487 O OE2 . GLU A 160 ? 1.1114 0.7567 1.0231 0.1431  -0.1946 0.1609  157 GLU A OE2 
2494 N N   . LYS A 161 ? 0.7820 0.4437 0.5317 0.0756  -0.1491 0.1746  158 LYS A N   
2495 C CA  . LYS A 161 ? 0.7949 0.4660 0.5141 0.0579  -0.1352 0.1803  158 LYS A CA  
2496 C C   . LYS A 161 ? 0.8061 0.5107 0.5177 0.0565  -0.1193 0.1575  158 LYS A C   
2497 O O   . LYS A 161 ? 0.7781 0.4903 0.4843 0.0451  -0.1024 0.1527  158 LYS A O   
2498 C CB  . LYS A 161 ? 0.8906 0.5639 0.5713 0.0482  -0.1462 0.2054  158 LYS A CB  
2499 C CG  . LYS A 161 ? 1.0747 0.7122 0.7657 0.0482  -0.1666 0.2316  158 LYS A CG  
2500 C CD  . LYS A 161 ? 1.1675 0.8116 0.8189 0.0376  -0.1803 0.2604  158 LYS A CD  
2501 C CE  . LYS A 161 ? 1.2031 0.8076 0.8698 0.0339  -0.2027 0.2904  158 LYS A CE  
2502 N NZ  . LYS A 161 ? 1.2877 0.9104 0.9253 0.0241  -0.2131 0.3153  158 LYS A NZ  
2516 N N   . GLY A 162 ? 0.7672 0.4911 0.4820 0.0680  -0.1272 0.1434  159 GLY A N   
2517 C CA  . GLY A 162 ? 0.8307 0.5837 0.5452 0.0677  -0.1173 0.1211  159 GLY A CA  
2518 C C   . GLY A 162 ? 0.7206 0.4745 0.4696 0.0685  -0.1054 0.1072  159 GLY A C   
2519 O O   . GLY A 162 ? 0.7158 0.4879 0.4644 0.0623  -0.0929 0.0932  159 GLY A O   
2523 N N   . MET A 163 ? 0.7329 0.4715 0.5127 0.0767  -0.1097 0.1102  160 MET A N   
2524 C CA  . MET A 163 ? 0.7270 0.4726 0.5360 0.0771  -0.0970 0.0979  160 MET A CA  
2525 C C   . MET A 163 ? 0.6819 0.4147 0.4825 0.0655  -0.0810 0.0982  160 MET A C   
2526 O O   . MET A 163 ? 0.6399 0.3855 0.4493 0.0602  -0.0674 0.0854  160 MET A O   
2527 C CB  . MET A 163 ? 0.6964 0.4377 0.5401 0.0902  -0.1042 0.0990  160 MET A CB  
2528 C CG  . MET A 163 ? 0.7087 0.4714 0.5757 0.1001  -0.1174 0.0968  160 MET A CG  
2529 S SD  . MET A 163 ? 0.7024 0.4966 0.5742 0.0942  -0.1170 0.0838  160 MET A SD  
2530 C CE  . MET A 163 ? 0.7676 0.5843 0.6737 0.0923  -0.1017 0.0766  160 MET A CE  
2540 N N   . LYS A 164 ? 0.7137 0.4205 0.5002 0.0604  -0.0848 0.1145  161 LYS A N   
2541 C CA  . LYS A 164 ? 0.6889 0.3821 0.4697 0.0472  -0.0732 0.1175  161 LYS A CA  
2542 C C   . LYS A 164 ? 0.7528 0.4691 0.5088 0.0335  -0.0599 0.1136  161 LYS A C   
2543 O O   . LYS A 164 ? 0.6962 0.4175 0.4585 0.0259  -0.0462 0.1034  161 LYS A O   
2544 C CB  . LYS A 164 ? 0.8447 0.5057 0.6189 0.0421  -0.0851 0.1407  161 LYS A CB  
2545 C CG  . LYS A 164 ? 1.0218 0.6586 0.8071 0.0320  -0.0806 0.1440  161 LYS A CG  
2546 C CD  . LYS A 164 ? 1.0441 0.6787 0.8618 0.0420  -0.0732 0.1195  161 LYS A CD  
2547 C CE  . LYS A 164 ? 1.1099 0.7353 0.9579 0.0625  -0.0852 0.1114  161 LYS A CE  
2548 N NZ  . LYS A 164 ? 1.0742 0.6616 0.9445 0.0664  -0.0995 0.1156  161 LYS A NZ  
2562 N N   . THR A 165 ? 0.7263 0.4603 0.4550 0.0317  -0.0646 0.1191  162 THR A N   
2563 C CA  . THR A 165 ? 0.7410 0.5044 0.4492 0.0223  -0.0525 0.1104  162 THR A CA  
2564 C C   . THR A 165 ? 0.6701 0.4519 0.3998 0.0265  -0.0453 0.0858  162 THR A C   
2565 O O   . THR A 165 ? 0.6297 0.4244 0.3580 0.0169  -0.0316 0.0771  162 THR A O   
2566 C CB  . THR A 165 ? 0.7047 0.4909 0.3825 0.0250  -0.0610 0.1134  162 THR A CB  
2567 O OG1 . THR A 165 ? 0.8118 0.5841 0.4683 0.0187  -0.0689 0.1406  162 THR A OG1 
2568 C CG2 . THR A 165 ? 0.7814 0.6044 0.4406 0.0179  -0.0484 0.0998  162 THR A CG2 
2576 N N   . PHE A 166 ? 0.6209 0.4062 0.3724 0.0398  -0.0562 0.0767  163 PHE A N   
2577 C CA  . PHE A 166 ? 0.5806 0.3846 0.3561 0.0415  -0.0527 0.0586  163 PHE A CA  
2578 C C   . PHE A 166 ? 0.6034 0.3999 0.3943 0.0343  -0.0380 0.0553  163 PHE A C   
2579 O O   . PHE A 166 ? 0.5475 0.3586 0.3427 0.0266  -0.0282 0.0439  163 PHE A O   
2580 C CB  . PHE A 166 ? 0.6132 0.4227 0.4141 0.0545  -0.0689 0.0562  163 PHE A CB  
2581 C CG  . PHE A 166 ? 0.6337 0.4639 0.4637 0.0541  -0.0692 0.0439  163 PHE A CG  
2582 C CD1 . PHE A 166 ? 0.6602 0.4933 0.5173 0.0551  -0.0644 0.0453  163 PHE A CD1 
2583 C CD2 . PHE A 166 ? 0.7197 0.5695 0.5517 0.0530  -0.0764 0.0307  163 PHE A CD2 
2584 C CE1 . PHE A 166 ? 0.6484 0.5051 0.5323 0.0521  -0.0659 0.0388  163 PHE A CE1 
2585 C CE2 . PHE A 166 ? 0.7597 0.6271 0.6230 0.0506  -0.0807 0.0229  163 PHE A CE2 
2586 C CZ  . PHE A 166 ? 0.6135 0.4850 0.5018 0.0488  -0.0753 0.0295  163 PHE A CZ  
2596 N N   . GLY A 167 ? 0.5799 0.3537 0.3799 0.0375  -0.0378 0.0634  164 GLY A N   
2597 C CA  . GLY A 167 ? 0.5927 0.3591 0.4062 0.0328  -0.0261 0.0568  164 GLY A CA  
2598 C C   . GLY A 167 ? 0.6319 0.3940 0.4284 0.0170  -0.0142 0.0579  164 GLY A C   
2599 O O   . GLY A 167 ? 0.5906 0.3625 0.3953 0.0105  -0.0038 0.0463  164 GLY A O   
2603 N N   . GLU A 168 ? 0.6165 0.3671 0.3898 0.0096  -0.0163 0.0739  165 GLU A N   
2604 C CA  . GLU A 168 ? 0.6299 0.3818 0.3887 -0.0073 -0.0053 0.0794  165 GLU A CA  
2605 C C   . GLU A 168 ? 0.6380 0.4237 0.3893 -0.0123 0.0041  0.0656  165 GLU A C   
2606 O O   . GLU A 168 ? 0.6511 0.4430 0.4046 -0.0237 0.0156  0.0605  165 GLU A O   
2607 C CB  . GLU A 168 ? 0.7356 0.4771 0.4712 -0.0160 -0.0108 0.1047  165 GLU A CB  
2608 C CG  . GLU A 168 ? 0.9028 0.6101 0.6476 -0.0095 -0.0260 0.1199  165 GLU A CG  
2609 C CD  . GLU A 168 ? 1.1598 0.8589 0.8822 -0.0210 -0.0345 0.1500  165 GLU A CD  
2610 O OE1 . GLU A 168 ? 1.1239 0.8462 0.8232 -0.0358 -0.0258 0.1604  165 GLU A OE1 
2611 O OE2 . GLU A 168 ? 1.2217 0.8943 0.9508 -0.0154 -0.0507 0.1645  165 GLU A OE2 
2618 N N   . THR A 169 ? 0.5967 0.4039 0.3413 -0.0034 -0.0031 0.0586  166 THR A N   
2619 C CA  . THR A 169 ? 0.5844 0.4235 0.3267 -0.0055 0.0016  0.0418  166 THR A CA  
2620 C C   . THR A 169 ? 0.6133 0.4573 0.3827 -0.0071 0.0064  0.0260  166 THR A C   
2621 O O   . THR A 169 ? 0.5919 0.4525 0.3629 -0.0155 0.0153  0.0159  166 THR A O   
2622 C CB  . THR A 169 ? 0.6286 0.4854 0.3656 0.0076  -0.0129 0.0337  166 THR A CB  
2623 O OG1 . THR A 169 ? 0.6325 0.4911 0.3389 0.0077  -0.0166 0.0481  166 THR A OG1 
2624 C CG2 . THR A 169 ? 0.6735 0.5620 0.4163 0.0090  -0.0132 0.0111  166 THR A CG2 
2632 N N   . LEU A 170 ? 0.5257 0.3590 0.3171 0.0002  0.0008  0.0246  167 LEU A N   
2633 C CA  . LEU A 170 ? 0.4948 0.3378 0.3108 -0.0021 0.0041  0.0131  167 LEU A CA  
2634 C C   . LEU A 170 ? 0.5140 0.3417 0.3332 -0.0105 0.0163  0.0135  167 LEU A C   
2635 O O   . LEU A 170 ? 0.4773 0.3146 0.3134 -0.0134 0.0199  0.0043  167 LEU A O   
2636 C CB  . LEU A 170 ? 0.4764 0.3256 0.3152 0.0091  -0.0080 0.0132  167 LEU A CB  
2637 C CG  . LEU A 170 ? 0.5137 0.3838 0.3643 0.0140  -0.0232 0.0068  167 LEU A CG  
2638 C CD1 . LEU A 170 ? 0.6363 0.5029 0.4651 0.0211  -0.0321 0.0094  167 LEU A CD1 
2639 C CD2 . LEU A 170 ? 0.5852 0.4677 0.4668 0.0200  -0.0355 0.0103  167 LEU A CD2 
2651 N N   . ASN A 171 ? 0.5498 0.3545 0.3542 -0.0152 0.0204  0.0246  168 ASN A N   
2652 C CA  . ASN A 171 ? 0.5406 0.3248 0.3514 -0.0216 0.0269  0.0244  168 ASN A CA  
2653 C C   . ASN A 171 ? 0.5281 0.3099 0.3596 -0.0110 0.0245  0.0144  168 ASN A C   
2654 O O   . ASN A 171 ? 0.5183 0.3032 0.3603 -0.0147 0.0305  0.0031  168 ASN A O   
2655 C CB  . ASN A 171 ? 0.6091 0.4030 0.4196 -0.0363 0.0377  0.0178  168 ASN A CB  
2656 C CG  . ASN A 171 ? 0.8958 0.6635 0.7060 -0.0466 0.0413  0.0247  168 ASN A CG  
2657 O OD1 . ASN A 171 ? 0.9294 0.6744 0.7328 -0.0477 0.0354  0.0405  168 ASN A OD1 
2658 N ND2 . ASN A 171 ? 0.8512 0.6210 0.6715 -0.0551 0.0480  0.0141  168 ASN A ND2 
2665 N N   . ILE A 172 ? 0.5356 0.3146 0.3728 0.0026  0.0155  0.0184  169 ILE A N   
2666 C CA  . ILE A 172 ? 0.5347 0.3198 0.3922 0.0147  0.0139  0.0091  169 ILE A CA  
2667 C C   . ILE A 172 ? 0.5490 0.3074 0.4115 0.0165  0.0146  0.0032  169 ILE A C   
2668 O O   . ILE A 172 ? 0.5801 0.3075 0.4348 0.0124  0.0095  0.0137  169 ILE A O   
2669 C CB  . ILE A 172 ? 0.6267 0.4170 0.4917 0.0289  0.0033  0.0160  169 ILE A CB  
2670 C CG1 . ILE A 172 ? 0.6584 0.4776 0.5276 0.0281  -0.0011 0.0182  169 ILE A CG1 
2671 C CG2 . ILE A 172 ? 0.6847 0.4816 0.5708 0.0432  0.0023  0.0070  169 ILE A CG2 
2672 C CD1 . ILE A 172 ? 0.7340 0.5874 0.6245 0.0274  0.0018  0.0104  169 ILE A CD1 
2684 N N   . ALA A 173 ? 0.5394 0.3117 0.4170 0.0229  0.0186  -0.0136 170 ALA A N   
2685 C CA  . ALA A 173 ? 0.5658 0.3143 0.4519 0.0274  0.0164  -0.0257 170 ALA A CA  
2686 C C   . ALA A 173 ? 0.5910 0.3212 0.4902 0.0451  0.0046  -0.0267 170 ALA A C   
2687 O O   . ALA A 173 ? 0.5798 0.3289 0.4859 0.0568  0.0018  -0.0236 170 ALA A O   
2688 C CB  . ALA A 173 ? 0.6614 0.4371 0.5569 0.0301  0.0240  -0.0467 170 ALA A CB  
2694 N N   . PRO A 174 ? 0.6265 0.3196 0.5339 0.0474  -0.0049 -0.0310 171 PRO A N   
2695 C CA  . PRO A 174 ? 0.6542 0.3260 0.5789 0.0646  -0.0200 -0.0324 171 PRO A CA  
2696 C C   . PRO A 174 ? 0.6412 0.3471 0.5846 0.0871  -0.0182 -0.0526 171 PRO A C   
2697 O O   . PRO A 174 ? 0.6885 0.3942 0.6422 0.0999  -0.0266 -0.0467 171 PRO A O   
2698 C CB  . PRO A 174 ? 0.7515 0.3813 0.6891 0.0629  -0.0324 -0.0399 171 PRO A CB  
2699 C CG  . PRO A 174 ? 0.7333 0.3537 0.6529 0.0383  -0.0254 -0.0256 171 PRO A CG  
2700 C CD  . PRO A 174 ? 0.7910 0.4554 0.6937 0.0313  -0.0061 -0.0280 171 PRO A CD  
2708 N N   . ILE A 175 ? 0.6843 0.4238 0.6325 0.0916  -0.0077 -0.0749 172 ILE A N   
2709 C CA  . ILE A 175 ? 0.7665 0.5493 0.7325 0.1124  -0.0044 -0.0934 172 ILE A CA  
2710 C C   . ILE A 175 ? 0.6350 0.4525 0.5996 0.1119  0.0002  -0.0747 172 ILE A C   
2711 O O   . ILE A 175 ? 0.5975 0.4388 0.5802 0.1290  -0.0028 -0.0786 172 ILE A O   
2712 C CB  . ILE A 175 ? 0.6918 0.5124 0.6584 0.1144  0.0069  -0.1179 172 ILE A CB  
2713 C CG1 . ILE A 175 ? 0.7961 0.6345 0.7429 0.0915  0.0190  -0.1042 172 ILE A CG1 
2714 C CG2 . ILE A 175 ? 0.9963 0.7837 0.9720 0.1219  -0.0026 -0.1432 172 ILE A CG2 
2715 C CD1 . ILE A 175 ? 0.8702 0.7555 0.8163 0.0914  0.0299  -0.1222 172 ILE A CD1 
2727 N N   . ASP A 176 ? 0.5868 0.4100 0.5336 0.0930  0.0060  -0.0557 173 ASP A N   
2728 C CA  . ASP A 176 ? 0.5367 0.3874 0.4860 0.0922  0.0052  -0.0383 173 ASP A CA  
2729 C C   . ASP A 176 ? 0.6264 0.4442 0.5733 0.0960  -0.0077 -0.0216 173 ASP A C   
2730 O O   . ASP A 176 ? 0.6001 0.4355 0.5613 0.1070  -0.0135 -0.0152 173 ASP A O   
2731 C CB  . ASP A 176 ? 0.5043 0.3719 0.4406 0.0732  0.0113  -0.0272 173 ASP A CB  
2732 C CG  . ASP A 176 ? 0.5126 0.4186 0.4529 0.0680  0.0218  -0.0391 173 ASP A CG  
2733 O OD1 . ASP A 176 ? 0.4763 0.4256 0.4328 0.0782  0.0250  -0.0454 173 ASP A OD1 
2734 O OD2 . ASP A 176 ? 0.4786 0.3770 0.4065 0.0529  0.0268  -0.0404 173 ASP A OD2 
2739 N N   . ALA A 177 ? 0.6646 0.4382 0.5942 0.0858  -0.0128 -0.0123 174 ALA A N   
2740 C CA  . ALA A 177 ? 0.7352 0.4784 0.6599 0.0880  -0.0262 0.0053  174 ALA A CA  
2741 C C   . ALA A 177 ? 0.7273 0.4625 0.6767 0.1086  -0.0375 -0.0016 174 ALA A C   
2742 O O   . ALA A 177 ? 0.8307 0.5662 0.7861 0.1164  -0.0472 0.0102  174 ALA A O   
2743 C CB  . ALA A 177 ? 0.7058 0.4084 0.6111 0.0730  -0.0297 0.0169  174 ALA A CB  
2749 N N   . LYS A 178 ? 0.6981 0.4259 0.6642 0.1188  -0.0382 -0.0226 175 LYS A N   
2750 C CA  . LYS A 178 ? 0.8281 0.5469 0.8220 0.1407  -0.0512 -0.0339 175 LYS A CA  
2751 C C   . LYS A 178 ? 0.8556 0.6254 0.8686 0.1568  -0.0462 -0.0405 175 LYS A C   
2752 O O   . LYS A 178 ? 0.9231 0.6893 0.9566 0.1725  -0.0581 -0.0394 175 LYS A O   
2753 C CB  . LYS A 178 ? 0.8030 0.5068 0.8132 0.1503  -0.0547 -0.0611 175 LYS A CB  
2754 C CG  . LYS A 178 ? 0.9870 0.6783 1.0311 0.1754  -0.0717 -0.0778 175 LYS A CG  
2755 C CD  . LYS A 178 ? 0.9507 0.6204 1.0132 0.1854  -0.0804 -0.1074 175 LYS A CD  
2756 C CE  . LYS A 178 ? 1.1164 0.7650 1.2174 0.2111  -0.1031 -0.1248 175 LYS A CE  
2757 N NZ  . LYS A 178 ? 1.3254 0.9490 1.4493 0.2231  -0.1170 -0.1574 175 LYS A NZ  
2771 N N   . MET A 179 ? 0.7265 0.5458 0.7357 0.1519  -0.0302 -0.0450 176 MET A N   
2772 C CA  . MET A 179 ? 0.7659 0.6429 0.7962 0.1642  -0.0248 -0.0483 176 MET A CA  
2773 C C   . MET A 179 ? 0.7629 0.6509 0.7909 0.1562  -0.0295 -0.0214 176 MET A C   
2774 O O   . MET A 179 ? 0.8199 0.7336 0.8706 0.1689  -0.0348 -0.0169 176 MET A O   
2775 C CB  . MET A 179 ? 0.6646 0.5935 0.6944 0.1609  -0.0079 -0.0630 176 MET A CB  
2776 C CG  . MET A 179 ? 0.8009 0.7999 0.8552 0.1741  -0.0009 -0.0682 176 MET A CG  
2777 S SD  . MET A 179 ? 0.7019 0.7656 0.7497 0.1640  0.0177  -0.0772 176 MET A SD  
2778 C CE  . MET A 179 ? 0.5823 0.6216 0.6249 0.1771  0.0197  -0.1161 176 MET A CE  
2788 N N   . MET A 180 ? 0.8089 0.6779 0.8119 0.1367  -0.0296 -0.0050 177 MET A N   
2789 C CA  . MET A 180 ? 0.8023 0.6797 0.8037 0.1303  -0.0375 0.0164  177 MET A CA  
2790 C C   . MET A 180 ? 0.9492 0.7942 0.9526 0.1389  -0.0541 0.0283  177 MET A C   
2791 O O   . MET A 180 ? 1.0099 0.8680 1.0216 0.1401  -0.0636 0.0425  177 MET A O   
2792 C CB  . MET A 180 ? 0.8678 0.7324 0.8428 0.1104  -0.0352 0.0250  177 MET A CB  
2793 C CG  . MET A 180 ? 0.8123 0.7055 0.7854 0.0997  -0.0216 0.0160  177 MET A CG  
2794 S SD  . MET A 180 ? 0.8766 0.7438 0.8192 0.0791  -0.0186 0.0196  177 MET A SD  
2795 C CE  . MET A 180 ? 0.7768 0.6893 0.7330 0.0687  -0.0194 0.0258  177 MET A CE  
2805 N N   . SER A 181 ? 0.9114 0.7136 0.9095 0.1437  -0.0604 0.0242  178 SER A N   
2806 C CA  . SER A 181 ? 1.0454 0.8130 1.0438 0.1496  -0.0783 0.0381  178 SER A CA  
2807 C C   . SER A 181 ? 1.1052 0.8723 1.1369 0.1714  -0.0871 0.0273  178 SER A C   
2808 O O   . SER A 181 ? 1.1381 0.8777 1.1757 0.1778  -0.1044 0.0391  178 SER A O   
2809 C CB  . SER A 181 ? 1.0063 0.7249 0.9764 0.1363  -0.0835 0.0480  178 SER A CB  
2810 O OG  . SER A 181 ? 0.9345 0.6321 0.9135 0.1395  -0.0821 0.0332  178 SER A OG  
2816 N N   . GLN A 182 ? 1.0265 0.8256 1.0806 0.1838  -0.0767 0.0038  179 GLN A N   
2817 C CA  . GLN A 182 ? 0.9824 0.7926 1.0728 0.2081  -0.0841 -0.0121 179 GLN A CA  
2818 C C   . GLN A 182 ? 0.9776 0.8065 1.0864 0.2159  -0.0941 0.0041  179 GLN A C   
2819 O O   . GLN A 182 ? 0.8653 0.7422 0.9798 0.2122  -0.0857 0.0118  179 GLN A O   
2820 C CB  . GLN A 182 ? 0.8975 0.7624 1.0065 0.2202  -0.0676 -0.0397 179 GLN A CB  
2821 C CG  . GLN A 182 ? 1.0459 0.8934 1.1522 0.2240  -0.0637 -0.0669 179 GLN A CG  
2822 C CD  . GLN A 182 ? 1.1916 0.9740 1.3060 0.2307  -0.0846 -0.0713 179 GLN A CD  
2823 O OE1 . GLN A 182 ? 1.2756 1.0074 1.3675 0.2131  -0.0937 -0.0498 179 GLN A OE1 
2824 N NE2 . GLN A 182 ? 1.1903 0.9768 1.3392 0.2561  -0.0938 -0.0994 179 GLN A NE2 
2833 N N   . PRO A 183 ? 1.0199 0.8124 1.1411 0.2257  -0.1141 0.0114  180 PRO A N   
2834 C CA  . PRO A 183 ? 1.0088 0.8229 1.1538 0.2359  -0.1244 0.0237  180 PRO A CA  
2835 C C   . PRO A 183 ? 0.9210 0.8008 1.1047 0.2547  -0.1136 0.0052  180 PRO A C   
2836 O O   . PRO A 183 ? 0.8420 0.7364 1.0431 0.2698  -0.1070 -0.0227 180 PRO A O   
2837 C CB  . PRO A 183 ? 0.9695 0.7294 1.1235 0.2445  -0.1488 0.0304  180 PRO A CB  
2838 C CG  . PRO A 183 ? 0.9706 0.6772 1.0925 0.2286  -0.1522 0.0356  180 PRO A CG  
2839 C CD  . PRO A 183 ? 1.0400 0.7691 1.1551 0.2250  -0.1311 0.0137  180 PRO A CD  
2847 N N   . ALA A 184 ? 0.8548 0.7781 1.0533 0.2534  -0.1129 0.0208  181 ALA A N   
2848 C CA  . ALA A 184 ? 0.8253 0.8208 1.0629 0.2692  -0.1029 0.0097  181 ALA A CA  
2849 C C   . ALA A 184 ? 0.8644 0.8567 1.1391 0.2965  -0.1139 -0.0090 181 ALA A C   
2850 O O   . ALA A 184 ? 0.8426 0.7764 1.1177 0.3011  -0.1346 -0.0036 181 ALA A O   
2851 C CB  . ALA A 184 ? 0.7264 0.7624 0.9780 0.2606  -0.1062 0.0365  181 ALA A CB  
2857 N N   . ASP A 185 ? 0.7754 0.8359 1.0831 0.3150  -0.1009 -0.0310 182 ASP A N   
2858 C CA  . ASP A 185 ? 0.9901 1.0559 1.3382 0.3448  -0.1105 -0.0564 182 ASP A CA  
2859 C C   . ASP A 185 ? 0.9167 0.9830 1.2958 0.3530  -0.1284 -0.0369 182 ASP A C   
2860 O O   . ASP A 185 ? 0.8549 0.8698 1.2490 0.3655  -0.1504 -0.0408 182 ASP A O   
2861 C CB  . ASP A 185 ? 0.8518 1.0012 1.2248 0.3639  -0.0898 -0.0886 182 ASP A CB  
2862 C CG  . ASP A 185 ? 0.9676 1.2051 1.3500 0.3542  -0.0718 -0.0694 182 ASP A CG  
2863 O OD1 . ASP A 185 ? 1.0487 1.2768 1.4208 0.3329  -0.0775 -0.0328 182 ASP A OD1 
2864 O OD2 . ASP A 185 ? 1.0104 1.3288 1.4117 0.3676  -0.0535 -0.0908 182 ASP A OD2 
2869 N N   . THR A 186 ? 0.8573 0.9801 1.2492 0.3451  -0.1220 -0.0142 183 THR A N   
2870 C CA  . THR A 186 ? 0.7930 0.9205 1.2176 0.3523  -0.1397 0.0048  183 THR A CA  
2871 C C   . THR A 186 ? 0.8061 0.8588 1.2009 0.3339  -0.1615 0.0348  183 THR A C   
2872 O O   . THR A 186 ? 0.7879 0.7956 1.1372 0.3143  -0.1601 0.0427  183 THR A O   
2873 C CB  . THR A 186 ? 0.7139 0.9306 1.1675 0.3487  -0.1280 0.0216  183 THR A CB  
2874 O OG1 . THR A 186 ? 0.7460 0.9728 1.1682 0.3211  -0.1182 0.0430  183 THR A OG1 
2875 C CG2 . THR A 186 ? 0.7054 1.0088 1.1935 0.3705  -0.1077 -0.0075 183 THR A CG2 
2883 N N   . GLU A 187 ? 0.8187 0.8505 0.9328 0.3369  -0.1451 -0.0255 184 GLU A N   
2884 C CA  . GLU A 187 ? 0.8494 0.8831 0.9474 0.3337  -0.1532 -0.0109 184 GLU A CA  
2885 C C   . GLU A 187 ? 0.8359 0.9105 0.9414 0.3170  -0.1449 -0.0178 184 GLU A C   
2886 O O   . GLU A 187 ? 0.8817 0.9518 0.9704 0.3069  -0.1460 -0.0053 184 GLU A O   
2887 C CB  . GLU A 187 ? 0.8227 0.8661 0.9233 0.3547  -0.1704 -0.0104 184 GLU A CB  
2888 C CG  . GLU A 187 ? 0.9417 0.9965 1.0281 0.3524  -0.1797 0.0015  184 GLU A CG  
2889 C CD  . GLU A 187 ? 1.0844 1.0945 1.1388 0.3429  -0.1810 0.0260  184 GLU A CD  
2890 O OE1 . GLU A 187 ? 1.0541 1.0233 1.0981 0.3382  -0.1750 0.0339  184 GLU A OE1 
2891 O OE2 . GLU A 187 ? 1.1484 1.1653 1.1876 0.3393  -0.1877 0.0369  184 GLU A OE2 
2898 N N   . GLU A 188 ? 0.7245 0.8383 0.8541 0.3132  -0.1362 -0.0378 185 GLU A N   
2899 C CA  . GLU A 188 ? 0.7639 0.9120 0.9003 0.2948  -0.1266 -0.0443 185 GLU A CA  
2900 C C   . GLU A 188 ? 0.7985 0.9205 0.9202 0.2770  -0.1154 -0.0344 185 GLU A C   
2901 O O   . GLU A 188 ? 0.7479 0.8790 0.8618 0.2638  -0.1125 -0.0293 185 GLU A O   
2902 C CB  . GLU A 188 ? 0.7135 0.9049 0.8769 0.2924  -0.1185 -0.0665 185 GLU A CB  
2903 C CG  . GLU A 188 ? 0.9484 1.1799 1.1291 0.3053  -0.1280 -0.0793 185 GLU A CG  
2904 C CD  . GLU A 188 ? 1.0439 1.3230 1.2493 0.2969  -0.1179 -0.1006 185 GLU A CD  
2905 O OE1 . GLU A 188 ? 0.8367 1.1155 1.0442 0.2812  -0.1038 -0.1043 185 GLU A OE1 
2906 O OE2 . GLU A 188 ? 0.9585 1.2753 1.1805 0.3057  -0.1241 -0.1136 185 GLU A OE2 
2913 N N   . GLY A 189 ? 0.8432 0.9331 0.9612 0.2766  -0.1092 -0.0325 186 GLY A N   
2914 C CA  . GLY A 189 ? 0.7045 0.7709 0.8099 0.2602  -0.0985 -0.0246 186 GLY A CA  
2915 C C   . GLY A 189 ? 0.7489 0.7792 0.8276 0.2571  -0.1038 -0.0036 186 GLY A C   
2916 O O   . GLY A 189 ? 0.5993 0.6228 0.6669 0.2423  -0.0968 0.0032  186 GLY A O   
2920 N N   . ARG A 190 ? 0.7644 0.7712 0.8314 0.2706  -0.1162 0.0071  187 ARG A N   
2921 C CA  . ARG A 190 ? 0.8005 0.7747 0.8396 0.2665  -0.1216 0.0282  187 ARG A CA  
2922 C C   . ARG A 190 ? 0.6698 0.6709 0.7022 0.2593  -0.1241 0.0316  187 ARG A C   
2923 O O   . ARG A 190 ? 0.5706 0.5572 0.5836 0.2468  -0.1204 0.0434  187 ARG A O   
2924 C CB  . ARG A 190 ? 0.7474 0.6928 0.7755 0.2825  -0.1351 0.0391  187 ARG A CB  
2925 C CG  . ARG A 190 ? 0.8623 0.7542 0.8651 0.2765  -0.1346 0.0580  187 ARG A CG  
2926 C CD  . ARG A 190 ? 0.9090 0.7692 0.9147 0.2902  -0.1394 0.0575  187 ARG A CD  
2927 N NE  . ARG A 190 ? 0.9569 0.8361 0.9758 0.3113  -0.1518 0.0499  187 ARG A NE  
2928 C CZ  . ARG A 190 ? 0.8934 0.7687 0.9279 0.3266  -0.1546 0.0381  187 ARG A CZ  
2929 N NH1 . ARG A 190 ? 0.8875 0.7410 0.9268 0.3231  -0.1457 0.0317  187 ARG A NH1 
2930 N NH2 . ARG A 190 ? 0.9241 0.8192 0.9697 0.3463  -0.1669 0.0316  187 ARG A NH2 
2944 N N   . ILE A 191 ? 0.6301 0.6714 0.6781 0.2668  -0.1300 0.0203  188 ILE A N   
2945 C CA  . ILE A 191 ? 0.5724 0.6406 0.6146 0.2604  -0.1333 0.0219  188 ILE A CA  
2946 C C   . ILE A 191 ? 0.5674 0.6563 0.6167 0.2428  -0.1203 0.0138  188 ILE A C   
2947 O O   . ILE A 191 ? 0.5901 0.6787 0.6239 0.2324  -0.1188 0.0214  188 ILE A O   
2948 C CB  . ILE A 191 ? 0.6616 0.7674 0.7197 0.2728  -0.1437 0.0110  188 ILE A CB  
2949 C CG1 . ILE A 191 ? 0.7475 0.8299 0.7963 0.2916  -0.1582 0.0209  188 ILE A CG1 
2950 C CG2 . ILE A 191 ? 0.6107 0.7467 0.6643 0.2645  -0.1463 0.0100  188 ILE A CG2 
2951 C CD1 . ILE A 191 ? 0.8662 0.9172 0.8830 0.2902  -0.1663 0.0433  188 ILE A CD1 
2963 N N   . GLU A 192 ? 0.5171 0.6245 0.5889 0.2391  -0.1107 -0.0016 189 GLU A N   
2964 C CA  . GLU A 192 ? 0.5716 0.6948 0.6493 0.2220  -0.0984 -0.0079 189 GLU A CA  
2965 C C   . GLU A 192 ? 0.5807 0.6676 0.6381 0.2128  -0.0920 0.0055  189 GLU A C   
2966 O O   . GLU A 192 ? 0.5056 0.5991 0.5563 0.2009  -0.0870 0.0077  189 GLU A O   
2967 C CB  . GLU A 192 ? 0.7548 0.8993 0.8568 0.2188  -0.0889 -0.0247 189 GLU A CB  
2968 C CG  . GLU A 192 ? 0.8453 1.0383 0.9671 0.2120  -0.0868 -0.0400 189 GLU A CG  
2969 C CD  . GLU A 192 ? 0.7974 1.0022 0.9157 0.1948  -0.0805 -0.0395 189 GLU A CD  
2970 O OE1 . GLU A 192 ? 0.7188 0.9136 0.8368 0.1836  -0.0696 -0.0394 189 GLU A OE1 
2971 O OE2 . GLU A 192 ? 0.9039 1.1285 1.0199 0.1926  -0.0867 -0.0399 189 GLU A OE2 
2978 N N   . GLN A 193 ? 0.5017 0.5504 0.5495 0.2178  -0.0921 0.0139  190 GLN A N   
2979 C CA  . GLN A 193 ? 0.5552 0.5684 0.5831 0.2080  -0.0859 0.0266  190 GLN A CA  
2980 C C   . GLN A 193 ? 0.5342 0.5385 0.5371 0.2039  -0.0911 0.0418  190 GLN A C   
2981 O O   . GLN A 193 ? 0.4955 0.4938 0.4863 0.1921  -0.0839 0.0472  190 GLN A O   
2982 C CB  . GLN A 193 ? 0.6742 0.6482 0.6966 0.2136  -0.0865 0.0322  190 GLN A CB  
2983 C CG  . GLN A 193 ? 0.7102 0.6449 0.7112 0.2028  -0.0809 0.0458  190 GLN A CG  
2984 C CD  . GLN A 193 ? 0.9763 0.8739 0.9748 0.2069  -0.0813 0.0489  190 GLN A CD  
2985 O OE1 . GLN A 193 ? 0.9851 0.8895 1.0025 0.2142  -0.0797 0.0357  190 GLN A OE1 
2986 N NE2 . GLN A 193 ? 1.1084 0.9674 1.0832 0.2012  -0.0828 0.0658  190 GLN A NE2 
2995 N N   . TYR A 194 ? 0.5245 0.5294 0.5185 0.2138  -0.1033 0.0485  191 TYR A N   
2996 C CA  . TYR A 194 ? 0.5271 0.5290 0.4963 0.2093  -0.1082 0.0617  191 TYR A CA  
2997 C C   . TYR A 194 ? 0.5081 0.5478 0.4837 0.2007  -0.1043 0.0523  191 TYR A C   
2998 O O   . TYR A 194 ? 0.4736 0.5090 0.4320 0.1901  -0.0993 0.0593  191 TYR A O   
2999 C CB  . TYR A 194 ? 0.5503 0.5497 0.5108 0.2221  -0.1229 0.0692  191 TYR A CB  
3000 C CG  . TYR A 194 ? 0.4966 0.5057 0.4350 0.2175  -0.1285 0.0785  191 TYR A CG  
3001 C CD1 . TYR A 194 ? 0.6502 0.6283 0.5568 0.2096  -0.1282 0.0976  191 TYR A CD1 
3002 C CD2 . TYR A 194 ? 0.5224 0.5731 0.4714 0.2192  -0.1332 0.0672  191 TYR A CD2 
3003 C CE1 . TYR A 194 ? 0.5678 0.5571 0.4527 0.2044  -0.1324 0.1051  191 TYR A CE1 
3004 C CE2 . TYR A 194 ? 0.6011 0.6622 0.5297 0.2144  -0.1379 0.0738  191 TYR A CE2 
3005 C CZ  . TYR A 194 ? 0.5604 0.5913 0.4565 0.2074  -0.1375 0.0926  191 TYR A CZ  
3006 O OH  . TYR A 194 ? 0.7025 0.7460 0.5770 0.2016  -0.1413 0.0981  191 TYR A OH  
3016 N N   . LYS A 195 ? 0.4968 0.5745 0.4976 0.2041  -0.1057 0.0356  192 LYS A N   
3017 C CA  . LYS A 195 ? 0.4756 0.5886 0.4840 0.1945  -0.1026 0.0257  192 LYS A CA  
3018 C C   . LYS A 195 ? 0.3643 0.4734 0.3746 0.1814  -0.0898 0.0236  192 LYS A C   
3019 O O   . LYS A 195 ? 0.3856 0.5070 0.3886 0.1722  -0.0873 0.0233  192 LYS A O   
3020 C CB  . LYS A 195 ? 0.4762 0.6294 0.5125 0.1972  -0.1048 0.0077  192 LYS A CB  
3021 C CG  . LYS A 195 ? 0.5181 0.6840 0.5560 0.2108  -0.1182 0.0070  192 LYS A CG  
3022 C CD  . LYS A 195 ? 0.6718 0.8846 0.7348 0.2080  -0.1188 -0.0117 192 LYS A CD  
3023 C CE  . LYS A 195 ? 0.7503 0.9792 0.8222 0.2231  -0.1305 -0.0162 192 LYS A CE  
3024 N NZ  . LYS A 195 ? 0.7124 0.9669 0.8131 0.2252  -0.1261 -0.0331 192 LYS A NZ  
3038 N N   . ARG A 196 ? 0.3799 0.4740 0.4010 0.1805  -0.0817 0.0206  193 ARG A N   
3039 C CA  . ARG A 196 ? 0.3943 0.4833 0.4179 0.1664  -0.0688 0.0182  193 ARG A CA  
3040 C C   . ARG A 196 ? 0.3532 0.4112 0.3508 0.1560  -0.0638 0.0326  193 ARG A C   
3041 O O   . ARG A 196 ? 0.3534 0.4143 0.3481 0.1398  -0.0548 0.0307  193 ARG A O   
3042 C CB  . ARG A 196 ? 0.4873 0.5671 0.5261 0.1681  -0.0619 0.0116  193 ARG A CB  
3043 C CG  . ARG A 196 ? 0.4995 0.6153 0.5653 0.1668  -0.0593 -0.0056 193 ARG A CG  
3044 C CD  . ARG A 196 ? 0.5213 0.6306 0.5986 0.1624  -0.0490 -0.0127 193 ARG A CD  
3045 N NE  . ARG A 196 ? 0.4591 0.5923 0.5567 0.1667  -0.0492 -0.0259 193 ARG A NE  
3046 C CZ  . ARG A 196 ? 0.5736 0.7024 0.6805 0.1676  -0.0430 -0.0329 193 ARG A CZ  
3047 N NH1 . ARG A 196 ? 0.5204 0.6213 0.6193 0.1639  -0.0362 -0.0288 193 ARG A NH1 
3048 N NH2 . ARG A 196 ? 0.4511 0.6056 0.5754 0.1721  -0.0436 -0.0452 193 ARG A NH2 
3062 N N   . THR A 197 ? 0.4050 0.4333 0.3833 0.1651  -0.0699 0.0469  194 THR A N   
3063 C CA  . THR A 197 ? 0.3950 0.3965 0.3480 0.1533  -0.0644 0.0610  194 THR A CA  
3064 C C   . THR A 197 ? 0.3760 0.3959 0.3150 0.1464  -0.0660 0.0633  194 THR A C   
3065 O O   . THR A 197 ? 0.3671 0.3859 0.2988 0.1308  -0.0561 0.0637  194 THR A O   
3066 C CB  . THR A 197 ? 0.4994 0.4628 0.4326 0.1632  -0.0713 0.0769  194 THR A CB  
3067 O OG1 . THR A 197 ? 0.4886 0.4353 0.4367 0.1687  -0.0689 0.0714  194 THR A OG1 
3068 C CG2 . THR A 197 ? 0.5465 0.4844 0.4533 0.1481  -0.0642 0.0915  194 THR A CG2 
3076 N N   . MET A 198 ? 0.3928 0.4313 0.3286 0.1584  -0.0787 0.0633  195 MET A N   
3077 C CA  . MET A 198 ? 0.3656 0.4247 0.2879 0.1523  -0.0811 0.0632  195 MET A CA  
3078 C C   . MET A 198 ? 0.3696 0.4554 0.3098 0.1391  -0.0726 0.0468  195 MET A C   
3079 O O   . MET A 198 ? 0.3740 0.4661 0.3030 0.1276  -0.0675 0.0456  195 MET A O   
3080 C CB  . MET A 198 ? 0.4070 0.4844 0.3250 0.1686  -0.0978 0.0644  195 MET A CB  
3081 C CG  . MET A 198 ? 0.4890 0.5344 0.3890 0.1761  -0.1053 0.0802  195 MET A CG  
3082 S SD  . MET A 198 ? 0.6289 0.6442 0.4879 0.1635  -0.0994 0.1010  195 MET A SD  
3083 C CE  . MET A 198 ? 0.7380 0.7887 0.5829 0.1585  -0.1035 0.0967  195 MET A CE  
3093 N N   . PHE A 199 ? 0.3250 0.4259 0.2923 0.1401  -0.0708 0.0336  196 PHE A N   
3094 C CA  . PHE A 199 ? 0.3018 0.4218 0.2839 0.1261  -0.0629 0.0196  196 PHE A CA  
3095 C C   . PHE A 199 ? 0.3091 0.4087 0.2862 0.1121  -0.0499 0.0219  196 PHE A C   
3096 O O   . PHE A 199 ? 0.2871 0.3931 0.2602 0.1015  -0.0452 0.0169  196 PHE A O   
3097 C CB  . PHE A 199 ? 0.3104 0.4497 0.3203 0.1279  -0.0627 0.0066  196 PHE A CB  
3098 C CG  . PHE A 199 ? 0.2756 0.4294 0.2983 0.1122  -0.0552 -0.0059 196 PHE A CG  
3099 C CD1 . PHE A 199 ? 0.3085 0.4888 0.3351 0.1080  -0.0604 -0.0157 196 PHE A CD1 
3100 C CD2 . PHE A 199 ? 0.2415 0.3808 0.2704 0.1017  -0.0442 -0.0077 196 PHE A CD2 
3101 C CE1 . PHE A 199 ? 0.2668 0.4554 0.3033 0.0932  -0.0545 -0.0267 196 PHE A CE1 
3102 C CE2 . PHE A 199 ? 0.2476 0.3951 0.2849 0.0877  -0.0388 -0.0174 196 PHE A CE2 
3103 C CZ  . PHE A 199 ? 0.2228 0.3934 0.2642 0.0835  -0.0439 -0.0268 196 PHE A CZ  
3113 N N   . TRP A 200 ? 0.2778 0.3543 0.2568 0.1125  -0.0443 0.0274  197 TRP A N   
3114 C CA  . TRP A 200 ? 0.2749 0.3339 0.2498 0.1004  -0.0332 0.0296  197 TRP A CA  
3115 C C   . TRP A 200 ? 0.3087 0.3617 0.2618 0.0944  -0.0311 0.0374  197 TRP A C   
3116 O O   . TRP A 200 ? 0.2852 0.3410 0.2381 0.0837  -0.0235 0.0326  197 TRP A O   
3117 C CB  . TRP A 200 ? 0.3463 0.3812 0.3238 0.1034  -0.0300 0.0352  197 TRP A CB  
3118 C CG  . TRP A 200 ? 0.3563 0.3716 0.3270 0.0924  -0.0204 0.0398  197 TRP A CG  
3119 C CD1 . TRP A 200 ? 0.3655 0.3814 0.3467 0.0828  -0.0124 0.0328  197 TRP A CD1 
3120 C CD2 . TRP A 200 ? 0.3490 0.3420 0.3001 0.0895  -0.0185 0.0527  197 TRP A CD2 
3121 N NE1 . TRP A 200 ? 0.3691 0.3676 0.3409 0.0751  -0.0059 0.0392  197 TRP A NE1 
3122 C CE2 . TRP A 200 ? 0.3832 0.3678 0.3369 0.0777  -0.0087 0.0513  197 TRP A CE2 
3123 C CE3 . TRP A 200 ? 0.4369 0.4161 0.3675 0.0949  -0.0245 0.0660  197 TRP A CE3 
3124 C CZ2 . TRP A 200 ? 0.4558 0.4222 0.3946 0.0698  -0.0037 0.0611  197 TRP A CZ2 
3125 C CZ3 . TRP A 200 ? 0.5444 0.5014 0.4574 0.0862  -0.0191 0.0775  197 TRP A CZ3 
3126 C CH2 . TRP A 200 ? 0.4867 0.4389 0.4052 0.0731  -0.0083 0.0743  197 TRP A CH2 
3137 N N   . LEU A 201 ? 0.3443 0.3903 0.2783 0.1016  -0.0380 0.0490  198 LEU A N   
3138 C CA  . LEU A 201 ? 0.3854 0.4263 0.2951 0.0948  -0.0352 0.0580  198 LEU A CA  
3139 C C   . LEU A 201 ? 0.3351 0.4020 0.2437 0.0892  -0.0344 0.0474  198 LEU A C   
3140 O O   . LEU A 201 ? 0.3897 0.4586 0.2927 0.0788  -0.0258 0.0447  198 LEU A O   
3141 C CB  . LEU A 201 ? 0.4237 0.4511 0.3115 0.1044  -0.0447 0.0735  198 LEU A CB  
3142 C CG  . LEU A 201 ? 0.6476 0.6433 0.5137 0.0996  -0.0409 0.0906  198 LEU A CG  
3143 C CD1 . LEU A 201 ? 0.6580 0.6442 0.4988 0.1099  -0.0533 0.1056  198 LEU A CD1 
3144 C CD2 . LEU A 201 ? 0.5570 0.5548 0.4124 0.0832  -0.0289 0.0914  198 LEU A CD2 
3156 N N   . GLU A 202 ? 0.3436 0.4320 0.2596 0.0960  -0.0434 0.0392  199 GLU A N   
3157 C CA  . GLU A 202 ? 0.3526 0.4648 0.2658 0.0912  -0.0445 0.0281  199 GLU A CA  
3158 C C   . GLU A 202 ? 0.3417 0.4612 0.2754 0.0826  -0.0378 0.0125  199 GLU A C   
3159 O O   . GLU A 202 ? 0.3171 0.4447 0.2469 0.0755  -0.0336 0.0040  199 GLU A O   
3160 C CB  . GLU A 202 ? 0.3824 0.5162 0.2955 0.1008  -0.0577 0.0246  199 GLU A CB  
3161 C CG  . GLU A 202 ? 0.4442 0.6029 0.3563 0.0951  -0.0594 0.0104  199 GLU A CG  
3162 C CD  . GLU A 202 ? 0.6480 0.8295 0.5541 0.1039  -0.0733 0.0085  199 GLU A CD  
3163 O OE1 . GLU A 202 ? 0.6162 0.8191 0.5200 0.0995  -0.0760 -0.0039 199 GLU A OE1 
3164 O OE2 . GLU A 202 ? 0.6065 0.7845 0.5113 0.1161  -0.0822 0.0183  199 GLU A OE2 
3171 N N   . PHE A 203 ? 0.2884 0.4041 0.2429 0.0832  -0.0368 0.0083  200 PHE A N   
3172 C CA  . PHE A 203 ? 0.2445 0.3671 0.2169 0.0753  -0.0332 -0.0057 200 PHE A CA  
3173 C C   . PHE A 203 ? 0.2292 0.3338 0.2105 0.0690  -0.0241 -0.0054 200 PHE A C   
3174 O O   . PHE A 203 ? 0.2273 0.3332 0.2200 0.0620  -0.0215 -0.0152 200 PHE A O   
3175 C CB  . PHE A 203 ? 0.2554 0.3950 0.2454 0.0785  -0.0399 -0.0132 200 PHE A CB  
3176 C CG  . PHE A 203 ? 0.2583 0.4216 0.2443 0.0826  -0.0498 -0.0185 200 PHE A CG  
3177 C CD1 . PHE A 203 ? 0.3173 0.4953 0.3067 0.0745  -0.0510 -0.0321 200 PHE A CD1 
3178 C CD2 . PHE A 203 ? 0.3181 0.4885 0.2965 0.0950  -0.0590 -0.0105 200 PHE A CD2 
3179 C CE1 . PHE A 203 ? 0.3320 0.5340 0.3176 0.0775  -0.0606 -0.0386 200 PHE A CE1 
3180 C CE2 . PHE A 203 ? 0.3633 0.5581 0.3368 0.0994  -0.0695 -0.0156 200 PHE A CE2 
3181 C CZ  . PHE A 203 ? 0.3616 0.5737 0.3393 0.0899  -0.0700 -0.0304 200 PHE A CZ  
3191 N N   . GLU A 204 ? 0.2222 0.3087 0.1980 0.0706  -0.0197 0.0055  201 GLU A N   
3192 C CA  . GLU A 204 ? 0.2043 0.2761 0.1888 0.0651  -0.0122 0.0052  201 GLU A CA  
3193 C C   . GLU A 204 ? 0.2239 0.2837 0.1978 0.0606  -0.0054 0.0111  201 GLU A C   
3194 O O   . GLU A 204 ? 0.2463 0.3040 0.2257 0.0548  -0.0003 0.0053  201 GLU A O   
3195 C CB  . GLU A 204 ? 0.2173 0.2809 0.2114 0.0697  -0.0127 0.0089  201 GLU A CB  
3196 C CG  . GLU A 204 ? 0.2176 0.2697 0.2210 0.0634  -0.0060 0.0067  201 GLU A CG  
3197 C CD  . GLU A 204 ? 0.2295 0.2845 0.2465 0.0659  -0.0067 0.0033  201 GLU A CD  
3198 O OE1 . GLU A 204 ? 0.2253 0.2976 0.2515 0.0662  -0.0103 -0.0038 201 GLU A OE1 
3199 O OE2 . GLU A 204 ? 0.2891 0.3304 0.3074 0.0668  -0.0033 0.0069  201 GLU A OE2 
3206 N N   . ILE A 205 ? 0.2519 0.3028 0.2112 0.0628  -0.0051 0.0226  202 ILE A N   
3207 C CA  . ILE A 205 ? 0.2900 0.3290 0.2425 0.0561  0.0026  0.0284  202 ILE A CA  
3208 C C   . ILE A 205 ? 0.2537 0.3058 0.2040 0.0499  0.0077  0.0207  202 ILE A C   
3209 O O   . ILE A 205 ? 0.2795 0.3297 0.2385 0.0450  0.0134  0.0158  202 ILE A O   
3210 C CB  . ILE A 205 ? 0.3447 0.3694 0.2792 0.0577  0.0015  0.0433  202 ILE A CB  
3211 C CG1 . ILE A 205 ? 0.4805 0.4905 0.4111 0.0485  0.0100  0.0492  202 ILE A CG1 
3212 C CG2 . ILE A 205 ? 0.3800 0.4155 0.2958 0.0594  -0.0024 0.0475  202 ILE A CG2 
3213 C CD1 . ILE A 205 ? 0.4975 0.5198 0.4207 0.0395  0.0171  0.0471  202 ILE A CD1 
3225 N N   . ARG A 206 ? 0.2605 0.3276 0.1998 0.0509  0.0053  0.0179  203 ARG A N   
3226 C CA  . ARG A 206 ? 0.2824 0.3636 0.2200 0.0462  0.0106  0.0084  203 ARG A CA  
3227 C C   . ARG A 206 ? 0.2739 0.3583 0.2295 0.0467  0.0097  -0.0062 203 ARG A C   
3228 O O   . ARG A 206 ? 0.2654 0.3515 0.2275 0.0440  0.0147  -0.0129 203 ARG A O   
3229 C CB  . ARG A 206 ? 0.2719 0.3698 0.1923 0.0472  0.0080  0.0070  203 ARG A CB  
3230 C CG  . ARG A 206 ? 0.3063 0.3996 0.2035 0.0453  0.0089  0.0230  203 ARG A CG  
3231 C CD  . ARG A 206 ? 0.3455 0.4548 0.2235 0.0478  0.0036  0.0232  203 ARG A CD  
3232 N NE  . ARG A 206 ? 0.3181 0.4298 0.2021 0.0566  -0.0077 0.0208  203 ARG A NE  
3233 C CZ  . ARG A 206 ? 0.3181 0.4458 0.1900 0.0605  -0.0153 0.0182  203 ARG A CZ  
3234 N NH1 . ARG A 206 ? 0.3823 0.5239 0.2330 0.0566  -0.0127 0.0182  203 ARG A NH1 
3235 N NH2 . ARG A 206 ? 0.3599 0.4928 0.2414 0.0680  -0.0255 0.0146  203 ARG A NH2 
3249 N N   . GLN A 207 ? 0.2444 0.3292 0.2079 0.0500  0.0029  -0.0109 204 GLN A N   
3250 C CA  . GLN A 207 ? 0.2216 0.3059 0.1987 0.0489  0.0010  -0.0235 204 GLN A CA  
3251 C C   . GLN A 207 ? 0.2314 0.3010 0.2200 0.0467  0.0043  -0.0222 204 GLN A C   
3252 O O   . GLN A 207 ? 0.2982 0.3647 0.2934 0.0457  0.0051  -0.0305 204 GLN A O   
3253 C CB  . GLN A 207 ? 0.2460 0.3352 0.2283 0.0500  -0.0062 -0.0271 204 GLN A CB  
3254 C CG  . GLN A 207 ? 0.2638 0.3706 0.2359 0.0523  -0.0115 -0.0313 204 GLN A CG  
3255 C CD  . GLN A 207 ? 0.2383 0.3499 0.1982 0.0573  -0.0148 -0.0192 204 GLN A CD  
3256 O OE1 . GLN A 207 ? 0.2528 0.3522 0.2093 0.0591  -0.0121 -0.0067 204 GLN A OE1 
3257 N NE2 . GLN A 207 ? 0.2459 0.3739 0.1979 0.0600  -0.0215 -0.0228 204 GLN A NE2 
3266 N N   . TYR A 208 ? 0.2028 0.2628 0.1929 0.0467  0.0056  -0.0122 205 TYR A N   
3267 C CA  . TYR A 208 ? 0.1823 0.2299 0.1823 0.0443  0.0078  -0.0120 205 TYR A CA  
3268 C C   . TYR A 208 ? 0.1997 0.2450 0.1987 0.0423  0.0135  -0.0103 205 TYR A C   
3269 O O   . TYR A 208 ? 0.2071 0.2485 0.2140 0.0414  0.0140  -0.0154 205 TYR A O   
3270 C CB  . TYR A 208 ? 0.1992 0.2389 0.2028 0.0452  0.0072  -0.0048 205 TYR A CB  
3271 C CG  . TYR A 208 ? 0.1809 0.2254 0.1915 0.0456  0.0028  -0.0086 205 TYR A CG  
3272 C CD1 . TYR A 208 ? 0.1950 0.2524 0.2046 0.0465  -0.0019 -0.0144 205 TYR A CD1 
3273 C CD2 . TYR A 208 ? 0.1861 0.2252 0.2045 0.0442  0.0036  -0.0075 205 TYR A CD2 
3274 C CE1 . TYR A 208 ? 0.2167 0.2823 0.2344 0.0451  -0.0056 -0.0189 205 TYR A CE1 
3275 C CE2 . TYR A 208 ? 0.2009 0.2492 0.2269 0.0429  0.0007  -0.0119 205 TYR A CE2 
3276 C CZ  . TYR A 208 ? 0.1905 0.2525 0.2169 0.0430  -0.0039 -0.0175 205 TYR A CZ  
3277 O OH  . TYR A 208 ? 0.2084 0.2833 0.2440 0.0401  -0.0065 -0.0229 205 TYR A OH  
3287 N N   . THR A 209 ? 0.2139 0.2619 0.2029 0.0410  0.0172  -0.0028 206 THR A N   
3288 C CA  . THR A 209 ? 0.2117 0.2604 0.2010 0.0366  0.0235  -0.0014 206 THR A CA  
3289 C C   . THR A 209 ? 0.2255 0.2900 0.2174 0.0366  0.0259  -0.0122 206 THR A C   
3290 O O   . THR A 209 ? 0.2204 0.2899 0.2179 0.0337  0.0304  -0.0145 206 THR A O   
3291 C CB  . THR A 209 ? 0.2329 0.2780 0.2093 0.0324  0.0275  0.0101  206 THR A CB  
3292 O OG1 . THR A 209 ? 0.2713 0.3271 0.2334 0.0329  0.0273  0.0120  206 THR A OG1 
3293 C CG2 . THR A 209 ? 0.2758 0.3026 0.2510 0.0344  0.0246  0.0194  206 THR A CG2 
3301 N N   . HIS A 210 ? 0.2019 0.2764 0.1908 0.0401  0.0231  -0.0201 207 HIS A N   
3302 C CA  . HIS A 210 ? 0.1889 0.2773 0.1823 0.0424  0.0245  -0.0335 207 HIS A CA  
3303 C C   . HIS A 210 ? 0.2418 0.3226 0.2448 0.0475  0.0176  -0.0443 207 HIS A C   
3304 O O   . HIS A 210 ? 0.2406 0.3299 0.2449 0.0514  0.0160  -0.0571 207 HIS A O   
3305 C CB  . HIS A 210 ? 0.2194 0.3270 0.1999 0.0414  0.0279  -0.0366 207 HIS A CB  
3306 C CG  . HIS A 210 ? 0.2419 0.3692 0.2271 0.0424  0.0330  -0.0494 207 HIS A CG  
3307 N ND1 . HIS A 210 ? 0.2602 0.3970 0.2502 0.0379  0.0402  -0.0480 207 HIS A ND1 
3308 C CD2 . HIS A 210 ? 0.2408 0.3816 0.2286 0.0479  0.0318  -0.0657 207 HIS A CD2 
3309 C CE1 . HIS A 210 ? 0.2622 0.4205 0.2587 0.0413  0.0434  -0.0631 207 HIS A CE1 
3310 N NE2 . HIS A 210 ? 0.2838 0.4437 0.2788 0.0481  0.0383  -0.0742 207 HIS A NE2 
3318 N N   . SER A 211 ? 0.2176 0.2810 0.2267 0.0470  0.0136  -0.0398 208 SER A N   
3319 C CA  . SER A 211 ? 0.2143 0.2664 0.2295 0.0492  0.0071  -0.0477 208 SER A CA  
3320 C C   . SER A 211 ? 0.2134 0.2595 0.2374 0.0533  0.0054  -0.0545 208 SER A C   
3321 O O   . SER A 211 ? 0.2240 0.2783 0.2517 0.0544  0.0093  -0.0539 208 SER A O   
3322 C CB  . SER A 211 ? 0.1982 0.2369 0.2145 0.0453  0.0042  -0.0400 208 SER A CB  
3323 O OG  . SER A 211 ? 0.2181 0.2483 0.2378 0.0435  0.0063  -0.0320 208 SER A OG  
3329 N N   . ASN A 212 ? 0.2166 0.2484 0.2437 0.0557  -0.0013 -0.0617 209 ASN A N   
3330 C CA  . ASN A 212 ? 0.2261 0.2513 0.2603 0.0629  -0.0056 -0.0708 209 ASN A CA  
3331 C C   . ASN A 212 ? 0.2798 0.2893 0.3175 0.0623  -0.0084 -0.0628 209 ASN A C   
3332 O O   . ASN A 212 ? 0.2789 0.2662 0.3152 0.0614  -0.0149 -0.0614 209 ASN A O   
3333 C CB  . ASN A 212 ? 0.2771 0.2890 0.3108 0.0659  -0.0126 -0.0821 209 ASN A CB  
3334 C CG  . ASN A 212 ? 0.3578 0.3577 0.3981 0.0755  -0.0191 -0.0917 209 ASN A CG  
3335 O OD1 . ASN A 212 ? 0.3106 0.3268 0.3578 0.0841  -0.0173 -0.0997 209 ASN A OD1 
3336 N ND2 . ASN A 212 ? 0.3456 0.3164 0.3837 0.0744  -0.0272 -0.0910 209 ASN A ND2 
3343 N N   . ILE A 213 ? 0.2102 0.2318 0.2514 0.0621  -0.0036 -0.0581 210 ILE A N   
3344 C CA  . ILE A 213 ? 0.2071 0.2204 0.2522 0.0626  -0.0062 -0.0529 210 ILE A CA  
3345 C C   . ILE A 213 ? 0.2242 0.2561 0.2790 0.0697  -0.0053 -0.0613 210 ILE A C   
3346 O O   . ILE A 213 ? 0.2414 0.2957 0.2978 0.0677  0.0023  -0.0639 210 ILE A O   
3347 C CB  . ILE A 213 ? 0.2557 0.2685 0.2972 0.0543  -0.0012 -0.0408 210 ILE A CB  
3348 C CG1 . ILE A 213 ? 0.2253 0.2262 0.2597 0.0481  -0.0013 -0.0341 210 ILE A CG1 
3349 C CG2 . ILE A 213 ? 0.2579 0.2647 0.3027 0.0549  -0.0043 -0.0374 210 ILE A CG2 
3350 C CD1 . ILE A 213 ? 0.2449 0.2255 0.2766 0.0468  -0.0079 -0.0335 210 ILE A CD1 
3362 N N   . THR A 214 ? 0.2321 0.2558 0.2931 0.0778  -0.0133 -0.0657 211 THR A N   
3363 C CA  . THR A 214 ? 0.2122 0.2563 0.2857 0.0864  -0.0142 -0.0754 211 THR A CA  
3364 C C   . THR A 214 ? 0.2290 0.2714 0.3058 0.0851  -0.0172 -0.0686 211 THR A C   
3365 O O   . THR A 214 ? 0.2539 0.2745 0.3220 0.0804  -0.0208 -0.0582 211 THR A O   
3366 C CB  . THR A 214 ? 0.3136 0.3515 0.3934 0.1008  -0.0235 -0.0889 211 THR A CB  
3367 O OG1 . THR A 214 ? 0.3500 0.3566 0.4248 0.1045  -0.0348 -0.0831 211 THR A OG1 
3368 C CG2 . THR A 214 ? 0.3390 0.3744 0.4141 0.1017  -0.0220 -0.0969 211 THR A CG2 
3376 N N   . LEU A 215 ? 0.2250 0.2934 0.3145 0.0887  -0.0155 -0.0757 212 LEU A N   
3377 C CA  . LEU A 215 ? 0.2283 0.2982 0.3224 0.0889  -0.0203 -0.0720 212 LEU A CA  
3378 C C   . LEU A 215 ? 0.3069 0.3507 0.3972 0.0990  -0.0345 -0.0704 212 LEU A C   
3379 O O   . LEU A 215 ? 0.2999 0.3304 0.3835 0.0952  -0.0390 -0.0611 212 LEU A O   
3380 C CB  . LEU A 215 ? 0.3054 0.4118 0.4169 0.0924  -0.0173 -0.0834 212 LEU A CB  
3381 C CG  . LEU A 215 ? 0.2962 0.4266 0.4089 0.0784  -0.0029 -0.0820 212 LEU A CG  
3382 C CD1 . LEU A 215 ? 0.2886 0.4589 0.4198 0.0810  0.0005  -0.0954 212 LEU A CD1 
3383 C CD2 . LEU A 215 ? 0.2889 0.4070 0.3926 0.0649  0.0010  -0.0685 212 LEU A CD2 
3395 N N   . ASP A 216 ? 0.2778 0.3116 0.3700 0.1110  -0.0418 -0.0790 213 ASP A N   
3396 C CA  . ASP A 216 ? 0.3766 0.3805 0.4619 0.1196  -0.0560 -0.0759 213 ASP A CA  
3397 C C   . ASP A 216 ? 0.3218 0.2920 0.3888 0.1097  -0.0576 -0.0614 213 ASP A C   
3398 O O   . ASP A 216 ? 0.4454 0.3925 0.5031 0.1116  -0.0676 -0.0536 213 ASP A O   
3399 C CB  . ASP A 216 ? 0.3987 0.3963 0.4844 0.1272  -0.0606 -0.0856 213 ASP A CB  
3400 C CG  . ASP A 216 ? 0.5394 0.5607 0.6381 0.1372  -0.0646 -0.0967 213 ASP A CG  
3401 O OD1 . ASP A 216 ? 0.5897 0.6071 0.6902 0.1453  -0.0694 -0.1062 213 ASP A OD1 
3402 O OD2 . ASP A 216 ? 0.5868 0.6311 0.6946 0.1371  -0.0635 -0.0972 213 ASP A OD2 
3407 N N   . ASP A 217 ? 0.3213 0.2902 0.3817 0.0975  -0.0475 -0.0570 214 ASP A N   
3408 C CA  . ASP A 217 ? 0.3543 0.2987 0.3992 0.0857  -0.0470 -0.0440 214 ASP A CA  
3409 C C   . ASP A 217 ? 0.3845 0.3311 0.4246 0.0788  -0.0459 -0.0340 214 ASP A C   
3410 O O   . ASP A 217 ? 0.4946 0.4194 0.5215 0.0733  -0.0502 -0.0244 214 ASP A O   
3411 C CB  . ASP A 217 ? 0.3964 0.3458 0.4382 0.0755  -0.0368 -0.0427 214 ASP A CB  
3412 C CG  . ASP A 217 ? 0.4281 0.3724 0.4713 0.0802  -0.0386 -0.0525 214 ASP A CG  
3413 O OD1 . ASP A 217 ? 0.4447 0.3651 0.4844 0.0862  -0.0483 -0.0556 214 ASP A OD1 
3414 O OD2 . ASP A 217 ? 0.3658 0.3285 0.4122 0.0777  -0.0306 -0.0572 214 ASP A OD2 
3419 N N   . PHE A 218 ? 0.3150 0.2881 0.3647 0.0773  -0.0395 -0.0365 215 PHE A N   
3420 C CA  . PHE A 218 ? 0.2894 0.2659 0.3353 0.0707  -0.0385 -0.0295 215 PHE A CA  
3421 C C   . PHE A 218 ? 0.3680 0.3375 0.4124 0.0793  -0.0513 -0.0291 215 PHE A C   
3422 O O   . PHE A 218 ? 0.3260 0.2833 0.3583 0.0743  -0.0549 -0.0205 215 PHE A O   
3423 C CB  . PHE A 218 ? 0.2802 0.2844 0.3368 0.0659  -0.0292 -0.0332 215 PHE A CB  
3424 C CG  . PHE A 218 ? 0.2862 0.2953 0.3415 0.0576  -0.0178 -0.0313 215 PHE A CG  
3425 C CD1 . PHE A 218 ? 0.4224 0.4202 0.4680 0.0486  -0.0132 -0.0230 215 PHE A CD1 
3426 C CD2 . PHE A 218 ? 0.3472 0.3741 0.4106 0.0593  -0.0122 -0.0382 215 PHE A CD2 
3427 C CE1 . PHE A 218 ? 0.4405 0.4420 0.4848 0.0432  -0.0047 -0.0211 215 PHE A CE1 
3428 C CE2 . PHE A 218 ? 0.3542 0.3838 0.4135 0.0523  -0.0032 -0.0349 215 PHE A CE2 
3429 C CZ  . PHE A 218 ? 0.2936 0.3095 0.3437 0.0452  -0.0004 -0.0262 215 PHE A CZ  
3439 N N   . THR A 219 ? 0.3236 0.3023 0.3797 0.0932  -0.0587 -0.0389 216 THR A N   
3440 C CA  . THR A 219 ? 0.3317 0.3076 0.3884 0.1039  -0.0724 -0.0394 216 THR A CA  
3441 C C   . THR A 219 ? 0.3841 0.3213 0.4214 0.1061  -0.0839 -0.0292 216 THR A C   
3442 O O   . THR A 219 ? 0.3830 0.3117 0.4107 0.1077  -0.0932 -0.0224 216 THR A O   
3443 C CB  . THR A 219 ? 0.3482 0.3464 0.4248 0.1200  -0.0777 -0.0544 216 THR A CB  
3444 O OG1 . THR A 219 ? 0.4282 0.4641 0.5205 0.1140  -0.0661 -0.0620 216 THR A OG1 
3445 C CG2 . THR A 219 ? 0.4162 0.4119 0.4937 0.1331  -0.0936 -0.0555 216 THR A CG2 
3453 N N   . LYS A 220 ? 0.3855 0.2990 0.4151 0.1041  -0.0831 -0.0274 217 LYS A N   
3454 C CA  . LYS A 220 ? 0.4322 0.3060 0.4422 0.1038  -0.0936 -0.0173 217 LYS A CA  
3455 C C   . LYS A 220 ? 0.4014 0.2642 0.3923 0.0890  -0.0912 -0.0028 217 LYS A C   
3456 O O   . LYS A 220 ? 0.5185 0.3543 0.4913 0.0895  -0.1021 0.0072  217 LYS A O   
3457 C CB  . LYS A 220 ? 0.5211 0.3743 0.5271 0.1001  -0.0908 -0.0191 217 LYS A CB  
3458 C CG  . LYS A 220 ? 0.6817 0.4983 0.6722 0.1009  -0.1015 -0.0133 217 LYS A CG  
3459 C CD  . LYS A 220 ? 0.8025 0.6034 0.7918 0.0960  -0.0982 -0.0178 217 LYS A CD  
3460 C CE  . LYS A 220 ? 0.9796 0.7407 0.9491 0.0898  -0.1063 -0.0081 217 LYS A CE  
3461 N NZ  . LYS A 220 ? 0.8569 0.6062 0.8309 0.0990  -0.1125 -0.0177 217 LYS A NZ  
3475 N N   . TYR A 221 ? 0.3886 0.2702 0.3816 0.0759  -0.0772 -0.0014 218 TYR A N   
3476 C CA  . TYR A 221 ? 0.4283 0.3036 0.4049 0.0615  -0.0726 0.0096  218 TYR A CA  
3477 C C   . TYR A 221 ? 0.3461 0.2488 0.3295 0.0583  -0.0665 0.0071  218 TYR A C   
3478 O O   . TYR A 221 ? 0.3544 0.2625 0.3323 0.0463  -0.0570 0.0107  218 TYR A O   
3479 C CB  . TYR A 221 ? 0.4589 0.3278 0.4305 0.0480  -0.0618 0.0127  218 TYR A CB  
3480 C CG  . TYR A 221 ? 0.4467 0.2895 0.4129 0.0489  -0.0670 0.0134  218 TYR A CG  
3481 C CD1 . TYR A 221 ? 0.5238 0.3341 0.4703 0.0451  -0.0761 0.0234  218 TYR A CD1 
3482 C CD2 . TYR A 221 ? 0.4742 0.3242 0.4536 0.0523  -0.0626 0.0040  218 TYR A CD2 
3483 C CE1 . TYR A 221 ? 0.6628 0.4453 0.6039 0.0444  -0.0811 0.0236  218 TYR A CE1 
3484 C CE2 . TYR A 221 ? 0.5445 0.3703 0.5194 0.0523  -0.0675 0.0026  218 TYR A CE2 
3485 C CZ  . TYR A 221 ? 0.5632 0.3545 0.5196 0.0481  -0.0766 0.0121  218 TYR A CZ  
3486 O OH  . TYR A 221 ? 0.6803 0.4445 0.6321 0.0469  -0.0817 0.0101  218 TYR A OH  
3496 N N   . SER A 222 ? 0.3805 0.3013 0.3769 0.0690  -0.0722 -0.0003 219 SER A N   
3497 C CA  . SER A 222 ? 0.3113 0.2596 0.3175 0.0643  -0.0651 -0.0050 219 SER A CA  
3498 C C   . SER A 222 ? 0.2904 0.2353 0.2809 0.0549  -0.0650 0.0022  219 SER A C   
3499 O O   . SER A 222 ? 0.3561 0.3154 0.3502 0.0460  -0.0551 -0.0003 219 SER A O   
3500 C CB  . SER A 222 ? 0.3745 0.3459 0.3985 0.0762  -0.0717 -0.0152 219 SER A CB  
3501 O OG  . SER A 222 ? 0.3976 0.3599 0.4137 0.0856  -0.0873 -0.0122 219 SER A OG  
3507 N N   . ASP A 223 ? 0.3276 0.2518 0.2991 0.0561  -0.0756 0.0110  220 ASP A N   
3508 C CA  . ASP A 223 ? 0.3411 0.2630 0.2945 0.0466  -0.0756 0.0177  220 ASP A CA  
3509 C C   . ASP A 223 ? 0.3895 0.3097 0.3357 0.0319  -0.0614 0.0207  220 ASP A C   
3510 O O   . ASP A 223 ? 0.3877 0.3140 0.3235 0.0235  -0.0576 0.0220  220 ASP A O   
3511 C CB  . ASP A 223 ? 0.4533 0.3491 0.3835 0.0496  -0.0898 0.0290  220 ASP A CB  
3512 C CG  . ASP A 223 ? 0.6773 0.5433 0.5973 0.0473  -0.0904 0.0366  220 ASP A CG  
3513 O OD1 . ASP A 223 ? 0.6733 0.5330 0.6061 0.0578  -0.0943 0.0316  220 ASP A OD1 
3514 O OD2 . ASP A 223 ? 0.7485 0.5989 0.6481 0.0339  -0.0862 0.0464  220 ASP A OD2 
3519 N N   . LYS A 224 ? 0.3058 0.2196 0.2576 0.0294  -0.0540 0.0205  221 LYS A N   
3520 C CA  . LYS A 224 ? 0.3023 0.2168 0.2490 0.0172  -0.0418 0.0224  221 LYS A CA  
3521 C C   . LYS A 224 ? 0.2769 0.2120 0.2399 0.0156  -0.0306 0.0141  221 LYS A C   
3522 O O   . LYS A 224 ? 0.2842 0.2232 0.2448 0.0077  -0.0212 0.0139  221 LYS A O   
3523 C CB  . LYS A 224 ? 0.3135 0.2123 0.2584 0.0143  -0.0400 0.0259  221 LYS A CB  
3524 C CG  . LYS A 224 ? 0.3625 0.2341 0.2867 0.0106  -0.0487 0.0363  221 LYS A CG  
3525 C CD  . LYS A 224 ? 0.3797 0.2369 0.3062 0.0073  -0.0466 0.0369  221 LYS A CD  
3526 C CE  . LYS A 224 ? 0.5098 0.3346 0.4150 0.0003  -0.0542 0.0477  221 LYS A CE  
3527 N NZ  . LYS A 224 ? 0.5815 0.3970 0.4636 -0.0071 -0.0580 0.0582  221 LYS A NZ  
3541 N N   . ILE A 225 ? 0.2681 0.2160 0.2476 0.0229  -0.0312 0.0071  222 ILE A N   
3542 C CA  . ILE A 225 ? 0.2386 0.1991 0.2319 0.0215  -0.0212 0.0014  222 ILE A CA  
3543 C C   . ILE A 225 ? 0.2403 0.2144 0.2386 0.0184  -0.0178 -0.0038 222 ILE A C   
3544 O O   . ILE A 225 ? 0.2452 0.2276 0.2464 0.0212  -0.0243 -0.0069 222 ILE A O   
3545 C CB  . ILE A 225 ? 0.2476 0.2136 0.2548 0.0293  -0.0224 -0.0028 222 ILE A CB  
3546 C CG1 . ILE A 225 ? 0.2579 0.2088 0.2608 0.0326  -0.0262 0.0002  222 ILE A CG1 
3547 C CG2 . ILE A 225 ? 0.2262 0.2042 0.2442 0.0269  -0.0127 -0.0069 222 ILE A CG2 
3548 C CD1 . ILE A 225 ? 0.2798 0.2368 0.2954 0.0422  -0.0290 -0.0063 222 ILE A CD1 
3560 N N   . THR A 226 ? 0.2382 0.2145 0.2386 0.0131  -0.0084 -0.0056 223 THR A N   
3561 C CA  . THR A 226 ? 0.2126 0.1976 0.2199 0.0097  -0.0039 -0.0114 223 THR A CA  
3562 C C   . THR A 226 ? 0.2114 0.1977 0.2286 0.0101  0.0032  -0.0123 223 THR A C   
3563 O O   . THR A 226 ? 0.2203 0.2007 0.2359 0.0111  0.0071  -0.0093 223 THR A O   
3564 C CB  . THR A 226 ? 0.2389 0.2215 0.2373 0.0039  0.0001  -0.0133 223 THR A CB  
3565 O OG1 . THR A 226 ? 0.2971 0.2789 0.2825 0.0025  -0.0065 -0.0113 223 THR A OG1 
3566 C CG2 . THR A 226 ? 0.2655 0.2525 0.2706 -0.0001 0.0040  -0.0204 223 THR A CG2 
3574 N N   . LEU A 227 ? 0.1940 0.1890 0.2207 0.0086  0.0046  -0.0162 224 LEU A N   
3575 C CA  . LEU A 227 ? 0.2061 0.2007 0.2386 0.0066  0.0115  -0.0157 224 LEU A CA  
3576 C C   . LEU A 227 ? 0.2111 0.1984 0.2415 0.0004  0.0161  -0.0180 224 LEU A C   
3577 O O   . LEU A 227 ? 0.2443 0.2355 0.2752 -0.0042 0.0142  -0.0230 224 LEU A O   
3578 C CB  . LEU A 227 ? 0.2237 0.2327 0.2665 0.0063  0.0113  -0.0186 224 LEU A CB  
3579 C CG  . LEU A 227 ? 0.2019 0.2197 0.2490 0.0143  0.0053  -0.0198 224 LEU A CG  
3580 C CD1 . LEU A 227 ? 0.2217 0.2599 0.2814 0.0136  0.0060  -0.0257 224 LEU A CD1 
3581 C CD2 . LEU A 227 ? 0.2272 0.2364 0.2701 0.0190  0.0067  -0.0156 224 LEU A CD2 
3593 N N   . LEU A 228 ? 0.2050 0.1815 0.2331 0.0011  0.0212  -0.0152 225 LEU A N   
3594 C CA  . LEU A 228 ? 0.2218 0.1868 0.2476 -0.0025 0.0248  -0.0179 225 LEU A CA  
3595 C C   . LEU A 228 ? 0.2457 0.2022 0.2732 -0.0057 0.0289  -0.0146 225 LEU A C   
3596 O O   . LEU A 228 ? 0.2420 0.1966 0.2685 -0.0017 0.0303  -0.0087 225 LEU A O   
3597 C CB  . LEU A 228 ? 0.2205 0.1783 0.2413 0.0026  0.0261  -0.0182 225 LEU A CB  
3598 C CG  . LEU A 228 ? 0.2160 0.1802 0.2314 0.0028  0.0237  -0.0212 225 LEU A CG  
3599 C CD1 . LEU A 228 ? 0.2401 0.2032 0.2528 0.0070  0.0266  -0.0218 225 LEU A CD1 
3600 C CD2 . LEU A 228 ? 0.2660 0.2313 0.2787 -0.0028 0.0225  -0.0283 225 LEU A CD2 
3612 N N   . ASN A 229 ? 0.2364 0.1865 0.2648 -0.0138 0.0306  -0.0183 226 ASN A N   
3613 C CA  . ASN A 229 ? 0.2434 0.1801 0.2703 -0.0201 0.0346  -0.0144 226 ASN A CA  
3614 C C   . ASN A 229 ? 0.2693 0.1833 0.2916 -0.0209 0.0354  -0.0180 226 ASN A C   
3615 O O   . ASN A 229 ? 0.3009 0.2154 0.3241 -0.0242 0.0340  -0.0267 226 ASN A O   
3616 C CB  . ASN A 229 ? 0.2475 0.1962 0.2804 -0.0319 0.0364  -0.0166 226 ASN A CB  
3617 C CG  . ASN A 229 ? 0.2603 0.2285 0.2977 -0.0313 0.0377  -0.0128 226 ASN A CG  
3618 O OD1 . ASN A 229 ? 0.2774 0.2462 0.3117 -0.0229 0.0373  -0.0076 226 ASN A OD1 
3619 N ND2 . ASN A 229 ? 0.2852 0.2711 0.3306 -0.0408 0.0393  -0.0169 226 ASN A ND2 
3626 N N   . GLY A 230 ? 0.2753 0.1688 0.2919 -0.0173 0.0367  -0.0120 227 GLY A N   
3627 C CA  . GLY A 230 ? 0.2800 0.1486 0.2926 -0.0163 0.0365  -0.0161 227 GLY A CA  
3628 C C   . GLY A 230 ? 0.3321 0.1871 0.3437 -0.0309 0.0384  -0.0186 227 GLY A C   
3629 O O   . GLY A 230 ? 0.3535 0.2125 0.3651 -0.0417 0.0411  -0.0128 227 GLY A O   
3633 N N   . THR A 231 ? 0.3422 0.1815 0.3529 -0.0322 0.0374  -0.0282 228 THR A N   
3634 C CA  . THR A 231 ? 0.3804 0.2027 0.3896 -0.0474 0.0388  -0.0318 228 THR A CA  
3635 C C   . THR A 231 ? 0.3840 0.1714 0.3838 -0.0507 0.0399  -0.0217 228 THR A C   
3636 O O   . THR A 231 ? 0.4583 0.2322 0.4554 -0.0672 0.0423  -0.0204 228 THR A O   
3637 C CB  . THR A 231 ? 0.4400 0.2544 0.4501 -0.0477 0.0369  -0.0469 228 THR A CB  
3638 O OG1 . THR A 231 ? 0.4635 0.2570 0.4694 -0.0330 0.0352  -0.0494 228 THR A OG1 
3639 C CG2 . THR A 231 ? 0.3890 0.2361 0.4047 -0.0465 0.0352  -0.0553 228 THR A CG2 
3647 N N   . ASP A 232 ? 0.4155 0.1882 0.4094 -0.0361 0.0377  -0.0142 229 ASP A N   
3648 C CA  . ASP A 232 ? 0.4317 0.1668 0.4136 -0.0365 0.0366  -0.0036 229 ASP A CA  
3649 C C   . ASP A 232 ? 0.4553 0.1961 0.4302 -0.0367 0.0379  0.0125  229 ASP A C   
3650 O O   . ASP A 232 ? 0.5682 0.2784 0.5300 -0.0352 0.0359  0.0240  229 ASP A O   
3651 C CB  . ASP A 232 ? 0.5182 0.2292 0.4978 -0.0178 0.0313  -0.0080 229 ASP A CB  
3652 C CG  . ASP A 232 ? 0.6504 0.3497 0.6343 -0.0180 0.0302  -0.0250 229 ASP A CG  
3653 O OD1 . ASP A 232 ? 0.6853 0.3757 0.6686 -0.0352 0.0324  -0.0302 229 ASP A OD1 
3654 O OD2 . ASP A 232 ? 0.6597 0.3624 0.6481 -0.0015 0.0276  -0.0346 229 ASP A OD2 
3659 N N   . SER A 233 ? 0.4018 0.1794 0.3835 -0.0386 0.0407  0.0136  230 SER A N   
3660 C CA  . SER A 233 ? 0.4264 0.2149 0.4021 -0.0391 0.0425  0.0262  230 SER A CA  
3661 C C   . SER A 233 ? 0.4312 0.2446 0.4111 -0.0563 0.0487  0.0266  230 SER A C   
3662 O O   . SER A 233 ? 0.4051 0.2420 0.3854 -0.0553 0.0508  0.0314  230 SER A O   
3663 C CB  . SER A 233 ? 0.4263 0.2365 0.4069 -0.0219 0.0394  0.0256  230 SER A CB  
3664 O OG  . SER A 233 ? 0.3981 0.2287 0.3910 -0.0175 0.0386  0.0132  230 SER A OG  
3670 N N   . ARG A 234 ? 0.4396 0.2506 0.4238 -0.0719 0.0515  0.0200  231 ARG A N   
3671 C CA  . ARG A 234 ? 0.4172 0.2567 0.4083 -0.0882 0.0573  0.0184  231 ARG A CA  
3672 C C   . ARG A 234 ? 0.4287 0.2635 0.4071 -0.0984 0.0627  0.0324  231 ARG A C   
3673 O O   . ARG A 234 ? 0.4666 0.2655 0.4283 -0.1010 0.0622  0.0438  231 ARG A O   
3674 C CB  . ARG A 234 ? 0.5038 0.3413 0.5018 -0.1052 0.0591  0.0085  231 ARG A CB  
3675 C CG  . ARG A 234 ? 0.6309 0.4628 0.6354 -0.0970 0.0536  -0.0045 231 ARG A CG  
3676 C CD  . ARG A 234 ? 0.5960 0.4661 0.6142 -0.0887 0.0508  -0.0141 231 ARG A CD  
3677 N NE  . ARG A 234 ? 0.8842 0.7864 0.9142 -0.1022 0.0533  -0.0201 231 ARG A NE  
3678 C CZ  . ARG A 234 ? 0.8318 0.7696 0.8730 -0.0955 0.0508  -0.0255 231 ARG A CZ  
3679 N NH1 . ARG A 234 ? 0.5448 0.4888 0.5855 -0.0779 0.0465  -0.0242 231 ARG A NH1 
3680 N NH2 . ARG A 234 ? 0.6719 0.6396 0.7257 -0.1070 0.0523  -0.0324 231 ARG A NH2 
3694 N N   . GLY A 235 ? 0.4108 0.2827 0.3964 -0.1038 0.0675  0.0312  232 GLY A N   
3695 C CA  . GLY A 235 ? 0.4433 0.3203 0.4174 -0.1142 0.0739  0.0425  232 GLY A CA  
3696 C C   . GLY A 235 ? 0.4291 0.3095 0.3939 -0.0986 0.0716  0.0507  232 GLY A C   
3697 O O   . GLY A 235 ? 0.4312 0.3197 0.3848 -0.1060 0.0768  0.0595  232 GLY A O   
3701 N N   . SER A 236 ? 0.4106 0.2864 0.3788 -0.0785 0.0641  0.0479  233 SER A N   
3702 C CA  . SER A 236 ? 0.3845 0.2643 0.3447 -0.0646 0.0612  0.0546  233 SER A CA  
3703 C C   . SER A 236 ? 0.3705 0.2909 0.3431 -0.0596 0.0628  0.0463  233 SER A C   
3704 O O   . SER A 236 ? 0.3321 0.2749 0.3213 -0.0610 0.0633  0.0348  233 SER A O   
3705 C CB  . SER A 236 ? 0.3951 0.2545 0.3546 -0.0461 0.0529  0.0544  233 SER A CB  
3706 O OG  . SER A 236 ? 0.4039 0.2778 0.3798 -0.0387 0.0502  0.0416  233 SER A OG  
3712 N N   . PHE A 237 ? 0.3490 0.2776 0.3127 -0.0529 0.0624  0.0521  234 PHE A N   
3713 C CA  . PHE A 237 ? 0.3240 0.2878 0.2976 -0.0477 0.0636  0.0438  234 PHE A CA  
3714 C C   . PHE A 237 ? 0.2885 0.2629 0.2787 -0.0348 0.0577  0.0325  234 PHE A C   
3715 O O   . PHE A 237 ? 0.2630 0.2629 0.2668 -0.0355 0.0589  0.0225  234 PHE A O   
3716 C CB  . PHE A 237 ? 0.3321 0.2990 0.2912 -0.0418 0.0630  0.0514  234 PHE A CB  
3717 C CG  . PHE A 237 ? 0.2840 0.2798 0.2525 -0.0322 0.0617  0.0417  234 PHE A CG  
3718 C CD1 . PHE A 237 ? 0.2691 0.2953 0.2451 -0.0386 0.0679  0.0337  234 PHE A CD1 
3719 C CD2 . PHE A 237 ? 0.2815 0.2748 0.2529 -0.0172 0.0544  0.0391  234 PHE A CD2 
3720 C CE1 . PHE A 237 ? 0.2603 0.3103 0.2459 -0.0283 0.0657  0.0229  234 PHE A CE1 
3721 C CE2 . PHE A 237 ? 0.2975 0.3137 0.2772 -0.0094 0.0527  0.0294  234 PHE A CE2 
3722 C CZ  . PHE A 237 ? 0.2595 0.3023 0.2458 -0.0144 0.0580  0.0214  234 PHE A CZ  
3732 N N   . PRO A 238 ? 0.2655 0.2226 0.2555 -0.0236 0.0514  0.0331  235 PRO A N   
3733 C CA  . PRO A 238 ? 0.2709 0.2389 0.2741 -0.0143 0.0467  0.0235  235 PRO A CA  
3734 C C   . PRO A 238 ? 0.2607 0.2366 0.2754 -0.0205 0.0473  0.0153  235 PRO A C   
3735 O O   . PRO A 238 ? 0.2449 0.2371 0.2698 -0.0154 0.0442  0.0075  235 PRO A O   
3736 C CB  . PRO A 238 ? 0.3091 0.2573 0.3085 -0.0044 0.0417  0.0262  235 PRO A CB  
3737 C CG  . PRO A 238 ? 0.3491 0.2826 0.3339 -0.0033 0.0417  0.0370  235 PRO A CG  
3738 C CD  . PRO A 238 ? 0.3315 0.2615 0.3091 -0.0176 0.0477  0.0423  235 PRO A CD  
3746 N N   . GLN A 239 ? 0.2782 0.2421 0.2911 -0.0315 0.0503  0.0166  236 GLN A N   
3747 C CA  . GLN A 239 ? 0.2569 0.2323 0.2814 -0.0381 0.0503  0.0076  236 GLN A CA  
3748 C C   . GLN A 239 ? 0.2546 0.2615 0.2892 -0.0428 0.0532  0.0018  236 GLN A C   
3749 O O   . GLN A 239 ? 0.2634 0.2884 0.3104 -0.0398 0.0495  -0.0074 236 GLN A O   
3750 C CB  . GLN A 239 ? 0.2728 0.2284 0.2937 -0.0505 0.0528  0.0087  236 GLN A CB  
3751 C CG  . GLN A 239 ? 0.3159 0.2416 0.3291 -0.0429 0.0490  0.0112  236 GLN A CG  
3752 C CD  . GLN A 239 ? 0.2978 0.2092 0.3131 -0.0502 0.0484  0.0049  236 GLN A CD  
3753 O OE1 . GLN A 239 ? 0.3391 0.2601 0.3605 -0.0636 0.0510  -0.0002 236 GLN A OE1 
3754 N NE2 . GLN A 239 ? 0.3286 0.2192 0.3400 -0.0412 0.0448  0.0034  236 GLN A NE2 
3763 N N   . ASP A 240 ? 0.2598 0.2752 0.2889 -0.0493 0.0593  0.0065  237 ASP A N   
3764 C CA  . ASP A 240 ? 0.2335 0.2834 0.2732 -0.0526 0.0630  -0.0009 237 ASP A CA  
3765 C C   . ASP A 240 ? 0.2333 0.2987 0.2805 -0.0363 0.0572  -0.0077 237 ASP A C   
3766 O O   . ASP A 240 ? 0.2206 0.3130 0.2821 -0.0338 0.0561  -0.0180 237 ASP A O   
3767 C CB  . ASP A 240 ? 0.2803 0.3361 0.3092 -0.0637 0.0718  0.0060  237 ASP A CB  
3768 C CG  . ASP A 240 ? 0.3539 0.3985 0.3771 -0.0837 0.0784  0.0114  237 ASP A CG  
3769 O OD1 . ASP A 240 ? 0.3829 0.4284 0.4167 -0.0901 0.0771  0.0049  237 ASP A OD1 
3770 O OD2 . ASP A 240 ? 0.4429 0.4772 0.4497 -0.0939 0.0845  0.0222  237 ASP A OD2 
3775 N N   . VAL A 241 ? 0.2198 0.2686 0.2583 -0.0253 0.0530  -0.0026 238 VAL A N   
3776 C CA  . VAL A 241 ? 0.1758 0.2334 0.2205 -0.0115 0.0467  -0.0089 238 VAL A CA  
3777 C C   . VAL A 241 ? 0.2020 0.2601 0.2567 -0.0070 0.0401  -0.0152 238 VAL A C   
3778 O O   . VAL A 241 ? 0.2118 0.2870 0.2769 -0.0003 0.0358  -0.0235 238 VAL A O   
3779 C CB  . VAL A 241 ? 0.1921 0.2322 0.2260 -0.0032 0.0437  -0.0026 238 VAL A CB  
3780 C CG1 . VAL A 241 ? 0.2085 0.2536 0.2481 0.0085  0.0370  -0.0090 238 VAL A CG1 
3781 C CG2 . VAL A 241 ? 0.2425 0.2835 0.2646 -0.0068 0.0488  0.0039  238 VAL A CG2 
3791 N N   . ASN A 242 ? 0.2054 0.2448 0.2563 -0.0100 0.0384  -0.0117 239 ASN A N   
3792 C CA  . ASN A 242 ? 0.2072 0.2480 0.2645 -0.0068 0.0320  -0.0172 239 ASN A CA  
3793 C C   . ASN A 242 ? 0.1879 0.2525 0.2582 -0.0120 0.0318  -0.0256 239 ASN A C   
3794 O O   . ASN A 242 ? 0.2019 0.2779 0.2799 -0.0046 0.0245  -0.0319 239 ASN A O   
3795 C CB  . ASN A 242 ? 0.1955 0.2150 0.2458 -0.0102 0.0315  -0.0139 239 ASN A CB  
3796 C CG  . ASN A 242 ? 0.2324 0.2367 0.2751 -0.0017 0.0285  -0.0099 239 ASN A CG  
3797 O OD1 . ASN A 242 ? 0.2223 0.2309 0.2654 0.0059  0.0251  -0.0101 239 ASN A OD1 
3798 N ND2 . ASN A 242 ? 0.2419 0.2294 0.2787 -0.0031 0.0295  -0.0077 239 ASN A ND2 
3805 N N   . PHE A 243 ? 0.1858 0.2591 0.2586 -0.0248 0.0391  -0.0259 240 PHE A N   
3806 C CA  . PHE A 243 ? 0.1951 0.2974 0.2831 -0.0309 0.0394  -0.0356 240 PHE A CA  
3807 C C   . PHE A 243 ? 0.1787 0.3088 0.2781 -0.0207 0.0372  -0.0435 240 PHE A C   
3808 O O   . PHE A 243 ? 0.2026 0.3554 0.3164 -0.0159 0.0314  -0.0533 240 PHE A O   
3809 C CB  . PHE A 243 ? 0.2330 0.3399 0.3207 -0.0494 0.0492  -0.0340 240 PHE A CB  
3810 C CG  . PHE A 243 ? 0.2518 0.3326 0.3315 -0.0597 0.0500  -0.0298 240 PHE A CG  
3811 C CD1 . PHE A 243 ? 0.3542 0.4303 0.4372 -0.0564 0.0427  -0.0350 240 PHE A CD1 
3812 C CD2 . PHE A 243 ? 0.3373 0.3977 0.4053 -0.0722 0.0573  -0.0212 240 PHE A CD2 
3813 C CE1 . PHE A 243 ? 0.4746 0.5271 0.5505 -0.0650 0.0433  -0.0337 240 PHE A CE1 
3814 C CE2 . PHE A 243 ? 0.4529 0.4857 0.5138 -0.0801 0.0571  -0.0189 240 PHE A CE2 
3815 C CZ  . PHE A 243 ? 0.3660 0.3962 0.4318 -0.0762 0.0504  -0.0262 240 PHE A CZ  
3825 N N   . TYR A 244 ? 0.1823 0.3113 0.2757 -0.0161 0.0408  -0.0403 241 TYR A N   
3826 C CA  . TYR A 244 ? 0.1788 0.3326 0.2829 -0.0051 0.0385  -0.0499 241 TYR A CA  
3827 C C   . TYR A 244 ? 0.1824 0.3266 0.2888 0.0116  0.0262  -0.0529 241 TYR A C   
3828 O O   . TYR A 244 ? 0.1860 0.3507 0.3063 0.0211  0.0198  -0.0633 241 TYR A O   
3829 C CB  . TYR A 244 ? 0.1718 0.3266 0.2670 -0.0048 0.0452  -0.0469 241 TYR A CB  
3830 C CG  . TYR A 244 ? 0.1798 0.3635 0.2871 0.0057  0.0442  -0.0597 241 TYR A CG  
3831 C CD1 . TYR A 244 ? 0.1763 0.3974 0.2990 0.0006  0.0495  -0.0706 241 TYR A CD1 
3832 C CD2 . TYR A 244 ? 0.1688 0.3430 0.2735 0.0207  0.0375  -0.0624 241 TYR A CD2 
3833 C CE1 . TYR A 244 ? 0.1878 0.4376 0.3238 0.0123  0.0481  -0.0849 241 TYR A CE1 
3834 C CE2 . TYR A 244 ? 0.1762 0.3742 0.2925 0.0319  0.0356  -0.0761 241 TYR A CE2 
3835 C CZ  . TYR A 244 ? 0.1841 0.4201 0.3161 0.0289  0.0408  -0.0876 241 TYR A CZ  
3836 O OH  . TYR A 244 ? 0.2253 0.4892 0.3713 0.0415  0.0391  -0.1039 241 TYR A OH  
3846 N N   . ILE A 245 ? 0.1750 0.2889 0.2680 0.0151  0.0225  -0.0441 242 ILE A N   
3847 C CA  . ILE A 245 ? 0.1791 0.2809 0.2711 0.0275  0.0114  -0.0450 242 ILE A CA  
3848 C C   . ILE A 245 ? 0.1630 0.2744 0.2633 0.0285  0.0042  -0.0498 242 ILE A C   
3849 O O   . ILE A 245 ? 0.2029 0.3211 0.3100 0.0402  -0.0055 -0.0556 242 ILE A O   
3850 C CB  . ILE A 245 ? 0.1706 0.2423 0.2473 0.0272  0.0103  -0.0350 242 ILE A CB  
3851 C CG1 . ILE A 245 ? 0.2014 0.2661 0.2708 0.0278  0.0153  -0.0313 242 ILE A CG1 
3852 C CG2 . ILE A 245 ? 0.2035 0.2619 0.2769 0.0363  -0.0005 -0.0346 242 ILE A CG2 
3853 C CD1 . ILE A 245 ? 0.2058 0.2469 0.2628 0.0257  0.0158  -0.0225 242 ILE A CD1 
3865 N N   . ASN A 246 ? 0.1719 0.2812 0.2704 0.0168  0.0076  -0.0472 243 ASN A N   
3866 C CA  . ASN A 246 ? 0.2013 0.3222 0.3070 0.0167  0.0004  -0.0527 243 ASN A CA  
3867 C C   . ASN A 246 ? 0.1825 0.3389 0.3079 0.0209  -0.0022 -0.0647 243 ASN A C   
3868 O O   . ASN A 246 ? 0.1920 0.3587 0.3246 0.0315  -0.0136 -0.0705 243 ASN A O   
3869 C CB  . ASN A 246 ? 0.1835 0.2981 0.2851 0.0016  0.0060  -0.0504 243 ASN A CB  
3870 C CG  . ASN A 246 ? 0.2118 0.3441 0.3226 -0.0014 -0.0001 -0.0581 243 ASN A CG  
3871 O OD1 . ASN A 246 ? 0.2452 0.4027 0.3697 -0.0101 0.0036  -0.0657 243 ASN A OD1 
3872 N ND2 . ASN A 246 ? 0.2432 0.3638 0.3457 0.0046  -0.0097 -0.0564 243 ASN A ND2 
3879 N N   . LYS A 247 ? 0.1681 0.3450 0.3019 0.0131  0.0080  -0.0689 244 LYS A N   
3880 C CA  . LYS A 247 ? 0.1604 0.3775 0.3152 0.0157  0.0074  -0.0823 244 LYS A CA  
3881 C C   . LYS A 247 ? 0.1673 0.3914 0.3296 0.0369  -0.0032 -0.0894 244 LYS A C   
3882 O O   . LYS A 247 ? 0.1834 0.4324 0.3618 0.0463  -0.0120 -0.1002 244 LYS A O   
3883 C CB  . LYS A 247 ? 0.1942 0.4316 0.3535 0.0024  0.0220  -0.0845 244 LYS A CB  
3884 C CG  . LYS A 247 ? 0.1814 0.4670 0.3641 0.0037  0.0239  -0.1002 244 LYS A CG  
3885 C CD  . LYS A 247 ? 0.1663 0.4719 0.3496 -0.0101 0.0394  -0.1014 244 LYS A CD  
3886 C CE  . LYS A 247 ? 0.2624 0.6122 0.4642 -0.0107 0.0412  -0.1165 244 LYS A CE  
3887 N NZ  . LYS A 247 ? 0.3878 0.7504 0.5835 -0.0317 0.0563  -0.1141 244 LYS A NZ  
3901 N N   . GLU A 248 ? 0.1768 0.3787 0.3279 0.0449  -0.0033 -0.0843 245 GLU A N   
3902 C CA  . GLU A 248 ? 0.1781 0.3839 0.3359 0.0640  -0.0121 -0.0923 245 GLU A CA  
3903 C C   . GLU A 248 ? 0.2149 0.3907 0.3628 0.0770  -0.0270 -0.0867 245 GLU A C   
3904 O O   . GLU A 248 ? 0.2857 0.4624 0.4400 0.0944  -0.0376 -0.0939 245 GLU A O   
3905 C CB  . GLU A 248 ? 0.1903 0.3893 0.3411 0.0648  -0.0042 -0.0915 245 GLU A CB  
3906 C CG  . GLU A 248 ? 0.1760 0.4049 0.3333 0.0536  0.0103  -0.0970 245 GLU A CG  
3907 C CD  . GLU A 248 ? 0.1904 0.4645 0.3707 0.0559  0.0113  -0.1128 245 GLU A CD  
3908 O OE1 . GLU A 248 ? 0.1917 0.4671 0.3784 0.0700  -0.0014 -0.1198 245 GLU A OE1 
3909 O OE2 . GLU A 248 ? 0.2249 0.5212 0.4066 0.0409  0.0241  -0.1145 245 GLU A OE2 
3916 N N   . THR A 249 ? 0.2229 0.3724 0.3549 0.0691  -0.0283 -0.0747 246 THR A N   
3917 C CA  . THR A 249 ? 0.2352 0.3554 0.3539 0.0779  -0.0407 -0.0674 246 THR A CA  
3918 C C   . THR A 249 ? 0.2689 0.3877 0.3832 0.0749  -0.0481 -0.0641 246 THR A C   
3919 O O   . THR A 249 ? 0.2972 0.3976 0.4015 0.0841  -0.0608 -0.0595 246 THR A O   
3920 C CB  . THR A 249 ? 0.2502 0.3368 0.3495 0.0720  -0.0361 -0.0555 246 THR A CB  
3921 O OG1 . THR A 249 ? 0.2422 0.3235 0.3334 0.0569  -0.0275 -0.0485 246 THR A OG1 
3922 C CG2 . THR A 249 ? 0.2955 0.3823 0.3965 0.0739  -0.0291 -0.0584 246 THR A CG2 
3930 N N   . GLY A 250 ? 0.2201 0.3557 0.3394 0.0615  -0.0410 -0.0659 247 GLY A N   
3931 C CA  . GLY A 250 ? 0.2354 0.3688 0.3484 0.0567  -0.0471 -0.0634 247 GLY A CA  
3932 C C   . GLY A 250 ? 0.2636 0.3656 0.3546 0.0489  -0.0445 -0.0517 247 GLY A C   
3933 O O   . GLY A 250 ? 0.3011 0.4002 0.3840 0.0453  -0.0499 -0.0499 247 GLY A O   
3937 N N   . ILE A 251 ? 0.2601 0.3413 0.3416 0.0464  -0.0370 -0.0447 248 ILE A N   
3938 C CA  . ILE A 251 ? 0.2548 0.3107 0.3178 0.0393  -0.0338 -0.0352 248 ILE A CA  
3939 C C   . ILE A 251 ? 0.2654 0.3265 0.3290 0.0259  -0.0251 -0.0368 248 ILE A C   
3940 O O   . ILE A 251 ? 0.2421 0.3125 0.3147 0.0193  -0.0159 -0.0397 248 ILE A O   
3941 C CB  . ILE A 251 ? 0.2471 0.2852 0.3035 0.0399  -0.0280 -0.0294 248 ILE A CB  
3942 C CG1 . ILE A 251 ? 0.2763 0.3024 0.3289 0.0519  -0.0378 -0.0277 248 ILE A CG1 
3943 C CG2 . ILE A 251 ? 0.2726 0.2922 0.3145 0.0312  -0.0218 -0.0221 248 ILE A CG2 
3944 C CD1 . ILE A 251 ? 0.3200 0.3338 0.3700 0.0529  -0.0328 -0.0254 248 ILE A CD1 
3956 N N   . PRO A 252 ? 0.2888 0.3418 0.3411 0.0209  -0.0274 -0.0348 249 PRO A N   
3957 C CA  . PRO A 252 ? 0.3336 0.3903 0.3872 0.0089  -0.0205 -0.0388 249 PRO A CA  
3958 C C   . PRO A 252 ? 0.2317 0.2734 0.2816 0.0025  -0.0088 -0.0349 249 PRO A C   
3959 O O   . PRO A 252 ? 0.2492 0.2756 0.2906 0.0061  -0.0067 -0.0285 249 PRO A O   
3960 C CB  . PRO A 252 ? 0.3867 0.4367 0.4259 0.0074  -0.0266 -0.0379 249 PRO A CB  
3961 C CG  . PRO A 252 ? 0.5476 0.5803 0.5726 0.0149  -0.0312 -0.0288 249 PRO A CG  
3962 C CD  . PRO A 252 ? 0.4029 0.4398 0.4380 0.0250  -0.0355 -0.0283 249 PRO A CD  
3970 N N   . ILE A 253 ? 0.2532 0.2991 0.3094 -0.0075 -0.0021 -0.0392 250 ILE A N   
3971 C CA  . ILE A 253 ? 0.2453 0.2739 0.2966 -0.0136 0.0071  -0.0361 250 ILE A CA  
3972 C C   . ILE A 253 ? 0.2630 0.2823 0.3067 -0.0194 0.0072  -0.0401 250 ILE A C   
3973 O O   . ILE A 253 ? 0.2556 0.2857 0.3035 -0.0255 0.0042  -0.0475 250 ILE A O   
3974 C CB  . ILE A 253 ? 0.2336 0.2681 0.2940 -0.0219 0.0143  -0.0371 250 ILE A CB  
3975 C CG1 . ILE A 253 ? 0.2192 0.2646 0.2855 -0.0161 0.0154  -0.0344 250 ILE A CG1 
3976 C CG2 . ILE A 253 ? 0.2957 0.3073 0.3486 -0.0276 0.0218  -0.0330 250 ILE A CG2 
3977 C CD1 . ILE A 253 ? 0.2879 0.3479 0.3635 -0.0253 0.0221  -0.0366 250 ILE A CD1 
3989 N N   . VAL A 254 ? 0.2325 0.2345 0.2664 -0.0173 0.0105  -0.0370 251 VAL A N   
3990 C CA  . VAL A 254 ? 0.2313 0.2231 0.2583 -0.0216 0.0124  -0.0424 251 VAL A CA  
3991 C C   . VAL A 254 ? 0.2397 0.2139 0.2677 -0.0244 0.0198  -0.0414 251 VAL A C   
3992 O O   . VAL A 254 ? 0.2491 0.2157 0.2766 -0.0192 0.0228  -0.0345 251 VAL A O   
3993 C CB  . VAL A 254 ? 0.2514 0.2398 0.2665 -0.0163 0.0106  -0.0409 251 VAL A CB  
3994 C CG1 . VAL A 254 ? 0.2526 0.2323 0.2609 -0.0191 0.0141  -0.0480 251 VAL A CG1 
3995 C CG2 . VAL A 254 ? 0.3126 0.3139 0.3232 -0.0145 0.0019  -0.0404 251 VAL A CG2 
4005 N N   . ASP A 255 ? 0.2701 0.2365 0.2989 -0.0326 0.0216  -0.0484 252 ASP A N   
4006 C CA  . ASP A 255 ? 0.2965 0.2402 0.3239 -0.0350 0.0269  -0.0475 252 ASP A CA  
4007 C C   . ASP A 255 ? 0.3310 0.2615 0.3512 -0.0281 0.0279  -0.0517 252 ASP A C   
4008 O O   . ASP A 255 ? 0.3231 0.2609 0.3389 -0.0278 0.0257  -0.0594 252 ASP A O   
4009 C CB  . ASP A 255 ? 0.3384 0.2763 0.3696 -0.0484 0.0283  -0.0536 252 ASP A CB  
4010 C CG  . ASP A 255 ? 0.4494 0.4041 0.4896 -0.0564 0.0291  -0.0502 252 ASP A CG  
4011 O OD1 . ASP A 255 ? 0.3982 0.3567 0.4397 -0.0521 0.0313  -0.0413 252 ASP A OD1 
4012 O OD2 . ASP A 255 ? 0.4961 0.4625 0.5427 -0.0675 0.0279  -0.0578 252 ASP A OD2 
4017 N N   . ILE A 256 ? 0.3049 0.2182 0.3234 -0.0218 0.0309  -0.0472 253 ILE A N   
4018 C CA  . ILE A 256 ? 0.2954 0.2021 0.3100 -0.0125 0.0319  -0.0518 253 ILE A CA  
4019 C C   . ILE A 256 ? 0.3201 0.1996 0.3342 -0.0092 0.0336  -0.0522 253 ILE A C   
4020 O O   . ILE A 256 ? 0.3190 0.1863 0.3332 -0.0114 0.0342  -0.0430 253 ILE A O   
4021 C CB  . ILE A 256 ? 0.2518 0.1728 0.2660 -0.0041 0.0317  -0.0454 253 ILE A CB  
4022 C CG1 . ILE A 256 ? 0.2621 0.1867 0.2734 0.0027  0.0334  -0.0528 253 ILE A CG1 
4023 C CG2 . ILE A 256 ? 0.2776 0.1931 0.2945 0.0008  0.0325  -0.0347 253 ILE A CG2 
4024 C CD1 . ILE A 256 ? 0.2598 0.2021 0.2694 0.0059  0.0334  -0.0483 253 ILE A CD1 
4036 N N   . PRO A 257 ? 0.3323 0.2005 0.3446 -0.0040 0.0341  -0.0627 254 PRO A N   
4037 C CA  . PRO A 257 ? 0.3476 0.1847 0.3587 0.0000  0.0339  -0.0637 254 PRO A CA  
4038 C C   . PRO A 257 ? 0.3268 0.1549 0.3380 0.0104  0.0330  -0.0521 254 PRO A C   
4039 O O   . PRO A 257 ? 0.3624 0.2100 0.3762 0.0176  0.0332  -0.0475 254 PRO A O   
4040 C CB  . PRO A 257 ? 0.3444 0.1787 0.3554 0.0075  0.0342  -0.0795 254 PRO A CB  
4041 C CG  . PRO A 257 ? 0.3732 0.2316 0.3823 -0.0008 0.0348  -0.0876 254 PRO A CG  
4042 C CD  . PRO A 257 ? 0.3213 0.2030 0.3312 -0.0037 0.0343  -0.0756 254 PRO A CD  
4050 N N   . GLY A 258 ? 0.3725 0.1691 0.3796 0.0103  0.0316  -0.0473 255 GLY A N   
4051 C CA  . GLY A 258 ? 0.4280 0.2127 0.4324 0.0202  0.0293  -0.0356 255 GLY A CA  
4052 C C   . GLY A 258 ? 0.4184 0.2092 0.4191 0.0117  0.0305  -0.0206 255 GLY A C   
4053 O O   . GLY A 258 ? 0.3872 0.1917 0.3892 -0.0019 0.0332  -0.0194 255 GLY A O   
4057 N N   . GLY A 259 ? 0.3855 0.1672 0.3817 0.0206  0.0279  -0.0099 256 GLY A N   
4058 C CA  . GLY A 259 ? 0.4271 0.2148 0.4179 0.0137  0.0292  0.0040  256 GLY A CA  
4059 C C   . GLY A 259 ? 0.4147 0.2329 0.4106 0.0212  0.0289  0.0063  256 GLY A C   
4060 O O   . GLY A 259 ? 0.3458 0.1871 0.3500 0.0236  0.0298  -0.0021 256 GLY A O   
4064 N N   . HIS A 260 ? 0.3950 0.2125 0.3843 0.0239  0.0274  0.0180  257 HIS A N   
4065 C CA  . HIS A 260 ? 0.3795 0.2238 0.3732 0.0309  0.0264  0.0193  257 HIS A CA  
4066 C C   . HIS A 260 ? 0.3784 0.2319 0.3803 0.0451  0.0234  0.0112  257 HIS A C   
4067 O O   . HIS A 260 ? 0.3592 0.2379 0.3681 0.0469  0.0241  0.0072  257 HIS A O   
4068 C CB  . HIS A 260 ? 0.4116 0.2511 0.3948 0.0330  0.0243  0.0322  257 HIS A CB  
4069 C CG  . HIS A 260 ? 0.4150 0.2826 0.4012 0.0339  0.0248  0.0333  257 HIS A CG  
4070 N ND1 . HIS A 260 ? 0.4086 0.2973 0.4014 0.0256  0.0287  0.0286  257 HIS A ND1 
4071 C CD2 . HIS A 260 ? 0.5095 0.3873 0.4935 0.0428  0.0210  0.0374  257 HIS A CD2 
4072 C CE1 . HIS A 260 ? 0.4650 0.3728 0.4591 0.0292  0.0276  0.0295  257 HIS A CE1 
4073 N NE2 . HIS A 260 ? 0.5451 0.4479 0.5340 0.0387  0.0233  0.0346  257 HIS A NE2 
4081 N N   . LEU A 261 ? 0.3764 0.2098 0.3776 0.0551  0.0199  0.0081  258 LEU A N   
4082 C CA  . LEU A 261 ? 0.3790 0.2241 0.3900 0.0691  0.0176  -0.0019 258 LEU A CA  
4083 C C   . LEU A 261 ? 0.3357 0.1790 0.3523 0.0679  0.0206  -0.0159 258 LEU A C   
4084 O O   . LEU A 261 ? 0.3618 0.2025 0.3841 0.0803  0.0185  -0.0254 258 LEU A O   
4085 C CB  . LEU A 261 ? 0.4014 0.2292 0.4095 0.0850  0.0104  0.0023  258 LEU A CB  
4086 C CG  . LEU A 261 ? 0.5318 0.3757 0.5396 0.0932  0.0058  0.0099  258 LEU A CG  
4087 C CD1 . LEU A 261 ? 0.5708 0.4244 0.5713 0.0808  0.0087  0.0199  258 LEU A CD1 
4088 C CD2 . LEU A 261 ? 0.5964 0.4149 0.5965 0.1077  -0.0030 0.0170  258 LEU A CD2 
4100 N N   . GLY A 262 ? 0.3325 0.1802 0.3479 0.0537  0.0250  -0.0184 259 GLY A N   
4101 C CA  . GLY A 262 ? 0.3715 0.2147 0.3889 0.0508  0.0272  -0.0312 259 GLY A CA  
4102 C C   . GLY A 262 ? 0.3043 0.1707 0.3296 0.0583  0.0290  -0.0436 259 GLY A C   
4103 O O   . GLY A 262 ? 0.3218 0.1823 0.3489 0.0618  0.0298  -0.0562 259 GLY A O   
4107 N N   . TYR A 263 ? 0.3295 0.2224 0.3591 0.0599  0.0299  -0.0410 260 TYR A N   
4108 C CA  . TYR A 263 ? 0.3230 0.2405 0.3592 0.0644  0.0327  -0.0519 260 TYR A CA  
4109 C C   . TYR A 263 ? 0.3250 0.2414 0.3692 0.0808  0.0307  -0.0610 260 TYR A C   
4110 O O   . TYR A 263 ? 0.3030 0.2386 0.3533 0.0845  0.0343  -0.0742 260 TYR A O   
4111 C CB  . TYR A 263 ? 0.3034 0.2465 0.3419 0.0605  0.0338  -0.0461 260 TYR A CB  
4112 C CG  . TYR A 263 ? 0.2612 0.2011 0.3000 0.0645  0.0297  -0.0346 260 TYR A CG  
4113 C CD1 . TYR A 263 ? 0.2661 0.2132 0.3119 0.0772  0.0265  -0.0357 260 TYR A CD1 
4114 C CD2 . TYR A 263 ? 0.3035 0.2357 0.3358 0.0562  0.0288  -0.0241 260 TYR A CD2 
4115 C CE1 . TYR A 263 ? 0.3153 0.2603 0.3592 0.0808  0.0219  -0.0253 260 TYR A CE1 
4116 C CE2 . TYR A 263 ? 0.2793 0.2100 0.3100 0.0596  0.0255  -0.0146 260 TYR A CE2 
4117 C CZ  . TYR A 263 ? 0.3320 0.2684 0.3674 0.0715  0.0218  -0.0148 260 TYR A CZ  
4118 O OH  . TYR A 263 ? 0.3638 0.3002 0.3956 0.0743  0.0179  -0.0055 260 TYR A OH  
4128 N N   . ILE A 264 ? 0.3044 0.1998 0.3483 0.0914  0.0249  -0.0550 261 ILE A N   
4129 C CA  . ILE A 264 ? 0.3177 0.2081 0.3694 0.1097  0.0211  -0.0647 261 ILE A CA  
4130 C C   . ILE A 264 ? 0.3794 0.2299 0.4251 0.1143  0.0175  -0.0677 261 ILE A C   
4131 O O   . ILE A 264 ? 0.4229 0.2718 0.4734 0.1244  0.0172  -0.0784 261 ILE A O   
4132 C CB  . ILE A 264 ? 0.3986 0.2969 0.4552 0.1225  0.0148  -0.0573 261 ILE A CB  
4133 C CG1 . ILE A 264 ? 0.4320 0.3381 0.4994 0.1387  0.0119  -0.0673 261 ILE A CG1 
4134 C CG2 . ILE A 264 ? 0.4305 0.3000 0.4745 0.1202  0.0093  -0.0395 261 ILE A CG2 
4135 C CD1 . ILE A 264 ? 0.5029 0.4362 0.5800 0.1473  0.0079  -0.0646 261 ILE A CD1 
4147 N N   . GLN A 265 ? 0.3995 0.2228 0.4333 0.1018  0.0171  -0.0567 262 GLN A N   
4148 C CA  . GLN A 265 ? 0.4300 0.2133 0.4567 0.1016  0.0144  -0.0592 262 GLN A CA  
4149 C C   . GLN A 265 ? 0.3807 0.1670 0.4100 0.0960  0.0192  -0.0768 262 GLN A C   
4150 O O   . GLN A 265 ? 0.4472 0.2140 0.4731 0.1008  0.0184  -0.0845 262 GLN A O   
4151 C CB  . GLN A 265 ? 0.4224 0.1836 0.4364 0.0854  0.0145  -0.0429 262 GLN A CB  
4152 C CG  . GLN A 265 ? 0.4619 0.2108 0.4686 0.0905  0.0091  -0.0255 262 GLN A CG  
4153 C CD  . GLN A 265 ? 0.5344 0.2823 0.5312 0.0726  0.0122  -0.0101 262 GLN A CD  
4154 O OE1 . GLN A 265 ? 0.5333 0.2951 0.5314 0.0571  0.0180  -0.0124 262 GLN A OE1 
4155 N NE2 . GLN A 265 ? 0.5904 0.3236 0.5769 0.0755  0.0078  0.0052  262 GLN A NE2 
4164 N N   . LYS A 266 ? 0.3672 0.1813 0.3967 0.0822  0.0253  -0.0788 263 LYS A N   
4165 C CA  . LYS A 266 ? 0.4457 0.2643 0.4740 0.0738  0.0294  -0.0934 263 LYS A CA  
4166 C C   . LYS A 266 ? 0.3391 0.1990 0.3708 0.0701  0.0348  -0.0990 263 LYS A C   
4167 O O   . LYS A 266 ? 0.3297 0.2024 0.3562 0.0558  0.0373  -0.0960 263 LYS A O   
4168 C CB  . LYS A 266 ? 0.4040 0.2049 0.4239 0.0556  0.0297  -0.0874 263 LYS A CB  
4169 C CG  . LYS A 266 ? 0.5174 0.2750 0.5313 0.0553  0.0252  -0.0800 263 LYS A CG  
4170 C CD  . LYS A 266 ? 0.5525 0.2958 0.5600 0.0353  0.0266  -0.0774 263 LYS A CD  
4171 C CE  . LYS A 266 ? 0.6976 0.3944 0.6970 0.0328  0.0228  -0.0697 263 LYS A CE  
4172 N NZ  . LYS A 266 ? 0.6565 0.3401 0.6507 0.0105  0.0249  -0.0677 263 LYS A NZ  
4186 N N   . PRO A 267 ? 0.3435 0.2258 0.3838 0.0826  0.0363  -0.1068 264 PRO A N   
4187 C CA  . PRO A 267 ? 0.3334 0.2542 0.3749 0.0762  0.0419  -0.1087 264 PRO A CA  
4188 C C   . PRO A 267 ? 0.2989 0.2318 0.3335 0.0659  0.0467  -0.1204 264 PRO A C   
4189 O O   . PRO A 267 ? 0.3142 0.2673 0.3427 0.0542  0.0495  -0.1149 264 PRO A O   
4190 C CB  . PRO A 267 ? 0.3710 0.3128 0.4250 0.0919  0.0426  -0.1171 264 PRO A CB  
4191 C CG  . PRO A 267 ? 0.4447 0.3605 0.5006 0.1057  0.0376  -0.1222 264 PRO A CG  
4192 C CD  . PRO A 267 ? 0.3627 0.2382 0.4110 0.1017  0.0324  -0.1115 264 PRO A CD  
4200 N N   . GLU A 268 ? 0.3485 0.2679 0.3826 0.0700  0.0469  -0.1361 265 GLU A N   
4201 C CA  . GLU A 268 ? 0.3685 0.3001 0.3941 0.0598  0.0509  -0.1481 265 GLU A CA  
4202 C C   . GLU A 268 ? 0.3587 0.2827 0.3742 0.0432  0.0486  -0.1369 265 GLU A C   
4203 O O   . GLU A 268 ? 0.3404 0.2857 0.3476 0.0327  0.0507  -0.1347 265 GLU A O   
4204 C CB  . GLU A 268 ? 0.4009 0.3162 0.4258 0.0667  0.0497  -0.1640 265 GLU A CB  
4205 C CG  . GLU A 268 ? 0.5843 0.5135 0.6162 0.0814  0.0509  -0.1720 265 GLU A CG  
4206 C CD  . GLU A 268 ? 0.7774 0.6775 0.8154 0.0963  0.0447  -0.1667 265 GLU A CD  
4207 O OE1 . GLU A 268 ? 0.6467 0.5498 0.6902 0.1088  0.0445  -0.1757 265 GLU A OE1 
4208 O OE2 . GLU A 268 ? 0.5670 0.4422 0.6038 0.0950  0.0401  -0.1529 265 GLU A OE2 
4215 N N   . GLY A 269 ? 0.3468 0.2410 0.3625 0.0407  0.0439  -0.1293 266 GLY A N   
4216 C CA  . GLY A 269 ? 0.3562 0.2473 0.3654 0.0254  0.0418  -0.1205 266 GLY A CA  
4217 C C   . GLY A 269 ? 0.3157 0.2241 0.3242 0.0205  0.0413  -0.1037 266 GLY A C   
4218 O O   . GLY A 269 ? 0.3101 0.2298 0.3130 0.0099  0.0400  -0.0997 266 GLY A O   
4222 N N   . PHE A 270 ? 0.2953 0.2049 0.3096 0.0288  0.0413  -0.0943 267 PHE A N   
4223 C CA  . PHE A 270 ? 0.2951 0.2205 0.3090 0.0253  0.0408  -0.0807 267 PHE A CA  
4224 C C   . PHE A 270 ? 0.2496 0.2013 0.2580 0.0208  0.0436  -0.0836 267 PHE A C   
4225 O O   . PHE A 270 ? 0.2524 0.2125 0.2549 0.0125  0.0417  -0.0756 267 PHE A O   
4226 C CB  . PHE A 270 ? 0.2796 0.2022 0.3006 0.0357  0.0400  -0.0729 267 PHE A CB  
4227 C CG  . PHE A 270 ? 0.2392 0.1681 0.2601 0.0319  0.0383  -0.0583 267 PHE A CG  
4228 C CD1 . PHE A 270 ? 0.2426 0.1933 0.2629 0.0296  0.0395  -0.0547 267 PHE A CD1 
4229 C CD2 . PHE A 270 ? 0.2629 0.1753 0.2837 0.0304  0.0356  -0.0483 267 PHE A CD2 
4230 C CE1 . PHE A 270 ? 0.2408 0.1953 0.2616 0.0275  0.0375  -0.0433 267 PHE A CE1 
4231 C CE2 . PHE A 270 ? 0.2512 0.1714 0.2722 0.0283  0.0344  -0.0371 267 PHE A CE2 
4232 C CZ  . PHE A 270 ? 0.2693 0.2098 0.2908 0.0273  0.0349  -0.0351 267 PHE A CZ  
4242 N N   . ALA A 271 ? 0.2669 0.2316 0.2765 0.0264  0.0479  -0.0952 268 ALA A N   
4243 C CA  . ALA A 271 ? 0.2854 0.2753 0.2868 0.0199  0.0518  -0.0981 268 ALA A CA  
4244 C C   . ALA A 271 ? 0.2855 0.2761 0.2740 0.0093  0.0500  -0.1007 268 ALA A C   
4245 O O   . ALA A 271 ? 0.2915 0.2944 0.2694 0.0009  0.0492  -0.0934 268 ALA A O   
4246 C CB  . ALA A 271 ? 0.2933 0.2997 0.2990 0.0270  0.0579  -0.1130 268 ALA A CB  
4252 N N   . ASP A 272 ? 0.3000 0.2769 0.2886 0.0094  0.0486  -0.1112 269 ASP A N   
4253 C CA  . ASP A 272 ? 0.3224 0.3032 0.2993 -0.0004 0.0462  -0.1162 269 ASP A CA  
4254 C C   . ASP A 272 ? 0.2988 0.2801 0.2716 -0.0080 0.0402  -0.1015 269 ASP A C   
4255 O O   . ASP A 272 ? 0.3019 0.2960 0.2621 -0.0150 0.0377  -0.0995 269 ASP A O   
4256 C CB  . ASP A 272 ? 0.3493 0.3118 0.3291 0.0000  0.0448  -0.1297 269 ASP A CB  
4257 C CG  . ASP A 272 ? 0.4831 0.4487 0.4636 0.0073  0.0500  -0.1489 269 ASP A CG  
4258 O OD1 . ASP A 272 ? 0.4945 0.4838 0.4701 0.0087  0.0552  -0.1533 269 ASP A OD1 
4259 O OD2 . ASP A 272 ? 0.5555 0.5002 0.5407 0.0109  0.0489  -0.1606 269 ASP A OD2 
4264 N N   . VAL A 273 ? 0.2705 0.2385 0.2530 -0.0061 0.0375  -0.0913 270 VAL A N   
4265 C CA  . VAL A 273 ? 0.2508 0.2214 0.2323 -0.0112 0.0320  -0.0792 270 VAL A CA  
4266 C C   . VAL A 273 ? 0.2611 0.2438 0.2367 -0.0109 0.0315  -0.0686 270 VAL A C   
4267 O O   . VAL A 273 ? 0.2593 0.2488 0.2266 -0.0154 0.0263  -0.0628 270 VAL A O   
4268 C CB  . VAL A 273 ? 0.2724 0.2281 0.2653 -0.0100 0.0306  -0.0727 270 VAL A CB  
4269 C CG1 . VAL A 273 ? 0.2765 0.2390 0.2708 -0.0131 0.0259  -0.0621 270 VAL A CG1 
4270 C CG2 . VAL A 273 ? 0.3078 0.2493 0.3036 -0.0140 0.0305  -0.0824 270 VAL A CG2 
4280 N N   . LEU A 274 ? 0.2394 0.2239 0.2194 -0.0055 0.0360  -0.0657 271 LEU A N   
4281 C CA  . LEU A 274 ? 0.2392 0.2336 0.2132 -0.0076 0.0359  -0.0563 271 LEU A CA  
4282 C C   . LEU A 274 ? 0.2460 0.2527 0.2032 -0.0149 0.0365  -0.0586 271 LEU A C   
4283 O O   . LEU A 274 ? 0.2749 0.2834 0.2216 -0.0197 0.0326  -0.0485 271 LEU A O   
4284 C CB  . LEU A 274 ? 0.2664 0.2650 0.2488 -0.0020 0.0410  -0.0557 271 LEU A CB  
4285 C CG  . LEU A 274 ? 0.2628 0.2501 0.2578 0.0049  0.0394  -0.0503 271 LEU A CG  
4286 C CD1 . LEU A 274 ? 0.2679 0.2642 0.2702 0.0104  0.0433  -0.0509 271 LEU A CD1 
4287 C CD2 . LEU A 274 ? 0.2631 0.2451 0.2578 0.0025  0.0339  -0.0390 271 LEU A CD2 
4299 N N   . LEU A 275 ? 0.2667 0.2807 0.2197 -0.0157 0.0412  -0.0717 272 LEU A N   
4300 C CA  . LEU A 275 ? 0.2672 0.2950 0.2015 -0.0236 0.0424  -0.0743 272 LEU A CA  
4301 C C   . LEU A 275 ? 0.2974 0.3216 0.2200 -0.0286 0.0334  -0.0705 272 LEU A C   
4302 O O   . LEU A 275 ? 0.3580 0.3878 0.2625 -0.0350 0.0300  -0.0630 272 LEU A O   
4303 C CB  . LEU A 275 ? 0.2800 0.3187 0.2139 -0.0221 0.0499  -0.0919 272 LEU A CB  
4304 C CG  . LEU A 275 ? 0.3433 0.3937 0.2872 -0.0172 0.0585  -0.0970 272 LEU A CG  
4305 C CD1 . LEU A 275 ? 0.3901 0.4491 0.3381 -0.0118 0.0647  -0.1170 272 LEU A CD1 
4306 C CD2 . LEU A 275 ? 0.3511 0.4182 0.2825 -0.0266 0.0626  -0.0884 272 LEU A CD2 
4318 N N   . ASN A 276 ? 0.2706 0.2859 0.2027 -0.0262 0.0291  -0.0755 273 ASN A N   
4319 C CA  . ASN A 276 ? 0.3090 0.3249 0.2342 -0.0300 0.0195  -0.0724 273 ASN A CA  
4320 C C   . ASN A 276 ? 0.3193 0.3317 0.2429 -0.0288 0.0125  -0.0563 273 ASN A C   
4321 O O   . ASN A 276 ? 0.3602 0.3763 0.2711 -0.0312 0.0039  -0.0509 273 ASN A O   
4322 C CB  . ASN A 276 ? 0.2843 0.2927 0.2236 -0.0292 0.0174  -0.0808 273 ASN A CB  
4323 C CG  . ASN A 276 ? 0.3055 0.3148 0.2427 -0.0314 0.0212  -0.0980 273 ASN A CG  
4324 O OD1 . ASN A 276 ? 0.2983 0.3181 0.2220 -0.0335 0.0248  -0.1051 273 ASN A OD1 
4325 N ND2 . ASN A 276 ? 0.3801 0.3775 0.3301 -0.0316 0.0212  -0.1056 273 ASN A ND2 
4332 N N   . MET A 277 ? 0.2888 0.2936 0.2250 -0.0241 0.0150  -0.0491 274 MET A N   
4333 C CA  . MET A 277 ? 0.2705 0.2704 0.2064 -0.0219 0.0085  -0.0360 274 MET A CA  
4334 C C   . MET A 277 ? 0.3178 0.3178 0.2358 -0.0261 0.0078  -0.0268 274 MET A C   
4335 O O   . MET A 277 ? 0.3361 0.3314 0.2433 -0.0264 -0.0012 -0.0175 274 MET A O   
4336 C CB  . MET A 277 ? 0.2983 0.2909 0.2512 -0.0164 0.0112  -0.0320 274 MET A CB  
4337 C CG  . MET A 277 ? 0.2540 0.2438 0.2227 -0.0138 0.0114  -0.0370 274 MET A CG  
4338 S SD  . MET A 277 ? 0.2835 0.2651 0.2674 -0.0083 0.0175  -0.0342 274 MET A SD  
4339 C CE  . MET A 277 ? 0.2852 0.2664 0.2662 -0.0058 0.0154  -0.0230 274 MET A CE  
4349 N N   . TRP A 278 ? 0.2996 0.3042 0.2149 -0.0293 0.0170  -0.0288 275 TRP A N   
4350 C CA  . TRP A 278 ? 0.3132 0.3169 0.2161 -0.0352 0.0188  -0.0190 275 TRP A CA  
4351 C C   . TRP A 278 ? 0.3480 0.3649 0.2342 -0.0442 0.0261  -0.0233 275 TRP A C   
4352 O O   . TRP A 278 ? 0.3880 0.4049 0.2592 -0.0527 0.0277  -0.0144 275 TRP A O   
4353 C CB  . TRP A 278 ? 0.3015 0.3033 0.2204 -0.0319 0.0242  -0.0174 275 TRP A CB  
4354 C CG  . TRP A 278 ? 0.2762 0.2659 0.2073 -0.0250 0.0178  -0.0110 275 TRP A CG  
4355 C CD1 . TRP A 278 ? 0.2866 0.2677 0.2161 -0.0215 0.0079  -0.0058 275 TRP A CD1 
4356 C CD2 . TRP A 278 ? 0.2692 0.2573 0.2167 -0.0199 0.0212  -0.0111 275 TRP A CD2 
4357 N NE1 . TRP A 278 ? 0.3085 0.2835 0.2524 -0.0151 0.0059  -0.0032 275 TRP A NE1 
4358 C CE2 . TRP A 278 ? 0.2646 0.2430 0.2184 -0.0146 0.0139  -0.0059 275 TRP A CE2 
4359 C CE3 . TRP A 278 ? 0.3033 0.2993 0.2609 -0.0187 0.0291  -0.0159 275 TRP A CE3 
4360 C CZ2 . TRP A 278 ? 0.2847 0.2605 0.2523 -0.0093 0.0149  -0.0048 275 TRP A CZ2 
4361 C CZ3 . TRP A 278 ? 0.2773 0.2698 0.2483 -0.0129 0.0288  -0.0139 275 TRP A CZ3 
4362 C CH2 . TRP A 278 ? 0.2824 0.2645 0.2571 -0.0090 0.0220  -0.0081 275 TRP A CH2 
4373 N N   . GLY A 279 ? 0.3399 0.3683 0.2280 -0.0435 0.0312  -0.0374 276 GLY A N   
4374 C CA  . GLY A 279 ? 0.3729 0.4185 0.2468 -0.0513 0.0398  -0.0448 276 GLY A CA  
4375 C C   . GLY A 279 ? 0.4679 0.5165 0.3149 -0.0593 0.0345  -0.0414 276 GLY A C   
4376 O O   . GLY A 279 ? 0.5045 0.5685 0.3343 -0.0681 0.0414  -0.0457 276 GLY A O   
4377 O OXT . GLY A 279 ? 0.4683 0.5060 0.3099 -0.0570 0.0231  -0.0348 276 GLY A OXT 
4381 N N   . GLY B 3   ? 0.6734 0.9726 0.8295 0.0741  0.0443  -0.1566 0   GLY B N   
4382 C CA  . GLY B 3   ? 0.5849 0.9017 0.7379 0.0494  0.0517  -0.1593 0   GLY B CA  
4383 C C   . GLY B 3   ? 0.4212 0.7159 0.5599 0.0377  0.0537  -0.1494 0   GLY B C   
4384 O O   . GLY B 3   ? 0.5438 0.8265 0.6699 0.0274  0.0608  -0.1483 0   GLY B O   
4388 N N   . MET B 4   ? 0.3246 0.6149 0.4648 0.0397  0.0471  -0.1425 1   MET B N   
4389 C CA  . MET B 4   ? 0.2301 0.4950 0.3556 0.0283  0.0464  -0.1308 1   MET B CA  
4390 C C   . MET B 4   ? 0.2449 0.5233 0.3699 0.0046  0.0509  -0.1300 1   MET B C   
4391 O O   . MET B 4   ? 0.2596 0.5736 0.4008 -0.0010 0.0542  -0.1405 1   MET B O   
4392 C CB  . MET B 4   ? 0.2506 0.4975 0.3746 0.0422  0.0353  -0.1218 1   MET B CB  
4393 C CG  . MET B 4   ? 0.2449 0.4646 0.3624 0.0606  0.0321  -0.1173 1   MET B CG  
4394 S SD  . MET B 4   ? 0.2923 0.4896 0.4039 0.0751  0.0207  -0.1046 1   MET B SD  
4395 C CE  . MET B 4   ? 0.2993 0.4617 0.3904 0.0573  0.0214  -0.0916 1   MET B CE  
4405 N N   . GLU B 5   ? 0.2155 0.4655 0.3224 -0.0097 0.0517  -0.1178 2   GLU B N   
4406 C CA  . GLU B 5   ? 0.2343 0.4863 0.3381 -0.0316 0.0554  -0.1136 2   GLU B CA  
4407 C C   . GLU B 5   ? 0.2295 0.4728 0.3371 -0.0305 0.0470  -0.1092 2   GLU B C   
4408 O O   . GLU B 5   ? 0.2188 0.4478 0.3250 -0.0146 0.0386  -0.1054 2   GLU B O   
4409 C CB  . GLU B 5   ? 0.2554 0.4797 0.3375 -0.0456 0.0591  -0.1012 2   GLU B CB  
4410 C CG  . GLU B 5   ? 0.3200 0.5512 0.3942 -0.0472 0.0667  -0.1052 2   GLU B CG  
4411 C CD  . GLU B 5   ? 0.3948 0.6584 0.4752 -0.0631 0.0778  -0.1135 2   GLU B CD  
4412 O OE1 . GLU B 5   ? 0.4485 0.7083 0.5222 -0.0827 0.0818  -0.1058 2   GLU B OE1 
4413 O OE2 . GLU B 5   ? 0.5530 0.8459 0.6460 -0.0559 0.0827  -0.1279 2   GLU B OE2 
4420 N N   . THR B 6   ? 0.2336 0.4860 0.3460 -0.0485 0.0502  -0.1105 3   THR B N   
4421 C CA  . THR B 6   ? 0.1962 0.4428 0.3133 -0.0500 0.0434  -0.1095 3   THR B CA  
4422 C C   . THR B 6   ? 0.2798 0.5021 0.3867 -0.0707 0.0469  -0.1006 3   THR B C   
4423 O O   . THR B 6   ? 0.2780 0.5074 0.3843 -0.0893 0.0561  -0.1009 3   THR B O   
4424 C CB  . THR B 6   ? 0.2406 0.5285 0.3800 -0.0498 0.0427  -0.1248 3   THR B CB  
4425 O OG1 . THR B 6   ? 0.2321 0.5417 0.3815 -0.0273 0.0379  -0.1320 3   THR B OG1 
4426 C CG2 . THR B 6   ? 0.2387 0.5236 0.3830 -0.0545 0.0362  -0.1264 3   THR B CG2 
4434 N N   . LEU B 7   ? 0.2503 0.4446 0.3499 -0.0673 0.0399  -0.0927 4   LEU B N   
4435 C CA  . LEU B 7   ? 0.2361 0.4079 0.3307 -0.0841 0.0417  -0.0867 4   LEU B CA  
4436 C C   . LEU B 7   ? 0.2446 0.4230 0.3510 -0.0823 0.0355  -0.0952 4   LEU B C   
4437 O O   . LEU B 7   ? 0.2477 0.4207 0.3526 -0.0660 0.0270  -0.0946 4   LEU B O   
4438 C CB  . LEU B 7   ? 0.2676 0.3998 0.3430 -0.0820 0.0392  -0.0708 4   LEU B CB  
4439 C CG  . LEU B 7   ? 0.2677 0.3707 0.3371 -0.0953 0.0399  -0.0627 4   LEU B CG  
4440 C CD1 . LEU B 7   ? 0.3340 0.4382 0.4019 -0.1173 0.0500  -0.0603 4   LEU B CD1 
4441 C CD2 . LEU B 7   ? 0.3013 0.3711 0.3542 -0.0880 0.0354  -0.0483 4   LEU B CD2 
4453 N N   . GLU B 8   ? 0.2771 0.4667 0.3943 -0.1000 0.0401  -0.1031 5   GLU B N   
4454 C CA  . GLU B 8   ? 0.2480 0.4489 0.3778 -0.1004 0.0347  -0.1146 5   GLU B CA  
4455 C C   . GLU B 8   ? 0.3142 0.4754 0.4348 -0.1062 0.0328  -0.1070 5   GLU B C   
4456 O O   . GLU B 8   ? 0.3655 0.5020 0.4799 -0.1225 0.0395  -0.0995 5   GLU B O   
4457 C CB  . GLU B 8   ? 0.3368 0.5736 0.4858 -0.1168 0.0406  -0.1302 5   GLU B CB  
4458 C CG  . GLU B 8   ? 0.5876 0.8088 0.7385 -0.1431 0.0493  -0.1304 5   GLU B CG  
4459 C CD  . GLU B 8   ? 0.7558 1.0066 0.9173 -0.1518 0.0542  -0.1429 5   GLU B CD  
4460 O OE1 . GLU B 8   ? 0.6860 0.9213 0.8471 -0.1690 0.0598  -0.1436 5   GLU B OE1 
4461 O OE2 . GLU B 8   ? 0.6238 0.9119 0.7939 -0.1406 0.0524  -0.1519 5   GLU B OE2 
4468 N N   . LEU B 9   ? 0.3089 0.4631 0.4274 -0.0918 0.0240  -0.1080 6   LEU B N   
4469 C CA  . LEU B 9   ? 0.2690 0.3880 0.3798 -0.0930 0.0214  -0.1025 6   LEU B CA  
4470 C C   . LEU B 9   ? 0.2471 0.3794 0.3692 -0.0936 0.0167  -0.1177 6   LEU B C   
4471 O O   . LEU B 9   ? 0.2727 0.4423 0.4071 -0.0917 0.0142  -0.1312 6   LEU B O   
4472 C CB  . LEU B 9   ? 0.3039 0.4016 0.4000 -0.0753 0.0160  -0.0897 6   LEU B CB  
4473 C CG  . LEU B 9   ? 0.3121 0.3982 0.3966 -0.0750 0.0201  -0.0764 6   LEU B CG  
4474 C CD1 . LEU B 9   ? 0.2771 0.3472 0.3499 -0.0584 0.0146  -0.0667 6   LEU B CD1 
4475 C CD2 . LEU B 9   ? 0.3330 0.3938 0.4115 -0.0924 0.0267  -0.0677 6   LEU B CD2 
4487 N N   . GLN B 10  ? 0.3214 0.4243 0.4395 -0.0956 0.0150  -0.1164 7   GLN B N   
4488 C CA  . GLN B 10  ? 0.3516 0.4655 0.4785 -0.0956 0.0106  -0.1319 7   GLN B CA  
4489 C C   . GLN B 10  ? 0.2401 0.3794 0.3642 -0.0750 0.0018  -0.1348 7   GLN B C   
4490 O O   . GLN B 10  ? 0.2829 0.4063 0.3945 -0.0602 -0.0018 -0.1234 7   GLN B O   
4491 C CB  . GLN B 10  ? 0.3607 0.4350 0.4830 -0.0989 0.0109  -0.1294 7   GLN B CB  
4492 C CG  . GLN B 10  ? 0.7382 0.8206 0.8689 -0.0997 0.0071  -0.1472 7   GLN B CG  
4493 C CD  . GLN B 10  ? 0.7539 0.7961 0.8830 -0.1034 0.0085  -0.1475 7   GLN B CD  
4494 O OE1 . GLN B 10  ? 0.7345 0.7425 0.8624 -0.1147 0.0145  -0.1389 7   GLN B OE1 
4495 N NE2 . GLN B 10  ? 0.8294 0.8762 0.9578 -0.0927 0.0029  -0.1569 7   GLN B NE2 
4504 N N   . GLY B 11  ? 0.2532 0.4331 0.3890 -0.0744 -0.0016 -0.1496 8   GLY B N   
4505 C CA  . GLY B 11  ? 0.2796 0.4850 0.4119 -0.0549 -0.0104 -0.1515 8   GLY B CA  
4506 C C   . GLY B 11  ? 0.2667 0.4838 0.3937 -0.0388 -0.0124 -0.1406 8   GLY B C   
4507 O O   . GLY B 11  ? 0.2559 0.4891 0.3779 -0.0213 -0.0196 -0.1393 8   GLY B O   
4511 N N   . ALA B 12  ? 0.2150 0.4233 0.3419 -0.0438 -0.0060 -0.1326 9   ALA B N   
4512 C CA  . ALA B 12  ? 0.1938 0.4121 0.3168 -0.0282 -0.0075 -0.1246 9   ALA B CA  
4513 C C   . ALA B 12  ? 0.2697 0.4911 0.3975 -0.0378 0.0006  -0.1229 9   ALA B C   
4514 O O   . ALA B 12  ? 0.2601 0.4632 0.3870 -0.0551 0.0077  -0.1206 9   ALA B O   
4515 C CB  . ALA B 12  ? 0.2139 0.4016 0.3197 -0.0145 -0.0098 -0.1092 9   ALA B CB  
4521 N N   . LYS B 13  ? 0.1967 0.4408 0.3286 -0.0254 -0.0004 -0.1234 10  LYS B N   
4522 C CA  . LYS B 13  ? 0.1955 0.4412 0.3285 -0.0296 0.0071  -0.1205 10  LYS B CA  
4523 C C   . LYS B 13  ? 0.1962 0.4163 0.3143 -0.0148 0.0060  -0.1070 10  LYS B C   
4524 O O   . LYS B 13  ? 0.1938 0.4189 0.3099 0.0042  -0.0002 -0.1049 10  LYS B O   
4525 C CB  . LYS B 13  ? 0.1878 0.4790 0.3389 -0.0261 0.0076  -0.1335 10  LYS B CB  
4526 C CG  . LYS B 13  ? 0.2011 0.5208 0.3692 -0.0450 0.0102  -0.1489 10  LYS B CG  
4527 C CD  . LYS B 13  ? 0.2231 0.5831 0.4047 -0.0420 0.0117  -0.1606 10  LYS B CD  
4528 C CE  . LYS B 13  ? 0.3126 0.6911 0.5002 -0.0498 0.0097  -0.1731 10  LYS B CE  
4529 N NZ  . LYS B 13  ? 0.3524 0.7659 0.5480 -0.0423 0.0089  -0.1832 10  LYS B NZ  
4543 N N   . LEU B 14  ? 0.2066 0.3972 0.3130 -0.0240 0.0115  -0.0971 11  LEU B N   
4544 C CA  . LEU B 14  ? 0.1810 0.3464 0.2734 -0.0134 0.0107  -0.0856 11  LEU B CA  
4545 C C   . LEU B 14  ? 0.2248 0.4006 0.3186 -0.0111 0.0163  -0.0871 11  LEU B C   
4546 O O   . LEU B 14  ? 0.2351 0.4163 0.3298 -0.0256 0.0237  -0.0888 11  LEU B O   
4547 C CB  . LEU B 14  ? 0.1932 0.3242 0.2726 -0.0235 0.0124  -0.0750 11  LEU B CB  
4548 C CG  . LEU B 14  ? 0.2282 0.3343 0.2941 -0.0137 0.0104  -0.0642 11  LEU B CG  
4549 C CD1 . LEU B 14  ? 0.2291 0.3279 0.2922 -0.0005 0.0034  -0.0619 11  LEU B CD1 
4550 C CD2 . LEU B 14  ? 0.2589 0.3389 0.3141 -0.0252 0.0132  -0.0547 11  LEU B CD2 
4562 N N   . ARG B 15  ? 0.1714 0.3501 0.2650 0.0068  0.0133  -0.0867 12  ARG B N   
4563 C CA  . ARG B 15  ? 0.1821 0.3710 0.2786 0.0113  0.0185  -0.0907 12  ARG B CA  
4564 C C   . ARG B 15  ? 0.1844 0.3429 0.2659 0.0144  0.0200  -0.0815 12  ARG B C   
4565 O O   . ARG B 15  ? 0.1962 0.3316 0.2688 0.0218  0.0151  -0.0732 12  ARG B O   
4566 C CB  . ARG B 15  ? 0.1775 0.3911 0.2867 0.0303  0.0147  -0.0985 12  ARG B CB  
4567 C CG  . ARG B 15  ? 0.2484 0.5034 0.3764 0.0265  0.0166  -0.1120 12  ARG B CG  
4568 C CD  . ARG B 15  ? 0.2249 0.4911 0.3582 0.0125  0.0147  -0.1155 12  ARG B CD  
4569 N NE  . ARG B 15  ? 0.2291 0.5392 0.3826 0.0071  0.0167  -0.1304 12  ARG B NE  
4570 C CZ  . ARG B 15  ? 0.1828 0.5231 0.3497 0.0150  0.0095  -0.1391 12  ARG B CZ  
4571 N NH1 . ARG B 15  ? 0.1695 0.5024 0.3307 0.0317  -0.0005 -0.1337 12  ARG B NH1 
4572 N NH2 . ARG B 15  ? 0.1862 0.5538 0.3634 0.0041  0.0117  -0.1504 12  ARG B NH2 
4586 N N   . TYR B 16  ? 0.1834 0.3444 0.2622 0.0079  0.0272  -0.0841 13  TYR B N   
4587 C CA  . TYR B 16  ? 0.1967 0.3335 0.2620 0.0089  0.0288  -0.0779 13  TYR B CA  
4588 C C   . TYR B 16  ? 0.1912 0.3415 0.2589 0.0101  0.0358  -0.0868 13  TYR B C   
4589 O O   . TYR B 16  ? 0.2030 0.3805 0.2799 0.0042  0.0414  -0.0959 13  TYR B O   
4590 C CB  . TYR B 16  ? 0.1896 0.3066 0.2413 -0.0065 0.0295  -0.0680 13  TYR B CB  
4591 C CG  . TYR B 16  ? 0.2072 0.3368 0.2585 -0.0244 0.0358  -0.0690 13  TYR B CG  
4592 C CD1 . TYR B 16  ? 0.2149 0.3531 0.2739 -0.0332 0.0355  -0.0702 13  TYR B CD1 
4593 C CD2 . TYR B 16  ? 0.2344 0.3663 0.2763 -0.0337 0.0425  -0.0686 13  TYR B CD2 
4594 C CE1 . TYR B 16  ? 0.2459 0.3934 0.3046 -0.0516 0.0426  -0.0705 13  TYR B CE1 
4595 C CE2 . TYR B 16  ? 0.2440 0.3863 0.2832 -0.0515 0.0493  -0.0674 13  TYR B CE2 
4596 C CZ  . TYR B 16  ? 0.2946 0.4429 0.3423 -0.0607 0.0496  -0.0677 13  TYR B CZ  
4597 O OH  . TYR B 16  ? 0.3002 0.4565 0.3455 -0.0800 0.0574  -0.0660 13  TYR B OH  
4607 N N   . HIS B 17  ? 0.2031 0.3346 0.2627 0.0169  0.0362  -0.0853 14  HIS B N   
4608 C CA  . HIS B 17  ? 0.2184 0.3581 0.2773 0.0163  0.0433  -0.0944 14  HIS B CA  
4609 C C   . HIS B 17  ? 0.2248 0.3592 0.2684 -0.0015 0.0473  -0.0895 14  HIS B C   
4610 O O   . HIS B 17  ? 0.2589 0.3717 0.2909 -0.0068 0.0431  -0.0781 14  HIS B O   
4611 C CB  . HIS B 17  ? 0.2658 0.3861 0.3233 0.0306  0.0422  -0.0966 14  HIS B CB  
4612 C CG  . HIS B 17  ? 0.2596 0.3785 0.3284 0.0498  0.0373  -0.0974 14  HIS B CG  
4613 N ND1 . HIS B 17  ? 0.2750 0.4155 0.3591 0.0626  0.0392  -0.1087 14  HIS B ND1 
4614 C CD2 . HIS B 17  ? 0.2968 0.3967 0.3631 0.0589  0.0303  -0.0876 14  HIS B CD2 
4615 C CE1 . HIS B 17  ? 0.2800 0.4129 0.3696 0.0798  0.0328  -0.1045 14  HIS B CE1 
4616 N NE2 . HIS B 17  ? 0.2955 0.4041 0.3735 0.0771  0.0277  -0.0915 14  HIS B NE2 
4624 N N   . GLN B 18  ? 0.2551 0.4105 0.2983 -0.0098 0.0554  -0.0979 15  GLN B N   
4625 C CA  . GLN B 18  ? 0.2852 0.4371 0.3109 -0.0259 0.0593  -0.0923 15  GLN B CA  
4626 C C   . GLN B 18  ? 0.2985 0.4639 0.3215 -0.0255 0.0667  -0.1049 15  GLN B C   
4627 O O   . GLN B 18  ? 0.2881 0.4802 0.3221 -0.0242 0.0735  -0.1177 15  GLN B O   
4628 C CB  . GLN B 18  ? 0.2996 0.4640 0.3232 -0.0425 0.0629  -0.0866 15  GLN B CB  
4629 C CG  . GLN B 18  ? 0.3152 0.4811 0.3198 -0.0590 0.0684  -0.0806 15  GLN B CG  
4630 C CD  . GLN B 18  ? 0.4035 0.5686 0.4024 -0.0758 0.0705  -0.0691 15  GLN B CD  
4631 O OE1 . GLN B 18  ? 0.4321 0.5960 0.4425 -0.0764 0.0682  -0.0676 15  GLN B OE1 
4632 N NE2 . GLN B 18  ? 0.4569 0.6260 0.4384 -0.0906 0.0764  -0.0627 15  GLN B NE2 
4641 N N   . VAL B 19  ? 0.2705 0.4196 0.2797 -0.0267 0.0654  -0.1030 16  VAL B N   
4642 C CA  . VAL B 19  ? 0.3236 0.4830 0.3295 -0.0260 0.0718  -0.1170 16  VAL B CA  
4643 C C   . VAL B 19  ? 0.3187 0.4727 0.3026 -0.0390 0.0716  -0.1106 16  VAL B C   
4644 O O   . VAL B 19  ? 0.3225 0.4544 0.2978 -0.0396 0.0642  -0.0992 16  VAL B O   
4645 C CB  . VAL B 19  ? 0.4232 0.5673 0.4394 -0.0088 0.0699  -0.1267 16  VAL B CB  
4646 C CG1 . VAL B 19  ? 0.5341 0.6816 0.5704 0.0067  0.0676  -0.1294 16  VAL B CG1 
4647 C CG2 . VAL B 19  ? 0.5217 0.6362 0.5286 -0.0079 0.0629  -0.1172 16  VAL B CG2 
4657 N N   . GLY B 20  ? 0.3352 0.5117 0.3104 -0.0486 0.0796  -0.1186 17  GLY B N   
4658 C CA  . GLY B 20  ? 0.3431 0.5194 0.2965 -0.0594 0.0794  -0.1150 17  GLY B CA  
4659 C C   . GLY B 20  ? 0.3443 0.5298 0.2808 -0.0756 0.0811  -0.1000 17  GLY B C   
4660 O O   . GLY B 20  ? 0.3800 0.5749 0.3225 -0.0812 0.0849  -0.0951 17  GLY B O   
4664 N N   . GLN B 21  ? 0.3211 0.5045 0.2361 -0.0836 0.0784  -0.0929 18  GLN B N   
4665 C CA  . GLN B 21  ? 0.3904 0.5795 0.2839 -0.0984 0.0792  -0.0765 18  GLN B CA  
4666 C C   . GLN B 21  ? 0.3935 0.5655 0.2705 -0.0988 0.0687  -0.0629 18  GLN B C   
4667 O O   . GLN B 21  ? 0.3843 0.5513 0.2620 -0.0921 0.0640  -0.0715 18  GLN B O   
4668 C CB  . GLN B 21  ? 0.3921 0.6106 0.2748 -0.1088 0.0890  -0.0853 18  GLN B CB  
4669 C CG  . GLN B 21  ? 0.4724 0.7079 0.3771 -0.1062 0.0968  -0.0987 18  GLN B CG  
4670 C CD  . GLN B 21  ? 0.5769 0.8361 0.4768 -0.1146 0.1027  -0.1047 18  GLN B CD  
4671 O OE1 . GLN B 21  ? 0.5919 0.8543 0.4702 -0.1262 0.1023  -0.0924 18  GLN B OE1 
4672 N NE2 . GLN B 21  ? 0.5591 0.8353 0.4787 -0.1083 0.1078  -0.1231 18  GLN B NE2 
4681 N N   . GLY B 22  ? 0.3798 0.5428 0.2429 -0.1067 0.0652  -0.0418 19  GLY B N   
4682 C CA  . GLY B 22  ? 0.3557 0.5029 0.2054 -0.1051 0.0542  -0.0268 19  GLY B CA  
4683 C C   . GLY B 22  ? 0.3387 0.4587 0.1974 -0.1003 0.0470  -0.0112 19  GLY B C   
4684 O O   . GLY B 22  ? 0.3699 0.4844 0.2424 -0.1008 0.0509  -0.0106 19  GLY B O   
4688 N N   . PRO B 23  ? 0.3560 0.4610 0.2086 -0.0953 0.0362  0.0002  20  PRO B N   
4689 C CA  . PRO B 23  ? 0.3617 0.4412 0.2242 -0.0894 0.0295  0.0129  20  PRO B CA  
4690 C C   . PRO B 23  ? 0.3126 0.3842 0.1996 -0.0803 0.0302  0.0011  20  PRO B C   
4691 O O   . PRO B 23  ? 0.3292 0.4082 0.2254 -0.0745 0.0320  -0.0147 20  PRO B O   
4692 C CB  . PRO B 23  ? 0.3753 0.4470 0.2294 -0.0834 0.0179  0.0219  20  PRO B CB  
4693 C CG  . PRO B 23  ? 0.5292 0.6230 0.3679 -0.0873 0.0181  0.0144  20  PRO B CG  
4694 C CD  . PRO B 23  ? 0.4005 0.5142 0.2375 -0.0947 0.0297  0.0004  20  PRO B CD  
4702 N N   . VAL B 24  ? 0.3133 0.3685 0.2102 -0.0788 0.0287  0.0090  21  VAL B N   
4703 C CA  . VAL B 24  ? 0.2853 0.3352 0.2033 -0.0705 0.0291  -0.0007 21  VAL B CA  
4704 C C   . VAL B 24  ? 0.2810 0.3189 0.2061 -0.0590 0.0211  -0.0027 21  VAL B C   
4705 O O   . VAL B 24  ? 0.2967 0.3226 0.2167 -0.0567 0.0137  0.0079  21  VAL B O   
4706 C CB  . VAL B 24  ? 0.2921 0.3310 0.2179 -0.0739 0.0300  0.0066  21  VAL B CB  
4707 C CG1 . VAL B 24  ? 0.2723 0.3057 0.2177 -0.0637 0.0278  -0.0017 21  VAL B CG1 
4708 C CG2 . VAL B 24  ? 0.3545 0.4085 0.2782 -0.0863 0.0398  0.0048  21  VAL B CG2 
4718 N N   . LEU B 25  ? 0.2507 0.2920 0.1880 -0.0515 0.0231  -0.0159 22  LEU B N   
4719 C CA  . LEU B 25  ? 0.2558 0.2855 0.2014 -0.0418 0.0178  -0.0186 22  LEU B CA  
4720 C C   . LEU B 25  ? 0.2642 0.2896 0.2256 -0.0343 0.0193  -0.0236 22  LEU B C   
4721 O O   . LEU B 25  ? 0.2490 0.2841 0.2172 -0.0317 0.0248  -0.0340 22  LEU B O   
4722 C CB  . LEU B 25  ? 0.2699 0.3062 0.2128 -0.0408 0.0191  -0.0296 22  LEU B CB  
4723 C CG  . LEU B 25  ? 0.3074 0.3324 0.2594 -0.0329 0.0165  -0.0348 22  LEU B CG  
4724 C CD1 . LEU B 25  ? 0.3793 0.3933 0.3323 -0.0304 0.0090  -0.0243 22  LEU B CD1 
4725 C CD2 . LEU B 25  ? 0.3303 0.3621 0.2778 -0.0356 0.0186  -0.0463 22  LEU B CD2 
4737 N N   . ILE B 26  ? 0.2507 0.2635 0.2179 -0.0302 0.0145  -0.0166 23  ILE B N   
4738 C CA  . ILE B 26  ? 0.2324 0.2429 0.2125 -0.0229 0.0147  -0.0204 23  ILE B CA  
4739 C C   . ILE B 26  ? 0.2216 0.2230 0.2064 -0.0136 0.0121  -0.0230 23  ILE B C   
4740 O O   . ILE B 26  ? 0.2447 0.2367 0.2272 -0.0127 0.0076  -0.0176 23  ILE B O   
4741 C CB  . ILE B 26  ? 0.2338 0.2373 0.2174 -0.0247 0.0118  -0.0134 23  ILE B CB  
4742 C CG1 . ILE B 26  ? 0.2589 0.2683 0.2378 -0.0359 0.0156  -0.0100 23  ILE B CG1 
4743 C CG2 . ILE B 26  ? 0.2226 0.2282 0.2183 -0.0173 0.0114  -0.0187 23  ILE B CG2 
4744 C CD1 . ILE B 26  ? 0.2920 0.2902 0.2735 -0.0396 0.0133  -0.0032 23  ILE B CD1 
4756 N N   . PHE B 27  ? 0.2044 0.2088 0.1964 -0.0064 0.0151  -0.0307 24  PHE B N   
4757 C CA  . PHE B 27  ? 0.2185 0.2119 0.2147 0.0025  0.0139  -0.0316 24  PHE B CA  
4758 C C   . PHE B 27  ? 0.2176 0.2104 0.2208 0.0096  0.0115  -0.0291 24  PHE B C   
4759 O O   . PHE B 27  ? 0.2053 0.2095 0.2145 0.0125  0.0129  -0.0331 24  PHE B O   
4760 C CB  . PHE B 27  ? 0.2127 0.2058 0.2112 0.0073  0.0185  -0.0406 24  PHE B CB  
4761 C CG  . PHE B 27  ? 0.2486 0.2408 0.2404 0.0007  0.0206  -0.0454 24  PHE B CG  
4762 C CD1 . PHE B 27  ? 0.2761 0.2584 0.2643 -0.0020 0.0181  -0.0428 24  PHE B CD1 
4763 C CD2 . PHE B 27  ? 0.2850 0.2894 0.2746 -0.0029 0.0253  -0.0540 24  PHE B CD2 
4764 C CE1 . PHE B 27  ? 0.2807 0.2657 0.2633 -0.0087 0.0195  -0.0490 24  PHE B CE1 
4765 C CE2 . PHE B 27  ? 0.3107 0.3168 0.2933 -0.0093 0.0271  -0.0603 24  PHE B CE2 
4766 C CZ  . PHE B 27  ? 0.2783 0.2745 0.2575 -0.0122 0.0237  -0.0578 24  PHE B CZ  
4776 N N   . ILE B 28  ? 0.2142 0.1966 0.2168 0.0125  0.0082  -0.0238 25  ILE B N   
4777 C CA  . ILE B 28  ? 0.2309 0.2140 0.2380 0.0189  0.0056  -0.0216 25  ILE B CA  
4778 C C   . ILE B 28  ? 0.2028 0.1774 0.2097 0.0278  0.0065  -0.0206 25  ILE B C   
4779 O O   . ILE B 28  ? 0.2292 0.1927 0.2328 0.0264  0.0068  -0.0175 25  ILE B O   
4780 C CB  . ILE B 28  ? 0.2165 0.1955 0.2227 0.0155  0.0018  -0.0167 25  ILE B CB  
4781 C CG1 . ILE B 28  ? 0.2129 0.1934 0.2171 0.0066  0.0011  -0.0148 25  ILE B CG1 
4782 C CG2 . ILE B 28  ? 0.2172 0.2010 0.2278 0.0213  -0.0003 -0.0173 25  ILE B CG2 
4783 C CD1 . ILE B 28  ? 0.2162 0.1892 0.2204 0.0050  -0.0028 -0.0099 25  ILE B CD1 
4795 N N   . PRO B 29  ? 0.1972 0.1768 0.2076 0.0368  0.0067  -0.0224 26  PRO B N   
4796 C CA  . PRO B 29  ? 0.2233 0.1915 0.2317 0.0462  0.0078  -0.0191 26  PRO B CA  
4797 C C   . PRO B 29  ? 0.2381 0.2019 0.2425 0.0486  0.0054  -0.0121 26  PRO B C   
4798 O O   . PRO B 29  ? 0.2314 0.2050 0.2368 0.0468  0.0021  -0.0120 26  PRO B O   
4799 C CB  . PRO B 29  ? 0.2448 0.2237 0.2587 0.0569  0.0074  -0.0226 26  PRO B CB  
4800 C CG  . PRO B 29  ? 0.2398 0.2389 0.2587 0.0526  0.0045  -0.0263 26  PRO B CG  
4801 C CD  . PRO B 29  ? 0.2248 0.2223 0.2417 0.0392  0.0059  -0.0274 26  PRO B CD  
4809 N N   . GLY B 30  ? 0.2643 0.2131 0.2642 0.0526  0.0079  -0.0071 27  GLY B N   
4810 C CA  . GLY B 30  ? 0.2671 0.2121 0.2613 0.0557  0.0072  0.0003  27  GLY B CA  
4811 C C   . GLY B 30  ? 0.2677 0.2189 0.2594 0.0681  0.0046  0.0041  27  GLY B C   
4812 O O   . GLY B 30  ? 0.2813 0.2493 0.2782 0.0724  0.0009  -0.0006 27  GLY B O   
4816 N N   . ALA B 31  ? 0.3213 0.2604 0.3049 0.0736  0.0064  0.0130  28  ALA B N   
4817 C CA  . ALA B 31  ? 0.3277 0.2756 0.3058 0.0856  0.0027  0.0189  28  ALA B CA  
4818 C C   . ALA B 31  ? 0.3580 0.3123 0.3411 0.0978  -0.0002 0.0167  28  ALA B C   
4819 O O   . ALA B 31  ? 0.3993 0.3713 0.3814 0.1077  -0.0057 0.0179  28  ALA B O   
4820 C CB  . ALA B 31  ? 0.3723 0.3029 0.3380 0.0886  0.0063  0.0313  28  ALA B CB  
4826 N N   . ASN B 32  ? 0.3400 0.2823 0.3290 0.0984  0.0032  0.0127  29  ASN B N   
4827 C CA  . ASN B 32  ? 0.3304 0.2821 0.3268 0.1112  0.0007  0.0087  29  ASN B CA  
4828 C C   . ASN B 32  ? 0.3075 0.2899 0.3139 0.1085  -0.0035 -0.0018 29  ASN B C   
4829 O O   . ASN B 32  ? 0.3147 0.3150 0.3279 0.1198  -0.0073 -0.0052 29  ASN B O   
4830 C CB  . ASN B 32  ? 0.3401 0.2731 0.3414 0.1116  0.0064  0.0040  29  ASN B CB  
4831 C CG  . ASN B 32  ? 0.3767 0.3156 0.3840 0.0969  0.0093  -0.0070 29  ASN B CG  
4832 O OD1 . ASN B 32  ? 0.4010 0.3323 0.4041 0.0841  0.0115  -0.0060 29  ASN B OD1 
4833 N ND2 . ASN B 32  ? 0.3222 0.2767 0.3392 0.0989  0.0095  -0.0172 29  ASN B ND2 
4840 N N   . GLY B 33  ? 0.2759 0.2645 0.2839 0.0939  -0.0027 -0.0069 30  GLY B N   
4841 C CA  . GLY B 33  ? 0.2788 0.2925 0.2947 0.0883  -0.0058 -0.0153 30  GLY B CA  
4842 C C   . GLY B 33  ? 0.2452 0.2709 0.2716 0.0848  -0.0036 -0.0252 30  GLY B C   
4843 O O   . GLY B 33  ? 0.2417 0.2851 0.2742 0.0761  -0.0044 -0.0318 30  GLY B O   
4847 N N   . THR B 34  ? 0.2633 0.2792 0.2918 0.0898  0.0002  -0.0270 31  THR B N   
4848 C CA  . THR B 34  ? 0.2601 0.2923 0.2991 0.0892  0.0028  -0.0376 31  THR B CA  
4849 C C   . THR B 34  ? 0.2607 0.2793 0.2978 0.0801  0.0091  -0.0416 31  THR B C   
4850 O O   . THR B 34  ? 0.2790 0.2734 0.3089 0.0792  0.0116  -0.0372 31  THR B O   
4851 C CB  . THR B 34  ? 0.2908 0.3333 0.3377 0.1073  0.0008  -0.0400 31  THR B CB  
4852 O OG1 . THR B 34  ? 0.3273 0.3426 0.3684 0.1179  0.0026  -0.0334 31  THR B OG1 
4853 C CG2 . THR B 34  ? 0.3290 0.3922 0.3775 0.1159  -0.0067 -0.0372 31  THR B CG2 
4861 N N   . GLY B 35  ? 0.2588 0.2952 0.3020 0.0720  0.0121  -0.0505 32  GLY B N   
4862 C CA  . GLY B 35  ? 0.2657 0.2949 0.3050 0.0613  0.0175  -0.0547 32  GLY B CA  
4863 C C   . GLY B 35  ? 0.2607 0.2833 0.3033 0.0691  0.0223  -0.0622 32  GLY B C   
4864 O O   . GLY B 35  ? 0.2597 0.2729 0.2970 0.0608  0.0266  -0.0659 32  GLY B O   
4868 N N   . ASP B 36  ? 0.2661 0.2939 0.3175 0.0854  0.0213  -0.0652 33  ASP B N   
4869 C CA  . ASP B 36  ? 0.2715 0.2911 0.3280 0.0946  0.0262  -0.0736 33  ASP B CA  
4870 C C   . ASP B 36  ? 0.2925 0.2782 0.3402 0.0929  0.0289  -0.0701 33  ASP B C   
4871 O O   . ASP B 36  ? 0.3268 0.3044 0.3766 0.0930  0.0346  -0.0800 33  ASP B O   
4872 C CB  . ASP B 36  ? 0.3115 0.3392 0.3791 0.1156  0.0233  -0.0751 33  ASP B CB  
4873 C CG  . ASP B 36  ? 0.3795 0.3978 0.4424 0.1259  0.0161  -0.0612 33  ASP B CG  
4874 O OD1 . ASP B 36  ? 0.4628 0.4935 0.5337 0.1422  0.0120  -0.0607 33  ASP B OD1 
4875 O OD2 . ASP B 36  ? 0.3875 0.3891 0.4386 0.1174  0.0145  -0.0509 33  ASP B OD2 
4880 N N   . ILE B 37  ? 0.3153 0.2828 0.3537 0.0896  0.0258  -0.0577 34  ILE B N   
4881 C CA  . ILE B 37  ? 0.2961 0.2332 0.3274 0.0858  0.0290  -0.0545 34  ILE B CA  
4882 C C   . ILE B 37  ? 0.3277 0.2657 0.3552 0.0695  0.0330  -0.0628 34  ILE B C   
4883 O O   . ILE B 37  ? 0.3397 0.2574 0.3645 0.0657  0.0372  -0.0664 34  ILE B O   
4884 C CB  . ILE B 37  ? 0.2911 0.2150 0.3139 0.0846  0.0252  -0.0398 34  ILE B CB  
4885 C CG1 . ILE B 37  ? 0.3478 0.2384 0.3657 0.0850  0.0296  -0.0358 34  ILE B CG1 
4886 C CG2 . ILE B 37  ? 0.3185 0.2551 0.3364 0.0702  0.0223  -0.0367 34  ILE B CG2 
4887 C CD1 . ILE B 37  ? 0.3611 0.2387 0.3705 0.0853  0.0274  -0.0210 34  ILE B CD1 
4899 N N   . PHE B 38  ? 0.2679 0.2295 0.2947 0.0597  0.0321  -0.0661 35  PHE B N   
4900 C CA  . PHE B 38  ? 0.2569 0.2232 0.2776 0.0449  0.0348  -0.0721 35  PHE B CA  
4901 C C   . PHE B 38  ? 0.2663 0.2472 0.2910 0.0444  0.0404  -0.0868 35  PHE B C   
4902 O O   . PHE B 38  ? 0.2771 0.2660 0.2952 0.0322  0.0427  -0.0924 35  PHE B O   
4903 C CB  . PHE B 38  ? 0.2412 0.2219 0.2565 0.0342  0.0307  -0.0649 35  PHE B CB  
4904 C CG  . PHE B 38  ? 0.2830 0.2518 0.2940 0.0325  0.0258  -0.0530 35  PHE B CG  
4905 C CD1 . PHE B 38  ? 0.2811 0.2349 0.2870 0.0266  0.0260  -0.0510 35  PHE B CD1 
4906 C CD2 . PHE B 38  ? 0.2899 0.2651 0.3032 0.0366  0.0215  -0.0456 35  PHE B CD2 
4907 C CE1 . PHE B 38  ? 0.2793 0.2255 0.2826 0.0251  0.0224  -0.0413 35  PHE B CE1 
4908 C CE2 . PHE B 38  ? 0.2923 0.2584 0.3018 0.0353  0.0178  -0.0364 35  PHE B CE2 
4909 C CZ  . PHE B 38  ? 0.2905 0.2424 0.2952 0.0299  0.0184  -0.0341 35  PHE B CZ  
4919 N N   . LEU B 39  ? 0.2768 0.2643 0.3120 0.0576  0.0425  -0.0935 36  LEU B N   
4920 C CA  . LEU B 39  ? 0.2865 0.2940 0.3264 0.0560  0.0484  -0.1088 36  LEU B CA  
4921 C C   . LEU B 39  ? 0.3185 0.3125 0.3558 0.0528  0.0543  -0.1214 36  LEU B C   
4922 O O   . LEU B 39  ? 0.3360 0.3476 0.3693 0.0429  0.0587  -0.1321 36  LEU B O   
4923 C CB  . LEU B 39  ? 0.2846 0.3073 0.3390 0.0720  0.0491  -0.1147 36  LEU B CB  
4924 C CG  . LEU B 39  ? 0.3398 0.3869 0.3977 0.0702  0.0447  -0.1077 36  LEU B CG  
4925 C CD1 . LEU B 39  ? 0.3442 0.4100 0.4180 0.0871  0.0437  -0.1131 36  LEU B CD1 
4926 C CD2 . LEU B 39  ? 0.3749 0.4451 0.4269 0.0523  0.0476  -0.1100 36  LEU B CD2 
4938 N N   . PRO B 40  ? 0.3055 0.2693 0.3442 0.0595  0.0552  -0.1213 37  PRO B N   
4939 C CA  . PRO B 40  ? 0.3292 0.2810 0.3654 0.0527  0.0610  -0.1353 37  PRO B CA  
4940 C C   . PRO B 40  ? 0.2970 0.2569 0.3203 0.0335  0.0597  -0.1343 37  PRO B C   
4941 O O   . PRO B 40  ? 0.3442 0.3142 0.3637 0.0249  0.0642  -0.1489 37  PRO B O   
4942 C CB  . PRO B 40  ? 0.3828 0.2973 0.4217 0.0614  0.0614  -0.1305 37  PRO B CB  
4943 C CG  . PRO B 40  ? 0.3455 0.2581 0.3917 0.0796  0.0577  -0.1200 37  PRO B CG  
4944 C CD  . PRO B 40  ? 0.3200 0.2603 0.3635 0.0742  0.0521  -0.1108 37  PRO B CD  
4952 N N   . LEU B 41  ? 0.2897 0.2467 0.3065 0.0278  0.0534  -0.1183 38  LEU B N   
4953 C CA  . LEU B 41  ? 0.3017 0.2691 0.3071 0.0119  0.0507  -0.1159 38  LEU B CA  
4954 C C   . LEU B 41  ? 0.3079 0.3053 0.3073 0.0050  0.0511  -0.1182 38  LEU B C   
4955 O O   . LEU B 41  ? 0.3076 0.3177 0.2976 -0.0063 0.0522  -0.1247 38  LEU B O   
4956 C CB  . LEU B 41  ? 0.2997 0.2580 0.3017 0.0095  0.0441  -0.0991 38  LEU B CB  
4957 C CG  . LEU B 41  ? 0.2711 0.2408 0.2631 -0.0037 0.0396  -0.0943 38  LEU B CG  
4958 C CD1 . LEU B 41  ? 0.3068 0.2739 0.2954 -0.0128 0.0421  -0.1065 38  LEU B CD1 
4959 C CD2 . LEU B 41  ? 0.2608 0.2218 0.2528 -0.0028 0.0339  -0.0793 38  LEU B CD2 
4971 N N   . ALA B 42  ? 0.3006 0.3108 0.3048 0.0107  0.0504  -0.1130 39  ALA B N   
4972 C CA  . ALA B 42  ? 0.3088 0.3464 0.3076 0.0025  0.0523  -0.1143 39  ALA B CA  
4973 C C   . ALA B 42  ? 0.2855 0.3382 0.2828 -0.0008 0.0599  -0.1324 39  ALA B C   
4974 O O   . ALA B 42  ? 0.3425 0.4147 0.3281 -0.0126 0.0617  -0.1341 39  ALA B O   
4975 C CB  . ALA B 42  ? 0.2878 0.3378 0.2960 0.0093  0.0520  -0.1099 39  ALA B CB  
4981 N N   . GLU B 43  ? 0.2943 0.3384 0.3027 0.0102  0.0647  -0.1460 40  GLU B N   
4982 C CA  . GLU B 43  ? 0.3474 0.4051 0.3562 0.0084  0.0726  -0.1663 40  GLU B CA  
4983 C C   . GLU B 43  ? 0.3124 0.3698 0.3073 -0.0054 0.0725  -0.1715 40  GLU B C   
4984 O O   . GLU B 43  ? 0.3958 0.4738 0.3844 -0.0132 0.0755  -0.1793 40  GLU B O   
4985 C CB  . GLU B 43  ? 0.3717 0.4107 0.3955 0.0242  0.0740  -0.1723 40  GLU B CB  
4986 C CG  . GLU B 43  ? 0.5497 0.6026 0.5874 0.0375  0.0747  -0.1717 40  GLU B CG  
4987 C CD  . GLU B 43  ? 0.6005 0.6906 0.6374 0.0298  0.0788  -0.1775 40  GLU B CD  
4988 O OE1 . GLU B 43  ? 0.5601 0.6610 0.5930 0.0232  0.0830  -0.1883 40  GLU B OE1 
4989 O OE2 . GLU B 43  ? 0.4699 0.5786 0.5103 0.0295  0.0779  -0.1713 40  GLU B OE2 
4996 N N   . GLN B 44  ? 0.3281 0.3643 0.3191 -0.0087 0.0674  -0.1645 41  GLN B N   
4997 C CA  . GLN B 44  ? 0.3209 0.3601 0.3002 -0.0216 0.0663  -0.1704 41  GLN B CA  
4998 C C   . GLN B 44  ? 0.3456 0.4059 0.3085 -0.0336 0.0608  -0.1580 41  GLN B C   
4999 O O   . GLN B 44  ? 0.3939 0.4676 0.3446 -0.0443 0.0601  -0.1647 41  GLN B O   
5000 C CB  . GLN B 44  ? 0.3822 0.3923 0.3660 -0.0210 0.0628  -0.1665 41  GLN B CB  
5001 C CG  . GLN B 44  ? 0.3533 0.3374 0.3514 -0.0094 0.0673  -0.1736 41  GLN B CG  
5002 C CD  . GLN B 44  ? 0.4586 0.4473 0.4589 -0.0115 0.0715  -0.1888 41  GLN B CD  
5003 O OE1 . GLN B 44  ? 0.4759 0.4770 0.4685 -0.0239 0.0709  -0.1961 41  GLN B OE1 
5004 N NE2 . GLN B 44  ? 0.5157 0.4974 0.5265 0.0011  0.0754  -0.1940 41  GLN B NE2 
5013 N N   . LEU B 45  ? 0.3042 0.3676 0.2664 -0.0317 0.0569  -0.1405 42  LEU B N   
5014 C CA  . LEU B 45  ? 0.2953 0.3714 0.2430 -0.0411 0.0512  -0.1253 42  LEU B CA  
5015 C C   . LEU B 45  ? 0.3363 0.4363 0.2762 -0.0465 0.0555  -0.1234 42  LEU B C   
5016 O O   . LEU B 45  ? 0.3123 0.4220 0.2377 -0.0551 0.0518  -0.1105 42  LEU B O   
5017 C CB  . LEU B 45  ? 0.2893 0.3485 0.2415 -0.0367 0.0438  -0.1065 42  LEU B CB  
5018 C CG  . LEU B 45  ? 0.3006 0.3395 0.2577 -0.0345 0.0393  -0.1051 42  LEU B CG  
5019 C CD1 . LEU B 45  ? 0.3246 0.3501 0.2869 -0.0292 0.0335  -0.0885 42  LEU B CD1 
5020 C CD2 . LEU B 45  ? 0.3301 0.3793 0.2755 -0.0447 0.0355  -0.1078 42  LEU B CD2 
5032 N N   . LYS B 46  ? 0.3188 0.4287 0.2683 -0.0414 0.0635  -0.1354 43  LYS B N   
5033 C CA  . LYS B 46  ? 0.3568 0.4887 0.3036 -0.0461 0.0683  -0.1319 43  LYS B CA  
5034 C C   . LYS B 46  ? 0.3663 0.5230 0.2932 -0.0600 0.0722  -0.1343 43  LYS B C   
5035 O O   . LYS B 46  ? 0.3585 0.5315 0.2786 -0.0676 0.0757  -0.1264 43  LYS B O   
5036 C CB  . LYS B 46  ? 0.3368 0.4765 0.3019 -0.0357 0.0756  -0.1461 43  LYS B CB  
5037 C CG  . LYS B 46  ? 0.3698 0.5153 0.3397 -0.0325 0.0810  -0.1653 43  LYS B CG  
5038 C CD  . LYS B 46  ? 0.5098 0.6653 0.4989 -0.0219 0.0855  -0.1741 43  LYS B CD  
5039 C CE  . LYS B 46  ? 0.4677 0.6159 0.4658 -0.0144 0.0877  -0.1894 43  LYS B CE  
5040 N NZ  . LYS B 46  ? 0.6546 0.8067 0.6725 -0.0001 0.0903  -0.1964 43  LYS B NZ  
5054 N N   . ASP B 47  ? 0.4004 0.5612 0.3172 -0.0643 0.0719  -0.1448 44  ASP B N   
5055 C CA  . ASP B 47  ? 0.4005 0.5827 0.2995 -0.0761 0.0719  -0.1412 44  ASP B CA  
5056 C C   . ASP B 47  ? 0.3689 0.5500 0.2461 -0.0845 0.0642  -0.1220 44  ASP B C   
5057 O O   . ASP B 47  ? 0.4092 0.6069 0.2697 -0.0936 0.0632  -0.1145 44  ASP B O   
5058 C CB  . ASP B 47  ? 0.4411 0.6280 0.3426 -0.0764 0.0722  -0.1575 44  ASP B CB  
5059 C CG  . ASP B 47  ? 0.6169 0.8027 0.5393 -0.0672 0.0792  -0.1756 44  ASP B CG  
5060 O OD1 . ASP B 47  ? 0.7361 0.9054 0.6694 -0.0608 0.0786  -0.1873 44  ASP B OD1 
5061 O OD2 . ASP B 47  ? 0.6514 0.8518 0.5798 -0.0663 0.0851  -0.1773 44  ASP B OD2 
5066 N N   . HIS B 48  ? 0.3317 0.4892 0.2157 -0.0787 0.0558  -0.1092 45  HIS B N   
5067 C CA  . HIS B 48  ? 0.3648 0.5171 0.2349 -0.0827 0.0458  -0.0896 45  HIS B CA  
5068 C C   . HIS B 48  ? 0.3265 0.4624 0.2013 -0.0801 0.0419  -0.0692 45  HIS B C   
5069 O O   . HIS B 48  ? 0.3645 0.4990 0.2250 -0.0846 0.0360  -0.0512 45  HIS B O   
5070 C CB  . HIS B 48  ? 0.3208 0.4610 0.1953 -0.0787 0.0375  -0.0929 45  HIS B CB  
5071 C CG  . HIS B 48  ? 0.3695 0.5240 0.2397 -0.0828 0.0400  -0.1137 45  HIS B CG  
5072 N ND1 . HIS B 48  ? 0.4840 0.6326 0.3689 -0.0785 0.0471  -0.1350 45  HIS B ND1 
5073 C CD2 . HIS B 48  ? 0.4179 0.5916 0.2712 -0.0905 0.0357  -0.1167 45  HIS B CD2 
5074 C CE1 . HIS B 48  ? 0.4779 0.6375 0.3608 -0.0830 0.0469  -0.1478 45  HIS B CE1 
5075 N NE2 . HIS B 48  ? 0.4813 0.6575 0.3464 -0.0901 0.0400  -0.1371 45  HIS B NE2 
5083 N N   . PHE B 49  ? 0.2967 0.4199 0.1912 -0.0723 0.0447  -0.0717 46  PHE B N   
5084 C CA  . PHE B 49  ? 0.2973 0.4056 0.1984 -0.0698 0.0415  -0.0560 46  PHE B CA  
5085 C C   . PHE B 49  ? 0.3145 0.4299 0.2284 -0.0687 0.0495  -0.0618 46  PHE B C   
5086 O O   . PHE B 49  ? 0.2951 0.4195 0.2193 -0.0639 0.0556  -0.0786 46  PHE B O   
5087 C CB  . PHE B 49  ? 0.2867 0.3724 0.2013 -0.0597 0.0341  -0.0528 46  PHE B CB  
5088 C CG  . PHE B 49  ? 0.2929 0.3732 0.1996 -0.0600 0.0258  -0.0475 46  PHE B CG  
5089 C CD1 . PHE B 49  ? 0.3573 0.4304 0.2564 -0.0612 0.0183  -0.0297 46  PHE B CD1 
5090 C CD2 . PHE B 49  ? 0.3107 0.3928 0.2195 -0.0586 0.0253  -0.0608 46  PHE B CD2 
5091 C CE1 . PHE B 49  ? 0.4016 0.4732 0.2958 -0.0599 0.0096  -0.0252 46  PHE B CE1 
5092 C CE2 . PHE B 49  ? 0.3581 0.4394 0.2617 -0.0596 0.0173  -0.0571 46  PHE B CE2 
5093 C CZ  . PHE B 49  ? 0.3719 0.4497 0.2686 -0.0596 0.0091  -0.0393 46  PHE B CZ  
5103 N N   . THR B 50  ? 0.2986 0.4096 0.2131 -0.0728 0.0492  -0.0488 47  THR B N   
5104 C CA  . THR B 50  ? 0.2918 0.4066 0.2235 -0.0697 0.0539  -0.0535 47  THR B CA  
5105 C C   . THR B 50  ? 0.2970 0.3920 0.2439 -0.0569 0.0471  -0.0530 47  THR B C   
5106 O O   . THR B 50  ? 0.3074 0.3858 0.2538 -0.0563 0.0406  -0.0403 47  THR B O   
5107 C CB  . THR B 50  ? 0.3081 0.4251 0.2352 -0.0808 0.0566  -0.0412 47  THR B CB  
5108 O OG1 . THR B 50  ? 0.3225 0.4590 0.2338 -0.0935 0.0642  -0.0410 47  THR B OG1 
5109 C CG2 . THR B 50  ? 0.3418 0.4657 0.2888 -0.0779 0.0604  -0.0480 47  THR B CG2 
5117 N N   . VAL B 51  ? 0.2578 0.3532 0.2170 -0.0463 0.0486  -0.0662 48  VAL B N   
5118 C CA  . VAL B 51  ? 0.2581 0.3346 0.2289 -0.0344 0.0428  -0.0648 48  VAL B CA  
5119 C C   . VAL B 51  ? 0.2655 0.3457 0.2503 -0.0296 0.0430  -0.0640 48  VAL B C   
5120 O O   . VAL B 51  ? 0.2577 0.3560 0.2520 -0.0276 0.0487  -0.0740 48  VAL B O   
5121 C CB  . VAL B 51  ? 0.2529 0.3242 0.2297 -0.0250 0.0444  -0.0777 48  VAL B CB  
5122 C CG1 . VAL B 51  ? 0.2941 0.3450 0.2800 -0.0143 0.0390  -0.0732 48  VAL B CG1 
5123 C CG2 . VAL B 51  ? 0.2937 0.3657 0.2577 -0.0316 0.0446  -0.0817 48  VAL B CG2 
5133 N N   . VAL B 52  ? 0.2333 0.2984 0.2206 -0.0269 0.0366  -0.0539 49  VAL B N   
5134 C CA  . VAL B 52  ? 0.2280 0.2966 0.2275 -0.0231 0.0353  -0.0531 49  VAL B CA  
5135 C C   . VAL B 52  ? 0.2692 0.3227 0.2752 -0.0102 0.0297  -0.0519 49  VAL B C   
5136 O O   . VAL B 52  ? 0.2786 0.3151 0.2789 -0.0100 0.0248  -0.0439 49  VAL B O   
5137 C CB  . VAL B 52  ? 0.2572 0.3218 0.2522 -0.0338 0.0336  -0.0425 49  VAL B CB  
5138 C CG1 . VAL B 52  ? 0.2424 0.3089 0.2499 -0.0302 0.0312  -0.0432 49  VAL B CG1 
5139 C CG2 . VAL B 52  ? 0.2734 0.3524 0.2606 -0.0477 0.0404  -0.0420 49  VAL B CG2 
5149 N N   . ALA B 53  ? 0.2159 0.2764 0.2333 0.0009  0.0306  -0.0594 50  ALA B N   
5150 C CA  . ALA B 53  ? 0.2155 0.2620 0.2372 0.0139  0.0260  -0.0571 50  ALA B CA  
5151 C C   . ALA B 53  ? 0.2141 0.2712 0.2457 0.0197  0.0229  -0.0569 50  ALA B C   
5152 O O   . ALA B 53  ? 0.2337 0.3107 0.2755 0.0244  0.0250  -0.0649 50  ALA B O   
5153 C CB  . ALA B 53  ? 0.2425 0.2845 0.2678 0.0244  0.0289  -0.0649 50  ALA B CB  
5159 N N   . VAL B 54  ? 0.2124 0.2593 0.2416 0.0192  0.0177  -0.0490 51  VAL B N   
5160 C CA  . VAL B 54  ? 0.2092 0.2683 0.2460 0.0203  0.0145  -0.0496 51  VAL B CA  
5161 C C   . VAL B 54  ? 0.2246 0.2852 0.2663 0.0359  0.0105  -0.0499 51  VAL B C   
5162 O O   . VAL B 54  ? 0.2418 0.2841 0.2773 0.0428  0.0089  -0.0442 51  VAL B O   
5163 C CB  . VAL B 54  ? 0.2739 0.3210 0.3054 0.0119  0.0114  -0.0424 51  VAL B CB  
5164 C CG1 . VAL B 54  ? 0.3153 0.3740 0.3546 0.0117  0.0083  -0.0452 51  VAL B CG1 
5165 C CG2 . VAL B 54  ? 0.3338 0.3776 0.3589 -0.0021 0.0147  -0.0396 51  VAL B CG2 
5175 N N   . ASP B 55  ? 0.2022 0.2854 0.2543 0.0408  0.0087  -0.0559 52  ASP B N   
5176 C CA  . ASP B 55  ? 0.1704 0.2584 0.2249 0.0537  0.0027  -0.0540 52  ASP B CA  
5177 C C   . ASP B 55  ? 0.1911 0.2786 0.2433 0.0458  -0.0009 -0.0518 52  ASP B C   
5178 O O   . ASP B 55  ? 0.2097 0.3133 0.2691 0.0362  -0.0004 -0.0579 52  ASP B O   
5179 C CB  . ASP B 55  ? 0.1901 0.3074 0.2578 0.0631  0.0012  -0.0627 52  ASP B CB  
5180 C CG  . ASP B 55  ? 0.2053 0.3217 0.2767 0.0770  0.0033  -0.0651 52  ASP B CG  
5181 O OD1 . ASP B 55  ? 0.2379 0.3316 0.3020 0.0761  0.0074  -0.0622 52  ASP B OD1 
5182 O OD2 . ASP B 55  ? 0.2281 0.3683 0.3112 0.0890  0.0010  -0.0716 52  ASP B OD2 
5187 N N   . ARG B 56  ? 0.1951 0.2642 0.2383 0.0485  -0.0035 -0.0440 53  ARG B N   
5188 C CA  . ARG B 56  ? 0.1822 0.2521 0.2246 0.0422  -0.0065 -0.0441 53  ARG B CA  
5189 C C   . ARG B 56  ? 0.1611 0.2577 0.2118 0.0467  -0.0108 -0.0517 53  ARG B C   
5190 O O   . ARG B 56  ? 0.2004 0.3130 0.2554 0.0584  -0.0130 -0.0538 53  ARG B O   
5191 C CB  . ARG B 56  ? 0.2017 0.2518 0.2340 0.0456  -0.0080 -0.0359 53  ARG B CB  
5192 C CG  . ARG B 56  ? 0.2085 0.2374 0.2349 0.0382  -0.0046 -0.0307 53  ARG B CG  
5193 C CD  . ARG B 56  ? 0.2070 0.2210 0.2269 0.0379  -0.0058 -0.0250 53  ARG B CD  
5194 N NE  . ARG B 56  ? 0.2328 0.2390 0.2467 0.0470  -0.0053 -0.0195 53  ARG B NE  
5195 C CZ  . ARG B 56  ? 0.2225 0.2312 0.2321 0.0542  -0.0074 -0.0164 53  ARG B CZ  
5196 N NH1 . ARG B 56  ? 0.2183 0.2387 0.2293 0.0535  -0.0105 -0.0203 53  ARG B NH1 
5197 N NH2 . ARG B 56  ? 0.2627 0.2612 0.2657 0.0615  -0.0058 -0.0096 53  ARG B NH2 
5211 N N   . ARG B 57  ? 0.1840 0.2866 0.2382 0.0370  -0.0120 -0.0570 54  ARG B N   
5212 C CA  . ARG B 57  ? 0.1972 0.3300 0.2631 0.0354  -0.0146 -0.0683 54  ARG B CA  
5213 C C   . ARG B 57  ? 0.1953 0.3477 0.2607 0.0509  -0.0213 -0.0694 54  ARG B C   
5214 O O   . ARG B 57  ? 0.2037 0.3867 0.2799 0.0542  -0.0243 -0.0783 54  ARG B O   
5215 C CB  . ARG B 57  ? 0.1899 0.3223 0.2602 0.0204  -0.0139 -0.0752 54  ARG B CB  
5216 C CG  . ARG B 57  ? 0.2121 0.3291 0.2744 0.0216  -0.0167 -0.0727 54  ARG B CG  
5217 C CD  . ARG B 57  ? 0.1974 0.3203 0.2673 0.0096  -0.0169 -0.0837 54  ARG B CD  
5218 N NE  . ARG B 57  ? 0.2285 0.3375 0.3033 -0.0063 -0.0112 -0.0844 54  ARG B NE  
5219 C CZ  . ARG B 57  ? 0.2239 0.3375 0.3080 -0.0198 -0.0095 -0.0947 54  ARG B CZ  
5220 N NH1 . ARG B 57  ? 0.2104 0.3433 0.3008 -0.0198 -0.0133 -0.1072 54  ARG B NH1 
5221 N NH2 . ARG B 57  ? 0.2383 0.3364 0.3248 -0.0342 -0.0036 -0.0925 54  ARG B NH2 
5235 N N   . ASP B 58  ? 0.2079 0.3457 0.2610 0.0604  -0.0238 -0.0603 55  ASP B N   
5236 C CA  . ASP B 58  ? 0.2050 0.3595 0.2541 0.0756  -0.0302 -0.0584 55  ASP B CA  
5237 C C   . ASP B 58  ? 0.1993 0.3522 0.2468 0.0914  -0.0309 -0.0510 55  ASP B C   
5238 O O   . ASP B 58  ? 0.2456 0.4089 0.2877 0.1065  -0.0365 -0.0462 55  ASP B O   
5239 C CB  . ASP B 58  ? 0.2116 0.3528 0.2468 0.0777  -0.0317 -0.0518 55  ASP B CB  
5240 C CG  . ASP B 58  ? 0.2331 0.3824 0.2715 0.0661  -0.0327 -0.0622 55  ASP B CG  
5241 O OD1 . ASP B 58  ? 0.2808 0.4589 0.3239 0.0679  -0.0378 -0.0718 55  ASP B OD1 
5242 O OD2 . ASP B 58  ? 0.2371 0.3650 0.2734 0.0564  -0.0287 -0.0612 55  ASP B OD2 
5247 N N   . TYR B 59  ? 0.2066 0.3475 0.2586 0.0889  -0.0254 -0.0505 56  TYR B N   
5248 C CA  . TYR B 59  ? 0.2098 0.3424 0.2603 0.1037  -0.0249 -0.0442 56  TYR B CA  
5249 C C   . TYR B 59  ? 0.2488 0.3957 0.3132 0.1047  -0.0218 -0.0529 56  TYR B C   
5250 O O   . TYR B 59  ? 0.2160 0.3708 0.2883 0.0901  -0.0174 -0.0612 56  TYR B O   
5251 C CB  . TYR B 59  ? 0.2225 0.3182 0.2613 0.1010  -0.0196 -0.0341 56  TYR B CB  
5252 C CG  . TYR B 59  ? 0.1927 0.2717 0.2178 0.0992  -0.0205 -0.0251 56  TYR B CG  
5253 C CD1 . TYR B 59  ? 0.2515 0.3234 0.2660 0.1126  -0.0232 -0.0147 56  TYR B CD1 
5254 C CD2 . TYR B 59  ? 0.2209 0.2915 0.2437 0.0849  -0.0184 -0.0266 56  TYR B CD2 
5255 C CE1 . TYR B 59  ? 0.2805 0.3391 0.2821 0.1099  -0.0226 -0.0067 56  TYR B CE1 
5256 C CE2 . TYR B 59  ? 0.2421 0.3006 0.2541 0.0839  -0.0185 -0.0200 56  TYR B CE2 
5257 C CZ  . TYR B 59  ? 0.2720 0.3257 0.2736 0.0956  -0.0201 -0.0105 56  TYR B CZ  
5258 O OH  . TYR B 59  ? 0.2781 0.3228 0.2686 0.0936  -0.0191 -0.0043 56  TYR B OH  
5268 N N   . GLY B 60  ? 0.2521 0.3997 0.3188 0.1223  -0.0233 -0.0501 57  GLY B N   
5269 C CA  . GLY B 60  ? 0.2524 0.4076 0.3311 0.1250  -0.0187 -0.0580 57  GLY B CA  
5270 C C   . GLY B 60  ? 0.2119 0.4078 0.3081 0.1202  -0.0195 -0.0724 57  GLY B C   
5271 O O   . GLY B 60  ? 0.2366 0.4574 0.3368 0.1246  -0.0263 -0.0753 57  GLY B O   
5275 N N   . GLU B 61  ? 0.1943 0.3951 0.2979 0.1071  -0.0120 -0.0809 58  GLU B N   
5276 C CA  . GLU B 61  ? 0.2029 0.4426 0.3238 0.0995  -0.0105 -0.0949 58  GLU B CA  
5277 C C   . GLU B 61  ? 0.1595 0.4055 0.2801 0.0779  -0.0094 -0.0983 58  GLU B C   
5278 O O   . GLU B 61  ? 0.1658 0.4450 0.3012 0.0694  -0.0082 -0.1102 58  GLU B O   
5279 C CB  . GLU B 61  ? 0.1805 0.4251 0.3091 0.0953  -0.0016 -0.1028 58  GLU B CB  
5280 C CG  . GLU B 61  ? 0.2102 0.4451 0.3383 0.1129  -0.0026 -0.1008 58  GLU B CG  
5281 C CD  . GLU B 61  ? 0.3496 0.6057 0.4839 0.1255  -0.0105 -0.1021 58  GLU B CD  
5282 O OE1 . GLU B 61  ? 0.3157 0.6050 0.4616 0.1176  -0.0105 -0.1130 58  GLU B OE1 
5283 O OE2 . GLU B 61  ? 0.5320 0.7716 0.6591 0.1423  -0.0162 -0.0922 58  GLU B OE2 
5290 N N   . SER B 62  ? 0.1920 0.4083 0.2979 0.0693  -0.0096 -0.0889 59  SER B N   
5291 C CA  . SER B 62  ? 0.1837 0.4032 0.2897 0.0527  -0.0100 -0.0921 59  SER B CA  
5292 C C   . SER B 62  ? 0.1920 0.4391 0.3046 0.0605  -0.0184 -0.0980 59  SER B C   
5293 O O   . SER B 62  ? 0.2192 0.4765 0.3314 0.0799  -0.0248 -0.0953 59  SER B O   
5294 C CB  . SER B 62  ? 0.1863 0.3687 0.2764 0.0453  -0.0089 -0.0813 59  SER B CB  
5295 O OG  . SER B 62  ? 0.1862 0.3500 0.2715 0.0360  -0.0017 -0.0778 59  SER B OG  
5301 N N   . GLU B 63  ? 0.1677 0.4297 0.2873 0.0451  -0.0183 -0.1071 60  GLU B N   
5302 C CA  . GLU B 63  ? 0.1789 0.4708 0.3049 0.0505  -0.0265 -0.1153 60  GLU B CA  
5303 C C   . GLU B 63  ? 0.2217 0.5068 0.3462 0.0332  -0.0260 -0.1206 60  GLU B C   
5304 O O   . GLU B 63  ? 0.2129 0.4855 0.3405 0.0141  -0.0187 -0.1233 60  GLU B O   
5305 C CB  . GLU B 63  ? 0.2429 0.5784 0.3872 0.0525  -0.0279 -0.1287 60  GLU B CB  
5306 C CG  . GLU B 63  ? 0.2261 0.5752 0.3840 0.0298  -0.0198 -0.1405 60  GLU B CG  
5307 C CD  . GLU B 63  ? 0.2518 0.6303 0.4181 0.0317  -0.0194 -0.1503 60  GLU B CD  
5308 O OE1 . GLU B 63  ? 0.2105 0.5902 0.3798 0.0371  -0.0152 -0.1488 60  GLU B OE1 
5309 O OE2 . GLU B 63  ? 0.2696 0.6705 0.4395 0.0285  -0.0231 -0.1603 60  GLU B OE2 
5316 N N   . LEU B 64  ? 0.1905 0.4814 0.3087 0.0404  -0.0334 -0.1212 61  LEU B N   
5317 C CA  . LEU B 64  ? 0.1935 0.4853 0.3137 0.0254  -0.0336 -0.1309 61  LEU B CA  
5318 C C   . LEU B 64  ? 0.2323 0.5651 0.3722 0.0148  -0.0345 -0.1496 61  LEU B C   
5319 O O   . LEU B 64  ? 0.2496 0.6074 0.3915 0.0258  -0.0374 -0.1524 61  LEU B O   
5320 C CB  . LEU B 64  ? 0.1948 0.4849 0.3020 0.0364  -0.0408 -0.1278 61  LEU B CB  
5321 C CG  . LEU B 64  ? 0.2023 0.4562 0.2907 0.0464  -0.0399 -0.1103 61  LEU B CG  
5322 C CD1 . LEU B 64  ? 0.2628 0.5194 0.3390 0.0526  -0.0455 -0.1103 61  LEU B CD1 
5323 C CD2 . LEU B 64  ? 0.2061 0.4221 0.2910 0.0335  -0.0318 -0.1042 61  LEU B CD2 
5335 N N   . THR B 65  ? 0.1969 0.5227 0.3437 -0.0068 -0.0292 -0.1593 62  THR B N   
5336 C CA  . THR B 65  ? 0.2157 0.5639 0.3725 -0.0188 -0.0260 -0.1738 62  THR B CA  
5337 C C   . THR B 65  ? 0.2385 0.5889 0.3919 -0.0225 -0.0289 -0.1833 62  THR B C   
5338 O O   . THR B 65  ? 0.2856 0.6557 0.4468 -0.0310 -0.0266 -0.1963 62  THR B O   
5339 C CB  . THR B 65  ? 0.2297 0.5667 0.3962 -0.0416 -0.0151 -0.1772 62  THR B CB  
5340 O OG1 . THR B 65  ? 0.2937 0.5942 0.4558 -0.0546 -0.0117 -0.1730 62  THR B OG1 
5341 C CG2 . THR B 65  ? 0.2421 0.5835 0.4121 -0.0382 -0.0109 -0.1700 62  THR B CG2 
5349 N N   . GLU B 66  ? 0.2647 0.5960 0.4069 -0.0164 -0.0333 -0.1779 63  GLU B N   
5350 C CA  . GLU B 66  ? 0.3147 0.6471 0.4514 -0.0170 -0.0360 -0.1861 63  GLU B CA  
5351 C C   . GLU B 66  ? 0.2694 0.5982 0.3896 0.0024  -0.0438 -0.1751 63  GLU B C   
5352 O O   . GLU B 66  ? 0.2665 0.5770 0.3807 0.0095  -0.0449 -0.1618 63  GLU B O   
5353 C CB  . GLU B 66  ? 0.3953 0.6956 0.5348 -0.0355 -0.0297 -0.1913 63  GLU B CB  
5354 C CG  . GLU B 66  ? 0.6218 0.9149 0.7747 -0.0567 -0.0203 -0.1980 63  GLU B CG  
5355 C CD  . GLU B 66  ? 0.9000 1.2171 1.0622 -0.0651 -0.0181 -0.2142 63  GLU B CD  
5356 O OE1 . GLU B 66  ? 0.8707 1.1945 1.0295 -0.0611 -0.0216 -0.2222 63  GLU B OE1 
5357 O OE2 . GLU B 66  ? 0.9217 1.2520 1.0945 -0.0761 -0.0125 -0.2197 63  GLU B OE2 
5364 N N   . PRO B 67  ? 0.2959 0.6410 0.4080 0.0104  -0.0482 -0.1796 64  PRO B N   
5365 C CA  . PRO B 67  ? 0.3006 0.6416 0.3942 0.0280  -0.0543 -0.1674 64  PRO B CA  
5366 C C   . PRO B 67  ? 0.2979 0.6062 0.3841 0.0239  -0.0528 -0.1629 64  PRO B C   
5367 O O   . PRO B 67  ? 0.2870 0.5767 0.3804 0.0081  -0.0477 -0.1723 64  PRO B O   
5368 C CB  . PRO B 67  ? 0.3597 0.7271 0.4481 0.0324  -0.0573 -0.1765 64  PRO B CB  
5369 C CG  . PRO B 67  ? 0.3914 0.7839 0.4959 0.0236  -0.0550 -0.1901 64  PRO B CG  
5370 C CD  . PRO B 67  ? 0.3823 0.7514 0.5006 0.0038  -0.0474 -0.1956 64  PRO B CD  
5378 N N   . LEU B 68  ? 0.3304 0.6244 0.4001 0.0386  -0.0547 -0.1459 65  LEU B N   
5379 C CA  . LEU B 68  ? 0.3031 0.5629 0.3618 0.0369  -0.0499 -0.1390 65  LEU B CA  
5380 C C   . LEU B 68  ? 0.2896 0.5609 0.3467 0.0313  -0.0515 -0.1552 65  LEU B C   
5381 O O   . LEU B 68  ? 0.3250 0.6283 0.3805 0.0356  -0.0560 -0.1632 65  LEU B O   
5382 C CB  . LEU B 68  ? 0.3497 0.5968 0.3900 0.0528  -0.0507 -0.1192 65  LEU B CB  
5383 C CG  . LEU B 68  ? 0.3687 0.5944 0.4070 0.0592  -0.0477 -0.1020 65  LEU B CG  
5384 C CD1 . LEU B 68  ? 0.3197 0.5366 0.3393 0.0738  -0.0489 -0.0854 65  LEU B CD1 
5385 C CD2 . LEU B 68  ? 0.3167 0.5084 0.3606 0.0470  -0.0401 -0.0997 65  LEU B CD2 
5397 N N   . PRO B 69  ? 0.2996 0.5422 0.3561 0.0237  -0.0460 -0.1576 66  PRO B N   
5398 C CA  . PRO B 69  ? 0.3498 0.6030 0.4028 0.0214  -0.0470 -0.1729 66  PRO B CA  
5399 C C   . PRO B 69  ? 0.3204 0.5924 0.3536 0.0365  -0.0515 -0.1649 66  PRO B C   
5400 O O   . PRO B 69  ? 0.3852 0.6453 0.4063 0.0475  -0.0510 -0.1446 66  PRO B O   
5401 C CB  . PRO B 69  ? 0.4423 0.6563 0.4985 0.0143  -0.0398 -0.1726 66  PRO B CB  
5402 C CG  . PRO B 69  ? 0.4386 0.6237 0.4945 0.0159  -0.0361 -0.1532 66  PRO B CG  
5403 C CD  . PRO B 69  ? 0.3554 0.5577 0.4164 0.0165  -0.0388 -0.1490 66  PRO B CD  
5411 N N   . ASP B 70  ? 0.3532 0.6475 0.3856 0.0365  -0.0515 -0.1747 67  ASP B N   
5412 C CA  . ASP B 70  ? 0.4073 0.7187 0.4203 0.0494  -0.0542 -0.1655 67  ASP B CA  
5413 C C   . ASP B 70  ? 0.3832 0.6712 0.3815 0.0534  -0.0508 -0.1562 67  ASP B C   
5414 O O   . ASP B 70  ? 0.4193 0.7103 0.3984 0.0648  -0.0522 -0.1401 67  ASP B O   
5415 C CB  . ASP B 70  ? 0.4877 0.8260 0.5032 0.0466  -0.0540 -0.1799 67  ASP B CB  
5416 C CG  . ASP B 70  ? 0.5895 0.9575 0.6153 0.0457  -0.0575 -0.1875 67  ASP B CG  
5417 O OD1 . ASP B 70  ? 0.5532 0.9285 0.5769 0.0538  -0.0614 -0.1764 67  ASP B OD1 
5418 O OD2 . ASP B 70  ? 0.7067 1.0914 0.7430 0.0375  -0.0561 -0.2050 67  ASP B OD2 
5423 N N   . SER B 71  ? 0.3518 0.6140 0.3589 0.0442  -0.0454 -0.1651 68  SER B N   
5424 C CA  . SER B 71  ? 0.3642 0.6045 0.3622 0.0473  -0.0398 -0.1574 68  SER B CA  
5425 C C   . SER B 71  ? 0.3359 0.5502 0.3294 0.0527  -0.0370 -0.1333 68  SER B C   
5426 O O   . SER B 71  ? 0.3296 0.5275 0.3162 0.0553  -0.0319 -0.1240 68  SER B O   
5427 C CB  . SER B 71  ? 0.4349 0.6534 0.4481 0.0374  -0.0345 -0.1727 68  SER B CB  
5428 O OG  . SER B 71  ? 0.4984 0.6927 0.5274 0.0294  -0.0332 -0.1709 68  SER B OG  
5434 N N   . ALA B 72  ? 0.3105 0.5221 0.3091 0.0537  -0.0397 -0.1245 69  ALA B N   
5435 C CA  . ALA B 72  ? 0.2755 0.4616 0.2707 0.0579  -0.0366 -0.1043 69  ALA B CA  
5436 C C   . ALA B 72  ? 0.2862 0.4756 0.2616 0.0690  -0.0363 -0.0878 69  ALA B C   
5437 O O   . ALA B 72  ? 0.2977 0.4632 0.2692 0.0706  -0.0317 -0.0731 69  ALA B O   
5438 C CB  . ALA B 72  ? 0.2888 0.4735 0.2937 0.0572  -0.0389 -0.1000 69  ALA B CB  
5444 N N   A SER B 73  ? 0.2974 0.5159 0.2599 0.0759  -0.0411 -0.0896 70  SER B N   
5445 N N   B SER B 73  ? 0.2979 0.5164 0.2605 0.0759  -0.0411 -0.0896 70  SER B N   
5446 C CA  A SER B 73  ? 0.3422 0.5624 0.2833 0.0856  -0.0401 -0.0726 70  SER B CA  
5447 C CA  B SER B 73  ? 0.3424 0.5624 0.2836 0.0856  -0.0400 -0.0726 70  SER B CA  
5448 C C   A SER B 73  ? 0.3460 0.5586 0.2791 0.0820  -0.0329 -0.0731 70  SER B C   
5449 C C   B SER B 73  ? 0.3489 0.5568 0.2838 0.0814  -0.0322 -0.0721 70  SER B C   
5450 O O   A SER B 73  ? 0.3799 0.5887 0.2957 0.0872  -0.0295 -0.0574 70  SER B O   
5451 O O   B SER B 73  ? 0.3403 0.5356 0.2621 0.0851  -0.0277 -0.0552 70  SER B O   
5452 C CB  A SER B 73  ? 0.3246 0.5805 0.2521 0.0947  -0.0479 -0.0736 70  SER B CB  
5453 C CB  B SER B 73  ? 0.3231 0.5797 0.2503 0.0939  -0.0475 -0.0750 70  SER B CB  
5454 O OG  A SER B 73  ? 0.3771 0.6587 0.3105 0.0882  -0.0505 -0.0967 70  SER B OG  
5455 O OG  B SER B 73  ? 0.3467 0.6166 0.2801 0.1003  -0.0550 -0.0733 70  SER B OG  
5466 N N   . ASN B 74  ? 0.2945 0.5055 0.2401 0.0733  -0.0301 -0.0910 71  ASN B N   
5467 C CA  . ASN B 74  ? 0.3571 0.5627 0.2989 0.0707  -0.0230 -0.0936 71  ASN B CA  
5468 C C   . ASN B 74  ? 0.3227 0.4978 0.2673 0.0696  -0.0170 -0.0782 71  ASN B C   
5469 O O   . ASN B 74  ? 0.3212 0.4755 0.2800 0.0662  -0.0175 -0.0766 71  ASN B O   
5470 C CB  . ASN B 74  ? 0.3431 0.5505 0.3008 0.0633  -0.0219 -0.1172 71  ASN B CB  
5471 C CG  . ASN B 74  ? 0.5751 0.7906 0.5273 0.0630  -0.0158 -0.1252 71  ASN B CG  
5472 O OD1 . ASN B 74  ? 0.4908 0.6895 0.4448 0.0626  -0.0096 -0.1176 71  ASN B OD1 
5473 N ND2 . ASN B 74  ? 0.7683 1.0124 0.7145 0.0628  -0.0175 -0.1417 71  ASN B ND2 
5481 N N   . PRO B 75  ? 0.3103 0.4836 0.2419 0.0713  -0.0110 -0.0672 72  PRO B N   
5482 C CA  . PRO B 75  ? 0.3214 0.4680 0.2568 0.0690  -0.0055 -0.0537 72  PRO B CA  
5483 C C   . PRO B 75  ? 0.3444 0.4762 0.2994 0.0632  -0.0029 -0.0640 72  PRO B C   
5484 O O   . PRO B 75  ? 0.3491 0.4598 0.3107 0.0610  -0.0007 -0.0549 72  PRO B O   
5485 C CB  . PRO B 75  ? 0.4010 0.5541 0.3181 0.0701  0.0012  -0.0424 72  PRO B CB  
5486 C CG  . PRO B 75  ? 0.3797 0.5623 0.2878 0.0713  0.0008  -0.0556 72  PRO B CG  
5487 C CD  . PRO B 75  ? 0.3631 0.5596 0.2743 0.0745  -0.0086 -0.0652 72  PRO B CD  
5495 N N   . ASP B 76  ? 0.3161 0.4579 0.2806 0.0612  -0.0037 -0.0831 73  ASP B N   
5496 C CA  . ASP B 76  ? 0.3929 0.5197 0.3760 0.0578  -0.0020 -0.0930 73  ASP B CA  
5497 C C   . ASP B 76  ? 0.3790 0.4921 0.3763 0.0545  -0.0070 -0.0994 73  ASP B C   
5498 O O   . ASP B 76  ? 0.3558 0.4539 0.3679 0.0523  -0.0064 -0.1069 73  ASP B O   
5499 C CB  . ASP B 76  ? 0.4808 0.6236 0.4670 0.0582  0.0013  -0.1111 73  ASP B CB  
5500 C CG  . ASP B 76  ? 0.6899 0.8494 0.6624 0.0599  0.0078  -0.1062 73  ASP B CG  
5501 O OD1 . ASP B 76  ? 0.7622 0.9439 0.7300 0.0607  0.0101  -0.1203 73  ASP B OD1 
5502 O OD2 . ASP B 76  ? 0.7757 0.9262 0.7424 0.0594  0.0114  -0.0893 73  ASP B OD2 
5507 N N   . SER B 77  ? 0.3062 0.4243 0.2997 0.0543  -0.0118 -0.0962 74  SER B N   
5508 C CA  . SER B 77  ? 0.2653 0.3731 0.2720 0.0492  -0.0153 -0.1025 74  SER B CA  
5509 C C   . SER B 77  ? 0.2626 0.3443 0.2763 0.0470  -0.0142 -0.0905 74  SER B C   
5510 O O   . SER B 77  ? 0.2979 0.3739 0.3042 0.0497  -0.0129 -0.0756 74  SER B O   
5511 C CB  . SER B 77  ? 0.2770 0.4018 0.2788 0.0501  -0.0204 -0.1019 74  SER B CB  
5512 O OG  . SER B 77  ? 0.2881 0.4036 0.3029 0.0436  -0.0225 -0.1061 74  SER B OG  
5518 N N   . ASP B 78  ? 0.2595 0.3247 0.2867 0.0416  -0.0146 -0.0968 75  ASP B N   
5519 C CA  . ASP B 78  ? 0.2539 0.2980 0.2854 0.0390  -0.0145 -0.0849 75  ASP B CA  
5520 C C   . ASP B 78  ? 0.2374 0.2769 0.2755 0.0321  -0.0166 -0.0875 75  ASP B C   
5521 O O   . ASP B 78  ? 0.2397 0.2617 0.2816 0.0283  -0.0161 -0.0797 75  ASP B O   
5522 C CB  . ASP B 78  ? 0.3557 0.3815 0.3947 0.0396  -0.0128 -0.0835 75  ASP B CB  
5523 C CG  . ASP B 78  ? 0.3195 0.3348 0.3703 0.0370  -0.0131 -0.0963 75  ASP B CG  
5524 O OD1 . ASP B 78  ? 0.3969 0.4210 0.4508 0.0339  -0.0137 -0.1100 75  ASP B OD1 
5525 O OD2 . ASP B 78  ? 0.5014 0.4987 0.5593 0.0386  -0.0129 -0.0926 75  ASP B OD2 
5530 N N   . TYR B 79  ? 0.2588 0.3175 0.2970 0.0302  -0.0188 -0.0972 76  TYR B N   
5531 C CA  . TYR B 79  ? 0.2163 0.2763 0.2619 0.0225  -0.0201 -0.1009 76  TYR B CA  
5532 C C   . TYR B 79  ? 0.2410 0.2956 0.2835 0.0230  -0.0197 -0.0865 76  TYR B C   
5533 O O   . TYR B 79  ? 0.2252 0.2665 0.2738 0.0156  -0.0182 -0.0840 76  TYR B O   
5534 C CB  . TYR B 79  ? 0.2454 0.3346 0.2911 0.0219  -0.0233 -0.1135 76  TYR B CB  
5535 C CG  . TYR B 79  ? 0.2339 0.3299 0.2879 0.0143  -0.0242 -0.1160 76  TYR B CG  
5536 C CD1 . TYR B 79  ? 0.2929 0.3767 0.3592 0.0017  -0.0219 -0.1249 76  TYR B CD1 
5537 C CD2 . TYR B 79  ? 0.2313 0.3436 0.2812 0.0197  -0.0265 -0.1084 76  TYR B CD2 
5538 C CE1 . TYR B 79  ? 0.2936 0.3845 0.3678 -0.0072 -0.0211 -0.1269 76  TYR B CE1 
5539 C CE2 . TYR B 79  ? 0.2369 0.3578 0.2961 0.0127  -0.0264 -0.1114 76  TYR B CE2 
5540 C CZ  . TYR B 79  ? 0.2797 0.3915 0.3508 -0.0014 -0.0234 -0.1207 76  TYR B CZ  
5541 O OH  . TYR B 79  ? 0.2733 0.3960 0.3538 -0.0100 -0.0221 -0.1238 76  TYR B OH  
5551 N N   . ARG B 80  ? 0.2199 0.2849 0.2524 0.0315  -0.0207 -0.0776 77  ARG B N   
5552 C CA  . ARG B 80  ? 0.1890 0.2520 0.2201 0.0327  -0.0205 -0.0676 77  ARG B CA  
5553 C C   . ARG B 80  ? 0.2223 0.2614 0.2532 0.0300  -0.0174 -0.0576 77  ARG B C   
5554 O O   . ARG B 80  ? 0.2232 0.2573 0.2574 0.0253  -0.0163 -0.0544 77  ARG B O   
5555 C CB  . ARG B 80  ? 0.2035 0.2794 0.2241 0.0436  -0.0222 -0.0601 77  ARG B CB  
5556 C CG  . ARG B 80  ? 0.1992 0.3039 0.2200 0.0480  -0.0269 -0.0677 77  ARG B CG  
5557 C CD  . ARG B 80  ? 0.1862 0.2993 0.1971 0.0605  -0.0291 -0.0567 77  ARG B CD  
5558 N NE  . ARG B 80  ? 0.2075 0.3082 0.2215 0.0614  -0.0270 -0.0488 77  ARG B NE  
5559 C CZ  . ARG B 80  ? 0.2186 0.2995 0.2258 0.0651  -0.0237 -0.0369 77  ARG B CZ  
5560 N NH1 . ARG B 80  ? 0.2480 0.3183 0.2449 0.0675  -0.0216 -0.0297 77  ARG B NH1 
5561 N NH2 . ARG B 80  ? 0.2212 0.2930 0.2327 0.0648  -0.0216 -0.0333 77  ARG B NH2 
5575 N N   . VAL B 81  ? 0.2153 0.2431 0.2422 0.0329  -0.0160 -0.0528 78  VAL B N   
5576 C CA  . VAL B 81  ? 0.2097 0.2191 0.2364 0.0308  -0.0142 -0.0438 78  VAL B CA  
5577 C C   . VAL B 81  ? 0.2351 0.2313 0.2694 0.0229  -0.0142 -0.0462 78  VAL B C   
5578 O O   . VAL B 81  ? 0.2164 0.2031 0.2501 0.0189  -0.0133 -0.0394 78  VAL B O   
5579 C CB  . VAL B 81  ? 0.2066 0.2112 0.2293 0.0352  -0.0128 -0.0394 78  VAL B CB  
5580 C CG1 . VAL B 81  ? 0.2764 0.2794 0.3049 0.0353  -0.0131 -0.0475 78  VAL B CG1 
5581 C CG2 . VAL B 81  ? 0.2216 0.2131 0.2434 0.0334  -0.0115 -0.0303 78  VAL B CG2 
5591 N N   . LYS B 82  ? 0.2188 0.2137 0.2596 0.0202  -0.0149 -0.0558 79  LYS B N   
5592 C CA  . LYS B 82  ? 0.2450 0.2231 0.2925 0.0125  -0.0144 -0.0570 79  LYS B CA  
5593 C C   . LYS B 82  ? 0.2192 0.2015 0.2688 0.0037  -0.0130 -0.0576 79  LYS B C   
5594 O O   . LYS B 82  ? 0.2596 0.2278 0.3090 -0.0028 -0.0115 -0.0509 79  LYS B O   
5595 C CB  . LYS B 82  ? 0.2587 0.2324 0.3137 0.0118  -0.0147 -0.0690 79  LYS B CB  
5596 C CG  . LYS B 82  ? 0.2980 0.2663 0.3536 0.0201  -0.0152 -0.0693 79  LYS B CG  
5597 C CD  . LYS B 82  ? 0.3705 0.3228 0.4249 0.0224  -0.0159 -0.0569 79  LYS B CD  
5598 C CE  . LYS B 82  ? 0.4575 0.4041 0.5173 0.0301  -0.0167 -0.0596 79  LYS B CE  
5599 N NZ  . LYS B 82  ? 0.3740 0.3080 0.4335 0.0327  -0.0187 -0.0475 79  LYS B NZ  
5613 N N   . ARG B 83  ? 0.2189 0.2228 0.2699 0.0037  -0.0136 -0.0653 80  ARG B N   
5614 C CA  . ARG B 83  ? 0.2085 0.2225 0.2638 -0.0043 -0.0121 -0.0677 80  ARG B CA  
5615 C C   . ARG B 83  ? 0.1962 0.2103 0.2458 -0.0026 -0.0105 -0.0570 80  ARG B C   
5616 O O   . ARG B 83  ? 0.2259 0.2392 0.2778 -0.0113 -0.0075 -0.0555 80  ARG B O   
5617 C CB  . ARG B 83  ? 0.2119 0.2539 0.2711 -0.0023 -0.0144 -0.0793 80  ARG B CB  
5618 C CG  . ARG B 83  ? 0.2170 0.2762 0.2844 -0.0110 -0.0129 -0.0856 80  ARG B CG  
5619 C CD  . ARG B 83  ? 0.2713 0.3178 0.3474 -0.0270 -0.0090 -0.0913 80  ARG B CD  
5620 N NE  . ARG B 83  ? 0.2583 0.2869 0.3310 -0.0335 -0.0047 -0.0797 80  ARG B NE  
5621 C CZ  . ARG B 83  ? 0.3024 0.3219 0.3799 -0.0482 0.0001  -0.0804 80  ARG B CZ  
5622 N NH1 . ARG B 83  ? 0.3228 0.3439 0.4105 -0.0595 0.0018  -0.0927 80  ARG B NH1 
5623 N NH2 . ARG B 83  ? 0.2884 0.2975 0.3599 -0.0528 0.0037  -0.0688 80  ARG B NH2 
5637 N N   . ASP B 84  ? 0.1920 0.2079 0.2343 0.0076  -0.0118 -0.0505 81  ASP B N   
5638 C CA  . ASP B 84  ? 0.1959 0.2091 0.2331 0.0092  -0.0099 -0.0421 81  ASP B CA  
5639 C C   . ASP B 84  ? 0.2141 0.2081 0.2487 0.0024  -0.0082 -0.0349 81  ASP B C   
5640 O O   . ASP B 84  ? 0.2166 0.2103 0.2494 -0.0030 -0.0056 -0.0315 81  ASP B O   
5641 C CB  . ASP B 84  ? 0.2137 0.2269 0.2438 0.0200  -0.0109 -0.0366 81  ASP B CB  
5642 C CG  . ASP B 84  ? 0.2529 0.2839 0.2823 0.0285  -0.0123 -0.0388 81  ASP B CG  
5643 O OD1 . ASP B 84  ? 0.2229 0.2710 0.2586 0.0273  -0.0131 -0.0454 81  ASP B OD1 
5644 O OD2 . ASP B 84  ? 0.2321 0.2601 0.2546 0.0370  -0.0125 -0.0330 81  ASP B OD2 
5649 N N   . ALA B 85  ? 0.2319 0.2112 0.2658 0.0036  -0.0098 -0.0323 82  ALA B N   
5650 C CA  . ALA B 85  ? 0.2354 0.1974 0.2661 -0.0007 -0.0097 -0.0241 82  ALA B CA  
5651 C C   . ALA B 85  ? 0.2479 0.2030 0.2810 -0.0118 -0.0074 -0.0240 82  ALA B C   
5652 O O   . ALA B 85  ? 0.2433 0.1929 0.2706 -0.0174 -0.0056 -0.0165 82  ALA B O   
5653 C CB  . ALA B 85  ? 0.2399 0.1903 0.2720 0.0049  -0.0125 -0.0227 82  ALA B CB  
5659 N N   . GLN B 86  ? 0.2265 0.1830 0.2674 -0.0163 -0.0068 -0.0329 83  GLN B N   
5660 C CA  . GLN B 86  ? 0.2236 0.1730 0.2674 -0.0292 -0.0032 -0.0334 83  GLN B CA  
5661 C C   . GLN B 86  ? 0.2576 0.2243 0.3001 -0.0356 0.0007  -0.0334 83  GLN B C   
5662 O O   . GLN B 86  ? 0.2606 0.2203 0.3000 -0.0463 0.0047  -0.0278 83  GLN B O   
5663 C CB  . GLN B 86  ? 0.2729 0.2226 0.3271 -0.0339 -0.0029 -0.0460 83  GLN B CB  
5664 C CG  . GLN B 86  ? 0.3184 0.2531 0.3762 -0.0489 0.0016  -0.0458 83  GLN B CG  
5665 C CD  . GLN B 86  ? 0.3584 0.2952 0.4281 -0.0556 0.0026  -0.0612 83  GLN B CD  
5666 O OE1 . GLN B 86  ? 0.4125 0.3597 0.4865 -0.0477 -0.0009 -0.0717 83  GLN B OE1 
5667 N NE2 . GLN B 86  ? 0.4725 0.4014 0.5471 -0.0715 0.0078  -0.0634 83  GLN B NE2 
5676 N N   . ASP B 87  ? 0.2292 0.2187 0.2740 -0.0290 -0.0001 -0.0394 84  ASP B N   
5677 C CA  . ASP B 87  ? 0.2351 0.2429 0.2805 -0.0327 0.0036  -0.0409 84  ASP B CA  
5678 C C   . ASP B 87  ? 0.2526 0.2516 0.2876 -0.0343 0.0058  -0.0304 84  ASP B C   
5679 O O   . ASP B 87  ? 0.2482 0.2530 0.2817 -0.0441 0.0109  -0.0293 84  ASP B O   
5680 C CB  . ASP B 87  ? 0.2247 0.2548 0.2734 -0.0211 0.0012  -0.0471 84  ASP B CB  
5681 C CG  . ASP B 87  ? 0.2680 0.3169 0.3266 -0.0204 -0.0011 -0.0588 84  ASP B CG  
5682 O OD1 . ASP B 87  ? 0.2687 0.3153 0.3336 -0.0310 0.0002  -0.0649 84  ASP B OD1 
5683 O OD2 . ASP B 87  ? 0.2585 0.3249 0.3183 -0.0091 -0.0042 -0.0622 84  ASP B OD2 
5688 N N   . ILE B 88  ? 0.2323 0.2199 0.2600 -0.0256 0.0025  -0.0236 85  ILE B N   
5689 C CA  . ILE B 88  ? 0.2185 0.2012 0.2362 -0.0269 0.0038  -0.0155 85  ILE B CA  
5690 C C   . ILE B 88  ? 0.2490 0.2164 0.2605 -0.0372 0.0052  -0.0068 85  ILE B C   
5691 O O   . ILE B 88  ? 0.2638 0.2344 0.2674 -0.0442 0.0089  -0.0021 85  ILE B O   
5692 C CB  . ILE B 88  ? 0.2235 0.1993 0.2366 -0.0165 -0.0002 -0.0117 85  ILE B CB  
5693 C CG1 . ILE B 88  ? 0.2342 0.2214 0.2511 -0.0070 -0.0006 -0.0178 85  ILE B CG1 
5694 C CG2 . ILE B 88  ? 0.2482 0.2203 0.2512 -0.0190 0.0004  -0.0047 85  ILE B CG2 
5695 C CD1 . ILE B 88  ? 0.2711 0.2721 0.2883 -0.0066 0.0031  -0.0219 85  ILE B CD1 
5707 N N   . ALA B 89  ? 0.2450 0.1948 0.2590 -0.0377 0.0026  -0.0041 86  ALA B N   
5708 C CA  . ALA B 89  ? 0.2689 0.1996 0.2767 -0.0465 0.0038  0.0060  86  ALA B CA  
5709 C C   . ALA B 89  ? 0.3035 0.2396 0.3121 -0.0614 0.0109  0.0045  86  ALA B C   
5710 O O   . ALA B 89  ? 0.3191 0.2486 0.3170 -0.0702 0.0142  0.0147  86  ALA B O   
5711 C CB  . ALA B 89  ? 0.3339 0.2434 0.3471 -0.0427 0.0000  0.0068  86  ALA B CB  
5717 N N   . GLU B 90  ? 0.3017 0.2518 0.3225 -0.0652 0.0135  -0.0080 87  GLU B N   
5718 C CA  . GLU B 90  ? 0.2938 0.2532 0.3178 -0.0809 0.0210  -0.0111 87  GLU B CA  
5719 C C   . GLU B 90  ? 0.2898 0.2714 0.3084 -0.0832 0.0254  -0.0112 87  GLU B C   
5720 O O   . GLU B 90  ? 0.3102 0.2947 0.3239 -0.0970 0.0324  -0.0071 87  GLU B O   
5721 C CB  . GLU B 90  ? 0.3143 0.2879 0.3544 -0.0844 0.0219  -0.0264 87  GLU B CB  
5722 C CG  . GLU B 90  ? 0.3998 0.3509 0.4447 -0.0823 0.0181  -0.0283 87  GLU B CG  
5723 C CD  . GLU B 90  ? 0.6617 0.6192 0.7206 -0.0926 0.0208  -0.0420 87  GLU B CD  
5724 O OE1 . GLU B 90  ? 0.8124 0.7543 0.8724 -0.1083 0.0265  -0.0397 87  GLU B OE1 
5725 O OE2 . GLU B 90  ? 0.5533 0.5306 0.6211 -0.0853 0.0171  -0.0549 87  GLU B OE2 
5732 N N   . LEU B 91  ? 0.2722 0.2688 0.2917 -0.0703 0.0222  -0.0160 88  LEU B N   
5733 C CA  . LEU B 91  ? 0.2547 0.2704 0.2697 -0.0705 0.0263  -0.0176 88  LEU B CA  
5734 C C   . LEU B 91  ? 0.3057 0.3095 0.3037 -0.0758 0.0279  -0.0049 88  LEU B C   
5735 O O   . LEU B 91  ? 0.2963 0.3114 0.2881 -0.0863 0.0347  -0.0036 88  LEU B O   
5736 C CB  . LEU B 91  ? 0.2447 0.2711 0.2636 -0.0546 0.0221  -0.0241 88  LEU B CB  
5737 C CG  . LEU B 91  ? 0.2722 0.3166 0.2886 -0.0520 0.0261  -0.0285 88  LEU B CG  
5738 C CD1 . LEU B 91  ? 0.2985 0.3686 0.3241 -0.0604 0.0332  -0.0378 88  LEU B CD1 
5739 C CD2 . LEU B 91  ? 0.2819 0.3289 0.3025 -0.0360 0.0217  -0.0333 88  LEU B CD2 
5751 N N   . ALA B 92  ? 0.2743 0.2573 0.2642 -0.0690 0.0215  0.0047  89  ALA B N   
5752 C CA  . ALA B 92  ? 0.3022 0.2761 0.2751 -0.0726 0.0212  0.0174  89  ALA B CA  
5753 C C   . ALA B 92  ? 0.3352 0.2997 0.3004 -0.0881 0.0269  0.0270  89  ALA B C   
5754 O O   . ALA B 92  ? 0.3515 0.3232 0.3031 -0.0965 0.0316  0.0332  89  ALA B O   
5755 C CB  . ALA B 92  ? 0.2953 0.2509 0.2641 -0.0619 0.0125  0.0253  89  ALA B CB  
5761 N N   . LYS B 93  ? 0.3173 0.2646 0.2899 -0.0928 0.0270  0.0285  90  LYS B N   
5762 C CA  . LYS B 93  ? 0.3433 0.2758 0.3085 -0.1087 0.0331  0.0389  90  LYS B CA  
5763 C C   . LYS B 93  ? 0.3447 0.3013 0.3122 -0.1238 0.0437  0.0318  90  LYS B C   
5764 O O   . LYS B 93  ? 0.3812 0.3337 0.3362 -0.1381 0.0506  0.0422  90  LYS B O   
5765 C CB  . LYS B 93  ? 0.3727 0.2799 0.3480 -0.1103 0.0313  0.0389  90  LYS B CB  
5766 C CG  . LYS B 93  ? 0.4542 0.3373 0.4266 -0.0957 0.0216  0.0471  90  LYS B CG  
5767 C CD  . LYS B 93  ? 0.5673 0.4189 0.5454 -0.0993 0.0214  0.0509  90  LYS B CD  
5768 C CE  . LYS B 93  ? 0.6612 0.5091 0.6551 -0.0875 0.0157  0.0384  90  LYS B CE  
5769 N NZ  . LYS B 93  ? 0.7568 0.5764 0.7487 -0.0759 0.0086  0.0478  90  LYS B NZ  
5783 N N   . SER B 94  ? 0.3436 0.3268 0.3270 -0.1205 0.0452  0.0145  91  SER B N   
5784 C CA  . SER B 94  ? 0.3455 0.3574 0.3345 -0.1330 0.0551  0.0053  91  SER B CA  
5785 C C   . SER B 94  ? 0.3204 0.3510 0.2963 -0.1337 0.0593  0.0072  91  SER B C   
5786 O O   . SER B 94  ? 0.3811 0.4311 0.3558 -0.1478 0.0692  0.0045  91  SER B O   
5787 C CB  . SER B 94  ? 0.3429 0.3794 0.3537 -0.1263 0.0538  -0.0136 91  SER B CB  
5788 O OG  . SER B 94  ? 0.3547 0.4091 0.3675 -0.1104 0.0500  -0.0210 91  SER B OG  
5794 N N   . LEU B 95  ? 0.3230 0.3498 0.2896 -0.1202 0.0527  0.0105  92  LEU B N   
5795 C CA  . LEU B 95  ? 0.3583 0.4051 0.3146 -0.1193 0.0561  0.0080  92  LEU B CA  
5796 C C   . LEU B 95  ? 0.4133 0.4471 0.3455 -0.1235 0.0550  0.0244  92  LEU B C   
5797 O O   . LEU B 95  ? 0.4213 0.4736 0.3419 -0.1277 0.0599  0.0228  92  LEU B O   
5798 C CB  . LEU B 95  ? 0.3238 0.3790 0.2877 -0.1013 0.0501  -0.0030 92  LEU B CB  
5799 C CG  . LEU B 95  ? 0.3373 0.4118 0.3225 -0.0941 0.0510  -0.0195 92  LEU B CG  
5800 C CD1 . LEU B 95  ? 0.4218 0.4952 0.4107 -0.0765 0.0446  -0.0255 92  LEU B CD1 
5801 C CD2 . LEU B 95  ? 0.4005 0.5060 0.3914 -0.1025 0.0611  -0.0302 92  LEU B CD2 
5813 N N   . SER B 96  ? 0.3910 0.3953 0.3154 -0.1220 0.0485  0.0396  93  SER B N   
5814 C CA  . SER B 96  ? 0.4125 0.4053 0.3145 -0.1212 0.0441  0.0557  93  SER B CA  
5815 C C   . SER B 96  ? 0.3855 0.3462 0.2796 -0.1260 0.0416  0.0743  93  SER B C   
5816 O O   . SER B 96  ? 0.4793 0.4209 0.3874 -0.1216 0.0380  0.0729  93  SER B O   
5817 C CB  . SER B 96  ? 0.3892 0.3819 0.2921 -0.1043 0.0340  0.0521  93  SER B CB  
5818 O OG  . SER B 96  ? 0.4622 0.4476 0.3453 -0.1024 0.0282  0.0664  93  SER B OG  
5824 N N   . ASP B 97  ? 0.4516 0.4057 0.3229 -0.1347 0.0437  0.0916  94  ASP B N   
5825 C CA  . ASP B 97  ? 0.5221 0.4413 0.3834 -0.1355 0.0394  0.1122  94  ASP B CA  
5826 C C   . ASP B 97  ? 0.5959 0.5038 0.4488 -0.1187 0.0261  0.1222  94  ASP B C   
5827 O O   . ASP B 97  ? 0.7097 0.5876 0.5580 -0.1146 0.0205  0.1379  94  ASP B O   
5828 C CB  . ASP B 97  ? 0.6615 0.5758 0.5010 -0.1536 0.0485  0.1292  94  ASP B CB  
5829 C CG  . ASP B 97  ? 0.7958 0.7268 0.6456 -0.1712 0.0625  0.1177  94  ASP B CG  
5830 O OD1 . ASP B 97  ? 0.8196 0.7419 0.6902 -0.1747 0.0650  0.1079  94  ASP B OD1 
5831 O OD2 . ASP B 97  ? 0.8145 0.7701 0.6545 -0.1792 0.0702  0.1158  94  ASP B OD2 
5836 N N   . GLU B 98  ? 0.5196 0.4507 0.3717 -0.1089 0.0210  0.1126  95  GLU B N   
5837 C CA  . GLU B 98  ? 0.4987 0.4251 0.3484 -0.0930 0.0083  0.1173  95  GLU B CA  
5838 C C   . GLU B 98  ? 0.4057 0.3334 0.2791 -0.0805 0.0037  0.1009  95  GLU B C   
5839 O O   . GLU B 98  ? 0.4091 0.3488 0.2971 -0.0828 0.0095  0.0847  95  GLU B O   
5840 C CB  . GLU B 98  ? 0.5208 0.4736 0.3535 -0.0922 0.0060  0.1164  95  GLU B CB  
5841 C CG  . GLU B 98  ? 0.6659 0.6196 0.4697 -0.1009 0.0070  0.1358  95  GLU B CG  
5842 C CD  . GLU B 98  ? 0.9534 0.8749 0.7483 -0.0963 0.0000  0.1594  95  GLU B CD  
5843 O OE1 . GLU B 98  ? 0.9396 0.8573 0.7327 -0.0819 -0.0124 0.1659  95  GLU B OE1 
5844 O OE2 . GLU B 98  ? 1.0429 0.9431 0.8344 -0.1066 0.0072  0.1702  95  GLU B OE2 
5851 N N   . PRO B 99  ? 0.4017 0.3188 0.2793 -0.0667 -0.0068 0.1049  96  PRO B N   
5852 C CA  . PRO B 99  ? 0.3601 0.2836 0.2570 -0.0557 -0.0106 0.0894  96  PRO B CA  
5853 C C   . PRO B 99  ? 0.3783 0.3291 0.2749 -0.0566 -0.0078 0.0753  96  PRO B C   
5854 O O   . PRO B 99  ? 0.3933 0.3590 0.2740 -0.0618 -0.0068 0.0781  96  PRO B O   
5855 C CB  . PRO B 99  ? 0.3864 0.3000 0.2839 -0.0423 -0.0220 0.0978  96  PRO B CB  
5856 C CG  . PRO B 99  ? 0.5169 0.4136 0.3975 -0.0443 -0.0250 0.1185  96  PRO B CG  
5857 C CD  . PRO B 99  ? 0.5110 0.4108 0.3761 -0.0603 -0.0155 0.1242  96  PRO B CD  
5865 N N   . VAL B 100 ? 0.3347 0.2912 0.2484 -0.0513 -0.0065 0.0602  97  VAL B N   
5866 C CA  . VAL B 100 ? 0.3077 0.2848 0.2241 -0.0523 -0.0020 0.0457  97  VAL B CA  
5867 C C   . VAL B 100 ? 0.2918 0.2730 0.2158 -0.0422 -0.0078 0.0381  97  VAL B C   
5868 O O   . VAL B 100 ? 0.2987 0.2701 0.2284 -0.0344 -0.0147 0.0425  97  VAL B O   
5869 C CB  . VAL B 100 ? 0.2683 0.2502 0.1973 -0.0555 0.0058  0.0343  97  VAL B CB  
5870 C CG1 . VAL B 100 ? 0.3197 0.2998 0.2435 -0.0682 0.0128  0.0403  97  VAL B CG1 
5871 C CG2 . VAL B 100 ? 0.3065 0.2781 0.2526 -0.0467 0.0027  0.0292  97  VAL B CG2 
5881 N N   . TYR B 101 ? 0.2667 0.2630 0.1916 -0.0430 -0.0041 0.0259  98  TYR B N   
5882 C CA  . TYR B 101 ? 0.2676 0.2667 0.2008 -0.0359 -0.0071 0.0171  98  TYR B CA  
5883 C C   . TYR B 101 ? 0.2553 0.2486 0.2038 -0.0307 -0.0037 0.0088  98  TYR B C   
5884 O O   . TYR B 101 ? 0.2433 0.2402 0.1952 -0.0331 0.0024  0.0037  98  TYR B O   
5885 C CB  . TYR B 101 ? 0.2488 0.2638 0.1748 -0.0398 -0.0045 0.0075  98  TYR B CB  
5886 C CG  . TYR B 101 ? 0.3279 0.3537 0.2367 -0.0447 -0.0087 0.0145  98  TYR B CG  
5887 C CD1 . TYR B 101 ? 0.3311 0.3638 0.2251 -0.0529 -0.0048 0.0204  98  TYR B CD1 
5888 C CD2 . TYR B 101 ? 0.2906 0.3218 0.1977 -0.0414 -0.0164 0.0154  98  TYR B CD2 
5889 C CE1 . TYR B 101 ? 0.3506 0.3945 0.2259 -0.0570 -0.0090 0.0281  98  TYR B CE1 
5890 C CE2 . TYR B 101 ? 0.3337 0.3782 0.2241 -0.0449 -0.0216 0.0218  98  TYR B CE2 
5891 C CZ  . TYR B 101 ? 0.3251 0.3753 0.1985 -0.0523 -0.0180 0.0290  98  TYR B CZ  
5892 O OH  . TYR B 101 ? 0.3809 0.4452 0.2349 -0.0553 -0.0236 0.0372  98  TYR B OH  
5902 N N   . ILE B 102 ? 0.2291 0.2158 0.1867 -0.0235 -0.0075 0.0075  99  ILE B N   
5903 C CA  . ILE B 102 ? 0.2158 0.1974 0.1853 -0.0180 -0.0050 0.0017  99  ILE B CA  
5904 C C   . ILE B 102 ? 0.2236 0.2047 0.1982 -0.0135 -0.0055 -0.0041 99  ILE B C   
5905 O O   . ILE B 102 ? 0.2200 0.2017 0.1945 -0.0127 -0.0101 -0.0017 99  ILE B O   
5906 C CB  . ILE B 102 ? 0.2117 0.1830 0.1874 -0.0146 -0.0080 0.0075  99  ILE B CB  
5907 C CG1 . ILE B 102 ? 0.2687 0.2371 0.2406 -0.0209 -0.0063 0.0128  99  ILE B CG1 
5908 C CG2 . ILE B 102 ? 0.2151 0.1845 0.2012 -0.0085 -0.0062 0.0014  99  ILE B CG2 
5909 C CD1 . ILE B 102 ? 0.2614 0.2169 0.2396 -0.0190 -0.0088 0.0173  99  ILE B CD1 
5921 N N   . LEU B 103 ? 0.2272 0.2074 0.2071 -0.0105 -0.0008 -0.0115 100 LEU B N   
5922 C CA  . LEU B 103 ? 0.2149 0.1900 0.1995 -0.0070 0.0001  -0.0157 100 LEU B CA  
5923 C C   . LEU B 103 ? 0.2324 0.2013 0.2236 0.0000  0.0023  -0.0160 100 LEU B C   
5924 O O   . LEU B 103 ? 0.2175 0.1891 0.2102 0.0022  0.0050  -0.0187 100 LEU B O   
5925 C CB  . LEU B 103 ? 0.2143 0.1918 0.1963 -0.0103 0.0041  -0.0242 100 LEU B CB  
5926 C CG  . LEU B 103 ? 0.2399 0.2089 0.2266 -0.0093 0.0062  -0.0286 100 LEU B CG  
5927 C CD1 . LEU B 103 ? 0.2538 0.2274 0.2373 -0.0161 0.0080  -0.0372 100 LEU B CD1 
5928 C CD2 . LEU B 103 ? 0.2839 0.2423 0.2751 -0.0023 0.0108  -0.0302 100 LEU B CD2 
5940 N N   . GLY B 104 ? 0.2156 0.1792 0.2106 0.0035  0.0007  -0.0133 101 GLY B N   
5941 C CA  . GLY B 104 ? 0.2121 0.1710 0.2107 0.0102  0.0025  -0.0128 101 GLY B CA  
5942 C C   . GLY B 104 ? 0.2299 0.1808 0.2290 0.0111  0.0055  -0.0134 101 GLY B C   
5943 O O   . GLY B 104 ? 0.2772 0.2284 0.2766 0.0061  0.0051  -0.0140 101 GLY B O   
5947 N N   A SER B 105 ? 0.2308 0.1749 0.2299 0.0171  0.0086  -0.0131 102 SER B N   
5948 N N   B SER B 105 ? 0.2318 0.1760 0.2309 0.0173  0.0085  -0.0128 102 SER B N   
5949 C CA  A SER B 105 ? 0.2466 0.1790 0.2448 0.0177  0.0125  -0.0113 102 SER B CA  
5950 C CA  B SER B 105 ? 0.2466 0.1790 0.2449 0.0181  0.0126  -0.0113 102 SER B CA  
5951 C C   A SER B 105 ? 0.2582 0.1892 0.2550 0.0247  0.0124  -0.0052 102 SER B C   
5952 C C   B SER B 105 ? 0.2583 0.1888 0.2549 0.0250  0.0125  -0.0051 102 SER B C   
5953 O O   A SER B 105 ? 0.2465 0.1834 0.2432 0.0314  0.0101  -0.0043 102 SER B O   
5954 O O   B SER B 105 ? 0.2481 0.1839 0.2445 0.0320  0.0104  -0.0041 102 SER B O   
5955 C CB  A SER B 105 ? 0.3152 0.2358 0.3128 0.0191  0.0174  -0.0153 102 SER B CB  
5956 C CB  B SER B 105 ? 0.3099 0.2316 0.3075 0.0201  0.0171  -0.0155 102 SER B CB  
5957 O OG  A SER B 105 ? 0.3305 0.2357 0.3268 0.0177  0.0221  -0.0127 102 SER B OG  
5958 O OG  B SER B 105 ? 0.3927 0.3163 0.3909 0.0296  0.0165  -0.0149 102 SER B OG  
5969 N N   . SER B 106 ? 0.2750 0.2004 0.2703 0.0224  0.0151  -0.0015 103 SER B N   
5970 C CA  . SER B 106 ? 0.2866 0.2109 0.2776 0.0282  0.0161  0.0051  103 SER B CA  
5971 C C   . SER B 106 ? 0.2405 0.1802 0.2332 0.0316  0.0109  0.0041  103 SER B C   
5972 O O   . SER B 106 ? 0.2546 0.2020 0.2521 0.0272  0.0080  0.0008  103 SER B O   
5973 C CB  . SER B 106 ? 0.3212 0.2329 0.3073 0.0361  0.0187  0.0093  103 SER B CB  
5974 O OG  . SER B 106 ? 0.3735 0.2814 0.3522 0.0398  0.0210  0.0178  103 SER B OG  
5979 N N   . SER B 107 ? 0.2575 0.2022 0.2470 0.0396  0.0089  0.0063  104 SER B N   
5980 C CA  . SER B 107 ? 0.2604 0.2193 0.2529 0.0407  0.0044  0.0027  104 SER B CA  
5981 C C   . SER B 107 ? 0.2411 0.2045 0.2398 0.0373  0.0012  -0.0028 104 SER B C   
5982 O O   . SER B 107 ? 0.2360 0.2060 0.2386 0.0352  -0.0017 -0.0060 104 SER B O   
5983 C CB  . SER B 107 ? 0.3477 0.3148 0.3354 0.0490  0.0026  0.0045  104 SER B CB  
5984 O OG  . SER B 107 ? 0.3384 0.3045 0.3261 0.0549  0.0017  0.0049  104 SER B OG  
5990 N N   . GLY B 108 ? 0.2321 0.1909 0.2315 0.0361  0.0025  -0.0040 105 GLY B N   
5991 C CA  . GLY B 108 ? 0.2331 0.1963 0.2362 0.0308  0.0007  -0.0080 105 GLY B CA  
5992 C C   . GLY B 108 ? 0.2051 0.1659 0.2091 0.0239  -0.0005 -0.0074 105 GLY B C   
5993 O O   . GLY B 108 ? 0.2105 0.1742 0.2162 0.0201  -0.0029 -0.0082 105 GLY B O   
5997 N N   A SER B 109 ? 0.2294 0.1853 0.2325 0.0222  0.0013  -0.0058 106 SER B N   
5998 N N   B SER B 109 ? 0.2298 0.1858 0.2330 0.0222  0.0012  -0.0058 106 SER B N   
5999 C CA  A SER B 109 ? 0.2126 0.1708 0.2183 0.0175  -0.0011 -0.0056 106 SER B CA  
6000 C CA  B SER B 109 ? 0.2135 0.1718 0.2193 0.0176  -0.0012 -0.0056 106 SER B CA  
6001 C C   A SER B 109 ? 0.1988 0.1615 0.2085 0.0203  -0.0042 -0.0053 106 SER B C   
6002 C C   B SER B 109 ? 0.1990 0.1617 0.2087 0.0203  -0.0043 -0.0053 106 SER B C   
6003 O O   A SER B 109 ? 0.2105 0.1748 0.2235 0.0188  -0.0079 -0.0050 106 SER B O   
6004 O O   B SER B 109 ? 0.2119 0.1760 0.2247 0.0189  -0.0080 -0.0050 106 SER B O   
6005 C CB  A SER B 109 ? 0.2301 0.1858 0.2361 0.0139  0.0019  -0.0059 106 SER B CB  
6006 C CB  B SER B 109 ? 0.2295 0.1853 0.2355 0.0140  0.0018  -0.0059 106 SER B CB  
6007 O OG  A SER B 109 ? 0.2841 0.2405 0.2911 0.0159  0.0043  -0.0041 106 SER B OG  
6008 O OG  B SER B 109 ? 0.2739 0.2365 0.2839 0.0106  -0.0015 -0.0066 106 SER B OG  
6019 N N   . ILE B 110 ? 0.1997 0.1646 0.2090 0.0249  -0.0030 -0.0057 107 ILE B N   
6020 C CA  . ILE B 110 ? 0.1908 0.1606 0.2041 0.0275  -0.0054 -0.0082 107 ILE B CA  
6021 C C   . ILE B 110 ? 0.1889 0.1578 0.2045 0.0268  -0.0085 -0.0105 107 ILE B C   
6022 O O   . ILE B 110 ? 0.2081 0.1749 0.2286 0.0265  -0.0112 -0.0118 107 ILE B O   
6023 C CB  . ILE B 110 ? 0.2146 0.1897 0.2246 0.0318  -0.0028 -0.0086 107 ILE B CB  
6024 C CG1 . ILE B 110 ? 0.2167 0.1906 0.2242 0.0302  0.0016  -0.0053 107 ILE B CG1 
6025 C CG2 . ILE B 110 ? 0.2071 0.1891 0.2214 0.0345  -0.0048 -0.0141 107 ILE B CG2 
6026 C CD1 . ILE B 110 ? 0.2653 0.2433 0.2662 0.0335  0.0053  -0.0030 107 ILE B CD1 
6038 N N   . VAL B 111 ? 0.2055 0.1757 0.2187 0.0263  -0.0077 -0.0110 108 VAL B N   
6039 C CA  . VAL B 111 ? 0.2221 0.1922 0.2380 0.0227  -0.0094 -0.0132 108 VAL B CA  
6040 C C   . VAL B 111 ? 0.2151 0.1776 0.2308 0.0178  -0.0109 -0.0093 108 VAL B C   
6041 O O   . VAL B 111 ? 0.2146 0.1717 0.2332 0.0156  -0.0129 -0.0091 108 VAL B O   
6042 C CB  . VAL B 111 ? 0.1990 0.1756 0.2137 0.0225  -0.0078 -0.0151 108 VAL B CB  
6043 C CG1 . VAL B 111 ? 0.2173 0.1948 0.2352 0.0159  -0.0081 -0.0173 108 VAL B CG1 
6044 C CG2 . VAL B 111 ? 0.2088 0.1951 0.2234 0.0291  -0.0080 -0.0181 108 VAL B CG2 
6054 N N   . ALA B 112 ? 0.2099 0.1715 0.2215 0.0160  -0.0100 -0.0062 109 ALA B N   
6055 C CA  . ALA B 112 ? 0.2106 0.1686 0.2196 0.0119  -0.0123 -0.0019 109 ALA B CA  
6056 C C   . ALA B 112 ? 0.2036 0.1580 0.2170 0.0148  -0.0164 0.0004  109 ALA B C   
6057 O O   . ALA B 112 ? 0.2297 0.1779 0.2422 0.0134  -0.0195 0.0049  109 ALA B O   
6058 C CB  . ALA B 112 ? 0.2184 0.1794 0.2231 0.0097  -0.0107 -0.0017 109 ALA B CB  
6064 N N   . MET B 113 ? 0.2178 0.1760 0.2359 0.0195  -0.0162 -0.0024 110 MET B N   
6065 C CA  . MET B 113 ? 0.2299 0.1876 0.2545 0.0238  -0.0197 -0.0022 110 MET B CA  
6066 C C   . MET B 113 ? 0.2255 0.1745 0.2542 0.0257  -0.0214 -0.0037 110 MET B C   
6067 O O   . MET B 113 ? 0.2436 0.1853 0.2758 0.0284  -0.0253 -0.0006 110 MET B O   
6068 C CB  . MET B 113 ? 0.2126 0.1791 0.2417 0.0273  -0.0173 -0.0065 110 MET B CB  
6069 C CG  . MET B 113 ? 0.2283 0.2018 0.2564 0.0244  -0.0157 -0.0057 110 MET B CG  
6070 S SD  . MET B 113 ? 0.2216 0.2040 0.2529 0.0258  -0.0103 -0.0096 110 MET B SD  
6071 C CE  . MET B 113 ? 0.2790 0.2642 0.3083 0.0185  -0.0075 -0.0085 110 MET B CE  
6081 N N   . HIS B 114 ? 0.2137 0.1632 0.2424 0.0244  -0.0186 -0.0087 111 HIS B N   
6082 C CA  . HIS B 114 ? 0.2298 0.1709 0.2630 0.0238  -0.0193 -0.0123 111 HIS B CA  
6083 C C   . HIS B 114 ? 0.2243 0.1540 0.2541 0.0173  -0.0199 -0.0065 111 HIS B C   
6084 O O   . HIS B 114 ? 0.2792 0.1957 0.3130 0.0164  -0.0211 -0.0066 111 HIS B O   
6085 C CB  . HIS B 114 ? 0.2198 0.1696 0.2541 0.0237  -0.0167 -0.0207 111 HIS B CB  
6086 C CG  . HIS B 114 ? 0.2298 0.1891 0.2666 0.0299  -0.0159 -0.0263 111 HIS B CG  
6087 N ND1 . HIS B 114 ? 0.2541 0.2122 0.2979 0.0334  -0.0166 -0.0339 111 HIS B ND1 
6088 C CD2 . HIS B 114 ? 0.2295 0.1990 0.2622 0.0326  -0.0138 -0.0251 111 HIS B CD2 
6089 C CE1 . HIS B 114 ? 0.2608 0.2314 0.3042 0.0379  -0.0148 -0.0377 111 HIS B CE1 
6090 N NE2 . HIS B 114 ? 0.2300 0.2066 0.2663 0.0371  -0.0129 -0.0314 111 HIS B NE2 
6098 N N   . VAL B 115 ? 0.2310 0.1648 0.2534 0.0121  -0.0183 -0.0020 112 VAL B N   
6099 C CA  . VAL B 115 ? 0.2422 0.1671 0.2594 0.0048  -0.0181 0.0047  112 VAL B CA  
6100 C C   . VAL B 115 ? 0.2546 0.1683 0.2698 0.0080  -0.0228 0.0135  112 VAL B C   
6101 O O   . VAL B 115 ? 0.2881 0.1861 0.3026 0.0056  -0.0238 0.0188  112 VAL B O   
6102 C CB  . VAL B 115 ? 0.2591 0.1941 0.2687 -0.0005 -0.0150 0.0062  112 VAL B CB  
6103 C CG1 . VAL B 115 ? 0.2650 0.1929 0.2668 -0.0091 -0.0140 0.0142  112 VAL B CG1 
6104 C CG2 . VAL B 115 ? 0.2320 0.1780 0.2450 -0.0018 -0.0112 -0.0020 112 VAL B CG2 
6114 N N   . LEU B 116 ? 0.2592 0.1807 0.2737 0.0135  -0.0258 0.0153  113 LEU B N   
6115 C CA  . LEU B 116 ? 0.2949 0.2107 0.3083 0.0183  -0.0317 0.0235  113 LEU B CA  
6116 C C   . LEU B 116 ? 0.3250 0.2280 0.3483 0.0258  -0.0345 0.0222  113 LEU B C   
6117 O O   . LEU B 116 ? 0.3614 0.2491 0.3830 0.0280  -0.0382 0.0308  113 LEU B O   
6118 C CB  . LEU B 116 ? 0.2884 0.2203 0.3021 0.0219  -0.0341 0.0225  113 LEU B CB  
6119 C CG  . LEU B 116 ? 0.3207 0.2535 0.3347 0.0284  -0.0416 0.0298  113 LEU B CG  
6120 C CD1 . LEU B 116 ? 0.3562 0.2822 0.3573 0.0243  -0.0444 0.0415  113 LEU B CD1 
6121 C CD2 . LEU B 116 ? 0.3605 0.3132 0.3777 0.0297  -0.0428 0.0251  113 LEU B CD2 
6133 N N   . LYS B 117 ? 0.2760 0.1843 0.3088 0.0298  -0.0324 0.0117  114 LYS B N   
6134 C CA  . LYS B 117 ? 0.2793 0.1779 0.3229 0.0376  -0.0343 0.0070  114 LYS B CA  
6135 C C   . LYS B 117 ? 0.3181 0.1946 0.3625 0.0333  -0.0329 0.0076  114 LYS B C   
6136 O O   . LYS B 117 ? 0.3437 0.2024 0.3930 0.0391  -0.0361 0.0110  114 LYS B O   
6137 C CB  . LYS B 117 ? 0.3326 0.2452 0.3836 0.0407  -0.0310 -0.0057 114 LYS B CB  
6138 C CG  . LYS B 117 ? 0.3936 0.3008 0.4568 0.0497  -0.0324 -0.0133 114 LYS B CG  
6139 C CD  . LYS B 117 ? 0.3810 0.3063 0.4494 0.0528  -0.0289 -0.0249 114 LYS B CD  
6140 C CE  . LYS B 117 ? 0.5570 0.4790 0.6386 0.0623  -0.0298 -0.0346 114 LYS B CE  
6141 N NZ  . LYS B 117 ? 0.4935 0.4381 0.5806 0.0670  -0.0268 -0.0443 114 LYS B NZ  
6155 N N   . ASP B 118 ? 0.3338 0.2113 0.3746 0.0233  -0.0280 0.0037  115 ASP B N   
6156 C CA  . ASP B 118 ? 0.3656 0.2252 0.4095 0.0167  -0.0253 0.0008  115 ASP B CA  
6157 C C   . ASP B 118 ? 0.3226 0.1683 0.3569 0.0068  -0.0239 0.0128  115 ASP B C   
6158 O O   . ASP B 118 ? 0.3792 0.2028 0.4157 0.0014  -0.0222 0.0143  115 ASP B O   
6159 C CB  . ASP B 118 ? 0.3320 0.2054 0.3797 0.0109  -0.0208 -0.0127 115 ASP B CB  
6160 C CG  . ASP B 118 ? 0.4192 0.3042 0.4751 0.0193  -0.0213 -0.0253 115 ASP B CG  
6161 O OD1 . ASP B 118 ? 0.5132 0.3914 0.5754 0.0284  -0.0239 -0.0265 115 ASP B OD1 
6162 O OD2 . ASP B 118 ? 0.5239 0.4262 0.5796 0.0169  -0.0188 -0.0341 115 ASP B OD2 
6167 N N   . TYR B 119 ? 0.3456 0.2033 0.3691 0.0031  -0.0238 0.0207  116 TYR B N   
6168 C CA  . TYR B 119 ? 0.3607 0.2104 0.3732 -0.0075 -0.0213 0.0315  116 TYR B CA  
6169 C C   . TYR B 119 ? 0.3584 0.2137 0.3590 -0.0043 -0.0254 0.0439  116 TYR B C   
6170 O O   . TYR B 119 ? 0.3371 0.2044 0.3275 -0.0118 -0.0226 0.0471  116 TYR B O   
6171 C CB  . TYR B 119 ? 0.3493 0.2143 0.3608 -0.0187 -0.0148 0.0242  116 TYR B CB  
6172 C CG  . TYR B 119 ? 0.3876 0.2544 0.4112 -0.0212 -0.0119 0.0099  116 TYR B CG  
6173 C CD1 . TYR B 119 ? 0.4661 0.3139 0.4949 -0.0289 -0.0091 0.0081  116 TYR B CD1 
6174 C CD2 . TYR B 119 ? 0.3621 0.2492 0.3914 -0.0157 -0.0121 -0.0015 116 TYR B CD2 
6175 C CE1 . TYR B 119 ? 0.4123 0.2651 0.4526 -0.0318 -0.0069 -0.0074 116 TYR B CE1 
6176 C CE2 . TYR B 119 ? 0.3880 0.2805 0.4268 -0.0171 -0.0105 -0.0145 116 TYR B CE2 
6177 C CZ  . TYR B 119 ? 0.3699 0.2471 0.4146 -0.0252 -0.0082 -0.0185 116 TYR B CZ  
6178 O OH  . TYR B 119 ? 0.5024 0.3883 0.5570 -0.0274 -0.0069 -0.0341 116 TYR B OH  
6188 N N   . PRO B 120 ? 0.3542 0.2025 0.3560 0.0068  -0.0323 0.0503  117 PRO B N   
6189 C CA  . PRO B 120 ? 0.3651 0.2237 0.3561 0.0102  -0.0374 0.0605  117 PRO B CA  
6190 C C   . PRO B 120 ? 0.3851 0.2366 0.3592 0.0007  -0.0359 0.0743  117 PRO B C   
6191 O O   . PRO B 120 ? 0.3695 0.2367 0.3321 -0.0008 -0.0379 0.0793  117 PRO B O   
6192 C CB  . PRO B 120 ? 0.3903 0.2411 0.3885 0.0247  -0.0455 0.0647  117 PRO B CB  
6193 C CG  . PRO B 120 ? 0.4178 0.2441 0.4262 0.0267  -0.0436 0.0613  117 PRO B CG  
6194 C CD  . PRO B 120 ? 0.4011 0.2332 0.4148 0.0172  -0.0359 0.0478  117 PRO B CD  
6202 N N   . GLU B 121 ? 0.3821 0.2117 0.3538 -0.0072 -0.0317 0.0799  118 GLU B N   
6203 C CA  . GLU B 121 ? 0.4212 0.2431 0.3754 -0.0177 -0.0290 0.0945  118 GLU B CA  
6204 C C   . GLU B 121 ? 0.4049 0.2502 0.3510 -0.0297 -0.0223 0.0893  118 GLU B C   
6205 O O   . GLU B 121 ? 0.4436 0.2912 0.3727 -0.0374 -0.0205 0.1007  118 GLU B O   
6206 C CB  . GLU B 121 ? 0.4977 0.2880 0.4535 -0.0248 -0.0246 0.1003  118 GLU B CB  
6207 C CG  . GLU B 121 ? 0.5111 0.3040 0.4780 -0.0364 -0.0159 0.0854  118 GLU B CG  
6208 C CD  . GLU B 121 ? 0.6371 0.4277 0.6236 -0.0281 -0.0174 0.0694  118 GLU B CD  
6209 O OE1 . GLU B 121 ? 0.5169 0.3045 0.5094 -0.0132 -0.0245 0.0691  118 GLU B OE1 
6210 O OE2 . GLU B 121 ? 0.5934 0.3877 0.5892 -0.0370 -0.0113 0.0565  118 GLU B OE2 
6217 N N   . VAL B 122 ? 0.3648 0.2279 0.3219 -0.0307 -0.0185 0.0729  119 VAL B N   
6218 C CA  . VAL B 122 ? 0.3533 0.2385 0.3045 -0.0395 -0.0125 0.0672  119 VAL B CA  
6219 C C   . VAL B 122 ? 0.3366 0.2423 0.2835 -0.0332 -0.0163 0.0638  119 VAL B C   
6220 O O   . VAL B 122 ? 0.3582 0.2818 0.3006 -0.0389 -0.0115 0.0578  119 VAL B O   
6221 C CB  . VAL B 122 ? 0.3122 0.2075 0.2763 -0.0442 -0.0061 0.0519  119 VAL B CB  
6222 C CG1 . VAL B 122 ? 0.3658 0.2428 0.3366 -0.0516 -0.0024 0.0519  119 VAL B CG1 
6223 C CG2 . VAL B 122 ? 0.3481 0.2525 0.3246 -0.0331 -0.0094 0.0402  119 VAL B CG2 
6233 N N   . VAL B 123 ? 0.3288 0.2333 0.2784 -0.0219 -0.0242 0.0661  120 VAL B N   
6234 C CA  . VAL B 123 ? 0.2889 0.2131 0.2384 -0.0171 -0.0272 0.0597  120 VAL B CA  
6235 C C   . VAL B 123 ? 0.3144 0.2452 0.2494 -0.0162 -0.0331 0.0703  120 VAL B C   
6236 O O   . VAL B 123 ? 0.3479 0.2694 0.2817 -0.0086 -0.0405 0.0805  120 VAL B O   
6237 C CB  . VAL B 123 ? 0.2834 0.2085 0.2478 -0.0064 -0.0311 0.0520  120 VAL B CB  
6238 C CG1 . VAL B 123 ? 0.3060 0.2502 0.2708 -0.0043 -0.0326 0.0450  120 VAL B CG1 
6239 C CG2 . VAL B 123 ? 0.3131 0.2335 0.2897 -0.0067 -0.0261 0.0422  120 VAL B CG2 
6249 N N   . LYS B 124 ? 0.3058 0.2542 0.2298 -0.0232 -0.0301 0.0672  121 LYS B N   
6250 C CA  . LYS B 124 ? 0.3020 0.2639 0.2125 -0.0222 -0.0363 0.0735  121 LYS B CA  
6251 C C   . LYS B 124 ? 0.3136 0.2904 0.2336 -0.0152 -0.0414 0.0634  121 LYS B C   
6252 O O   . LYS B 124 ? 0.3305 0.3113 0.2513 -0.0073 -0.0503 0.0689  121 LYS B O   
6253 C CB  . LYS B 124 ? 0.3516 0.3282 0.2462 -0.0334 -0.0303 0.0719  121 LYS B CB  
6254 C CG  . LYS B 124 ? 0.3919 0.3851 0.2687 -0.0342 -0.0364 0.0784  121 LYS B CG  
6255 C CD  . LYS B 124 ? 0.4710 0.4758 0.3304 -0.0466 -0.0286 0.0785  121 LYS B CD  
6256 C CE  . LYS B 124 ? 0.7145 0.7320 0.5501 -0.0490 -0.0341 0.0910  121 LYS B CE  
6257 N NZ  . LYS B 124 ? 0.7192 0.7648 0.5464 -0.0554 -0.0312 0.0769  121 LYS B NZ  
6271 N N   . LYS B 125 ? 0.2809 0.2661 0.2090 -0.0181 -0.0354 0.0486  122 LYS B N   
6272 C CA  . LYS B 125 ? 0.2837 0.2802 0.2223 -0.0142 -0.0375 0.0377  122 LYS B CA  
6273 C C   . LYS B 125 ? 0.2312 0.2211 0.1827 -0.0138 -0.0305 0.0271  122 LYS B C   
6274 O O   . LYS B 125 ? 0.2605 0.2456 0.2108 -0.0180 -0.0237 0.0246  122 LYS B O   
6275 C CB  . LYS B 125 ? 0.3064 0.3232 0.2361 -0.0201 -0.0376 0.0302  122 LYS B CB  
6276 C CG  . LYS B 125 ? 0.3243 0.3532 0.2386 -0.0205 -0.0454 0.0402  122 LYS B CG  
6277 C CD  . LYS B 125 ? 0.3434 0.3801 0.2655 -0.0118 -0.0555 0.0428  122 LYS B CD  
6278 C CE  . LYS B 125 ? 0.4336 0.4884 0.3402 -0.0113 -0.0645 0.0509  122 LYS B CE  
6279 N NZ  . LYS B 125 ? 0.4668 0.5287 0.3832 0.0002  -0.0756 0.0557  122 LYS B NZ  
6293 N N   . ILE B 126 ? 0.2290 0.2206 0.1926 -0.0087 -0.0320 0.0212  123 ILE B N   
6294 C CA  . ILE B 126 ? 0.2218 0.2069 0.1955 -0.0074 -0.0260 0.0135  123 ILE B CA  
6295 C C   . ILE B 126 ? 0.2202 0.2127 0.2010 -0.0072 -0.0250 0.0049  123 ILE B C   
6296 O O   . ILE B 126 ? 0.2352 0.2378 0.2187 -0.0062 -0.0301 0.0047  123 ILE B O   
6297 C CB  . ILE B 126 ? 0.2327 0.2056 0.2146 -0.0013 -0.0270 0.0175  123 ILE B CB  
6298 C CG1 . ILE B 126 ? 0.2380 0.2056 0.2267 -0.0001 -0.0212 0.0113  123 ILE B CG1 
6299 C CG2 . ILE B 126 ? 0.2683 0.2440 0.2582 0.0057  -0.0332 0.0195  123 ILE B CG2 
6300 C CD1 . ILE B 126 ? 0.2705 0.2273 0.2638 0.0027  -0.0215 0.0143  123 ILE B CD1 
6312 N N   . ALA B 127 ? 0.2028 0.1907 0.1866 -0.0087 -0.0182 -0.0023 124 ALA B N   
6313 C CA  . ALA B 127 ? 0.2140 0.2038 0.2039 -0.0101 -0.0152 -0.0098 124 ALA B CA  
6314 C C   . ALA B 127 ? 0.1976 0.1773 0.1943 -0.0056 -0.0109 -0.0102 124 ALA B C   
6315 O O   . ALA B 127 ? 0.2253 0.1979 0.2206 -0.0031 -0.0079 -0.0095 124 ALA B O   
6316 C CB  . ALA B 127 ? 0.2491 0.2417 0.2340 -0.0164 -0.0108 -0.0183 124 ALA B CB  
6322 N N   . PHE B 128 ? 0.2124 0.1942 0.2162 -0.0050 -0.0106 -0.0118 125 PHE B N   
6323 C CA  . PHE B 128 ? 0.1915 0.1657 0.1996 -0.0016 -0.0062 -0.0116 125 PHE B CA  
6324 C C   . PHE B 128 ? 0.2132 0.1824 0.2220 -0.0067 0.0000  -0.0166 125 PHE B C   
6325 O O   . PHE B 128 ? 0.2202 0.1962 0.2337 -0.0119 0.0006  -0.0201 125 PHE B O   
6326 C CB  . PHE B 128 ? 0.2209 0.2009 0.2363 0.0024  -0.0090 -0.0093 125 PHE B CB  
6327 C CG  . PHE B 128 ? 0.2189 0.2003 0.2352 0.0076  -0.0151 -0.0050 125 PHE B CG  
6328 C CD1 . PHE B 128 ? 0.2061 0.1794 0.2174 0.0091  -0.0153 -0.0022 125 PHE B CD1 
6329 C CD2 . PHE B 128 ? 0.2454 0.2355 0.2683 0.0110  -0.0202 -0.0040 125 PHE B CD2 
6330 C CE1 . PHE B 128 ? 0.2167 0.1873 0.2289 0.0125  -0.0201 0.0022  125 PHE B CE1 
6331 C CE2 . PHE B 128 ? 0.2553 0.2417 0.2791 0.0167  -0.0257 0.0007  125 PHE B CE2 
6332 C CZ  . PHE B 128 ? 0.2302 0.2051 0.2480 0.0165  -0.0251 0.0040  125 PHE B CZ  
6342 N N   . HIS B 129 ? 0.2171 0.1745 0.2220 -0.0053 0.0049  -0.0176 126 HIS B N   
6343 C CA  . HIS B 129 ? 0.2320 0.1787 0.2371 -0.0091 0.0114  -0.0215 126 HIS B CA  
6344 C C   . HIS B 129 ? 0.2759 0.2137 0.2818 -0.0055 0.0154  -0.0161 126 HIS B C   
6345 O O   . HIS B 129 ? 0.2695 0.2022 0.2723 0.0024  0.0155  -0.0113 126 HIS B O   
6346 C CB  . HIS B 129 ? 0.2270 0.1651 0.2281 -0.0076 0.0144  -0.0257 126 HIS B CB  
6347 C CG  . HIS B 129 ? 0.2376 0.1600 0.2394 -0.0106 0.0214  -0.0304 126 HIS B CG  
6348 N ND1 . HIS B 129 ? 0.3285 0.2339 0.3290 -0.0040 0.0259  -0.0257 126 HIS B ND1 
6349 C CD2 . HIS B 129 ? 0.2565 0.1760 0.2599 -0.0195 0.0247  -0.0394 126 HIS B CD2 
6350 C CE1 . HIS B 129 ? 0.3536 0.2428 0.3550 -0.0083 0.0321  -0.0305 126 HIS B CE1 
6351 N NE2 . HIS B 129 ? 0.3212 0.2187 0.3250 -0.0186 0.0320  -0.0400 126 HIS B NE2 
6359 N N   . GLU B 130 ? 0.2566 0.1950 0.2663 -0.0119 0.0188  -0.0170 127 GLU B N   
6360 C CA  . GLU B 130 ? 0.2989 0.2286 0.3074 -0.0112 0.0245  -0.0115 127 GLU B CA  
6361 C C   . GLU B 130 ? 0.2625 0.1968 0.2682 -0.0020 0.0219  -0.0051 127 GLU B C   
6362 O O   . GLU B 130 ? 0.2656 0.1895 0.2649 0.0045  0.0241  0.0004  127 GLU B O   
6363 C CB  . GLU B 130 ? 0.3102 0.2176 0.3141 -0.0120 0.0313  -0.0108 127 GLU B CB  
6364 C CG  . GLU B 130 ? 0.3515 0.2560 0.3603 -0.0246 0.0353  -0.0198 127 GLU B CG  
6365 C CD  . GLU B 130 ? 0.3578 0.2374 0.3645 -0.0293 0.0445  -0.0190 127 GLU B CD  
6366 O OE1 . GLU B 130 ? 0.3591 0.2349 0.3704 -0.0405 0.0483  -0.0281 127 GLU B OE1 
6367 O OE2 . GLU B 130 ? 0.4193 0.2818 0.4194 -0.0215 0.0476  -0.0098 127 GLU B OE2 
6374 N N   . PRO B 131 ? 0.2417 0.1921 0.2524 -0.0009 0.0172  -0.0060 128 PRO B N   
6375 C CA  . PRO B 131 ? 0.2561 0.2121 0.2655 0.0068  0.0149  -0.0027 128 PRO B CA  
6376 C C   . PRO B 131 ? 0.2633 0.2199 0.2700 0.0064  0.0207  0.0010  128 PRO B C   
6377 O O   . PRO B 131 ? 0.2923 0.2534 0.3031 -0.0009 0.0252  -0.0004 128 PRO B O   
6378 C CB  . PRO B 131 ? 0.2560 0.2262 0.2731 0.0077  0.0086  -0.0062 128 PRO B CB  
6379 C CG  . PRO B 131 ? 0.2600 0.2376 0.2833 0.0002  0.0092  -0.0100 128 PRO B CG  
6380 C CD  . PRO B 131 ? 0.3139 0.2791 0.3327 -0.0060 0.0134  -0.0111 128 PRO B CD  
6388 N N   . PRO B 132 ? 0.2476 0.2022 0.2471 0.0136  0.0209  0.0054  129 PRO B N   
6389 C CA  . PRO B 132 ? 0.2314 0.1889 0.2253 0.0135  0.0265  0.0100  129 PRO B CA  
6390 C C   . PRO B 132 ? 0.2595 0.2350 0.2566 0.0174  0.0240  0.0061  129 PRO B C   
6391 O O   . PRO B 132 ? 0.2944 0.2753 0.2843 0.0191  0.0278  0.0092  129 PRO B O   
6392 C CB  . PRO B 132 ? 0.3070 0.2516 0.2890 0.0201  0.0277  0.0177  129 PRO B CB  
6393 C CG  . PRO B 132 ? 0.2867 0.2335 0.2715 0.0267  0.0203  0.0138  129 PRO B CG  
6394 C CD  . PRO B 132 ? 0.2802 0.2283 0.2745 0.0210  0.0176  0.0072  129 PRO B CD  
6402 N N   . ILE B 133 ? 0.2528 0.2368 0.2597 0.0190  0.0181  -0.0007 130 ILE B N   
6403 C CA  . ILE B 133 ? 0.2322 0.2305 0.2442 0.0234  0.0158  -0.0063 130 ILE B CA  
6404 C C   . ILE B 133 ? 0.2246 0.2365 0.2418 0.0193  0.0212  -0.0088 130 ILE B C   
6405 O O   . ILE B 133 ? 0.2468 0.2604 0.2699 0.0125  0.0237  -0.0092 130 ILE B O   
6406 C CB  . ILE B 133 ? 0.2449 0.2436 0.2659 0.0265  0.0083  -0.0112 130 ILE B CB  
6407 C CG1 . ILE B 133 ? 0.2330 0.2422 0.2601 0.0321  0.0062  -0.0181 130 ILE B CG1 
6408 C CG2 . ILE B 133 ? 0.2486 0.2482 0.2773 0.0221  0.0064  -0.0119 130 ILE B CG2 
6409 C CD1 . ILE B 133 ? 0.2835 0.2866 0.3152 0.0359  -0.0004 -0.0213 130 ILE B CD1 
6421 N N   . ASN B 134 ? 0.2091 0.2335 0.2247 0.0227  0.0236  -0.0121 131 ASN B N   
6422 C CA  . ASN B 134 ? 0.2215 0.2627 0.2422 0.0186  0.0300  -0.0156 131 ASN B CA  
6423 C C   . ASN B 134 ? 0.2115 0.2703 0.2447 0.0247  0.0273  -0.0267 131 ASN B C   
6424 O O   . ASN B 134 ? 0.1996 0.2762 0.2405 0.0221  0.0323  -0.0317 131 ASN B O   
6425 C CB  . ASN B 134 ? 0.2263 0.2691 0.2319 0.0157  0.0384  -0.0089 131 ASN B CB  
6426 C CG  . ASN B 134 ? 0.2416 0.2907 0.2377 0.0235  0.0364  -0.0107 131 ASN B CG  
6427 O OD1 . ASN B 134 ? 0.2385 0.3020 0.2423 0.0283  0.0340  -0.0213 131 ASN B OD1 
6428 N ND2 . ASN B 134 ? 0.2592 0.2978 0.2387 0.0253  0.0371  -0.0010 131 ASN B ND2 
6435 N N   . THR B 135 ? 0.1880 0.2420 0.2250 0.0323  0.0199  -0.0313 132 THR B N   
6436 C CA  . THR B 135 ? 0.1790 0.2461 0.2250 0.0391  0.0187  -0.0426 132 THR B CA  
6437 C C   . THR B 135 ? 0.1919 0.2738 0.2551 0.0404  0.0188  -0.0491 132 THR B C   
6438 O O   . THR B 135 ? 0.2129 0.3132 0.2832 0.0435  0.0226  -0.0583 132 THR B O   
6439 C CB  . THR B 135 ? 0.2379 0.2924 0.2864 0.0453  0.0110  -0.0460 132 THR B CB  
6440 O OG1 . THR B 135 ? 0.2173 0.2591 0.2527 0.0430  0.0097  -0.0388 132 THR B OG1 
6441 C CG2 . THR B 135 ? 0.2468 0.3112 0.3000 0.0514  0.0113  -0.0583 132 THR B CG2 
6449 N N   . PHE B 136 ? 0.2147 0.2912 0.2854 0.0390  0.0141  -0.0456 133 PHE B N   
6450 C CA  . PHE B 136 ? 0.2087 0.3010 0.2969 0.0420  0.0118  -0.0514 133 PHE B CA  
6451 C C   . PHE B 136 ? 0.2108 0.3207 0.3031 0.0325  0.0188  -0.0513 133 PHE B C   
6452 O O   . PHE B 136 ? 0.2197 0.3475 0.3282 0.0342  0.0165  -0.0567 133 PHE B O   
6453 C CB  . PHE B 136 ? 0.2220 0.3015 0.3152 0.0460  0.0018  -0.0474 133 PHE B CB  
6454 C CG  . PHE B 136 ? 0.2052 0.2697 0.2866 0.0378  0.0010  -0.0378 133 PHE B CG  
6455 C CD1 . PHE B 136 ? 0.2026 0.2752 0.2851 0.0288  0.0042  -0.0360 133 PHE B CD1 
6456 C CD2 . PHE B 136 ? 0.2219 0.2657 0.2924 0.0384  -0.0022 -0.0324 133 PHE B CD2 
6457 C CE1 . PHE B 136 ? 0.2168 0.2750 0.2892 0.0215  0.0043  -0.0294 133 PHE B CE1 
6458 C CE2 . PHE B 136 ? 0.2320 0.2639 0.2925 0.0316  -0.0020 -0.0254 133 PHE B CE2 
6459 C CZ  . PHE B 136 ? 0.2198 0.2581 0.2813 0.0237  0.0011  -0.0242 133 PHE B CZ  
6469 N N   . LEU B 137 ? 0.1998 0.3059 0.2786 0.0227  0.0271  -0.0453 134 LEU B N   
6470 C CA  . LEU B 137 ? 0.2017 0.3213 0.2842 0.0111  0.0351  -0.0449 134 LEU B CA  
6471 C C   . LEU B 137 ? 0.2169 0.3652 0.3091 0.0109  0.0425  -0.0541 134 LEU B C   
6472 O O   . LEU B 137 ? 0.2255 0.3793 0.3143 0.0177  0.0442  -0.0587 134 LEU B O   
6473 C CB  . LEU B 137 ? 0.2104 0.3116 0.2743 0.0011  0.0423  -0.0341 134 LEU B CB  
6474 C CG  . LEU B 137 ? 0.2039 0.2783 0.2582 0.0002  0.0372  -0.0260 134 LEU B CG  
6475 C CD1 . LEU B 137 ? 0.2495 0.3062 0.2864 -0.0067 0.0450  -0.0158 134 LEU B CD1 
6476 C CD2 . LEU B 137 ? 0.2428 0.3199 0.3085 -0.0044 0.0328  -0.0288 134 LEU B CD2 
6488 N N   . PRO B 138 ? 0.2068 0.3758 0.3110 0.0021  0.0478  -0.0581 135 PRO B N   
6489 C CA  . PRO B 138 ? 0.2344 0.4341 0.3480 -0.0001 0.0569  -0.0672 135 PRO B CA  
6490 C C   . PRO B 138 ? 0.2675 0.4647 0.3620 -0.0090 0.0694  -0.0609 135 PRO B C   
6491 O O   . PRO B 138 ? 0.2956 0.5177 0.3936 -0.0094 0.0773  -0.0684 135 PRO B O   
6492 C CB  . PRO B 138 ? 0.2265 0.4486 0.3580 -0.0098 0.0593  -0.0724 135 PRO B CB  
6493 C CG  . PRO B 138 ? 0.2707 0.4730 0.4000 -0.0133 0.0517  -0.0660 135 PRO B CG  
6494 C CD  . PRO B 138 ? 0.2170 0.3841 0.3271 -0.0073 0.0461  -0.0558 135 PRO B CD  
6502 N N   . ASP B 139 ? 0.2116 0.3813 0.2862 -0.0161 0.0718  -0.0474 136 ASP B N   
6503 C CA  . ASP B 139 ? 0.2638 0.4264 0.3167 -0.0225 0.0820  -0.0378 136 ASP B CA  
6504 C C   . ASP B 139 ? 0.2548 0.3937 0.2895 -0.0126 0.0753  -0.0304 136 ASP B C   
6505 O O   . ASP B 139 ? 0.2636 0.3844 0.2779 -0.0165 0.0796  -0.0175 136 ASP B O   
6506 C CB  . ASP B 139 ? 0.2754 0.4265 0.3213 -0.0396 0.0918  -0.0278 136 ASP B CB  
6507 C CG  . ASP B 139 ? 0.3320 0.4550 0.3774 -0.0419 0.0853  -0.0218 136 ASP B CG  
6508 O OD1 . ASP B 139 ? 0.2990 0.4132 0.3494 -0.0313 0.0733  -0.0245 136 ASP B OD1 
6509 O OD2 . ASP B 139 ? 0.4095 0.5191 0.4500 -0.0558 0.0932  -0.0149 136 ASP B OD2 
6514 N N   A SER B 140 ? 0.2157 0.3553 0.2581 0.0005  0.0649  -0.0384 137 SER B N   
6515 N N   B SER B 140 ? 0.2137 0.3535 0.2564 0.0005  0.0649  -0.0385 137 SER B N   
6516 C CA  A SER B 140 ? 0.2392 0.3600 0.2673 0.0089  0.0584  -0.0336 137 SER B CA  
6517 C CA  B SER B 140 ? 0.2379 0.3597 0.2669 0.0093  0.0582  -0.0344 137 SER B CA  
6518 C C   A SER B 140 ? 0.2441 0.3706 0.2523 0.0087  0.0649  -0.0293 137 SER B C   
6519 C C   B SER B 140 ? 0.2419 0.3687 0.2507 0.0089  0.0647  -0.0296 137 SER B C   
6520 O O   A SER B 140 ? 0.2611 0.3706 0.2522 0.0110  0.0626  -0.0193 137 SER B O   
6521 O O   B SER B 140 ? 0.2606 0.3701 0.2525 0.0113  0.0622  -0.0199 137 SER B O   
6522 C CB  A SER B 140 ? 0.2146 0.3376 0.2554 0.0210  0.0483  -0.0447 137 SER B CB  
6523 C CB  B SER B 140 ? 0.2107 0.3362 0.2530 0.0215  0.0484  -0.0462 137 SER B CB  
6524 O OG  A SER B 140 ? 0.1961 0.3054 0.2243 0.0272  0.0432  -0.0423 137 SER B OG  
6525 O OG  B SER B 140 ? 0.2490 0.3990 0.2996 0.0262  0.0517  -0.0593 137 SER B OG  
6536 N N   . THR B 141 ? 0.2458 0.3987 0.2560 0.0068  0.0728  -0.0371 138 THR B N   
6537 C CA  . THR B 141 ? 0.2857 0.4478 0.2749 0.0068  0.0788  -0.0334 138 THR B CA  
6538 C C   . THR B 141 ? 0.3124 0.4568 0.2798 -0.0018 0.0853  -0.0139 138 THR B C   
6539 O O   . THR B 141 ? 0.2934 0.4294 0.2398 0.0023  0.0837  -0.0045 138 THR B O   
6540 C CB  . THR B 141 ? 0.2788 0.4746 0.2739 0.0043  0.0881  -0.0455 138 THR B CB  
6541 O OG1 . THR B 141 ? 0.2924 0.5020 0.3100 0.0141  0.0819  -0.0642 138 THR B OG1 
6542 C CG2 . THR B 141 ? 0.2699 0.4784 0.2411 0.0042  0.0942  -0.0423 138 THR B CG2 
6551 N N   . TYR B 142 ? 0.2954 0.4339 0.2677 -0.0137 0.0925  -0.0077 139 TYR B N   
6552 C CA  . TYR B 142 ? 0.3508 0.4666 0.3035 -0.0222 0.0992  0.0112  139 TYR B CA  
6553 C C   . TYR B 142 ? 0.3100 0.3956 0.2531 -0.0138 0.0896  0.0210  139 TYR B C   
6554 O O   . TYR B 142 ? 0.3608 0.4332 0.2819 -0.0113 0.0908  0.0350  139 TYR B O   
6555 C CB  . TYR B 142 ? 0.3165 0.4286 0.2806 -0.0374 0.1077  0.0130  139 TYR B CB  
6556 C CG  . TYR B 142 ? 0.3647 0.4447 0.3122 -0.0461 0.1138  0.0315  139 TYR B CG  
6557 C CD1 . TYR B 142 ? 0.4197 0.4691 0.3676 -0.0423 0.1062  0.0370  139 TYR B CD1 
6558 C CD2 . TYR B 142 ? 0.4649 0.5444 0.3964 -0.0585 0.1280  0.0434  139 TYR B CD2 
6559 C CE1 . TYR B 142 ? 0.4942 0.5115 0.4282 -0.0489 0.1119  0.0529  139 TYR B CE1 
6560 C CE2 . TYR B 142 ? 0.5365 0.5815 0.4526 -0.0660 0.1339  0.0614  139 TYR B CE2 
6561 C CZ  . TYR B 142 ? 0.5878 0.6012 0.5061 -0.0604 0.1255  0.0654  139 TYR B CZ  
6562 O OH  . TYR B 142 ? 0.6396 0.6165 0.5441 -0.0665 0.1316  0.0820  139 TYR B OH  
6572 N N   . TRP B 143 ? 0.2873 0.3626 0.2464 -0.0091 0.0798  0.0142  140 TRP B N   
6573 C CA  . TRP B 143 ? 0.2845 0.3329 0.2367 -0.0029 0.0722  0.0225  140 TRP B CA  
6574 C C   . TRP B 143 ? 0.3075 0.3603 0.2503 0.0099  0.0640  0.0212  140 TRP B C   
6575 O O   . TRP B 143 ? 0.3337 0.3711 0.2618 0.0154  0.0611  0.0320  140 TRP B O   
6576 C CB  . TRP B 143 ? 0.2711 0.3101 0.2422 -0.0034 0.0653  0.0155  140 TRP B CB  
6577 C CG  . TRP B 143 ? 0.3282 0.3609 0.3065 -0.0167 0.0728  0.0173  140 TRP B CG  
6578 C CD1 . TRP B 143 ? 0.3168 0.3682 0.3132 -0.0243 0.0754  0.0071  140 TRP B CD1 
6579 C CD2 . TRP B 143 ? 0.3547 0.3614 0.3230 -0.0245 0.0789  0.0293  140 TRP B CD2 
6580 N NE1 . TRP B 143 ? 0.3113 0.3520 0.3095 -0.0379 0.0831  0.0112  140 TRP B NE1 
6581 C CE2 . TRP B 143 ? 0.3598 0.3707 0.3408 -0.0385 0.0856  0.0247  140 TRP B CE2 
6582 C CE3 . TRP B 143 ? 0.4002 0.3804 0.3510 -0.0201 0.0791  0.0431  140 TRP B CE3 
6583 C CZ2 . TRP B 143 ? 0.4131 0.4000 0.3896 -0.0501 0.0934  0.0325  140 TRP B CZ2 
6584 C CZ3 . TRP B 143 ? 0.4130 0.3674 0.3593 -0.0295 0.0865  0.0519  140 TRP B CZ3 
6585 C CH2 . TRP B 143 ? 0.4750 0.4317 0.4339 -0.0453 0.0940  0.0462  140 TRP B CH2 
6596 N N   . LYS B 144 ? 0.2672 0.3413 0.2197 0.0151  0.0600  0.0068  141 LYS B N   
6597 C CA  . LYS B 144 ? 0.2975 0.3789 0.2423 0.0252  0.0531  0.0027  141 LYS B CA  
6598 C C   . LYS B 144 ? 0.3166 0.4055 0.2374 0.0261  0.0579  0.0127  141 LYS B C   
6599 O O   . LYS B 144 ? 0.3507 0.4343 0.2583 0.0335  0.0523  0.0192  141 LYS B O   
6600 C CB  . LYS B 144 ? 0.2767 0.3787 0.2366 0.0291  0.0501  -0.0159 141 LYS B CB  
6601 C CG  . LYS B 144 ? 0.3477 0.4580 0.3013 0.0375  0.0434  -0.0231 141 LYS B CG  
6602 C CD  . LYS B 144 ? 0.3765 0.5069 0.3422 0.0407  0.0429  -0.0422 141 LYS B CD  
6603 C CE  . LYS B 144 ? 0.4715 0.6058 0.4345 0.0474  0.0352  -0.0512 141 LYS B CE  
6604 N NZ  . LYS B 144 ? 0.4926 0.6455 0.4343 0.0485  0.0381  -0.0491 141 LYS B NZ  
6618 N N   . ASP B 145 ? 0.3024 0.4058 0.2171 0.0187  0.0684  0.0143  142 ASP B N   
6619 C CA  . ASP B 145 ? 0.3322 0.4449 0.2214 0.0192  0.0736  0.0248  142 ASP B CA  
6620 C C   . ASP B 145 ? 0.3893 0.4746 0.2603 0.0187  0.0752  0.0471  142 ASP B C   
6621 O O   . ASP B 145 ? 0.4224 0.5094 0.2711 0.0251  0.0735  0.0580  142 ASP B O   
6622 C CB  . ASP B 145 ? 0.3352 0.4709 0.2220 0.0098  0.0861  0.0214  142 ASP B CB  
6623 C CG  . ASP B 145 ? 0.4010 0.5677 0.2996 0.0138  0.0848  -0.0005 142 ASP B CG  
6624 O OD1 . ASP B 145 ? 0.4204 0.5883 0.3280 0.0233  0.0742  -0.0125 142 ASP B OD1 
6625 O OD2 . ASP B 145 ? 0.3815 0.5713 0.2806 0.0073  0.0949  -0.0063 142 ASP B OD2 
6630 N N   . LYS B 146 ? 0.3940 0.4543 0.2740 0.0120  0.0780  0.0535  143 LYS B N   
6631 C CA  . LYS B 146 ? 0.4062 0.4361 0.2715 0.0130  0.0790  0.0730  143 LYS B CA  
6632 C C   . LYS B 146 ? 0.4081 0.4294 0.2710 0.0274  0.0665  0.0742  143 LYS B C   
6633 O O   . LYS B 146 ? 0.4567 0.4687 0.3002 0.0352  0.0645  0.0891  143 LYS B O   
6634 C CB  . LYS B 146 ? 0.4670 0.4725 0.3458 0.0027  0.0839  0.0752  143 LYS B CB  
6635 C CG  . LYS B 146 ? 0.5200 0.5261 0.3975 -0.0136 0.0982  0.0798  143 LYS B CG  
6636 C CD  . LYS B 146 ? 0.6100 0.5980 0.4613 -0.0169 0.1071  0.1017  143 LYS B CD  
6637 C CE  . LYS B 146 ? 0.7592 0.7409 0.6129 -0.0365 0.1223  0.1059  143 LYS B CE  
6638 N NZ  . LYS B 146 ? 0.9779 0.9412 0.8046 -0.0423 0.1333  0.1288  143 LYS B NZ  
6652 N N   . ASN B 147 ? 0.3784 0.4028 0.2614 0.0310  0.0579  0.0595  144 ASN B N   
6653 C CA  . ASN B 147 ? 0.3785 0.3982 0.2622 0.0428  0.0468  0.0584  144 ASN B CA  
6654 C C   . ASN B 147 ? 0.3612 0.4025 0.2294 0.0521  0.0419  0.0587  144 ASN B C   
6655 O O   . ASN B 147 ? 0.4030 0.4391 0.2591 0.0619  0.0364  0.0685  144 ASN B O   
6656 C CB  . ASN B 147 ? 0.3435 0.3674 0.2498 0.0432  0.0398  0.0416  144 ASN B CB  
6657 C CG  . ASN B 147 ? 0.3638 0.3667 0.2836 0.0370  0.0412  0.0418  144 ASN B CG  
6658 O OD1 . ASN B 147 ? 0.4028 0.3842 0.3165 0.0345  0.0456  0.0534  144 ASN B OD1 
6659 N ND2 . ASN B 147 ? 0.3510 0.3599 0.2891 0.0346  0.0376  0.0287  144 ASN B ND2 
6666 N N   . ASP B 148 ? 0.3637 0.4317 0.2328 0.0496  0.0436  0.0466  145 ASP B N   
6667 C CA  . ASP B 148 ? 0.3770 0.4695 0.2314 0.0571  0.0391  0.0438  145 ASP B CA  
6668 C C   . ASP B 148 ? 0.3668 0.4573 0.1931 0.0600  0.0432  0.0644  145 ASP B C   
6669 O O   . ASP B 148 ? 0.4054 0.5073 0.2167 0.0702  0.0361  0.0692  145 ASP B O   
6670 C CB  . ASP B 148 ? 0.3966 0.5172 0.2569 0.0530  0.0422  0.0259  145 ASP B CB  
6671 C CG  . ASP B 148 ? 0.4735 0.5957 0.3603 0.0522  0.0373  0.0059  145 ASP B CG  
6672 O OD1 . ASP B 148 ? 0.4396 0.5459 0.3380 0.0552  0.0303  0.0049  145 ASP B OD1 
6673 O OD2 . ASP B 148 ? 0.4073 0.5473 0.3027 0.0492  0.0408  -0.0090 145 ASP B OD2 
6678 N N   . ASP B 149 ? 0.4022 0.4797 0.2205 0.0507  0.0547  0.0768  146 ASP B N   
6679 C CA  . ASP B 149 ? 0.4047 0.4766 0.1943 0.0519  0.0602  0.0988  146 ASP B CA  
6680 C C   . ASP B 149 ? 0.4876 0.5307 0.2689 0.0622  0.0544  0.1167  146 ASP B C   
6681 O O   . ASP B 149 ? 0.5097 0.5573 0.2688 0.0728  0.0500  0.1304  146 ASP B O   
6682 C CB  . ASP B 149 ? 0.4954 0.5602 0.2809 0.0366  0.0755  0.1063  146 ASP B CB  
6683 C CG  . ASP B 149 ? 0.6121 0.7126 0.3989 0.0289  0.0824  0.0914  146 ASP B CG  
6684 O OD1 . ASP B 149 ? 0.6360 0.7656 0.4190 0.0360  0.0762  0.0790  146 ASP B OD1 
6685 O OD2 . ASP B 149 ? 0.6660 0.7674 0.4577 0.0152  0.0946  0.0910  146 ASP B OD2 
6690 N N   . ILE B 150 ? 0.4944 0.5094 0.2933 0.0603  0.0538  0.1162  147 ILE B N   
6691 C CA  . ILE B 150 ? 0.5777 0.5652 0.3710 0.0712  0.0488  0.1310  147 ILE B CA  
6692 C C   . ILE B 150 ? 0.5114 0.5174 0.3054 0.0873  0.0346  0.1252  147 ILE B C   
6693 O O   . ILE B 150 ? 0.5542 0.5549 0.3321 0.1006  0.0292  0.1402  147 ILE B O   
6694 C CB  . ILE B 150 ? 0.5833 0.5401 0.3966 0.0649  0.0516  0.1280  147 ILE B CB  
6695 C CG1 . ILE B 150 ? 0.6136 0.5479 0.4223 0.0499  0.0658  0.1384  147 ILE B CG1 
6696 C CG2 . ILE B 150 ? 0.6894 0.6239 0.5029 0.0787  0.0443  0.1363  147 ILE B CG2 
6697 C CD1 . ILE B 150 ? 0.7267 0.6604 0.5585 0.0350  0.0712  0.1231  147 ILE B CD1 
6709 N N   . VAL B 151 ? 0.4465 0.4740 0.2597 0.0866  0.0281  0.1035  148 VAL B N   
6710 C CA  . VAL B 151 ? 0.4689 0.5174 0.2843 0.0993  0.0155  0.0957  148 VAL B CA  
6711 C C   . VAL B 151 ? 0.4707 0.5460 0.2620 0.1070  0.0121  0.1022  148 VAL B C   
6712 O O   . VAL B 151 ? 0.5317 0.6127 0.3130 0.1207  0.0036  0.1109  148 VAL B O   
6713 C CB  . VAL B 151 ? 0.4456 0.5108 0.2847 0.0942  0.0111  0.0713  148 VAL B CB  
6714 C CG1 . VAL B 151 ? 0.5177 0.6087 0.3586 0.1043  -0.0005 0.0617  148 VAL B CG1 
6715 C CG2 . VAL B 151 ? 0.4466 0.4874 0.3064 0.0891  0.0125  0.0670  148 VAL B CG2 
6725 N N   . HIS B 152 ? 0.4894 0.5841 0.2720 0.0984  0.0185  0.0970  149 HIS B N   
6726 C CA  . HIS B 152 ? 0.4981 0.6194 0.2586 0.1031  0.0160  0.1013  149 HIS B CA  
6727 C C   . HIS B 152 ? 0.5077 0.6075 0.2519 0.1078  0.0164  0.1251  149 HIS B C   
6728 O O   . HIS B 152 ? 0.5674 0.6811 0.3037 0.1170  0.0078  0.1285  149 HIS B O   
6729 C CB  . HIS B 152 ? 0.4700 0.6108 0.2250 0.0910  0.0257  0.0925  149 HIS B CB  
6730 C CG  . HIS B 152 ? 0.5473 0.7190 0.2904 0.0922  0.0220  0.0869  149 HIS B CG  
6731 N ND1 . HIS B 152 ? 0.6066 0.8088 0.3591 0.0965  0.0126  0.0663  149 HIS B ND1 
6732 C CD2 . HIS B 152 ? 0.5415 0.7179 0.2641 0.0888  0.0268  0.0988  149 HIS B CD2 
6733 C CE1 . HIS B 152 ? 0.5805 0.8059 0.3196 0.0961  0.0118  0.0652  149 HIS B CE1 
6734 N NE2 . HIS B 152 ? 0.5442 0.7549 0.2636 0.0920  0.0200  0.0853  149 HIS B NE2 
6741 N N   . GLN B 153 ? 0.5344 0.6004 0.2742 0.1007  0.0266  0.1408  150 GLN B N   
6742 C CA  . GLN B 153 ? 0.5653 0.6044 0.2906 0.1037  0.0277  0.1631  150 GLN B CA  
6743 C C   . GLN B 153 ? 0.5628 0.5929 0.2947 0.1198  0.0157  0.1672  150 GLN B C   
6744 O O   . GLN B 153 ? 0.5971 0.6305 0.3161 0.1285  0.0096  0.1779  150 GLN B O   
6745 C CB  . GLN B 153 ? 0.6628 0.6651 0.3893 0.0912  0.0407  0.1739  150 GLN B CB  
6746 C CG  . GLN B 153 ? 0.7827 0.7536 0.4938 0.0891  0.0449  0.1958  150 GLN B CG  
6747 C CD  . GLN B 153 ? 1.0204 0.9501 0.7433 0.0817  0.0527  0.2016  150 GLN B CD  
6748 O OE1 . GLN B 153 ? 0.9065 0.8095 0.6346 0.0903  0.0478  0.2090  150 GLN B OE1 
6749 N NE2 . GLN B 153 ? 0.9415 0.8681 0.6709 0.0653  0.0650  0.1961  150 GLN B NE2 
6758 N N   . ILE B 154 ? 0.6565 0.6760 0.4086 0.1239  0.0124  0.1585  151 ILE B N   
6759 C CA  . ILE B 154 ? 0.6332 0.6453 0.3947 0.1384  0.0023  0.1603  151 ILE B CA  
6760 C C   . ILE B 154 ? 0.6105 0.6621 0.3727 0.1487  -0.0097 0.1498  151 ILE B C   
6761 O O   . ILE B 154 ? 0.6524 0.7078 0.4094 0.1602  -0.0170 0.1575  151 ILE B O   
6762 C CB  . ILE B 154 ? 0.5878 0.5827 0.3714 0.1387  0.0023  0.1510  151 ILE B CB  
6763 C CG1 . ILE B 154 ? 0.6368 0.5918 0.4213 0.1280  0.0142  0.1604  151 ILE B CG1 
6764 C CG2 . ILE B 154 ? 0.7144 0.7096 0.5100 0.1533  -0.0079 0.1488  151 ILE B CG2 
6765 C CD1 . ILE B 154 ? 0.7681 0.7043 0.5737 0.1280  0.0144  0.1514  151 ILE B CD1 
6777 N N   . LEU B 155 ? 0.5853 0.6670 0.3555 0.1444  -0.0119 0.1308  152 LEU B N   
6778 C CA  . LEU B 155 ? 0.6300 0.7518 0.4017 0.1502  -0.0217 0.1176  152 LEU B CA  
6779 C C   . LEU B 155 ? 0.7214 0.8587 0.4708 0.1468  -0.0189 0.1247  152 LEU B C   
6780 O O   . LEU B 155 ? 0.8004 0.9145 0.5330 0.1442  -0.0122 0.1439  152 LEU B O   
6781 C CB  . LEU B 155 ? 0.6506 0.7944 0.4393 0.1445  -0.0240 0.0938  152 LEU B CB  
6782 C CG  . LEU B 155 ? 0.6709 0.7939 0.4782 0.1441  -0.0237 0.0889  152 LEU B CG  
6783 C CD1 . LEU B 155 ? 0.6735 0.8210 0.4968 0.1389  -0.0281 0.0648  152 LEU B CD1 
6784 C CD2 . LEU B 155 ? 0.7342 0.8419 0.5515 0.1552  -0.0291 0.0955  152 LEU B CD2 
6796 N N   . THR B 156 ? 0.5875 1.0760 0.8667 0.0169  -0.0793 0.0389  153 THR B N   
6797 C CA  . THR B 156 ? 0.5325 1.0418 0.8255 0.0232  -0.0626 0.0298  153 THR B CA  
6798 C C   . THR B 156 ? 0.4626 0.9900 0.7509 -0.0026 -0.0505 0.0281  153 THR B C   
6799 O O   . THR B 156 ? 0.4263 0.9421 0.7031 -0.0081 -0.0373 0.0240  153 THR B O   
6800 C CB  . THR B 156 ? 0.3267 0.8668 0.6500 0.0474  -0.0647 0.0249  153 THR B CB  
6801 O OG1 . THR B 156 ? 0.3906 0.9712 0.7303 0.0339  -0.0661 0.0260  153 THR B OG1 
6802 C CG2 . THR B 156 ? 0.5176 1.0379 0.8433 0.0695  -0.0819 0.0291  153 THR B CG2 
6810 N N   . GLU B 157 ? 0.3074 0.8607 0.6020 -0.0189 -0.0552 0.0316  154 GLU B N   
6811 C CA  . GLU B 157 ? 0.4283 1.0035 0.7212 -0.0393 -0.0433 0.0294  154 GLU B CA  
6812 C C   . GLU B 157 ? 0.4367 0.9792 0.6964 -0.0667 -0.0400 0.0332  154 GLU B C   
6813 O O   . GLU B 157 ? 0.3371 0.8770 0.5867 -0.0767 -0.0274 0.0299  154 GLU B O   
6814 C CB  . GLU B 157 ? 0.4184 1.0353 0.7300 -0.0477 -0.0490 0.0318  154 GLU B CB  
6815 C CG  . GLU B 157 ? 0.3992 1.0580 0.7466 -0.0232 -0.0466 0.0255  154 GLU B CG  
6816 C CD  . GLU B 157 ? 0.4608 1.1659 0.8293 -0.0325 -0.0519 0.0277  154 GLU B CD  
6817 O OE1 . GLU B 157 ? 0.4821 1.1850 0.8359 -0.0581 -0.0586 0.0347  154 GLU B OE1 
6818 O OE2 . GLU B 157 ? 0.4767 1.2202 0.8758 -0.0140 -0.0491 0.0222  154 GLU B OE2 
6825 N N   . GLY B 158 ? 0.4628 0.9780 0.7028 -0.0793 -0.0516 0.0398  155 GLY B N   
6826 C CA  . GLY B 158 ? 0.3818 0.8595 0.5886 -0.1022 -0.0492 0.0422  155 GLY B CA  
6827 C C   . GLY B 158 ? 0.4278 0.8779 0.6244 -0.0943 -0.0401 0.0383  155 GLY B C   
6828 O O   . GLY B 158 ? 0.3401 0.7685 0.5153 -0.1101 -0.0329 0.0376  155 GLY B O   
6832 N N   . LEU B 159 ? 0.4028 0.8512 0.6129 -0.0696 -0.0412 0.0360  156 LEU B N   
6833 C CA  . LEU B 159 ? 0.3877 0.8164 0.5923 -0.0596 -0.0318 0.0316  156 LEU B CA  
6834 C C   . LEU B 159 ? 0.3473 0.7953 0.5591 -0.0587 -0.0166 0.0250  156 LEU B C   
6835 O O   . LEU B 159 ? 0.3300 0.7579 0.5262 -0.0655 -0.0075 0.0227  156 LEU B O   
6836 C CB  . LEU B 159 ? 0.4338 0.8500 0.6467 -0.0316 -0.0368 0.0304  156 LEU B CB  
6837 C CG  . LEU B 159 ? 0.4791 0.8592 0.6799 -0.0162 -0.0274 0.0246  156 LEU B CG  
6838 C CD1 . LEU B 159 ? 0.4580 0.7863 0.6256 -0.0295 -0.0269 0.0268  156 LEU B CD1 
6839 C CD2 . LEU B 159 ? 0.4892 0.8634 0.7009 0.0112  -0.0343 0.0239  156 LEU B CD2 
6851 N N   . GLU B 160 ? 0.3047 0.7914 0.5392 -0.0505 -0.0141 0.0219  157 GLU B N   
6852 C CA  . GLU B 160 ? 0.3464 0.8534 0.5870 -0.0489 0.0006  0.0150  157 GLU B CA  
6853 C C   . GLU B 160 ? 0.3293 0.8276 0.5467 -0.0780 0.0065  0.0175  157 GLU B C   
6854 O O   . GLU B 160 ? 0.3357 0.8246 0.5415 -0.0814 0.0177  0.0137  157 GLU B O   
6855 C CB  . GLU B 160 ? 0.3731 0.9256 0.6427 -0.0366 0.0011  0.0115  157 GLU B CB  
6856 C CG  . GLU B 160 ? 0.4285 0.9862 0.7192 -0.0032 -0.0008 0.0059  157 GLU B CG  
6857 C CD  . GLU B 160 ? 0.4147 1.0146 0.7352 0.0093  -0.0050 0.0040  157 GLU B CD  
6858 O OE1 . GLU B 160 ? 0.4724 1.1027 0.7991 -0.0087 -0.0049 0.0066  157 GLU B OE1 
6859 O OE2 . GLU B 160 ? 0.5307 1.1315 0.8674 0.0373  -0.0091 0.0000  157 GLU B OE2 
6866 N N   . LYS B 161 ? 0.3293 0.8268 0.5364 -0.0993 -0.0019 0.0242  158 LYS B N   
6867 C CA  . LYS B 161 ? 0.2554 0.7409 0.4371 -0.1269 0.0015  0.0273  158 LYS B CA  
6868 C C   . LYS B 161 ? 0.4035 0.8385 0.5550 -0.1359 0.0017  0.0289  158 LYS B C   
6869 O O   . LYS B 161 ? 0.3518 0.7723 0.4846 -0.1476 0.0091  0.0280  158 LYS B O   
6870 C CB  . LYS B 161 ? 0.4988 0.9946 0.6763 -0.1456 -0.0085 0.0337  158 LYS B CB  
6871 C CG  . LYS B 161 ? 0.6539 1.1222 0.7972 -0.1747 -0.0100 0.0385  158 LYS B CG  
6872 C CD  . LYS B 161 ? 0.6254 1.0441 0.7415 -0.1829 -0.0197 0.0426  158 LYS B CD  
6873 C CE  . LYS B 161 ? 0.7301 1.1172 0.8096 -0.2093 -0.0213 0.0465  158 LYS B CE  
6874 N NZ  . LYS B 161 ? 0.6395 0.9975 0.7010 -0.2100 -0.0135 0.0439  158 LYS B NZ  
6888 N N   . GLY B 162 ? 0.3258 0.7335 0.4719 -0.1301 -0.0067 0.0311  159 GLY B N   
6889 C CA  . GLY B 162 ? 0.3629 0.7235 0.4818 -0.1378 -0.0069 0.0320  159 GLY B CA  
6890 C C   . GLY B 162 ? 0.2856 0.6388 0.4055 -0.1264 0.0042  0.0269  159 GLY B C   
6891 O O   . GLY B 162 ? 0.3415 0.6625 0.4373 -0.1374 0.0073  0.0274  159 GLY B O   
6895 N N   . MET B 163 ? 0.2782 0.6571 0.4237 -0.1030 0.0091  0.0220  160 MET B N   
6896 C CA  . MET B 163 ? 0.2573 0.6229 0.3992 -0.0896 0.0196  0.0159  160 MET B CA  
6897 C C   . MET B 163 ? 0.3385 0.7201 0.4743 -0.1027 0.0306  0.0136  160 MET B C   
6898 O O   . MET B 163 ? 0.2536 0.6163 0.3752 -0.1033 0.0383  0.0110  160 MET B O   
6899 C CB  . MET B 163 ? 0.2845 0.6655 0.4496 -0.0600 0.0212  0.0102  160 MET B CB  
6900 C CG  . MET B 163 ? 0.2912 0.6355 0.4506 -0.0433 0.0119  0.0115  160 MET B CG  
6901 S SD  . MET B 163 ? 0.3350 0.6155 0.4591 -0.0528 0.0079  0.0148  160 MET B SD  
6902 C CE  . MET B 163 ? 0.4425 0.6997 0.5568 -0.0411 0.0182  0.0083  160 MET B CE  
6912 N N   . LYS B 164 ? 0.3162 0.7275 0.4586 -0.1124 0.0309  0.0146  161 LYS B N   
6913 C CA  . LYS B 164 ? 0.2967 0.7160 0.4267 -0.1265 0.0399  0.0131  161 LYS B CA  
6914 C C   . LYS B 164 ? 0.3868 0.7640 0.4809 -0.1504 0.0359  0.0190  161 LYS B C   
6915 O O   . LYS B 164 ? 0.3587 0.7181 0.4344 -0.1562 0.0423  0.0177  161 LYS B O   
6916 C CB  . LYS B 164 ? 0.3798 0.8435 0.5258 -0.1324 0.0409  0.0130  161 LYS B CB  
6917 C CG  . LYS B 164 ? 0.5786 1.0844 0.7573 -0.1075 0.0485  0.0047  161 LYS B CG  
6918 C CD  . LYS B 164 ? 0.6744 1.1702 0.8531 -0.0887 0.0591  -0.0035 161 LYS B CD  
6919 C CE  . LYS B 164 ? 0.6682 1.1573 0.8645 -0.0605 0.0548  -0.0069 161 LYS B CE  
6920 N NZ  . LYS B 164 ? 0.4766 0.9504 0.6694 -0.0420 0.0638  -0.0150 161 LYS B NZ  
6934 N N   . THR B 165 ? 0.3423 0.6987 0.4239 -0.1630 0.0244  0.0253  162 THR B N   
6935 C CA  . THR B 165 ? 0.3841 0.6928 0.4298 -0.1816 0.0188  0.0300  162 THR B CA  
6936 C C   . THR B 165 ? 0.3712 0.6432 0.4056 -0.1727 0.0208  0.0283  162 THR B C   
6937 O O   . THR B 165 ? 0.4170 0.6581 0.4254 -0.1827 0.0216  0.0298  162 THR B O   
6938 C CB  . THR B 165 ? 0.4459 0.7366 0.4809 -0.1920 0.0061  0.0352  162 THR B CB  
6939 O OG1 . THR B 165 ? 0.5143 0.8408 0.5594 -0.2015 0.0040  0.0373  162 THR B OG1 
6940 C CG2 . THR B 165 ? 0.5520 0.7901 0.5481 -0.2084 -0.0006 0.0390  162 THR B CG2 
6948 N N   . PHE B 166 ? 0.3139 0.5883 0.3667 -0.1543 0.0206  0.0258  163 PHE B N   
6949 C CA  . PHE B 166 ? 0.3241 0.5577 0.3642 -0.1395 0.0213  0.0230  163 PHE B CA  
6950 C C   . PHE B 166 ? 0.3101 0.5474 0.3456 -0.1374 0.0320  0.0193  163 PHE B C   
6951 O O   . PHE B 166 ? 0.3076 0.5078 0.3186 -0.1419 0.0311  0.0203  163 PHE B O   
6952 C CB  . PHE B 166 ? 0.3239 0.5576 0.3823 -0.1143 0.0186  0.0196  163 PHE B CB  
6953 C CG  . PHE B 166 ? 0.3391 0.5346 0.3872 -0.0981 0.0188  0.0164  163 PHE B CG  
6954 C CD1 . PHE B 166 ? 0.3928 0.5470 0.4214 -0.1001 0.0116  0.0184  163 PHE B CD1 
6955 C CD2 . PHE B 166 ? 0.3229 0.5253 0.3816 -0.0802 0.0259  0.0109  163 PHE B CD2 
6956 C CE1 . PHE B 166 ? 0.4211 0.5459 0.4433 -0.0858 0.0118  0.0155  163 PHE B CE1 
6957 C CE2 . PHE B 166 ? 0.3679 0.5364 0.4170 -0.0674 0.0252  0.0085  163 PHE B CE2 
6958 C CZ  . PHE B 166 ? 0.3298 0.4624 0.3625 -0.0706 0.0182  0.0111  163 PHE B CZ  
6968 N N   . GLY B 167 ? 0.3166 0.5997 0.3748 -0.1307 0.0417  0.0148  164 GLY B N   
6969 C CA  . GLY B 167 ? 0.2996 0.5870 0.3519 -0.1278 0.0529  0.0099  164 GLY B CA  
6970 C C   . GLY B 167 ? 0.3516 0.6269 0.3767 -0.1522 0.0540  0.0140  164 GLY B C   
6971 O O   . GLY B 167 ? 0.3366 0.5889 0.3415 -0.1552 0.0580  0.0133  164 GLY B O   
6975 N N   . GLU B 168 ? 0.3160 0.5996 0.3362 -0.1687 0.0482  0.0186  165 GLU B N   
6976 C CA  . GLU B 168 ? 0.3413 0.6056 0.3312 -0.1913 0.0456  0.0230  165 GLU B CA  
6977 C C   . GLU B 168 ? 0.4173 0.6242 0.3759 -0.1996 0.0354  0.0285  165 GLU B C   
6978 O O   . GLU B 168 ? 0.4587 0.6386 0.3907 -0.2092 0.0346  0.0304  165 GLU B O   
6979 C CB  . GLU B 168 ? 0.4005 0.6892 0.3922 -0.2072 0.0414  0.0262  165 GLU B CB  
6980 C CG  . GLU B 168 ? 0.4472 0.7938 0.4701 -0.1988 0.0509  0.0207  165 GLU B CG  
6981 C CD  . GLU B 168 ? 0.6736 1.0465 0.7019 -0.2131 0.0456  0.0244  165 GLU B CD  
6982 O OE1 . GLU B 168 ? 0.7018 1.0459 0.7086 -0.2290 0.0344  0.0311  165 GLU B OE1 
6983 O OE2 . GLU B 168 ? 0.6595 1.0812 0.7125 -0.2082 0.0524  0.0204  165 GLU B OE2 
6990 N N   . THR B 169 ? 0.3748 0.5615 0.3355 -0.1950 0.0269  0.0307  166 THR B N   
6991 C CA  . THR B 169 ? 0.4032 0.5346 0.3351 -0.2001 0.0166  0.0348  166 THR B CA  
6992 C C   . THR B 169 ? 0.4479 0.5549 0.3714 -0.1908 0.0202  0.0334  166 THR B C   
6993 O O   . THR B 169 ? 0.4668 0.5335 0.3612 -0.1978 0.0138  0.0366  166 THR B O   
6994 C CB  . THR B 169 ? 0.4336 0.5524 0.3719 -0.1949 0.0083  0.0356  166 THR B CB  
6995 O OG1 . THR B 169 ? 0.4660 0.6053 0.4077 -0.2058 0.0041  0.0377  166 THR B OG1 
6996 C CG2 . THR B 169 ? 0.4982 0.5598 0.4082 -0.1966 -0.0020 0.0378  166 THR B CG2 
7004 N N   . LEU B 170 ? 0.3487 0.4745 0.2954 -0.1683 0.0273  0.0269  167 LEU B N   
7005 C CA  . LEU B 170 ? 0.3589 0.4610 0.2988 -0.1530 0.0287  0.0233  167 LEU B CA  
7006 C C   . LEU B 170 ? 0.3882 0.5063 0.3212 -0.1589 0.0390  0.0213  167 LEU B C   
7007 O O   . LEU B 170 ? 0.3374 0.4357 0.2621 -0.1482 0.0398  0.0183  167 LEU B O   
7008 C CB  . LEU B 170 ? 0.3184 0.4275 0.2826 -0.1268 0.0300  0.0171  167 LEU B CB  
7009 C CG  . LEU B 170 ? 0.3169 0.3937 0.2791 -0.1161 0.0200  0.0178  167 LEU B CG  
7010 C CD1 . LEU B 170 ? 0.4187 0.5010 0.3832 -0.1260 0.0142  0.0212  167 LEU B CD1 
7011 C CD2 . LEU B 170 ? 0.3430 0.4222 0.3230 -0.0933 0.0219  0.0125  167 LEU B CD2 
7023 N N   . ASN B 171 ? 0.3182 0.4726 0.2537 -0.1763 0.0470  0.0225  168 ASN B N   
7024 C CA  . ASN B 171 ? 0.3259 0.5004 0.2567 -0.1794 0.0577  0.0184  168 ASN B CA  
7025 C C   . ASN B 171 ? 0.3542 0.5442 0.3017 -0.1567 0.0679  0.0092  168 ASN B C   
7026 O O   . ASN B 171 ? 0.3500 0.5273 0.2817 -0.1548 0.0725  0.0061  168 ASN B O   
7027 C CB  . ASN B 171 ? 0.3685 0.5043 0.2623 -0.1947 0.0519  0.0233  168 ASN B CB  
7028 C CG  . ASN B 171 ? 0.4695 0.6285 0.3564 -0.2041 0.0605  0.0200  168 ASN B CG  
7029 O OD1 . ASN B 171 ? 0.5818 0.7813 0.4853 -0.2081 0.0666  0.0171  168 ASN B OD1 
7030 N ND2 . ASN B 171 ? 0.4948 0.6277 0.3559 -0.2085 0.0603  0.0206  168 ASN B ND2 
7037 N N   . ILE B 172 ? 0.3416 0.5554 0.3198 -0.1376 0.0692  0.0043  169 ILE B N   
7038 C CA  . ILE B 172 ? 0.3272 0.5533 0.3224 -0.1126 0.0763  -0.0055 169 ILE B CA  
7039 C C   . ILE B 172 ? 0.3070 0.5741 0.3066 -0.1158 0.0919  -0.0124 169 ILE B C   
7040 O O   . ILE B 172 ? 0.3299 0.6276 0.3369 -0.1277 0.0944  -0.0109 169 ILE B O   
7041 C CB  . ILE B 172 ? 0.3356 0.5774 0.3604 -0.0938 0.0723  -0.0077 169 ILE B CB  
7042 C CG1 . ILE B 172 ? 0.3308 0.5338 0.3495 -0.0913 0.0585  -0.0018 169 ILE B CG1 
7043 C CG2 . ILE B 172 ? 0.3175 0.5677 0.3575 -0.0677 0.0782  -0.0176 169 ILE B CG2 
7044 C CD1 . ILE B 172 ? 0.4269 0.5856 0.4275 -0.0835 0.0540  -0.0024 169 ILE B CD1 
7056 N N   . ALA B 173 ? 0.3146 0.5731 0.3077 -0.1020 0.0986  -0.0207 170 ALA B N   
7057 C CA  . ALA B 173 ? 0.2768 0.5687 0.2715 -0.1015 0.1133  -0.0292 170 ALA B CA  
7058 C C   . ALA B 173 ? 0.3134 0.6498 0.3437 -0.0841 0.1178  -0.0358 170 ALA B C   
7059 O O   . ALA B 173 ? 0.3440 0.6851 0.3958 -0.0650 0.1143  -0.0384 170 ALA B O   
7060 C CB  . ALA B 173 ? 0.3620 0.6302 0.3400 -0.0887 0.1184  -0.0376 170 ALA B CB  
7066 N N   . PRO B 174 ? 0.3317 0.7007 0.3684 -0.0901 0.1247  -0.0384 171 PRO B N   
7067 C CA  . PRO B 174 ? 0.3742 0.7861 0.4452 -0.0727 0.1281  -0.0444 171 PRO B CA  
7068 C C   . PRO B 174 ? 0.3874 0.7986 0.4734 -0.0408 0.1320  -0.0556 171 PRO B C   
7069 O O   . PRO B 174 ? 0.4106 0.8373 0.5233 -0.0228 0.1270  -0.0571 171 PRO B O   
7070 C CB  . PRO B 174 ? 0.4126 0.8553 0.4811 -0.0848 0.1378  -0.0473 171 PRO B CB  
7071 C CG  . PRO B 174 ? 0.3888 0.8069 0.4252 -0.1147 0.1339  -0.0381 171 PRO B CG  
7072 C CD  . PRO B 174 ? 0.3287 0.6983 0.3421 -0.1133 0.1288  -0.0356 171 PRO B CD  
7080 N N   . ILE B 175 ? 0.4086 0.7983 0.4749 -0.0336 0.1393  -0.0634 172 ILE B N   
7081 C CA  . ILE B 175 ? 0.5162 0.8963 0.5903 -0.0036 0.1417  -0.0749 172 ILE B CA  
7082 C C   . ILE B 175 ? 0.5226 0.8850 0.6085 0.0095  0.1302  -0.0718 172 ILE B C   
7083 O O   . ILE B 175 ? 0.5235 0.8935 0.6312 0.0339  0.1268  -0.0768 172 ILE B O   
7084 C CB  . ILE B 175 ? 0.6014 0.9507 0.6442 -0.0032 0.1487  -0.0822 172 ILE B CB  
7085 C CG1 . ILE B 175 ? 0.6301 0.9684 0.6780 0.0277  0.1517  -0.0958 172 ILE B CG1 
7086 C CG2 . ILE B 175 ? 0.5781 0.8872 0.5940 -0.0190 0.1415  -0.0749 172 ILE B CG2 
7087 C CD1 . ILE B 175 ? 0.7321 1.1061 0.8105 0.0477  0.1554  -0.1022 172 ILE B CD1 
7099 N N   . ASP B 176 ? 0.4202 0.7531 0.4904 -0.0067 0.1216  -0.0619 173 ASP B N   
7100 C CA  . ASP B 176 ? 0.4049 0.7058 0.4809 0.0032  0.1062  -0.0554 173 ASP B CA  
7101 C C   . ASP B 176 ? 0.3598 0.6923 0.4634 0.0036  0.1004  -0.0498 173 ASP B C   
7102 O O   . ASP B 176 ? 0.4610 0.7925 0.5820 0.0236  0.0934  -0.0511 173 ASP B O   
7103 C CB  . ASP B 176 ? 0.3327 0.5875 0.3823 -0.0139 0.0969  -0.0458 173 ASP B CB  
7104 C CG  . ASP B 176 ? 0.3723 0.5904 0.3965 -0.0108 0.0983  -0.0506 173 ASP B CG  
7105 O OD1 . ASP B 176 ? 0.3752 0.5852 0.4016 0.0094  0.1007  -0.0598 173 ASP B OD1 
7106 O OD2 . ASP B 176 ? 0.3265 0.5230 0.3267 -0.0289 0.0965  -0.0452 173 ASP B OD2 
7111 N N   . ALA B 177 ? 0.3864 0.7450 0.4920 -0.0198 0.1018  -0.0428 174 ALA B N   
7112 C CA  . ALA B 177 ? 0.4850 0.8762 0.6160 -0.0216 0.0958  -0.0376 174 ALA B CA  
7113 C C   . ALA B 177 ? 0.5083 0.9313 0.6661 0.0016  0.0980  -0.0453 174 ALA B C   
7114 O O   . ALA B 177 ? 0.5181 0.9546 0.6973 0.0117  0.0890  -0.0425 174 ALA B O   
7115 C CB  . ALA B 177 ? 0.4491 0.8509 0.5705 -0.0511 0.0946  -0.0290 174 ALA B CB  
7121 N N   . LYS B 178 ? 0.4420 0.8753 0.5976 0.0103  0.1093  -0.0550 175 LYS B N   
7122 C CA  . LYS B 178 ? 0.5819 1.0416 0.7616 0.0344  0.1117  -0.0634 175 LYS B CA  
7123 C C   . LYS B 178 ? 0.6035 1.0389 0.7904 0.0631  0.1040  -0.0677 175 LYS B C   
7124 O O   . LYS B 178 ? 0.5150 0.9641 0.7245 0.0784  0.0956  -0.0667 175 LYS B O   
7125 C CB  . LYS B 178 ? 0.5805 1.0526 0.7525 0.0366  0.1263  -0.0734 175 LYS B CB  
7126 C CG  . LYS B 178 ? 0.7464 1.2337 0.9371 0.0662  0.1304  -0.0850 175 LYS B CG  
7127 C CD  . LYS B 178 ? 0.7207 1.2167 0.8988 0.0657  0.1460  -0.0951 175 LYS B CD  
7128 C CE  . LYS B 178 ? 0.6228 1.1236 0.8135 0.0969  0.1507  -0.1083 175 LYS B CE  
7129 N NZ  . LYS B 178 ? 0.9476 1.4511 1.1211 0.0957  0.1666  -0.1187 175 LYS B NZ  
7143 N N   . MET B 179 ? 0.4602 0.8569 0.6259 0.0699  0.1055  -0.0722 176 MET B N   
7144 C CA  . MET B 179 ? 0.5830 0.9499 0.7504 0.0961  0.0972  -0.0763 176 MET B CA  
7145 C C   . MET B 179 ? 0.5696 0.9253 0.7451 0.0951  0.0821  -0.0655 176 MET B C   
7146 O O   . MET B 179 ? 0.6049 0.9580 0.7948 0.1159  0.0726  -0.0659 176 MET B O   
7147 C CB  . MET B 179 ? 0.5242 0.8473 0.6623 0.0991  0.1008  -0.0825 176 MET B CB  
7148 C CG  . MET B 179 ? 0.5371 0.8618 0.6664 0.1098  0.1130  -0.0955 176 MET B CG  
7149 S SD  . MET B 179 ? 0.5701 0.8445 0.6606 0.1083  0.1170  -0.1029 176 MET B SD  
7150 C CE  . MET B 179 ? 0.6698 0.8935 0.7563 0.1338  0.1018  -0.1044 176 MET B CE  
7160 N N   . MET B 180 ? 0.5176 0.8581 0.6796 0.0695  0.0777  -0.0544 177 MET B N   
7161 C CA  . MET B 180 ? 0.6638 0.9842 0.8267 0.0649  0.0631  -0.0433 177 MET B CA  
7162 C C   . MET B 180 ? 0.5763 0.9388 0.7686 0.0706  0.0571  -0.0402 177 MET B C   
7163 O O   . MET B 180 ? 0.5176 0.8646 0.7143 0.0790  0.0442  -0.0346 177 MET B O   
7164 C CB  . MET B 180 ? 0.6945 0.9961 0.8382 0.0371  0.0611  -0.0340 177 MET B CB  
7165 C CG  . MET B 180 ? 0.6471 0.8996 0.7626 0.0323  0.0607  -0.0337 177 MET B CG  
7166 S SD  . MET B 180 ? 0.6724 0.9189 0.7665 0.0024  0.0649  -0.0282 177 MET B SD  
7167 C CE  . MET B 180 ? 0.7131 0.9440 0.8054 -0.0107 0.0519  -0.0166 177 MET B CE  
7177 N N   . SER B 181 ? 0.5947 1.0092 0.8055 0.0642  0.0654  -0.0430 178 SER B N   
7178 C CA  . SER B 181 ? 0.5651 1.0115 0.7980 0.0627  0.0576  -0.0378 178 SER B CA  
7179 C C   . SER B 181 ? 0.5686 1.0336 0.8223 0.0884  0.0570  -0.0450 178 SER B C   
7180 O O   . SER B 181 ? 0.5172 1.0091 0.7914 0.0904  0.0492  -0.0412 178 SER B O   
7181 C CB  . SER B 181 ? 0.5143 0.9879 0.7454 0.0342  0.0630  -0.0333 178 SER B CB  
7182 O OG  . SER B 181 ? 0.5888 1.0822 0.8197 0.0341  0.0765  -0.0413 178 SER B OG  
7188 N N   . GLN B 182 ? 0.6299 1.0795 0.8779 0.1078  0.0642  -0.0555 179 GLN B N   
7189 C CA  . GLN B 182 ? 0.5995 1.0629 0.8649 0.1331  0.0641  -0.0635 179 GLN B CA  
7190 C C   . GLN B 182 ? 0.6325 1.0872 0.9115 0.1501  0.0470  -0.0580 179 GLN B C   
7191 O O   . GLN B 182 ? 0.6170 1.0309 0.8822 0.1579  0.0375  -0.0547 179 GLN B O   
7192 C CB  . GLN B 182 ? 0.7151 1.1488 0.9645 0.1508  0.0722  -0.0751 179 GLN B CB  
7193 C CG  . GLN B 182 ? 0.7714 1.2225 1.0360 0.1740  0.0767  -0.0856 179 GLN B CG  
7194 C CD  . GLN B 182 ? 0.7927 1.2772 1.0585 0.1650  0.0943  -0.0935 179 GLN B CD  
7195 O OE1 . GLN B 182 ? 0.7502 1.2204 0.9935 0.1521  0.1047  -0.0966 179 GLN B OE1 
7196 N NE2 . GLN B 182 ? 0.7555 1.2848 1.0469 0.1716  0.0974  -0.0968 179 GLN B NE2 
7205 N N   . PRO B 183 ? 0.5118 1.0027 0.8162 0.1557  0.0420  -0.0566 180 PRO B N   
7206 C CA  . PRO B 183 ? 0.4845 0.9642 0.8000 0.1741  0.0249  -0.0517 180 PRO B CA  
7207 C C   . PRO B 183 ? 0.5989 1.0403 0.9056 0.2026  0.0219  -0.0591 180 PRO B C   
7208 O O   . PRO B 183 ? 0.5995 1.0425 0.9045 0.2140  0.0334  -0.0704 180 PRO B O   
7209 C CB  . PRO B 183 ? 0.4514 0.9833 0.7973 0.1751  0.0235  -0.0514 180 PRO B CB  
7210 C CG  . PRO B 183 ? 0.4859 1.0504 0.8313 0.1455  0.0346  -0.0493 180 PRO B CG  
7211 C CD  . PRO B 183 ? 0.3920 0.9354 0.7146 0.1410  0.0497  -0.0568 180 PRO B CD  
7219 N N   . ALA B 184 ? 0.4949 0.8990 0.7929 0.2125  0.0057  -0.0523 181 ALA B N   
7220 C CA  . ALA B 184 ? 0.5742 0.9402 0.8639 0.2390  -0.0013 -0.0570 181 ALA B CA  
7221 C C   . ALA B 184 ? 0.5513 0.9491 0.8677 0.2586  -0.0036 -0.0617 181 ALA B C   
7222 O O   . ALA B 184 ? 0.5611 1.0039 0.9026 0.2525  -0.0065 -0.0571 181 ALA B O   
7223 C CB  . ALA B 184 ? 0.5986 0.9185 0.8715 0.2415  -0.0196 -0.0463 181 ALA B CB  
7229 N N   . ASP B 185 ? 0.7043 1.0775 1.0144 0.2822  -0.0026 -0.0710 182 ASP B N   
7230 C CA  . ASP B 185 ? 0.7147 1.1170 1.0496 0.3042  -0.0032 -0.0776 182 ASP B CA  
7231 C C   . ASP B 185 ? 0.7695 1.1614 1.1145 0.3192  -0.0243 -0.0685 182 ASP B C   
7232 O O   . ASP B 185 ? 0.6975 1.1025 1.0599 0.3422  -0.0276 -0.0740 182 ASP B O   
7233 C CB  . ASP B 185 ? 0.8497 1.2293 1.1721 0.3234  0.0070  -0.0924 182 ASP B CB  
7234 C CG  . ASP B 185 ? 0.8813 1.1892 1.1703 0.3333  -0.0031 -0.0917 182 ASP B CG  
7235 O OD1 . ASP B 185 ? 0.9562 1.2330 1.2325 0.3259  -0.0177 -0.0795 182 ASP B OD1 
7236 O OD2 . ASP B 185 ? 0.9831 1.2653 1.2571 0.3469  0.0038  -0.1034 182 ASP B OD2 
7241 N N   . THR B 186 ? 0.6358 1.0064 0.9706 0.3064  -0.0385 -0.0547 183 THR B N   
7242 C CA  . THR B 186 ? 0.6397 0.9986 0.9802 0.3166  -0.0595 -0.0439 183 THR B CA  
7243 C C   . THR B 186 ? 0.6285 1.0114 0.9777 0.2939  -0.0678 -0.0307 183 THR B C   
7244 O O   . THR B 186 ? 0.5851 0.9613 0.9195 0.2718  -0.0626 -0.0272 183 THR B O   
7245 C CB  . THR B 186 ? 0.6434 0.9310 0.9501 0.3254  -0.0725 -0.0391 183 THR B CB  
7246 O OG1 . THR B 186 ? 0.7572 1.0129 1.0359 0.3067  -0.0665 -0.0376 183 THR B OG1 
7247 C CG2 . THR B 186 ? 0.6920 0.9523 0.9913 0.3515  -0.0711 -0.0502 183 THR B CG2 
7255 N N   . GLU B 187 ? 0.4645 0.8731 0.8361 0.2997  -0.0819 -0.0233 184 GLU B N   
7256 C CA  . GLU B 187 ? 0.5148 0.9385 0.8904 0.2788  -0.0933 -0.0100 184 GLU B CA  
7257 C C   . GLU B 187 ? 0.5577 0.9286 0.8984 0.2663  -0.1018 -0.0004 184 GLU B C   
7258 O O   . GLU B 187 ? 0.5207 0.8989 0.8545 0.2425  -0.1009 0.0054  184 GLU B O   
7259 C CB  . GLU B 187 ? 0.5279 0.9711 0.9257 0.2904  -0.1119 -0.0019 184 GLU B CB  
7260 C CG  . GLU B 187 ? 0.6496 1.0766 1.0346 0.2735  -0.1302 0.0142  184 GLU B CG  
7261 C CD  . GLU B 187 ? 0.8872 1.3448 1.2972 0.2779  -0.1480 0.0231  184 GLU B CD  
7262 O OE1 . GLU B 187 ? 0.8541 1.3509 1.2954 0.2940  -0.1458 0.0166  184 GLU B OE1 
7263 O OE2 . GLU B 187 ? 0.7056 1.1481 1.1030 0.2648  -0.1646 0.0366  184 GLU B OE2 
7270 N N   . GLU B 188 ? 0.6295 0.9461 0.9467 0.2817  -0.1108 0.0016  185 GLU B N   
7271 C CA  . GLU B 188 ? 0.6326 0.8975 0.9152 0.2702  -0.1202 0.0117  185 GLU B CA  
7272 C C   . GLU B 188 ? 0.6419 0.8880 0.9045 0.2570  -0.1051 0.0055  185 GLU B C   
7273 O O   . GLU B 188 ? 0.5954 0.8285 0.8413 0.2379  -0.1074 0.0127  185 GLU B O   
7274 C CB  . GLU B 188 ? 0.6916 0.9037 0.9532 0.2886  -0.1342 0.0158  185 GLU B CB  
7275 C CG  . GLU B 188 ? 0.8092 1.0368 1.0874 0.2996  -0.1522 0.0251  185 GLU B CG  
7276 C CD  . GLU B 188 ? 0.8656 1.0684 1.1424 0.3276  -0.1592 0.0210  185 GLU B CD  
7277 O OE1 . GLU B 188 ? 0.8258 0.9983 1.0880 0.3382  -0.1499 0.0101  185 GLU B OE1 
7278 O OE2 . GLU B 188 ? 0.8511 1.0646 1.1411 0.3388  -0.1746 0.0286  185 GLU B OE2 
7285 N N   . GLY B 189 ? 0.5792 0.8245 0.8427 0.2669  -0.0899 -0.0079 186 GLY B N   
7286 C CA  . GLY B 189 ? 0.5429 0.7778 0.7909 0.2537  -0.0750 -0.0139 186 GLY B CA  
7287 C C   . GLY B 189 ? 0.5022 0.7820 0.7638 0.2310  -0.0662 -0.0122 186 GLY B C   
7288 O O   . GLY B 189 ? 0.5399 0.8064 0.7851 0.2151  -0.0607 -0.0108 186 GLY B O   
7292 N N   . ARG B 190 ? 0.4386 0.7713 0.7296 0.2283  -0.0651 -0.0122 187 ARG B N   
7293 C CA  . ARG B 190 ? 0.4148 0.7874 0.7158 0.2033  -0.0586 -0.0092 187 ARG B CA  
7294 C C   . ARG B 190 ? 0.3327 0.6922 0.6216 0.1874  -0.0729 0.0040  187 ARG B C   
7295 O O   . ARG B 190 ? 0.4166 0.7818 0.6964 0.1655  -0.0674 0.0069  187 ARG B O   
7296 C CB  . ARG B 190 ? 0.3602 0.7903 0.6936 0.2030  -0.0547 -0.0123 187 ARG B CB  
7297 C CG  . ARG B 190 ? 0.4659 0.9182 0.8106 0.2130  -0.0370 -0.0260 187 ARG B CG  
7298 C CD  . ARG B 190 ? 0.4314 0.9454 0.8038 0.2021  -0.0294 -0.0282 187 ARG B CD  
7299 N NE  . ARG B 190 ? 0.3713 0.9088 0.7698 0.2220  -0.0390 -0.0286 187 ARG B NE  
7300 C CZ  . ARG B 190 ? 0.3841 0.9267 0.7938 0.2469  -0.0341 -0.0385 187 ARG B CZ  
7301 N NH1 . ARG B 190 ? 0.4620 0.9930 0.8601 0.2531  -0.0181 -0.0499 187 ARG B NH1 
7302 N NH2 . ARG B 190 ? 0.4103 0.9699 0.8430 0.2661  -0.0460 -0.0372 187 ARG B NH2 
7316 N N   . ILE B 191 ? 0.4799 0.8221 0.7671 0.1972  -0.0916 0.0126  188 ILE B N   
7317 C CA  . ILE B 191 ? 0.3927 0.7163 0.6623 0.1824  -0.1059 0.0252  188 ILE B CA  
7318 C C   . ILE B 191 ? 0.5013 0.7820 0.7396 0.1753  -0.1019 0.0260  188 ILE B C   
7319 O O   . ILE B 191 ? 0.4432 0.7167 0.6659 0.1495  -0.0985 0.0314  188 ILE B O   
7320 C CB  . ILE B 191 ? 0.4319 0.7354 0.6988 0.1951  -0.1269 0.0348  188 ILE B CB  
7321 C CG1 . ILE B 191 ? 0.4383 0.7894 0.7373 0.1975  -0.1335 0.0362  188 ILE B CG1 
7322 C CG2 . ILE B 191 ? 0.4652 0.7383 0.7040 0.1798  -0.1408 0.0474  188 ILE B CG2 
7323 C CD1 . ILE B 191 ? 0.4208 0.7558 0.7216 0.2148  -0.1534 0.0450  188 ILE B CD1 
7335 N N   . GLU B 192 ? 0.5274 0.7672 0.7506 0.1910  -0.0993 0.0207  189 GLU B N   
7336 C CA  . GLU B 192 ? 0.5708 0.7612 0.7614 0.1782  -0.0931 0.0215  189 GLU B CA  
7337 C C   . GLU B 192 ? 0.4391 0.6457 0.6296 0.1578  -0.0738 0.0159  189 GLU B C   
7338 O O   . GLU B 192 ? 0.3912 0.5724 0.5596 0.1361  -0.0696 0.0202  189 GLU B O   
7339 C CB  . GLU B 192 ? 0.5337 0.6821 0.7105 0.2000  -0.0948 0.0155  189 GLU B CB  
7340 C CG  . GLU B 192 ? 0.6912 0.7880 0.8347 0.1855  -0.0880 0.0159  189 GLU B CG  
7341 C CD  . GLU B 192 ? 0.8666 0.9225 0.9820 0.1702  -0.0998 0.0288  189 GLU B CD  
7342 O OE1 . GLU B 192 ? 0.9016 0.9192 0.9915 0.1575  -0.0950 0.0298  189 GLU B OE1 
7343 O OE2 . GLU B 192 ? 0.9417 1.0052 1.0601 0.1701  -0.1138 0.0379  189 GLU B OE2 
7350 N N   . GLN B 193 ? 0.4674 0.7162 0.6816 0.1646  -0.0620 0.0061  190 GLN B N   
7351 C CA  . GLN B 193 ? 0.4236 0.6824 0.6337 0.1457  -0.0445 0.0011  190 GLN B CA  
7352 C C   . GLN B 193 ? 0.3712 0.6510 0.5821 0.1187  -0.0443 0.0084  190 GLN B C   
7353 O O   . GLN B 193 ? 0.3501 0.6109 0.5424 0.0983  -0.0366 0.0097  190 GLN B O   
7354 C CB  . GLN B 193 ? 0.5339 0.8311 0.7659 0.1596  -0.0317 -0.0114 190 GLN B CB  
7355 C CG  . GLN B 193 ? 0.6375 0.9732 0.8782 0.1392  -0.0167 -0.0145 190 GLN B CG  
7356 C CD  . GLN B 193 ? 0.8652 1.2463 1.1305 0.1493  -0.0069 -0.0240 190 GLN B CD  
7357 O OE1 . GLN B 193 ? 0.7059 1.0811 0.9781 0.1719  -0.0090 -0.0298 190 GLN B OE1 
7358 N NE2 . GLN B 193 ? 0.8196 1.2363 1.0921 0.1286  0.0040  -0.0247 190 GLN B NE2 
7367 N N   . TYR B 194 ? 0.3332 0.6494 0.5640 0.1186  -0.0540 0.0134  191 TYR B N   
7368 C CA  . TYR B 194 ? 0.3217 0.6506 0.5485 0.0928  -0.0571 0.0210  191 TYR B CA  
7369 C C   . TYR B 194 ? 0.3785 0.6577 0.5739 0.0800  -0.0638 0.0288  191 TYR B C   
7370 O O   . TYR B 194 ? 0.2973 0.5667 0.4772 0.0577  -0.0590 0.0310  191 TYR B O   
7371 C CB  . TYR B 194 ? 0.3192 0.6950 0.5727 0.0966  -0.0690 0.0253  191 TYR B CB  
7372 C CG  . TYR B 194 ? 0.3195 0.6910 0.5603 0.0735  -0.0789 0.0352  191 TYR B CG  
7373 C CD1 . TYR B 194 ? 0.4030 0.7388 0.6244 0.0745  -0.0932 0.0434  191 TYR B CD1 
7374 C CD2 . TYR B 194 ? 0.5465 0.9455 0.7904 0.0488  -0.0737 0.0361  191 TYR B CD2 
7375 C CE1 . TYR B 194 ? 0.3974 0.7271 0.6038 0.0533  -0.1011 0.0511  191 TYR B CE1 
7376 C CE2 . TYR B 194 ? 0.4992 0.8895 0.7277 0.0276  -0.0828 0.0439  191 TYR B CE2 
7377 C CZ  . TYR B 194 ? 0.5557 0.9118 0.7656 0.0307  -0.0960 0.0508  191 TYR B CZ  
7378 O OH  . TYR B 194 ? 0.6481 0.9938 0.8396 0.0098  -0.1045 0.0575  191 TYR B OH  
7388 N N   . LYS B 195 ? 0.3593 0.6070 0.5440 0.0938  -0.0752 0.0330  192 LYS B N   
7389 C CA  . LYS B 195 ? 0.4394 0.6430 0.5939 0.0812  -0.0806 0.0402  192 LYS B CA  
7390 C C   . LYS B 195 ? 0.4285 0.6023 0.5631 0.0701  -0.0670 0.0361  192 LYS B C   
7391 O O   . LYS B 195 ? 0.3435 0.5003 0.4597 0.0517  -0.0649 0.0392  192 LYS B O   
7392 C CB  . LYS B 195 ? 0.4983 0.6717 0.6431 0.0981  -0.0946 0.0453  192 LYS B CB  
7393 C CG  . LYS B 195 ? 0.5913 0.7877 0.7522 0.1102  -0.1122 0.0514  192 LYS B CG  
7394 C CD  . LYS B 195 ? 0.8107 0.9849 0.9492 0.0970  -0.1263 0.0630  192 LYS B CD  
7395 C CE  . LYS B 195 ? 0.7776 0.9690 0.9113 0.0708  -0.1222 0.0652  192 LYS B CE  
7396 N NZ  . LYS B 195 ? 0.6778 0.8348 0.7792 0.0546  -0.1292 0.0735  192 LYS B NZ  
7410 N N   . ARG B 196 ? 0.3464 0.5136 0.4844 0.0822  -0.0583 0.0284  193 ARG B N   
7411 C CA  . ARG B 196 ? 0.4185 0.5601 0.5398 0.0732  -0.0467 0.0243  193 ARG B CA  
7412 C C   . ARG B 196 ? 0.2897 0.4499 0.4125 0.0547  -0.0366 0.0222  193 ARG B C   
7413 O O   . ARG B 196 ? 0.2779 0.4161 0.3831 0.0407  -0.0324 0.0231  193 ARG B O   
7414 C CB  . ARG B 196 ? 0.4573 0.5914 0.5824 0.0908  -0.0410 0.0162  193 ARG B CB  
7415 C CG  . ARG B 196 ? 0.4625 0.5646 0.5685 0.0844  -0.0328 0.0129  193 ARG B CG  
7416 C CD  . ARG B 196 ? 0.5279 0.6210 0.6356 0.1028  -0.0291 0.0044  193 ARG B CD  
7417 N NE  . ARG B 196 ? 0.6566 0.7890 0.7858 0.1119  -0.0211 -0.0037 193 ARG B NE  
7418 C CZ  . ARG B 196 ? 0.7201 0.8845 0.8589 0.0988  -0.0118 -0.0055 193 ARG B CZ  
7419 N NH1 . ARG B 196 ? 0.7137 0.8696 0.8403 0.0776  -0.0083 -0.0015 193 ARG B NH1 
7420 N NH2 . ARG B 196 ? 0.7392 0.9449 0.8997 0.1070  -0.0060 -0.0116 193 ARG B NH2 
7434 N N   . THR B 197 ? 0.2817 0.4826 0.4249 0.0542  -0.0333 0.0194  194 THR B N   
7435 C CA  . THR B 197 ? 0.2911 0.5058 0.4320 0.0344  -0.0254 0.0186  194 THR B CA  
7436 C C   . THR B 197 ? 0.2110 0.4171 0.3393 0.0171  -0.0324 0.0254  194 THR B C   
7437 O O   . THR B 197 ? 0.2172 0.4064 0.3293 0.0019  -0.0276 0.0251  194 THR B O   
7438 C CB  . THR B 197 ? 0.2389 0.5019 0.4035 0.0345  -0.0206 0.0150  194 THR B CB  
7439 O OG1 . THR B 197 ? 0.3745 0.6449 0.5491 0.0523  -0.0131 0.0071  194 THR B OG1 
7440 C CG2 . THR B 197 ? 0.3440 0.6144 0.5010 0.0121  -0.0130 0.0149  194 THR B CG2 
7448 N N   . MET B 198 ? 0.2283 0.4447 0.3626 0.0199  -0.0442 0.0309  195 MET B N   
7449 C CA  . MET B 198 ? 0.2131 0.4201 0.3326 0.0037  -0.0516 0.0369  195 MET B CA  
7450 C C   . MET B 198 ? 0.2337 0.3975 0.3271 -0.0005 -0.0499 0.0377  195 MET B C   
7451 O O   . MET B 198 ? 0.2433 0.3938 0.3202 -0.0158 -0.0482 0.0380  195 MET B O   
7452 C CB  . MET B 198 ? 0.2699 0.4927 0.3985 0.0093  -0.0661 0.0432  195 MET B CB  
7453 C CG  . MET B 198 ? 0.3678 0.6399 0.5220 0.0067  -0.0699 0.0438  195 MET B CG  
7454 S SD  . MET B 198 ? 0.4334 0.7227 0.5835 -0.0208 -0.0625 0.0423  195 MET B SD  
7455 C CE  . MET B 198 ? 0.5814 0.8322 0.6986 -0.0373 -0.0705 0.0474  195 MET B CE  
7465 N N   . PHE B 199 ? 0.2474 0.3893 0.3365 0.0129  -0.0501 0.0374  196 PHE B N   
7466 C CA  . PHE B 199 ? 0.2299 0.3361 0.2964 0.0077  -0.0474 0.0380  196 PHE B CA  
7467 C C   . PHE B 199 ? 0.2508 0.3486 0.3113 -0.0001 -0.0358 0.0323  196 PHE B C   
7468 O O   . PHE B 199 ? 0.2467 0.3290 0.2916 -0.0111 -0.0333 0.0320  196 PHE B O   
7469 C CB  . PHE B 199 ? 0.2463 0.3309 0.3087 0.0216  -0.0508 0.0395  196 PHE B CB  
7470 C CG  . PHE B 199 ? 0.2491 0.3024 0.2901 0.0142  -0.0479 0.0407  196 PHE B CG  
7471 C CD1 . PHE B 199 ? 0.2746 0.3147 0.2987 0.0056  -0.0541 0.0466  196 PHE B CD1 
7472 C CD2 . PHE B 199 ? 0.3060 0.3461 0.3436 0.0146  -0.0388 0.0357  196 PHE B CD2 
7473 C CE1 . PHE B 199 ? 0.3447 0.3617 0.3504 -0.0028 -0.0493 0.0469  196 PHE B CE1 
7474 C CE2 . PHE B 199 ? 0.2919 0.3096 0.3129 0.0066  -0.0356 0.0364  196 PHE B CE2 
7475 C CZ  . PHE B 199 ? 0.2832 0.2912 0.2894 -0.0017 -0.0403 0.0418  196 PHE B CZ  
7485 N N   . TRP B 200 ? 0.1875 0.2951 0.2591 0.0061  -0.0288 0.0273  197 TRP B N   
7486 C CA  . TRP B 200 ? 0.1961 0.2947 0.2610 -0.0007 -0.0196 0.0227  197 TRP B CA  
7487 C C   . TRP B 200 ? 0.2199 0.3251 0.2792 -0.0164 -0.0189 0.0230  197 TRP B C   
7488 O O   . TRP B 200 ? 0.2137 0.3002 0.2592 -0.0238 -0.0155 0.0212  197 TRP B O   
7489 C CB  . TRP B 200 ? 0.2361 0.3464 0.3125 0.0082  -0.0131 0.0176  197 TRP B CB  
7490 C CG  . TRP B 200 ? 0.2429 0.3507 0.3139 -0.0003 -0.0050 0.0138  197 TRP B CG  
7491 C CD1 . TRP B 200 ? 0.2778 0.3629 0.3376 -0.0009 -0.0007 0.0112  197 TRP B CD1 
7492 C CD2 . TRP B 200 ? 0.2264 0.3556 0.3019 -0.0104 -0.0014 0.0129  197 TRP B CD2 
7493 N NE1 . TRP B 200 ? 0.3112 0.4001 0.3673 -0.0095 0.0043  0.0090  197 TRP B NE1 
7494 C CE2 . TRP B 200 ? 0.3537 0.4678 0.4177 -0.0163 0.0043  0.0102  197 TRP B CE2 
7495 C CE3 . TRP B 200 ? 0.2727 0.4329 0.3602 -0.0162 -0.0033 0.0147  197 TRP B CE3 
7496 C CZ2 . TRP B 200 ? 0.3021 0.4268 0.3631 -0.0285 0.0081  0.0097  197 TRP B CZ2 
7497 C CZ3 . TRP B 200 ? 0.3626 0.5365 0.4485 -0.0298 0.0015  0.0140  197 TRP B CZ3 
7498 C CH2 . TRP B 200 ? 0.3305 0.4842 0.4015 -0.0361 0.0070  0.0118  197 TRP B CH2 
7509 N N   . LEU B 201 ? 0.2018 0.3329 0.2712 -0.0212 -0.0230 0.0252  198 LEU B N   
7510 C CA  . LEU B 201 ? 0.2095 0.3439 0.2706 -0.0383 -0.0240 0.0260  198 LEU B CA  
7511 C C   . LEU B 201 ? 0.2141 0.3238 0.2552 -0.0456 -0.0281 0.0274  198 LEU B C   
7512 O O   . LEU B 201 ? 0.2746 0.3669 0.3004 -0.0551 -0.0257 0.0249  198 LEU B O   
7513 C CB  . LEU B 201 ? 0.2326 0.4024 0.3092 -0.0436 -0.0293 0.0290  198 LEU B CB  
7514 C CG  . LEU B 201 ? 0.4388 0.6268 0.5165 -0.0599 -0.0269 0.0288  198 LEU B CG  
7515 C CD1 . LEU B 201 ? 0.3804 0.5685 0.4588 -0.0598 -0.0169 0.0248  198 LEU B CD1 
7516 C CD2 . LEU B 201 ? 0.4291 0.6603 0.5295 -0.0603 -0.0327 0.0319  198 LEU B CD2 
7528 N N   . GLU B 202 ? 0.2486 0.3548 0.2877 -0.0409 -0.0344 0.0309  199 GLU B N   
7529 C CA  . GLU B 202 ? 0.2496 0.3365 0.2683 -0.0495 -0.0377 0.0317  199 GLU B CA  
7530 C C   . GLU B 202 ? 0.2634 0.3247 0.2696 -0.0455 -0.0314 0.0284  199 GLU B C   
7531 O O   . GLU B 202 ? 0.2883 0.3333 0.2780 -0.0526 -0.0289 0.0250  199 GLU B O   
7532 C CB  . GLU B 202 ? 0.2856 0.3801 0.3041 -0.0490 -0.0481 0.0377  199 GLU B CB  
7533 C CG  . GLU B 202 ? 0.3819 0.4562 0.3764 -0.0580 -0.0510 0.0384  199 GLU B CG  
7534 C CD  . GLU B 202 ? 0.5356 0.6159 0.5271 -0.0585 -0.0629 0.0455  199 GLU B CD  
7535 O OE1 . GLU B 202 ? 0.5740 0.6392 0.5434 -0.0675 -0.0657 0.0463  199 GLU B OE1 
7536 O OE2 . GLU B 202 ? 0.5237 0.6237 0.5338 -0.0496 -0.0697 0.0501  199 GLU B OE2 
7543 N N   . PHE B 203 ? 0.2283 0.2863 0.2423 -0.0344 -0.0283 0.0285  200 PHE B N   
7544 C CA  . PHE B 203 ? 0.2054 0.2437 0.2089 -0.0322 -0.0239 0.0269  200 PHE B CA  
7545 C C   . PHE B 203 ? 0.2108 0.2426 0.2185 -0.0278 -0.0162 0.0222  200 PHE B C   
7546 O O   . PHE B 203 ? 0.2392 0.2584 0.2400 -0.0275 -0.0123 0.0204  200 PHE B O   
7547 C CB  . PHE B 203 ? 0.2436 0.2771 0.2463 -0.0261 -0.0290 0.0323  200 PHE B CB  
7548 C CG  . PHE B 203 ? 0.2881 0.3224 0.2812 -0.0315 -0.0374 0.0377  200 PHE B CG  
7549 C CD1 . PHE B 203 ? 0.2906 0.3116 0.2641 -0.0402 -0.0360 0.0376  200 PHE B CD1 
7550 C CD2 . PHE B 203 ? 0.2935 0.3435 0.2966 -0.0282 -0.0467 0.0424  200 PHE B CD2 
7551 C CE1 . PHE B 203 ? 0.3705 0.3905 0.3313 -0.0468 -0.0441 0.0426  200 PHE B CE1 
7552 C CE2 . PHE B 203 ? 0.3197 0.3702 0.3125 -0.0342 -0.0563 0.0479  200 PHE B CE2 
7553 C CZ  . PHE B 203 ? 0.3794 0.4131 0.3494 -0.0441 -0.0550 0.0482  200 PHE B CZ  
7563 N N   . GLU B 204 ? 0.2004 0.2420 0.2187 -0.0255 -0.0140 0.0203  201 GLU B N   
7564 C CA  . GLU B 204 ? 0.1837 0.2181 0.2040 -0.0217 -0.0081 0.0165  201 GLU B CA  
7565 C C   . GLU B 204 ? 0.2009 0.2348 0.2187 -0.0273 -0.0053 0.0133  201 GLU B C   
7566 O O   . GLU B 204 ? 0.2218 0.2423 0.2331 -0.0276 -0.0026 0.0103  201 GLU B O   
7567 C CB  . GLU B 204 ? 0.1981 0.2384 0.2293 -0.0119 -0.0077 0.0168  201 GLU B CB  
7568 C CG  . GLU B 204 ? 0.2267 0.2567 0.2572 -0.0083 -0.0028 0.0132  201 GLU B CG  
7569 C CD  . GLU B 204 ? 0.2295 0.2533 0.2628 0.0011  -0.0038 0.0134  201 GLU B CD  
7570 O OE1 . GLU B 204 ? 0.2309 0.2453 0.2597 0.0027  -0.0078 0.0168  201 GLU B OE1 
7571 O OE2 . GLU B 204 ? 0.2629 0.2895 0.3006 0.0065  -0.0008 0.0100  201 GLU B OE2 
7578 N N   . ILE B 205 ? 0.1896 0.2379 0.2118 -0.0324 -0.0064 0.0143  202 ILE B N   
7579 C CA  . ILE B 205 ? 0.2155 0.2606 0.2329 -0.0388 -0.0039 0.0124  202 ILE B CA  
7580 C C   . ILE B 205 ? 0.2264 0.2498 0.2277 -0.0445 -0.0053 0.0103  202 ILE B C   
7581 O O   . ILE B 205 ? 0.2449 0.2543 0.2407 -0.0427 -0.0036 0.0078  202 ILE B O   
7582 C CB  . ILE B 205 ? 0.2393 0.3064 0.2630 -0.0467 -0.0044 0.0143  202 ILE B CB  
7583 C CG1 . ILE B 205 ? 0.2445 0.3039 0.2584 -0.0557 -0.0021 0.0133  202 ILE B CG1 
7584 C CG2 . ILE B 205 ? 0.2769 0.3521 0.2984 -0.0556 -0.0104 0.0173  202 ILE B CG2 
7585 C CD1 . ILE B 205 ? 0.3835 0.4665 0.4026 -0.0661 -0.0008 0.0153  202 ILE B CD1 
7597 N N   . ARG B 206 ? 0.2233 0.2426 0.2160 -0.0506 -0.0092 0.0108  203 ARG B N   
7598 C CA  . ARG B 206 ? 0.2397 0.2360 0.2151 -0.0543 -0.0106 0.0072  203 ARG B CA  
7599 C C   . ARG B 206 ? 0.2520 0.2372 0.2270 -0.0442 -0.0071 0.0032  203 ARG B C   
7600 O O   . ARG B 206 ? 0.2572 0.2274 0.2260 -0.0410 -0.0067 -0.0005 203 ARG B O   
7601 C CB  . ARG B 206 ? 0.2569 0.2498 0.2206 -0.0630 -0.0153 0.0075  203 ARG B CB  
7602 C CG  . ARG B 206 ? 0.2706 0.2749 0.2334 -0.0762 -0.0199 0.0114  203 ARG B CG  
7603 C CD  . ARG B 206 ? 0.2673 0.2723 0.2205 -0.0853 -0.0259 0.0126  203 ARG B CD  
7604 N NE  . ARG B 206 ? 0.2865 0.3067 0.2500 -0.0788 -0.0265 0.0152  203 ARG B NE  
7605 C CZ  . ARG B 206 ? 0.2907 0.3130 0.2466 -0.0847 -0.0322 0.0169  203 ARG B CZ  
7606 N NH1 . ARG B 206 ? 0.3317 0.3420 0.2691 -0.0978 -0.0374 0.0157  203 ARG B NH1 
7607 N NH2 . ARG B 206 ? 0.3004 0.3334 0.2641 -0.0781 -0.0336 0.0202  203 ARG B NH2 
7621 N N   . GLN B 207 ? 0.2377 0.2310 0.2190 -0.0395 -0.0054 0.0042  204 GLN B N   
7622 C CA  . GLN B 207 ? 0.2319 0.2195 0.2126 -0.0330 -0.0015 0.0008  204 GLN B CA  
7623 C C   . GLN B 207 ? 0.2353 0.2221 0.2246 -0.0268 0.0009  -0.0004 204 GLN B C   
7624 O O   . GLN B 207 ? 0.2714 0.2526 0.2600 -0.0222 0.0030  -0.0047 204 GLN B O   
7625 C CB  . GLN B 207 ? 0.2449 0.2406 0.2280 -0.0328 -0.0011 0.0041  204 GLN B CB  
7626 C CG  . GLN B 207 ? 0.2322 0.2279 0.2042 -0.0394 -0.0044 0.0055  204 GLN B CG  
7627 C CD  . GLN B 207 ? 0.2380 0.2444 0.2144 -0.0436 -0.0105 0.0110  204 GLN B CD  
7628 O OE1 . GLN B 207 ? 0.2285 0.2437 0.2162 -0.0419 -0.0111 0.0127  204 GLN B OE1 
7629 N NE2 . GLN B 207 ? 0.2670 0.2752 0.2349 -0.0492 -0.0150 0.0137  204 GLN B NE2 
7638 N N   . TYR B 208 ? 0.1952 0.1892 0.1929 -0.0260 0.0007  0.0027  205 TYR B N   
7639 C CA  . TYR B 208 ? 0.1916 0.1835 0.1949 -0.0211 0.0024  0.0016  205 TYR B CA  
7640 C C   . TYR B 208 ? 0.2087 0.1911 0.2063 -0.0225 0.0007  -0.0001 205 TYR B C   
7641 O O   . TYR B 208 ? 0.2214 0.1970 0.2193 -0.0183 0.0002  -0.0025 205 TYR B O   
7642 C CB  . TYR B 208 ? 0.2145 0.2145 0.2259 -0.0186 0.0032  0.0043  205 TYR B CB  
7643 C CG  . TYR B 208 ? 0.1820 0.1840 0.1966 -0.0158 0.0032  0.0064  205 TYR B CG  
7644 C CD1 . TYR B 208 ? 0.2087 0.2116 0.2191 -0.0184 0.0021  0.0082  205 TYR B CD1 
7645 C CD2 . TYR B 208 ? 0.2015 0.2011 0.2197 -0.0117 0.0036  0.0070  205 TYR B CD2 
7646 C CE1 . TYR B 208 ? 0.2054 0.2070 0.2150 -0.0178 0.0010  0.0114  205 TYR B CE1 
7647 C CE2 . TYR B 208 ? 0.2029 0.1987 0.2199 -0.0106 0.0020  0.0099  205 TYR B CE2 
7648 C CZ  . TYR B 208 ? 0.2258 0.2226 0.2384 -0.0140 0.0005  0.0127  205 TYR B CZ  
7649 O OH  . TYR B 208 ? 0.2447 0.2349 0.2523 -0.0148 -0.0022 0.0168  205 TYR B OH  
7659 N N   . THR B 209 ? 0.2262 0.2090 0.2185 -0.0293 -0.0011 0.0018  206 THR B N   
7660 C CA  . THR B 209 ? 0.2353 0.2059 0.2182 -0.0332 -0.0036 0.0017  206 THR B CA  
7661 C C   . THR B 209 ? 0.2488 0.1992 0.2196 -0.0320 -0.0077 -0.0013 206 THR B C   
7662 O O   . THR B 209 ? 0.2731 0.2084 0.2351 -0.0324 -0.0116 -0.0014 206 THR B O   
7663 C CB  . THR B 209 ? 0.2477 0.2248 0.2261 -0.0439 -0.0041 0.0050  206 THR B CB  
7664 O OG1 . THR B 209 ? 0.2510 0.2280 0.2237 -0.0508 -0.0067 0.0058  206 THR B OG1 
7665 C CG2 . THR B 209 ? 0.2547 0.2540 0.2465 -0.0419 0.0006  0.0063  206 THR B CG2 
7673 N N   . HIS B 210 ? 0.2281 0.1759 0.1964 -0.0299 -0.0076 -0.0043 207 HIS B N   
7674 C CA  . HIS B 210 ? 0.2511 0.1793 0.2083 -0.0252 -0.0108 -0.0094 207 HIS B CA  
7675 C C   . HIS B 210 ? 0.2615 0.1974 0.2284 -0.0145 -0.0068 -0.0144 207 HIS B C   
7676 O O   . HIS B 210 ? 0.2957 0.2235 0.2560 -0.0095 -0.0065 -0.0203 207 HIS B O   
7677 C CB  . HIS B 210 ? 0.2823 0.1969 0.2229 -0.0326 -0.0140 -0.0106 207 HIS B CB  
7678 C CG  . HIS B 210 ? 0.3203 0.2057 0.2434 -0.0291 -0.0199 -0.0153 207 HIS B CG  
7679 N ND1 . HIS B 210 ? 0.3479 0.2144 0.2607 -0.0316 -0.0262 -0.0128 207 HIS B ND1 
7680 C CD2 . HIS B 210 ? 0.3657 0.2354 0.2782 -0.0221 -0.0208 -0.0228 207 HIS B CD2 
7681 C CE1 . HIS B 210 ? 0.4129 0.2506 0.3091 -0.0258 -0.0322 -0.0179 207 HIS B CE1 
7682 N NE2 . HIS B 210 ? 0.3911 0.2308 0.2874 -0.0192 -0.0286 -0.0248 207 HIS B NE2 
7690 N N   . SER B 211 ? 0.2316 0.1838 0.2134 -0.0114 -0.0033 -0.0126 208 SER B N   
7691 C CA  . SER B 211 ? 0.2372 0.2009 0.2288 -0.0047 0.0010  -0.0163 208 SER B CA  
7692 C C   . SER B 211 ? 0.2475 0.2073 0.2435 0.0046  -0.0018 -0.0205 208 SER B C   
7693 O O   . SER B 211 ? 0.2649 0.2103 0.2550 0.0059  -0.0080 -0.0195 208 SER B O   
7694 C CB  . SER B 211 ? 0.2483 0.2273 0.2508 -0.0075 0.0043  -0.0119 208 SER B CB  
7695 O OG  . SER B 211 ? 0.2293 0.2076 0.2365 -0.0073 0.0019  -0.0092 208 SER B OG  
7701 N N   . ASN B 212 ? 0.2384 0.2124 0.2445 0.0109  0.0023  -0.0252 209 ASN B N   
7702 C CA  . ASN B 212 ? 0.2624 0.2371 0.2748 0.0226  -0.0004 -0.0312 209 ASN B CA  
7703 C C   . ASN B 212 ? 0.3100 0.2944 0.3355 0.0241  -0.0039 -0.0281 209 ASN B C   
7704 O O   . ASN B 212 ? 0.2943 0.3007 0.3349 0.0253  -0.0005 -0.0294 209 ASN B O   
7705 C CB  . ASN B 212 ? 0.2875 0.2788 0.3063 0.0286  0.0068  -0.0388 209 ASN B CB  
7706 C CG  . ASN B 212 ? 0.4287 0.4245 0.4566 0.0437  0.0044  -0.0467 209 ASN B CG  
7707 O OD1 . ASN B 212 ? 0.4162 0.3930 0.4390 0.0508  -0.0047 -0.0469 209 ASN B OD1 
7708 N ND2 . ASN B 212 ? 0.4613 0.4838 0.5028 0.0486  0.0120  -0.0529 209 ASN B ND2 
7715 N N   . ILE B 213 ? 0.2634 0.2310 0.2812 0.0224  -0.0112 -0.0240 210 ILE B N   
7716 C CA  . ILE B 213 ? 0.2589 0.2292 0.2834 0.0235  -0.0168 -0.0212 210 ILE B CA  
7717 C C   . ILE B 213 ? 0.3266 0.2759 0.3417 0.0311  -0.0268 -0.0222 210 ILE B C   
7718 O O   . ILE B 213 ? 0.3238 0.2498 0.3209 0.0276  -0.0301 -0.0206 210 ILE B O   
7719 C CB  . ILE B 213 ? 0.2778 0.2453 0.2973 0.0127  -0.0161 -0.0147 210 ILE B CB  
7720 C CG1 . ILE B 213 ? 0.2566 0.2390 0.2826 0.0066  -0.0083 -0.0133 210 ILE B CG1 
7721 C CG2 . ILE B 213 ? 0.2877 0.2534 0.3089 0.0128  -0.0229 -0.0123 210 ILE B CG2 
7722 C CD1 . ILE B 213 ? 0.2402 0.2418 0.2806 0.0072  -0.0061 -0.0145 210 ILE B CD1 
7734 N N   . THR B 214 ? 0.3076 0.2646 0.3341 0.0406  -0.0329 -0.0243 211 THR B N   
7735 C CA  . THR B 214 ? 0.3067 0.2416 0.3238 0.0494  -0.0451 -0.0245 211 THR B CA  
7736 C C   . THR B 214 ? 0.3251 0.2603 0.3436 0.0461  -0.0532 -0.0188 211 THR B C   
7737 O O   . THR B 214 ? 0.3302 0.2863 0.3609 0.0400  -0.0494 -0.0170 211 THR B O   
7738 C CB  . THR B 214 ? 0.3442 0.2868 0.3733 0.0676  -0.0477 -0.0330 211 THR B CB  
7739 O OG1 . THR B 214 ? 0.3732 0.3501 0.4278 0.0717  -0.0462 -0.0347 211 THR B OG1 
7740 C CG2 . THR B 214 ? 0.3801 0.3248 0.4071 0.0709  -0.0383 -0.0402 211 THR B CG2 
7748 N N   . LEU B 215 ? 0.3704 0.2789 0.3731 0.0492  -0.0655 -0.0159 212 LEU B N   
7749 C CA  . LEU B 215 ? 0.4176 0.3246 0.4190 0.0465  -0.0750 -0.0106 212 LEU B CA  
7750 C C   . LEU B 215 ? 0.4411 0.3778 0.4688 0.0563  -0.0781 -0.0139 212 LEU B C   
7751 O O   . LEU B 215 ? 0.4167 0.3642 0.4491 0.0497  -0.0814 -0.0102 212 LEU B O   
7752 C CB  . LEU B 215 ? 0.5145 0.3857 0.4926 0.0492  -0.0895 -0.0066 212 LEU B CB  
7753 C CG  . LEU B 215 ? 0.6064 0.4505 0.5561 0.0337  -0.0877 -0.0010 212 LEU B CG  
7754 C CD1 . LEU B 215 ? 0.7267 0.5337 0.6510 0.0344  -0.1037 0.0041  212 LEU B CD1 
7755 C CD2 . LEU B 215 ? 0.5251 0.3816 0.4728 0.0179  -0.0793 0.0032  212 LEU B CD2 
7767 N N   . ASP B 216 ? 0.3996 0.3513 0.4442 0.0714  -0.0769 -0.0214 213 ASP B N   
7768 C CA  . ASP B 216 ? 0.4071 0.3949 0.4805 0.0801  -0.0785 -0.0252 213 ASP B CA  
7769 C C   . ASP B 216 ? 0.4233 0.4401 0.5099 0.0658  -0.0676 -0.0237 213 ASP B C   
7770 O O   . ASP B 216 ? 0.3848 0.4252 0.4876 0.0638  -0.0718 -0.0225 213 ASP B O   
7771 C CB  . ASP B 216 ? 0.4047 0.4063 0.4930 0.0984  -0.0752 -0.0353 213 ASP B CB  
7772 C CG  . ASP B 216 ? 0.6402 0.6267 0.7283 0.1185  -0.0908 -0.0381 213 ASP B CG  
7773 O OD1 . ASP B 216 ? 0.6880 0.6525 0.7634 0.1171  -0.1054 -0.0311 213 ASP B OD1 
7774 O OD2 . ASP B 216 ? 0.8508 0.8450 0.9491 0.1364  -0.0888 -0.0478 213 ASP B OD2 
7779 N N   . ASP B 217 ? 0.3158 0.3291 0.3939 0.0551  -0.0551 -0.0232 214 ASP B N   
7780 C CA  . ASP B 217 ? 0.3570 0.3901 0.4428 0.0416  -0.0463 -0.0210 214 ASP B CA  
7781 C C   . ASP B 217 ? 0.4148 0.4388 0.4917 0.0306  -0.0525 -0.0147 214 ASP B C   
7782 O O   . ASP B 217 ? 0.4753 0.5168 0.5613 0.0219  -0.0509 -0.0133 214 ASP B O   
7783 C CB  . ASP B 217 ? 0.3524 0.3781 0.4279 0.0344  -0.0344 -0.0211 214 ASP B CB  
7784 C CG  . ASP B 217 ? 0.4103 0.4467 0.4927 0.0430  -0.0271 -0.0280 214 ASP B CG  
7785 O OD1 . ASP B 217 ? 0.3433 0.4076 0.4453 0.0497  -0.0252 -0.0330 214 ASP B OD1 
7786 O OD2 . ASP B 217 ? 0.3433 0.3622 0.4114 0.0426  -0.0230 -0.0289 214 ASP B OD2 
7791 N N   . PHE B 218 ? 0.3247 0.3203 0.3813 0.0295  -0.0595 -0.0109 215 PHE B N   
7792 C CA  . PHE B 218 ? 0.3716 0.3571 0.4162 0.0192  -0.0648 -0.0059 215 PHE B CA  
7793 C C   . PHE B 218 ? 0.3970 0.3911 0.4503 0.0234  -0.0784 -0.0047 215 PHE B C   
7794 O O   . PHE B 218 ? 0.3776 0.3812 0.4336 0.0146  -0.0811 -0.0028 215 PHE B O   
7795 C CB  . PHE B 218 ? 0.3861 0.3411 0.4046 0.0145  -0.0663 -0.0023 215 PHE B CB  
7796 C CG  . PHE B 218 ? 0.3506 0.2998 0.3613 0.0093  -0.0543 -0.0029 215 PHE B CG  
7797 C CD1 . PHE B 218 ? 0.4051 0.3696 0.4251 0.0046  -0.0441 -0.0044 215 PHE B CD1 
7798 C CD2 . PHE B 218 ? 0.4334 0.3623 0.4275 0.0084  -0.0546 -0.0014 215 PHE B CD2 
7799 C CE1 . PHE B 218 ? 0.4533 0.4140 0.4674 0.0010  -0.0349 -0.0045 215 PHE B CE1 
7800 C CE2 . PHE B 218 ? 0.4406 0.3686 0.4300 0.0030  -0.0445 -0.0017 215 PHE B CE2 
7801 C CZ  . PHE B 218 ? 0.4037 0.3485 0.4041 0.0004  -0.0351 -0.0033 215 PHE B CZ  
7811 N N   . THR B 219 ? 0.3526 0.3417 0.4090 0.0370  -0.0884 -0.0058 216 THR B N   
7812 C CA  . THR B 219 ? 0.3645 0.3608 0.4288 0.0427  -0.1041 -0.0039 216 THR B CA  
7813 C C   . THR B 219 ? 0.3697 0.4070 0.4636 0.0426  -0.1030 -0.0067 216 THR B C   
7814 O O   . THR B 219 ? 0.3570 0.4041 0.4558 0.0384  -0.1140 -0.0037 216 THR B O   
7815 C CB  . THR B 219 ? 0.4274 0.4099 0.4907 0.0605  -0.1155 -0.0054 216 THR B CB  
7816 O OG1 . THR B 219 ? 0.4543 0.4584 0.5394 0.0742  -0.1080 -0.0133 216 THR B OG1 
7817 C CG2 . THR B 219 ? 0.4395 0.3796 0.4706 0.0571  -0.1178 -0.0014 216 THR B CG2 
7825 N N   . LYS B 220 ? 0.3270 0.3894 0.4395 0.0450  -0.0903 -0.0122 217 LYS B N   
7826 C CA  . LYS B 220 ? 0.2943 0.3985 0.4342 0.0416  -0.0885 -0.0143 217 LYS B CA  
7827 C C   . LYS B 220 ? 0.2610 0.3652 0.3932 0.0217  -0.0891 -0.0092 217 LYS B C   
7828 O O   . LYS B 220 ? 0.2981 0.4292 0.4470 0.0164  -0.0955 -0.0083 217 LYS B O   
7829 C CB  . LYS B 220 ? 0.3630 0.4932 0.5192 0.0429  -0.0729 -0.0201 217 LYS B CB  
7830 C CG  . LYS B 220 ? 0.5691 0.6919 0.7247 0.0588  -0.0674 -0.0264 217 LYS B CG  
7831 C CD  . LYS B 220 ? 0.6479 0.8071 0.8242 0.0602  -0.0536 -0.0331 217 LYS B CD  
7832 C CE  . LYS B 220 ? 0.6591 0.8055 0.8286 0.0737  -0.0462 -0.0400 217 LYS B CE  
7833 N NZ  . LYS B 220 ? 0.6012 0.7817 0.7864 0.0733  -0.0315 -0.0468 217 LYS B NZ  
7847 N N   . TYR B 221 ? 0.3174 0.3921 0.4244 0.0109  -0.0829 -0.0063 218 TYR B N   
7848 C CA  . TYR B 221 ? 0.3488 0.4181 0.4450 -0.0065 -0.0823 -0.0031 218 TYR B CA  
7849 C C   . TYR B 221 ? 0.3753 0.4097 0.4427 -0.0114 -0.0877 0.0003  218 TYR B C   
7850 O O   . TYR B 221 ? 0.3071 0.3254 0.3575 -0.0222 -0.0819 0.0010  218 TYR B O   
7851 C CB  . TYR B 221 ? 0.3819 0.4520 0.4757 -0.0153 -0.0678 -0.0041 218 TYR B CB  
7852 C CG  . TYR B 221 ? 0.3606 0.4617 0.4773 -0.0114 -0.0595 -0.0076 218 TYR B CG  
7853 C CD1 . TYR B 221 ? 0.4783 0.6128 0.6149 -0.0190 -0.0603 -0.0078 218 TYR B CD1 
7854 C CD2 . TYR B 221 ? 0.4882 0.5852 0.6045 -0.0018 -0.0505 -0.0108 218 TYR B CD2 
7855 C CE1 . TYR B 221 ? 0.4551 0.6206 0.6113 -0.0168 -0.0512 -0.0115 218 TYR B CE1 
7856 C CE2 . TYR B 221 ? 0.5022 0.6267 0.6362 0.0012  -0.0420 -0.0148 218 TYR B CE2 
7857 C CZ  . TYR B 221 ? 0.4696 0.6291 0.6235 -0.0062 -0.0417 -0.0152 218 TYR B CZ  
7858 O OH  . TYR B 221 ? 0.6208 0.8109 0.7914 -0.0043 -0.0316 -0.0197 218 TYR B OH  
7868 N N   . SER B 222 ? 0.3482 0.3704 0.4085 -0.0037 -0.0995 0.0023  219 SER B N   
7869 C CA  . SER B 222 ? 0.4057 0.3944 0.4355 -0.0092 -0.1025 0.0055  219 SER B CA  
7870 C C   . SER B 222 ? 0.3352 0.3169 0.3505 -0.0239 -0.1056 0.0070  219 SER B C   
7871 O O   . SER B 222 ? 0.3555 0.3129 0.3453 -0.0310 -0.1011 0.0073  219 SER B O   
7872 C CB  . SER B 222 ? 0.4286 0.4031 0.4503 -0.0002 -0.1168 0.0086  219 SER B CB  
7873 O OG  . SER B 222 ? 0.4724 0.4611 0.5044 0.0004  -0.1319 0.0107  219 SER B OG  
7879 N N   . ASP B 223 ? 0.3090 0.3124 0.3396 -0.0290 -0.1130 0.0073  220 ASP B N   
7880 C CA  . ASP B 223 ? 0.3298 0.3238 0.3442 -0.0441 -0.1176 0.0083  220 ASP B CA  
7881 C C   . ASP B 223 ? 0.3267 0.3073 0.3280 -0.0531 -0.1038 0.0054  220 ASP B C   
7882 O O   . ASP B 223 ? 0.3815 0.3425 0.3601 -0.0637 -0.1053 0.0048  220 ASP B O   
7883 C CB  . ASP B 223 ? 0.3175 0.3414 0.3536 -0.0497 -0.1282 0.0094  220 ASP B CB  
7884 C CG  . ASP B 223 ? 0.4754 0.5052 0.5151 -0.0449 -0.1467 0.0129  220 ASP B CG  
7885 O OD1 . ASP B 223 ? 0.5403 0.5428 0.5567 -0.0417 -0.1531 0.0155  220 ASP B OD1 
7886 O OD2 . ASP B 223 ? 0.5163 0.5801 0.5827 -0.0447 -0.1556 0.0135  220 ASP B OD2 
7891 N N   . LYS B 224 ? 0.2767 0.2663 0.2906 -0.0487 -0.0915 0.0034  221 LYS B N   
7892 C CA  . LYS B 224 ? 0.2940 0.2710 0.2971 -0.0554 -0.0803 0.0012  221 LYS B CA  
7893 C C   . LYS B 224 ? 0.2883 0.2423 0.2728 -0.0506 -0.0709 -0.0006 221 LYS B C   
7894 O O   . LYS B 224 ? 0.3088 0.2500 0.2824 -0.0543 -0.0633 -0.0030 221 LYS B O   
7895 C CB  . LYS B 224 ? 0.2833 0.2810 0.3069 -0.0553 -0.0721 0.0007  221 LYS B CB  
7896 C CG  . LYS B 224 ? 0.3569 0.3846 0.4020 -0.0617 -0.0787 0.0021  221 LYS B CG  
7897 C CD  . LYS B 224 ? 0.5860 0.6406 0.6546 -0.0563 -0.0702 0.0011  221 LYS B CD  
7898 C CE  . LYS B 224 ? 0.6073 0.6657 0.6753 -0.0699 -0.0641 0.0021  221 LYS B CE  
7899 N NZ  . LYS B 224 ? 0.5031 0.5855 0.5832 -0.0836 -0.0724 0.0040  221 LYS B NZ  
7913 N N   . ILE B 225 ? 0.2816 0.2303 0.2619 -0.0429 -0.0719 0.0005  222 ILE B N   
7914 C CA  . ILE B 225 ? 0.2704 0.2071 0.2406 -0.0385 -0.0615 -0.0008 222 ILE B CA  
7915 C C   . ILE B 225 ? 0.3107 0.2264 0.2540 -0.0428 -0.0624 -0.0010 222 ILE B C   
7916 O O   . ILE B 225 ? 0.3402 0.2493 0.2737 -0.0448 -0.0728 0.0019  222 ILE B O   
7917 C CB  . ILE B 225 ? 0.2731 0.2179 0.2556 -0.0289 -0.0607 0.0006  222 ILE B CB  
7918 C CG1 . ILE B 225 ? 0.2776 0.2447 0.2849 -0.0245 -0.0577 -0.0005 222 ILE B CG1 
7919 C CG2 . ILE B 225 ? 0.2726 0.2074 0.2452 -0.0271 -0.0509 -0.0002 222 ILE B CG2 
7920 C CD1 . ILE B 225 ? 0.2969 0.2708 0.3153 -0.0136 -0.0586 -0.0007 222 ILE B CD1 
7932 N N   . THR B 226 ? 0.3119 0.2187 0.2438 -0.0435 -0.0513 -0.0044 223 THR B N   
7933 C CA  . THR B 226 ? 0.3016 0.1944 0.2102 -0.0466 -0.0473 -0.0057 223 THR B CA  
7934 C C   . THR B 226 ? 0.3029 0.2012 0.2159 -0.0419 -0.0366 -0.0061 223 THR B C   
7935 O O   . THR B 226 ? 0.3099 0.2166 0.2361 -0.0371 -0.0292 -0.0082 223 THR B O   
7936 C CB  . THR B 226 ? 0.3450 0.2254 0.2357 -0.0513 -0.0434 -0.0112 223 THR B CB  
7937 O OG1 . THR B 226 ? 0.3751 0.2498 0.2607 -0.0580 -0.0548 -0.0105 223 THR B OG1 
7938 C CG2 . THR B 226 ? 0.3839 0.2536 0.2496 -0.0550 -0.0378 -0.0137 223 THR B CG2 
7946 N N   . LEU B 227 ? 0.3016 0.1947 0.2019 -0.0448 -0.0366 -0.0036 224 LEU B N   
7947 C CA  . LEU B 227 ? 0.3032 0.2019 0.2035 -0.0442 -0.0267 -0.0038 224 LEU B CA  
7948 C C   . LEU B 227 ? 0.3565 0.2532 0.2390 -0.0488 -0.0172 -0.0084 224 LEU B C   
7949 O O   . LEU B 227 ? 0.3680 0.2531 0.2291 -0.0558 -0.0205 -0.0086 224 LEU B O   
7950 C CB  . LEU B 227 ? 0.3197 0.2121 0.2139 -0.0470 -0.0331 0.0021  224 LEU B CB  
7951 C CG  . LEU B 227 ? 0.3006 0.1930 0.2095 -0.0403 -0.0438 0.0052  224 LEU B CG  
7952 C CD1 . LEU B 227 ? 0.3598 0.2368 0.2547 -0.0429 -0.0526 0.0107  224 LEU B CD1 
7953 C CD2 . LEU B 227 ? 0.3181 0.2247 0.2497 -0.0326 -0.0382 0.0032  224 LEU B CD2 
7965 N N   . LEU B 228 ? 0.3138 0.2227 0.2046 -0.0444 -0.0057 -0.0124 225 LEU B N   
7966 C CA  . LEU B 228 ? 0.3144 0.2269 0.1925 -0.0456 0.0050  -0.0187 225 LEU B CA  
7967 C C   . LEU B 228 ? 0.3230 0.2513 0.2020 -0.0492 0.0137  -0.0176 225 LEU B C   
7968 O O   . LEU B 228 ? 0.2951 0.2366 0.1925 -0.0450 0.0162  -0.0159 225 LEU B O   
7969 C CB  . LEU B 228 ? 0.3266 0.2408 0.2136 -0.0356 0.0105  -0.0257 225 LEU B CB  
7970 C CG  . LEU B 228 ? 0.3308 0.2277 0.2118 -0.0352 0.0029  -0.0277 225 LEU B CG  
7971 C CD1 . LEU B 228 ? 0.3555 0.2501 0.2445 -0.0255 0.0071  -0.0332 225 LEU B CD1 
7972 C CD2 . LEU B 228 ? 0.3626 0.2444 0.2164 -0.0429 0.0008  -0.0310 225 LEU B CD2 
7984 N N   . ASN B 229 ? 0.3447 0.2729 0.2028 -0.0587 0.0185  -0.0186 226 ASN B N   
7985 C CA  . ASN B 229 ? 0.3456 0.2921 0.2014 -0.0660 0.0280  -0.0180 226 ASN B CA  
7986 C C   . ASN B 229 ? 0.3312 0.2924 0.1810 -0.0632 0.0420  -0.0278 226 ASN B C   
7987 O O   . ASN B 229 ? 0.3885 0.3371 0.2175 -0.0659 0.0427  -0.0322 226 ASN B O   
7988 C CB  . ASN B 229 ? 0.3460 0.2802 0.1785 -0.0823 0.0221  -0.0102 226 ASN B CB  
7989 C CG  . ASN B 229 ? 0.3857 0.3105 0.2250 -0.0843 0.0113  -0.0015 226 ASN B CG  
7990 O OD1 . ASN B 229 ? 0.3972 0.3306 0.2596 -0.0753 0.0110  -0.0016 226 ASN B OD1 
7991 N ND2 . ASN B 229 ? 0.4611 0.3667 0.2781 -0.0963 0.0023  0.0059  226 ASN B ND2 
7998 N N   . GLY B 230 ? 0.3377 0.3263 0.2050 -0.0578 0.0527  -0.0316 227 GLY B N   
7999 C CA  . GLY B 230 ? 0.3460 0.3540 0.2098 -0.0536 0.0671  -0.0420 227 GLY B CA  
8000 C C   . GLY B 230 ? 0.4092 0.4265 0.2497 -0.0708 0.0749  -0.0416 227 GLY B C   
8001 O O   . GLY B 230 ? 0.4047 0.4236 0.2383 -0.0866 0.0716  -0.0325 227 GLY B O   
8005 N N   . THR B 231 ? 0.4022 0.4236 0.2273 -0.0686 0.0854  -0.0519 228 THR B N   
8006 C CA  . THR B 231 ? 0.3996 0.4332 0.2006 -0.0861 0.0950  -0.0525 228 THR B CA  
8007 C C   . THR B 231 ? 0.4731 0.5515 0.2915 -0.0894 0.1092  -0.0547 228 THR B C   
8008 O O   . THR B 231 ? 0.4661 0.5582 0.2669 -0.1091 0.1161  -0.0515 228 THR B O   
8009 C CB  . THR B 231 ? 0.4812 0.5041 0.2569 -0.0834 0.1021  -0.0638 228 THR B CB  
8010 O OG1 . THR B 231 ? 0.5517 0.5890 0.3449 -0.0614 0.1120  -0.0776 228 THR B OG1 
8011 C CG2 . THR B 231 ? 0.5868 0.5672 0.3423 -0.0855 0.0864  -0.0598 228 THR B CG2 
8019 N N   . ASP B 232 ? 0.4002 0.5022 0.2519 -0.0722 0.1129  -0.0591 229 ASP B N   
8020 C CA  . ASP B 232 ? 0.4122 0.5624 0.2845 -0.0738 0.1257  -0.0619 229 ASP B CA  
8021 C C   . ASP B 232 ? 0.4055 0.5654 0.2970 -0.0819 0.1176  -0.0502 229 ASP B C   
8022 O O   . ASP B 232 ? 0.3888 0.5901 0.3013 -0.0836 0.1258  -0.0512 229 ASP B O   
8023 C CB  . ASP B 232 ? 0.4118 0.5861 0.3085 -0.0477 0.1354  -0.0760 229 ASP B CB  
8024 C CG  . ASP B 232 ? 0.5082 0.6837 0.3862 -0.0406 0.1481  -0.0903 229 ASP B CG  
8025 O OD1 . ASP B 232 ? 0.5185 0.6928 0.3711 -0.0583 0.1529  -0.0886 229 ASP B OD1 
8026 O OD2 . ASP B 232 ? 0.5319 0.7021 0.4191 -0.0165 0.1501  -0.1018 229 ASP B OD2 
8031 N N   . SER B 233 ? 0.3734 0.4978 0.2582 -0.0868 0.1017  -0.0397 230 SER B N   
8032 C CA  . SER B 233 ? 0.3216 0.4487 0.2211 -0.0931 0.0930  -0.0298 230 SER B CA  
8033 C C   . SER B 233 ? 0.3683 0.4667 0.2418 -0.1146 0.0825  -0.0179 230 SER B C   
8034 O O   . SER B 233 ? 0.3567 0.4371 0.2347 -0.1161 0.0706  -0.0101 230 SER B O   
8035 C CB  . SER B 233 ? 0.3353 0.4478 0.2558 -0.0737 0.0835  -0.0298 230 SER B CB  
8036 O OG  . SER B 233 ? 0.3791 0.4588 0.2867 -0.0649 0.0777  -0.0326 230 SER B OG  
8042 N N   . ARG B 234 ? 0.3787 0.4708 0.2228 -0.1312 0.0865  -0.0167 231 ARG B N   
8043 C CA  . ARG B 234 ? 0.4233 0.4850 0.2391 -0.1521 0.0751  -0.0048 231 ARG B CA  
8044 C C   . ARG B 234 ? 0.4079 0.4824 0.2298 -0.1673 0.0729  0.0034  231 ARG B C   
8045 O O   . ARG B 234 ? 0.4159 0.5315 0.2561 -0.1707 0.0838  0.0001  231 ARG B O   
8046 C CB  . ARG B 234 ? 0.4477 0.5040 0.2284 -0.1701 0.0807  -0.0044 231 ARG B CB  
8047 C CG  . ARG B 234 ? 0.5825 0.6352 0.3551 -0.1580 0.0872  -0.0149 231 ARG B CG  
8048 C CD  . ARG B 234 ? 0.5843 0.5983 0.3558 -0.1440 0.0717  -0.0134 231 ARG B CD  
8049 N NE  . ARG B 234 ? 0.8850 0.8630 0.6209 -0.1569 0.0605  -0.0065 231 ARG B NE  
8050 C CZ  . ARG B 234 ? 0.8066 0.7513 0.5390 -0.1494 0.0441  -0.0023 231 ARG B CZ  
8051 N NH1 . ARG B 234 ? 0.5952 0.5376 0.3557 -0.1312 0.0379  -0.0040 231 ARG B NH1 
8052 N NH2 . ARG B 234 ? 0.9379 0.8526 0.6376 -0.1611 0.0333  0.0039  231 ARG B NH2 
8066 N N   . GLY B 235 ? 0.4333 0.4712 0.2398 -0.1759 0.0573  0.0136  232 GLY B N   
8067 C CA  . GLY B 235 ? 0.4439 0.4828 0.2496 -0.1916 0.0521  0.0218  232 GLY B CA  
8068 C C   . GLY B 235 ? 0.4053 0.4522 0.2409 -0.1777 0.0480  0.0208  232 GLY B C   
8069 O O   . GLY B 235 ? 0.4277 0.4713 0.2610 -0.1905 0.0422  0.0272  232 GLY B O   
8073 N N   . SER B 236 ? 0.3655 0.4204 0.2263 -0.1533 0.0501  0.0131  233 SER B N   
8074 C CA  . SER B 236 ? 0.3269 0.3902 0.2144 -0.1408 0.0464  0.0122  233 SER B CA  
8075 C C   . SER B 236 ? 0.3322 0.3549 0.2134 -0.1339 0.0316  0.0165  233 SER B C   
8076 O O   . SER B 236 ? 0.3775 0.3698 0.2417 -0.1315 0.0244  0.0180  233 SER B O   
8077 C CB  . SER B 236 ? 0.3064 0.3955 0.2217 -0.1187 0.0548  0.0027  233 SER B CB  
8078 O OG  . SER B 236 ? 0.3611 0.4256 0.2719 -0.1041 0.0514  -0.0010 233 SER B OG  
8084 N N   . PHE B 237 ? 0.3377 0.3619 0.2333 -0.1301 0.0267  0.0179  234 PHE B N   
8085 C CA  . PHE B 237 ? 0.3239 0.3129 0.2134 -0.1239 0.0140  0.0208  234 PHE B CA  
8086 C C   . PHE B 237 ? 0.3170 0.2925 0.2143 -0.1046 0.0111  0.0166  234 PHE B C   
8087 O O   . PHE B 237 ? 0.3245 0.2694 0.2083 -0.1025 0.0011  0.0191  234 PHE B O   
8088 C CB  . PHE B 237 ? 0.3320 0.3291 0.2352 -0.1235 0.0114  0.0216  234 PHE B CB  
8089 C CG  . PHE B 237 ? 0.2963 0.2650 0.1996 -0.1121 0.0015  0.0214  234 PHE B CG  
8090 C CD1 . PHE B 237 ? 0.3863 0.3188 0.2667 -0.1185 -0.0094 0.0255  234 PHE B CD1 
8091 C CD2 . PHE B 237 ? 0.2811 0.2591 0.2060 -0.0948 0.0030  0.0169  234 PHE B CD2 
8092 C CE1 . PHE B 237 ? 0.3571 0.2674 0.2392 -0.1058 -0.0172 0.0236  234 PHE B CE1 
8093 C CE2 . PHE B 237 ? 0.3128 0.2695 0.2381 -0.0850 -0.0042 0.0159  234 PHE B CE2 
8094 C CZ  . PHE B 237 ? 0.3235 0.2480 0.2285 -0.0897 -0.0137 0.0185  234 PHE B CZ  
8104 N N   . PRO B 238 ? 0.3014 0.2970 0.2188 -0.0906 0.0183  0.0105  235 PRO B N   
8105 C CA  . PRO B 238 ? 0.2990 0.2799 0.2211 -0.0758 0.0144  0.0074  235 PRO B CA  
8106 C C   . PRO B 238 ? 0.3156 0.2763 0.2175 -0.0795 0.0104  0.0084  235 PRO B C   
8107 O O   . PRO B 238 ? 0.3473 0.2885 0.2475 -0.0723 0.0020  0.0089  235 PRO B O   
8108 C CB  . PRO B 238 ? 0.3196 0.3242 0.2616 -0.0636 0.0231  0.0011  235 PRO B CB  
8109 C CG  . PRO B 238 ? 0.3189 0.3500 0.2739 -0.0674 0.0282  0.0016  235 PRO B CG  
8110 C CD  . PRO B 238 ? 0.3224 0.3537 0.2601 -0.0868 0.0283  0.0064  235 PRO B CD  
8118 N N   . GLN B 239 ? 0.3275 0.2930 0.2129 -0.0920 0.0155  0.0093  236 GLN B N   
8119 C CA  . GLN B 239 ? 0.3669 0.3106 0.2288 -0.0975 0.0102  0.0113  236 GLN B CA  
8120 C C   . GLN B 239 ? 0.4036 0.3161 0.2477 -0.1042 -0.0040 0.0190  236 GLN B C   
8121 O O   . GLN B 239 ? 0.4255 0.3155 0.2592 -0.1004 -0.0140 0.0208  236 GLN B O   
8122 C CB  . GLN B 239 ? 0.3819 0.3394 0.2274 -0.1108 0.0203  0.0100  236 GLN B CB  
8123 C CG  . GLN B 239 ? 0.3959 0.3824 0.2585 -0.1003 0.0340  0.0005  236 GLN B CG  
8124 C CD  . GLN B 239 ? 0.3659 0.3559 0.2098 -0.1054 0.0421  -0.0044 236 GLN B CD  
8125 O OE1 . GLN B 239 ? 0.4361 0.4113 0.2522 -0.1207 0.0392  0.0003  236 GLN B OE1 
8126 N NE2 . GLN B 239 ? 0.3839 0.3918 0.2408 -0.0924 0.0521  -0.0141 236 GLN B NE2 
8135 N N   . ASP B 240 ? 0.3743 0.2838 0.2143 -0.1136 -0.0061 0.0235  237 ASP B N   
8136 C CA  . ASP B 240 ? 0.4328 0.3078 0.2550 -0.1174 -0.0207 0.0299  237 ASP B CA  
8137 C C   . ASP B 240 ? 0.3824 0.2460 0.2206 -0.0984 -0.0290 0.0272  237 ASP B C   
8138 O O   . ASP B 240 ? 0.4491 0.2847 0.2751 -0.0945 -0.0420 0.0302  237 ASP B O   
8139 C CB  . ASP B 240 ? 0.4658 0.3390 0.2801 -0.1315 -0.0211 0.0341  237 ASP B CB  
8140 C CG  . ASP B 240 ? 0.5327 0.4128 0.3252 -0.1548 -0.0155 0.0388  237 ASP B CG  
8141 O OD1 . ASP B 240 ? 0.6057 0.4813 0.3817 -0.1604 -0.0143 0.0399  237 ASP B OD1 
8142 O OD2 . ASP B 240 ? 0.6670 0.5578 0.4579 -0.1688 -0.0123 0.0414  237 ASP B OD2 
8147 N N   . VAL B 241 ? 0.3449 0.2306 0.2101 -0.0863 -0.0220 0.0215  238 VAL B N   
8148 C CA  . VAL B 241 ? 0.3117 0.1920 0.1929 -0.0697 -0.0278 0.0185  238 VAL B CA  
8149 C C   . VAL B 241 ? 0.3322 0.2065 0.2125 -0.0630 -0.0327 0.0176  238 VAL B C   
8150 O O   . VAL B 241 ? 0.3724 0.2306 0.2517 -0.0552 -0.0437 0.0186  238 VAL B O   
8151 C CB  . VAL B 241 ? 0.3231 0.2281 0.2297 -0.0611 -0.0190 0.0136  238 VAL B CB  
8152 C CG1 . VAL B 241 ? 0.3284 0.2312 0.2501 -0.0467 -0.0233 0.0105  238 VAL B CG1 
8153 C CG2 . VAL B 241 ? 0.3111 0.2216 0.2177 -0.0684 -0.0164 0.0150  238 VAL B CG2 
8163 N N   . ASN B 242 ? 0.3335 0.2214 0.2142 -0.0654 -0.0252 0.0152  239 ASN B N   
8164 C CA  . ASN B 242 ? 0.3309 0.2117 0.2072 -0.0618 -0.0306 0.0145  239 ASN B CA  
8165 C C   . ASN B 242 ? 0.3690 0.2236 0.2200 -0.0689 -0.0432 0.0206  239 ASN B C   
8166 O O   . ASN B 242 ? 0.3786 0.2222 0.2301 -0.0621 -0.0544 0.0217  239 ASN B O   
8167 C CB  . ASN B 242 ? 0.3415 0.2369 0.2170 -0.0642 -0.0200 0.0099  239 ASN B CB  
8168 C CG  . ASN B 242 ? 0.3241 0.2360 0.2231 -0.0530 -0.0137 0.0041  239 ASN B CG  
8169 O OD1 . ASN B 242 ? 0.3237 0.2370 0.2389 -0.0446 -0.0178 0.0040  239 ASN B OD1 
8170 N ND2 . ASN B 242 ? 0.3565 0.2803 0.2560 -0.0527 -0.0036 -0.0009 239 ASN B ND2 
8177 N N   . PHE B 243 ? 0.3989 0.2434 0.2271 -0.0835 -0.0425 0.0253  240 PHE B N   
8178 C CA  . PHE B 243 ? 0.4489 0.2634 0.2488 -0.0913 -0.0562 0.0324  240 PHE B CA  
8179 C C   . PHE B 243 ? 0.4262 0.2191 0.2293 -0.0802 -0.0712 0.0350  240 PHE B C   
8180 O O   . PHE B 243 ? 0.4536 0.2256 0.2451 -0.0767 -0.0858 0.0387  240 PHE B O   
8181 C CB  . PHE B 243 ? 0.4927 0.2987 0.2651 -0.1118 -0.0529 0.0380  240 PHE B CB  
8182 C CG  . PHE B 243 ? 0.5982 0.4232 0.3614 -0.1232 -0.0396 0.0355  240 PHE B CG  
8183 C CD1 . PHE B 243 ? 0.6174 0.4397 0.3720 -0.1218 -0.0412 0.0336  240 PHE B CD1 
8184 C CD2 . PHE B 243 ? 0.6062 0.4528 0.3688 -0.1355 -0.0257 0.0345  240 PHE B CD2 
8185 C CE1 . PHE B 243 ? 0.7148 0.5533 0.4588 -0.1309 -0.0281 0.0294  240 PHE B CE1 
8186 C CE2 . PHE B 243 ? 0.6255 0.4931 0.3813 -0.1437 -0.0121 0.0304  240 PHE B CE2 
8187 C CZ  . PHE B 243 ? 0.6794 0.5416 0.4250 -0.1407 -0.0128 0.0273  240 PHE B CZ  
8197 N N   . TYR B 244 ? 0.4223 0.2195 0.2398 -0.0744 -0.0684 0.0326  241 TYR B N   
8198 C CA  . TYR B 244 ? 0.4599 0.2380 0.2814 -0.0612 -0.0809 0.0326  241 TYR B CA  
8199 C C   . TYR B 244 ? 0.4315 0.2222 0.2770 -0.0434 -0.0851 0.0280  241 TYR B C   
8200 O O   . TYR B 244 ? 0.4276 0.2016 0.2701 -0.0338 -0.0997 0.0297  241 TYR B O   
8201 C CB  . TYR B 244 ? 0.4309 0.2129 0.2618 -0.0592 -0.0752 0.0295  241 TYR B CB  
8202 C CG  . TYR B 244 ? 0.4588 0.2180 0.2893 -0.0455 -0.0874 0.0282  241 TYR B CG  
8203 C CD1 . TYR B 244 ? 0.5258 0.2454 0.3270 -0.0499 -0.1017 0.0338  241 TYR B CD1 
8204 C CD2 . TYR B 244 ? 0.4399 0.2159 0.2976 -0.0277 -0.0848 0.0208  241 TYR B CD2 
8205 C CE1 . TYR B 244 ? 0.5165 0.2127 0.3165 -0.0346 -0.1133 0.0311  241 TYR B CE1 
8206 C CE2 . TYR B 244 ? 0.4734 0.2308 0.3313 -0.0132 -0.0947 0.0177  241 TYR B CE2 
8207 C CZ  . TYR B 244 ? 0.5529 0.2702 0.3827 -0.0152 -0.1091 0.0223  241 TYR B CZ  
8208 O OH  . TYR B 244 ? 0.6005 0.2956 0.4286 0.0018  -0.1197 0.0181  241 TYR B OH  
8218 N N   . ILE B 245 ? 0.3961 0.2168 0.2654 -0.0394 -0.0734 0.0226  242 ILE B N   
8219 C CA  . ILE B 245 ? 0.3693 0.2050 0.2610 -0.0262 -0.0767 0.0188  242 ILE B CA  
8220 C C   . ILE B 245 ? 0.3715 0.1969 0.2516 -0.0278 -0.0885 0.0225  242 ILE B C   
8221 O O   . ILE B 245 ? 0.4145 0.2373 0.3030 -0.0168 -0.1009 0.0227  242 ILE B O   
8222 C CB  . ILE B 245 ? 0.3297 0.1936 0.2418 -0.0258 -0.0629 0.0138  242 ILE B CB  
8223 C CG1 . ILE B 245 ? 0.3452 0.2200 0.2697 -0.0232 -0.0532 0.0106  242 ILE B CG1 
8224 C CG2 . ILE B 245 ? 0.3483 0.2270 0.2796 -0.0173 -0.0668 0.0111  242 ILE B CG2 
8225 C CD1 . ILE B 245 ? 0.3768 0.2743 0.3160 -0.0242 -0.0408 0.0071  242 ILE B CD1 
8237 N N   . ASN B 246 ? 0.3851 0.2052 0.2446 -0.0417 -0.0853 0.0253  243 ASN B N   
8238 C CA  . ASN B 246 ? 0.4147 0.2227 0.2579 -0.0458 -0.0966 0.0292  243 ASN B CA  
8239 C C   . ASN B 246 ? 0.4363 0.2147 0.2611 -0.0436 -0.1150 0.0359  243 ASN B C   
8240 O O   . ASN B 246 ? 0.4672 0.2405 0.2935 -0.0367 -0.1297 0.0380  243 ASN B O   
8241 C CB  . ASN B 246 ? 0.4263 0.2331 0.2470 -0.0620 -0.0875 0.0299  243 ASN B CB  
8242 C CG  . ASN B 246 ? 0.4928 0.2807 0.2869 -0.0702 -0.0996 0.0351  243 ASN B CG  
8243 O OD1 . ASN B 246 ? 0.5236 0.2878 0.2887 -0.0807 -0.1063 0.0419  243 ASN B OD1 
8244 N ND2 . ASN B 246 ? 0.4888 0.2856 0.2901 -0.0673 -0.1034 0.0325  243 ASN B ND2 
8251 N N   . LYS B 247 ? 0.4867 0.2438 0.2924 -0.0500 -0.1158 0.0398  244 LYS B N   
8252 C CA  . LYS B 247 ? 0.5571 0.2783 0.3403 -0.0480 -0.1347 0.0467  244 LYS B CA  
8253 C C   . LYS B 247 ? 0.5337 0.2563 0.3402 -0.0253 -0.1469 0.0433  244 LYS B C   
8254 O O   . LYS B 247 ? 0.5723 0.2763 0.3703 -0.0178 -0.1656 0.0476  244 LYS B O   
8255 C CB  . LYS B 247 ? 0.5831 0.2824 0.3452 -0.0587 -0.1322 0.0501  244 LYS B CB  
8256 C CG  . LYS B 247 ? 0.7826 0.4367 0.5106 -0.0628 -0.1513 0.0587  244 LYS B CG  
8257 C CD  . LYS B 247 ? 0.9429 0.5869 0.6486 -0.0823 -0.1438 0.0603  244 LYS B CD  
8258 C CE  . LYS B 247 ? 1.1207 0.7323 0.8029 -0.0840 -0.1593 0.0619  244 LYS B CE  
8259 N NZ  . LYS B 247 ? 1.2828 0.8819 0.9793 -0.0600 -0.1716 0.0572  244 LYS B NZ  
8273 N N   . GLU B 248 ? 0.4851 0.2312 0.3212 -0.0137 -0.1365 0.0355  245 GLU B N   
8274 C CA  . GLU B 248 ? 0.5432 0.2929 0.4011 0.0080  -0.1452 0.0308  245 GLU B CA  
8275 C C   . GLU B 248 ? 0.4843 0.2669 0.3729 0.0191  -0.1468 0.0267  245 GLU B C   
8276 O O   . GLU B 248 ? 0.5564 0.3425 0.4609 0.0371  -0.1584 0.0242  245 GLU B O   
8277 C CB  . GLU B 248 ? 0.5196 0.2781 0.3918 0.0143  -0.1332 0.0239  245 GLU B CB  
8278 C CG  . GLU B 248 ? 0.5284 0.2539 0.3720 0.0044  -0.1337 0.0273  245 GLU B CG  
8279 C CD  . GLU B 248 ? 0.6863 0.3700 0.5078 0.0131  -0.1535 0.0308  245 GLU B CD  
8280 O OE1 . GLU B 248 ? 0.8680 0.5536 0.7062 0.0349  -0.1634 0.0261  245 GLU B OE1 
8281 O OE2 . GLU B 248 ? 0.7917 0.4433 0.5793 -0.0025 -0.1590 0.0379  245 GLU B OE2 
8288 N N   . THR B 249 ? 0.4527 0.2593 0.3497 0.0088  -0.1359 0.0257  246 THR B N   
8289 C CA  . THR B 249 ? 0.4264 0.2652 0.3517 0.0154  -0.1360 0.0219  246 THR B CA  
8290 C C   . THR B 249 ? 0.4379 0.2769 0.3525 0.0051  -0.1433 0.0261  246 THR B C   
8291 O O   . THR B 249 ? 0.4351 0.2975 0.3707 0.0096  -0.1480 0.0243  246 THR B O   
8292 C CB  . THR B 249 ? 0.4271 0.2951 0.3742 0.0130  -0.1172 0.0157  246 THR B CB  
8293 O OG1 . THR B 249 ? 0.3804 0.2459 0.3122 -0.0029 -0.1067 0.0171  246 THR B OG1 
8294 C CG2 . THR B 249 ? 0.4146 0.2837 0.3698 0.0202  -0.1081 0.0112  246 THR B CG2 
8302 N N   . GLY B 250 ? 0.4410 0.2573 0.3238 -0.0102 -0.1429 0.0312  247 GLY B N   
8303 C CA  . GLY B 250 ? 0.4343 0.2496 0.3030 -0.0216 -0.1474 0.0339  247 GLY B CA  
8304 C C   . GLY B 250 ? 0.4174 0.2542 0.2954 -0.0296 -0.1320 0.0284  247 GLY B C   
8305 O O   . GLY B 250 ? 0.4504 0.2848 0.3147 -0.0394 -0.1349 0.0293  247 GLY B O   
8309 N N   . ILE B 251 ? 0.3865 0.2414 0.2850 -0.0255 -0.1171 0.0229  248 ILE B N   
8310 C CA  . ILE B 251 ? 0.3796 0.2501 0.2848 -0.0319 -0.1035 0.0179  248 ILE B CA  
8311 C C   . ILE B 251 ? 0.4073 0.2626 0.2836 -0.0449 -0.0956 0.0183  248 ILE B C   
8312 O O   . ILE B 251 ? 0.4022 0.2456 0.2638 -0.0486 -0.0909 0.0204  248 ILE B O   
8313 C CB  . ILE B 251 ? 0.3743 0.2627 0.3029 -0.0252 -0.0901 0.0132  248 ILE B CB  
8314 C CG1 . ILE B 251 ? 0.3864 0.2959 0.3441 -0.0141 -0.0960 0.0114  248 ILE B CG1 
8315 C CG2 . ILE B 251 ? 0.3761 0.2719 0.3044 -0.0319 -0.0765 0.0091  248 ILE B CG2 
8316 C CD1 . ILE B 251 ? 0.3741 0.2976 0.3510 -0.0064 -0.0854 0.0076  248 ILE B CD1 
8328 N N   . PRO B 252 ? 0.3868 0.2423 0.2533 -0.0526 -0.0935 0.0157  249 PRO B N   
8329 C CA  . PRO B 252 ? 0.4091 0.2504 0.2454 -0.0642 -0.0868 0.0150  249 PRO B CA  
8330 C C   . PRO B 252 ? 0.4074 0.2570 0.2462 -0.0645 -0.0679 0.0099  249 PRO B C   
8331 O O   . PRO B 252 ? 0.3703 0.2346 0.2310 -0.0577 -0.0598 0.0056  249 PRO B O   
8332 C CB  . PRO B 252 ? 0.4195 0.2585 0.2463 -0.0702 -0.0908 0.0121  249 PRO B CB  
8333 C CG  . PRO B 252 ? 0.4179 0.2754 0.2755 -0.0628 -0.0936 0.0098  249 PRO B CG  
8334 C CD  . PRO B 252 ? 0.3677 0.2353 0.2479 -0.0522 -0.0992 0.0135  249 PRO B CD  
8342 N N   . ILE B 253 ? 0.4152 0.2559 0.2302 -0.0734 -0.0618 0.0109  250 ILE B N   
8343 C CA  . ILE B 253 ? 0.4085 0.2599 0.2224 -0.0754 -0.0441 0.0054  250 ILE B CA  
8344 C C   . ILE B 253 ? 0.4195 0.2669 0.2132 -0.0813 -0.0379 -0.0008 250 ILE B C   
8345 O O   . ILE B 253 ? 0.4734 0.3058 0.2395 -0.0913 -0.0441 0.0016  250 ILE B O   
8346 C CB  . ILE B 253 ? 0.4204 0.2697 0.2216 -0.0832 -0.0397 0.0097  250 ILE B CB  
8347 C CG1 . ILE B 253 ? 0.4200 0.2691 0.2377 -0.0772 -0.0457 0.0145  250 ILE B CG1 
8348 C CG2 . ILE B 253 ? 0.4857 0.3532 0.2889 -0.0850 -0.0211 0.0033  250 ILE B CG2 
8349 C CD1 . ILE B 253 ? 0.4470 0.2872 0.2481 -0.0874 -0.0454 0.0203  250 ILE B CD1 
8361 N N   . VAL B 254 ? 0.4220 0.2804 0.2266 -0.0750 -0.0261 -0.0089 251 VAL B N   
8362 C CA  . VAL B 254 ? 0.3857 0.2403 0.1715 -0.0776 -0.0171 -0.0174 251 VAL B CA  
8363 C C   . VAL B 254 ? 0.3981 0.2698 0.1866 -0.0755 0.0001  -0.0226 251 VAL B C   
8364 O O   . VAL B 254 ? 0.3831 0.2703 0.1963 -0.0669 0.0057  -0.0231 251 VAL B O   
8365 C CB  . VAL B 254 ? 0.4145 0.2643 0.2088 -0.0708 -0.0193 -0.0232 251 VAL B CB  
8366 C CG1 . VAL B 254 ? 0.4830 0.3274 0.2594 -0.0697 -0.0080 -0.0341 251 VAL B CG1 
8367 C CG2 . VAL B 254 ? 0.4625 0.2998 0.2524 -0.0759 -0.0365 -0.0182 251 VAL B CG2 
8377 N N   . ASP B 255 ? 0.4746 0.3459 0.2381 -0.0837 0.0086  -0.0267 252 ASP B N   
8378 C CA  . ASP B 255 ? 0.4597 0.3531 0.2268 -0.0817 0.0260  -0.0331 252 ASP B CA  
8379 C C   . ASP B 255 ? 0.4266 0.3228 0.1981 -0.0687 0.0354  -0.0457 252 ASP B C   
8380 O O   . ASP B 255 ? 0.4857 0.3623 0.2399 -0.0683 0.0316  -0.0511 252 ASP B O   
8381 C CB  . ASP B 255 ? 0.5067 0.4028 0.2449 -0.0971 0.0329  -0.0325 252 ASP B CB  
8382 C CG  . ASP B 255 ? 0.5704 0.4613 0.3021 -0.1104 0.0239  -0.0196 252 ASP B CG  
8383 O OD1 . ASP B 255 ? 0.5797 0.4773 0.3344 -0.1059 0.0200  -0.0140 252 ASP B OD1 
8384 O OD2 . ASP B 255 ? 0.7002 0.5780 0.4005 -0.1259 0.0205  -0.0151 252 ASP B OD2 
8389 N N   . ILE B 256 ? 0.4290 0.3476 0.2229 -0.0577 0.0463  -0.0504 253 ILE B N   
8390 C CA  . ILE B 256 ? 0.4362 0.3541 0.2367 -0.0420 0.0529  -0.0618 253 ILE B CA  
8391 C C   . ILE B 256 ? 0.3930 0.3412 0.2036 -0.0344 0.0696  -0.0699 253 ILE B C   
8392 O O   . ILE B 256 ? 0.4337 0.4071 0.2572 -0.0398 0.0743  -0.0645 253 ILE B O   
8393 C CB  . ILE B 256 ? 0.3695 0.2804 0.1945 -0.0316 0.0436  -0.0581 253 ILE B CB  
8394 C CG1 . ILE B 256 ? 0.3908 0.2858 0.2125 -0.0190 0.0447  -0.0679 253 ILE B CG1 
8395 C CG2 . ILE B 256 ? 0.3645 0.2990 0.2177 -0.0279 0.0455  -0.0519 253 ILE B CG2 
8396 C CD1 . ILE B 256 ? 0.3951 0.2744 0.2297 -0.0157 0.0326  -0.0627 253 ILE B CD1 
8408 N N   . PRO B 257 ? 0.4143 0.3612 0.2161 -0.0230 0.0792  -0.0835 254 PRO B N   
8409 C CA  . PRO B 257 ? 0.4276 0.4089 0.2394 -0.0147 0.0963  -0.0928 254 PRO B CA  
8410 C C   . PRO B 257 ? 0.4152 0.4226 0.2632 -0.0031 0.0974  -0.0898 254 PRO B C   
8411 O O   . PRO B 257 ? 0.4268 0.4211 0.2906 0.0042  0.0868  -0.0844 254 PRO B O   
8412 C CB  . PRO B 257 ? 0.4813 0.4487 0.2776 0.0001  0.1033  -0.1091 254 PRO B CB  
8413 C CG  . PRO B 257 ? 0.5246 0.4545 0.2890 -0.0119 0.0934  -0.1074 254 PRO B CG  
8414 C CD  . PRO B 257 ? 0.4495 0.3650 0.2270 -0.0191 0.0760  -0.0923 254 PRO B CD  
8422 N N   . GLY B 258 ? 0.4166 0.4636 0.2769 -0.0026 0.1108  -0.0934 255 GLY B N   
8423 C CA  . GLY B 258 ? 0.4096 0.4869 0.3037 0.0069  0.1124  -0.0909 255 GLY B CA  
8424 C C   . GLY B 258 ? 0.3384 0.4266 0.2421 -0.0104 0.1061  -0.0764 255 GLY B C   
8425 O O   . GLY B 258 ? 0.3844 0.4553 0.2692 -0.0286 0.0999  -0.0678 255 GLY B O   
8429 N N   . GLY B 259 ? 0.3454 0.4598 0.2779 -0.0037 0.1062  -0.0736 256 GLY B N   
8430 C CA  . GLY B 259 ? 0.3463 0.4676 0.2878 -0.0184 0.0992  -0.0606 256 GLY B CA  
8431 C C   . GLY B 259 ? 0.3453 0.4441 0.2989 -0.0112 0.0854  -0.0537 256 GLY B C   
8432 O O   . GLY B 259 ? 0.3222 0.3888 0.2667 -0.0049 0.0780  -0.0545 256 GLY B O   
8436 N N   . HIS B 260 ? 0.2793 0.3960 0.2522 -0.0143 0.0820  -0.0468 257 HIS B N   
8437 C CA  . HIS B 260 ? 0.3009 0.3997 0.2844 -0.0089 0.0702  -0.0403 257 HIS B CA  
8438 C C   . HIS B 260 ? 0.3176 0.4060 0.3101 0.0117  0.0681  -0.0463 257 HIS B C   
8439 O O   . HIS B 260 ? 0.2894 0.3515 0.2803 0.0146  0.0585  -0.0424 257 HIS B O   
8440 C CB  . HIS B 260 ? 0.2923 0.4151 0.2930 -0.0155 0.0684  -0.0337 257 HIS B CB  
8441 C CG  . HIS B 260 ? 0.3014 0.4060 0.3084 -0.0140 0.0571  -0.0266 257 HIS B CG  
8442 N ND1 . HIS B 260 ? 0.3260 0.4016 0.3189 -0.0228 0.0491  -0.0207 257 HIS B ND1 
8443 C CD2 . HIS B 260 ? 0.4090 0.5217 0.4342 -0.0051 0.0526  -0.0246 257 HIS B CD2 
8444 C CE1 . HIS B 260 ? 0.3717 0.4401 0.3743 -0.0192 0.0417  -0.0164 257 HIS B CE1 
8445 N NE2 . HIS B 260 ? 0.3819 0.4708 0.4023 -0.0095 0.0434  -0.0182 257 HIS B NE2 
8453 N N   . LEU B 261 ? 0.3156 0.4234 0.3165 0.0259  0.0765  -0.0560 258 LEU B N   
8454 C CA  . LEU B 261 ? 0.3598 0.4521 0.3647 0.0468  0.0737  -0.0626 258 LEU B CA  
8455 C C   . LEU B 261 ? 0.3072 0.3802 0.2913 0.0531  0.0791  -0.0734 258 LEU B C   
8456 O O   . LEU B 261 ? 0.3311 0.4028 0.3178 0.0723  0.0823  -0.0834 258 LEU B O   
8457 C CB  . LEU B 261 ? 0.3332 0.4581 0.3635 0.0630  0.0768  -0.0666 258 LEU B CB  
8458 C CG  . LEU B 261 ? 0.3840 0.5319 0.4340 0.0554  0.0717  -0.0566 258 LEU B CG  
8459 C CD1 . LEU B 261 ? 0.4258 0.6136 0.5024 0.0706  0.0752  -0.0611 258 LEU B CD1 
8460 C CD2 . LEU B 261 ? 0.4471 0.5648 0.4950 0.0543  0.0588  -0.0480 258 LEU B CD2 
8472 N N   . GLY B 262 ? 0.3272 0.3810 0.2884 0.0379  0.0786  -0.0715 259 GLY B N   
8473 C CA  . GLY B 262 ? 0.3510 0.3895 0.2889 0.0403  0.0847  -0.0819 259 GLY B CA  
8474 C C   . GLY B 262 ? 0.3756 0.3795 0.3040 0.0553  0.0788  -0.0885 259 GLY B C   
8475 O O   . GLY B 262 ? 0.3977 0.3925 0.3108 0.0644  0.0853  -0.1006 259 GLY B O   
8479 N N   . TYR B 263 ? 0.3462 0.3293 0.2812 0.0570  0.0667  -0.0809 260 TYR B N   
8480 C CA  . TYR B 263 ? 0.3553 0.3016 0.2785 0.0676  0.0593  -0.0852 260 TYR B CA  
8481 C C   . TYR B 263 ? 0.4133 0.3623 0.3442 0.0913  0.0628  -0.0954 260 TYR B C   
8482 O O   . TYR B 263 ? 0.4195 0.3347 0.3333 0.1015  0.0589  -0.1027 260 TYR B O   
8483 C CB  . TYR B 263 ? 0.3640 0.2920 0.2932 0.0609  0.0461  -0.0734 260 TYR B CB  
8484 C CG  . TYR B 263 ? 0.3593 0.3145 0.3135 0.0596  0.0448  -0.0643 260 TYR B CG  
8485 C CD1 . TYR B 263 ? 0.3518 0.3160 0.3226 0.0744  0.0432  -0.0646 260 TYR B CD1 
8486 C CD2 . TYR B 263 ? 0.3005 0.2701 0.2598 0.0438  0.0442  -0.0557 260 TYR B CD2 
8487 C CE1 . TYR B 263 ? 0.3452 0.3336 0.3366 0.0717  0.0413  -0.0563 260 TYR B CE1 
8488 C CE2 . TYR B 263 ? 0.3301 0.3213 0.3086 0.0416  0.0430  -0.0485 260 TYR B CE2 
8489 C CZ  . TYR B 263 ? 0.3461 0.3474 0.3406 0.0549  0.0416  -0.0487 260 TYR B CZ  
8490 O OH  . TYR B 263 ? 0.3635 0.3857 0.3753 0.0516  0.0393  -0.0414 260 TYR B OH  
8500 N N   . ILE B 264 ? 0.3660 0.3538 0.3215 0.1006  0.0692  -0.0964 261 ILE B N   
8501 C CA  . ILE B 264 ? 0.3770 0.3746 0.3431 0.1257  0.0732  -0.1072 261 ILE B CA  
8502 C C   . ILE B 264 ? 0.3838 0.4174 0.3527 0.1317  0.0898  -0.1198 261 ILE B C   
8503 O O   . ILE B 264 ? 0.4327 0.4647 0.3995 0.1534  0.0951  -0.1337 261 ILE B O   
8504 C CB  . ILE B 264 ? 0.4149 0.4323 0.4092 0.1344  0.0663  -0.0993 261 ILE B CB  
8505 C CG1 . ILE B 264 ? 0.4179 0.4407 0.4239 0.1634  0.0665  -0.1096 261 ILE B CG1 
8506 C CG2 . ILE B 264 ? 0.4249 0.4892 0.4410 0.1213  0.0718  -0.0919 261 ILE B CG2 
8507 C CD1 . ILE B 264 ? 0.5124 0.4877 0.4941 0.1780  0.0618  -0.1190 261 ILE B CD1 
8519 N N   . GLN B 265 ? 0.3731 0.4360 0.3434 0.1122  0.0980  -0.1156 262 GLN B N   
8520 C CA  . GLN B 265 ? 0.3788 0.4780 0.3487 0.1127  0.1150  -0.1264 262 GLN B CA  
8521 C C   . GLN B 265 ? 0.4133 0.4837 0.3500 0.1135  0.1209  -0.1384 262 GLN B C   
8522 O O   . GLN B 265 ? 0.4831 0.5693 0.4169 0.1280  0.1336  -0.1537 262 GLN B O   
8523 C CB  . GLN B 265 ? 0.3937 0.5236 0.3682 0.0871  0.1196  -0.1161 262 GLN B CB  
8524 C CG  . GLN B 265 ? 0.3777 0.5461 0.3849 0.0858  0.1173  -0.1072 262 GLN B CG  
8525 C CD  . GLN B 265 ? 0.3718 0.5491 0.3763 0.0579  0.1150  -0.0935 262 GLN B CD  
8526 O OE1 . GLN B 265 ? 0.4580 0.6086 0.4378 0.0413  0.1124  -0.0890 262 GLN B OE1 
8527 N NE2 . GLN B 265 ? 0.4026 0.6168 0.4316 0.0529  0.1150  -0.0870 262 GLN B NE2 
8536 N N   . LYS B 266 ? 0.4520 0.4808 0.3633 0.0980  0.1114  -0.1319 263 LYS B N   
8537 C CA  . LYS B 266 ? 0.4622 0.4618 0.3384 0.0933  0.1149  -0.1411 263 LYS B CA  
8538 C C   . LYS B 266 ? 0.4598 0.4057 0.3169 0.0910  0.0992  -0.1371 263 LYS B C   
8539 O O   . LYS B 266 ? 0.4611 0.3862 0.2997 0.0712  0.0922  -0.1295 263 LYS B O   
8540 C CB  . LYS B 266 ? 0.5017 0.5171 0.3630 0.0686  0.1217  -0.1364 263 LYS B CB  
8541 C CG  . LYS B 266 ? 0.6784 0.7466 0.5530 0.0696  0.1396  -0.1430 263 LYS B CG  
8542 C CD  . LYS B 266 ? 0.6961 0.7851 0.5623 0.0421  0.1440  -0.1334 263 LYS B CD  
8543 C CE  . LYS B 266 ? 0.7477 0.8660 0.6018 0.0397  0.1626  -0.1444 263 LYS B CE  
8544 N NZ  . LYS B 266 ? 0.8142 0.9481 0.6561 0.0111  0.1653  -0.1331 263 LYS B NZ  
8558 N N   . PRO B 267 ? 0.5186 0.4406 0.3788 0.1107  0.0925  -0.1420 264 PRO B N   
8559 C CA  . PRO B 267 ? 0.5021 0.3756 0.3468 0.1054  0.0764  -0.1358 264 PRO B CA  
8560 C C   . PRO B 267 ? 0.5198 0.3566 0.3272 0.0950  0.0744  -0.1420 264 PRO B C   
8561 O O   . PRO B 267 ? 0.5371 0.3492 0.3338 0.0781  0.0623  -0.1322 264 PRO B O   
8562 C CB  . PRO B 267 ? 0.5226 0.3790 0.3755 0.1299  0.0710  -0.1412 264 PRO B CB  
8563 C CG  . PRO B 267 ? 0.5916 0.4803 0.4567 0.1515  0.0853  -0.1553 264 PRO B CG  
8564 C CD  . PRO B 267 ? 0.5092 0.4496 0.3901 0.1377  0.0976  -0.1514 264 PRO B CD  
8572 N N   . GLU B 268 ? 0.5791 0.4149 0.3669 0.1036  0.0860  -0.1580 265 GLU B N   
8573 C CA  . GLU B 268 ? 0.5881 0.3865 0.3369 0.0929  0.0834  -0.1646 265 GLU B CA  
8574 C C   . GLU B 268 ? 0.6221 0.4309 0.3620 0.0658  0.0819  -0.1539 265 GLU B C   
8575 O O   . GLU B 268 ? 0.6040 0.3823 0.3248 0.0500  0.0694  -0.1477 265 GLU B O   
8576 C CB  . GLU B 268 ? 0.6287 0.4356 0.3712 0.1048  0.0944  -0.1813 265 GLU B CB  
8577 C CG  . GLU B 268 ? 0.7936 0.5675 0.5021 0.0932  0.0894  -0.1868 265 GLU B CG  
8578 C CD  . GLU B 268 ? 0.9467 0.7299 0.6479 0.1052  0.1018  -0.2050 265 GLU B CD  
8579 O OE1 . GLU B 268 ? 0.9646 0.7694 0.6892 0.1251  0.1113  -0.2132 265 GLU B OE1 
8580 O OE2 . GLU B 268 ? 1.0191 0.7884 0.6918 0.0940  0.1021  -0.2106 265 GLU B OE2 
8587 N N   . GLY B 269 ? 0.5439 0.3956 0.2984 0.0594  0.0926  -0.1503 266 GLY B N   
8588 C CA  . GLY B 269 ? 0.5434 0.4012 0.2877 0.0346  0.0894  -0.1393 266 GLY B CA  
8589 C C   . GLY B 269 ? 0.5178 0.3705 0.2792 0.0229  0.0739  -0.1216 266 GLY B C   
8590 O O   . GLY B 269 ? 0.5475 0.3855 0.2947 0.0053  0.0640  -0.1133 266 GLY B O   
8594 N N   . PHE B 270 ? 0.4697 0.3371 0.2622 0.0330  0.0716  -0.1159 267 PHE B N   
8595 C CA  . PHE B 270 ? 0.4389 0.3020 0.2477 0.0240  0.0582  -0.1009 267 PHE B CA  
8596 C C   . PHE B 270 ? 0.4548 0.2786 0.2473 0.0190  0.0446  -0.0994 267 PHE B C   
8597 O O   . PHE B 270 ? 0.4490 0.2664 0.2403 0.0038  0.0339  -0.0892 267 PHE B O   
8598 C CB  . PHE B 270 ? 0.4253 0.3084 0.2660 0.0371  0.0591  -0.0973 267 PHE B CB  
8599 C CG  . PHE B 270 ? 0.3780 0.2727 0.2393 0.0274  0.0510  -0.0826 267 PHE B CG  
8600 C CD1 . PHE B 270 ? 0.3882 0.2619 0.2529 0.0241  0.0385  -0.0753 267 PHE B CD1 
8601 C CD2 . PHE B 270 ? 0.3558 0.2831 0.2333 0.0219  0.0564  -0.0767 267 PHE B CD2 
8602 C CE1 . PHE B 270 ? 0.3868 0.2726 0.2704 0.0172  0.0326  -0.0636 267 PHE B CE1 
8603 C CE2 . PHE B 270 ? 0.3395 0.2739 0.2337 0.0145  0.0489  -0.0646 267 PHE B CE2 
8604 C CZ  . PHE B 270 ? 0.3431 0.2576 0.2410 0.0134  0.0376  -0.0587 267 PHE B CZ  
8614 N N   . ALA B 271 ? 0.4933 0.2907 0.2735 0.0316  0.0440  -0.1095 268 ALA B N   
8615 C CA  . ALA B 271 ? 0.5044 0.2624 0.2663 0.0246  0.0306  -0.1082 268 ALA B CA  
8616 C C   . ALA B 271 ? 0.5267 0.2693 0.2606 0.0074  0.0261  -0.1090 268 ALA B C   
8617 O O   . ALA B 271 ? 0.5685 0.2957 0.2975 -0.0070 0.0128  -0.1009 268 ALA B O   
8618 C CB  . ALA B 271 ? 0.5550 0.2819 0.3029 0.0416  0.0307  -0.1202 268 ALA B CB  
8624 N N   . ASP B 272 ? 0.5641 0.3125 0.2791 0.0080  0.0369  -0.1186 269 ASP B N   
8625 C CA  . ASP B 272 ? 0.5864 0.3185 0.2705 -0.0087 0.0323  -0.1197 269 ASP B CA  
8626 C C   . ASP B 272 ? 0.5429 0.2890 0.2379 -0.0267 0.0219  -0.1037 269 ASP B C   
8627 O O   . ASP B 272 ? 0.5822 0.3095 0.2618 -0.0409 0.0089  -0.0992 269 ASP B O   
8628 C CB  . ASP B 272 ? 0.6093 0.3525 0.2733 -0.0058 0.0480  -0.1316 269 ASP B CB  
8629 C CG  . ASP B 272 ? 0.8119 0.5354 0.4583 0.0085  0.0538  -0.1477 269 ASP B CG  
8630 O OD1 . ASP B 272 ? 0.8136 0.5104 0.4607 0.0149  0.0443  -0.1488 269 ASP B OD1 
8631 O OD2 . ASP B 272 ? 0.8263 0.5667 0.4639 0.0131  0.0671  -0.1576 269 ASP B OD2 
8636 N N   . VAL B 273 ? 0.5056 0.2843 0.2266 -0.0259 0.0266  -0.0955 270 VAL B N   
8637 C CA  . VAL B 273 ? 0.4807 0.2703 0.2128 -0.0396 0.0161  -0.0811 270 VAL B CA  
8638 C C   . VAL B 273 ? 0.4750 0.2565 0.2246 -0.0416 0.0025  -0.0729 270 VAL B C   
8639 O O   . VAL B 273 ? 0.4945 0.2709 0.2414 -0.0540 -0.0104 -0.0652 270 VAL B O   
8640 C CB  . VAL B 273 ? 0.5134 0.3354 0.2665 -0.0384 0.0240  -0.0749 270 VAL B CB  
8641 C CG1 . VAL B 273 ? 0.4983 0.3264 0.2644 -0.0487 0.0115  -0.0607 270 VAL B CG1 
8642 C CG2 . VAL B 273 ? 0.5700 0.4022 0.3031 -0.0423 0.0364  -0.0810 270 VAL B CG2 
8652 N N   . LEU B 274 ? 0.4765 0.2597 0.2453 -0.0301 0.0047  -0.0738 271 LEU B N   
8653 C CA  . LEU B 274 ? 0.4745 0.2515 0.2578 -0.0342 -0.0070 -0.0659 271 LEU B CA  
8654 C C   . LEU B 274 ? 0.5035 0.2511 0.2634 -0.0449 -0.0181 -0.0682 271 LEU B C   
8655 O O   . LEU B 274 ? 0.5054 0.2542 0.2732 -0.0562 -0.0301 -0.0599 271 LEU B O   
8656 C CB  . LEU B 274 ? 0.4639 0.2415 0.2643 -0.0212 -0.0032 -0.0670 271 LEU B CB  
8657 C CG  . LEU B 274 ? 0.4516 0.2598 0.2792 -0.0126 0.0047  -0.0626 271 LEU B CG  
8658 C CD1 . LEU B 274 ? 0.4389 0.2436 0.2809 -0.0012 0.0049  -0.0623 271 LEU B CD1 
8659 C CD2 . LEU B 274 ? 0.3977 0.2266 0.2429 -0.0219 -0.0004 -0.0514 271 LEU B CD2 
8671 N N   . LEU B 275 ? 0.5054 0.2271 0.2365 -0.0416 -0.0144 -0.0800 272 LEU B N   
8672 C CA  . LEU B 275 ? 0.5521 0.2422 0.2565 -0.0535 -0.0257 -0.0828 272 LEU B CA  
8673 C C   . LEU B 275 ? 0.5922 0.2871 0.2850 -0.0696 -0.0342 -0.0777 272 LEU B C   
8674 O O   . LEU B 275 ? 0.6696 0.3541 0.3566 -0.0837 -0.0483 -0.0729 272 LEU B O   
8675 C CB  . LEU B 275 ? 0.5937 0.2529 0.2678 -0.0443 -0.0192 -0.0979 272 LEU B CB  
8676 C CG  . LEU B 275 ? 0.6381 0.2822 0.3207 -0.0311 -0.0186 -0.1003 272 LEU B CG  
8677 C CD1 . LEU B 275 ? 0.7062 0.3362 0.3729 -0.0142 -0.0086 -0.1142 272 LEU B CD1 
8678 C CD2 . LEU B 275 ? 0.8043 0.4321 0.4874 -0.0439 -0.0331 -0.0916 272 LEU B CD2 
8690 N N   . ASN B 276 ? 0.5542 0.2655 0.2433 -0.0687 -0.0266 -0.0781 273 ASN B N   
8691 C CA  . ASN B 276 ? 0.5941 0.3090 0.2719 -0.0833 -0.0364 -0.0716 273 ASN B CA  
8692 C C   . ASN B 276 ? 0.5975 0.3329 0.3052 -0.0889 -0.0486 -0.0577 273 ASN B C   
8693 O O   . ASN B 276 ? 0.6093 0.3416 0.3116 -0.1015 -0.0634 -0.0520 273 ASN B O   
8694 C CB  . ASN B 276 ? 0.6181 0.3457 0.2855 -0.0819 -0.0253 -0.0735 273 ASN B CB  
8695 C CG  . ASN B 276 ? 0.8674 0.5868 0.5082 -0.0973 -0.0349 -0.0699 273 ASN B CG  
8696 O OD1 . ASN B 276 ? 1.0359 0.7706 0.6825 -0.1021 -0.0378 -0.0608 273 ASN B OD1 
8697 N ND2 . ASN B 276 ? 0.9339 0.6328 0.5523 -0.1033 -0.0400 -0.0739 273 ASN B ND2 
8704 N N   . MET B 277 ? 0.5242 0.2816 0.2636 -0.0792 -0.0428 -0.0529 274 MET B N   
8705 C CA  . MET B 277 ? 0.4814 0.2601 0.2501 -0.0818 -0.0521 -0.0416 274 MET B CA  
8706 C C   . MET B 277 ? 0.5268 0.3009 0.3040 -0.0887 -0.0627 -0.0390 274 MET B C   
8707 O O   . MET B 277 ? 0.5359 0.3219 0.3245 -0.0971 -0.0753 -0.0317 274 MET B O   
8708 C CB  . MET B 277 ? 0.4935 0.2939 0.2903 -0.0701 -0.0423 -0.0386 274 MET B CB  
8709 C CG  . MET B 277 ? 0.5048 0.3145 0.2971 -0.0653 -0.0317 -0.0399 274 MET B CG  
8710 S SD  . MET B 277 ? 0.4354 0.2676 0.2567 -0.0528 -0.0204 -0.0380 274 MET B SD  
8711 C CE  . MET B 277 ? 0.4271 0.2696 0.2780 -0.0520 -0.0290 -0.0305 274 MET B CE  
8721 N N   . TRP B 278 ? 0.5045 0.2628 0.2777 -0.0851 -0.0580 -0.0446 275 TRP B N   
8722 C CA  . TRP B 278 ? 0.4940 0.2520 0.2804 -0.0912 -0.0652 -0.0404 275 TRP B CA  
8723 C C   . TRP B 278 ? 0.5759 0.2996 0.3347 -0.0997 -0.0707 -0.0465 275 TRP B C   
8724 O O   . TRP B 278 ? 0.5812 0.3019 0.3459 -0.1096 -0.0785 -0.0422 275 TRP B O   
8725 C CB  . TRP B 278 ? 0.4692 0.2388 0.2785 -0.0795 -0.0560 -0.0387 275 TRP B CB  
8726 C CG  . TRP B 278 ? 0.4338 0.2365 0.2728 -0.0741 -0.0532 -0.0315 275 TRP B CG  
8727 C CD1 . TRP B 278 ? 0.4313 0.2537 0.2817 -0.0780 -0.0597 -0.0256 275 TRP B CD1 
8728 C CD2 . TRP B 278 ? 0.4359 0.2527 0.2948 -0.0628 -0.0439 -0.0300 275 TRP B CD2 
8729 N NE1 . TRP B 278 ? 0.4235 0.2687 0.2982 -0.0697 -0.0547 -0.0213 275 TRP B NE1 
8730 C CE2 . TRP B 278 ? 0.3762 0.2193 0.2563 -0.0614 -0.0448 -0.0237 275 TRP B CE2 
8731 C CE3 . TRP B 278 ? 0.4588 0.2668 0.3184 -0.0535 -0.0362 -0.0332 275 TRP B CE3 
8732 C CZ2 . TRP B 278 ? 0.3800 0.2402 0.2804 -0.0526 -0.0377 -0.0211 275 TRP B CZ2 
8733 C CZ3 . TRP B 278 ? 0.3976 0.2252 0.2788 -0.0449 -0.0298 -0.0298 275 TRP B CZ3 
8734 C CH2 . TRP B 278 ? 0.3627 0.2157 0.2633 -0.0455 -0.0303 -0.0239 275 TRP B CH2 
8745 N N   . GLY B 279 ? 0.5798 0.2768 0.3069 -0.0970 -0.0667 -0.0565 276 GLY B N   
8746 C CA  . GLY B 279 ? 0.6429 0.3128 0.3489 -0.0997 -0.0691 -0.0604 276 GLY B CA  
8747 C C   . GLY B 279 ? 0.7236 0.3915 0.4166 -0.1148 -0.0803 -0.0566 276 GLY B C   
8748 O O   . GLY B 279 ? 0.9175 0.5630 0.5916 -0.1201 -0.0842 -0.0586 276 GLY B O   
8749 O OXT . GLY B 279 ? 0.7667 0.4542 0.4672 -0.1216 -0.0864 -0.0510 276 GLY B OXT 
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