data_8ZX8
# 
_entry.id   8ZX8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8ZX8         pdb_00008zx8 10.2210/pdb8zx8/pdb 
WWPDB D_1300048695 ?            ?                   
# 
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 2025-04-09 ? 
2 'Structure model' 1 1 2025-04-16 ? 
# 
_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                        8ZX8 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              cma@gate.sinica.edu.tw 
_pdbx_contact_author.name_first         Che 
_pdbx_contact_author.name_last          Ma 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4741-2307 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lo, J.M.' 1 0000-0002-3002-9491 
'Ma, C.'   2 0000-0002-4741-2307 
# 
_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                10875 
_citation.page_last                 10885 
_citation.title                     'Structure-Based Mechanism and Specificity of Human Galactosyltransferase beta 3GalT5.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.4c11724 
_citation.pdbx_database_id_PubMed   40130308 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lo, J.M.'    1 ? 
primary 'Kung, C.C.'  2 ? 
primary 'Cheng, T.R.' 3 ? 
primary 'Wong, C.H.'  4 ? 
primary 'Ma, C.'      5 ? 
# 
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 'Beta-1,3-galactosyltransferase 5' 32550.551 2  ? ? ? ? 
2  branched    syn '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   2  ? ? ? ? 
3  branched    syn 'alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose' 367.349   1  ? ? ? ? 
4  branched    syn 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose
;
1056.964  1  ? ? ? ? 
5  branched    syn 
'2-acetamido-2-deoxy-beta-D-galactopyranose-(1-3)-alpha-D-galactopyranose-(1-4)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose' 
707.630   1  ? ? ? ? 
6  branched    syn '2-acetamido-2-deoxy-beta-D-galactopyranose-(1-3)-alpha-D-galactopyranose-(1-4)-beta-D-galactopyranose' 545.490 
1  ? ? ? ? 
7  non-polymer syn 'MANGANESE (II) ION' 54.938    2  ? ? ? ? 
8  non-polymer syn "URIDINE-5'-DIPHOSPHATE" 404.161   2  ? ? ? ? 
9  non-polymer syn '2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL' 282.334   2  ? 
? ? ? 
10 non-polymer syn 'DI(HYDROXYETHYL)ETHER' 106.120   2  ? ? ? ? 
11 non-polymer syn beta-D-galactopyranose 180.156   1  ? ? ? ? 
12 water       nat water 18.015    87 ? ? ? ? 
# 
_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       
;FKEQSFVYKKDGNFLKLPDTDCRQTPPFLVLLVTSSHKQLAERMAIRQTWGKERMVKGKQLKTFFLLGTTSSAAETKEVD
QESQRHGDIIQKDFLDVYYNLTLKTMMGIEWVHRFCPQAAFVMKTDSDMFINVDYLTELLLKKNRTTRFFTGFLKLNEFP
IRQPFSKWFVSKSEYPWDRYPPFCSGTGYVFSGDVASQVYNVSKSVPYIKLEDVFVGLCLERLNIRLEELHSQPTFFPGG
LRFSVCLFRRIVACHFIKPRTLLDYWQALENSRGEDCP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;FKEQSFVYKKDGNFLKLPDTDCRQTPPFLVLLVTSSHKQLAERMAIRQTWGKERMVKGKQLKTFFLLGTTSSAAETKEVD
QESQRHGDIIQKDFLDVYYNLTLKTMMGIEWVHRFCPQAAFVMKTDSDMFINVDYLTELLLKKNRTTRFFTGFLKLNEFP
IRQPFSKWFVSKSEYPWDRYPPFCSGTGYVFSGDVASQVYNVSKSVPYIKLEDVFVGLCLERLNIRLEELHSQPTFFPGG
LRFSVCLFRRIVACHFIKPRTLLDYWQALENSRGEDCP
;
_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 
7  'MANGANESE (II) ION'                                                                            MN  
8  "URIDINE-5'-DIPHOSPHATE"                                                                        UDP 
9  '2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL' B3P 
10 'DI(HYDROXYETHYL)ETHER'                                                                         PEG 
11 beta-D-galactopyranose                                                                          GAL 
12 water                                                                                           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PHE n 
1 2   LYS n 
1 3   GLU n 
1 4   GLN n 
1 5   SER n 
1 6   PHE n 
1 7   VAL n 
1 8   TYR n 
1 9   LYS n 
1 10  LYS n 
1 11  ASP n 
1 12  GLY n 
1 13  ASN n 
1 14  PHE n 
1 15  LEU n 
1 16  LYS n 
1 17  LEU n 
1 18  PRO n 
1 19  ASP n 
1 20  THR n 
1 21  ASP n 
1 22  CYS n 
1 23  ARG n 
1 24  GLN n 
1 25  THR n 
1 26  PRO n 
1 27  PRO n 
1 28  PHE n 
1 29  LEU n 
1 30  VAL n 
1 31  LEU n 
1 32  LEU n 
1 33  VAL n 
1 34  THR n 
1 35  SER n 
1 36  SER n 
1 37  HIS n 
1 38  LYS n 
1 39  GLN n 
1 40  LEU n 
1 41  ALA n 
1 42  GLU n 
1 43  ARG n 
1 44  MET n 
1 45  ALA n 
1 46  ILE n 
1 47  ARG n 
1 48  GLN n 
1 49  THR n 
1 50  TRP n 
1 51  GLY n 
1 52  LYS n 
1 53  GLU n 
1 54  ARG n 
1 55  MET n 
1 56  VAL n 
1 57  LYS n 
1 58  GLY n 
1 59  LYS n 
1 60  GLN n 
1 61  LEU n 
1 62  LYS n 
1 63  THR n 
1 64  PHE n 
1 65  PHE n 
1 66  LEU n 
1 67  LEU n 
1 68  GLY n 
1 69  THR n 
1 70  THR n 
1 71  SER n 
1 72  SER n 
1 73  ALA n 
1 74  ALA n 
1 75  GLU n 
1 76  THR n 
1 77  LYS n 
1 78  GLU n 
1 79  VAL n 
1 80  ASP n 
1 81  GLN n 
1 82  GLU n 
1 83  SER n 
1 84  GLN n 
1 85  ARG n 
1 86  HIS n 
1 87  GLY n 
1 88  ASP n 
1 89  ILE n 
1 90  ILE n 
1 91  GLN n 
1 92  LYS n 
1 93  ASP n 
1 94  PHE n 
1 95  LEU n 
1 96  ASP n 
1 97  VAL n 
1 98  TYR n 
1 99  TYR n 
1 100 ASN n 
1 101 LEU n 
1 102 THR n 
1 103 LEU n 
1 104 LYS n 
1 105 THR n 
1 106 MET n 
1 107 MET n 
1 108 GLY n 
1 109 ILE n 
1 110 GLU n 
1 111 TRP n 
1 112 VAL n 
1 113 HIS n 
1 114 ARG n 
1 115 PHE n 
1 116 CYS n 
1 117 PRO n 
1 118 GLN n 
1 119 ALA n 
1 120 ALA n 
1 121 PHE n 
1 122 VAL n 
1 123 MET n 
1 124 LYS n 
1 125 THR n 
1 126 ASP n 
1 127 SER n 
1 128 ASP n 
1 129 MET n 
1 130 PHE n 
1 131 ILE n 
1 132 ASN n 
1 133 VAL n 
1 134 ASP n 
1 135 TYR n 
1 136 LEU n 
1 137 THR n 
1 138 GLU n 
1 139 LEU n 
1 140 LEU n 
1 141 LEU n 
1 142 LYS n 
1 143 LYS n 
1 144 ASN n 
1 145 ARG n 
1 146 THR n 
1 147 THR n 
1 148 ARG n 
1 149 PHE n 
1 150 PHE n 
1 151 THR n 
1 152 GLY n 
1 153 PHE n 
1 154 LEU n 
1 155 LYS n 
1 156 LEU n 
1 157 ASN n 
1 158 GLU n 
1 159 PHE n 
1 160 PRO n 
1 161 ILE n 
1 162 ARG n 
1 163 GLN n 
1 164 PRO n 
1 165 PHE n 
1 166 SER n 
1 167 LYS n 
1 168 TRP n 
1 169 PHE n 
1 170 VAL n 
1 171 SER n 
1 172 LYS n 
1 173 SER n 
1 174 GLU n 
1 175 TYR n 
1 176 PRO n 
1 177 TRP n 
1 178 ASP n 
1 179 ARG n 
1 180 TYR n 
1 181 PRO n 
1 182 PRO n 
1 183 PHE n 
1 184 CYS n 
1 185 SER n 
1 186 GLY n 
1 187 THR n 
1 188 GLY n 
1 189 TYR n 
1 190 VAL n 
1 191 PHE n 
1 192 SER n 
1 193 GLY n 
1 194 ASP n 
1 195 VAL n 
1 196 ALA n 
1 197 SER n 
1 198 GLN n 
1 199 VAL n 
1 200 TYR n 
1 201 ASN n 
1 202 VAL n 
1 203 SER n 
1 204 LYS n 
1 205 SER n 
1 206 VAL n 
1 207 PRO n 
1 208 TYR n 
1 209 ILE n 
1 210 LYS n 
1 211 LEU n 
1 212 GLU n 
1 213 ASP n 
1 214 VAL n 
1 215 PHE n 
1 216 VAL n 
1 217 GLY n 
1 218 LEU n 
1 219 CYS n 
1 220 LEU n 
1 221 GLU n 
1 222 ARG n 
1 223 LEU n 
1 224 ASN n 
1 225 ILE n 
1 226 ARG n 
1 227 LEU n 
1 228 GLU n 
1 229 GLU n 
1 230 LEU n 
1 231 HIS n 
1 232 SER n 
1 233 GLN n 
1 234 PRO n 
1 235 THR n 
1 236 PHE n 
1 237 PHE n 
1 238 PRO n 
1 239 GLY n 
1 240 GLY n 
1 241 LEU n 
1 242 ARG n 
1 243 PHE n 
1 244 SER n 
1 245 VAL n 
1 246 CYS n 
1 247 LEU n 
1 248 PHE n 
1 249 ARG n 
1 250 ARG n 
1 251 ILE n 
1 252 VAL n 
1 253 ALA n 
1 254 CYS n 
1 255 HIS n 
1 256 PHE n 
1 257 ILE n 
1 258 LYS n 
1 259 PRO n 
1 260 ARG n 
1 261 THR n 
1 262 LEU n 
1 263 LEU n 
1 264 ASP n 
1 265 TYR n 
1 266 TRP n 
1 267 GLN n 
1 268 ALA n 
1 269 LEU n 
1 270 GLU n 
1 271 ASN n 
1 272 SER n 
1 273 ARG n 
1 274 GLY n 
1 275 GLU n 
1 276 ASP n 
1 277 CYS n 
1 278 PRO 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                   278 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 B3GALT5 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            Sf9 
_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_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
3 oligosaccharide 
4 oligosaccharide 
5 oligosaccharide 
6 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1  2 DGlcpNAcb1-4DGlcpNAcb1- 'Glycam Condensed Sequence' GMML       1.0   
2  2 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1' WURCS                       PDB2Glycan 1.1.0 
3  2 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}' LINUCS                      PDB-CARE   ?     
4  3 LFucpa1-6DGlcpNAcb1- 'Glycam Condensed Sequence' GMML       1.0   
5  3 'WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2/a6-b1' WURCS                       PDB2Glycan 1.1.0 
6  3 '[]{[(4+1)][b-D-GlcpNAc]{[(6+1)][a-L-Fucp]{}}}' LINUCS                      PDB-CARE   ?     
7  4 'DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-' 'Glycam Condensed Sequence' GMML       1.0   
8  4 
'WURCS=2.0/4,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1a_1-5]/1-1-2-3-3-4/a4-b1_a6-f1_b4-c1_c3-d1_c6-e1' 
WURCS                       PDB2Glycan 1.1.0 
9  4 
'[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}[(6+1)][a-L-Fucp]{}}}'     
LINUCS                      PDB-CARE   ?     
10 5 DGalpNAcb1-3DGalpa1-4DGalpb1-4DGlcpb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
11 5 'WURCS=2.0/4,4,3/[a2122h-1b_1-5][a2112h-1b_1-5][a2112h-1a_1-5][a2112h-1b_1-5_2*NCC/3=O]/1-2-3-4/a4-b1_b4-c1_c3-d1' WURCS 
PDB2Glycan 1.1.0 
12 5 '[][b-D-Glcp]{[(4+1)][b-D-Galp]{[(4+1)][a-D-Galp]{[(3+1)][b-D-GalpNAc]{}}}}' LINUCS                      PDB-CARE   ?     
13 6 DGalpNAcb1-3DGalpa1-4DGalpb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
14 6 'WURCS=2.0/3,3,2/[a2112h-1b_1-5][a2112h-1a_1-5][a2112h-1b_1-5_2*NCC/3=O]/1-2-3/a4-b1_b3-c1' WURCS                       
PDB2Glycan 1.1.0 
15 6 '[][D-1-deoxy-Galp]{[(4+1)][a-D-Galp]{[(3+1)][b-D-GalpNAc]{}}}' LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1  2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2  3 2 FUC C1 O1 1 NAG O6 HO6 sing ? 
3  4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
4  4 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
5  4 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
6  4 5 MAN C1 O1 3 BMA O6 HO6 sing ? 
7  4 6 FUC C1 O1 1 NAG O6 HO6 sing ? 
8  5 2 GAL C1 O1 1 BGC O4 HO4 sing ? 
9  5 3 GLA C1 O1 2 GAL O4 HO4 sing ? 
10 5 4 NGA C1 O1 3 GLA O3 HO3 sing ? 
11 6 2 GLA C1 O1 1 GAL O4 HO4 sing ? 
12 6 3 NGA C1 O1 2 GLA O3 HO3 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'           y ALANINE ? 'C3 H7 N O2'       89.093  
ARG 'L-peptide linking'           y ARGININE ? 'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking'           y ASPARAGINE ? 'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking'           y 'ASPARTIC ACID' ? 'C4 H7 N O4'       133.103 
B3P non-polymer                   . 
'2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL' ? 'C11 H26 N2 O6'    282.334 
BGC 'D-saccharide, beta linking'  . beta-D-glucopyranose 'beta-D-glucose; D-glucose; glucose' 'C6 H12 O6'        180.156 
BMA 'D-saccharide, beta linking'  . beta-D-mannopyranose 'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'        180.156 
CYS 'L-peptide linking'           y CYSTEINE ? 'C3 H7 N O2 S'     121.158 
FUC 'L-saccharide, alpha linking' . alpha-L-fucopyranose 'alpha-L-fucose; 6-deoxy-alpha-L-galactopyranose; L-fucose; fucose' 
'C6 H12 O5'        164.156 
GAL 'D-saccharide, beta linking'  . beta-D-galactopyranose 'beta-D-galactose; D-galactose; galactose' 'C6 H12 O6'        180.156 
GLA 'D-saccharide, alpha linking' . alpha-D-galactopyranose 'alpha-D-galactose; D-galactose; galactose; ALPHA D-GALACTOSE' 
'C6 H12 O6'        180.156 
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 
MAN 'D-saccharide, alpha linking' . alpha-D-mannopyranose 'alpha-D-mannose; D-mannose; mannose' 'C6 H12 O6'        180.156 
MET 'L-peptide linking'           y METHIONINE ? 'C5 H11 N O2 S'    149.211 
MN  non-polymer                   . 'MANGANESE (II) ION' ? 'Mn 2'             54.938  
NAG 'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'      221.208 
NGA 'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-galactopyranose 
;N-acetyl-beta-D-galactosamine; 2-acetamido-2-deoxy-beta-D-galactose; 2-acetamido-2-deoxy-D-galactose; 2-acetamido-2-deoxy-galactose; N-ACETYL-D-GALACTOSAMINE
;
'C8 H15 N O6'      221.208 
PEG non-polymer                   . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3'        106.120 
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 
UDP 'RNA linking'                 . "URIDINE-5'-DIPHOSPHATE" ? 'C9 H14 N2 O12 P2' 404.161 
VAL 'L-peptide linking'           y VALINE ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BGC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpb                           
BGC 'COMMON NAME'                         GMML     1.0 b-D-glucopyranose                
BGC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Glcp                         
BGC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc                              
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                           
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose                
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                         
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                              
FUC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 LFucpa                           
FUC 'COMMON NAME'                         GMML     1.0 a-L-fucopyranose                 
FUC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-L-Fucp                         
FUC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Fuc                              
GAL 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGalpb                           
GAL 'COMMON NAME'                         GMML     1.0 b-D-galactopyranose              
GAL 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Galp                         
GAL 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Gal                              
GLA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGalpa                           
GLA 'COMMON NAME'                         GMML     1.0 a-D-galactopyranose              
GLA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Galp                         
GLA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Gal                              
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                           
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose                
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                         
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                              
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                        
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine   
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                      
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                           
NGA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGalpNAcb                        
NGA 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-galactopyranosamine 
NGA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GalpNAc                      
NGA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GalNAc                           
# 
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   PHE 1   31  ?   ?   ?   A . n 
A 1 2   LYS 2   32  ?   ?   ?   A . n 
A 1 3   GLU 3   33  ?   ?   ?   A . n 
A 1 4   GLN 4   34  ?   ?   ?   A . n 
A 1 5   SER 5   35  ?   ?   ?   A . n 
A 1 6   PHE 6   36  ?   ?   ?   A . n 
A 1 7   VAL 7   37  ?   ?   ?   A . n 
A 1 8   TYR 8   38  ?   ?   ?   A . n 
A 1 9   LYS 9   39  ?   ?   ?   A . n 
A 1 10  LYS 10  40  ?   ?   ?   A . n 
A 1 11  ASP 11  41  ?   ?   ?   A . n 
A 1 12  GLY 12  42  42  GLY GLY A . n 
A 1 13  ASN 13  43  43  ASN ASN A . n 
A 1 14  PHE 14  44  44  PHE PHE A . n 
A 1 15  LEU 15  45  45  LEU LEU A . n 
A 1 16  LYS 16  46  46  LYS LYS A . n 
A 1 17  LEU 17  47  47  LEU LEU A . n 
A 1 18  PRO 18  48  48  PRO PRO A . n 
A 1 19  ASP 19  49  49  ASP ASP A . n 
A 1 20  THR 20  50  50  THR THR A . n 
A 1 21  ASP 21  51  51  ASP ASP A . n 
A 1 22  CYS 22  52  52  CYS CYS A . n 
A 1 23  ARG 23  53  53  ARG ARG A . n 
A 1 24  GLN 24  54  54  GLN GLN A . n 
A 1 25  THR 25  55  55  THR THR A . n 
A 1 26  PRO 26  56  56  PRO PRO A . n 
A 1 27  PRO 27  57  57  PRO PRO A . n 
A 1 28  PHE 28  58  58  PHE PHE A . n 
A 1 29  LEU 29  59  59  LEU LEU A . n 
A 1 30  VAL 30  60  60  VAL VAL A . n 
A 1 31  LEU 31  61  61  LEU LEU A . n 
A 1 32  LEU 32  62  62  LEU LEU A . n 
A 1 33  VAL 33  63  63  VAL VAL A . n 
A 1 34  THR 34  64  64  THR THR A . n 
A 1 35  SER 35  65  65  SER SER A . n 
A 1 36  SER 36  66  66  SER SER A . n 
A 1 37  HIS 37  67  67  HIS HIS A . n 
A 1 38  LYS 38  68  68  LYS LYS A . n 
A 1 39  GLN 39  69  69  GLN GLN A . n 
A 1 40  LEU 40  70  70  LEU LEU A . n 
A 1 41  ALA 41  71  71  ALA ALA A . n 
A 1 42  GLU 42  72  72  GLU GLU A . n 
A 1 43  ARG 43  73  73  ARG ARG A . n 
A 1 44  MET 44  74  74  MET MET A . n 
A 1 45  ALA 45  75  75  ALA ALA A . n 
A 1 46  ILE 46  76  76  ILE ILE A . n 
A 1 47  ARG 47  77  77  ARG ARG A . n 
A 1 48  GLN 48  78  78  GLN GLN A . n 
A 1 49  THR 49  79  79  THR THR A . n 
A 1 50  TRP 50  80  80  TRP TRP A . n 
A 1 51  GLY 51  81  81  GLY GLY A . n 
A 1 52  LYS 52  82  82  LYS LYS A . n 
A 1 53  GLU 53  83  83  GLU GLU A . n 
A 1 54  ARG 54  84  84  ARG ARG A . n 
A 1 55  MET 55  85  85  MET MET A . n 
A 1 56  VAL 56  86  86  VAL VAL A . n 
A 1 57  LYS 57  87  87  LYS LYS A . n 
A 1 58  GLY 58  88  88  GLY GLY A . n 
A 1 59  LYS 59  89  89  LYS LYS A . n 
A 1 60  GLN 60  90  90  GLN GLN A . n 
A 1 61  LEU 61  91  91  LEU LEU A . n 
A 1 62  LYS 62  92  92  LYS LYS A . n 
A 1 63  THR 63  93  93  THR THR A . n 
A 1 64  PHE 64  94  94  PHE PHE A . n 
A 1 65  PHE 65  95  95  PHE PHE A . n 
A 1 66  LEU 66  96  96  LEU LEU A . n 
A 1 67  LEU 67  97  97  LEU LEU A . n 
A 1 68  GLY 68  98  98  GLY GLY A . n 
A 1 69  THR 69  99  99  THR THR A . n 
A 1 70  THR 70  100 100 THR THR A . n 
A 1 71  SER 71  101 101 SER SER A . n 
A 1 72  SER 72  102 102 SER SER A . n 
A 1 73  ALA 73  103 103 ALA ALA A . n 
A 1 74  ALA 74  104 104 ALA ALA A . n 
A 1 75  GLU 75  105 105 GLU GLU A . n 
A 1 76  THR 76  106 106 THR THR A . n 
A 1 77  LYS 77  107 107 LYS LYS A . n 
A 1 78  GLU 78  108 108 GLU GLU A . n 
A 1 79  VAL 79  109 109 VAL VAL A . n 
A 1 80  ASP 80  110 110 ASP ASP A . n 
A 1 81  GLN 81  111 111 GLN GLN A . n 
A 1 82  GLU 82  112 112 GLU GLU A . n 
A 1 83  SER 83  113 113 SER SER A . n 
A 1 84  GLN 84  114 114 GLN GLN A . n 
A 1 85  ARG 85  115 115 ARG ARG A . n 
A 1 86  HIS 86  116 116 HIS HIS A . n 
A 1 87  GLY 87  117 117 GLY GLY A . n 
A 1 88  ASP 88  118 118 ASP ASP A . n 
A 1 89  ILE 89  119 119 ILE ILE A . n 
A 1 90  ILE 90  120 120 ILE ILE A . n 
A 1 91  GLN 91  121 121 GLN GLN A . n 
A 1 92  LYS 92  122 122 LYS LYS A . n 
A 1 93  ASP 93  123 123 ASP ASP A . n 
A 1 94  PHE 94  124 124 PHE PHE A . n 
A 1 95  LEU 95  125 125 LEU LEU A . n 
A 1 96  ASP 96  126 126 ASP ASP A . n 
A 1 97  VAL 97  127 127 VAL VAL A . n 
A 1 98  TYR 98  128 128 TYR TYR A . n 
A 1 99  TYR 99  129 129 TYR TYR A . n 
A 1 100 ASN 100 130 130 ASN ASN A . n 
A 1 101 LEU 101 131 131 LEU LEU A . n 
A 1 102 THR 102 132 132 THR THR A . n 
A 1 103 LEU 103 133 133 LEU LEU A . n 
A 1 104 LYS 104 134 134 LYS LYS A . n 
A 1 105 THR 105 135 135 THR THR A . n 
A 1 106 MET 106 136 136 MET MET A . n 
A 1 107 MET 107 137 137 MET MET A . n 
A 1 108 GLY 108 138 138 GLY GLY A . n 
A 1 109 ILE 109 139 139 ILE ILE A . n 
A 1 110 GLU 110 140 140 GLU GLU A . n 
A 1 111 TRP 111 141 141 TRP TRP A . n 
A 1 112 VAL 112 142 142 VAL VAL A . n 
A 1 113 HIS 113 143 143 HIS HIS A . n 
A 1 114 ARG 114 144 144 ARG ARG A . n 
A 1 115 PHE 115 145 145 PHE PHE A . n 
A 1 116 CYS 116 146 146 CYS CYS A . n 
A 1 117 PRO 117 147 147 PRO PRO A . n 
A 1 118 GLN 118 148 148 GLN GLN A . n 
A 1 119 ALA 119 149 149 ALA ALA A . n 
A 1 120 ALA 120 150 150 ALA ALA A . n 
A 1 121 PHE 121 151 151 PHE PHE A . n 
A 1 122 VAL 122 152 152 VAL VAL A . n 
A 1 123 MET 123 153 153 MET MET A . n 
A 1 124 LYS 124 154 154 LYS LYS A . n 
A 1 125 THR 125 155 155 THR THR A . n 
A 1 126 ASP 126 156 156 ASP ASP A . n 
A 1 127 SER 127 157 157 SER SER A . n 
A 1 128 ASP 128 158 158 ASP ASP A . n 
A 1 129 MET 129 159 159 MET MET A . n 
A 1 130 PHE 130 160 160 PHE PHE A . n 
A 1 131 ILE 131 161 161 ILE ILE A . n 
A 1 132 ASN 132 162 162 ASN ASN A . n 
A 1 133 VAL 133 163 163 VAL VAL A . n 
A 1 134 ASP 134 164 164 ASP ASP A . n 
A 1 135 TYR 135 165 165 TYR TYR A . n 
A 1 136 LEU 136 166 166 LEU LEU A . n 
A 1 137 THR 137 167 167 THR THR A . n 
A 1 138 GLU 138 168 168 GLU GLU A . n 
A 1 139 LEU 139 169 169 LEU LEU A . n 
A 1 140 LEU 140 170 170 LEU LEU A . n 
A 1 141 LEU 141 171 171 LEU LEU A . n 
A 1 142 LYS 142 172 172 LYS LYS A . n 
A 1 143 LYS 143 173 173 LYS LYS A . n 
A 1 144 ASN 144 174 174 ASN ASN A . n 
A 1 145 ARG 145 175 175 ARG ARG A . n 
A 1 146 THR 146 176 176 THR THR A . n 
A 1 147 THR 147 177 177 THR THR A . n 
A 1 148 ARG 148 178 178 ARG ARG A . n 
A 1 149 PHE 149 179 179 PHE PHE A . n 
A 1 150 PHE 150 180 180 PHE PHE A . n 
A 1 151 THR 151 181 181 THR THR A . n 
A 1 152 GLY 152 182 182 GLY GLY A . n 
A 1 153 PHE 153 183 183 PHE PHE A . n 
A 1 154 LEU 154 184 184 LEU LEU A . n 
A 1 155 LYS 155 185 185 LYS LYS A . n 
A 1 156 LEU 156 186 186 LEU LEU A . n 
A 1 157 ASN 157 187 187 ASN ASN A . n 
A 1 158 GLU 158 188 188 GLU GLU A . n 
A 1 159 PHE 159 189 189 PHE PHE A . n 
A 1 160 PRO 160 190 190 PRO PRO A . n 
A 1 161 ILE 161 191 191 ILE ILE A . n 
A 1 162 ARG 162 192 192 ARG ARG A . n 
A 1 163 GLN 163 193 193 GLN GLN A . n 
A 1 164 PRO 164 194 194 PRO PRO A . n 
A 1 165 PHE 165 195 195 PHE PHE A . n 
A 1 166 SER 166 196 196 SER SER A . n 
A 1 167 LYS 167 197 197 LYS LYS A . n 
A 1 168 TRP 168 198 198 TRP TRP A . n 
A 1 169 PHE 169 199 199 PHE PHE A . n 
A 1 170 VAL 170 200 200 VAL VAL A . n 
A 1 171 SER 171 201 201 SER SER A . n 
A 1 172 LYS 172 202 202 LYS LYS A . n 
A 1 173 SER 173 203 203 SER SER A . n 
A 1 174 GLU 174 204 204 GLU GLU A . n 
A 1 175 TYR 175 205 205 TYR TYR A . n 
A 1 176 PRO 176 206 206 PRO PRO A . n 
A 1 177 TRP 177 207 207 TRP TRP A . n 
A 1 178 ASP 178 208 208 ASP ASP A . n 
A 1 179 ARG 179 209 209 ARG ARG A . n 
A 1 180 TYR 180 210 210 TYR TYR A . n 
A 1 181 PRO 181 211 211 PRO PRO A . n 
A 1 182 PRO 182 212 212 PRO PRO A . n 
A 1 183 PHE 183 213 213 PHE PHE A . n 
A 1 184 CYS 184 214 214 CYS CYS A . n 
A 1 185 SER 185 215 215 SER SER A . n 
A 1 186 GLY 186 216 216 GLY GLY A . n 
A 1 187 THR 187 217 217 THR THR A . n 
A 1 188 GLY 188 218 218 GLY GLY A . n 
A 1 189 TYR 189 219 219 TYR TYR A . n 
A 1 190 VAL 190 220 220 VAL VAL A . n 
A 1 191 PHE 191 221 221 PHE PHE A . n 
A 1 192 SER 192 222 222 SER SER A . n 
A 1 193 GLY 193 223 223 GLY GLY A . n 
A 1 194 ASP 194 224 224 ASP ASP A . n 
A 1 195 VAL 195 225 225 VAL VAL A . n 
A 1 196 ALA 196 226 226 ALA ALA A . n 
A 1 197 SER 197 227 227 SER SER A . n 
A 1 198 GLN 198 228 228 GLN GLN A . n 
A 1 199 VAL 199 229 229 VAL VAL A . n 
A 1 200 TYR 200 230 230 TYR TYR A . n 
A 1 201 ASN 201 231 231 ASN ASN A . n 
A 1 202 VAL 202 232 232 VAL VAL A . n 
A 1 203 SER 203 233 233 SER SER A . n 
A 1 204 LYS 204 234 234 LYS LYS A . n 
A 1 205 SER 205 235 235 SER SER A . n 
A 1 206 VAL 206 236 236 VAL VAL A . n 
A 1 207 PRO 207 237 237 PRO PRO A . n 
A 1 208 TYR 208 238 238 TYR TYR A . n 
A 1 209 ILE 209 239 239 ILE ILE A . n 
A 1 210 LYS 210 240 240 LYS LYS A . n 
A 1 211 LEU 211 241 241 LEU LEU A . n 
A 1 212 GLU 212 242 242 GLU GLU A . n 
A 1 213 ASP 213 243 243 ASP ASP A . n 
A 1 214 VAL 214 244 244 VAL VAL A . n 
A 1 215 PHE 215 245 245 PHE PHE A . n 
A 1 216 VAL 216 246 246 VAL VAL A . n 
A 1 217 GLY 217 247 247 GLY GLY A . n 
A 1 218 LEU 218 248 248 LEU LEU A . n 
A 1 219 CYS 219 249 249 CYS CYS A . n 
A 1 220 LEU 220 250 250 LEU LEU A . n 
A 1 221 GLU 221 251 251 GLU GLU A . n 
A 1 222 ARG 222 252 252 ARG ARG A . n 
A 1 223 LEU 223 253 253 LEU LEU A . n 
A 1 224 ASN 224 254 254 ASN ASN A . n 
A 1 225 ILE 225 255 255 ILE ILE A . n 
A 1 226 ARG 226 256 256 ARG ARG A . n 
A 1 227 LEU 227 257 257 LEU LEU A . n 
A 1 228 GLU 228 258 258 GLU GLU A . n 
A 1 229 GLU 229 259 259 GLU GLU A . n 
A 1 230 LEU 230 260 260 LEU LEU A . n 
A 1 231 HIS 231 261 261 HIS HIS A . n 
A 1 232 SER 232 262 262 SER SER A . n 
A 1 233 GLN 233 263 263 GLN GLN A . n 
A 1 234 PRO 234 264 264 PRO PRO A . n 
A 1 235 THR 235 265 265 THR THR A . n 
A 1 236 PHE 236 266 266 PHE PHE A . n 
A 1 237 PHE 237 267 267 PHE PHE A . n 
A 1 238 PRO 238 268 268 PRO PRO A . n 
A 1 239 GLY 239 269 269 GLY GLY A . n 
A 1 240 GLY 240 270 270 GLY GLY A . n 
A 1 241 LEU 241 271 271 LEU LEU A . n 
A 1 242 ARG 242 272 272 ARG ARG A . n 
A 1 243 PHE 243 273 273 PHE PHE A . n 
A 1 244 SER 244 274 274 SER SER A . n 
A 1 245 VAL 245 275 275 VAL VAL A . n 
A 1 246 CYS 246 276 276 CYS CYS A . n 
A 1 247 LEU 247 277 277 LEU LEU A . n 
A 1 248 PHE 248 278 278 PHE PHE A . n 
A 1 249 ARG 249 279 279 ARG ARG A . n 
A 1 250 ARG 250 280 280 ARG ARG A . n 
A 1 251 ILE 251 281 281 ILE ILE A . n 
A 1 252 VAL 252 282 282 VAL VAL A . n 
A 1 253 ALA 253 283 283 ALA ALA A . n 
A 1 254 CYS 254 284 284 CYS CYS A . n 
A 1 255 HIS 255 285 285 HIS HIS A . n 
A 1 256 PHE 256 286 286 PHE PHE A . n 
A 1 257 ILE 257 287 287 ILE ILE A . n 
A 1 258 LYS 258 288 288 LYS LYS A . n 
A 1 259 PRO 259 289 289 PRO PRO A . n 
A 1 260 ARG 260 290 290 ARG ARG A . n 
A 1 261 THR 261 291 291 THR THR A . n 
A 1 262 LEU 262 292 292 LEU LEU A . n 
A 1 263 LEU 263 293 293 LEU LEU A . n 
A 1 264 ASP 264 294 294 ASP ASP A . n 
A 1 265 TYR 265 295 295 TYR TYR A . n 
A 1 266 TRP 266 296 296 TRP TRP A . n 
A 1 267 GLN 267 297 297 GLN GLN A . n 
A 1 268 ALA 268 298 298 ALA ALA A . n 
A 1 269 LEU 269 299 299 LEU LEU A . n 
A 1 270 GLU 270 300 300 GLU GLU A . n 
A 1 271 ASN 271 301 301 ASN ASN A . n 
A 1 272 SER 272 302 302 SER SER A . n 
A 1 273 ARG 273 303 303 ARG ARG A . n 
A 1 274 GLY 274 304 304 GLY GLY A . n 
A 1 275 GLU 275 305 305 GLU GLU A . n 
A 1 276 ASP 276 306 306 ASP ASP A . n 
A 1 277 CYS 277 307 307 CYS CYS A . n 
A 1 278 PRO 278 308 308 PRO PRO A . n 
B 1 1   PHE 1   31  ?   ?   ?   B . n 
B 1 2   LYS 2   32  ?   ?   ?   B . n 
B 1 3   GLU 3   33  ?   ?   ?   B . n 
B 1 4   GLN 4   34  ?   ?   ?   B . n 
B 1 5   SER 5   35  ?   ?   ?   B . n 
B 1 6   PHE 6   36  ?   ?   ?   B . n 
B 1 7   VAL 7   37  ?   ?   ?   B . n 
B 1 8   TYR 8   38  ?   ?   ?   B . n 
B 1 9   LYS 9   39  ?   ?   ?   B . n 
B 1 10  LYS 10  40  ?   ?   ?   B . n 
B 1 11  ASP 11  41  ?   ?   ?   B . n 
B 1 12  GLY 12  42  ?   ?   ?   B . n 
B 1 13  ASN 13  43  43  ASN ASN B . n 
B 1 14  PHE 14  44  44  PHE PHE B . n 
B 1 15  LEU 15  45  45  LEU LEU B . n 
B 1 16  LYS 16  46  46  LYS LYS B . n 
B 1 17  LEU 17  47  47  LEU LEU B . n 
B 1 18  PRO 18  48  48  PRO PRO B . n 
B 1 19  ASP 19  49  49  ASP ASP B . n 
B 1 20  THR 20  50  50  THR THR B . n 
B 1 21  ASP 21  51  51  ASP ASP B . n 
B 1 22  CYS 22  52  52  CYS CYS B . n 
B 1 23  ARG 23  53  53  ARG ARG B . n 
B 1 24  GLN 24  54  54  GLN GLN B . n 
B 1 25  THR 25  55  55  THR THR B . n 
B 1 26  PRO 26  56  56  PRO PRO B . n 
B 1 27  PRO 27  57  57  PRO PRO B . n 
B 1 28  PHE 28  58  58  PHE PHE B . n 
B 1 29  LEU 29  59  59  LEU LEU B . n 
B 1 30  VAL 30  60  60  VAL VAL B . n 
B 1 31  LEU 31  61  61  LEU LEU B . n 
B 1 32  LEU 32  62  62  LEU LEU B . n 
B 1 33  VAL 33  63  63  VAL VAL B . n 
B 1 34  THR 34  64  64  THR THR B . n 
B 1 35  SER 35  65  65  SER SER B . n 
B 1 36  SER 36  66  66  SER SER B . n 
B 1 37  HIS 37  67  67  HIS HIS B . n 
B 1 38  LYS 38  68  68  LYS LYS B . n 
B 1 39  GLN 39  69  69  GLN GLN B . n 
B 1 40  LEU 40  70  70  LEU LEU B . n 
B 1 41  ALA 41  71  71  ALA ALA B . n 
B 1 42  GLU 42  72  72  GLU GLU B . n 
B 1 43  ARG 43  73  73  ARG ARG B . n 
B 1 44  MET 44  74  74  MET MET B . n 
B 1 45  ALA 45  75  75  ALA ALA B . n 
B 1 46  ILE 46  76  76  ILE ILE B . n 
B 1 47  ARG 47  77  77  ARG ARG B . n 
B 1 48  GLN 48  78  78  GLN GLN B . n 
B 1 49  THR 49  79  79  THR THR B . n 
B 1 50  TRP 50  80  80  TRP TRP B . n 
B 1 51  GLY 51  81  81  GLY GLY B . n 
B 1 52  LYS 52  82  82  LYS LYS B . n 
B 1 53  GLU 53  83  83  GLU GLU B . n 
B 1 54  ARG 54  84  84  ARG ARG B . n 
B 1 55  MET 55  85  85  MET MET B . n 
B 1 56  VAL 56  86  86  VAL VAL B . n 
B 1 57  LYS 57  87  87  LYS LYS B . n 
B 1 58  GLY 58  88  88  GLY GLY B . n 
B 1 59  LYS 59  89  89  LYS LYS B . n 
B 1 60  GLN 60  90  90  GLN GLN B . n 
B 1 61  LEU 61  91  91  LEU LEU B . n 
B 1 62  LYS 62  92  92  LYS LYS B . n 
B 1 63  THR 63  93  93  THR THR B . n 
B 1 64  PHE 64  94  94  PHE PHE B . n 
B 1 65  PHE 65  95  95  PHE PHE B . n 
B 1 66  LEU 66  96  96  LEU LEU B . n 
B 1 67  LEU 67  97  97  LEU LEU B . n 
B 1 68  GLY 68  98  98  GLY GLY B . n 
B 1 69  THR 69  99  99  THR THR B . n 
B 1 70  THR 70  100 100 THR THR B . n 
B 1 71  SER 71  101 101 SER SER B . n 
B 1 72  SER 72  102 102 SER SER B . n 
B 1 73  ALA 73  103 103 ALA ALA B . n 
B 1 74  ALA 74  104 104 ALA ALA B . n 
B 1 75  GLU 75  105 105 GLU GLU B . n 
B 1 76  THR 76  106 106 THR THR B . n 
B 1 77  LYS 77  107 107 LYS LYS B . n 
B 1 78  GLU 78  108 108 GLU GLU B . n 
B 1 79  VAL 79  109 109 VAL VAL B . n 
B 1 80  ASP 80  110 110 ASP ASP B . n 
B 1 81  GLN 81  111 111 GLN GLN B . n 
B 1 82  GLU 82  112 112 GLU GLU B . n 
B 1 83  SER 83  113 113 SER SER B . n 
B 1 84  GLN 84  114 114 GLN GLN B . n 
B 1 85  ARG 85  115 115 ARG ARG B . n 
B 1 86  HIS 86  116 116 HIS HIS B . n 
B 1 87  GLY 87  117 117 GLY GLY B . n 
B 1 88  ASP 88  118 118 ASP ASP B . n 
B 1 89  ILE 89  119 119 ILE ILE B . n 
B 1 90  ILE 90  120 120 ILE ILE B . n 
B 1 91  GLN 91  121 121 GLN GLN B . n 
B 1 92  LYS 92  122 122 LYS LYS B . n 
B 1 93  ASP 93  123 123 ASP ASP B . n 
B 1 94  PHE 94  124 124 PHE PHE B . n 
B 1 95  LEU 95  125 125 LEU LEU B . n 
B 1 96  ASP 96  126 126 ASP ASP B . n 
B 1 97  VAL 97  127 127 VAL VAL B . n 
B 1 98  TYR 98  128 128 TYR TYR B . n 
B 1 99  TYR 99  129 129 TYR TYR B . n 
B 1 100 ASN 100 130 130 ASN ASN B . n 
B 1 101 LEU 101 131 131 LEU LEU B . n 
B 1 102 THR 102 132 132 THR THR B . n 
B 1 103 LEU 103 133 133 LEU LEU B . n 
B 1 104 LYS 104 134 134 LYS LYS B . n 
B 1 105 THR 105 135 135 THR THR B . n 
B 1 106 MET 106 136 136 MET MET B . n 
B 1 107 MET 107 137 137 MET MET B . n 
B 1 108 GLY 108 138 138 GLY GLY B . n 
B 1 109 ILE 109 139 139 ILE ILE B . n 
B 1 110 GLU 110 140 140 GLU GLU B . n 
B 1 111 TRP 111 141 141 TRP TRP B . n 
B 1 112 VAL 112 142 142 VAL VAL B . n 
B 1 113 HIS 113 143 143 HIS HIS B . n 
B 1 114 ARG 114 144 144 ARG ARG B . n 
B 1 115 PHE 115 145 145 PHE PHE B . n 
B 1 116 CYS 116 146 146 CYS CYS B . n 
B 1 117 PRO 117 147 147 PRO PRO B . n 
B 1 118 GLN 118 148 148 GLN GLN B . n 
B 1 119 ALA 119 149 149 ALA ALA B . n 
B 1 120 ALA 120 150 150 ALA ALA B . n 
B 1 121 PHE 121 151 151 PHE PHE B . n 
B 1 122 VAL 122 152 152 VAL VAL B . n 
B 1 123 MET 123 153 153 MET MET B . n 
B 1 124 LYS 124 154 154 LYS LYS B . n 
B 1 125 THR 125 155 155 THR THR B . n 
B 1 126 ASP 126 156 156 ASP ASP B . n 
B 1 127 SER 127 157 157 SER SER B . n 
B 1 128 ASP 128 158 158 ASP ASP B . n 
B 1 129 MET 129 159 159 MET MET B . n 
B 1 130 PHE 130 160 160 PHE PHE B . n 
B 1 131 ILE 131 161 161 ILE ILE B . n 
B 1 132 ASN 132 162 162 ASN ASN B . n 
B 1 133 VAL 133 163 163 VAL VAL B . n 
B 1 134 ASP 134 164 164 ASP ASP B . n 
B 1 135 TYR 135 165 165 TYR TYR B . n 
B 1 136 LEU 136 166 166 LEU LEU B . n 
B 1 137 THR 137 167 167 THR THR B . n 
B 1 138 GLU 138 168 168 GLU GLU B . n 
B 1 139 LEU 139 169 169 LEU LEU B . n 
B 1 140 LEU 140 170 170 LEU LEU B . n 
B 1 141 LEU 141 171 171 LEU LEU B . n 
B 1 142 LYS 142 172 172 LYS LYS B . n 
B 1 143 LYS 143 173 173 LYS LYS B . n 
B 1 144 ASN 144 174 174 ASN ASN B . n 
B 1 145 ARG 145 175 175 ARG ARG B . n 
B 1 146 THR 146 176 176 THR THR B . n 
B 1 147 THR 147 177 177 THR THR B . n 
B 1 148 ARG 148 178 178 ARG ARG B . n 
B 1 149 PHE 149 179 179 PHE PHE B . n 
B 1 150 PHE 150 180 180 PHE PHE B . n 
B 1 151 THR 151 181 181 THR THR B . n 
B 1 152 GLY 152 182 182 GLY GLY B . n 
B 1 153 PHE 153 183 183 PHE PHE B . n 
B 1 154 LEU 154 184 184 LEU LEU B . n 
B 1 155 LYS 155 185 185 LYS LYS B . n 
B 1 156 LEU 156 186 186 LEU LEU B . n 
B 1 157 ASN 157 187 187 ASN ASN B . n 
B 1 158 GLU 158 188 188 GLU GLU B . n 
B 1 159 PHE 159 189 189 PHE PHE B . n 
B 1 160 PRO 160 190 190 PRO PRO B . n 
B 1 161 ILE 161 191 191 ILE ILE B . n 
B 1 162 ARG 162 192 192 ARG ARG B . n 
B 1 163 GLN 163 193 193 GLN GLN B . n 
B 1 164 PRO 164 194 194 PRO PRO B . n 
B 1 165 PHE 165 195 195 PHE PHE B . n 
B 1 166 SER 166 196 196 SER SER B . n 
B 1 167 LYS 167 197 197 LYS LYS B . n 
B 1 168 TRP 168 198 198 TRP TRP B . n 
B 1 169 PHE 169 199 199 PHE PHE B . n 
B 1 170 VAL 170 200 200 VAL VAL B . n 
B 1 171 SER 171 201 201 SER SER B . n 
B 1 172 LYS 172 202 202 LYS LYS B . n 
B 1 173 SER 173 203 203 SER SER B . n 
B 1 174 GLU 174 204 204 GLU GLU B . n 
B 1 175 TYR 175 205 205 TYR TYR B . n 
B 1 176 PRO 176 206 206 PRO PRO B . n 
B 1 177 TRP 177 207 207 TRP TRP B . n 
B 1 178 ASP 178 208 208 ASP ASP B . n 
B 1 179 ARG 179 209 209 ARG ARG B . n 
B 1 180 TYR 180 210 210 TYR TYR B . n 
B 1 181 PRO 181 211 211 PRO PRO B . n 
B 1 182 PRO 182 212 212 PRO PRO B . n 
B 1 183 PHE 183 213 213 PHE PHE B . n 
B 1 184 CYS 184 214 214 CYS CYS B . n 
B 1 185 SER 185 215 215 SER SER B . n 
B 1 186 GLY 186 216 216 GLY GLY B . n 
B 1 187 THR 187 217 217 THR THR B . n 
B 1 188 GLY 188 218 218 GLY GLY B . n 
B 1 189 TYR 189 219 219 TYR TYR B . n 
B 1 190 VAL 190 220 220 VAL VAL B . n 
B 1 191 PHE 191 221 221 PHE PHE B . n 
B 1 192 SER 192 222 222 SER SER B . n 
B 1 193 GLY 193 223 223 GLY GLY B . n 
B 1 194 ASP 194 224 224 ASP ASP B . n 
B 1 195 VAL 195 225 225 VAL VAL B . n 
B 1 196 ALA 196 226 226 ALA ALA B . n 
B 1 197 SER 197 227 227 SER SER B . n 
B 1 198 GLN 198 228 228 GLN GLN B . n 
B 1 199 VAL 199 229 229 VAL VAL B . n 
B 1 200 TYR 200 230 230 TYR TYR B . n 
B 1 201 ASN 201 231 231 ASN ASN B . n 
B 1 202 VAL 202 232 232 VAL VAL B . n 
B 1 203 SER 203 233 233 SER SER B . n 
B 1 204 LYS 204 234 234 LYS LYS B . n 
B 1 205 SER 205 235 235 SER SER B . n 
B 1 206 VAL 206 236 236 VAL VAL B . n 
B 1 207 PRO 207 237 237 PRO PRO B . n 
B 1 208 TYR 208 238 238 TYR TYR B . n 
B 1 209 ILE 209 239 239 ILE ILE B . n 
B 1 210 LYS 210 240 240 LYS LYS B . n 
B 1 211 LEU 211 241 241 LEU LEU B . n 
B 1 212 GLU 212 242 242 GLU GLU B . n 
B 1 213 ASP 213 243 243 ASP ASP B . n 
B 1 214 VAL 214 244 244 VAL VAL B . n 
B 1 215 PHE 215 245 245 PHE PHE B . n 
B 1 216 VAL 216 246 246 VAL VAL B . n 
B 1 217 GLY 217 247 247 GLY GLY B . n 
B 1 218 LEU 218 248 248 LEU LEU B . n 
B 1 219 CYS 219 249 249 CYS CYS B . n 
B 1 220 LEU 220 250 250 LEU LEU B . n 
B 1 221 GLU 221 251 251 GLU GLU B . n 
B 1 222 ARG 222 252 252 ARG ARG B . n 
B 1 223 LEU 223 253 253 LEU LEU B . n 
B 1 224 ASN 224 254 254 ASN ASN B . n 
B 1 225 ILE 225 255 255 ILE ILE B . n 
B 1 226 ARG 226 256 256 ARG ARG B . n 
B 1 227 LEU 227 257 257 LEU LEU B . n 
B 1 228 GLU 228 258 258 GLU GLU B . n 
B 1 229 GLU 229 259 259 GLU GLU B . n 
B 1 230 LEU 230 260 260 LEU LEU B . n 
B 1 231 HIS 231 261 261 HIS HIS B . n 
B 1 232 SER 232 262 262 SER SER B . n 
B 1 233 GLN 233 263 263 GLN GLN B . n 
B 1 234 PRO 234 264 264 PRO PRO B . n 
B 1 235 THR 235 265 265 THR THR B . n 
B 1 236 PHE 236 266 266 PHE PHE B . n 
B 1 237 PHE 237 267 267 PHE PHE B . n 
B 1 238 PRO 238 268 268 PRO PRO B . n 
B 1 239 GLY 239 269 269 GLY GLY B . n 
B 1 240 GLY 240 270 270 GLY GLY B . n 
B 1 241 LEU 241 271 271 LEU LEU B . n 
B 1 242 ARG 242 272 272 ARG ARG B . n 
B 1 243 PHE 243 273 273 PHE PHE B . n 
B 1 244 SER 244 274 274 SER SER B . n 
B 1 245 VAL 245 275 275 VAL VAL B . n 
B 1 246 CYS 246 276 276 CYS CYS B . n 
B 1 247 LEU 247 277 277 LEU LEU B . n 
B 1 248 PHE 248 278 278 PHE PHE B . n 
B 1 249 ARG 249 279 279 ARG ARG B . n 
B 1 250 ARG 250 280 280 ARG ARG B . n 
B 1 251 ILE 251 281 281 ILE ILE B . n 
B 1 252 VAL 252 282 282 VAL VAL B . n 
B 1 253 ALA 253 283 283 ALA ALA B . n 
B 1 254 CYS 254 284 284 CYS CYS B . n 
B 1 255 HIS 255 285 285 HIS HIS B . n 
B 1 256 PHE 256 286 286 PHE PHE B . n 
B 1 257 ILE 257 287 287 ILE ILE B . n 
B 1 258 LYS 258 288 288 LYS LYS B . n 
B 1 259 PRO 259 289 289 PRO PRO B . n 
B 1 260 ARG 260 290 290 ARG ARG B . n 
B 1 261 THR 261 291 291 THR THR B . n 
B 1 262 LEU 262 292 292 LEU LEU B . n 
B 1 263 LEU 263 293 293 LEU LEU B . n 
B 1 264 ASP 264 294 294 ASP ASP B . n 
B 1 265 TYR 265 295 295 TYR TYR B . n 
B 1 266 TRP 266 296 296 TRP TRP B . n 
B 1 267 GLN 267 297 297 GLN GLN B . n 
B 1 268 ALA 268 298 298 ALA ALA B . n 
B 1 269 LEU 269 299 299 LEU LEU B . n 
B 1 270 GLU 270 300 300 GLU GLU B . n 
B 1 271 ASN 271 301 301 ASN ASN B . n 
B 1 272 SER 272 302 302 SER SER B . n 
B 1 273 ARG 273 303 303 ARG ARG B . n 
B 1 274 GLY 274 304 304 GLY GLY B . n 
B 1 275 GLU 275 305 305 GLU GLU B . n 
B 1 276 ASP 276 306 306 ASP ASP B . n 
B 1 277 CYS 277 307 307 CYS CYS B . n 
B 1 278 PRO 278 308 308 PRO PRO B . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
C 2 NAG 1 E NAG 1 E NAG 1 n 
C 2 NAG 2 E NAG 2 E NAG 2 n 
D 3 NAG 1 F NAG 1 F NAG 2 n 
D 3 FUC 2 F FUC 2 F FUC 3 n 
E 2 NAG 1 G NAG 1 G NAG 1 n 
E 2 NAG 2 G NAG 2 G NAG 2 n 
F 4 NAG 1 H NAG 1 H NAG 1 n 
F 4 NAG 2 H NAG 2 H NAG 2 n 
F 4 BMA 3 H BMA 3 H BMA 3 n 
F 4 MAN 4 H MAN 4 H MAN 4 n 
F 4 MAN 5 H MAN 5 H MAN 5 n 
F 4 FUC 6 H FUC 6 H FUC 6 n 
G 5 BGC 1 D BGC 1 D BGC 5 n 
G 5 GAL 2 D GAL 2 D GAL 4 n 
G 5 GLA 3 D GLA 3 D GLA 3 n 
G 5 NGA 4 D NGA 4 D NGA 2 n 
H 6 GAL 1 I GAL 1 I GAL 3 n 
H 6 GLA 2 I GLA 2 I GLA 2 n 
H 6 NGA 3 I NGA 3 I NGA 1 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 GAL ? ? GAL ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NGA ? ? NGA ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
I 7  MN  1  401 310 MN  MN  A . 
J 8  UDP 1  402 311 UDP UDP A . 
K 9  B3P 1  403 312 B3P BIS A . 
L 10 PEG 1  404 319 PEG PEG A . 
M 10 PEG 1  405 320 PEG PEG A . 
N 11 GAL 1  406 1   GAL GAL A . 
O 7  MN  1  401 310 MN  MN  B . 
P 8  UDP 1  402 311 UDP UDP B . 
Q 9  B3P 1  403 312 B3P BIS B . 
R 12 HOH 1  501 68  HOH HOH A . 
R 12 HOH 2  502 74  HOH HOH A . 
R 12 HOH 3  503 80  HOH HOH A . 
R 12 HOH 4  504 11  HOH HOH A . 
R 12 HOH 5  505 64  HOH HOH A . 
R 12 HOH 6  506 60  HOH HOH A . 
R 12 HOH 7  507 34  HOH HOH A . 
R 12 HOH 8  508 2   HOH HOH A . 
R 12 HOH 9  509 49  HOH HOH A . 
R 12 HOH 10 510 23  HOH HOH A . 
R 12 HOH 11 511 19  HOH HOH A . 
R 12 HOH 12 512 32  HOH HOH A . 
R 12 HOH 13 513 77  HOH HOH A . 
R 12 HOH 14 514 65  HOH HOH A . 
R 12 HOH 15 515 38  HOH HOH A . 
R 12 HOH 16 516 35  HOH HOH A . 
R 12 HOH 17 517 85  HOH HOH A . 
R 12 HOH 18 518 30  HOH HOH A . 
R 12 HOH 19 519 20  HOH HOH A . 
R 12 HOH 20 520 45  HOH HOH A . 
R 12 HOH 21 521 66  HOH HOH A . 
R 12 HOH 22 522 62  HOH HOH A . 
R 12 HOH 23 523 3   HOH HOH A . 
R 12 HOH 24 524 12  HOH HOH A . 
R 12 HOH 25 525 8   HOH HOH A . 
R 12 HOH 26 526 55  HOH HOH A . 
R 12 HOH 27 527 1   HOH HOH A . 
R 12 HOH 28 528 25  HOH HOH A . 
R 12 HOH 29 529 13  HOH HOH A . 
R 12 HOH 30 530 9   HOH HOH A . 
R 12 HOH 31 531 69  HOH HOH A . 
R 12 HOH 32 532 63  HOH HOH A . 
R 12 HOH 33 533 43  HOH HOH A . 
R 12 HOH 34 534 22  HOH HOH A . 
R 12 HOH 35 535 61  HOH HOH A . 
R 12 HOH 36 536 42  HOH HOH A . 
R 12 HOH 37 537 39  HOH HOH A . 
R 12 HOH 38 538 16  HOH HOH A . 
R 12 HOH 39 539 47  HOH HOH A . 
R 12 HOH 40 540 27  HOH HOH A . 
R 12 HOH 41 541 5   HOH HOH A . 
R 12 HOH 42 542 7   HOH HOH A . 
R 12 HOH 43 543 44  HOH HOH A . 
R 12 HOH 44 544 18  HOH HOH A . 
R 12 HOH 45 545 15  HOH HOH A . 
R 12 HOH 46 546 14  HOH HOH A . 
R 12 HOH 47 547 56  HOH HOH A . 
R 12 HOH 48 548 59  HOH HOH A . 
R 12 HOH 49 549 33  HOH HOH A . 
R 12 HOH 50 550 54  HOH HOH A . 
R 12 HOH 51 551 21  HOH HOH A . 
R 12 HOH 52 552 4   HOH HOH A . 
R 12 HOH 53 553 48  HOH HOH A . 
R 12 HOH 54 554 58  HOH HOH A . 
R 12 HOH 55 555 81  HOH HOH A . 
R 12 HOH 56 556 73  HOH HOH A . 
R 12 HOH 57 557 37  HOH HOH A . 
R 12 HOH 58 558 10  HOH HOH A . 
R 12 HOH 59 559 50  HOH HOH A . 
R 12 HOH 60 560 41  HOH HOH A . 
R 12 HOH 61 561 40  HOH HOH A . 
R 12 HOH 62 562 76  HOH HOH A . 
R 12 HOH 63 563 71  HOH HOH A . 
R 12 HOH 64 564 52  HOH HOH A . 
R 12 HOH 65 565 67  HOH HOH A . 
R 12 HOH 66 566 36  HOH HOH A . 
R 12 HOH 67 567 51  HOH HOH A . 
R 12 HOH 68 568 79  HOH HOH A . 
R 12 HOH 69 569 78  HOH HOH A . 
S 12 HOH 1  501 31  HOH HOH B . 
S 12 HOH 2  502 46  HOH HOH B . 
S 12 HOH 3  503 53  HOH HOH B . 
S 12 HOH 4  504 24  HOH HOH B . 
S 12 HOH 5  505 29  HOH HOH B . 
S 12 HOH 6  506 70  HOH HOH B . 
S 12 HOH 7  507 75  HOH HOH B . 
S 12 HOH 8  508 6   HOH HOH B . 
S 12 HOH 9  509 28  HOH HOH B . 
S 12 HOH 10 510 57  HOH HOH B . 
S 12 HOH 11 511 26  HOH HOH B . 
S 12 HOH 12 512 72  HOH HOH B . 
S 12 HOH 13 513 83  HOH HOH B . 
S 12 HOH 14 514 82  HOH HOH B . 
S 12 HOH 15 515 84  HOH HOH B . 
S 12 HOH 16 516 86  HOH HOH B . 
S 12 HOH 17 517 17  HOH HOH B . 
S 12 HOH 18 518 87  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 I GAL 1   ? O1 ? H GAL 1 O1 
2 1 N 1 A GAL 406 ? O1 ? N GAL 1 O1 
# 
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   ? ? ? 1.19.1_4122 1 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? Blu-Ice  ? ? ? .           2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot     ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.709 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZX8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.802 
_cell.length_a_esd                 ? 
_cell.length_b                     86.535 
_cell.length_b_esd                 ? 
_cell.length_c                     87.635 
_cell.length_c_esd                 ? 
_cell.volume                       360708.168 
_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                         8ZX8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_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                   8ZX8 
_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             2.77 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.60 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M BIS-TRIS Propane pH8.5, 0.2M Potassium Sodium Tartrate, 20% w/v PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277.15 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RAYONIX MX300HE' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-06-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_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                        'NSRRC BEAMLINE BL15A1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL15A1 
_diffrn_source.pdbx_synchrotron_site       NSRRC 
# 
_reflns.B_iso_Wilson_estimate                          37.63 
_reflns.entry_id                                       8ZX8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.4 
_reflns.d_resolution_low                               50 
_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                                     24050 
_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                           98 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.85 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.13 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.4 
_reflns_shell.d_res_low                                     2.49 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1042 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               2.6 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          85 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.742 
_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                               50.11 
_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                                 8ZX8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.40 
_refine.ls_d_res_low                             30.72 
_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                     24050 
_refine.ls_number_reflns_R_free                  1170 
_refine.ls_number_reflns_R_work                  22880 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    85.77 
_refine.ls_percent_reflns_R_free                 4.86 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1998 
_refine.ls_R_factor_R_free                       0.2193 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1988 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.8338 
_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                            0.3135 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        30.72 
_refine_hist.number_atoms_solvent             87 
_refine_hist.number_atoms_total               4819 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4382 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         350 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0084  ? 4856 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1975  ? 6574 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0737  ? 765  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0209  ? 786  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.9240 ? 1846 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.40 2.50  . . 69  1272 38.55 . . . . 0.2640 . . . . . . . . . . . 0.3179 
'X-RAY DIFFRACTION' 2.50 2.64  . . 92  2055 61.48 . . . . 0.2542 . . . . . . . . . . . 0.2965 
'X-RAY DIFFRACTION' 2.64 2.80  . . 171 2893 87.69 . . . . 0.2592 . . . . . . . . . . . 0.3021 
'X-RAY DIFFRACTION' 2.80 3.02  . . 145 3297 99.31 . . . . 0.2450 . . . . . . . . . . . 0.2773 
'X-RAY DIFFRACTION' 3.02 3.32  . . 173 3327 99.89 . . . . 0.2299 . . . . . . . . . . . 0.2717 
'X-RAY DIFFRACTION' 3.32 3.80  . . 167 3345 99.94 . . . . 0.2047 . . . . . . . . . . . 0.2284 
'X-RAY DIFFRACTION' 3.80 4.78  . . 176 3318 99.18 . . . . 0.1574 . . . . . . . . . . . 0.1594 
'X-RAY DIFFRACTION' 4.79 30.72 . . 177 3373 99.66 . . . . 0.1691 . . . . . . . . . . . 0.1841 
# 
_struct.entry_id                     8ZX8 
_struct.title                        'Structure-Based Mechanism and Specificity of Human Galactosyltransferase B3GalT5' 
_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        8ZX8 
_struct_keywords.text            
;globo-series glycosphingolipid biosynthesis, Oxocarbenium, SNi-like, SN2-like, double displacement, inverting galactosyltransferase, Michaelis complex, TRANSFERASE
;
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1  ? 
B N N 1  ? 
C N N 2  ? 
D N N 3  ? 
E N N 2  ? 
F N N 4  ? 
G N N 5  ? 
H N N 6  ? 
I N N 7  ? 
J N N 8  ? 
K N N 9  ? 
L N N 10 ? 
M N N 10 ? 
N N N 11 ? 
O N N 7  ? 
P N N 8  ? 
Q N N 9  ? 
R N N 12 ? 
S N N 12 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    B3GT5_HUMAN 
_struct_ref.pdbx_db_accession          Q9Y2C3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;FKEQSFVYKKDGNFLKLPDTDCRQTPPFLVLLVTSSHKQLAERMAIRQTWGKERMVKGKQLKTFFLLGTTSSAAETKEVD
QESQRHGDIIQKDFLDVYYNLTLKTMMGIEWVHRFCPQAAFVMKTDSDMFINVDYLTELLLKKNRTTRFFTGFLKLNEFP
IRQPFSKWFVSKSEYPWDRYPPFCSGTGYVFSGDVASQVYNVSKSVPYIKLEDVFVGLCLERLNIRLEELHSQPTFFPGG
LRFSVCLFRRIVACHFIKPRTLLDYWQALENSRGEDCP
;
_struct_ref.pdbx_align_begin           31 
# 
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 8ZX8 A 1 ? 278 ? Q9Y2C3 31 ? 308 ? 31 308 
2 1 8ZX8 B 1 ? 278 ? Q9Y2C3 31 ? 308 ? 31 308 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
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)' 1660  ? 
1 MORE         -2    ? 
1 'SSA (A^2)'  13370 ? 
2 'ABSA (A^2)' 2260  ? 
2 MORE         8     ? 
2 'SSA (A^2)'  13930 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G,I,J,K,L,M,N,R 
2 1 B,E,F,H,O,P,Q,S       
# 
_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 GLN A 39  ? THR A 49  ? GLN A 69  THR A 79  1 ? 11 
HELX_P HELX_P2  AA2 SER A 72  ? GLY A 87  ? SER A 102 GLY A 117 1 ? 16 
HELX_P HELX_P3  AA3 VAL A 97  ? TYR A 99  ? VAL A 127 TYR A 129 5 ? 3  
HELX_P HELX_P4  AA4 ASN A 100 ? CYS A 116 ? ASN A 130 CYS A 146 1 ? 17 
HELX_P HELX_P5  AA5 ASN A 132 ? ASN A 144 ? ASN A 162 ASN A 174 1 ? 13 
HELX_P HELX_P6  AA6 GLY A 193 ? LYS A 204 ? GLY A 223 LYS A 234 1 ? 12 
HELX_P HELX_P7  AA7 LEU A 211 ? ASN A 224 ? LEU A 241 ASN A 254 1 ? 14 
HELX_P HELX_P8  AA8 SER A 244 ? ARG A 249 ? SER A 274 ARG A 279 1 ? 6  
HELX_P HELX_P9  AA9 LYS A 258 ? SER A 272 ? LYS A 288 SER A 302 1 ? 15 
HELX_P HELX_P10 AB1 GLN B 39  ? THR B 49  ? GLN B 69  THR B 79  1 ? 11 
HELX_P HELX_P11 AB2 SER B 72  ? GLY B 87  ? SER B 102 GLY B 117 1 ? 16 
HELX_P HELX_P12 AB3 VAL B 97  ? TYR B 99  ? VAL B 127 TYR B 129 5 ? 3  
HELX_P HELX_P13 AB4 ASN B 100 ? CYS B 116 ? ASN B 130 CYS B 146 1 ? 17 
HELX_P HELX_P14 AB5 ASN B 132 ? ASN B 144 ? ASN B 162 ASN B 174 1 ? 13 
HELX_P HELX_P15 AB6 GLY B 193 ? LYS B 204 ? GLY B 223 LYS B 234 1 ? 12 
HELX_P HELX_P16 AB7 LEU B 211 ? ASN B 224 ? LEU B 241 ASN B 254 1 ? 14 
HELX_P HELX_P17 AB8 SER B 244 ? ARG B 249 ? SER B 274 ARG B 279 1 ? 6  
HELX_P HELX_P18 AB9 LYS B 258 ? SER B 272 ? LYS B 288 SER B 302 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 22  SG  ? ? ? 1_555 A CYS 116 SG  ? ? A CYS 52  A CYS 146 1_555 ? ? ? ? ? ? ? 2.092 ? ?               
disulf2  disulf ?    ? A CYS 246 SG  ? ? ? 1_555 A CYS 277 SG  ? ? A CYS 276 A CYS 307 1_555 ? ? ? ? ? ? ? 2.020 ? ?               
disulf3  disulf ?    ? B CYS 22  SG  ? ? ? 1_555 B CYS 116 SG  ? ? B CYS 52  B CYS 146 1_555 ? ? ? ? ? ? ? 2.049 ? ?               
disulf4  disulf ?    ? B CYS 246 SG  ? ? ? 1_555 B CYS 277 SG  ? ? B CYS 276 B CYS 307 1_555 ? ? ? ? ? ? ? 2.048 ? ?               
covale1  covale one  ? A ASN 100 ND2 ? ? ? 1_555 C NAG .   C1  ? ? A ASN 130 E NAG 1   1_555 ? ? ? ? ? ? ? 1.455 ? N-Glycosylation 
covale2  covale one  ? A ASN 144 ND2 ? ? ? 1_555 D NAG .   C1  ? ? A ASN 174 F NAG 1   1_555 ? ? ? ? ? ? ? 1.459 ? N-Glycosylation 
covale3  covale one  ? B ASN 100 ND2 ? ? ? 1_555 E NAG .   C1  ? ? B ASN 130 G NAG 1   1_555 ? ? ? ? ? ? ? 1.402 ? N-Glycosylation 
covale4  covale one  ? B ASN 144 ND2 ? ? ? 1_555 F NAG .   C1  ? ? B ASN 174 H NAG 1   1_555 ? ? ? ? ? ? ? 1.421 ? N-Glycosylation 
covale5  covale both ? C NAG .   O4  ? ? ? 1_555 C NAG .   C1  ? ? E NAG 1   E NAG 2   1_555 ? ? ? ? ? ? ? 1.453 ? ?               
covale6  covale both ? D NAG .   O6  ? ? ? 1_555 D FUC .   C1  ? ? F NAG 1   F FUC 2   1_555 ? ? ? ? ? ? ? 1.401 ? ?               
covale7  covale both ? E NAG .   O4  ? ? ? 1_555 E NAG .   C1  ? ? G NAG 1   G NAG 2   1_555 ? ? ? ? ? ? ? 1.396 ? ?               
covale8  covale both ? F NAG .   O4  ? ? ? 1_555 F NAG .   C1  ? ? H NAG 1   H NAG 2   1_555 ? ? ? ? ? ? ? 1.387 ? ?               
covale9  covale both ? F NAG .   O6  ? ? ? 1_555 F FUC .   C1  ? ? H NAG 1   H FUC 6   1_555 ? ? ? ? ? ? ? 1.398 ? ?               
covale10 covale both ? F NAG .   O4  ? ? ? 1_555 F BMA .   C1  ? ? H NAG 2   H BMA 3   1_555 ? ? ? ? ? ? ? 1.392 ? ?               
covale11 covale both ? F BMA .   O3  ? ? ? 1_555 F MAN .   C1  ? ? H BMA 3   H MAN 4   1_555 ? ? ? ? ? ? ? 1.388 ? ?               
covale12 covale both ? F BMA .   O6  ? ? ? 1_555 F MAN .   C1  ? ? H BMA 3   H MAN 5   1_555 ? ? ? ? ? ? ? 1.406 ? ?               
covale13 covale both ? G BGC .   O4  ? ? ? 1_555 G GAL .   C1  ? ? D BGC 1   D GAL 2   1_555 ? ? ? ? ? ? ? 1.390 ? ?               
covale14 covale both ? G GAL .   O4  ? ? ? 1_555 G GLA .   C1  ? ? D GAL 2   D GLA 3   1_555 ? ? ? ? ? ? ? 1.392 ? ?               
covale15 covale both ? G GLA .   O3  ? ? ? 1_555 G NGA .   C1  ? ? D GLA 3   D NGA 4   1_555 ? ? ? ? ? ? ? 1.644 ? ?               
covale16 covale both ? H GAL .   O4  ? ? ? 1_555 H GLA .   C1  ? ? I GAL 1   I GLA 2   1_555 ? ? ? ? ? ? ? 1.440 ? ?               
covale17 covale both ? H GLA .   O3  ? ? ? 1_555 H NGA .   C1  ? ? I GLA 2   I NGA 3   1_555 ? ? ? ? ? ? ? 1.396 ? ?               
metalc1  metalc ?    ? A ASP 128 OD1 ? ? ? 1_555 I MN  .   MN  ? ? A ASP 158 A MN  401 1_555 ? ? ? ? ? ? ? 2.617 ? ?               
metalc2  metalc ?    ? A ASP 128 OD2 ? ? ? 1_555 I MN  .   MN  ? ? A ASP 158 A MN  401 1_555 ? ? ? ? ? ? ? 2.795 ? ?               
metalc3  metalc ?    ? A HIS 255 NE2 ? ? ? 1_555 I MN  .   MN  ? ? A HIS 285 A MN  401 1_555 ? ? ? ? ? ? ? 2.133 ? ?               
metalc4  metalc ?    ? I MN  .   MN  ? ? ? 1_555 J UDP .   O2A ? ? A MN  401 A UDP 402 1_555 ? ? ? ? ? ? ? 2.370 ? ?               
metalc5  metalc ?    ? I MN  .   MN  ? ? ? 1_555 J UDP .   O3B ? ? A MN  401 A UDP 402 1_555 ? ? ? ? ? ? ? 2.115 ? ?               
metalc6  metalc ?    ? I MN  .   MN  ? ? ? 1_555 R HOH .   O   ? ? A MN  401 A HOH 502 1_555 ? ? ? ? ? ? ? 1.851 ? ?               
metalc7  metalc ?    ? B ASP 128 OD1 ? ? ? 1_555 O MN  .   MN  ? ? B ASP 158 B MN  401 1_555 ? ? ? ? ? ? ? 2.675 ? ?               
metalc8  metalc ?    ? B ASP 128 OD2 ? ? ? 1_555 O MN  .   MN  ? ? B ASP 158 B MN  401 1_555 ? ? ? ? ? ? ? 2.735 ? ?               
metalc9  metalc ?    ? B HIS 255 NE2 ? ? ? 1_555 O MN  .   MN  ? ? B HIS 285 B MN  401 1_555 ? ? ? ? ? ? ? 2.185 ? ?               
metalc10 metalc ?    ? O MN  .   MN  ? ? ? 1_555 P UDP .   O2B ? ? B MN  401 B UDP 402 1_555 ? ? ? ? ? ? ? 2.721 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
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  OD1 ? A ASP 128 ? A ASP 158 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 OD2 ? A ASP 128 ? A ASP 158 ? 1_555 48.1  ? 
2  OD1 ? A ASP 128 ? A ASP 158 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 NE2 ? A HIS 255 ? A HIS 285 ? 1_555 85.5  ? 
3  OD2 ? A ASP 128 ? A ASP 158 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 NE2 ? A HIS 255 ? A HIS 285 ? 1_555 73.8  ? 
4  OD1 ? A ASP 128 ? A ASP 158 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 O2A ? J UDP .   ? A UDP 402 ? 1_555 96.1  ? 
5  OD2 ? A ASP 128 ? A ASP 158 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 O2A ? J UDP .   ? A UDP 402 ? 1_555 94.8  ? 
6  NE2 ? A HIS 255 ? A HIS 285 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 O2A ? J UDP .   ? A UDP 402 ? 1_555 163.2 ? 
7  OD1 ? A ASP 128 ? A ASP 158 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 O3B ? J UDP .   ? A UDP 402 ? 1_555 174.1 ? 
8  OD2 ? A ASP 128 ? A ASP 158 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 O3B ? J UDP .   ? A UDP 402 ? 1_555 129.4 ? 
9  NE2 ? A HIS 255 ? A HIS 285 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 O3B ? J UDP .   ? A UDP 402 ? 1_555 98.9  ? 
10 O2A ? J UDP .   ? A UDP 402 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 O3B ? J UDP .   ? A UDP 402 ? 1_555 78.5  ? 
11 OD1 ? A ASP 128 ? A ASP 158 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 O   ? R HOH .   ? A HOH 502 ? 1_555 81.0  ? 
12 OD2 ? A ASP 128 ? A ASP 158 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 O   ? R HOH .   ? A HOH 502 ? 1_555 128.6 ? 
13 NE2 ? A HIS 255 ? A HIS 285 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 O   ? R HOH .   ? A HOH 502 ? 1_555 99.5  ? 
14 O2A ? J UDP .   ? A UDP 402 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 O   ? R HOH .   ? A HOH 502 ? 1_555 97.3  ? 
15 O3B ? J UDP .   ? A UDP 402 ? 1_555 MN ? I MN . ? A MN 401 ? 1_555 O   ? R HOH .   ? A HOH 502 ? 1_555 102.0 ? 
16 OD1 ? B ASP 128 ? B ASP 158 ? 1_555 MN ? O MN . ? B MN 401 ? 1_555 OD2 ? B ASP 128 ? B ASP 158 ? 1_555 48.1  ? 
17 OD1 ? B ASP 128 ? B ASP 158 ? 1_555 MN ? O MN . ? B MN 401 ? 1_555 NE2 ? B HIS 255 ? B HIS 285 ? 1_555 89.4  ? 
18 OD2 ? B ASP 128 ? B ASP 158 ? 1_555 MN ? O MN . ? B MN 401 ? 1_555 NE2 ? B HIS 255 ? B HIS 285 ? 1_555 72.2  ? 
19 OD1 ? B ASP 128 ? B ASP 158 ? 1_555 MN ? O MN . ? B MN 401 ? 1_555 O2B ? P UDP .   ? B UDP 402 ? 1_555 154.2 ? 
20 OD2 ? B ASP 128 ? B ASP 158 ? 1_555 MN ? O MN . ? B MN 401 ? 1_555 O2B ? P UDP .   ? B UDP 402 ? 1_555 110.2 ? 
21 NE2 ? B HIS 255 ? B HIS 285 ? 1_555 MN ? O MN . ? B MN 401 ? 1_555 O2B ? P UDP .   ? B UDP 402 ? 1_555 96.6  ? 
# 
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 NAG C .   ? ASN A 100 ? NAG E 1   ? 1_555 ASN A 130 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG D .   ? ASN A 144 ? NAG F 1   ? 1_555 ASN A 174 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 NAG E .   ? ASN B 100 ? NAG G 1   ? 1_555 ASN B 130 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4 NAG F .   ? ASN B 144 ? NAG H 1   ? 1_555 ASN B 174 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5 CYS A 22  ? CYS A 116 ? CYS A 52  ? 1_555 CYS A 146 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6 CYS A 246 ? CYS A 277 ? CYS A 276 ? 1_555 CYS A 307 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7 CYS B 22  ? CYS B 116 ? CYS B 52  ? 1_555 CYS B 146 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8 CYS B 246 ? CYS B 277 ? CYS B 276 ? 1_555 CYS B 307 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 3 ? 
AA5 ? 6 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA7 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 14  ? LYS A 16  ? PHE A 44  LYS A 46  
AA1 2 ILE A 89  ? LEU A 95  ? ILE A 119 LEU A 125 
AA1 3 LYS A 59  ? THR A 69  ? LYS A 89  THR A 99  
AA1 4 ARG A 54  ? VAL A 56  ? ARG A 84  VAL A 86  
AA2 1 PHE A 14  ? LYS A 16  ? PHE A 44  LYS A 46  
AA2 2 ILE A 89  ? LEU A 95  ? ILE A 119 LEU A 125 
AA2 3 LYS A 59  ? THR A 69  ? LYS A 89  THR A 99  
AA2 4 LEU A 29  ? THR A 34  ? LEU A 59  THR A 64  
AA2 5 PHE A 121 ? THR A 125 ? PHE A 151 THR A 155 
AA2 6 PHE A 183 ? SER A 192 ? PHE A 213 SER A 222 
AA2 7 PHE A 150 ? LYS A 155 ? PHE A 180 LYS A 185 
AA3 1 MET A 129 ? ILE A 131 ? MET A 159 ILE A 161 
AA3 2 ALA A 253 ? HIS A 255 ? ALA A 283 HIS A 285 
AA3 3 PHE A 236 ? PHE A 237 ? PHE A 266 PHE A 267 
AA4 1 ARG B 54  ? VAL B 56  ? ARG B 84  VAL B 86  
AA4 2 LYS B 59  ? THR B 69  ? LYS B 89  THR B 99  
AA4 3 ILE B 89  ? LEU B 95  ? ILE B 119 LEU B 125 
AA5 1 ARG B 54  ? VAL B 56  ? ARG B 84  VAL B 86  
AA5 2 LYS B 59  ? THR B 69  ? LYS B 89  THR B 99  
AA5 3 LEU B 29  ? THR B 34  ? LEU B 59  THR B 64  
AA5 4 PHE B 121 ? ASP B 126 ? PHE B 151 ASP B 156 
AA5 5 GLY B 188 ? SER B 192 ? GLY B 218 SER B 222 
AA5 6 PHE B 150 ? THR B 151 ? PHE B 180 THR B 181 
AA6 1 MET B 129 ? ILE B 131 ? MET B 159 ILE B 161 
AA6 2 ALA B 253 ? HIS B 255 ? ALA B 283 HIS B 285 
AA6 3 PHE B 236 ? PHE B 237 ? PHE B 266 PHE B 267 
AA7 1 LEU B 154 ? LYS B 155 ? LEU B 184 LYS B 185 
AA7 2 PHE B 183 ? CYS B 184 ? PHE B 213 CYS B 214 
# 
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 15  ? N LEU A 45  O GLN A 91  ? O GLN A 121 
AA1 2 3 O PHE A 94  ? O PHE A 124 N THR A 69  ? N THR A 99  
AA1 3 4 O LYS A 59  ? O LYS A 89  N VAL A 56  ? N VAL A 86  
AA2 1 2 N LEU A 15  ? N LEU A 45  O GLN A 91  ? O GLN A 121 
AA2 2 3 O PHE A 94  ? O PHE A 124 N THR A 69  ? N THR A 99  
AA2 3 4 O LEU A 66  ? O LEU A 96  N VAL A 33  ? N VAL A 63  
AA2 4 5 N LEU A 32  ? N LEU A 62  O MET A 123 ? O MET A 153 
AA2 5 6 N VAL A 122 ? N VAL A 152 O PHE A 191 ? O PHE A 221 
AA2 6 7 O PHE A 183 ? O PHE A 213 N LYS A 155 ? N LYS A 185 
AA3 1 2 N PHE A 130 ? N PHE A 160 O CYS A 254 ? O CYS A 284 
AA3 2 3 O HIS A 255 ? O HIS A 285 N PHE A 237 ? N PHE A 267 
AA4 1 2 N VAL B 56  ? N VAL B 86  O LYS B 59  ? O LYS B 89  
AA4 2 3 N THR B 69  ? N THR B 99  O PHE B 94  ? O PHE B 124 
AA5 1 2 N VAL B 56  ? N VAL B 86  O LYS B 59  ? O LYS B 89  
AA5 2 3 O PHE B 64  ? O PHE B 94  N LEU B 31  ? N LEU B 61  
AA5 3 4 N VAL B 30  ? N VAL B 60  O MET B 123 ? O MET B 153 
AA5 4 5 N VAL B 122 ? N VAL B 152 O PHE B 191 ? O PHE B 221 
AA5 5 6 O VAL B 190 ? O VAL B 220 N THR B 151 ? N THR B 181 
AA6 1 2 N PHE B 130 ? N PHE B 160 O CYS B 254 ? O CYS B 284 
AA6 2 3 O HIS B 255 ? O HIS B 285 N PHE B 237 ? N PHE B 267 
AA7 1 2 N LYS B 155 ? N LYS B 185 O PHE B 183 ? O PHE B 213 
# 
_pdbx_entry_details.entry_id                   8ZX8 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O3 
_pdbx_validate_close_contact.auth_asym_id_1   D 
_pdbx_validate_close_contact.auth_comp_id_1   NGA 
_pdbx_validate_close_contact.auth_seq_id_1    4 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   C1 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   GAL 
_pdbx_validate_close_contact.auth_seq_id_2    406 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 43  ? ? 74.71   34.85   
2 1 GLN A 69  ? ? -86.99  47.77   
3 1 THR A 79  ? ? -112.02 -113.47 
4 1 CYS A 146 ? ? -143.68 52.27   
5 1 ASP A 158 ? ? -93.49  59.71   
6 1 GLN B 69  ? ? -83.27  45.32   
7 1 THR B 79  ? ? -112.05 -116.85 
8 1 CYS B 146 ? ? -151.90 47.90   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 84  ? ? 0.107 'SIDE CHAIN' 
2 1 ARG A 209 ? ? 0.217 'SIDE CHAIN' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         8.87347452071 
_pdbx_refine_tls.origin_y         8.2221905263 
_pdbx_refine_tls.origin_z         15.0324233144 
_pdbx_refine_tls.T[1][1]          0.473818869028 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0510981919592 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.080332225961 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.204633413476 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0181692539603 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.403105237756 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.296576063697 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.238363961811 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.645163583511 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.18815894154 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0820303737001 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.60009434428 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0288431231377 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.12041344341 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0219745145461 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.250969223847 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.00374618588802 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0199151746183 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.124903089459 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.146515221887 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0215606681804 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   all 
# 
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 PHE 31 ? A PHE 1  
2  1 Y 1 A LYS 32 ? A LYS 2  
3  1 Y 1 A GLU 33 ? A GLU 3  
4  1 Y 1 A GLN 34 ? A GLN 4  
5  1 Y 1 A SER 35 ? A SER 5  
6  1 Y 1 A PHE 36 ? A PHE 6  
7  1 Y 1 A VAL 37 ? A VAL 7  
8  1 Y 1 A TYR 38 ? A TYR 8  
9  1 Y 1 A LYS 39 ? A LYS 9  
10 1 Y 1 A LYS 40 ? A LYS 10 
11 1 Y 1 A ASP 41 ? A ASP 11 
12 1 Y 1 B PHE 31 ? B PHE 1  
13 1 Y 1 B LYS 32 ? B LYS 2  
14 1 Y 1 B GLU 33 ? B GLU 3  
15 1 Y 1 B GLN 34 ? B GLN 4  
16 1 Y 1 B SER 35 ? B SER 5  
17 1 Y 1 B PHE 36 ? B PHE 6  
18 1 Y 1 B VAL 37 ? B VAL 7  
19 1 Y 1 B TYR 38 ? B TYR 8  
20 1 Y 1 B LYS 39 ? B LYS 9  
21 1 Y 1 B LYS 40 ? B LYS 10 
22 1 Y 1 B ASP 41 ? B ASP 11 
23 1 Y 1 B GLY 42 ? B GLY 12 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
B3P C1     C  N N 74  
B3P C2     C  N N 75  
B3P C3     C  N N 76  
B3P N1     N  N N 77  
B3P C4     C  N N 78  
B3P C5     C  N N 79  
B3P C6     C  N N 80  
B3P C7     C  N N 81  
B3P N2     N  N N 82  
B3P C8     C  N N 83  
B3P C9     C  N N 84  
B3P C10    C  N N 85  
B3P C11    C  N N 86  
B3P O1     O  N N 87  
B3P O2     O  N N 88  
B3P O3     O  N N 89  
B3P O4     O  N N 90  
B3P O5     O  N N 91  
B3P O6     O  N N 92  
B3P H11    H  N N 93  
B3P H12    H  N N 94  
B3P H21    H  N N 95  
B3P H22    H  N N 96  
B3P H31    H  N N 97  
B3P H32    H  N N 98  
B3P HN1    H  N N 99  
B3P H51    H  N N 100 
B3P H52    H  N N 101 
B3P H61    H  N N 102 
B3P H62    H  N N 103 
B3P H71    H  N N 104 
B3P H72    H  N N 105 
B3P HN2    H  N N 106 
B3P H91    H  N N 107 
B3P H92    H  N N 108 
B3P H101   H  N N 109 
B3P H102   H  N N 110 
B3P H111   H  N N 111 
B3P H112   H  N N 112 
B3P HO1    H  N N 113 
B3P HO2    H  N N 114 
B3P HO3    H  N N 115 
B3P HO4    H  N N 116 
B3P HO5    H  N N 117 
B3P HO6    H  N N 118 
BGC C2     C  N R 119 
BGC C3     C  N S 120 
BGC C4     C  N S 121 
BGC C5     C  N R 122 
BGC C6     C  N N 123 
BGC C1     C  N R 124 
BGC O1     O  N N 125 
BGC O2     O  N N 126 
BGC O3     O  N N 127 
BGC O4     O  N N 128 
BGC O5     O  N N 129 
BGC O6     O  N N 130 
BGC H2     H  N N 131 
BGC H3     H  N N 132 
BGC H4     H  N N 133 
BGC H5     H  N N 134 
BGC H61    H  N N 135 
BGC H62    H  N N 136 
BGC H1     H  N N 137 
BGC HO1    H  N N 138 
BGC HO2    H  N N 139 
BGC HO3    H  N N 140 
BGC HO4    H  N N 141 
BGC HO6    H  N N 142 
BMA C1     C  N R 143 
BMA C2     C  N S 144 
BMA C3     C  N S 145 
BMA C4     C  N S 146 
BMA C5     C  N R 147 
BMA C6     C  N N 148 
BMA O1     O  N N 149 
BMA O2     O  N N 150 
BMA O3     O  N N 151 
BMA O4     O  N N 152 
BMA O5     O  N N 153 
BMA O6     O  N N 154 
BMA H1     H  N N 155 
BMA H2     H  N N 156 
BMA H3     H  N N 157 
BMA H4     H  N N 158 
BMA H5     H  N N 159 
BMA H61    H  N N 160 
BMA H62    H  N N 161 
BMA HO1    H  N N 162 
BMA HO2    H  N N 163 
BMA HO3    H  N N 164 
BMA HO4    H  N N 165 
BMA HO6    H  N N 166 
CYS N      N  N N 167 
CYS CA     C  N R 168 
CYS C      C  N N 169 
CYS O      O  N N 170 
CYS CB     C  N N 171 
CYS SG     S  N N 172 
CYS OXT    O  N N 173 
CYS H      H  N N 174 
CYS H2     H  N N 175 
CYS HA     H  N N 176 
CYS HB2    H  N N 177 
CYS HB3    H  N N 178 
CYS HG     H  N N 179 
CYS HXT    H  N N 180 
FUC C1     C  N R 181 
FUC C2     C  N S 182 
FUC C3     C  N R 183 
FUC C4     C  N S 184 
FUC C5     C  N S 185 
FUC C6     C  N N 186 
FUC O1     O  N N 187 
FUC O2     O  N N 188 
FUC O3     O  N N 189 
FUC O4     O  N N 190 
FUC O5     O  N N 191 
FUC H1     H  N N 192 
FUC H2     H  N N 193 
FUC H3     H  N N 194 
FUC H4     H  N N 195 
FUC H5     H  N N 196 
FUC H61    H  N N 197 
FUC H62    H  N N 198 
FUC H63    H  N N 199 
FUC HO1    H  N N 200 
FUC HO2    H  N N 201 
FUC HO3    H  N N 202 
FUC HO4    H  N N 203 
GAL C1     C  N R 204 
GAL C2     C  N R 205 
GAL C3     C  N S 206 
GAL C4     C  N R 207 
GAL C5     C  N R 208 
GAL C6     C  N N 209 
GAL O1     O  N N 210 
GAL O2     O  N N 211 
GAL O3     O  N N 212 
GAL O4     O  N N 213 
GAL O5     O  N N 214 
GAL O6     O  N N 215 
GAL H1     H  N N 216 
GAL H2     H  N N 217 
GAL H3     H  N N 218 
GAL H4     H  N N 219 
GAL H5     H  N N 220 
GAL H61    H  N N 221 
GAL H62    H  N N 222 
GAL HO1    H  N N 223 
GAL HO2    H  N N 224 
GAL HO3    H  N N 225 
GAL HO4    H  N N 226 
GAL HO6    H  N N 227 
GLA C1     C  N S 228 
GLA C2     C  N R 229 
GLA C3     C  N S 230 
GLA C4     C  N R 231 
GLA C5     C  N R 232 
GLA C6     C  N N 233 
GLA O1     O  N N 234 
GLA O2     O  N N 235 
GLA O3     O  N N 236 
GLA O4     O  N N 237 
GLA O5     O  N N 238 
GLA O6     O  N N 239 
GLA H1     H  N N 240 
GLA H2     H  N N 241 
GLA H3     H  N N 242 
GLA H4     H  N N 243 
GLA H5     H  N N 244 
GLA H61    H  N N 245 
GLA H62    H  N N 246 
GLA HO1    H  N N 247 
GLA HO2    H  N N 248 
GLA HO3    H  N N 249 
GLA HO4    H  N N 250 
GLA HO6    H  N N 251 
GLN N      N  N N 252 
GLN CA     C  N S 253 
GLN C      C  N N 254 
GLN O      O  N N 255 
GLN CB     C  N N 256 
GLN CG     C  N N 257 
GLN CD     C  N N 258 
GLN OE1    O  N N 259 
GLN NE2    N  N N 260 
GLN OXT    O  N N 261 
GLN H      H  N N 262 
GLN H2     H  N N 263 
GLN HA     H  N N 264 
GLN HB2    H  N N 265 
GLN HB3    H  N N 266 
GLN HG2    H  N N 267 
GLN HG3    H  N N 268 
GLN HE21   H  N N 269 
GLN HE22   H  N N 270 
GLN HXT    H  N N 271 
GLU N      N  N N 272 
GLU CA     C  N S 273 
GLU C      C  N N 274 
GLU O      O  N N 275 
GLU CB     C  N N 276 
GLU CG     C  N N 277 
GLU CD     C  N N 278 
GLU OE1    O  N N 279 
GLU OE2    O  N N 280 
GLU OXT    O  N N 281 
GLU H      H  N N 282 
GLU H2     H  N N 283 
GLU HA     H  N N 284 
GLU HB2    H  N N 285 
GLU HB3    H  N N 286 
GLU HG2    H  N N 287 
GLU HG3    H  N N 288 
GLU HE2    H  N N 289 
GLU HXT    H  N N 290 
GLY N      N  N N 291 
GLY CA     C  N N 292 
GLY C      C  N N 293 
GLY O      O  N N 294 
GLY OXT    O  N N 295 
GLY H      H  N N 296 
GLY H2     H  N N 297 
GLY HA2    H  N N 298 
GLY HA3    H  N N 299 
GLY HXT    H  N N 300 
HIS N      N  N N 301 
HIS CA     C  N S 302 
HIS C      C  N N 303 
HIS O      O  N N 304 
HIS CB     C  N N 305 
HIS CG     C  Y N 306 
HIS ND1    N  Y N 307 
HIS CD2    C  Y N 308 
HIS CE1    C  Y N 309 
HIS NE2    N  Y N 310 
HIS OXT    O  N N 311 
HIS H      H  N N 312 
HIS H2     H  N N 313 
HIS HA     H  N N 314 
HIS HB2    H  N N 315 
HIS HB3    H  N N 316 
HIS HD1    H  N N 317 
HIS HD2    H  N N 318 
HIS HE1    H  N N 319 
HIS HE2    H  N N 320 
HIS HXT    H  N N 321 
HOH O      O  N N 322 
HOH H1     H  N N 323 
HOH H2     H  N N 324 
ILE N      N  N N 325 
ILE CA     C  N S 326 
ILE C      C  N N 327 
ILE O      O  N N 328 
ILE CB     C  N S 329 
ILE CG1    C  N N 330 
ILE CG2    C  N N 331 
ILE CD1    C  N N 332 
ILE OXT    O  N N 333 
ILE H      H  N N 334 
ILE H2     H  N N 335 
ILE HA     H  N N 336 
ILE HB     H  N N 337 
ILE HG12   H  N N 338 
ILE HG13   H  N N 339 
ILE HG21   H  N N 340 
ILE HG22   H  N N 341 
ILE HG23   H  N N 342 
ILE HD11   H  N N 343 
ILE HD12   H  N N 344 
ILE HD13   H  N N 345 
ILE HXT    H  N N 346 
LEU N      N  N N 347 
LEU CA     C  N S 348 
LEU C      C  N N 349 
LEU O      O  N N 350 
LEU CB     C  N N 351 
LEU CG     C  N N 352 
LEU CD1    C  N N 353 
LEU CD2    C  N N 354 
LEU OXT    O  N N 355 
LEU H      H  N N 356 
LEU H2     H  N N 357 
LEU HA     H  N N 358 
LEU HB2    H  N N 359 
LEU HB3    H  N N 360 
LEU HG     H  N N 361 
LEU HD11   H  N N 362 
LEU HD12   H  N N 363 
LEU HD13   H  N N 364 
LEU HD21   H  N N 365 
LEU HD22   H  N N 366 
LEU HD23   H  N N 367 
LEU HXT    H  N N 368 
LYS N      N  N N 369 
LYS CA     C  N S 370 
LYS C      C  N N 371 
LYS O      O  N N 372 
LYS CB     C  N N 373 
LYS CG     C  N N 374 
LYS CD     C  N N 375 
LYS CE     C  N N 376 
LYS NZ     N  N N 377 
LYS OXT    O  N N 378 
LYS H      H  N N 379 
LYS H2     H  N N 380 
LYS HA     H  N N 381 
LYS HB2    H  N N 382 
LYS HB3    H  N N 383 
LYS HG2    H  N N 384 
LYS HG3    H  N N 385 
LYS HD2    H  N N 386 
LYS HD3    H  N N 387 
LYS HE2    H  N N 388 
LYS HE3    H  N N 389 
LYS HZ1    H  N N 390 
LYS HZ2    H  N N 391 
LYS HZ3    H  N N 392 
LYS HXT    H  N N 393 
MAN C1     C  N S 394 
MAN C2     C  N S 395 
MAN C3     C  N S 396 
MAN C4     C  N S 397 
MAN C5     C  N R 398 
MAN C6     C  N N 399 
MAN O1     O  N N 400 
MAN O2     O  N N 401 
MAN O3     O  N N 402 
MAN O4     O  N N 403 
MAN O5     O  N N 404 
MAN O6     O  N N 405 
MAN H1     H  N N 406 
MAN H2     H  N N 407 
MAN H3     H  N N 408 
MAN H4     H  N N 409 
MAN H5     H  N N 410 
MAN H61    H  N N 411 
MAN H62    H  N N 412 
MAN HO1    H  N N 413 
MAN HO2    H  N N 414 
MAN HO3    H  N N 415 
MAN HO4    H  N N 416 
MAN HO6    H  N N 417 
MET N      N  N N 418 
MET CA     C  N S 419 
MET C      C  N N 420 
MET O      O  N N 421 
MET CB     C  N N 422 
MET CG     C  N N 423 
MET SD     S  N N 424 
MET CE     C  N N 425 
MET OXT    O  N N 426 
MET H      H  N N 427 
MET H2     H  N N 428 
MET HA     H  N N 429 
MET HB2    H  N N 430 
MET HB3    H  N N 431 
MET HG2    H  N N 432 
MET HG3    H  N N 433 
MET HE1    H  N N 434 
MET HE2    H  N N 435 
MET HE3    H  N N 436 
MET HXT    H  N N 437 
MN  MN     MN N N 438 
NAG C1     C  N R 439 
NAG C2     C  N R 440 
NAG C3     C  N R 441 
NAG C4     C  N S 442 
NAG C5     C  N R 443 
NAG C6     C  N N 444 
NAG C7     C  N N 445 
NAG C8     C  N N 446 
NAG N2     N  N N 447 
NAG O1     O  N N 448 
NAG O3     O  N N 449 
NAG O4     O  N N 450 
NAG O5     O  N N 451 
NAG O6     O  N N 452 
NAG O7     O  N N 453 
NAG H1     H  N N 454 
NAG H2     H  N N 455 
NAG H3     H  N N 456 
NAG H4     H  N N 457 
NAG H5     H  N N 458 
NAG H61    H  N N 459 
NAG H62    H  N N 460 
NAG H81    H  N N 461 
NAG H82    H  N N 462 
NAG H83    H  N N 463 
NAG HN2    H  N N 464 
NAG HO1    H  N N 465 
NAG HO3    H  N N 466 
NAG HO4    H  N N 467 
NAG HO6    H  N N 468 
NGA C1     C  N R 469 
NGA C2     C  N R 470 
NGA C3     C  N R 471 
NGA C4     C  N R 472 
NGA C5     C  N R 473 
NGA C6     C  N N 474 
NGA C7     C  N N 475 
NGA C8     C  N N 476 
NGA N2     N  N N 477 
NGA O1     O  N N 478 
NGA O3     O  N N 479 
NGA O4     O  N N 480 
NGA O5     O  N N 481 
NGA O6     O  N N 482 
NGA O7     O  N N 483 
NGA H1     H  N N 484 
NGA H2     H  N N 485 
NGA H3     H  N N 486 
NGA H4     H  N N 487 
NGA H5     H  N N 488 
NGA H61    H  N N 489 
NGA H62    H  N N 490 
NGA H81    H  N N 491 
NGA H82    H  N N 492 
NGA H83    H  N N 493 
NGA HN2    H  N N 494 
NGA HO1    H  N N 495 
NGA HO3    H  N N 496 
NGA HO4    H  N N 497 
NGA HO6    H  N N 498 
PEG C1     C  N N 499 
PEG O1     O  N N 500 
PEG C2     C  N N 501 
PEG O2     O  N N 502 
PEG C3     C  N N 503 
PEG C4     C  N N 504 
PEG O4     O  N N 505 
PEG H11    H  N N 506 
PEG H12    H  N N 507 
PEG HO1    H  N N 508 
PEG H21    H  N N 509 
PEG H22    H  N N 510 
PEG H31    H  N N 511 
PEG H32    H  N N 512 
PEG H41    H  N N 513 
PEG H42    H  N N 514 
PEG HO4    H  N N 515 
PHE N      N  N N 516 
PHE CA     C  N S 517 
PHE C      C  N N 518 
PHE O      O  N N 519 
PHE CB     C  N N 520 
PHE CG     C  Y N 521 
PHE CD1    C  Y N 522 
PHE CD2    C  Y N 523 
PHE CE1    C  Y N 524 
PHE CE2    C  Y N 525 
PHE CZ     C  Y N 526 
PHE OXT    O  N N 527 
PHE H      H  N N 528 
PHE H2     H  N N 529 
PHE HA     H  N N 530 
PHE HB2    H  N N 531 
PHE HB3    H  N N 532 
PHE HD1    H  N N 533 
PHE HD2    H  N N 534 
PHE HE1    H  N N 535 
PHE HE2    H  N N 536 
PHE HZ     H  N N 537 
PHE HXT    H  N N 538 
PRO N      N  N N 539 
PRO CA     C  N S 540 
PRO C      C  N N 541 
PRO O      O  N N 542 
PRO CB     C  N N 543 
PRO CG     C  N N 544 
PRO CD     C  N N 545 
PRO OXT    O  N N 546 
PRO H      H  N N 547 
PRO HA     H  N N 548 
PRO HB2    H  N N 549 
PRO HB3    H  N N 550 
PRO HG2    H  N N 551 
PRO HG3    H  N N 552 
PRO HD2    H  N N 553 
PRO HD3    H  N N 554 
PRO HXT    H  N N 555 
SER N      N  N N 556 
SER CA     C  N S 557 
SER C      C  N N 558 
SER O      O  N N 559 
SER CB     C  N N 560 
SER OG     O  N N 561 
SER OXT    O  N N 562 
SER H      H  N N 563 
SER H2     H  N N 564 
SER HA     H  N N 565 
SER HB2    H  N N 566 
SER HB3    H  N N 567 
SER HG     H  N N 568 
SER HXT    H  N N 569 
THR N      N  N N 570 
THR CA     C  N S 571 
THR C      C  N N 572 
THR O      O  N N 573 
THR CB     C  N R 574 
THR OG1    O  N N 575 
THR CG2    C  N N 576 
THR OXT    O  N N 577 
THR H      H  N N 578 
THR H2     H  N N 579 
THR HA     H  N N 580 
THR HB     H  N N 581 
THR HG1    H  N N 582 
THR HG21   H  N N 583 
THR HG22   H  N N 584 
THR HG23   H  N N 585 
THR HXT    H  N N 586 
TRP N      N  N N 587 
TRP CA     C  N S 588 
TRP C      C  N N 589 
TRP O      O  N N 590 
TRP CB     C  N N 591 
TRP CG     C  Y N 592 
TRP CD1    C  Y N 593 
TRP CD2    C  Y N 594 
TRP NE1    N  Y N 595 
TRP CE2    C  Y N 596 
TRP CE3    C  Y N 597 
TRP CZ2    C  Y N 598 
TRP CZ3    C  Y N 599 
TRP CH2    C  Y N 600 
TRP OXT    O  N N 601 
TRP H      H  N N 602 
TRP H2     H  N N 603 
TRP HA     H  N N 604 
TRP HB2    H  N N 605 
TRP HB3    H  N N 606 
TRP HD1    H  N N 607 
TRP HE1    H  N N 608 
TRP HE3    H  N N 609 
TRP HZ2    H  N N 610 
TRP HZ3    H  N N 611 
TRP HH2    H  N N 612 
TRP HXT    H  N N 613 
TYR N      N  N N 614 
TYR CA     C  N S 615 
TYR C      C  N N 616 
TYR O      O  N N 617 
TYR CB     C  N N 618 
TYR CG     C  Y N 619 
TYR CD1    C  Y N 620 
TYR CD2    C  Y N 621 
TYR CE1    C  Y N 622 
TYR CE2    C  Y N 623 
TYR CZ     C  Y N 624 
TYR OH     O  N N 625 
TYR OXT    O  N N 626 
TYR H      H  N N 627 
TYR H2     H  N N 628 
TYR HA     H  N N 629 
TYR HB2    H  N N 630 
TYR HB3    H  N N 631 
TYR HD1    H  N N 632 
TYR HD2    H  N N 633 
TYR HE1    H  N N 634 
TYR HE2    H  N N 635 
TYR HH     H  N N 636 
TYR HXT    H  N N 637 
UDP N1     N  N N 638 
UDP C2     C  N N 639 
UDP N3     N  N N 640 
UDP C4     C  N N 641 
UDP C5     C  N N 642 
UDP C6     C  N N 643 
UDP O2     O  N N 644 
UDP O4     O  N N 645 
UDP "C1'"  C  N R 646 
UDP "C2'"  C  N R 647 
UDP "O2'"  O  N N 648 
UDP "C3'"  C  N S 649 
UDP "C4'"  C  N R 650 
UDP "O4'"  O  N N 651 
UDP "O3'"  O  N N 652 
UDP "C5'"  C  N N 653 
UDP "O5'"  O  N N 654 
UDP PA     P  N N 655 
UDP O1A    O  N N 656 
UDP O2A    O  N N 657 
UDP O3A    O  N N 658 
UDP PB     P  N N 659 
UDP O1B    O  N N 660 
UDP O2B    O  N N 661 
UDP O3B    O  N N 662 
UDP HN3    H  N N 663 
UDP H5     H  N N 664 
UDP H6     H  N N 665 
UDP "H1'"  H  N N 666 
UDP "H2'"  H  N N 667 
UDP "HO2'" H  N N 668 
UDP "H3'"  H  N N 669 
UDP "H4'"  H  N N 670 
UDP "HO3'" H  N N 671 
UDP "H5'1" H  N N 672 
UDP "H5'2" H  N N 673 
UDP HOA2   H  N N 674 
UDP HOB2   H  N N 675 
UDP HOB3   H  N N 676 
VAL N      N  N N 677 
VAL CA     C  N S 678 
VAL C      C  N N 679 
VAL O      O  N N 680 
VAL CB     C  N N 681 
VAL CG1    C  N N 682 
VAL CG2    C  N N 683 
VAL OXT    O  N N 684 
VAL H      H  N N 685 
VAL H2     H  N N 686 
VAL HA     H  N N 687 
VAL HB     H  N N 688 
VAL HG11   H  N N 689 
VAL HG12   H  N N 690 
VAL HG13   H  N N 691 
VAL HG21   H  N N 692 
VAL HG22   H  N N 693 
VAL HG23   H  N N 694 
VAL HXT    H  N N 695 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
B3P C1    C2     sing N N 70  
B3P C1    C3     sing N N 71  
B3P C1    H11    sing N N 72  
B3P C1    H12    sing N N 73  
B3P C2    N2     sing N N 74  
B3P C2    H21    sing N N 75  
B3P C2    H22    sing N N 76  
B3P C3    N1     sing N N 77  
B3P C3    H31    sing N N 78  
B3P C3    H32    sing N N 79  
B3P N1    C4     sing N N 80  
B3P N1    HN1    sing N N 81  
B3P C4    C5     sing N N 82  
B3P C4    C6     sing N N 83  
B3P C4    C7     sing N N 84  
B3P C5    O4     sing N N 85  
B3P C5    H51    sing N N 86  
B3P C5    H52    sing N N 87  
B3P C6    O5     sing N N 88  
B3P C6    H61    sing N N 89  
B3P C6    H62    sing N N 90  
B3P C7    O6     sing N N 91  
B3P C7    H71    sing N N 92  
B3P C7    H72    sing N N 93  
B3P N2    C8     sing N N 94  
B3P N2    HN2    sing N N 95  
B3P C8    C9     sing N N 96  
B3P C8    C10    sing N N 97  
B3P C8    C11    sing N N 98  
B3P C9    O1     sing N N 99  
B3P C9    H91    sing N N 100 
B3P C9    H92    sing N N 101 
B3P C10   O2     sing N N 102 
B3P C10   H101   sing N N 103 
B3P C10   H102   sing N N 104 
B3P C11   O3     sing N N 105 
B3P C11   H111   sing N N 106 
B3P C11   H112   sing N N 107 
B3P O1    HO1    sing N N 108 
B3P O2    HO2    sing N N 109 
B3P O3    HO3    sing N N 110 
B3P O4    HO4    sing N N 111 
B3P O5    HO5    sing N N 112 
B3P O6    HO6    sing N N 113 
BGC C2    C3     sing N N 114 
BGC C2    C1     sing N N 115 
BGC C2    O2     sing N N 116 
BGC C2    H2     sing N N 117 
BGC C3    C4     sing N N 118 
BGC C3    O3     sing N N 119 
BGC C3    H3     sing N N 120 
BGC C4    C5     sing N N 121 
BGC C4    O4     sing N N 122 
BGC C4    H4     sing N N 123 
BGC C5    C6     sing N N 124 
BGC C5    O5     sing N N 125 
BGC C5    H5     sing N N 126 
BGC C6    O6     sing N N 127 
BGC C6    H61    sing N N 128 
BGC C6    H62    sing N N 129 
BGC C1    O1     sing N N 130 
BGC C1    O5     sing N N 131 
BGC C1    H1     sing N N 132 
BGC O1    HO1    sing N N 133 
BGC O2    HO2    sing N N 134 
BGC O3    HO3    sing N N 135 
BGC O4    HO4    sing N N 136 
BGC O6    HO6    sing N N 137 
BMA C1    C2     sing N N 138 
BMA C1    O1     sing N N 139 
BMA C1    O5     sing N N 140 
BMA C1    H1     sing N N 141 
BMA C2    C3     sing N N 142 
BMA C2    O2     sing N N 143 
BMA C2    H2     sing N N 144 
BMA C3    C4     sing N N 145 
BMA C3    O3     sing N N 146 
BMA C3    H3     sing N N 147 
BMA C4    C5     sing N N 148 
BMA C4    O4     sing N N 149 
BMA C4    H4     sing N N 150 
BMA C5    C6     sing N N 151 
BMA C5    O5     sing N N 152 
BMA C5    H5     sing N N 153 
BMA C6    O6     sing N N 154 
BMA C6    H61    sing N N 155 
BMA C6    H62    sing N N 156 
BMA O1    HO1    sing N N 157 
BMA O2    HO2    sing N N 158 
BMA O3    HO3    sing N N 159 
BMA O4    HO4    sing N N 160 
BMA O6    HO6    sing N N 161 
CYS N     CA     sing N N 162 
CYS N     H      sing N N 163 
CYS N     H2     sing N N 164 
CYS CA    C      sing N N 165 
CYS CA    CB     sing N N 166 
CYS CA    HA     sing N N 167 
CYS C     O      doub N N 168 
CYS C     OXT    sing N N 169 
CYS CB    SG     sing N N 170 
CYS CB    HB2    sing N N 171 
CYS CB    HB3    sing N N 172 
CYS SG    HG     sing N N 173 
CYS OXT   HXT    sing N N 174 
FUC C1    C2     sing N N 175 
FUC C1    O1     sing N N 176 
FUC C1    O5     sing N N 177 
FUC C1    H1     sing N N 178 
FUC C2    C3     sing N N 179 
FUC C2    O2     sing N N 180 
FUC C2    H2     sing N N 181 
FUC C3    C4     sing N N 182 
FUC C3    O3     sing N N 183 
FUC C3    H3     sing N N 184 
FUC C4    C5     sing N N 185 
FUC C4    O4     sing N N 186 
FUC C4    H4     sing N N 187 
FUC C5    C6     sing N N 188 
FUC C5    O5     sing N N 189 
FUC C5    H5     sing N N 190 
FUC C6    H61    sing N N 191 
FUC C6    H62    sing N N 192 
FUC C6    H63    sing N N 193 
FUC O1    HO1    sing N N 194 
FUC O2    HO2    sing N N 195 
FUC O3    HO3    sing N N 196 
FUC O4    HO4    sing N N 197 
GAL C1    C2     sing N N 198 
GAL C1    O1     sing N N 199 
GAL C1    O5     sing N N 200 
GAL C1    H1     sing N N 201 
GAL C2    C3     sing N N 202 
GAL C2    O2     sing N N 203 
GAL C2    H2     sing N N 204 
GAL C3    C4     sing N N 205 
GAL C3    O3     sing N N 206 
GAL C3    H3     sing N N 207 
GAL C4    C5     sing N N 208 
GAL C4    O4     sing N N 209 
GAL C4    H4     sing N N 210 
GAL C5    C6     sing N N 211 
GAL C5    O5     sing N N 212 
GAL C5    H5     sing N N 213 
GAL C6    O6     sing N N 214 
GAL C6    H61    sing N N 215 
GAL C6    H62    sing N N 216 
GAL O1    HO1    sing N N 217 
GAL O2    HO2    sing N N 218 
GAL O3    HO3    sing N N 219 
GAL O4    HO4    sing N N 220 
GAL O6    HO6    sing N N 221 
GLA C1    C2     sing N N 222 
GLA C1    O1     sing N N 223 
GLA C1    O5     sing N N 224 
GLA C1    H1     sing N N 225 
GLA C2    C3     sing N N 226 
GLA C2    O2     sing N N 227 
GLA C2    H2     sing N N 228 
GLA C3    C4     sing N N 229 
GLA C3    O3     sing N N 230 
GLA C3    H3     sing N N 231 
GLA C4    C5     sing N N 232 
GLA C4    O4     sing N N 233 
GLA C4    H4     sing N N 234 
GLA C5    C6     sing N N 235 
GLA C5    O5     sing N N 236 
GLA C5    H5     sing N N 237 
GLA C6    O6     sing N N 238 
GLA C6    H61    sing N N 239 
GLA C6    H62    sing N N 240 
GLA O1    HO1    sing N N 241 
GLA O2    HO2    sing N N 242 
GLA O3    HO3    sing N N 243 
GLA O4    HO4    sing N N 244 
GLA O6    HO6    sing N N 245 
GLN N     CA     sing N N 246 
GLN N     H      sing N N 247 
GLN N     H2     sing N N 248 
GLN CA    C      sing N N 249 
GLN CA    CB     sing N N 250 
GLN CA    HA     sing N N 251 
GLN C     O      doub N N 252 
GLN C     OXT    sing N N 253 
GLN CB    CG     sing N N 254 
GLN CB    HB2    sing N N 255 
GLN CB    HB3    sing N N 256 
GLN CG    CD     sing N N 257 
GLN CG    HG2    sing N N 258 
GLN CG    HG3    sing N N 259 
GLN CD    OE1    doub N N 260 
GLN CD    NE2    sing N N 261 
GLN NE2   HE21   sing N N 262 
GLN NE2   HE22   sing N N 263 
GLN OXT   HXT    sing N N 264 
GLU N     CA     sing N N 265 
GLU N     H      sing N N 266 
GLU N     H2     sing N N 267 
GLU CA    C      sing N N 268 
GLU CA    CB     sing N N 269 
GLU CA    HA     sing N N 270 
GLU C     O      doub N N 271 
GLU C     OXT    sing N N 272 
GLU CB    CG     sing N N 273 
GLU CB    HB2    sing N N 274 
GLU CB    HB3    sing N N 275 
GLU CG    CD     sing N N 276 
GLU CG    HG2    sing N N 277 
GLU CG    HG3    sing N N 278 
GLU CD    OE1    doub N N 279 
GLU CD    OE2    sing N N 280 
GLU OE2   HE2    sing N N 281 
GLU OXT   HXT    sing N N 282 
GLY N     CA     sing N N 283 
GLY N     H      sing N N 284 
GLY N     H2     sing N N 285 
GLY CA    C      sing N N 286 
GLY CA    HA2    sing N N 287 
GLY CA    HA3    sing N N 288 
GLY C     O      doub N N 289 
GLY C     OXT    sing N N 290 
GLY OXT   HXT    sing N N 291 
HIS N     CA     sing N N 292 
HIS N     H      sing N N 293 
HIS N     H2     sing N N 294 
HIS CA    C      sing N N 295 
HIS CA    CB     sing N N 296 
HIS CA    HA     sing N N 297 
HIS C     O      doub N N 298 
HIS C     OXT    sing N N 299 
HIS CB    CG     sing N N 300 
HIS CB    HB2    sing N N 301 
HIS CB    HB3    sing N N 302 
HIS CG    ND1    sing Y N 303 
HIS CG    CD2    doub Y N 304 
HIS ND1   CE1    doub Y N 305 
HIS ND1   HD1    sing N N 306 
HIS CD2   NE2    sing Y N 307 
HIS CD2   HD2    sing N N 308 
HIS CE1   NE2    sing Y N 309 
HIS CE1   HE1    sing N N 310 
HIS NE2   HE2    sing N N 311 
HIS OXT   HXT    sing N N 312 
HOH O     H1     sing N N 313 
HOH O     H2     sing N N 314 
ILE N     CA     sing N N 315 
ILE N     H      sing N N 316 
ILE N     H2     sing N N 317 
ILE CA    C      sing N N 318 
ILE CA    CB     sing N N 319 
ILE CA    HA     sing N N 320 
ILE C     O      doub N N 321 
ILE C     OXT    sing N N 322 
ILE CB    CG1    sing N N 323 
ILE CB    CG2    sing N N 324 
ILE CB    HB     sing N N 325 
ILE CG1   CD1    sing N N 326 
ILE CG1   HG12   sing N N 327 
ILE CG1   HG13   sing N N 328 
ILE CG2   HG21   sing N N 329 
ILE CG2   HG22   sing N N 330 
ILE CG2   HG23   sing N N 331 
ILE CD1   HD11   sing N N 332 
ILE CD1   HD12   sing N N 333 
ILE CD1   HD13   sing N N 334 
ILE OXT   HXT    sing N N 335 
LEU N     CA     sing N N 336 
LEU N     H      sing N N 337 
LEU N     H2     sing N N 338 
LEU CA    C      sing N N 339 
LEU CA    CB     sing N N 340 
LEU CA    HA     sing N N 341 
LEU C     O      doub N N 342 
LEU C     OXT    sing N N 343 
LEU CB    CG     sing N N 344 
LEU CB    HB2    sing N N 345 
LEU CB    HB3    sing N N 346 
LEU CG    CD1    sing N N 347 
LEU CG    CD2    sing N N 348 
LEU CG    HG     sing N N 349 
LEU CD1   HD11   sing N N 350 
LEU CD1   HD12   sing N N 351 
LEU CD1   HD13   sing N N 352 
LEU CD2   HD21   sing N N 353 
LEU CD2   HD22   sing N N 354 
LEU CD2   HD23   sing N N 355 
LEU OXT   HXT    sing N N 356 
LYS N     CA     sing N N 357 
LYS N     H      sing N N 358 
LYS N     H2     sing N N 359 
LYS CA    C      sing N N 360 
LYS CA    CB     sing N N 361 
LYS CA    HA     sing N N 362 
LYS C     O      doub N N 363 
LYS C     OXT    sing N N 364 
LYS CB    CG     sing N N 365 
LYS CB    HB2    sing N N 366 
LYS CB    HB3    sing N N 367 
LYS CG    CD     sing N N 368 
LYS CG    HG2    sing N N 369 
LYS CG    HG3    sing N N 370 
LYS CD    CE     sing N N 371 
LYS CD    HD2    sing N N 372 
LYS CD    HD3    sing N N 373 
LYS CE    NZ     sing N N 374 
LYS CE    HE2    sing N N 375 
LYS CE    HE3    sing N N 376 
LYS NZ    HZ1    sing N N 377 
LYS NZ    HZ2    sing N N 378 
LYS NZ    HZ3    sing N N 379 
LYS OXT   HXT    sing N N 380 
MAN C1    C2     sing N N 381 
MAN C1    O1     sing N N 382 
MAN C1    O5     sing N N 383 
MAN C1    H1     sing N N 384 
MAN C2    C3     sing N N 385 
MAN C2    O2     sing N N 386 
MAN C2    H2     sing N N 387 
MAN C3    C4     sing N N 388 
MAN C3    O3     sing N N 389 
MAN C3    H3     sing N N 390 
MAN C4    C5     sing N N 391 
MAN C4    O4     sing N N 392 
MAN C4    H4     sing N N 393 
MAN C5    C6     sing N N 394 
MAN C5    O5     sing N N 395 
MAN C5    H5     sing N N 396 
MAN C6    O6     sing N N 397 
MAN C6    H61    sing N N 398 
MAN C6    H62    sing N N 399 
MAN O1    HO1    sing N N 400 
MAN O2    HO2    sing N N 401 
MAN O3    HO3    sing N N 402 
MAN O4    HO4    sing N N 403 
MAN O6    HO6    sing N N 404 
MET N     CA     sing N N 405 
MET N     H      sing N N 406 
MET N     H2     sing N N 407 
MET CA    C      sing N N 408 
MET CA    CB     sing N N 409 
MET CA    HA     sing N N 410 
MET C     O      doub N N 411 
MET C     OXT    sing N N 412 
MET CB    CG     sing N N 413 
MET CB    HB2    sing N N 414 
MET CB    HB3    sing N N 415 
MET CG    SD     sing N N 416 
MET CG    HG2    sing N N 417 
MET CG    HG3    sing N N 418 
MET SD    CE     sing N N 419 
MET CE    HE1    sing N N 420 
MET CE    HE2    sing N N 421 
MET CE    HE3    sing N N 422 
MET OXT   HXT    sing N N 423 
NAG C1    C2     sing N N 424 
NAG C1    O1     sing N N 425 
NAG C1    O5     sing N N 426 
NAG C1    H1     sing N N 427 
NAG C2    C3     sing N N 428 
NAG C2    N2     sing N N 429 
NAG C2    H2     sing N N 430 
NAG C3    C4     sing N N 431 
NAG C3    O3     sing N N 432 
NAG C3    H3     sing N N 433 
NAG C4    C5     sing N N 434 
NAG C4    O4     sing N N 435 
NAG C4    H4     sing N N 436 
NAG C5    C6     sing N N 437 
NAG C5    O5     sing N N 438 
NAG C5    H5     sing N N 439 
NAG C6    O6     sing N N 440 
NAG C6    H61    sing N N 441 
NAG C6    H62    sing N N 442 
NAG C7    C8     sing N N 443 
NAG C7    N2     sing N N 444 
NAG C7    O7     doub N N 445 
NAG C8    H81    sing N N 446 
NAG C8    H82    sing N N 447 
NAG C8    H83    sing N N 448 
NAG N2    HN2    sing N N 449 
NAG O1    HO1    sing N N 450 
NAG O3    HO3    sing N N 451 
NAG O4    HO4    sing N N 452 
NAG O6    HO6    sing N N 453 
NGA C1    C2     sing N N 454 
NGA C1    O1     sing N N 455 
NGA C1    O5     sing N N 456 
NGA C1    H1     sing N N 457 
NGA C2    C3     sing N N 458 
NGA C2    N2     sing N N 459 
NGA C2    H2     sing N N 460 
NGA C3    C4     sing N N 461 
NGA C3    O3     sing N N 462 
NGA C3    H3     sing N N 463 
NGA C4    C5     sing N N 464 
NGA C4    O4     sing N N 465 
NGA C4    H4     sing N N 466 
NGA C5    C6     sing N N 467 
NGA C5    O5     sing N N 468 
NGA C5    H5     sing N N 469 
NGA C6    O6     sing N N 470 
NGA C6    H61    sing N N 471 
NGA C6    H62    sing N N 472 
NGA C7    C8     sing N N 473 
NGA C7    N2     sing N N 474 
NGA C7    O7     doub N N 475 
NGA C8    H81    sing N N 476 
NGA C8    H82    sing N N 477 
NGA C8    H83    sing N N 478 
NGA N2    HN2    sing N N 479 
NGA O1    HO1    sing N N 480 
NGA O3    HO3    sing N N 481 
NGA O4    HO4    sing N N 482 
NGA O6    HO6    sing N N 483 
PEG C1    O1     sing N N 484 
PEG C1    C2     sing N N 485 
PEG C1    H11    sing N N 486 
PEG C1    H12    sing N N 487 
PEG O1    HO1    sing N N 488 
PEG C2    O2     sing N N 489 
PEG C2    H21    sing N N 490 
PEG C2    H22    sing N N 491 
PEG O2    C3     sing N N 492 
PEG C3    C4     sing N N 493 
PEG C3    H31    sing N N 494 
PEG C3    H32    sing N N 495 
PEG C4    O4     sing N N 496 
PEG C4    H41    sing N N 497 
PEG C4    H42    sing N N 498 
PEG O4    HO4    sing N N 499 
PHE N     CA     sing N N 500 
PHE N     H      sing N N 501 
PHE N     H2     sing N N 502 
PHE CA    C      sing N N 503 
PHE CA    CB     sing N N 504 
PHE CA    HA     sing N N 505 
PHE C     O      doub N N 506 
PHE C     OXT    sing N N 507 
PHE CB    CG     sing N N 508 
PHE CB    HB2    sing N N 509 
PHE CB    HB3    sing N N 510 
PHE CG    CD1    doub Y N 511 
PHE CG    CD2    sing Y N 512 
PHE CD1   CE1    sing Y N 513 
PHE CD1   HD1    sing N N 514 
PHE CD2   CE2    doub Y N 515 
PHE CD2   HD2    sing N N 516 
PHE CE1   CZ     doub Y N 517 
PHE CE1   HE1    sing N N 518 
PHE CE2   CZ     sing Y N 519 
PHE CE2   HE2    sing N N 520 
PHE CZ    HZ     sing N N 521 
PHE OXT   HXT    sing N N 522 
PRO N     CA     sing N N 523 
PRO N     CD     sing N N 524 
PRO N     H      sing N N 525 
PRO CA    C      sing N N 526 
PRO CA    CB     sing N N 527 
PRO CA    HA     sing N N 528 
PRO C     O      doub N N 529 
PRO C     OXT    sing N N 530 
PRO CB    CG     sing N N 531 
PRO CB    HB2    sing N N 532 
PRO CB    HB3    sing N N 533 
PRO CG    CD     sing N N 534 
PRO CG    HG2    sing N N 535 
PRO CG    HG3    sing N N 536 
PRO CD    HD2    sing N N 537 
PRO CD    HD3    sing N N 538 
PRO OXT   HXT    sing N N 539 
SER N     CA     sing N N 540 
SER N     H      sing N N 541 
SER N     H2     sing N N 542 
SER CA    C      sing N N 543 
SER CA    CB     sing N N 544 
SER CA    HA     sing N N 545 
SER C     O      doub N N 546 
SER C     OXT    sing N N 547 
SER CB    OG     sing N N 548 
SER CB    HB2    sing N N 549 
SER CB    HB3    sing N N 550 
SER OG    HG     sing N N 551 
SER OXT   HXT    sing N N 552 
THR N     CA     sing N N 553 
THR N     H      sing N N 554 
THR N     H2     sing N N 555 
THR CA    C      sing N N 556 
THR CA    CB     sing N N 557 
THR CA    HA     sing N N 558 
THR C     O      doub N N 559 
THR C     OXT    sing N N 560 
THR CB    OG1    sing N N 561 
THR CB    CG2    sing N N 562 
THR CB    HB     sing N N 563 
THR OG1   HG1    sing N N 564 
THR CG2   HG21   sing N N 565 
THR CG2   HG22   sing N N 566 
THR CG2   HG23   sing N N 567 
THR OXT   HXT    sing N N 568 
TRP N     CA     sing N N 569 
TRP N     H      sing N N 570 
TRP N     H2     sing N N 571 
TRP CA    C      sing N N 572 
TRP CA    CB     sing N N 573 
TRP CA    HA     sing N N 574 
TRP C     O      doub N N 575 
TRP C     OXT    sing N N 576 
TRP CB    CG     sing N N 577 
TRP CB    HB2    sing N N 578 
TRP CB    HB3    sing N N 579 
TRP CG    CD1    doub Y N 580 
TRP CG    CD2    sing Y N 581 
TRP CD1   NE1    sing Y N 582 
TRP CD1   HD1    sing N N 583 
TRP CD2   CE2    doub Y N 584 
TRP CD2   CE3    sing Y N 585 
TRP NE1   CE2    sing Y N 586 
TRP NE1   HE1    sing N N 587 
TRP CE2   CZ2    sing Y N 588 
TRP CE3   CZ3    doub Y N 589 
TRP CE3   HE3    sing N N 590 
TRP CZ2   CH2    doub Y N 591 
TRP CZ2   HZ2    sing N N 592 
TRP CZ3   CH2    sing Y N 593 
TRP CZ3   HZ3    sing N N 594 
TRP CH2   HH2    sing N N 595 
TRP OXT   HXT    sing N N 596 
TYR N     CA     sing N N 597 
TYR N     H      sing N N 598 
TYR N     H2     sing N N 599 
TYR CA    C      sing N N 600 
TYR CA    CB     sing N N 601 
TYR CA    HA     sing N N 602 
TYR C     O      doub N N 603 
TYR C     OXT    sing N N 604 
TYR CB    CG     sing N N 605 
TYR CB    HB2    sing N N 606 
TYR CB    HB3    sing N N 607 
TYR CG    CD1    doub Y N 608 
TYR CG    CD2    sing Y N 609 
TYR CD1   CE1    sing Y N 610 
TYR CD1   HD1    sing N N 611 
TYR CD2   CE2    doub Y N 612 
TYR CD2   HD2    sing N N 613 
TYR CE1   CZ     doub Y N 614 
TYR CE1   HE1    sing N N 615 
TYR CE2   CZ     sing Y N 616 
TYR CE2   HE2    sing N N 617 
TYR CZ    OH     sing N N 618 
TYR OH    HH     sing N N 619 
TYR OXT   HXT    sing N N 620 
UDP N1    C2     sing N N 621 
UDP N1    C6     sing N N 622 
UDP N1    "C1'"  sing N N 623 
UDP C2    N3     sing N N 624 
UDP C2    O2     doub N N 625 
UDP N3    C4     sing N N 626 
UDP N3    HN3    sing N N 627 
UDP C4    C5     sing N N 628 
UDP C4    O4     doub N N 629 
UDP C5    C6     doub N N 630 
UDP C5    H5     sing N N 631 
UDP C6    H6     sing N N 632 
UDP "C1'" "C2'"  sing N N 633 
UDP "C1'" "O4'"  sing N N 634 
UDP "C1'" "H1'"  sing N N 635 
UDP "C2'" "O2'"  sing N N 636 
UDP "C2'" "C3'"  sing N N 637 
UDP "C2'" "H2'"  sing N N 638 
UDP "O2'" "HO2'" sing N N 639 
UDP "C3'" "C4'"  sing N N 640 
UDP "C3'" "O3'"  sing N N 641 
UDP "C3'" "H3'"  sing N N 642 
UDP "C4'" "O4'"  sing N N 643 
UDP "C4'" "C5'"  sing N N 644 
UDP "C4'" "H4'"  sing N N 645 
UDP "O3'" "HO3'" sing N N 646 
UDP "C5'" "O5'"  sing N N 647 
UDP "C5'" "H5'1" sing N N 648 
UDP "C5'" "H5'2" sing N N 649 
UDP "O5'" PA     sing N N 650 
UDP PA    O1A    doub N N 651 
UDP PA    O2A    sing N N 652 
UDP PA    O3A    sing N N 653 
UDP O2A   HOA2   sing N N 654 
UDP O3A   PB     sing N N 655 
UDP PB    O1B    doub N N 656 
UDP PB    O2B    sing N N 657 
UDP PB    O3B    sing N N 658 
UDP O2B   HOB2   sing N N 659 
UDP O3B   HOB3   sing N N 660 
VAL N     CA     sing N N 661 
VAL N     H      sing N N 662 
VAL N     H2     sing N N 663 
VAL CA    C      sing N N 664 
VAL CA    CB     sing N N 665 
VAL CA    HA     sing N N 666 
VAL C     O      doub N N 667 
VAL C     OXT    sing N N 668 
VAL CB    CG1    sing N N 669 
VAL CB    CG2    sing N N 670 
VAL CB    HB     sing N N 671 
VAL CG1   HG11   sing N N 672 
VAL CG1   HG12   sing N N 673 
VAL CG1   HG13   sing N N 674 
VAL CG2   HG21   sing N N 675 
VAL CG2   HG22   sing N N 676 
VAL CG2   HG23   sing N N 677 
VAL OXT   HXT    sing N N 678 
# 
_pdbx_audit_support.funding_organization   'Academia Sinica (Taiwan)' 
_pdbx_audit_support.country                Taiwan 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 NAG 2 n 
3 NAG 1 n 
3 FUC 2 n 
4 NAG 1 n 
4 NAG 2 n 
4 BMA 3 n 
4 MAN 4 n 
4 MAN 5 n 
4 FUC 6 n 
5 BGC 1 n 
5 GAL 2 n 
5 GLA 3 n 
5 NGA 4 n 
6 GAL 1 n 
6 GLA 2 n 
6 NGA 3 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          
'Sulfur-SAD was used to solve initial phase with 20 sulfur containing atoms found in one asymmetric unit' 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8ZX8 
_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]   0.020920 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002091 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011556 
_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]   0.011468 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H  ? ? 0.51345  0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MN ? ? 20.23591 4.67902 ? ? 2.76514  44.01191 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135  5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . GLY A 1  12  ? 9.82631   20.06264  24.14589  1.000 66.94987  ? 42  GLY A N     1 
ATOM   2    C  CA    . GLY A 1  12  ? 11.07345  20.45246  24.77370  1.000 77.39926  ? 42  GLY A CA    1 
ATOM   3    C  C     . GLY A 1  12  ? 12.33328  19.81925  24.20655  1.000 79.57774  ? 42  GLY A C     1 
ATOM   4    O  O     . GLY A 1  12  ? 13.16930  19.32014  24.96045  1.000 91.04265  ? 42  GLY A O     1 
ATOM   5    N  N     . ASN A 1  13  ? 12.46409  19.83119  22.87653  1.000 63.49900  ? 43  ASN A N     1 
ATOM   6    C  CA    . ASN A 1  13  ? 13.65892  19.34998  22.18038  1.000 58.84602  ? 43  ASN A CA    1 
ATOM   7    C  C     . ASN A 1  13  ? 13.76868  17.82296  22.15541  1.000 56.17938  ? 43  ASN A C     1 
ATOM   8    O  O     . ASN A 1  13  ? 14.87460  17.28779  22.20527  1.000 50.87227  ? 43  ASN A O     1 
ATOM   9    C  CB    . ASN A 1  13  ? 14.94710  19.92179  22.80218  1.000 63.74564  ? 43  ASN A CB    1 
ATOM   10   C  CG    . ASN A 1  13  ? 14.87037  21.41881  23.05915  1.000 84.30879  ? 43  ASN A CG    1 
ATOM   11   O  OD1   . ASN A 1  13  ? 14.16739  22.14990  22.35223  1.000 95.25380  ? 43  ASN A OD1   1 
ATOM   12   N  ND2   . ASN A 1  13  ? 15.60658  21.87873  24.07303  1.000 76.61866  ? 43  ASN A ND2   1 
ATOM   13   N  N     . PHE A 1  14  ? 12.65655  17.10313  22.06058  1.000 50.05681  ? 44  PHE A N     1 
ATOM   14   C  CA    . PHE A 1  14  ? 12.72232  15.64112  22.01761  1.000 36.06166  ? 44  PHE A CA    1 
ATOM   15   C  C     . PHE A 1  14  ? 13.01004  15.16903  20.59659  1.000 45.14086  ? 44  PHE A C     1 
ATOM   16   O  O     . PHE A 1  14  ? 12.37799  15.63311  19.64066  1.000 57.67330  ? 44  PHE A O     1 
ATOM   17   C  CB    . PHE A 1  14  ? 11.41129  15.02734  22.52481  1.000 31.96751  ? 44  PHE A CB    1 
ATOM   18   C  CG    . PHE A 1  14  ? 11.23651  15.12341  24.02184  1.000 41.65150  ? 44  PHE A CG    1 
ATOM   19   C  CD1   . PHE A 1  14  ? 10.75477  16.28251  24.61287  1.000 46.23404  ? 44  PHE A CD1   1 
ATOM   20   C  CD2   . PHE A 1  14  ? 11.56945  14.05238  24.84082  1.000 36.30706  ? 44  PHE A CD2   1 
ATOM   21   C  CE1   . PHE A 1  14  ? 10.59498  16.37357  25.98789  1.000 41.41090  ? 44  PHE A CE1   1 
ATOM   22   C  CE2   . PHE A 1  14  ? 11.41166  14.13445  26.21684  1.000 34.97235  ? 44  PHE A CE2   1 
ATOM   23   C  CZ    . PHE A 1  14  ? 10.93492  15.28354  26.79787  1.000 37.16890  ? 44  PHE A CZ    1 
ATOM   24   N  N     . LEU A 1  15  ? 13.98288  14.26088  20.45948  1.000 47.78857  ? 45  LEU A N     1 
ATOM   25   C  CA    . LEU A 1  15  ? 14.24361  13.64880  19.15646  1.000 44.32053  ? 45  LEU A CA    1 
ATOM   26   C  C     . LEU A 1  15  ? 13.23339  12.55295  18.83263  1.000 39.95719  ? 45  LEU A C     1 
ATOM   27   O  O     . LEU A 1  15  ? 12.83420  12.38898  17.67169  1.000 50.48993  ? 45  LEU A O     1 
ATOM   28   C  CB    . LEU A 1  15  ? 15.66451  13.08657  19.10428  1.000 42.07899  ? 45  LEU A CB    1 
ATOM   29   C  CG    . LEU A 1  15  ? 16.76273  14.00841  19.61510  1.000 46.05056  ? 45  LEU A CG    1 
ATOM   30   C  CD1   . LEU A 1  15  ? 18.12559  13.40019  19.28993  1.000 42.95745  ? 45  LEU A CD1   1 
ATOM   31   C  CD2   . LEU A 1  15  ? 16.61786  15.39942  19.01608  1.000 47.40189  ? 45  LEU A CD2   1 
ATOM   32   N  N     . LYS A 1  16  ? 12.81141  11.79104  19.83771  1.000 42.55734  ? 46  LYS A N     1 
ATOM   33   C  CA    . LYS A 1  16  ? 11.79222  10.76120  19.67789  1.000 36.89357  ? 46  LYS A CA    1 
ATOM   34   C  C     . LYS A 1  16  ? 10.74540  10.89340  20.77403  1.000 41.58522  ? 46  LYS A C     1 
ATOM   35   O  O     . LYS A 1  16  ? 11.07559  11.10538  21.94597  1.000 45.64864  ? 46  LYS A O     1 
ATOM   36   C  CB    . LYS A 1  16  ? 12.42201  9.35410   19.70484  1.000 43.87129  ? 46  LYS A CB    1 
ATOM   37   C  CG    . LYS A 1  16  ? 13.38381  9.10792   18.54671  1.000 49.47325  ? 46  LYS A CG    1 
ATOM   38   C  CD    . LYS A 1  16  ? 13.98159  7.71082   18.58967  1.000 45.18480  ? 46  LYS A CD    1 
ATOM   39   C  CE    . LYS A 1  16  ? 14.72936  7.38867   17.29658  1.000 53.17913  ? 46  LYS A CE    1 
ATOM   40   N  NZ    . LYS A 1  16  ? 15.77948  8.41249   16.99840  1.000 57.55643  ? 46  LYS A NZ    1 
ATOM   41   N  N     . LEU A 1  17  ? 9.47932   10.77258  20.38220  1.000 39.40595  ? 47  LEU A N     1 
ATOM   42   C  CA    . LEU A 1  17  ? 8.33445   10.80679  21.28136  1.000 41.58799  ? 47  LEU A CA    1 
ATOM   43   C  C     . LEU A 1  17  ? 7.47622   9.57392   21.03752  1.000 40.97937  ? 47  LEU A C     1 
ATOM   44   O  O     . LEU A 1  17  ? 7.12502   9.29094   19.87857  1.000 50.87363  ? 47  LEU A O     1 
ATOM   45   C  CB    . LEU A 1  17  ? 7.49662   12.07492  21.07844  1.000 38.10787  ? 47  LEU A CB    1 
ATOM   46   C  CG    . LEU A 1  17  ? 8.03590   13.41785  21.57033  1.000 42.90922  ? 47  LEU A CG    1 
ATOM   47   C  CD1   . LEU A 1  17  ? 6.99903   14.47900  21.25744  1.000 35.81461  ? 47  LEU A CD1   1 
ATOM   48   C  CD2   . LEU A 1  17  ? 8.33910   13.38284  23.05929  1.000 34.39277  ? 47  LEU A CD2   1 
ATOM   49   N  N     . PRO A 1  18  ? 7.09125   8.83101   22.08659  1.000 41.14342  ? 48  PRO A N     1 
ATOM   50   C  CA    . PRO A 1  18  ? 6.21804   7.66314   21.88175  1.000 50.23485  ? 48  PRO A CA    1 
ATOM   51   C  C     . PRO A 1  18  ? 4.86802   8.06134   21.30392  1.000 57.09904  ? 48  PRO A C     1 
ATOM   52   O  O     . PRO A 1  18  ? 4.28524   9.08544   21.67397  1.000 47.76760  ? 48  PRO A O     1 
ATOM   53   C  CB    . PRO A 1  18  ? 6.04814   7.07621   23.28679  1.000 38.07819  ? 48  PRO A CB    1 
ATOM   54   C  CG    . PRO A 1  18  ? 7.09236   7.73307   24.12962  1.000 45.61234  ? 48  PRO A CG    1 
ATOM   55   C  CD    . PRO A 1  18  ? 7.42148   9.05200   23.50154  1.000 41.50772  ? 48  PRO A CD    1 
ATOM   56   N  N     . ASP A 1  19  ? 4.35876   7.19839   20.41602  1.000 70.19574  ? 49  ASP A N     1 
ATOM   57   C  CA    . ASP A 1  19  ? 3.04870   7.34558   19.78119  1.000 72.08910  ? 49  ASP A CA    1 
ATOM   58   C  C     . ASP A 1  19  ? 1.97878   6.95478   20.79235  1.000 69.96177  ? 49  ASP A C     1 
ATOM   59   O  O     . ASP A 1  19  ? 1.37160   5.87987   20.72947  1.000 85.88503  ? 49  ASP A O     1 
ATOM   60   C  CB    . ASP A 1  19  ? 2.97439   6.49855   18.51223  1.000 81.83161  ? 49  ASP A CB    1 
ATOM   61   C  CG    . ASP A 1  19  ? 1.58730   6.51875   17.85742  1.000 101.12026 ? 49  ASP A CG    1 
ATOM   62   O  OD1   . ASP A 1  19  ? 0.63347   7.10092   18.43053  1.000 90.35899  ? 49  ASP A OD1   1 
ATOM   63   O  OD2   . ASP A 1  19  ? 1.44406   5.94574   16.75245  1.000 114.22127 ? 49  ASP A OD2   1 
ATOM   64   N  N     . THR A 1  20  ? 1.78105   7.87883   21.73435  1.000 57.66818  ? 50  THR A N     1 
ATOM   65   C  CA    . THR A 1  20  ? 0.78216   7.64802   22.78650  1.000 67.17709  ? 50  THR A CA    1 
ATOM   66   C  C     . THR A 1  20  ? 0.07840   8.93914   23.06756  1.000 55.24438  ? 50  THR A C     1 
ATOM   67   O  O     . THR A 1  20  ? 0.67754   9.99404   22.84944  1.000 61.53248  ? 50  THR A O     1 
ATOM   68   C  CB    . THR A 1  20  ? 1.43525   7.10596   24.05842  1.000 64.82010  ? 50  THR A CB    1 
ATOM   69   O  OG1   . THR A 1  20  ? 2.39246   8.08182   24.45026  1.000 65.36921  ? 50  THR A OG1   1 
ATOM   70   C  CG2   . THR A 1  20  ? 2.11201   5.76484   23.84437  1.000 68.12225  ? 50  THR A CG2   1 
ATOM   71   N  N     . ASP A 1  21  ? -1.14354  8.84835   23.56973  1.000 59.98556  ? 51  ASP A N     1 
ATOM   72   C  CA    . ASP A 1  21  ? -1.96931  10.01949  23.87181  1.000 50.06045  ? 51  ASP A CA    1 
ATOM   73   C  C     . ASP A 1  21  ? -2.58315  9.86162   25.26490  1.000 61.13417  ? 51  ASP A C     1 
ATOM   74   O  O     . ASP A 1  21  ? -3.67122  9.29580   25.40906  1.000 71.45489  ? 51  ASP A O     1 
ATOM   75   C  CB    . ASP A 1  21  ? -3.04044  10.18362  22.78995  1.000 71.74006  ? 51  ASP A CB    1 
ATOM   76   C  CG    . ASP A 1  21  ? -3.91922  11.40677  22.99604  1.000 83.64484  ? 51  ASP A CG    1 
ATOM   77   O  OD1   . ASP A 1  21  ? -4.32701  11.68887  24.14308  1.000 72.58635  ? 51  ASP A OD1   1 
ATOM   78   O  OD2   . ASP A 1  21  ? -4.21225  12.08679  21.98306  1.000 85.35731  ? 51  ASP A OD2   1 
ATOM   79   N  N     . CYS A 1  22  ? -1.90692  10.39155  26.29179  1.000 53.72750  ? 52  CYS A N     1 
ATOM   80   C  CA    . CYS A 1  22  ? -2.37376  10.21466  27.66586  1.000 55.63655  ? 52  CYS A CA    1 
ATOM   81   C  C     . CYS A 1  22  ? -3.63959  10.99587  27.99101  1.000 55.48335  ? 52  CYS A C     1 
ATOM   82   O  O     . CYS A 1  22  ? -4.31951  10.66801  28.97311  1.000 65.34951  ? 52  CYS A O     1 
ATOM   83   C  CB    . CYS A 1  22  ? -1.28256  10.62252  28.65570  1.000 57.53330  ? 52  CYS A CB    1 
ATOM   84   S  SG    . CYS A 1  22  ? 0.18126   9.61728   28.51252  1.000 62.79611  ? 52  CYS A SG    1 
ATOM   85   N  N     . ARG A 1  23  ? -3.94853  12.05290  27.24102  1.000 59.13350  ? 53  ARG A N     1 
ATOM   86   C  CA    . ARG A 1  23  ? -5.21039  12.75310  27.47418  1.000 67.68575  ? 53  ARG A CA    1 
ATOM   87   C  C     . ARG A 1  23  ? -6.38458  11.86028  27.10536  1.000 72.87468  ? 53  ARG A C     1 
ATOM   88   O  O     . ARG A 1  23  ? -7.35649  11.74445  27.86250  1.000 58.26470  ? 53  ARG A O     1 
ATOM   89   C  CB    . ARG A 1  23  ? -5.24129  14.05908  26.67914  1.000 69.35280  ? 53  ARG A CB    1 
ATOM   90   C  CG    . ARG A 1  23  ? -6.32608  15.03027  27.10626  1.000 76.43718  ? 53  ARG A CG    1 
ATOM   91   C  CD    . ARG A 1  23  ? -7.06716  15.56335  25.88735  1.000 93.52752  ? 53  ARG A CD    1 
ATOM   92   N  NE    . ARG A 1  23  ? -7.65244  14.46642  25.12446  1.000 105.56093 ? 53  ARG A NE    1 
ATOM   93   C  CZ    . ARG A 1  23  ? -8.17459  14.58547  23.91253  1.000 95.45155  ? 53  ARG A CZ    1 
ATOM   94   N  NH1   . ARG A 1  23  ? -8.20349  15.74745  23.27850  1.000 79.33253  ? 53  ARG A NH1   1 
ATOM   95   N  NH2   . ARG A 1  23  ? -8.67484  13.50453  23.31563  1.000 96.30035  ? 53  ARG A NH2   1 
ATOM   96   N  N     . GLN A 1  24  ? -6.29584  11.19723  25.94637  1.000 76.36139  ? 54  GLN A N     1 
ATOM   97   C  CA    . GLN A 1  24  ? -7.34505  10.27938  25.52354  1.000 91.90724  ? 54  GLN A CA    1 
ATOM   98   C  C     . GLN A 1  24  ? -7.49209  9.12343   26.50860  1.000 85.86321  ? 54  GLN A C     1 
ATOM   99   O  O     . GLN A 1  24  ? -8.59007  8.84162   27.00576  1.000 82.30386  ? 54  GLN A O     1 
ATOM   100  C  CB    . GLN A 1  24  ? -7.03032  9.75429   24.11851  1.000 91.89529  ? 54  GLN A CB    1 
ATOM   101  C  CG    . GLN A 1  24  ? -8.16554  8.99645   23.43869  1.000 100.42995 ? 54  GLN A CG    1 
ATOM   102  C  CD    . GLN A 1  24  ? -9.09050  9.90457   22.63979  1.000 107.88336 ? 54  GLN A CD    1 
ATOM   103  O  OE1   . GLN A 1  24  ? -8.71438  11.01050  22.25471  1.000 104.94761 ? 54  GLN A OE1   1 
ATOM   104  N  NE2   . GLN A 1  24  ? -10.30961 9.43476   22.38598  1.000 90.37401  ? 54  GLN A NE2   1 
ATOM   105  N  N     . THR A 1  25  ? -6.37915  8.45327   26.81846  1.000 77.62113  ? 55  THR A N     1 
ATOM   106  C  CA    . THR A 1  25  ? -6.36323  7.25429   27.65550  1.000 71.58899  ? 55  THR A CA    1 
ATOM   107  C  C     . THR A 1  25  ? -5.33105  7.43316   28.76035  1.000 58.67304  ? 55  THR A C     1 
ATOM   108  O  O     . THR A 1  25  ? -4.19414  6.96598   28.64020  1.000 53.61277  ? 55  THR A O     1 
ATOM   109  C  CB    . THR A 1  25  ? -6.05354  6.01122   26.81749  1.000 93.46705  ? 55  THR A CB    1 
ATOM   110  O  OG1   . THR A 1  25  ? -4.89061  6.25401   26.01732  1.000 96.60058  ? 55  THR A OG1   1 
ATOM   111  C  CG2   . THR A 1  25  ? -7.22672  5.67737   25.90466  1.000 78.34840  ? 55  THR A CG2   1 
ATOM   112  N  N     . PRO A 1  26  ? -5.69479  8.09625   29.84838  1.000 57.87087  ? 56  PRO A N     1 
ATOM   113  C  CA    . PRO A 1  26  ? -4.74661  8.30113   30.95324  1.000 48.15671  ? 56  PRO A CA    1 
ATOM   114  C  C     . PRO A 1  26  ? -4.23974  6.96807   31.47521  1.000 50.36666  ? 56  PRO A C     1 
ATOM   115  O  O     . PRO A 1  26  ? -5.03683  6.09020   31.84635  1.000 52.00693  ? 56  PRO A O     1 
ATOM   116  C  CB    . PRO A 1  26  ? -5.58735  9.02129   32.01934  1.000 45.06483  ? 56  PRO A CB    1 
ATOM   117  C  CG    . PRO A 1  26  ? -6.77736  9.56446   31.27949  1.000 50.20679  ? 56  PRO A CG    1 
ATOM   118  C  CD    . PRO A 1  26  ? -7.03867  8.59247   30.17255  1.000 43.41461  ? 56  PRO A CD    1 
ATOM   119  N  N     . PRO A 1  27  ? -2.92877  6.76386   31.51403  1.000 47.11147  ? 57  PRO A N     1 
ATOM   120  C  CA    . PRO A 1  27  ? -2.42090  5.49480   32.04600  1.000 28.85654  ? 57  PRO A CA    1 
ATOM   121  C  C     . PRO A 1  27  ? -2.48469  5.47585   33.56501  1.000 30.19590  ? 57  PRO A C     1 
ATOM   122  O  O     . PRO A 1  27  ? -2.38044  6.50785   34.23397  1.000 41.15617  ? 57  PRO A O     1 
ATOM   123  C  CB    . PRO A 1  27  ? -0.97398  5.44455   31.53380  1.000 36.70460  ? 57  PRO A CB    1 
ATOM   124  C  CG    . PRO A 1  27  ? -0.60179  6.84549   31.24871  1.000 39.04846  ? 57  PRO A CG    1 
ATOM   125  C  CD    . PRO A 1  27  ? -1.86972  7.60568   30.93686  1.000 34.86943  ? 57  PRO A CD    1 
ATOM   126  N  N     . PHE A 1  28  ? -2.67780  4.28190   34.11507  1.000 32.29432  ? 58  PHE A N     1 
ATOM   127  C  CA    . PHE A 1  28  ? -2.57862  4.14792   35.55506  1.000 26.30934  ? 58  PHE A CA    1 
ATOM   128  C  C     . PHE A 1  28  ? -1.12658  4.08671   35.97986  1.000 32.89106  ? 58  PHE A C     1 
ATOM   129  O  O     . PHE A 1  28  ? -0.74734  4.68168   36.99379  1.000 34.62906  ? 58  PHE A O     1 
ATOM   130  C  CB    . PHE A 1  28  ? -3.29875  2.90405   36.05020  1.000 26.17903  ? 58  PHE A CB    1 
ATOM   131  C  CG    . PHE A 1  28  ? -3.16358  2.68307   37.52819  1.000 26.04536  ? 58  PHE A CG    1 
ATOM   132  C  CD1   . PHE A 1  28  ? -3.92234  3.42122   38.42227  1.000 26.35625  ? 58  PHE A CD1   1 
ATOM   133  C  CD2   . PHE A 1  28  ? -2.25966  1.74995   38.02809  1.000 26.64678  ? 58  PHE A CD2   1 
ATOM   134  C  CE1   . PHE A 1  28  ? -3.78618  3.23524   39.78126  1.000 26.25244  ? 58  PHE A CE1   1 
ATOM   135  C  CE2   . PHE A 1  28  ? -2.11750  1.56096   39.40307  1.000 25.52530  ? 58  PHE A CE2   1 
ATOM   136  C  CZ    . PHE A 1  28  ? -2.88426  2.30811   40.28116  1.000 28.35017  ? 58  PHE A CZ    1 
ATOM   137  N  N     . LEU A 1  29  ? -0.31280  3.34256   35.23277  1.000 25.71527  ? 59  LEU A N     1 
ATOM   138  C  CA    . LEU A 1  29  ? 1.10223   3.21034   35.56858  1.000 26.44821  ? 59  LEU A CA    1 
ATOM   139  C  C     . LEU A 1  29  ? 1.91208   3.35318   34.29647  1.000 31.93861  ? 59  LEU A C     1 
ATOM   140  O  O     . LEU A 1  29  ? 1.65283   2.66319   33.30152  1.000 31.78331  ? 59  LEU A O     1 
ATOM   141  C  CB    . LEU A 1  29  ? 1.40211   1.85232   36.23958  1.000 24.30974  ? 59  LEU A CB    1 
ATOM   142  C  CG    . LEU A 1  29  ? 2.88613   1.64909   36.61438  1.000 29.66199  ? 59  LEU A CG    1 
ATOM   143  C  CD1   . LEU A 1  29  ? 3.28144   2.59807   37.75730  1.000 37.85394  ? 59  LEU A CD1   1 
ATOM   144  C  CD2   . LEU A 1  29  ? 3.14196   0.21307   37.01139  1.000 26.98116  ? 59  LEU A CD2   1 
ATOM   145  N  N     . VAL A 1  30  ? 2.90522   4.23102   34.33730  1.000 25.08900  ? 60  VAL A N     1 
ATOM   146  C  CA    . VAL A 1  30  ? 3.84810   4.39684   33.24617  1.000 31.41407  ? 60  VAL A CA    1 
ATOM   147  C  C     . VAL A 1  30  ? 5.20309   3.92965   33.76299  1.000 28.08555  ? 60  VAL A C     1 
ATOM   148  O  O     . VAL A 1  30  ? 5.67331   4.43460   34.79091  1.000 26.41213  ? 60  VAL A O     1 
ATOM   149  C  CB    . VAL A 1  30  ? 3.93726   5.86382   32.78911  1.000 36.60781  ? 60  VAL A CB    1 
ATOM   150  C  CG1   . VAL A 1  30  ? 5.17318   6.06560   31.93294  1.000 29.63609  ? 60  VAL A CG1   1 
ATOM   151  C  CG2   . VAL A 1  30  ? 2.67422   6.26599   32.03628  1.000 32.04123  ? 60  VAL A CG2   1 
ATOM   152  N  N     . LEU A 1  31  ? 5.81885   2.98653   33.06094  1.000 31.40254  ? 61  LEU A N     1 
ATOM   153  C  CA    . LEU A 1  31  ? 7.18482   2.54832   33.34476  1.000 28.62982  ? 61  LEU A CA    1 
ATOM   154  C  C     . LEU A 1  31  ? 8.13481   3.28515   32.41261  1.000 27.77802  ? 61  LEU A C     1 
ATOM   155  O  O     . LEU A 1  31  ? 7.91764   3.31114   31.19964  1.000 28.65094  ? 61  LEU A O     1 
ATOM   156  C  CB    . LEU A 1  31  ? 7.34355   1.02429   33.15478  1.000 23.38817  ? 61  LEU A CB    1 
ATOM   157  C  CG    . LEU A 1  31  ? 6.36653   0.15847   33.95294  1.000 28.63550  ? 61  LEU A CG    1 
ATOM   158  C  CD1   . LEU A 1  31  ? 6.46823   -1.30756  33.50897  1.000 30.14934  ? 61  LEU A CD1   1 
ATOM   159  C  CD2   . LEU A 1  31  ? 6.65275   0.28047   35.43690  1.000 35.45300  ? 61  LEU A CD2   1 
ATOM   160  N  N     . LEU A 1  32  ? 9.14399   3.89500   33.02445  1.000 23.16095  ? 62  LEU A N     1 
ATOM   161  C  CA    . LEU A 1  32  ? 10.21398  4.55881   32.25328  1.000 23.29328  ? 62  LEU A CA    1 
ATOM   162  C  C     . LEU A 1  32  ? 11.48189  3.74362   32.52713  1.000 23.16775  ? 62  LEU A C     1 
ATOM   163  O  O     . LEU A 1  32  ? 11.92605  3.70859   33.67807  1.000 28.09361  ? 62  LEU A O     1 
ATOM   164  C  CB    . LEU A 1  32  ? 10.34427  6.03080   32.62422  1.000 23.31476  ? 62  LEU A CB    1 
ATOM   165  C  CG    . LEU A 1  32  ? 9.11337   6.90099   32.36337  1.000 24.80583  ? 62  LEU A CG    1 
ATOM   166  C  CD1   . LEU A 1  32  ? 9.38765   8.31696   32.81529  1.000 26.50934  ? 62  LEU A CD1   1 
ATOM   167  C  CD2   . LEU A 1  32  ? 8.75316   6.87200   30.89642  1.000 27.41128  ? 62  LEU A CD2   1 
ATOM   168  N  N     . VAL A 1  33  ? 12.00265  3.08551   31.50608  1.000 23.40594  ? 63  VAL A N     1 
ATOM   169  C  CA    . VAL A 1  33  ? 13.15653  2.16733   31.68095  1.000 23.62147  ? 63  VAL A CA    1 
ATOM   170  C  C     . VAL A 1  33  ? 14.42954  2.78012   31.09375  1.000 23.63918  ? 63  VAL A C     1 
ATOM   171  O  O     . VAL A 1  33  ? 14.40445  3.20909   29.95274  1.000 26.73389  ? 63  VAL A O     1 
ATOM   172  C  CB    . VAL A 1  33  ? 12.85923  0.78636   31.06103  1.000 23.59295  ? 63  VAL A CB    1 
ATOM   173  C  CG1   . VAL A 1  33  ? 13.99810  -0.19781  31.28590  1.000 23.65449  ? 63  VAL A CG1   1 
ATOM   174  C  CG2   . VAL A 1  33  ? 11.53220  0.21859   31.54223  1.000 23.48725  ? 63  VAL A CG2   1 
ATOM   175  N  N     . THR A 1  34  ? 15.48266  2.79097   31.88861  1.000 23.84146  ? 64  THR A N     1 
ATOM   176  C  CA    . THR A 1  34  ? 16.77668  3.31276   31.44441  1.000 26.85687  ? 64  THR A CA    1 
ATOM   177  C  C     . THR A 1  34  ? 17.55141  2.17362   30.81834  1.000 32.07539  ? 64  THR A C     1 
ATOM   178  O  O     . THR A 1  34  ? 17.46930  1.04964   31.32838  1.000 30.33753  ? 64  THR A O     1 
ATOM   179  C  CB    . THR A 1  34  ? 17.49594  3.94668   32.63930  1.000 23.62235  ? 64  THR A CB    1 
ATOM   180  O  OG1   . THR A 1  34  ? 17.78690  2.90366   33.56129  1.000 28.51263  ? 64  THR A OG1   1 
ATOM   181  C  CG2   . THR A 1  34  ? 16.65120  5.01883   33.30338  1.000 24.27389  ? 64  THR A CG2   1 
ATOM   182  N  N     . SER A 1  35  ? 18.24130  2.44848   29.72424  1.000 30.99317  ? 65  SER A N     1 
ATOM   183  C  CA    . SER A 1  35  ? 19.08405  1.42132   29.06315  1.000 30.32402  ? 65  SER A CA    1 
ATOM   184  C  C     . SER A 1  35  ? 20.01702  2.09115   28.05600  1.000 30.79720  ? 65  SER A C     1 
ATOM   185  O  O     . SER A 1  35  ? 19.64811  3.13619   27.51702  1.000 31.98137  ? 65  SER A O     1 
ATOM   186  C  CB    . SER A 1  35  ? 18.25979  0.33543   28.41030  1.000 30.05316  ? 65  SER A CB    1 
ATOM   187  O  OG    . SER A 1  35  ? 17.75468  0.74648   27.15135  1.000 37.20333  ? 65  SER A OG    1 
ATOM   188  N  N     . SER A 1  36  ? 21.18990  1.51096   27.84786  1.000 32.13907  ? 66  SER A N     1 
ATOM   189  C  CA    . SER A 1  36  ? 22.13783  2.00778   26.83071  1.000 32.23394  ? 66  SER A CA    1 
ATOM   190  C  C     . SER A 1  36  ? 21.66657  1.52181   25.45379  1.000 38.26560  ? 66  SER A C     1 
ATOM   191  O  O     . SER A 1  36  ? 20.86842  0.58794   25.41993  1.000 38.93854  ? 66  SER A O     1 
ATOM   192  C  CB    . SER A 1  36  ? 23.51980  1.51857   27.13553  1.000 31.36144  ? 66  SER A CB    1 
ATOM   193  O  OG    . SER A 1  36  ? 23.99105  2.06853   28.35545  1.000 46.25327  ? 66  SER A OG    1 
ATOM   194  N  N     . HIS A 1  37  ? 22.17151  2.10870   24.37270  1.000 37.47021  ? 67  HIS A N     1 
ATOM   195  C  CA    . HIS A 1  37  ? 21.72727  1.76373   22.99677  1.000 39.05485  ? 67  HIS A CA    1 
ATOM   196  C  C     . HIS A 1  37  ? 22.06699  0.31967   22.63877  1.000 40.70922  ? 67  HIS A C     1 
ATOM   197  O  O     . HIS A 1  37  ? 21.31879  -0.30724  21.87889  1.000 39.93106  ? 67  HIS A O     1 
ATOM   198  C  CB    . HIS A 1  37  ? 22.41627  2.68359   21.98465  1.000 44.89974  ? 67  HIS A CB    1 
ATOM   199  C  CG    . HIS A 1  37  ? 22.22953  4.14563   22.17364  1.000 44.12711  ? 67  HIS A CG    1 
ATOM   200  N  ND1   . HIS A 1  37  ? 21.67451  4.92669   21.18669  1.000 37.38988  ? 67  HIS A ND1   1 
ATOM   201  C  CD2   . HIS A 1  37  ? 22.53480  4.96961   23.17657  1.000 41.21189  ? 67  HIS A CD2   1 
ATOM   202  C  CE1   . HIS A 1  37  ? 21.64177  6.17870   21.59766  1.000 50.53525  ? 67  HIS A CE1   1 
ATOM   203  N  NE2   . HIS A 1  37  ? 22.15594  6.22766   22.80359  1.000 50.03511  ? 67  HIS A NE2   1 
ATOM   204  N  N     . LYS A 1  38  ? 23.17598  -0.18649  23.16763  1.000 42.38005  ? 68  LYS A N     1 
ATOM   205  C  CA    . LYS A 1  38  ? 23.63172  -1.56157  22.84861  1.000 43.40106  ? 68  LYS A CA    1 
ATOM   206  C  C     . LYS A 1  38  ? 22.79467  -2.59142  23.61375  1.000 40.69772  ? 68  LYS A C     1 
ATOM   207  O  O     . LYS A 1  38  ? 22.86343  -3.77244  23.26178  1.000 34.59692  ? 68  LYS A O     1 
ATOM   208  C  CB    . LYS A 1  38  ? 25.10176  -1.69279  23.24041  1.000 42.14185  ? 68  LYS A CB    1 
ATOM   209  C  CG    . LYS A 1  38  ? 25.33892  -1.93079  24.72038  1.000 60.48755  ? 68  LYS A CG    1 
ATOM   210  C  CD    . LYS A 1  38  ? 26.79592  -2.22101  25.04919  1.000 64.71483  ? 68  LYS A CD    1 
ATOM   211  C  CE    . LYS A 1  38  ? 27.42520  -1.12808  25.84307  1.000 73.66907  ? 68  LYS A CE    1 
ATOM   212  N  NZ    . LYS A 1  38  ? 28.81920  -1.44729  26.16589  1.000 83.30445  ? 68  LYS A NZ    1 
ATOM   213  N  N     . GLN A 1  39  ? 22.02087  -2.14227  24.60285  1.000 40.55852  ? 69  GLN A N     1 
ATOM   214  C  CA    . GLN A 1  39  ? 21.23984  -3.07012  25.44898  1.000 30.07686  ? 69  GLN A CA    1 
ATOM   215  C  C     . GLN A 1  39  ? 19.88171  -3.36293  24.80618  1.000 33.13874  ? 69  GLN A C     1 
ATOM   216  O  O     . GLN A 1  39  ? 18.86782  -3.27575  25.50832  1.000 39.60425  ? 69  GLN A O     1 
ATOM   217  C  CB    . GLN A 1  39  ? 21.15613  -2.46107  26.84198  1.000 37.88588  ? 69  GLN A CB    1 
ATOM   218  C  CG    . GLN A 1  39  ? 22.45923  -2.49225  27.62580  1.000 27.83770  ? 69  GLN A CG    1 
ATOM   219  C  CD    . GLN A 1  39  ? 22.26950  -2.04218  29.05381  1.000 35.53626  ? 69  GLN A CD    1 
ATOM   220  O  OE1   . GLN A 1  39  ? 21.83072  -0.92210  29.32084  1.000 35.70021  ? 69  GLN A OE1   1 
ATOM   221  N  NE2   . GLN A 1  39  ? 22.58149  -2.92620  29.98979  1.000 46.14757  ? 69  GLN A NE2   1 
ATOM   222  N  N     . LEU A 1  40  ? 19.87448  -3.68496  23.51719  1.000 32.31702  ? 70  LEU A N     1 
ATOM   223  C  CA    . LEU A 1  40  ? 18.63033  -4.09778  22.87137  1.000 35.90046  ? 70  LEU A CA    1 
ATOM   224  C  C     . LEU A 1  40  ? 18.07620  -5.39468  23.46849  1.000 34.58220  ? 70  LEU A C     1 
ATOM   225  O  O     . LEU A 1  40  ? 16.85920  -5.54848  23.59766  1.000 39.29343  ? 70  LEU A O     1 
ATOM   226  C  CB    . LEU A 1  40  ? 18.85209  -4.26686  21.37035  1.000 32.10559  ? 70  LEU A CB    1 
ATOM   227  C  CG    . LEU A 1  40  ? 17.62991  -4.81869  20.65353  1.000 38.12923  ? 70  LEU A CG    1 
ATOM   228  C  CD1   . LEU A 1  40  ? 16.41808  -3.92349  20.92167  1.000 38.65693  ? 70  LEU A CD1   1 
ATOM   229  C  CD2   . LEU A 1  40  ? 17.90068  -4.95878  19.16250  1.000 37.78152  ? 70  LEU A CD2   1 
ATOM   230  N  N     . ALA A 1  41  ? 18.94310  -6.34781  23.80840  1.000 36.78802  ? 71  ALA A N     1 
ATOM   231  C  CA    . ALA A 1  41  ? 18.45898  -7.60171  24.39850  1.000 38.77677  ? 71  ALA A CA    1 
ATOM   232  C  C     . ALA A 1  41  ? 17.66120  -7.34455  25.67360  1.000 34.37167  ? 71  ALA A C     1 
ATOM   233  O  O     . ALA A 1  41  ? 16.60414  -7.95438  25.89277  1.000 30.60080  ? 71  ALA A O     1 
ATOM   234  C  CB    . ALA A 1  41  ? 19.63488  -8.54189  24.68036  1.000 28.48244  ? 71  ALA A CB    1 
ATOM   235  N  N     . GLU A 1  42  ? 18.16246  -6.44460  26.52351  1.000 34.83272  ? 72  GLU A N     1 
ATOM   236  C  CA    . GLU A 1  42  ? 17.43569  -6.03346  27.71959  1.000 30.02184  ? 72  GLU A CA    1 
ATOM   237  C  C     . GLU A 1  42  ? 16.04972  -5.52125  27.36677  1.000 26.85797  ? 72  GLU A C     1 
ATOM   238  O  O     . GLU A 1  42  ? 15.04174  -5.93307  27.95792  1.000 32.10556  ? 72  GLU A O     1 
ATOM   239  C  CB    . GLU A 1  42  ? 18.22396  -4.94556  28.45645  1.000 33.19913  ? 72  GLU A CB    1 
ATOM   240  C  CG    . GLU A 1  42  ? 19.29201  -5.47370  29.38432  1.000 46.60910  ? 72  GLU A CG    1 
ATOM   241  C  CD    . GLU A 1  42  ? 20.54783  -5.95792  28.66916  1.000 48.34577  ? 72  GLU A CD    1 
ATOM   242  O  OE1   . GLU A 1  42  ? 20.66969  -5.78597  27.43614  1.000 37.84499  ? 72  GLU A OE1   1 
ATOM   243  O  OE2   . GLU A 1  42  ? 21.41884  -6.50703  29.36506  1.000 50.04657  ? 72  GLU A OE2   1 
ATOM   244  N  N     . ARG A 1  43  ? 15.98074  -4.58226  26.41975  1.000 28.04681  ? 73  ARG A N     1 
ATOM   245  C  CA    . ARG A 1  43  ? 14.69979  -3.97707  26.10791  1.000 28.15441  ? 73  ARG A CA    1 
ATOM   246  C  C     . ARG A 1  43  ? 13.73855  -4.99294  25.50407  1.000 29.56020  ? 73  ARG A C     1 
ATOM   247  O  O     . ARG A 1  43  ? 12.54259  -4.98574  25.81724  1.000 30.03519  ? 73  ARG A O     1 
ATOM   248  C  CB    . ARG A 1  43  ? 14.90385  -2.78313  25.16085  1.000 33.28481  ? 73  ARG A CB    1 
ATOM   249  C  CG    . ARG A 1  43  ? 15.70611  -1.65424  25.78971  1.000 37.13206  ? 73  ARG A CG    1 
ATOM   250  C  CD    . ARG A 1  43  ? 15.60120  -0.35825  24.97268  1.000 31.66660  ? 73  ARG A CD    1 
ATOM   251  N  NE    . ARG A 1  43  ? 16.32601  -0.45440  23.70659  1.000 35.08064  ? 73  ARG A NE    1 
ATOM   252  C  CZ    . ARG A 1  43  ? 17.63802  -0.30761  23.58740  1.000 43.24524  ? 73  ARG A CZ    1 
ATOM   253  N  NH1   . ARG A 1  43  ? 18.40620  -0.08670  24.64029  1.000 32.02354  ? 73  ARG A NH1   1 
ATOM   254  N  NH2   . ARG A 1  43  ? 18.19384  -0.39473  22.38433  1.000 31.66817  ? 73  ARG A NH2   1 
ATOM   255  N  N     . MET A 1  44  ? 14.23429  -5.88504  24.65103  1.000 27.53148  ? 74  MET A N     1 
ATOM   256  C  CA    . MET A 1  44  ? 13.34105  -6.90092  24.08719  1.000 32.89491  ? 74  MET A CA    1 
ATOM   257  C  C     . MET A 1  44  ? 12.81806  -7.83380  25.17828  1.000 31.17112  ? 74  MET A C     1 
ATOM   258  O  O     . MET A 1  44  ? 11.62301  -8.16361  25.20446  1.000 33.02840  ? 74  MET A O     1 
ATOM   259  C  CB    . MET A 1  44  ? 14.05277  -7.69906  22.99211  1.000 27.78078  ? 74  MET A CB    1 
ATOM   260  C  CG    . MET A 1  44  ? 14.37272  -6.91315  21.72404  1.000 40.70713  ? 74  MET A CG    1 
ATOM   261  S  SD    . MET A 1  44  ? 12.97477  -5.99795  21.03321  1.000 41.76483  ? 74  MET A SD    1 
ATOM   262  C  CE    . MET A 1  44  ? 11.76054  -7.29076  20.81041  1.000 34.76337  ? 74  MET A CE    1 
ATOM   263  N  N     . ALA A 1  45  ? 13.68312  -8.23891  26.11318  1.000 32.40494  ? 75  ALA A N     1 
ATOM   264  C  CA    . ALA A 1  45  ? 13.20113  -9.11280  27.18527  1.000 26.78731  ? 75  ALA A CA    1 
ATOM   265  C  C     . ALA A 1  45  ? 12.14236  -8.40461  28.02239  1.000 33.14893  ? 75  ALA A C     1 
ATOM   266  O  O     . ALA A 1  45  ? 11.16232  -9.01745  28.45855  1.000 27.06326  ? 75  ALA A O     1 
ATOM   267  C  CB    . ALA A 1  45  ? 14.37418  -9.57796  28.05812  1.000 26.74987  ? 75  ALA A CB    1 
ATOM   268  N  N     . ILE A 1  46  ? 12.30460  -7.11063  28.27533  1.000 28.47179  ? 76  ILE A N     1 
ATOM   269  C  CA    . ILE A 1  46  ? 11.27382  -6.35045  29.04045  1.000 28.70516  ? 76  ILE A CA    1 
ATOM   270  C  C     . ILE A 1  46  ? 9.98772   -6.26327  28.20063  1.000 31.04611  ? 76  ILE A C     1 
ATOM   271  O  O     . ILE A 1  46  ? 8.91077   -6.46708  28.76878  1.000 25.54260  ? 76  ILE A O     1 
ATOM   272  C  CB    . ILE A 1  46  ? 11.81110  -4.96252  29.45434  1.000 29.67559  ? 76  ILE A CB    1 
ATOM   273  C  CG1   . ILE A 1  46  ? 12.93222  -5.07867  30.47719  1.000 24.78963  ? 76  ILE A CG1   1 
ATOM   274  C  CG2   . ILE A 1  46  ? 10.69331  -4.04033  29.93547  1.000 24.52865  ? 76  ILE A CG2   1 
ATOM   275  C  CD1   . ILE A 1  46  ? 13.89040  -3.90282  30.46602  1.000 25.04417  ? 76  ILE A CD1   1 
ATOM   276  N  N     . ARG A 1  47  ? 10.12258  -5.99733  26.90260  1.000 32.39123  ? 77  ARG A N     1 
ATOM   277  C  CA    . ARG A 1  47  ? 8.95948   -5.84617  25.98876  1.000 32.94799  ? 77  ARG A CA    1 
ATOM   278  C  C     . ARG A 1  47  ? 8.14827   -7.15305  25.92491  1.000 35.00630  ? 77  ARG A C     1 
ATOM   279  O  O     . ARG A 1  47  ? 6.91826   -7.07286  25.81408  1.000 32.51996  ? 77  ARG A O     1 
ATOM   280  C  CB    . ARG A 1  47  ? 9.47737   -5.37029  24.62767  1.000 27.33826  ? 77  ARG A CB    1 
ATOM   281  C  CG    . ARG A 1  47  ? 9.51857   -3.87031  24.38262  1.000 28.79699  ? 77  ARG A CG    1 
ATOM   282  C  CD    . ARG A 1  47  ? 9.81241   -3.57940  22.92358  1.000 34.40664  ? 77  ARG A CD    1 
ATOM   283  N  NE    . ARG A 1  47  ? 10.39259  -2.24949  22.71546  1.000 31.06836  ? 77  ARG A NE    1 
ATOM   284  C  CZ    . ARG A 1  47  ? 11.64058  -2.02970  22.34528  1.000 40.60261  ? 77  ARG A CZ    1 
ATOM   285  N  NH1   . ARG A 1  47  ? 12.48140  -3.03784  22.21419  1.000 30.48699  ? 77  ARG A NH1   1 
ATOM   286  N  NH2   . ARG A 1  47  ? 12.04474  -0.79777  22.10419  1.000 29.88785  ? 77  ARG A NH2   1 
ATOM   287  N  N     . GLN A 1  48  ? 8.81210   -8.29615  26.04785  1.000 29.53519  ? 78  GLN A N     1 
ATOM   288  C  CA    . GLN A 1  48  ? 8.10990   -9.59904  26.06699  1.000 29.53696  ? 78  GLN A CA    1 
ATOM   289  C  C     . GLN A 1  48  ? 7.61104   -9.94392  27.48407  1.000 38.98792  ? 78  GLN A C     1 
ATOM   290  O  O     . GLN A 1  48  ? 6.68093   -10.75777 27.57822  1.000 38.57537  ? 78  GLN A O     1 
ATOM   291  C  CB    . GLN A 1  48  ? 9.07166   -10.64220 25.50988  1.000 38.43458  ? 78  GLN A CB    1 
ATOM   292  C  CG    . GLN A 1  48  ? 9.36848   -10.49629 24.02284  1.000 48.24859  ? 78  GLN A CG    1 
ATOM   293  C  CD    . GLN A 1  48  ? 10.78637  -10.87553 23.65765  1.000 48.95023  ? 78  GLN A CD    1 
ATOM   294  O  OE1   . GLN A 1  48  ? 11.50037  -11.52862 24.42557  1.000 48.03150  ? 78  GLN A OE1   1 
ATOM   295  N  NE2   . GLN A 1  48  ? 11.21227  -10.45863 22.47758  1.000 57.86792  ? 78  GLN A NE2   1 
ATOM   296  N  N     . THR A 1  49  ? 8.13529   -9.29397  28.52497  1.000 30.24863  ? 79  THR A N     1 
ATOM   297  C  CA    . THR A 1  49  ? 7.76942   -9.66787  29.91004  1.000 31.28786  ? 79  THR A CA    1 
ATOM   298  C  C     . THR A 1  49  ? 6.95569   -8.59672  30.61612  1.000 29.57449  ? 79  THR A C     1 
ATOM   299  O  O     . THR A 1  49  ? 5.82566   -8.36756  30.18827  1.000 34.10320  ? 79  THR A O     1 
ATOM   300  C  CB    . THR A 1  49  ? 9.04347   -10.02905 30.67487  1.000 35.04422  ? 79  THR A CB    1 
ATOM   301  O  OG1   . THR A 1  49  ? 9.90464   -8.89819  30.63672  1.000 34.77422  ? 79  THR A OG1   1 
ATOM   302  C  CG2   . THR A 1  49  ? 9.74420   -11.24318 30.09181  1.000 26.86986  ? 79  THR A CG2   1 
ATOM   303  N  N     . TRP A 1  50  ? 7.50393   -7.96478  31.65602  1.000 27.20290  ? 80  TRP A N     1 
ATOM   304  C  CA    . TRP A 1  50  ? 6.75120   -6.98563  32.49110  1.000 35.93923  ? 80  TRP A CA    1 
ATOM   305  C  C     . TRP A 1  50  ? 6.48031   -5.64261  31.79310  1.000 25.37277  ? 80  TRP A C     1 
ATOM   306  O  O     . TRP A 1  50  ? 5.74052   -4.84848  32.36518  1.000 30.80367  ? 80  TRP A O     1 
ATOM   307  C  CB    . TRP A 1  50  ? 7.45442   -6.77371  33.83999  1.000 27.86130  ? 80  TRP A CB    1 
ATOM   308  C  CG    . TRP A 1  50  ? 8.92646   -6.45994  33.80478  1.000 34.65617  ? 80  TRP A CG    1 
ATOM   309  C  CD1   . TRP A 1  50  ? 9.95235   -7.34210  33.97067  1.000 31.14419  ? 80  TRP A CD1   1 
ATOM   310  C  CD2   . TRP A 1  50  ? 9.53965   -5.16204  33.65666  1.000 23.97058  ? 80  TRP A CD2   1 
ATOM   311  N  NE1   . TRP A 1  50  ? 11.15344  -6.69229  33.91048  1.000 24.17357  ? 80  TRP A NE1   1 
ATOM   312  C  CE2   . TRP A 1  50  ? 10.93363  -5.35726  33.72247  1.000 25.25528  ? 80  TRP A CE2   1 
ATOM   313  C  CE3   . TRP A 1  50  ? 9.05383   -3.86697  33.46769  1.000 30.85263  ? 80  TRP A CE3   1 
ATOM   314  C  CZ2   . TRP A 1  50  ? 11.83978  -4.30540  33.61132  1.000 31.15334  ? 80  TRP A CZ2   1 
ATOM   315  C  CZ3   . TRP A 1  50  ? 9.94897   -2.82911  33.35454  1.000 23.51076  ? 80  TRP A CZ3   1 
ATOM   316  C  CH2   . TRP A 1  50  ? 11.32295  -3.04733  33.42235  1.000 29.35327  ? 80  TRP A CH2   1 
ATOM   317  N  N     . GLY A 1  51  ? 7.03519   -5.41973  30.60901  1.000 26.84618  ? 81  GLY A N     1 
ATOM   318  C  CA    . GLY A 1  51  ? 6.81028   -4.17472  29.85801  1.000 31.58120  ? 81  GLY A CA    1 
ATOM   319  C  C     . GLY A 1  51  ? 5.67812   -4.28757  28.86817  1.000 28.81502  ? 81  GLY A C     1 
ATOM   320  O  O     . GLY A 1  51  ? 5.34320   -3.26354  28.26818  1.000 35.61266  ? 81  GLY A O     1 
ATOM   321  N  N     . LYS A 1  52  ? 5.12591   -5.48649  28.68628  1.000 34.70631  ? 82  LYS A N     1 
ATOM   322  C  CA    . LYS A 1  52  ? 3.99375   -5.71134  27.75444  1.000 34.40839  ? 82  LYS A CA    1 
ATOM   323  C  C     . LYS A 1  52  ? 2.81794   -4.85114  28.20358  1.000 39.54424  ? 82  LYS A C     1 
ATOM   324  O  O     . LYS A 1  52  ? 2.33107   -5.02803  29.32465  1.000 44.55752  ? 82  LYS A O     1 
ATOM   325  C  CB    . LYS A 1  52  ? 3.50751   -7.15926  27.68255  1.000 33.81201  ? 82  LYS A CB    1 
ATOM   326  C  CG    . LYS A 1  52  ? 2.41433   -7.41612  26.66471  1.000 53.44155  ? 82  LYS A CG    1 
ATOM   327  C  CD    . LYS A 1  52  ? 1.88011   -8.84204  26.70982  1.000 81.97319  ? 82  LYS A CD    1 
ATOM   328  C  CE    . LYS A 1  52  ? 1.03989   -9.17694  25.51795  1.000 84.40846  ? 82  LYS A CE    1 
ATOM   329  N  NZ    . LYS A 1  52  ? -0.11799  -8.28676  25.37808  1.000 72.23455  ? 82  LYS A NZ    1 
ATOM   330  N  N     . GLU A 1  53  ? 2.40396   -3.94710  27.33061  1.000 41.38316  ? 83  GLU A N     1 
ATOM   331  C  CA    . GLU A 1  53  ? 1.29515   -3.03592  27.66774  1.000 46.66864  ? 83  GLU A CA    1 
ATOM   332  C  C     . GLU A 1  53  ? 0.02704   -3.87771  27.81194  1.000 49.37869  ? 83  GLU A C     1 
ATOM   333  O  O     . GLU A 1  53  ? -0.19621  -4.76370  26.97299  1.000 44.41152  ? 83  GLU A O     1 
ATOM   334  C  CB    . GLU A 1  53  ? 1.28518   -1.93294  26.61871  1.000 47.65382  ? 83  GLU A CB    1 
ATOM   335  C  CG    . GLU A 1  53  ? 2.53133   -1.05614  26.70751  1.000 47.48849  ? 83  GLU A CG    1 
ATOM   336  C  CD    . GLU A 1  53  ? 2.45043   0.22685   25.90848  1.000 68.38643  ? 83  GLU A CD    1 
ATOM   337  O  OE1   . GLU A 1  53  ? 1.55832   0.30897   25.04360  1.000 65.96651  ? 83  GLU A OE1   1 
ATOM   338  O  OE2   . GLU A 1  53  ? 3.27060   1.13573   26.14234  1.000 62.01210  ? 83  GLU A OE2   1 
ATOM   339  N  N     . ARG A 1  54  ? -0.74577  -3.60956  28.86004  1.000 44.71936  ? 84  ARG A N     1 
ATOM   340  C  CA    . ARG A 1  54  ? -1.93486  -4.44336  29.13222  1.000 44.21777  ? 84  ARG A CA    1 
ATOM   341  C  C     . ARG A 1  54  ? -2.80361  -3.77620  30.19032  1.000 41.80893  ? 84  ARG A C     1 
ATOM   342  O  O     . ARG A 1  54  ? -2.36437  -2.78125  30.78923  1.000 41.75588  ? 84  ARG A O     1 
ATOM   343  C  CB    . ARG A 1  54  ? -1.49500  -5.79842  29.68920  1.000 41.44082  ? 84  ARG A CB    1 
ATOM   344  C  CG    . ARG A 1  54  ? -0.63283  -5.77952  30.94008  1.000 44.25567  ? 84  ARG A CG    1 
ATOM   345  C  CD    . ARG A 1  54  ? -0.57696  -7.17251  31.53512  1.000 48.40214  ? 84  ARG A CD    1 
ATOM   346  N  NE    . ARG A 1  54  ? 0.49615   -7.33265  32.52097  1.000 58.81166  ? 84  ARG A NE    1 
ATOM   347  C  CZ    . ARG A 1  54  ? 0.28729   -7.57358  33.80201  1.000 51.15387  ? 84  ARG A CZ    1 
ATOM   348  N  NH1   . ARG A 1  54  ? -0.85974  -8.08639  34.19618  1.000 39.75984  ? 84  ARG A NH1   1 
ATOM   349  N  NH2   . ARG A 1  54  ? 1.22146   -7.28670  34.68787  1.000 62.86450  ? 84  ARG A NH2   1 
ATOM   350  N  N     . MET A 1  55  ? -4.00067  -4.31300  30.38351  1.000 43.35364  ? 85  MET A N     1 
ATOM   351  C  CA    . MET A 1  55  ? -4.86044  -3.81184  31.47561  1.000 50.36052  ? 85  MET A CA    1 
ATOM   352  C  C     . MET A 1  55  ? -4.58341  -4.69284  32.69360  1.000 52.39190  ? 85  MET A C     1 
ATOM   353  O  O     . MET A 1  55  ? -4.68162  -5.92183  32.57665  1.000 54.96771  ? 85  MET A O     1 
ATOM   354  C  CB    . MET A 1  55  ? -6.34050  -3.82561  31.09381  1.000 41.98861  ? 85  MET A CB    1 
ATOM   355  C  CG    . MET A 1  55  ? -6.68949  -2.84959  29.99483  1.000 55.51653  ? 85  MET A CG    1 
ATOM   356  S  SD    . MET A 1  55  ? -6.83414  -1.16155  30.61181  1.000 77.45195  ? 85  MET A SD    1 
ATOM   357  C  CE    . MET A 1  55  ? -7.69021  -0.37246  29.24290  1.000 59.81490  ? 85  MET A CE    1 
ATOM   358  N  N     . VAL A 1  56  ? -4.18916  -4.07787  33.79552  1.000 61.46113  ? 86  VAL A N     1 
ATOM   359  C  CA    . VAL A 1  56  ? -3.87710  -4.78989  35.03150  1.000 61.06767  ? 86  VAL A CA    1 
ATOM   360  C  C     . VAL A 1  56  ? -4.96791  -4.39769  36.00964  1.000 62.00941  ? 86  VAL A C     1 
ATOM   361  O  O     . VAL A 1  56  ? -5.00066  -3.25567  36.48761  1.000 63.89017  ? 86  VAL A O     1 
ATOM   362  C  CB    . VAL A 1  56  ? -2.47997  -4.43909  35.57030  1.000 54.24000  ? 86  VAL A CB    1 
ATOM   363  C  CG1   . VAL A 1  56  ? -2.15192  -5.23411  36.83828  1.000 49.57380  ? 86  VAL A CG1   1 
ATOM   364  C  CG2   . VAL A 1  56  ? -1.43016  -4.66129  34.49016  1.000 41.78098  ? 86  VAL A CG2   1 
ATOM   365  N  N     . LYS A 1  57  ? -5.88502  -5.32653  36.28580  1.000 73.98274  ? 87  LYS A N     1 
ATOM   366  C  CA    . LYS A 1  57  ? -7.03185  -5.03833  37.14695  1.000 69.07563  ? 87  LYS A CA    1 
ATOM   367  C  C     . LYS A 1  57  ? -7.82774  -3.85322  36.60002  1.000 68.08025  ? 87  LYS A C     1 
ATOM   368  O  O     . LYS A 1  57  ? -8.32950  -3.01512  37.35607  1.000 66.58730  ? 87  LYS A O     1 
ATOM   369  C  CB    . LYS A 1  57  ? -6.58861  -4.77636  38.58688  1.000 69.79883  ? 87  LYS A CB    1 
ATOM   370  C  CG    . LYS A 1  57  ? -5.87071  -5.94945  39.24081  1.000 80.42113  ? 87  LYS A CG    1 
ATOM   371  C  CD    . LYS A 1  57  ? -6.79388  -7.15230  39.38297  1.000 74.88783  ? 87  LYS A CD    1 
ATOM   372  C  CE    . LYS A 1  57  ? -6.09196  -8.30339  40.09491  1.000 90.99184  ? 87  LYS A CE    1 
ATOM   373  N  NZ    . LYS A 1  57  ? -6.97413  -9.49725  40.23607  1.000 80.42587  ? 87  LYS A NZ    1 
ATOM   374  N  N     . GLY A 1  58  ? -7.93891  -3.78324  35.27503  1.000 56.69239  ? 88  GLY A N     1 
ATOM   375  C  CA    . GLY A 1  58  ? -8.64283  -2.69815  34.62210  1.000 57.46881  ? 88  GLY A CA    1 
ATOM   376  C  C     . GLY A 1  58  ? -7.88764  -1.39127  34.54596  1.000 54.60613  ? 88  GLY A C     1 
ATOM   377  O  O     . GLY A 1  58  ? -8.48553  -0.37719  34.16701  1.000 53.63278  ? 88  GLY A O     1 
ATOM   378  N  N     . LYS A 1  59  ? -6.60059  -1.37546  34.89078  1.000 57.75699  ? 89  LYS A N     1 
ATOM   379  C  CA    . LYS A 1  59  ? -5.79940  -0.15659  34.88163  1.000 47.18483  ? 89  LYS A CA    1 
ATOM   380  C  C     . LYS A 1  59  ? -4.77256  -0.23578  33.76149  1.000 37.92424  ? 89  LYS A C     1 
ATOM   381  O  O     . LYS A 1  59  ? -4.14575  -1.27589  33.56844  1.000 41.82606  ? 89  LYS A O     1 
ATOM   382  C  CB    . LYS A 1  59  ? -5.10318  0.03834   36.22853  1.000 37.59167  ? 89  LYS A CB    1 
ATOM   383  C  CG    . LYS A 1  59  ? -6.04101  0.05452   37.43666  1.000 40.40299  ? 89  LYS A CG    1 
ATOM   384  C  CD    . LYS A 1  59  ? -7.13286  1.10469   37.30878  1.000 49.49179  ? 89  LYS A CD    1 
ATOM   385  C  CE    . LYS A 1  59  ? -7.98068  1.14586   38.58090  1.000 57.45304  ? 89  LYS A CE    1 
ATOM   386  N  NZ    . LYS A 1  59  ? -8.65485  -0.16502  38.85203  1.000 67.64090  ? 89  LYS A NZ    1 
ATOM   387  N  N     . GLN A 1  60  ? -4.58850  0.84817   33.01444  1.000 33.71954  ? 90  GLN A N     1 
ATOM   388  C  CA    . GLN A 1  60  ? -3.69466  0.78599   31.86531  1.000 40.35681  ? 90  GLN A CA    1 
ATOM   389  C  C     . GLN A 1  60  ? -2.23059  0.90777   32.29511  1.000 36.04566  ? 90  GLN A C     1 
ATOM   390  O  O     . GLN A 1  60  ? -1.86434  1.84074   33.04103  1.000 33.43969  ? 90  GLN A O     1 
ATOM   391  C  CB    . GLN A 1  60  ? -4.01163  1.87401   30.84233  1.000 37.06601  ? 90  GLN A CB    1 
ATOM   392  C  CG    . GLN A 1  60  ? -3.05581  1.81083   29.63420  1.000 39.32810  ? 90  GLN A CG    1 
ATOM   393  C  CD    . GLN A 1  60  ? -3.39012  0.69485   28.66128  1.000 51.08987  ? 90  GLN A CD    1 
ATOM   394  O  OE1   . GLN A 1  60  ? -4.52120  0.60302   28.19643  1.000 58.82256  ? 90  GLN A OE1   1 
ATOM   395  N  NE2   . GLN A 1  60  ? -2.40730  -0.15931  28.34416  1.000 56.70166  ? 90  GLN A NE2   1 
ATOM   396  N  N     . LEU A 1  61  ? -1.40780  -0.02437  31.80302  1.000 40.23340  ? 91  LEU A N     1 
ATOM   397  C  CA    . LEU A 1  61  ? 0.04623   0.01840   31.93582  1.000 32.25755  ? 91  LEU A CA    1 
ATOM   398  C  C     . LEU A 1  61  ? 0.66311   0.45027   30.61272  1.000 32.10105  ? 91  LEU A C     1 
ATOM   399  O  O     . LEU A 1  61  ? 0.29488   -0.07170  29.55679  1.000 38.26752  ? 91  LEU A O     1 
ATOM   400  C  CB    . LEU A 1  61  ? 0.57906   -1.36767  32.31879  1.000 32.04690  ? 91  LEU A CB    1 
ATOM   401  C  CG    . LEU A 1  61  ? 2.09504   -1.50191  32.29858  1.000 36.55078  ? 91  LEU A CG    1 
ATOM   402  C  CD1   . LEU A 1  61  ? 2.61331   -0.85395  33.55649  1.000 28.79206  ? 91  LEU A CD1   1 
ATOM   403  C  CD2   . LEU A 1  61  ? 2.52379   -2.97298  32.21657  1.000 41.82472  ? 91  LEU A CD2   1 
ATOM   404  N  N     . LYS A 1  62  ? 1.58727   1.41313   30.66257  1.000 34.12161  ? 92  LYS A N     1 
ATOM   405  C  CA    . LYS A 1  62  ? 2.36117   1.81597   29.48945  1.000 30.36415  ? 92  LYS A CA    1 
ATOM   406  C  C     . LYS A 1  62  ? 3.84520   1.73675   29.81425  1.000 34.46373  ? 92  LYS A C     1 
ATOM   407  O  O     . LYS A 1  62  ? 4.24040   1.99372   30.95518  1.000 31.79520  ? 92  LYS A O     1 
ATOM   408  C  CB    . LYS A 1  62  ? 2.03834   3.25901   29.03845  1.000 39.03989  ? 92  LYS A CB    1 
ATOM   409  C  CG    . LYS A 1  62  ? 0.56734   3.54123   28.73965  1.000 43.01729  ? 92  LYS A CG    1 
ATOM   410  C  CD    . LYS A 1  62  ? 0.14406   2.94126   27.41872  1.000 41.12739  ? 92  LYS A CD    1 
ATOM   411  C  CE    . LYS A 1  62  ? 0.87000   3.58611   26.26360  1.000 43.91688  ? 92  LYS A CE    1 
ATOM   412  N  NZ    . LYS A 1  62  ? 0.73870   2.74410   25.03465  1.000 48.59653  ? 92  LYS A NZ    1 
ATOM   413  N  N     . THR A 1  63  ? 4.66301   1.41459   28.81014  1.000 30.15535  ? 93  THR A N     1 
ATOM   414  C  CA    . THR A 1  63  ? 6.09701   1.21037   29.01395  1.000 39.85992  ? 93  THR A CA    1 
ATOM   415  C  C     . THR A 1  63  ? 6.89598   1.93821   27.94682  1.000 30.36936  ? 93  THR A C     1 
ATOM   416  O  O     . THR A 1  63  ? 6.66778   1.73521   26.74986  1.000 38.01168  ? 93  THR A O     1 
ATOM   417  C  CB    . THR A 1  63  ? 6.46377   -0.28969  28.99794  1.000 43.14064  ? 93  THR A CB    1 
ATOM   418  O  OG1   . THR A 1  63  ? 5.78281   -0.96255  30.06006  1.000 44.65809  ? 93  THR A OG1   1 
ATOM   419  C  CG2   . THR A 1  63  ? 7.95677   -0.47292  29.18974  1.000 26.40386  ? 93  THR A CG2   1 
ATOM   420  N  N     . PHE A 1  64  ? 7.84617   2.77307   28.38066  1.000 28.94259  ? 94  PHE A N     1 
ATOM   421  C  CA    . PHE A 1  64  ? 8.69316   3.52791   27.47152  1.000 29.59917  ? 94  PHE A CA    1 
ATOM   422  C  C     . PHE A 1  64  ? 10.14620  3.38670   27.90033  1.000 32.38469  ? 94  PHE A C     1 
ATOM   423  O  O     . PHE A 1  64  ? 10.43933  3.18769   29.08629  1.000 32.22493  ? 94  PHE A O     1 
ATOM   424  C  CB    . PHE A 1  64  ? 8.30339   5.03097   27.43753  1.000 30.70503  ? 94  PHE A CB    1 
ATOM   425  C  CG    . PHE A 1  64  ? 6.82641   5.25920   27.29073  1.000 32.01818  ? 94  PHE A CG    1 
ATOM   426  C  CD1   . PHE A 1  64  ? 6.19520   5.01727   26.07683  1.000 30.39031  ? 94  PHE A CD1   1 
ATOM   427  C  CD2   . PHE A 1  64  ? 6.06262   5.69135   28.35482  1.000 37.27682  ? 94  PHE A CD2   1 
ATOM   428  C  CE1   . PHE A 1  64  ? 4.83121   5.21048   25.93601  1.000 27.75847  ? 94  PHE A CE1   1 
ATOM   429  C  CE2   . PHE A 1  64  ? 4.69464   5.89756   28.21401  1.000 36.09187  ? 94  PHE A CE2   1 
ATOM   430  C  CZ    . PHE A 1  64  ? 4.08743   5.65963   27.00810  1.000 37.09234  ? 94  PHE A CZ    1 
ATOM   431  N  N     . PHE A 1  65  ? 11.04208  3.49453   26.91920  1.000 32.23070  ? 95  PHE A N     1 
ATOM   432  C  CA    . PHE A 1  65  ? 12.48009  3.37031   27.11801  1.000 24.62398  ? 95  PHE A CA    1 
ATOM   433  C  C     . PHE A 1  65  ? 13.18027  4.71119   26.91687  1.000 30.94378  ? 95  PHE A C     1 
ATOM   434  O  O     . PHE A 1  65  ? 12.97623  5.37619   25.89488  1.000 26.84741  ? 95  PHE A O     1 
ATOM   435  C  CB    . PHE A 1  65  ? 13.04879  2.32619   26.16996  1.000 25.77739  ? 95  PHE A CB    1 
ATOM   436  C  CG    . PHE A 1  65  ? 12.49261  0.96728   26.41807  1.000 33.04441  ? 95  PHE A CG    1 
ATOM   437  C  CD1   . PHE A 1  65  ? 13.06961  0.13522   27.37502  1.000 24.69333  ? 95  PHE A CD1   1 
ATOM   438  C  CD2   . PHE A 1  65  ? 11.35445  0.53744   25.75024  1.000 31.98896  ? 95  PHE A CD2   1 
ATOM   439  C  CE1   . PHE A 1  65  ? 12.53845  -1.12069  27.63413  1.000 27.63167  ? 95  PHE A CE1   1 
ATOM   440  C  CE2   . PHE A 1  65  ? 10.80329  -0.72546  26.00036  1.000 35.12567  ? 95  PHE A CE2   1 
ATOM   441  C  CZ    . PHE A 1  65  ? 11.40629  -1.55653  26.95630  1.000 26.60709  ? 95  PHE A CZ    1 
ATOM   442  N  N     . LEU A 1  66  ? 14.02646  5.08509   27.88074  1.000 36.78842  ? 96  LEU A N     1 
ATOM   443  C  CA    . LEU A 1  66  ? 14.70667  6.38398   27.88661  1.000 24.84381  ? 96  LEU A CA    1 
ATOM   444  C  C     . LEU A 1  66  ? 16.08256  6.22774   27.24542  1.000 25.99852  ? 96  LEU A C     1 
ATOM   445  O  O     . LEU A 1  66  ? 16.88949  5.41663   27.69634  1.000 29.45100  ? 96  LEU A O     1 
ATOM   446  C  CB    . LEU A 1  66  ? 14.84095  6.90100   29.31858  1.000 24.50038  ? 96  LEU A CB    1 
ATOM   447  C  CG    . LEU A 1  66  ? 13.55208  7.01623   30.12975  1.000 24.14140  ? 96  LEU A CG    1 
ATOM   448  C  CD1   . LEU A 1  66  ? 13.82135  7.50223   31.56270  1.000 23.84929  ? 96  LEU A CD1   1 
ATOM   449  C  CD2   . LEU A 1  66  ? 12.56713  7.96936   29.42686  1.000 27.91665  ? 96  LEU A CD2   1 
ATOM   450  N  N     . LEU A 1  67  ? 16.35653  6.99467   26.19636  1.000 25.75393  ? 97  LEU A N     1 
ATOM   451  C  CA    . LEU A 1  67  ? 17.64543  6.92445   25.52919  1.000 26.27230  ? 97  LEU A CA    1 
ATOM   452  C  C     . LEU A 1  67  ? 18.17062  8.33136   25.28707  1.000 30.25202  ? 97  LEU A C     1 
ATOM   453  O  O     . LEU A 1  67  ? 17.39673  9.25847   25.06015  1.000 36.14664  ? 97  LEU A O     1 
ATOM   454  C  CB    . LEU A 1  67  ? 17.54412  6.18342   24.18022  1.000 26.63138  ? 97  LEU A CB    1 
ATOM   455  C  CG    . LEU A 1  67  ? 17.45690  4.65344   24.29628  1.000 28.94835  ? 97  LEU A CG    1 
ATOM   456  C  CD1   . LEU A 1  67  ? 16.94363  4.06648   23.00337  1.000 27.51834  ? 97  LEU A CD1   1 
ATOM   457  C  CD2   . LEU A 1  67  ? 18.83086  4.08723   24.63011  1.000 29.35139  ? 97  LEU A CD2   1 
ATOM   458  N  N     . GLY A 1  68  ? 19.48365  8.47815   25.35389  1.000 27.12248  ? 98  GLY A N     1 
ATOM   459  C  CA    . GLY A 1  68  ? 20.14076  9.64103   24.80676  1.000 35.90701  ? 98  GLY A CA    1 
ATOM   460  C  C     . GLY A 1  68  ? 20.68752  9.36191   23.42070  1.000 40.68611  ? 98  GLY A C     1 
ATOM   461  O  O     . GLY A 1  68  ? 20.17528  8.51197   22.67379  1.000 33.71242  ? 98  GLY A O     1 
ATOM   462  N  N     . THR A 1  69  ? 21.76558  10.05473  23.07653  1.000 34.66194  ? 99  THR A N     1 
ATOM   463  C  CA    . THR A 1  69  ? 22.43038  9.87559   21.79444  1.000 36.87763  ? 99  THR A CA    1 
ATOM   464  C  C     . THR A 1  69  ? 23.80331  9.25238   22.00727  1.000 41.51491  ? 99  THR A C     1 
ATOM   465  O  O     . THR A 1  69  ? 24.30345  9.14733   23.13620  1.000 40.22987  ? 99  THR A O     1 
ATOM   466  C  CB    . THR A 1  69  ? 22.53148  11.20855  21.03839  1.000 38.56872  ? 99  THR A CB    1 
ATOM   467  O  OG1   . THR A 1  69  ? 23.01576  12.23050  21.91829  1.000 36.26033  ? 99  THR A OG1   1 
ATOM   468  C  CG2   . THR A 1  69  ? 21.17447  11.61575  20.51656  1.000 32.10124  ? 99  THR A CG2   1 
ATOM   469  N  N     . THR A 1  70  ? 24.40409  8.81125   20.90220  1.000 45.79679  ? 100 THR A N     1 
ATOM   470  C  CA    . THR A 1  70  ? 25.71599  8.19004   20.94004  1.000 50.31400  ? 100 THR A CA    1 
ATOM   471  C  C     . THR A 1  70  ? 26.52390  8.64288   19.73291  1.000 52.82959  ? 100 THR A C     1 
ATOM   472  O  O     . THR A 1  70  ? 25.97483  9.09494   18.72497  1.000 56.50498  ? 100 THR A O     1 
ATOM   473  C  CB    . THR A 1  70  ? 25.60776  6.65906   20.96910  1.000 48.39389  ? 100 THR A CB    1 
ATOM   474  O  OG1   . THR A 1  70  ? 26.91365  6.08185   20.87693  1.000 53.35099  ? 100 THR A OG1   1 
ATOM   475  C  CG2   . THR A 1  70  ? 24.74152  6.16816   19.82023  1.000 51.33226  ? 100 THR A CG2   1 
ATOM   476  N  N     . SER A 1  71  ? 27.84990  8.52168   19.85573  1.000 54.56863  ? 101 SER A N     1 
ATOM   477  C  CA    . SER A 1  71  ? 28.73379  8.83850   18.73660  1.000 61.81407  ? 101 SER A CA    1 
ATOM   478  C  C     . SER A 1  71  ? 28.63147  7.79049   17.62865  1.000 63.57526  ? 101 SER A C     1 
ATOM   479  O  O     . SER A 1  71  ? 28.72736  8.13144   16.44262  1.000 65.61148  ? 101 SER A O     1 
ATOM   480  C  CB    . SER A 1  71  ? 30.17888  8.96429   19.22140  1.000 54.96683  ? 101 SER A CB    1 
ATOM   481  O  OG    . SER A 1  71  ? 30.79370  7.68920   19.36835  1.000 78.55790  ? 101 SER A OG    1 
ATOM   482  N  N     . SER A 1  72  ? 28.42433  6.52853   17.99571  1.000 61.98995  ? 102 SER A N     1 
ATOM   483  C  CA    . SER A 1  72  ? 28.34202  5.43652   17.03075  1.000 58.78615  ? 102 SER A CA    1 
ATOM   484  C  C     . SER A 1  72  ? 27.19492  5.64367   16.04891  1.000 55.90642  ? 102 SER A C     1 
ATOM   485  O  O     . SER A 1  72  ? 26.02498  5.70486   16.44407  1.000 59.91931  ? 102 SER A O     1 
ATOM   486  C  CB    . SER A 1  72  ? 28.17391  4.11256   17.77782  1.000 60.77105  ? 102 SER A CB    1 
ATOM   487  O  OG    . SER A 1  72  ? 27.76763  3.07760   16.89690  1.000 66.72310  ? 102 SER A OG    1 
ATOM   488  N  N     . ALA A 1  73  ? 27.52675  5.73258   14.75786  1.000 70.25777  ? 103 ALA A N     1 
ATOM   489  C  CA    . ALA A 1  73  ? 26.48963  5.83671   13.73700  1.000 72.64632  ? 103 ALA A CA    1 
ATOM   490  C  C     . ALA A 1  73  ? 25.69141  4.54183   13.61415  1.000 66.06237  ? 103 ALA A C     1 
ATOM   491  O  O     . ALA A 1  73  ? 24.48537  4.57102   13.32731  1.000 66.66315  ? 103 ALA A O     1 
ATOM   492  C  CB    . ALA A 1  73  ? 27.11750  6.20857   12.39590  1.000 54.61541  ? 103 ALA A CB    1 
ATOM   493  N  N     . ALA A 1  74  ? 26.34426  3.40074   13.84909  1.000 63.27616  ? 104 ALA A N     1 
ATOM   494  C  CA    . ALA A 1  74  ? 25.64905  2.12085   13.80622  1.000 65.79343  ? 104 ALA A CA    1 
ATOM   495  C  C     . ALA A 1  74  ? 24.56919  2.04605   14.88037  1.000 69.63718  ? 104 ALA A C     1 
ATOM   496  O  O     . ALA A 1  74  ? 23.42109  1.68222   14.59954  1.000 64.16791  ? 104 ALA A O     1 
ATOM   497  C  CB    . ALA A 1  74  ? 26.65089  0.97569   13.96812  1.000 55.43404  ? 104 ALA A CB    1 
ATOM   498  N  N     . GLU A 1  75  ? 24.92641  2.37403   16.12431  1.000 62.24703  ? 105 GLU A N     1 
ATOM   499  C  CA    . GLU A 1  75  ? 23.94556  2.34521   17.20445  1.000 55.95944  ? 105 GLU A CA    1 
ATOM   500  C  C     . GLU A 1  75  ? 22.84168  3.36838   16.96157  1.000 57.00566  ? 105 GLU A C     1 
ATOM   501  O  O     . GLU A 1  75  ? 21.66368  3.10057   17.23874  1.000 58.59332  ? 105 GLU A O     1 
ATOM   502  C  CB    . GLU A 1  75  ? 24.63478  2.59814   18.54335  1.000 56.57833  ? 105 GLU A CB    1 
ATOM   503  C  CG    . GLU A 1  75  ? 25.67967  1.54699   18.91723  1.000 61.46509  ? 105 GLU A CG    1 
ATOM   504  C  CD    . GLU A 1  75  ? 26.35090  1.83592   20.24913  1.000 82.02820  ? 105 GLU A CD    1 
ATOM   505  O  OE1   . GLU A 1  75  ? 26.10815  2.91898   20.82214  1.000 80.06965  ? 105 GLU A OE1   1 
ATOM   506  O  OE2   . GLU A 1  75  ? 27.12383  0.97782   20.72905  1.000 96.19224  ? 105 GLU A OE2   1 
ATOM   507  N  N     . THR A 1  76  ? 23.20180  4.54831   16.44949  1.000 56.05215  ? 106 THR A N     1 
ATOM   508  C  CA    . THR A 1  76  ? 22.18891  5.53546   16.09660  1.000 50.71925  ? 106 THR A CA    1 
ATOM   509  C  C     . THR A 1  76  ? 21.16668  4.94359   15.13376  1.000 56.01532  ? 106 THR A C     1 
ATOM   510  O  O     . THR A 1  76  ? 19.95373  5.09379   15.31792  1.000 59.85698  ? 106 THR A O     1 
ATOM   511  C  CB    . THR A 1  76  ? 22.84402  6.77434   15.47947  1.000 58.60663  ? 106 THR A CB    1 
ATOM   512  O  OG1   . THR A 1  76  ? 23.83122  7.30121   16.37632  1.000 54.23756  ? 106 THR A OG1   1 
ATOM   513  C  CG2   . THR A 1  76  ? 21.78714  7.83449   15.20259  1.000 41.34972  ? 106 THR A CG2   1 
ATOM   514  N  N     . LYS A 1  77  ? 21.64543  4.26148   14.09071  1.000 54.14891  ? 107 LYS A N     1 
ATOM   515  C  CA    . LYS A 1  77  ? 20.73020  3.70160   13.09786  1.000 61.57812  ? 107 LYS A CA    1 
ATOM   516  C  C     . LYS A 1  77  ? 19.89811  2.56875   13.68800  1.000 63.60104  ? 107 LYS A C     1 
ATOM   517  O  O     . LYS A 1  77  ? 18.69705  2.45793   13.40217  1.000 55.98328  ? 107 LYS A O     1 
ATOM   518  C  CB    . LYS A 1  77  ? 21.51396  3.21344   11.88476  1.000 60.21126  ? 107 LYS A CB    1 
ATOM   519  C  CG    . LYS A 1  77  ? 20.64971  2.57455   10.80990  1.000 65.28790  ? 107 LYS A CG    1 
ATOM   520  C  CD    . LYS A 1  77  ? 19.61979  3.55269   10.25401  1.000 77.34344  ? 107 LYS A CD    1 
ATOM   521  C  CE    . LYS A 1  77  ? 18.85353  2.94678   9.08314   1.000 92.98342  ? 107 LYS A CE    1 
ATOM   522  N  NZ    . LYS A 1  77  ? 17.75760  3.84194   8.60226   1.000 88.75939  ? 107 LYS A NZ    1 
ATOM   523  N  N     . GLU A 1  78  ? 20.52209  1.71867   14.50394  1.000 55.37389  ? 108 GLU A N     1 
ATOM   524  C  CA    . GLU A 1  78  ? 19.78401  0.65781   15.18308  1.000 44.27384  ? 108 GLU A CA    1 
ATOM   525  C  C     . GLU A 1  78  ? 18.62921  1.23401   15.98322  1.000 53.17221  ? 108 GLU A C     1 
ATOM   526  O  O     . GLU A 1  78  ? 17.49713  0.75219   15.89539  1.000 47.18439  ? 108 GLU A O     1 
ATOM   527  C  CB    . GLU A 1  78  ? 20.72002  -0.12431  16.09697  1.000 58.38266  ? 108 GLU A CB    1 
ATOM   528  C  CG    . GLU A 1  78  ? 21.83080  -0.86351  15.37784  1.000 57.83054  ? 108 GLU A CG    1 
ATOM   529  C  CD    . GLU A 1  78  ? 22.95886  -1.27666  16.30669  1.000 78.55033  ? 108 GLU A CD    1 
ATOM   530  O  OE1   . GLU A 1  78  ? 22.81606  -1.13660  17.54171  1.000 76.42721  ? 108 GLU A OE1   1 
ATOM   531  O  OE2   . GLU A 1  78  ? 24.00572  -1.72984  15.79756  1.000 79.08834  ? 108 GLU A OE2   1 
ATOM   532  N  N     . VAL A 1  79  ? 18.90549  2.27899   16.77315  1.000 51.77914  ? 109 VAL A N     1 
ATOM   533  C  CA    . VAL A 1  79  ? 17.88570  2.84718   17.65027  1.000 49.23574  ? 109 VAL A CA    1 
ATOM   534  C  C     . VAL A 1  79  ? 16.81570  3.56333   16.83440  1.000 52.78320  ? 109 VAL A C     1 
ATOM   535  O  O     . VAL A 1  79  ? 15.62773  3.50652   17.16957  1.000 49.10055  ? 109 VAL A O     1 
ATOM   536  C  CB    . VAL A 1  79  ? 18.54299  3.77211   18.69516  1.000 51.58775  ? 109 VAL A CB    1 
ATOM   537  C  CG1   . VAL A 1  79  ? 17.53822  4.75128   19.25027  1.000 56.92268  ? 109 VAL A CG1   1 
ATOM   538  C  CG2   . VAL A 1  79  ? 19.11001  2.93605   19.82510  1.000 40.32071  ? 109 VAL A CG2   1 
ATOM   539  N  N     . ASP A 1  80  ? 17.20465  4.23723   15.75033  1.000 52.85766  ? 110 ASP A N     1 
ATOM   540  C  CA    . ASP A 1  80  ? 16.20662  4.81036   14.85245  1.000 54.95879  ? 110 ASP A CA    1 
ATOM   541  C  C     . ASP A 1  80  ? 15.24238  3.74250   14.35161  1.000 52.34598  ? 110 ASP A C     1 
ATOM   542  O  O     . ASP A 1  80  ? 14.01242  3.91070   14.41178  1.000 52.25765  ? 110 ASP A O     1 
ATOM   543  C  CB    . ASP A 1  80  ? 16.90757  5.50322   13.68633  1.000 52.29548  ? 110 ASP A CB    1 
ATOM   544  C  CG    . ASP A 1  80  ? 17.72482  6.69610   14.13118  1.000 79.05591  ? 110 ASP A CG    1 
ATOM   545  O  OD1   . ASP A 1  80  ? 17.50005  7.19617   15.25920  1.000 66.54189  ? 110 ASP A OD1   1 
ATOM   546  O  OD2   . ASP A 1  80  ? 18.59078  7.14894   13.35205  1.000 88.26882  ? 110 ASP A OD2   1 
ATOM   547  N  N     . GLN A 1  81  ? 15.77314  2.61440   13.88657  1.000 45.85404  ? 111 GLN A N     1 
ATOM   548  C  CA    . GLN A 1  81  ? 14.91990  1.50952   13.38772  1.000 52.92477  ? 111 GLN A CA    1 
ATOM   549  C  C     . GLN A 1  81  ? 14.03696  0.93569   14.50186  1.000 53.12857  ? 111 GLN A C     1 
ATOM   550  O  O     . GLN A 1  81  ? 12.86488  0.65087   14.23503  1.000 47.13278  ? 111 GLN A O     1 
ATOM   551  C  CB    . GLN A 1  81  ? 15.81865  0.40437   12.84563  1.000 55.59004  ? 111 GLN A CB    1 
ATOM   552  C  CG    . GLN A 1  81  ? 16.59854  0.78121   11.59151  1.000 67.23705  ? 111 GLN A CG    1 
ATOM   553  C  CD    . GLN A 1  81  ? 17.71234  -0.18998  11.28639  1.000 73.22817  ? 111 GLN A CD    1 
ATOM   554  O  OE1   . GLN A 1  81  ? 18.43122  -0.06312  10.28828  1.000 70.34835  ? 111 GLN A OE1   1 
ATOM   555  N  NE2   . GLN A 1  81  ? 17.87230  -1.18398  12.14639  1.000 63.10736  ? 111 GLN A NE2   1 
ATOM   556  N  N     . GLU A 1  82  ? 14.59410  0.77364   15.70079  1.000 51.90446  ? 112 GLU A N     1 
ATOM   557  C  CA    . GLU A 1  82  ? 13.82518  0.25380   16.85791  1.000 43.72980  ? 112 GLU A CA    1 
ATOM   558  C  C     . GLU A 1  82  ? 12.63436  1.17999   17.14305  1.000 45.53841  ? 112 GLU A C     1 
ATOM   559  O  O     . GLU A 1  82  ? 11.52131  0.66617   17.30622  1.000 45.12776  ? 112 GLU A O     1 
ATOM   560  C  CB    . GLU A 1  82  ? 14.78432  0.11268   18.03578  1.000 44.89449  ? 112 GLU A CB    1 
ATOM   561  C  CG    . GLU A 1  82  ? 14.17239  -0.53719  19.27089  1.000 47.92716  ? 112 GLU A CG    1 
ATOM   562  C  CD    . GLU A 1  82  ? 15.13555  -0.55231  20.44475  1.000 47.08587  ? 112 GLU A CD    1 
ATOM   563  O  OE1   . GLU A 1  82  ? 16.34854  -0.39150  20.20758  1.000 47.54676  ? 112 GLU A OE1   1 
ATOM   564  O  OE2   . GLU A 1  82  ? 14.67768  -0.71720  21.58882  1.000 47.51902  ? 112 GLU A OE2   1 
ATOM   565  N  N     . SER A 1  83  ? 12.86858  2.48896   17.17498  1.000 42.29424  ? 113 SER A N     1 
ATOM   566  C  CA    . SER A 1  83  ? 11.76376  3.45014   17.41710  1.000 42.63863  ? 113 SER A CA    1 
ATOM   567  C  C     . SER A 1  83  ? 10.67359  3.28628   16.35426  1.000 44.98259  ? 113 SER A C     1 
ATOM   568  O  O     . SER A 1  83  ? 9.49665   3.37447   16.69942  1.000 44.47661  ? 113 SER A O     1 
ATOM   569  C  CB    . SER A 1  83  ? 12.25399  4.86206   17.47099  1.000 44.43518  ? 113 SER A CB    1 
ATOM   570  O  OG    . SER A 1  83  ? 11.33722  5.69323   18.16710  1.000 51.59939  ? 113 SER A OG    1 
ATOM   571  N  N     . GLN A 1  84  ? 11.07038  3.04018   15.10721  1.000 56.44220  ? 114 GLN A N     1 
ATOM   572  C  CA    . GLN A 1  84  ? 10.08620  2.89730   13.99935  1.000 55.14312  ? 114 GLN A CA    1 
ATOM   573  C  C     . GLN A 1  84  ? 9.26902   1.61044   14.18750  1.000 44.20777  ? 114 GLN A C     1 
ATOM   574  O  O     . GLN A 1  84  ? 8.06199   1.64962   13.92667  1.000 59.70915  ? 114 GLN A O     1 
ATOM   575  C  CB    . GLN A 1  84  ? 10.79003  2.96715   12.64825  1.000 62.89796  ? 114 GLN A CB    1 
ATOM   576  C  CG    . GLN A 1  84  ? 11.17019  4.38008   12.22716  1.000 62.13305  ? 114 GLN A CG    1 
ATOM   577  C  CD    . GLN A 1  84  ? 12.54312  4.46985   11.59496  1.000 85.01514  ? 114 GLN A CD    1 
ATOM   578  O  OE1   . GLN A 1  84  ? 13.07689  3.48775   11.06992  1.000 96.12558  ? 114 GLN A OE1   1 
ATOM   579  N  NE2   . GLN A 1  84  ? 13.13031  5.65675   11.64085  1.000 69.77257  ? 114 GLN A NE2   1 
ATOM   580  N  N     . ARG A 1  85  ? 9.90292   0.53735   14.64444  1.000 43.69522  ? 115 ARG A N     1 
ATOM   581  C  CA    . ARG A 1  85  ? 9.17775   -0.73653  14.85458  1.000 43.14493  ? 115 ARG A CA    1 
ATOM   582  C  C     . ARG A 1  85  ? 8.38393   -0.72637  16.16469  1.000 51.67260  ? 115 ARG A C     1 
ATOM   583  O  O     . ARG A 1  85  ? 7.27484   -1.28219  16.16186  1.000 54.74692  ? 115 ARG A O     1 
ATOM   584  C  CB    . ARG A 1  85  ? 10.12657  -1.93568  14.93548  1.000 49.05621  ? 115 ARG A CB    1 
ATOM   585  C  CG    . ARG A 1  85  ? 11.07038  -2.13586  13.76136  1.000 61.98920  ? 115 ARG A CG    1 
ATOM   586  C  CD    . ARG A 1  85  ? 11.95021  -3.35499  13.97027  1.000 56.10590  ? 115 ARG A CD    1 
ATOM   587  N  NE    . ARG A 1  85  ? 13.37826  -3.02222  13.94707  1.000 75.37784  ? 115 ARG A NE    1 
ATOM   588  C  CZ    . ARG A 1  85  ? 14.14543  -2.91031  15.01996  1.000 74.08673  ? 115 ARG A CZ    1 
ATOM   589  N  NH1   . ARG A 1  85  ? 13.65355  -3.19220  16.21403  1.000 71.52445  ? 115 ARG A NH1   1 
ATOM   590  N  NH2   . ARG A 1  85  ? 15.40147  -2.51951  14.89877  1.000 69.56553  ? 115 ARG A NH2   1 
ATOM   591  N  N     . HIS A 1  86  ? 8.89617   -0.10242  17.22960  1.000 45.35778  ? 116 HIS A N     1 
ATOM   592  C  CA    . HIS A 1  86  ? 8.22334   -0.23127  18.55070  1.000 44.18398  ? 116 HIS A CA    1 
ATOM   593  C  C     . HIS A 1  86  ? 7.51360   1.04585   19.00476  1.000 32.98292  ? 116 HIS A C     1 
ATOM   594  O  O     . HIS A 1  86  ? 6.51868   0.92303   19.73390  1.000 43.26992  ? 116 HIS A O     1 
ATOM   595  C  CB    . HIS A 1  86  ? 9.23540   -0.75540  19.57257  1.000 41.22877  ? 116 HIS A CB    1 
ATOM   596  C  CG    . HIS A 1  86  ? 9.82914   -2.07251  19.21553  1.000 43.85872  ? 116 HIS A CG    1 
ATOM   597  N  ND1   . HIS A 1  86  ? 9.11197   -3.24339  19.29666  1.000 44.54418  ? 116 HIS A ND1   1 
ATOM   598  C  CD2   . HIS A 1  86  ? 11.04603  -2.41071  18.79337  1.000 42.13602  ? 116 HIS A CD2   1 
ATOM   599  C  CE1   . HIS A 1  86  ? 9.88676   -4.24952  18.93159  1.000 41.43470  ? 116 HIS A CE1   1 
ATOM   600  N  NE2   . HIS A 1  86  ? 11.06579  -3.76672  18.62041  1.000 52.62253  ? 116 HIS A NE2   1 
ATOM   601  N  N     . GLY A 1  87  ? 8.00673   2.21176   18.61466  1.000 41.87044  ? 117 GLY A N     1 
ATOM   602  C  CA    . GLY A 1  87  ? 7.33598   3.48288   18.94871  1.000 49.34830  ? 117 GLY A CA    1 
ATOM   603  C  C     . GLY A 1  87  ? 7.22922   3.71794   20.43672  1.000 44.85549  ? 117 GLY A C     1 
ATOM   604  O  O     . GLY A 1  87  ? 6.23437   4.32511   20.86484  1.000 44.86240  ? 117 GLY A O     1 
ATOM   605  N  N     . ASP A 1  88  ? 8.21725   3.25881   21.19860  1.000 37.90538  ? 118 ASP A N     1 
ATOM   606  C  CA    . ASP A 1  88  ? 8.12647   3.38086   22.64861  1.000 38.95330  ? 118 ASP A CA    1 
ATOM   607  C  C     . ASP A 1  88  ? 9.41064   3.93968   23.23641  1.000 36.31195  ? 118 ASP A C     1 
ATOM   608  O  O     . ASP A 1  88  ? 9.71077   3.70166   24.40938  1.000 37.95211  ? 118 ASP A O     1 
ATOM   609  C  CB    . ASP A 1  88  ? 7.77135   2.03394   23.29969  1.000 36.53055  ? 118 ASP A CB    1 
ATOM   610  C  CG    . ASP A 1  88  ? 8.72612   0.91978   22.91960  1.000 42.91224  ? 118 ASP A CG    1 
ATOM   611  O  OD1   . ASP A 1  88  ? 9.76408   1.19359   22.28244  1.000 38.49016  ? 118 ASP A OD1   1 
ATOM   612  O  OD2   . ASP A 1  88  ? 8.45099   -0.25817  23.28267  1.000 50.55442  ? 118 ASP A OD2   1 
ATOM   613  N  N     . ILE A 1  89  ? 10.15965  4.71054   22.44929  1.000 31.64030  ? 119 ILE A N     1 
ATOM   614  C  CA    . ILE A 1  89  ? 11.41881  5.30435   22.87710  1.000 29.35433  ? 119 ILE A CA    1 
ATOM   615  C  C     . ILE A 1  89  ? 11.22607  6.80339   23.07908  1.000 31.34908  ? 119 ILE A C     1 
ATOM   616  O  O     . ILE A 1  89  ? 10.64306  7.48445   22.22514  1.000 42.43311  ? 119 ILE A O     1 
ATOM   617  C  CB    . ILE A 1  89  ? 12.53062  5.01515   21.86095  1.000 26.32569  ? 119 ILE A CB    1 
ATOM   618  C  CG1   . ILE A 1  89  ? 12.86339  3.51509   21.88795  1.000 32.35970  ? 119 ILE A CG1   1 
ATOM   619  C  CG2   . ILE A 1  89  ? 13.75579  5.83696   22.17476  1.000 31.54182  ? 119 ILE A CG2   1 
ATOM   620  C  CD1   . ILE A 1  89  ? 13.97920  3.13089   20.96281  1.000 40.65932  ? 119 ILE A CD1   1 
ATOM   621  N  N     . ILE A 1  90  ? 11.66731  7.29935   24.23200  1.000 33.49037  ? 120 ILE A N     1 
ATOM   622  C  CA    . ILE A 1  90  ? 11.76457  8.72134   24.53695  1.000 28.99306  ? 120 ILE A CA    1 
ATOM   623  C  C     . ILE A 1  90  ? 13.23561  9.09711   24.40673  1.000 27.57602  ? 120 ILE A C     1 
ATOM   624  O  O     . ILE A 1  90  ? 14.08562  8.51800   25.10063  1.000 37.83004  ? 120 ILE A O     1 
ATOM   625  C  CB    . ILE A 1  90  ? 11.25382  9.03047   25.95501  1.000 25.42957  ? 120 ILE A CB    1 
ATOM   626  C  CG1   . ILE A 1  90  ? 9.78777   8.60670   26.12122  1.000 25.23452  ? 120 ILE A CG1   1 
ATOM   627  C  CG2   . ILE A 1  90  ? 11.48810  10.53944  26.30493  1.000 33.48935  ? 120 ILE A CG2   1 
ATOM   628  C  CD1   . ILE A 1  90  ? 9.35795   8.45481   27.58629  1.000 29.34678  ? 120 ILE A CD1   1 
ATOM   629  N  N     . GLN A 1  91  ? 13.54865  10.07404  23.55366  1.000 30.85574  ? 121 GLN A N     1 
ATOM   630  C  CA    . GLN A 1  91  ? 14.93967  10.40781  23.29746  1.000 29.45621  ? 121 GLN A CA    1 
ATOM   631  C  C     . GLN A 1  91  ? 15.15990  11.91177  23.26239  1.000 35.79467  ? 121 GLN A C     1 
ATOM   632  O  O     . GLN A 1  91  ? 14.34894  12.65188  22.69248  1.000 42.11040  ? 121 GLN A O     1 
ATOM   633  C  CB    . GLN A 1  91  ? 15.42939  9.82569   21.97341  1.000 36.00740  ? 121 GLN A CB    1 
ATOM   634  C  CG    . GLN A 1  91  ? 16.93739  9.97445   21.76620  1.000 36.28484  ? 121 GLN A CG    1 
ATOM   635  C  CD    . GLN A 1  91  ? 17.37412  9.45234   20.39815  1.000 39.90118  ? 121 GLN A CD    1 
ATOM   636  O  OE1   . GLN A 1  91  ? 16.77903  9.78541   19.38222  1.000 48.36727  ? 121 GLN A OE1   1 
ATOM   637  N  NE2   . GLN A 1  91  ? 18.41098  8.62518   20.37803  1.000 39.75580  ? 121 GLN A NE2   1 
ATOM   638  N  N     . LYS A 1  92  ? 16.27605  12.34461  23.85322  1.000 34.84754  ? 122 LYS A N     1 
ATOM   639  C  CA    . LYS A 1  92  ? 16.78424  13.70253  23.69611  1.000 31.01625  ? 122 LYS A CA    1 
ATOM   640  C  C     . LYS A 1  92  ? 18.26818  13.63029  23.35791  1.000 42.89501  ? 122 LYS A C     1 
ATOM   641  O  O     . LYS A 1  92  ? 18.92504  12.59319  23.52485  1.000 39.78864  ? 122 LYS A O     1 
ATOM   642  C  CB    . LYS A 1  92  ? 16.55155  14.55460  24.94812  1.000 30.01221  ? 122 LYS A CB    1 
ATOM   643  C  CG    . LYS A 1  92  ? 15.09364  14.90284  25.20331  1.000 37.60049  ? 122 LYS A CG    1 
ATOM   644  C  CD    . LYS A 1  92  ? 14.90395  15.83190  26.40331  1.000 27.79836  ? 122 LYS A CD    1 
ATOM   645  C  CE    . LYS A 1  92  ? 15.49013  17.19980  26.13219  1.000 41.11119  ? 122 LYS A CE    1 
ATOM   646  N  NZ    . LYS A 1  92  ? 15.04143  18.20490  27.14322  1.000 48.03159  ? 122 LYS A NZ    1 
ATOM   647  N  N     . ASP A 1  93  ? 18.80129  14.75519  22.87480  1.000 38.76589  ? 123 ASP A N     1 
ATOM   648  C  CA    . ASP A 1  93  ? 20.18824  14.80796  22.40161  1.000 41.83358  ? 123 ASP A CA    1 
ATOM   649  C  C     . ASP A 1  93  ? 21.13644  15.10884  23.55747  1.000 49.78169  ? 123 ASP A C     1 
ATOM   650  O  O     . ASP A 1  93  ? 21.56465  16.24278  23.77938  1.000 58.24134  ? 123 ASP A O     1 
ATOM   651  C  CB    . ASP A 1  93  ? 20.33625  15.84790  21.29456  1.000 51.77277  ? 123 ASP A CB    1 
ATOM   652  C  CG    . ASP A 1  93  ? 21.69115  15.79367  20.62437  1.000 63.22545  ? 123 ASP A CG    1 
ATOM   653  O  OD1   . ASP A 1  93  ? 22.47805  14.87255  20.94329  1.000 78.31691  ? 123 ASP A OD1   1 
ATOM   654  O  OD2   . ASP A 1  93  ? 21.96917  16.66760  19.77631  1.000 86.39655  ? 123 ASP A OD2   1 
ATOM   655  N  N     . PHE A 1  94  ? 21.49138  14.06181  24.29145  1.000 38.72554  ? 124 PHE A N     1 
ATOM   656  C  CA    . PHE A 1  94  ? 22.56253  14.14167  25.26630  1.000 30.99044  ? 124 PHE A CA    1 
ATOM   657  C  C     . PHE A 1  94  ? 23.35531  12.85054  25.16623  1.000 38.87608  ? 124 PHE A C     1 
ATOM   658  O  O     . PHE A 1  94  ? 22.79411  11.78862  24.89434  1.000 32.50271  ? 124 PHE A O     1 
ATOM   659  C  CB    . PHE A 1  94  ? 22.02976  14.35979  26.68637  1.000 29.24643  ? 124 PHE A CB    1 
ATOM   660  C  CG    . PHE A 1  94  ? 21.23165  13.19893  27.20351  1.000 28.32241  ? 124 PHE A CG    1 
ATOM   661  C  CD1   . PHE A 1  94  ? 19.86460  13.13214  26.97470  1.000 34.75664  ? 124 PHE A CD1   1 
ATOM   662  C  CD2   . PHE A 1  94  ? 21.85358  12.16585  27.88845  1.000 27.95138  ? 124 PHE A CD2   1 
ATOM   663  C  CE1   . PHE A 1  94  ? 19.12450  12.03827  27.43984  1.000 31.83641  ? 124 PHE A CE1   1 
ATOM   664  C  CE2   . PHE A 1  94  ? 21.12447  11.08698  28.35159  1.000 27.19492  ? 124 PHE A CE2   1 
ATOM   665  C  CZ    . PHE A 1  94  ? 19.76043  11.02219  28.12478  1.000 31.63564  ? 124 PHE A CZ    1 
ATOM   666  N  N     . LEU A 1  95  ? 24.66735  12.95034  25.37104  1.000 35.33781  ? 125 LEU A N     1 
ATOM   667  C  CA    . LEU A 1  95  ? 25.51616  11.77720  25.29296  1.000 33.70573  ? 125 LEU A CA    1 
ATOM   668  C  C     . LEU A 1  95  ? 25.08914  10.74930  26.33805  1.000 39.37063  ? 125 LEU A C     1 
ATOM   669  O  O     . LEU A 1  95  ? 25.12635  11.01533  27.54304  1.000 30.62592  ? 125 LEU A O     1 
ATOM   670  C  CB    . LEU A 1  95  ? 26.98025  12.15698  25.50175  1.000 34.08752  ? 125 LEU A CB    1 
ATOM   671  C  CG    . LEU A 1  95  ? 27.94004  10.96382  25.39065  1.000 43.69439  ? 125 LEU A CG    1 
ATOM   672  C  CD1   . LEU A 1  95  ? 27.86875  10.34379  23.99668  1.000 37.08116  ? 125 LEU A CD1   1 
ATOM   673  C  CD2   . LEU A 1  95  ? 29.36515  11.33061  25.75544  1.000 38.08937  ? 125 LEU A CD2   1 
ATOM   674  N  N     . ASP A 1  96  ? 24.68789  9.57235   25.87914  1.000 35.40009  ? 126 ASP A N     1 
ATOM   675  C  CA    . ASP A 1  96  ? 24.12286  8.55946   26.76425  1.000 28.32656  ? 126 ASP A CA    1 
ATOM   676  C  C     . ASP A 1  96  ? 25.26481  7.75330   27.38011  1.000 38.64152  ? 126 ASP A C     1 
ATOM   677  O  O     . ASP A 1  96  ? 25.74458  6.78221   26.80507  1.000 37.51924  ? 126 ASP A O     1 
ATOM   678  C  CB    . ASP A 1  96  ? 23.14861  7.69159   25.98041  1.000 36.45882  ? 126 ASP A CB    1 
ATOM   679  C  CG    . ASP A 1  96  ? 22.27260  6.84676   26.87355  1.000 38.71836  ? 126 ASP A CG    1 
ATOM   680  O  OD1   . ASP A 1  96  ? 22.67073  6.61373   28.03850  1.000 30.28836  ? 126 ASP A OD1   1 
ATOM   681  O  OD2   . ASP A 1  96  ? 21.19447  6.41991   26.40371  1.000 36.10652  ? 126 ASP A OD2   1 
ATOM   682  N  N     . VAL A 1  97  ? 25.70404  8.16127   28.57804  1.000 35.77472  ? 127 VAL A N     1 
ATOM   683  C  CA    . VAL A 1  97  ? 26.75104  7.46912   29.32591  1.000 30.86250  ? 127 VAL A CA    1 
ATOM   684  C  C     . VAL A 1  97  ? 26.37424  7.44623   30.80397  1.000 36.14973  ? 127 VAL A C     1 
ATOM   685  O  O     . VAL A 1  97  ? 25.51042  8.20038   31.24806  1.000 33.88871  ? 127 VAL A O     1 
ATOM   686  C  CB    . VAL A 1  97  ? 28.13212  8.14790   29.16970  1.000 32.63665  ? 127 VAL A CB    1 
ATOM   687  C  CG1   . VAL A 1  97  ? 28.61791  8.04278   27.73664  1.000 30.00860  ? 127 VAL A CG1   1 
ATOM   688  C  CG2   . VAL A 1  97  ? 28.05041  9.59393   29.62067  1.000 29.26460  ? 127 VAL A CG2   1 
ATOM   689  N  N     . TYR A 1  98  ? 27.00421  6.58615   31.59791  1.000 37.59613  ? 128 TYR A N     1 
ATOM   690  C  CA    . TYR A 1  98  ? 26.60539  6.42726   33.02497  1.000 34.16346  ? 128 TYR A CA    1 
ATOM   691  C  C     . TYR A 1  98  ? 26.57370  7.76128   33.75293  1.000 30.18063  ? 128 TYR A C     1 
ATOM   692  O  O     . TYR A 1  98  ? 25.67384  7.99345   34.56805  1.000 27.85405  ? 128 TYR A O     1 
ATOM   693  C  CB    . TYR A 1  98  ? 27.52134  5.46913   33.79287  1.000 27.24290  ? 128 TYR A CB    1 
ATOM   694  C  CG    . TYR A 1  98  ? 26.90443  4.90027   35.06197  1.000 36.67452  ? 128 TYR A CG    1 
ATOM   695  C  CD1   . TYR A 1  98  ? 26.04525  3.81240   35.01012  1.000 29.03299  ? 128 TYR A CD1   1 
ATOM   696  C  CD2   . TYR A 1  98  ? 27.17768  5.45126   36.30691  1.000 36.77522  ? 128 TYR A CD2   1 
ATOM   697  C  CE1   . TYR A 1  98  ? 25.47432  3.29252   36.15721  1.000 32.70191  ? 128 TYR A CE1   1 
ATOM   698  C  CE2   . TYR A 1  98  ? 26.60976  4.94038   37.46101  1.000 40.90330  ? 128 TYR A CE2   1 
ATOM   699  C  CZ    . TYR A 1  98  ? 25.75358  3.85852   37.38516  1.000 41.59206  ? 128 TYR A CZ    1 
ATOM   700  O  OH    . TYR A 1  98  ? 25.18966  3.33564   38.51025  1.000 47.06755  ? 128 TYR A OH    1 
ATOM   701  N  N     . TYR A 1  99  ? 27.55880  8.60612   33.50977  1.000 27.18605  ? 129 TYR A N     1 
ATOM   702  C  CA    . TYR A 1  99  ? 27.64210  9.89113   34.27072  1.000 31.71076  ? 129 TYR A CA    1 
ATOM   703  C  C     . TYR A 1  99  ? 26.66019  10.93627  33.74083  1.000 32.85627  ? 129 TYR A C     1 
ATOM   704  O  O     . TYR A 1  99  ? 26.67044  12.05928  34.24479  1.000 37.95631  ? 129 TYR A O     1 
ATOM   705  C  CB    . TYR A 1  99  ? 29.10618  10.30590  34.38451  1.000 36.83098  ? 129 TYR A CB    1 
ATOM   706  C  CG    . TYR A 1  99  ? 29.82016  9.34682   35.32644  1.000 51.27656  ? 129 TYR A CG    1 
ATOM   707  C  CD1   . TYR A 1  99  ? 29.23727  8.95794   36.52153  1.000 42.73377  ? 129 TYR A CD1   1 
ATOM   708  C  CD2   . TYR A 1  99  ? 31.04903  8.79661   34.99228  1.000 54.30836  ? 129 TYR A CD2   1 
ATOM   709  C  CE1   . TYR A 1  99  ? 29.86524  8.06687   37.37347  1.000 57.95872  ? 129 TYR A CE1   1 
ATOM   710  C  CE2   . TYR A 1  99  ? 31.68701  7.90554   35.83422  1.000 56.41929  ? 129 TYR A CE2   1 
ATOM   711  C  CZ    . TYR A 1  99  ? 31.09611  7.54066   37.02631  1.000 65.48076  ? 129 TYR A CZ    1 
ATOM   712  O  OH    . TYR A 1  99  ? 31.74109  6.65959   37.84025  1.000 56.57209  ? 129 TYR A OH    1 
ATOM   713  N  N     . ASN A 1  100 ? 25.86900  10.58936  32.73995  1.000 29.01332  ? 130 ASN A N     1 
ATOM   714  C  CA    . ASN A 1  100 ? 24.76808  11.44152  32.30607  1.000 27.22265  ? 130 ASN A CA    1 
ATOM   715  C  C     . ASN A 1  100 ? 23.39804  10.88875  32.69628  1.000 29.35649  ? 130 ASN A C     1 
ATOM   716  O  O     . ASN A 1  100 ? 22.37106  11.38990  32.21941  1.000 27.57557  ? 130 ASN A O     1 
ATOM   717  C  CB    . ASN A 1  100 ? 24.83390  11.65847  30.78806  1.000 27.88567  ? 130 ASN A CB    1 
ATOM   718  C  CG    . ASN A 1  100 ? 25.45306  13.00736  30.43993  1.000 33.92317  ? 130 ASN A CG    1 
ATOM   719  O  OD1   . ASN A 1  100 ? 25.48932  13.89238  31.28090  1.000 35.99313  ? 130 ASN A OD1   1 
ATOM   720  N  ND2   . ASN A 1  100 ? 25.92492  13.16625  29.20786  1.000 38.28520  ? 130 ASN A ND2   1 
ATOM   721  N  N     . LEU A 1  101 ? 23.35000  9.86978   33.56431  1.000 29.54207  ? 131 LEU A N     1 
ATOM   722  C  CA    . LEU A 1  101 ? 22.05697  9.32700   33.97251  1.000 26.41401  ? 131 LEU A CA    1 
ATOM   723  C  C     . LEU A 1  101 ? 21.12522  10.37916  34.57161  1.000 24.90143  ? 131 LEU A C     1 
ATOM   724  O  O     . LEU A 1  101 ? 19.90519  10.24335  34.47678  1.000 24.58120  ? 131 LEU A O     1 
ATOM   725  C  CB    . LEU A 1  101 ? 22.28293  8.17499   34.95351  1.000 27.45276  ? 131 LEU A CB    1 
ATOM   726  C  CG    . LEU A 1  101 ? 22.72563  6.92390   34.20349  1.000 24.71673  ? 131 LEU A CG    1 
ATOM   727  C  CD1   . LEU A 1  101 ? 23.03058  5.78388   35.20048  1.000 27.74198  ? 131 LEU A CD1   1 
ATOM   728  C  CD2   . LEU A 1  101 ? 21.66042  6.51604   33.18165  1.000 24.67383  ? 131 LEU A CD2   1 
ATOM   729  N  N     . THR A 1  102 ? 21.65647  11.44210  35.18350  1.000 25.16776  ? 132 THR A N     1 
ATOM   730  C  CA    . THR A 1  102 ? 20.74871  12.45426  35.71660  1.000 25.08355  ? 132 THR A CA    1 
ATOM   731  C  C     . THR A 1  102 ? 19.95866  13.14035  34.59369  1.000 25.45265  ? 132 THR A C     1 
ATOM   732  O  O     . THR A 1  102 ? 18.72569  13.28754  34.68485  1.000 27.54121  ? 132 THR A O     1 
ATOM   733  C  CB    . THR A 1  102 ? 21.51698  13.47316  36.55846  1.000 25.39895  ? 132 THR A CB    1 
ATOM   734  O  OG1   . THR A 1  102 ? 22.01704  12.82312  37.75041  1.000 24.94792  ? 132 THR A OG1   1 
ATOM   735  C  CG2   . THR A 1  102 ? 20.61622  14.65831  36.94755  1.000 25.50801  ? 132 THR A CG2   1 
ATOM   736  N  N     . LEU A 1  103 ? 20.63356  13.48521  33.48858  1.000 26.09318  ? 133 LEU A N     1 
ATOM   737  C  CA    . LEU A 1  103 ? 19.91048  14.01429  32.34067  1.000 26.44619  ? 133 LEU A CA    1 
ATOM   738  C  C     . LEU A 1  103 ? 18.86027  13.02344  31.88384  1.000 28.24261  ? 133 LEU A C     1 
ATOM   739  O  O     . LEU A 1  103 ? 17.72028  13.40261  31.57099  1.000 27.95700  ? 133 LEU A O     1 
ATOM   740  C  CB    . LEU A 1  103 ? 20.87237  14.30910  31.19353  1.000 27.21346  ? 133 LEU A CB    1 
ATOM   741  C  CG    . LEU A 1  103 ? 21.92858  15.37995  31.46635  1.000 33.26286  ? 133 LEU A CG    1 
ATOM   742  C  CD1   . LEU A 1  103 ? 22.73945  15.65378  30.20723  1.000 35.23248  ? 133 LEU A CD1   1 
ATOM   743  C  CD2   . LEU A 1  103 ? 21.25485  16.63307  31.98641  1.000 30.31516  ? 133 LEU A CD2   1 
ATOM   744  N  N     . LYS A 1  104 ? 19.21306  11.73539  31.87283  1.000 25.63427  ? 134 LYS A N     1 
ATOM   745  C  CA    . LYS A 1  104 ? 18.26484  10.75952  31.35299  1.000 25.36934  ? 134 LYS A CA    1 
ATOM   746  C  C     . LYS A 1  104 ? 17.01895  10.74074  32.21816  1.000 27.01456  ? 134 LYS A C     1 
ATOM   747  O  O     . LYS A 1  104 ? 15.88489  10.77490  31.70732  1.000 26.23026  ? 134 LYS A O     1 
ATOM   748  C  CB    . LYS A 1  104 ? 18.90661  9.36942   31.28094  1.000 25.11471  ? 134 LYS A CB    1 
ATOM   749  C  CG    . LYS A 1  104 ? 17.95336  8.33155   30.70310  1.000 24.86027  ? 134 LYS A CG    1 
ATOM   750  C  CD    . LYS A 1  104 ? 18.65011  6.99243   30.41905  1.000 26.98026  ? 134 LYS A CD    1 
ATOM   751  C  CE    . LYS A 1  104 ? 19.56496  7.10125   29.19592  1.000 25.52964  ? 134 LYS A CE    1 
ATOM   752  N  NZ    . LYS A 1  104 ? 19.87667  5.73319   28.63391  1.000 33.23707  ? 134 LYS A NZ    1 
ATOM   753  N  N     . THR A 1  105 ? 17.22213  10.72475  33.54814  1.000 25.90904  ? 135 THR A N     1 
ATOM   754  C  CA    . THR A 1  105 ? 16.07426  10.70795  34.45330  1.000 26.71573  ? 135 THR A CA    1 
ATOM   755  C  C     . THR A 1  105 ? 15.25743  11.97808  34.27337  1.000 24.30355  ? 135 THR A C     1 
ATOM   756  O  O     . THR A 1  105 ? 14.01142  11.93927  34.21054  1.000 24.18663  ? 135 THR A O     1 
ATOM   757  C  CB    . THR A 1  105 ? 16.56643  10.54492  35.90223  1.000 28.95087  ? 135 THR A CB    1 
ATOM   758  O  OG1   . THR A 1  105 ? 16.94124  9.16687   36.11622  1.000 34.05958  ? 135 THR A OG1   1 
ATOM   759  C  CG2   . THR A 1  105 ? 15.50364  10.94112  36.93237  1.000 23.38315  ? 135 THR A CG2   1 
ATOM   760  N  N     . MET A 1  106 ? 15.94059  13.10797  34.13324  1.000 24.78491  ? 136 MET A N     1 
ATOM   761  C  CA    . MET A 1  106 ? 15.17077  14.33709  34.03931  1.000 25.14103  ? 136 MET A CA    1 
ATOM   762  C  C     . MET A 1  106 ? 14.43259  14.38316  32.70942  1.000 25.40439  ? 136 MET A C     1 
ATOM   763  O  O     . MET A 1  106 ? 13.30667  14.89734  32.64256  1.000 27.37535  ? 136 MET A O     1 
ATOM   764  C  CB    . MET A 1  106 ? 16.07699  15.54995  34.24315  1.000 25.68762  ? 136 MET A CB    1 
ATOM   765  C  CG    . MET A 1  106 ? 16.47223  15.78493  35.70709  1.000 29.15166  ? 136 MET A CG    1 
ATOM   766  S  SD    . MET A 1  106 ? 15.06538  15.78318  36.83829  1.000 36.45698  ? 136 MET A SD    1 
ATOM   767  C  CE    . MET A 1  106 ? 13.98646  16.99333  36.03940  1.000 33.21263  ? 136 MET A CE    1 
ATOM   768  N  N     . MET A 1  107 ? 14.98835  13.73804  31.67336  1.000 27.50615  ? 137 MET A N     1 
ATOM   769  C  CA    . MET A 1  107 ? 14.24216  13.63813  30.41846  1.000 26.38252  ? 137 MET A CA    1 
ATOM   770  C  C     . MET A 1  107 ? 12.93907  12.88734  30.64166  1.000 30.12930  ? 137 MET A C     1 
ATOM   771  O  O     . MET A 1  107 ? 11.86309  13.34250  30.23180  1.000 25.44428  ? 137 MET A O     1 
ATOM   772  C  CB    . MET A 1  107 ? 15.09490  12.94696  29.34937  1.000 25.91271  ? 137 MET A CB    1 
ATOM   773  C  CG    . MET A 1  107 ? 14.30666  12.50005  28.09449  1.000 30.01125  ? 137 MET A CG    1 
ATOM   774  S  SD    . MET A 1  107 ? 15.30136  11.66086  26.87037  1.000 44.04615  ? 137 MET A SD    1 
ATOM   775  C  CE    . MET A 1  107 ? 15.62823  10.08783  27.73237  1.000 34.70125  ? 137 MET A CE    1 
ATOM   776  N  N     . GLY A 1  108 ? 13.01099  11.76135  31.35169  1.000 25.11697  ? 138 GLY A N     1 
ATOM   777  C  CA    . GLY A 1  108 ? 11.79891  11.01254  31.58788  1.000 24.43092  ? 138 GLY A CA    1 
ATOM   778  C  C     . GLY A 1  108 ? 10.81315  11.83072  32.37599  1.000 25.31741  ? 138 GLY A C     1 
ATOM   779  O  O     . GLY A 1  108 ? 9.62211   11.88190  32.05015  1.000 26.27921  ? 138 GLY A O     1 
ATOM   780  N  N     . ILE A 1  109 ? 11.30640  12.55267  33.37690  1.000 26.46930  ? 139 ILE A N     1 
ATOM   781  C  CA    . ILE A 1  109 ? 10.38263  13.30784  34.20401  1.000 24.49872  ? 139 ILE A CA    1 
ATOM   782  C  C     . ILE A 1  109 ? 9.78269   14.43291  33.37706  1.000 27.47309  ? 139 ILE A C     1 
ATOM   783  O  O     . ILE A 1  109 ? 8.57475   14.71311  33.44921  1.000 29.90131  ? 139 ILE A O     1 
ATOM   784  C  CB    . ILE A 1  109 ? 11.11588  13.80777  35.46889  1.000 28.37059  ? 139 ILE A CB    1 
ATOM   785  C  CG1   . ILE A 1  109 ? 11.22185  12.66378  36.49891  1.000 24.57220  ? 139 ILE A CG1   1 
ATOM   786  C  CG2   . ILE A 1  109 ? 10.47016  15.06588  36.03894  1.000 30.04531  ? 139 ILE A CG2   1 
ATOM   787  C  CD1   . ILE A 1  109 ? 12.26804  12.90265  37.61276  1.000 33.25064  ? 139 ILE A CD1   1 
ATOM   788  N  N     . GLU A 1  110 ? 10.59966  15.00676  32.48293  1.000 26.20511  ? 140 GLU A N     1 
ATOM   789  C  CA    . GLU A 1  110 ? 10.11071  16.07881  31.62996  1.000 31.63426  ? 140 GLU A CA    1 
ATOM   790  C  C     . GLU A 1  110 ? 9.04050   15.53995  30.70413  1.000 34.67236  ? 140 GLU A C     1 
ATOM   791  O  O     . GLU A 1  110 ? 7.99957   16.17911  30.50125  1.000 33.16654  ? 140 GLU A O     1 
ATOM   792  C  CB    . GLU A 1  110 ? 11.25970  16.67661  30.83079  1.000 33.04020  ? 140 GLU A CB    1 
ATOM   793  C  CG    . GLU A 1  110 ? 10.80873  17.77865  29.85682  1.000 43.60651  ? 140 GLU A CG    1 
ATOM   794  C  CD    . GLU A 1  110 ? 11.93669  18.26345  28.94865  1.000 52.06940  ? 140 GLU A CD    1 
ATOM   795  O  OE1   . GLU A 1  110 ? 13.06162  17.74727  29.07551  1.000 45.17858  ? 140 GLU A OE1   1 
ATOM   796  O  OE2   . GLU A 1  110 ? 11.69171  19.14746  28.10366  1.000 48.05873  ? 140 GLU A OE2   1 
ATOM   797  N  N     . TRP A 1  111 ? 9.25124   14.31991  30.20313  1.000 25.68921  ? 141 TRP A N     1 
ATOM   798  C  CA    . TRP A 1  111 ? 8.27202   13.75203  29.29528  1.000 25.71592  ? 141 TRP A CA    1 
ATOM   799  C  C     . TRP A 1  111 ? 6.94310   13.61626  30.01547  1.000 28.28215  ? 141 TRP A C     1 
ATOM   800  O  O     . TRP A 1  111 ? 5.89610   14.06341  29.50960  1.000 32.68373  ? 141 TRP A O     1 
ATOM   801  C  CB    . TRP A 1  111 ? 8.76373   12.40794  28.73426  1.000 25.42807  ? 141 TRP A CB    1 
ATOM   802  C  CG    . TRP A 1  111 ? 7.74351   11.82207  27.81741  1.000 32.52258  ? 141 TRP A CG    1 
ATOM   803  C  CD1   . TRP A 1  111 ? 7.58037   12.09306  26.48543  1.000 36.77187  ? 141 TRP A CD1   1 
ATOM   804  C  CD2   . TRP A 1  111 ? 6.69142   10.92625  28.18558  1.000 31.64973  ? 141 TRP A CD2   1 
ATOM   805  N  NE1   . TRP A 1  111 ? 6.49620   11.39622  25.99960  1.000 36.50175  ? 141 TRP A NE1   1 
ATOM   806  C  CE2   . TRP A 1  111 ? 5.93322   10.67134  27.02270  1.000 28.96034  ? 141 TRP A CE2   1 
ATOM   807  C  CE3   . TRP A 1  111 ? 6.33549   10.29134  29.38465  1.000 28.65199  ? 141 TRP A CE3   1 
ATOM   808  C  CZ2   . TRP A 1  111 ? 4.82809   9.81651   27.01487  1.000 33.21508  ? 141 TRP A CZ2   1 
ATOM   809  C  CZ3   . TRP A 1  111 ? 5.22936   9.44151   29.37883  1.000 33.83892  ? 141 TRP A CZ3   1 
ATOM   810  C  CH2   . TRP A 1  111 ? 4.48516   9.21560   28.19394  1.000 37.52365  ? 141 TRP A CH2   1 
ATOM   811  N  N     . VAL A 1  112 ? 6.97519   13.08929  31.25048  1.000 27.57688  ? 142 VAL A N     1 
ATOM   812  C  CA    . VAL A 1  112 ? 5.73027   12.93651  31.99066  1.000 31.35553  ? 142 VAL A CA    1 
ATOM   813  C  C     . VAL A 1  112 ? 5.07450   14.29462  32.14371  1.000 30.43617  ? 142 VAL A C     1 
ATOM   814  O  O     . VAL A 1  112 ? 3.87149   14.46880  31.89687  1.000 40.01339  ? 142 VAL A O     1 
ATOM   815  C  CB    . VAL A 1  112 ? 5.97135   12.28551  33.36064  1.000 25.47173  ? 142 VAL A CB    1 
ATOM   816  C  CG1   . VAL A 1  112 ? 4.68447   12.27974  34.18182  1.000 24.78630  ? 142 VAL A CG1   1 
ATOM   817  C  CG2   . VAL A 1  112 ? 6.48810   10.85643  33.19062  1.000 35.71299  ? 142 VAL A CG2   1 
ATOM   818  N  N     . HIS A 1  113 ? 5.87871   15.28850  32.52257  1.000 33.43035  ? 143 HIS A N     1 
ATOM   819  C  CA    . HIS A 1  113 ? 5.31195   16.60760  32.76861  1.000 30.21749  ? 143 HIS A CA    1 
ATOM   820  C  C     . HIS A 1  113 ? 4.67286   17.15366  31.50968  1.000 38.62279  ? 143 HIS A C     1 
ATOM   821  O  O     . HIS A 1  113 ? 3.54495   17.65984  31.54682  1.000 40.37442  ? 143 HIS A O     1 
ATOM   822  C  CB    . HIS A 1  113 ? 6.39517   17.55044  33.26943  1.000 34.08426  ? 143 HIS A CB    1 
ATOM   823  C  CG    . HIS A 1  113 ? 6.03038   18.99550  33.16644  1.000 37.40488  ? 143 HIS A CG    1 
ATOM   824  N  ND1   . HIS A 1  113 ? 5.03558   19.56368  33.93056  1.000 39.29690  ? 143 HIS A ND1   1 
ATOM   825  C  CD2   . HIS A 1  113 ? 6.54844   19.99240  32.41234  1.000 37.25556  ? 143 HIS A CD2   1 
ATOM   826  C  CE1   . HIS A 1  113 ? 4.94574   20.85168  33.63654  1.000 34.30404  ? 143 HIS A CE1   1 
ATOM   827  N  NE2   . HIS A 1  113 ? 5.84866   21.13351  32.71840  1.000 30.25755  ? 143 HIS A NE2   1 
ATOM   828  N  N     . ARG A 1  114 ? 5.34268   16.99953  30.36959  1.000 36.03755  ? 144 ARG A N     1 
ATOM   829  C  CA    . ARG A 1  114 ? 4.87363   17.71057  29.18664  1.000 33.14583  ? 144 ARG A CA    1 
ATOM   830  C  C     . ARG A 1  114 ? 3.81640   16.92471  28.43281  1.000 39.70372  ? 144 ARG A C     1 
ATOM   831  O  O     . ARG A 1  114 ? 2.90641   17.51684  27.84192  1.000 34.72178  ? 144 ARG A O     1 
ATOM   832  C  CB    . ARG A 1  114 ? 6.02954   17.99436  28.23247  1.000 30.14012  ? 144 ARG A CB    1 
ATOM   833  C  CG    . ARG A 1  114 ? 7.04877   19.01021  28.71530  1.000 43.59692  ? 144 ARG A CG    1 
ATOM   834  C  CD    . ARG A 1  114 ? 8.05566   19.27902  27.61315  1.000 47.19010  ? 144 ARG A CD    1 
ATOM   835  N  NE    . ARG A 1  114 ? 9.11786   20.16786  28.06398  1.000 57.84424  ? 144 ARG A NE    1 
ATOM   836  C  CZ    . ARG A 1  114 ? 9.03307   21.48988  28.06895  1.000 63.11498  ? 144 ARG A CZ    1 
ATOM   837  N  NH1   . ARG A 1  114 ? 7.96810   22.11603  27.59608  1.000 66.91780  ? 144 ARG A NH1   1 
ATOM   838  N  NH2   . ARG A 1  114 ? 10.03725  22.20473  28.57079  1.000 58.70393  ? 144 ARG A NH2   1 
ATOM   839  N  N     . PHE A 1  115 ? 3.91520   15.60169  28.43683  1.000 36.11803  ? 145 PHE A N     1 
ATOM   840  C  CA    . PHE A 1  115 ? 3.09195   14.80180  27.56097  1.000 33.75438  ? 145 PHE A CA    1 
ATOM   841  C  C     . PHE A 1  115 ? 2.21789   13.78296  28.27312  1.000 38.25861  ? 145 PHE A C     1 
ATOM   842  O  O     . PHE A 1  115 ? 1.30671   13.24208  27.64126  1.000 47.54791  ? 145 PHE A O     1 
ATOM   843  C  CB    . PHE A 1  115 ? 3.97269   14.08963  26.52587  1.000 33.64663  ? 145 PHE A CB    1 
ATOM   844  C  CG    . PHE A 1  115 ? 4.80973   15.02647  25.71673  1.000 39.22356  ? 145 PHE A CG    1 
ATOM   845  C  CD1   . PHE A 1  115 ? 4.23273   15.84754  24.75178  1.000 52.54135  ? 145 PHE A CD1   1 
ATOM   846  C  CD2   . PHE A 1  115 ? 6.17577   15.11427  25.92653  1.000 39.96842  ? 145 PHE A CD2   1 
ATOM   847  C  CE1   . PHE A 1  115 ? 5.00276   16.72639  24.01565  1.000 40.00804  ? 145 PHE A CE1   1 
ATOM   848  C  CE2   . PHE A 1  115 ? 6.95481   15.98712  25.18040  1.000 40.62409  ? 145 PHE A CE2   1 
ATOM   849  C  CZ    . PHE A 1  115 ? 6.36480   16.79319  24.21946  1.000 36.46465  ? 145 PHE A CZ    1 
ATOM   850  N  N     . CYS A 1  116 ? 2.44302   13.52696  29.55810  1.000 45.01269  ? 146 CYS A N     1 
ATOM   851  C  CA    . CYS A 1  116 ? 1.59096   12.55611  30.22524  1.000 29.94264  ? 146 CYS A CA    1 
ATOM   852  C  C     . CYS A 1  116 ? 1.31623   12.96220  31.66527  1.000 39.99923  ? 146 CYS A C     1 
ATOM   853  O  O     . CYS A 1  116 ? 1.51923   12.16219  32.58726  1.000 42.74491  ? 146 CYS A O     1 
ATOM   854  C  CB    . CYS A 1  116 ? 2.24374   11.18101  30.17719  1.000 34.63242  ? 146 CYS A CB    1 
ATOM   855  S  SG    . CYS A 1  116 ? 1.09355   9.81720   30.38439  1.000 51.15248  ? 146 CYS A SG    1 
ATOM   856  N  N     . PRO A 1  117 ? 0.85145   14.18828  31.90830  1.000 39.24530  ? 147 PRO A N     1 
ATOM   857  C  CA    . PRO A 1  117 ? 0.49570   14.57737  33.27933  1.000 43.33723  ? 147 PRO A CA    1 
ATOM   858  C  C     . PRO A 1  117 ? -0.70434  13.83058  33.81852  1.000 45.91134  ? 147 PRO A C     1 
ATOM   859  O  O     . PRO A 1  117 ? -0.97316  13.89566  35.02456  1.000 42.29709  ? 147 PRO A O     1 
ATOM   860  C  CB    . PRO A 1  117 ? 0.20292   16.07642  33.14133  1.000 44.02003  ? 147 PRO A CB    1 
ATOM   861  C  CG    . PRO A 1  117 ? -0.32825  16.19246  31.75940  1.000 40.39952  ? 147 PRO A CG    1 
ATOM   862  C  CD    . PRO A 1  117 ? 0.51448   15.24630  30.93431  1.000 38.57038  ? 147 PRO A CD    1 
ATOM   863  N  N     . GLN A 1  118 ? -1.40158  13.08866  32.96264  1.000 49.12701  ? 148 GLN A N     1 
ATOM   864  C  CA    . GLN A 1  118 ? -2.54964  12.29486  33.38982  1.000 46.23097  ? 148 GLN A CA    1 
ATOM   865  C  C     . GLN A 1  118 ? -2.14975  11.00281  34.10380  1.000 50.52776  ? 148 GLN A C     1 
ATOM   866  O  O     . GLN A 1  118 ? -2.98775  10.39797  34.78494  1.000 47.15146  ? 148 GLN A O     1 
ATOM   867  C  CB    . GLN A 1  118 ? -3.42186  11.96896  32.17295  1.000 53.07287  ? 148 GLN A CB    1 
ATOM   868  C  CG    . GLN A 1  118 ? -3.99477  13.19303  31.45300  1.000 54.73820  ? 148 GLN A CG    1 
ATOM   869  C  CD    . GLN A 1  118 ? -3.03681  13.82885  30.45584  1.000 57.87041  ? 148 GLN A CD    1 
ATOM   870  O  OE1   . GLN A 1  118 ? -1.91491  13.35366  30.25170  1.000 60.24541  ? 148 GLN A OE1   1 
ATOM   871  N  NE2   . GLN A 1  118 ? -3.48272  14.90890  29.81787  1.000 56.02454  ? 148 GLN A NE2   1 
ATOM   872  N  N     . ALA A 1  119 ? -0.89483  10.57161  33.97864  1.000 46.80724  ? 149 ALA A N     1 
ATOM   873  C  CA    . ALA A 1  119 ? -0.46594  9.32056   34.60962  1.000 34.62716  ? 149 ALA A CA    1 
ATOM   874  C  C     . ALA A 1  119 ? -0.73273  9.34565   36.10366  1.000 28.76192  ? 149 ALA A C     1 
ATOM   875  O  O     . ALA A 1  119 ? -0.33949  10.28061  36.80758  1.000 29.75855  ? 149 ALA A O     1 
ATOM   876  C  CB    . ALA A 1  119 ? 1.02499   9.08232   34.34942  1.000 39.39568  ? 149 ALA A CB    1 
ATOM   877  N  N     . ALA A 1  120 ? -1.39882  8.30577   36.61278  1.000 29.97189  ? 150 ALA A N     1 
ATOM   878  C  CA    . ALA A 1  120 ? -1.58764  8.23484   38.06081  1.000 25.90658  ? 150 ALA A CA    1 
ATOM   879  C  C     . ALA A 1  120 ? -0.25958  7.98965   38.76663  1.000 31.08845  ? 150 ALA A C     1 
ATOM   880  O  O     . ALA A 1  120 ? 0.05167   8.63963   39.77757  1.000 30.16140  ? 150 ALA A O     1 
ATOM   881  C  CB    . ALA A 1  120 ? -2.57876  7.14101   38.42998  1.000 25.81620  ? 150 ALA A CB    1 
ATOM   882  N  N     . PHE A 1  121 ? 0.51920   7.07651   38.21855  1.000 28.88210  ? 151 PHE A N     1 
ATOM   883  C  CA    . PHE A 1  121 ? 1.79024   6.71233   38.86938  1.000 28.60949  ? 151 PHE A CA    1 
ATOM   884  C  C     . PHE A 1  121 ? 2.83006   6.50314   37.80025  1.000 24.41963  ? 151 PHE A C     1 
ATOM   885  O  O     . PHE A 1  121 ? 2.51284   6.14515   36.66230  1.000 26.01301  ? 151 PHE A O     1 
ATOM   886  C  CB    . PHE A 1  121 ? 1.59816   5.47239   39.74545  1.000 23.91075  ? 151 PHE A CB    1 
ATOM   887  C  CG    . PHE A 1  121 ? 0.70336   5.65456   40.95957  1.000 31.26161  ? 151 PHE A CG    1 
ATOM   888  C  CD1   . PHE A 1  121 ? 1.17861   6.26952   42.10948  1.000 29.67393  ? 151 PHE A CD1   1 
ATOM   889  C  CD2   . PHE A 1  121 ? -0.61071  5.20277   40.94376  1.000 32.64779  ? 151 PHE A CD2   1 
ATOM   890  C  CE1   . PHE A 1  121 ? 0.35879   6.42868   43.21059  1.000 30.53820  ? 151 PHE A CE1   1 
ATOM   891  C  CE2   . PHE A 1  121 ? -1.42454  5.36793   42.04787  1.000 26.11291  ? 151 PHE A CE2   1 
ATOM   892  C  CZ    . PHE A 1  121 ? -0.93728  5.97589   43.17678  1.000 33.13710  ? 151 PHE A CZ    1 
ATOM   893  N  N     . VAL A 1  122 ? 4.07115   6.73495   38.18307  1.000 25.69832  ? 152 VAL A N     1 
ATOM   894  C  CA    . VAL A 1  122 ? 5.19499   6.56575   37.22992  1.000 26.85946  ? 152 VAL A CA    1 
ATOM   895  C  C     . VAL A 1  122 ? 6.30497   5.80059   37.95279  1.000 22.80494  ? 152 VAL A C     1 
ATOM   896  O  O     . VAL A 1  122 ? 6.65018   6.17157   39.07573  1.000 26.28524  ? 152 VAL A O     1 
ATOM   897  C  CB    . VAL A 1  122 ? 5.72012   7.89365   36.64981  1.000 29.63121  ? 152 VAL A CB    1 
ATOM   898  C  CG1   . VAL A 1  122 ? 6.80294   7.66845   35.60866  1.000 25.64961  ? 152 VAL A CG1   1 
ATOM   899  C  CG2   . VAL A 1  122 ? 4.60918   8.77181   36.09494  1.000 25.10106  ? 152 VAL A CG2   1 
ATOM   900  N  N     . MET A 1  123 ? 6.80971   4.75750   37.31175  1.000 25.94159  ? 153 MET A N     1 
ATOM   901  C  CA    . MET A 1  123 ? 7.95568   4.02433   37.89161  1.000 28.63773  ? 153 MET A CA    1 
ATOM   902  C  C     . MET A 1  123 ? 9.19459   4.21811   37.01443  1.000 22.39194  ? 153 MET A C     1 
ATOM   903  O  O     . MET A 1  123 ? 9.11438   3.93809   35.81745  1.000 28.24263  ? 153 MET A O     1 
ATOM   904  C  CB    . MET A 1  123 ? 7.67246   2.52638   38.03769  1.000 22.41845  ? 153 MET A CB    1 
ATOM   905  C  CG    . MET A 1  123 ? 8.87840   1.72621   38.49055  1.000 26.50007  ? 153 MET A CG    1 
ATOM   906  S  SD    . MET A 1  123 ? 8.49820   0.02728   38.95665  1.000 32.90809  ? 153 MET A SD    1 
ATOM   907  C  CE    . MET A 1  123 ? 9.54337   -0.15384  40.40451  1.000 30.03138  ? 153 MET A CE    1 
ATOM   908  N  N     . LYS A 1  124 ? 10.26575  4.73896   37.59827  1.000 22.20247  ? 154 LYS A N     1 
ATOM   909  C  CA    . LYS A 1  124 ? 11.54866  4.81574   36.87009  1.000 22.26152  ? 154 LYS A CA    1 
ATOM   910  C  C     . LYS A 1  124 ? 12.32451  3.54363   37.23302  1.000 22.08904  ? 154 LYS A C     1 
ATOM   911  O  O     . LYS A 1  124 ? 12.56064  3.31262   38.41900  1.000 25.32773  ? 154 LYS A O     1 
ATOM   912  C  CB    . LYS A 1  124 ? 12.34691  6.07762   37.20894  1.000 22.27998  ? 154 LYS A CB    1 
ATOM   913  C  CG    . LYS A 1  124 ? 13.73784  6.16939   36.59375  1.000 31.92931  ? 154 LYS A CG    1 
ATOM   914  C  CD    . LYS A 1  124 ? 14.88489  5.72923   37.49760  1.000 25.92517  ? 154 LYS A CD    1 
ATOM   915  C  CE    . LYS A 1  124 ? 16.20683  5.91100   36.83642  1.000 43.73838  ? 154 LYS A CE    1 
ATOM   916  N  NZ    . LYS A 1  124 ? 17.23573  4.94985   37.23730  1.000 40.36019  ? 154 LYS A NZ    1 
ATOM   917  N  N     . THR A 1  125 ? 12.71425  2.77254   36.23399  1.000 22.55372  ? 155 THR A N     1 
ATOM   918  C  CA    . THR A 1  125 ? 13.36709  1.49344   36.54094  1.000 28.77160  ? 155 THR A CA    1 
ATOM   919  C  C     . THR A 1  125 ? 14.58794  1.28622   35.69277  1.000 23.25975  ? 155 THR A C     1 
ATOM   920  O  O     . THR A 1  125 ? 14.77192  1.98417   34.69273  1.000 22.69297  ? 155 THR A O     1 
ATOM   921  C  CB    . THR A 1  125 ? 12.39189  0.31559   36.40711  1.000 24.58848  ? 155 THR A CB    1 
ATOM   922  O  OG1   . THR A 1  125 ? 13.10377  -0.82851  36.86404  1.000 30.07917  ? 155 THR A OG1   1 
ATOM   923  C  CG2   . THR A 1  125 ? 11.91166  0.11763   34.98418  1.000 27.73562  ? 155 THR A CG2   1 
ATOM   924  N  N     . ASP A 1  126 ? 15.37685  0.31311   36.10369  1.000 25.47336  ? 156 ASP A N     1 
ATOM   925  C  CA    . ASP A 1  126 ? 16.58469  -0.04910  35.34554  1.000 22.72684  ? 156 ASP A CA    1 
ATOM   926  C  C     . ASP A 1  126 ? 16.27537  -1.23108  34.42561  1.000 26.23159  ? 156 ASP A C     1 
ATOM   927  O  O     . ASP A 1  126 ? 15.14030  -1.72190  34.45479  1.000 23.45115  ? 156 ASP A O     1 
ATOM   928  C  CB    . ASP A 1  126 ? 17.72480  -0.19725  36.32838  1.000 34.91576  ? 156 ASP A CB    1 
ATOM   929  C  CG    . ASP A 1  126 ? 18.22108  1.12669   36.89228  1.000 43.79886  ? 156 ASP A CG    1 
ATOM   930  O  OD1   . ASP A 1  126 ? 17.87517  2.17473   36.31829  1.000 45.81305  ? 156 ASP A OD1   1 
ATOM   931  O  OD2   . ASP A 1  126 ? 18.95822  1.09960   37.89118  1.000 36.50404  ? 156 ASP A OD2   1 
ATOM   932  N  N     . SER A 1  127 ? 17.25720  -1.65426  33.63649  1.000 26.13034  ? 157 SER A N     1 
ATOM   933  C  CA    . SER A 1  127 ? 17.03789  -2.70925  32.61855  1.000 23.83517  ? 157 SER A CA    1 
ATOM   934  C  C     . SER A 1  127 ? 17.31375  -4.11228  33.18556  1.000 31.63246  ? 157 SER A C     1 
ATOM   935  O  O     . SER A 1  127 ? 16.73752  -5.07520  32.66066  1.000 30.97612  ? 157 SER A O     1 
ATOM   936  C  CB    . SER A 1  127 ? 17.88378  -2.38942  31.42343  1.000 24.28744  ? 157 SER A CB    1 
ATOM   937  O  OG    . SER A 1  127 ? 19.19689  -2.01561  31.80623  1.000 38.15409  ? 157 SER A OG    1 
ATOM   938  N  N     . ASP A 1  128 ? 18.14687  -4.21338  34.21344  1.000 23.74133  ? 158 ASP A N     1 
ATOM   939  C  CA    . ASP A 1  128 ? 18.51975  -5.51542  34.82743  1.000 29.69333  ? 158 ASP A CA    1 
ATOM   940  C  C     . ASP A 1  128 ? 17.55888  -5.74623  35.98957  1.000 23.74819  ? 158 ASP A C     1 
ATOM   941  O  O     . ASP A 1  128 ? 17.99701  -5.88327  37.13851  1.000 23.21047  ? 158 ASP A O     1 
ATOM   942  C  CB    . ASP A 1  128 ? 19.99679  -5.56764  35.15323  1.000 24.00574  ? 158 ASP A CB    1 
ATOM   943  C  CG    . ASP A 1  128 ? 20.49709  -4.51169  36.11613  1.000 39.45184  ? 158 ASP A CG    1 
ATOM   944  O  OD1   . ASP A 1  128 ? 19.89527  -3.42260  36.14618  1.000 23.28705  ? 158 ASP A OD1   1 
ATOM   945  O  OD2   . ASP A 1  128 ? 21.47314  -4.81183  36.82600  1.000 45.69020  ? 158 ASP A OD2   1 
ATOM   946  N  N     . MET A 1  129 ? 16.28182  -5.79304  35.65575  1.000 23.46858  ? 159 MET A N     1 
ATOM   947  C  CA    . MET A 1  129 ? 15.29596  -5.85886  36.74388  1.000 23.15272  ? 159 MET A CA    1 
ATOM   948  C  C     . MET A 1  129 ? 14.06279  -6.68767  36.44308  1.000 25.31399  ? 159 MET A C     1 
ATOM   949  O  O     . MET A 1  129 ? 13.69261  -6.81165  35.27313  1.000 27.22230  ? 159 MET A O     1 
ATOM   950  C  CB    . MET A 1  129 ? 14.77123  -4.45276  37.05992  1.000 22.75595  ? 159 MET A CB    1 
ATOM   951  C  CG    . MET A 1  129 ? 15.80545  -3.44791  37.50374  1.000 22.77469  ? 159 MET A CG    1 
ATOM   952  S  SD    . MET A 1  129 ? 16.02471  -3.36790  39.28971  1.000 27.04572  ? 159 MET A SD    1 
ATOM   953  C  CE    . MET A 1  129 ? 14.38075  -3.69262  39.93195  1.000 21.94617  ? 159 MET A CE    1 
ATOM   954  N  N     . PHE A 1  130 ? 13.55183  -7.34856  37.46617  1.000 24.04475  ? 160 PHE A N     1 
ATOM   955  C  CA    . PHE A 1  130 ? 12.22473  -7.95135  37.41837  1.000 24.69090  ? 160 PHE A CA    1 
ATOM   956  C  C     . PHE A 1  130 ? 11.25497  -7.02518  38.13548  1.000 23.57887  ? 160 PHE A C     1 
ATOM   957  O  O     . PHE A 1  130 ? 11.52319  -6.60219  39.26143  1.000 26.91149  ? 160 PHE A O     1 
ATOM   958  C  CB    . PHE A 1  130 ? 12.20561  -9.32233  38.10141  1.000 23.97167  ? 160 PHE A CB    1 
ATOM   959  C  CG    . PHE A 1  130 ? 10.78357  -9.82910  38.39462  1.000 24.26107  ? 160 PHE A CG    1 
ATOM   960  C  CD1   . PHE A 1  130 ? 10.07733  -10.48801 37.43774  1.000 24.81470  ? 160 PHE A CD1   1 
ATOM   961  C  CD2   . PHE A 1  130 ? 10.21177  -9.63297  39.63670  1.000 27.97907  ? 160 PHE A CD2   1 
ATOM   962  C  CE1   . PHE A 1  130 ? 8.76329   -10.95080 37.68794  1.000 27.69105  ? 160 PHE A CE1   1 
ATOM   963  C  CE2   . PHE A 1  130 ? 8.93474   -10.09676 39.91689  1.000 26.57352  ? 160 PHE A CE2   1 
ATOM   964  C  CZ    . PHE A 1  130 ? 8.20549   -10.75768 38.91701  1.000 24.99591  ? 160 PHE A CZ    1 
ATOM   965  N  N     . ILE A 1  131 ? 10.11493  -6.73402  37.50063  1.000 23.50966  ? 161 ILE A N     1 
ATOM   966  C  CA    A ILE A 1  131 ? 9.07614   -5.88084  38.07474  0.770 24.33871  ? 161 ILE A CA    1 
ATOM   967  C  CA    B ILE A 1  131 ? 9.08415   -5.89284  38.09574  0.230 23.32392  ? 161 ILE A CA    1 
ATOM   968  C  C     . ILE A 1  131 ? 7.77602   -6.67063  38.09895  1.000 23.80905  ? 161 ILE A C     1 
ATOM   969  O  O     . ILE A 1  131 ? 7.38879   -7.25060  37.07902  1.000 28.57618  ? 161 ILE A O     1 
ATOM   970  C  CB    A ILE A 1  131 ? 8.86524   -4.58383  37.26774  0.770 28.19243  ? 161 ILE A CB    1 
ATOM   971  C  CB    B ILE A 1  131 ? 8.92325   -4.55684  37.34373  0.230 26.51758  ? 161 ILE A CB    1 
ATOM   972  C  CG1   A ILE A 1  131 ? 10.16235  -3.78204  37.15253  0.770 26.45284  ? 161 ILE A CG1   1 
ATOM   973  C  CG1   B ILE A 1  131 ? 10.21040  -3.72903  37.46853  0.230 26.83615  ? 161 ILE A CG1   1 
ATOM   974  C  CG2   A ILE A 1  131 ? 7.76546   -3.72964  37.92586  0.770 23.09254  ? 161 ILE A CG2   1 
ATOM   975  C  CG2   B ILE A 1  131 ? 7.73445   -3.76963  37.90587  0.230 25.32970  ? 161 ILE A CG2   1 
ATOM   976  C  CD1   A ILE A 1  131 ? 10.76559  -3.41109  38.49544  0.770 26.69656  ? 161 ILE A CD1   1 
ATOM   977  C  CD1   B ILE A 1  131 ? 10.22749  -2.45606  36.64949  0.230 26.22120  ? 161 ILE A CD1   1 
ATOM   978  N  N     . ASN A 1  132 ? 7.11518   -6.69450  39.24704  1.000 23.75959  ? 162 ASN A N     1 
ATOM   979  C  CA    . ASN A 1  132 ? 5.82809   -7.38329  39.37224  1.000 24.28829  ? 162 ASN A CA    1 
ATOM   980  C  C     . ASN A 1  132 ? 4.77526   -6.27812  39.33635  1.000 24.26744  ? 162 ASN A C     1 
ATOM   981  O  O     . ASN A 1  132 ? 4.41549   -5.70104  40.35738  1.000 24.09413  ? 162 ASN A O     1 
ATOM   982  C  CB    . ASN A 1  132 ? 5.73213   -8.20624  40.64427  1.000 24.41565  ? 162 ASN A CB    1 
ATOM   983  C  CG    . ASN A 1  132 ? 4.44101   -9.01303  40.69048  1.000 25.11395  ? 162 ASN A CG    1 
ATOM   984  O  OD1   . ASN A 1  132 ? 3.47598   -8.64990  40.03060  1.000 30.32817  ? 162 ASN A OD1   1 
ATOM   985  N  ND2   . ASN A 1  132 ? 4.42295   -10.10401 41.46151  1.000 30.38787  ? 162 ASN A ND2   1 
ATOM   986  N  N     . VAL A 1  133 ? 4.32014   -5.97309  38.12840  1.000 29.43705  ? 163 VAL A N     1 
ATOM   987  C  CA    . VAL A 1  133 ? 3.38228   -4.87895  37.95050  1.000 29.79395  ? 163 VAL A CA    1 
ATOM   988  C  C     . VAL A 1  133 ? 2.04232   -5.20272  38.59270  1.000 30.14990  ? 163 VAL A C     1 
ATOM   989  O  O     . VAL A 1  133 ? 1.34753   -4.30859  39.08377  1.000 33.83287  ? 163 VAL A O     1 
ATOM   990  C  CB    . VAL A 1  133 ? 3.23913   -4.57597  36.45551  1.000 30.66487  ? 163 VAL A CB    1 
ATOM   991  C  CG1   . VAL A 1  133 ? 2.04824   -3.63179  36.21765  1.000 41.01140  ? 163 VAL A CG1   1 
ATOM   992  C  CG2   . VAL A 1  133 ? 4.55414   -3.98419  35.89931  1.000 24.22062  ? 163 VAL A CG2   1 
ATOM   993  N  N     . ASP A 1  134 ? 1.64812   -6.48265  38.60279  1.000 27.22330  ? 164 ASP A N     1 
ATOM   994  C  CA    . ASP A 1  134 ? 0.36515   -6.85843  39.20298  1.000 31.22278  ? 164 ASP A CA    1 
ATOM   995  C  C     . ASP A 1  134 ? 0.34240   -6.53639  40.68897  1.000 35.03553  ? 164 ASP A C     1 
ATOM   996  O  O     . ASP A 1  134 ? -0.59943  -5.90122  41.19908  1.000 37.49908  ? 164 ASP A O     1 
ATOM   997  C  CB    . ASP A 1  134 ? 0.09788   -8.35640  38.96706  1.000 36.98005  ? 164 ASP A CB    1 
ATOM   998  C  CG    . ASP A 1  134 ? 0.16861   -8.73445  37.49106  1.000 53.34722  ? 164 ASP A CG    1 
ATOM   999  O  OD1   . ASP A 1  134 ? 1.27450   -9.06364  37.00691  1.000 51.82728  ? 164 ASP A OD1   1 
ATOM   1000 O  OD2   . ASP A 1  134 ? -0.87947  -8.69531  36.80920  1.000 51.30547  ? 164 ASP A OD2   1 
ATOM   1001 N  N     . TYR A 1  135 ? 1.40244   -6.92853  41.39984  1.000 25.49343  ? 165 TYR A N     1 
ATOM   1002 C  CA    . TYR A 1  135 ? 1.45867   -6.68850  42.83382  1.000 31.74169  ? 165 TYR A CA    1 
ATOM   1003 C  C     . TYR A 1  135 ? 1.65795   -5.20852  43.12175  1.000 31.09301  ? 165 TYR A C     1 
ATOM   1004 O  O     . TYR A 1  135 ? 1.10316   -4.68841  44.09081  1.000 34.72071  ? 165 TYR A O     1 
ATOM   1005 C  CB    . TYR A 1  135 ? 2.58663   -7.50766  43.46869  1.000 34.07410  ? 165 TYR A CB    1 
ATOM   1006 C  CG    . TYR A 1  135 ? 2.53683   -7.57361  44.98170  1.000 24.95766  ? 165 TYR A CG    1 
ATOM   1007 C  CD1   . TYR A 1  135 ? 1.40885   -8.04841  45.63187  1.000 25.59697  ? 165 TYR A CD1   1 
ATOM   1008 C  CD2   . TYR A 1  135 ? 3.60300   -7.18975  45.74154  1.000 24.33248  ? 165 TYR A CD2   1 
ATOM   1009 C  CE1   . TYR A 1  135 ? 1.35702   -8.12336  47.00188  1.000 31.26216  ? 165 TYR A CE1   1 
ATOM   1010 C  CE2   . TYR A 1  135 ? 3.57118   -7.25871  47.12955  1.000 24.28037  ? 165 TYR A CE2   1 
ATOM   1011 C  CZ    . TYR A 1  135 ? 2.44019   -7.73151  47.75672  1.000 34.57743  ? 165 TYR A CZ    1 
ATOM   1012 O  OH    . TYR A 1  135 ? 2.40037   -7.79846  49.13372  1.000 41.83132  ? 165 TYR A OH    1 
ATOM   1013 N  N     . LEU A 1  136 ? 2.48894   -4.52568  42.31362  1.000 27.19380  ? 166 LEU A N     1 
ATOM   1014 C  CA    . LEU A 1  136 ? 2.65119   -3.07770  42.48155  1.000 29.44468  ? 166 LEU A CA    1 
ATOM   1015 C  C     . LEU A 1  136 ? 1.31229   -2.35949  42.34771  1.000 34.21521  ? 166 LEU A C     1 
ATOM   1016 O  O     . LEU A 1  136 ? 0.98554   -1.47042  43.13673  1.000 30.63042  ? 166 LEU A O     1 
ATOM   1017 C  CB    . LEU A 1  136 ? 3.61014   -2.51988  41.43640  1.000 27.82673  ? 166 LEU A CB    1 
ATOM   1018 C  CG    . LEU A 1  136 ? 3.75538   -0.97490  41.43834  1.000 30.52382  ? 166 LEU A CG    1 
ATOM   1019 C  CD1   . LEU A 1  136 ? 4.18365   -0.44293  42.78326  1.000 23.70508  ? 166 LEU A CD1   1 
ATOM   1020 C  CD2   . LEU A 1  136 ? 4.75830   -0.59109  40.37819  1.000 24.47394  ? 166 LEU A CD2   1 
ATOM   1021 N  N     . THR A 1  137 ? 0.56609   -2.68240  41.30283  1.000 26.70477  ? 167 THR A N     1 
ATOM   1022 C  CA    . THR A 1  137 ? -0.74284  -2.06420  41.09199  1.000 32.66548  ? 167 THR A CA    1 
ATOM   1023 C  C     . THR A 1  137 ? -1.66071  -2.30803  42.28312  1.000 42.12888  ? 167 THR A C     1 
ATOM   1024 O  O     . THR A 1  137 ? -2.33750  -1.38590  42.76519  1.000 38.76197  ? 167 THR A O     1 
ATOM   1025 C  CB    . THR A 1  137 ? -1.35410  -2.60515  39.80109  1.000 28.69756  ? 167 THR A CB    1 
ATOM   1026 O  OG1   . THR A 1  137 ? -0.59618  -2.13130  38.68297  1.000 35.43260  ? 167 THR A OG1   1 
ATOM   1027 C  CG2   . THR A 1  137 ? -2.82405  -2.16192  39.65228  1.000 32.53235  ? 167 THR A CG2   1 
ATOM   1028 N  N     . GLU A 1  138 ? -1.71684  -3.55900  42.75617  1.000 36.92801  ? 168 GLU A N     1 
ATOM   1029 C  CA    . GLU A 1  138 ? -2.51673  -3.86884  43.94129  1.000 34.21343  ? 168 GLU A CA    1 
ATOM   1030 C  C     . GLU A 1  138 ? -2.11543  -3.00987  45.14121  1.000 35.17249  ? 168 GLU A C     1 
ATOM   1031 O  O     . GLU A 1  138 ? -2.97224  -2.43772  45.83531  1.000 46.36280  ? 168 GLU A O     1 
ATOM   1032 C  CB    . GLU A 1  138 ? -2.40292  -5.36785  44.25732  1.000 31.44932  ? 168 GLU A CB    1 
ATOM   1033 C  CG    . GLU A 1  138 ? -2.75179  -5.75375  45.67237  1.000 42.64915  ? 168 GLU A CG    1 
ATOM   1034 C  CD    . GLU A 1  138 ? -2.61099  -7.25077  45.91140  1.000 58.76202  ? 168 GLU A CD    1 
ATOM   1035 O  OE1   . GLU A 1  138 ? -2.52324  -7.99581  44.91041  1.000 55.00868  ? 168 GLU A OE1   1 
ATOM   1036 O  OE2   . GLU A 1  138 ? -2.58089  -7.67574  47.08441  1.000 58.87393  ? 168 GLU A OE2   1 
ATOM   1037 N  N     . LEU A 1  139 ? -0.80337  -2.87507  45.39002  1.000 35.45349  ? 169 LEU A N     1 
ATOM   1038 C  CA    . LEU A 1  139 ? -0.36109  -2.09011  46.53894  1.000 41.31583  ? 169 LEU A CA    1 
ATOM   1039 C  C     . LEU A 1  139 ? -0.65988  -0.60206  46.35494  1.000 42.21653  ? 169 LEU A C     1 
ATOM   1040 O  O     . LEU A 1  139 ? -1.04164  0.08202   47.30897  1.000 44.17798  ? 169 LEU A O     1 
ATOM   1041 C  CB    . LEU A 1  139 ? 1.13891   -2.31133  46.78874  1.000 36.29970  ? 169 LEU A CB    1 
ATOM   1042 C  CG    . LEU A 1  139 ? 1.52275   -3.73038  47.25873  1.000 39.77030  ? 169 LEU A CG    1 
ATOM   1043 C  CD1   . LEU A 1  139 ? 3.05477   -3.84361  47.52152  1.000 29.40525  ? 169 LEU A CD1   1 
ATOM   1044 C  CD2   . LEU A 1  139 ? 0.75587   -4.08422  48.50384  1.000 37.95687  ? 169 LEU A CD2   1 
ATOM   1045 N  N     . LEU A 1  140 ? -0.49597  -0.08713  45.13590  1.000 37.53393  ? 170 LEU A N     1 
ATOM   1046 C  CA    . LEU A 1  140 ? -0.78778  1.32691   44.88290  1.000 43.11194  ? 170 LEU A CA    1 
ATOM   1047 C  C     . LEU A 1  140 ? -2.27671  1.61615   45.05209  1.000 46.00247  ? 170 LEU A C     1 
ATOM   1048 O  O     . LEU A 1  140 ? -2.65947  2.62223   45.65912  1.000 53.07182  ? 170 LEU A O     1 
ATOM   1049 C  CB    . LEU A 1  140 ? -0.33391  1.71180   43.47782  1.000 33.78454  ? 170 LEU A CB    1 
ATOM   1050 C  CG    . LEU A 1  140 ? 1.17705   1.73956   43.20861  1.000 28.70826  ? 170 LEU A CG    1 
ATOM   1051 C  CD1   . LEU A 1  140 ? 1.40987   1.87448   41.71558  1.000 23.83365  ? 170 LEU A CD1   1 
ATOM   1052 C  CD2   . LEU A 1  140 ? 1.84934   2.89147   43.97849  1.000 23.84036  ? 170 LEU A CD2   1 
ATOM   1053 N  N     . LEU A 1  141 ? -3.12893  0.74127   44.50524  1.000 47.19370  ? 171 LEU A N     1 
ATOM   1054 C  CA    . LEU A 1  141 ? -4.57088  0.89550   44.66943  1.000 40.69993  ? 171 LEU A CA    1 
ATOM   1055 C  C     . LEU A 1  141 ? -4.96268  0.83661   46.13749  1.000 41.95668  ? 171 LEU A C     1 
ATOM   1056 O  O     . LEU A 1  141 ? -5.96053  1.44278   46.54261  1.000 56.65642  ? 171 LEU A O     1 
ATOM   1057 C  CB    . LEU A 1  141 ? -5.30516  -0.17841  43.86157  1.000 39.87781  ? 171 LEU A CB    1 
ATOM   1058 C  CG    . LEU A 1  141 ? -5.26433  0.06354   42.35355  1.000 46.67980  ? 171 LEU A CG    1 
ATOM   1059 C  CD1   . LEU A 1  141 ? -5.80962  -1.13339  41.58266  1.000 38.91163  ? 171 LEU A CD1   1 
ATOM   1060 C  CD2   . LEU A 1  141 ? -6.04618  1.33566   41.99562  1.000 38.29947  ? 171 LEU A CD2   1 
ATOM   1061 N  N     . LYS A 1  142 ? -4.18068  0.12651   46.94840  1.000 41.87684  ? 172 LYS A N     1 
ATOM   1062 C  CA    . LYS A 1  142 ? -4.44950  0.05359   48.37544  1.000 48.30192  ? 172 LYS A CA    1 
ATOM   1063 C  C     . LYS A 1  142 ? -3.86221  1.21052   49.18333  1.000 58.12180  ? 172 LYS A C     1 
ATOM   1064 O  O     . LYS A 1  142 ? -4.28701  1.43162   50.32638  1.000 63.72932  ? 172 LYS A O     1 
ATOM   1065 C  CB    . LYS A 1  142 ? -3.89163  -1.26148  48.92840  1.000 61.21277  ? 172 LYS A CB    1 
ATOM   1066 C  CG    . LYS A 1  142 ? -4.01545  -1.40242  50.42242  1.000 67.38715  ? 172 LYS A CG    1 
ATOM   1067 C  CD    . LYS A 1  142 ? -2.90451  -2.27558  50.97529  1.000 65.56945  ? 172 LYS A CD    1 
ATOM   1068 C  CE    . LYS A 1  142 ? -2.70082  -3.51363  50.10930  1.000 81.13709  ? 172 LYS A CE    1 
ATOM   1069 N  NZ    . LYS A 1  142 ? -2.06989  -4.63371  50.87725  1.000 84.79415  ? 172 LYS A NZ    1 
ATOM   1070 N  N     . LYS A 1  143 ? -2.89217  1.94135   48.63917  1.000 65.72370  ? 173 LYS A N     1 
ATOM   1071 C  CA    . LYS A 1  143 ? -2.19890  2.92827   49.46105  1.000 69.51307  ? 173 LYS A CA    1 
ATOM   1072 C  C     . LYS A 1  143 ? -3.04567  4.17441   49.71213  1.000 59.26145  ? 173 LYS A C     1 
ATOM   1073 O  O     . LYS A 1  143 ? -2.81342  4.86740   50.70907  1.000 62.37750  ? 173 LYS A O     1 
ATOM   1074 C  CB    . LYS A 1  143 ? -0.86293  3.29604   48.79685  1.000 61.72575  ? 173 LYS A CB    1 
ATOM   1075 C  CG    . LYS A 1  143 ? 0.12930   3.98091   49.69569  1.000 47.21027  ? 173 LYS A CG    1 
ATOM   1076 C  CD    . LYS A 1  143 ? 0.74729   3.03084   50.68464  1.000 39.06382  ? 173 LYS A CD    1 
ATOM   1077 C  CE    . LYS A 1  143 ? 1.92249   3.68568   51.39645  1.000 42.62187  ? 173 LYS A CE    1 
ATOM   1078 N  NZ    . LYS A 1  143 ? 2.21956   2.99767   52.67743  1.000 38.33743  ? 173 LYS A NZ    1 
ATOM   1079 N  N     . ASN A 1  144 ? -4.03874  4.44854   48.85826  1.000 57.54067  ? 174 ASN A N     1 
ATOM   1080 C  CA    . ASN A 1  144 ? -4.85354  5.66467   48.93633  1.000 76.55242  ? 174 ASN A CA    1 
ATOM   1081 C  C     . ASN A 1  144 ? -3.97734  6.91553   48.95718  1.000 76.34493  ? 174 ASN A C     1 
ATOM   1082 O  O     . ASN A 1  144 ? -4.26109  7.87960   49.66819  1.000 92.11334  ? 174 ASN A O     1 
ATOM   1083 C  CB    . ASN A 1  144 ? -5.78237  5.66785   50.15746  1.000 76.30279  ? 174 ASN A CB    1 
ATOM   1084 C  CG    . ASN A 1  144 ? -6.60955  4.40999   50.28161  1.000 81.14729  ? 174 ASN A CG    1 
ATOM   1085 O  OD1   . ASN A 1  144 ? -7.05478  3.83503   49.28969  1.000 79.54842  ? 174 ASN A OD1   1 
ATOM   1086 N  ND2   . ASN A 1  144 ? -6.81845  3.97906   51.51665  1.000 81.60466  ? 174 ASN A ND2   1 
ATOM   1087 N  N     . ARG A 1  145 ? -2.90245  6.90434   48.16703  1.000 76.84038  ? 175 ARG A N     1 
ATOM   1088 C  CA    . ARG A 1  145 ? -1.99328  8.05120   48.04887  1.000 62.37367  ? 175 ARG A CA    1 
ATOM   1089 C  C     . ARG A 1  145 ? -1.89843  8.41314   46.57084  1.000 57.24720  ? 175 ARG A C     1 
ATOM   1090 O  O     . ARG A 1  145 ? -1.22465  7.71701   45.80677  1.000 69.15495  ? 175 ARG A O     1 
ATOM   1091 C  CB    . ARG A 1  145 ? -0.61825  7.73700   48.63269  1.000 53.86046  ? 175 ARG A CB    1 
ATOM   1092 C  CG    . ARG A 1  145 ? -0.60411  7.36304   50.12070  1.000 58.32228  ? 175 ARG A CG    1 
ATOM   1093 C  CD    . ARG A 1  145 ? -0.63579  8.60107   51.02666  1.000 54.48586  ? 175 ARG A CD    1 
ATOM   1094 N  NE    . ARG A 1  145 ? 0.56532   9.41287   50.86248  1.000 64.09122  ? 175 ARG A NE    1 
ATOM   1095 C  CZ    . ARG A 1  145 ? 0.64738   10.47884  50.07743  1.000 59.47768  ? 175 ARG A CZ    1 
ATOM   1096 N  NH1   . ARG A 1  145 ? -0.41164  10.95099  49.44257  1.000 51.44835  ? 175 ARG A NH1   1 
ATOM   1097 N  NH2   . ARG A 1  145 ? 1.82345   11.08865  49.92925  1.000 61.23151  ? 175 ARG A NH2   1 
ATOM   1098 N  N     . THR A 1  146 ? -2.56732  9.50323   46.17291  1.000 54.50598  ? 176 THR A N     1 
ATOM   1099 C  CA    . THR A 1  146 ? -2.62844  9.92620   44.77790  1.000 44.30328  ? 176 THR A CA    1 
ATOM   1100 C  C     . THR A 1  146 ? -1.80029  11.17206  44.45675  1.000 49.66094  ? 176 THR A C     1 
ATOM   1101 O  O     . THR A 1  146 ? -1.66940  11.51901  43.27472  1.000 40.51810  ? 176 THR A O     1 
ATOM   1102 C  CB    . THR A 1  146 ? -4.08745  10.20142  44.38110  1.000 49.52589  ? 176 THR A CB    1 
ATOM   1103 O  OG1   . THR A 1  146 ? -4.19063  10.31439  42.95711  1.000 67.28732  ? 176 THR A OG1   1 
ATOM   1104 C  CG2   . THR A 1  146 ? -4.56816  11.50151  44.99812  1.000 43.39438  ? 176 THR A CG2   1 
ATOM   1105 N  N     . THR A 1  147 ? -1.27104  11.87401  45.45666  1.000 42.03752  ? 177 THR A N     1 
ATOM   1106 C  CA    . THR A 1  147 ? -0.51988  13.09888  45.22252  1.000 38.01051  ? 177 THR A CA    1 
ATOM   1107 C  C     . THR A 1  147 ? 0.70425   13.15671  46.12635  1.000 37.37467  ? 177 THR A C     1 
ATOM   1108 O  O     . THR A 1  147 ? 0.68733   12.64675  47.24736  1.000 35.79536  ? 177 THR A O     1 
ATOM   1109 C  CB    . THR A 1  147 ? -1.36364  14.37402  45.47860  1.000 43.31139  ? 177 THR A CB    1 
ATOM   1110 O  OG1   . THR A 1  147 ? -1.84346  14.33914  46.82766  1.000 48.80460  ? 177 THR A OG1   1 
ATOM   1111 C  CG2   . THR A 1  147 ? -2.53577  14.44518  44.51276  1.000 41.78664  ? 177 THR A CG2   1 
ATOM   1112 N  N     . ARG A 1  148 ? 1.75429   13.81754  45.63518  1.000 40.42082  ? 178 ARG A N     1 
ATOM   1113 C  CA    . ARG A 1  148 ? 2.99942   14.00336  46.39501  1.000 40.12390  ? 178 ARG A CA    1 
ATOM   1114 C  C     . ARG A 1  148 ? 3.45431   12.69531  47.04198  1.000 31.49332  ? 178 ARG A C     1 
ATOM   1115 O  O     . ARG A 1  148 ? 3.84246   12.64728  48.21593  1.000 27.14312  ? 178 ARG A O     1 
ATOM   1116 C  CB    . ARG A 1  148 ? 2.82374   15.10842  47.43800  1.000 34.09302  ? 178 ARG A CB    1 
ATOM   1117 C  CG    . ARG A 1  148 ? 2.47586   16.44846  46.79601  1.000 35.36294  ? 178 ARG A CG    1 
ATOM   1118 C  CD    . ARG A 1  148 ? 2.13017   17.50754  47.83402  1.000 29.49868  ? 178 ARG A CD    1 
ATOM   1119 N  NE    . ARG A 1  148 ? 3.19134   17.72140  48.81687  1.000 43.29738  ? 178 ARG A NE    1 
ATOM   1120 C  CZ    . ARG A 1  148 ? 4.24744   18.50523  48.63470  1.000 45.75663  ? 178 ARG A CZ    1 
ATOM   1121 N  NH1   . ARG A 1  148 ? 4.47937   19.09316  47.47265  1.000 37.53006  ? 178 ARG A NH1   1 
ATOM   1122 N  NH2   . ARG A 1  148 ? 5.09761   18.69813  49.64258  1.000 43.09514  ? 178 ARG A NH2   1 
ATOM   1123 N  N     . PHE A 1  149 ? 3.39303   11.61330  46.26502  1.000 36.84409  ? 179 PHE A N     1 
ATOM   1124 C  CA    . PHE A 1  149 ? 3.71988   10.26626  46.73201  1.000 34.56919  ? 179 PHE A CA    1 
ATOM   1125 C  C     . PHE A 1  149 ? 5.00872   9.79104   46.07485  1.000 25.16679  ? 179 PHE A C     1 
ATOM   1126 O  O     . PHE A 1  149 ? 5.15957   9.93498   44.86083  1.000 27.11834  ? 179 PHE A O     1 
ATOM   1127 C  CB    . PHE A 1  149 ? 2.58368   9.29543   46.39420  1.000 31.68682  ? 179 PHE A CB    1 
ATOM   1128 C  CG    . PHE A 1  149 ? 2.86051   7.87539   46.76620  1.000 32.87151  ? 179 PHE A CG    1 
ATOM   1129 C  CD1   . PHE A 1  149 ? 2.95863   7.50142   48.09220  1.000 36.41526  ? 179 PHE A CD1   1 
ATOM   1130 C  CD2   . PHE A 1  149 ? 3.03722   6.91634   45.78121  1.000 27.24517  ? 179 PHE A CD2   1 
ATOM   1131 C  CE1   . PHE A 1  149 ? 3.20548   6.18439   48.44220  1.000 35.75867  ? 179 PHE A CE1   1 
ATOM   1132 C  CE2   . PHE A 1  149 ? 3.27906   5.59431   46.11821  1.000 35.34655  ? 179 PHE A CE2   1 
ATOM   1133 C  CZ    . PHE A 1  149 ? 3.37019   5.22933   47.45521  1.000 40.18676  ? 179 PHE A CZ    1 
ATOM   1134 N  N     . PHE A 1  150 ? 5.92274   9.22391   46.87674  1.000 24.26527  ? 180 PHE A N     1 
ATOM   1135 C  CA    . PHE A 1  150 ? 7.20259   8.74970   46.34458  1.000 26.94233  ? 180 PHE A CA    1 
ATOM   1136 C  C     . PHE A 1  150 ? 7.66252   7.57565   47.18055  1.000 29.70660  ? 180 PHE A C     1 
ATOM   1137 O  O     . PHE A 1  150 ? 7.76771   7.68467   48.41053  1.000 23.00574  ? 180 PHE A O     1 
ATOM   1138 C  CB    . PHE A 1  150 ? 8.26177   9.86853   46.35440  1.000 22.05117  ? 180 PHE A CB    1 
ATOM   1139 C  CG    . PHE A 1  150 ? 9.44960   9.61132   45.44324  1.000 21.89844  ? 180 PHE A CG    1 
ATOM   1140 C  CD1   . PHE A 1  150 ? 10.50253  8.79116   45.84212  1.000 21.45909  ? 180 PHE A CD1   1 
ATOM   1141 C  CD2   . PHE A 1  150 ? 9.51353   10.22827  44.20022  1.000 25.31898  ? 180 PHE A CD2   1 
ATOM   1142 C  CE1   . PHE A 1  150 ? 11.60938  8.57597   45.00697  1.000 23.91491  ? 180 PHE A CE1   1 
ATOM   1143 C  CE2   . PHE A 1  150 ? 10.60638  10.01407  43.34607  1.000 22.97488  ? 180 PHE A CE2   1 
ATOM   1144 C  CZ    . PHE A 1  150 ? 11.65730  9.20392   43.75295  1.000 26.29540  ? 180 PHE A CZ    1 
ATOM   1145 N  N     . THR A 1  151 ? 7.95225   6.45259   46.52254  1.000 23.77610  ? 181 THR A N     1 
ATOM   1146 C  CA    . THR A 1  151 ? 8.31817   5.26955   47.27953  1.000 26.74749  ? 181 THR A CA    1 
ATOM   1147 C  C     . THR A 1  151 ? 9.35294   4.44736   46.51641  1.000 22.70105  ? 181 THR A C     1 
ATOM   1148 O  O     . THR A 1  151 ? 9.70082   4.73628   45.37335  1.000 27.91857  ? 181 THR A O     1 
ATOM   1149 C  CB    . THR A 1  151 ? 7.07108   4.41076   47.59572  1.000 24.96148  ? 181 THR A CB    1 
ATOM   1150 O  OG1   . THR A 1  151 ? 7.43504   3.36672   48.51870  1.000 34.20338  ? 181 THR A OG1   1 
ATOM   1151 C  CG2   . THR A 1  151 ? 6.50881   3.81481   46.34182  1.000 21.72264  ? 181 THR A CG2   1 
ATOM   1152 N  N     . GLY A 1  152 ? 9.84086   3.41431   47.16437  1.000 27.15894  ? 182 GLY A N     1 
ATOM   1153 C  CA    . GLY A 1  152 ? 10.86165  2.56013   46.56425  1.000 20.65606  ? 182 GLY A CA    1 
ATOM   1154 C  C     . GLY A 1  152 ? 11.63369  1.87904   47.67417  1.000 24.35532  ? 182 GLY A C     1 
ATOM   1155 O  O     . GLY A 1  152 ? 11.07779  1.57116   48.72425  1.000 28.66663  ? 182 GLY A O     1 
ATOM   1156 N  N     . PHE A 1  153 ? 12.92762  1.63283   47.42299  1.000 23.34213  ? 183 PHE A N     1 
ATOM   1157 C  CA    . PHE A 1  153 ? 13.81670  1.19472   48.48788  1.000 20.94833  ? 183 PHE A CA    1 
ATOM   1158 C  C     . PHE A 1  153 ? 14.36899  2.45565   49.14177  1.000 28.53228  ? 183 PHE A C     1 
ATOM   1159 O  O     . PHE A 1  153 ? 15.17601  3.15851   48.53864  1.000 26.23353  ? 183 PHE A O     1 
ATOM   1160 C  CB    . PHE A 1  153 ? 14.96749  0.31752   47.96675  1.000 19.96585  ? 183 PHE A CB    1 
ATOM   1161 C  CG    . PHE A 1  153 ? 15.87757  -0.14359  49.06964  1.000 19.74328  ? 183 PHE A CG    1 
ATOM   1162 C  CD1   . PHE A 1  153 ? 15.53350  -1.23551  49.84972  1.000 22.13384  ? 183 PHE A CD1   1 
ATOM   1163 C  CD2   . PHE A 1  153 ? 17.05471  0.52223   49.33546  1.000 26.60256  ? 183 PHE A CD2   1 
ATOM   1164 C  CE1   . PHE A 1  153 ? 16.36458  -1.66361  50.88662  1.000 25.98041  ? 183 PHE A CE1   1 
ATOM   1165 C  CE2   . PHE A 1  153 ? 17.89479  0.11213   50.36835  1.000 20.22574  ? 183 PHE A CE2   1 
ATOM   1166 C  CZ    . PHE A 1  153 ? 17.55172  -0.99179  51.14243  1.000 23.82834  ? 183 PHE A CZ    1 
ATOM   1167 N  N     . LEU A 1  154 ? 13.92920  2.75576   50.35782  1.000 25.45731  ? 184 LEU A N     1 
ATOM   1168 C  CA    . LEU A 1  154 ? 14.32249  4.01271   50.99973  1.000 31.67577  ? 184 LEU A CA    1 
ATOM   1169 C  C     . LEU A 1  154 ? 15.75555  3.94850   51.50254  1.000 24.22406  ? 184 LEU A C     1 
ATOM   1170 O  O     . LEU A 1  154 ? 16.15648  2.96646   52.13351  1.000 30.33751  ? 184 LEU A O     1 
ATOM   1171 C  CB    . LEU A 1  154 ? 13.39170  4.34889   52.16485  1.000 24.28453  ? 184 LEU A CB    1 
ATOM   1172 C  CG    . LEU A 1  154 ? 12.08776  5.05309   51.79601  1.000 36.34279  ? 184 LEU A CG    1 
ATOM   1173 C  CD1   . LEU A 1  154 ? 11.25450  4.13719   50.91515  1.000 28.95391  ? 184 LEU A CD1   1 
ATOM   1174 C  CD2   . LEU A 1  154 ? 11.33301  5.49624   53.05810  1.000 38.91838  ? 184 LEU A CD2   1 
ATOM   1175 N  N     . LYS A 1  155 ? 16.52367  4.99437   51.20540  1.000 24.93699  ? 185 LYS A N     1 
ATOM   1176 C  CA    . LYS A 1  155 ? 17.93575  5.13416   51.65720  1.000 30.29783  ? 185 LYS A CA    1 
ATOM   1177 C  C     . LYS A 1  155 ? 17.93807  6.43619   52.46716  1.000 40.03318  ? 185 LYS A C     1 
ATOM   1178 O  O     . LYS A 1  155 ? 17.98316  7.51216   51.86612  1.000 38.25278  ? 185 LYS A O     1 
ATOM   1179 C  CB    . LYS A 1  155 ? 18.88558  5.05898   50.46107  1.000 23.61171  ? 185 LYS A CB    1 
ATOM   1180 C  CG    . LYS A 1  155 ? 18.74326  3.82598   49.58813  1.000 29.22221  ? 185 LYS A CG    1 
ATOM   1181 C  CD    . LYS A 1  155 ? 19.43510  3.94783   48.23703  1.000 28.06700  ? 185 LYS A CD    1 
ATOM   1182 C  CE    . LYS A 1  155 ? 20.92309  3.85060   48.33783  1.000 31.83154  ? 185 LYS A CE    1 
ATOM   1183 N  NZ    . LYS A 1  155 ? 21.34901  2.65155   49.06680  1.000 33.58665  ? 185 LYS A NZ    1 
ATOM   1184 N  N     . LEU A 1  156 ? 17.94024  6.33022   53.78417  1.000 34.37916  ? 186 LEU A N     1 
ATOM   1185 C  CA    . LEU A 1  156 ? 17.69654  7.49129   54.63017  1.000 39.37712  ? 186 LEU A CA    1 
ATOM   1186 C  C     . LEU A 1  156 ? 18.92572  7.99111   55.36198  1.000 45.83371  ? 186 LEU A C     1 
ATOM   1187 O  O     . LEU A 1  156 ? 18.90696  9.12413   55.85695  1.000 53.03174  ? 186 LEU A O     1 
ATOM   1188 C  CB    . LEU A 1  156 ? 16.61463  7.17349   55.66832  1.000 31.35630  ? 186 LEU A CB    1 
ATOM   1189 C  CG    . LEU A 1  156 ? 15.30247  6.70068   55.06952  1.000 38.87375  ? 186 LEU A CG    1 
ATOM   1190 C  CD1   . LEU A 1  156 ? 14.29858  6.41387   56.17467  1.000 33.49292  ? 186 LEU A CD1   1 
ATOM   1191 C  CD2   . LEU A 1  156 ? 14.75649  7.71473   54.07056  1.000 27.08822  ? 186 LEU A CD2   1 
ATOM   1192 N  N     . ASN A 1  157 ? 19.96061  7.18596   55.51386  1.000 44.39930  ? 187 ASN A N     1 
ATOM   1193 C  CA    . ASN A 1  157 ? 21.17279  7.75978   56.14768  1.000 55.48416  ? 187 ASN A CA    1 
ATOM   1194 C  C     . ASN A 1  157 ? 22.34360  7.38157   55.24653  1.000 56.78698  ? 187 ASN A C     1 
ATOM   1195 O  O     . ASN A 1  157 ? 23.07950  6.44647   55.58545  1.000 73.73611  ? 187 ASN A O     1 
ATOM   1196 C  CB    . ASN A 1  157 ? 21.24993  7.36681   57.61868  1.000 76.55457  ? 187 ASN A CB    1 
ATOM   1197 C  CG    . ASN A 1  157 ? 22.57307  7.72662   58.24948  1.000 94.48217  ? 187 ASN A CG    1 
ATOM   1198 O  OD1   . ASN A 1  157 ? 23.05623  8.84954   58.08639  1.000 92.99295  ? 187 ASN A OD1   1 
ATOM   1199 N  ND2   . ASN A 1  157 ? 23.17603  6.78855   58.96743  1.000 84.04459  ? 187 ASN A ND2   1 
ATOM   1200 N  N     . GLU A 1  158 ? 22.47055  8.05852   54.11349  1.000 46.27860  ? 188 GLU A N     1 
ATOM   1201 C  CA    . GLU A 1  158 ? 23.50136  7.65933   53.12936  1.000 31.60367  ? 188 GLU A CA    1 
ATOM   1202 C  C     . GLU A 1  158 ? 24.63752  8.68215   53.14117  1.000 35.74588  ? 188 GLU A C     1 
ATOM   1203 O  O     . GLU A 1  158 ? 24.38372  9.88319   53.26517  1.000 35.45102  ? 188 GLU A O     1 
ATOM   1204 C  CB    . GLU A 1  158 ? 22.88013  7.44339   51.74745  1.000 33.30630  ? 188 GLU A CB    1 
ATOM   1205 C  CG    . GLU A 1  158 ? 21.91694  6.26454   51.67662  1.000 46.50806  ? 188 GLU A CG    1 
ATOM   1206 C  CD    . GLU A 1  158 ? 22.61773  4.92143   51.71856  1.000 43.22895  ? 188 GLU A CD    1 
ATOM   1207 O  OE1   . GLU A 1  158 ? 23.76265  4.85823   51.24540  1.000 42.70578  ? 188 GLU A OE1   1 
ATOM   1208 O  OE2   . GLU A 1  158 ? 22.02565  3.95454   52.22667  1.000 59.84060  ? 188 GLU A OE2   1 
ATOM   1209 N  N     . PHE A 1  159 ? 25.85743  8.17996   53.06602  1.000 29.97020  ? 189 PHE A N     1 
ATOM   1210 C  CA    . PHE A 1  159 ? 27.04557  9.05277   53.09383  1.000 32.25186  ? 189 PHE A CA    1 
ATOM   1211 C  C     . PHE A 1  159 ? 27.67137  9.01163   51.72074  1.000 28.36255  ? 189 PHE A C     1 
ATOM   1212 O  O     . PHE A 1  159 ? 27.75812  7.95260   51.10576  1.000 23.33404  ? 189 PHE A O     1 
ATOM   1213 C  CB    . PHE A 1  159 ? 27.94265  8.56666   54.23372  1.000 28.38139  ? 189 PHE A CB    1 
ATOM   1214 C  CG    . PHE A 1  159 ? 27.33286  8.70680   55.61780  1.000 46.20300  ? 189 PHE A CG    1 
ATOM   1215 C  CD1   . PHE A 1  159 ? 27.48915  9.87780   56.34974  1.000 47.30029  ? 189 PHE A CD1   1 
ATOM   1216 C  CD2   . PHE A 1  159 ? 26.59678  7.67493   56.18193  1.000 46.03180  ? 189 PHE A CD2   1 
ATOM   1217 C  CE1   . PHE A 1  159 ? 26.92634  10.00392  57.60882  1.000 53.36910  ? 189 PHE A CE1   1 
ATOM   1218 C  CE2   . PHE A 1  159 ? 26.03398  7.81206   57.43900  1.000 46.29012  ? 189 PHE A CE2   1 
ATOM   1219 C  CZ    . PHE A 1  159 ? 26.20026  8.97505   58.14695  1.000 51.67239  ? 189 PHE A CZ    1 
ATOM   1220 N  N     . PRO A 1  160 ? 28.06548  10.17155  51.18065  1.000 26.69967  ? 190 PRO A N     1 
ATOM   1221 C  CA    . PRO A 1  160 ? 28.75531  10.23541  49.87156  1.000 26.17927  ? 190 PRO A CA    1 
ATOM   1222 C  C     . PRO A 1  160 ? 29.96616  9.29322   49.85742  1.000 29.66544  ? 190 PRO A C     1 
ATOM   1223 O  O     . PRO A 1  160 ? 30.71529  9.23013   50.84932  1.000 26.98093  ? 190 PRO A O     1 
ATOM   1224 C  CB    . PRO A 1  160 ? 29.00453  11.72936  49.72248  1.000 23.32368  ? 190 PRO A CB    1 
ATOM   1225 C  CG    . PRO A 1  160 ? 28.95181  12.29541  51.11747  1.000 27.12877  ? 190 PRO A CG    1 
ATOM   1226 C  CD    . PRO A 1  160 ? 27.83677  11.53861  51.73165  1.000 23.88324  ? 190 PRO A CD    1 
ATOM   1227 N  N     . ILE A 1  161 ? 30.11589  8.53916   48.77342  1.000 28.36787  ? 191 ILE A N     1 
ATOM   1228 C  CA    . ILE A 1  161 ? 31.28173  7.62997   48.62028  1.000 23.52096  ? 191 ILE A CA    1 
ATOM   1229 C  C     . ILE A 1  161 ? 32.48480  8.45777   48.16309  1.000 26.04641  ? 191 ILE A C     1 
ATOM   1230 O  O     . ILE A 1  161 ? 32.43574  9.05475   47.08208  1.000 26.46333  ? 191 ILE A O     1 
ATOM   1231 C  CB    . ILE A 1  161 ? 30.96841  6.46099   47.67336  1.000 36.26926  ? 191 ILE A CB    1 
ATOM   1232 C  CG1   . ILE A 1  161 ? 29.92335  5.52118   48.27453  1.000 22.39127  ? 191 ILE A CG1   1 
ATOM   1233 C  CG2   . ILE A 1  161 ? 32.24924  5.72478   47.28321  1.000 23.68672  ? 191 ILE A CG2   1 
ATOM   1234 C  CD1   . ILE A 1  161 ? 29.27506  4.58825   47.27065  1.000 33.60349  ? 191 ILE A CD1   1 
ATOM   1235 N  N     . ARG A 1  162 ? 33.50392  8.48563   49.00095  1.000 25.25188  ? 192 ARG A N     1 
ATOM   1236 C  CA    . ARG A 1  162 ? 34.70500  9.24844   48.71776  1.000 34.48624  ? 192 ARG A CA    1 
ATOM   1237 C  C     . ARG A 1  162 ? 35.87880  8.35924   48.31063  1.000 39.09011  ? 192 ARG A C     1 
ATOM   1238 O  O     . ARG A 1  162 ? 37.00687  8.84306   48.25146  1.000 28.69796  ? 192 ARG A O     1 
ATOM   1239 C  CB    . ARG A 1  162 ? 35.08930  10.09741  49.93969  1.000 34.52119  ? 192 ARG A CB    1 
ATOM   1240 C  CG    . ARG A 1  162 ? 33.92451  10.87161  50.55483  1.000 31.77732  ? 192 ARG A CG    1 
ATOM   1241 C  CD    . ARG A 1  162 ? 33.36553  11.87967  49.55987  1.000 31.40037  ? 192 ARG A CD    1 
ATOM   1242 N  NE    . ARG A 1  162 ? 32.55578  12.86782  50.26396  1.000 39.47726  ? 192 ARG A NE    1 
ATOM   1243 C  CZ    . ARG A 1  162 ? 31.93386  13.88890  49.68601  1.000 25.85265  ? 192 ARG A CZ    1 
ATOM   1244 N  NH1   . ARG A 1  162 ? 31.94771  14.05086  48.38001  1.000 27.03963  ? 192 ARG A NH1   1 
ATOM   1245 N  NH2   . ARG A 1  162 ? 31.29610  14.77002  50.44507  1.000 25.26008  ? 192 ARG A NH2   1 
ATOM   1246 N  N     . GLN A 1  163 ? 35.61655  7.11327   47.90670  1.000 39.79461  ? 193 GLN A N     1 
ATOM   1247 C  CA    . GLN A 1  163 ? 36.68533  6.22409   47.36458  1.000 38.40209  ? 193 GLN A CA    1 
ATOM   1248 C  C     . GLN A 1  163 ? 36.91119  6.61101   45.89754  1.000 37.90765  ? 193 GLN A C     1 
ATOM   1249 O  O     . GLN A 1  163 ? 36.00804  6.36813   45.08567  1.000 40.22448  ? 193 GLN A O     1 
ATOM   1250 C  CB    . GLN A 1  163 ? 36.35013  4.75114   47.56067  1.000 40.62727  ? 193 GLN A CB    1 
ATOM   1251 C  CG    . GLN A 1  163 ? 37.21816  4.05204   48.59657  1.000 71.94680  ? 193 GLN A CG    1 
ATOM   1252 C  CD    . GLN A 1  163 ? 37.51289  2.61098   48.24157  1.000 88.92083  ? 193 GLN A CD    1 
ATOM   1253 O  OE1   . GLN A 1  163 ? 36.64970  1.88210   47.73971  1.000 92.50179  ? 193 GLN A OE1   1 
ATOM   1254 N  NE2   . GLN A 1  163 ? 38.73985  2.18480   48.49441  1.000 85.96511  ? 193 GLN A NE2   1 
ATOM   1255 N  N     . PRO A 1  164 ? 38.09022  7.13281   45.51936  1.000 33.84152  ? 194 PRO A N     1 
ATOM   1256 C  CA    . PRO A 1  164 ? 38.35812  7.70373   44.15330  1.000 34.80006  ? 194 PRO A CA    1 
ATOM   1257 C  C     . PRO A 1  164 ? 38.02782  6.81175   42.95838  1.000 39.73381  ? 194 PRO A C     1 
ATOM   1258 O  O     . PRO A 1  164 ? 37.66676  7.37877   41.90941  1.000 39.24628  ? 194 PRO A O     1 
ATOM   1259 C  CB    . PRO A 1  164 ? 39.83519  8.08150   44.21809  1.000 30.01713  ? 194 PRO A CB    1 
ATOM   1260 C  CG    . PRO A 1  164 ? 40.39222  7.26144   45.35604  1.000 43.52344  ? 194 PRO A CG    1 
ATOM   1261 C  CD    . PRO A 1  164 ? 39.31136  7.23664   46.37119  1.000 44.15858  ? 194 PRO A CD    1 
ATOM   1262 N  N     . PHE A 1  165 ? 38.11763  5.49674   43.07740  1.000 32.39764  ? 195 PHE A N     1 
ATOM   1263 C  CA    . PHE A 1  165 ? 37.91433  4.65473   41.87245  1.000 32.71703  ? 195 PHE A CA    1 
ATOM   1264 C  C     . PHE A 1  165 ? 36.56821  3.91194   41.89666  1.000 32.77073  ? 195 PHE A C     1 
ATOM   1265 O  O     . PHE A 1  165 ? 36.35596  3.09995   40.99472  1.000 41.09638  ? 195 PHE A O     1 
ATOM   1266 C  CB    . PHE A 1  165 ? 39.19618  3.82553   41.77630  1.000 33.33324  ? 195 PHE A CB    1 
ATOM   1267 C  CG    . PHE A 1  165 ? 40.44633  4.69033   41.84610  1.000 36.21319  ? 195 PHE A CG    1 
ATOM   1268 C  CD1   . PHE A 1  165 ? 40.81731  5.48624   40.77303  1.000 31.51755  ? 195 PHE A CD1   1 
ATOM   1269 C  CD2   . PHE A 1  165 ? 41.22550  4.72924   42.99500  1.000 35.75968  ? 195 PHE A CD2   1 
ATOM   1270 C  CE1   . PHE A 1  165 ? 41.94644  6.28407   40.84185  1.000 41.48053  ? 195 PHE A CE1   1 
ATOM   1271 C  CE2   . PHE A 1  165 ? 42.35163  5.53007   43.05682  1.000 36.31013  ? 195 PHE A CE2   1 
ATOM   1272 C  CZ    . PHE A 1  165 ? 42.70860  6.30498   41.97974  1.000 37.46480  ? 195 PHE A CZ    1 
ATOM   1273 N  N     . SER A 1  166 ? 35.68739  4.20911   42.85478  1.000 32.50356  ? 196 SER A N     1 
ATOM   1274 C  CA    . SER A 1  166 ? 34.33730  3.59633   42.90898  1.000 30.34821  ? 196 SER A CA    1 
ATOM   1275 C  C     . SER A 1  166 ? 33.43225  4.20344   41.83409  1.000 34.00954  ? 196 SER A C     1 
ATOM   1276 O  O     . SER A 1  166 ? 33.63639  5.37439   41.49802  1.000 38.02305  ? 196 SER A O     1 
ATOM   1277 C  CB    . SER A 1  166 ? 33.73052  3.75546   44.27406  1.000 31.61088  ? 196 SER A CB    1 
ATOM   1278 O  OG    . SER A 1  166 ? 32.41744  3.21867   44.34426  1.000 44.21276  ? 196 SER A OG    1 
ATOM   1279 N  N     . LYS A 1  167 ? 32.47406  3.43257   41.33024  1.000 32.36626  ? 197 LYS A N     1 
ATOM   1280 C  CA    . LYS A 1  167 ? 31.52100  3.92169   40.30136  1.000 39.83485  ? 197 LYS A CA    1 
ATOM   1281 C  C     . LYS A 1  167 ? 30.68126  5.07884   40.86144  1.000 36.29471  ? 197 LYS A C     1 
ATOM   1282 O  O     . LYS A 1  167 ? 30.32729  5.96787   40.08546  1.000 40.82947  ? 197 LYS A O     1 
ATOM   1283 C  CB    . LYS A 1  167 ? 30.66975  2.72081   39.88051  1.000 37.82724  ? 197 LYS A CB    1 
ATOM   1284 C  CG    . LYS A 1  167 ? 29.68563  2.93694   38.74364  1.000 56.03021  ? 197 LYS A CG    1 
ATOM   1285 C  CD    . LYS A 1  167 ? 28.40352  2.13414   38.92684  1.000 57.07878  ? 197 LYS A CD    1 
ATOM   1286 C  CE    . LYS A 1  167 ? 28.39022  0.85112   38.16588  1.000 55.55379  ? 197 LYS A CE    1 
ATOM   1287 N  NZ    . LYS A 1  167 ? 27.49306  0.89223   37.01000  1.000 49.21449  ? 197 LYS A NZ    1 
ATOM   1288 N  N     . TRP A 1  168 ? 30.41543  5.06692   42.16348  1.000 31.56438  ? 198 TRP A N     1 
ATOM   1289 C  CA    . TRP A 1  168 ? 29.56468  6.09807   42.78757  1.000 31.97836  ? 198 TRP A CA    1 
ATOM   1290 C  C     . TRP A 1  168 ? 30.40495  7.12496   43.54342  1.000 31.60482  ? 198 TRP A C     1 
ATOM   1291 O  O     . TRP A 1  168 ? 29.87017  7.80007   44.41047  1.000 26.89719  ? 198 TRP A O     1 
ATOM   1292 C  CB    . TRP A 1  168 ? 28.56770  5.38426   43.70172  1.000 47.08673  ? 198 TRP A CB    1 
ATOM   1293 C  CG    . TRP A 1  168 ? 27.70344  4.39237   42.97287  1.000 56.16477  ? 198 TRP A CG    1 
ATOM   1294 C  CD1   . TRP A 1  168 ? 27.13829  4.54343   41.74095  1.000 47.39456  ? 198 TRP A CD1   1 
ATOM   1295 C  CD2   . TRP A 1  168 ? 27.31130  3.08545   43.43997  1.000 61.28991  ? 198 TRP A CD2   1 
ATOM   1296 N  NE1   . TRP A 1  168 ? 26.41907  3.42453   41.41208  1.000 44.23927  ? 198 TRP A NE1   1 
ATOM   1297 C  CE2   . TRP A 1  168 ? 26.50807  2.51654   42.43209  1.000 63.01869  ? 198 TRP A CE2   1 
ATOM   1298 C  CE3   . TRP A 1  168 ? 27.55834  2.34944   44.60495  1.000 64.96093  ? 198 TRP A CE3   1 
ATOM   1299 C  CZ2   . TRP A 1  168 ? 25.95089  1.24564   42.55821  1.000 69.74938  ? 198 TRP A CZ2   1 
ATOM   1300 C  CZ3   . TRP A 1  168 ? 27.00916  1.09353   44.72706  1.000 77.05315  ? 198 TRP A CZ3   1 
ATOM   1301 C  CH2   . TRP A 1  168 ? 26.21294  0.55363   43.71619  1.000 73.52021  ? 198 TRP A CH2   1 
ATOM   1302 N  N     . PHE A 1  169 ? 31.67892  7.25875   43.17824  1.000 25.95383  ? 199 PHE A N     1 
ATOM   1303 C  CA    . PHE A 1  169 ? 32.55616  8.27063   43.80709  1.000 25.62435  ? 199 PHE A CA    1 
ATOM   1304 C  C     . PHE A 1  169 ? 32.14234  9.70169   43.44911  1.000 25.95660  ? 199 PHE A C     1 
ATOM   1305 O  O     . PHE A 1  169 ? 31.94322  9.99268   42.27312  1.000 26.37354  ? 199 PHE A O     1 
ATOM   1306 C  CB    . PHE A 1  169 ? 34.02808  8.08439   43.43389  1.000 26.48003  ? 199 PHE A CB    1 
ATOM   1307 C  CG    . PHE A 1  169 ? 34.88833  9.27927   43.81774  1.000 29.17095  ? 199 PHE A CG    1 
ATOM   1308 C  CD1   . PHE A 1  169 ? 35.19755  9.53226   45.14569  1.000 33.02549  ? 199 PHE A CD1   1 
ATOM   1309 C  CD2   . PHE A 1  169 ? 35.35133  10.16316  42.85365  1.000 28.07816  ? 199 PHE A CD2   1 
ATOM   1310 C  CE1   . PHE A 1  169 ? 35.96577  10.62914  45.49655  1.000 27.99608  ? 199 PHE A CE1   1 
ATOM   1311 C  CE2   . PHE A 1  169 ? 36.11655  11.25905  43.21151  1.000 28.78336  ? 199 PHE A CE2   1 
ATOM   1312 C  CZ    . PHE A 1  169 ? 36.42277  11.48804  44.52846  1.000 28.53544  ? 199 PHE A CZ    1 
ATOM   1313 N  N     . VAL A 1  170 ? 31.97661  10.54874  44.46510  1.000 31.23330  ? 200 VAL A N     1 
ATOM   1314 C  CA    . VAL A 1  170 ? 31.74581  11.97577  44.25109  1.000 30.94873  ? 200 VAL A CA    1 
ATOM   1315 C  C     . VAL A 1  170 ? 32.78304  12.75163  45.04193  1.000 26.79643  ? 200 VAL A C     1 
ATOM   1316 O  O     . VAL A 1  170 ? 32.95117  12.52264  46.24591  1.000 26.37321  ? 200 VAL A O     1 
ATOM   1317 C  CB    . VAL A 1  170 ? 30.30793  12.41201  44.63028  1.000 25.62706  ? 200 VAL A CB    1 
ATOM   1318 C  CG1   . VAL A 1  170 ? 29.29969  11.69914  43.73544  1.000 25.22212  ? 200 VAL A CG1   1 
ATOM   1319 C  CG2   . VAL A 1  170 ? 30.04009  12.11910  46.09433  1.000 27.09151  ? 200 VAL A CG2   1 
ATOM   1320 N  N     . SER A 1  171 ? 33.49509  13.64250  44.35380  1.000 27.78643  ? 201 SER A N     1 
ATOM   1321 C  CA    . SER A 1  171 ? 34.44132  14.53037  45.01165  1.000 31.65895  ? 201 SER A CA    1 
ATOM   1322 C  C     . SER A 1  171 ? 33.70260  15.51551  45.90972  1.000 28.21227  ? 201 SER A C     1 
ATOM   1323 O  O     . SER A 1  171 ? 32.48161  15.68270  45.81788  1.000 29.66923  ? 201 SER A O     1 
ATOM   1324 C  CB    . SER A 1  171 ? 35.26730  15.30721  43.98651  1.000 34.65130  ? 201 SER A CB    1 
ATOM   1325 O  OG    . SER A 1  171 ? 34.49437  16.33331  43.37059  1.000 37.97456  ? 201 SER A OG    1 
ATOM   1326 N  N     . LYS A 1  172 ? 34.45382  16.17442  46.79060  1.000 29.41386  ? 202 LYS A N     1 
ATOM   1327 C  CA    . LYS A 1  172 ? 33.84810  17.20454  47.62265  1.000 35.54485  ? 202 LYS A CA    1 
ATOM   1328 C  C     . LYS A 1  172 ? 33.35317  18.37859  46.78969  1.000 31.81358  ? 202 LYS A C     1 
ATOM   1329 O  O     . LYS A 1  172 ? 32.34631  18.99476  47.13981  1.000 33.80091  ? 202 LYS A O     1 
ATOM   1330 C  CB    . LYS A 1  172 ? 34.84632  17.66341  48.69550  1.000 33.63880  ? 202 LYS A CB    1 
ATOM   1331 C  CG    . LYS A 1  172 ? 35.25426  16.51338  49.61248  1.000 38.13274  ? 202 LYS A CG    1 
ATOM   1332 C  CD    . LYS A 1  172 ? 35.08252  16.85445  51.08549  1.000 46.64624  ? 202 LYS A CD    1 
ATOM   1333 C  CE    . LYS A 1  172 ? 35.67647  15.76238  51.96344  1.000 53.05736  ? 202 LYS A CE    1 
ATOM   1334 N  NZ    . LYS A 1  172 ? 35.48117  14.43139  51.31851  1.000 66.52454  ? 202 LYS A NZ    1 
ATOM   1335 N  N     . SER A 1  173 ? 34.00806  18.69146  45.67059  1.000 30.18131  ? 203 SER A N     1 
ATOM   1336 C  CA    A SER A 1  173 ? 33.48811  19.75752  44.81963  0.729 30.83207  ? 203 SER A CA    1 
ATOM   1337 C  CA    B SER A 1  173 ? 33.48711  19.75552  44.82063  0.271 30.82993  ? 203 SER A CA    1 
ATOM   1338 C  C     . SER A 1  173 ? 32.19195  19.34270  44.13382  1.000 30.11319  ? 203 SER A C     1 
ATOM   1339 O  O     . SER A 1  173 ? 31.32105  20.18483  43.89691  1.000 32.69236  ? 203 SER A O     1 
ATOM   1340 C  CB    A SER A 1  173 ? 34.52403  20.17232  43.77347  0.729 32.06671  ? 203 SER A CB    1 
ATOM   1341 C  CB    B SER A 1  173 ? 34.53003  20.15632  43.78347  0.271 32.05650  ? 203 SER A CB    1 
ATOM   1342 O  OG    A SER A 1  173 ? 34.57674  19.26828  42.68849  0.729 36.37959  ? 203 SER A OG    1 
ATOM   1343 O  OG    B SER A 1  173 ? 35.66921  20.67716  44.43830  0.271 40.06966  ? 203 SER A OG    1 
ATOM   1344 N  N     . GLU A 1  174 ? 32.04771  18.05271  43.81788  1.000 29.39727  ? 204 GLU A N     1 
ATOM   1345 C  CA    . GLU A 1  174 ? 30.82154  17.55189  43.19806  1.000 28.71344  ? 204 GLU A CA    1 
ATOM   1346 C  C     . GLU A 1  174 ? 29.67267  17.51010  44.19322  1.000 29.63640  ? 204 GLU A C     1 
ATOM   1347 O  O     . GLU A 1  174 ? 28.52968  17.84327  43.84637  1.000 33.94898  ? 204 GLU A O     1 
ATOM   1348 C  CB    . GLU A 1  174 ? 31.05124  16.15783  42.60807  1.000 28.30552  ? 204 GLU A CB    1 
ATOM   1349 C  CG    . GLU A 1  174 ? 31.80106  16.16268  41.28596  1.000 34.23119  ? 204 GLU A CG    1 
ATOM   1350 C  CD    . GLU A 1  174 ? 32.25578  14.76559  40.85194  1.000 41.19273  ? 204 GLU A CD    1 
ATOM   1351 O  OE1   . GLU A 1  174 ? 32.63177  13.94756  41.72291  1.000 36.26489  ? 204 GLU A OE1   1 
ATOM   1352 O  OE2   . GLU A 1  174 ? 32.23457  14.49356  39.63495  1.000 36.25761  ? 204 GLU A OE2   1 
ATOM   1353 N  N     . TYR A 1  175 ? 29.94477  17.07209  45.42419  1.000 27.32884  ? 205 TYR A N     1 
ATOM   1354 C  CA    . TYR A 1  175 ? 28.94992  17.01428  46.53533  1.000 26.54555  ? 205 TYR A CA    1 
ATOM   1355 C  C     . TYR A 1  175 ? 29.71814  17.32720  47.80322  1.000 26.65222  ? 205 TYR A C     1 
ATOM   1356 O  O     . TYR A 1  175 ? 30.45708  16.49209  48.28814  1.000 26.38063  ? 205 TYR A O     1 
ATOM   1357 C  CB    . TYR A 1  175 ? 28.15373  15.71641  46.68748  1.000 25.54704  ? 205 TYR A CB    1 
ATOM   1358 C  CG    . TYR A 1  175 ? 27.00589  15.83662  47.67964  1.000 24.93128  ? 205 TYR A CG    1 
ATOM   1359 C  CD1   . TYR A 1  175 ? 25.81494  16.44180  47.31278  1.000 24.94693  ? 205 TYR A CD1   1 
ATOM   1360 C  CD2   . TYR A 1  175 ? 27.13800  15.37464  48.98263  1.000 24.41537  ? 205 TYR A CD2   1 
ATOM   1361 C  CE1   . TYR A 1  175 ? 24.76908  16.56699  48.20892  1.000 24.49534  ? 205 TYR A CE1   1 
ATOM   1362 C  CE2   . TYR A 1  175 ? 26.10114  15.49683  49.88877  1.000 23.94010  ? 205 TYR A CE2   1 
ATOM   1363 C  CZ    . TYR A 1  175 ? 24.91518  16.09400  49.49792  1.000 24.00214  ? 205 TYR A CZ    1 
ATOM   1364 O  OH    . TYR A 1  175 ? 23.88232  16.22219  50.36306  1.000 25.93947  ? 205 TYR A OH    1 
ATOM   1365 N  N     . PRO A 1  176 ? 29.56041  18.53024  48.37321  1.000 29.95368  ? 206 PRO A N     1 
ATOM   1366 C  CA    . PRO A 1  176 ? 30.44763  18.97813  49.45107  1.000 27.89584  ? 206 PRO A CA    1 
ATOM   1367 C  C     . PRO A 1  176 ? 29.99678  18.68324  50.87014  1.000 26.66523  ? 206 PRO A C     1 
ATOM   1368 O  O     . PRO A 1  176 ? 30.71797  19.05915  51.80303  1.000 31.66522  ? 206 PRO A O     1 
ATOM   1369 C  CB    . PRO A 1  176 ? 30.50184  20.50211  49.22002  1.000 28.43347  ? 206 PRO A CB    1 
ATOM   1370 C  CG    . PRO A 1  176 ? 29.18381  20.82830  48.63219  1.000 28.25888  ? 206 PRO A CG    1 
ATOM   1371 C  CD    . PRO A 1  176 ? 28.79550  19.63534  47.76128  1.000 27.60481  ? 206 PRO A CD    1 
ATOM   1372 N  N     . TRP A 1  177 ? 28.86869  17.99942  51.02132  1.000 29.56578  ? 207 TRP A N     1 
ATOM   1373 C  CA    . TRP A 1  177 ? 28.31685  17.79155  52.37840  1.000 25.17820  ? 207 TRP A CA    1 
ATOM   1374 C  C     . TRP A 1  177 ? 28.53469  16.35953  52.86541  1.000 26.32591  ? 207 TRP A C     1 
ATOM   1375 O  O     . TRP A 1  177 ? 28.83844  15.49546  52.04439  1.000 27.62994  ? 207 TRP A O     1 
ATOM   1376 C  CB    . TRP A 1  177 ? 26.86393  18.28378  52.42658  1.000 24.99824  ? 207 TRP A CB    1 
ATOM   1377 C  CG    . TRP A 1  177 ? 26.74612  19.74679  52.09756  1.000 25.88743  ? 207 TRP A CG    1 
ATOM   1378 C  CD1   . TRP A 1  177 ? 27.20238  20.79274  52.84046  1.000 30.98623  ? 207 TRP A CD1   1 
ATOM   1379 C  CD2   . TRP A 1  177 ? 26.16604  20.31685  50.91062  1.000 27.77352  ? 207 TRP A CD2   1 
ATOM   1380 N  NE1   . TRP A 1  177 ? 26.93048  21.97776  52.21147  1.000 27.33744  ? 207 TRP A NE1   1 
ATOM   1381 C  CE2   . TRP A 1  177 ? 26.30328  21.71783  51.02456  1.000 30.70617  ? 207 TRP A CE2   1 
ATOM   1382 C  CE3   . TRP A 1  177 ? 25.54980  19.78791  49.77472  1.000 26.09606  ? 207 TRP A CE3   1 
ATOM   1383 C  CZ2   . TRP A 1  177 ? 25.83728  22.58687  50.04460  1.000 27.90703  ? 207 TRP A CZ2   1 
ATOM   1384 C  CZ3   . TRP A 1  177 ? 25.09281  20.65395  48.80976  1.000 26.71598  ? 207 TRP A CZ3   1 
ATOM   1385 C  CH2   . TRP A 1  177 ? 25.23604  22.03193  48.94370  1.000 27.60879  ? 207 TRP A CH2   1 
ATOM   1386 N  N     . ASP A 1  178 ? 28.38183  16.12859  54.16244  1.000 23.90737  ? 208 ASP A N     1 
ATOM   1387 C  CA    . ASP A 1  178 ? 28.71171  14.81656  54.78143  1.000 32.42418  ? 208 ASP A CA    1 
ATOM   1388 C  C     . ASP A 1  178 ? 27.65951  13.74772  54.51861  1.000 30.91247  ? 208 ASP A C     1 
ATOM   1389 O  O     . ASP A 1  178 ? 28.01932  12.57366  54.49259  1.000 35.08328  ? 208 ASP A O     1 
ATOM   1390 C  CB    . ASP A 1  178 ? 28.91794  14.98357  56.27640  1.000 37.10367  ? 208 ASP A CB    1 
ATOM   1391 C  CG    . ASP A 1  178 ? 30.08314  15.85640  56.71521  1.000 49.34154  ? 208 ASP A CG    1 
ATOM   1392 O  OD1   . ASP A 1  178 ? 30.96307  16.12823  55.88008  1.000 57.16176  ? 208 ASP A OD1   1 
ATOM   1393 O  OD2   . ASP A 1  178 ? 30.09337  16.25943  57.89520  1.000 43.48264  ? 208 ASP A OD2   1 
ATOM   1394 N  N     . ARG A 1  179 ? 26.41555  14.15291  54.35877  1.000 28.10901  ? 209 ARG A N     1 
ATOM   1395 C  CA    . ARG A 1  179 ? 25.32137  13.19207  54.16795  1.000 30.37541  ? 209 ARG A CA    1 
ATOM   1396 C  C     . ARG A 1  179 ? 24.51126  13.58917  52.94405  1.000 30.64583  ? 209 ARG A C     1 
ATOM   1397 O  O     . ARG A 1  179 ? 24.53440  14.75215  52.58401  1.000 24.43244  ? 209 ARG A O     1 
ATOM   1398 C  CB    . ARG A 1  179 ? 24.41354  13.18225  55.39607  1.000 34.58111  ? 209 ARG A CB    1 
ATOM   1399 C  CG    . ARG A 1  179 ? 25.04959  12.48419  56.58400  1.000 51.97407  ? 209 ARG A CG    1 
ATOM   1400 C  CD    . ARG A 1  179 ? 24.01857  11.69337  57.35317  1.000 58.79209  ? 209 ARG A CD    1 
ATOM   1401 N  NE    . ARG A 1  179 ? 23.01080  12.57255  57.95028  1.000 77.10234  ? 209 ARG A NE    1 
ATOM   1402 C  CZ    . ARG A 1  179 ? 21.95082  12.14673  58.61744  1.000 87.09472  ? 209 ARG A CZ    1 
ATOM   1403 N  NH1   . ARG A 1  179 ? 21.19060  11.18984  58.11457  1.000 72.95412  ? 209 ARG A NH1   1 
ATOM   1404 N  NH2   . ARG A 1  179 ? 21.65807  12.67781  59.79047  1.000 85.42524  ? 209 ARG A NH2   1 
ATOM   1405 N  N     . TYR A 1  180 ? 23.88302  12.60725  52.32516  1.000 21.68223  ? 210 TYR A N     1 
ATOM   1406 C  CA    . TYR A 1  180 ? 22.98791  12.86335  51.18528  1.000 25.52025  ? 210 TYR A CA    1 
ATOM   1407 C  C     . TYR A 1  180 ? 21.61602  13.11059  51.75946  1.000 28.73079  ? 210 TYR A C     1 
ATOM   1408 O  O     . TYR A 1  180 ? 21.35214  12.80766  52.92851  1.000 32.72669  ? 210 TYR A O     1 
ATOM   1409 C  CB    . TYR A 1  180 ? 22.95559  11.62133  50.30332  1.000 21.58381  ? 210 TYR A CB    1 
ATOM   1410 C  CG    . TYR A 1  180 ? 24.10843  11.46012  49.32716  1.000 21.96074  ? 210 TYR A CG    1 
ATOM   1411 C  CD1   . TYR A 1  180 ? 24.67352  12.56202  48.70405  1.000 22.62261  ? 210 TYR A CD1   1 
ATOM   1412 C  CD2   . TYR A 1  180 ? 24.61519  10.20403  49.02413  1.000 21.74133  ? 210 TYR A CD2   1 
ATOM   1413 C  CE1   . TYR A 1  180 ? 25.71237  12.42183  47.80391  1.000 23.05910  ? 210 TYR A CE1   1 
ATOM   1414 C  CE2   . TYR A 1  180 ? 25.65504  10.04984  48.12599  1.000 22.16888  ? 210 TYR A CE2   1 
ATOM   1415 C  CZ    . TYR A 1  180 ? 26.20413  11.16174  47.51988  1.000 22.82847  ? 210 TYR A CZ    1 
ATOM   1416 O  OH    . TYR A 1  180 ? 27.22499  11.03155  46.63375  1.000 27.21496  ? 210 TYR A OH    1 
ATOM   1417 N  N     . PRO A 1  181 ? 20.68801  13.68971  50.98957  1.000 25.77643  ? 211 PRO A N     1 
ATOM   1418 C  CA    . PRO A 1  181 ? 19.29809  13.81594  51.46276  1.000 21.78799  ? 211 PRO A CA    1 
ATOM   1419 C  C     . PRO A 1  181 ? 18.64688  12.44804  51.44989  1.000 25.44503  ? 211 PRO A C     1 
ATOM   1420 O  O     . PRO A 1  181 ? 19.24065  11.51793  50.88083  1.000 23.09266  ? 211 PRO A O     1 
ATOM   1421 C  CB    . PRO A 1  181 ? 18.69409  14.71101  50.41182  1.000 24.25754  ? 211 PRO A CB    1 
ATOM   1422 C  CG    . PRO A 1  181 ? 19.46187  14.38385  49.15272  1.000 28.13327  ? 211 PRO A CG    1 
ATOM   1423 C  CD    . PRO A 1  181 ? 20.86391  14.26264  49.62353  1.000 28.48329  ? 211 PRO A CD    1 
ATOM   1424 N  N     . PRO A 1  182 ? 17.44493  12.25425  52.02806  1.000 34.66433  ? 212 PRO A N     1 
ATOM   1425 C  CA    . PRO A 1  182 ? 16.74070  10.97936  51.82020  1.000 25.96915  ? 212 PRO A CA    1 
ATOM   1426 C  C     . PRO A 1  182 ? 16.52646  10.76835  50.33323  1.000 25.00371  ? 212 PRO A C     1 
ATOM   1427 O  O     . PRO A 1  182 ? 16.17950  11.69638  49.60525  1.000 21.22407  ? 212 PRO A O     1 
ATOM   1428 C  CB    . PRO A 1  182 ? 15.40783  11.16159  52.56337  1.000 26.62976  ? 212 PRO A CB    1 
ATOM   1429 C  CG    . PRO A 1  182 ? 15.58315  12.41358  53.42531  1.000 21.00739  ? 212 PRO A CG    1 
ATOM   1430 C  CD    . PRO A 1  182 ? 16.59418  13.26240  52.70715  1.000 27.94703  ? 212 PRO A CD    1 
ATOM   1431 N  N     . PHE A 1  183 ? 16.67420  9.52831   49.90625  1.000 22.49809  ? 213 PHE A N     1 
ATOM   1432 C  CA    . PHE A 1  183 ? 16.39996  9.20431   48.49229  1.000 21.95768  ? 213 PHE A CA    1 
ATOM   1433 C  C     . PHE A 1  183 ? 16.02771  7.73337   48.36939  1.000 24.29279  ? 213 PHE A C     1 
ATOM   1434 O  O     . PHE A 1  183 ? 16.17772  6.97337   49.31639  1.000 20.12391  ? 213 PHE A O     1 
ATOM   1435 C  CB    . PHE A 1  183 ? 17.59491  9.62810   47.63312  1.000 23.44788  ? 213 PHE A CB    1 
ATOM   1436 C  CG    . PHE A 1  183 ? 18.86779  8.80390   47.74997  1.000 27.57425  ? 213 PHE A CG    1 
ATOM   1437 C  CD1   . PHE A 1  183 ? 19.79797  9.07078   48.74283  1.000 21.65826  ? 213 PHE A CD1   1 
ATOM   1438 C  CD2   . PHE A 1  183 ? 19.13751  7.78583   46.84696  1.000 27.73846  ? 213 PHE A CD2   1 
ATOM   1439 C  CE1   . PHE A 1  183 ? 20.95987  8.32860   48.83969  1.000 22.65359  ? 213 PHE A CE1   1 
ATOM   1440 C  CE2   . PHE A 1  183 ? 20.30141  7.04765   46.94882  1.000 25.85261  ? 213 PHE A CE2   1 
ATOM   1441 C  CZ    . PHE A 1  183 ? 21.20459  7.31854   47.94469  1.000 32.29972  ? 213 PHE A CZ    1 
ATOM   1442 N  N     . CYS A 1  184 ? 15.53549  7.35941   47.20047  1.000 20.54212  ? 214 CYS A N     1 
ATOM   1443 C  CA    . CYS A 1  184 ? 15.24723  5.94145   46.95555  1.000 26.95149  ? 214 CYS A CA    1 
ATOM   1444 C  C     . CYS A 1  184 ? 16.18700  5.38927   45.89543  1.000 23.06503  ? 214 CYS A C     1 
ATOM   1445 O  O     . CYS A 1  184 ? 16.55598  6.08718   44.94936  1.000 30.54399  ? 214 CYS A O     1 
ATOM   1446 C  CB    . CYS A 1  184 ? 13.80813  5.72366   46.49175  1.000 24.67390  ? 214 CYS A CB    1 
ATOM   1447 S  SG    . CYS A 1  184 ? 12.54936  6.05790   47.75692  1.000 32.16507  ? 214 CYS A SG    1 
ATOM   1448 N  N     . SER A 1  185 ? 16.57381  4.12521   45.98542  1.000 25.34863  ? 215 SER A N     1 
ATOM   1449 C  CA    . SER A 1  185 ? 17.44157  3.51304   44.93832  1.000 24.06253  ? 215 SER A CA    1 
ATOM   1450 C  C     . SER A 1  185 ? 16.91242  3.76709   43.51938  1.000 25.47266  ? 215 SER A C     1 
ATOM   1451 O  O     . SER A 1  185 ? 15.69137  3.67627   43.31355  1.000 27.62489  ? 215 SER A O     1 
ATOM   1452 C  CB    . SER A 1  185 ? 17.67937  2.04001   45.17633  1.000 22.63296  ? 215 SER A CB    1 
ATOM   1453 O  OG    . SER A 1  185 ? 18.51115  1.47385   44.17823  1.000 27.35573  ? 215 SER A OG    1 
ATOM   1454 N  N     . GLY A 1  186 ? 17.81732  4.01492   42.57625  1.000 21.06001  ? 216 GLY A N     1 
ATOM   1455 C  CA    . GLY A 1  186 ? 17.45017  4.25493   41.17629  1.000 21.37180  ? 216 GLY A CA    1 
ATOM   1456 C  C     . GLY A 1  186 ? 17.10787  2.97497   40.45738  1.000 29.14452  ? 216 GLY A C     1 
ATOM   1457 O  O     . GLY A 1  186 ? 16.63873  3.08001   39.32144  1.000 35.74627  ? 216 GLY A O     1 
ATOM   1458 N  N     . THR A 1  187 ? 17.32877  1.82195   41.07938  1.000 21.27838  ? 217 THR A N     1 
ATOM   1459 C  CA    . THR A 1  187 ? 16.89249  0.53200   40.51348  1.000 27.12662  ? 217 THR A CA    1 
ATOM   1460 C  C     . THR A 1  187 ? 15.42545  0.61822   40.11968  1.000 21.77091  ? 217 THR A C     1 
ATOM   1461 O  O     . THR A 1  187 ? 15.15523  0.25123   38.97873  1.000 31.60432  ? 217 THR A O     1 
ATOM   1462 C  CB    . THR A 1  187 ? 17.20746  -0.56002  41.54147  1.000 21.23328  ? 217 THR A CB    1 
ATOM   1463 O  OG1   . THR A 1  187 ? 16.68070  -0.14390  42.79453  1.000 27.43490  ? 217 THR A OG1   1 
ATOM   1464 C  CG2   . THR A 1  187 ? 18.70044  -0.79825  41.67827  1.000 21.31727  ? 217 THR A CG2   1 
ATOM   1465 N  N     . GLY A 1  188 ? 14.51363  0.98239   41.02679  1.000 21.23433  ? 218 GLY A N     1 
ATOM   1466 C  CA    . GLY A 1  188 ? 13.09864  1.23361   40.76698  1.000 25.77171  ? 218 GLY A CA    1 
ATOM   1467 C  C     . GLY A 1  188 ? 12.53093  2.17173   41.80903  1.000 21.71920  ? 218 GLY A C     1 
ATOM   1468 O  O     . GLY A 1  188 ? 12.69206  1.93274   43.01202  1.000 30.06522  ? 218 GLY A O     1 
ATOM   1469 N  N     . TYR A 1  189 ? 11.94204  3.26881   41.36908  1.000 25.86893  ? 219 TYR A N     1 
ATOM   1470 C  CA    . TYR A 1  189 ? 11.25731  4.17694   42.32215  1.000 23.80669  ? 219 TYR A CA    1 
ATOM   1471 C  C     . TYR A 1  189 ? 9.92028   4.53813   41.68932  1.000 22.07291  ? 219 TYR A C     1 
ATOM   1472 O  O     . TYR A 1  189 ? 9.81313   4.60112   40.46834  1.000 21.84953  ? 219 TYR A O     1 
ATOM   1473 C  CB    . TYR A 1  189 ? 12.08257  5.37483   42.81500  1.000 21.18470  ? 219 TYR A CB    1 
ATOM   1474 C  CG    . TYR A 1  189 ? 12.78858  6.27269   41.82188  1.000 25.32348  ? 219 TYR A CG    1 
ATOM   1475 C  CD1   . TYR A 1  189 ? 12.07960  7.15878   41.02395  1.000 21.70536  ? 219 TYR A CD1   1 
ATOM   1476 C  CD2   . TYR A 1  189 ? 14.17356  6.27247   41.73269  1.000 24.86667  ? 219 TYR A CD2   1 
ATOM   1477 C  CE1   . TYR A 1  189 ? 12.73062  7.99965   40.14384  1.000 24.49189  ? 219 TYR A CE1   1 
ATOM   1478 C  CE2   . TYR A 1  189 ? 14.83457  7.10734   40.85257  1.000 25.41815  ? 219 TYR A CE2   1 
ATOM   1479 C  CZ    . TYR A 1  189 ? 14.10860  7.97543   40.05865  1.000 24.11232  ? 219 TYR A CZ    1 
ATOM   1480 O  OH    . TYR A 1  189 ? 14.74761  8.79230   39.19053  1.000 29.02303  ? 219 TYR A OH    1 
ATOM   1481 N  N     . VAL A 1  190 ? 8.91743   4.72132   42.53346  1.000 26.43254  ? 220 VAL A N     1 
ATOM   1482 C  CA    . VAL A 1  190 ? 7.54741   5.01052   42.03164  1.000 22.84636  ? 220 VAL A CA    1 
ATOM   1483 C  C     . VAL A 1  190 ? 7.06470   6.33461   42.62867  1.000 22.32110  ? 220 VAL A C     1 
ATOM   1484 O  O     . VAL A 1  190 ? 7.31890   6.59961   43.80762  1.000 24.32849  ? 220 VAL A O     1 
ATOM   1485 C  CB    . VAL A 1  190 ? 6.55426   3.86868   42.31181  1.000 22.45413  ? 220 VAL A CB    1 
ATOM   1486 C  CG1   . VAL A 1  190 ? 5.20721   4.09887   41.63699  1.000 25.97992  ? 220 VAL A CG1   1 
ATOM   1487 C  CG2   . VAL A 1  190 ? 7.12000   2.50858   41.93077  1.000 21.98945  ? 220 VAL A CG2   1 
ATOM   1488 N  N     . PHE A 1  191 ? 6.40371   7.11969   41.80074  1.000 22.44248  ? 221 PHE A N     1 
ATOM   1489 C  CA    . PHE A 1  191 ? 5.86697   8.41079   42.27477  1.000 26.83276  ? 221 PHE A CA    1 
ATOM   1490 C  C     . PHE A 1  191 ? 4.53093   8.67398   41.63395  1.000 29.49674  ? 221 PHE A C     1 
ATOM   1491 O  O     . PHE A 1  191 ? 4.25770   8.21399   40.51700  1.000 24.71274  ? 221 PHE A O     1 
ATOM   1492 C  CB    . PHE A 1  191 ? 6.80612   9.58363   41.95661  1.000 22.74240  ? 221 PHE A CB    1 
ATOM   1493 C  CG    . PHE A 1  191 ? 7.42493   9.64949   40.57152  1.000 22.79452  ? 221 PHE A CG    1 
ATOM   1494 C  CD1   . PHE A 1  191 ? 8.58078   8.93930   40.27038  1.000 28.47454  ? 221 PHE A CD1   1 
ATOM   1495 C  CD2   . PHE A 1  191 ? 6.87193   10.45755  39.58557  1.000 25.60102  ? 221 PHE A CD2   1 
ATOM   1496 C  CE1   . PHE A 1  191 ? 9.14862   9.01018   39.01330  1.000 23.29572  ? 221 PHE A CE1   1 
ATOM   1497 C  CE2   . PHE A 1  191 ? 7.44976   10.52943  38.33149  1.000 23.89526  ? 221 PHE A CE2   1 
ATOM   1498 C  CZ    . PHE A 1  191 ? 8.58761   9.81024   38.05036  1.000 26.83507  ? 221 PHE A CZ    1 
ATOM   1499 N  N     . SER A 1  192 ? 3.67114   9.35414   42.37205  1.000 27.99579  ? 222 SER A N     1 
ATOM   1500 C  CA    . SER A 1  192 ? 2.44513   9.84531   41.74620  1.000 32.15600  ? 222 SER A CA    1 
ATOM   1501 C  C     . SER A 1  192 ? 2.79613   10.85023  40.65413  1.000 27.76231  ? 222 SER A C     1 
ATOM   1502 O  O     . SER A 1  192 ? 3.77627   11.60407  40.75497  1.000 29.00341  ? 222 SER A O     1 
ATOM   1503 C  CB    . SER A 1  192 ? 1.51337   10.46849  42.78731  1.000 28.53699  ? 222 SER A CB    1 
ATOM   1504 O  OG    . SER A 1  192 ? 2.17263   11.39541  43.61620  1.000 40.33058  ? 222 SER A OG    1 
ATOM   1505 N  N     . GLY A 1  193 ? 1.97599   10.85832  39.60124  1.000 24.83523  ? 223 GLY A N     1 
ATOM   1506 C  CA    . GLY A 1  193 ? 2.31594   11.57724  38.38617  1.000 26.07782  ? 223 GLY A CA    1 
ATOM   1507 C  C     . GLY A 1  193 ? 2.53820   13.07621  38.56810  1.000 35.94905  ? 223 GLY A C     1 
ATOM   1508 O  O     . GLY A 1  193 ? 3.34219   13.66306  37.84797  1.000 35.97837  ? 223 GLY A O     1 
ATOM   1509 N  N     . ASP A 1  194 ? 1.81343   13.71035  39.50218  1.000 32.89953  ? 224 ASP A N     1 
ATOM   1510 C  CA    . ASP A 1  194 ? 2.00469   15.14632  39.76811  1.000 34.57127  ? 224 ASP A CA    1 
ATOM   1511 C  C     . ASP A 1  194 ? 3.43180   15.46011  40.21590  1.000 39.38663  ? 224 ASP A C     1 
ATOM   1512 O  O     . ASP A 1  194 ? 3.93995   16.58503  40.01980  1.000 39.22941  ? 224 ASP A O     1 
ATOM   1513 C  CB    . ASP A 1  194 ? 1.05891   15.59151  40.86523  1.000 28.34976  ? 224 ASP A CB    1 
ATOM   1514 C  CG    . ASP A 1  194 ? 1.25896   14.79951  42.12822  1.000 43.07128  ? 224 ASP A CG    1 
ATOM   1515 O  OD1   . ASP A 1  194 ? 1.23975   13.55551  42.02226  1.000 44.10033  ? 224 ASP A OD1   1 
ATOM   1516 O  OD2   . ASP A 1  194 ? 1.48720   15.38351  43.21617  1.000 45.30436  ? 224 ASP A OD2   1 
ATOM   1517 N  N     . VAL A 1  195 ? 4.06774   14.48603  40.88184  1.000 38.54803  ? 225 VAL A N     1 
ATOM   1518 C  CA    . VAL A 1  195 ? 5.44283   14.66783  41.32665  1.000 29.91374  ? 225 VAL A CA    1 
ATOM   1519 C  C     . VAL A 1  195 ? 6.35572   15.01865  40.15951  1.000 36.91145  ? 225 VAL A C     1 
ATOM   1520 O  O     . VAL A 1  195 ? 7.31387   15.77451  40.33536  1.000 34.50645  ? 225 VAL A O     1 
ATOM   1521 C  CB    . VAL A 1  195 ? 5.92273   13.40778  42.08162  1.000 36.26029  ? 225 VAL A CB    1 
ATOM   1522 C  CG1   . VAL A 1  195 ? 7.42679   13.48455  42.36541  1.000 29.32509  ? 225 VAL A CG1   1 
ATOM   1523 C  CG2   . VAL A 1  195 ? 5.15189   13.25093  43.36173  1.000 25.40985  ? 225 VAL A CG2   1 
ATOM   1524 N  N     . ALA A 1  196 ? 6.11247   14.46065  38.96356  1.000 33.19009  ? 226 ALA A N     1 
ATOM   1525 C  CA    . ALA A 1  196 ? 6.97736   14.76749  37.82243  1.000 24.66968  ? 226 ALA A CA    1 
ATOM   1526 C  C     . ALA A 1  196 ? 6.97555   16.25448  37.50039  1.000 33.39866  ? 226 ALA A C     1 
ATOM   1527 O  O     . ALA A 1  196 ? 8.02960   16.84230  37.21923  1.000 34.57409  ? 226 ALA A O     1 
ATOM   1528 C  CB    . ALA A 1  196 ? 6.57006   13.97151  36.58651  1.000 30.05112  ? 226 ALA A CB    1 
ATOM   1529 N  N     . SER A 1  197 ? 5.85768   16.94566  37.64553  1.000 31.77867  ? 227 SER A N     1 
ATOM   1530 C  CA    . SER A 1  197 ? 5.85285   18.37365  37.24248  1.000 36.52066  ? 227 SER A CA    1 
ATOM   1531 C  C     . SER A 1  197 ? 6.58913   19.22756  38.28836  1.000 35.16226  ? 227 SER A C     1 
ATOM   1532 O  O     . SER A 1  197 ? 7.32822   20.13843  37.89323  1.000 36.66777  ? 227 SER A O     1 
ATOM   1533 C  CB    . SER A 1  197 ? 4.45089   18.87086  37.01466  1.000 39.68415  ? 227 SER A CB    1 
ATOM   1534 O  OG    . SER A 1  197 ? 3.86464   18.25092  35.88176  1.000 54.34408  ? 227 SER A OG    1 
ATOM   1535 N  N     . GLN A 1  198 ? 6.40225   18.91663  39.56539  1.000 30.62040  ? 228 GLN A N     1 
ATOM   1536 C  CA    . GLN A 1  198 ? 7.03553   19.70356  40.64428  1.000 26.85495  ? 228 GLN A CA    1 
ATOM   1537 C  C     . GLN A 1  198 ? 8.56149   19.52832  40.58308  1.000 36.12705  ? 228 GLN A C     1 
ATOM   1538 O  O     . GLN A 1  198 ? 9.27068   20.49321  40.87695  1.000 31.40731  ? 228 GLN A O     1 
ATOM   1539 C  CB    . GLN A 1  198 ? 6.42265   19.30569  41.97938  1.000 26.92607  ? 228 GLN A CB    1 
ATOM   1540 C  CG    . GLN A 1  198 ? 4.90065   19.30593  42.00159  1.000 42.16448  ? 228 GLN A CG    1 
ATOM   1541 C  CD    . GLN A 1  198 ? 4.32971   18.62506  43.22569  1.000 57.67909  ? 228 GLN A CD    1 
ATOM   1542 O  OE1   . GLN A 1  198 ? 4.37295   19.16009  44.33767  1.000 54.02004  ? 228 GLN A OE1   1 
ATOM   1543 N  NE2   . GLN A 1  198 ? 3.79450   17.42914  43.03480  1.000 47.17636  ? 228 GLN A NE2   1 
ATOM   1544 N  N     . VAL A 1  199 ? 9.03925   18.33823  40.21305  1.000 31.66481  ? 229 VAL A N     1 
ATOM   1545 C  CA    . VAL A 1  199 ? 10.50820  18.08600  40.15285  1.000 25.34865  ? 229 VAL A CA    1 
ATOM   1546 C  C     . VAL A 1  199 ? 11.08516  18.86887  38.96075  1.000 28.57990  ? 229 VAL A C     1 
ATOM   1547 O  O     . VAL A 1  199 ? 12.06030  19.58372  39.16559  1.000 32.29907  ? 229 VAL A O     1 
ATOM   1548 C  CB    . VAL A 1  199 ? 10.89797  16.59694  40.13484  1.000 24.65602  ? 229 VAL A CB    1 
ATOM   1549 C  CG1   . VAL A 1  199 ? 12.34688  16.37970  39.72365  1.000 24.58598  ? 229 VAL A CG1   1 
ATOM   1550 C  CG2   . VAL A 1  199 ? 10.60504  15.91902  41.46490  1.000 26.68868  ? 229 VAL A CG2   1 
ATOM   1551 N  N     . TYR A 1  200 ? 10.47498  18.75393  37.78583  1.000 26.04771  ? 230 TYR A N     1 
ATOM   1552 C  CA    . TYR A 1  200 ? 10.98792  19.43482  36.56974  1.000 33.73642  ? 230 TYR A CA    1 
ATOM   1553 C  C     . TYR A 1  200 ? 11.09520  20.91281  36.86669  1.000 37.68086  ? 230 TYR A C     1 
ATOM   1554 O  O     . TYR A 1  200 ? 12.06724  21.56164  36.46553  1.000 50.37068  ? 230 TYR A O     1 
ATOM   1555 C  CB    . TYR A 1  200 ? 10.07572  19.18993  35.37288  1.000 26.69393  ? 230 TYR A CB    1 
ATOM   1556 C  CG    . TYR A 1  200 ? 10.51465  19.86582  34.08380  1.000 37.71261  ? 230 TYR A CG    1 
ATOM   1557 C  CD1   . TYR A 1  200 ? 11.72852  19.55361  33.49064  1.000 39.25192  ? 230 TYR A CD1   1 
ATOM   1558 C  CD2   . TYR A 1  200 ? 9.71171   20.81293  33.46388  1.000 44.37583  ? 230 TYR A CD2   1 
ATOM   1559 C  CE1   . TYR A 1  200 ? 12.13045  20.16051  32.31657  1.000 46.22945  ? 230 TYR A CE1   1 
ATOM   1560 C  CE2   . TYR A 1  200 ? 10.10064  21.42583  32.28781  1.000 47.34157  ? 230 TYR A CE2   1 
ATOM   1561 C  CZ    . TYR A 1  200 ? 11.31351  21.09962  31.71265  1.000 56.74651  ? 230 TYR A CZ    1 
ATOM   1562 O  OH    . TYR A 1  200 ? 11.71145  21.70053  30.55758  1.000 62.70410  ? 230 TYR A OH    1 
ATOM   1563 N  N     . ASN A 1  201 ? 10.12038  21.44598  37.60281  1.000 30.89642  ? 231 ASN A N     1 
ATOM   1564 C  CA    . ASN A 1  201 ? 10.08566  22.89100  37.95377  1.000 34.73912  ? 231 ASN A CA    1 
ATOM   1565 C  C     . ASN A 1  201 ? 11.29884  23.29283  38.80159  1.000 37.22733  ? 231 ASN A C     1 
ATOM   1566 O  O     . ASN A 1  201 ? 12.03692  24.19070  38.36446  1.000 39.56994  ? 231 ASN A O     1 
ATOM   1567 C  CB    . ASN A 1  201 ? 8.77481   23.25423  38.64194  1.000 33.28653  ? 231 ASN A CB    1 
ATOM   1568 C  CG    . ASN A 1  201 ? 8.63507   24.73925  38.85191  1.000 51.56454  ? 231 ASN A CG    1 
ATOM   1569 O  OD1   . ASN A 1  201 ? 8.14729   25.17636  39.89897  1.000 61.69546  ? 231 ASN A OD1   1 
ATOM   1570 N  ND2   . ASN A 1  201 ? 9.06306   25.52716  37.87883  1.000 53.85532  ? 231 ASN A ND2   1 
ATOM   1571 N  N     . VAL A 1  202 ? 11.50889  22.64883  39.94558  1.000 27.83386  ? 232 VAL A N     1 
ATOM   1572 C  CA    . VAL A 1  202 ? 12.60208  23.04769  40.86342  1.000 27.93961  ? 232 VAL A CA    1 
ATOM   1573 C  C     . VAL A 1  202 ? 13.95193  22.48646  40.40225  1.000 36.12158  ? 232 VAL A C     1 
ATOM   1574 O  O     . VAL A 1  202 ? 14.96908  22.94432  40.93309  1.000 33.13969  ? 232 VAL A O     1 
ATOM   1575 C  CB    . VAL A 1  202 ? 12.14419  22.53980  42.23649  1.000 27.41353  ? 232 VAL A CB    1 
ATOM   1576 C  CG1   . VAL A 1  202 ? 12.00696  21.02382  42.29956  1.000 33.08762  ? 232 VAL A CG1   1 
ATOM   1577 C  CG2   . VAL A 1  202 ? 13.00843  23.08670  43.35436  1.000 45.01075  ? 232 VAL A CG2   1 
ATOM   1578 N  N     . SER A 1  203 ? 13.95466  21.59943  39.41427  1.000 27.35146  ? 233 SER A N     1 
ATOM   1579 C  CA    . SER A 1  203 ? 15.19749  20.93822  38.93212  1.000 30.54532  ? 233 SER A CA    1 
ATOM   1580 C  C     . SER A 1  203 ? 16.32661  21.94804  38.70993  1.000 35.16798  ? 233 SER A C     1 
ATOM   1581 O  O     . SER A 1  203 ? 17.43065  21.71888  39.21279  1.000 35.93928  ? 233 SER A O     1 
ATOM   1582 C  CB    . SER A 1  203 ? 14.92419  20.16523  37.67518  1.000 26.95619  ? 233 SER A CB    1 
ATOM   1583 O  OG    . SER A 1  203 ? 14.74117  21.01823  36.55718  1.000 40.73352  ? 233 SER A OG    1 
ATOM   1584 N  N     . LYS A 1  204 ? 16.03568  23.02406  37.99094  1.000 31.55656  ? 234 LYS A N     1 
ATOM   1585 C  CA    . LYS A 1  204 ? 17.08979  24.00289  37.64077  1.000 33.42125  ? 234 LYS A CA    1 
ATOM   1586 C  C     . LYS A 1  204 ? 17.61408  24.74884  38.87967  1.000 33.55380  ? 234 LYS A C     1 
ATOM   1587 O  O     . LYS A 1  204 ? 18.70615  25.30567  38.78451  1.000 43.33404  ? 234 LYS A O     1 
ATOM   1588 C  CB    . LYS A 1  204 ? 16.50878  24.90695  36.55282  1.000 39.52494  ? 234 LYS A CB    1 
ATOM   1589 C  CG    . LYS A 1  204 ? 16.26849  24.21495  35.21988  1.000 58.82908  ? 234 LYS A CG    1 
ATOM   1590 C  CD    . LYS A 1  204 ? 15.89848  25.17297  34.09090  1.000 75.56172  ? 234 LYS A CD    1 
ATOM   1591 C  CE    . LYS A 1  204 ? 14.55561  25.80919  34.27007  1.000 87.63465  ? 234 LYS A CE    1 
ATOM   1592 N  NZ    . LYS A 1  204 ? 14.18458  26.62821  33.11409  1.000 96.57225  ? 234 LYS A NZ    1 
ATOM   1593 N  N     . SER A 1  205 ? 16.90423  24.71799  40.00377  1.000 29.56473  ? 235 SER A N     1 
ATOM   1594 C  CA    . SER A 1  205 ? 17.43651  25.50493  41.11768  1.000 33.36435  ? 235 SER A CA    1 
ATOM   1595 C  C     . SER A 1  205 ? 18.07652  24.64287  42.19161  1.000 32.15258  ? 235 SER A C     1 
ATOM   1596 O  O     . SER A 1  205 ? 18.59674  25.18181  43.16753  1.000 39.58746  ? 235 SER A O     1 
ATOM   1597 C  CB    . SER A 1  205 ? 16.33173  26.36413  41.74080  1.000 45.35146  ? 235 SER A CB    1 
ATOM   1598 O  OG    . SER A 1  205 ? 15.34769  25.55730  42.36296  1.000 44.80758  ? 235 SER A OG    1 
ATOM   1599 N  N     . VAL A 1  206 ? 18.06429  23.32586  42.02065  1.000 30.34800  ? 236 VAL A N     1 
ATOM   1600 C  CA    . VAL A 1  206 ? 18.62027  22.37880  42.97560  1.000 29.20736  ? 236 VAL A CA    1 
ATOM   1601 C  C     . VAL A 1  206 ? 20.05316  22.06456  42.55442  1.000 30.77745  ? 236 VAL A C     1 
ATOM   1602 O  O     . VAL A 1  206 ? 20.30797  21.88149  41.35439  1.000 29.87672  ? 236 VAL A O     1 
ATOM   1603 C  CB    . VAL A 1  206 ? 17.75207  21.10094  43.00676  1.000 29.48808  ? 236 VAL A CB    1 
ATOM   1604 C  CG1   . VAL A 1  206 ? 18.39402  20.02386  43.83270  1.000 26.01978  ? 236 VAL A CG1   1 
ATOM   1605 C  CG2   . VAL A 1  206 ? 16.31120  21.44218  43.50695  1.000 35.46735  ? 236 VAL A CG2   1 
ATOM   1606 N  N     . PRO A 1  207 ? 21.00828  21.99844  43.47829  1.000 27.75548  ? 237 PRO A N     1 
ATOM   1607 C  CA    . PRO A 1  207 ? 22.39117  21.65421  43.08310  1.000 33.68469  ? 237 PRO A CA    1 
ATOM   1608 C  C     . PRO A 1  207 ? 22.45786  20.36418  42.27113  1.000 30.92569  ? 237 PRO A C     1 
ATOM   1609 O  O     . PRO A 1  207 ? 21.88875  19.34728  42.64624  1.000 26.57242  ? 237 PRO A O     1 
ATOM   1610 C  CB    . PRO A 1  207 ? 23.10933  21.50414  44.42301  1.000 27.73847  ? 237 PRO A CB    1 
ATOM   1611 C  CG    . PRO A 1  207 ? 22.28959  22.30929  45.38810  1.000 31.23907  ? 237 PRO A CG    1 
ATOM   1612 C  CD    . PRO A 1  207 ? 20.87351  22.15450  44.93830  1.000 35.22623  ? 237 PRO A CD    1 
ATOM   1613 N  N     . TYR A 1  208 ? 23.17471  20.41303  41.15103  1.000 29.68384  ? 238 TYR A N     1 
ATOM   1614 C  CA    . TYR A 1  208 ? 23.33741  19.23998  40.31004  1.000 27.53156  ? 238 TYR A CA    1 
ATOM   1615 C  C     . TYR A 1  208 ? 24.20634  18.18486  40.98495  1.000 27.04318  ? 238 TYR A C     1 
ATOM   1616 O  O     . TYR A 1  208 ? 25.17848  18.50573  41.67981  1.000 30.48874  ? 238 TYR A O     1 
ATOM   1617 C  CB    . TYR A 1  208 ? 23.96629  19.64484  38.97995  1.000 28.34988  ? 238 TYR A CB    1 
ATOM   1618 C  CG    . TYR A 1  208 ? 24.27798  18.46177  38.09494  1.000 34.32148  ? 238 TYR A CG    1 
ATOM   1619 C  CD1   . TYR A 1  208 ? 23.29078  17.88190  37.30309  1.000 27.66738  ? 238 TYR A CD1   1 
ATOM   1620 C  CD2   . TYR A 1  208 ? 25.55789  17.89857  38.06378  1.000 32.00574  ? 238 TYR A CD2   1 
ATOM   1621 C  CE1   . TYR A 1  208 ? 23.57150  16.80383  36.50408  1.000 28.17014  ? 238 TYR A CE1   1 
ATOM   1622 C  CE2   . TYR A 1  208 ? 25.83961  16.82050  37.25677  1.000 30.72686  ? 238 TYR A CE2   1 
ATOM   1623 C  CZ    . TYR A 1  208 ? 24.84341  16.28063  36.47692  1.000 33.46536  ? 238 TYR A CZ    1 
ATOM   1624 O  OH    . TYR A 1  208 ? 25.11913  15.19157  35.66292  1.000 40.68670  ? 238 TYR A OH    1 
ATOM   1625 N  N     . ILE A 1  209 ? 23.85211  16.91991  40.77704  1.000 32.06055  ? 239 ILE A N     1 
ATOM   1626 C  CA    . ILE A 1  209 ? 24.74098  15.80278  41.10095  1.000 26.00467  ? 239 ILE A CA    1 
ATOM   1627 C  C     . ILE A 1  209 ? 24.53666  14.72379  40.05001  1.000 25.77071  ? 239 ILE A C     1 
ATOM   1628 O  O     . ILE A 1  209 ? 23.41656  14.51295  39.56317  1.000 27.19290  ? 239 ILE A O     1 
ATOM   1629 C  CB    . ILE A 1  209 ? 24.51709  15.26586  42.53200  1.000 25.28033  ? 239 ILE A CB    1 
ATOM   1630 C  CG1   . ILE A 1  209 ? 25.63398  14.27870  42.88987  1.000 25.10834  ? 239 ILE A CG1   1 
ATOM   1631 C  CG2   . ILE A 1  209 ? 23.13401  14.60408  42.68921  1.000 24.55650  ? 239 ILE A CG2   1 
ATOM   1632 C  CD1   . ILE A 1  209 ? 25.58110  13.77875  44.32689  1.000 24.47584  ? 239 ILE A CD1   1 
ATOM   1633 N  N     . LYS A 1  210 ? 25.63851  14.07160  39.66088  1.000 26.00179  ? 240 LYS A N     1 
ATOM   1634 C  CA    . LYS A 1  210 ? 25.62121  13.12657  38.56591  1.000 25.97362  ? 240 LYS A CA    1 
ATOM   1635 C  C     . LYS A 1  210 ? 24.96705  11.80569  38.94104  1.000 25.14616  ? 240 LYS A C     1 
ATOM   1636 O  O     . LYS A 1  210 ? 24.76580  10.97669  38.05909  1.000 25.09115  ? 240 LYS A O     1 
ATOM   1637 C  CB    . LYS A 1  210 ? 27.05410  12.86833  38.09372  1.000 28.08738  ? 240 LYS A CB    1 
ATOM   1638 C  CG    . LYS A 1  210 ? 27.93314  12.22322  39.15661  1.000 26.36639  ? 240 LYS A CG    1 
ATOM   1639 C  CD    . LYS A 1  210 ? 29.38806  12.09098  38.68342  1.000 29.33154  ? 240 LYS A CD    1 
ATOM   1640 C  CE    . LYS A 1  210 ? 30.22308  11.32688  39.70232  1.000 31.83324  ? 240 LYS A CE    1 
ATOM   1641 N  NZ    . LYS A 1  210 ? 31.70312  11.63165  39.64311  1.000 38.82333  ? 240 LYS A NZ    1 
ATOM   1642 N  N     . LEU A 1  211 ? 24.67919  11.57477  40.21808  1.000 24.57632  ? 241 LEU A N     1 
ATOM   1643 C  CA    . LEU A 1  211 ? 23.91506  10.36890  40.63922  1.000 23.84108  ? 241 LEU A CA    1 
ATOM   1644 C  C     . LEU A 1  211 ? 22.43510  10.74313  40.55442  1.000 25.39266  ? 241 LEU A C     1 
ATOM   1645 O  O     . LEU A 1  211 ? 22.01935  11.61522  41.30445  1.000 30.50046  ? 241 LEU A O     1 
ATOM   1646 C  CB    . LEU A 1  211 ? 24.36018  9.91087   42.02517  1.000 27.31865  ? 241 LEU A CB    1 
ATOM   1647 C  CG    . LEU A 1  211 ? 25.85916  9.65164   42.20597  1.000 30.21233  ? 241 LEU A CG    1 
ATOM   1648 C  CD1   . LEU A 1  211 ? 26.19031  9.31563   43.64594  1.000 25.16973  ? 241 LEU A CD1   1 
ATOM   1649 C  CD2   . LEU A 1  211 ? 26.33386  8.54554   41.28894  1.000 24.98434  ? 241 LEU A CD2   1 
ATOM   1650 N  N     . GLU A 1  212 ? 21.66288  10.07523  39.70554  1.000 29.44120  ? 242 GLU A N     1 
ATOM   1651 C  CA    . GLU A 1  212 ? 20.31392  10.56543  39.41771  1.000 24.71182  ? 242 GLU A CA    1 
ATOM   1652 C  C     . GLU A 1  212 ? 19.36305  10.35262  40.59185  1.000 22.82121  ? 242 GLU A C     1 
ATOM   1653 O  O     . GLU A 1  212 ? 18.48821  11.19376  40.83095  1.000 23.36547  ? 242 GLU A O     1 
ATOM   1654 C  CB    . GLU A 1  212 ? 19.78664  9.90248   38.13181  1.000 25.64432  ? 242 GLU A CB    1 
ATOM   1655 C  CG    . GLU A 1  212 ? 19.65940  8.36950   38.16687  1.000 26.08336  ? 242 GLU A CG    1 
ATOM   1656 C  CD    . GLU A 1  212 ? 18.35441  7.86872   38.83006  1.000 43.13229  ? 242 GLU A CD    1 
ATOM   1657 O  OE1   . GLU A 1  212 ? 17.31451  8.56988   38.72519  1.000 36.42935  ? 242 GLU A OE1   1 
ATOM   1658 O  OE2   . GLU A 1  212 ? 18.38033  6.79074   39.47609  1.000 37.31987  ? 242 GLU A OE2   1 
ATOM   1659 N  N     . ASP A 1  213 ? 19.53098  9.28061   41.35286  1.000 24.33115  ? 243 ASP A N     1 
ATOM   1660 C  CA    . ASP A 1  213 ? 18.63610  8.98279   42.50799  1.000 21.91921  ? 243 ASP A CA    1 
ATOM   1661 C  C     . ASP A 1  213 ? 18.87241  9.98878   43.64093  1.000 24.52414  ? 243 ASP A C     1 
ATOM   1662 O  O     . ASP A 1  213 ? 17.90256  10.38995  44.27505  1.000 22.45446  ? 243 ASP A O     1 
ATOM   1663 C  CB    . ASP A 1  213 ? 18.74193  7.52978   42.93602  1.000 28.80523  ? 243 ASP A CB    1 
ATOM   1664 C  CG    . ASP A 1  213 ? 20.12888  6.98357   43.23284  1.000 30.66406  ? 243 ASP A CG    1 
ATOM   1665 O  OD1   . ASP A 1  213 ? 21.12096  7.68541   42.96869  1.000 32.31721  ? 243 ASP A OD1   1 
ATOM   1666 O  OD2   . ASP A 1  213 ? 20.19777  5.84158   43.71387  1.000 41.03073  ? 243 ASP A OD2   1 
ATOM   1667 N  N     . VAL A 1  214 ? 20.11551  10.39959  43.86375  1.000 22.16746  ? 244 VAL A N     1 
ATOM   1668 C  CA    . VAL A 1  214 ? 20.40181  11.45758  44.87268  1.000 22.99719  ? 244 VAL A CA    1 
ATOM   1669 C  C     . VAL A 1  214 ? 19.82795  12.77765  44.32872  1.000 22.77647  ? 244 VAL A C     1 
ATOM   1670 O  O     . VAL A 1  214 ? 19.29418  13.54076  45.12777  1.000 23.15884  ? 244 VAL A O     1 
ATOM   1671 C  CB    . VAL A 1  214 ? 21.89788  11.56835  45.25047  1.000 22.50082  ? 244 VAL A CB    1 
ATOM   1672 C  CG1   . VAL A 1  214 ? 22.16920  12.71234  46.21440  1.000 22.72193  ? 244 VAL A CG1   1 
ATOM   1673 C  CG2   . VAL A 1  214 ? 22.43675  10.25928  45.80643  1.000 22.06922  ? 244 VAL A CG2   1 
ATOM   1674 N  N     . PHE A 1  215 ? 19.95480  13.02459  43.02169  1.000 23.18004  ? 245 PHE A N     1 
ATOM   1675 C  CA    . PHE A 1  215 ? 19.47594  14.31265  42.53172  1.000 23.70344  ? 245 PHE A CA    1 
ATOM   1676 C  C     . PHE A 1  215 ? 17.96499  14.43290  42.72693  1.000 28.13339  ? 245 PHE A C     1 
ATOM   1677 O  O     . PHE A 1  215 ? 17.45821  15.46899  43.19097  1.000 23.77646  ? 245 PHE A O     1 
ATOM   1678 C  CB    . PHE A 1  215 ? 19.83577  14.52156  41.06166  1.000 24.19670  ? 245 PHE A CB    1 
ATOM   1679 C  CG    . PHE A 1  215 ? 19.35190  15.84862  40.52469  1.000 24.79751  ? 245 PHE A CG    1 
ATOM   1680 C  CD1   . PHE A 1  215 ? 19.95415  17.02453  40.93958  1.000 26.93436  ? 245 PHE A CD1   1 
ATOM   1681 C  CD2   . PHE A 1  215 ? 18.26880  15.91776  39.67584  1.000 27.29418  ? 245 PHE A CD2   1 
ATOM   1682 C  CE1   . PHE A 1  215 ? 19.49328  18.27159  40.49260  1.000 25.98903  ? 245 PHE A CE1   1 
ATOM   1683 C  CE2   . PHE A 1  215 ? 17.80393  17.14382  39.20187  1.000 36.83124  ? 245 PHE A CE2   1 
ATOM   1684 C  CZ    . PHE A 1  215 ? 18.41717  18.32674  39.60975  1.000 26.02805  ? 245 PHE A CZ    1 
ATOM   1685 N  N     . VAL A 1  216 ? 17.23177  13.37300  42.39006  1.000 27.21535  ? 246 VAL A N     1 
ATOM   1686 C  CA    . VAL A 1  216 ? 15.78480  13.38424  42.61526  1.000 22.95317  ? 246 VAL A CA    1 
ATOM   1687 C  C     . VAL A 1  216 ? 15.48504  13.57533  44.10429  1.000 23.79594  ? 246 VAL A C     1 
ATOM   1688 O  O     . VAL A 1  216 ? 14.55721  14.30249  44.47340  1.000 25.49412  ? 246 VAL A O     1 
ATOM   1689 C  CB    . VAL A 1  216 ? 15.14052  12.09832  42.05338  1.000 27.22263  ? 246 VAL A CB    1 
ATOM   1690 C  CG1   . VAL A 1  216 ? 13.68057  11.99457  42.51059  1.000 26.45889  ? 246 VAL A CG1   1 
ATOM   1691 C  CG2   . VAL A 1  216 ? 15.25131  12.06726  40.52737  1.000 27.21445  ? 246 VAL A CG2   1 
ATOM   1692 N  N     . GLY A 1  217 ? 16.25306  12.93123  44.97721  1.000 28.80541  ? 247 GLY A N     1 
ATOM   1693 C  CA    . GLY A 1  217 ? 16.07729  13.15830  46.41222  1.000 22.20534  ? 247 GLY A CA    1 
ATOM   1694 C  C     . GLY A 1  217 ? 16.27658  14.61528  46.81115  1.000 24.52021  ? 247 GLY A C     1 
ATOM   1695 O  O     . GLY A 1  217 ? 15.52478  15.16343  47.63824  1.000 27.78483  ? 247 GLY A O     1 
ATOM   1696 N  N     . LEU A 1  218 ? 17.29960  15.26411  46.25499  1.000 23.09775  ? 248 LEU A N     1 
ATOM   1697 C  CA    . LEU A 1  218 ? 17.44887  16.70409  46.51393  1.000 29.80648  ? 248 LEU A CA    1 
ATOM   1698 C  C     . LEU A 1  218 ? 16.20693  17.48227  46.07408  1.000 26.93298  ? 248 LEU A C     1 
ATOM   1699 O  O     . LEU A 1  218 ? 15.76217  18.40336  46.76911  1.000 26.95136  ? 248 LEU A O     1 
ATOM   1700 C  CB    . LEU A 1  218 ? 18.69586  17.24687  45.82674  1.000 25.13783  ? 248 LEU A CB    1 
ATOM   1701 C  CG    . LEU A 1  218 ? 20.05786  16.79567  46.35857  1.000 25.89820  ? 248 LEU A CG    1 
ATOM   1702 C  CD1   . LEU A 1  218 ? 21.18080  17.24247  45.42640  1.000 24.65814  ? 248 LEU A CD1   1 
ATOM   1703 C  CD2   . LEU A 1  218 ? 20.28215  17.38568  47.77352  1.000 25.94334  ? 248 LEU A CD2   1 
ATOM   1704 N  N     . CYS A 1  219 ? 15.64971  17.13433  44.91017  1.000 25.75905  ? 249 CYS A N     1 
ATOM   1705 C  CA    . CYS A 1  219 ? 14.46576  17.84650  44.44531  1.000 24.47460  ? 249 CYS A CA    1 
ATOM   1706 C  C     . CYS A 1  219 ? 13.27285  17.59971  45.37748  1.000 25.86168  ? 249 CYS A C     1 
ATOM   1707 O  O     . CYS A 1  219 ? 12.53204  18.53384  45.70956  1.000 32.11172  ? 249 CYS A O     1 
ATOM   1708 C  CB    . CYS A 1  219 ? 14.12350  17.44551  43.00437  1.000 29.37745  ? 249 CYS A CB    1 
ATOM   1709 S  SG    . CYS A 1  219 ? 15.32840  17.91229  41.78119  1.000 26.64561  ? 249 CYS A SG    1 
ATOM   1710 N  N     . LEU A 1  220 ? 13.03670  16.34076  45.75955  1.000 29.25339  ? 250 LEU A N     1 
ATOM   1711 C  CA    . LEU A 1  220 ? 11.93678  16.02896  46.67771  1.000 26.93161  ? 250 LEU A CA    1 
ATOM   1712 C  C     . LEU A 1  220 ? 12.09408  16.76498  47.99367  1.000 28.30871  ? 250 LEU A C     1 
ATOM   1713 O  O     . LEU A 1  220 ? 11.11824  17.25315  48.58079  1.000 27.33076  ? 250 LEU A O     1 
ATOM   1714 C  CB    . LEU A 1  220 ? 11.87559  14.53498  46.95276  1.000 28.47371  ? 250 LEU A CB    1 
ATOM   1715 C  CG    . LEU A 1  220 ? 11.58928  13.63499  45.74883  1.000 27.55873  ? 250 LEU A CG    1 
ATOM   1716 C  CD1   . LEU A 1  220 ? 11.77412  12.19998  46.24585  1.000 22.10820  ? 250 LEU A CD1   1 
ATOM   1717 C  CD2   . LEU A 1  220 ? 10.17624  13.83520  45.23702  1.000 26.33626  ? 250 LEU A CD2   1 
ATOM   1718 N  N     . GLU A 1  221 ? 13.31616  16.82780  48.49550  1.000 25.92234  ? 251 GLU A N     1 
ATOM   1719 C  CA    . GLU A 1  221 ? 13.56345  17.56980  49.72644  1.000 27.70145  ? 251 GLU A CA    1 
ATOM   1720 C  C     . GLU A 1  221 ? 13.22766  19.04984  49.55445  1.000 30.98639  ? 251 GLU A C     1 
ATOM   1721 O  O     . GLU A 1  221 ? 12.62488  19.66096  50.44951  1.000 35.33869  ? 251 GLU A O     1 
ATOM   1722 C  CB    . GLU A 1  221 ? 15.01947  17.37858  50.12825  1.000 26.57923  ? 251 GLU A CB    1 
ATOM   1723 C  CG    . GLU A 1  221 ? 15.49577  18.27854  51.26116  1.000 36.08985  ? 251 GLU A CG    1 
ATOM   1724 C  CD    . GLU A 1  221 ? 16.93076  17.95732  51.57697  1.000 36.51295  ? 251 GLU A CD    1 
ATOM   1725 O  OE1   . GLU A 1  221 ? 17.81074  18.46416  50.84583  1.000 32.62134  ? 251 GLU A OE1   1 
ATOM   1726 O  OE2   . GLU A 1  221 ? 17.16676  17.14631  52.49696  1.000 31.64739  ? 251 GLU A OE2   1 
ATOM   1727 N  N     . ARG A 1  222 ? 13.60259  19.64175  48.41638  1.000 34.35583  ? 252 ARG A N     1 
ATOM   1728 C  CA    . ARG A 1  222 ? 13.26578  21.05380  48.20338  1.000 25.71459  ? 252 ARG A CA    1 
ATOM   1729 C  C     . ARG A 1  222 ? 11.75481  21.24203  48.16459  1.000 38.16995  ? 252 ARG A C     1 
ATOM   1730 O  O     . ARG A 1  222 ? 11.23603  22.28013  48.60263  1.000 45.53084  ? 252 ARG A O     1 
ATOM   1731 C  CB    . ARG A 1  222 ? 13.91769  21.56866  46.91528  1.000 31.53152  ? 252 ARG A CB    1 
ATOM   1732 C  CG    . ARG A 1  222 ? 13.50385  22.99871  46.45629  1.000 32.46982  ? 252 ARG A CG    1 
ATOM   1733 C  CD    . ARG A 1  222 ? 14.28312  24.12761  47.15815  1.000 30.77846  ? 252 ARG A CD    1 
ATOM   1734 N  NE    . ARG A 1  222 ? 15.69710  23.81439  47.36697  1.000 49.40228  ? 252 ARG A NE    1 
ATOM   1735 C  CZ    . ARG A 1  222 ? 16.69605  24.19821  46.57582  1.000 46.06971  ? 252 ARG A CZ    1 
ATOM   1736 N  NH1   . ARG A 1  222 ? 16.47902  24.92021  45.49183  1.000 32.61308  ? 252 ARG A NH1   1 
ATOM   1737 N  NH2   . ARG A 1  222 ? 17.95004  23.84902  46.88465  1.000 34.50522  ? 252 ARG A NH2   1 
ATOM   1738 N  N     . LEU A 1  223 ? 11.03958  20.22813  47.68571  1.000 35.96802  ? 253 LEU A N     1 
ATOM   1739 C  CA    . LEU A 1  223 ? 9.59056   20.22536  47.52691  1.000 31.94431  ? 253 LEU A CA    1 
ATOM   1740 C  C     . LEU A 1  223 ? 8.85268   19.83851  48.80603  1.000 32.24344  ? 253 LEU A C     1 
ATOM   1741 O  O     . LEU A 1  223 ? 7.61569   19.91071  48.83520  1.000 35.57526  ? 253 LEU A O     1 
ATOM   1742 C  CB    . LEU A 1  223 ? 9.24325   19.26538  46.38599  1.000 33.29706  ? 253 LEU A CB    1 
ATOM   1743 C  CG    . LEU A 1  223 ? 9.60313   19.73728  44.97893  1.000 35.37910  ? 253 LEU A CG    1 
ATOM   1744 C  CD1   . LEU A 1  223 ? 9.40181   18.62928  43.91899  1.000 27.40225  ? 253 LEU A CD1   1 
ATOM   1745 C  CD2   . LEU A 1  223 ? 8.78528   20.97440  44.62500  1.000 29.99450  ? 253 LEU A CD2   1 
ATOM   1746 N  N     . ASN A 1  224 ? 9.57676   19.44043  49.85094  1.000 29.29383  ? 254 ASN A N     1 
ATOM   1747 C  CA    . ASN A 1  224 ? 9.01286   18.96055  51.11203  1.000 38.58518  ? 254 ASN A CA    1 
ATOM   1748 C  C     . ASN A 1  224 ? 8.13363   17.71968  50.91919  1.000 49.38529  ? 254 ASN A C     1 
ATOM   1749 O  O     . ASN A 1  224 ? 7.20370   17.47185  51.70232  1.000 50.21486  ? 254 ASN A O     1 
ATOM   1750 C  CB    . ASN A 1  224 ? 8.24513   20.07669  51.83410  1.000 43.21394  ? 254 ASN A CB    1 
ATOM   1751 C  CG    . ASN A 1  224 ? 9.17237   21.20356  52.26794  1.000 47.20821  ? 254 ASN A CG    1 
ATOM   1752 O  OD1   . ASN A 1  224 ? 9.15846   22.28455  51.68991  1.000 60.07922  ? 254 ASN A OD1   1 
ATOM   1753 N  ND2   . ASN A 1  224 ? 10.00147  20.93946  53.26984  1.000 54.52710  ? 254 ASN A ND2   1 
ATOM   1754 N  N     . ILE A 1  225 ? 8.44837   16.91761  49.89817  1.000 42.04884  ? 255 ILE A N     1 
ATOM   1755 C  CA    . ILE A 1  225 ? 7.80813   15.62670  49.66129  1.000 26.66287  ? 255 ILE A CA    1 
ATOM   1756 C  C     . ILE A 1  225 ? 8.56907   14.56960  50.45022  1.000 31.47063  ? 255 ILE A C     1 
ATOM   1757 O  O     . ILE A 1  225 ? 9.78803   14.42441  50.30406  1.000 38.10766  ? 255 ILE A O     1 
ATOM   1758 C  CB    . ILE A 1  225 ? 7.78687   15.29666  48.15831  1.000 31.78148  ? 255 ILE A CB    1 
ATOM   1759 C  CG1   . ILE A 1  225 ? 6.91493   16.33177  47.42740  1.000 29.83987  ? 255 ILE A CG1   1 
ATOM   1760 C  CG2   . ILE A 1  225 ? 7.34161   13.84772  47.90841  1.000 35.14816  ? 255 ILE A CG2   1 
ATOM   1761 C  CD1   . ILE A 1  225 ? 6.98272   16.29372  45.89939  1.000 36.19141  ? 255 ILE A CD1   1 
ATOM   1762 N  N     . ARG A 1  226 ? 7.85708   13.84274  51.30734  1.000 35.47899  ? 256 ARG A N     1 
ATOM   1763 C  CA    . ARG A 1  226 ? 8.48305   12.87067  52.18328  1.000 42.44735  ? 256 ARG A CA    1 
ATOM   1764 C  C     . ARG A 1  226 ? 8.41474   11.47866  51.55833  1.000 37.13763  ? 256 ARG A C     1 
ATOM   1765 O  O     . ARG A 1  226 ? 7.39760   11.09580  50.97748  1.000 37.78632  ? 256 ARG A O     1 
ATOM   1766 C  CB    . ARG A 1  226 ? 7.80124   12.87281  53.55338  1.000 49.00389  ? 256 ARG A CB    1 
ATOM   1767 C  CG    . ARG A 1  226 ? 7.68454   14.26585  54.18835  1.000 60.68083  ? 256 ARG A CG    1 
ATOM   1768 C  CD    . ARG A 1  226 ? 8.66973   14.46373  55.33721  1.000 74.30052  ? 256 ARG A CD    1 
ATOM   1769 N  NE    . ARG A 1  226 ? 8.36503   15.66480  56.11622  1.000 97.54889  ? 256 ARG A NE    1 
ATOM   1770 C  CZ    . ARG A 1  226 ? 8.65523   15.82479  57.40117  1.000 95.11765  ? 256 ARG A CZ    1 
ATOM   1771 N  NH1   . ARG A 1  226 ? 9.27718   14.87871  58.09611  1.000 78.87256  ? 256 ARG A NH1   1 
ATOM   1772 N  NH2   . ARG A 1  226 ? 8.30549   16.95686  58.01019  1.000 93.44595  ? 256 ARG A NH2   1 
ATOM   1773 N  N     . LEU A 1  227 ? 9.51264   10.73749  51.66120  1.000 43.78068  ? 257 LEU A N     1 
ATOM   1774 C  CA    . LEU A 1  227 ? 9.50336   9.36048   51.19024  1.000 48.31297  ? 257 LEU A CA    1 
ATOM   1775 C  C     . LEU A 1  227 ? 8.62935   8.50864   52.09039  1.000 40.49817  ? 257 LEU A C     1 
ATOM   1776 O  O     . LEU A 1  227 ? 8.60654   8.69068   53.30839  1.000 43.28640  ? 257 LEU A O     1 
ATOM   1777 C  CB    . LEU A 1  227 ? 10.92226  8.76025   51.20006  1.000 28.50693  ? 257 LEU A CB    1 
ATOM   1778 C  CG    . LEU A 1  227 ? 12.02131  9.60606   50.56689  1.000 30.12617  ? 257 LEU A CG    1 
ATOM   1779 C  CD1   . LEU A 1  227 ? 13.33819  8.82486   50.59773  1.000 34.33977  ? 257 LEU A CD1   1 
ATOM   1780 C  CD2   . LEU A 1  227 ? 11.63317  9.96208   49.16293  1.000 36.11122  ? 257 LEU A CD2   1 
ATOM   1781 N  N     . GLU A 1  228 ? 7.94711   7.54373   51.49151  1.000 34.27940  ? 258 GLU A N     1 
ATOM   1782 C  CA    . GLU A 1  228 ? 7.16808   6.58788   52.32065  1.000 37.09932  ? 258 GLU A CA    1 
ATOM   1783 C  C     . GLU A 1  228 ? 7.34878   5.14783   51.82166  1.000 33.89789  ? 258 GLU A C     1 
ATOM   1784 O  O     . GLU A 1  228 ? 7.53259   4.96877   50.62264  1.000 31.77056  ? 258 GLU A O     1 
ATOM   1785 C  CB    . GLU A 1  228 ? 5.67614   6.90411   52.40084  1.000 36.27502  ? 258 GLU A CB    1 
ATOM   1786 C  CG    . GLU A 1  228 ? 5.07407   7.57417   51.17591  1.000 52.62756  ? 258 GLU A CG    1 
ATOM   1787 C  CD    . GLU A 1  228 ? 3.71221   8.15640   51.51608  1.000 74.12668  ? 258 GLU A CD    1 
ATOM   1788 O  OE1   . GLU A 1  228 ? 2.77311   7.36255   51.72623  1.000 71.84725  ? 258 GLU A OE1   1 
ATOM   1789 O  OE2   . GLU A 1  228 ? 3.58842   9.39542   51.58506  1.000 67.27139  ? 258 GLU A OE2   1 
ATOM   1790 N  N     . GLU A 1  229 ? 7.33975   4.18386   52.73869  1.000 32.75364  ? 259 GLU A N     1 
ATOM   1791 C  CA    . GLU A 1  229 ? 7.36848   2.76685   52.38573  1.000 37.02901  ? 259 GLU A CA    1 
ATOM   1792 C  C     . GLU A 1  229 ? 6.07232   2.36203   51.69792  1.000 30.28716  ? 259 GLU A C     1 
ATOM   1793 O  O     . GLU A 1  229 ? 4.98545   2.80421   52.07806  1.000 30.25268  ? 259 GLU A O     1 
ATOM   1794 C  CB    . GLU A 1  229 ? 7.57952   1.92585   53.63672  1.000 32.91077  ? 259 GLU A CB    1 
ATOM   1795 C  CG    . GLU A 1  229 ? 8.83869   2.29268   54.41054  1.000 38.86382  ? 259 GLU A CG    1 
ATOM   1796 C  CD    . GLU A 1  229 ? 10.08351  1.61646   53.86539  1.000 44.97925  ? 259 GLU A CD    1 
ATOM   1797 O  OE1   . GLU A 1  229 ? 9.96425   0.79545   52.93043  1.000 41.53355  ? 259 GLU A OE1   1 
ATOM   1798 O  OE2   . GLU A 1  229 ? 11.18162  1.89931   54.39023  1.000 55.01974  ? 259 GLU A OE2   1 
ATOM   1799 N  N     . LEU A 1  230 ? 6.19105   1.51898   50.66793  1.000 36.90600  ? 260 LEU A N     1 
ATOM   1800 C  CA    . LEU A 1  230 ? 5.00389   1.16315   49.90410  1.000 34.11604  ? 260 LEU A CA    1 
ATOM   1801 C  C     . LEU A 1  230 ? 4.08786   0.27032   50.72325  1.000 32.88453  ? 260 LEU A C     1 
ATOM   1802 O  O     . LEU A 1  230 ? 2.85987   0.39051   50.64442  1.000 31.83683  ? 260 LEU A O     1 
ATOM   1803 C  CB    . LEU A 1  230 ? 5.40660   0.47005   48.60207  1.000 28.74257  ? 260 LEU A CB    1 
ATOM   1804 C  CG    . LEU A 1  230 ? 4.28740   -0.01880  47.70124  1.000 33.06809  ? 260 LEU A CG    1 
ATOM   1805 C  CD1   . LEU A 1  230 ? 3.36152   1.14633   47.23633  1.000 25.07162  ? 260 LEU A CD1   1 
ATOM   1806 C  CD2   . LEU A 1  230 ? 4.83611   -0.79592  46.50518  1.000 23.26014  ? 260 LEU A CD2   1 
ATOM   1807 N  N     . HIS A 1  231 ? 4.67983   -0.60275  51.53820  1.000 30.67938  ? 261 HIS A N     1 
ATOM   1808 C  CA    . HIS A 1  231 ? 3.95076   -1.67062  52.19533  1.000 35.61489  ? 261 HIS A CA    1 
ATOM   1809 C  C     . HIS A 1  231 ? 4.61190   -1.95368  53.53525  1.000 42.71933  ? 261 HIS A C     1 
ATOM   1810 O  O     . HIS A 1  231 ? 5.74200   -1.52286  53.79608  1.000 43.25927  ? 261 HIS A O     1 
ATOM   1811 C  CB    . HIS A 1  231 ? 3.91244   -2.91464  51.29737  1.000 41.98732  ? 261 HIS A CB    1 
ATOM   1812 C  CG    . HIS A 1  231 ? 3.06833   -4.03449  51.82352  1.000 46.71267  ? 261 HIS A CG    1 
ATOM   1813 N  ND1   . HIS A 1  231 ? 3.60524   -5.15556  52.41648  1.000 49.85603  ? 261 HIS A ND1   1 
ATOM   1814 C  CD2   . HIS A 1  231 ? 1.72631   -4.21328  51.82571  1.000 35.43853  ? 261 HIS A CD2   1 
ATOM   1815 C  CE1   . HIS A 1  231 ? 2.63116   -5.97140  52.77464  1.000 50.27238  ? 261 HIS A CE1   1 
ATOM   1816 N  NE2   . HIS A 1  231 ? 1.48120   -5.42722  52.42678  1.000 46.99374  ? 261 HIS A NE2   1 
ATOM   1817 N  N     . SER A 1  232 ? 3.88890   -2.68055  54.39637  1.000 39.02723  ? 262 SER A N     1 
ATOM   1818 C  CA    . SER A 1  232 ? 4.43202   -3.05559  55.69530  1.000 44.89310  ? 262 SER A CA    1 
ATOM   1819 C  C     . SER A 1  232 ? 5.59185   -4.02278  55.57017  1.000 44.86629  ? 262 SER A C     1 
ATOM   1820 O  O     . SER A 1  232 ? 6.37496   -4.15688  56.51607  1.000 48.45533  ? 262 SER A O     1 
ATOM   1821 C  CB    . SER A 1  232 ? 3.33304   -3.67940  56.55947  1.000 45.57045  ? 262 SER A CB    1 
ATOM   1822 O  OG    . SER A 1  232 ? 2.48680   -4.51329  55.77762  1.000 57.26376  ? 262 SER A OG    1 
ATOM   1823 N  N     . GLN A 1  233 ? 5.71159   -4.70683  54.43618  1.000 53.35344  ? 263 GLN A N     1 
ATOM   1824 C  CA    . GLN A 1  233 ? 6.80240   -5.62001  54.13605  1.000 47.80095  ? 263 GLN A CA    1 
ATOM   1825 C  C     . GLN A 1  233 ? 7.67334   -5.03618  53.02291  1.000 39.58170  ? 263 GLN A C     1 
ATOM   1826 O  O     . GLN A 1  233 ? 7.18035   -4.27413  52.18696  1.000 49.94739  ? 263 GLN A O     1 
ATOM   1827 C  CB    . GLN A 1  233 ? 6.26913   -6.98994  53.69516  1.000 52.24832  ? 263 GLN A CB    1 
ATOM   1828 C  CG    . GLN A 1  233 ? 5.32316   -7.64576  54.69831  1.000 59.20770  ? 263 GLN A CG    1 
ATOM   1829 C  CD    . GLN A 1  233 ? 6.01329   -7.98983  55.99523  1.000 61.55214  ? 263 GLN A CD    1 
ATOM   1830 O  OE1   . GLN A 1  233 ? 7.10120   -8.56801  55.99010  1.000 55.76776  ? 263 GLN A OE1   1 
ATOM   1831 N  NE2   . GLN A 1  233 ? 5.40350   -7.61671  57.11730  1.000 63.97434  ? 263 GLN A NE2   1 
ATOM   1832 N  N     . PRO A 1  234 ? 8.96529   -5.35639  52.99974  1.000 37.97347  ? 264 PRO A N     1 
ATOM   1833 C  CA    . PRO A 1  234 ? 9.81521   -4.89755  51.89061  1.000 37.55493  ? 264 PRO A CA    1 
ATOM   1834 C  C     . PRO A 1  234 ? 9.32194   -5.44851  50.56170  1.000 38.04022  ? 264 PRO A C     1 
ATOM   1835 O  O     . PRO A 1  234 ? 8.90774   -6.60345  50.44979  1.000 32.95699  ? 264 PRO A O     1 
ATOM   1836 C  CB    . PRO A 1  234 ? 11.19917  -5.44776  52.24744  1.000 30.78609  ? 264 PRO A CB    1 
ATOM   1837 C  CG    . PRO A 1  234 ? 10.92212  -6.59069  53.20251  1.000 38.29986  ? 264 PRO A CG    1 
ATOM   1838 C  CD    . PRO A 1  234 ? 9.71030   -6.15947  53.98267  1.000 31.82902  ? 264 PRO A CD    1 
ATOM   1839 N  N     . THR A 1  235 ? 9.39193   -4.61355  49.53966  1.000 27.03054  ? 265 THR A N     1 
ATOM   1840 C  CA    . THR A 1  235 ? 8.95069   -4.97952  48.20174  1.000 23.68161  ? 265 THR A CA    1 
ATOM   1841 C  C     . THR A 1  235 ? 9.91459   -4.58471  47.09159  1.000 21.48772  ? 265 THR A C     1 
ATOM   1842 O  O     . THR A 1  235 ? 9.72237   -5.02871  45.94863  1.000 23.18576  ? 265 THR A O     1 
ATOM   1843 C  CB    . THR A 1  235 ? 7.58174   -4.35932  47.90691  1.000 31.95839  ? 265 THR A CB    1 
ATOM   1844 O  OG1   . THR A 1  235 ? 7.63600   -2.92632  48.11286  1.000 21.97972  ? 265 THR A OG1   1 
ATOM   1845 C  CG2   . THR A 1  235 ? 6.53077   -4.96512  48.83307  1.000 26.99800  ? 265 THR A CG2   1 
ATOM   1846 N  N     . PHE A 1  236 ? 10.93576  -3.77486  47.38743  1.000 27.49265  ? 266 PHE A N     1 
ATOM   1847 C  CA    . PHE A 1  236 ? 11.97469  -3.38205  46.43827  1.000 20.93914  ? 266 PHE A CA    1 
ATOM   1848 C  C     . PHE A 1  236 ? 13.30667  -3.94825  46.91710  1.000 20.76620  ? 266 PHE A C     1 
ATOM   1849 O  O     . PHE A 1  236 ? 13.66486  -3.77127  48.09005  1.000 20.50913  ? 266 PHE A O     1 
ATOM   1850 C  CB    . PHE A 1  236 ? 12.07892  -1.85207  46.35721  1.000 20.71791  ? 266 PHE A CB    1 
ATOM   1851 C  CG    . PHE A 1  236 ? 10.85995  -1.18389  45.80036  1.000 20.92613  ? 266 PHE A CG    1 
ATOM   1852 C  CD1   . PHE A 1  236 ? 9.75310   -0.92670  46.61351  1.000 21.01982  ? 266 PHE A CD1   1 
ATOM   1853 C  CD2   . PHE A 1  236 ? 10.82283  -0.79393  44.47136  1.000 21.07998  ? 266 PHE A CD2   1 
ATOM   1854 C  CE1   . PHE A 1  236 ? 8.64813   -0.27954  46.09964  1.000 21.27529  ? 266 PHE A CE1   1 
ATOM   1855 C  CE2   . PHE A 1  236 ? 9.70486   -0.13877  43.93949  1.000 21.29841  ? 266 PHE A CE2   1 
ATOM   1856 C  CZ    . PHE A 1  236 ? 8.60401   0.09943   44.75364  1.000 21.40841  ? 266 PHE A CZ    1 
ATOM   1857 N  N     . PHE A 1  237 ? 14.06145  -4.58539  46.02002  1.000 20.94085  ? 267 PHE A N     1 
ATOM   1858 C  CA    . PHE A 1  237 ? 15.25438  -5.34157  46.41488  1.000 20.91646  ? 267 PHE A CA    1 
ATOM   1859 C  C     . PHE A 1  237 ? 16.42731  -4.98578  45.50070  1.000 20.95323  ? 267 PHE A C     1 
ATOM   1860 O  O     . PHE A 1  237 ? 16.77707  -5.73286  44.57268  1.000 21.29191  ? 267 PHE A O     1 
ATOM   1861 C  CB    . PHE A 1  237 ? 14.92215  -6.84152  46.42897  1.000 21.29512  ? 267 PHE A CB    1 
ATOM   1862 C  CG    . PHE A 1  237 ? 13.88023  -7.18632  47.43812  1.000 21.33277  ? 267 PHE A CG    1 
ATOM   1863 C  CD1   . PHE A 1  237 ? 14.22938  -7.41134  48.76608  1.000 27.16092  ? 267 PHE A CD1   1 
ATOM   1864 C  CD2   . PHE A 1  237 ? 12.53918  -7.23712  47.09231  1.000 28.11061  ? 267 PHE A CD2   1 
ATOM   1865 C  CE1   . PHE A 1  237 ? 13.25847  -7.69516  49.71622  1.000 21.23095  ? 267 PHE A CE1   1 
ATOM   1866 C  CE2   . PHE A 1  237 ? 11.56626  -7.54194  48.03945  1.000 22.70296  ? 267 PHE A CE2   1 
ATOM   1867 C  CZ    . PHE A 1  237 ? 11.93141  -7.75996  49.35341  1.000 21.55645  ? 267 PHE A CZ    1 
ATOM   1868 N  N     . PRO A 1  238 ? 17.09353  -3.84388  45.77658  1.000 21.38102  ? 268 PRO A N     1 
ATOM   1869 C  CA    . PRO A 1  238 ? 18.27249  -3.38608  44.98240  1.000 22.96589  ? 268 PRO A CA    1 
ATOM   1870 C  C     . PRO A 1  238 ? 19.41335  -4.39026  45.09127  1.000 20.97244  ? 268 PRO A C     1 
ATOM   1871 O  O     . PRO A 1  238 ? 20.28622  -4.45842  44.21115  1.000 28.39314  ? 268 PRO A O     1 
ATOM   1872 C  CB    . PRO A 1  238 ? 18.55979  -2.01011  45.57632  1.000 20.50241  ? 268 PRO A CB    1 
ATOM   1873 C  CG    . PRO A 1  238 ? 17.27895  -1.59789  46.26249  1.000 22.36950  ? 268 PRO A CG    1 
ATOM   1874 C  CD    . PRO A 1  238 ? 16.78383  -2.85880  46.85759  1.000 23.11386  ? 268 PRO A CD    1 
ATOM   1875 N  N     . GLY A 1  239 ? 19.38937  -5.19023  46.13930  1.000 20.87492  ? 269 GLY A N     1 
ATOM   1876 C  CA    . GLY A 1  239 ? 20.44025  -6.18039  46.38718  1.000 21.07995  ? 269 GLY A CA    1 
ATOM   1877 C  C     . GLY A 1  239 ? 20.20994  -7.50137  45.69825  1.000 21.73452  ? 269 GLY A C     1 
ATOM   1878 O  O     . GLY A 1  239 ? 21.09681  -8.36051  45.69616  1.000 21.84407  ? 269 GLY A O     1 
ATOM   1879 N  N     . GLY A 1  240 ? 19.03983  -7.68920  45.11142  1.000 23.26478  ? 270 GLY A N     1 
ATOM   1880 C  CA    . GLY A 1  240 ? 18.71155  -8.95817  44.48150  1.000 26.10827  ? 270 GLY A CA    1 
ATOM   1881 C  C     . GLY A 1  240 ? 18.11553  -9.93005  45.48761  1.000 27.20799  ? 270 GLY A C     1 
ATOM   1882 O  O     . GLY A 1  240 ? 18.07474  -9.68100  46.70761  1.000 26.59313  ? 270 GLY A O     1 
ATOM   1883 N  N     . LEU A 1  241 ? 17.62828  -11.05498 44.96171  1.000 23.13725  ? 271 LEU A N     1 
ATOM   1884 C  CA    . LEU A 1  241 ? 16.92324  -12.04285 45.75784  1.000 23.02545  ? 271 LEU A CA    1 
ATOM   1885 C  C     . LEU A 1  241 ? 17.16494  -13.43590 45.20685  1.000 26.39892  ? 271 LEU A C     1 
ATOM   1886 O  O     . LEU A 1  241 ? 17.26574  -13.63396 43.99284  1.000 27.96003  ? 271 LEU A O     1 
ATOM   1887 C  CB    . LEU A 1  241 ? 15.40126  -11.83561 45.73004  1.000 24.94170  ? 271 LEU A CB    1 
ATOM   1888 C  CG    . LEU A 1  241 ? 14.78455  -10.65349 46.45110  1.000 31.55712  ? 271 LEU A CG    1 
ATOM   1889 C  CD1   . LEU A 1  241 ? 13.29451  -10.59227 46.06530  1.000 27.19211  ? 271 LEU A CD1   1 
ATOM   1890 C  CD2   . LEU A 1  241 ? 14.98773  -10.82148 47.95807  1.000 26.95063  ? 271 LEU A CD2   1 
ATOM   1891 N  N     . ARG A 1  242 ? 17.05491  -14.40786 46.10889  1.000 23.99768  ? 272 ARG A N     1 
ATOM   1892 C  CA    . ARG A 1  242 ? 17.03063  -15.81787 45.67394  1.000 24.80239  ? 272 ARG A CA    1 
ATOM   1893 C  C     . ARG A 1  242 ? 15.62852  -16.03467 45.10014  1.000 25.14725  ? 272 ARG A C     1 
ATOM   1894 O  O     . ARG A 1  242 ? 14.66166  -15.69049 45.77626  1.000 24.93422  ? 272 ARG A O     1 
ATOM   1895 C  CB    . ARG A 1  242 ? 17.33064  -16.77288 46.83192  1.000 25.04646  ? 272 ARG A CB    1 
ATOM   1896 C  CG    . ARG A 1  242 ? 17.04138  -18.25484 46.64700  1.000 25.95794  ? 272 ARG A CG    1 
ATOM   1897 C  CD    . ARG A 1  242 ? 17.04846  -18.93880 47.99702  1.000 26.08894  ? 272 ARG A CD    1 
ATOM   1898 N  NE    . ARG A 1  242 ? 17.50723  -20.32888 47.91600  1.000 46.25510  ? 272 ARG A NE    1 
ATOM   1899 C  CZ    . ARG A 1  242 ? 18.12426  -20.99295 48.87393  1.000 40.08329  ? 272 ARG A CZ    1 
ATOM   1900 N  NH1   . ARG A 1  242 ? 18.17450  -20.50092 50.09291  1.000 47.58493  ? 272 ARG A NH1   1 
ATOM   1901 N  NH2   . ARG A 1  242 ? 18.68204  -22.15404 48.59689  1.000 30.88727  ? 272 ARG A NH2   1 
ATOM   1902 N  N     . PHE A 1  243 ? 15.54127  -16.55369 43.89116  1.000 25.69716  ? 273 PHE A N     1 
ATOM   1903 C  CA    . PHE A 1  243 ? 14.26615  -16.69951 43.20434  1.000 26.05471  ? 273 PHE A CA    1 
ATOM   1904 C  C     . PHE A 1  243 ? 13.40405  -17.82735 43.76749  1.000 29.05617  ? 273 PHE A C     1 
ATOM   1905 O  O     . PHE A 1  243 ? 13.87491  -18.94142 44.01546  1.000 27.28183  ? 273 PHE A O     1 
ATOM   1906 C  CB    . PHE A 1  243 ? 14.47090  -16.97058 41.71932  1.000 26.51104  ? 273 PHE A CB    1 
ATOM   1907 C  CG    . PHE A 1  243 ? 13.17577  -17.19140 40.98251  1.000 26.94568  ? 273 PHE A CG    1 
ATOM   1908 C  CD1   . PHE A 1  243 ? 12.37389  -16.10328 40.61559  1.000 26.50814  ? 273 PHE A CD1   1 
ATOM   1909 C  CD2   . PHE A 1  243 ? 12.72452  -18.48334 40.67861  1.000 33.22455  ? 273 PHE A CD2   1 
ATOM   1910 C  CE1   . PHE A 1  243 ? 11.19077  -16.27912 39.97476  1.000 26.92315  ? 273 PHE A CE1   1 
ATOM   1911 C  CE2   . PHE A 1  243 ? 11.51040  -18.66316 40.02078  1.000 28.29989  ? 273 PHE A CE2   1 
ATOM   1912 C  CZ    . PHE A 1  243 ? 10.74652  -17.57305 39.66185  1.000 27.82748  ? 273 PHE A CZ    1 
ATOM   1913 N  N     . SER A 1  244 ? 12.11912  -17.53515 43.94766  1.000 26.72035  ? 274 SER A N     1 
ATOM   1914 C  CA    . SER A 1  244 ? 11.08797  -18.55998 44.01184  1.000 27.55128  ? 274 SER A CA    1 
ATOM   1915 C  C     . SER A 1  244 ? 9.79800   -17.93379 43.52400  1.000 27.54740  ? 274 SER A C     1 
ATOM   1916 O  O     . SER A 1  244 ? 9.60021   -16.72476 43.67199  1.000 26.84648  ? 274 SER A O     1 
ATOM   1917 C  CB    . SER A 1  244 ? 10.90807  -19.12991 45.41488  1.000 27.72279  ? 274 SER A CB    1 
ATOM   1918 O  OG    . SER A 1  244 ? 10.33434  -18.16680 46.27693  1.000 33.07676  ? 274 SER A OG    1 
ATOM   1919 N  N     . VAL A 1  245 ? 8.93279   -18.75867 42.92214  1.000 28.39537  ? 275 VAL A N     1 
ATOM   1920 C  CA    . VAL A 1  245 ? 7.64079   -18.27649 42.42030  1.000 33.52676  ? 275 VAL A CA    1 
ATOM   1921 C  C     . VAL A 1  245 ? 6.88506   -17.55733 43.52739  1.000 28.16709  ? 275 VAL A C     1 
ATOM   1922 O  O     . VAL A 1  245 ? 6.35721   -16.45226 43.33943  1.000 32.29212  ? 275 VAL A O     1 
ATOM   1923 C  CB    . VAL A 1  245 ? 6.81753   -19.45037 41.84245  1.000 29.65508  ? 275 VAL A CB    1 
ATOM   1924 C  CG1   . VAL A 1  245 ? 5.33157   -19.11414 41.77765  1.000 39.87679  ? 275 VAL A CG1   1 
ATOM   1925 C  CG2   . VAL A 1  245 ? 7.33628   -19.83750 40.45039  1.000 31.34234  ? 275 VAL A CG2   1 
ATOM   1926 N  N     . CYS A 1  246 ? 6.80712   -18.18329 44.70042  1.000 28.43619  ? 276 CYS A N     1 
ATOM   1927 C  CA    . CYS A 1  246 ? 5.91735   -17.64612 45.72352  1.000 28.30743  ? 276 CYS A CA    1 
ATOM   1928 C  C     . CYS A 1  246 ? 6.45963   -16.33819 46.29341  1.000 34.45008  ? 276 CYS A C     1 
ATOM   1929 O  O     . CYS A 1  246 ? 5.68482   -15.42906 46.59349  1.000 35.22856  ? 276 CYS A O     1 
ATOM   1930 C  CB    . CYS A 1  246 ? 5.67034   -18.68305 46.80959  1.000 33.53036  ? 276 CYS A CB    1 
ATOM   1931 S  SG    . CYS A 1  246 ? 4.65102   -20.07291 46.13677  1.000 53.84138  ? 276 CYS A SG    1 
ATOM   1932 N  N     . LEU A 1  247 ? 7.77967   -16.22139 46.43122  1.000 28.16017  ? 277 LEU A N     1 
ATOM   1933 C  CA    . LEU A 1  247 ? 8.36793   -14.92947 46.80711  1.000 28.31752  ? 277 LEU A CA    1 
ATOM   1934 C  C     . LEU A 1  247 ? 8.11294   -13.88146 45.73411  1.000 26.54216  ? 277 LEU A C     1 
ATOM   1935 O  O     . LEU A 1  247 ? 7.70916   -12.74239 46.03013  1.000 30.80125  ? 277 LEU A O     1 
ATOM   1936 C  CB    . LEU A 1  247 ? 9.87494   -15.08170 47.05990  1.000 25.36592  ? 277 LEU A CB    1 
ATOM   1937 C  CG    . LEU A 1  247 ? 10.57519  -13.75080 47.35277  1.000 32.22741  ? 277 LEU A CG    1 
ATOM   1938 C  CD1   . LEU A 1  247 ? 9.98146   -13.09867 48.61383  1.000 25.78419  ? 277 LEU A CD1   1 
ATOM   1939 C  CD2   . LEU A 1  247 ? 12.09518  -13.91504 47.45956  1.000 24.17881  ? 277 LEU A CD2   1 
ATOM   1940 N  N     . PHE A 1  248 ? 8.35671   -14.22854 44.47009  1.000 25.70045  ? 278 PHE A N     1 
ATOM   1941 C  CA    . PHE A 1  248 ? 8.29574   -13.18456 43.44907  1.000 25.34233  ? 278 PHE A CA    1 
ATOM   1942 C  C     . PHE A 1  248 ? 6.87177   -12.73134 43.18525  1.000 26.27009  ? 278 PHE A C     1 
ATOM   1943 O  O     . PHE A 1  248 ? 6.68787   -11.63733 42.65124  1.000 29.34166  ? 278 PHE A O     1 
ATOM   1944 C  CB    . PHE A 1  248 ? 8.96249   -13.62770 42.15499  1.000 25.58022  ? 278 PHE A CB    1 
ATOM   1945 C  CG    . PHE A 1  248 ? 10.44853  -13.33894 42.15277  1.000 25.10824  ? 278 PHE A CG    1 
ATOM   1946 C  CD1   . PHE A 1  248 ? 11.18664  -13.62802 43.28868  1.000 24.90334  ? 278 PHE A CD1   1 
ATOM   1947 C  CD2   . PHE A 1  248 ? 11.06548  -12.72106 41.07967  1.000 24.89893  ? 278 PHE A CD2   1 
ATOM   1948 C  CE1   . PHE A 1  248 ? 12.54569  -13.37823 43.34448  1.000 24.53826  ? 278 PHE A CE1   1 
ATOM   1949 C  CE2   . PHE A 1  248 ? 12.47853  -12.44328 41.14247  1.000 24.54919  ? 278 PHE A CE2   1 
ATOM   1950 C  CZ    . PHE A 1  248 ? 13.17764  -12.76636 42.27838  1.000 30.27441  ? 278 PHE A CZ    1 
ATOM   1951 N  N     . ARG A 1  249 ? 5.87170   -13.52617 43.58241  1.000 26.24928  ? 279 ARG A N     1 
ATOM   1952 C  CA    . ARG A 1  249 ? 4.50077   -13.02396 43.53358  1.000 29.62167  ? 279 ARG A CA    1 
ATOM   1953 C  C     . ARG A 1  249 ? 4.20109   -11.95188 44.56759  1.000 30.95473  ? 279 ARG A C     1 
ATOM   1954 O  O     . ARG A 1  249 ? 3.12717   -11.32871 44.48773  1.000 35.20125  ? 279 ARG A O     1 
ATOM   1955 C  CB    . ARG A 1  249 ? 3.50562   -14.17180 43.76076  1.000 29.48981  ? 279 ARG A CB    1 
ATOM   1956 C  CG    . ARG A 1  249 ? 3.27532   -15.08579 42.58781  1.000 33.82318  ? 279 ARG A CG    1 
ATOM   1957 C  CD    . ARG A 1  249 ? 2.30321   -16.16663 43.07098  1.000 35.27947  ? 279 ARG A CD    1 
ATOM   1958 N  NE    . ARG A 1  249 ? 2.06991   -17.22962 42.10404  1.000 49.20206  ? 279 ARG A NE    1 
ATOM   1959 C  CZ    . ARG A 1  249 ? 1.25478   -18.25748 42.33519  1.000 67.00350  ? 279 ARG A CZ    1 
ATOM   1960 N  NH1   . ARG A 1  249 ? 0.61192   -18.38435 43.48328  1.000 60.84716  ? 279 ARG A NH1   1 
ATOM   1961 N  NH2   . ARG A 1  249 ? 1.08551   -19.17748 41.38824  1.000 58.70003  ? 279 ARG A NH2   1 
ATOM   1962 N  N     . ARG A 1  250 ? 5.06825   -11.75099 45.56547  1.000 30.27413  ? 280 ARG A N     1 
ATOM   1963 C  CA    . ARG A 1  250 ? 4.76255   -10.80891 46.63148  1.000 32.68222  ? 280 ARG A CA    1 
ATOM   1964 C  C     . ARG A 1  250 ? 5.87873   -9.77808  46.78230  1.000 25.33418  ? 280 ARG A C     1 
ATOM   1965 O  O     . ARG A 1  250 ? 6.15796   -9.30009  47.88725  1.000 33.22948  ? 280 ARG A O     1 
ATOM   1966 C  CB    . ARG A 1  250 ? 4.49062   -11.53783 47.94754  1.000 26.51773  ? 280 ARG A CB    1 
ATOM   1967 C  CG    . ARG A 1  250 ? 5.66356   -12.34800 48.47540  1.000 41.65833  ? 280 ARG A CG    1 
ATOM   1968 C  CD    . ARG A 1  250 ? 5.32764   -13.03391 49.80947  1.000 50.60806  ? 280 ARG A CD    1 
ATOM   1969 N  NE    . ARG A 1  250 ? 6.51969   -13.38807 50.57632  1.000 61.85129  ? 280 ARG A NE    1 
ATOM   1970 C  CZ    . ARG A 1  250 ? 7.12650   -14.56917 50.53627  1.000 70.44265  ? 280 ARG A CZ    1 
ATOM   1971 N  NH1   . ARG A 1  250 ? 6.70823   -15.53713 49.73535  1.000 49.83512  ? 280 ARG A NH1   1 
ATOM   1972 N  NH2   . ARG A 1  250 ? 8.16957   -14.79031 51.33213  1.000 67.67832  ? 280 ARG A NH2   1 
ATOM   1973 N  N     . ILE A 1  251 ? 6.53263   -9.44122  45.68120  1.000 28.07326  ? 281 ILE A N     1 
ATOM   1974 C  CA    . ILE A 1  251 ? 7.50280   -8.33937  45.66003  1.000 24.53942  ? 281 ILE A CA    1 
ATOM   1975 C  C     . ILE A 1  251 ? 7.13879   -7.43835  44.49606  1.000 25.60399  ? 281 ILE A C     1 
ATOM   1976 O  O     . ILE A 1  251 ? 6.37460   -7.81925  43.61017  1.000 26.53138  ? 281 ILE A O     1 
ATOM   1977 C  CB    . ILE A 1  251 ? 8.96071   -8.82160  45.52185  1.000 23.08638  ? 281 ILE A CB    1 
ATOM   1978 C  CG1   . ILE A 1  251 ? 9.18642   -9.40768  44.12483  1.000 28.23278  ? 281 ILE A CG1   1 
ATOM   1979 C  CG2   . ILE A 1  251 ? 9.33971   -9.80263  46.66482  1.000 23.19226  ? 281 ILE A CG2   1 
ATOM   1980 C  CD1   . ILE A 1  251 ? 10.67733  -9.73692  43.82164  1.000 26.48438  ? 281 ILE A CD1   1 
ATOM   1981 N  N     . VAL A 1  252 ? 7.68998   -6.22743  44.50095  1.000 23.76069  ? 282 VAL A N     1 
ATOM   1982 C  CA    . VAL A 1  252 ? 7.52097   -5.29644  43.39594  1.000 23.91850  ? 282 VAL A CA    1 
ATOM   1983 C  C     . VAL A 1  252 ? 8.73184   -5.30666  42.46278  1.000 26.58109  ? 282 VAL A C     1 
ATOM   1984 O  O     . VAL A 1  252 ? 8.57967   -5.33667  41.24380  1.000 26.31069  ? 282 VAL A O     1 
ATOM   1985 C  CB    . VAL A 1  252 ? 7.25127   -3.87038  43.92994  1.000 24.79888  ? 282 VAL A CB    1 
ATOM   1986 C  CG1   . VAL A 1  252 ? 7.36127   -2.87543  42.78589  1.000 29.55329  ? 282 VAL A CG1   1 
ATOM   1987 C  CG2   . VAL A 1  252 ? 5.82537   -3.80414  44.56713  1.000 22.73788  ? 282 VAL A CG2   1 
ATOM   1988 N  N     . ALA A 1  253 ? 9.94992   -5.27783  43.00761  1.000 22.18970  ? 283 ALA A N     1 
ATOM   1989 C  CA    . ALA A 1  253 ? 11.10283  -5.07504  42.14144  1.000 22.08445  ? 283 ALA A CA    1 
ATOM   1990 C  C     . ALA A 1  253 ? 12.30479  -5.82521  42.66830  1.000 22.01323  ? 283 ALA A C     1 
ATOM   1991 O  O     . ALA A 1  253 ? 12.56196  -5.81722  43.87626  1.000 21.75314  ? 283 ALA A O     1 
ATOM   1992 C  CB    . ALA A 1  253 ? 11.47105  -3.57410  42.02035  1.000 21.75001  ? 283 ALA A CB    1 
ATOM   1993 N  N     . CYS A 1  254 ? 13.02256  -6.48935  41.75322  1.000 22.26143  ? 284 CYS A N     1 
ATOM   1994 C  CA    . CYS A 1  254 ? 14.25249  -7.18354  42.09507  1.000 22.27779  ? 284 CYS A CA    1 
ATOM   1995 C  C     . CYS A 1  254 ? 15.31940  -6.85573  41.05591  1.000 22.36335  ? 284 CYS A C     1 
ATOM   1996 O  O     . CYS A 1  254 ? 15.09321  -6.99673  39.84595  1.000 22.68350  ? 284 CYS A O     1 
ATOM   1997 C  CB    . CYS A 1  254 ? 14.01126  -8.70950  42.15015  1.000 22.74391  ? 284 CYS A CB    1 
ATOM   1998 S  SG    . CYS A 1  254 ? 15.45419  -9.66271  42.68897  1.000 22.85555  ? 284 CYS A SG    1 
ATOM   1999 N  N     . HIS A 1  255 ? 16.50352  -6.54791  41.56274  1.000 22.15509  ? 285 HIS A N     1 
ATOM   2000 C  CA    . HIS A 1  255 ? 17.66046  -6.18911  40.71157  1.000 22.35917  ? 285 HIS A CA    1 
ATOM   2001 C  C     . HIS A 1  255 ? 18.58124  -7.39026  40.47048  1.000 22.72473  ? 285 HIS A C     1 
ATOM   2002 O  O     . HIS A 1  255 ? 18.27614  -8.47420  40.97155  1.000 22.88453  ? 285 HIS A O     1 
ATOM   2003 C  CB    . HIS A 1  255 ? 18.40074  -5.04021  41.40943  1.000 21.92149  ? 285 HIS A CB    1 
ATOM   2004 C  CG    . HIS A 1  255 ? 19.45475  -4.30640  40.65627  1.000 26.37214  ? 285 HIS A CG    1 
ATOM   2005 N  ND1   . HIS A 1  255 ? 20.63789  -3.95757  41.26409  1.000 23.98826  ? 285 HIS A ND1   1 
ATOM   2006 C  CD2   . HIS A 1  255 ? 19.52665  -3.83444  39.41324  1.000 31.78476  ? 285 HIS A CD2   1 
ATOM   2007 C  CE1   . HIS A 1  255 ? 21.39487  -3.30771  40.40197  1.000 22.25801  ? 285 HIS A CE1   1 
ATOM   2008 N  NE2   . HIS A 1  255 ? 20.74173  -3.22064  39.27006  1.000 29.30407  ? 285 HIS A NE2   1 
ATOM   2009 N  N     . PHE A 1  256 ? 19.66717  -7.18246  39.71832  1.000 29.82211  ? 286 PHE A N     1 
ATOM   2010 C  CA    . PHE A 1  256 ? 20.68096  -8.23163  39.40921  1.000 23.47862  ? 286 PHE A CA    1 
ATOM   2011 C  C     . PHE A 1  256 ? 20.04867  -9.28855  38.52133  1.000 24.66979  ? 286 PHE A C     1 
ATOM   2012 O  O     . PHE A 1  256 ? 20.30051  -10.47459 38.71133  1.000 37.86792  ? 286 PHE A O     1 
ATOM   2013 C  CB    . PHE A 1  256 ? 21.33506  -8.70569  40.70613  1.000 24.75683  ? 286 PHE A CB    1 
ATOM   2014 C  CG    . PHE A 1  256 ? 22.16233  -7.61680  41.37099  1.000 29.31104  ? 286 PHE A CG    1 
ATOM   2015 C  CD1   . PHE A 1  256 ? 23.01135  -6.81396  40.62285  1.000 34.57309  ? 286 PHE A CD1   1 
ATOM   2016 C  CD2   . PHE A 1  256 ? 22.08155  -7.39275  42.73599  1.000 30.38693  ? 286 PHE A CD2   1 
ATOM   2017 C  CE1   . PHE A 1  256 ? 23.76459  -5.82606  41.22771  1.000 30.49483  ? 286 PHE A CE1   1 
ATOM   2018 C  CE2   . PHE A 1  256 ? 22.83779  -6.40285  43.33586  1.000 33.41409  ? 286 PHE A CE2   1 
ATOM   2019 C  CZ    . PHE A 1  256 ? 23.67481  -5.62201  42.58072  1.000 25.64119  ? 286 PHE A CZ    1 
ATOM   2020 N  N     . ILE A 1  257 ? 19.27160  -8.85846  37.53842  1.000 24.04081  ? 287 ILE A N     1 
ATOM   2021 C  CA    . ILE A 1  257 ? 18.52833  -9.83337  36.69155  1.000 26.65061  ? 287 ILE A CA    1 
ATOM   2022 C  C     . ILE A 1  257 ? 18.86316  -9.62146  35.20850  1.000 24.95014  ? 287 ILE A C     1 
ATOM   2023 O  O     . ILE A 1  257 ? 18.41123  -8.64241  34.60654  1.000 28.67030  ? 287 ILE A O     1 
ATOM   2024 C  CB    . ILE A 1  257 ? 17.02038  -9.83312  37.01676  1.000 24.32569  ? 287 ILE A CB    1 
ATOM   2025 C  CG1   . ILE A 1  257 ? 16.77644  -10.58804 38.31582  1.000 24.23715  ? 287 ILE A CG1   1 
ATOM   2026 C  CG2   . ILE A 1  257 ? 16.19013  -10.42002 35.87889  1.000 24.81895  ? 287 ILE A CG2   1 
ATOM   2027 C  CD1   . ILE A 1  257 ? 15.48159  -10.23882 39.01299  1.000 27.23583  ? 287 ILE A CD1   1 
ATOM   2028 N  N     . LYS A 1  258 ? 19.60393  -10.56660 34.65043  1.000 25.56616  ? 288 LYS A N     1 
ATOM   2029 C  CA    . LYS A 1  258 ? 19.99375  -10.50170 33.21937  1.000 29.21174  ? 288 LYS A CA    1 
ATOM   2030 C  C     . LYS A 1  258 ? 18.82656  -10.88954 32.30554  1.000 26.62763  ? 288 LYS A C     1 
ATOM   2031 O  O     . LYS A 1  258 ? 17.86653  -11.49038 32.78469  1.000 27.43095  ? 288 LYS A O     1 
ATOM   2032 C  CB    . LYS A 1  258 ? 21.23858  -11.37990 33.05022  1.000 26.71190  ? 288 LYS A CB    1 
ATOM   2033 C  CG    . LYS A 1  258 ? 21.00332  -12.85387 32.79330  1.000 33.32497  ? 288 LYS A CG    1 
ATOM   2034 C  CD    . LYS A 1  258 ? 22.28715  -13.55408 32.37614  1.000 33.02507  ? 288 LYS A CD    1 
ATOM   2035 C  CE    . LYS A 1  258 ? 22.52705  -14.82810 33.11015  1.000 41.58929  ? 288 LYS A CE    1 
ATOM   2036 N  NZ    . LYS A 1  258 ? 23.95702  -15.11732 33.21696  1.000 41.68167  ? 288 LYS A NZ    1 
ATOM   2037 N  N     . PRO A 1  259 ? 18.88543  -10.54259 31.00553  1.000 29.04222  ? 289 PRO A N     1 
ATOM   2038 C  CA    . PRO A 1  259 ? 17.77526  -10.79844 30.04269  1.000 30.72697  ? 289 PRO A CA    1 
ATOM   2039 C  C     . PRO A 1  259 ? 17.25704  -12.24036 30.07480  1.000 28.77908  ? 289 PRO A C     1 
ATOM   2040 O  O     . PRO A 1  259 ? 16.03303  -12.43116 30.21097  1.000 32.45265  ? 289 PRO A O     1 
ATOM   2041 C  CB    . PRO A 1  259 ? 18.38115  -10.34258 28.72159  1.000 27.30537  ? 289 PRO A CB    1 
ATOM   2042 C  CG    . PRO A 1  259 ? 19.38437  -9.28772  29.09842  1.000 26.98421  ? 289 PRO A CG    1 
ATOM   2043 C  CD    . PRO A 1  259 ? 20.01345  -9.83679  30.32235  1.000 26.86027  ? 289 PRO A CD    1 
ATOM   2044 N  N     . ARG A 1  260 ? 18.13587  -13.22850 29.95071  1.000 28.04027  ? 290 ARG A N     1 
ATOM   2045 C  CA    . ARG A 1  260 ? 17.71063  -14.65044 29.89181  1.000 31.31559  ? 290 ARG A CA    1 
ATOM   2046 C  C     . ARG A 1  260 ? 17.03775  -15.04629 31.21191  1.000 31.38998  ? 290 ARG A C     1 
ATOM   2047 O  O     . ARG A 1  260 ? 16.00164  -15.70913 31.15607  1.000 34.50830  ? 290 ARG A O     1 
ATOM   2048 C  CB    . ARG A 1  260 ? 18.92445  -15.52264 29.55266  1.000 32.36781  ? 290 ARG A CB    1 
ATOM   2049 C  CG    . ARG A 1  260 ? 18.70223  -17.02360 29.64074  1.000 43.80227  ? 290 ARG A CG    1 
ATOM   2050 C  CD    . ARG A 1  260 ? 17.98297  -17.53752 28.41185  1.000 47.55601  ? 290 ARG A CD    1 
ATOM   2051 N  NE    . ARG A 1  260 ? 16.53000  -17.55429 28.60805  1.000 71.15530  ? 290 ARG A NE    1 
ATOM   2052 C  CZ    . ARG A 1  260 ? 15.64489  -17.38418 27.64217  1.000 61.33728  ? 290 ARG A CZ    1 
ATOM   2053 N  NH1   . ARG A 1  260 ? 16.02681  -16.90527 26.47611  1.000 55.48560  ? 290 ARG A NH1   1 
ATOM   2054 N  NH2   . ARG A 1  260 ? 14.38087  -17.70097 27.84536  1.000 57.27563  ? 290 ARG A NH2   1 
ATOM   2055 N  N     . THR A 1  261 ? 17.61497  -14.64035 32.33582  1.000 27.85177  ? 291 THR A N     1 
ATOM   2056 C  CA    . THR A 1  261 ? 17.03111  -14.90222 33.66091  1.000 27.51239  ? 291 THR A CA    1 
ATOM   2057 C  C     . THR A 1  261 ? 15.63422  -14.30000 33.75708  1.000 27.10895  ? 291 THR A C     1 
ATOM   2058 O  O     . THR A 1  261 ? 14.77320  -14.95084 34.34222  1.000 29.41290  ? 291 THR A O     1 
ATOM   2059 C  CB    . THR A 1  261 ? 18.01734  -14.35634 34.69276  1.000 26.99449  ? 291 THR A CB    1 
ATOM   2060 O  OG1   . THR A 1  261 ? 19.21620  -15.10054 34.51561  1.000 30.06854  ? 291 THR A OG1   1 
ATOM   2061 C  CG2   . THR A 1  261 ? 17.52652  -14.49523 36.11783  1.000 26.59237  ? 291 THR A CG2   1 
ATOM   2062 N  N     . LEU A 1  262 ? 15.40533  -13.11698 33.18408  1.000 26.70022  ? 292 LEU A N     1 
ATOM   2063 C  CA    . LEU A 1  262 ? 14.08545  -12.43977 33.25024  1.000 26.34990  ? 292 LEU A CA    1 
ATOM   2064 C  C     . LEU A 1  262 ? 13.07021  -13.26263 32.45741  1.000 26.96731  ? 292 LEU A C     1 
ATOM   2065 O  O     . LEU A 1  262 ? 11.95425  -13.42644 32.93957  1.000 33.51419  ? 292 LEU A O     1 
ATOM   2066 C  CB    . LEU A 1  262 ? 14.18860  -10.99880 32.75319  1.000 25.87430  ? 292 LEU A CB    1 
ATOM   2067 C  CG    . LEU A 1  262 ? 12.88171  -10.21360 32.62735  1.000 34.07125  ? 292 LEU A CG    1 
ATOM   2068 C  CD1   . LEU A 1  262 ? 12.32494  -9.94147  34.00741  1.000 30.40209  ? 292 LEU A CD1   1 
ATOM   2069 C  CD2   . LEU A 1  262 ? 13.16181  -8.91666  31.89527  1.000 25.32440  ? 292 LEU A CD2   1 
ATOM   2070 N  N     . LEU A 1  263 ? 13.48897  -13.79573 31.31837  1.000 27.54491  ? 293 LEU A N     1 
ATOM   2071 C  CA    . LEU A 1  263 ? 12.60072  -14.64561 30.49351  1.000 30.69277  ? 293 LEU A CA    1 
ATOM   2072 C  C     . LEU A 1  263 ? 12.32761  -15.96755 31.22159  1.000 28.75395  ? 293 LEU A C     1 
ATOM   2073 O  O     . LEU A 1  263 ? 11.18254  -16.40337 31.21476  1.000 30.32263  ? 293 LEU A O     1 
ATOM   2074 C  CB    . LEU A 1  263 ? 13.25050  -14.82276 29.12443  1.000 28.72804  ? 293 LEU A CB    1 
ATOM   2075 C  CG    . LEU A 1  263 ? 13.46559  -13.53681 28.32536  1.000 30.11131  ? 293 LEU A CG    1 
ATOM   2076 C  CD1   . LEU A 1  263 ? 14.56042  -13.70502 27.29621  1.000 34.83749  ? 293 LEU A CD1   1 
ATOM   2077 C  CD2   . LEU A 1  263 ? 12.18357  -13.07863 27.67452  1.000 28.28384  ? 293 LEU A CD2   1 
ATOM   2078 N  N     . ASP A 1  264 ? 13.33462  -16.51269 31.89147  1.000 28.83946  ? 294 ASP A N     1 
ATOM   2079 C  CA    . ASP A 1  264 ? 13.17053  -17.77064 32.66453  1.000 34.18136  ? 294 ASP A CA    1 
ATOM   2080 C  C     . ASP A 1  264 ? 12.27273  -17.52346 33.88264  1.000 28.94532  ? 294 ASP A C     1 
ATOM   2081 O  O     . ASP A 1  264 ? 11.46064  -18.39333 34.18578  1.000 30.24736  ? 294 ASP A O     1 
ATOM   2082 C  CB    . ASP A 1  264 ? 14.51648  -18.38384 33.03436  1.000 29.61491  ? 294 ASP A CB    1 
ATOM   2083 C  CG    . ASP A 1  264 ? 15.41626  -18.77702 31.87724  1.000 32.99405  ? 294 ASP A CG    1 
ATOM   2084 O  OD1   . ASP A 1  264 ? 14.91309  -18.87097 30.74432  1.000 35.14568  ? 294 ASP A OD1   1 
ATOM   2085 O  OD2   . ASP A 1  264 ? 16.61426  -18.98320 32.12408  1.000 33.53781  ? 294 ASP A OD2   1 
ATOM   2086 N  N     . TYR A 1  265 ? 12.41000  -16.36347 34.52659  1.000 28.07970  ? 295 TYR A N     1 
ATOM   2087 C  CA    . TYR A 1  265 ? 11.53321  -16.07530 35.66270  1.000 29.56615  ? 295 TYR A CA    1 
ATOM   2088 C  C     . TYR A 1  265 ? 10.11018  -15.81008 35.19989  1.000 27.86126  ? 295 TYR A C     1 
ATOM   2089 O  O     . TYR A 1  265 ? 9.13721   -16.23991 35.84604  1.000 28.12654  ? 295 TYR A O     1 
ATOM   2090 C  CB    . TYR A 1  265 ? 12.02851  -14.86435 36.45560  1.000 26.81065  ? 295 TYR A CB    1 
ATOM   2091 C  CG    . TYR A 1  265 ? 13.29759  -15.04753 37.27443  1.000 26.59610  ? 295 TYR A CG    1 
ATOM   2092 C  CD1   . TYR A 1  265 ? 13.97441  -16.24763 37.31837  1.000 27.19094  ? 295 TYR A CD1   1 
ATOM   2093 C  CD2   . TYR A 1  265 ? 13.80486  -13.97458 38.00833  1.000 28.19340  ? 295 TYR A CD2   1 
ATOM   2094 C  CE1   . TYR A 1  265 ? 15.14149  -16.38079 38.08521  1.000 29.83289  ? 295 TYR A CE1   1 
ATOM   2095 C  CE2   . TYR A 1  265 ? 14.95395  -14.08874 38.76517  1.000 27.75571  ? 295 TYR A CE2   1 
ATOM   2096 C  CZ    . TYR A 1  265 ? 15.62476  -15.29385 38.80211  1.000 33.22975  ? 295 TYR A CZ    1 
ATOM   2097 O  OH    . TYR A 1  265 ? 16.77185  -15.39801 39.57196  1.000 32.99875  ? 295 TYR A OH    1 
ATOM   2098 N  N     . TRP A 1  266 ? 9.96815   -15.08009 34.09689  1.000 28.78765  ? 296 TRP A N     1 
ATOM   2099 C  CA    . TRP A 1  266 ? 8.64012   -14.80390 33.58206  1.000 27.90608  ? 296 TRP A CA    1 
ATOM   2100 C  C     . TRP A 1  266 ? 7.95386   -16.09980 33.16920  1.000 28.85207  ? 296 TRP A C     1 
ATOM   2101 O  O     . TRP A 1  266 ? 6.77687   -16.31261 33.48437  1.000 29.15627  ? 296 TRP A O     1 
ATOM   2102 C  CB    . TRP A 1  266 ? 8.73511   -13.82695 32.40602  1.000 27.64507  ? 296 TRP A CB    1 
ATOM   2103 C  CG    . TRP A 1  266 ? 7.44117   -13.15675 32.10318  1.000 41.38983  ? 296 TRP A CG    1 
ATOM   2104 C  CD1   . TRP A 1  266 ? 6.60999   -13.39765 31.04230  1.000 28.10628  ? 296 TRP A CD1   1 
ATOM   2105 C  CD2   . TRP A 1  266 ? 6.82844   -12.11864 32.86924  1.000 32.33302  ? 296 TRP A CD2   1 
ATOM   2106 N  NE1   . TRP A 1  266 ? 5.51813   -12.58348 31.11143  1.000 27.91516  ? 296 TRP A NE1   1 
ATOM   2107 C  CE2   . TRP A 1  266 ? 5.62441   -11.78847 32.22339  1.000 32.34527  ? 296 TRP A CE2   1 
ATOM   2108 C  CE3   . TRP A 1  266 ? 7.17871   -11.44666 34.04117  1.000 40.33796  ? 296 TRP A CE3   1 
ATOM   2109 C  CZ2   . TRP A 1  266 ? 4.77163   -10.79432 32.70448  1.000 33.66385  ? 296 TRP A CZ2   1 
ATOM   2110 C  CZ3   . TRP A 1  266 ? 6.32893   -10.45951 34.52126  1.000 41.79697  ? 296 TRP A CZ3   1 
ATOM   2111 C  CH2   . TRP A 1  266 ? 5.13989   -10.14334 33.84541  1.000 44.10725  ? 296 TRP A CH2   1 
ATOM   2112 N  N     . GLN A 1  267 ? 8.68762   -16.98694 32.49012  1.000 30.79912  ? 297 GLN A N     1 
ATOM   2113 C  CA    . GLN A 1  267 ? 8.13937   -18.29986 32.14324  1.000 30.41247  ? 297 GLN A CA    1 
ATOM   2114 C  C     . GLN A 1  267 ? 7.74342   -19.07876 33.39031  1.000 31.26749  ? 297 GLN A C     1 
ATOM   2115 O  O     . GLN A 1  267 ? 6.69832   -19.74560 33.41348  1.000 33.14506  ? 297 GLN A O     1 
ATOM   2116 C  CB    . GLN A 1  267 ? 9.15313   -19.09005 31.31812  1.000 38.73024  ? 297 GLN A CB    1 
ATOM   2117 C  CG    . GLN A 1  267 ? 8.62284   -20.41698 30.75523  1.000 44.09080  ? 297 GLN A CG    1 
ATOM   2118 C  CD    . GLN A 1  267 ? 7.49375   -20.18983 29.77938  1.000 60.69955  ? 297 GLN A CD    1 
ATOM   2119 O  OE1   . GLN A 1  267 ? 7.67870   -19.54889 28.74134  1.000 80.22937  ? 297 GLN A OE1   1 
ATOM   2120 N  NE2   . GLN A 1  267 ? 6.30471   -20.68663 30.11956  1.000 59.62476  ? 297 GLN A NE2   1 
ATOM   2121 N  N     . ALA A 1  268 ? 8.56957   -19.01886 34.44020  1.000 30.27898  ? 298 ALA A N     1 
ATOM   2122 C  CA    . ALA A 1  268 ? 8.24364   -19.70978 35.68726  1.000 30.54623  ? 298 ALA A CA    1 
ATOM   2123 C  C     . ALA A 1  268 ? 6.91279   -19.22755 36.24343  1.000 36.14030  ? 298 ALA A C     1 
ATOM   2124 O  O     . ALA A 1  268 ? 6.09173   -20.02441 36.70957  1.000 31.12266  ? 298 ALA A O     1 
ATOM   2125 C  CB    . ALA A 1  268 ? 9.33782   -19.46992 36.71910  1.000 29.93192  ? 298 ALA A CB    1 
ATOM   2126 N  N     . LEU A 1  269 ? 6.71800   -17.90952 36.27242  1.000 30.49751  ? 299 LEU A N     1 
ATOM   2127 C  CA    . LEU A 1  269 ? 5.47916   -17.37031 36.81458  1.000 32.71914  ? 299 LEU A CA    1 
ATOM   2128 C  C     . LEU A 1  269 ? 4.29298   -17.75015 35.93075  1.000 31.84803  ? 299 LEU A C     1 
ATOM   2129 O  O     . LEU A 1  269 ? 3.21800   -18.07196 36.44391  1.000 37.46359  ? 299 LEU A O     1 
ATOM   2130 C  CB    . LEU A 1  269 ? 5.59642   -15.84432 36.97952  1.000 28.53262  ? 299 LEU A CB    1 
ATOM   2131 C  CG    . LEU A 1  269 ? 6.67463   -15.45046 38.01335  1.000 36.70529  ? 299 LEU A CG    1 
ATOM   2132 C  CD1   . LEU A 1  269 ? 7.06985   -13.98453 37.93126  1.000 33.86162  ? 299 LEU A CD1   1 
ATOM   2133 C  CD2   . LEU A 1  269 ? 6.21677   -15.79535 39.41943  1.000 27.92265  ? 299 LEU A CD2   1 
ATOM   2134 N  N     . GLU A 1  270 ? 4.46780   -17.73921 34.60773  1.000 30.44813  ? 300 GLU A N     1 
ATOM   2135 C  CA    . GLU A 1  270 ? 3.40060   -18.23707 33.74289  1.000 35.00685  ? 300 GLU A CA    1 
ATOM   2136 C  C     . GLU A 1  270 ? 3.12240   -19.71902 33.99797  1.000 40.68768  ? 300 GLU A C     1 
ATOM   2137 O  O     . GLU A 1  270 ? 1.96035   -20.13583 34.08314  1.000 49.80931  ? 300 GLU A O     1 
ATOM   2138 C  CB    . GLU A 1  270 ? 3.74743   -18.01617 32.26983  1.000 39.73511  ? 300 GLU A CB    1 
ATOM   2139 C  CG    . GLU A 1  270 ? 3.44858   -16.61114 31.76883  1.000 59.71212  ? 300 GLU A CG    1 
ATOM   2140 C  CD    . GLU A 1  270 ? 1.96164   -16.28490 31.79903  1.000 82.19953  ? 300 GLU A CD    1 
ATOM   2141 O  OE1   . GLU A 1  270 ? 1.13946   -17.20478 31.57617  1.000 71.37307  ? 300 GLU A OE1   1 
ATOM   2142 O  OE2   . GLU A 1  270 ? 1.62286   -15.10884 32.05104  1.000 86.06674  ? 300 GLU A OE2   1 
ATOM   2143 N  N     . ASN A 1  271 ? 4.17729   -20.53318 34.11985  1.000 36.80635  ? 301 ASN A N     1 
ATOM   2144 C  CA    . ASN A 1  271 ? 3.98409   -21.98015 34.29492  1.000 35.70018  ? 301 ASN A CA    1 
ATOM   2145 C  C     . ASN A 1  271 ? 3.22421   -22.30799 35.56803  1.000 33.98673  ? 301 ASN A C     1 
ATOM   2146 O  O     . ASN A 1  271 ? 2.52306   -23.32288 35.62616  1.000 42.49515  ? 301 ASN A O     1 
ATOM   2147 C  CB    . ASN A 1  271 ? 5.33398   -22.71536 34.32275  1.000 34.88578  ? 301 ASN A CB    1 
ATOM   2148 C  CG    . ASN A 1  271 ? 6.02379   -22.72951 32.97266  1.000 44.02334  ? 301 ASN A CG    1 
ATOM   2149 O  OD1   . ASN A 1  271 ? 5.43571   -22.33444 31.96473  1.000 57.44334  ? 301 ASN A OD1   1 
ATOM   2150 N  ND2   . ASN A 1  271 ? 7.28071   -23.19671 32.94350  1.000 43.84252  ? 301 ASN A ND2   1 
ATOM   2151 N  N     . SER A 1  272 ? 3.37048   -21.49698 36.60999  1.000 39.80596  ? 302 SER A N     1 
ATOM   2152 C  CA    . SER A 1  272 ? 2.81262   -21.80786 37.92107  1.000 41.36156  ? 302 SER A CA    1 
ATOM   2153 C  C     . SER A 1  272 ? 1.56379   -20.99465 38.22722  1.000 37.78482  ? 302 SER A C     1 
ATOM   2154 O  O     . SER A 1  272 ? 1.05493   -21.04454 39.34929  1.000 47.53264  ? 302 SER A O     1 
ATOM   2155 C  CB    . SER A 1  272 ? 3.86780   -21.56399 39.00892  1.000 32.63992  ? 302 SER A CB    1 
ATOM   2156 O  OG    . SER A 1  272 ? 4.39899   -20.26308 38.84081  1.000 42.95871  ? 302 SER A OG    1 
ATOM   2157 N  N     . ARG A 1  273 ? 1.08678   -20.21360 37.27127  1.000 39.13923  ? 303 ARG A N     1 
ATOM   2158 C  CA    . ARG A 1  273 ? -0.15508  -19.49240 37.45442  1.000 44.08287  ? 303 ARG A CA    1 
ATOM   2159 C  C     . ARG A 1  273 ? -1.25920  -20.48722 37.77960  1.000 50.98231  ? 303 ARG A C     1 
ATOM   2160 O  O     . ARG A 1  273 ? -1.34445  -21.56022 37.16964  1.000 64.68644  ? 303 ARG A O     1 
ATOM   2161 C  CB    . ARG A 1  273 ? -0.45514  -18.69939 36.18143  1.000 48.23593  ? 303 ARG A CB    1 
ATOM   2162 C  CG    . ARG A 1  273 ? -1.87208  -18.20317 36.01862  1.000 72.09288  ? 303 ARG A CG    1 
ATOM   2163 C  CD    . ARG A 1  273 ? -2.06719  -17.65018 34.60263  1.000 79.10194  ? 303 ARG A CD    1 
ATOM   2164 N  NE    . ARG A 1  273 ? -1.25844  -18.37434 33.62254  1.000 76.25253  ? 303 ARG A NE    1 
ATOM   2165 C  CZ    . ARG A 1  273 ? -1.63870  -19.48430 32.99562  1.000 86.08456  ? 303 ARG A CZ    1 
ATOM   2166 N  NH1   . ARG A 1  273 ? -2.82476  -20.03211 33.20780  1.000 88.19596  ? 303 ARG A NH1   1 
ATOM   2167 N  NH2   . ARG A 1  273 ? -0.80391  -20.05946 32.13252  1.000 81.97445  ? 303 ARG A NH2   1 
ATOM   2168 N  N     . GLY A 1  274 ? -2.07001  -20.17406 38.78070  1.000 46.63513  ? 304 GLY A N     1 
ATOM   2169 C  CA    . GLY A 1  274 ? -3.10010  -21.10589 39.18487  1.000 60.89096  ? 304 GLY A CA    1 
ATOM   2170 C  C     . GLY A 1  274 ? -2.70010  -22.05692 40.28884  1.000 68.68422  ? 304 GLY A C     1 
ATOM   2171 O  O     . GLY A 1  274 ? -3.56214  -22.78777 40.79898  1.000 88.85759  ? 304 GLY A O     1 
ATOM   2172 N  N     . GLU A 1  275 ? -1.40507  -22.11112 40.56766  1.000 51.32050  ? 305 GLU A N     1 
ATOM   2173 C  CA    . GLU A 1  275 ? -0.95503  -22.90715 41.72063  1.000 54.09950  ? 305 GLU A CA    1 
ATOM   2174 C  C     . GLU A 1  275 ? -1.05272  -21.96610 42.91561  1.000 54.08123  ? 305 GLU A C     1 
ATOM   2175 O  O     . GLU A 1  275 ? -0.95955  -20.74612 42.73056  1.000 58.04141  ? 305 GLU A O     1 
ATOM   2176 C  CB    . GLU A 1  275 ? 0.45485   -23.45238 41.52045  1.000 61.24945  ? 305 GLU A CB    1 
ATOM   2177 C  CG    . GLU A 1  275 ? 0.56654   -24.38443 40.32146  1.000 63.94140  ? 305 GLU A CG    1 
ATOM   2178 C  CD    . GLU A 1  275 ? 1.30940   -25.63854 40.72039  1.000 64.56163  ? 305 GLU A CD    1 
ATOM   2179 O  OE1   . GLU A 1  275 ? 1.89055   -25.63260 41.82331  1.000 60.71617  ? 305 GLU A OE1   1 
ATOM   2180 O  OE2   . GLU A 1  275 ? 1.30214   -26.60756 39.93842  1.000 70.91775  ? 305 GLU A OE2   1 
ATOM   2181 N  N     . ASP A 1  276 ? -1.28165  -22.52703 44.08766  1.000 59.40180  ? 306 ASP A N     1 
ATOM   2182 C  CA    . ASP A 1  276 ? -1.45035  -21.67997 45.28366  1.000 63.89747  ? 306 ASP A CA    1 
ATOM   2183 C  C     . ASP A 1  276 ? -0.10623  -21.57316 45.98947  1.000 64.11986  ? 306 ASP A C     1 
ATOM   2184 O  O     . ASP A 1  276 ? 0.78460   -22.40431 45.74737  1.000 63.94291  ? 306 ASP A O     1 
ATOM   2185 C  CB    . ASP A 1  276 ? -2.54731  -22.22277 46.17783  1.000 76.39576  ? 306 ASP A CB    1 
ATOM   2186 C  CG    . ASP A 1  276 ? -3.95138  -22.13957 45.59702  1.000 98.62819  ? 306 ASP A CG    1 
ATOM   2187 O  OD1   . ASP A 1  276 ? -4.09644  -21.58258 44.48802  1.000 94.01144  ? 306 ASP A OD1   1 
ATOM   2188 O  OD2   . ASP A 1  276 ? -4.88936  -22.63340 46.25716  1.000 89.27566  ? 306 ASP A OD2   1 
ATOM   2189 N  N     . CYS A 1  277 ? 0.01904   -20.56116 46.82842  1.000 63.49936  ? 307 CYS A N     1 
ATOM   2190 C  CA    . CYS A 1  277 ? 1.27917   -20.38033 47.57524  1.000 71.93865  ? 307 CYS A CA    1 
ATOM   2191 C  C     . CYS A 1  277 ? 0.92439   -20.32924 49.05629  1.000 72.94234  ? 307 CYS A C     1 
ATOM   2192 O  O     . CYS A 1  277 ? -0.09847  -19.70306 49.39641  1.000 73.01718  ? 307 CYS A O     1 
ATOM   2193 C  CB    . CYS A 1  277 ? 1.99231   -19.11146 47.12511  1.000 58.46347  ? 307 CYS A CB    1 
ATOM   2194 S  SG    . CYS A 1  277 ? 2.87907   -19.29464 45.55899  1.000 62.04337  ? 307 CYS A SG    1 
ATOM   2195 N  N     . PRO A 1  278 ? 1.69541   -20.97533 49.94320  1.000 79.96401  ? 308 PRO A N     1 
ATOM   2196 C  CA    . PRO A 1  278 ? 1.45362   -20.86925 51.39523  1.000 80.08192  ? 308 PRO A CA    1 
ATOM   2197 C  C     . PRO A 1  278 ? 0.94189   -19.47116 51.69526  1.000 67.46411  ? 308 PRO A C     1 
ATOM   2198 O  O     . PRO A 1  278 ? 1.77401   -18.55430 51.52212  1.000 85.47001  ? 308 PRO A O     1 
ATOM   2199 C  CB    . PRO A 1  278 ? 2.82066   -21.15845 51.98405  1.000 87.80548  ? 308 PRO A CB    1 
ATOM   2200 C  CG    . PRO A 1  278 ? 3.39737   -22.18157 51.01900  1.000 75.86562  ? 308 PRO A CG    1 
ATOM   2201 C  CD    . PRO A 1  278 ? 2.86923   -21.85652 49.65807  1.000 70.53523  ? 308 PRO A CD    1 
ATOM   2202 N  N     . ASN B 1  13  ? 20.03565  29.11214  -8.81347  1.000 76.39185  ? 43  ASN B N     1 
ATOM   2203 C  CA    . ASN B 1  13  ? 19.18239  28.13528  -9.48336  1.000 74.10469  ? 43  ASN B CA    1 
ATOM   2204 C  C     . ASN B 1  13  ? 19.56051  26.69921  -9.14280  1.000 86.48306  ? 43  ASN B C     1 
ATOM   2205 O  O     . ASN B 1  13  ? 19.65195  26.32097  -7.97091  1.000 83.24450  ? 43  ASN B O     1 
ATOM   2206 C  CB    . ASN B 1  13  ? 19.23583  28.32060  -11.00034 1.000 76.66227  ? 43  ASN B CB    1 
ATOM   2207 C  CG    . ASN B 1  13  ? 18.08363  29.16071  -11.52273 1.000 91.51210  ? 43  ASN B CG    1 
ATOM   2208 O  OD1   . ASN B 1  13  ? 17.12591  29.43857  -10.79831 1.000 92.32431  ? 43  ASN B OD1   1 
ATOM   2209 N  ND2   . ASN B 1  13  ? 18.16216  29.55798  -12.79068 1.000 89.18882  ? 43  ASN B ND2   1 
ATOM   2210 N  N     . PHE B 1  14  ? 19.78212  25.89943  -10.18105 1.000 82.04193  ? 44  PHE B N     1 
ATOM   2211 C  CA    . PHE B 1  14  ? 19.89816  24.45740  -10.05339 1.000 81.23658  ? 44  PHE B CA    1 
ATOM   2212 C  C     . PHE B 1  14  ? 21.35817  24.02939  -10.02803 1.000 77.84564  ? 44  PHE B C     1 
ATOM   2213 O  O     . PHE B 1  14  ? 22.19290  24.57053  -10.75723 1.000 83.16297  ? 44  PHE B O     1 
ATOM   2214 C  CB    . PHE B 1  14  ? 19.16273  23.76364  -11.19926 1.000 67.89667  ? 44  PHE B CB    1 
ATOM   2215 C  CG    . PHE B 1  14  ? 17.66575  23.95064  -11.15866 1.000 64.55755  ? 44  PHE B CG    1 
ATOM   2216 C  CD1   . PHE B 1  14  ? 17.08057  25.10074  -11.64920 1.000 72.95302  ? 44  PHE B CD1   1 
ATOM   2217 C  CD2   . PHE B 1  14  ? 16.84894  22.96053  -10.63156 1.000 67.28569  ? 44  PHE B CD2   1 
ATOM   2218 C  CE1   . PHE B 1  14  ? 15.70458  25.26974  -11.61565 1.000 73.72491  ? 44  PHE B CE1   1 
ATOM   2219 C  CE2   . PHE B 1  14  ? 15.47495  23.12053  -10.59601 1.000 70.21223  ? 44  PHE B CE2   1 
ATOM   2220 C  CZ    . PHE B 1  14  ? 14.89977  24.27664  -11.09055 1.000 71.04309  ? 44  PHE B CZ    1 
ATOM   2221 N  N     . LEU B 1  15  ? 21.64948  23.04521  -9.17934  1.000 89.98199  ? 45  LEU B N     1 
ATOM   2222 C  CA    . LEU B 1  15  ? 22.99054  22.49317  -9.01196  1.000 91.42122  ? 45  LEU B CA    1 
ATOM   2223 C  C     . LEU B 1  15  ? 23.25617  21.34437  -9.98030  1.000 95.54966  ? 45  LEU B C     1 
ATOM   2224 O  O     . LEU B 1  15  ? 24.39101  21.15945  -10.42976 1.000 86.12383  ? 45  LEU B O     1 
ATOM   2225 C  CB    . LEU B 1  15  ? 23.18708  22.01187  -7.57113  1.000 86.19689  ? 45  LEU B CB    1 
ATOM   2226 C  CG    . LEU B 1  15  ? 22.61050  22.91164  -6.47173  1.000 90.52018  ? 45  LEU B CG    1 
ATOM   2227 C  CD1   . LEU B 1  15  ? 23.03701  22.42235  -5.09099  1.000 85.46510  ? 45  LEU B CD1   1 
ATOM   2228 C  CD2   . LEU B 1  15  ? 22.97943  24.38568  -6.67956  1.000 82.70902  ? 45  LEU B CD2   1 
ATOM   2229 N  N     . LYS B 1  16  ? 22.23106  20.55443  -10.28208 1.000 85.33903  ? 46  LYS B N     1 
ATOM   2230 C  CA    . LYS B 1  16  ? 22.30167  19.52065  -11.30432 1.000 79.38655  ? 46  LYS B CA    1 
ATOM   2231 C  C     . LYS B 1  16  ? 21.04835  19.62183  -12.15783 1.000 71.32340  ? 46  LYS B C     1 
ATOM   2232 O  O     . LYS B 1  16  ? 19.93755  19.72472  -11.62039 1.000 80.19668  ? 46  LYS B O     1 
ATOM   2233 C  CB    . LYS B 1  16  ? 22.41489  18.12252  -10.68865 1.000 85.51808  ? 46  LYS B CB    1 
ATOM   2234 C  CG    . LYS B 1  16  ? 23.72916  17.83636  -9.97221  1.000 80.47436  ? 46  LYS B CG    1 
ATOM   2235 C  CD    . LYS B 1  16  ? 23.80530  16.36328  -9.57954  1.000 84.32863  ? 46  LYS B CD    1 
ATOM   2236 C  CE    . LYS B 1  16  ? 25.14953  15.99914  -8.96012  1.000 94.56009  ? 46  LYS B CE    1 
ATOM   2237 N  NZ    . LYS B 1  16  ? 25.34904  16.62487  -7.62207  1.000 96.41159  ? 46  LYS B NZ    1 
ATOM   2238 N  N     . LEU B 1  17  ? 21.21985  19.60910  -13.47590 1.000 71.81347  ? 47  LEU B N     1 
ATOM   2239 C  CA    . LEU B 1  17  ? 20.10651  19.65430  -14.40147 1.000 80.36494  ? 47  LEU B CA    1 
ATOM   2240 C  C     . LEU B 1  17  ? 20.19314  18.47150  -15.35775 1.000 82.76761  ? 47  LEU B C     1 
ATOM   2241 O  O     . LEU B 1  17  ? 21.26293  18.21761  -15.93020 1.000 78.40084  ? 47  LEU B O     1 
ATOM   2242 C  CB    . LEU B 1  17  ? 20.09621  20.96947  -15.20519 1.000 75.16091  ? 47  LEU B CB    1 
ATOM   2243 C  CG    . LEU B 1  17  ? 19.33145  22.14235  -14.59766 1.000 77.14811  ? 47  LEU B CG    1 
ATOM   2244 C  CD1   . LEU B 1  17  ? 19.40211  23.35554  -15.50744 1.000 69.34535  ? 47  LEU B CD1   1 
ATOM   2245 C  CD2   . LEU B 1  17  ? 17.88554  21.74930  -14.35120 1.000 76.67478  ? 47  LEU B CD2   1 
ATOM   2246 N  N     . PRO B 1  18  ? 19.10607  17.72455  -15.54950 1.000 86.98370  ? 48  PRO B N     1 
ATOM   2247 C  CA    . PRO B 1  18  ? 19.11768  16.68176  -16.57572 1.000 83.16857  ? 48  PRO B CA    1 
ATOM   2248 C  C     . PRO B 1  18  ? 19.28916  17.30604  -17.95065 1.000 91.07347  ? 48  PRO B C     1 
ATOM   2249 O  O     . PRO B 1  18  ? 18.79407  18.40310  -18.22224 1.000 85.65187  ? 48  PRO B O     1 
ATOM   2250 C  CB    . PRO B 1  18  ? 17.75073  16.00273  -16.41635 1.000 90.28435  ? 48  PRO B CB    1 
ATOM   2251 C  CG    . PRO B 1  18  ? 16.88497  17.05461  -15.79180 1.000 80.80836  ? 48  PRO B CG    1 
ATOM   2252 C  CD    . PRO B 1  18  ? 17.79832  17.82641  -14.87498 1.000 83.31821  ? 48  PRO B CD    1 
ATOM   2253 N  N     . ASP B 1  19  ? 20.00984  16.59322  -18.80707 1.000 89.85035  ? 49  ASP B N     1 
ATOM   2254 C  CA    . ASP B 1  19  ? 20.35034  17.06750  -20.14410 1.000 89.83947  ? 49  ASP B CA    1 
ATOM   2255 C  C     . ASP B 1  19  ? 19.16599  16.79269  -21.06871 1.000 84.91691  ? 49  ASP B C     1 
ATOM   2256 O  O     . ASP B 1  19  ? 19.08774  15.75283  -21.71990 1.000 77.07660  ? 49  ASP B O     1 
ATOM   2257 C  CB    . ASP B 1  19  ? 21.61916  16.37659  -20.62772 1.000 93.15367  ? 49  ASP B CB    1 
ATOM   2258 C  CG    . ASP B 1  19  ? 22.33676  17.15581  -21.70083 1.000 87.45364  ? 49  ASP B CG    1 
ATOM   2259 O  OD1   . ASP B 1  19  ? 21.72955  18.08493  -22.27641 1.000 86.48880  ? 49  ASP B OD1   1 
ATOM   2260 O  OD2   . ASP B 1  19  ? 23.52066  16.84086  -21.95634 1.000 81.25217  ? 49  ASP B OD2   1 
ATOM   2261 N  N     . THR B 1  20  ? 18.22698  17.73571  -21.12216 1.000 82.07831  ? 50  THR B N     1 
ATOM   2262 C  CA    . THR B 1  20  ? 17.00169  17.53487  -21.88575 1.000 84.81936  ? 50  THR B CA    1 
ATOM   2263 C  C     . THR B 1  20  ? 16.62842  18.81003  -22.63034 1.000 81.49009  ? 50  THR B C     1 
ATOM   2264 O  O     . THR B 1  20  ? 16.99857  19.92095  -22.24125 1.000 79.20272  ? 50  THR B O     1 
ATOM   2265 C  CB    . THR B 1  20  ? 15.83503  17.11969  -20.98039 1.000 93.37422  ? 50  THR B CB    1 
ATOM   2266 O  OG1   . THR B 1  20  ? 14.72572  16.72487  -21.79906 1.000 91.52409  ? 50  THR B OG1   1 
ATOM   2267 C  CG2   . THR B 1  20  ? 15.41436  18.28251  -20.09399 1.000 80.29867  ? 50  THR B CG2   1 
ATOM   2268 N  N     . ASP B 1  21  ? 15.86801  18.62326  -23.71309 1.000 80.46571  ? 51  ASP B N     1 
ATOM   2269 C  CA    . ASP B 1  21  ? 15.34871  19.72243  -24.52767 1.000 79.81126  ? 51  ASP B CA    1 
ATOM   2270 C  C     . ASP B 1  21  ? 13.88860  19.39750  -24.82119 1.000 90.23164  ? 51  ASP B C     1 
ATOM   2271 O  O     . ASP B 1  21  ? 13.57622  18.73271  -25.81721 1.000 85.25031  ? 51  ASP B O     1 
ATOM   2272 C  CB    . ASP B 1  21  ? 16.16323  19.91669  -25.79994 1.000 84.33107  ? 51  ASP B CB    1 
ATOM   2273 C  CG    . ASP B 1  21  ? 15.81497  21.20385  -26.52754 1.000 99.07792  ? 51  ASP B CG    1 
ATOM   2274 O  OD1   . ASP B 1  21  ? 14.61895  21.55986  -26.58302 1.000 94.35319  ? 51  ASP B OD1   1 
ATOM   2275 O  OD2   . ASP B 1  21  ? 16.74578  21.85795  -27.03875 1.000 110.50509 ? 51  ASP B OD2   1 
ATOM   2276 N  N     . CYS B 1  22  ? 12.99293  19.86032  -23.94476 1.000 88.09026  ? 52  CYS B N     1 
ATOM   2277 C  CA    . CYS B 1  22  ? 11.57487  19.57936  -24.10028 1.000 79.55521  ? 52  CYS B CA    1 
ATOM   2278 C  C     . CYS B 1  22  ? 10.94844  20.36260  -25.24389 1.000 79.76595  ? 52  CYS B C     1 
ATOM   2279 O  O     . CYS B 1  22  ? 9.87326   19.98571  -25.71756 1.000 76.64693  ? 52  CYS B O     1 
ATOM   2280 C  CB    . CYS B 1  22  ? 10.83436  19.87809  -22.78994 1.000 75.01253  ? 52  CYS B CB    1 
ATOM   2281 S  SG    . CYS B 1  22  ? 11.20589  18.77480  -21.37731 1.000 89.60397  ? 52  CYS B SG    1 
ATOM   2282 N  N     . ARG B 1  23  ? 11.59128  21.43969  -25.69990 1.000 82.90531  ? 53  ARG B N     1 
ATOM   2283 C  CA    . ARG B 1  23  ? 11.03787  22.22093  -26.80153 1.000 79.19455  ? 53  ARG B CA    1 
ATOM   2284 C  C     . ARG B 1  23  ? 11.09737  21.43720  -28.11172 1.000 89.84058  ? 53  ARG B C     1 
ATOM   2285 O  O     . ARG B 1  23  ? 10.11909  21.40836  -28.86836 1.000 82.90351  ? 53  ARG B O     1 
ATOM   2286 C  CB    . ARG B 1  23  ? 11.77983  23.54795  -26.93054 1.000 85.49450  ? 53  ARG B CB    1 
ATOM   2287 C  CG    . ARG B 1  23  ? 11.12947  24.53515  -27.88309 1.000 85.73428  ? 53  ARG B CG    1 
ATOM   2288 C  CD    . ARG B 1  23  ? 11.39165  25.95905  -27.42289 1.000 100.14220 ? 53  ARG B CD    1 
ATOM   2289 N  NE    . ARG B 1  23  ? 12.81472  26.21501  -27.23537 1.000 118.34158 ? 53  ARG B NE    1 
ATOM   2290 C  CZ    . ARG B 1  23  ? 13.31300  27.19885  -26.49935 1.000 103.32649 ? 53  ARG B CZ    1 
ATOM   2291 N  NH1   . ARG B 1  23  ? 12.52926  28.03672  -25.84088 1.000 89.29473  ? 53  ARG B NH1   1 
ATOM   2292 N  NH2   . ARG B 1  23  ? 14.63304  27.33883  -26.41782 1.000 96.51949  ? 53  ARG B NH2   1 
ATOM   2293 N  N     . GLN B 1  24  ? 12.23726  20.79825  -28.39128 1.000 100.64289 ? 54  GLN B N     1 
ATOM   2294 C  CA    . GLN B 1  24  ? 12.35082  19.94850  -29.57350 1.000 94.65789  ? 54  GLN B CA    1 
ATOM   2295 C  C     . GLN B 1  24  ? 11.50387  18.69047  -29.42644 1.000 96.73299  ? 54  GLN B C     1 
ATOM   2296 O  O     . GLN B 1  24  ? 10.73752  18.33566  -30.33223 1.000 95.51530  ? 54  GLN B O     1 
ATOM   2297 C  CB    . GLN B 1  24  ? 13.81672  19.58654  -29.82512 1.000 93.10627  ? 54  GLN B CB    1 
ATOM   2298 C  CG    . GLN B 1  24  ? 14.05927  18.62679  -31.00342 1.000 104.36487 ? 54  GLN B CG    1 
ATOM   2299 C  CD    . GLN B 1  24  ? 13.98276  19.29807  -32.37225 1.000 108.66625 ? 54  GLN B CD    1 
ATOM   2300 O  OE1   . GLN B 1  24  ? 14.30071  20.48310  -32.52012 1.000 101.76620 ? 54  GLN B OE1   1 
ATOM   2301 N  NE2   . GLN B 1  24  ? 13.56538  18.53328  -33.38625 1.000 97.30045  ? 54  GLN B NE2   1 
ATOM   2302 N  N     . THR B 1  25  ? 11.62429  17.99923  -28.28763 1.000 92.30011  ? 55  THR B N     1 
ATOM   2303 C  CA    . THR B 1  25  ? 10.86839  16.78018  -28.01160 1.000 85.43292  ? 55  THR B CA    1 
ATOM   2304 C  C     . THR B 1  25  ? 9.99385   17.00693  -26.78323 1.000 85.95862  ? 55  THR B C     1 
ATOM   2305 O  O     . THR B 1  25  ? 10.38427  16.65469  -25.65645 1.000 92.66228  ? 55  THR B O     1 
ATOM   2306 C  CB    . THR B 1  25  ? 11.79146  15.57813  -27.81020 1.000 95.91791  ? 55  THR B CB    1 
ATOM   2307 O  OG1   . THR B 1  25  ? 12.76906  15.54535  -28.85757 1.000 105.37945 ? 55  THR B OG1   1 
ATOM   2308 C  CG2   . THR B 1  25  ? 10.98645  14.27514  -27.82017 1.000 80.52018  ? 55  THR B CG2   1 
ATOM   2309 N  N     . PRO B 1  26  ? 8.81179   17.59497  -26.95266 1.000 76.25029  ? 56  PRO B N     1 
ATOM   2310 C  CA    . PRO B 1  26  ? 7.89121   17.73974  -25.82629 1.000 73.38341  ? 56  PRO B CA    1 
ATOM   2311 C  C     . PRO B 1  26  ? 7.47440   16.37963  -25.29741 1.000 73.23965  ? 56  PRO B C     1 
ATOM   2312 O  O     . PRO B 1  26  ? 6.93012   15.54579  -26.04138 1.000 68.75569  ? 56  PRO B O     1 
ATOM   2313 C  CB    . PRO B 1  26  ? 6.69899   18.49087  -26.43668 1.000 67.50596  ? 56  PRO B CB    1 
ATOM   2314 C  CG    . PRO B 1  26  ? 6.79143   18.22018  -27.90277 1.000 69.15105  ? 56  PRO B CG    1 
ATOM   2315 C  CD    . PRO B 1  26  ? 8.25933   18.16823  -28.18933 1.000 69.78180  ? 56  PRO B CD    1 
ATOM   2316 N  N     . PRO B 1  27  ? 7.72088   16.10936  -24.01756 1.000 63.83516  ? 57  PRO B N     1 
ATOM   2317 C  CA    . PRO B 1  27  ? 7.27909   14.83725  -23.44166 1.000 64.75113  ? 57  PRO B CA    1 
ATOM   2318 C  C     . PRO B 1  27  ? 5.77418   14.82821  -23.21510 1.000 62.87296  ? 57  PRO B C     1 
ATOM   2319 O  O     . PRO B 1  27  ? 5.14527   15.86816  -22.98764 1.000 56.30407  ? 57  PRO B O     1 
ATOM   2320 C  CB    . PRO B 1  27  ? 8.04459   14.75597  -22.11496 1.000 62.64469  ? 57  PRO B CB    1 
ATOM   2321 C  CG    . PRO B 1  27  ? 8.32373   16.18689  -21.76177 1.000 58.56354  ? 57  PRO B CG    1 
ATOM   2322 C  CD    . PRO B 1  27  ? 8.48924   16.92316  -23.06068 1.000 59.92979  ? 57  PRO B CD    1 
ATOM   2323 N  N     . PHE B 1  28  ? 5.18814   13.63223  -23.30013 1.000 55.74963  ? 58  PHE B N     1 
ATOM   2324 C  CA    . PHE B 1  28  ? 3.78528   13.49316  -22.92963 1.000 45.56755  ? 58  PHE B CA    1 
ATOM   2325 C  C     . PHE B 1  28  ? 3.62184   13.34584  -21.42160 1.000 51.73606  ? 58  PHE B C     1 
ATOM   2326 O  O     . PHE B 1  28  ? 2.68406   13.89573  -20.83513 1.000 47.55733  ? 58  PHE B O     1 
ATOM   2327 C  CB    . PHE B 1  28  ? 3.15401   12.29931  -23.63264 1.000 45.49008  ? 58  PHE B CB    1 
ATOM   2328 C  CG    . PHE B 1  28  ? 1.77419   11.97221  -23.13619 1.000 50.61435  ? 58  PHE B CG    1 
ATOM   2329 C  CD1   . PHE B 1  28  ? 0.67201   12.64732  -23.62464 1.000 49.90832  ? 58  PHE B CD1   1 
ATOM   2330 C  CD2   . PHE B 1  28  ? 1.58055   10.99901  -22.17132 1.000 44.10541  ? 58  PHE B CD2   1 
ATOM   2331 C  CE1   . PHE B 1  28  ? -0.59582  12.35323  -23.16822 1.000 49.32520  ? 58  PHE B CE1   1 
ATOM   2332 C  CE2   . PHE B 1  28  ? 0.31272   10.69892  -21.70891 1.000 43.27542  ? 58  PHE B CE2   1 
ATOM   2333 C  CZ    . PHE B 1  28  ? -0.77646  11.37003  -22.20836 1.000 45.51910  ? 58  PHE B CZ    1 
ATOM   2334 N  N     . LEU B 1  29  ? 4.51408   12.59271  -20.78209 1.000 54.26519  ? 59  LEU B N     1 
ATOM   2335 C  CA    . LEU B 1  29  ? 4.43662   12.40141  -19.33810 1.000 43.54171  ? 59  LEU B CA    1 
ATOM   2336 C  C     . LEU B 1  29  ? 5.81685   12.57227  -18.73158 1.000 46.55345  ? 59  LEU B C     1 
ATOM   2337 O  O     . LEU B 1  29  ? 6.77568   11.91836  -19.15908 1.000 48.49501  ? 59  LEU B O     1 
ATOM   2338 C  CB    . LEU B 1  29  ? 3.85074   11.02834  -18.98917 1.000 42.90029  ? 59  LEU B CB    1 
ATOM   2339 C  CG    . LEU B 1  29  ? 3.67930   10.71603  -17.49617 1.000 46.97045  ? 59  LEU B CG    1 
ATOM   2340 C  CD1   . LEU B 1  29  ? 2.80557   11.75789  -16.80662 1.000 41.52895  ? 59  LEU B CD1   1 
ATOM   2341 C  CD2   . LEU B 1  29  ? 3.08936   9.31799   -17.31124 1.000 44.06077  ? 59  LEU B CD2   1 
ATOM   2342 N  N     . VAL B 1  30  ? 5.91522   13.46707  -17.74943 1.000 44.61619  ? 60  VAL B N     1 
ATOM   2343 C  CA    . VAL B 1  30  ? 7.14051   13.65990  -16.98385 1.000 51.59624  ? 60  VAL B CA    1 
ATOM   2344 C  C     . VAL B 1  30  ? 6.92303   13.11761  -15.58188 1.000 46.88125  ? 60  VAL B C     1 
ATOM   2345 O  O     . VAL B 1  30  ? 5.95829   13.49148  -14.90944 1.000 53.20312  ? 60  VAL B O     1 
ATOM   2346 C  CB    . VAL B 1  30  ? 7.55854   15.13989  -16.93070 1.000 47.50963  ? 60  VAL B CB    1 
ATOM   2347 C  CG1   . VAL B 1  30  ? 8.78388   15.30470  -16.02813 1.000 52.03535  ? 60  VAL B CG1   1 
ATOM   2348 C  CG2   . VAL B 1  30  ? 7.83001   15.67218  -18.32969 1.000 45.20061  ? 60  VAL B CG2   1 
ATOM   2349 N  N     . LEU B 1  31  ? 7.82520   12.24751  -15.13340 1.000 50.16219  ? 61  LEU B N     1 
ATOM   2350 C  CA    . LEU B 1  31  ? 7.77669   11.66724  -13.80251 1.000 47.97194  ? 61  LEU B CA    1 
ATOM   2351 C  C     . LEU B 1  31  ? 8.85402   12.34006  -12.95177 1.000 48.78789  ? 61  LEU B C     1 
ATOM   2352 O  O     . LEU B 1  31  ? 10.03388  12.33013  -13.31721 1.000 48.18793  ? 61  LEU B O     1 
ATOM   2353 C  CB    . LEU B 1  31  ? 7.98666   10.15325  -13.86290 1.000 43.66246  ? 61  LEU B CB    1 
ATOM   2354 C  CG    . LEU B 1  31  ? 7.02234   9.32643   -14.71571 1.000 45.03563  ? 61  LEU B CG    1 
ATOM   2355 C  CD1   . LEU B 1  31  ? 7.41432   7.85343   -14.73416 1.000 41.44531  ? 61  LEU B CD1   1 
ATOM   2356 C  CD2   . LEU B 1  31  ? 5.59052   9.48934   -14.24714 1.000 44.96400  ? 61  LEU B CD2   1 
ATOM   2357 N  N     . LEU B 1  32  ? 8.44044   12.94483  -11.83749 1.000 45.31536  ? 62  LEU B N     1 
ATOM   2358 C  CA    . LEU B 1  32  ? 9.35980   13.55062  -10.87871 1.000 41.08468  ? 62  LEU B CA    1 
ATOM   2359 C  C     . LEU B 1  32  ? 9.28727   12.72436  -9.60385  1.000 46.35927  ? 62  LEU B C     1 
ATOM   2360 O  O     . LEU B 1  32  ? 8.25253   12.71422  -8.92147  1.000 48.88283  ? 62  LEU B O     1 
ATOM   2361 C  CB    . LEU B 1  32  ? 8.99590   15.00757  -10.62427 1.000 41.21437  ? 62  LEU B CB    1 
ATOM   2362 C  CG    . LEU B 1  32  ? 8.89143   15.85684  -11.89905 1.000 44.83443  ? 62  LEU B CG    1 
ATOM   2363 C  CD1   . LEU B 1  32  ? 8.36155   17.23978  -11.60256 1.000 42.23304  ? 62  LEU B CD1   1 
ATOM   2364 C  CD2   . LEU B 1  32  ? 10.23817  15.93697  -12.59354 1.000 47.61372  ? 62  LEU B CD2   1 
ATOM   2365 N  N     . VAL B 1  33  ? 10.38039  12.03328  -9.27841  1.000 44.29498  ? 63  VAL B N     1 
ATOM   2366 C  CA    . VAL B 1  33  ? 10.41278  11.03306  -8.22363  1.000 49.15824  ? 63  VAL B CA    1 
ATOM   2367 C  C     . VAL B 1  33  ? 11.24022  11.55582  -7.06483  1.000 48.66205  ? 63  VAL B C     1 
ATOM   2368 O  O     . VAL B 1  33  ? 12.41316  11.90685  -7.23619  1.000 55.93448  ? 63  VAL B O     1 
ATOM   2369 C  CB    . VAL B 1  33  ? 10.99359  9.70617   -8.73112  1.000 42.67588  ? 63  VAL B CB    1 
ATOM   2370 C  CG1   . VAL B 1  33  ? 11.08600  8.69093   -7.60237  1.000 39.08155  ? 63  VAL B CG1   1 
ATOM   2371 C  CG2   . VAL B 1  33  ? 10.14615  9.17341   -9.89091  1.000 49.22141  ? 63  VAL B CG2   1 
ATOM   2372 N  N     . THR B 1  34  ? 10.64967  11.58457  -5.87460  1.000 45.76706  ? 64  THR B N     1 
ATOM   2373 C  CA    . THR B 1  34  ? 11.36112  12.00732  -4.67978  1.000 48.64372  ? 64  THR B CA    1 
ATOM   2374 C  C     . THR B 1  34  ? 12.08435  10.82318  -4.03630  1.000 58.15003  ? 64  THR B C     1 
ATOM   2375 O  O     . THR B 1  34  ? 11.52139  9.72916   -3.92931  1.000 53.84558  ? 64  THR B O     1 
ATOM   2376 C  CB    . THR B 1  34  ? 10.38950  12.64712  -3.68028  1.000 48.33874  ? 64  THR B CB    1 
ATOM   2377 O  OG1   . THR B 1  34  ? 9.33560   11.72906  -3.37908  1.000 53.12809  ? 64  THR B OG1   1 
ATOM   2378 C  CG2   . THR B 1  34  ? 9.77228   13.91424  -4.26179  1.000 53.63641  ? 64  THR B CG2   1 
ATOM   2379 N  N     . SER B 1  35  ? 13.33950  11.03410  -3.63872  1.000 60.64699  ? 65  SER B N     1 
ATOM   2380 C  CA    . SER B 1  35  ? 14.09677  10.00494  -2.92722  1.000 58.45806  ? 65  SER B CA    1 
ATOM   2381 C  C     . SER B 1  35  ? 15.28803  10.63879  -2.21954  1.000 61.66655  ? 65  SER B C     1 
ATOM   2382 O  O     . SER B 1  35  ? 15.76589  11.70887  -2.60849  1.000 63.94741  ? 65  SER B O     1 
ATOM   2383 C  CB    . SER B 1  35  ? 14.57341  8.89314   -3.86863  1.000 55.65460  ? 65  SER B CB    1 
ATOM   2384 O  OG    . SER B 1  35  ? 15.63810  9.32530   -4.69294  1.000 60.31482  ? 65  SER B OG    1 
ATOM   2385 N  N     . SER B 1  36  ? 15.75342  9.95557   -1.17285  1.000 64.80244  ? 66  SER B N     1 
ATOM   2386 C  CA    . SER B 1  36  ? 16.91372  10.37740  -0.40120  1.000 62.63117  ? 66  SER B CA    1 
ATOM   2387 C  C     . SER B 1  36  ? 18.20245  9.95854   -1.10277  1.000 71.25151  ? 66  SER B C     1 
ATOM   2388 O  O     . SER B 1  36  ? 18.20910  9.14774   -2.03494  1.000 71.56271  ? 66  SER B O     1 
ATOM   2389 C  CB    . SER B 1  36  ? 16.88924  9.77711   1.00368   1.000 60.93414  ? 66  SER B CB    1 
ATOM   2390 O  OG    . SER B 1  36  ? 15.63147  9.94099   1.62519   1.000 69.43587  ? 66  SER B OG    1 
ATOM   2391 N  N     . HIS B 1  37  ? 19.31663  10.50744  -0.61808  1.000 75.51646  ? 67  HIS B N     1 
ATOM   2392 C  CA    . HIS B 1  37  ? 20.61142  10.15355  -1.18563  1.000 73.55807  ? 67  HIS B CA    1 
ATOM   2393 C  C     . HIS B 1  37  ? 20.90947  8.66851   -1.02206  1.000 74.28241  ? 67  HIS B C     1 
ATOM   2394 O  O     . HIS B 1  37  ? 21.36512  8.00971   -1.96536  1.000 72.75394  ? 67  HIS B O     1 
ATOM   2395 C  CB    . HIS B 1  37  ? 21.70567  11.00341  -0.54387  1.000 74.82868  ? 67  HIS B CB    1 
ATOM   2396 C  CG    . HIS B 1  37  ? 21.60255  12.46048  -0.87053  1.000 79.43791  ? 67  HIS B CG    1 
ATOM   2397 N  ND1   . HIS B 1  37  ? 22.50325  13.10964  -1.68573  1.000 71.08945  ? 67  HIS B ND1   1 
ATOM   2398 C  CD2   . HIS B 1  37  ? 20.69169  13.39341  -0.50699  1.000 77.06447  ? 67  HIS B CD2   1 
ATOM   2399 C  CE1   . HIS B 1  37  ? 22.15821  14.37667  -1.80334  1.000 68.68058  ? 67  HIS B CE1   1 
ATOM   2400 N  NE2   . HIS B 1  37  ? 21.06047  14.57753  -1.09788  1.000 74.32015  ? 67  HIS B NE2   1 
ATOM   2401 N  N     . LYS B 1  38  ? 20.65292  8.11927   0.16593   1.000 74.28195  ? 68  LYS B N     1 
ATOM   2402 C  CA    . LYS B 1  38  ? 20.97201  6.72521   0.43652   1.000 84.10500  ? 68  LYS B CA    1 
ATOM   2403 C  C     . LYS B 1  38  ? 20.08173  5.74237   -0.31535  1.000 81.83404  ? 68  LYS B C     1 
ATOM   2404 O  O     . LYS B 1  38  ? 20.41870  4.55338   -0.37373  1.000 75.84611  ? 68  LYS B O     1 
ATOM   2405 C  CB    . LYS B 1  38  ? 20.87757  6.45490   1.93650   1.000 82.67029  ? 68  LYS B CB    1 
ATOM   2406 C  CG    . LYS B 1  38  ? 19.50680  6.73078   2.52407   1.000 84.73861  ? 68  LYS B CG    1 
ATOM   2407 C  CD    . LYS B 1  38  ? 19.52336  6.55447   4.02703   1.000 88.45102  ? 68  LYS B CD    1 
ATOM   2408 C  CE    . LYS B 1  38  ? 18.22659  7.02535   4.64861   1.000 84.38675  ? 68  LYS B CE    1 
ATOM   2409 N  NZ    . LYS B 1  38  ? 18.22415  6.82004   6.12157   1.000 105.94824 ? 68  LYS B NZ    1 
ATOM   2410 N  N     . GLN B 1  39  ? 18.96951  6.20550   -0.89184  1.000 86.13438  ? 69  GLN B N     1 
ATOM   2411 C  CA    . GLN B 1  39  ? 18.01027  5.30763   -1.52367  1.000 75.95410  ? 69  GLN B CA    1 
ATOM   2412 C  C     . GLN B 1  39  ? 18.41173  4.95093   -2.95089  1.000 68.28747  ? 69  GLN B C     1 
ATOM   2413 O  O     . GLN B 1  39  ? 17.57439  4.95912   -3.86058  1.000 73.44251  ? 69  GLN B O     1 
ATOM   2414 C  CB    . GLN B 1  39  ? 16.61728  5.93063   -1.49801  1.000 69.97325  ? 69  GLN B CB    1 
ATOM   2415 C  CG    . GLN B 1  39  ? 16.07681  6.14334   -0.09177  1.000 69.22858  ? 69  GLN B CG    1 
ATOM   2416 C  CD    . GLN B 1  39  ? 14.61082  6.53935   -0.07014  1.000 73.07253  ? 69  GLN B CD    1 
ATOM   2417 O  OE1   . GLN B 1  39  ? 14.25571  7.66941   -0.38677  1.000 74.18920  ? 69  GLN B OE1   1 
ATOM   2418 N  NE2   . GLN B 1  39  ? 13.75496  5.60027   0.30899   1.000 67.62102  ? 69  GLN B NE2   1 
ATOM   2419 N  N     . LEU B 1  40  ? 19.68966  4.61996   -3.15144  1.000 70.73826  ? 70  LEU B N     1 
ATOM   2420 C  CA    . LEU B 1  40  ? 20.15216  4.19723   -4.46770  1.000 66.99445  ? 70  LEU B CA    1 
ATOM   2421 C  C     . LEU B 1  40  ? 19.38697  2.97034   -4.96767  1.000 66.05756  ? 70  LEU B C     1 
ATOM   2422 O  O     . LEU B 1  40  ? 19.09652  2.85159   -6.16459  1.000 68.90226  ? 70  LEU B O     1 
ATOM   2423 C  CB    . LEU B 1  40  ? 21.65318  3.91022   -4.42332  1.000 65.43717  ? 70  LEU B CB    1 
ATOM   2424 C  CG    . LEU B 1  40  ? 22.29868  3.47049   -5.73366  1.000 80.44696  ? 70  LEU B CG    1 
ATOM   2425 C  CD1   . LEU B 1  40  ? 22.14529  4.56271   -6.77937  1.000 81.60859  ? 70  LEU B CD1   1 
ATOM   2426 C  CD2   . LEU B 1  40  ? 23.76076  3.11444   -5.52928  1.000 76.84378  ? 70  LEU B CD2   1 
ATOM   2427 N  N     . ALA B 1  41  ? 19.05430  2.04616   -4.06374  1.000 64.38434  ? 71  ALA B N     1 
ATOM   2428 C  CA    . ALA B 1  41  ? 18.32114  0.84824   -4.47471  1.000 71.53152  ? 71  ALA B CA    1 
ATOM   2429 C  C     . ALA B 1  41  ? 16.96092  1.20937   -5.06413  1.000 70.77661  ? 71  ALA B C     1 
ATOM   2430 O  O     . ALA B 1  41  ? 16.55153  0.65459   -6.09309  1.000 74.49584  ? 71  ALA B O     1 
ATOM   2431 C  CB    . ALA B 1  41  ? 18.16558  -0.11200  -3.29285  1.000 59.25168  ? 71  ALA B CB    1 
ATOM   2432 N  N     . GLU B 1  42  ? 16.24917  2.14524   -4.42366  1.000 69.63292  ? 72  GLU B N     1 
ATOM   2433 C  CA    . GLU B 1  42  ? 14.96797  2.60836   -4.95009  1.000 68.45914  ? 72  GLU B CA    1 
ATOM   2434 C  C     . GLU B 1  42  ? 15.10944  3.15065   -6.36503  1.000 61.30561  ? 72  GLU B C     1 
ATOM   2435 O  O     . GLU B 1  42  ? 14.35410  2.77185   -7.27182  1.000 73.78682  ? 72  GLU B O     1 
ATOM   2436 C  CB    . GLU B 1  42  ? 14.37732  3.68117   -4.03364  1.000 62.52462  ? 72  GLU B CB    1 
ATOM   2437 C  CG    . GLU B 1  42  ? 13.68278  3.15392   -2.79049  1.000 72.92721  ? 72  GLU B CG    1 
ATOM   2438 C  CD    . GLU B 1  42  ? 14.65618  2.64969   -1.72896  1.000 76.70755  ? 72  GLU B CD    1 
ATOM   2439 O  OE1   . GLU B 1  42  ? 15.88509  2.70073   -1.96341  1.000 69.86960  ? 72  GLU B OE1   1 
ATOM   2440 O  OE2   . GLU B 1  42  ? 14.17958  2.21047   -0.66287  1.000 66.04318  ? 72  GLU B OE2   1 
ATOM   2441 N  N     . ARG B 1  43  ? 16.05037  4.07669   -6.56719  1.000 53.94646  ? 73  ARG B N     1 
ATOM   2442 C  CA    . ARG B 1  43  ? 16.17288  4.70996   -7.87310  1.000 57.26715  ? 73  ARG B CA    1 
ATOM   2443 C  C     . ARG B 1  43  ? 16.60248  3.70818   -8.93647  1.000 67.46644  ? 73  ARG B C     1 
ATOM   2444 O  O     . ARG B 1  43  ? 16.11805  3.75642   -10.07128 1.000 63.86262  ? 73  ARG B O     1 
ATOM   2445 C  CB    . ARG B 1  43  ? 17.14492  5.88594   -7.80522  1.000 61.09166  ? 73  ARG B CB    1 
ATOM   2446 C  CG    . ARG B 1  43  ? 16.61322  7.06978   -7.01578  1.000 59.39270  ? 73  ARG B CG    1 
ATOM   2447 C  CD    . ARG B 1  43  ? 17.55720  8.26179   -7.06888  1.000 65.56690  ? 73  ARG B CD    1 
ATOM   2448 N  NE    . ARG B 1  43  ? 18.86442  7.94866   -6.49744  1.000 64.23340  ? 73  ARG B NE    1 
ATOM   2449 C  CZ    . ARG B 1  43  ? 19.17490  8.09639   -5.21652  1.000 65.12788  ? 73  ARG B CZ    1 
ATOM   2450 N  NH1   . ARG B 1  43  ? 18.29723  8.55522   -4.34110  1.000 57.45355  ? 73  ARG B NH1   1 
ATOM   2451 N  NH2   . ARG B 1  43  ? 20.39505  7.76730   -4.80205  1.000 57.94318  ? 73  ARG B NH2   1 
ATOM   2452 N  N     . MET B 1  44  ? 17.49561  2.78310   -8.58800  1.000 60.22516  ? 74  MET B N     1 
ATOM   2453 C  CA    . MET B 1  44  ? 17.88924  1.76130   -9.55236  1.000 63.78452  ? 74  MET B CA    1 
ATOM   2454 C  C     . MET B 1  44  ? 16.70510  0.87439   -9.92210  1.000 61.05591  ? 74  MET B C     1 
ATOM   2455 O  O     . MET B 1  44  ? 16.51765  0.53963   -11.10010 1.000 61.86873  ? 74  MET B O     1 
ATOM   2456 C  CB    . MET B 1  44  ? 19.04845  0.93918   -8.99197  1.000 71.96477  ? 74  MET B CB    1 
ATOM   2457 C  CG    . MET B 1  44  ? 20.33752  1.73014   -8.81129  1.000 71.31526  ? 74  MET B CG    1 
ATOM   2458 S  SD    . MET B 1  44  ? 20.75498  2.74444   -10.25423 1.000 84.81778  ? 74  MET B SD    1 
ATOM   2459 C  CE    . MET B 1  44  ? 20.63948  1.53571   -11.57644 1.000 59.38929  ? 74  MET B CE    1 
ATOM   2460 N  N     . ALA B 1  45  ? 15.89447  0.49418   -8.92988  1.000 56.71101  ? 75  ALA B N     1 
ATOM   2461 C  CA    . ALA B 1  45  ? 14.72435  -0.32675  -9.22161  1.000 52.09746  ? 75  ALA B CA    1 
ATOM   2462 C  C     . ALA B 1  45  ? 13.75502  0.41844   -10.12509 1.000 57.68164  ? 75  ALA B C     1 
ATOM   2463 O  O     . ALA B 1  45  ? 13.16167  -0.17536  -11.03599 1.000 54.33990  ? 75  ALA B O     1 
ATOM   2464 C  CB    . ALA B 1  45  ? 14.03884  -0.74302  -7.92444  1.000 48.42926  ? 75  ALA B CB    1 
ATOM   2465 N  N     . ILE B 1  46  ? 13.60211  1.71840   -9.90876  1.000 51.69495  ? 76  ILE B N     1 
ATOM   2466 C  CA    . ILE B 1  46  ? 12.62581  2.50257   -10.71823 1.000 53.12445  ? 76  ILE B CA    1 
ATOM   2467 C  C     . ILE B 1  46  ? 13.16127  2.59787   -12.15841 1.000 55.23041  ? 76  ILE B C     1 
ATOM   2468 O  O     . ILE B 1  46  ? 12.36591  2.42407   -13.09315 1.000 48.58747  ? 76  ILE B O     1 
ATOM   2469 C  CB    . ILE B 1  46  ? 12.37805  3.87644   -10.07485 1.000 46.13874  ? 76  ILE B CB    1 
ATOM   2470 C  CG1   . ILE B 1  46  ? 11.61254  3.75217   -8.76959  1.000 39.68263  ? 76  ILE B CG1   1 
ATOM   2471 C  CG2   . ILE B 1  46  ? 11.68569  4.82765   -11.04839 1.000 48.75890  ? 76  ILE B CG2   1 
ATOM   2472 C  CD1   . ILE B 1  46  ? 11.72788  4.97099   -7.87738  1.000 48.77867  ? 76  ILE B CD1   1 
ATOM   2473 N  N     . ARG B 1  47  ? 14.46621  2.81989   -12.30986 1.000 52.03320  ? 77  ARG B N     1 
ATOM   2474 C  CA    . ARG B 1  47  ? 15.07971  2.96317   -13.65306 1.000 58.88656  ? 77  ARG B CA    1 
ATOM   2475 C  C     . ARG B 1  47  ? 14.93240  1.66534   -14.46127 1.000 58.21442  ? 77  ARG B C     1 
ATOM   2476 O  O     . ARG B 1  47  ? 14.84894  1.75360   -15.69522 1.000 60.89278  ? 77  ARG B O     1 
ATOM   2477 C  CB    . ARG B 1  47  ? 16.56376  3.31013   -13.51054 1.000 59.59369  ? 77  ARG B CB    1 
ATOM   2478 C  CG    . ARG B 1  47  ? 16.89387  4.76607   -13.23136 1.000 65.47420  ? 77  ARG B CG    1 
ATOM   2479 C  CD    . ARG B 1  47  ? 18.36201  4.91199   -12.87488 1.000 68.09859  ? 77  ARG B CD    1 
ATOM   2480 N  NE    . ARG B 1  47  ? 18.71416  6.28091   -12.48973 1.000 70.97910  ? 77  ARG B NE    1 
ATOM   2481 C  CZ    . ARG B 1  47  ? 19.30559  6.60667   -11.35088 1.000 73.79469  ? 77  ARG B CZ    1 
ATOM   2482 N  NH1   . ARG B 1  47  ? 19.72589  5.66150   -10.53424 1.000 76.98791  ? 77  ARG B NH1   1 
ATOM   2483 N  NH2   . ARG B 1  47  ? 19.47471  7.87460   -11.03768 1.000 77.39172  ? 77  ARG B NH2   1 
ATOM   2484 N  N     . GLN B 1  48  ? 14.89964  0.51920   -13.78850 1.000 55.46572  ? 78  GLN B N     1 
ATOM   2485 C  CA    . GLN B 1  48  ? 14.79838  -0.78566  -14.48373 1.000 55.55338  ? 78  GLN B CA    1 
ATOM   2486 C  C     . GLN B 1  48  ? 13.33034  -1.20863  -14.57127 1.000 53.41730  ? 78  GLN B C     1 
ATOM   2487 O  O     . GLN B 1  48  ? 13.04907  -2.17848  -15.28336 1.000 63.21286  ? 78  GLN B O     1 
ATOM   2488 C  CB    . GLN B 1  48  ? 15.66666  -1.78182  -13.72926 1.000 59.37059  ? 78  GLN B CB    1 
ATOM   2489 C  CG    . GLN B 1  48  ? 17.13668  -1.38584  -13.66173 1.000 68.92582  ? 78  GLN B CG    1 
ATOM   2490 C  CD    . GLN B 1  48  ? 17.85412  -2.01409  -12.48813 1.000 74.94594  ? 78  GLN B CD    1 
ATOM   2491 O  OE1   . GLN B 1  48  ? 17.24543  -2.67826  -11.64104 1.000 74.28486  ? 78  GLN B OE1   1 
ATOM   2492 N  NE2   . GLN B 1  48  ? 19.15915  -1.80311  -12.42458 1.000 79.88334  ? 78  GLN B NE2   1 
ATOM   2493 N  N     . THR B 1  49  ? 12.44761  -0.52777  -13.85380 1.000 51.78719  ? 79  THR B N     1 
ATOM   2494 C  CA    . THR B 1  49  ? 10.99957  -0.79874  -13.97331 1.000 56.85323  ? 79  THR B CA    1 
ATOM   2495 C  C     . THR B 1  49  ? 10.22233  0.35139   -14.61278 1.000 53.45884  ? 79  THR B C     1 
ATOM   2496 O  O     . THR B 1  49  ? 10.47790  0.70664   -15.78480 1.000 52.68899  ? 79  THR B O     1 
ATOM   2497 C  CB    . THR B 1  49  ? 10.47109  -1.12503  -12.58018 1.000 53.20793  ? 79  THR B CB    1 
ATOM   2498 O  OG1   . THR B 1  49  ? 10.77939  0.01680   -11.79006 1.000 51.58648  ? 79  THR B OG1   1 
ATOM   2499 C  CG2   . THR B 1  49  ? 11.11430  -2.36815  -11.99668 1.000 52.72070  ? 79  THR B CG2   1 
ATOM   2500 N  N     . TRP B 1  50  ? 9.29762   0.96124   -13.87030 1.000 47.74337  ? 80  TRP B N     1 
ATOM   2501 C  CA    . TRP B 1  50  ? 8.39740   1.98737   -14.45675 1.000 52.11243  ? 80  TRP B CA    1 
ATOM   2502 C  C     . TRP B 1  50  ? 9.10525   3.27745   -14.87175 1.000 54.31863  ? 80  TRP B C     1 
ATOM   2503 O  O     . TRP B 1  50  ? 8.44702   4.11259   -15.49633 1.000 46.70909  ? 80  TRP B O     1 
ATOM   2504 C  CB    . TRP B 1  50  ? 7.24076   2.28818   -13.49426 1.000 47.26349  ? 80  TRP B CB    1 
ATOM   2505 C  CG    . TRP B 1  50  ? 7.60530   2.60888   -12.07333 1.000 50.46227  ? 80  TRP B CG    1 
ATOM   2506 C  CD1   . TRP B 1  50  ? 7.72768   1.73266   -11.03555 1.000 48.88237  ? 80  TRP B CD1   1 
ATOM   2507 C  CD2   . TRP B 1  50  ? 7.82451   3.91876   -11.52114 1.000 45.48477  ? 80  TRP B CD2   1 
ATOM   2508 N  NE1   . TRP B 1  50  ? 8.03712   2.40542   -9.88353  1.000 46.54320  ? 80  TRP B NE1   1 
ATOM   2509 C  CE2   . TRP B 1  50  ? 8.09803   3.74448   -10.14927 1.000 42.21959  ? 80  TRP B CE2   1 
ATOM   2510 C  CE3   . TRP B 1  50  ? 7.82632   5.21387   -12.05387 1.000 40.51987  ? 80  TRP B CE3   1 
ATOM   2511 C  CZ2   . TRP B 1  50  ? 8.36835   4.81930   -9.30615  1.000 39.84388  ? 80  TRP B CZ2   1 
ATOM   2512 C  CZ3   . TRP B 1  50  ? 8.09364   6.26970   -11.21675 1.000 40.70815  ? 80  TRP B CZ3   1 
ATOM   2513 C  CH2   . TRP B 1  50  ? 8.35914   6.07242   -9.86389  1.000 39.03503  ? 80  TRP B CH2   1 
ATOM   2514 N  N     . GLY B 1  51  ? 10.38337  3.43338   -14.55520 1.000 53.67104  ? 81  GLY B N     1 
ATOM   2515 C  CA    . GLY B 1  51  ? 11.05526  4.70344   -14.85818 1.000 54.16180  ? 81  GLY B CA    1 
ATOM   2516 C  C     . GLY B 1  51  ? 11.82278  4.63571   -16.15849 1.000 64.58708  ? 81  GLY B C     1 
ATOM   2517 O  O     . GLY B 1  51  ? 12.23960  5.69881   -16.64642 1.000 64.81819  ? 81  GLY B O     1 
ATOM   2518 N  N     . LYS B 1  52  ? 12.01957  3.43382   -16.69181 1.000 64.55729  ? 82  LYS B N     1 
ATOM   2519 C  CA    . LYS B 1  52  ? 12.69908  3.29309   -18.00309 1.000 67.75407  ? 82  LYS B CA    1 
ATOM   2520 C  C     . LYS B 1  52  ? 11.98170  4.18030   -19.02764 1.000 70.14029  ? 82  LYS B C     1 
ATOM   2521 O  O     . LYS B 1  52  ? 10.80059  3.91337   -19.31325 1.000 66.69958  ? 82  LYS B O     1 
ATOM   2522 C  CB    . LYS B 1  52  ? 12.70489  1.84419   -18.48640 1.000 64.71085  ? 82  LYS B CB    1 
ATOM   2523 C  CG    . LYS B 1  52  ? 13.83653  1.48038   -19.42390 1.000 68.50277  ? 82  LYS B CG    1 
ATOM   2524 C  CD    . LYS B 1  52  ? 13.95546  -0.02559  -19.60426 1.000 73.68203  ? 82  LYS B CD    1 
ATOM   2525 C  CE    . LYS B 1  52  ? 14.48592  -0.68384  -18.37759 1.000 62.46184  ? 82  LYS B CE    1 
ATOM   2526 N  NZ    . LYS B 1  52  ? 15.86202  -0.25990  -18.12102 1.000 86.49492  ? 82  LYS B NZ    1 
ATOM   2527 N  N     . GLU B 1  53  ? 12.68151  5.19041   -19.54269 1.000 75.57783  ? 83  GLU B N     1 
ATOM   2528 C  CA    . GLU B 1  53  ? 12.08415  6.08961   -20.52128 1.000 74.78195  ? 83  GLU B CA    1 
ATOM   2529 C  C     . GLU B 1  53  ? 11.80865  5.36689   -21.83433 1.000 67.32371  ? 83  GLU B C     1 
ATOM   2530 O  O     . GLU B 1  53  ? 12.52150  4.42896   -22.21279 1.000 69.99082  ? 83  GLU B O     1 
ATOM   2531 C  CB    . GLU B 1  53  ? 12.99306  7.29166   -20.75637 1.000 65.66958  ? 83  GLU B CB    1 
ATOM   2532 C  CG    . GLU B 1  53  ? 13.23554  8.11540   -19.50629 1.000 72.81643  ? 83  GLU B CG    1 
ATOM   2533 C  CD    . GLU B 1  53  ? 14.05544  9.35645   -19.77734 1.000 78.81346  ? 83  GLU B CD    1 
ATOM   2534 O  OE1   . GLU B 1  53  ? 14.63503  9.44668   -20.88354 1.000 79.33054  ? 83  GLU B OE1   1 
ATOM   2535 O  OE2   . GLU B 1  53  ? 14.11778  10.24227  -18.89218 1.000 68.08153  ? 83  GLU B OE2   1 
ATOM   2536 N  N     . ARG B 1  54  ? 10.76439  5.80204   -22.52685 1.000 66.42583  ? 84  ARG B N     1 
ATOM   2537 C  CA    . ARG B 1  54  ? 10.32095  5.05628   -23.69384 1.000 63.08940  ? 84  ARG B CA    1 
ATOM   2538 C  C     . ARG B 1  54  ? 9.12071   5.74742   -24.33224 1.000 64.09446  ? 84  ARG B C     1 
ATOM   2539 O  O     . ARG B 1  54  ? 8.58891   6.74032   -23.81884 1.000 68.20254  ? 84  ARG B O     1 
ATOM   2540 C  CB    . ARG B 1  54  ? 9.96208   3.62121   -23.32100 1.000 57.80702  ? 84  ARG B CB    1 
ATOM   2541 C  CG    . ARG B 1  54  ? 8.93050   3.53498   -22.21163 1.000 57.35628  ? 84  ARG B CG    1 
ATOM   2542 C  CD    . ARG B 1  54  ? 8.67765   2.10190   -21.79083 1.000 67.71331  ? 84  ARG B CD    1 
ATOM   2543 N  NE    . ARG B 1  54  ? 7.84510   2.03265   -20.59154 1.000 73.45486  ? 84  ARG B NE    1 
ATOM   2544 C  CZ    . ARG B 1  54  ? 6.54910   1.75666   -20.59511 1.000 82.36249  ? 84  ARG B CZ    1 
ATOM   2545 N  NH1   . ARG B 1  54  ? 5.89667   1.50389   -21.72192 1.000 72.18642  ? 84  ARG B NH1   1 
ATOM   2546 N  NH2   . ARG B 1  54  ? 5.89253   1.73042   -19.44287 1.000 83.95490  ? 84  ARG B NH2   1 
ATOM   2547 N  N     . MET B 1  55  ? 8.70229   5.18966   -25.46520 1.000 65.52732  ? 85  MET B N     1 
ATOM   2548 C  CA    . MET B 1  55  ? 7.47304   5.59480   -26.13066 1.000 69.48523  ? 85  MET B CA    1 
ATOM   2549 C  C     . MET B 1  55  ? 6.33821   4.70271   -25.65142 1.000 76.86318  ? 85  MET B C     1 
ATOM   2550 O  O     . MET B 1  55  ? 6.47322   3.47570   -25.61572 1.000 73.56590  ? 85  MET B O     1 
ATOM   2551 C  CB    . MET B 1  55  ? 7.61947   5.50912   -27.64973 1.000 72.81054  ? 85  MET B CB    1 
ATOM   2552 C  CG    . MET B 1  55  ? 8.39424   6.66724   -28.26278 1.000 78.29424  ? 85  MET B CG    1 
ATOM   2553 S  SD    . MET B 1  55  ? 7.50128   8.23323   -28.19712 1.000 96.43022  ? 85  MET B SD    1 
ATOM   2554 C  CE    . MET B 1  55  ? 8.70901   9.33738   -28.91834 1.000 84.48885  ? 85  MET B CE    1 
ATOM   2555 N  N     . VAL B 1  56  ? 5.22736   5.33064   -25.27787 1.000 98.05525  ? 86  VAL B N     1 
ATOM   2556 C  CA    . VAL B 1  56  ? 4.03955   4.66754   -24.76556 1.000 102.86144 ? 86  VAL B CA    1 
ATOM   2557 C  C     . VAL B 1  56  ? 2.89021   5.11173   -25.66404 1.000 97.66598  ? 86  VAL B C     1 
ATOM   2558 O  O     . VAL B 1  56  ? 2.42825   6.25471   -25.56863 1.000 95.29439  ? 86  VAL B O     1 
ATOM   2559 C  CB    . VAL B 1  56  ? 3.77010   5.03123   -23.29738 1.000 94.79168  ? 86  VAL B CB    1 
ATOM   2560 C  CG1   . VAL B 1  56  ? 2.59930   4.22912   -22.75011 1.000 83.78545  ? 86  VAL B CG1   1 
ATOM   2561 C  CG2   . VAL B 1  56  ? 5.02141   4.82105   -22.45390 1.000 86.12835  ? 86  VAL B CG2   1 
ATOM   2562 N  N     . LYS B 1  57  ? 2.43988   4.21691   -26.54305 1.000 99.15877  ? 87  LYS B N     1 
ATOM   2563 C  CA    . LYS B 1  57  ? 1.39851   4.54712   -27.52160 1.000 91.54099  ? 87  LYS B CA    1 
ATOM   2564 C  C     . LYS B 1  57  ? 1.78522   5.78429   -28.32148 1.000 84.31607  ? 87  LYS B C     1 
ATOM   2565 O  O     . LYS B 1  57  ? 0.94510   6.63936   -28.63299 1.000 88.72538  ? 87  LYS B O     1 
ATOM   2566 C  CB    . LYS B 1  57  ? 0.04277   4.74199   -26.83605 1.000 94.34870  ? 87  LYS B CB    1 
ATOM   2567 C  CG    . LYS B 1  57  ? -0.39090  3.58680   -25.94512 1.000 90.29473  ? 87  LYS B CG    1 
ATOM   2568 C  CD    . LYS B 1  57  ? -1.10820  2.49597   -26.72508 1.000 78.51985  ? 87  LYS B CD    1 
ATOM   2569 C  CE    . LYS B 1  57  ? -1.57285  1.39278   -25.78614 1.000 86.28800  ? 87  LYS B CE    1 
ATOM   2570 N  NZ    . LYS B 1  57  ? -2.51410  0.43391   -26.42498 1.000 83.30087  ? 87  LYS B NZ    1 
ATOM   2571 N  N     . GLY B 1  58  ? 3.07209   5.89035   -28.65594 1.000 83.18004  ? 88  GLY B N     1 
ATOM   2572 C  CA    . GLY B 1  58  ? 3.56982   7.02750   -29.39989 1.000 81.83224  ? 88  GLY B CA    1 
ATOM   2573 C  C     . GLY B 1  58  ? 3.78713   8.29334   -28.59671 1.000 84.11824  ? 88  GLY B C     1 
ATOM   2574 O  O     . GLY B 1  58  ? 4.05691   9.34346   -29.19359 1.000 75.94112  ? 88  GLY B O     1 
ATOM   2575 N  N     . LYS B 1  59  ? 3.68162   8.23906   -27.26968 1.000 85.39164  ? 89  LYS B N     1 
ATOM   2576 C  CA    . LYS B 1  59  ? 3.86796   9.38888   -26.39551 1.000 69.68958  ? 89  LYS B CA    1 
ATOM   2577 C  C     . LYS B 1  59  ? 5.15426   9.22770   -25.58803 1.000 62.95074  ? 89  LYS B C     1 
ATOM   2578 O  O     . LYS B 1  59  ? 5.48442   8.12561   -25.15238 1.000 72.68393  ? 89  LYS B O     1 
ATOM   2579 C  CB    . LYS B 1  59  ? 2.67431   9.55769   -25.44903 1.000 67.22939  ? 89  LYS B CB    1 
ATOM   2580 C  CG    . LYS B 1  59  ? 1.40707   10.12283  -26.09944 1.000 68.78105  ? 89  LYS B CG    1 
ATOM   2581 C  CD    . LYS B 1  59  ? 0.73072   9.11702   -27.01439 1.000 74.01331  ? 89  LYS B CD    1 
ATOM   2582 C  CE    . LYS B 1  59  ? -0.49253  9.72617   -27.68781 1.000 82.78033  ? 89  LYS B CE    1 
ATOM   2583 N  NZ    . LYS B 1  59  ? -1.11390  8.78437   -28.66277 1.000 75.65340  ? 89  LYS B NZ    1 
ATOM   2584 N  N     . GLN B 1  60  ? 5.86835   10.32865  -25.37007 1.000 63.75309  ? 90  GLN B N     1 
ATOM   2585 C  CA    . GLN B 1  60  ? 7.18558   10.26652  -24.73558 1.000 70.44513  ? 90  GLN B CA    1 
ATOM   2586 C  C     . GLN B 1  60  ? 7.08216   10.27120  -23.21054 1.000 63.74184  ? 90  GLN B C     1 
ATOM   2587 O  O     . GLN B 1  60  ? 6.37538   11.10908  -22.62610 1.000 66.68302  ? 90  GLN B O     1 
ATOM   2588 C  CB    . GLN B 1  60  ? 8.04842   11.44061  -25.20066 1.000 75.05275  ? 90  GLN B CB    1 
ATOM   2589 C  CG    . GLN B 1  60  ? 9.43565   11.46947  -24.57917 1.000 68.28806  ? 90  GLN B CG    1 
ATOM   2590 C  CD    . GLN B 1  60  ? 10.26450  10.25555  -24.96173 1.000 70.09762  ? 90  GLN B CD    1 
ATOM   2591 O  OE1   . GLN B 1  60  ? 10.54006  10.02779  -26.13588 1.000 78.80108  ? 90  GLN B OE1   1 
ATOM   2592 N  NE2   . GLN B 1  60  ? 10.64687  9.46634   -23.96704 1.000 69.40283  ? 90  GLN B NE2   1 
ATOM   2593 N  N     . LEU B 1  61  ? 7.79539   9.33606   -22.57000 1.000 62.23916  ? 91  LEU B N     1 
ATOM   2594 C  CA    . LEU B 1  61  ? 7.89994   9.26576   -21.11505 1.000 55.01403  ? 91  LEU B CA    1 
ATOM   2595 C  C     . LEU B 1  61  ? 9.29510   9.69866   -20.67949 1.000 58.01203  ? 91  LEU B C     1 
ATOM   2596 O  O     . LEU B 1  61  ? 10.29490  9.20777   -21.21096 1.000 58.90924  ? 91  LEU B O     1 
ATOM   2597 C  CB    . LEU B 1  61  ? 7.62313   7.85565   -20.59424 1.000 47.64506  ? 91  LEU B CB    1 
ATOM   2598 C  CG    . LEU B 1  61  ? 7.95568   7.68234   -19.10640 1.000 54.53975  ? 91  LEU B CG    1 
ATOM   2599 C  CD1   . LEU B 1  61  ? 6.86001   8.29616   -18.23686 1.000 56.59403  ? 91  LEU B CD1   1 
ATOM   2600 C  CD2   . LEU B 1  61  ? 8.20682   6.22126   -18.73380 1.000 58.70719  ? 91  LEU B CD2   1 
ATOM   2601 N  N     . LYS B 1  62  ? 9.35747   10.60046  -19.70032 1.000 57.73673  ? 92  LYS B N     1 
ATOM   2602 C  CA    . LYS B 1  62  ? 10.61969  11.07034  -19.14370 1.000 59.20943  ? 92  LYS B CA    1 
ATOM   2603 C  C     . LYS B 1  62  ? 10.59125  10.87602  -17.63573 1.000 55.33139  ? 92  LYS B C     1 
ATOM   2604 O  O     . LYS B 1  62  ? 9.54249   11.04290  -17.01130 1.000 49.60862  ? 92  LYS B O     1 
ATOM   2605 C  CB    . LYS B 1  62  ? 10.86156  12.54241  -19.48948 1.000 51.68631  ? 92  LYS B CB    1 
ATOM   2606 C  CG    . LYS B 1  62  ? 10.98100  12.81672  -20.98447 1.000 63.67780  ? 92  LYS B CG    1 
ATOM   2607 C  CD    . LYS B 1  62  ? 12.23378  12.16984  -21.58507 1.000 61.57545  ? 92  LYS B CD    1 
ATOM   2608 C  CE    . LYS B 1  62  ? 13.50496  12.85273  -21.09741 1.000 66.02946  ? 92  LYS B CE    1 
ATOM   2609 N  NZ    . LYS B 1  62  ? 14.73274  12.23384  -21.67800 1.000 70.80940  ? 92  LYS B NZ    1 
ATOM   2610 N  N     . THR B 1  63  ? 11.72947  10.51289  -17.04523 1.000 52.78578  ? 93  THR B N     1 
ATOM   2611 C  CA    . THR B 1  63  ? 11.77901  10.22160  -15.61731 1.000 55.88152  ? 93  THR B CA    1 
ATOM   2612 C  C     . THR B 1  63  ? 12.99624  10.87746  -14.99163 1.000 56.45948  ? 93  THR B C     1 
ATOM   2613 O  O     . THR B 1  63  ? 14.12508  10.64054  -15.42910 1.000 58.51525  ? 93  THR B O     1 
ATOM   2614 C  CB    . THR B 1  63  ? 11.81710  8.71154   -15.35164 1.000 57.30885  ? 93  THR B CB    1 
ATOM   2615 O  OG1   . THR B 1  63  ? 10.63390  8.09465   -15.87332 1.000 57.97324  ? 93  THR B OG1   1 
ATOM   2616 C  CG2   . THR B 1  63  ? 11.91166  8.44523   -13.84773 1.000 53.27869  ? 93  THR B CG2   1 
ATOM   2617 N  N     . PHE B 1  64  ? 12.76464  11.67224  -13.94338 1.000 53.28065  ? 94  PHE B N     1 
ATOM   2618 C  CA    . PHE B 1  64  ? 13.82491  12.36709  -13.23063 1.000 59.32520  ? 94  PHE B CA    1 
ATOM   2619 C  C     . PHE B 1  64  ? 13.64747  12.16278  -11.73260 1.000 47.09315  ? 94  PHE B C     1 
ATOM   2620 O  O     . PHE B 1  64  ? 12.54166  11.92268  -11.24124 1.000 46.26013  ? 94  PHE B O     1 
ATOM   2621 C  CB    . PHE B 1  64  ? 13.83179  13.87016  -13.56232 1.000 53.49773  ? 94  PHE B CB    1 
ATOM   2622 C  CG    . PHE B 1  64  ? 13.77224  14.16147  -15.03824 1.000 64.43491  ? 94  PHE B CG    1 
ATOM   2623 C  CD1   . PHE B 1  64  ? 14.88394  13.96163  -15.84369 1.000 64.27866  ? 94  PHE B CD1   1 
ATOM   2624 C  CD2   . PHE B 1  64  ? 12.60603  14.62359  -15.61970 1.000 65.72758  ? 94  PHE B CD2   1 
ATOM   2625 C  CE1   . PHE B 1  64  ? 14.83043  14.21991  -17.20162 1.000 65.93783  ? 94  PHE B CE1   1 
ATOM   2626 C  CE2   . PHE B 1  64  ? 12.54952  14.88788  -16.98063 1.000 67.08932  ? 94  PHE B CE2   1 
ATOM   2627 C  CZ    . PHE B 1  64  ? 13.66522  14.68003  -17.76809 1.000 65.08475  ? 94  PHE B CZ    1 
ATOM   2628 N  N     . PHE B 1  65  ? 14.75674  12.27062  -11.00900 1.000 47.30482  ? 95  PHE B N     1 
ATOM   2629 C  CA    . PHE B 1  65  ? 14.78729  12.09532  -9.56305  1.000 57.33783  ? 95  PHE B CA    1 
ATOM   2630 C  C     . PHE B 1  65  ? 15.16054  13.41718  -8.91291  1.000 58.36849  ? 95  PHE B C     1 
ATOM   2631 O  O     . PHE B 1  65  ? 16.21543  13.98524  -9.20819  1.000 58.84646  ? 95  PHE B O     1 
ATOM   2632 C  CB    . PHE B 1  65  ? 15.78242  11.00324  -9.17865  1.000 61.89654  ? 95  PHE B CB    1 
ATOM   2633 C  CG    . PHE B 1  65  ? 15.44821  9.65335   -9.74180  1.000 58.66099  ? 95  PHE B CG    1 
ATOM   2634 C  CD1   . PHE B 1  65  ? 14.63046  8.78221   -9.04568  1.000 55.96879  ? 95  PHE B CD1   1 
ATOM   2635 C  CD2   . PHE B 1  65  ? 15.95374  9.25661   -10.97107 1.000 60.92120  ? 95  PHE B CD2   1 
ATOM   2636 C  CE1   . PHE B 1  65  ? 14.32126  7.54232   -9.56082  1.000 53.04238  ? 95  PHE B CE1   1 
ATOM   2637 C  CE2   . PHE B 1  65  ? 15.65054  8.01172   -11.49022 1.000 58.59312  ? 95  PHE B CE2   1 
ATOM   2638 C  CZ    . PHE B 1  65  ? 14.83680  7.15457   -10.78209 1.000 55.39532  ? 95  PHE B CZ    1 
ATOM   2639 N  N     . LEU B 1  66  ? 14.29787  13.89300  -8.01749  1.000 61.87858  ? 96  LEU B N     1 
ATOM   2640 C  CA    . LEU B 1  66  ? 14.50715  15.13985  -7.30131  1.000 60.75903  ? 96  LEU B CA    1 
ATOM   2641 C  C     . LEU B 1  66  ? 15.36861  14.88459  -6.07068  1.000 65.61942  ? 96  LEU B C     1 
ATOM   2642 O  O     . LEU B 1  66  ? 15.02992  14.04142  -5.23373  1.000 61.83918  ? 96  LEU B O     1 
ATOM   2643 C  CB    . LEU B 1  66  ? 13.16330  15.75178  -6.90768  1.000 56.40115  ? 96  LEU B CB    1 
ATOM   2644 C  CG    . LEU B 1  66  ? 12.14288  15.83902  -8.03627  1.000 53.46567  ? 96  LEU B CG    1 
ATOM   2645 C  CD1   . LEU B 1  66  ? 10.82108  16.36491  -7.51167  1.000 45.90568  ? 96  LEU B CD1   1 
ATOM   2646 C  CD2   . LEU B 1  66  ? 12.67347  16.73324  -9.14529  1.000 54.53124  ? 96  LEU B CD2   1 
ATOM   2647 N  N     . LEU B 1  67  ? 16.47665  15.61756  -5.96495  1.000 65.22702  ? 97  LEU B N     1 
ATOM   2648 C  CA    . LEU B 1  67  ? 17.39407  15.50633  -4.84131  1.000 69.35016  ? 97  LEU B CA    1 
ATOM   2649 C  C     . LEU B 1  67  ? 17.73527  16.89622  -4.32815  1.000 68.78204  ? 97  LEU B C     1 
ATOM   2650 O  O     . LEU B 1  67  ? 17.75800  17.86937  -5.08296  1.000 65.00920  ? 97  LEU B O     1 
ATOM   2651 C  CB    . LEU B 1  67  ? 18.68493  14.75940  -5.22795  1.000 59.02313  ? 97  LEU B CB    1 
ATOM   2652 C  CG    . LEU B 1  67  ? 18.63092  13.22740  -5.21625  1.000 60.88623  ? 97  LEU B CG    1 
ATOM   2653 C  CD1   . LEU B 1  67  ? 19.90470  12.63151  -5.79985  1.000 65.17246  ? 97  LEU B CD1   1 
ATOM   2654 C  CD2   . LEU B 1  67  ? 18.39345  12.70810  -3.80427  1.000 69.05380  ? 97  LEU B CD2   1 
ATOM   2655 N  N     . GLY B 1  68  ? 17.98476  16.97895  -3.03223  1.000 73.75401  ? 98  GLY B N     1 
ATOM   2656 C  CA    . GLY B 1  68  ? 18.59700  18.13282  -2.41722  1.000 80.30537  ? 98  GLY B CA    1 
ATOM   2657 C  C     . GLY B 1  68  ? 20.07609  17.91676  -2.17882  1.000 77.87005  ? 98  GLY B C     1 
ATOM   2658 O  O     . GLY B 1  68  ? 20.76180  17.22491  -2.94022  1.000 78.95259  ? 98  GLY B O     1 
ATOM   2659 N  N     . THR B 1  69  ? 20.57949  18.49353  -1.09489  1.000 75.02387  ? 99  THR B N     1 
ATOM   2660 C  CA    . THR B 1  69  ? 21.97264  18.34844  -0.71044  1.000 66.55822  ? 99  THR B CA    1 
ATOM   2661 C  C     . THR B 1  69  ? 22.06214  17.63316  0.63038   1.000 74.36172  ? 99  THR B C     1 
ATOM   2662 O  O     . THR B 1  69  ? 21.07641  17.52302  1.36472   1.000 77.49254  ? 99  THR B O     1 
ATOM   2663 C  CB    . THR B 1  69  ? 22.65767  19.71642  -0.63241  1.000 59.65222  ? 99  THR B CB    1 
ATOM   2664 O  OG1   . THR B 1  69  ? 21.98304  20.52122  0.34001   1.000 76.20375  ? 99  THR B OG1   1 
ATOM   2665 C  CG2   . THR B 1  69  ? 22.58217  20.41170  -1.97424  1.000 65.64382  ? 99  THR B CG2   1 
ATOM   2666 N  N     . THR B 1  70  ? 23.26325  17.13909  0.93782   1.000 72.39947  ? 100 THR B N     1 
ATOM   2667 C  CA    . THR B 1  70  ? 23.48370  16.37484  2.15658   1.000 79.58123  ? 100 THR B CA    1 
ATOM   2668 C  C     . THR B 1  70  ? 24.81494  16.76570  2.78016   1.000 85.86366  ? 100 THR B C     1 
ATOM   2669 O  O     . THR B 1  70  ? 25.74468  17.18784  2.08690   1.000 82.54792  ? 100 THR B O     1 
ATOM   2670 C  CB    . THR B 1  70  ? 23.45260  14.85889  1.89728   1.000 82.72142  ? 100 THR B CB    1 
ATOM   2671 O  OG1   . THR B 1  70  ? 23.70905  14.14964  3.11604   1.000 90.41761  ? 100 THR B OG1   1 
ATOM   2672 C  CG2   . THR B 1  70  ? 24.50221  14.47210  0.86080   1.000 82.06921  ? 100 THR B CG2   1 
ATOM   2673 N  N     . SER B 1  71  ? 24.89044  16.62143  4.10511   1.000 99.76177  ? 101 SER B N     1 
ATOM   2674 C  CA    . SER B 1  71  ? 26.14670  16.86827  4.80769   1.000 94.82482  ? 101 SER B CA    1 
ATOM   2675 C  C     . SER B 1  71  ? 27.13762  15.73331  4.59408   1.000 99.74075  ? 101 SER B C     1 
ATOM   2676 O  O     . SER B 1  71  ? 28.35362  15.96430  4.61167   1.000 98.70380  ? 101 SER B O     1 
ATOM   2677 C  CB    . SER B 1  71  ? 25.87626  17.06297  6.29983   1.000 78.66606  ? 101 SER B CB    1 
ATOM   2678 O  OG    . SER B 1  71  ? 25.26146  15.90786  6.84382   1.000 87.55525  ? 101 SER B OG    1 
ATOM   2679 N  N     . SER B 1  72  ? 26.65254  14.50936  4.39401   1.000 98.89780  ? 102 SER B N     1 
ATOM   2680 C  CA    . SER B 1  72  ? 27.53248  13.35938  4.25644   1.000 97.94368  ? 102 SER B CA    1 
ATOM   2681 C  C     . SER B 1  72  ? 28.40301  13.48664  3.01614   1.000 90.69809  ? 102 SER B C     1 
ATOM   2682 O  O     . SER B 1  72  ? 27.89559  13.56987  1.89234   1.000 87.54202  ? 102 SER B O     1 
ATOM   2683 C  CB    . SER B 1  72  ? 26.71145  12.07340  4.19348   1.000 96.59189  ? 102 SER B CB    1 
ATOM   2684 O  OG    . SER B 1  72  ? 27.51429  10.98148  3.77595   1.000 94.24042  ? 102 SER B OG    1 
ATOM   2685 N  N     . ALA B 1  73  ? 29.72309  13.49659  3.22364   1.000 88.80420  ? 103 ALA B N     1 
ATOM   2686 C  CA    . ALA B 1  73  ? 30.64967  13.50682  2.09730   1.000 80.52547  ? 103 ALA B CA    1 
ATOM   2687 C  C     . ALA B 1  73  ? 30.46734  12.26900  1.23111   1.000 87.16250  ? 103 ALA B C     1 
ATOM   2688 O  O     . ALA B 1  73  ? 30.50788  12.35325  -0.00289  1.000 86.51692  ? 103 ALA B O     1 
ATOM   2689 C  CB    . ALA B 1  73  ? 32.08786  13.59670  2.60478   1.000 71.82243  ? 103 ALA B CB    1 
ATOM   2690 N  N     . ALA B 1  74  ? 30.26357  11.10787  1.86494   1.000 93.65002  ? 104 ALA B N     1 
ATOM   2691 C  CA    . ALA B 1  74  ? 30.08828  9.86702   1.11775   1.000 100.39567 ? 104 ALA B CA    1 
ATOM   2692 C  C     . ALA B 1  74  ? 28.83396  9.91421   0.24923   1.000 101.18048 ? 104 ALA B C     1 
ATOM   2693 O  O     . ALA B 1  74  ? 28.86352  9.52645   -0.92486  1.000 92.73332  ? 104 ALA B O     1 
ATOM   2694 C  CB    . ALA B 1  74  ? 30.03564  8.68182   2.08552   1.000 94.37410  ? 104 ALA B CB    1 
ATOM   2695 N  N     . GLU B 1  75  ? 27.72117  10.38810  0.81375   1.000 101.55862 ? 105 GLU B N     1 
ATOM   2696 C  CA    . GLU B 1  75  ? 26.48588  10.48427  0.03723   1.000 98.24113  ? 105 GLU B CA    1 
ATOM   2697 C  C     . GLU B 1  75  ? 26.60647  11.52350  -1.06860  1.000 96.11233  ? 105 GLU B C     1 
ATOM   2698 O  O     . GLU B 1  75  ? 26.10705  11.31173  -2.18046  1.000 92.91360  ? 105 GLU B O     1 
ATOM   2699 C  CB    . GLU B 1  75  ? 25.31023  10.80908  0.95774   1.000 87.17730  ? 105 GLU B CB    1 
ATOM   2700 C  CG    . GLU B 1  75  ? 24.87655  9.64790   1.84066   1.000 89.18154  ? 105 GLU B CG    1 
ATOM   2701 C  CD    . GLU B 1  75  ? 23.72190  10.01771  2.75417   1.000 97.96441  ? 105 GLU B CD    1 
ATOM   2702 O  OE1   . GLU B 1  75  ? 23.36692  11.21171  2.80055   1.000 104.09930 ? 105 GLU B OE1   1 
ATOM   2703 O  OE2   . GLU B 1  75  ? 23.17515  9.11658   3.42619   1.000 104.47459 ? 105 GLU B OE2   1 
ATOM   2704 N  N     . THR B 1  76  ? 27.25558  12.65643  -0.79061  1.000 92.03808  ? 106 THR B N     1 
ATOM   2705 C  CA    . THR B 1  76  ? 27.47519  13.64365  -1.84348  1.000 88.53278  ? 106 THR B CA    1 
ATOM   2706 C  C     . THR B 1  76  ? 28.27276  13.03089  -2.98891  1.000 96.54325  ? 106 THR B C     1 
ATOM   2707 O  O     . THR B 1  76  ? 27.92832  13.20113  -4.16275  1.000 99.11492  ? 106 THR B O     1 
ATOM   2708 C  CB    . THR B 1  76  ? 28.19341  14.86953  -1.28150  1.000 81.55001  ? 106 THR B CB    1 
ATOM   2709 O  OG1   . THR B 1  76  ? 27.42481  15.43031  -0.21609  1.000 80.47723  ? 106 THR B OG1   1 
ATOM   2710 C  CG2   . THR B 1  76  ? 28.37000  15.91576  -2.37135  1.000 80.94097  ? 106 THR B CG2   1 
ATOM   2711 N  N     . LYS B 1  77  ? 29.34688  12.31181  -2.66146  1.000 96.81763  ? 107 LYS B N     1 
ATOM   2712 C  CA    . LYS B 1  77  ? 30.14649  11.64202  -3.68590  1.000 101.48714 ? 107 LYS B CA    1 
ATOM   2713 C  C     . LYS B 1  77  ? 29.29418  10.65519  -4.48879  1.000 102.24955 ? 107 LYS B C     1 
ATOM   2714 O  O     . LYS B 1  77  ? 29.32972  10.63845  -5.73081  1.000 99.69953  ? 107 LYS B O     1 
ATOM   2715 C  CB    . LYS B 1  77  ? 31.33073  10.92988  -3.02749  1.000 97.95648  ? 107 LYS B CB    1 
ATOM   2716 C  CG    . LYS B 1  77  ? 32.24237  10.18407  -3.98499  1.000 105.41398 ? 107 LYS B CG    1 
ATOM   2717 C  CD    . LYS B 1  77  ? 32.65194  11.06731  -5.15096  1.000 109.91651 ? 107 LYS B CD    1 
ATOM   2718 C  CE    . LYS B 1  77  ? 33.18913  12.41021  -4.66588  1.000 99.30955  ? 107 LYS B CE    1 
ATOM   2719 N  NZ    . LYS B 1  77  ? 33.52370  13.30145  -5.80282  1.000 80.41575  ? 107 LYS B NZ    1 
ATOM   2720 N  N     . GLU B 1  78  ? 28.52944  9.81805   -3.78268  1.000 103.73632 ? 108 GLU B N     1 
ATOM   2721 C  CA    . GLU B 1  78  ? 27.69919  8.81519   -4.44257  1.000 108.17287 ? 108 GLU B CA    1 
ATOM   2722 C  C     . GLU B 1  78  ? 26.72683  9.46940   -5.41607  1.000 111.37036 ? 108 GLU B C     1 
ATOM   2723 O  O     . GLU B 1  78  ? 26.57540  9.01764   -6.55711  1.000 111.86999 ? 108 GLU B O     1 
ATOM   2724 C  CB    . GLU B 1  78  ? 26.94758  7.98798   -3.39646  1.000 96.78614  ? 108 GLU B CB    1 
ATOM   2725 C  CG    . GLU B 1  78  ? 27.85089  7.08880   -2.55599  1.000 107.83551 ? 108 GLU B CG    1 
ATOM   2726 C  CD    . GLU B 1  78  ? 27.19637  6.62953   -1.26184  1.000 119.58807 ? 108 GLU B CD    1 
ATOM   2727 O  OE1   . GLU B 1  78  ? 25.98345  6.87150   -1.07033  1.000 120.30661 ? 108 GLU B OE1   1 
ATOM   2728 O  OE2   . GLU B 1  78  ? 27.90469  6.02335   -0.42523  1.000 119.94548 ? 108 GLU B OE2   1 
ATOM   2729 N  N     . VAL B 1  79  ? 26.06400  10.54531  -4.98360  1.000 95.72084  ? 109 VAL B N     1 
ATOM   2730 C  CA    . VAL B 1  79  ? 25.07768  11.20050  -5.84109  1.000 92.29301  ? 109 VAL B CA    1 
ATOM   2731 C  C     . VAL B 1  79  ? 25.74424  11.90774  -7.01220  1.000 91.70308  ? 109 VAL B C     1 
ATOM   2732 O  O     . VAL B 1  79  ? 25.18583  11.95497  -8.11198  1.000 88.95669  ? 109 VAL B O     1 
ATOM   2733 C  CB    . VAL B 1  79  ? 24.20699  12.17433  -5.02156  1.000 82.64723  ? 109 VAL B CB    1 
ATOM   2734 C  CG1   . VAL B 1  79  ? 23.53165  13.17653  -5.94610  1.000 73.38324  ? 109 VAL B CG1   1 
ATOM   2735 C  CG2   . VAL B 1  79  ? 23.16429  11.40417  -4.22533  1.000 75.73570  ? 109 VAL B CG2   1 
ATOM   2736 N  N     . ASP B 1  80  ? 26.94132  12.46269  -6.81553  1.000 90.45060  ? 110 ASP B N     1 
ATOM   2737 C  CA    . ASP B 1  80  ? 27.64890  13.07592  -7.93567  1.000 95.52890  ? 110 ASP B CA    1 
ATOM   2738 C  C     . ASP B 1  80  ? 27.94049  12.04514  -9.01999  1.000 101.88680 ? 110 ASP B C     1 
ATOM   2739 O  O     . ASP B 1  80  ? 27.64005  12.25839  -10.20583 1.000 90.20094  ? 110 ASP B O     1 
ATOM   2740 C  CB    . ASP B 1  80  ? 28.94509  13.72581  -7.44802  1.000 101.67464 ? 110 ASP B CB    1 
ATOM   2741 C  CG    . ASP B 1  80  ? 28.72453  14.68257  -6.29574  1.000 113.41420 ? 110 ASP B CG    1 
ATOM   2742 O  OD1   . ASP B 1  80  ? 27.62256  15.26456  -6.21020  1.000 112.87850 ? 110 ASP B OD1   1 
ATOM   2743 O  OD2   . ASP B 1  80  ? 29.64884  14.84140  -5.46705  1.000 108.93442 ? 110 ASP B OD2   1 
ATOM   2744 N  N     . GLN B 1  81  ? 28.52163  10.90706  -8.62545  1.000 119.24886 ? 111 GLN B N     1 
ATOM   2745 C  CA    . GLN B 1  81  ? 28.84126  9.87626   -9.60878  1.000 118.40758 ? 111 GLN B CA    1 
ATOM   2746 C  C     . GLN B 1  81  ? 27.57603  9.27940   -10.22443 1.000 121.09263 ? 111 GLN B C     1 
ATOM   2747 O  O     . GLN B 1  81  ? 27.55158  8.95564   -11.41949 1.000 103.28814 ? 111 GLN B O     1 
ATOM   2748 C  CB    . GLN B 1  81  ? 29.70649  8.78812   -8.96733  1.000 122.35902 ? 111 GLN B CB    1 
ATOM   2749 C  CG    . GLN B 1  81  ? 31.10863  9.26804   -8.59976  1.000 125.03708 ? 111 GLN B CG    1 
ATOM   2750 C  CD    . GLN B 1  81  ? 31.96287  8.18190   -7.96830  1.000 126.43422 ? 111 GLN B CD    1 
ATOM   2751 O  OE1   . GLN B 1  81  ? 31.52620  7.47072   -7.06229  1.000 127.56464 ? 111 GLN B OE1   1 
ATOM   2752 N  NE2   . GLN B 1  81  ? 33.19368  8.04700   -8.45379  1.000 110.93869 ? 111 GLN B NE2   1 
ATOM   2753 N  N     . GLU B 1  82  ? 26.51732  9.14124   -9.42906  1.000 100.37202 ? 112 GLU B N     1 
ATOM   2754 C  CA    . GLU B 1  82  ? 25.25312  8.64435   -9.95869  1.000 94.74402  ? 112 GLU B CA    1 
ATOM   2755 C  C     . GLU B 1  82  ? 24.67774  9.59957   -10.99328 1.000 90.87379  ? 112 GLU B C     1 
ATOM   2756 O  O     . GLU B 1  82  ? 24.18734  9.16879   -12.04418 1.000 83.05200  ? 112 GLU B O     1 
ATOM   2757 C  CB    . GLU B 1  82  ? 24.26855  8.43512   -8.80836  1.000 91.34690  ? 112 GLU B CB    1 
ATOM   2758 C  CG    . GLU B 1  82  ? 22.91540  7.88821   -9.21797  1.000 87.46881  ? 112 GLU B CG    1 
ATOM   2759 C  CD    . GLU B 1  82  ? 22.00084  7.69896   -8.02367  1.000 100.24576 ? 112 GLU B CD    1 
ATOM   2760 O  OE1   . GLU B 1  82  ? 22.48327  7.83372   -6.87882  1.000 104.38741 ? 112 GLU B OE1   1 
ATOM   2761 O  OE2   . GLU B 1  82  ? 20.80377  7.41501   -8.22628  1.000 96.46295  ? 112 GLU B OE2   1 
ATOM   2762 N  N     . SER B 1  83  ? 24.72685  10.90551  -10.71202 1.000 90.20724  ? 113 SER B N     1 
ATOM   2763 C  CA    . SER B 1  83  ? 24.26049  11.89171  -11.67964 1.000 83.92895  ? 113 SER B CA    1 
ATOM   2764 C  C     . SER B 1  83  ? 25.07701  11.82498  -12.96196 1.000 83.36148  ? 113 SER B C     1 
ATOM   2765 O  O     . SER B 1  83  ? 24.52360  11.92421  -14.06374 1.000 78.31352  ? 113 SER B O     1 
ATOM   2766 C  CB    . SER B 1  83  ? 24.32972  13.29559  -11.07738 1.000 78.20532  ? 113 SER B CB    1 
ATOM   2767 O  OG    . SER B 1  83  ? 23.89538  14.27179  -12.00901 1.000 74.97947  ? 113 SER B OG    1 
ATOM   2768 N  N     . GLN B 1  84  ? 26.39406  11.65495  -12.83949 1.000 84.67797  ? 114 GLN B N     1 
ATOM   2769 C  CA    . GLN B 1  84  ? 27.21860  11.57019  -14.03982 1.000 85.68324  ? 114 GLN B CA    1 
ATOM   2770 C  C     . GLN B 1  84  ? 26.89530  10.31936  -14.84696 1.000 82.04171  ? 114 GLN B C     1 
ATOM   2771 O  O     . GLN B 1  84  ? 26.87083  10.36062  -16.08194 1.000 70.90762  ? 114 GLN B O     1 
ATOM   2772 C  CB    . GLN B 1  84  ? 28.69874  11.61611  -13.66737 1.000 102.45574 ? 114 GLN B CB    1 
ATOM   2773 C  CG    . GLN B 1  84  ? 29.20484  13.03106  -13.43926 1.000 111.04840 ? 114 GLN B CG    1 
ATOM   2774 C  CD    . GLN B 1  84  ? 30.62103  13.07294  -12.91478 1.000 105.68837 ? 114 GLN B CD    1 
ATOM   2775 O  OE1   . GLN B 1  84  ? 31.32803  12.06194  -12.91626 1.000 98.97950  ? 114 GLN B OE1   1 
ATOM   2776 N  NE2   . GLN B 1  84  ? 31.04421  14.24484  -12.45970 1.000 94.90292  ? 114 GLN B NE2   1 
ATOM   2777 N  N     . ARG B 1  85  ? 26.63254  9.19822   -14.17309 1.000 98.45552  ? 115 ARG B N     1 
ATOM   2778 C  CA    . ARG B 1  85  ? 26.35126  7.96137   -14.90025 1.000 91.33711  ? 115 ARG B CA    1 
ATOM   2779 C  C     . ARG B 1  85  ? 24.97003  7.95851   -15.53673 1.000 90.14731  ? 115 ARG B C     1 
ATOM   2780 O  O     . ARG B 1  85  ? 24.79362  7.38574   -16.61478 1.000 89.15915  ? 115 ARG B O     1 
ATOM   2781 C  CB    . ARG B 1  85  ? 26.48461  6.75718   -13.97455 1.000 92.98745  ? 115 ARG B CB    1 
ATOM   2782 C  CG    . ARG B 1  85  ? 26.25534  5.43033   -14.67374 1.000 84.04451  ? 115 ARG B CG    1 
ATOM   2783 C  CD    . ARG B 1  85  ? 26.06371  4.32812   -13.65989 1.000 93.71339  ? 115 ARG B CD    1 
ATOM   2784 N  NE    . ARG B 1  85  ? 26.94814  4.51688   -12.51819 1.000 103.59475 ? 115 ARG B NE    1 
ATOM   2785 C  CZ    . ARG B 1  85  ? 26.72859  4.00963   -11.31121 1.000 108.92841 ? 115 ARG B CZ    1 
ATOM   2786 N  NH1   . ARG B 1  85  ? 25.65569  3.27958   -11.05096 1.000 95.64205  ? 115 ARG B NH1   1 
ATOM   2787 N  NH2   . ARG B 1  85  ? 27.60696  4.24842   -10.33949 1.000 106.36521 ? 115 ARG B NH2   1 
ATOM   2788 N  N     . HIS B 1  86  ? 23.97627  8.58739   -14.89822 1.000 93.09938  ? 116 HIS B N     1 
ATOM   2789 C  CA    . HIS B 1  86  ? 22.60209  8.49649   -15.36773 1.000 83.90924  ? 116 HIS B CA    1 
ATOM   2790 C  C     . HIS B 1  86  ? 22.02590  9.80160   -15.89724 1.000 74.79632  ? 116 HIS B C     1 
ATOM   2791 O  O     . HIS B 1  86  ? 21.08160  9.75177   -16.69490 1.000 74.93801  ? 116 HIS B O     1 
ATOM   2792 C  CB    . HIS B 1  86  ? 21.68851  7.97226   -14.24649 1.000 84.21125  ? 116 HIS B CB    1 
ATOM   2793 C  CG    . HIS B 1  86  ? 22.05569  6.60316   -13.75592 1.000 88.14935  ? 116 HIS B CG    1 
ATOM   2794 N  ND1   . HIS B 1  86  ? 21.87340  5.46732   -14.51408 1.000 79.04237  ? 116 HIS B ND1   1 
ATOM   2795 C  CD2   . HIS B 1  86  ? 22.58913  6.19091   -12.58220 1.000 91.03986  ? 116 HIS B CD2   1 
ATOM   2796 C  CE1   . HIS B 1  86  ? 22.28765  4.41417   -13.83246 1.000 86.67150  ? 116 HIS B CE1   1 
ATOM   2797 N  NE2   . HIS B 1  86  ? 22.72209  4.82393   -12.65554 1.000 89.82167  ? 116 HIS B NE2   1 
ATOM   2798 N  N     . GLY B 1  87  ? 22.54306  10.95551  -15.47819 1.000 71.18586  ? 117 GLY B N     1 
ATOM   2799 C  CA    . GLY B 1  87  ? 22.07686  12.22563  -16.01975 1.000 79.26648  ? 117 GLY B CA    1 
ATOM   2800 C  C     . GLY B 1  87  ? 20.59693  12.49560  -15.83814 1.000 83.78726  ? 117 GLY B C     1 
ATOM   2801 O  O     . GLY B 1  87  ? 20.00664  13.23677  -16.64177 1.000 78.98977  ? 117 GLY B O     1 
ATOM   2802 N  N     . ASP B 1  88  ? 19.97732  11.94138  -14.79003 1.000 81.99563  ? 118 ASP B N     1 
ATOM   2803 C  CA    . ASP B 1  88  ? 18.53740  12.05635  -14.58846 1.000 67.37378  ? 118 ASP B CA    1 
ATOM   2804 C  C     . ASP B 1  88  ? 18.17591  12.69607  -13.25019 1.000 69.17040  ? 118 ASP B C     1 
ATOM   2805 O  O     . ASP B 1  88  ? 17.04408  12.52998  -12.77880 1.000 81.18656  ? 118 ASP B O     1 
ATOM   2806 C  CB    . ASP B 1  88  ? 17.86935  10.68138  -14.71250 1.000 69.70235  ? 118 ASP B CB    1 
ATOM   2807 C  CG    . ASP B 1  88  ? 18.47670  9.63718   -13.77094 1.000 80.23771  ? 118 ASP B CG    1 
ATOM   2808 O  OD1   . ASP B 1  88  ? 19.31302  9.99500   -12.91318 1.000 72.90334  ? 118 ASP B OD1   1 
ATOM   2809 O  OD2   . ASP B 1  88  ? 18.11164  8.44621   -13.89405 1.000 74.48345  ? 118 ASP B OD2   1 
ATOM   2810 N  N     . ILE B 1  89  ? 19.08314  13.44594  -12.63738 1.000 70.47649  ? 119 ILE B N     1 
ATOM   2811 C  CA    . ILE B 1  89  ? 18.87664  14.00766  -11.30218 1.000 67.18338  ? 119 ILE B CA    1 
ATOM   2812 C  C     . ILE B 1  89  ? 18.65361  15.51069  -11.41679 1.000 67.43909  ? 119 ILE B C     1 
ATOM   2813 O  O     . ILE B 1  89  ? 19.39135  16.20983  -12.11892 1.000 61.45018  ? 119 ILE B O     1 
ATOM   2814 C  CB    . ILE B 1  89  ? 20.06399  13.69146  -10.37569 1.000 63.42093  ? 119 ILE B CB    1 
ATOM   2815 C  CG1   . ILE B 1  89  ? 20.13708  12.18541  -10.12103 1.000 76.89779  ? 119 ILE B CG1   1 
ATOM   2816 C  CG2   . ILE B 1  89  ? 19.92149  14.44219  -9.06348  1.000 66.76978  ? 119 ILE B CG2   1 
ATOM   2817 C  CD1   . ILE B 1  89  ? 21.26142  11.76121  -9.19854  1.000 77.97274  ? 119 ILE B CD1   1 
ATOM   2818 N  N     . ILE B 1  90  ? 17.62287  16.00255  -10.73030 1.000 68.66858  ? 120 ILE B N     1 
ATOM   2819 C  CA    . ILE B 1  90  ? 17.33693  17.43052  -10.59289 1.000 65.13830  ? 120 ILE B CA    1 
ATOM   2820 C  C     . ILE B 1  90  ? 17.65047  17.82022  -9.15393  1.000 66.43806  ? 120 ILE B C     1 
ATOM   2821 O  O     . ILE B 1  90  ? 17.01382  17.32703  -8.22079  1.000 63.85371  ? 120 ILE B O     1 
ATOM   2822 C  CB    . ILE B 1  90  ? 15.87580  17.75860  -10.92828 1.000 60.04660  ? 120 ILE B CB    1 
ATOM   2823 C  CG1   . ILE B 1  90  ? 15.52727  17.28190  -12.34224 1.000 60.98387  ? 120 ILE B CG1   1 
ATOM   2824 C  CG2   . ILE B 1  90  ? 15.59589  19.25356  -10.71786 1.000 55.60416  ? 120 ILE B CG2   1 
ATOM   2825 C  CD1   . ILE B 1  90  ? 14.04217  17.21596  -12.60670 1.000 56.83811  ? 120 ILE B CD1   1 
ATOM   2826 N  N     . GLN B 1  91  ? 18.61554  18.71618  -8.97510  1.000 73.90550  ? 121 GLN B N     1 
ATOM   2827 C  CA    . GLN B 1  91  ? 19.09204  19.06290  -7.64721  1.000 72.51305  ? 121 GLN B CA    1 
ATOM   2828 C  C     . GLN B 1  91  ? 19.16211  20.57387  -7.47892  1.000 68.17148  ? 121 GLN B C     1 
ATOM   2829 O  O     . GLN B 1  91  ? 19.40775  21.31906  -8.43586  1.000 72.66695  ? 121 GLN B O     1 
ATOM   2830 C  CB    . GLN B 1  91  ? 20.47314  18.45584  -7.38286  1.000 71.70499  ? 121 GLN B CB    1 
ATOM   2831 C  CG    . GLN B 1  91  ? 20.98067  18.67054  -5.97000  1.000 76.02015  ? 121 GLN B CG    1 
ATOM   2832 C  CD    . GLN B 1  91  ? 22.36574  18.09949  -5.76564  1.000 78.48464  ? 121 GLN B CD    1 
ATOM   2833 O  OE1   . GLN B 1  91  ? 23.24943  18.29766  -6.59493  1.000 74.60914  ? 121 GLN B OE1   1 
ATOM   2834 N  NE2   . GLN B 1  91  ? 22.54815  17.37327  -4.67186  1.000 72.09492  ? 121 GLN B NE2   1 
ATOM   2835 N  N     . LYS B 1  92  ? 18.92157  21.01761  -6.24374  1.000 68.29417  ? 122 LYS B N     1 
ATOM   2836 C  CA    . LYS B 1  92  ? 19.17874  22.38552  -5.81255  1.000 71.99676  ? 122 LYS B CA    1 
ATOM   2837 C  C     . LYS B 1  92  ? 19.76627  22.32622  -4.41178  1.000 82.52874  ? 122 LYS B C     1 
ATOM   2838 O  O     . LYS B 1  92  ? 19.77751  21.27309  -3.76201  1.000 83.40093  ? 122 LYS B O     1 
ATOM   2839 C  CB    . LYS B 1  92  ? 17.90674  23.24353  -5.84290  1.000 68.59800  ? 122 LYS B CB    1 
ATOM   2840 C  CG    . LYS B 1  92  ? 17.41921  23.54983  -7.24265  1.000 70.76223  ? 122 LYS B CG    1 
ATOM   2841 C  CD    . LYS B 1  92  ? 16.22321  24.49983  -7.25100  1.000 72.21942  ? 122 LYS B CD    1 
ATOM   2842 C  CE    . LYS B 1  92  ? 16.58641  25.88273  -6.74385  1.000 71.98818  ? 122 LYS B CE    1 
ATOM   2843 N  NZ    . LYS B 1  92  ? 15.46134  26.83977  -6.94623  1.000 75.42422  ? 122 LYS B NZ    1 
ATOM   2844 N  N     . ASP B 1  93  ? 20.26545  23.46912  -3.94273  1.000 86.86979  ? 123 ASP B N     1 
ATOM   2845 C  CA    . ASP B 1  93  ? 21.00992  23.52986  -2.68300  1.000 80.15404  ? 123 ASP B CA    1 
ATOM   2846 C  C     . ASP B 1  93  ? 20.04036  23.73562  -1.52359  1.000 85.20530  ? 123 ASP B C     1 
ATOM   2847 O  O     . ASP B 1  93  ? 19.80054  24.85053  -1.05127  1.000 100.34388 ? 123 ASP B O     1 
ATOM   2848 C  CB    . ASP B 1  93  ? 22.05791  24.63087  -2.74016  1.000 84.46398  ? 123 ASP B CB    1 
ATOM   2849 C  CG    . ASP B 1  93  ? 22.95736  24.64361  -1.52050  1.000 96.54081  ? 123 ASP B CG    1 
ATOM   2850 O  OD1   . ASP B 1  93  ? 22.89066  23.68644  -0.72067  1.000 99.36366  ? 123 ASP B OD1   1 
ATOM   2851 O  OD2   . ASP B 1  93  ? 23.72343  25.61857  -1.35658  1.000 91.81832  ? 123 ASP B OD2   1 
ATOM   2852 N  N     . PHE B 1  94  ? 19.47853  22.62653  -1.04661  1.000 73.75218  ? 124 PHE B N     1 
ATOM   2853 C  CA    . PHE B 1  94  ? 18.65999  22.65428  0.16070   1.000 68.07795  ? 124 PHE B CA    1 
ATOM   2854 C  C     . PHE B 1  94  ? 18.84726  21.34912  0.91536   1.000 71.45826  ? 124 PHE B C     1 
ATOM   2855 O  O     . PHE B 1  94  ? 19.02503  20.28725  0.30607   1.000 74.54394  ? 124 PHE B O     1 
ATOM   2856 C  CB    . PHE B 1  94  ? 17.17787  22.90535  -0.15669  1.000 68.00851  ? 124 PHE B CB    1 
ATOM   2857 C  CG    . PHE B 1  94  ? 16.51158  21.78851  -0.91268  1.000 76.72831  ? 124 PHE B CG    1 
ATOM   2858 C  CD1   . PHE B 1  94  ? 16.64806  21.68480  -2.28375  1.000 73.88138  ? 124 PHE B CD1   1 
ATOM   2859 C  CD2   . PHE B 1  94  ? 15.73682  20.85338  -0.24958  1.000 68.93084  ? 124 PHE B CD2   1 
ATOM   2860 C  CE1   . PHE B 1  94  ? 16.03580  20.65795  -2.98273  1.000 67.53683  ? 124 PHE B CE1   1 
ATOM   2861 C  CE2   . PHE B 1  94  ? 15.12156  19.82953  -0.93956  1.000 66.18370  ? 124 PHE B CE2   1 
ATOM   2862 C  CZ    . PHE B 1  94  ? 15.26905  19.73281  -2.30764  1.000 71.32341  ? 124 PHE B CZ    1 
ATOM   2863 N  N     . LEU B 1  95  ? 18.84276  21.43984  2.24538   1.000 70.65014  ? 125 LEU B N     1 
ATOM   2864 C  CA    . LEU B 1  95  ? 19.02507  20.27167  3.09007   1.000 73.48634  ? 125 LEU B CA    1 
ATOM   2865 C  C     . LEU B 1  95  ? 17.92996  19.24973  2.80726   1.000 75.01511  ? 125 LEU B C     1 
ATOM   2866 O  O     . LEU B 1  95  ? 16.75808  19.47667  3.12275   1.000 69.57224  ? 125 LEU B O     1 
ATOM   2867 C  CB    . LEU B 1  95  ? 19.03563  20.66536  4.56914   1.000 74.31021  ? 125 LEU B CB    1 
ATOM   2868 C  CG    . LEU B 1  95  ? 19.22700  19.52915  5.57684   1.000 79.56845  ? 125 LEU B CG    1 
ATOM   2869 C  CD1   . LEU B 1  95  ? 20.58193  18.86218  5.39919   1.000 72.77621  ? 125 LEU B CD1   1 
ATOM   2870 C  CD2   . LEU B 1  95  ? 19.04354  20.03085  7.00201   1.000 75.63611  ? 125 LEU B CD2   1 
ATOM   2871 N  N     . ASP B 1  96  ? 18.30873  18.12685  2.21489   1.000 75.55738  ? 126 ASP B N     1 
ATOM   2872 C  CA    . ASP B 1  96  ? 17.34357  17.11995  1.77804   1.000 74.21931  ? 126 ASP B CA    1 
ATOM   2873 C  C     . ASP B 1  96  ? 16.90401  16.29670  2.98504   1.000 67.26325  ? 126 ASP B C     1 
ATOM   2874 O  O     . ASP B 1  96  ? 17.47613  15.25363  3.30060   1.000 67.65787  ? 126 ASP B O     1 
ATOM   2875 C  CB    . ASP B 1  96  ? 17.93715  16.24617  0.68164   1.000 73.67362  ? 126 ASP B CB    1 
ATOM   2876 C  CG    . ASP B 1  96  ? 16.88087  15.46633  -0.05413  1.000 70.80441  ? 126 ASP B CG    1 
ATOM   2877 O  OD1   . ASP B 1  96  ? 15.71804  15.48824  0.39731   1.000 69.24752  ? 126 ASP B OD1   1 
ATOM   2878 O  OD2   . ASP B 1  96  ? 17.20848  14.84554  -1.08238  1.000 67.06949  ? 126 ASP B OD2   1 
ATOM   2879 N  N     . VAL B 1  97  ? 15.86227  16.77656  3.66353   1.000 63.20552  ? 127 VAL B N     1 
ATOM   2880 C  CA    . VAL B 1  97  ? 15.28270  16.09233  4.81060   1.000 67.70457  ? 127 VAL B CA    1 
ATOM   2881 C  C     . VAL B 1  97  ? 13.76965  16.16536  4.68318   1.000 63.71242  ? 127 VAL B C     1 
ATOM   2882 O  O     . VAL B 1  97  ? 13.22438  16.98452  3.94056   1.000 59.42444  ? 127 VAL B O     1 
ATOM   2883 C  CB    . VAL B 1  97  ? 15.73521  16.69205  6.15556   1.000 72.56760  ? 127 VAL B CB    1 
ATOM   2884 C  CG1   . VAL B 1  97  ? 17.23327  16.49600  6.34095   1.000 66.57926  ? 127 VAL B CG1   1 
ATOM   2885 C  CG2   . VAL B 1  97  ? 15.35824  18.17203  6.21701   1.000 65.36402  ? 127 VAL B CG2   1 
ATOM   2886 N  N     . TYR B 1  98  ? 13.09193  15.30121  5.43426   1.000 55.10148  ? 128 TYR B N     1 
ATOM   2887 C  CA    . TYR B 1  98  ? 11.65286  15.17125  5.25777   1.000 56.56049  ? 128 TYR B CA    1 
ATOM   2888 C  C     . TYR B 1  98  ? 10.97389  16.53525  5.30631   1.000 57.60625  ? 128 TYR B C     1 
ATOM   2889 O  O     . TYR B 1  98  ? 10.14856  16.86043  4.44369   1.000 59.21347  ? 128 TYR B O     1 
ATOM   2890 C  CB    . TYR B 1  98  ? 11.07025  14.23004  6.30979   1.000 51.94244  ? 128 TYR B CB    1 
ATOM   2891 C  CG    . TYR B 1  98  ? 9.67612   13.78012  5.96122   1.000 58.71643  ? 128 TYR B CG    1 
ATOM   2892 C  CD1   . TYR B 1  98  ? 9.46879   12.70129  5.10908   1.000 57.38111  ? 128 TYR B CD1   1 
ATOM   2893 C  CD2   . TYR B 1  98  ? 8.56331   14.44402  6.45878   1.000 63.11988  ? 128 TYR B CD2   1 
ATOM   2894 C  CE1   . TYR B 1  98  ? 8.19267   12.28937  4.77547   1.000 63.71800  ? 128 TYR B CE1   1 
ATOM   2895 C  CE2   . TYR B 1  98  ? 7.28518   14.04309  6.13318   1.000 57.47346  ? 128 TYR B CE2   1 
ATOM   2896 C  CZ    . TYR B 1  98  ? 7.10586   12.96427  5.28502   1.000 60.38609  ? 128 TYR B CZ    1 
ATOM   2897 O  OH    . TYR B 1  98  ? 5.83273   12.56034  4.95241   1.000 75.90482  ? 128 TYR B OH    1 
ATOM   2898 N  N     . TYR B 1  99  ? 11.34026  17.36104  6.28034   1.000 58.70564  ? 129 TYR B N     1 
ATOM   2899 C  CA    . TYR B 1  99  ? 10.61435  18.60500  6.50488   1.000 56.48198  ? 129 TYR B CA    1 
ATOM   2900 C  C     . TYR B 1  99  ? 10.96498  19.69520  5.50997   1.000 62.67112  ? 129 TYR B C     1 
ATOM   2901 O  O     . TYR B 1  99  ? 10.48203  20.82118  5.64239   1.000 62.77818  ? 129 TYR B O     1 
ATOM   2902 C  CB    . TYR B 1  99  ? 10.83189  19.06970  7.94389   1.000 56.45831  ? 129 TYR B CB    1 
ATOM   2903 C  CG    . TYR B 1  99  ? 10.07523  18.15351  8.86398   1.000 64.23712  ? 129 TYR B CG    1 
ATOM   2904 C  CD1   . TYR B 1  99  ? 8.78710   17.74358  8.53538   1.000 64.64977  ? 129 TYR B CD1   1 
ATOM   2905 C  CD2   . TYR B 1  99  ? 10.64866  17.63927  10.01966  1.000 62.37173  ? 129 TYR B CD2   1 
ATOM   2906 C  CE1   . TYR B 1  99  ? 8.07740   16.89042  9.33947   1.000 74.71566  ? 129 TYR B CE1   1 
ATOM   2907 C  CE2   . TYR B 1  99  ? 9.94396   16.77110  10.84075  1.000 73.30695  ? 129 TYR B CE2   1 
ATOM   2908 C  CZ    . TYR B 1  99  ? 8.65883   16.40218  10.48915  1.000 77.99015  ? 129 TYR B CZ    1 
ATOM   2909 O  OH    . TYR B 1  99  ? 7.93512   15.54102  11.28324  1.000 73.72990  ? 129 TYR B OH    1 
ATOM   2910 N  N     . ASN B 1  100 ? 11.75760  19.37041  4.49561   1.000 64.13286  ? 130 ASN B N     1 
ATOM   2911 C  CA    . ASN B 1  100 ? 11.97118  20.25465  3.36371   1.000 58.56392  ? 130 ASN B CA    1 
ATOM   2912 C  C     . ASN B 1  100 ? 11.32169  19.73491  2.08784   1.000 56.86713  ? 130 ASN B C     1 
ATOM   2913 O  O     . ASN B 1  100 ? 11.62029  20.24114  0.99984   1.000 57.90252  ? 130 ASN B O     1 
ATOM   2914 C  CB    . ASN B 1  100 ? 13.45909  20.46668  3.13920   1.000 63.41513  ? 130 ASN B CB    1 
ATOM   2915 C  CG    . ASN B 1  100 ? 13.94032  21.75956  3.71828   1.000 70.25670  ? 130 ASN B CG    1 
ATOM   2916 O  OD1   . ASN B 1  100 ? 13.15844  22.66750  4.02977   1.000 72.78431  ? 130 ASN B OD1   1 
ATOM   2917 N  ND2   . ASN B 1  100 ? 15.24637  21.85552  3.87181   1.000 81.91610  ? 130 ASN B ND2   1 
ATOM   2918 N  N     . LEU B 1  101 ? 10.43273  18.74690  2.19797   1.000 51.87943  ? 131 LEU B N     1 
ATOM   2919 C  CA    . LEU B 1  101 ? 9.81228   18.19115  1.00409   1.000 49.12758  ? 131 LEU B CA    1 
ATOM   2920 C  C     . LEU B 1  101 ? 9.03299   19.24331  0.22560   1.000 51.21717  ? 131 LEU B C     1 
ATOM   2921 O  O     . LEU B 1  101 ? 9.00753   19.18957  -1.01240  1.000 51.11286  ? 131 LEU B O     1 
ATOM   2922 C  CB    . LEU B 1  101 ? 8.91642   17.00707  1.38118   1.000 46.87828  ? 131 LEU B CB    1 
ATOM   2923 C  CG    . LEU B 1  101 ? 9.71251   15.73001  1.64662   1.000 43.04885  ? 131 LEU B CG    1 
ATOM   2924 C  CD1   . LEU B 1  101 ? 8.79065   14.58793  2.04772   1.000 45.62748  ? 131 LEU B CD1   1 
ATOM   2925 C  CD2   . LEU B 1  101 ? 10.55305  15.35026  0.42922   1.000 43.91212  ? 131 LEU B CD2   1 
ATOM   2926 N  N     . THR B 1  102 ? 8.40325   20.21318  0.89904   1.000 50.80057  ? 132 THR B N     1 
ATOM   2927 C  CA    . THR B 1  102 ? 7.74497   21.27934  0.14651   1.000 41.76580  ? 132 THR B CA    1 
ATOM   2928 C  C     . THR B 1  102 ? 8.73461   21.90453  -0.82373  1.000 46.87550  ? 132 THR B C     1 
ATOM   2929 O  O     . THR B 1  102 ? 8.45716   22.02978  -2.02460  1.000 53.22970  ? 132 THR B O     1 
ATOM   2930 C  CB    . THR B 1  102 ? 7.14733   22.33815  1.07395   1.000 44.87301  ? 132 THR B CB    1 
ATOM   2931 O  OG1   . THR B 1  102 ? 6.15264   21.75198  1.91520   1.000 43.27538  ? 132 THR B OG1   1 
ATOM   2932 C  CG2   . THR B 1  102 ? 6.47802   23.43832  0.25343   1.000 39.45675  ? 132 THR B CG2   1 
ATOM   2933 N  N     . LEU B 1  103 ? 9.93180   22.23342  -0.32711  1.000 50.28852  ? 133 LEU B N     1 
ATOM   2934 C  CA    . LEU B 1  103 ? 10.98347  22.74260  -1.20140  1.000 46.79126  ? 133 LEU B CA    1 
ATOM   2935 C  C     . LEU B 1  103 ? 11.22503  21.78384  -2.36169  1.000 49.73897  ? 133 LEU B C     1 
ATOM   2936 O  O     . LEU B 1  103 ? 11.16060  22.17908  -3.53359  1.000 57.16620  ? 133 LEU B O     1 
ATOM   2937 C  CB    . LEU B 1  103 ? 12.26877  22.97543  -0.40484  1.000 54.01303  ? 133 LEU B CB    1 
ATOM   2938 C  CG    . LEU B 1  103 ? 12.13525  23.87317  0.84040   1.000 66.83765  ? 133 LEU B CG    1 
ATOM   2939 C  CD1   . LEU B 1  103 ? 13.50447  24.21604  1.43196   1.000 62.55796  ? 133 LEU B CD1   1 
ATOM   2940 C  CD2   . LEU B 1  103 ? 11.34514  25.13024  0.53496   1.000 51.96203  ? 133 LEU B CD2   1 
ATOM   2941 N  N     . LYS B 1  104 ? 11.45414  20.50378  -2.05605  1.000 51.26433  ? 134 LYS B N     1 
ATOM   2942 C  CA    . LYS B 1  104 ? 11.68674  19.54300  -3.12933  1.000 48.08478  ? 134 LYS B CA    1 
ATOM   2943 C  C     . LYS B 1  104 ? 10.55036  19.60421  -4.14189  1.000 49.97389  ? 134 LYS B C     1 
ATOM   2944 O  O     . LYS B 1  104 ? 10.78590  19.75646  -5.34695  1.000 49.58185  ? 134 LYS B O     1 
ATOM   2945 C  CB    . LYS B 1  104 ? 11.84494  18.12988  -2.56569  1.000 45.34783  ? 134 LYS B CB    1 
ATOM   2946 C  CG    . LYS B 1  104 ? 12.09853  17.10310  -3.64899  1.000 48.35812  ? 134 LYS B CG    1 
ATOM   2947 C  CD    . LYS B 1  104 ? 12.56874  15.79298  -3.07744  1.000 59.59479  ? 134 LYS B CD    1 
ATOM   2948 C  CE    . LYS B 1  104 ? 13.99793  15.89487  -2.57696  1.000 50.71864  ? 134 LYS B CE    1 
ATOM   2949 N  NZ    . LYS B 1  104 ? 14.59798  14.54184  -2.41747  1.000 59.24303  ? 134 LYS B NZ    1 
ATOM   2950 N  N     . THR B 1  105 ? 9.30254   19.57312  -3.66343  1.000 39.91638  ? 135 THR B N     1 
ATOM   2951 C  CA    . THR B 1  105 ? 8.19418   19.59532  -4.61201  1.000 46.67481  ? 135 THR B CA    1 
ATOM   2952 C  C     . THR B 1  105 ? 8.24787   20.87150  -5.44077  1.000 48.99927  ? 135 THR B C     1 
ATOM   2953 O  O     . THR B 1  105 ? 8.20541   20.82975  -6.68076  1.000 53.42181  ? 135 THR B O     1 
ATOM   2954 C  CB    . THR B 1  105 ? 6.85945   19.45318  -3.88354  1.000 41.51442  ? 135 THR B CB    1 
ATOM   2955 O  OG1   . THR B 1  105 ? 6.65757   18.07311  -3.54075  1.000 44.05824  ? 135 THR B OG1   1 
ATOM   2956 C  CG2   . THR B 1  105 ? 5.70713   19.93137  -4.75701  1.000 39.08503  ? 135 THR B CG2   1 
ATOM   2957 N  N     . MET B 1  106 ? 8.42013   22.01836  -4.77559  1.000 46.30561  ? 136 MET B N     1 
ATOM   2958 C  CA    . MET B 1  106 ? 8.47485   23.26451  -5.53235  1.000 47.01365  ? 136 MET B CA    1 
ATOM   2959 C  C     . MET B 1  106 ? 9.66350   23.26471  -6.48080  1.000 56.41461  ? 136 MET B C     1 
ATOM   2960 O  O     . MET B 1  106 ? 9.54507   23.71194  -7.62966  1.000 56.41507  ? 136 MET B O     1 
ATOM   2961 C  CB    . MET B 1  106 ? 8.49721   24.46732  -4.59511  1.000 51.38099  ? 136 MET B CB    1 
ATOM   2962 C  CG    . MET B 1  106 ? 7.13344   24.79120  -3.97953  1.000 54.42601  ? 136 MET B CG    1 
ATOM   2963 S  SD    . MET B 1  106 ? 5.75900   24.85645  -5.15900  1.000 56.25810  ? 136 MET B SD    1 
ATOM   2964 C  CE    . MET B 1  106 ? 6.38957   26.06469  -6.32599  1.000 53.07308  ? 136 MET B CE    1 
ATOM   2965 N  N     . MET B 1  107 ? 10.80065  22.69361  -6.05534  1.000 52.62601  ? 137 MET B N     1 
ATOM   2966 C  CA    . MET B 1  107 ? 11.90130  22.54280  -6.99579  1.000 52.64629  ? 137 MET B CA    1 
ATOM   2967 C  C     . MET B 1  107 ? 11.39782  21.90407  -8.27873  1.000 54.64849  ? 137 MET B C     1 
ATOM   2968 O  O     . MET B 1  107 ? 11.47041  22.49930  -9.35964  1.000 54.02721  ? 137 MET B O     1 
ATOM   2969 C  CB    . MET B 1  107 ? 13.03152  21.71367  -6.39639  1.000 55.66624  ? 137 MET B CB    1 
ATOM   2970 C  CG    . MET B 1  107 ? 14.15615  21.43387  -7.39087  1.000 45.77904  ? 137 MET B CG    1 
ATOM   2971 S  SD    . MET B 1  107 ? 15.51539  20.45873  -6.73258  1.000 57.37536  ? 137 MET B SD    1 
ATOM   2972 C  CE    . MET B 1  107 ? 14.69851  18.90066  -6.37860  1.000 54.15854  ? 137 MET B CE    1 
ATOM   2973 N  N     . GLY B 1  108 ? 10.80786  20.71105  -8.15476  1.000 54.04269  ? 138 GLY B N     1 
ATOM   2974 C  CA    . GLY B 1  108 ? 10.33141  20.01730  -9.33873  1.000 47.84677  ? 138 GLY B CA    1 
ATOM   2975 C  C     . GLY B 1  108 ? 9.39011   20.88447  -10.14519 1.000 49.47586  ? 138 GLY B C     1 
ATOM   2976 O  O     . GLY B 1  108 ? 9.51965   21.00372  -11.36522 1.000 49.53245  ? 138 GLY B O     1 
ATOM   2977 N  N     . ILE B 1  109 ? 8.45137   21.54233  -9.46370  1.000 47.13071  ? 139 ILE B N     1 
ATOM   2978 C  CA    . ILE B 1  109 ? 7.48110   22.34749  -10.18717 1.000 51.31238  ? 139 ILE B CA    1 
ATOM   2979 C  C     . ILE B 1  109 ? 8.20084   23.47963  -10.90521 1.000 53.82955  ? 139 ILE B C     1 
ATOM   2980 O  O     . ILE B 1  109 ? 8.00039   23.70488  -12.10608 1.000 59.68699  ? 139 ILE B O     1 
ATOM   2981 C  CB    . ILE B 1  109 ? 6.38246   22.85129  -9.23265  1.000 51.71938  ? 139 ILE B CB    1 
ATOM   2982 C  CG1   . ILE B 1  109 ? 5.43958   21.69323  -8.89654  1.000 53.95128  ? 139 ILE B CG1   1 
ATOM   2983 C  CG2   . ILE B 1  109 ? 5.62324   24.02242  -9.83813  1.000 52.27130  ? 139 ILE B CG2   1 
ATOM   2984 C  CD1   . ILE B 1  109 ? 4.46400   21.99000  -7.79411  1.000 52.05638  ? 139 ILE B CD1   1 
ATOM   2985 N  N     . GLU B 1  110 ? 9.11211   24.15548  -10.19441 1.000 54.71691  ? 140 GLU B N     1 
ATOM   2986 C  CA    . GLU B 1  110 ? 9.91487   25.18561  -10.83949 1.000 51.10949  ? 140 GLU B CA    1 
ATOM   2987 C  C     . GLU B 1  110 ? 10.55239  24.63587  -12.10585 1.000 64.99332  ? 140 GLU B C     1 
ATOM   2988 O  O     . GLU B 1  110 ? 10.49300  25.26609  -13.16769 1.000 64.70206  ? 140 GLU B O     1 
ATOM   2989 C  CB    . GLU B 1  110 ? 10.98123  25.71241  -9.87878  1.000 59.72717  ? 140 GLU B CB    1 
ATOM   2990 C  CG    . GLU B 1  110 ? 11.84902  26.81952  -10.47088 1.000 66.48712  ? 140 GLU B CG    1 
ATOM   2991 C  CD    . GLU B 1  110 ? 12.96037  27.27532  -9.53520  1.000 76.06321  ? 140 GLU B CD    1 
ATOM   2992 O  OE1   . GLU B 1  110 ? 13.03579  26.75909  -8.39634  1.000 74.68232  ? 140 GLU B OE1   1 
ATOM   2993 O  OE2   . GLU B 1  110 ? 13.76522  28.14840  -9.93732  1.000 79.63462  ? 140 GLU B OE2   1 
ATOM   2994 N  N     . TRP B 1  111 ? 11.12342  23.42785  -12.02531 1.000 68.99866  ? 141 TRP B N     1 
ATOM   2995 C  CA    . TRP B 1  111 ? 11.78097  22.86209  -13.19968 1.000 66.28647  ? 141 TRP B CA    1 
ATOM   2996 C  C     . TRP B 1  111 ? 10.79554  22.74034  -14.35633 1.000 61.11389  ? 141 TRP B C     1 
ATOM   2997 O  O     . TRP B 1  111 ? 11.05513  23.24157  -15.46033 1.000 58.58125  ? 141 TRP B O     1 
ATOM   2998 C  CB    . TRP B 1  111 ? 12.40810  21.51102  -12.85819 1.000 67.26999  ? 141 TRP B CB    1 
ATOM   2999 C  CG    . TRP B 1  111 ? 13.20767  20.91025  -13.97962 1.000 77.31099  ? 141 TRP B CG    1 
ATOM   3000 C  CD1   . TRP B 1  111 ? 14.53657  21.11130  -14.24008 1.000 76.65797  ? 141 TRP B CD1   1 
ATOM   3001 C  CD2   . TRP B 1  111 ? 12.73529  20.00246  -14.98463 1.000 74.53319  ? 141 TRP B CD2   1 
ATOM   3002 N  NE1   . TRP B 1  111 ? 14.91616  20.38752  -15.34537 1.000 78.05395  ? 141 TRP B NE1   1 
ATOM   3003 C  CE2   . TRP B 1  111 ? 13.82898  19.69863  -15.81810 1.000 77.85774  ? 141 TRP B CE2   1 
ATOM   3004 C  CE3   . TRP B 1  111 ? 11.49419  19.41852  -15.25629 1.000 64.93864  ? 141 TRP B CE3   1 
ATOM   3005 C  CZ2   . TRP B 1  111 ? 13.71756  18.83586  -16.91024 1.000 77.07685  ? 141 TRP B CZ2   1 
ATOM   3006 C  CZ3   . TRP B 1  111 ? 11.38778  18.56275  -16.33443 1.000 71.61400  ? 141 TRP B CZ3   1 
ATOM   3007 C  CH2   . TRP B 1  111 ? 12.49047  18.28191  -17.14990 1.000 72.04609  ? 141 TRP B CH2   1 
ATOM   3008 N  N     . VAL B 1  112 ? 9.62663   22.13629  -14.11002 1.000 60.17966  ? 142 VAL B N     1 
ATOM   3009 C  CA    . VAL B 1  112 ? 8.65322   22.01452  -15.19068 1.000 52.10295  ? 142 VAL B CA    1 
ATOM   3010 C  C     . VAL B 1  112 ? 8.33102   23.39464  -15.74427 1.000 60.99330  ? 142 VAL B C     1 
ATOM   3011 O  O     . VAL B 1  112 ? 8.18657   23.57989  -16.96218 1.000 52.72959  ? 142 VAL B O     1 
ATOM   3012 C  CB    . VAL B 1  112 ? 7.38040   21.29043  -14.70635 1.000 49.92101  ? 142 VAL B CB    1 
ATOM   3013 C  CG1   . VAL B 1  112 ? 6.33498   21.28266  -15.81796 1.000 45.37654  ? 142 VAL B CG1   1 
ATOM   3014 C  CG2   . VAL B 1  112 ? 7.71756   19.87733  -14.26177 1.000 44.46759  ? 142 VAL B CG2   1 
ATOM   3015 N  N     . HIS B 1  113 ? 8.23536   24.39346  -14.86503 1.000 59.66111  ? 143 HIS B N     1 
ATOM   3016 C  CA    . HIS B 1  113 ? 7.87119   25.72855  -15.31561 1.000 58.37112  ? 143 HIS B CA    1 
ATOM   3017 C  C     . HIS B 1  113 ? 8.98188   26.35672  -16.15090 1.000 59.82165  ? 143 HIS B C     1 
ATOM   3018 O  O     . HIS B 1  113 ? 8.70953   27.10292  -17.09564 1.000 54.33041  ? 143 HIS B O     1 
ATOM   3019 C  CB    . HIS B 1  113 ? 7.53965   26.61530  -14.11531 1.000 60.38078  ? 143 HIS B CB    1 
ATOM   3020 C  CG    . HIS B 1  113 ? 7.41453   28.06638  -14.45396 1.000 62.70423  ? 143 HIS B CG    1 
ATOM   3021 N  ND1   . HIS B 1  113 ? 6.42622   28.55755  -15.27548 1.000 57.63599  ? 143 HIS B ND1   1 
ATOM   3022 C  CD2   . HIS B 1  113 ? 8.15168   29.13929  -14.07001 1.000 61.33004  ? 143 HIS B CD2   1 
ATOM   3023 C  CE1   . HIS B 1  113 ? 6.55619   29.86857  -15.38826 1.000 67.68653  ? 143 HIS B CE1   1 
ATOM   3024 N  NE2   . HIS B 1  113 ? 7.59646   30.24342  -14.66657 1.000 61.90957  ? 143 HIS B NE2   1 
ATOM   3025 N  N     . ARG B 1  114 ? 10.23901  26.06565  -15.81943 1.000 64.09799  ? 144 ARG B N     1 
ATOM   3026 C  CA    . ARG B 1  114 ? 11.34475  26.71478  -16.50571 1.000 61.80283  ? 144 ARG B CA    1 
ATOM   3027 C  C     . ARG B 1  114 ? 11.78528  25.94504  -17.74104 1.000 64.70866  ? 144 ARG B C     1 
ATOM   3028 O  O     . ARG B 1  114 ? 11.99189  26.54526  -18.79999 1.000 71.86036  ? 144 ARG B O     1 
ATOM   3029 C  CB    . ARG B 1  114 ? 12.54211  26.88058  -15.56513 1.000 65.58977  ? 144 ARG B CB    1 
ATOM   3030 C  CG    . ARG B 1  114 ? 12.31653  27.86835  -14.43384 1.000 63.29336  ? 144 ARG B CG    1 
ATOM   3031 C  CD    . ARG B 1  114 ? 13.63679  28.19420  -13.75026 1.000 74.93101  ? 144 ARG B CD    1 
ATOM   3032 N  NE    . ARG B 1  114 ? 13.44127  28.89294  -12.48705 1.000 89.81491  ? 144 ARG B NE    1 
ATOM   3033 C  CZ    . ARG B 1  114 ? 13.13131  30.17992  -12.38566 1.000 86.42728  ? 144 ARG B CZ    1 
ATOM   3034 N  NH1   . ARG B 1  114 ? 12.96092  30.93914  -13.45644 1.000 72.28184  ? 144 ARG B NH1   1 
ATOM   3035 N  NH2   . ARG B 1  114 ? 12.98377  30.71367  -11.17550 1.000 96.02863  ? 144 ARG B NH2   1 
ATOM   3036 N  N     . PHE B 1  115 ? 11.92732  24.62801  -17.63337 1.000 70.63765  ? 145 PHE B N     1 
ATOM   3037 C  CA    . PHE B 1  115 ? 12.59693  23.85523  -18.66078 1.000 63.00541  ? 145 PHE B CA    1 
ATOM   3038 C  C     . PHE B 1  115 ? 11.71366  22.82337  -19.35366 1.000 65.40710  ? 145 PHE B C     1 
ATOM   3039 O  O     . PHE B 1  115 ? 12.18931  22.17057  -20.28998 1.000 73.54934  ? 145 PHE B O     1 
ATOM   3040 C  CB    . PHE B 1  115 ? 13.82915  23.16509  -18.06338 1.000 65.47620  ? 145 PHE B CB    1 
ATOM   3041 C  CG    . PHE B 1  115 ? 14.69746  24.08792  -17.26152 1.000 77.82730  ? 145 PHE B CG    1 
ATOM   3042 C  CD1   . PHE B 1  115 ? 15.39623  25.11205  -17.88157 1.000 86.68875  ? 145 PHE B CD1   1 
ATOM   3043 C  CD2   . PHE B 1  115 ? 14.80497  23.94864  -15.88559 1.000 76.41338  ? 145 PHE B CD2   1 
ATOM   3044 C  CE1   . PHE B 1  115 ? 16.18951  25.97689  -17.14668 1.000 87.68751  ? 145 PHE B CE1   1 
ATOM   3045 C  CE2   . PHE B 1  115 ? 15.60225  24.80348  -15.14471 1.000 76.32373  ? 145 PHE B CE2   1 
ATOM   3046 C  CZ    . PHE B 1  115 ? 16.29502  25.82061  -15.77976 1.000 78.41397  ? 145 PHE B CZ    1 
ATOM   3047 N  N     . CYS B 1  116 ? 10.46082  22.66230  -18.94722 1.000 61.08845  ? 146 CYS B N     1 
ATOM   3048 C  CA    . CYS B 1  116 ? 9.64854   21.68745  -19.65712 1.000 59.55908  ? 146 CYS B CA    1 
ATOM   3049 C  C     . CYS B 1  116 ? 8.16656   22.04544  -19.61149 1.000 63.31203  ? 146 CYS B C     1 
ATOM   3050 O  O     . CYS B 1  116 ? 7.32667   21.17739  -19.32736 1.000 62.40675  ? 146 CYS B O     1 
ATOM   3051 C  CB    . CYS B 1  116 ? 9.86676   20.29432  -19.07149 1.000 56.63562  ? 146 CYS B CB    1 
ATOM   3052 S  SG    . CYS B 1  116 ? 9.52332   18.92956  -20.21765 1.000 88.51807  ? 146 CYS B SG    1 
ATOM   3053 N  N     . PRO B 1  117 ? 7.79746   23.29951  -19.90309 1.000 60.01852  ? 147 PRO B N     1 
ATOM   3054 C  CA    . PRO B 1  117 ? 6.37046   23.66452  -19.90748 1.000 54.28838  ? 147 PRO B CA    1 
ATOM   3055 C  C     . PRO B 1  117 ? 5.59803   23.03976  -21.05332 1.000 62.65429  ? 147 PRO B C     1 
ATOM   3056 O  O     . PRO B 1  117 ? 4.36601   23.17377  -21.08883 1.000 56.55506  ? 147 PRO B O     1 
ATOM   3057 C  CB    . PRO B 1  117 ? 6.39643   25.19254  -20.01917 1.000 57.53833  ? 147 PRO B CB    1 
ATOM   3058 C  CG    . PRO B 1  117 ? 7.69016   25.48268  -20.72660 1.000 53.43317  ? 147 PRO B CG    1 
ATOM   3059 C  CD    . PRO B 1  117 ? 8.66534   24.44258  -20.25118 1.000 59.87974  ? 147 PRO B CD    1 
ATOM   3060 N  N     . GLN B 1  118 ? 6.27167   22.38295  -21.98571 1.000 66.77772  ? 148 GLN B N     1 
ATOM   3061 C  CA    . GLN B 1  118 ? 5.59227   21.68518  -23.06760 1.000 59.89354  ? 148 GLN B CA    1 
ATOM   3062 C  C     . GLN B 1  118 ? 5.03742   20.33909  -22.63267 1.000 64.00516  ? 148 GLN B C     1 
ATOM   3063 O  O     . GLN B 1  118 ? 4.28113   19.72325  -23.39352 1.000 62.63830  ? 148 GLN B O     1 
ATOM   3064 C  CB    . GLN B 1  118 ? 6.54582   21.49242  -24.25500 1.000 58.65902  ? 148 GLN B CB    1 
ATOM   3065 C  CG    . GLN B 1  118 ? 7.18163   22.78153  -24.78597 1.000 64.59954  ? 148 GLN B CG    1 
ATOM   3066 C  CD    . GLN B 1  118 ? 8.35495   23.24934  -23.94031 1.000 67.72154  ? 148 GLN B CD    1 
ATOM   3067 O  OE1   . GLN B 1  118 ? 8.73431   22.60514  -22.95959 1.000 72.06259  ? 148 GLN B OE1   1 
ATOM   3068 N  NE2   . GLN B 1  118 ? 8.93481   24.38542  -24.31729 1.000 67.34899  ? 148 GLN B NE2   1 
ATOM   3069 N  N     . ALA B 1  119 ? 5.38187   19.86684  -21.43590 1.000 58.15157  ? 149 ALA B N     1 
ATOM   3070 C  CA    . ALA B 1  119 ? 4.92603   18.55875  -20.98200 1.000 56.41345  ? 149 ALA B CA    1 
ATOM   3071 C  C     . ALA B 1  119 ? 3.40706   18.53374  -20.90444 1.000 57.12292  ? 149 ALA B C     1 
ATOM   3072 O  O     . ALA B 1  119 ? 2.78930   19.39861  -20.27703 1.000 56.85694  ? 149 ALA B O     1 
ATOM   3073 C  CB    . ALA B 1  119 ? 5.54154   18.22746  -19.62130 1.000 51.05087  ? 149 ALA B CB    1 
ATOM   3074 N  N     . ALA B 1  120 ? 2.79381   17.54988  -21.56341 1.000 48.82216  ? 150 ALA B N     1 
ATOM   3075 C  CA    . ALA B 1  120 ? 1.34183   17.46487  -21.50789 1.000 45.04781  ? 150 ALA B CA    1 
ATOM   3076 C  C     . ALA B 1  120 ? 0.87836   17.16558  -20.08877 1.000 50.64153  ? 150 ALA B C     1 
ATOM   3077 O  O     . ALA B 1  120 ? -0.12346  17.72449  -19.62628 1.000 48.32852  ? 150 ALA B O     1 
ATOM   3078 C  CB    . ALA B 1  120 ? 0.82346   16.40708  -22.48291 1.000 45.07098  ? 150 ALA B CB    1 
ATOM   3079 N  N     . PHE B 1  121 ? 1.60562   16.29543  -19.38423 1.000 44.00948  ? 151 PHE B N     1 
ATOM   3080 C  CA    . PHE B 1  121 ? 1.23112   15.90215  -18.03517 1.000 45.54487  ? 151 PHE B CA    1 
ATOM   3081 C  C     . PHE B 1  121 ? 2.48343   15.63797  -17.20769 1.000 46.54301  ? 151 PHE B C     1 
ATOM   3082 O  O     . PHE B 1  121 ? 3.52524   15.22708  -17.72617 1.000 49.39634  ? 151 PHE B O     1 
ATOM   3083 C  CB    . PHE B 1  121 ? 0.30712   14.67416  -18.04408 1.000 42.26231  ? 151 PHE B CB    1 
ATOM   3084 C  CG    . PHE B 1  121 ? -1.00414  14.91831  -18.72553 1.000 42.24792  ? 151 PHE B CG    1 
ATOM   3085 C  CD1   . PHE B 1  121 ? -2.04488  15.53817  -18.05402 1.000 41.88816  ? 151 PHE B CD1   1 
ATOM   3086 C  CD2   . PHE B 1  121 ? -1.18864  14.55958  -20.05154 1.000 42.77837  ? 151 PHE B CD2   1 
ATOM   3087 C  CE1   . PHE B 1  121 ? -3.25312  15.79031  -18.68651 1.000 42.06229  ? 151 PHE B CE1   1 
ATOM   3088 C  CE2   . PHE B 1  121 ? -2.39588  14.79772  -20.69104 1.000 42.91149  ? 151 PHE B CE2   1 
ATOM   3089 C  CZ    . PHE B 1  121 ? -3.43062  15.40859  -20.01452 1.000 47.65721  ? 151 PHE B CZ    1 
ATOM   3090 N  N     . VAL B 1  122 ? 2.35992   15.90570  -15.90959 1.000 41.93964  ? 152 VAL B N     1 
ATOM   3091 C  CA    . VAL B 1  122 ? 3.44228   15.72550  -14.95903 1.000 41.71693  ? 152 VAL B CA    1 
ATOM   3092 C  C     . VAL B 1  122 ? 2.88972   14.93626  -13.78399 1.000 40.74152  ? 152 VAL B C     1 
ATOM   3093 O  O     . VAL B 1  122 ? 1.80391   15.25216  -13.27752 1.000 41.48422  ? 152 VAL B O     1 
ATOM   3094 C  CB    . VAL B 1  122 ? 4.00247   17.07539  -14.46296 1.000 42.16565  ? 152 VAL B CB    1 
ATOM   3095 C  CG1   . VAL B 1  122 ? 5.15284   16.85418  -13.47244 1.000 44.04185  ? 152 VAL B CG1   1 
ATOM   3096 C  CG2   . VAL B 1  122 ? 4.44804   17.93264  -15.63395 1.000 44.61160  ? 152 VAL B CG2   1 
ATOM   3097 N  N     . MET B 1  123 ? 3.61287   13.91417  -13.36148 1.000 40.45980  ? 153 MET B N     1 
ATOM   3098 C  CA    . MET B 1  123 ? 3.28832   13.19291  -12.14150 1.000 43.65747  ? 153 MET B CA    1 
ATOM   3099 C  C     . MET B 1  123 ? 4.43969   13.33070  -11.15591 1.000 41.88905  ? 153 MET B C     1 
ATOM   3100 O  O     . MET B 1  123 ? 5.58657   13.02677  -11.48940 1.000 42.21226  ? 153 MET B O     1 
ATOM   3101 C  CB    . MET B 1  123 ? 3.01022   11.72097  -12.40971 1.000 39.35514  ? 153 MET B CB    1 
ATOM   3102 C  CG    . MET B 1  123 ? 2.85869   10.92071  -11.13782 1.000 44.14392  ? 153 MET B CG    1 
ATOM   3103 S  SD    . MET B 1  123 ? 2.27556   9.24678   -11.45194 1.000 49.56207  ? 153 MET B SD    1 
ATOM   3104 C  CE    . MET B 1  123 ? 1.83819   8.75443   -9.78288  1.000 57.00441  ? 153 MET B CE    1 
ATOM   3105 N  N     . LYS B 1  124 ? 4.12915   13.79445  -9.94869  1.000 42.38421  ? 154 LYS B N     1 
ATOM   3106 C  CA    . LYS B 1  124 ? 5.08456   13.81422  -8.84405  1.000 40.78729  ? 154 LYS B CA    1 
ATOM   3107 C  C     . LYS B 1  124 ? 4.77090   12.62603  -7.94118  1.000 41.98138  ? 154 LYS B C     1 
ATOM   3108 O  O     . LYS B 1  124 ? 3.62706   12.46595  -7.50378  1.000 42.18209  ? 154 LYS B O     1 
ATOM   3109 C  CB    . LYS B 1  124 ? 4.99386   15.13506  -8.08074  1.000 40.41542  ? 154 LYS B CB    1 
ATOM   3110 C  CG    . LYS B 1  124 ? 5.84333   15.20979  -6.80704  1.000 47.28277  ? 154 LYS B CG    1 
ATOM   3111 C  CD    . LYS B 1  124 ? 4.97078   14.88555  -5.61378  1.000 44.43766  ? 154 LYS B CD    1 
ATOM   3112 C  CE    . LYS B 1  124 ? 5.77022   14.40730  -4.43018  1.000 49.75694  ? 154 LYS B CE    1 
ATOM   3113 N  NZ    . LYS B 1  124 ? 4.83564   14.12207  -3.32489  1.000 59.31857  ? 154 LYS B NZ    1 
ATOM   3114 N  N     . THR B 1  125 ? 5.78699   11.79897  -7.67573  1.000 38.56266  ? 155 THR B N     1 
ATOM   3115 C  CA    . THR B 1  125 ? 5.58524   10.52483  -6.98792  1.000 47.49237  ? 155 THR B CA    1 
ATOM   3116 C  C     . THR B 1  125 ? 6.71561   10.22862  -5.99841  1.000 43.11309  ? 155 THR B C     1 
ATOM   3117 O  O     . THR B 1  125 ? 7.84556   10.69965  -6.15473  1.000 39.98116  ? 155 THR B O     1 
ATOM   3118 C  CB    . THR B 1  125 ? 5.46986   9.36404   -8.00212  1.000 49.26936  ? 155 THR B CB    1 
ATOM   3119 O  OG1   . THR B 1  125 ? 5.06110   8.16090   -7.33022  1.000 51.10820  ? 155 THR B OG1   1 
ATOM   3120 C  CG2   . THR B 1  125 ? 6.80960   9.12718   -8.68967  1.000 40.66559  ? 155 THR B CG2   1 
ATOM   3121 N  N     . ASP B 1  126 ? 6.38896   9.35542   -5.05746  1.000 45.33422  ? 156 ASP B N     1 
ATOM   3122 C  CA    . ASP B 1  126 ? 7.39633   8.91022   -4.07794  1.000 44.14028  ? 156 ASP B CA    1 
ATOM   3123 C  C     . ASP B 1  126 ? 8.19509   7.77634   -4.70947  1.000 46.56398  ? 156 ASP B C     1 
ATOM   3124 O  O     . ASP B 1  126 ? 7.82168   7.30957   -5.78943  1.000 48.52893  ? 156 ASP B O     1 
ATOM   3125 C  CB    . ASP B 1  126 ? 6.71582   8.56495   -2.75975  1.000 52.73749  ? 156 ASP B CB    1 
ATOM   3126 C  CG    . ASP B 1  126 ? 6.09610   9.74179   -2.02127  1.000 54.15804  ? 156 ASP B CG    1 
ATOM   3127 O  OD1   . ASP B 1  126 ? 6.32595   10.88888  -2.44912  1.000 53.06799  ? 156 ASP B OD1   1 
ATOM   3128 O  OD2   . ASP B 1  126 ? 5.40448   9.49959   -1.01907  1.000 61.48516  ? 156 ASP B OD2   1 
ATOM   3129 N  N     . SER B 1  127 ? 9.24234   7.33420   -4.03796  1.000 54.09964  ? 157 SER B N     1 
ATOM   3130 C  CA    . SER B 1  127 ? 10.14313  6.32131   -4.57150  1.000 53.91450  ? 157 SER B CA    1 
ATOM   3131 C  C     . SER B 1  127 ? 9.71825   4.90024   -4.23064  1.000 58.54405  ? 157 SER B C     1 
ATOM   3132 O  O     . SER B 1  127 ? 10.07497  3.96439   -4.95597  1.000 57.67747  ? 157 SER B O     1 
ATOM   3133 C  CB    . SER B 1  127 ? 11.56832  6.55819   -4.06699  1.000 46.72669  ? 157 SER B CB    1 
ATOM   3134 O  OG    . SER B 1  127 ? 11.62185  6.49190   -2.65602  1.000 56.17871  ? 157 SER B OG    1 
ATOM   3135 N  N     . ASP B 1  128 ? 8.97366   4.69801   -3.14940  1.000 46.55333  ? 158 ASP B N     1 
ATOM   3136 C  CA    . ASP B 1  128 ? 8.50478   3.35394   -2.79451  1.000 52.87929  ? 158 ASP B CA    1 
ATOM   3137 C  C     . ASP B 1  128 ? 7.13455   3.10308   -3.42305  1.000 50.07584  ? 158 ASP B C     1 
ATOM   3138 O  O     . ASP B 1  128 ? 6.12580   2.86495   -2.74972  1.000 43.47310  ? 158 ASP B O     1 
ATOM   3139 C  CB    . ASP B 1  128 ? 8.47735   3.18063   -1.28053  1.000 55.37608  ? 158 ASP B CB    1 
ATOM   3140 C  CG    . ASP B 1  128 ? 7.68461   4.26349   -0.59301  1.000 56.94087  ? 158 ASP B CG    1 
ATOM   3141 O  OD1   . ASP B 1  128 ? 7.70443   5.41159   -1.08978  1.000 54.62742  ? 158 ASP B OD1   1 
ATOM   3142 O  OD2   . ASP B 1  128 ? 7.03600   3.96528   0.43217   1.000 58.94019  ? 158 ASP B OD2   1 
ATOM   3143 N  N     . MET B 1  129 ? 7.12505   3.15236   -4.75603  1.000 39.94710  ? 159 MET B N     1 
ATOM   3144 C  CA    . MET B 1  129 ? 5.90375   3.13853   -5.53858  1.000 42.24224  ? 159 MET B CA    1 
ATOM   3145 C  C     . MET B 1  129 ? 6.02530   2.18677   -6.72082  1.000 38.96172  ? 159 MET B C     1 
ATOM   3146 O  O     . MET B 1  129 ? 7.10910   1.97688   -7.26427  1.000 44.11784  ? 159 MET B O     1 
ATOM   3147 C  CB    . MET B 1  129 ? 5.57555   4.54164   -6.08516  1.000 43.96844  ? 159 MET B CB    1 
ATOM   3148 C  CG    . MET B 1  129 ? 5.24895   5.60443   -5.04082  1.000 49.96989  ? 159 MET B CG    1 
ATOM   3149 S  SD    . MET B 1  129 ? 3.64024   5.43227   -4.26825  1.000 52.00132  ? 159 MET B SD    1 
ATOM   3150 C  CE    . MET B 1  129 ? 2.52276   5.99755   -5.56171  1.000 47.29100  ? 159 MET B CE    1 
ATOM   3151 N  N     . PHE B 1  130 ? 4.89315   1.61486   -7.11051  1.000 40.22260  ? 160 PHE B N     1 
ATOM   3152 C  CA    . PHE B 1  130 ? 4.72366   1.03614   -8.43257  1.000 37.87067  ? 160 PHE B CA    1 
ATOM   3153 C  C     . PHE B 1  130 ? 3.84536   1.98631   -9.23204  1.000 37.61666  ? 160 PHE B C     1 
ATOM   3154 O  O     . PHE B 1  130 ? 2.77454   2.38121   -8.75956  1.000 37.15537  ? 160 PHE B O     1 
ATOM   3155 C  CB    . PHE B 1  130 ? 4.07267   -0.34687  -8.37061  1.000 37.56999  ? 160 PHE B CB    1 
ATOM   3156 C  CG    . PHE B 1  130 ? 3.58617   -0.85159  -9.71554  1.000 41.94250  ? 160 PHE B CG    1 
ATOM   3157 C  CD1   . PHE B 1  130 ? 4.43085   -1.56042  -10.55600 1.000 39.03287  ? 160 PHE B CD1   1 
ATOM   3158 C  CD2   . PHE B 1  130 ? 2.28701   -0.60750  -10.13300 1.000 38.16271  ? 160 PHE B CD2   1 
ATOM   3159 C  CE1   . PHE B 1  130 ? 3.99138   -2.01916  -11.80393 1.000 39.60475  ? 160 PHE B CE1   1 
ATOM   3160 C  CE2   . PHE B 1  130 ? 1.84254   -1.05924  -11.36893 1.000 45.07419  ? 160 PHE B CE2   1 
ATOM   3161 C  CZ    . PHE B 1  130 ? 2.70023   -1.77207  -12.20040 1.000 43.17796  ? 160 PHE B CZ    1 
ATOM   3162 N  N     . ILE B 1  131 ? 4.29791   2.34755   -10.42714 1.000 42.70892  ? 161 ILE B N     1 
ATOM   3163 C  CA    . ILE B 1  131 ? 3.51958   3.18075   -11.33567 1.000 38.47615  ? 161 ILE B CA    1 
ATOM   3164 C  C     . ILE B 1  131 ? 3.30309   2.41001   -12.62675 1.000 39.14339  ? 161 ILE B C     1 
ATOM   3165 O  O     . ILE B 1  131 ? 4.26186   1.90713   -13.22322 1.000 45.13624  ? 161 ILE B O     1 
ATOM   3166 C  CB    . ILE B 1  131 ? 4.19947   4.52580   -11.63365 1.000 38.71206  ? 161 ILE B CB    1 
ATOM   3167 C  CG1   . ILE B 1  131 ? 4.53196   5.29153   -10.34461 1.000 41.40919  ? 161 ILE B CG1   1 
ATOM   3168 C  CG2   . ILE B 1  131 ? 3.30213   5.37400   -12.55314 1.000 40.46426  ? 161 ILE B CG2   1 
ATOM   3169 C  CD1   . ILE B 1  131 ? 3.31623   5.83839   -9.63204  1.000 42.33640  ? 161 ILE B CD1   1 
ATOM   3170 N  N     . ASN B 1  132 ? 2.04593   2.33111   -13.05130 1.000 41.87826  ? 162 ASN B N     1 
ATOM   3171 C  CA    . ASN B 1  132 ? 1.67044   1.75938   -14.34928 1.000 42.48130  ? 162 ASN B CA    1 
ATOM   3172 C  C     . ASN B 1  132 ? 1.51308   2.92059   -15.33098 1.000 42.60191  ? 162 ASN B C     1 
ATOM   3173 O  O     . ASN B 1  132 ? 0.44504   3.51862   -15.44545 1.000 42.18330  ? 162 ASN B O     1 
ATOM   3174 C  CB    . ASN B 1  132 ? 0.38648   0.95236   -14.23796 1.000 39.59596  ? 162 ASN B CB    1 
ATOM   3175 C  CG    . ASN B 1  132 ? 0.07700   0.16763   -15.51001 1.000 42.50506  ? 162 ASN B CG    1 
ATOM   3176 O  OD1   . ASN B 1  132 ? 0.57959   0.48285   -16.59213 1.000 44.32231  ? 162 ASN B OD1   1 
ATOM   3177 N  ND2   . ASN B 1  132 ? -0.74896  -0.86239  -15.37691 1.000 40.34246  ? 162 ASN B ND2   1 
ATOM   3178 N  N     . VAL B 1  133 ? 2.60081   3.22873   -16.04832 1.000 41.31227  ? 163 VAL B N     1 
ATOM   3179 C  CA    . VAL B 1  133 ? 2.59546   4.33993   -16.99009 1.000 50.79181  ? 163 VAL B CA    1 
ATOM   3180 C  C     . VAL B 1  133 ? 1.71400   4.04018   -18.20282 1.000 49.05002  ? 163 VAL B C     1 
ATOM   3181 O  O     . VAL B 1  133 ? 1.13878   4.95831   -18.80041 1.000 49.50370  ? 163 VAL B O     1 
ATOM   3182 C  CB    . VAL B 1  133 ? 4.04231   4.67201   -17.40856 1.000 47.62782  ? 163 VAL B CB    1 
ATOM   3183 C  CG1   . VAL B 1  133 ? 4.05591   5.76023   -18.47434 1.000 56.34466  ? 163 VAL B CG1   1 
ATOM   3184 C  CG2   . VAL B 1  133 ? 4.85776   5.10575   -16.20178 1.000 41.28329  ? 163 VAL B CG2   1 
ATOM   3185 N  N     . ASP B 1  134 ? 1.59486   2.76826   -18.58104 1.000 48.94444  ? 164 ASP B N     1 
ATOM   3186 C  CA    . ASP B 1  134 ? 0.72943   2.41850   -19.70279 1.000 47.37683  ? 164 ASP B CA    1 
ATOM   3187 C  C     . ASP B 1  134 ? -0.72945  2.72844   -19.38817 1.000 42.52593  ? 164 ASP B C     1 
ATOM   3188 O  O     . ASP B 1  134 ? -1.41874  3.39961   -20.16978 1.000 49.06730  ? 164 ASP B O     1 
ATOM   3189 C  CB    . ASP B 1  134 ? 0.91330   0.94157   -20.05116 1.000 52.32694  ? 164 ASP B CB    1 
ATOM   3190 C  CG    . ASP B 1  134 ? 2.37221   0.58461   -20.28778 1.000 78.68917  ? 164 ASP B CG    1 
ATOM   3191 O  OD1   . ASP B 1  134 ? 2.88379   0.83884   -21.39892 1.000 75.22984  ? 164 ASP B OD1   1 
ATOM   3192 O  OD2   . ASP B 1  134 ? 3.02156   0.07341   -19.34313 1.000 82.39307  ? 164 ASP B OD2   1 
ATOM   3193 N  N     . TYR B 1  135 ? -1.21402  2.26920   -18.23209 1.000 41.15522  ? 165 TYR B N     1 
ATOM   3194 C  CA    . TYR B 1  135 ? -2.59588  2.56114   -17.87651 1.000 43.39997  ? 165 TYR B CA    1 
ATOM   3195 C  C     . TYR B 1  135 ? -2.78677  4.04508   -17.59013 1.000 47.21400  ? 165 TYR B C     1 
ATOM   3196 O  O     . TYR B 1  135 ? -3.83389  4.61015   -17.92262 1.000 46.56392  ? 165 TYR B O     1 
ATOM   3197 C  CB    . TYR B 1  135 ? -3.03044  1.70989   -16.68452 1.000 40.27187  ? 165 TYR B CB    1 
ATOM   3198 C  CG    . TYR B 1  135 ? -4.52535  1.64585   -16.44098 1.000 40.08582  ? 165 TYR B CG    1 
ATOM   3199 C  CD1   . TYR B 1  135 ? -5.39872  1.20906   -17.43274 1.000 40.58907  ? 165 TYR B CD1   1 
ATOM   3200 C  CD2   . TYR B 1  135 ? -5.05788  1.97959   -15.20271 1.000 40.41260  ? 165 TYR B CD2   1 
ATOM   3201 C  CE1   . TYR B 1  135 ? -6.76364  1.14102   -17.20824 1.000 48.71026  ? 165 TYR B CE1   1 
ATOM   3202 C  CE2   . TYR B 1  135 ? -6.41779  1.90855   -14.95921 1.000 44.97056  ? 165 TYR B CE2   1 
ATOM   3203 C  CZ    . TYR B 1  135 ? -7.27217  1.48776   -15.97098 1.000 51.62516  ? 165 TYR B CZ    1 
ATOM   3204 O  OH    . TYR B 1  135 ? -8.62808  1.40572   -15.72649 1.000 59.08465  ? 165 TYR B OH    1 
ATOM   3205 N  N     . LEU B 1  136 ? -1.80153  4.69194   -16.95736 1.000 45.74194  ? 166 LEU B N     1 
ATOM   3206 C  CA    . LEU B 1  136 ? -1.93242  6.12289   -16.68902 1.000 40.02842  ? 166 LEU B CA    1 
ATOM   3207 C  C     . LEU B 1  136 ? -2.07290  6.89816   -17.98480 1.000 47.43723  ? 166 LEU B C     1 
ATOM   3208 O  O     . LEU B 1  136 ? -2.90594  7.80318   -18.09530 1.000 40.59903  ? 166 LEU B O     1 
ATOM   3209 C  CB    . LEU B 1  136 ? -0.74012  6.64771   -15.89235 1.000 39.81187  ? 166 LEU B CB    1 
ATOM   3210 C  CG    . LEU B 1  136 ? -0.74904  8.17067   -15.69603 1.000 39.76589  ? 166 LEU B CG    1 
ATOM   3211 C  CD1   . LEU B 1  136 ? -2.01977  8.61854   -15.00046 1.000 39.29137  ? 166 LEU B CD1   1 
ATOM   3212 C  CD2   . LEU B 1  136 ? 0.47126   8.64251   -14.92839 1.000 40.79446  ? 166 LEU B CD2   1 
ATOM   3213 N  N     . THR B 1  137 ? -1.23527  6.57736   -18.97318 1.000 49.96912  ? 167 THR B N     1 
ATOM   3214 C  CA    . THR B 1  137 ? -1.34277  7.19463   -20.29501 1.000 53.27079  ? 167 THR B CA    1 
ATOM   3215 C  C     . THR B 1  137 ? -2.72599  6.97177   -20.90154 1.000 52.34951  ? 167 THR B C     1 
ATOM   3216 O  O     . THR B 1  137 ? -3.36318  7.91487   -21.39811 1.000 49.72846  ? 167 THR B O     1 
ATOM   3217 C  CB    . THR B 1  137 ? -0.26511  6.63282   -21.21954 1.000 46.29308  ? 167 THR B CB    1 
ATOM   3218 O  OG1   . THR B 1  137 ? 1.02305   7.06472   -20.77293 1.000 53.85294  ? 167 THR B OG1   1 
ATOM   3219 C  CG2   . THR B 1  137 ? -0.48765  7.10512   -22.65435 1.000 55.65777  ? 167 THR B CG2   1 
ATOM   3220 N  N     . GLU B 1  138 ? -3.18800  5.72177   -20.89563 1.000 50.38602  ? 168 GLU B N     1 
ATOM   3221 C  CA    . GLU B 1  138 ? -4.51320  5.42189   -21.42919 1.000 43.07703  ? 168 GLU B CA    1 
ATOM   3222 C  C     . GLU B 1  138 ? -5.58194  6.27275   -20.75062 1.000 47.04315  ? 168 GLU B C     1 
ATOM   3223 O  O     . GLU B 1  138 ? -6.46219  6.84789   -21.41717 1.000 52.20371  ? 168 GLU B O     1 
ATOM   3224 C  CB    . GLU B 1  138 ? -4.79415  3.92485   -21.26840 1.000 45.84307  ? 168 GLU B CB    1 
ATOM   3225 C  CG    . GLU B 1  138 ? -6.21727  3.47292   -21.57996 1.000 52.33579  ? 168 GLU B CG    1 
ATOM   3226 C  CD    . GLU B 1  138 ? -6.38121  1.96089   -21.41321 1.000 79.93037  ? 168 GLU B CD    1 
ATOM   3227 O  OE1   . GLU B 1  138 ? -5.36525  1.23791   -21.51275 1.000 87.82164  ? 168 GLU B OE1   1 
ATOM   3228 O  OE2   . GLU B 1  138 ? -7.51812  1.49085   -21.16988 1.000 82.18489  ? 168 GLU B OE2   1 
ATOM   3229 N  N     . LEU B 1  139 ? -5.49644  6.40747   -19.42662 1.000 51.78459  ? 169 LEU B N     1 
ATOM   3230 C  CA    . LEU B 1  139 ? -6.52417  7.14233   -18.70508 1.000 40.61762  ? 169 LEU B CA    1 
ATOM   3231 C  C     . LEU B 1  139 ? -6.41925  8.64138   -18.94481 1.000 40.75974  ? 169 LEU B C     1 
ATOM   3232 O  O     . LEU B 1  139 ? -7.44027  9.31939   -18.99329 1.000 46.25128  ? 169 LEU B O     1 
ATOM   3233 C  CB    . LEU B 1  139 ? -6.45061  6.83502   -17.20817 1.000 44.87647  ? 169 LEU B CB    1 
ATOM   3234 C  CG    . LEU B 1  139 ? -6.86146  5.41493   -16.78531 1.000 43.55230  ? 169 LEU B CG    1 
ATOM   3235 C  CD1   . LEU B 1  139 ? -6.68989  5.20062   -15.28042 1.000 48.64406  ? 169 LEU B CD1   1 
ATOM   3236 C  CD2   . LEU B 1  139 ? -8.28962  5.13002   -17.20284 1.000 42.50717  ? 169 LEU B CD2   1 
ATOM   3237 N  N     . LEU B 1  140 ? -5.20430  9.17240   -19.09015 1.000 40.91556  ? 170 LEU B N     1 
ATOM   3238 C  CA    . LEU B 1  140 ? -5.05839  10.59945  -19.34791 1.000 48.75034  ? 170 LEU B CA    1 
ATOM   3239 C  C     . LEU B 1  140 ? -5.59991  10.95274  -20.72564 1.000 49.05856  ? 170 LEU B C     1 
ATOM   3240 O  O     . LEU B 1  140 ? -6.26697  11.98378  -20.89717 1.000 46.57489  ? 170 LEU B O     1 
ATOM   3241 C  CB    . LEU B 1  140 ? -3.59135  11.01742  -19.23638 1.000 41.31729  ? 170 LEU B CB    1 
ATOM   3242 C  CG    . LEU B 1  140 ? -2.98382  10.99613  -17.82361 1.000 42.01670  ? 170 LEU B CG    1 
ATOM   3243 C  CD1   . LEU B 1  140 ? -1.49785  11.11814  -17.91414 1.000 41.00405  ? 170 LEU B CD1   1 
ATOM   3244 C  CD2   . LEU B 1  140 ? -3.57149  12.12195  -16.96815 1.000 40.42452  ? 170 LEU B CD2   1 
ATOM   3245 N  N     . LEU B 1  141 ? -5.33128  10.10195  -21.71391 1.000 44.95251  ? 171 LEU B N     1 
ATOM   3246 C  CA    . LEU B 1  141 ? -5.91078  10.30423  -23.03965 1.000 47.47624  ? 171 LEU B CA    1 
ATOM   3247 C  C     . LEU B 1  141 ? -7.43476  10.23923  -22.99310 1.000 42.66726  ? 171 LEU B C     1 
ATOM   3248 O  O     . LEU B 1  141 ? -8.12697  11.10234  -23.54866 1.000 45.58785  ? 171 LEU B O     1 
ATOM   3249 C  CB    . LEU B 1  141 ? -5.33115  9.26943   -24.00509 1.000 43.25876  ? 171 LEU B CB    1 
ATOM   3250 C  CG    . LEU B 1  141 ? -3.84624  9.52147   -24.25259 1.000 47.04226  ? 171 LEU B CG    1 
ATOM   3251 C  CD1   . LEU B 1  141 ? -3.18449  8.32760   -24.91709 1.000 55.20049  ? 171 LEU B CD1   1 
ATOM   3252 C  CD2   . LEU B 1  141 ? -3.66756  10.75565  -25.12040 1.000 44.20211  ? 171 LEU B CD2   1 
ATOM   3253 N  N     . LYS B 1  142 ? -8.00552  9.23909   -22.34309 1.000 42.27909  ? 172 LYS B N     1 
ATOM   3254 C  CA    . LYS B 1  142 ? -9.47950  9.15508   -22.27155 1.000 42.24125  ? 172 LYS B CA    1 
ATOM   3255 C  C     . LYS B 1  142 ? -10.05120 10.35093  -21.50009 1.000 50.48619  ? 172 LYS B C     1 
ATOM   3256 O  O     . LYS B 1  142 ? -11.05638 10.91203  -21.96760 1.000 52.68141  ? 172 LYS B O     1 
ATOM   3257 C  CB    . LYS B 1  142 ? -9.97926  7.85895   -21.62464 1.000 48.42406  ? 172 LYS B CB    1 
ATOM   3258 C  CG    . LYS B 1  142 ? -11.32100 8.00482   -20.93110 1.000 71.31445  ? 172 LYS B CG    1 
ATOM   3259 C  CD    . LYS B 1  142 ? -12.02088 6.69875   -20.58511 1.000 77.74221  ? 172 LYS B CD    1 
ATOM   3260 C  CE    . LYS B 1  142 ? -13.05748 6.89453   -19.52068 1.000 89.22493  ? 172 LYS B CE    1 
ATOM   3261 N  NZ    . LYS B 1  142 ? -12.97824 8.22340   -18.91544 1.000 81.92783  ? 172 LYS B NZ    1 
ATOM   3262 N  N     . LYS B 1  143 ? -9.46377  10.70369  -20.35324 1.000 51.66709  ? 173 LYS B N     1 
ATOM   3263 C  CA    . LYS B 1  143 ? -10.00547 11.80152  -19.55281 1.000 41.33046  ? 173 LYS B CA    1 
ATOM   3264 C  C     . LYS B 1  143 ? -10.04276 13.08469  -20.36053 1.000 44.71686  ? 173 LYS B C     1 
ATOM   3265 O  O     . LYS B 1  143 ? -10.98771 13.87267  -20.23701 1.000 42.10861  ? 173 LYS B O     1 
ATOM   3266 C  CB    . LYS B 1  143 ? -9.17499  11.99325  -18.27608 1.000 43.95890  ? 173 LYS B CB    1 
ATOM   3267 C  CG    . LYS B 1  143 ? -9.70363  13.08806  -17.33365 1.000 44.49172  ? 173 LYS B CG    1 
ATOM   3268 C  CD    . LYS B 1  143 ? -11.07842 12.73195  -16.78521 1.000 48.83326  ? 173 LYS B CD    1 
ATOM   3269 C  CE    . LYS B 1  143 ? -11.41195 13.53070  -15.54592 1.000 57.69918  ? 173 LYS B CE    1 
ATOM   3270 N  NZ    . LYS B 1  143 ? -12.65471 13.02757  -14.89356 1.000 65.50035  ? 173 LYS B NZ    1 
ATOM   3271 N  N     . ASN B 1  144 ? -9.07809  13.29087  -21.24784 1.000 42.23907  ? 174 ASN B N     1 
ATOM   3272 C  CA    . ASN B 1  144 ? -9.11644  14.45806  -22.17859 1.000 42.86395  ? 174 ASN B CA    1 
ATOM   3273 C  C     . ASN B 1  144 ? -9.21615  15.78091  -21.41927 1.000 42.83615  ? 174 ASN B C     1 
ATOM   3274 O  O     . ASN B 1  144 ? -9.93132  16.67901  -21.88182 1.000 44.16337  ? 174 ASN B O     1 
ATOM   3275 C  CB    . ASN B 1  144 ? -10.18584 14.24829  -23.25023 1.000 43.28884  ? 174 ASN B CB    1 
ATOM   3276 C  CG    . ASN B 1  144 ? -10.07228 15.19054  -24.42108 1.000 43.99840  ? 174 ASN B CG    1 
ATOM   3277 O  OD1   . ASN B 1  144 ? -9.01451  15.29466  -25.04545 1.000 46.89855  ? 174 ASN B OD1   1 
ATOM   3278 N  ND2   . ASN B 1  144 ? -11.16038 15.88560  -24.70152 1.000 44.28703  ? 174 ASN B ND2   1 
ATOM   3279 N  N     . ARG B 1  145 ? -8.52472  15.89867  -20.29251 1.000 45.70128  ? 175 ARG B N     1 
ATOM   3280 C  CA    . ARG B 1  145 ? -8.47944  17.15752  -19.55726 1.000 42.42706  ? 175 ARG B CA    1 
ATOM   3281 C  C     . ARG B 1  145 ? -7.04147  17.64053  -19.65170 1.000 44.55423  ? 175 ARG B C     1 
ATOM   3282 O  O     . ARG B 1  145 ? -6.16421  17.13538  -18.95014 1.000 50.65496  ? 175 ARG B O     1 
ATOM   3283 C  CB    . ARG B 1  145 ? -8.93790  16.96222  -18.12013 1.000 48.03809  ? 175 ARG B CB    1 
ATOM   3284 C  CG    . ARG B 1  145 ? -10.40786 16.61320  -17.99665 1.000 49.91584  ? 175 ARG B CG    1 
ATOM   3285 C  CD    . ARG B 1  145 ? -11.24082 17.87419  -17.90508 1.000 47.69959  ? 175 ARG B CD    1 
ATOM   3286 N  NE    . ARG B 1  145 ? -10.82939 18.70395  -16.78106 1.000 61.09819  ? 175 ARG B NE    1 
ATOM   3287 C  CZ    . ARG B 1  145 ? -10.02542 19.75896  -16.87214 1.000 58.21203  ? 175 ARG B CZ    1 
ATOM   3288 N  NH1   . ARG B 1  145 ? -9.53785  20.15920  -18.03424 1.000 52.71358  ? 175 ARG B NH1   1 
ATOM   3289 N  NH2   . ARG B 1  145 ? -9.69900  20.42473  -15.76613 1.000 54.10017  ? 175 ARG B NH2   1 
ATOM   3290 N  N     . THR B 1  146 ? -6.80180  18.61671  -20.52659 1.000 50.69766  ? 176 THR B N     1 
ATOM   3291 C  CA    . THR B 1  146 ? -5.45193  19.01878  -20.89001 1.000 46.22797  ? 176 THR B CA    1 
ATOM   3292 C  C     . THR B 1  146 ? -5.01070  20.34765  -20.29190 1.000 51.53269  ? 176 THR B C     1 
ATOM   3293 O  O     . THR B 1  146 ? -3.84777  20.72768  -20.47526 1.000 46.66613  ? 176 THR B O     1 
ATOM   3294 C  CB    . THR B 1  146 ? -5.33950  19.10209  -22.41504 1.000 56.12496  ? 176 THR B CB    1 
ATOM   3295 O  OG1   . THR B 1  146 ? -6.27368  20.07020  -22.90549 1.000 51.79018  ? 176 THR B OG1   1 
ATOM   3296 C  CG2   . THR B 1  146 ? -5.66074  17.75122  -23.03120 1.000 45.92557  ? 176 THR B CG2   1 
ATOM   3297 N  N     . THR B 1  147 ? -5.88944  21.06251  -19.59642 1.000 43.99019  ? 177 THR B N     1 
ATOM   3298 C  CA    . THR B 1  147 ? -5.49417  22.27936  -18.89432 1.000 45.20262  ? 177 THR B CA    1 
ATOM   3299 C  C     . THR B 1  147 ? -6.18366  22.35108  -17.54104 1.000 52.59634  ? 177 THR B C     1 
ATOM   3300 O  O     . THR B 1  147 ? -7.30160  21.84705  -17.36773 1.000 44.95573  ? 177 THR B O     1 
ATOM   3301 C  CB    . THR B 1  147 ? -5.83246  23.55653  -19.69793 1.000 53.20616  ? 177 THR B CB    1 
ATOM   3302 O  OG1   . THR B 1  147 ? -7.25351  23.67557  -19.83637 1.000 48.67467  ? 177 THR B OG1   1 
ATOM   3303 C  CG2   . THR B 1  147 ? -5.20097  23.51381  -21.06117 1.000 45.86151  ? 177 THR B CG2   1 
ATOM   3304 N  N     . ARG B 1  148 ? -5.51830  23.01288  -16.59116 1.000 51.86158  ? 178 ARG B N     1 
ATOM   3305 C  CA    . ARG B 1  148 ? -6.05079  23.22161  -15.24491 1.000 49.60932  ? 178 ARG B CA    1 
ATOM   3306 C  C     . ARG B 1  148 ? -6.60058  21.92149  -14.66898 1.000 50.39077  ? 178 ARG B C     1 
ATOM   3307 O  O     . ARG B 1  148 ? -7.69937  21.86938  -14.10358 1.000 45.78366  ? 178 ARG B O     1 
ATOM   3308 C  CB    . ARG B 1  148 ? -7.11579  24.31661  -15.24129 1.000 49.17401  ? 178 ARG B CB    1 
ATOM   3309 C  CG    . ARG B 1  148 ? -6.53087  25.71366  -15.48221 1.000 57.16737  ? 178 ARG B CG    1 
ATOM   3310 C  CD    . ARG B 1  148 ? -7.60792  26.76069  -15.62059 1.000 58.34996  ? 178 ARG B CD    1 
ATOM   3311 N  NE    . ARG B 1  148 ? -8.45947  26.88945  -14.44225 1.000 55.13326  ? 178 ARG B NE    1 
ATOM   3312 C  CZ    . ARG B 1  148 ? -8.16607  27.63423  -13.38220 1.000 57.85700  ? 178 ARG B CZ    1 
ATOM   3313 N  NH1   . ARG B 1  148 ? -6.99803  28.24820  -13.26651 1.000 51.45949  ? 178 ARG B NH1   1 
ATOM   3314 N  NH2   . ARG B 1  148 ? -9.07171  27.77103  -12.41783 1.000 53.57352  ? 178 ARG B NH2   1 
ATOM   3315 N  N     . PHE B 1  149 ? -5.81065  20.85352  -14.82650 1.000 49.22436  ? 179 PHE B N     1 
ATOM   3316 C  CA    . PHE B 1  149 ? -6.20250  19.50744  -14.42363 1.000 48.37519  ? 179 PHE B CA    1 
ATOM   3317 C  C     . PHE B 1  149 ? -5.27809  19.00620  -13.32208 1.000 46.95543  ? 179 PHE B C     1 
ATOM   3318 O  O     . PHE B 1  149 ? -4.05014  19.07322  -13.45653 1.000 41.27335  ? 179 PHE B O     1 
ATOM   3319 C  CB    . PHE B 1  149 ? -6.16996  18.54168  -15.61784 1.000 41.57076  ? 179 PHE B CB    1 
ATOM   3320 C  CG    . PHE B 1  149 ? -6.54083  17.11461  -15.27100 1.000 41.27247  ? 179 PHE B CG    1 
ATOM   3321 C  CD1   . PHE B 1  149 ? -7.81667  16.78553  -14.84259 1.000 50.06401  ? 179 PHE B CD1   1 
ATOM   3322 C  CD2   . PHE B 1  149 ? -5.60889  16.09864  -15.40956 1.000 40.47013  ? 179 PHE B CD2   1 
ATOM   3323 C  CE1   . PHE B 1  149 ? -8.15456  15.46647  -14.53374 1.000 52.27063  ? 179 PHE B CE1   1 
ATOM   3324 C  CE2   . PHE B 1  149 ? -5.94178  14.77558  -15.10371 1.000 46.16293  ? 179 PHE B CE2   1 
ATOM   3325 C  CZ    . PHE B 1  149 ? -7.21462  14.46649  -14.67430 1.000 44.53630  ? 179 PHE B CZ    1 
ATOM   3326 N  N     . PHE B 1  150 ? -5.87470  18.47798  -12.25797 1.000 43.93051  ? 180 PHE B N     1 
ATOM   3327 C  CA    . PHE B 1  150 ? -5.10728  17.95675  -11.13336 1.000 39.34497  ? 180 PHE B CA    1 
ATOM   3328 C  C     . PHE B 1  150 ? -5.84807  16.76163  -10.55633 1.000 38.73200  ? 180 PHE B C     1 
ATOM   3329 O  O     . PHE B 1  150 ? -7.03894  16.86657  -10.22886 1.000 49.28895  ? 180 PHE B O     1 
ATOM   3330 C  CB    . PHE B 1  150 ? -4.89987  19.04052  -10.07121 1.000 39.33345  ? 180 PHE B CB    1 
ATOM   3331 C  CG    . PHE B 1  150 ? -3.75452  18.76132  -9.13470  1.000 44.14688  ? 180 PHE B CG    1 
ATOM   3332 C  CD1   . PHE B 1  150 ? -3.92213  17.87410  -8.06882  1.000 43.81251  ? 180 PHE B CD1   1 
ATOM   3333 C  CD2   . PHE B 1  150 ? -2.51259  19.33436  -9.33405  1.000 39.28818  ? 180 PHE B CD2   1 
ATOM   3334 C  CE1   . PHE B 1  150 ? -2.86380  17.58892  -7.19628  1.000 40.27560  ? 180 PHE B CE1   1 
ATOM   3335 C  CE2   . PHE B 1  150 ? -1.45227  19.05717  -8.46950  1.000 40.43829  ? 180 PHE B CE2   1 
ATOM   3336 C  CZ    . PHE B 1  150 ? -1.62388  18.18095  -7.40462  1.000 42.98796  ? 180 PHE B CZ    1 
ATOM   3337 N  N     . THR B 1  151 ? -5.15302  15.62960  -10.42283 1.000 42.09038  ? 181 THR B N     1 
ATOM   3338 C  CA    . THR B 1  151 ? -5.79285  14.41451  -9.96084  1.000 38.20187  ? 181 THR B CA    1 
ATOM   3339 C  C     . THR B 1  151 ? -4.81555  13.58133  -9.13738  1.000 37.36313  ? 181 THR B C     1 
ATOM   3340 O  O     . THR B 1  151 ? -3.60155  13.81532  -9.13179  1.000 43.14968  ? 181 THR B O     1 
ATOM   3341 C  CB    . THR B 1  151 ? -6.31329  13.56175  -11.12382 1.000 45.17255  ? 181 THR B CB    1 
ATOM   3342 O  OG1   . THR B 1  151 ? -7.19911  12.55165  -10.61470 1.000 39.82041  ? 181 THR B OG1   1 
ATOM   3343 C  CG2   . THR B 1  151 ? -5.15055  12.88889  -11.80740 1.000 40.20628  ? 181 THR B CG2   1 
ATOM   3344 N  N     . GLY B 1  152 ? -5.37231  12.56520  -8.48938  1.000 38.44362  ? 182 GLY B N     1 
ATOM   3345 C  CA    . GLY B 1  152 ? -4.59403  11.59704  -7.73388  1.000 45.01392  ? 182 GLY B CA    1 
ATOM   3346 C  C     . GLY B 1  152 ? -5.49566  10.90384  -6.74768  1.000 40.48917  ? 182 GLY B C     1 
ATOM   3347 O  O     . GLY B 1  152 ? -6.66279  10.63191  -7.06730  1.000 46.79604  ? 182 GLY B O     1 
ATOM   3348 N  N     . PHE B 1  153 ? -4.99721  10.64058  -5.54093  1.000 43.29555  ? 183 PHE B N     1 
ATOM   3349 C  CA    . PHE B 1  153 ? -5.85381  10.20136  -4.44770  1.000 42.94911  ? 183 PHE B CA    1 
ATOM   3350 C  C     . PHE B 1  153 ? -6.36753  11.43721  -3.72125  1.000 38.46725  ? 183 PHE B C     1 
ATOM   3351 O  O     . PHE B 1  153 ? -5.62525  12.09605  -2.98539  1.000 45.61407  ? 183 PHE B O     1 
ATOM   3352 C  CB    . PHE B 1  153 ? -5.09745  9.26516   -3.50017  1.000 39.88854  ? 183 PHE B CB    1 
ATOM   3353 C  CG    . PHE B 1  153 ? -5.95604  8.73293   -2.38396  1.000 44.58445  ? 183 PHE B CG    1 
ATOM   3354 C  CD1   . PHE B 1  153 ? -6.75511  7.61297   -2.57290  1.000 43.51223  ? 183 PHE B CD1   1 
ATOM   3355 C  CD2   . PHE B 1  153 ? -5.97157  9.35767   -1.14883  1.000 41.61614  ? 183 PHE B CD2   1 
ATOM   3356 C  CE1   . PHE B 1  153 ? -7.54573  7.12876   -1.54470  1.000 41.01126  ? 183 PHE B CE1   1 
ATOM   3357 C  CE2   . PHE B 1  153 ? -6.76019  8.88646   -0.12563  1.000 39.78792  ? 183 PHE B CE2   1 
ATOM   3358 C  CZ    . PHE B 1  153 ? -7.54727  7.76851   -0.31757  1.000 46.13567  ? 183 PHE B CZ    1 
ATOM   3359 N  N     . LEU B 1  154 ? -7.64360  11.75626  -3.91470  1.000 41.28238  ? 184 LEU B N     1 
ATOM   3360 C  CA    . LEU B 1  154 ? -8.20739  12.98315  -3.37023  1.000 42.65641  ? 184 LEU B CA    1 
ATOM   3361 C  C     . LEU B 1  154 ? -8.45783  12.85084  -1.87117  1.000 42.62014  ? 184 LEU B C     1 
ATOM   3362 O  O     . LEU B 1  154 ? -9.04966  11.87174  -1.40515  1.000 48.15698  ? 184 LEU B O     1 
ATOM   3363 C  CB    . LEU B 1  154 ? -9.49866  13.35030  -4.09767  1.000 43.30367  ? 184 LEU B CB    1 
ATOM   3364 C  CG    . LEU B 1  154 ? -9.30717  14.01559  -5.46761  1.000 49.70442  ? 184 LEU B CG    1 
ATOM   3365 C  CD1   . LEU B 1  154 ? -8.58054  13.10479  -6.45207  1.000 48.70441  ? 184 LEU B CD1   1 
ATOM   3366 C  CD2   . LEU B 1  154 ? -10.65038 14.48071  -6.04401  1.000 56.20502  ? 184 LEU B CD2   1 
ATOM   3367 N  N     . LYS B 1  155 ? -7.99154  13.85068  -1.12113  1.000 44.60381  ? 185 LYS B N     1 
ATOM   3368 C  CA    . LYS B 1  155 ? -8.17700  13.95538  0.32496   1.000 38.87656  ? 185 LYS B CA    1 
ATOM   3369 C  C     . LYS B 1  155 ? -8.94090  15.25333  0.57751   1.000 44.14348  ? 185 LYS B C     1 
ATOM   3370 O  O     . LYS B 1  155 ? -8.33988  16.33332  0.59951   1.000 46.71644  ? 185 LYS B O     1 
ATOM   3371 C  CB    . LYS B 1  155 ? -6.82673  13.92822  1.04245   1.000 41.80125  ? 185 LYS B CB    1 
ATOM   3372 C  CG    . LYS B 1  155 ? -6.01486  12.70029  0.70489   1.000 45.90429  ? 185 LYS B CG    1 
ATOM   3373 C  CD    . LYS B 1  155 ? -4.56870  12.79719  1.13736   1.000 42.86365  ? 185 LYS B CD    1 
ATOM   3374 C  CE    . LYS B 1  155 ? -4.44513  12.80887  2.65832   1.000 56.82393  ? 185 LYS B CE    1 
ATOM   3375 N  NZ    . LYS B 1  155 ? -4.99490  11.57475  3.28227   1.000 58.76494  ? 185 LYS B NZ    1 
ATOM   3376 N  N     . LEU B 1  156 ? -10.25782 15.14329  0.76899   1.000 47.45983  ? 186 LEU B N     1 
ATOM   3377 C  CA    . LEU B 1  156 ? -11.14383 16.29531  0.73956   1.000 47.19562  ? 186 LEU B CA    1 
ATOM   3378 C  C     . LEU B 1  156 ? -11.60231 16.77102  2.11283   1.000 59.18544  ? 186 LEU B C     1 
ATOM   3379 O  O     . LEU B 1  156 ? -12.10227 17.89400  2.22025   1.000 61.82522  ? 186 LEU B O     1 
ATOM   3380 C  CB    . LEU B 1  156 ? -12.38515 15.98149  -0.09704  1.000 42.86007  ? 186 LEU B CB    1 
ATOM   3381 C  CG    . LEU B 1  156 ? -12.05468 15.52978  -1.52326  1.000 58.57637  ? 186 LEU B CG    1 
ATOM   3382 C  CD1   . LEU B 1  156 ? -13.31599 15.19896  -2.34086  1.000 52.03900  ? 186 LEU B CD1   1 
ATOM   3383 C  CD2   . LEU B 1  156 ? -11.19494 16.57492  -2.21837  1.000 48.30446  ? 186 LEU B CD2   1 
ATOM   3384 N  N     . ASN B 1  157 ? -11.46592 15.96280  3.15661   1.000 68.82545  ? 187 ASN B N     1 
ATOM   3385 C  CA    . ASN B 1  157 ? -11.89842 16.37953  4.49086   1.000 75.11475  ? 187 ASN B CA    1 
ATOM   3386 C  C     . ASN B 1  157 ? -10.77305 16.11831  5.49338   1.000 65.35834  ? 187 ASN B C     1 
ATOM   3387 O  O     . ASN B 1  157 ? -10.89870 15.33312  6.43327   1.000 73.24631  ? 187 ASN B O     1 
ATOM   3388 C  CB    . ASN B 1  157 ? -13.18628 15.65745  4.87819   1.000 88.82073  ? 187 ASN B CB    1 
ATOM   3389 C  CG    . ASN B 1  157 ? -13.94186 16.37523  5.97662   1.000 100.11989 ? 187 ASN B CG    1 
ATOM   3390 O  OD1   . ASN B 1  157 ? -14.32892 17.53326  5.81601   1.000 101.40182 ? 187 ASN B OD1   1 
ATOM   3391 N  ND2   . ASN B 1  157 ? -14.16245 15.68700  7.09156   1.000 81.87297  ? 187 ASN B ND2   1 
ATOM   3392 N  N     . GLU B 1  158 ? -9.64512  16.79035  5.28210   1.000 55.30842  ? 188 GLU B N     1 
ATOM   3393 C  CA    . GLU B 1  158 ? -8.45382  16.56518  6.08061   1.000 53.72061  ? 188 GLU B CA    1 
ATOM   3394 C  C     . GLU B 1  158 ? -8.31241  17.63496  7.15877   1.000 50.08329  ? 188 GLU B C     1 
ATOM   3395 O  O     . GLU B 1  158 ? -8.63049  18.80600  6.93014   1.000 52.01281  ? 188 GLU B O     1 
ATOM   3396 C  CB    . GLU B 1  158 ? -7.20715  16.53636  5.20113   1.000 53.54252  ? 188 GLU B CB    1 
ATOM   3397 C  CG    . GLU B 1  158 ? -7.12950  15.31154  4.30785   1.000 59.85267  ? 188 GLU B CG    1 
ATOM   3398 C  CD    . GLU B 1  158 ? -6.99820  14.01838  5.10553   1.000 67.49759  ? 188 GLU B CD    1 
ATOM   3399 O  OE1   . GLU B 1  158 ? -6.22083  13.97717  6.08723   1.000 65.88616  ? 188 GLU B OE1   1 
ATOM   3400 O  OE2   . GLU B 1  158 ? -7.67734  13.04145  4.74358   1.000 77.78127  ? 188 GLU B OE2   1 
ATOM   3401 N  N     . PHE B 1  159 ? -7.82798  17.22171  8.32551   1.000 47.74060  ? 189 PHE B N     1 
ATOM   3402 C  CA    . PHE B 1  159 ? -7.59456  18.11848  9.44061   1.000 44.99021  ? 189 PHE B CA    1 
ATOM   3403 C  C     . PHE B 1  159 ? -6.13140  18.06638  9.85205   1.000 44.75806  ? 189 PHE B C     1 
ATOM   3404 O  O     . PHE B 1  159 ? -5.52541  16.98538  9.84559   1.000 37.98430  ? 189 PHE B O     1 
ATOM   3405 C  CB    . PHE B 1  159 ? -8.48211  17.75723  10.63686  1.000 42.79953  ? 189 PHE B CB    1 
ATOM   3406 C  CG    . PHE B 1  159 ? -9.93824  17.68231  10.29640  1.000 54.67749  ? 189 PHE B CG    1 
ATOM   3407 C  CD1   . PHE B 1  159 ? -10.69926 18.83733  10.21492  1.000 63.64531  ? 189 PHE B CD1   1 
ATOM   3408 C  CD2   . PHE B 1  159 ? -10.54634 16.46237  10.04237  1.000 58.59115  ? 189 PHE B CD2   1 
ATOM   3409 C  CE1   . PHE B 1  159 ? -12.04038 18.78141  9.89241   1.000 63.57051  ? 189 PHE B CE1   1 
ATOM   3410 C  CE2   . PHE B 1  159 ? -11.89446 16.39944  9.72386   1.000 63.97025  ? 189 PHE B CE2   1 
ATOM   3411 C  CZ    . PHE B 1  159 ? -12.64048 17.56246  9.64938   1.000 67.02677  ? 189 PHE B CZ    1 
ATOM   3412 N  N     . PRO B 1  160 ? -5.53027  19.20031  10.19206  1.000 38.36835  ? 190 PRO B N     1 
ATOM   3413 C  CA    . PRO B 1  160 ? -4.12012  19.19122  10.59753  1.000 39.84452  ? 190 PRO B CA    1 
ATOM   3414 C  C     . PRO B 1  160 ? -3.90067  18.27697  11.79725  1.000 41.47004  ? 190 PRO B C     1 
ATOM   3415 O  O     . PRO B 1  160 ? -4.72033  18.22078  12.71855  1.000 38.50056  ? 190 PRO B O     1 
ATOM   3416 C  CB    . PRO B 1  160 ? -3.83198  20.65915  10.93672  1.000 42.33802  ? 190 PRO B CB    1 
ATOM   3417 C  CG    . PRO B 1  160 ? -5.19194  21.32613  11.03937  1.000 45.58516  ? 190 PRO B CG    1 
ATOM   3418 C  CD    . PRO B 1  160 ? -6.09828  20.56132  10.14355  1.000 34.71394  ? 190 PRO B CD    1 
ATOM   3419 N  N     . ILE B 1  161 ? -2.78768  17.55697  11.77869  1.000 33.75309  ? 191 ILE B N     1 
ATOM   3420 C  CA    . ILE B 1  161 ? -2.45429  16.61074  12.84336  1.000 38.15472  ? 191 ILE B CA    1 
ATOM   3421 C  C     . ILE B 1  161 ? -1.69488  17.36752  13.92424  1.000 45.18608  ? 191 ILE B C     1 
ATOM   3422 O  O     . ILE B 1  161 ? -0.62197  17.92356  13.66295  1.000 44.19785  ? 191 ILE B O     1 
ATOM   3423 C  CB    . ILE B 1  161 ? -1.62749  15.43185  12.31381  1.000 48.60065  ? 191 ILE B CB    1 
ATOM   3424 C  CG1   . ILE B 1  161 ? -2.48084  14.55605  11.39195  1.000 43.56112  ? 191 ILE B CG1   1 
ATOM   3425 C  CG2   . ILE B 1  161 ? -1.00805  14.62460  13.48741  1.000 40.86635  ? 191 ILE B CG2   1 
ATOM   3426 C  CD1   . ILE B 1  161 ? -1.67811  13.48419  10.70142  1.000 55.86584  ? 191 ILE B CD1   1 
ATOM   3427 N  N     . ARG B 1  162 ? -2.23342  17.36526  15.14044  1.000 49.95555  ? 192 ARG B N     1 
ATOM   3428 C  CA    . ARG B 1  162 ? -1.68300  18.13303  16.25139  1.000 49.29168  ? 192 ARG B CA    1 
ATOM   3429 C  C     . ARG B 1  162 ? -0.93562  17.26982  17.26493  1.000 52.61967  ? 192 ARG B C     1 
ATOM   3430 O  O     . ARG B 1  162 ? -0.54123  17.78860  18.31389  1.000 50.35416  ? 192 ARG B O     1 
ATOM   3431 C  CB    . ARG B 1  162 ? -2.80574  18.90589  16.94497  1.000 37.58104  ? 192 ARG B CB    1 
ATOM   3432 C  CG    . ARG B 1  162 ? -3.64308  19.79009  16.02347  1.000 40.15621  ? 192 ARG B CG    1 
ATOM   3433 C  CD    . ARG B 1  162 ? -2.82533  20.87923  15.34339  1.000 32.58210  ? 192 ARG B CD    1 
ATOM   3434 N  NE    . ARG B 1  162 ? -3.71157  21.84337  14.69193  1.000 43.04941  ? 192 ARG B NE    1 
ATOM   3435 C  CZ    . ARG B 1  162 ? -3.30784  22.85852  13.94098  1.000 46.00582  ? 192 ARG B CZ    1 
ATOM   3436 N  NH1   . ARG B 1  162 ? -2.02895  23.03757  13.65954  1.000 46.58384  ? 192 ARG B NH1   1 
ATOM   3437 N  NH2   . ARG B 1  162 ? -4.21003  23.69763  13.44850  1.000 45.87623  ? 192 ARG B NH2   1 
ATOM   3438 N  N     . GLN B 1  163 ? -0.73973  15.97187  16.99659  1.000 58.42032  ? 193 GLN B N     1 
ATOM   3439 C  CA    . GLN B 1  163 ? -0.01139  15.09168  17.91113  1.000 42.44052  ? 193 GLN B CA    1 
ATOM   3440 C  C     . GLN B 1  163 ? 1.48653   15.28471  17.71461  1.000 51.07830  ? 193 GLN B C     1 
ATOM   3441 O  O     . GLN B 1  163 ? 2.01213   14.94993  16.64734  1.000 53.00392  ? 193 GLN B O     1 
ATOM   3442 C  CB    . GLN B 1  163 ? -0.39049  13.62273  17.66897  1.000 51.97445  ? 193 GLN B CB    1 
ATOM   3443 C  CG    . GLN B 1  163 ? -1.89551  13.32675  17.61647  1.000 56.60476  ? 193 GLN B CG    1 
ATOM   3444 C  CD    . GLN B 1  163 ? -2.21976  11.97789  16.95931  1.000 69.96433  ? 193 GLN B CD    1 
ATOM   3445 O  OE1   . GLN B 1  163 ? -2.40251  10.96374  17.64317  1.000 73.67936  ? 193 GLN B OE1   1 
ATOM   3446 N  NE2   . GLN B 1  163 ? -2.30526  11.97316  15.62834  1.000 62.76472  ? 193 GLN B NE2   1 
ATOM   3447 N  N     . PRO B 1  164 ? 2.21191   15.81350  18.70845  1.000 57.67398  ? 194 PRO B N     1 
ATOM   3448 C  CA    . PRO B 1  164 ? 3.62682   16.16354  18.46399  1.000 46.48811  ? 194 PRO B CA    1 
ATOM   3449 C  C     . PRO B 1  164 ? 4.52969   14.99061  18.12641  1.000 42.72056  ? 194 PRO B C     1 
ATOM   3450 O  O     . PRO B 1  164 ? 5.63650   15.21471  17.62604  1.000 42.76077  ? 194 PRO B O     1 
ATOM   3451 C  CB    . PRO B 1  164 ? 4.05432   16.84527  19.77797  1.000 42.81561  ? 194 PRO B CB    1 
ATOM   3452 C  CG    . PRO B 1  164 ? 2.94268   16.63107  20.74634  1.000 44.38422  ? 194 PRO B CG    1 
ATOM   3453 C  CD    . PRO B 1  164 ? 1.69938   16.41825  19.94677  1.000 45.10069  ? 194 PRO B CD    1 
ATOM   3454 N  N     . PHE B 1  165 ? 4.10677   13.74956  18.36131  1.000 49.37598  ? 195 PHE B N     1 
ATOM   3455 C  CA    . PHE B 1  165 ? 4.90661   12.60464  17.95177  1.000 51.22017  ? 195 PHE B CA    1 
ATOM   3456 C  C     . PHE B 1  165 ? 4.74306   12.23595  16.48075  1.000 54.16478  ? 195 PHE B C     1 
ATOM   3457 O  O     . PHE B 1  165 ? 5.52486   11.42705  15.96929  1.000 61.10508  ? 195 PHE B O     1 
ATOM   3458 C  CB    . PHE B 1  165 ? 4.54093   11.39247  18.81065  1.000 51.06142  ? 195 PHE B CB    1 
ATOM   3459 C  CG    . PHE B 1  165 ? 3.08492   11.05648  18.78413  1.000 53.30962  ? 195 PHE B CG    1 
ATOM   3460 C  CD1   . PHE B 1  165 ? 2.55953   10.28370  17.76117  1.000 58.60083  ? 195 PHE B CD1   1 
ATOM   3461 C  CD2   . PHE B 1  165 ? 2.23129   11.52628  19.77355  1.000 58.39178  ? 195 PHE B CD2   1 
ATOM   3462 C  CE1   . PHE B 1  165 ? 1.20652   9.97971   17.73061  1.000 58.50591  ? 195 PHE B CE1   1 
ATOM   3463 C  CE2   . PHE B 1  165 ? 0.87928   11.22229  19.74699  1.000 55.66492  ? 195 PHE B CE2   1 
ATOM   3464 C  CZ    . PHE B 1  165 ? 0.37089   10.44151  18.72002  1.000 51.16215  ? 195 PHE B CZ    1 
ATOM   3465 N  N     . SER B 1  166 ? 3.75080   12.79910  15.79124  1.000 55.26571  ? 196 SER B N     1 
ATOM   3466 C  CA    . SER B 1  166 ? 3.48728   12.45739  14.39427  1.000 46.54873  ? 196 SER B CA    1 
ATOM   3467 C  C     . SER B 1  166 ? 4.50893   13.10158  13.46002  1.000 46.90907  ? 196 SER B C     1 
ATOM   3468 O  O     . SER B 1  166 ? 4.87600   14.27054  13.62513  1.000 46.72326  ? 196 SER B O     1 
ATOM   3469 C  CB    . SER B 1  166 ? 2.08313   12.91448  13.99889  1.000 41.28594  ? 196 SER B CB    1 
ATOM   3470 O  OG    . SER B 1  166 ? 1.84561   12.65077  12.62193  1.000 46.91371  ? 196 SER B OG    1 
ATOM   3471 N  N     . LYS B 1  167 ? 4.95155   12.34179  12.44870  1.000 44.21947  ? 197 LYS B N     1 
ATOM   3472 C  CA    . LYS B 1  167 ? 5.81417   12.95599  11.44150  1.000 56.26917  ? 197 LYS B CA    1 
ATOM   3473 C  C     . LYS B 1  167 ? 5.08389   14.06315  10.69101  1.000 47.48218  ? 197 LYS B C     1 
ATOM   3474 O  O     . LYS B 1  167 ? 5.72867   14.91728  10.07894  1.000 55.70140  ? 197 LYS B O     1 
ATOM   3475 C  CB    . LYS B 1  167 ? 6.35580   11.90620  10.45708  1.000 50.85578  ? 197 LYS B CB    1 
ATOM   3476 C  CG    . LYS B 1  167 ? 5.37939   11.45042  9.38435   1.000 61.64931  ? 197 LYS B CG    1 
ATOM   3477 C  CD    . LYS B 1  167 ? 6.01903   10.42362  8.43790   1.000 60.85168  ? 197 LYS B CD    1 
ATOM   3478 C  CE    . LYS B 1  167 ? 7.40286   10.87371  7.97947   1.000 68.72868  ? 197 LYS B CE    1 
ATOM   3479 N  NZ    . LYS B 1  167 ? 8.04150   9.91190   7.02403   1.000 69.14372  ? 197 LYS B NZ    1 
ATOM   3480 N  N     . TRP B 1  168 ? 3.75893   14.05514  10.78450  1.000 45.11583  ? 198 TRP B N     1 
ATOM   3481 C  CA    . TRP B 1  168 ? 2.93667   15.06129  10.08602  1.000 49.74809  ? 198 TRP B CA    1 
ATOM   3482 C  C     . TRP B 1  168 ? 2.35405   16.05809  11.08545  1.000 43.97501  ? 198 TRP B C     1 
ATOM   3483 O  O     . TRP B 1  168 ? 1.34193   16.67816  10.76195  1.000 42.94050  ? 198 TRP B O     1 
ATOM   3484 C  CB    . TRP B 1  168 ? 1.84037   14.33746  9.30028   1.000 52.64759  ? 198 TRP B CB    1 
ATOM   3485 C  CG    . TRP B 1  168 ? 2.34100   13.31166  8.31988   1.000 55.23220  ? 198 TRP B CG    1 
ATOM   3486 C  CD1   . TRP B 1  168 ? 3.41369   13.40683  7.48750   1.000 53.58161  ? 198 TRP B CD1   1 
ATOM   3487 C  CD2   . TRP B 1  168 ? 1.73990   12.02672  8.05784   1.000 62.80107  ? 198 TRP B CD2   1 
ATOM   3488 N  NE1   . TRP B 1  168 ? 3.53640   12.26398  6.73921   1.000 59.35448  ? 198 TRP B NE1   1 
ATOM   3489 C  CE2   . TRP B 1  168 ? 2.52452   11.40492  7.06441   1.000 63.22039  ? 198 TRP B CE2   1 
ATOM   3490 C  CE3   . TRP B 1  168 ? 0.62908   11.34862  8.56811   1.000 67.48746  ? 198 TRP B CE3   1 
ATOM   3491 C  CZ2   . TRP B 1  168 ? 2.22433   10.13903  6.57126   1.000 70.80949  ? 198 TRP B CZ2   1 
ATOM   3492 C  CZ3   . TRP B 1  168 ? 0.33389   10.09572  8.07896   1.000 87.26115  ? 198 TRP B CZ3   1 
ATOM   3493 C  CH2   . TRP B 1  168 ? 1.11252   9.50792   7.08555   1.000 88.46667  ? 198 TRP B CH2   1 
ATOM   3494 N  N     . PHE B 1  169 ? 2.96849   16.21584  12.25125  1.000 41.64879  ? 199 PHE B N     1 
ATOM   3495 C  CA    . PHE B 1  169 ? 2.54586   17.21564  13.21961  1.000 45.50556  ? 199 PHE B CA    1 
ATOM   3496 C  C     . PHE B 1  169 ? 2.81267   18.61775  12.68781  1.000 37.60088  ? 199 PHE B C     1 
ATOM   3497 O  O     . PHE B 1  169 ? 3.89046   18.88986  12.15046  1.000 44.49449  ? 199 PHE B O     1 
ATOM   3498 C  CB    . PHE B 1  169 ? 3.30035   17.00836  14.53729  1.000 46.93017  ? 199 PHE B CB    1 
ATOM   3499 C  CG    . PHE B 1  169 ? 3.27270   18.20517  15.45255  1.000 44.36074  ? 199 PHE B CG    1 
ATOM   3500 C  CD1   . PHE B 1  169 ? 2.13497   18.50203  16.17804  1.000 36.63914  ? 199 PHE B CD1   1 
ATOM   3501 C  CD2   . PHE B 1  169 ? 4.37775   19.01914  15.58130  1.000 40.07231  ? 199 PHE B CD2   1 
ATOM   3502 C  CE1   . PHE B 1  169 ? 2.10429   19.59285  17.01528  1.000 35.96143  ? 199 PHE B CE1   1 
ATOM   3503 C  CE2   . PHE B 1  169 ? 4.35608   20.11596  16.42754  1.000 37.92951  ? 199 PHE B CE2   1 
ATOM   3504 C  CZ    . PHE B 1  169 ? 3.21435   20.40082  17.14303  1.000 35.93294  ? 199 PHE B CZ    1 
ATOM   3505 N  N     . VAL B 1  170 ? 1.82772   19.51173  12.82936  1.000 37.20303  ? 200 VAL B N     1 
ATOM   3506 C  CA    . VAL B 1  170 ? 2.02363   20.93578  12.56858  1.000 50.24111  ? 200 VAL B CA    1 
ATOM   3507 C  C     . VAL B 1  170 ? 1.48908   21.74854  13.74195  1.000 43.61779  ? 200 VAL B C     1 
ATOM   3508 O  O     . VAL B 1  170 ? 0.34223   21.55546  14.16434  1.000 47.86452  ? 200 VAL B O     1 
ATOM   3509 C  CB    . VAL B 1  170 ? 1.35214   21.39006  11.25593  1.000 48.49745  ? 200 VAL B CB    1 
ATOM   3510 C  CG1   . VAL B 1  170 ? 2.05869   20.79230  10.06554  1.000 41.49520  ? 200 VAL B CG1   1 
ATOM   3511 C  CG2   . VAL B 1  170 ? -0.12186  21.02106  11.26041  1.000 46.29259  ? 200 VAL B CG2   1 
ATOM   3512 N  N     . SER B 1  171 ? 2.30027   22.67243  14.24684  1.000 43.50170  ? 201 SER B N     1 
ATOM   3513 C  CA    . SER B 1  171 ? 1.84867   23.55421  15.31420  1.000 45.80958  ? 201 SER B CA    1 
ATOM   3514 C  C     . SER B 1  171 ? 0.76748   24.50532  14.79380  1.000 47.73860  ? 201 SER B C     1 
ATOM   3515 O  O     . SER B 1  171 ? 0.55203   24.64257  13.58691  1.000 51.66794  ? 201 SER B O     1 
ATOM   3516 C  CB    . SER B 1  171 ? 3.01389   24.36509  15.87293  1.000 43.99996  ? 201 SER B CB    1 
ATOM   3517 O  OG    . SER B 1  171 ? 3.30357   25.45726  15.01005  1.000 53.44399  ? 201 SER B OG    1 
ATOM   3518 N  N     . LYS B 1  172 ? 0.08684   25.18013  15.72619  1.000 45.59312  ? 202 LYS B N     1 
ATOM   3519 C  CA    . LYS B 1  172 ? -0.92532  26.13822  15.30477  1.000 54.06424  ? 202 LYS B CA    1 
ATOM   3520 C  C     . LYS B 1  172 ? -0.30155  27.37435  14.67780  1.000 53.18426  ? 202 LYS B C     1 
ATOM   3521 O  O     . LYS B 1  172 ? -0.96284  28.05352  13.88919  1.000 57.05905  ? 202 LYS B O     1 
ATOM   3522 C  CB    . LYS B 1  172 ? -1.82288  26.52599  16.47519  1.000 50.27211  ? 202 LYS B CB    1 
ATOM   3523 C  CG    . LYS B 1  172 ? -2.68570  25.38189  16.95528  1.000 48.25607  ? 202 LYS B CG    1 
ATOM   3524 C  CD    . LYS B 1  172 ? -4.08556  25.83282  17.33690  1.000 60.88659  ? 202 LYS B CD    1 
ATOM   3525 C  CE    . LYS B 1  172 ? -4.88434  24.67770  17.92696  1.000 63.25142  ? 202 LYS B CE    1 
ATOM   3526 N  NZ    . LYS B 1  172 ? -6.20114  25.14159  18.45755  1.000 88.78798  ? 202 LYS B NZ    1 
ATOM   3527 N  N     . SER B 1  173 ? 0.95657   27.66328  14.98838  1.000 53.64044  ? 203 SER B N     1 
ATOM   3528 C  CA    . SER B 1  173 ? 1.64231   28.73443  14.27435  1.000 56.84289  ? 203 SER B CA    1 
ATOM   3529 C  C     . SER B 1  173 ? 2.14280   28.26171  12.91106  1.000 53.60110  ? 203 SER B C     1 
ATOM   3530 O  O     . SER B 1  173 ? 2.29346   29.08190  11.99718  1.000 63.97195  ? 203 SER B O     1 
ATOM   3531 C  CB    . SER B 1  173 ? 2.78763   29.28024  15.12703  1.000 52.10634  ? 203 SER B CB    1 
ATOM   3532 O  OG    . SER B 1  173 ? 3.78571   28.30219  15.35546  1.000 59.93667  ? 203 SER B OG    1 
ATOM   3533 N  N     . GLU B 1  174 ? 2.39073   26.95374  12.75070  1.000 51.61956  ? 204 GLU B N     1 
ATOM   3534 C  CA    . GLU B 1  174 ? 2.73423   26.42101  11.43446  1.000 52.01827  ? 204 GLU B CA    1 
ATOM   3535 C  C     . GLU B 1  174 ? 1.51289   26.37121  10.51791  1.000 50.96307  ? 204 GLU B C     1 
ATOM   3536 O  O     . GLU B 1  174 ? 1.60944   26.68246  9.32394   1.000 37.04430  ? 204 GLU B O     1 
ATOM   3537 C  CB    . GLU B 1  174 ? 3.36728   25.03398  11.56493  1.000 50.54278  ? 204 GLU B CB    1 
ATOM   3538 C  CG    . GLU B 1  174 ? 4.80246   25.04087  12.06440  1.000 51.60525  ? 204 GLU B CG    1 
ATOM   3539 C  CD    . GLU B 1  174 ? 5.33457   23.64281  12.35791  1.000 64.52166  ? 204 GLU B CD    1 
ATOM   3540 O  OE1   . GLU B 1  174 ? 4.57877   22.81470  12.90802  1.000 63.74143  ? 204 GLU B OE1   1 
ATOM   3541 O  OE2   . GLU B 1  174 ? 6.51044   23.36987  12.02041  1.000 74.59326  ? 204 GLU B OE2   1 
ATOM   3542 N  N     . TYR B 1  175 ? 0.36109   25.98310  11.05526  1.000 52.38528  ? 205 TYR B N     1 
ATOM   3543 C  CA    . TYR B 1  175 ? -0.89519  26.02326  10.30874  1.000 42.66341  ? 205 TYR B CA    1 
ATOM   3544 C  C     . TYR B 1  175 ? -2.01982  26.32806  11.29122  1.000 49.34205  ? 205 TYR B C     1 
ATOM   3545 O  O     . TYR B 1  175 ? -2.41653  25.46190  12.08119  1.000 39.88463  ? 205 TYR B O     1 
ATOM   3546 C  CB    . TYR B 1  175 ? -1.16848  24.70442  9.55557   1.000 40.05007  ? 205 TYR B CB    1 
ATOM   3547 C  CG    . TYR B 1  175 ? -2.38482  24.78861  8.65604   1.000 41.61713  ? 205 TYR B CG    1 
ATOM   3548 C  CD1   . TYR B 1  175 ? -2.29030  25.32588  7.37712   1.000 36.76369  ? 205 TYR B CD1   1 
ATOM   3549 C  CD2   . TYR B 1  175 ? -3.63366  24.35653  9.08842   1.000 39.80859  ? 205 TYR B CD2   1 
ATOM   3550 C  CE1   . TYR B 1  175 ? -3.39861  25.42206  6.54955   1.000 37.11510  ? 205 TYR B CE1   1 
ATOM   3551 C  CE2   . TYR B 1  175 ? -4.74996  24.45071  8.26986   1.000 43.34594  ? 205 TYR B CE2   1 
ATOM   3552 C  CZ    . TYR B 1  175 ? -4.62244  24.99197  6.98992   1.000 43.12032  ? 205 TYR B CZ    1 
ATOM   3553 O  OH    . TYR B 1  175 ? -5.71575  25.09515  6.15535   1.000 42.98076  ? 205 TYR B OH    1 
ATOM   3554 N  N     . PRO B 1  176 ? -2.55383  27.54807  11.26668  1.000 47.10478  ? 206 PRO B N     1 
ATOM   3555 C  CA    . PRO B 1  176 ? -3.46242  27.99486  12.33311  1.000 47.01430  ? 206 PRO B CA    1 
ATOM   3556 C  C     . PRO B 1  176 ? -4.93648  27.65590  12.17259  1.000 45.93899  ? 206 PRO B C     1 
ATOM   3557 O  O     . PRO B 1  176 ? -5.70614  27.97171  13.08595  1.000 54.67636  ? 206 PRO B O     1 
ATOM   3558 C  CB    . PRO B 1  176 ? -3.26242  29.52086  12.31935  1.000 40.62971  ? 206 PRO B CB    1 
ATOM   3559 C  CG    . PRO B 1  176 ? -2.88995  29.83715  10.91028  1.000 47.09150  ? 206 PRO B CG    1 
ATOM   3560 C  CD    . PRO B 1  176 ? -2.08514  28.66225  10.42273  1.000 47.42814  ? 206 PRO B CD    1 
ATOM   3561 N  N     . TRP B 1  177 ? -5.37490  27.05213  11.06563  1.000 46.93237  ? 207 TRP B N     1 
ATOM   3562 C  CA    . TRP B 1  177 ? -6.80198  26.83218  10.86312  1.000 45.94874  ? 207 TRP B CA    1 
ATOM   3563 C  C     . TRP B 1  177 ? -7.18289  25.37712  11.12996  1.000 46.33469  ? 207 TRP B C     1 
ATOM   3564 O  O     . TRP B 1  177 ? -6.33187  24.48611  11.19746  1.000 44.66343  ? 207 TRP B O     1 
ATOM   3565 C  CB    . TRP B 1  177 ? -7.22951  27.26247  9.45337   1.000 44.82279  ? 207 TRP B CB    1 
ATOM   3566 C  CG    . TRP B 1  177 ? -6.99658  28.74052  9.23459   1.000 47.74346  ? 207 TRP B CG    1 
ATOM   3567 C  CD1   . TRP B 1  177 ? -7.72338  29.77141  9.75908   1.000 48.34644  ? 207 TRP B CD1   1 
ATOM   3568 C  CD2   . TRP B 1  177 ? -5.94987  29.33967  8.46332   1.000 47.70734  ? 207 TRP B CD2   1 
ATOM   3569 N  NE1   . TRP B 1  177 ? -7.19053  30.97949  9.35413   1.000 46.10020  ? 207 TRP B NE1   1 
ATOM   3570 C  CE2   . TRP B 1  177 ? -6.09782  30.73965  8.56567   1.000 45.96287  ? 207 TRP B CE2   1 
ATOM   3571 C  CE3   . TRP B 1  177 ? -4.89515  28.82882  7.70782   1.000 45.29946  ? 207 TRP B CE3   1 
ATOM   3572 C  CZ2   . TRP B 1  177 ? -5.24906  31.62878  7.91654   1.000 46.38641  ? 207 TRP B CZ2   1 
ATOM   3573 C  CZ3   . TRP B 1  177 ? -4.04239  29.71995  7.06569   1.000 48.73363  ? 207 TRP B CZ3   1 
ATOM   3574 C  CH2   . TRP B 1  177 ? -4.22734  31.10493  7.17605   1.000 40.92576  ? 207 TRP B CH2   1 
ATOM   3575 N  N     . ASP B 1  178 ? -8.49082  25.16109  11.30741  1.000 64.89559  ? 208 ASP B N     1 
ATOM   3576 C  CA    . ASP B 1  178 ? -9.02467  23.86701  11.72734  1.000 56.69445  ? 208 ASP B CA    1 
ATOM   3577 C  C     . ASP B 1  178 ? -8.97709  22.81524  10.62610  1.000 53.29560  ? 208 ASP B C     1 
ATOM   3578 O  O     . ASP B 1  178 ? -8.98298  21.61717  10.92886  1.000 53.76164  ? 208 ASP B O     1 
ATOM   3579 C  CB    . ASP B 1  178 ? -10.47850 24.00492  12.18891  1.000 57.74754  ? 208 ASP B CB    1 
ATOM   3580 C  CG    . ASP B 1  178 ? -10.62304 24.89867  13.39815  1.000 91.86733  ? 208 ASP B CG    1 
ATOM   3581 O  OD1   . ASP B 1  178 ? -9.59979  25.20353  14.04983  1.000 97.12516  ? 208 ASP B OD1   1 
ATOM   3582 O  OD2   . ASP B 1  178 ? -11.77192 25.29761  13.70067  1.000 103.16901 ? 208 ASP B OD2   1 
ATOM   3583 N  N     . ARG B 1  179 ? -8.97056  23.22650  9.36319   1.000 54.54823  ? 209 ARG B N     1 
ATOM   3584 C  CA    . ARG B 1  179 ? -9.10898  22.29373  8.25904   1.000 47.73577  ? 209 ARG B CA    1 
ATOM   3585 C  C     . ARG B 1  179 ? -8.04437  22.57294  7.21170   1.000 45.25513  ? 209 ARG B C     1 
ATOM   3586 O  O     . ARG B 1  179 ? -7.57842  23.70697  7.06176   1.000 44.86097  ? 209 ARG B O     1 
ATOM   3587 C  CB    . ARG B 1  179 ? -10.50322 22.38187  7.62858   1.000 48.16472  ? 209 ARG B CB    1 
ATOM   3588 C  CG    . ARG B 1  179 ? -11.62485 22.10667  8.61295   1.000 63.01596  ? 209 ARG B CG    1 
ATOM   3589 C  CD    . ARG B 1  179 ? -12.98007 22.44580  8.01253   1.000 91.32994  ? 209 ARG B CD    1 
ATOM   3590 N  NE    . ARG B 1  179 ? -13.25153 21.68906  6.79347   1.000 106.38109 ? 209 ARG B NE    1 
ATOM   3591 C  CZ    . ARG B 1  179 ? -13.86355 20.51307  6.75746   1.000 101.12307 ? 209 ARG B CZ    1 
ATOM   3592 N  NH1   . ARG B 1  179 ? -14.27514 19.91284  7.86549   1.000 89.79308  ? 209 ARG B NH1   1 
ATOM   3593 N  NH2   . ARG B 1  179 ? -14.07300 19.92931  5.57941   1.000 87.62602  ? 209 ARG B NH2   1 
ATOM   3594 N  N     . TYR B 1  180 ? -7.64264  21.51209  6.50833   1.000 43.48192  ? 210 TYR B N     1 
ATOM   3595 C  CA    . TYR B 1  180 ? -6.79508  21.63533  5.34104   1.000 35.83509  ? 210 TYR B CA    1 
ATOM   3596 C  C     . TYR B 1  180 ? -7.65954  21.91959  4.10942   1.000 38.04016  ? 210 TYR B C     1 
ATOM   3597 O  O     . TYR B 1  180 ? -8.86454  21.65559  4.10882   1.000 36.74981  ? 210 TYR B O     1 
ATOM   3598 C  CB    . TYR B 1  180 ? -5.98916  20.36036  5.14447   1.000 35.16810  ? 210 TYR B CB    1 
ATOM   3599 C  CG    . TYR B 1  180 ? -4.76183  20.25717  6.03099   1.000 40.96488  ? 210 TYR B CG    1 
ATOM   3600 C  CD1   . TYR B 1  180 ? -4.05368  21.39209  6.39896   1.000 35.05291  ? 210 TYR B CD1   1 
ATOM   3601 C  CD2   . TYR B 1  180 ? -4.32066  19.02507  6.49957   1.000 41.96702  ? 210 TYR B CD2   1 
ATOM   3602 C  CE1   . TYR B 1  180 ? -2.92638  21.30592  7.20852   1.000 40.81514  ? 210 TYR B CE1   1 
ATOM   3603 C  CE2   . TYR B 1  180 ? -3.19136  18.93290  7.29712   1.000 38.56027  ? 210 TYR B CE2   1 
ATOM   3604 C  CZ    . TYR B 1  180 ? -2.50822  20.06982  7.65410   1.000 36.24166  ? 210 TYR B CZ    1 
ATOM   3605 O  OH    . TYR B 1  180 ? -1.38592  19.96165  8.44166   1.000 39.59922  ? 210 TYR B OH    1 
ATOM   3606 N  N     . PRO B 1  181 ? -7.08093  22.47480  3.05332   1.000 46.57694  ? 211 PRO B N     1 
ATOM   3607 C  CA    . PRO B 1  181 ? -7.80041  22.55107  1.78161   1.000 47.99878  ? 211 PRO B CA    1 
ATOM   3608 C  C     . PRO B 1  181 ? -7.96063  21.15919  1.21738   1.000 36.84309  ? 211 PRO B C     1 
ATOM   3609 O  O     . PRO B 1  181 ? -7.33044  20.21108  1.72394   1.000 39.44226  ? 211 PRO B O     1 
ATOM   3610 C  CB    . PRO B 1  181 ? -6.86773  23.39825  0.90643   1.000 46.45601  ? 211 PRO B CB    1 
ATOM   3611 C  CG    . PRO B 1  181 ? -5.52555  23.04714  1.39385   1.000 44.19227  ? 211 PRO B CG    1 
ATOM   3612 C  CD    . PRO B 1  181 ? -5.67199  22.88183  2.89788   1.000 43.42184  ? 211 PRO B CD    1 
ATOM   3613 N  N     . PRO B 1  182 ? -8.76402  20.98641  0.17364   1.000 44.37600  ? 212 PRO B N     1 
ATOM   3614 C  CA    . PRO B 1  182 ? -8.68931  19.73057  -0.58965  1.000 39.95501  ? 212 PRO B CA    1 
ATOM   3615 C  C     . PRO B 1  182 ? -7.28352  19.57568  -1.14021  1.000 38.25001  ? 212 PRO B C     1 
ATOM   3616 O  O     . PRO B 1  182 ? -6.68469  20.53977  -1.61823  1.000 39.77354  ? 212 PRO B O     1 
ATOM   3617 C  CB    . PRO B 1  182 ? -9.71874  19.92381  -1.72022  1.000 41.96352  ? 212 PRO B CB    1 
ATOM   3618 C  CG    . PRO B 1  182 ? -10.49660 21.15074  -1.36867  1.000 37.99678  ? 212 PRO B CG    1 
ATOM   3619 C  CD    . PRO B 1  182 ? -9.61926  21.98755  -0.48683  1.000 37.96457  ? 212 PRO B CD    1 
ATOM   3620 N  N     . PHE B 1  183 ? -6.73849  18.36666  -1.05766  1.000 36.15511  ? 213 PHE B N     1 
ATOM   3621 C  CA    . PHE B 1  183 ? -5.48675  18.09779  -1.74319  1.000 36.13273  ? 213 PHE B CA    1 
ATOM   3622 C  C     . PHE B 1  183 ? -5.44089  16.61586  -2.08052  1.000 36.61769  ? 213 PHE B C     1 
ATOM   3623 O  O     . PHE B 1  183 ? -6.34076  15.85179  -1.72434  1.000 46.68182  ? 213 PHE B O     1 
ATOM   3624 C  CB    . PHE B 1  183 ? -4.25844  18.52762  -0.92356  1.000 35.94837  ? 213 PHE B CB    1 
ATOM   3625 C  CG    . PHE B 1  183 ? -4.06296  17.75135  0.36420   1.000 35.24965  ? 213 PHE B CG    1 
ATOM   3626 C  CD1   . PHE B 1  183 ? -4.85855  18.01512  1.47556   1.000 39.35936  ? 213 PHE B CD1   1 
ATOM   3627 C  CD2   . PHE B 1  183 ? -3.07993  16.78032  0.46563   1.000 44.06066  ? 213 PHE B CD2   1 
ATOM   3628 C  CE1   . PHE B 1  183 ? -4.68510  17.30587  2.67035   1.000 45.88083  ? 213 PHE B CE1   1 
ATOM   3629 C  CE2   . PHE B 1  183 ? -2.88848  16.06507  1.66441   1.000 44.34247  ? 213 PHE B CE2   1 
ATOM   3630 C  CZ    . PHE B 1  183 ? -3.70307  16.32985  2.75877   1.000 44.33824  ? 213 PHE B CZ    1 
ATOM   3631 N  N     . CYS B 1  184 ? -4.39215  16.22901  -2.79199  1.000 35.77733  ? 214 CYS B N     1 
ATOM   3632 C  CA    . CYS B 1  184 ? -4.15031  14.84509  -3.19037  1.000 42.80890  ? 214 CYS B CA    1 
ATOM   3633 C  C     . CYS B 1  184 ? -2.92404  14.31293  -2.46494  1.000 48.11690  ? 214 CYS B C     1 
ATOM   3634 O  O     . CYS B 1  184 ? -1.90900  15.01091  -2.36917  1.000 50.24403  ? 214 CYS B O     1 
ATOM   3635 C  CB    . CYS B 1  184 ? -3.91388  14.72140  -4.69648  1.000 43.90082  ? 214 CYS B CB    1 
ATOM   3636 S  SG    . CYS B 1  184 ? -5.33127  15.11763  -5.75387  1.000 47.91188  ? 214 CYS B SG    1 
ATOM   3637 N  N     . SER B 1  185 ? -2.94791  13.03486  -2.10220  1.000 44.84329  ? 215 SER B N     1 
ATOM   3638 C  CA    . SER B 1  185 ? -1.77367  12.38972  -1.45877  1.000 47.54848  ? 215 SER B CA    1 
ATOM   3639 C  C     . SER B 1  185 ? -0.48696  12.65687  -2.23920  1.000 41.71412  ? 215 SER B C     1 
ATOM   3640 O  O     . SER B 1  185 ? -0.50743  12.55813  -3.47521  1.000 40.96810  ? 215 SER B O     1 
ATOM   3641 C  CB    . SER B 1  185 ? -1.99462  10.91568  -1.30299  1.000 37.66567  ? 215 SER B CB    1 
ATOM   3642 O  OG    . SER B 1  185 ? -0.80248  10.25960  -0.90758  1.000 50.80377  ? 215 SER B OG    1 
ATOM   3643 N  N     . GLY B 1  186 ? 0.60330   12.93572  -1.52855  1.000 47.53369  ? 216 GLY B N     1 
ATOM   3644 C  CA    . GLY B 1  186 ? 1.91207   13.13384  -2.16400  1.000 39.43425  ? 216 GLY B CA    1 
ATOM   3645 C  C     . GLY B 1  186 ? 2.51789   11.82693  -2.60750  1.000 42.54452  ? 216 GLY B C     1 
ATOM   3646 O  O     . GLY B 1  186 ? 3.53863   11.87907  -3.30487  1.000 48.99520  ? 216 GLY B O     1 
ATOM   3647 N  N     . THR B 1  187 ? 1.94203   10.68886  -2.22452  1.000 36.69418  ? 217 THR B N     1 
ATOM   3648 C  CA    . THR B 1  187 ? 2.42482   9.40397   -2.76697  1.000 43.49652  ? 217 THR B CA    1 
ATOM   3649 C  C     . THR B 1  187 ? 2.62727   9.67727   -4.22899  1.000 48.43728  ? 217 THR B C     1 
ATOM   3650 O  O     . THR B 1  187 ? 3.59406   9.14638   -4.78846  1.000 48.39287  ? 217 THR B O     1 
ATOM   3651 C  CB    . THR B 1  187 ? 1.44693   8.26791   -2.47484  1.000 47.37122  ? 217 THR B CB    1 
ATOM   3652 O  OG1   . THR B 1  187 ? 0.18674   8.68502   -2.98428  1.000 53.18619  ? 217 THR B OG1   1 
ATOM   3653 C  CG2   . THR B 1  187 ? 1.36448   7.95660   -0.99287  1.000 39.59650  ? 217 THR B CG2   1 
ATOM   3654 N  N     . GLY B 1  188 ? 1.73805   10.47040  -4.83049  1.000 45.20843  ? 218 GLY B N     1 
ATOM   3655 C  CA    . GLY B 1  188 ? 1.97855   10.97368  -6.18547  1.000 51.06055  ? 218 GLY B CA    1 
ATOM   3656 C  C     . GLY B 1  188 ? 0.70430   11.42182  -6.84090  1.000 45.63076  ? 218 GLY B C     1 
ATOM   3657 O  O     . GLY B 1  188 ? -0.32663  10.76479  -6.66665  1.000 46.55466  ? 218 GLY B O     1 
ATOM   3658 N  N     . TYR B 1  189 ? 0.79104   12.52797  -7.56370  1.000 41.15322  ? 219 TYR B N     1 
ATOM   3659 C  CA    . TYR B 1  189 ? -0.41019  13.10811  -8.18813  1.000 41.65044  ? 219 TYR B CA    1 
ATOM   3660 C  C     . TYR B 1  189 ? -0.03272  13.54440  -9.58418  1.000 37.84819  ? 219 TYR B C     1 
ATOM   3661 O  O     . TYR B 1  189 ? 1.15517   13.67446  -9.89060  1.000 44.15244  ? 219 TYR B O     1 
ATOM   3662 C  CB    . TYR B 1  189 ? -0.82283  14.22091  -7.22675  1.000 40.24370  ? 219 TYR B CB    1 
ATOM   3663 C  CG    . TYR B 1  189 ? 0.28737   15.12780  -6.71897  1.000 45.84875  ? 219 TYR B CG    1 
ATOM   3664 C  CD1   . TYR B 1  189 ? 0.95505   15.99198  -7.57605  1.000 40.85387  ? 219 TYR B CD1   1 
ATOM   3665 C  CD2   . TYR B 1  189 ? 0.64487   15.13652  -5.37711  1.000 47.18671  ? 219 TYR B CD2   1 
ATOM   3666 C  CE1   . TYR B 1  189 ? 1.95423   16.82688  -7.11625  1.000 49.35886  ? 219 TYR B CE1   1 
ATOM   3667 C  CE2   . TYR B 1  189 ? 1.64505   15.96842  -4.90531  1.000 45.02502  ? 219 TYR B CE2   1 
ATOM   3668 C  CZ    . TYR B 1  189 ? 2.29873   16.81659  -5.77538  1.000 50.21090  ? 219 TYR B CZ    1 
ATOM   3669 O  OH    . TYR B 1  189 ? 3.28290   17.64250  -5.33258  1.000 56.73196  ? 219 TYR B OH    1 
ATOM   3670 N  N     . VAL B 1  190 ? -1.03703  13.74958  -10.41976 1.000 38.12919  ? 220 VAL B N     1 
ATOM   3671 C  CA    . VAL B 1  190 ? -0.76456  14.11687  -11.83579 1.000 38.86844  ? 220 VAL B CA    1 
ATOM   3672 C  C     . VAL B 1  190 ? -1.47067  15.43594  -12.15425 1.000 39.25703  ? 220 VAL B C     1 
ATOM   3673 O  O     . VAL B 1  190 ? -2.60851  15.63086  -11.71778 1.000 46.23766  ? 220 VAL B O     1 
ATOM   3674 C  CB    . VAL B 1  190 ? -1.16894  13.01808  -12.82787 1.000 39.00828  ? 220 VAL B CB    1 
ATOM   3675 C  CG1   . VAL B 1  190 ? -0.75047  13.36237  -14.25095 1.000 39.79071  ? 220 VAL B CG1   1 
ATOM   3676 C  CG2   . VAL B 1  190 ? -0.60679  11.66499  -12.41836 1.000 45.88187  ? 220 VAL B CG2   1 
ATOM   3677 N  N     . PHE B 1  191 ? -0.78794  16.29209  -12.89533 1.000 39.93337  ? 221 PHE B N     1 
ATOM   3678 C  CA    . PHE B 1  191 ? -1.41209  17.56618  -13.29283 1.000 40.42744  ? 221 PHE B CA    1 
ATOM   3679 C  C     . PHE B 1  191 ? -1.03362  17.87147  -14.71991 1.000 44.41654  ? 221 PHE B C     1 
ATOM   3680 O  O     . PHE B 1  191 ? 0.04421   17.46056  -15.17540 1.000 41.51559  ? 221 PHE B O     1 
ATOM   3681 C  CB    . PHE B 1  191 ? -0.95072  18.67298  -12.33277 1.000 40.47488  ? 221 PHE B CB    1 
ATOM   3682 C  CG    . PHE B 1  191 ? 0.55235   18.77893  -12.13631 1.000 40.69615  ? 221 PHE B CG    1 
ATOM   3683 C  CD1   . PHE B 1  191 ? 1.19871   18.00473  -11.18272 1.000 44.69593  ? 221 PHE B CD1   1 
ATOM   3684 C  CD2   . PHE B 1  191 ? 1.30807   19.65608  -12.89942 1.000 42.96875  ? 221 PHE B CD2   1 
ATOM   3685 C  CE1   . PHE B 1  191 ? 2.56778   18.10768  -11.00021 1.000 43.51374  ? 221 PHE B CE1   1 
ATOM   3686 C  CE2   . PHE B 1  191 ? 2.67614   19.75104  -12.71491 1.000 41.85860  ? 221 PHE B CE2   1 
ATOM   3687 C  CZ    . PHE B 1  191 ? 3.30149   18.98284  -11.76730 1.000 41.48018  ? 221 PHE B CZ    1 
ATOM   3688 N  N     . SER B 1  192 ? -1.93589  18.53463  -15.43643 1.000 50.84737  ? 222 SER B N     1 
ATOM   3689 C  CA    . SER B 1  192 ? -1.57938  19.01890  -16.76647 1.000 42.50337  ? 222 SER B CA    1 
ATOM   3690 C  C     . SER B 1  192 ? -0.42534  20.00987  -16.65569 1.000 43.08267  ? 222 SER B C     1 
ATOM   3691 O  O     . SER B 1  192 ? -0.27096  20.70466  -15.64761 1.000 45.03896  ? 222 SER B O     1 
ATOM   3692 C  CB    . SER B 1  192 ? -2.79364  19.65305  -17.46688 1.000 42.86171  ? 222 SER B CB    1 
ATOM   3693 O  OG    . SER B 1  192 ? -3.46534  20.60989  -16.66043 1.000 50.19867  ? 222 SER B OG    1 
ATOM   3694 N  N     . GLY B 1  193 ? 0.43428   20.02708  -17.67401 1.000 45.24933  ? 223 GLY B N     1 
ATOM   3695 C  CA    . GLY B 1  193 ? 1.67732   20.78006  -17.58532 1.000 47.47121  ? 223 GLY B CA    1 
ATOM   3696 C  C     . GLY B 1  193 ? 1.50344   22.25899  -17.26695 1.000 48.77055  ? 223 GLY B C     1 
ATOM   3697 O  O     . GLY B 1  193 ? 2.33071   22.84784  -16.56414 1.000 50.90392  ? 223 GLY B O     1 
ATOM   3698 N  N     . ASP B 1  194 ? 0.42726   22.88810  -17.76141 1.000 53.81856  ? 224 ASP B N     1 
ATOM   3699 C  CA    . ASP B 1  194 ? 0.18937   24.30804  -17.48103 1.000 56.31476  ? 224 ASP B CA    1 
ATOM   3700 C  C     . ASP B 1  194 ? 0.08194   24.59473  -15.98293 1.000 65.82869  ? 224 ASP B C     1 
ATOM   3701 O  O     . ASP B 1  194 ? 0.42612   25.70563  -15.51883 1.000 55.42102  ? 224 ASP B O     1 
ATOM   3702 C  CB    . ASP B 1  194 ? -1.09089  24.74919  -18.18446 1.000 54.36066  ? 224 ASP B CB    1 
ATOM   3703 C  CG    . ASP B 1  194 ? -2.29774  23.92511  -17.77118 1.000 67.89037  ? 224 ASP B CG    1 
ATOM   3704 O  OD1   . ASP B 1  194 ? -2.21175  22.67612  -17.78547 1.000 63.14584  ? 224 ASP B OD1   1 
ATOM   3705 O  OD2   . ASP B 1  194 ? -3.33960  24.51704  -17.41466 1.000 70.46794  ? 224 ASP B OD2   1 
ATOM   3706 N  N     . VAL B 1  195 ? -0.41578  23.62057  -15.21394 1.000 53.43422  ? 225 VAL B N     1 
ATOM   3707 C  CA    . VAL B 1  195 ? -0.58024  23.82927  -13.77884 1.000 43.54021  ? 225 VAL B CA    1 
ATOM   3708 C  C     . VAL B 1  195 ? 0.76201   24.11213  -13.11928 1.000 54.54447  ? 225 VAL B C     1 
ATOM   3709 O  O     . VAL B 1  195 ? 0.82439   24.83292  -12.11716 1.000 49.00673  ? 225 VAL B O     1 
ATOM   3710 C  CB    . VAL B 1  195 ? -1.28600  22.62214  -13.12883 1.000 47.30712  ? 225 VAL B CB    1 
ATOM   3711 C  CG1   . VAL B 1  195 ? -1.30443  22.77383  -11.61879 1.000 45.69187  ? 225 VAL B CG1   1 
ATOM   3712 C  CG2   . VAL B 1  195 ? -2.71020  22.49326  -13.65832 1.000 50.24761  ? 225 VAL B CG2   1 
ATOM   3713 N  N     . ALA B 1  196 ? 1.85481   23.54223  -13.64181 1.000 50.61491  ? 226 ALA B N     1 
ATOM   3714 C  CA    . ALA B 1  196 ? 3.16603   23.80511  -13.05925 1.000 44.14098  ? 226 ALA B CA    1 
ATOM   3715 C  C     . ALA B 1  196 ? 3.45305   25.29710  -13.01505 1.000 46.62610  ? 226 ALA B C     1 
ATOM   3716 O  O     . ALA B 1  196 ? 3.85645   25.84588  -11.97908 1.000 53.00835  ? 226 ALA B O     1 
ATOM   3717 C  CB    . ALA B 1  196 ? 4.25873   23.08626  -13.84181 1.000 44.48601  ? 226 ALA B CB    1 
ATOM   3718 N  N     . SER B 1  197 ? 3.25763   25.97233  -14.14983 1.000 55.47767  ? 227 SER B N     1 
ATOM   3719 C  CA    . SER B 1  197 ? 3.52962   27.40234  -14.19064 1.000 55.60015  ? 227 SER B CA    1 
ATOM   3720 C  C     . SER B 1  197 ? 2.55696   28.15916  -13.30512 1.000 51.13326  ? 227 SER B C     1 
ATOM   3721 O  O     . SER B 1  197 ? 2.95322   29.10501  -12.61007 1.000 50.44068  ? 227 SER B O     1 
ATOM   3722 C  CB    . SER B 1  197 ? 3.48109   27.90964  -15.63151 1.000 56.83010  ? 227 SER B CB    1 
ATOM   3723 O  OG    . SER B 1  197 ? 4.61381   27.45479  -16.35703 1.000 64.44414  ? 227 SER B OG    1 
ATOM   3724 N  N     . GLN B 1  198 ? 1.28196   27.75016  -13.28772 1.000 58.09430  ? 228 GLN B N     1 
ATOM   3725 C  CA    . GLN B 1  198 ? 0.31727   28.49700  -12.47520 1.000 51.89214  ? 228 GLN B CA    1 
ATOM   3726 C  C     . GLN B 1  198 ? 0.63883   28.38768  -10.97435 1.000 49.18924  ? 228 GLN B C     1 
ATOM   3727 O  O     . GLN B 1  198 ? 0.62511   29.39653  -10.24413 1.000 47.05403  ? 228 GLN B O     1 
ATOM   3728 C  CB    . GLN B 1  198 ? -1.10584  28.03007  -12.77877 1.000 50.02260  ? 228 GLN B CB    1 
ATOM   3729 C  CG    . GLN B 1  198 ? -1.64034  28.56135  -14.11846 1.000 54.48774  ? 228 GLN B CG    1 
ATOM   3730 C  CD    . GLN B 1  198 ? -3.01348  28.02143  -14.46905 1.000 76.23124  ? 228 GLN B CD    1 
ATOM   3731 O  OE1   . GLN B 1  198 ? -3.99221  28.26929  -13.76264 1.000 80.65188  ? 228 GLN B OE1   1 
ATOM   3732 N  NE2   . GLN B 1  198 ? -3.09090  27.27666  -15.56918 1.000 73.18781  ? 228 GLN B NE2   1 
ATOM   3733 N  N     . VAL B 1  199 ? 0.92701   27.17258  -10.49471 1.000 45.31925  ? 229 VAL B N     1 
ATOM   3734 C  CA    . VAL B 1  199 ? 1.28653   26.98529  -9.09288  1.000 43.75380  ? 229 VAL B CA    1 
ATOM   3735 C  C     . VAL B 1  199 ? 2.57066   27.73521  -8.76121  1.000 54.82327  ? 229 VAL B C     1 
ATOM   3736 O  O     . VAL B 1  199 ? 2.67206   28.39200  -7.71511  1.000 53.12426  ? 229 VAL B O     1 
ATOM   3737 C  CB    . VAL B 1  199 ? 1.42165   25.48922  -8.75124  1.000 45.28907  ? 229 VAL B CB    1 
ATOM   3738 C  CG1   . VAL B 1  199 ? 2.20615   25.33694  -7.43957  1.000 42.22866  ? 229 VAL B CG1   1 
ATOM   3739 C  CG2   . VAL B 1  199 ? 0.05170   24.86020  -8.63286  1.000 44.30263  ? 229 VAL B CG2   1 
ATOM   3740 N  N     . TYR B 1  200 ? 3.60134   27.59939  -9.60662  1.000 50.02798  ? 230 TYR B N     1 
ATOM   3741 C  CA    . TYR B 1  200 ? 4.84545   28.30832  -9.32494  1.000 54.52771  ? 230 TYR B CA    1 
ATOM   3742 C  C     . TYR B 1  200 ? 4.61049   29.81331  -9.25054  1.000 55.62214  ? 230 TYR B C     1 
ATOM   3743 O  O     . TYR B 1  200 ? 5.20481   30.50113  -8.41162  1.000 63.26249  ? 230 TYR B O     1 
ATOM   3744 C  CB    . TYR B 1  200 ? 5.90505   27.98454  -10.38841 1.000 54.60197  ? 230 TYR B CB    1 
ATOM   3745 C  CG    . TYR B 1  200 ? 7.18612   28.78250  -10.23072 1.000 63.91818  ? 230 TYR B CG    1 
ATOM   3746 C  CD1   . TYR B 1  200 ? 8.18044   28.36531  -9.36118  1.000 68.75425  ? 230 TYR B CD1   1 
ATOM   3747 C  CD2   . TYR B 1  200 ? 7.39585   29.95665  -10.95156 1.000 63.35612  ? 230 TYR B CD2   1 
ATOM   3748 C  CE1   . TYR B 1  200 ? 9.35350   29.08327  -9.21147  1.000 65.41078  ? 230 TYR B CE1   1 
ATOM   3749 C  CE2   . TYR B 1  200 ? 8.56891   30.67961  -10.80885 1.000 67.93453  ? 230 TYR B CE2   1 
ATOM   3750 C  CZ    . TYR B 1  200 ? 9.54323   30.23942  -9.93630  1.000 69.97055  ? 230 TYR B CZ    1 
ATOM   3751 O  OH    . TYR B 1  200 ? 10.71429  30.94739  -9.78360  1.000 70.68911  ? 230 TYR B OH    1 
ATOM   3752 N  N     . ASN B 1  201 ? 3.72717   30.33149  -10.10710 1.000 65.56264  ? 231 ASN B N     1 
ATOM   3753 C  CA    . ASN B 1  201 ? 3.39318   31.74649  -10.08468 1.000 65.73837  ? 231 ASN B CA    1 
ATOM   3754 C  C     . ASN B 1  201 ? 2.77469   32.14721  -8.75037  1.000 57.66546  ? 231 ASN B C     1 
ATOM   3755 O  O     . ASN B 1  201 ? 3.18392   33.13608  -8.13231  1.000 67.38075  ? 231 ASN B O     1 
ATOM   3756 C  CB    . ASN B 1  201 ? 2.44276   32.06773  -11.23126 1.000 70.55299  ? 231 ASN B CB    1 
ATOM   3757 C  CG    . ASN B 1  201 ? 2.14372   33.54376  -11.35284 1.000 91.73690  ? 231 ASN B CG    1 
ATOM   3758 O  OD1   . ASN B 1  201 ? 1.16193   34.04665  -10.80237 1.000 98.38828  ? 231 ASN B OD1   1 
ATOM   3759 N  ND2   . ASN B 1  201 ? 2.99644   34.24491  -12.08901 1.000 89.73212  ? 231 ASN B ND2   1 
ATOM   3760 N  N     . VAL B 1  202 ? 1.77785   31.38712  -8.29515  1.000 57.21816  ? 232 VAL B N     1 
ATOM   3761 C  CA    . VAL B 1  202 ? 1.03830   31.79788  -7.10279  1.000 51.12701  ? 232 VAL B CA    1 
ATOM   3762 C  C     . VAL B 1  202 ? 1.73479   31.42260  -5.79913  1.000 55.94415  ? 232 VAL B C     1 
ATOM   3763 O  O     . VAL B 1  202 ? 1.32519   31.90738  -4.73587  1.000 45.98109  ? 232 VAL B O     1 
ATOM   3764 C  CB    . VAL B 1  202 ? -0.38571  31.20889  -7.13438  1.000 58.35426  ? 232 VAL B CB    1 
ATOM   3765 C  CG1   . VAL B 1  202 ? -0.34661  29.71683  -6.83670  1.000 44.39637  ? 232 VAL B CG1   1 
ATOM   3766 C  CG2   . VAL B 1  202 ? -1.29734  31.93269  -6.16688  1.000 56.15612  ? 232 VAL B CG2   1 
ATOM   3767 N  N     . SER B 1  203 ? 2.79177   30.60561  -5.85069  1.000 49.27843  ? 233 SER B N     1 
ATOM   3768 C  CA    . SER B 1  203 ? 3.28422   29.95235  -4.63701  1.000 52.31108  ? 233 SER B CA    1 
ATOM   3769 C  C     . SER B 1  203 ? 3.79362   30.95113  -3.59400  1.000 58.68657  ? 233 SER B C     1 
ATOM   3770 O  O     . SER B 1  203 ? 3.56407   30.76488  -2.39195  1.000 55.68110  ? 233 SER B O     1 
ATOM   3771 C  CB    . SER B 1  203 ? 4.37408   28.94542  -4.99663  1.000 47.33820  ? 233 SER B CB    1 
ATOM   3772 O  OG    . SER B 1  203 ? 5.45783   29.57056  -5.66091  1.000 48.76867  ? 233 SER B OG    1 
ATOM   3773 N  N     . LYS B 1  204 ? 4.49946   32.00522  -4.01604  1.000 60.88425  ? 234 LYS B N     1 
ATOM   3774 C  CA    . LYS B 1  204 ? 5.07484   32.90701  -3.02207  1.000 55.71004  ? 234 LYS B CA    1 
ATOM   3775 C  C     . LYS B 1  204 ? 4.04309   33.83288  -2.37549  1.000 53.27123  ? 234 LYS B C     1 
ATOM   3776 O  O     . LYS B 1  204 ? 4.39444   34.56868  -1.43847  1.000 53.59617  ? 234 LYS B O     1 
ATOM   3777 C  CB    . LYS B 1  204 ? 6.20961   33.73413  -3.63432  1.000 64.86481  ? 234 LYS B CB    1 
ATOM   3778 C  CG    . LYS B 1  204 ? 7.55361   33.02212  -3.63898  1.000 62.22261  ? 234 LYS B CG    1 
ATOM   3779 C  CD    . LYS B 1  204 ? 8.54726   33.69332  -4.57921  1.000 63.12327  ? 234 LYS B CD    1 
ATOM   3780 C  CE    . LYS B 1  204 ? 9.89751   33.95717  -3.90766  1.000 87.91806  ? 234 LYS B CE    1 
ATOM   3781 N  NZ    . LYS B 1  204 ? 9.86988   35.10497  -2.94941  1.000 73.02087  ? 234 LYS B NZ    1 
ATOM   3782 N  N     . SER B 1  205 ? 2.78992   33.81198  -2.82403  1.000 57.24060  ? 235 SER B N     1 
ATOM   3783 C  CA    . SER B 1  205 ? 1.71817   34.53984  -2.15747  1.000 55.42068  ? 235 SER B CA    1 
ATOM   3784 C  C     . SER B 1  205 ? 0.84849   33.64467  -1.28933  1.000 51.34600  ? 235 SER B C     1 
ATOM   3785 O  O     . SER B 1  205 ? -0.07326  34.14754  -0.62988  1.000 49.50437  ? 235 SER B O     1 
ATOM   3786 C  CB    . SER B 1  205 ? 0.83479   35.27106  -3.17499  1.000 47.73985  ? 235 SER B CB    1 
ATOM   3787 O  OG    . SER B 1  205 ? -0.19139  34.42217  -3.66578  1.000 58.64425  ? 235 SER B OG    1 
ATOM   3788 N  N     . VAL B 1  206 ? 1.10849   32.34166  -1.27770  1.000 52.67570  ? 236 VAL B N     1 
ATOM   3789 C  CA    . VAL B 1  206 ? 0.29976   31.37052  -0.54860  1.000 52.54876  ? 236 VAL B CA    1 
ATOM   3790 C  C     . VAL B 1  206 ? 1.02025   31.01424  0.75506   1.000 51.21666  ? 236 VAL B C     1 
ATOM   3791 O  O     . VAL B 1  206 ? 2.23625   30.77624  0.75355   1.000 44.17217  ? 236 VAL B O     1 
ATOM   3792 C  CB    . VAL B 1  206 ? 0.03543   30.11770  -1.40476  1.000 48.94625  ? 236 VAL B CB    1 
ATOM   3793 C  CG1   . VAL B 1  206 ? -0.61526  29.02553  -0.57074  1.000 52.43395  ? 236 VAL B CG1   1 
ATOM   3794 C  CG2   . VAL B 1  206 ? -0.83702  30.47395  -2.61836  1.000 44.42738  ? 236 VAL B CG2   1 
ATOM   3795 N  N     . PRO B 1  207 ? 0.31467   30.95401  1.87531   1.000 43.85278  ? 237 PRO B N     1 
ATOM   3796 C  CA    . PRO B 1  207 ? 0.97915   30.63574  3.15199   1.000 41.70953  ? 237 PRO B CA    1 
ATOM   3797 C  C     . PRO B 1  207 ? 1.71611   29.30376  3.06344   1.000 50.25387  ? 237 PRO B C     1 
ATOM   3798 O  O     . PRO B 1  207 ? 1.17492   28.30486  2.57844   1.000 45.81842  ? 237 PRO B O     1 
ATOM   3799 C  CB    . PRO B 1  207 ? -0.17848  30.59254  4.14942   1.000 49.43859  ? 237 PRO B CB    1 
ATOM   3800 C  CG    . PRO B 1  207 ? -1.27171  31.40468  3.51800   1.000 50.10540  ? 237 PRO B CG    1 
ATOM   3801 C  CD    . PRO B 1  207 ? -1.13127  31.17599  2.03490   1.000 47.91169  ? 237 PRO B CD    1 
ATOM   3802 N  N     . TYR B 1  208 ? 2.96228   29.30465  3.53297   1.000 41.95005  ? 238 TYR B N     1 
ATOM   3803 C  CA    . TYR B 1  208 ? 3.81925   28.13167  3.45641   1.000 44.82561  ? 238 TYR B CA    1 
ATOM   3804 C  C     . TYR B 1  208 ? 3.45464   27.10045  4.52533   1.000 46.18606  ? 238 TYR B C     1 
ATOM   3805 O  O     . TYR B 1  208 ? 3.05407   27.43421  5.64755   1.000 49.37834  ? 238 TYR B O     1 
ATOM   3806 C  CB    . TYR B 1  208 ? 5.28531   28.54063  3.60894   1.000 44.47917  ? 238 TYR B CB    1 
ATOM   3807 C  CG    . TYR B 1  208 ? 6.24938   27.38758  3.81334   1.000 41.58151  ? 238 TYR B CG    1 
ATOM   3808 C  CD1   . TYR B 1  208 ? 6.48785   26.86531  5.08214   1.000 48.05232  ? 238 TYR B CD1   1 
ATOM   3809 C  CD2   . TYR B 1  208 ? 6.93297   26.83080  2.74297   1.000 43.43756  ? 238 TYR B CD2   1 
ATOM   3810 C  CE1   . TYR B 1  208 ? 7.36292   25.81527  5.27260   1.000 59.89654  ? 238 TYR B CE1   1 
ATOM   3811 C  CE2   . TYR B 1  208 ? 7.82104   25.79076  2.92242   1.000 44.73721  ? 238 TYR B CE2   1 
ATOM   3812 C  CZ    . TYR B 1  208 ? 8.02951   25.27949  4.18823   1.000 55.21063  ? 238 TYR B CZ    1 
ATOM   3813 O  OH    . TYR B 1  208 ? 8.90658   24.23745  4.38269   1.000 62.98466  ? 238 TYR B OH    1 
ATOM   3814 N  N     . ILE B 1  209 ? 3.59250   25.83052  4.15501   1.000 46.11958  ? 239 ILE B N     1 
ATOM   3815 C  CA    . ILE B 1  209 ? 3.45584   24.70033  5.06883   1.000 46.07466  ? 239 ILE B CA    1 
ATOM   3816 C  C     . ILE B 1  209 ? 4.48568   23.66241  4.67023   1.000 41.66229  ? 239 ILE B C     1 
ATOM   3817 O  O     . ILE B 1  209 ? 4.75723   23.47366  3.48109   1.000 44.07879  ? 239 ILE B O     1 
ATOM   3818 C  CB    . ILE B 1  209 ? 2.04182   24.09334  5.04723   1.000 47.88992  ? 239 ILE B CB    1 
ATOM   3819 C  CG1   . ILE B 1  209 ? 1.87625   23.08611  6.19509   1.000 45.79421  ? 239 ILE B CG1   1 
ATOM   3820 C  CG2   . ILE B 1  209 ? 1.77131   23.39963  3.69119   1.000 42.97182  ? 239 ILE B CG2   1 
ATOM   3821 C  CD1   . ILE B 1  209 ? 0.45135   22.70006  6.46154   1.000 50.08472  ? 239 ILE B CD1   1 
ATOM   3822 N  N     . LYS B 1  210 ? 5.06305   22.98320  5.65887   1.000 47.12277  ? 240 LYS B N     1 
ATOM   3823 C  CA    . LYS B 1  210 ? 6.13294   22.03825  5.39027   1.000 43.80392  ? 240 LYS B CA    1 
ATOM   3824 C  C     . LYS B 1  210 ? 5.62573   20.71237  4.83119   1.000 49.65889  ? 240 LYS B C     1 
ATOM   3825 O  O     . LYS B 1  210 ? 6.44161   19.84243  4.52570   1.000 44.24973  ? 240 LYS B O     1 
ATOM   3826 C  CB    . LYS B 1  210 ? 6.94342   21.77398  6.66191   1.000 52.03190  ? 240 LYS B CB    1 
ATOM   3827 C  CG    . LYS B 1  210 ? 6.17282   21.01376  7.73904   1.000 51.45609  ? 240 LYS B CG    1 
ATOM   3828 C  CD    . LYS B 1  210 ? 6.98530   20.89549  9.02371   1.000 55.11749  ? 240 LYS B CD    1 
ATOM   3829 C  CE    . LYS B 1  210 ? 6.18271   20.20827  10.11887  1.000 64.70884  ? 240 LYS B CE    1 
ATOM   3830 N  NZ    . LYS B 1  210 ? 6.88120   20.24399  11.43562  1.000 65.39035  ? 240 LYS B NZ    1 
ATOM   3831 N  N     . LEU B 1  211 ? 4.31569   20.52840  4.72464   1.000 45.55632  ? 241 LEU B N     1 
ATOM   3832 C  CA    . LEU B 1  211 ? 3.73245   19.33153  4.12061   1.000 43.46975  ? 241 LEU B CA    1 
ATOM   3833 C  C     . LEU B 1  211 ? 3.41991   19.65083  2.65879   1.000 37.64698  ? 241 LEU B C     1 
ATOM   3834 O  O     . LEU B 1  211 ? 2.50281   20.42390  2.37630   1.000 35.82314  ? 241 LEU B O     1 
ATOM   3835 C  CB    . LEU B 1  211 ? 2.47774   18.90838  4.88299   1.000 42.08840  ? 241 LEU B CB    1 
ATOM   3836 C  CG    . LEU B 1  211 ? 2.75629   18.59107  6.36882   1.000 48.71024  ? 241 LEU B CG    1 
ATOM   3837 C  CD1   . LEU B 1  211 ? 1.47357   18.30392  7.11124   1.000 46.26348  ? 241 LEU B CD1   1 
ATOM   3838 C  CD2   . LEU B 1  211 ? 3.71333   17.43404  6.47522   1.000 36.32754  ? 241 LEU B CD2   1 
ATOM   3839 N  N     . GLU B 1  212 ? 4.16856   19.03902  1.73838   1.000 41.00397  ? 242 GLU B N     1 
ATOM   3840 C  CA    . GLU B 1  212 ? 4.17504   19.50931  0.35348   1.000 45.55117  ? 242 GLU B CA    1 
ATOM   3841 C  C     . GLU B 1  212 ? 2.81579   19.31546  -0.32405  1.000 41.86293  ? 242 GLU B C     1 
ATOM   3842 O  O     . GLU B 1  212 ? 2.35451   20.19162  -1.07570  1.000 44.27397  ? 242 GLU B O     1 
ATOM   3843 C  CB    . GLU B 1  212 ? 5.29874   18.82947  -0.43908  1.000 37.01871  ? 242 GLU B CB    1 
ATOM   3844 C  CG    . GLU B 1  212 ? 5.24070   17.29249  -0.53538  1.000 41.54001  ? 242 GLU B CG    1 
ATOM   3845 C  CD    . GLU B 1  212 ? 4.37126   16.79974  -1.69416  1.000 60.58575  ? 242 GLU B CD    1 
ATOM   3846 O  OE1   . GLU B 1  212 ? 4.23588   17.52195  -2.71296  1.000 58.83745  ? 242 GLU B OE1   1 
ATOM   3847 O  OE2   . GLU B 1  212 ? 3.80830   15.68271  -1.58418  1.000 64.75891  ? 242 GLU B OE2   1 
ATOM   3848 N  N     . ASP B 1  213 ? 2.14288   18.18541  -0.07103  1.000 40.72067  ? 243 ASP B N     1 
ATOM   3849 C  CA    . ASP B 1  213 ? 0.86962   17.95356  -0.74860  1.000 40.58721  ? 243 ASP B CA    1 
ATOM   3850 C  C     . ASP B 1  213 ? -0.19819  18.93146  -0.26400  1.000 36.28385  ? 243 ASP B C     1 
ATOM   3851 O  O     . ASP B 1  213 ? -0.98749  19.44863  -1.06560  1.000 40.34538  ? 243 ASP B O     1 
ATOM   3852 C  CB    . ASP B 1  213 ? 0.42367   16.48153  -0.60974  1.000 44.69274  ? 243 ASP B CB    1 
ATOM   3853 C  CG    . ASP B 1  213 ? 0.55020   15.92623  0.82509   1.000 54.76664  ? 243 ASP B CG    1 
ATOM   3854 O  OD1   . ASP B 1  213 ? 0.82357   16.68103  1.78515   1.000 41.84880  ? 243 ASP B OD1   1 
ATOM   3855 O  OD2   . ASP B 1  213 ? 0.36825   14.69220  0.98391   1.000 55.07904  ? 243 ASP B OD2   1 
ATOM   3856 N  N     . VAL B 1  214 ? -0.19671  19.25719  1.03107   1.000 37.48884  ? 244 VAL B N     1 
ATOM   3857 C  CA    . VAL B 1  214 ? -1.10552  20.28909  1.51662   1.000 39.34035  ? 244 VAL B CA    1 
ATOM   3858 C  C     . VAL B 1  214 ? -0.78175  21.63223  0.87678   1.000 42.12004  ? 244 VAL B C     1 
ATOM   3859 O  O     . VAL B 1  214 ? -1.68089  22.38731  0.49128   1.000 43.59256  ? 244 VAL B O     1 
ATOM   3860 C  CB    . VAL B 1  214 ? -1.06094  20.39577  3.05263   1.000 40.94578  ? 244 VAL B CB    1 
ATOM   3861 C  CG1   . VAL B 1  214 ? -2.02677  21.46869  3.50421   1.000 35.75396  ? 244 VAL B CG1   1 
ATOM   3862 C  CG2   . VAL B 1  214 ? -1.39070  19.06064  3.71647   1.000 43.32784  ? 244 VAL B CG2   1 
ATOM   3863 N  N     . PHE B 1  215 ? 0.50622   21.97024  0.78537   1.000 36.94458  ? 245 PHE B N     1 
ATOM   3864 C  CA    . PHE B 1  215 ? 0.86201   23.25936  0.20950   1.000 37.85055  ? 245 PHE B CA    1 
ATOM   3865 C  C     . PHE B 1  215 ? 0.35747   23.36666  -1.22529  1.000 40.49615  ? 245 PHE B C     1 
ATOM   3866 O  O     . PHE B 1  215 ? -0.23468  24.38074  -1.62085  1.000 41.48974  ? 245 PHE B O     1 
ATOM   3867 C  CB    . PHE B 1  215 ? 2.36902   23.46834  0.24498   1.000 39.83982  ? 245 PHE B CB    1 
ATOM   3868 C  CG    . PHE B 1  215 ? 2.77680   24.77547  -0.35790  1.000 40.58966  ? 245 PHE B CG    1 
ATOM   3869 C  CD1   . PHE B 1  215 ? 2.44904   25.96034  0.27447   1.000 46.70250  ? 245 PHE B CD1   1 
ATOM   3870 C  CD2   . PHE B 1  215 ? 3.42534   24.82072  -1.57813  1.000 43.55523  ? 245 PHE B CD2   1 
ATOM   3871 C  CE1   . PHE B 1  215 ? 2.80284   27.17845  -0.28441  1.000 50.08237  ? 245 PHE B CE1   1 
ATOM   3872 C  CE2   . PHE B 1  215 ? 3.77714   26.03183  -2.14401  1.000 49.19666  ? 245 PHE B CE2   1 
ATOM   3873 C  CZ    . PHE B 1  215 ? 3.46839   27.20870  -1.49265  1.000 49.48339  ? 245 PHE B CZ    1 
ATOM   3874 N  N     . VAL B 1  216 ? 0.60516   22.32982  -2.02359  1.000 38.14272  ? 246 VAL B N     1 
ATOM   3875 C  CA    . VAL B 1  216 ? 0.08365   22.33811  -3.38840  1.000 38.59806  ? 246 VAL B CA    1 
ATOM   3876 C  C     . VAL B 1  216 ? -1.42534  22.52511  -3.37379  1.000 38.55547  ? 246 VAL B C     1 
ATOM   3877 O  O     . VAL B 1  216 ? -1.97764  23.28428  -4.17743  1.000 39.20045  ? 246 VAL B O     1 
ATOM   3878 C  CB    . VAL B 1  216 ? 0.51837   21.06526  -4.12783  1.000 41.50571  ? 246 VAL B CB    1 
ATOM   3879 C  CG1   . VAL B 1  216 ? -0.24513  20.91954  -5.45957  1.000 38.66777  ? 246 VAL B CG1   1 
ATOM   3880 C  CG2   . VAL B 1  216 ? 2.02228   21.11030  -4.36638  1.000 40.52137  ? 246 VAL B CG2   1 
ATOM   3881 N  N     . GLY B 1  217 ? -2.11701  21.82193  -2.47268  1.000 37.85530  ? 247 GLY B N     1 
ATOM   3882 C  CA    . GLY B 1  217 ? -3.55396  22.02591  -2.34410  1.000 37.89141  ? 247 GLY B CA    1 
ATOM   3883 C  C     . GLY B 1  217 ? -3.92386  23.47986  -2.09566  1.000 42.85381  ? 247 GLY B C     1 
ATOM   3884 O  O     . GLY B 1  217 ? -4.90306  23.99298  -2.64618  1.000 39.02406  ? 247 GLY B O     1 
ATOM   3885 N  N     . LEU B 1  218 ? -3.15553  24.16168  -1.23680  1.000 44.20272  ? 248 LEU B N     1 
ATOM   3886 C  CA    . LEU B 1  218 ? -3.42243  25.58363  -0.98141  1.000 47.00071  ? 248 LEU B CA    1 
ATOM   3887 C  C     . LEU B 1  218 ? -3.26990  26.40889  -2.25429  1.000 41.63289  ? 248 LEU B C     1 
ATOM   3888 O  O     . LEU B 1  218 ? -4.09301  27.28895  -2.54380  1.000 41.53868  ? 248 LEU B O     1 
ATOM   3889 C  CB    . LEU B 1  218 ? -2.47902  26.12239  0.11035   1.000 44.78103  ? 248 LEU B CB    1 
ATOM   3890 C  CG    . LEU B 1  218 ? -2.67647  25.69709  1.57234   1.000 38.64374  ? 248 LEU B CG    1 
ATOM   3891 C  CD1   . LEU B 1  218 ? -1.48215  26.10691  2.43397   1.000 41.07510  ? 248 LEU B CD1   1 
ATOM   3892 C  CD2   . LEU B 1  218 ? -3.95326  26.28298  2.11794   1.000 39.67745  ? 248 LEU B CD2   1 
ATOM   3893 N  N     . CYS B 1  219 ? -2.21219  26.14104  -3.02274  1.000 47.80470  ? 249 CYS B N     1 
ATOM   3894 C  CA    . CYS B 1  219 ? -2.02867  26.84031  -4.29967  1.000 45.76314  ? 249 CYS B CA    1 
ATOM   3895 C  C     . CYS B 1  219 ? -3.19103  26.58151  -5.25729  1.000 42.75472  ? 249 CYS B C     1 
ATOM   3896 O  O     . CYS B 1  219 ? -3.74425  27.51264  -5.85488  1.000 47.36566  ? 249 CYS B O     1 
ATOM   3897 C  CB    . CYS B 1  219 ? -0.70091  26.41844  -4.93825  1.000 42.18616  ? 249 CYS B CB    1 
ATOM   3898 S  SG    . CYS B 1  219 ? 0.73745   26.84223  -3.97071  1.000 42.02727  ? 249 CYS B SG    1 
ATOM   3899 N  N     . LEU B 1  220 ? -3.56010  25.31055  -5.43041  1.000 40.68699  ? 250 LEU B N     1 
ATOM   3900 C  CA    . LEU B 1  220 ? -4.66744  24.96174  -6.32307  1.000 44.39790  ? 250 LEU B CA    1 
ATOM   3901 C  C     . LEU B 1  220 ? -5.95028  25.65866  -5.90644  1.000 50.97814  ? 250 LEU B C     1 
ATOM   3902 O  O     . LEU B 1  220 ? -6.71859  26.13484  -6.75406  1.000 48.95872  ? 250 LEU B O     1 
ATOM   3903 C  CB    . LEU B 1  220 ? -4.88845  23.44874  -6.32730  1.000 39.95183  ? 250 LEU B CB    1 
ATOM   3904 C  CG    . LEU B 1  220 ? -3.76066  22.59686  -6.88690  1.000 47.97270  ? 250 LEU B CG    1 
ATOM   3905 C  CD1   . LEU B 1  220 ? -4.10459  21.12281  -6.67608  1.000 41.17082  ? 250 LEU B CD1   1 
ATOM   3906 C  CD2   . LEU B 1  220 ? -3.53221  22.92716  -8.36292  1.000 42.67450  ? 250 LEU B CD2   1 
ATOM   3907 N  N     . GLU B 1  221 ? -6.21179  25.70439  -4.60134  1.000 42.15618  ? 251 GLU B N     1 
ATOM   3908 C  CA    . GLU B 1  221 ? -7.37560  26.42129  -4.09675  1.000 46.91799  ? 251 GLU B CA    1 
ATOM   3909 C  C     . GLU B 1  221 ? -7.30272  27.90536  -4.44047  1.000 50.74076  ? 251 GLU B C     1 
ATOM   3910 O  O     . GLU B 1  221 ? -8.29488  28.50346  -4.87197  1.000 49.63141  ? 251 GLU B O     1 
ATOM   3911 C  CB    . GLU B 1  221 ? -7.46603  26.20998  -2.58776  1.000 47.02153  ? 251 GLU B CB    1 
ATOM   3912 C  CG    . GLU B 1  221 ? -8.62678  26.87485  -1.91719  1.000 47.76706  ? 251 GLU B CG    1 
ATOM   3913 C  CD    . GLU B 1  221 ? -8.60422  26.61054  -0.43425  1.000 59.88660  ? 251 GLU B CD    1 
ATOM   3914 O  OE1   . GLU B 1  221 ? -7.71296  27.15939  0.24853   1.000 54.04009  ? 251 GLU B OE1   1 
ATOM   3915 O  OE2   . GLU B 1  221 ? -9.45705  25.82844  0.03991   1.000 63.57553  ? 251 GLU B OE2   1 
ATOM   3916 N  N     . ARG B 1  222 ? -6.13064  28.51532  -4.25378  1.000 49.43550  ? 252 ARG B N     1 
ATOM   3917 C  CA    . ARG B 1  222 ? -5.95878  29.91540  -4.64355  1.000 56.41047  ? 252 ARG B CA    1 
ATOM   3918 C  C     . ARG B 1  222 ? -6.25434  30.10671  -6.12940  1.000 47.86495  ? 252 ARG B C     1 
ATOM   3919 O  O     . ARG B 1  222 ? -6.85449  31.11880  -6.53097  1.000 52.27252  ? 252 ARG B O     1 
ATOM   3920 C  CB    . ARG B 1  222 ? -4.53865  30.38432  -4.29999  1.000 52.37297  ? 252 ARG B CB    1 
ATOM   3921 C  CG    . ARG B 1  222 ? -4.19083  31.79942  -4.79083  1.000 58.59755  ? 252 ARG B CG    1 
ATOM   3922 C  CD    . ARG B 1  222 ? -4.90752  32.86226  -3.97934  1.000 54.13220  ? 252 ARG B CD    1 
ATOM   3923 N  NE    . ARG B 1  222 ? -4.62499  32.72396  -2.55547  1.000 63.65892  ? 252 ARG B NE    1 
ATOM   3924 C  CZ    . ARG B 1  222 ? -3.53876  33.19683  -1.95678  1.000 68.91295  ? 252 ARG B CZ    1 
ATOM   3925 N  NH1   . ARG B 1  222 ? -2.61301  33.86596  -2.62799  1.000 56.97278  ? 252 ARG B NH1   1 
ATOM   3926 N  NH2   . ARG B 1  222 ? -3.37427  32.98056  -0.64789  1.000 61.77654  ? 252 ARG B NH2   1 
ATOM   3927 N  N     . LEU B 1  223 ? -5.86365  29.13988  -6.95675  1.000 53.60283  ? 253 LEU B N     1 
ATOM   3928 C  CA    . LEU B 1  223 ? -6.04420  29.22118  -8.40267  1.000 48.56324  ? 253 LEU B CA    1 
ATOM   3929 C  C     . LEU B 1  223 ? -7.44537  28.83629  -8.87122  1.000 51.86167  ? 253 LEU B C     1 
ATOM   3930 O  O     . LEU B 1  223 ? -7.73782  28.97254  -10.06508 1.000 55.32080  ? 253 LEU B O     1 
ATOM   3931 C  CB    . LEU B 1  223 ? -5.00646  28.34332  -9.09524  1.000 49.43749  ? 253 LEU B CB    1 
ATOM   3932 C  CG    . LEU B 1  223 ? -3.56839  28.81428  -8.91568  1.000 45.97205  ? 253 LEU B CG    1 
ATOM   3933 C  CD1   . LEU B 1  223 ? -2.60056  27.73236  -9.35727  1.000 43.89651  ? 253 LEU B CD1   1 
ATOM   3934 C  CD2   . LEU B 1  223 ? -3.32768  30.10344  -9.70450  1.000 45.37725  ? 253 LEU B CD2   1 
ATOM   3935 N  N     . ASN B 1  224 ? -8.32804  28.39811  -7.97898  1.000 48.20077  ? 254 ASN B N     1 
ATOM   3936 C  CA    . ASN B 1  224 ? -9.65619  27.91719  -8.35458  1.000 51.41469  ? 254 ASN B CA    1 
ATOM   3937 C  C     . ASN B 1  224 ? -9.58352  26.65237  -9.21887  1.000 51.14947  ? 254 ASN B C     1 
ATOM   3938 O  O     . ASN B 1  224 ? -10.52979 26.35053  -9.95858  1.000 60.89558  ? 254 ASN B O     1 
ATOM   3939 C  CB    . ASN B 1  224 ? -10.46046 29.00235  -9.09006  1.000 44.41837  ? 254 ASN B CB    1 
ATOM   3940 C  CG    . ASN B 1  224 ? -10.58315 30.29718  -8.28874  1.000 60.58614  ? 254 ASN B CG    1 
ATOM   3941 O  OD1   . ASN B 1  224 ? -10.86370 30.27693  -7.08964  1.000 81.55972  ? 254 ASN B OD1   1 
ATOM   3942 N  ND2   . ASN B 1  224 ? -10.37140 31.43032  -8.95858  1.000 63.22569  ? 254 ASN B ND2   1 
ATOM   3943 N  N     . ILE B 1  225 ? -8.48349  25.90835  -9.14844  1.000 52.45147  ? 255 ILE B N     1 
ATOM   3944 C  CA    . ILE B 1  225 ? -8.35477  24.63850  -9.86275  1.000 45.47117  ? 255 ILE B CA    1 
ATOM   3945 C  C     . ILE B 1  225 ? -8.95645  23.54232  -8.99276  1.000 45.88618  ? 255 ILE B C     1 
ATOM   3946 O  O     . ILE B 1  225 ? -8.41305  23.20510  -7.93903  1.000 52.36065  ? 255 ILE B O     1 
ATOM   3947 C  CB    . ILE B 1  225 ? -6.89490  24.32656  -10.21137 1.000 41.77940  ? 255 ILE B CB    1 
ATOM   3948 C  CG1   . ILE B 1  225 ? -6.36828  25.32977  -11.23636 1.000 49.25556  ? 255 ILE B CG1   1 
ATOM   3949 C  CG2   . ILE B 1  225 ? -6.75909  22.89367  -10.70672 1.000 41.22464  ? 255 ILE B CG2   1 
ATOM   3950 C  CD1   . ILE B 1  225 ? -4.87336  25.27481  -11.44993 1.000 51.97555  ? 255 ILE B CD1   1 
ATOM   3951 N  N     . ARG B 1  226 ? -10.08361 22.98441  -9.42245  1.000 51.08767  ? 256 ARG B N     1 
ATOM   3952 C  CA    . ARG B 1  226 ? -10.74432 21.95425  -8.63842  1.000 54.69616  ? 256 ARG B CA    1 
ATOM   3953 C  C     . ARG B 1  226 ? -10.11043 20.59931  -8.91794  1.000 48.27142  ? 256 ARG B C     1 
ATOM   3954 O  O     . ARG B 1  226 ? -9.74086  20.29854  -10.05214 1.000 51.64445  ? 256 ARG B O     1 
ATOM   3955 C  CB    . ARG B 1  226 ? -12.24144 21.91433  -8.95586  1.000 58.29270  ? 256 ARG B CB    1 
ATOM   3956 C  CG    . ARG B 1  226 ? -12.97132 23.22027  -8.66232  1.000 80.09157  ? 256 ARG B CG    1 
ATOM   3957 C  CD    . ARG B 1  226 ? -12.97676 23.54296  -7.16925  1.000 91.19556  ? 256 ARG B CD    1 
ATOM   3958 N  NE    . ARG B 1  226 ? -13.70965 24.77590  -6.88272  1.000 106.92141 ? 256 ARG B NE    1 
ATOM   3959 C  CZ    . ARG B 1  226 ? -14.09819 25.15765  -5.67549  1.000 110.24549 ? 256 ARG B CZ    1 
ATOM   3960 N  NH1   . ARG B 1  226 ? -13.85179 24.41843  -4.60074  1.000 97.51083  ? 256 ARG B NH1   1 
ATOM   3961 N  NH2   . ARG B 1  226 ? -14.76214 26.30263  -5.53700  1.000 100.00820 ? 256 ARG B NH2   1 
ATOM   3962 N  N     . LEU B 1  227 ? -9.96704  19.79509  -7.86216  1.000 39.28016  ? 257 LEU B N     1 
ATOM   3963 C  CA    . LEU B 1  227 ? -9.46911  18.43312  -8.02463  1.000 40.89629  ? 257 LEU B CA    1 
ATOM   3964 C  C     . LEU B 1  227 ? -10.48939 17.57428  -8.75342  1.000 49.47360  ? 257 LEU B C     1 
ATOM   3965 O  O     . LEU B 1  227 ? -11.69630 17.70324  -8.52794  1.000 51.94254  ? 257 LEU B O     1 
ATOM   3966 C  CB    . LEU B 1  227 ? -9.16360  17.80883  -6.65887  1.000 39.73605  ? 257 LEU B CB    1 
ATOM   3967 C  CG    . LEU B 1  227 ? -8.23524  18.57463  -5.71406  1.000 48.06798  ? 257 LEU B CG    1 
ATOM   3968 C  CD1   . LEU B 1  227 ? -7.95477  17.74937  -4.44234  1.000 42.47222  ? 257 LEU B CD1   1 
ATOM   3969 C  CD2   . LEU B 1  227 ? -6.94950  18.95677  -6.42146  1.000 39.78796  ? 257 LEU B CD2   1 
ATOM   3970 N  N     . GLU B 1  228 ? -10.00471 16.67545  -9.61479  1.000 48.17182  ? 258 GLU B N     1 
ATOM   3971 C  CA    . GLU B 1  228 ? -10.85797 15.70760  -10.29367 1.000 49.33972  ? 258 GLU B CA    1 
ATOM   3972 C  C     . GLU B 1  228 ? -10.30492 14.29956  -10.13917 1.000 48.90665  ? 258 GLU B C     1 
ATOM   3973 O  O     . GLU B 1  228 ? -9.08893  14.10156  -10.16567 1.000 46.74836  ? 258 GLU B O     1 
ATOM   3974 C  CB    . GLU B 1  228 ? -10.99453 16.00491  -11.79156 1.000 50.14259  ? 258 GLU B CB    1 
ATOM   3975 C  CG    . GLU B 1  228 ? -11.54365 17.36298  -12.12707 1.000 58.92907  ? 258 GLU B CG    1 
ATOM   3976 C  CD    . GLU B 1  228 ? -11.51521 17.61629  -13.61803 1.000 65.04851  ? 258 GLU B CD    1 
ATOM   3977 O  OE1   . GLU B 1  228 ? -11.95050 16.71745  -14.37205 1.000 65.20482  ? 258 GLU B OE1   1 
ATOM   3978 O  OE2   . GLU B 1  228 ? -11.02836 18.69338  -14.03599 1.000 57.29293  ? 258 GLU B OE2   1 
ATOM   3979 N  N     . GLU B 1  229 ? -11.20587 13.32254  -10.00004 1.000 53.03110  ? 259 GLU B N     1 
ATOM   3980 C  CA    . GLU B 1  229 ? -10.82992 11.91456  -10.09647 1.000 58.16040  ? 259 GLU B CA    1 
ATOM   3981 C  C     . GLU B 1  229 ? -10.38645 11.56985  -11.51771 1.000 55.26769  ? 259 GLU B C     1 
ATOM   3982 O  O     . GLU B 1  229 ? -10.94582 12.06806  -12.50040 1.000 38.80016  ? 259 GLU B O     1 
ATOM   3983 C  CB    . GLU B 1  229 ? -12.00177 11.01848  -9.69122  1.000 49.28621  ? 259 GLU B CB    1 
ATOM   3984 C  CG    . GLU B 1  229 ? -12.56925 11.28519  -8.30395  1.000 71.49450  ? 259 GLU B CG    1 
ATOM   3985 C  CD    . GLU B 1  229 ? -11.73683 10.65896  -7.19039  1.000 79.56747  ? 259 GLU B CD    1 
ATOM   3986 O  OE1   . GLU B 1  229 ? -10.79095 9.90102   -7.49991  1.000 78.44187  ? 259 GLU B OE1   1 
ATOM   3987 O  OE2   . GLU B 1  229 ? -12.02539 10.93771  -6.00523  1.000 86.18739  ? 259 GLU B OE2   1 
ATOM   3988 N  N     . LEU B 1  230 ? -9.36850  10.71087  -11.62627 1.000 48.78457  ? 260 LEU B N     1 
ATOM   3989 C  CA    . LEU B 1  230 ? -8.84799  10.33514  -12.93854 1.000 47.76237  ? 260 LEU B CA    1 
ATOM   3990 C  C     . LEU B 1  230 ? -9.81627  9.41330   -13.67337 1.000 46.05718  ? 260 LEU B C     1 
ATOM   3991 O  O     . LEU B 1  230 ? -9.88273  9.44656   -14.90934 1.000 49.38828  ? 260 LEU B O     1 
ATOM   3992 C  CB    . LEU B 1  230 ? -7.48694  9.64910   -12.80320 1.000 47.07646  ? 260 LEU B CB    1 
ATOM   3993 C  CG    . LEU B 1  230 ? -6.87643  9.12537   -14.10454 1.000 38.86436  ? 260 LEU B CG    1 
ATOM   3994 C  CD1   . LEU B 1  230 ? -6.67279  10.27257  -15.06737 1.000 40.36001  ? 260 LEU B CD1   1 
ATOM   3995 C  CD2   . LEU B 1  230 ? -5.55735  8.41932   -13.86918 1.000 38.57413  ? 260 LEU B CD2   1 
ATOM   3996 N  N     . HIS B 1  231 ? -10.59100 8.61915   -12.94025 1.000 45.78210  ? 261 HIS B N     1 
ATOM   3997 C  CA    . HIS B 1  231 ? -11.36823 7.54528   -13.53718 1.000 44.35700  ? 261 HIS B CA    1 
ATOM   3998 C  C     . HIS B 1  231 ? -12.53889 7.22409   -12.61781 1.000 56.60819  ? 261 HIS B C     1 
ATOM   3999 O  O     . HIS B 1  231 ? -12.55945 7.61585   -11.44972 1.000 63.27141  ? 261 HIS B O     1 
ATOM   4000 C  CB    . HIS B 1  231 ? -10.48033 6.32232   -13.78377 1.000 49.38880  ? 261 HIS B CB    1 
ATOM   4001 C  CG    . HIS B 1  231 ? -11.18058 5.18247   -14.44674 1.000 59.99941  ? 261 HIS B CG    1 
ATOM   4002 N  ND1   . HIS B 1  231 ? -11.36135 3.96534   -13.82593 1.000 58.19626  ? 261 HIS B ND1   1 
ATOM   4003 C  CD2   . HIS B 1  231 ? -11.73304 5.06972   -15.67456 1.000 58.86529  ? 261 HIS B CD2   1 
ATOM   4004 C  CE1   . HIS B 1  231 ? -12.00567 3.15251   -14.64585 1.000 55.58991  ? 261 HIS B CE1   1 
ATOM   4005 N  NE2   . HIS B 1  231 ? -12.24509 3.79975   -15.77263 1.000 55.23857  ? 261 HIS B NE2   1 
ATOM   4006 N  N     . SER B 1  232 ? -13.52610 6.51121   -13.17059 1.000 53.96087  ? 262 SER B N     1 
ATOM   4007 C  CA    . SER B 1  232 ? -14.69781 6.10606   -12.39923 1.000 61.02648  ? 262 SER B CA    1 
ATOM   4008 C  C     . SER B 1  232 ? -14.35340 5.10983   -11.30257 1.000 66.15669  ? 262 SER B C     1 
ATOM   4009 O  O     . SER B 1  232 ? -15.13605 4.94463   -10.36331 1.000 69.69333  ? 262 SER B O     1 
ATOM   4010 C  CB    . SER B 1  232 ? -15.75216 5.50125   -13.32696 1.000 69.41839  ? 262 SER B CB    1 
ATOM   4011 O  OG    . SER B 1  232 ? -15.21644 4.40841   -14.06339 1.000 71.78785  ? 262 SER B OG    1 
ATOM   4012 N  N     . GLN B 1  233 ? -13.21444 4.44884   -11.40113 1.000 59.38618  ? 263 GLN B N     1 
ATOM   4013 C  CA    . GLN B 1  233 ? -12.73906 3.55062   -10.37050 1.000 58.22664  ? 263 GLN B CA    1 
ATOM   4014 C  C     . GLN B 1  233 ? -11.46882 4.10449   -9.73286  1.000 52.53373  ? 263 GLN B C     1 
ATOM   4015 O  O     . GLN B 1  233 ? -10.73105 4.86961   -10.36398 1.000 51.99015  ? 263 GLN B O     1 
ATOM   4016 C  CB    . GLN B 1  233 ? -12.45328 2.15274   -10.93189 1.000 64.55426  ? 263 GLN B CB    1 
ATOM   4017 C  CG    . GLN B 1  233 ? -13.67350 1.45987   -11.50658 1.000 59.82433  ? 263 GLN B CG    1 
ATOM   4018 C  CD    . GLN B 1  233 ? -14.77511 1.29766   -10.47820 1.000 84.87610  ? 263 GLN B CD    1 
ATOM   4019 O  OE1   . GLN B 1  233 ? -14.60874 0.61245   -9.46741  1.000 94.86675  ? 263 GLN B OE1   1 
ATOM   4020 N  NE2   . GLN B 1  233 ? -15.91520 1.92771   -10.72864 1.000 80.85269  ? 263 GLN B NE2   1 
ATOM   4021 N  N     . PRO B 1  234 ? -11.18635 3.73822   -8.48504  1.000 55.45029  ? 264 PRO B N     1 
ATOM   4022 C  CA    . PRO B 1  234 ? -9.94911  4.20109   -7.85541  1.000 51.54260  ? 264 PRO B CA    1 
ATOM   4023 C  C     . PRO B 1  234 ? -8.72439  3.66723   -8.59098  1.000 49.53997  ? 264 PRO B C     1 
ATOM   4024 O  O     . PRO B 1  234 ? -8.66354  2.49831   -8.97524  1.000 45.22244  ? 264 PRO B O     1 
ATOM   4025 C  CB    . PRO B 1  234 ? -10.04758 3.64179   -6.43149  1.000 52.02394  ? 264 PRO B CB    1 
ATOM   4026 C  CG    . PRO B 1  234 ? -10.97263 2.46782   -6.54938  1.000 59.82534  ? 264 PRO B CG    1 
ATOM   4027 C  CD    . PRO B 1  234 ? -11.97103 2.85305   -7.60793  1.000 45.74803  ? 264 PRO B CD    1 
ATOM   4028 N  N     . THR B 1  235 ? -7.75146  4.54327   -8.79216  1.000 44.93525  ? 265 THR B N     1 
ATOM   4029 C  CA    . THR B 1  235 ? -6.52572  4.16641   -9.46370  1.000 43.84158  ? 265 THR B CA    1 
ATOM   4030 C  C     . THR B 1  235 ? -5.25743  4.54024   -8.70410  1.000 41.83711  ? 265 THR B C     1 
ATOM   4031 O  O     . THR B 1  235 ? -4.18258  4.08532   -9.10060  1.000 42.46873  ? 265 THR B O     1 
ATOM   4032 C  CB    . THR B 1  235 ? -6.48024  4.78570   -10.87259 1.000 47.46297  ? 265 THR B CB    1 
ATOM   4033 O  OG1   . THR B 1  235 ? -6.66120  6.20468   -10.78722 1.000 38.01358  ? 265 THR B OG1   1 
ATOM   4034 C  CG2   . THR B 1  235 ? -7.60257  4.19989   -11.75029 1.000 40.86288  ? 265 THR B CG2   1 
ATOM   4035 N  N     . PHE B 1  236 ? -5.33903  5.36402   -7.65490  1.000 43.47139  ? 266 PHE B N     1 
ATOM   4036 C  CA    . PHE B 1  236 ? -4.19172  5.68784   -6.81526  1.000 44.34491  ? 266 PHE B CA    1 
ATOM   4037 C  C     . PHE B 1  236 ? -4.39920  5.05756   -5.43831  1.000 41.10345  ? 266 PHE B C     1 
ATOM   4038 O  O     . PHE B 1  236 ? -5.49199  5.15444   -4.86688  1.000 41.05372  ? 266 PHE B O     1 
ATOM   4039 C  CB    . PHE B 1  236 ? -4.01666  7.20581   -6.68401  1.000 35.66697  ? 266 PHE B CB    1 
ATOM   4040 C  CG    . PHE B 1  236 ? -3.71114  7.90508   -7.98498  1.000 37.23802  ? 266 PHE B CG    1 
ATOM   4041 C  CD1   . PHE B 1  236 ? -4.72748  8.22127   -8.87553  1.000 40.30016  ? 266 PHE B CD1   1 
ATOM   4042 C  CD2   . PHE B 1  236 ? -2.40826  8.26714   -8.30639  1.000 42.36485  ? 266 PHE B CD2   1 
ATOM   4043 C  CE1   . PHE B 1  236 ? -4.44792  8.87052   -10.07050 1.000 37.05426  ? 266 PHE B CE1   1 
ATOM   4044 C  CE2   . PHE B 1  236 ? -2.12471  8.92539   -9.49636  1.000 36.88714  ? 266 PHE B CE2   1 
ATOM   4045 C  CZ    . PHE B 1  236 ? -3.15103  9.22358   -10.37791 1.000 37.22903  ? 266 PHE B CZ    1 
ATOM   4046 N  N     . PHE B 1  237 ? -3.35500  4.42844   -4.89783  1.000 38.10594  ? 267 PHE B N     1 
ATOM   4047 C  CA    . PHE B 1  237 ? -3.47354  3.65418   -3.65795  1.000 43.69018  ? 267 PHE B CA    1 
ATOM   4048 C  C     . PHE B 1  237 ? -2.33218  3.96798   -2.70131  1.000 42.03006  ? 267 PHE B C     1 
ATOM   4049 O  O     . PHE B 1  237 ? -1.36214  3.19895   -2.57784  1.000 41.01548  ? 267 PHE B O     1 
ATOM   4050 C  CB    . PHE B 1  237 ? -3.55966  2.15725   -3.96423  1.000 38.40386  ? 267 PHE B CB    1 
ATOM   4051 C  CG    . PHE B 1  237 ? -4.77497  1.79442   -4.76485  1.000 40.33003  ? 267 PHE B CG    1 
ATOM   4052 C  CD1   . PHE B 1  237 ? -4.73649  1.80871   -6.15186  1.000 48.56660  ? 267 PHE B CD1   1 
ATOM   4053 C  CD2   . PHE B 1  237 ? -5.96773  1.48029   -4.13547  1.000 41.16737  ? 267 PHE B CD2   1 
ATOM   4054 C  CE1   . PHE B 1  237 ? -5.86577  1.48987   -6.89350  1.000 42.22589  ? 267 PHE B CE1   1 
ATOM   4055 C  CE2   . PHE B 1  237 ? -7.09601  1.15945   -4.86911  1.000 39.07744  ? 267 PHE B CE2   1 
ATOM   4056 C  CZ    . PHE B 1  237 ? -7.05053  1.17274   -6.25313  1.000 36.19651  ? 267 PHE B CZ    1 
ATOM   4057 N  N     . PRO B 1  238 ? -2.42591  5.09883   -1.99404  1.000 40.57145  ? 268 PRO B N     1 
ATOM   4058 C  CA    . PRO B 1  238 ? -1.40453  5.42462   -0.98236  1.000 40.12662  ? 268 PRO B CA    1 
ATOM   4059 C  C     . PRO B 1  238 ? -1.31911  4.39438   0.13840   1.000 40.08069  ? 268 PRO B C     1 
ATOM   4060 O  O     . PRO B 1  238 ? -0.27187  4.29724   0.78698   1.000 40.55121  ? 268 PRO B O     1 
ATOM   4061 C  CB    . PRO B 1  238 ? -1.86332  6.79350   -0.43890  1.000 41.07570  ? 268 PRO B CB    1 
ATOM   4062 C  CG    . PRO B 1  238 ? -2.86270  7.32773   -1.47742  1.000 45.91238  ? 268 PRO B CG    1 
ATOM   4063 C  CD    . PRO B 1  238 ? -3.49393  6.11485   -2.07443  1.000 39.09796  ? 268 PRO B CD    1 
ATOM   4064 N  N     . GLY B 1  239 ? -2.40202  3.66133   0.40465   1.000 37.50065  ? 269 GLY B N     1 
ATOM   4065 C  CA    . GLY B 1  239 ? -2.39863  2.63912   1.43444   1.000 37.30598  ? 269 GLY B CA    1 
ATOM   4066 C  C     . GLY B 1  239 ? -1.83580  1.30420   1.01095   1.000 41.75860  ? 269 GLY B C     1 
ATOM   4067 O  O     . GLY B 1  239 ? -1.71249  0.41103   1.86071   1.000 47.21391  ? 269 GLY B O     1 
ATOM   4068 N  N     . GLY B 1  240 ? -1.47928  1.14347   -0.26322  1.000 44.20535  ? 270 GLY B N     1 
ATOM   4069 C  CA    . GLY B 1  240 ? -0.92347  -0.09843  -0.76269  1.000 38.76288  ? 270 GLY B CA    1 
ATOM   4070 C  C     . GLY B 1  240 ? -1.99664  -1.07534  -1.20749  1.000 41.25491  ? 270 GLY B C     1 
ATOM   4071 O  O     . GLY B 1  240 ? -3.19857  -0.87037  -1.01900  1.000 45.31919  ? 270 GLY B O     1 
ATOM   4072 N  N     . LEU B 1  241 ? -1.54088  -2.18221  -1.80989  1.000 42.98776  ? 271 LEU B N     1 
ATOM   4073 C  CA    . LEU B 1  241 ? -2.46411  -3.13908  -2.40974  1.000 44.47831  ? 271 LEU B CA    1 
ATOM   4074 C  C     . LEU B 1  241 ? -1.90409  -4.55010  -2.35325  1.000 45.19526  ? 271 LEU B C     1 
ATOM   4075 O  O     . LEU B 1  241 ? -0.69113  -4.76008  -2.44675  1.000 50.82318  ? 271 LEU B O     1 
ATOM   4076 C  CB    . LEU B 1  241 ? -2.75566  -2.83378  -3.88057  1.000 42.38110  ? 271 LEU B CB    1 
ATOM   4077 C  CG    . LEU B 1  241 ? -3.73981  -1.76568  -4.29798  1.000 49.63671  ? 271 LEU B CG    1 
ATOM   4078 C  CD1   . LEU B 1  241 ? -3.72138  -1.73337  -5.81898  1.000 50.07571  ? 271 LEU B CD1   1 
ATOM   4079 C  CD2   . LEU B 1  241 ? -5.12960  -2.06779  -3.75252  1.000 41.29531  ? 271 LEU B CD2   1 
ATOM   4080 N  N     . ARG B 1  242 ? -2.82005  -5.51112  -2.23810  1.000 38.94336  ? 272 ARG B N     1 
ATOM   4081 C  CA    . ARG B 1  242 ? -2.50113  -6.91908  -2.43452  1.000 38.66064  ? 272 ARG B CA    1 
ATOM   4082 C  C     . ARG B 1  242 ? -2.20469  -7.15177  -3.91068  1.000 39.32738  ? 272 ARG B C     1 
ATOM   4083 O  O     . ARG B 1  242 ? -3.02901  -6.82759  -4.77230  1.000 46.84745  ? 272 ARG B O     1 
ATOM   4084 C  CB    . ARG B 1  242 ? -3.67596  -7.77617  -1.96625  1.000 42.53418  ? 272 ARG B CB    1 
ATOM   4085 C  CG    . ARG B 1  242 ? -3.53106  -9.27412  -2.21062  1.000 47.02856  ? 272 ARG B CG    1 
ATOM   4086 C  CD    . ARG B 1  242 ? -4.86196  -9.96117  -1.92726  1.000 43.72543  ? 272 ARG B CD    1 
ATOM   4087 N  NE    . ARG B 1  242 ? -4.67672  -11.24831 -1.27260  1.000 59.65616  ? 272 ARG B NE    1 
ATOM   4088 C  CZ    . ARG B 1  242 ? -5.66158  -12.04838 -0.89540  1.000 55.45999  ? 272 ARG B CZ    1 
ATOM   4089 N  NH1   . ARG B 1  242 ? -6.92865  -11.72334 -1.08885  1.000 60.41796  ? 272 ARG B NH1   1 
ATOM   4090 N  NH2   . ARG B 1  242 ? -5.36937  -13.20650 -0.31375  1.000 56.71598  ? 272 ARG B NH2   1 
ATOM   4091 N  N     . PHE B 1  243 ? -1.03981  -7.69371  -4.21823  1.000 41.81269  ? 273 PHE B N     1 
ATOM   4092 C  CA    . PHE B 1  243 ? -0.61833  -7.75443  -5.60940  1.000 41.07365  ? 273 PHE B CA    1 
ATOM   4093 C  C     . PHE B 1  243 ? -1.33562  -8.84926  -6.38035  1.000 46.81423  ? 273 PHE B C     1 
ATOM   4094 O  O     . PHE B 1  243 ? -1.50744  -9.96736  -5.88852  1.000 48.06156  ? 273 PHE B O     1 
ATOM   4095 C  CB    . PHE B 1  243 ? 0.88463   -7.97541  -5.73101  1.000 45.15375  ? 273 PHE B CB    1 
ATOM   4096 C  CG    . PHE B 1  243 ? 1.31909   -8.18312  -7.14321  1.000 45.90902  ? 273 PHE B CG    1 
ATOM   4097 C  CD1   . PHE B 1  243 ? 1.52279   -7.10794  -7.97707  1.000 42.04076  ? 273 PHE B CD1   1 
ATOM   4098 C  CD2   . PHE B 1  243 ? 1.48190   -9.46001  -7.64754  1.000 46.77172  ? 273 PHE B CD2   1 
ATOM   4099 C  CE1   . PHE B 1  243 ? 1.90629   -7.29067  -9.28625  1.000 39.66933  ? 273 PHE B CE1   1 
ATOM   4100 C  CE2   . PHE B 1  243 ? 1.86440   -9.65674  -8.96272  1.000 50.41213  ? 273 PHE B CE2   1 
ATOM   4101 C  CZ    . PHE B 1  243 ? 2.07710   -8.56757  -9.78258  1.000 51.96364  ? 273 PHE B CZ    1 
ATOM   4102 N  N     . SER B 1  244 ? -1.75108  -8.51001  -7.60213  1.000 43.06582  ? 274 SER B N     1 
ATOM   4103 C  CA    . SER B 1  244 ? -2.05747  -9.49879  -8.62422  1.000 45.97753  ? 274 SER B CA    1 
ATOM   4104 C  C     . SER B 1  244 ? -1.80098  -8.86551  -9.98518  1.000 49.42585  ? 274 SER B C     1 
ATOM   4105 O  O     . SER B 1  244 ? -1.92803  -7.64747  -10.15488 1.000 51.71206  ? 274 SER B O     1 
ATOM   4106 C  CB    . SER B 1  244 ? -3.49443  -10.00681 -8.52079  1.000 42.27865  ? 274 SER B CB    1 
ATOM   4107 O  OG    . SER B 1  244 ? -4.41759  -9.03371  -8.96124  1.000 45.52435  ? 274 SER B OG    1 
ATOM   4108 N  N     . VAL B 1  245 ? -1.41534  -9.70331  -10.94750 1.000 45.61445  ? 275 VAL B N     1 
ATOM   4109 C  CA    . VAL B 1  245 ? -1.16885  -9.21203  -12.30249 1.000 48.28854  ? 275 VAL B CA    1 
ATOM   4110 C  C     . VAL B 1  245 ? -2.40104  -8.48391  -12.83188 1.000 45.44958  ? 275 VAL B C     1 
ATOM   4111 O  O     . VAL B 1  245 ? -2.31224  -7.36880  -13.36868 1.000 52.22516  ? 275 VAL B O     1 
ATOM   4112 C  CB    . VAL B 1  245 ? -0.76219  -10.38584 -13.21589 1.000 50.82295  ? 275 VAL B CB    1 
ATOM   4113 C  CG1   . VAL B 1  245 ? -1.01274  -10.04554 -14.67373 1.000 61.66886  ? 275 VAL B CG1   1 
ATOM   4114 C  CG2   . VAL B 1  245 ? 0.68989   -10.73790 -12.97951 1.000 49.52946  ? 275 VAL B CG2   1 
ATOM   4115 N  N     . CYS B 1  246 ? -3.57398  -9.09394  -12.66057 1.000 48.77997  ? 276 CYS B N     1 
ATOM   4116 C  CA    . CYS B 1  246 ? -4.78420  -8.52782  -13.24099 1.000 54.89736  ? 276 CYS B CA    1 
ATOM   4117 C  C     . CYS B 1  246 ? -5.16194  -7.21396  -12.56558 1.000 53.41570  ? 276 CYS B C     1 
ATOM   4118 O  O     . CYS B 1  246 ? -5.60918  -6.27481  -13.23722 1.000 53.12302  ? 276 CYS B O     1 
ATOM   4119 C  CB    . CYS B 1  246 ? -5.92117  -9.54083  -13.15678 1.000 62.76519  ? 276 CYS B CB    1 
ATOM   4120 S  SG    . CYS B 1  246 ? -5.67560  -10.95160 -14.27616 1.000 93.76984  ? 276 CYS B SG    1 
ATOM   4121 N  N     . LEU B 1  247 ? -4.97644  -7.12223  -11.24963 1.000 52.82064  ? 277 LEU B N     1 
ATOM   4122 C  CA    . LEU B 1  247 ? -5.25318  -5.86237  -10.56726 1.000 44.52047  ? 277 LEU B CA    1 
ATOM   4123 C  C     . LEU B 1  247 ? -4.27033  -4.78029  -10.99541 1.000 47.69060  ? 277 LEU B C     1 
ATOM   4124 O  O     . LEU B 1  247 ? -4.67145  -3.65122  -11.31202 1.000 41.74171  ? 277 LEU B O     1 
ATOM   4125 C  CB    . LEU B 1  247 ? -5.21161  -6.06169  -9.05432  1.000 47.28929  ? 277 LEU B CB    1 
ATOM   4126 C  CG    . LEU B 1  247 ? -5.40330  -4.78986  -8.23298  1.000 44.51704  ? 277 LEU B CG    1 
ATOM   4127 C  CD1   . LEU B 1  247 ? -6.76241  -4.15379  -8.53734  1.000 53.05964  ? 277 LEU B CD1   1 
ATOM   4128 C  CD2   . LEU B 1  247 ? -5.25474  -5.09117  -6.74710  1.000 39.05866  ? 277 LEU B CD2   1 
ATOM   4129 N  N     . PHE B 1  248 ? -2.97634  -5.09729  -11.00996 1.000 40.55452  ? 278 PHE B N     1 
ATOM   4130 C  CA    . PHE B 1  248 ? -1.99244  -4.06324  -11.29711 1.000 39.18534  ? 278 PHE B CA    1 
ATOM   4131 C  C     . PHE B 1  248 ? -1.99299  -3.64993  -12.75803 1.000 41.09762  ? 278 PHE B C     1 
ATOM   4132 O  O     . PHE B 1  248 ? -1.38311  -2.61987  -13.08804 1.000 50.58416  ? 278 PHE B O     1 
ATOM   4133 C  CB    . PHE B 1  248 ? -0.59428  -4.50933  -10.86373 1.000 41.79145  ? 278 PHE B CB    1 
ATOM   4134 C  CG    . PHE B 1  248 ? -0.28374  -4.20364  -9.40978  1.000 38.45394  ? 278 PHE B CG    1 
ATOM   4135 C  CD1   . PHE B 1  248 ? -1.22237  -4.46484  -8.42449  1.000 38.35820  ? 278 PHE B CD1   1 
ATOM   4136 C  CD2   . PHE B 1  248 ? 0.92940   -3.65772  -9.04512  1.000 38.21559  ? 278 PHE B CD2   1 
ATOM   4137 C  CE1   . PHE B 1  248 ? -0.94987  -4.18412  -7.09553  1.000 46.73932  ? 278 PHE B CE1   1 
ATOM   4138 C  CE2   . PHE B 1  248 ? 1.21090   -3.37600  -7.71417  1.000 40.38514  ? 278 PHE B CE2   1 
ATOM   4139 C  CZ    . PHE B 1  248 ? 0.26727   -3.64819  -6.74187  1.000 41.84318  ? 278 PHE B CZ    1 
ATOM   4140 N  N     . ARG B 1  249 ? -2.65132  -4.40775  -13.63694 1.000 46.00431  ? 279 ARG B N     1 
ATOM   4141 C  CA    . ARG B 1  249 ? -2.83483  -3.90446  -14.99676 1.000 41.87969  ? 279 ARG B CA    1 
ATOM   4142 C  C     . ARG B 1  249 ? -3.82485  -2.74444  -15.06815 1.000 44.92435  ? 279 ARG B C     1 
ATOM   4143 O  O     . ARG B 1  249 ? -3.79921  -1.98424  -16.03800 1.000 46.21534  ? 279 ARG B O     1 
ATOM   4144 C  CB    . ARG B 1  249 ? -3.31418  -5.02327  -15.91782 1.000 41.59470  ? 279 ARG B CB    1 
ATOM   4145 C  CG    . ARG B 1  249 ? -2.24634  -6.03219  -16.32743 1.000 49.52018  ? 279 ARG B CG    1 
ATOM   4146 C  CD    . ARG B 1  249 ? -2.89168  -7.07000  -17.22040 1.000 50.81243  ? 279 ARG B CD    1 
ATOM   4147 N  NE    . ARG B 1  249 ? -1.97286  -8.10591  -17.67696 1.000 71.37048  ? 279 ARG B NE    1 
ATOM   4148 C  CZ    . ARG B 1  249 ? -2.27621  -9.00571  -18.60704 1.000 79.63782  ? 279 ARG B CZ    1 
ATOM   4149 N  NH1   . ARG B 1  249 ? -3.46443  -9.02159  -19.19359 1.000 74.89289  ? 279 ARG B NH1   1 
ATOM   4150 N  NH2   . ARG B 1  249 ? -1.36335  -9.91065  -18.95357 1.000 69.49030  ? 279 ARG B NH2   1 
ATOM   4151 N  N     . ARG B 1  250 ? -4.71148  -2.60464  -14.08379 1.000 47.20587  ? 280 ARG B N     1 
ATOM   4152 C  CA    . ARG B 1  250 ? -5.74449  -1.58263  -14.12019 1.000 45.60630  ? 280 ARG B CA    1 
ATOM   4153 C  C     . ARG B 1  250 ? -5.65303  -0.65088  -12.90803 1.000 41.21297  ? 280 ARG B C     1 
ATOM   4154 O  O     . ARG B 1  250 ? -6.66583  -0.20999  -12.36556 1.000 38.72899  ? 280 ARG B O     1 
ATOM   4155 C  CB    . ARG B 1  250 ? -7.13153  -2.21260  -14.21980 1.000 53.25015  ? 280 ARG B CB    1 
ATOM   4156 C  CG    . ARG B 1  250 ? -7.45013  -3.20083  -13.12989 1.000 63.10213  ? 280 ARG B CG    1 
ATOM   4157 C  CD    . ARG B 1  250 ? -8.82121  -3.83378  -13.33450 1.000 69.30938  ? 280 ARG B CD    1 
ATOM   4158 N  NE    . ARG B 1  250 ? -9.32275  -4.43603  -12.10344 1.000 73.18918  ? 280 ARG B NE    1 
ATOM   4159 C  CZ    . ARG B 1  250 ? -9.13262  -5.70011  -11.74577 1.000 82.52372  ? 280 ARG B CZ    1 
ATOM   4160 N  NH1   . ARG B 1  250 ? -8.47092  -6.54495  -12.52520 1.000 94.73631  ? 280 ARG B NH1   1 
ATOM   4161 N  NH2   . ARG B 1  250 ? -9.61619  -6.12435  -10.58268 1.000 75.52744  ? 280 ARG B NH2   1 
ATOM   4162 N  N     . ILE B 1  251 ? -4.43487  -0.34598  -12.47042 1.000 38.69972  ? 281 ILE B N     1 
ATOM   4163 C  CA    . ILE B 1  251 ? -4.20749  0.70081   -11.48129 1.000 38.07127  ? 281 ILE B CA    1 
ATOM   4164 C  C     . ILE B 1  251 ? -3.11768  1.62192   -12.00251 1.000 40.66413  ? 281 ILE B C     1 
ATOM   4165 O  O     . ILE B 1  251 ? -2.33301  1.26510   -12.88488 1.000 42.79808  ? 281 ILE B O     1 
ATOM   4166 C  CB    . ILE B 1  251 ? -3.82697  0.14852   -10.08855 1.000 37.58435  ? 281 ILE B CB    1 
ATOM   4167 C  CG1   . ILE B 1  251 ? -2.44899  -0.49547  -10.13820 1.000 38.37119  ? 281 ILE B CG1   1 
ATOM   4168 C  CG2   . ILE B 1  251 ? -4.87179  -0.84158  -9.59236  1.000 37.62825  ? 281 ILE B CG2   1 
ATOM   4169 C  CD1   . ILE B 1  251 ? -1.83749  -0.70176  -8.78547  1.000 43.35788  ? 281 ILE B CD1   1 
ATOM   4170 N  N     . VAL B 1  252 ? -3.07246  2.82680   -11.44127 1.000 37.75558  ? 282 VAL B N     1 
ATOM   4171 C  CA    . VAL B 1  252 ? -2.05960  3.79887   -11.80445 1.000 37.86941  ? 282 VAL B CA    1 
ATOM   4172 C  C     . VAL B 1  252 ? -0.90322  3.81266   -10.80388 1.000 37.51025  ? 282 VAL B C     1 
ATOM   4173 O  O     . VAL B 1  252 ? 0.25863   3.84873   -11.20531 1.000 38.48977  ? 282 VAL B O     1 
ATOM   4174 C  CB    . VAL B 1  252 ? -2.68964  5.20090   -11.94392 1.000 37.81472  ? 282 VAL B CB    1 
ATOM   4175 C  CG1   . VAL B 1  252 ? -1.59468  6.23592   -12.04812 1.000 43.97518  ? 282 VAL B CG1   1 
ATOM   4176 C  CG2   . VAL B 1  252 ? -3.61910  5.24816   -13.16957 1.000 38.30405  ? 282 VAL B CG2   1 
ATOM   4177 N  N     . ALA B 1  253 ? -1.18073  3.78839   -9.50178  1.000 43.54202  ? 283 ALA B N     1 
ATOM   4178 C  CA    . ALA B 1  253 ? -0.10537  3.99818   -8.53714  1.000 43.62910  ? 283 ALA B CA    1 
ATOM   4179 C  C     . ALA B 1  253 ? -0.37790  3.19592   -7.27421  1.000 38.46287  ? 283 ALA B C     1 
ATOM   4180 O  O     . ALA B 1  253 ? -1.49270  3.21082   -6.75379  1.000 37.28933  ? 283 ALA B O     1 
ATOM   4181 C  CB    . ALA B 1  253 ? 0.03676   5.49211   -8.19889  1.000 36.37786  ? 283 ALA B CB    1 
ATOM   4182 N  N     . CYS B 1  254 ? 0.64528   2.50981   -6.78273  1.000 37.91662  ? 284 CYS B N     1 
ATOM   4183 C  CA    . CYS B 1  254 ? 0.52674   1.75555   -5.54085  1.000 41.67262  ? 284 CYS B CA    1 
ATOM   4184 C  C     . CYS B 1  254 ? 1.74107   2.03437   -4.67024  1.000 40.81117  ? 284 CYS B C     1 
ATOM   4185 O  O     . CYS B 1  254 ? 2.87790   1.89646   -5.12470  1.000 40.61736  ? 284 CYS B O     1 
ATOM   4186 C  CB    . CYS B 1  254 ? 0.38563   0.25561   -5.81411  1.000 41.45755  ? 284 CYS B CB    1 
ATOM   4187 S  SG    . CYS B 1  254 ? 0.22520   -0.74870  -4.30225  1.000 47.36964  ? 284 CYS B SG    1 
ATOM   4188 N  N     . HIS B 1  255 ? 1.48654   2.41111   -3.42107  1.000 39.25645  ? 285 HIS B N     1 
ATOM   4189 C  CA    . HIS B 1  255 ? 2.48091   2.79990   -2.43336  1.000 42.24136  ? 285 HIS B CA    1 
ATOM   4190 C  C     . HIS B 1  255 ? 2.96821   1.57973   -1.63680  1.000 47.14266  ? 285 HIS B C     1 
ATOM   4191 O  O     . HIS B 1  255 ? 2.43815   0.46976   -1.76783  1.000 43.56589  ? 285 HIS B O     1 
ATOM   4192 C  CB    . HIS B 1  255 ? 1.86326   3.86371   -1.51591  1.000 42.07167  ? 285 HIS B CB    1 
ATOM   4193 C  CG    . HIS B 1  255 ? 2.85060   4.56852   -0.63313  1.000 42.94643  ? 285 HIS B CG    1 
ATOM   4194 N  ND1   . HIS B 1  255 ? 2.51507   5.03426   0.61409   1.000 39.48918  ? 285 HIS B ND1   1 
ATOM   4195 C  CD2   . HIS B 1  255 ? 4.14753   4.89655   -0.82255  1.000 41.32351  ? 285 HIS B CD2   1 
ATOM   4196 C  CE1   . HIS B 1  255 ? 3.56428   5.62015   1.15882   1.000 41.17023  ? 285 HIS B CE1   1 
ATOM   4197 N  NE2   . HIS B 1  255 ? 4.56996   5.54632   0.30943   1.000 52.79471  ? 285 HIS B NE2   1 
ATOM   4198 N  N     . PHE B 1  256 ? 4.00352   1.79855   -0.81714  1.000 46.70602  ? 286 PHE B N     1 
ATOM   4199 C  CA    . PHE B 1  256 ? 4.53886   0.78636   0.11345   1.000 44.91734  ? 286 PHE B CA    1 
ATOM   4200 C  C     . PHE B 1  256 ? 5.16658   -0.40449  -0.62204  1.000 49.62642  ? 286 PHE B C     1 
ATOM   4201 O  O     . PHE B 1  256 ? 4.96671   -1.56457  -0.24520  1.000 54.50759  ? 286 PHE B O     1 
ATOM   4202 C  CB    . PHE B 1  256 ? 3.46123   0.30616   1.09075   1.000 44.52914  ? 286 PHE B CB    1 
ATOM   4203 C  CG    . PHE B 1  256 ? 2.99259   1.37496   2.04115   1.000 44.90116  ? 286 PHE B CG    1 
ATOM   4204 C  CD1   . PHE B 1  256 ? 3.90482   2.22583   2.65198   1.000 52.45709  ? 286 PHE B CD1   1 
ATOM   4205 C  CD2   . PHE B 1  256 ? 1.64269   1.54392   2.30169   1.000 46.85755  ? 286 PHE B CD2   1 
ATOM   4206 C  CE1   . PHE B 1  256 ? 3.47815   3.21665   3.52535   1.000 58.32203  ? 286 PHE B CE1   1 
ATOM   4207 C  CE2   . PHE B 1  256 ? 1.20501   2.54074   3.16506   1.000 44.15207  ? 286 PHE B CE2   1 
ATOM   4208 C  CZ    . PHE B 1  256 ? 2.12125   3.37161   3.77989   1.000 49.23313  ? 286 PHE B CZ    1 
ATOM   4209 N  N     . ILE B 1  257 ? 5.97320   -0.11129  -1.63528  1.000 52.62822  ? 287 ILE B N     1 
ATOM   4210 C  CA    . ILE B 1  257 ? 6.61489   -1.14312  -2.44273  1.000 47.48167  ? 287 ILE B CA    1 
ATOM   4211 C  C     . ILE B 1  257 ? 8.12291   -0.91514  -2.39325  1.000 52.43630  ? 287 ILE B C     1 
ATOM   4212 O  O     . ILE B 1  257 ? 8.61773   0.09697   -2.90523  1.000 48.96671  ? 287 ILE B O     1 
ATOM   4213 C  CB    . ILE B 1  257 ? 6.08835   -1.13882  -3.88454  1.000 46.22654  ? 287 ILE B CB    1 
ATOM   4214 C  CG1   . ILE B 1  257 ? 4.63535   -1.63281  -3.88709  1.000 48.25524  ? 287 ILE B CG1   1 
ATOM   4215 C  CG2   . ILE B 1  257 ? 6.97001   -1.96863  -4.79604  1.000 46.94606  ? 287 ILE B CG2   1 
ATOM   4216 C  CD1   . ILE B 1  257 ? 3.96584   -1.58053  -5.23783  1.000 55.94012  ? 287 ILE B CD1   1 
ATOM   4217 N  N     . LYS B 1  258 ? 8.85714   -1.85327  -1.76172  1.000 50.40143  ? 288 LYS B N     1 
ATOM   4218 C  CA    . LYS B 1  258 ? 10.31018  -1.77430  -1.66525  1.000 54.50867  ? 288 LYS B CA    1 
ATOM   4219 C  C     . LYS B 1  258 ? 10.97469  -2.23003  -2.96560  1.000 57.67163  ? 288 LYS B C     1 
ATOM   4220 O  O     . LYS B 1  258 ? 10.35038  -2.89886  -3.79350  1.000 62.59411  ? 288 LYS B O     1 
ATOM   4221 C  CB    . LYS B 1  258 ? 10.80662  -2.62855  -0.49762  1.000 55.57524  ? 288 LYS B CB    1 
ATOM   4222 C  CG    . LYS B 1  258 ? 10.81250  -4.12248  -0.79293  1.000 85.90947  ? 288 LYS B CG    1 
ATOM   4223 C  CD    . LYS B 1  258 ? 11.38193  -4.92673  0.37469   1.000 94.22742  ? 288 LYS B CD    1 
ATOM   4224 C  CE    . LYS B 1  258 ? 11.62178  -6.37765  -0.01970  1.000 91.87810  ? 288 LYS B CE    1 
ATOM   4225 N  NZ    . LYS B 1  258 ? 12.50514  -7.07086  0.95582   1.000 96.98438  ? 288 LYS B NZ    1 
ATOM   4226 N  N     . PRO B 1  259 ? 12.25562  -1.89600  -3.15601  1.000 59.61712  ? 289 PRO B N     1 
ATOM   4227 C  CA    . PRO B 1  259 ? 12.90313  -2.18273  -4.45331  1.000 62.36295  ? 289 PRO B CA    1 
ATOM   4228 C  C     . PRO B 1  259 ? 12.79696  -3.63364  -4.90357  1.000 59.05529  ? 289 PRO B C     1 
ATOM   4229 O  O     . PRO B 1  259 ? 12.37753  -3.89740  -6.04147  1.000 59.49077  ? 289 PRO B O     1 
ATOM   4230 C  CB    . PRO B 1  259 ? 14.35723  -1.75479  -4.20777  1.000 63.18518  ? 289 PRO B CB    1 
ATOM   4231 C  CG    . PRO B 1  259 ? 14.25463  -0.69901  -3.14351  1.000 56.40523  ? 289 PRO B CG    1 
ATOM   4232 C  CD    . PRO B 1  259 ? 13.14897  -1.16720  -2.23619  1.000 52.82573  ? 289 PRO B CD    1 
ATOM   4233 N  N     . ARG B 1  260 ? 13.18727  -4.58882  -4.05992  1.000 59.76514  ? 290 ARG B N     1 
ATOM   4234 C  CA    . ARG B 1  260 ? 13.07312  -5.99474  -4.43117  1.000 62.00426  ? 290 ARG B CA    1 
ATOM   4235 C  C     . ARG B 1  260 ? 11.65795  -6.32464  -4.88270  1.000 59.52896  ? 290 ARG B C     1 
ATOM   4236 O  O     . ARG B 1  260 ? 11.45356  -6.96642  -5.92576  1.000 58.86408  ? 290 ARG B O     1 
ATOM   4237 C  CB    . ARG B 1  260 ? 13.47756  -6.87899  -3.25050  1.000 75.39867  ? 290 ARG B CB    1 
ATOM   4238 C  CG    . ARG B 1  260 ? 13.25447  -8.37594  -3.46673  1.000 84.21063  ? 290 ARG B CG    1 
ATOM   4239 C  CD    . ARG B 1  260 ? 14.30812  -8.95575  -4.39425  1.000 82.99625  ? 290 ARG B CD    1 
ATOM   4240 N  NE    . ARG B 1  260 ? 13.83961  -9.08147  -5.76510  1.000 94.75590  ? 290 ARG B NE    1 
ATOM   4241 C  CZ    . ARG B 1  260 ? 14.57221  -8.79625  -6.83431  1.000 97.10519  ? 290 ARG B CZ    1 
ATOM   4242 N  NH1   . ARG B 1  260 ? 15.79726  -8.30928  -6.71467  1.000 96.21909  ? 290 ARG B NH1   1 
ATOM   4243 N  NH2   . ARG B 1  260 ? 14.06075  -8.99899  -8.04716  1.000 84.89624  ? 290 ARG B NH2   1 
ATOM   4244 N  N     . THR B 1  261 ? 10.66725  -5.88379  -4.10524  1.000 54.74924  ? 291 THR B N     1 
ATOM   4245 C  CA    . THR B 1  261 ? 9.27812   -6.16072  -4.43978  1.000 49.10580  ? 291 THR B CA    1 
ATOM   4246 C  C     . THR B 1  261 ? 8.91262   -5.56744  -5.78952  1.000 57.45294  ? 291 THR B C     1 
ATOM   4247 O  O     . THR B 1  261 ? 8.19232   -6.19727  -6.57438  1.000 55.16546  ? 291 THR B O     1 
ATOM   4248 C  CB    . THR B 1  261 ? 8.35253   -5.61394  -3.35632  1.000 44.00710  ? 291 THR B CB    1 
ATOM   4249 O  OG1   . THR B 1  261 ? 8.74400   -6.13921  -2.08057  1.000 57.69633  ? 291 THR B OG1   1 
ATOM   4250 C  CG2   . THR B 1  261 ? 6.91942   -6.01887  -3.63486  1.000 48.62184  ? 291 THR B CG2   1 
ATOM   4251 N  N     . LEU B 1  262 ? 9.38652   -4.35038  -6.06644  1.000 45.37809  ? 292 LEU B N     1 
ATOM   4252 C  CA    . LEU B 1  262 ? 9.06805   -3.69812  -7.32919  1.000 43.82520  ? 292 LEU B CA    1 
ATOM   4253 C  C     . LEU B 1  262 ? 9.66061   -4.46288  -8.49657  1.000 51.37958  ? 292 LEU B C     1 
ATOM   4254 O  O     . LEU B 1  262 ? 9.00922   -4.63266  -9.53036  1.000 54.97079  ? 292 LEU B O     1 
ATOM   4255 C  CB    . LEU B 1  262 ? 9.59006   -2.25812  -7.31708  1.000 49.47482  ? 292 LEU B CB    1 
ATOM   4256 C  CG    . LEU B 1  262 ? 9.44358   -1.45485  -8.61486  1.000 51.44070  ? 292 LEU B CG    1 
ATOM   4257 C  CD1   . LEU B 1  262 ? 7.99241   -1.37375  -9.04530  1.000 49.21492  ? 292 LEU B CD1   1 
ATOM   4258 C  CD2   . LEU B 1  262 ? 10.02664  -0.05089  -8.46079  1.000 46.29291  ? 292 LEU B CD2   1 
ATOM   4259 N  N     . LEU B 1  263 ? 10.91165  -4.90891  -8.36013  1.000 46.65467  ? 293 LEU B N     1 
ATOM   4260 C  CA    . LEU B 1  263 ? 11.50525  -5.70669  -9.42352  1.000 51.34620  ? 293 LEU B CA    1 
ATOM   4261 C  C     . LEU B 1  263 ? 10.71316  -6.99264  -9.64749  1.000 56.91652  ? 293 LEU B C     1 
ATOM   4262 O  O     . LEU B 1  263 ? 10.49773  -7.41140  -10.79050 1.000 61.93949  ? 293 LEU B O     1 
ATOM   4263 C  CB    . LEU B 1  263 ? 12.96538  -6.00477  -9.08713  1.000 47.97492  ? 293 LEU B CB    1 
ATOM   4264 C  CG    . LEU B 1  263 ? 13.82341  -4.73879  -9.02119  1.000 56.25202  ? 293 LEU B CG    1 
ATOM   4265 C  CD1   . LEU B 1  263 ? 15.19263  -5.03292  -8.43576  1.000 56.96000  ? 293 LEU B CD1   1 
ATOM   4266 C  CD2   . LEU B 1  263 ? 13.96189  -4.12250  -10.40311 1.000 55.78653  ? 293 LEU B CD2   1 
ATOM   4267 N  N     . ASP B 1  264 ? 10.22657  -7.60187  -8.56243  1.000 50.32623  ? 294 ASP B N     1 
ATOM   4268 C  CA    . ASP B 1  264 ? 9.43451   -8.81883  -8.70639  1.000 55.29628  ? 294 ASP B CA    1 
ATOM   4269 C  C     . ASP B 1  264 ? 8.08926   -8.54469  -9.37383  1.000 57.18842  ? 294 ASP B C     1 
ATOM   4270 O  O     . ASP B 1  264 ? 7.63094   -9.34151  -10.19982 1.000 51.92784  ? 294 ASP B O     1 
ATOM   4271 C  CB    . ASP B 1  264 ? 9.22801   -9.48111  -7.34545  1.000 57.10014  ? 294 ASP B CB    1 
ATOM   4272 C  CG    . ASP B 1  264 ? 10.48821  -10.14423 -6.82206  1.000 63.48104  ? 294 ASP B CG    1 
ATOM   4273 O  OD1   . ASP B 1  264 ? 11.35190  -10.51706 -7.64246  1.000 63.50195  ? 294 ASP B OD1   1 
ATOM   4274 O  OD2   . ASP B 1  264 ? 10.61167  -10.28949 -5.58914  1.000 63.23848  ? 294 ASP B OD2   1 
ATOM   4275 N  N     . TYR B 1  265 ? 7.42740   -7.43976  -9.01135  1.000 50.04053  ? 295 TYR B N     1 
ATOM   4276 C  CA    . TYR B 1  265 ? 6.15116   -7.10162  -9.63780  1.000 49.34470  ? 295 TYR B CA    1 
ATOM   4277 C  C     . TYR B 1  265 ? 6.34461   -6.81031  -11.12081 1.000 46.13847  ? 295 TYR B C     1 
ATOM   4278 O  O     . TYR B 1  265 ? 5.54529   -7.25013  -11.96460 1.000 44.26766  ? 295 TYR B O     1 
ATOM   4279 C  CB    . TYR B 1  265 ? 5.51243   -5.89376  -8.94831  1.000 52.80662  ? 295 TYR B CB    1 
ATOM   4280 C  CG    . TYR B 1  265 ? 4.90094   -6.14004  -7.58513  1.000 49.77383  ? 295 TYR B CG    1 
ATOM   4281 C  CD1   . TYR B 1  265 ? 4.92716   -7.39717  -6.99140  1.000 52.48178  ? 295 TYR B CD1   1 
ATOM   4282 C  CD2   . TYR B 1  265 ? 4.29721   -5.09718  -6.88569  1.000 50.65348  ? 295 TYR B CD2   1 
ATOM   4283 C  CE1   . TYR B 1  265 ? 4.36062   -7.60542  -5.74123  1.000 46.24636  ? 295 TYR B CE1   1 
ATOM   4284 C  CE2   . TYR B 1  265 ? 3.73367   -5.29744  -5.63452  1.000 46.79267  ? 295 TYR B CE2   1 
ATOM   4285 C  CZ    . TYR B 1  265 ? 3.76788   -6.55156  -5.06579  1.000 50.95936  ? 295 TYR B CZ    1 
ATOM   4286 O  OH    . TYR B 1  265 ? 3.20535   -6.75382  -3.82462  1.000 58.26273  ? 295 TYR B OH    1 
ATOM   4287 N  N     . TRP B 1  266 ? 7.39349   -6.05825  -11.46005 1.000 52.06876  ? 296 TRP B N     1 
ATOM   4288 C  CA    . TRP B 1  266 ? 7.67396   -5.77196  -12.85910 1.000 47.58433  ? 296 TRP B CA    1 
ATOM   4289 C  C     . TRP B 1  266 ? 7.90167   -7.06580  -13.63245 1.000 52.42811  ? 296 TRP B C     1 
ATOM   4290 O  O     . TRP B 1  266 ? 7.33326   -7.27357  -14.71428 1.000 50.36305  ? 296 TRP B O     1 
ATOM   4291 C  CB    . TRP B 1  266 ? 8.88293   -4.85294  -12.96836 1.000 44.81615  ? 296 TRP B CB    1 
ATOM   4292 C  CG    . TRP B 1  266 ? 8.92944   -4.12967  -14.26322 1.000 52.63892  ? 296 TRP B CG    1 
ATOM   4293 C  CD1   . TRP B 1  266 ? 9.77805   -4.37146  -15.30459 1.000 52.05877  ? 296 TRP B CD1   1 
ATOM   4294 C  CD2   . TRP B 1  266 ? 8.08529   -3.04958  -14.67368 1.000 55.19532  ? 296 TRP B CD2   1 
ATOM   4295 N  NE1   . TRP B 1  266 ? 9.51367   -3.50224  -16.34231 1.000 57.46454  ? 296 TRP B NE1   1 
ATOM   4296 C  CE2   . TRP B 1  266 ? 8.48281   -2.68031  -15.97676 1.000 56.46376  ? 296 TRP B CE2   1 
ATOM   4297 C  CE3   . TRP B 1  266 ? 7.03153   -2.35570  -14.06814 1.000 52.47729  ? 296 TRP B CE3   1 
ATOM   4298 C  CZ2   . TRP B 1  266 ? 7.86755   -1.64316  -16.67831 1.000 59.34449  ? 296 TRP B CZ2   1 
ATOM   4299 C  CZ3   . TRP B 1  266 ? 6.42027   -1.32455  -14.76970 1.000 59.87238  ? 296 TRP B CZ3   1 
ATOM   4300 C  CH2   . TRP B 1  266 ? 6.84078   -0.98429  -16.06079 1.000 65.19659  ? 296 TRP B CH2   1 
ATOM   4301 N  N     . GLN B 1  267 ? 8.72987   -7.95792  -13.07895 1.000 51.19883  ? 297 GLN B N     1 
ATOM   4302 C  CA    . GLN B 1  267 ? 8.94663   -9.25679  -13.70430 1.000 53.97230  ? 297 GLN B CA    1 
ATOM   4303 C  C     . GLN B 1  267 ? 7.63557   -10.02775 -13.85397 1.000 52.48497  ? 297 GLN B C     1 
ATOM   4304 O  O     . GLN B 1  267 ? 7.38717   -10.63953 -14.89400 1.000 51.22561  ? 297 GLN B O     1 
ATOM   4305 C  CB    . GLN B 1  267 ? 9.95793   -10.06196 -12.88784 1.000 53.01571  ? 297 GLN B CB    1 
ATOM   4306 C  CG    . GLN B 1  267 ? 10.48266  -11.29982 -13.60030 1.000 60.56406  ? 297 GLN B CG    1 
ATOM   4307 C  CD    . GLN B 1  267 ? 11.15616  -10.97555 -14.92748 1.000 77.65334  ? 297 GLN B CD    1 
ATOM   4308 O  OE1   . GLN B 1  267 ? 12.17815  -10.28654 -14.97472 1.000 91.60143  ? 297 GLN B OE1   1 
ATOM   4309 N  NE2   . GLN B 1  267 ? 10.57975  -11.47032 -16.01937 1.000 67.48430  ? 297 GLN B NE2   1 
ATOM   4310 N  N     . ALA B 1  268 ? 6.79996   -10.02196 -12.81865 1.000 45.83107  ? 298 ALA B N     1 
ATOM   4311 C  CA    . ALA B 1  268 ? 5.50792   -10.69894 -12.90331 1.000 43.65747  ? 298 ALA B CA    1 
ATOM   4312 C  C     . ALA B 1  268 ? 4.70548   -10.18769 -14.08790 1.000 48.73112  ? 298 ALA B C     1 
ATOM   4313 O  O     . ALA B 1  268 ? 4.13019   -10.97053 -14.85185 1.000 54.23373  ? 298 ALA B O     1 
ATOM   4314 C  CB    . ALA B 1  268 ? 4.72941   -10.50021 -11.60297 1.000 42.68896  ? 298 ALA B CB    1 
ATOM   4315 N  N     . LEU B 1  269 ? 4.66542   -8.86465  -14.25961 1.000 53.46005  ? 299 LEU B N     1 
ATOM   4316 C  CA    . LEU B 1  269 ? 3.88802   -8.28042  -15.34920 1.000 45.89812  ? 299 LEU B CA    1 
ATOM   4317 C  C     . LEU B 1  269 ? 4.48050   -8.63614  -16.70849 1.000 57.43220  ? 299 LEU B C     1 
ATOM   4318 O  O     . LEU B 1  269 ? 3.74014   -8.90894  -17.66227 1.000 49.79424  ? 299 LEU B O     1 
ATOM   4319 C  CB    . LEU B 1  269 ? 3.80009   -6.76546  -15.16285 1.000 42.78456  ? 299 LEU B CB    1 
ATOM   4320 C  CG    . LEU B 1  269 ? 2.92254   -6.38870  -13.96844 1.000 51.45258  ? 299 LEU B CG    1 
ATOM   4321 C  CD1   . LEU B 1  269 ? 3.36078   -5.04683  -13.35433 1.000 42.64738  ? 299 LEU B CD1   1 
ATOM   4322 C  CD2   . LEU B 1  269 ? 1.44539   -6.37361  -14.37088 1.000 44.64518  ? 299 LEU B CD2   1 
ATOM   4323 N  N     . GLU B 1  270 ? 5.80746   -8.65013  -16.81799 1.000 57.95569  ? 300 GLU B N     1 
ATOM   4324 C  CA    . GLU B 1  270 ? 6.42300   -9.10687  -18.05732 1.000 66.63562  ? 300 GLU B CA    1 
ATOM   4325 C  C     . GLU B 1  270 ? 6.05188   -10.56081 -18.35148 1.000 63.75912  ? 300 GLU B C     1 
ATOM   4326 O  O     . GLU B 1  270 ? 5.54647   -10.88158 -19.43236 1.000 71.14223  ? 300 GLU B O     1 
ATOM   4327 C  CB    . GLU B 1  270 ? 7.94002   -8.92689  -17.99585 1.000 60.20883  ? 300 GLU B CB    1 
ATOM   4328 C  CG    . GLU B 1  270 ? 8.40704   -7.47290  -17.95272 1.000 74.92850  ? 300 GLU B CG    1 
ATOM   4329 C  CD    . GLU B 1  270 ? 8.13956   -6.71663  -19.25247 1.000 102.53298 ? 300 GLU B CD    1 
ATOM   4330 O  OE1   . GLU B 1  270 ? 7.85017   -7.36641  -20.28249 1.000 95.69550  ? 300 GLU B OE1   1 
ATOM   4331 O  OE2   . GLU B 1  270 ? 8.22057   -5.46763  -19.24424 1.000 100.67752 ? 300 GLU B OE2   1 
ATOM   4332 N  N     . ASN B 1  271 ? 6.26824   -11.45501 -17.37575 1.000 56.78708  ? 301 ASN B N     1 
ATOM   4333 C  CA    . ASN B 1  271 ? 6.04716   -12.88397 -17.57497 1.000 57.60034  ? 301 ASN B CA    1 
ATOM   4334 C  C     . ASN B 1  271 ? 4.61000   -13.19188 -17.98249 1.000 53.92371  ? 301 ASN B C     1 
ATOM   4335 O  O     . ASN B 1  271 ? 4.36473   -14.17473 -18.69160 1.000 55.95773  ? 301 ASN B O     1 
ATOM   4336 C  CB    . ASN B 1  271 ? 6.38763   -13.66424 -16.29526 1.000 53.62069  ? 301 ASN B CB    1 
ATOM   4337 C  CG    . ASN B 1  271 ? 7.85677   -13.60832 -15.94379 1.000 54.72171  ? 301 ASN B CG    1 
ATOM   4338 O  OD1   . ASN B 1  271 ? 8.68447   -13.15716 -16.73601 1.000 67.50855  ? 301 ASN B OD1   1 
ATOM   4339 N  ND2   . ASN B 1  271 ? 8.19322   -14.07457 -14.74102 1.000 53.25957  ? 301 ASN B ND2   1 
ATOM   4340 N  N     . SER B 1  272 ? 3.65418   -12.39997 -17.51697 1.000 57.15773  ? 302 SER B N     1 
ATOM   4341 C  CA    . SER B 1  272 ? 2.24407   -12.62390 -17.80848 1.000 55.19750  ? 302 SER B CA    1 
ATOM   4342 C  C     . SER B 1  272 ? 1.73165   -11.75366 -18.94811 1.000 53.71953  ? 302 SER B C     1 
ATOM   4343 O  O     . SER B 1  272 ? 0.53853   -11.80359 -19.26867 1.000 59.12907  ? 302 SER B O     1 
ATOM   4344 C  CB    . SER B 1  272 ? 1.40654   -12.38016 -16.55612 1.000 48.03100  ? 302 SER B CB    1 
ATOM   4345 O  OG    . SER B 1  272 ? 1.74176   -11.12228 -15.99098 1.000 56.43490  ? 302 SER B OG    1 
ATOM   4346 N  N     . ARG B 1  273 ? 2.60243   -10.94554 -19.54227 1.000 66.70081  ? 303 ARG B N     1 
ATOM   4347 C  CA    . ARG B 1  273 ? 2.26398   -10.20729 -20.74999 1.000 62.81223  ? 303 ARG B CA    1 
ATOM   4348 C  C     . ARG B 1  273 ? 1.67959   -11.15707 -21.78597 1.000 69.00185  ? 303 ARG B C     1 
ATOM   4349 O  O     . ARG B 1  273 ? 2.30145   -12.16200 -22.13641 1.000 80.02597  ? 303 ARG B O     1 
ATOM   4350 C  CB    . ARG B 1  273 ? 3.52278   -9.52118  -21.28732 1.000 62.12149  ? 303 ARG B CB    1 
ATOM   4351 C  CG    . ARG B 1  273 ? 3.29644   -8.33799  -22.20399 1.000 89.89116  ? 303 ARG B CG    1 
ATOM   4352 C  CD    . ARG B 1  273 ? 4.62722   -7.91287  -22.81240 1.000 100.26431 ? 303 ARG B CD    1 
ATOM   4353 N  NE    . ARG B 1  273 ? 5.42307   -9.08480  -23.17694 1.000 103.57730 ? 303 ARG B NE    1 
ATOM   4354 C  CZ    . ARG B 1  273 ? 5.30064   -9.74856  -24.31803 1.000 113.07799 ? 303 ARG B CZ    1 
ATOM   4355 N  NH1   . ARG B 1  273 ? 4.45229   -9.36336  -25.26264 1.000 115.76488 ? 303 ARG B NH1   1 
ATOM   4356 N  NH2   . ARG B 1  273 ? 6.04456   -10.83252 -24.52254 1.000 108.13160 ? 303 ARG B NH2   1 
ATOM   4357 N  N     . GLY B 1  274 ? 0.47241   -10.86697 -22.24945 1.000 70.08867  ? 304 GLY B N     1 
ATOM   4358 C  CA    . GLY B 1  274 ? -0.17396  -11.72476 -23.22239 1.000 83.61325  ? 304 GLY B CA    1 
ATOM   4359 C  C     . GLY B 1  274 ? -1.10675  -12.76988 -22.65626 1.000 71.45326  ? 304 GLY B C     1 
ATOM   4360 O  O     . GLY B 1  274 ? -1.66905  -13.55071 -23.43721 1.000 66.57457  ? 304 GLY B O     1 
ATOM   4361 N  N     . GLU B 1  275 ? -1.27425  -12.83315 -21.34021 1.000 66.14429  ? 305 GLU B N     1 
ATOM   4362 C  CA    . GLU B 1  275 ? -2.37604  -13.57427 -20.74595 1.000 59.61092  ? 305 GLU B CA    1 
ATOM   4363 C  C     . GLU B 1  275 ? -3.58098  -12.65029 -20.60330 1.000 70.43359  ? 305 GLU B C     1 
ATOM   4364 O  O     . GLU B 1  275 ? -3.46500  -11.42428 -20.67409 1.000 78.35639  ? 305 GLU B O     1 
ATOM   4365 C  CB    . GLU B 1  275 ? -1.98253  -14.14155 -19.37921 1.000 62.02740  ? 305 GLU B CB    1 
ATOM   4366 C  CG    . GLU B 1  275 ? -0.56651  -14.70657 -19.31786 1.000 67.24883  ? 305 GLU B CG    1 
ATOM   4367 C  CD    . GLU B 1  275 ? -0.52954  -16.22156 -19.39319 1.000 74.22000  ? 305 GLU B CD    1 
ATOM   4368 O  OE1   . GLU B 1  275 ? -1.31327  -16.86971 -18.66203 1.000 82.13560  ? 305 GLU B OE1   1 
ATOM   4369 O  OE2   . GLU B 1  275 ? 0.28216   -16.76640 -20.17861 1.000 84.85600  ? 305 GLU B OE2   1 
ATOM   4370 N  N     . ASP B 1  276 ? -4.74690  -13.25133 -20.39299 1.000 82.73170  ? 306 ASP B N     1 
ATOM   4371 C  CA    . ASP B 1  276 ? -5.99487  -12.50334 -20.30537 1.000 92.38566  ? 306 ASP B CA    1 
ATOM   4372 C  C     . ASP B 1  276 ? -6.46332  -12.36564 -18.85716 1.000 93.11786  ? 306 ASP B C     1 
ATOM   4373 O  O     . ASP B 1  276 ? -6.09299  -13.14883 -17.97647 1.000 91.47167  ? 306 ASP B O     1 
ATOM   4374 C  CB    . ASP B 1  276 ? -7.08518  -13.17316 -21.14010 1.000 106.96732 ? 306 ASP B CB    1 
ATOM   4375 C  CG    . ASP B 1  276 ? -6.82974  -13.06485 -22.63017 1.000 119.32442 ? 306 ASP B CG    1 
ATOM   4376 O  OD1   . ASP B 1  276 ? -5.76388  -12.53178 -23.02046 1.000 116.66639 ? 306 ASP B OD1   1 
ATOM   4377 O  OD2   . ASP B 1  276 ? -7.69204  -13.51169 -23.41694 1.000 126.64877 ? 306 ASP B OD2   1 
ATOM   4378 N  N     . CYS B 1  277 ? -7.29723  -11.34568 -18.62664 1.000 93.97190  ? 307 CYS B N     1 
ATOM   4379 C  CA    . CYS B 1  277 ? -7.89275  -11.02395 -17.33935 1.000 95.76360  ? 307 CYS B CA    1 
ATOM   4380 C  C     . CYS B 1  277 ? -9.36782  -10.70390 -17.54773 1.000 94.63560  ? 307 CYS B C     1 
ATOM   4381 O  O     . CYS B 1  277 ? -9.72620  -10.08769 -18.56247 1.000 86.46943  ? 307 CYS B O     1 
ATOM   4382 C  CB    . CYS B 1  277 ? -7.19249  -9.82509  -16.67536 1.000 101.27170 ? 307 CYS B CB    1 
ATOM   4383 S  SG    . CYS B 1  277 ? -5.47129  -10.10121 -16.12806 1.000 110.79291 ? 307 CYS B SG    1 
ATOM   4384 N  N     . PRO B 1  278 ? -10.24447 -11.10109 -16.61148 1.000 95.92134  ? 308 PRO B N     1 
ATOM   4385 C  CA    . PRO B 1  278 ? -11.69751 -10.89106 -16.72089 1.000 87.14980  ? 308 PRO B CA    1 
ATOM   4386 C  C     . PRO B 1  278 ? -12.08759 -9.43201  -16.94744 1.000 94.31814  ? 308 PRO B C     1 
ATOM   4387 O  O     . PRO B 1  278 ? -13.26453 -9.09204  -16.79893 1.000 82.44630  ? 308 PRO B O     1 
ATOM   4388 C  CB    . PRO B 1  278 ? -12.22701 -11.38334 -15.36880 1.000 84.30836  ? 308 PRO B CB    1 
ATOM   4389 C  CG    . PRO B 1  278 ? -11.16882 -12.31545 -14.85239 1.000 91.49638  ? 308 PRO B CG    1 
ATOM   4390 C  CD    . PRO B 1  278 ? -9.87000  -11.75835 -15.34476 1.000 90.27241  ? 308 PRO B CD    1 
HETATM 4391 C  C1    . NAG C 2  .   ? 26.52700  14.43700  28.83300  1.000 40.09491  ? 1   NAG E C1    1 
HETATM 4392 C  C2    . NAG C 2  .   ? 28.04500  14.43800  28.71700  1.000 41.58730  ? 1   NAG E C2    1 
HETATM 4393 C  C3    . NAG C 2  .   ? 28.55000  15.82400  28.27700  1.000 40.71677  ? 1   NAG E C3    1 
HETATM 4394 C  C4    . NAG C 2  .   ? 27.80900  16.34200  27.05100  1.000 50.57442  ? 1   NAG E C4    1 
HETATM 4395 C  C5    . NAG C 2  .   ? 26.30400  16.25500  27.27800  1.000 39.13120  ? 1   NAG E C5    1 
HETATM 4396 C  C6    . NAG C 2  .   ? 25.50500  16.61200  26.05100  1.000 38.96700  ? 1   NAG E C6    1 
HETATM 4397 C  C7    . NAG C 2  .   ? 29.56400  13.11600  30.13400  1.000 43.73531  ? 1   NAG E C7    1 
HETATM 4398 C  C8    . NAG C 2  .   ? 30.10300  12.92100  31.52400  1.000 42.45830  ? 1   NAG E C8    1 
HETATM 4399 N  N2    . NAG C 2  .   ? 28.65000  14.08100  29.99000  1.000 41.34042  ? 1   NAG E N2    1 
HETATM 4400 O  O3    . NAG C 2  .   ? 29.94600  15.75100  28.01200  1.000 52.85156  ? 1   NAG E O3    1 
HETATM 4401 O  O4    . NAG C 2  .   ? 28.16100  17.70500  26.80700  1.000 65.14613  ? 1   NAG E O4    1 
HETATM 4402 O  O5    . NAG C 2  .   ? 25.94700  14.90300  27.61000  1.000 37.66593  ? 1   NAG E O5    1 
HETATM 4403 O  O6    . NAG C 2  .   ? 25.67000  15.61100  25.05500  1.000 43.19514  ? 1   NAG E O6    1 
HETATM 4404 O  O7    . NAG C 2  .   ? 29.92200  12.41700  29.19300  1.000 44.66490  ? 1   NAG E O7    1 
HETATM 4405 C  C1    . NAG C 2  .   ? 28.67300  17.87200  25.45700  1.000 65.58619  ? 2   NAG E C1    1 
HETATM 4406 C  C2    . NAG C 2  .   ? 28.83900  19.35000  25.12300  1.000 67.92448  ? 2   NAG E C2    1 
HETATM 4407 C  C3    . NAG C 2  .   ? 29.54300  19.53400  23.76900  1.000 82.02890  ? 2   NAG E C3    1 
HETATM 4408 C  C4    . NAG C 2  .   ? 30.79900  18.68100  23.64400  1.000 89.19508  ? 2   NAG E C4    1 
HETATM 4409 C  C5    . NAG C 2  .   ? 30.46700  17.24000  23.99900  1.000 90.82483  ? 2   NAG E C5    1 
HETATM 4410 C  C6    . NAG C 2  .   ? 31.66200  16.31400  23.97400  1.000 92.46899  ? 2   NAG E C6    1 
HETATM 4411 C  C7    . NAG C 2  .   ? 26.82100  20.29000  26.18200  1.000 58.63943  ? 2   NAG E C7    1 
HETATM 4412 C  C8    . NAG C 2  .   ? 25.51800  21.00000  25.93700  1.000 53.95354  ? 2   NAG E C8    1 
HETATM 4413 N  N2    . NAG C 2  .   ? 27.54500  20.01400  25.09400  1.000 58.54450  ? 2   NAG E N2    1 
HETATM 4414 O  O3    . NAG C 2  .   ? 29.88000  20.90500  23.59900  1.000 89.04012  ? 2   NAG E O3    1 
HETATM 4415 O  O4    . NAG C 2  .   ? 31.26500  18.73100  22.29900  1.000 104.62625 ? 2   NAG E O4    1 
HETATM 4416 O  O5    . NAG C 2  .   ? 29.92800  17.20200  25.32800  1.000 79.52272  ? 2   NAG E O5    1 
HETATM 4417 O  O6    . NAG C 2  .   ? 31.32100  15.04600  24.51800  1.000 73.43672  ? 2   NAG E O6    1 
HETATM 4418 O  O7    . NAG C 2  .   ? 27.18900  19.96600  27.31200  1.000 74.15763  ? 2   NAG E O7    1 
HETATM 4419 C  C1    . NAG D 3  .   ? -7.46700  2.72000   51.86700  1.000 84.28081  ? 1   NAG F C1    1 
HETATM 4420 C  C2    . NAG D 3  .   ? -7.07000  2.16800   53.23300  1.000 84.52500  ? 1   NAG F C2    1 
HETATM 4421 C  C3    . NAG D 3  .   ? -7.88300  0.91800   53.55100  1.000 93.78001  ? 1   NAG F C3    1 
HETATM 4422 C  C4    . NAG D 3  .   ? -9.37600  1.15400   53.37400  1.000 90.12788  ? 1   NAG F C4    1 
HETATM 4423 C  C5    . NAG D 3  .   ? -9.65400  1.77400   52.00700  1.000 90.53959  ? 1   NAG F C5    1 
HETATM 4424 C  C6    . NAG D 3  .   ? -11.08300 2.22300   51.83100  1.000 83.21713  ? 1   NAG F C6    1 
HETATM 4425 C  C7    . NAG D 3  .   ? -4.82300  2.51600   54.08800  1.000 85.59804  ? 1   NAG F C7    1 
HETATM 4426 C  C8    . NAG D 3  .   ? -3.44200  2.73200   53.55000  1.000 72.09977  ? 1   NAG F C8    1 
HETATM 4427 N  N2    . NAG D 3  .   ? -5.66000  1.85800   53.29100  1.000 78.70885  ? 1   NAG F N2    1 
HETATM 4428 O  O3    . NAG D 3  .   ? -7.59600  0.51500   54.88300  1.000 89.07473  ? 1   NAG F O3    1 
HETATM 4429 O  O4    . NAG D 3  .   ? -10.01800 -0.11300  53.47800  1.000 81.04695  ? 1   NAG F O4    1 
HETATM 4430 O  O5    . NAG D 3  .   ? -8.86100  2.96400   51.86000  1.000 90.65063  ? 1   NAG F O5    1 
HETATM 4431 O  O6    . NAG D 3  .   ? -11.49800 2.92400   52.99700  1.000 97.47907  ? 1   NAG F O6    1 
HETATM 4432 O  O7    . NAG D 3  .   ? -5.16800  2.92600   55.19100  1.000 80.56745  ? 1   NAG F O7    1 
HETATM 4433 C  C1    . FUC D 3  .   ? -12.32400 4.03200   52.76700  1.000 94.41469  ? 2   FUC F C1    1 
HETATM 4434 C  C2    . FUC D 3  .   ? -12.72400 4.58200   54.11300  1.000 97.52918  ? 2   FUC F C2    1 
HETATM 4435 C  C3    . FUC D 3  .   ? -11.54300 5.19700   54.83300  1.000 99.55790  ? 2   FUC F C3    1 
HETATM 4436 C  C4    . FUC D 3  .   ? -10.85600 6.22600   53.95600  1.000 101.55519 ? 2   FUC F C4    1 
HETATM 4437 C  C5    . FUC D 3  .   ? -10.47100 5.58500   52.63000  1.000 102.60602 ? 2   FUC F C5    1 
HETATM 4438 C  C6    . FUC D 3  .   ? -9.87000  6.56200   51.64800  1.000 72.76918  ? 2   FUC F C6    1 
HETATM 4439 O  O2    . FUC D 3  .   ? -13.30900 3.55200   54.90200  1.000 86.57428  ? 2   FUC F O2    1 
HETATM 4440 O  O3    . FUC D 3  .   ? -11.99100 5.81400   56.03700  1.000 104.20110 ? 2   FUC F O3    1 
HETATM 4441 O  O4    . FUC D 3  .   ? -11.71700 7.33600   53.72500  1.000 105.10572 ? 2   FUC F O4    1 
HETATM 4442 O  O5    . FUC D 3  .   ? -11.64400 5.02600   51.99400  1.000 102.50883 ? 2   FUC F O5    1 
HETATM 4443 C  C1    . NAG E 2  .   ? 15.94300  22.95400  4.39400   1.000 71.25598  ? 1   NAG G C1    1 
HETATM 4444 C  C2    . NAG E 2  .   ? 16.28800  22.85700  5.88100   1.000 71.04909  ? 1   NAG G C2    1 
HETATM 4445 C  C3    . NAG E 2  .   ? 17.06200  24.09000  6.33200   1.000 82.44330  ? 1   NAG G C3    1 
HETATM 4446 C  C4    . NAG E 2  .   ? 18.21300  24.38200  5.38400   1.000 89.66344  ? 1   NAG G C4    1 
HETATM 4447 C  C5    . NAG E 2  .   ? 17.68800  24.47800  3.95900   1.000 76.96961  ? 1   NAG G C5    1 
HETATM 4448 C  C6    . NAG E 2  .   ? 18.78200  24.75800  2.96200   1.000 73.52350  ? 1   NAG G C6    1 
HETATM 4449 C  C7    . NAG E 2  .   ? 15.00900  21.80500  7.66700   1.000 62.77137  ? 1   NAG G C7    1 
HETATM 4450 C  C8    . NAG E 2  .   ? 13.68600  21.72800  8.36200   1.000 61.17544  ? 1   NAG G C8    1 
HETATM 4451 N  N2    . NAG E 2  .   ? 15.10200  22.70900  6.69400   1.000 64.45612  ? 1   NAG G N2    1 
HETATM 4452 O  O3    . NAG E 2  .   ? 17.53300  23.88500  7.65600   1.000 82.45426  ? 1   NAG G O3    1 
HETATM 4453 O  O4    . NAG E 2  .   ? 18.75500  25.66400  5.66500   1.000 103.11295 ? 1   NAG G O4    1 
HETATM 4454 O  O5    . NAG E 2  .   ? 17.08500  23.22300  3.60200   1.000 77.70103  ? 1   NAG G O5    1 
HETATM 4455 O  O6    . NAG E 2  .   ? 19.93100  23.96700  3.23800   1.000 82.24503  ? 1   NAG G O6    1 
HETATM 4456 O  O7    . NAG E 2  .   ? 15.95100  21.08300  7.97500   1.000 56.96859  ? 1   NAG G O7    1 
HETATM 4457 C  C1    . NAG E 2  .   ? 19.75300  26.03300  6.56900   1.000 108.29737 ? 2   NAG G C1    1 
HETATM 4458 C  C2    . NAG E 2  .   ? 21.18800  25.67500  6.18100   1.000 108.80100 ? 2   NAG G C2    1 
HETATM 4459 C  C3    . NAG E 2  .   ? 21.91600  26.92700  5.71300   1.000 111.46608 ? 2   NAG G C3    1 
HETATM 4460 C  C4    . NAG E 2  .   ? 20.94700  27.82400  4.96000   1.000 111.47643 ? 2   NAG G C4    1 
HETATM 4461 C  C5    . NAG E 2  .   ? 19.90700  28.36700  5.93400   1.000 112.43389 ? 2   NAG G C5    1 
HETATM 4462 C  C6    . NAG E 2  .   ? 18.60400  28.72500  5.25600   1.000 101.24976 ? 2   NAG G C6    1 
HETATM 4463 C  C7    . NAG E 2  .   ? 21.36300  23.97100  7.89600   1.000 104.95070 ? 2   NAG G C7    1 
HETATM 4464 C  C8    . NAG E 2  .   ? 21.17500  24.07900  9.37800   1.000 93.09436  ? 2   NAG G C8    1 
HETATM 4465 N  N2    . NAG E 2  .   ? 21.86700  25.04500  7.29000   1.000 104.90634 ? 2   NAG G N2    1 
HETATM 4466 O  O3    . NAG E 2  .   ? 23.01700  26.56400  4.89600   1.000 113.08006 ? 2   NAG G O3    1 
HETATM 4467 O  O4    . NAG E 2  .   ? 21.65200  28.91500  4.37700   1.000 113.98514 ? 2   NAG G O4    1 
HETATM 4468 O  O5    . NAG E 2  .   ? 19.61100  27.39200  6.95800   1.000 113.89997 ? 2   NAG G O5    1 
HETATM 4469 O  O6    . NAG E 2  .   ? 17.53300  28.80400  6.18900   1.000 107.05717 ? 2   NAG G O6    1 
HETATM 4470 O  O7    . NAG E 2  .   ? 21.06600  22.95600  7.27400   1.000 108.71965 ? 2   NAG G O7    1 
HETATM 4471 C  C1    . NAG F 4  .   ? -11.40600 16.49500  -25.96200 1.000 44.99045  ? 1   NAG H C1    1 
HETATM 4472 C  C2    . NAG F 4  .   ? -12.09300 15.53100  -26.92500 1.000 45.19536  ? 1   NAG H C2    1 
HETATM 4473 C  C3    . NAG F 4  .   ? -12.69800 16.30300  -28.08400 1.000 45.90071  ? 1   NAG H C3    1 
HETATM 4474 C  C4    . NAG F 4  .   ? -13.61200 17.38300  -27.53900 1.000 45.97654  ? 1   NAG H C4    1 
HETATM 4475 C  C5    . NAG F 4  .   ? -12.79100 18.33700  -26.67800 1.000 49.32026  ? 1   NAG H C5    1 
HETATM 4476 C  C6    . NAG F 4  .   ? -13.60700 19.40600  -26.01000 1.000 55.87410  ? 1   NAG H C6    1 
HETATM 4477 C  C7    . NAG F 4  .   ? -11.24000 13.21900  -27.26500 1.000 44.90134  ? 1   NAG H C7    1 
HETATM 4478 C  C8    . NAG F 4  .   ? -12.23400 12.69400  -26.27700 1.000 50.88685  ? 1   NAG H C8    1 
HETATM 4479 N  N2    . NAG F 4  .   ? -11.16000 14.54100  -27.41300 1.000 45.19955  ? 1   NAG H N2    1 
HETATM 4480 O  O3    . NAG F 4  .   ? -13.40900 15.42600  -28.94100 1.000 46.10499  ? 1   NAG H O3    1 
HETATM 4481 O  O4    . NAG F 4  .   ? -14.18600 18.06000  -28.64800 1.000 46.67227  ? 1   NAG H O4    1 
HETATM 4482 O  O5    . NAG F 4  .   ? -12.19500 17.60900  -25.59100 1.000 55.43430  ? 1   NAG H O5    1 
HETATM 4483 O  O6    . NAG F 4  .   ? -14.58100 18.79100  -25.19000 1.000 68.05068  ? 1   NAG H O6    1 
HETATM 4484 O  O7    . NAG F 4  .   ? -10.51300 12.46900  -27.90300 1.000 54.76053  ? 1   NAG H O7    1 
HETATM 4485 H  H1    . NAG F 4  .   ? -10.55900 16.80400  -26.35700 1.000 53.22304  ? 1   NAG H H1    1 
HETATM 4486 H  H2    . NAG F 4  .   ? -12.84000 15.11700  -26.44000 1.000 53.46892  ? 1   NAG H H2    1 
HETATM 4487 H  H3    . NAG F 4  .   ? -11.96300 16.73200  -28.59200 1.000 54.31534  ? 1   NAG H H3    1 
HETATM 4488 H  H4    . NAG F 4  .   ? -14.32300 16.96900  -26.98900 1.000 54.40634  ? 1   NAG H H4    1 
HETATM 4489 H  H5    . NAG F 4  .   ? -12.08400 18.74900  -27.22800 1.000 59.33741  ? 1   NAG H H5    1 
HETATM 4490 H  H61   . NAG F 4  .   ? -14.04100 19.96800  -26.68100 1.000 67.20202  ? 1   NAG H H61   1 
HETATM 4491 H  H62   . NAG F 4  .   ? -13.02400 19.96900  -25.46200 1.000 67.20202  ? 1   NAG H H62   1 
HETATM 4492 H  H81   . NAG F 4  .   ? -13.13400 12.88600  -26.58600 1.000 61.21732  ? 1   NAG H H81   1 
HETATM 4493 H  H82   . NAG F 4  .   ? -12.09100 13.11800  -25.41500 1.000 61.21732  ? 1   NAG H H82   1 
HETATM 4494 H  H83   . NAG F 4  .   ? -12.12300 11.73400  -26.18500 1.000 61.21732  ? 1   NAG H H83   1 
HETATM 4495 H  HN2   . NAG F 4  .   ? -10.46100 14.83200  -27.85000 1.000 53.47396  ? 1   NAG H HN2   1 
HETATM 4496 H  HO3   . NAG F 4  .   ? -14.21500 15.66200  -28.93000 1.000 54.56048  ? 1   NAG H HO3   1 
HETATM 4497 C  C1    . NAG F 4  .   ? -15.49300 18.51700  -28.55900 1.000 46.86504  ? 2   NAG H C1    1 
HETATM 4498 C  C2    . NAG F 4  .   ? -15.87800 19.21700  -29.86000 1.000 47.95057  ? 2   NAG H C2    1 
HETATM 4499 C  C3    . NAG F 4  .   ? -17.30300 19.73400  -29.74400 1.000 47.92732  ? 2   NAG H C3    1 
HETATM 4500 C  C4    . NAG F 4  .   ? -18.23500 18.61700  -29.30600 1.000 48.23344  ? 2   NAG H C4    1 
HETATM 4501 C  C5    . NAG F 4  .   ? -17.71100 17.95500  -28.03900 1.000 46.77924  ? 2   NAG H C5    1 
HETATM 4502 C  C6    . NAG F 4  .   ? -18.54600 16.78300  -27.59300 1.000 51.69637  ? 2   NAG H C6    1 
HETATM 4503 C  C7    . NAG F 4  .   ? -13.79900 20.17000  -30.75900 1.000 48.25857  ? 2   NAG H C7    1 
HETATM 4504 C  C8    . NAG F 4  .   ? -12.91000 21.36900  -30.68300 1.000 48.66984  ? 2   NAG H C8    1 
HETATM 4505 N  N2    . NAG F 4  .   ? -15.00700 20.31400  -30.22000 1.000 48.11429  ? 2   NAG H N2    1 
HETATM 4506 O  O3    . NAG F 4  .   ? -17.70000 20.27200  -30.99400 1.000 48.66321  ? 2   NAG H O3    1 
HETATM 4507 O  O4    . NAG F 4  .   ? -19.52600 19.14300  -29.02800 1.000 47.82740  ? 2   NAG H O4    1 
HETATM 4508 O  O5    . NAG F 4  .   ? -16.39200 17.45700  -28.30700 1.000 46.56253  ? 2   NAG H O5    1 
HETATM 4509 O  O6    . NAG F 4  .   ? -18.40500 15.69600  -28.48400 1.000 48.99032  ? 2   NAG H O6    1 
HETATM 4510 O  O7    . NAG F 4  .   ? -13.43300 19.12500  -31.28100 1.000 48.14014  ? 2   NAG H O7    1 
HETATM 4511 H  H1    . NAG F 4  .   ? -15.56400 19.17000  -27.82700 1.000 55.47254  ? 2   NAG H H1    1 
HETATM 4512 H  H2    . NAG F 4  .   ? -15.86200 18.54400  -30.58000 1.000 57.69378  ? 2   NAG H H2    1 
HETATM 4513 H  H3    . NAG F 4  .   ? -17.32000 20.45100  -29.05900 1.000 56.74728  ? 2   NAG H H3    1 
HETATM 4514 H  H4    . NAG F 4  .   ? -18.30200 17.94100  -30.02600 1.000 58.03323  ? 2   NAG H H4    1 
HETATM 4515 H  H5    . NAG F 4  .   ? -17.66700 18.62600  -27.31600 1.000 55.36958  ? 2   NAG H H5    1 
HETATM 4516 H  H61   . NAG F 4  .   ? -19.48800 17.04600  -27.54700 1.000 62.18875  ? 2   NAG H H61   1 
HETATM 4517 H  H62   . NAG F 4  .   ? -18.26400 16.50500  -26.70000 1.000 62.18875  ? 2   NAG H H62   1 
HETATM 4518 H  H81   . NAG F 4  .   ? -12.82200 21.64800  -29.75700 1.000 57.63830  ? 2   NAG H H81   1 
HETATM 4519 H  H82   . NAG F 4  .   ? -13.29600 22.09300  -31.20200 1.000 57.63830  ? 2   NAG H H82   1 
HETATM 4520 H  H83   . NAG F 4  .   ? -12.03400 21.14700  -31.03800 1.000 57.63830  ? 2   NAG H H83   1 
HETATM 4521 H  HN2   . NAG F 4  .   ? -15.29000 21.12800  -30.07000 1.000 56.97164  ? 2   NAG H HN2   1 
HETATM 4522 H  HO3   . NAG F 4  .   ? -18.45700 19.95800  -31.18000 1.000 57.63034  ? 2   NAG H HO3   1 
HETATM 4523 H  HO6   . NAG F 4  .   ? -17.71500 15.81400  -28.96200 1.000 58.94148  ? 2   NAG H HO6   1 
HETATM 4524 C  C1    . BMA F 4  .   ? -20.62000 18.67500  -29.75000 1.000 48.19390  ? 3   BMA H C1    1 
HETATM 4525 C  C2    . BMA F 4  .   ? -21.84700 18.60500  -28.89700 1.000 48.17132  ? 3   BMA H C2    1 
HETATM 4526 C  C3    . BMA F 4  .   ? -23.06700 18.30100  -29.72600 1.000 48.72532  ? 3   BMA H C3    1 
HETATM 4527 C  C4    . BMA F 4  .   ? -23.17600 19.25900  -30.88300 1.000 49.42316  ? 3   BMA H C4    1 
HETATM 4528 C  C5    . BMA F 4  .   ? -21.88300 19.27600  -31.66800 1.000 49.37216  ? 3   BMA H C5    1 
HETATM 4529 C  C6    . BMA F 4  .   ? -21.87400 20.33800  -32.71800 1.000 50.09038  ? 3   BMA H C6    1 
HETATM 4530 O  O2    . BMA F 4  .   ? -22.02000 19.82800  -28.19100 1.000 48.33382  ? 3   BMA H O2    1 
HETATM 4531 O  O3    . BMA F 4  .   ? -24.23000 18.43300  -28.93000 1.000 59.18951  ? 3   BMA H O3    1 
HETATM 4532 O  O4    . BMA F 4  .   ? -24.23100 18.86000  -31.73900 1.000 49.92482  ? 3   BMA H O4    1 
HETATM 4533 O  O5    . BMA F 4  .   ? -20.79600 19.59300  -30.80900 1.000 51.63887  ? 3   BMA H O5    1 
HETATM 4534 O  O6    . BMA F 4  .   ? -22.16500 21.60600  -32.12600 1.000 50.36995  ? 3   BMA H O6    1 
HETATM 4535 H  H1    . BMA F 4  .   ? -20.41800 17.78200  -30.12300 1.000 57.06718  ? 3   BMA H H1    1 
HETATM 4536 H  H2    . BMA F 4  .   ? -21.71700 17.87700  -28.24600 1.000 57.76894  ? 3   BMA H H2    1 
HETATM 4537 H  H3    . BMA F 4  .   ? -23.00600 17.37600  -30.07200 1.000 57.70488  ? 3   BMA H H3    1 
HETATM 4538 H  H4    . BMA F 4  .   ? -23.36600 20.15900  -30.53200 1.000 58.54229  ? 3   BMA H H4    1 
HETATM 4539 H  H5    . BMA F 4  .   ? -21.73500 18.39200  -32.08000 1.000 58.48109  ? 3   BMA H H5    1 
HETATM 4540 H  H61   . BMA F 4  .   ? -22.54200 20.12600  -33.40100 1.000 59.34294  ? 3   BMA H H61   1 
HETATM 4541 H  H62   . BMA F 4  .   ? -20.99400 20.37200  -33.14500 1.000 59.34294  ? 3   BMA H H62   1 
HETATM 4542 H  HO2   . BMA F 4  .   ? -22.83300 19.91600  -27.99500 1.000 57.23508  ? 3   BMA H HO2   1 
HETATM 4543 H  HO4   . BMA F 4  .   ? -24.10400 18.06400  -31.97200 1.000 59.14428  ? 3   BMA H HO4   1 
HETATM 4544 C  C1    . MAN F 4  .   ? -24.81600 17.24500  -28.51600 1.000 58.95282  ? 4   MAN H C1    1 
HETATM 4545 C  C2    . MAN F 4  .   ? -26.18600 17.61900  -28.04800 1.000 66.35391  ? 4   MAN H C2    1 
HETATM 4546 C  C3    . MAN F 4  .   ? -26.10900 18.51200  -26.83100 1.000 59.41813  ? 4   MAN H C3    1 
HETATM 4547 C  C4    . MAN F 4  .   ? -25.21800 17.91600  -25.75700 1.000 61.66843  ? 4   MAN H C4    1 
HETATM 4548 C  C5    . MAN F 4  .   ? -23.88600 17.45900  -26.32100 1.000 51.87138  ? 4   MAN H C5    1 
HETATM 4549 C  C6    . MAN F 4  .   ? -23.08700 16.64200  -25.34300 1.000 63.05238  ? 4   MAN H C6    1 
HETATM 4550 O  O2    . MAN F 4  .   ? -26.94600 16.44400  -27.78600 1.000 73.43839  ? 4   MAN H O2    1 
HETATM 4551 O  O3    . MAN F 4  .   ? -27.42200 18.70900  -26.32200 1.000 69.79751  ? 4   MAN H O3    1 
HETATM 4552 O  O4    . MAN F 4  .   ? -24.95900 18.90800  -24.77900 1.000 61.05844  ? 4   MAN H O4    1 
HETATM 4553 O  O5    . MAN F 4  .   ? -24.09300 16.62000  -27.46400 1.000 52.67990  ? 4   MAN H O5    1 
HETATM 4554 O  O6    . MAN F 4  .   ? -21.76400 16.44400  -25.81900 1.000 70.13196  ? 4   MAN H O6    1 
HETATM 4555 H  H1    . MAN F 4  .   ? -24.87900 16.62200  -29.28100 1.000 70.89649  ? 4   MAN H H1    1 
HETATM 4556 H  H2    . MAN F 4  .   ? -26.62100 18.12000  -28.77800 1.000 79.77779  ? 4   MAN H H2    1 
HETATM 4557 H  H3    . MAN F 4  .   ? -25.73800 19.39000  -27.09800 1.000 71.45486  ? 4   MAN H H3    1 
HETATM 4558 H  H4    . MAN F 4  .   ? -25.67600 17.15100  -25.33800 1.000 74.15521  ? 4   MAN H H4    1 
HETATM 4559 H  H5    . MAN F 4  .   ? -23.36200 18.24900  -26.57900 1.000 62.39876  ? 4   MAN H H5    1 
HETATM 4560 H  H61   . MAN F 4  .   ? -23.52000 15.77400  -25.21500 1.000 75.81596  ? 4   MAN H H61   1 
HETATM 4561 H  H62   . MAN F 4  .   ? -23.05600 17.10100  -24.48000 1.000 75.81596  ? 4   MAN H H62   1 
HETATM 4562 H  HO2   . MAN F 4  .   ? -27.41900 16.57200  -27.10300 1.000 88.27917  ? 4   MAN H HO2   1 
HETATM 4563 H  HO3   . MAN F 4  .   ? -27.47600 18.34300  -25.56800 1.000 83.91011  ? 4   MAN H HO3   1 
HETATM 4564 H  HO4   . MAN F 4  .   ? -24.45300 19.49200  -25.10900 1.000 73.42324  ? 4   MAN H HO4   1 
HETATM 4565 H  HO6   . MAN F 4  .   ? -21.77100 16.43600  -26.66600 1.000 84.31146  ? 4   MAN H HO6   1 
HETATM 4566 C  C1    . MAN F 4  .   ? -22.27900 22.70500  -32.99600 1.000 53.86440  ? 5   MAN H C1    1 
HETATM 4567 C  C2    . MAN F 4  .   ? -22.59300 23.92900  -32.17400 1.000 59.69395  ? 5   MAN H C2    1 
HETATM 4568 C  C3    . MAN F 4  .   ? -24.00000 23.89700  -31.62000 1.000 68.95816  ? 5   MAN H C3    1 
HETATM 4569 C  C4    . MAN F 4  .   ? -25.00500 23.61900  -32.71400 1.000 61.40344  ? 5   MAN H C4    1 
HETATM 4570 C  C5    . MAN F 4  .   ? -24.61400 22.36100  -33.46900 1.000 62.93059  ? 5   MAN H C5    1 
HETATM 4571 C  C6    . MAN F 4  .   ? -25.49500 22.08700  -34.66100 1.000 52.35314  ? 5   MAN H C6    1 
HETATM 4572 O  O2    . MAN F 4  .   ? -22.39100 25.09500  -32.96400 1.000 54.21605  ? 5   MAN H O2    1 
HETATM 4573 O  O3    . MAN F 4  .   ? -24.29900 25.14200  -31.00100 1.000 65.02192  ? 5   MAN H O3    1 
HETATM 4574 O  O4    . MAN F 4  .   ? -26.28700 23.44700  -32.13200 1.000 63.66436  ? 5   MAN H O4    1 
HETATM 4575 O  O5    . MAN F 4  .   ? -23.28800 22.51400  -33.98600 1.000 52.97860  ? 5   MAN H O5    1 
HETATM 4576 O  O6    . MAN F 4  .   ? -25.17700 22.96100  -35.73400 1.000 58.60844  ? 5   MAN H O6    1 
HETATM 4577 H  H1    . MAN F 4  .   ? -21.41700 22.86000  -33.46000 1.000 64.79038  ? 5   MAN H H1    1 
HETATM 4578 H  H2    . MAN F 4  .   ? -21.96000 23.94600  -31.41800 1.000 71.78584  ? 5   MAN H H2    1 
HETATM 4579 H  H3    . MAN F 4  .   ? -24.06200 23.17700  -30.94200 1.000 82.90289  ? 5   MAN H H3    1 
HETATM 4580 H  H4    . MAN F 4  .   ? -25.02600 24.38100  -33.33700 1.000 73.83722  ? 5   MAN H H4    1 
HETATM 4581 H  H5    . MAN F 4  .   ? -24.64400 21.59000  -32.85400 1.000 75.66981  ? 5   MAN H H5    1 
HETATM 4582 H  H61   . MAN F 4  .   ? -26.43300 22.20600  -34.41100 1.000 62.05826  ? 5   MAN H H61   1 
HETATM 4583 H  H62   . MAN F 4  .   ? -25.37000 21.16000  -34.95000 1.000 62.05826  ? 5   MAN H H62   1 
HETATM 4584 H  HO2   . MAN F 4  .   ? -22.95500 25.67700  -32.74100 1.000 65.21237  ? 5   MAN H HO2   1 
HETATM 4585 H  HO3   . MAN F 4  .   ? -24.90800 25.51900  -31.43900 1.000 78.17941  ? 5   MAN H HO3   1 
HETATM 4586 H  HO4   . MAN F 4  .   ? -26.30300 22.71400  -31.72300 1.000 76.55033  ? 5   MAN H HO4   1 
HETATM 4587 H  HO6   . MAN F 4  .   ? -24.45600 23.37000  -35.55900 1.000 70.48323  ? 5   MAN H HO6   1 
HETATM 4588 C  C1    . FUC F 4  .   ? -15.66600 19.60800  -24.85900 1.000 95.16969  ? 6   FUC H C1    1 
HETATM 4589 C  C2    . FUC F 4  .   ? -16.62400 18.77100  -24.05400 1.000 87.05000  ? 6   FUC H C2    1 
HETATM 4590 C  C3    . FUC F 4  .   ? -16.07000 18.41900  -22.68800 1.000 94.24105  ? 6   FUC H C3    1 
HETATM 4591 C  C4    . FUC F 4  .   ? -15.53400 19.64500  -21.97100 1.000 98.09900  ? 6   FUC H C4    1 
HETATM 4592 C  C5    . FUC F 4  .   ? -14.55300 20.37600  -22.87500 1.000 94.17091  ? 6   FUC H C5    1 
HETATM 4593 C  C6    . FUC F 4  .   ? -14.03400 21.66100  -22.28100 1.000 92.66673  ? 6   FUC H C6    1 
HETATM 4594 O  O2    . FUC F 4  .   ? -16.92900 17.58200  -24.77100 1.000 84.38145  ? 6   FUC H O2    1 
HETATM 4595 O  O3    . FUC F 4  .   ? -17.10100 17.81700  -21.91200 1.000 83.34715  ? 6   FUC H O3    1 
HETATM 4596 O  O4    . FUC F 4  .   ? -16.60300 20.51500  -21.61800 1.000 116.81177 ? 6   FUC H O4    1 
HETATM 4597 O  O5    . FUC F 4  .   ? -15.21800 20.73300  -24.10600 1.000 95.51786  ? 6   FUC H O5    1 
HETATM 4598 H  H1    . FUC F 4  .   ? -16.11500 19.92800  -25.68100 1.000 114.35673 ? 6   FUC H H1    1 
HETATM 4599 H  H2    . FUC F 4  .   ? -17.45300 19.29100  -23.93600 1.000 104.61311 ? 6   FUC H H2    1 
HETATM 4600 H  H3    . FUC F 4  .   ? -15.33200 17.76900  -22.80000 1.000 113.24236 ? 6   FUC H H3    1 
HETATM 4601 H  H4    . FUC F 4  .   ? -15.06300 19.36000  -21.15400 1.000 117.87191 ? 6   FUC H H4    1 
HETATM 4602 H  H5    . FUC F 4  .   ? -13.78800 19.78000  -23.06800 1.000 113.15819 ? 6   FUC H H5    1 
HETATM 4603 H  H61   . FUC F 4  .   ? -14.66100 22.37800  -22.46600 1.000 111.35318 ? 6   FUC H H61   1 
HETATM 4604 H  H62   . FUC F 4  .   ? -13.17300 21.87400  -22.67300 1.000 111.35318 ? 6   FUC H H62   1 
HETATM 4605 H  H63   . FUC F 4  .   ? -13.93600 21.55600  -21.32100 1.000 111.35318 ? 6   FUC H H63   1 
HETATM 4606 H  HO2   . FUC F 4  .   ? -16.43400 17.54100  -25.45100 1.000 101.41084 ? 6   FUC H HO2   1 
HETATM 4607 H  HO3   . FUC F 4  .   ? -17.62600 18.42200  -21.65700 1.000 100.16968 ? 6   FUC H HO3   1 
HETATM 4608 H  HO4   . FUC F 4  .   ? -16.82400 20.97500  -22.28600 1.000 140.32723 ? 6   FUC H HO4   1 
HETATM 4609 C  C2    . BGC G 5  .   ? 33.33800  -2.51000  44.55100  1.000 120.92400 ? 1   BGC D C2    1 
HETATM 4610 C  C3    . BGC G 5  .   ? 32.25300  -1.61300  45.11300  1.000 112.73084 ? 1   BGC D C3    1 
HETATM 4611 C  C4    . BGC G 5  .   ? 30.96500  -1.72200  44.31400  1.000 110.98689 ? 1   BGC D C4    1 
HETATM 4612 C  C5    . BGC G 5  .   ? 30.57600  -3.17400  44.08300  1.000 110.92845 ? 1   BGC D C5    1 
HETATM 4613 C  C6    . BGC G 5  .   ? 29.40200  -3.30900  43.14600  1.000 105.04475 ? 1   BGC D C6    1 
HETATM 4614 C  C1    . BGC G 5  .   ? 32.84200  -3.90900  44.27400  1.000 127.69149 ? 1   BGC D C1    1 
HETATM 4615 O  O1    . BGC G 5  .   ? 33.84400  -4.61800  43.61800  1.000 114.38935 ? 1   BGC D O1    1 
HETATM 4616 O  O2    . BGC G 5  .   ? 34.44300  -2.56400  45.45100  1.000 122.94671 ? 1   BGC D O2    1 
HETATM 4617 O  O3    . BGC G 5  .   ? 32.72200  -0.26600  45.09500  1.000 97.67054  ? 1   BGC D O3    1 
HETATM 4618 O  O4    . BGC G 5  .   ? 29.91400  -1.08600  45.02900  1.000 115.24552 ? 1   BGC D O4    1 
HETATM 4619 O  O5    . BGC G 5  .   ? 31.66900  -3.86800  43.46600  1.000 118.68109 ? 1   BGC D O5    1 
HETATM 4620 O  O6    . BGC G 5  .   ? 29.70000  -2.73100  41.88200  1.000 109.34699 ? 1   BGC D O6    1 
HETATM 4621 C  C1    . GAL G 5  .   ? 29.77400  -1.45100  46.36300  1.000 105.41118 ? 2   GAL D C1    1 
HETATM 4622 C  C2    . GAL G 5  .   ? 29.72800  -0.21900  47.24200  1.000 104.33098 ? 2   GAL D C2    1 
HETATM 4623 C  C3    . GAL G 5  .   ? 29.50000  -0.62200  48.67900  1.000 95.27513  ? 2   GAL D C3    1 
HETATM 4624 C  C4    . GAL G 5  .   ? 28.21800  -1.42100  48.76600  1.000 86.87262  ? 2   GAL D C4    1 
HETATM 4625 C  C5    . GAL G 5  .   ? 28.34100  -2.64500  47.88500  1.000 92.15784  ? 2   GAL D C5    1 
HETATM 4626 C  C6    . GAL G 5  .   ? 27.07800  -3.47500  47.86300  1.000 91.48884  ? 2   GAL D C6    1 
HETATM 4627 O  O2    . GAL G 5  .   ? 30.92200  0.54400   47.11200  1.000 97.96316  ? 2   GAL D O2    1 
HETATM 4628 O  O3    . GAL G 5  .   ? 29.45100  0.54500   49.49300  1.000 82.72911  ? 2   GAL D O3    1 
HETATM 4629 O  O4    . GAL G 5  .   ? 27.12800  -0.64400  48.28100  1.000 85.71088  ? 2   GAL D O4    1 
HETATM 4630 O  O5    . GAL G 5  .   ? 28.58600  -2.22300  46.52800  1.000 96.77052  ? 2   GAL D O5    1 
HETATM 4631 O  O6    . GAL G 5  .   ? 26.30500  -3.21900  46.69200  1.000 106.69572 ? 2   GAL D O6    1 
HETATM 4632 C  C1    . GLA G 5  .   ? 25.99500  -0.41200  49.05500  1.000 72.62383  ? 3   GLA D C1    1 
HETATM 4633 C  C2    . GLA G 5  .   ? 24.91100  0.17600   48.17000  1.000 75.26243  ? 3   GLA D C2    1 
HETATM 4634 C  C3    . GLA G 5  .   ? 25.27300  1.57300   47.70500  1.000 72.64055  ? 3   GLA D C3    1 
HETATM 4635 C  C4    . GLA G 5  .   ? 25.61200  2.44000   48.89400  1.000 65.23819  ? 3   GLA D C4    1 
HETATM 4636 C  C5    . GLA G 5  .   ? 26.72300  1.78700   49.69200  1.000 74.41654  ? 3   GLA D C5    1 
HETATM 4637 C  C6    . GLA G 5  .   ? 27.09100  2.57400   50.92800  1.000 62.72297  ? 3   GLA D C6    1 
HETATM 4638 O  O2    . GLA G 5  .   ? 24.65000  -0.68600  47.06300  1.000 73.22438  ? 3   GLA D O2    1 
HETATM 4639 O  O3    . GLA G 5  .   ? 24.17800  2.14300   46.99500  1.000 68.03978  ? 3   GLA D O3    1 
HETATM 4640 O  O4    . GLA G 5  .   ? 24.47300  2.57400   49.73000  1.000 42.04420  ? 3   GLA D O4    1 
HETATM 4641 O  O5    . GLA G 5  .   ? 26.28400  0.48600   50.13000  1.000 77.25845  ? 3   GLA D O5    1 
HETATM 4642 O  O6    . GLA G 5  .   ? 27.33600  1.71800   52.03500  1.000 78.83765  ? 3   GLA D O6    1 
HETATM 4643 C  C1    . NGA G 5  .   ? 24.80700  3.12200   45.83400  1.000 60.27596  ? 4   NGA D C1    1 
HETATM 4644 C  C2    . NGA G 5  .   ? 23.49000  3.19300   45.06900  1.000 63.83258  ? 4   NGA D C2    1 
HETATM 4645 C  C3    . NGA G 5  .   ? 23.49000  4.36800   44.10100  1.000 58.78633  ? 4   NGA D C3    1 
HETATM 4646 C  C4    . NGA G 5  .   ? 23.88200  5.66300   44.79500  1.000 56.16524  ? 4   NGA D C4    1 
HETATM 4647 C  C5    . NGA G 5  .   ? 25.17000  5.46000   45.57700  1.000 52.55623  ? 4   NGA D C5    1 
HETATM 4648 C  C6    . NGA G 5  .   ? 25.52400  6.66000   46.41600  1.000 40.19602  ? 4   NGA D C6    1 
HETATM 4649 C  C7    . NGA G 5  .   ? 22.18900  1.19300   44.70600  1.000 71.20307  ? 4   NGA D C7    1 
HETATM 4650 C  C8    . NGA G 5  .   ? 22.06800  -0.11500  43.98500  1.000 52.50515  ? 4   NGA D C8    1 
HETATM 4651 N  N2    . NGA G 5  .   ? 23.22700  1.95800   44.36600  1.000 75.61771  ? 4   NGA D N2    1 
HETATM 4652 O  O3    . NGA G 5  .   ? 22.18300  4.46400   43.56500  1.000 56.53428  ? 4   NGA D O3    1 
HETATM 4653 O  O4    . NGA G 5  .   ? 22.85200  6.03100   45.70600  1.000 57.34252  ? 4   NGA D O4    1 
HETATM 4654 O  O5    . NGA G 5  .   ? 25.01100  4.35900   46.49000  1.000 65.08587  ? 4   NGA D O5    1 
HETATM 4655 O  O6    . NGA G 5  .   ? 26.78300  6.48200   47.02900  1.000 35.51480  ? 4   NGA D O6    1 
HETATM 4656 O  O7    . NGA G 5  .   ? 21.38500  1.55000   45.56000  1.000 60.56815  ? 4   NGA D O7    1 
HETATM 4657 C  C1    . GAL H 6  .   ? -0.57400  7.13000   10.61000  1.000 104.71199 ? 1   GAL I C1    1 
HETATM 4658 C  C2    . GAL H 6  .   ? -1.60400  8.26200   10.61400  1.000 114.89433 ? 1   GAL I C2    1 
HETATM 4659 C  C3    . GAL H 6  .   ? -2.98000  7.71900   10.34200  1.000 115.33072 ? 1   GAL I C3    1 
HETATM 4660 C  C4    . GAL H 6  .   ? -2.98800  7.27300   8.89500   1.000 109.94834 ? 1   GAL I C4    1 
HETATM 4661 C  C5    . GAL H 6  .   ? -1.91300  6.19600   8.68200   1.000 106.00019 ? 1   GAL I C5    1 
HETATM 4662 C  C6    . GAL H 6  .   ? -1.46900  6.08500   7.22900   1.000 107.40631 ? 1   GAL I C6    1 
HETATM 4663 O  O2    . GAL H 6  .   ? -1.65000  8.96000   11.85800  1.000 123.45679 ? 1   GAL I O2    1 
HETATM 4664 O  O3    . GAL H 6  .   ? -3.95800  8.73600   10.49900  1.000 121.42657 ? 1   GAL I O3    1 
HETATM 4665 O  O4    . GAL H 6  .   ? -2.69300  8.38300   8.04500   1.000 117.02956 ? 1   GAL I O4    1 
HETATM 4666 O  O5    . GAL H 6  .   ? -0.63500  6.39400   9.38600   1.000 114.05047 ? 1   GAL I O5    1 
HETATM 4667 O  O6    . GAL H 6  .   ? -0.12300  5.63300   7.16100   1.000 110.24307 ? 1   GAL I O6    1 
HETATM 4668 C  C1    . GLA H 6  .   ? -3.77700  8.67000   7.14200   1.000 106.91530 ? 2   GLA I C1    1 
HETATM 4669 C  C2    . GLA H 6  .   ? -3.25100  9.40100   5.90700   1.000 105.37035 ? 2   GLA I C2    1 
HETATM 4670 C  C3    . GLA H 6  .   ? -2.82300  10.78700  6.26200   1.000 96.90521  ? 2   GLA I C3    1 
HETATM 4671 C  C4    . GLA H 6  .   ? -3.94800  11.53800  6.91500   1.000 94.02640  ? 2   GLA I C4    1 
HETATM 4672 C  C5    . GLA H 6  .   ? -4.43100  10.82300  8.18900   1.000 96.06837  ? 2   GLA I C5    1 
HETATM 4673 C  C6    . GLA H 6  .   ? -5.59600  11.53900  8.82000   1.000 92.37803  ? 2   GLA I C6    1 
HETATM 4674 O  O2    . GLA H 6  .   ? -2.16400  8.63800   5.33100   1.000 89.64524  ? 2   GLA I O2    1 
HETATM 4675 O  O3    . GLA H 6  .   ? -2.39800  11.44500  5.04700   1.000 99.41404  ? 2   GLA I O3    1 
HETATM 4676 O  O4    . GLA H 6  .   ? -5.04500  11.64100  6.01100   1.000 93.30643  ? 2   GLA I O4    1 
HETATM 4677 O  O5    . GLA H 6  .   ? -4.84400  9.43800   7.87900   1.000 90.88179  ? 2   GLA I O5    1 
HETATM 4678 O  O6    . GLA H 6  .   ? -5.81800  10.97800  10.10100  1.000 94.80847  ? 2   GLA I O6    1 
HETATM 4679 C  C1    . NGA H 6  .   ? -1.27800  12.26400  5.20400   1.000 82.91175  ? 3   NGA I C1    1 
HETATM 4680 C  C2    . NGA H 6  .   ? -0.38900  12.30800  3.96300   1.000 80.75032  ? 3   NGA I C2    1 
HETATM 4681 C  C3    . NGA H 6  .   ? 0.81400   13.20200  4.24000   1.000 73.72499  ? 3   NGA I C3    1 
HETATM 4682 C  C4    . NGA H 6  .   ? 0.37200   14.56600  4.74500   1.000 67.93199  ? 3   NGA I C4    1 
HETATM 4683 C  C5    . NGA H 6  .   ? -0.53400  14.39100  5.95500   1.000 74.11788  ? 3   NGA I C5    1 
HETATM 4684 C  C6    . NGA H 6  .   ? -1.10300  15.69300  6.46100   1.000 66.54636  ? 3   NGA I C6    1 
HETATM 4685 C  C7    . NGA H 6  .   ? -0.58200  10.25400  2.64000   1.000 72.11688  ? 3   NGA I C7    1 
HETATM 4686 C  C8    . NGA H 6  .   ? -0.04300  8.87600   2.42200   1.000 69.31509  ? 3   NGA I C8    1 
HETATM 4687 N  N2    . NGA H 6  .   ? 0.04100   10.98400  3.56300   1.000 80.05977  ? 3   NGA I N2    1 
HETATM 4688 O  O3    . NGA H 6  .   ? 1.59400   13.31900  3.06100   1.000 68.45578  ? 3   NGA I O3    1 
HETATM 4689 O  O4    . NGA H 6  .   ? -0.37400  15.22900  3.73000   1.000 69.15944  ? 3   NGA I O4    1 
HETATM 4690 O  O5    . NGA H 6  .   ? -1.65600  13.58000  5.56600   1.000 81.35553  ? 3   NGA I O5    1 
HETATM 4691 O  O6    . NGA H 6  .   ? -1.60800  15.55000  7.78600   1.000 60.38403  ? 3   NGA I O6    1 
HETATM 4692 O  O7    . NGA H 6  .   ? -1.54500  10.67800  2.01300   1.000 61.40266  ? 3   NGA I O7    1 
HETATM 4693 MN MN    . MN  I 7  .   ? 21.61567  -2.14482  37.64890  1.000 39.06434  ? 401 MN  A MN    1 
HETATM 4694 N  N1    . UDP J 8  .   ? 22.43867  3.00687   31.78064  1.000 29.66437  ? 402 UDP A N1    1 
HETATM 4695 C  C2    . UDP J 8  .   ? 21.99666  3.81191   30.74968  1.000 37.48593  ? 402 UDP A C2    1 
HETATM 4696 N  N3    . UDP J 8  .   ? 22.99065  4.40174   30.01952  1.000 34.97574  ? 402 UDP A N3    1 
HETATM 4697 C  C4    . UDP J 8  .   ? 24.34866  4.28053   30.21934  1.000 37.34972  ? 402 UDP A C4    1 
HETATM 4698 C  C5    . UDP J 8  .   ? 24.72767  3.42250   31.30231  1.000 26.97547  ? 402 UDP A C5    1 
HETATM 4699 C  C6    . UDP J 8  .   ? 23.77468  2.83067   32.03346  1.000 33.50597  ? 402 UDP A C6    1 
HETATM 4700 O  O2    . UDP J 8  .   ? 20.81565  3.99309   30.50184  1.000 39.55017  ? 402 UDP A O2    1 
HETATM 4701 O  O4    . UDP J 8  .   ? 25.11565  4.86039   29.45922  1.000 38.94215  ? 402 UDP A O4    1 
HETATM 4702 C  "C1'" . UDP J 8  .   ? 21.41768  2.34606   32.60180  1.000 28.06796  ? 402 UDP A "C1'" 1 
HETATM 4703 C  "C2'" . UDP J 8  .   ? 21.55645  0.82704   32.60983  1.000 32.48612  ? 402 UDP A "C2'" 1 
HETATM 4704 O  "O2'" . UDP J 8  .   ? 20.99220  0.25509   31.45292  1.000 35.46796  ? 402 UDP A "O2'" 1 
HETATM 4705 C  "C3'" . UDP J 8  .   ? 20.75157  0.51020   33.87095  1.000 39.95728  ? 402 UDP A "C3'" 1 
HETATM 4706 C  "C4'" . UDP J 8  .   ? 21.12088  1.67217   34.80986  1.000 42.58976  ? 402 UDP A "C4'" 1 
HETATM 4707 O  "O4'" . UDP J 8  .   ? 21.60293  2.73207   33.94276  1.000 32.39740  ? 402 UDP A "O4'" 1 
HETATM 4708 O  "O3'" . UDP J 8  .   ? 19.36653  0.50441   33.56114  1.000 25.62082  ? 402 UDP A "O3'" 1 
HETATM 4709 C  "C5'" . UDP J 8  .   ? 22.14898  1.37504   35.87473  1.000 31.20788  ? 402 UDP A "C5'" 1 
HETATM 4710 O  "O5'" . UDP J 8  .   ? 23.38583  0.94883   35.26357  1.000 38.05565  ? 402 UDP A "O5'" 1 
HETATM 4711 P  PA    . UDP J 8  .   ? 24.08368  -0.41427  35.72351  1.000 40.08375  ? 402 UDP A PA    1 
HETATM 4712 O  O1A   . UDP J 8  .   ? 25.21251  -0.71347  34.80337  1.000 41.88151  ? 402 UDP A O1A   1 
HETATM 4713 O  O2A   . UDP J 8  .   ? 23.04354  -1.46910  35.88169  1.000 41.98737  ? 402 UDP A O2A   1 
HETATM 4714 O  O3A   . UDP J 8  .   ? 24.70394  -0.00133  37.14541  1.000 40.86999  ? 402 UDP A O3A   1 
HETATM 4715 P  PB    . UDP J 8  .   ? 24.29513  -0.16322  38.70048  1.000 56.47889  ? 402 UDP A PB    1 
HETATM 4716 O  O1B   . UDP J 8  .   ? 25.49715  -0.67438  39.41933  1.000 78.75857  ? 402 UDP A O1B   1 
HETATM 4717 O  O2B   . UDP J 8  .   ? 23.87641  1.19786   39.15049  1.000 53.68802  ? 402 UDP A O2B   1 
HETATM 4718 O  O3B   . UDP J 8  .   ? 23.15198  -1.14704  38.70666  1.000 43.78847  ? 402 UDP A O3B   1 
HETATM 4719 C  C1    . B3P K 9  .   ? 23.59949  21.02632  53.36796  1.000 31.26056  ? 403 B3P A C1    1 
HETATM 4720 C  C2    . B3P K 9  .   ? 23.36922  19.51835  53.14103  1.000 28.43237  ? 403 B3P A C2    1 
HETATM 4721 C  C3    . B3P K 9  .   ? 23.14845  21.81736  52.13100  1.000 31.78994  ? 403 B3P A C3    1 
HETATM 4722 N  N1    . B3P K 9  .   ? 21.69549  21.99959  52.20919  1.000 26.16381  ? 403 B3P A N1    1 
HETATM 4723 C  C4    . B3P K 9  .   ? 21.08647  22.82065  51.14325  1.000 35.24943  ? 403 B3P A C4    1 
HETATM 4724 C  C5    . B3P K 9  .   ? 21.47872  24.28959  51.30315  1.000 27.91686  ? 403 B3P A C5    1 
HETATM 4725 C  C6    . B3P K 9  .   ? 19.58946  22.60589  51.33246  1.000 28.23181  ? 403 B3P A C6    1 
HETATM 4726 C  C7    . B3P K 9  .   ? 21.52621  22.43754  49.72420  1.000 34.16964  ? 403 B3P A C7    1 
HETATM 4727 N  N2    . B3P K 9  .   ? 21.97122  19.20958  53.48823  1.000 28.61711  ? 403 B3P A N2    1 
HETATM 4728 C  C8    . B3P K 9  .   ? 21.47395  17.89465  53.03734  1.000 31.98603  ? 403 B3P A C8    1 
HETATM 4729 C  C9    . B3P K 9  .   ? 20.12602  17.68788  53.73953  1.000 25.10521  ? 403 B3P A C9    1 
HETATM 4730 C  C10   . B3P K 9  .   ? 22.44683  16.77550  53.40624  1.000 27.41333  ? 403 B3P A C10   1 
HETATM 4731 C  C11   . B3P K 9  .   ? 21.27874  17.87663  51.53237  1.000 30.77942  ? 403 B3P A C11   1 
HETATM 4732 O  O1    . B3P K 9  .   ? 19.65278  16.39895  53.49464  1.000 36.67492  ? 403 B3P A O1    1 
HETATM 4733 O  O2    . B3P K 9  .   ? 22.62002  16.77252  54.79421  1.000 31.24125  ? 403 B3P A O2    1 
HETATM 4734 O  O3    . B3P K 9  .   ? 20.56987  19.01773  51.15543  1.000 31.68584  ? 403 B3P A O3    1 
HETATM 4735 O  O4    . B3P K 9  .   ? 21.12897  24.76069  52.57519  1.000 31.77827  ? 403 B3P A O4    1 
HETATM 4736 O  O5    . B3P K 9  .   ? 18.83347  23.41099  50.47454  1.000 37.82891  ? 403 B3P A O5    1 
HETATM 4737 O  O6    . B3P K 9  .   ? 21.29996  21.07857  49.47527  1.000 27.92072  ? 403 B3P A O6    1 
HETATM 4738 H  H11   . B3P K 9  .   ? 24.53554  21.19318  53.53682  1.000 37.66577  ? 403 B3P A H11   1 
HETATM 4739 H  H12   . B3P K 9  .   ? 23.07764  21.31243  54.13202  1.000 37.66577  ? 403 B3P A H12   1 
HETATM 4740 H  H21   . B3P K 9  .   ? 23.98122  19.02327  53.70696  1.000 34.27194  ? 403 B3P A H21   1 
HETATM 4741 H  H22   . B3P K 9  .   ? 23.54506  19.30630  52.21201  1.000 34.27194  ? 403 B3P A H22   1 
HETATM 4742 H  H31   . B3P K 9  .   ? 23.59858  22.67428  52.10891  1.000 38.30103  ? 403 B3P A H31   1 
HETATM 4743 H  H32   . B3P K 9  .   ? 23.37926  21.30430  51.34298  1.000 38.30103  ? 403 B3P A H32   1 
HETATM 4744 H  HN1   . B3P K 9  .   ? 21.48265  22.34464  53.00021  1.000 31.02030  ? 403 B3P A HN1   1 
HETATM 4745 H  H51   . B3P K 9  .   ? 22.43672  24.37344  51.18802  1.000 33.65333  ? 403 B3P A H51   1 
HETATM 4746 H  H52   . B3P K 9  .   ? 21.03771  24.82064  50.62120  1.000 33.65333  ? 403 B3P A H52   1 
HETATM 4747 H  H61   . B3P K 9  .   ? 19.35962  22.80596  52.25149  1.000 34.03128  ? 403 B3P A H61   1 
HETATM 4748 H  H62   . B3P K 9  .   ? 19.38229  21.67692  51.16152  1.000 34.03128  ? 403 B3P A H62   1 
HETATM 4749 H  H71   . B3P K 9  .   ? 21.02521  22.96160  49.08326  1.000 41.15667  ? 403 B3P A H71   1 
HETATM 4750 H  H72   . B3P K 9  .   ? 22.46823  22.63839  49.61207  1.000 41.15667  ? 403 B3P A H72   1 
HETATM 4751 H  HN2   . B3P K 9  .   ? 21.86336  19.28562  54.36625  1.000 34.49363  ? 403 B3P A HN2   1 
HETATM 4752 H  H91   . B3P K 9  .   ? 19.48707  18.33097  53.40260  1.000 30.27936  ? 403 B3P A H91   1 
HETATM 4753 H  H92   . B3P K 9  .   ? 20.22817  17.82789  54.69351  1.000 30.27936  ? 403 B3P A H92   1 
HETATM 4754 H  H101  . B3P K 9  .   ? 22.10165  15.91855  53.11131  1.000 33.04910  ? 403 B3P A H101  1 
HETATM 4755 H  H102  . B3P K 9  .   ? 23.29579  16.92636  52.96912  1.000 33.04910  ? 403 B3P A H102  1 
HETATM 4756 H  H111  . B3P K 9  .   ? 22.14369  17.90948  51.10625  1.000 37.08841  ? 403 B3P A H111  1 
HETATM 4757 H  H112  . B3P K 9  .   ? 20.81458  17.07270  51.25446  1.000 37.08841  ? 403 B3P A H112  1 
HETATM 4758 H  HO1   . B3P K 9  .   ? 19.88279  15.87093  54.11762  1.000 44.16300  ? 403 B3P A HO1   1 
HETATM 4759 H  HO2   . B3P K 9  .   ? 23.30797  16.30741  54.98913  1.000 37.64260  ? 403 B3P A HO2   1 
HETATM 4760 H  HO3   . B3P K 9  .   ? 19.75183  18.83086  51.03755  1.000 38.17611  ? 403 B3P A HO3   1 
HETATM 4761 H  HO4   . B3P K 9  .   ? 20.32201  25.02681  52.57329  1.000 38.28703  ? 403 B3P A HO4   1 
HETATM 4762 H  HO5   . B3P K 9  .   ? 18.68964  24.16502  50.83354  1.000 45.54779  ? 403 B3P A HO5   1 
HETATM 4763 H  HO6   . B3P K 9  .   ? 21.92194  20.61048  49.81820  1.000 33.65797  ? 403 B3P A HO6   1 
HETATM 4764 C  C1    . PEG L 10 .   ? 10.66434  14.61227  16.16093  1.000 67.58062  ? 404 PEG A C1    1 
HETATM 4765 O  O1    . PEG L 10 .   ? 10.23515  14.55130  14.81199  1.000 73.24882  ? 404 PEG A O1    1 
HETATM 4766 C  C2    . PEG L 10 .   ? 9.52450   14.75848  17.11608  1.000 57.09978  ? 404 PEG A C2    1 
HETATM 4767 O  O2    . PEG L 10 .   ? 8.72031   13.58661  17.09323  1.000 67.47314  ? 404 PEG A O2    1 
HETATM 4768 C  C3    . PEG L 10 .   ? 9.48414   12.39349  17.21816  1.000 62.14341  ? 404 PEG A C3    1 
HETATM 4769 C  C4    . PEG L 10 .   ? 8.59094   11.20063  17.13231  1.000 61.64807  ? 404 PEG A C4    1 
HETATM 4770 O  O4    . PEG L 10 .   ? 9.22068   10.10451  16.50926  1.000 54.35208  ? 404 PEG A O4    1 
HETATM 4771 C  C1    . PEG M 10 .   ? 2.82191   -12.81088 37.06481  1.000 61.91691  ? 405 PEG A C1    1 
HETATM 4772 O  O1    . PEG M 10 .   ? 3.82682   -12.58007 36.10166  1.000 74.47305  ? 405 PEG A O1    1 
HETATM 4773 C  C2    . PEG M 10 .   ? 3.16119   -12.22190 38.39375  1.000 62.29824  ? 405 PEG A C2    1 
HETATM 4774 O  O2    . PEG M 10 .   ? 1.96734   -11.90269 39.09590  1.000 62.21470  ? 405 PEG A O2    1 
HETATM 4775 C  C3    . PEG M 10 .   ? 1.98445   -12.36065 40.44191  1.000 48.21068  ? 405 PEG A C3    1 
HETATM 4776 C  C4    . PEG M 10 .   ? 1.10570   -11.49449 41.28001  1.000 52.66735  ? 405 PEG A C4    1 
HETATM 4777 O  O4    . PEG M 10 .   ? 1.77994   -10.98156 42.40590  1.000 56.44172  ? 405 PEG A O4    1 
HETATM 4778 C  C1    . GAL N 11 .   ? 22.17100  3.87400   41.45300  0.764 52.81925  ? 406 GAL A C1    1 
HETATM 4779 C  C2    . GAL N 11 .   ? 21.18300  3.06700   40.61900  0.764 40.26177  ? 406 GAL A C2    1 
HETATM 4780 C  C3    . GAL N 11 .   ? 21.01500  3.64300   39.24400  0.764 39.66873  ? 406 GAL A C3    1 
HETATM 4781 C  C4    . GAL N 11 .   ? 21.21500  5.13200   39.31600  0.764 44.50660  ? 406 GAL A C4    1 
HETATM 4782 C  C5    . GAL N 11 .   ? 22.64900  5.43800   39.57200  0.764 43.20170  ? 406 GAL A C5    1 
HETATM 4783 C  C6    . GAL N 11 .   ? 22.88600  6.90100   39.85600  0.764 39.61402  ? 406 GAL A C6    1 
HETATM 4784 O  O2    . GAL N 11 .   ? 21.58400  1.70200   40.57000  0.764 45.50252  ? 406 GAL A O2    1 
HETATM 4785 O  O3    . GAL N 11 .   ? 19.70400  3.36000   38.77400  0.764 41.64558  ? 406 GAL A O3    1 
HETATM 4786 O  O4    . GAL N 11 .   ? 20.46200  5.65700   40.40400  0.764 34.29121  ? 406 GAL A O4    1 
HETATM 4787 O  O5    . GAL N 11 .   ? 23.07800  4.73500   40.74200  0.764 50.29611  ? 406 GAL A O5    1 
HETATM 4788 O  O6    . GAL N 11 .   ? 22.94300  7.67000   38.65900  0.764 29.18732  ? 406 GAL A O6    1 
HETATM 4789 MN MN    . MN  O 7  .   ? 6.39420   6.57618   0.93096   1.000 59.88135  ? 401 MN  B MN    1 
HETATM 4790 N  N1    . UDP P 8  .   ? 12.07120  11.78516  0.87691   1.000 62.91474  ? 402 UDP B N1    1 
HETATM 4791 C  C2    . UDP P 8  .   ? 13.22502  12.37426  0.38860   1.000 68.46748  ? 402 UDP B C2    1 
HETATM 4792 N  N3    . UDP P 8  .   ? 14.06138  12.87805  1.34439   1.000 70.45627  ? 402 UDP B N3    1 
HETATM 4793 C  C4    . UDP P 8  .   ? 13.87589  12.86277  2.70946   1.000 71.48885  ? 402 UDP B C4    1 
HETATM 4794 C  C5    . UDP P 8  .   ? 12.66305  12.23569  3.13978   1.000 68.89664  ? 402 UDP B C5    1 
HETATM 4795 C  C6    . UDP P 8  .   ? 11.82271  11.73188  2.22499   1.000 65.84451  ? 402 UDP B C6    1 
HETATM 4796 O  O2    . UDP P 8  .   ? 13.49758  12.45350  -0.79949  1.000 66.27266  ? 402 UDP B O2    1 
HETATM 4797 O  O4    . UDP P 8  .   ? 14.72917  13.36362  3.43824   1.000 84.02184  ? 402 UDP B O4    1 
HETATM 4798 C  "C1'" . UDP P 8  .   ? 11.11784  11.20337  -0.08985  1.000 64.50229  ? 402 UDP B "C1'" 1 
HETATM 4799 C  "C2'" . UDP P 8  .   ? 10.94990  9.69733   0.09990   1.000 67.07657  ? 402 UDP B "C2'" 1 
HETATM 4800 O  "O2'" . UDP P 8  .   ? 11.89959  9.04249   -0.70860  1.000 60.20182  ? 402 UDP B "O2'" 1 
HETATM 4801 C  "C3'" . UDP P 8  .   ? 9.51572   9.50544   -0.38661  1.000 61.59337  ? 402 UDP B "C3'" 1 
HETATM 4802 C  "C4'" . UDP P 8  .   ? 8.82893   10.77033  0.15691   1.000 59.25304  ? 402 UDP B "C4'" 1 
HETATM 4803 O  "O4'" . UDP P 8  .   ? 9.85292   11.79333  0.11474   1.000 64.81730  ? 402 UDP B "O4'" 1 
HETATM 4804 O  "O3'" . UDP P 8  .   ? 9.49018   9.45973   -1.80361  1.000 63.29528  ? 402 UDP B "O3'" 1 
HETATM 4805 C  "C5'" . UDP P 8  .   ? 8.27945   10.71504  1.56011   1.000 56.19916  ? 402 UDP B "C5'" 1 
HETATM 4806 O  "O5'" . UDP P 8  .   ? 7.90157   9.36197   1.88597   1.000 77.48310  ? 402 UDP B "O5'" 1 
HETATM 4807 P  PA    . UDP P 8  .   ? 8.63099   8.49673   3.01652   1.000 63.86479  ? 402 UDP B PA    1 
HETATM 4808 O  O1A   . UDP P 8  .   ? 9.81919   9.21962   3.54522   1.000 70.09287  ? 402 UDP B O1A   1 
HETATM 4809 O  O2A   . UDP P 8  .   ? 8.83079   7.11084   2.51215   1.000 63.86217  ? 402 UDP B O2A   1 
HETATM 4810 O  O3A   . UDP P 8  .   ? 7.48741   8.49251   4.12894   1.000 62.00621  ? 402 UDP B O3A   1 
HETATM 4811 P  PB    . UDP P 8  .   ? 5.89737   8.28953   4.04950   1.000 77.38734  ? 402 UDP B PB    1 
HETATM 4812 O  O1B   . UDP P 8  .   ? 5.34903   9.31973   3.10592   1.000 71.55457  ? 402 UDP B O1B   1 
HETATM 4813 O  O2B   . UDP P 8  .   ? 5.70318   6.89164   3.54428   1.000 63.97566  ? 402 UDP B O2B   1 
HETATM 4814 O  O3B   . UDP P 8  .   ? 5.40290   8.47724   5.45372   1.000 80.97784  ? 402 UDP B O3B   1 
HETATM 4815 C  C1    . B3P Q 9  .   ? -8.91265  29.82212  6.36354   1.000 57.81492  ? 403 B3P B C1    1 
HETATM 4816 C  C2    . B3P Q 9  .   ? -8.76182  28.31921  5.93817   1.000 52.43165  ? 403 B3P B C2    1 
HETATM 4817 C  C3    . B3P Q 9  .   ? -8.72810  30.80737  5.16167   1.000 56.94001  ? 403 B3P B C3    1 
HETATM 4818 N  N1    . B3P Q 9  .   ? -7.40532  30.54549  4.58312   1.000 60.91671  ? 403 B3P B N1    1 
HETATM 4819 C  C4    . B3P Q 9  .   ? -7.05075  31.38273  3.41216   1.000 63.81693  ? 403 B3P B C4    1 
HETATM 4820 C  C5    . B3P Q 9  .   ? -5.59388  31.03579  3.08154   1.000 73.66181  ? 403 B3P B C5    1 
HETATM 4821 C  C6    . B3P Q 9  .   ? -7.09161  32.87066  3.76849   1.000 63.73232  ? 403 B3P B C6    1 
HETATM 4822 C  C7    . B3P Q 9  .   ? -7.89522  31.11699  2.16842   1.000 61.52708  ? 403 B3P B C7    1 
HETATM 4823 N  N2    . B3P Q 9  .   ? -9.62326  28.06046  4.76044   1.000 56.83331  ? 403 B3P B N2    1 
HETATM 4824 C  C8    . B3P Q 9  .   ? -9.14357  26.90363  3.96202   1.000 55.59179  ? 403 B3P B C8    1 
HETATM 4825 C  C9    . B3P Q 9  .   ? -9.04123  25.66543  4.87472   1.000 63.75829  ? 403 B3P B C9    1 
HETATM 4826 C  C10   . B3P Q 9  .   ? -10.19297 26.57885  2.89334   1.000 53.82010  ? 403 B3P B C10   1 
HETATM 4827 C  C11   . B3P Q 9  .   ? -7.82581  27.34375  3.31461   1.000 48.88302  ? 403 B3P B C11   1 
HETATM 4828 O  O1    . B3P Q 9  .   ? -10.25096 25.61829  5.60016   1.000 47.56492  ? 403 B3P B O1    1 
HETATM 4829 O  O2    . B3P Q 9  .   ? -9.92619  25.31697  2.32198   1.000 50.90279  ? 403 B3P B O2    1 
HETATM 4830 O  O3    . B3P Q 9  .   ? -7.12899  26.22685  2.85412   1.000 68.27724  ? 403 B3P B O3    1 
HETATM 4831 O  O4    . B3P Q 9  .   ? -5.46993  29.64182  2.95721   1.000 66.79922  ? 403 B3P B O4    1 
HETATM 4832 O  O5    . B3P Q 9  .   ? -8.37668  33.39370  3.58308   1.000 67.39357  ? 403 B3P B O5    1 
HETATM 4833 O  O6    . B3P Q 9  .   ? -7.36959  31.99119  1.18741   1.000 69.54646  ? 403 B3P B O6    1 
HETATM 4834 H  H11   . B3P Q 9  .   ? -8.24140  30.02398  7.03533   1.000 69.53101  ? 403 B3P B H11   1 
HETATM 4835 H  H12   . B3P Q 9  .   ? -9.79151  29.95605  6.74589   1.000 69.53101  ? 403 B3P B H12   1 
HETATM 4836 H  H21   . B3P Q 9  .   ? -9.03655  27.74506  6.67215   1.000 63.07108  ? 403 B3P B H21   1 
HETATM 4837 H  H22   . B3P Q 9  .   ? -7.83691  28.13125  5.71378   1.000 63.07108  ? 403 B3P B H22   1 
HETATM 4838 H  H31   . B3P Q 9  .   ? -9.41635  30.65352  4.49590   1.000 68.48111  ? 403 B3P B H31   1 
HETATM 4839 H  H32   . B3P Q 9  .   ? -8.78498  31.72531  5.46888   1.000 68.48111  ? 403 B3P B H32   1 
HETATM 4840 H  HN1   . B3P Q 9  .   ? -6.80508  30.71835  5.21793   1.000 73.25316  ? 403 B3P B HN1   1 
HETATM 4841 H  H51   . B3P Q 9  .   ? -5.33919  31.45996  2.24454   1.000 88.54727  ? 403 B3P B H51   1 
HETATM 4842 H  H52   . B3P Q 9  .   ? -5.01261  31.34864  3.79439   1.000 88.54727  ? 403 B3P B H52   1 
HETATM 4843 H  H61   . B3P Q 9  .   ? -6.46882  33.35177  3.19835   1.000 76.63188  ? 403 B3P B H61   1 
HETATM 4844 H  H62   . B3P Q 9  .   ? -6.83226  32.98346  4.69641   1.000 76.63188  ? 403 B3P B H62   1 
HETATM 4845 H  H71   . B3P Q 9  .   ? -7.81133  30.19105  1.88620   1.000 73.98560  ? 403 B3P B H71   1 
HETATM 4846 H  H72   . B3P Q 9  .   ? -8.82816  31.32096  2.33882   1.000 73.98560  ? 403 B3P B H72   1 
HETATM 4847 H  HN2   . B3P Q 9  .   ? -9.60846  28.78257  4.23958   1.000 68.35307  ? 403 B3P B HN2   1 
HETATM 4848 H  H91   . B3P Q 9  .   ? -8.28901  25.75231  5.47846   1.000 76.66305  ? 403 B3P B H91   1 
HETATM 4849 H  H92   . B3P Q 9  .   ? -8.93944  24.86254  4.34151   1.000 76.66305  ? 403 B3P B H92   1 
HETATM 4850 H  H101  . B3P Q 9  .   ? -11.07282 26.56477  3.30367   1.000 64.73722  ? 403 B3P B H101  1 
HETATM 4851 H  H102  . B3P Q 9  .   ? -10.16423 27.25800  2.20247   1.000 64.73722  ? 403 B3P B H102  1 
HETATM 4852 H  H111  . B3P Q 9  .   ? -8.01809  27.92991  2.56881   1.000 58.81272  ? 403 B3P B H111  1 
HETATM 4853 H  H112  . B3P Q 9  .   ? -7.28856  27.80961  3.97151   1.000 58.81272  ? 403 B3P B H112  1 
HETATM 4854 H  HO1   . B3P Q 9  .   ? -10.07365 25.53812  6.42808   1.000 57.23100  ? 403 B3P B HO1   1 
HETATM 4855 H  HO2   . B3P Q 9  .   ? -10.54712 24.77293  2.52210   1.000 61.23645  ? 403 B3P B HO2   1 
HETATM 4856 H  HO3   . B3P Q 9  .   ? -6.48579  26.04973  3.37784   1.000 82.08579  ? 403 B3P B HO3   1 
HETATM 4857 H  HO4   . B3P Q 9  .   ? -5.38324  29.43999  2.13613   1.000 80.31217  ? 403 B3P B HO4   1 
HETATM 4858 H  HO5   . B3P Q 9  .   ? -8.33488  34.03981  3.03520   1.000 81.02538  ? 403 B3P B HO5   1 
HETATM 4859 H  HO6   . B3P Q 9  .   ? -7.96967  32.55424  0.95975   1.000 83.60885  ? 403 B3P B HO6   1 
HETATM 4860 O  O     . HOH R 12 .   ? 17.08700  19.66700  48.22500  1.000 39.53326  ? 501 HOH A O     1 
HETATM 4861 O  O     . HOH R 12 .   ? 20.35200  -0.80700  37.45300  1.000 43.56597  ? 502 HOH A O     1 
HETATM 4862 O  O     . HOH R 12 .   ? 11.72700  3.46700   56.20000  1.000 45.18838  ? 503 HOH A O     1 
HETATM 4863 O  O     . HOH R 12 .   ? 14.04000  2.52400   45.01800  1.000 24.29920  ? 504 HOH A O     1 
HETATM 4864 O  O     . HOH R 12 .   ? 19.76800  21.66600  47.56900  1.000 40.58074  ? 505 HOH A O     1 
HETATM 4865 O  O     . HOH R 12 .   ? 21.03900  -3.71900  32.37600  1.000 34.47045  ? 506 HOH A O     1 
HETATM 4866 O  O     . HOH R 12 .   ? 14.84400  13.89800  49.94400  1.000 27.80403  ? 507 HOH A O     1 
HETATM 4867 O  O     . HOH R 12 .   ? 18.52000  -7.73200  32.13800  1.000 31.86816  ? 508 HOH A O     1 
HETATM 4868 O  O     . HOH R 12 .   ? 16.82400  -13.45000 41.40000  1.000 30.11770  ? 509 HOH A O     1 
HETATM 4869 O  O     . HOH R 12 .   ? 28.47100  8.53400   46.56100  1.000 23.04491  ? 510 HOH A O     1 
HETATM 4870 O  O     . HOH R 12 .   ? 7.41000   -1.83700  51.08800  1.000 33.31320  ? 511 HOH A O     1 
HETATM 4871 O  O     . HOH R 12 .   ? 26.12400  6.07200   49.60500  1.000 37.71039  ? 512 HOH A O     1 
HETATM 4872 O  O     . HOH R 12 .   ? 24.35700  -1.39200  32.33600  1.000 44.07729  ? 513 HOH A O     1 
HETATM 4873 O  O     . HOH R 12 .   ? 25.44700  7.87100   37.65400  1.000 44.85672  ? 514 HOH A O     1 
HETATM 4874 O  O     . HOH R 12 .   ? 15.86600  2.62400   27.63100  1.000 34.38556  ? 515 HOH A O     1 
HETATM 4875 O  O     . HOH R 12 .   ? 12.33600  13.87500  51.11900  1.000 25.02797  ? 516 HOH A O     1 
HETATM 4876 O  O     . HOH R 12 .   ? 18.07300  -17.80200 39.56000  1.000 34.11328  ? 517 HOH A O     1 
HETATM 4877 O  O     . HOH R 12 .   ? 24.30400  12.22300  35.63000  1.000 36.62488  ? 518 HOH A O     1 
HETATM 4878 O  O     . HOH R 12 .   ? 5.32800   10.08100  49.47800  1.000 34.10571  ? 519 HOH A O     1 
HETATM 4879 O  O     . HOH R 12 .   ? 18.62000  7.48200   34.70800  1.000 37.00442  ? 520 HOH A O     1 
HETATM 4880 O  O     . HOH R 12 .   ? 32.06100  13.06000  52.98400  1.000 33.73895  ? 521 HOH A O     1 
HETATM 4881 O  O     . HOH R 12 .   ? 3.81000   -6.44200  34.11600  1.000 37.30438  ? 522 HOH A O     1 
HETATM 4882 O  O     . HOH R 12 .   ? 20.27600  9.51600   52.51500  1.000 31.79149  ? 523 HOH A O     1 
HETATM 4883 O  O     . HOH R 12 .   ? 4.78300   -7.90500  36.16600  1.000 34.98042  ? 524 HOH A O     1 
HETATM 4884 O  O     . HOH R 12 .   ? 22.77600  8.28200   30.27900  1.000 28.13936  ? 525 HOH A O     1 
HETATM 4885 O  O     . HOH R 12 .   ? 20.88300  4.37300   54.74600  1.000 42.63243  ? 526 HOH A O     1 
HETATM 4886 O  O     . HOH R 12 .   ? 15.40100  9.12300   44.44300  1.000 21.58274  ? 527 HOH A O     1 
HETATM 4887 O  O     . HOH R 12 .   ? 9.22200   18.01400  54.83200  1.000 61.42148  ? 528 HOH A O     1 
HETATM 4888 O  O     . HOH R 12 .   ? 3.12100   -7.12900  31.52900  1.000 40.37167  ? 529 HOH A O     1 
HETATM 4889 O  O     . HOH R 12 .   ? 2.71600   -17.66800 39.38600  1.000 38.40350  ? 530 HOH A O     1 
HETATM 4890 O  O     . HOH R 12 .   ? 22.09500  -6.49200  23.40200  1.000 37.53544  ? 531 HOH A O     1 
HETATM 4891 O  O     . HOH R 12 .   ? 14.92900  0.65800   53.24300  1.000 35.66601  ? 532 HOH A O     1 
HETATM 4892 O  O     . HOH R 12 .   ? 28.29100  18.53100  55.68400  1.000 36.43444  ? 533 HOH A O     1 
HETATM 4893 O  O     . HOH R 12 .   ? 26.32700  20.97600  42.50200  1.000 30.06349  ? 534 HOH A O     1 
HETATM 4894 O  O     . HOH R 12 .   ? 15.34100  16.41700  54.55700  1.000 33.77005  ? 535 HOH A O     1 
HETATM 4895 O  O     . HOH R 12 .   ? 8.93000   0.53300   50.29000  1.000 31.65044  ? 536 HOH A O     1 
HETATM 4896 O  O     . HOH R 12 .   ? 38.85600  3.85200   45.30000  1.000 46.26796  ? 537 HOH A O     1 
HETATM 4897 O  O     . HOH R 12 .   ? 29.00900  21.65600  44.74900  1.000 34.64067  ? 538 HOH A O     1 
HETATM 4898 O  O     . HOH R 12 .   ? 25.52300  16.66100  55.46600  1.000 31.86081  ? 539 HOH A O     1 
HETATM 4899 O  O     . HOH R 12 .   ? 27.93500  17.71200  41.02100  1.000 30.09148  ? 540 HOH A O     1 
HETATM 4900 O  O     . HOH R 12 .   ? 12.63800  0.59500   51.80200  1.000 25.72796  ? 541 HOH A O     1 
HETATM 4901 O  O     . HOH R 12 .   ? 18.48400  -11.19400 41.99200  1.000 23.56424  ? 542 HOH A O     1 
HETATM 4902 O  O     . HOH R 12 .   ? 11.56800  -5.68300  16.44400  1.000 49.39578  ? 543 HOH A O     1 
HETATM 4903 O  O     . HOH R 12 .   ? 20.80400  -12.66200 36.35500  1.000 26.82022  ? 544 HOH A O     1 
HETATM 4904 O  O     . HOH R 12 .   ? 30.03800  8.05600   31.94700  1.000 37.14274  ? 545 HOH A O     1 
HETATM 4905 O  O     . HOH R 12 .   ? 20.94500  25.75500  44.93800  1.000 30.03502  ? 546 HOH A O     1 
HETATM 4906 O  O     . HOH R 12 .   ? -1.26700  12.65200  38.40500  1.000 38.92036  ? 547 HOH A O     1 
HETATM 4907 O  O     . HOH R 12 .   ? 35.71300  6.62900   39.71400  1.000 33.70184  ? 548 HOH A O     1 
HETATM 4908 O  O     . HOH R 12 .   ? 17.08500  -13.85000 49.07800  1.000 32.23616  ? 549 HOH A O     1 
HETATM 4909 O  O     . HOH R 12 .   ? 26.22600  5.18100   53.05900  1.000 37.47790  ? 550 HOH A O     1 
HETATM 4910 O  O     . HOH R 12 .   ? 16.08200  -10.83800 25.01900  1.000 35.79065  ? 551 HOH A O     1 
HETATM 4911 O  O     . HOH R 12 .   ? 10.99400  -2.04000  50.26300  1.000 29.61660  ? 552 HOH A O     1 
HETATM 4912 O  O     . HOH R 12 .   ? 32.98300  0.48700   42.23300  1.000 45.30593  ? 553 HOH A O     1 
HETATM 4913 O  O     . HOH R 12 .   ? 16.90600  16.18900  30.38000  1.000 36.73042  ? 554 HOH A O     1 
HETATM 4914 O  O     . HOH R 12 .   ? 6.54000   5.14700   55.62100  1.000 40.69803  ? 555 HOH A O     1 
HETATM 4915 O  O     . HOH R 12 .   ? 29.79500  15.88300  38.21200  1.000 32.21361  ? 556 HOH A O     1 
HETATM 4916 O  O     . HOH R 12 .   ? 11.86800  11.70200  53.53300  1.000 42.45889  ? 557 HOH A O     1 
HETATM 4917 O  O     . HOH R 12 .   ? 21.23200  -12.78200 29.33000  1.000 28.66811  ? 558 HOH A O     1 
HETATM 4918 O  O     . HOH R 12 .   ? 20.09900  -14.79200 42.99600  1.000 39.05945  ? 559 HOH A O     1 
HETATM 4919 O  O     . HOH R 12 .   ? 17.64100  -5.63400  48.84000  1.000 29.30251  ? 560 HOH A O     1 
HETATM 4920 O  O     . HOH R 12 .   ? 31.10200  22.21600  41.36400  1.000 34.57887  ? 561 HOH A O     1 
HETATM 4921 O  O     . HOH R 12 .   ? 20.05900  -16.33700 37.80500  1.000 40.87694  ? 562 HOH A O     1 
HETATM 4922 O  O     . HOH R 12 .   ? 5.00700   20.97200  25.83900  1.000 43.40056  ? 563 HOH A O     1 
HETATM 4923 O  O     . HOH R 12 .   ? 20.66400  -13.63200 46.80200  1.000 39.16338  ? 564 HOH A O     1 
HETATM 4924 O  O     . HOH R 12 .   ? 13.22500  -2.86200  51.82300  1.000 48.03742  ? 565 HOH A O     1 
HETATM 4925 O  O     . HOH R 12 .   ? 13.05000  15.61300  53.24900  1.000 35.20320  ? 566 HOH A O     1 
HETATM 4926 O  O     . HOH R 12 .   ? 21.51600  -11.84500 42.85600  1.000 35.24965  ? 567 HOH A O     1 
HETATM 4927 O  O     . HOH R 12 .   ? 15.95600  -1.01400  54.88300  1.000 34.57096  ? 568 HOH A O     1 
HETATM 4928 O  O     . HOH R 12 .   ? 27.21700  -4.79100  44.67200  1.000 65.14017  ? 569 HOH A O     1 
HETATM 4929 O  O     . HOH S 12 .   ? -0.97500  17.52300  9.76500   1.000 37.39795  ? 501 HOH B O     1 
HETATM 4930 O  O     . HOH S 12 .   ? -2.58000  11.79100  -5.21600  1.000 43.62125  ? 502 HOH B O     1 
HETATM 4931 O  O     . HOH S 12 .   ? -8.90800  18.26100  2.82600   1.000 43.39268  ? 503 HOH B O     1 
HETATM 4932 O  O     . HOH S 12 .   ? -8.68600  19.30200  -12.41100 1.000 43.04456  ? 504 HOH B O     1 
HETATM 4933 O  O     . HOH S 12 .   ? 0.78200   -8.61400  -17.47900 1.000 54.58729  ? 505 HOH B O     1 
HETATM 4934 O  O     . HOH S 12 .   ? -8.16100  14.42300  8.58800   1.000 46.86738  ? 506 HOH B O     1 
HETATM 4935 O  O     . HOH S 12 .   ? -4.20200  15.31600  7.97700   1.000 49.57429  ? 507 HOH B O     1 
HETATM 4936 O  O     . HOH S 12 .   ? -6.88000  14.04900  -18.79100 1.000 41.52488  ? 508 HOH B O     1 
HETATM 4937 O  O     . HOH S 12 .   ? -10.13700 8.31200   -17.62000 1.000 48.97037  ? 509 HOH B O     1 
HETATM 4938 O  O     . HOH S 12 .   ? -7.11400  -1.35400  -20.42700 1.000 45.24630  ? 510 HOH B O     1 
HETATM 4939 O  O     . HOH S 12 .   ? -1.90100  17.87800  -3.46400  1.000 39.16553  ? 511 HOH B O     1 
HETATM 4940 O  O     . HOH S 12 .   ? -7.85500  6.88000   -6.78600  1.000 38.25584  ? 512 HOH B O     1 
HETATM 4941 O  O     . HOH S 12 .   ? -4.53700  -11.27800 -5.20200  1.000 45.13834  ? 513 HOH B O     1 
HETATM 4942 O  O     . HOH S 12 .   ? -5.77900  3.37800   -0.68000  1.000 40.82955  ? 514 HOH B O     1 
HETATM 4943 O  O     . HOH S 12 .   ? 4.45600   12.63100  0.40500   1.000 49.83030  ? 515 HOH B O     1 
HETATM 4944 O  O     . HOH S 12 .   ? -4.94200  -3.17800  1.54000   1.000 48.94081  ? 516 HOH B O     1 
HETATM 4945 O  O     . HOH S 12 .   ? -18.68900 14.68900  -31.33200 1.000 47.53757  ? 517 HOH B O     1 
HETATM 4946 O  O     . HOH S 12 .   ? -25.40700 13.54000  -27.29500 1.000 51.76656  ? 518 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 12  ? 0.99679 0.64843 0.89858 -0.05675 0.04036  0.03177  42  GLY A N     
2    C  CA    . GLY A 12  ? 1.12897 0.78032 1.03153 -0.06497 0.04189  0.03405  42  GLY A CA    
3    C  C     . GLY A 12  ? 1.15001 0.81503 1.05856 -0.07641 0.05078  0.03658  42  GLY A C     
4    O  O     . GLY A 12  ? 1.28610 0.96569 1.20742 -0.07869 0.05631  0.03607  42  GLY A O     
5    N  N     . ASN A 13  ? 0.95079 0.61210 0.84979 -0.08281 0.05210  0.03914  43  ASN A N     
6    C  CA    . ASN A 13  ? 0.88663 0.56105 0.78820 -0.09339 0.05990  0.04197  43  ASN A CA    
7    C  C     . ASN A 13  ? 0.83925 0.53700 0.75831 -0.08892 0.06896  0.03856  43  ASN A C     
8    O  O     . ASN A 13  ? 0.76424 0.47793 0.69075 -0.09436 0.07588  0.03930  43  ASN A O     
9    C  CB    . ASN A 13  ? 0.94814 0.62458 0.84932 -0.10340 0.06064  0.04529  43  ASN A CB    
10   C  CG    . ASN A 13  ? 1.22294 0.87403 1.10638 -0.10763 0.05031  0.04845  43  ASN A CG    
11   O  OD1   . ASN A 13  ? 1.37377 1.00485 1.24059 -0.10707 0.04336  0.04977  43  ASN A OD1   
12   N  ND2   . ASN A 13  ? 1.12489 0.77560 1.01067 -0.11170 0.04871  0.04954  43  ASN A ND2   
13   N  N     . PHE A 14  ? 0.75904 0.45910 0.68379 -0.07924 0.06859  0.03494  44  PHE A N     
14   C  CA    . PHE A 14  ? 0.57081 0.28965 0.50972 -0.07535 0.07580  0.03186  44  PHE A CA    
15   C  C     . PHE A 14  ? 0.68692 0.40882 0.61940 -0.07945 0.07952  0.03309  44  PHE A C     
16   O  O     . PHE A 14  ? 0.85390 0.56319 0.77424 -0.07988 0.07546  0.03444  44  PHE A O     
17   C  CB    . PHE A 14  ? 0.51551 0.23617 0.46294 -0.06457 0.07332  0.02811  44  PHE A CB    
18   C  CG    . PHE A 14  ? 0.63347 0.35798 0.59112 -0.05920 0.07182  0.02630  44  PHE A CG    
19   C  CD1   . PHE A 14  ? 0.69838 0.40948 0.64882 -0.05636 0.06453  0.02692  44  PHE A CD1   
20   C  CD2   . PHE A 14  ? 0.55517 0.29595 0.52839 -0.05640 0.07732  0.02385  44  PHE A CD2   
21   C  CE1   . PHE A 14  ? 0.63300 0.34816 0.59226 -0.05051 0.06303  0.02513  44  PHE A CE1   
22   C  CE2   . PHE A 14  ? 0.53386 0.27862 0.51631 -0.05133 0.07610  0.02233  44  PHE A CE2   
23   C  CZ    . PHE A 14  ? 0.56779 0.30064 0.54382 -0.04828 0.06922  0.02297  44  PHE A CZ    
24   N  N     . LEU A 15  ? 0.71242 0.45116 0.65217 -0.08174 0.08701  0.03242  45  LEU A N     
25   C  CA    . LEU A 15  ? 0.66861 0.41247 0.60290 -0.08346 0.09077  0.03281  45  LEU A CA    
26   C  C     . LEU A 15  ? 0.61155 0.35637 0.55027 -0.07485 0.09037  0.02893  45  LEU A C     
27   O  O     . LEU A 15  ? 0.74952 0.48921 0.67966 -0.07452 0.08945  0.02927  45  LEU A O     
28   C  CB    . LEU A 15  ? 0.63247 0.39500 0.57134 -0.08772 0.09842  0.03321  45  LEU A CB    
29   C  CG    . LEU A 15  ? 0.68206 0.44806 0.61959 -0.09690 0.09932  0.03702  45  LEU A CG    
30   C  CD1   . LEU A 15  ? 0.63464 0.42227 0.57527 -0.10077 0.10714  0.03757  45  LEU A CD1   
31   C  CD2   . LEU A 15  ? 0.71032 0.45869 0.63205 -0.10516 0.09353  0.04221  45  LEU A CD2   
32   N  N     . LYS A 16  ? 0.63812 0.38923 0.58963 -0.06835 0.09071  0.02552  46  LYS A N     
33   C  CA    . LYS A 16  ? 0.56471 0.31636 0.52072 -0.06138 0.08926  0.02243  46  LYS A CA    
34   C  C     . LYS A 16  ? 0.62223 0.37147 0.58635 -0.05604 0.08476  0.02118  46  LYS A C     
35   O  O     . LYS A 16  ? 0.66946 0.42339 0.64159 -0.05543 0.08555  0.02086  46  LYS A O     
36   C  CB    . LYS A 16  ? 0.64639 0.41116 0.60936 -0.05882 0.09475  0.01950  46  LYS A CB    
37   C  CG    . LYS A 16  ? 0.71861 0.48820 0.67294 -0.06203 0.09909  0.02022  46  LYS A CG    
38   C  CD    . LYS A 16  ? 0.65879 0.44013 0.61790 -0.05752 0.10353  0.01662  46  LYS A CD    
39   C  CE    . LYS A 16  ? 0.76186 0.54801 0.71069 -0.05840 0.10692  0.01684  46  LYS A CE    
40   N  NZ    . LYS A 16  ? 0.81697 0.60924 0.76067 -0.06615 0.11024  0.02082  46  LYS A NZ    
41   N  N     . LEU A 17  ? 0.59739 0.34056 0.55930 -0.05197 0.07995  0.02055  47  LEU A N     
42   C  CA    . LEU A 17  ? 0.62232 0.36628 0.59156 -0.04621 0.07545  0.01952  47  LEU A CA    
43   C  C     . LEU A 17  ? 0.61103 0.36032 0.58568 -0.04275 0.07461  0.01774  47  LEU A C     
44   O  O     . LEU A 17  ? 0.74064 0.48472 0.70760 -0.04342 0.07328  0.01776  47  LEU A O     
45   C  CB    . LEU A 17  ? 0.58561 0.31715 0.54517 -0.04448 0.06878  0.02094  47  LEU A CB    
46   C  CG    . LEU A 17  ? 0.65154 0.37426 0.60456 -0.04680 0.06670  0.02276  47  LEU A CG    
47   C  CD1   . LEU A 17  ? 0.57016 0.27903 0.51159 -0.04299 0.05884  0.02334  47  LEU A CD1   
48   C  CD2   . LEU A 17  ? 0.53700 0.26806 0.50171 -0.04429 0.06800  0.02177  47  LEU A CD2   
49   N  N     . PRO A 18  ? 0.60580 0.36473 0.59274 -0.03946 0.07477  0.01647  48  PRO A N     
50   C  CA    . PRO A 18  ? 0.71816 0.48122 0.70931 -0.03760 0.07283  0.01551  48  PRO A CA    
51   C  C     . PRO A 18  ? 0.80816 0.56680 0.79455 -0.03542 0.06661  0.01638  48  PRO A C     
52   O  O     . PRO A 18  ? 0.69099 0.44789 0.67607 -0.03250 0.06301  0.01717  48  PRO A O     
53   C  CB    . PRO A 18  ? 0.55601 0.33013 0.56066 -0.03522 0.07359  0.01493  48  PRO A CB    
54   C  CG    . PRO A 18  ? 0.64978 0.42583 0.65745 -0.03568 0.07734  0.01482  48  PRO A CG    
55   C  CD    . PRO A 18  ? 0.60483 0.37074 0.60154 -0.03775 0.07622  0.01620  48  PRO A CD    
56   N  N     . ASP A 19  ? 0.97563 0.73256 0.95893 -0.03620 0.06486  0.01595  49  ASP A N     
57   C  CA    . ASP A 19  ? 1.00173 0.75621 0.98112 -0.03444 0.05890  0.01657  49  ASP A CA    
58   C  C     . ASP A 19  ? 0.96684 0.73363 0.95776 -0.03184 0.05560  0.01718  49  ASP A C     
59   O  O     . ASP A 19  ? 1.16536 0.93728 1.16060 -0.03328 0.05356  0.01743  49  ASP A O     
60   C  CB    . ASP A 19  ? 1.12966 0.87796 1.10162 -0.03659 0.05810  0.01591  49  ASP A CB    
61   C  CG    . ASP A 19  ? 1.37550 1.12241 1.34420 -0.03515 0.05165  0.01649  49  ASP A CG    
62   O  OD1   . ASP A 19  ? 1.23568 0.98879 1.20876 -0.03205 0.04788  0.01733  49  ASP A OD1   
63   O  OD2   . ASP A 19  ? 1.54611 1.28638 1.50740 -0.03658 0.05011  0.01594  49  ASP A OD2   
64   N  N     . THR A 20  ? 0.80830 0.57963 0.80320 -0.02814 0.05473  0.01763  50  THR A N     
65   C  CA    . THR A 20  ? 0.92018 0.70608 0.92616 -0.02479 0.05186  0.01848  50  THR A CA    
66   C  C     . THR A 20  ? 0.77003 0.55643 0.77257 -0.01853 0.04761  0.01862  50  THR A C     
67   O  O     . THR A 20  ? 0.85668 0.63120 0.85008 -0.01748 0.04789  0.01807  50  THR A O     
68   C  CB    . THR A 20  ? 0.88363 0.67835 0.90089 -0.02533 0.05607  0.01839  50  THR A CB    
69   O  OG1   . THR A 20  ? 0.89359 0.68224 0.90790 -0.02399 0.05892  0.01763  50  THR A OG1   
70   C  CG2   . THR A 20  ? 0.92518 0.71869 0.94446 -0.03029 0.05948  0.01780  50  THR A CG2   
71   N  N     . ASP A 21  ? 0.82331 0.62354 0.83234 -0.01447 0.04343  0.01948  51  ASP A N     
72   C  CA    . ASP A 21  ? 0.69797 0.50097 0.70313 -0.00634 0.03841  0.01915  51  ASP A CA    
73   C  C     . ASP A 21  ? 0.82729 0.65036 0.84518 -0.00151 0.03760  0.02001  51  ASP A C     
74   O  O     . ASP A 21  ? 0.95015 0.78972 0.97508 -0.00077 0.03474  0.02150  51  ASP A O     
75   C  CB    . ASP A 21  ? 0.97559 0.77713 0.97307 -0.00467 0.03302  0.01917  51  ASP A CB    
76   C  CG    . ASP A 21  ? 1.12787 0.93136 1.11890 0.00517  0.02709  0.01823  51  ASP A CG    
77   O  OD1   . ASP A 21  ? 0.98089 0.79811 0.97895 0.01154  0.02580  0.01828  51  ASP A OD1   
78   O  OD2   . ASP A 21  ? 1.15816 0.94906 1.13597 0.00721  0.02338  0.01727  51  ASP A OD2   
79   N  N     . CYS A 22  ? 0.73277 0.55533 0.75330 0.00170  0.03983  0.01931  52  CYS A N     
80   C  CA    . CYS A 22  ? 0.74651 0.58828 0.77915 0.00652  0.03968  0.02012  52  CYS A CA    
81   C  C     . CYS A 22  ? 0.74109 0.59493 0.77209 0.01668  0.03345  0.01998  52  CYS A C     
82   O  O     . CYS A 22  ? 0.85533 0.73046 0.89720 0.02047  0.03278  0.02133  52  CYS A O     
83   C  CB    . CYS A 22  ? 0.77143 0.60827 0.80631 0.00789  0.04335  0.01908  52  CYS A CB    
84   S  SG    . CYS A 22  ? 0.83947 0.66817 0.87832 -0.00232 0.05090  0.01901  52  CYS A SG    
85   N  N     . ARG A 23  ? 0.79619 0.63746 0.81316 0.02187  0.02873  0.01836  53  ARG A N     
86   C  CA    . ARG A 23  ? 0.90137 0.75495 0.91543 0.03290  0.02221  0.01772  53  ARG A CA    
87   C  C     . ARG A 23  ? 0.95762 0.83160 0.97968 0.03060  0.02042  0.01981  53  ARG A C     
88   O  O     . ARG A 23  ? 0.76167 0.65996 0.79216 0.03647  0.01803  0.02099  53  ARG A O     
89   C  CB    . ARG A 23  ? 0.93591 0.76836 0.93082 0.03884  0.01691  0.01529  53  ARG A CB    
90   C  CG    . ARG A 23  ? 1.02483 0.86610 1.01334 0.05326  0.00957  0.01352  53  ARG A CG    
91   C  CD    . ARG A 23  ? 1.24895 1.08120 1.22347 0.05663  0.00383  0.01221  53  ARG A CD    
92   N  NE    . ARG A 23  ? 1.39431 1.23926 1.37726 0.04895  0.00547  0.01422  53  ARG A NE    
93   C  CZ    . ARG A 23  ? 1.27187 1.10943 1.24542 0.04833  0.00208  0.01361  53  ARG A CZ    
94   N  NH1   . ARG A 23  ? 1.08069 0.89797 1.03562 0.05486  -0.00304 0.01111  53  ARG A NH1   
95   N  NH2   . ARG A 23  ? 1.27581 1.12530 1.25787 0.04075  0.00336  0.01563  53  ARG A NH2   
96   N  N     . GLN A 24  ? 1.00558 0.87081 1.02500 0.02173  0.02140  0.02055  54  GLN A N     
97   C  CA    . GLN A 24  ? 1.19451 1.07680 1.22075 0.01771  0.01919  0.02285  54  GLN A CA    
98   C  C     . GLN A 24  ? 1.10545 1.00874 1.14823 0.01228  0.02201  0.02606  54  GLN A C     
99   O  O     . GLN A 24  ? 1.04918 0.97756 1.10044 0.01456  0.01906  0.02838  54  GLN A O     
100  C  CB    . GLN A 24  ? 1.20247 1.06764 1.22150 0.00904  0.01980  0.02274  54  GLN A CB    
101  C  CG    . GLN A 24  ? 1.30522 1.18335 1.32732 0.00527  0.01584  0.02470  54  GLN A CG    
102  C  CD    . GLN A 24  ? 1.40350 1.28067 1.41490 0.01295  0.00981  0.02298  54  GLN A CD    
103  O  OE1   . GLN A 24  ? 1.37666 1.23591 1.37495 0.01904  0.00869  0.02020  54  GLN A OE1   
104  N  NE2   . GLN A 24  ? 1.17372 1.07009 1.18999 0.01234  0.00545  0.02481  54  GLN A NE2   
105  N  N     . THR A 25  ? 1.00275 0.89674 1.04976 0.00510  0.02758  0.02638  55  THR A N     
106  C  CA    . THR A 25  ? 0.91692 0.82573 0.97741 -0.00144 0.03025  0.02938  55  THR A CA    
107  C  C     . THR A 25  ? 0.75291 0.65854 0.81786 0.00066  0.03519  0.02833  55  THR A C     
108  O  O     . THR A 25  ? 0.69412 0.58492 0.75800 -0.00513 0.03972  0.02739  55  THR A O     
109  C  CB    . THR A 25  ? 1.19748 1.09655 1.25729 -0.01293 0.03132  0.03062  55  THR A CB    
110  O  OG1   . THR A 25  ? 1.24893 1.12294 1.29851 -0.01473 0.03451  0.02768  55  THR A OG1   
111  C  CG2   . THR A 25  ? 1.00426 0.91065 1.06197 -0.01576 0.02573  0.03239  55  THR A CG2   
112  N  N     . PRO A 26  ? 0.73641 0.65641 0.80601 0.00948  0.03425  0.02830  56  PRO A N     
113  C  CA    . PRO A 26  ? 0.61286 0.53018 0.68669 0.01204  0.03850  0.02721  56  PRO A CA    
114  C  C     . PRO A 26  ? 0.63590 0.55780 0.72000 0.00300  0.04292  0.02939  56  PRO A C     
115  O  O     . PRO A 26  ? 0.64739 0.58814 0.74049 -0.00089 0.04163  0.03294  56  PRO A O     
116  C  CB    . PRO A 26  ? 0.56544 0.50325 0.64356 0.02343  0.03540  0.02751  56  PRO A CB    
117  C  CG    . PRO A 26  ? 0.63028 0.57533 0.70201 0.02887  0.02932  0.02741  56  PRO A CG    
118  C  CD    . PRO A 26  ? 0.54519 0.48734 0.61703 0.01789  0.02907  0.02937  56  PRO A CD    
119  N  N     . PRO A 27  ? 0.60074 0.50615 0.68313 -0.00079 0.04778  0.02754  57  PRO A N     
120  C  CA    . PRO A 27  ? 0.36581 0.27425 0.45636 -0.00814 0.05149  0.02909  57  PRO A CA    
121  C  C     . PRO A 27  ? 0.37371 0.29869 0.47490 -0.00378 0.05311  0.03029  57  PRO A C     
122  O  O     . PRO A 27  ? 0.51185 0.43915 0.61274 0.00504  0.05304  0.02863  57  PRO A O     
123  C  CB    . PRO A 27  ? 0.47479 0.36121 0.55861 -0.01165 0.05599  0.02607  57  PRO A CB    
124  C  CG    . PRO A 27  ? 0.51105 0.38634 0.58627 -0.00551 0.05549  0.02351  57  PRO A CG    
125  C  CD    . PRO A 27  ? 0.45668 0.33980 0.52840 0.00043  0.04965  0.02425  57  PRO A CD    
126  N  N     . PHE A 28  ? 0.39388 0.32965 0.50350 -0.01000 0.05398  0.03334  58  PHE A N     
127  C  CA    . PHE A 28  ? 0.31013 0.25996 0.42954 -0.00676 0.05625  0.03453  58  PHE A CA    
128  C  C     . PHE A 28  ? 0.39875 0.33348 0.51748 -0.00690 0.06161  0.03138  58  PHE A C     
129  O  O     . PHE A 28  ? 0.41805 0.35705 0.54065 -0.00016 0.06360  0.03009  58  PHE A O     
130  C  CB    . PHE A 28  ? 0.30003 0.26672 0.42794 -0.01406 0.05493  0.03949  58  PHE A CB    
131  C  CG    . PHE A 28  ? 0.29033 0.27129 0.42798 -0.01137 0.05751  0.04106  58  PHE A CG    
132  C  CD1   . PHE A 28  ? 0.28496 0.28775 0.42871 -0.00243 0.05618  0.04238  58  PHE A CD1   
133  C  CD2   . PHE A 28  ? 0.30008 0.27250 0.43988 -0.01678 0.06110  0.04089  58  PHE A CD2   
134  C  CE1   . PHE A 28  ? 0.27633 0.29246 0.42868 0.00060  0.05863  0.04379  58  PHE A CE1   
135  C  CE2   . PHE A 28  ? 0.27884 0.26381 0.42720 -0.01401 0.06352  0.04225  58  PHE A CE2   
136  C  CZ    . PHE A 28  ? 0.30505 0.31212 0.46001 -0.00551 0.06242  0.04384  58  PHE A CZ    
137  N  N     . LEU A 29  ? 0.31514 0.23318 0.42874 -0.01406 0.06370  0.03004  59  LEU A N     
138  C  CA    . LEU A 29  ? 0.32890 0.23440 0.44161 -0.01426 0.06886  0.02691  59  LEU A CA    
139  C  C     . LEU A 29  ? 0.40850 0.29445 0.51058 -0.01717 0.07011  0.02404  59  LEU A C     
140  O  O     . LEU A 29  ? 0.41038 0.29005 0.50719 -0.02274 0.06815  0.02473  59  LEU A O     
141  C  CB    . LEU A 29  ? 0.29907 0.20740 0.41719 -0.01959 0.07070  0.02832  59  LEU A CB    
142  C  CG    . LEU A 29  ? 0.37100 0.26788 0.48814 -0.01897 0.07603  0.02468  59  LEU A CG    
143  C  CD1   . LEU A 29  ? 0.47057 0.37409 0.59362 -0.01137 0.07859  0.02329  59  LEU A CD1   
144  C  CD2   . LEU A 29  ? 0.33693 0.23252 0.45571 -0.02437 0.07665  0.02566  59  LEU A CD2   
145  N  N     . VAL A 30  ? 0.32600 0.20271 0.42456 -0.01371 0.07313  0.02105  60  VAL A N     
146  C  CA    . VAL A 30  ? 0.41474 0.27513 0.50372 -0.01669 0.07520  0.01862  60  VAL A CA    
147  C  C     . VAL A 30  ? 0.37326 0.22959 0.46427 -0.01776 0.08057  0.01629  60  VAL A C     
148  O  O     . VAL A 30  ? 0.34894 0.20943 0.44517 -0.01389 0.08268  0.01543  60  VAL A O     
149  C  CB    . VAL A 30  ? 0.48546 0.33836 0.56711 -0.01303 0.07378  0.01761  60  VAL A CB    
150  C  CG1   . VAL A 30  ? 0.40476 0.24331 0.47797 -0.01665 0.07715  0.01552  60  VAL A CG1   
151  C  CG2   . VAL A 30  ? 0.42855 0.28319 0.50567 -0.01173 0.06833  0.01923  60  VAL A CG2   
152  N  N     . LEU A 31  ? 0.41949 0.26795 0.50571 -0.02217 0.08237  0.01502  61  LEU A N     
153  C  CA    . LEU A 31  ? 0.38577 0.23026 0.47178 -0.02246 0.08739  0.01218  61  LEU A CA    
154  C  C     . LEU A 31  ? 0.38077 0.21624 0.45843 -0.02336 0.08987  0.01027  61  LEU A C     
155  O  O     . LEU A 31  ? 0.39695 0.22533 0.46632 -0.02579 0.08818  0.01053  61  LEU A O     
156  C  CB    . LEU A 31  ? 0.32123 0.16235 0.40506 -0.02551 0.08731  0.01154  61  LEU A CB    
157  C  CG    . LEU A 31  ? 0.38295 0.23179 0.47329 -0.02691 0.08403  0.01439  61  LEU A CG    
158  C  CD1   . LEU A 31  ? 0.40709 0.24746 0.49099 -0.03085 0.08210  0.01394  61  LEU A CD1   
159  C  CD2   . LEU A 31  ? 0.46284 0.32123 0.56299 -0.02342 0.08670  0.01434  61  LEU A CD2   
160  N  N     . LEU A 32  ? 0.32112 0.15776 0.40112 -0.02174 0.09357  0.00873  62  LEU A N     
161  C  CA    . LEU A 32  ? 0.32737 0.15770 0.39997 -0.02391 0.09638  0.00747  62  LEU A CA    
162  C  C     . LEU A 32  ? 0.32443 0.15747 0.39836 -0.02400 0.10148  0.00466  62  LEU A C     
163  O  O     . LEU A 32  ? 0.38232 0.22133 0.46377 -0.02161 0.10362  0.00367  62  LEU A O     
164  C  CB    . LEU A 32  ? 0.32830 0.15706 0.40049 -0.02288 0.09541  0.00839  62  LEU A CB    
165  C  CG    . LEU A 32  ? 0.34941 0.17480 0.41830 -0.02103 0.08974  0.01054  62  LEU A CG    
166  C  CD1   . LEU A 32  ? 0.37336 0.19432 0.43955 -0.01931 0.08803  0.01094  62  LEU A CD1   
167  C  CD2   . LEU A 32  ? 0.38824 0.20588 0.44739 -0.02433 0.08789  0.01131  62  LEU A CD2   
168  N  N     . VAL A 33  ? 0.33129 0.16042 0.39760 -0.02579 0.10301  0.00321  63  VAL A N     
169  C  CA    . VAL A 33  ? 0.33316 0.16539 0.39896 -0.02431 0.10726  -0.00005 63  VAL A CA    
170  C  C     . VAL A 33  ? 0.33424 0.16882 0.39512 -0.02610 0.11154  -0.00111 63  VAL A C     
171  O  O     . VAL A 33  ? 0.37754 0.20781 0.43042 -0.02893 0.11092  0.00005  63  VAL A O     
172  C  CB    . VAL A 33  ? 0.33670 0.16349 0.39623 -0.02357 0.10523  -0.00142 63  VAL A CB    
173  C  CG1   . VAL A 33  ? 0.33758 0.16645 0.39473 -0.02026 0.10866  -0.00536 63  VAL A CG1   
174  C  CG2   . VAL A 33  ? 0.33453 0.15965 0.39822 -0.02394 0.10027  0.00075  63  VAL A CG2   
175  N  N     . THR A 34  ? 0.33264 0.17484 0.39838 -0.02468 0.11562  -0.00303 64  THR A N     
176  C  CA    . THR A 34  ? 0.37007 0.21814 0.43224 -0.02704 0.11993  -0.00370 64  THR A CA    
177  C  C     . THR A 34  ? 0.43708 0.28862 0.49302 -0.02408 0.12273  -0.00712 64  THR A C     
178  O  O     . THR A 34  ? 0.41486 0.26566 0.47217 -0.01936 0.12229  -0.00983 64  THR A O     
179  C  CB    . THR A 34  ? 0.32385 0.17930 0.39439 -0.02706 0.12234  -0.00397 64  THR A CB    
180  O  OG1   . THR A 34  ? 0.38228 0.24259 0.45848 -0.02185 0.12414  -0.00721 64  THR A OG1   
181  C  CG2   . THR A 34  ? 0.33229 0.18269 0.40731 -0.02814 0.11848  -0.00109 64  THR A CG2   
182  N  N     . SER A 35  ? 0.42497 0.27962 0.47300 -0.02647 0.12498  -0.00688 65  SER A N     
183  C  CA    . SER A 35  ? 0.41725 0.27712 0.45780 -0.02218 0.12770  -0.01052 65  SER A CA    
184  C  C     . SER A 35  ? 0.42244 0.29108 0.45664 -0.02601 0.13124  -0.00921 65  SER A C     
185  O  O     . SER A 35  ? 0.43954 0.30396 0.47165 -0.03229 0.12984  -0.00519 65  SER A O     
186  C  CB    . SER A 35  ? 0.42012 0.26874 0.45303 -0.01858 0.12361  -0.01197 65  SER A CB    
187  O  OG    . SER A 35  ? 0.51543 0.35776 0.54036 -0.02192 0.12157  -0.00959 65  SER A OG    
188  N  N     . SER A 36  ? 0.43640 0.31754 0.46720 -0.02213 0.13547  -0.01241 66  SER A N     
189  C  CA    . SER A 36  ? 0.43578 0.32897 0.45999 -0.02545 0.13921  -0.01102 66  SER A CA    
190  C  C     . SER A 36  ? 0.51876 0.40427 0.53089 -0.02331 0.13705  -0.01127 66  SER A C     
191  O  O     . SER A 36  ? 0.53249 0.40555 0.54145 -0.01805 0.13312  -0.01367 66  SER A O     
192  C  CB    . SER A 36  ? 0.41818 0.33016 0.44325 -0.02088 0.14436  -0.01458 66  SER A CB    
193  O  OG    . SER A 36  ? 0.60064 0.52005 0.63672 -0.02365 0.14627  -0.01403 66  SER A OG    
194  N  N     . HIS A 37  ? 0.50853 0.40147 0.51370 -0.02751 0.13930  -0.00872 67  HIS A N     
195  C  CA    . HIS A 37  ? 0.53505 0.42069 0.52817 -0.02567 0.13723  -0.00864 67  HIS A CA    
196  C  C     . HIS A 37  ? 0.55820 0.44549 0.54307 -0.01463 0.13715  -0.01444 67  HIS A C     
197  O  O     . HIS A 37  ? 0.55576 0.42962 0.53182 -0.01099 0.13297  -0.01565 67  HIS A O     
198  C  CB    . HIS A 37  ? 0.60728 0.50415 0.59455 -0.03235 0.14053  -0.00461 67  HIS A CB    
199  C  CG    . HIS A 37  ? 0.59708 0.49101 0.58854 -0.04359 0.13990  0.00130  67  HIS A CG    
200  N  ND1   . HIS A 37  ? 0.51738 0.40195 0.50132 -0.04972 0.13752  0.00557  67  HIS A ND1   
201  C  CD2   . HIS A 37  ? 0.55597 0.45354 0.55636 -0.04944 0.14064  0.00355  67  HIS A CD2   
202  C  CE1   . HIS A 37  ? 0.68374 0.56526 0.67111 -0.05886 0.13647  0.01019  67  HIS A CE1   
203  N  NE2   . HIS A 37  ? 0.67157 0.56067 0.66886 -0.05886 0.13818  0.00905  67  HIS A NE2   
204  N  N     . LYS A 38  ? 0.57360 0.47641 0.56023 -0.00907 0.14113  -0.01809 68  LYS A N     
205  C  CA    . LYS A 38  ? 0.58933 0.49390 0.56581 0.00310  0.14064  -0.02429 68  LYS A CA    
206  C  C     . LYS A 38  ? 0.56120 0.44705 0.53807 0.00859  0.13514  -0.02769 68  LYS A C     
207  O  O     . LYS A 38  ? 0.48988 0.36924 0.45541 0.01819  0.13225  -0.03251 68  LYS A O     
208  C  CB    . LYS A 38  ? 0.56464 0.49348 0.54308 0.00754  0.14658  -0.02713 68  LYS A CB    
209  C  CG    . LYS A 38  ? 0.79285 0.72350 0.78190 0.00946  0.14730  -0.02952 68  LYS A CG    
210  C  CD    . LYS A 38  ? 0.83811 0.79315 0.82761 0.01570  0.15270  -0.03328 68  LYS A CD    
211  C  CE    . LYS A 38  ? 0.94176 0.91271 0.94462 0.00668  0.15715  -0.02964 68  LYS A CE    
212  N  NZ    . LYS A 38  ? 1.05510 1.05135 1.05874 0.01278  0.16221  -0.03335 68  LYS A NZ    
213  N  N     . GLN A 39  ? 0.55845 0.43573 0.54685 0.00262  0.13329  -0.02502 69  GLN A N     
214  C  CA    . GLN A 39  ? 0.43026 0.29224 0.42029 0.00635  0.12834  -0.02730 69  GLN A CA    
215  C  C     . GLN A 39  ? 0.47753 0.31987 0.46173 0.00424  0.12172  -0.02544 69  GLN A C     
216  O  O     . GLN A 39  ? 0.56018 0.39272 0.55188 0.00017  0.11821  -0.02310 69  GLN A O     
217  C  CB    . GLN A 39  ? 0.52283 0.38866 0.52800 0.00183  0.12999  -0.02539 69  GLN A CB    
218  C  CG    . GLN A 39  ? 0.38813 0.27127 0.39830 0.00552  0.13537  -0.02834 69  GLN A CG    
219  C  CD    . GLN A 39  ? 0.48072 0.36467 0.50482 0.00224  0.13596  -0.02696 69  GLN A CD    
220  O  OE1   . GLN A 39  ? 0.48015 0.36380 0.51250 -0.00556 0.13607  -0.02243 69  GLN A OE1   
221  N  NE2   . GLN A 39  ? 0.61466 0.49850 0.64024 0.00887  0.13582  -0.03105 69  GLN A NE2   
222  N  N     . LEU A 40  ? 0.47278 0.31106 0.44407 0.00708  0.12007  -0.02638 70  LEU A N     
223  C  CA    . LEU A 40  ? 0.52674 0.34610 0.49121 0.00576  0.11320  -0.02517 70  LEU A CA    
224  C  C     . LEU A 40  ? 0.51646 0.32063 0.47687 0.01019  0.10698  -0.02802 70  LEU A C     
225  O  O     . LEU A 40  ? 0.57994 0.37076 0.54227 0.00562  0.10138  -0.02541 70  LEU A O     
226  C  CB    . LEU A 40  ? 0.48389 0.30201 0.43397 0.00921  0.11258  -0.02624 70  LEU A CB    
227  C  CG    . LEU A 40  ? 0.56980 0.36771 0.51123 0.00867  0.10485  -0.02561 70  LEU A CG    
228  C  CD1   . LEU A 40  ? 0.57475 0.36704 0.52699 -0.00112 0.10281  -0.02015 70  LEU A CD1   
229  C  CD2   . LEU A 40  ? 0.57063 0.36757 0.49733 0.01288  0.10436  -0.02689 70  LEU A CD2   
230  N  N     . ALA A 41  ? 0.54603 0.35201 0.49973 0.01897  0.10737  -0.03323 71  ALA A N     
231  C  CA    . ALA A 41  ? 0.57878 0.36805 0.52650 0.02273  0.10067  -0.03575 71  ALA A CA    
232  C  C     . ALA A 41  ? 0.51887 0.30578 0.48132 0.01561  0.09964  -0.03213 71  ALA A C     
233  O  O     . ALA A 41  ? 0.47684 0.24847 0.43739 0.01249  0.09284  -0.03042 71  ALA A O     
234  C  CB    . ALA A 41  ? 0.45044 0.24317 0.38859 0.03411  0.10168  -0.04224 71  ALA A CB    
235  N  N     . GLU A 42  ? 0.51467 0.31734 0.49147 0.01290  0.10607  -0.03074 72  GLU A N     
236  C  CA    . GLU A 42  ? 0.44883 0.25174 0.44012 0.00683  0.10568  -0.02717 72  GLU A CA    
237  C  C     . GLU A 42  ? 0.40999 0.20538 0.40510 -0.00099 0.10157  -0.02198 72  GLU A C     
238  O  O     . GLU A 42  ? 0.47803 0.26521 0.47662 -0.00426 0.09669  -0.01971 72  GLU A O     
239  C  CB    . GLU A 42  ? 0.47872 0.29949 0.48320 0.00505  0.11299  -0.02633 72  GLU A CB    
240  C  CG    . GLU A 42  ? 0.64546 0.47401 0.65147 0.01152  0.11625  -0.03067 72  GLU A CG    
241  C  CD    . GLU A 42  ? 0.66875 0.50490 0.66327 0.01968  0.11909  -0.03573 72  GLU A CD    
242  O  OE1   . GLU A 42  ? 0.53825 0.37543 0.52426 0.01997  0.11930  -0.03556 72  GLU A OE1   
243  O  OE2   . GLU A 42  ? 0.68851 0.53065 0.68238 0.02637  0.12114  -0.03997 72  GLU A OE2   
244  N  N     . ARG A 43  ? 0.42392 0.22327 0.41846 -0.00428 0.10348  -0.01979 73  ARG A N     
245  C  CA    . ARG A 43  ? 0.42589 0.21961 0.42424 -0.01092 0.09983  -0.01514 73  ARG A CA    
246  C  C     . ARG A 43  ? 0.45225 0.23022 0.44068 -0.01112 0.09214  -0.01505 73  ARG A C     
247  O  O     . ARG A 43  ? 0.45812 0.23137 0.45171 -0.01610 0.08759  -0.01155 73  ARG A O     
248  C  CB    . ARG A 43  ? 0.48927 0.28871 0.48668 -0.01398 0.10308  -0.01310 73  ARG A CB    
249  C  CG    . ARG A 43  ? 0.53016 0.34345 0.53724 -0.01604 0.10932  -0.01200 73  ARG A CG    
250  C  CD    . ARG A 43  ? 0.46058 0.27593 0.46668 -0.02129 0.11067  -0.00853 73  ARG A CD    
251  N  NE    . ARG A 43  ? 0.50693 0.32443 0.50155 -0.01965 0.11274  -0.00983 73  ARG A NE    
252  C  CZ    . ARG A 43  ? 0.60661 0.43700 0.59951 -0.01799 0.11830  -0.01140 73  ARG A CZ    
253  N  NH1   . ARG A 43  ? 0.45794 0.29920 0.45961 -0.01784 0.12221  -0.01216 73  ARG A NH1   
254  N  NH2   . ARG A 43  ? 0.46248 0.29621 0.44456 -0.01629 0.11991  -0.01215 73  ARG A NH2   
255  N  N     . MET A 44  ? 0.43410 0.20425 0.40773 -0.00562 0.09011  -0.01880 74  MET A N     
256  C  CA    . MET A 44  ? 0.51153 0.26430 0.47403 -0.00605 0.08165  -0.01877 74  MET A CA    
257  C  C     . MET A 44  ? 0.49157 0.23654 0.45625 -0.00754 0.07671  -0.01824 74  MET A C     
258  O  O     . MET A 44  ? 0.51788 0.25413 0.48292 -0.01339 0.07020  -0.01478 74  MET A O     
259  C  CB    . MET A 44  ? 0.45552 0.20026 0.39976 0.00171  0.07986  -0.02349 74  MET A CB    
260  C  CG    . MET A 44  ? 0.61882 0.36940 0.55846 0.00242  0.08330  -0.02328 74  MET A CG    
261  S  SD    . MET A 44  ? 0.63194 0.37849 0.57644 -0.00661 0.08027  -0.01761 74  MET A SD    
262  C  CE    . MET A 44  ? 0.55363 0.27897 0.48825 -0.00821 0.06897  -0.01728 74  MET A CE    
263  N  N     . ALA A 45  ? 0.50522 0.25433 0.47169 -0.00286 0.07966  -0.02126 75  ALA A N     
264  C  CA    . ALA A 45  ? 0.43618 0.17749 0.40413 -0.00472 0.07493  -0.02037 75  ALA A CA    
265  C  C     . ALA A 45  ? 0.50851 0.25787 0.49313 -0.01308 0.07510  -0.01452 75  ALA A C     
266  O  O     . ALA A 45  ? 0.43374 0.17575 0.41879 -0.01830 0.06888  -0.01130 75  ALA A O     
267  C  CB    . ALA A 45  ? 0.43467 0.17993 0.40177 0.00252  0.07862  -0.02493 75  ALA A CB    
268  N  N     . ILE A 46  ? 0.43974 0.20453 0.43753 -0.01450 0.08165  -0.01285 76  ILE A N     
269  C  CA    . ILE A 46  ? 0.43495 0.20818 0.44753 -0.02076 0.08147  -0.00766 76  ILE A CA    
270  C  C     . ILE A 46  ? 0.46740 0.23490 0.47732 -0.02639 0.07560  -0.00388 76  ILE A C     
271  O  O     . ILE A 46  ? 0.39534 0.16393 0.41123 -0.03150 0.07133  0.00013  76  ILE A O     
272  C  CB    . ILE A 46  ? 0.43830 0.22655 0.46269 -0.02003 0.08881  -0.00727 76  ILE A CB    
273  C  CG1   . ILE A 46  ? 0.37254 0.16780 0.40155 -0.01545 0.09390  -0.01039 76  ILE A CG1   
274  C  CG2   . ILE A 46  ? 0.36669 0.16232 0.40297 -0.02482 0.08775  -0.00240 76  ILE A CG2   
275  C  CD1   . ILE A 46  ? 0.37000 0.17707 0.40450 -0.01402 0.10086  -0.01140 76  ILE A CD1   
276  N  N     . ARG A 47  ? 0.48896 0.25172 0.49004 -0.02536 0.07543  -0.00508 77  ARG A N     
277  C  CA    . ARG A 47  ? 0.49890 0.25626 0.49672 -0.03009 0.07003  -0.00195 77  ARG A CA    
278  C  C     . ARG A 47  ? 0.53202 0.27623 0.52183 -0.03354 0.06129  -0.00068 77  ARG A C     
279  O  O     . ARG A 47  ? 0.49916 0.24400 0.49246 -0.03961 0.05637  0.00356  77  ARG A O     
280  C  CB    . ARG A 47  ? 0.43199 0.18629 0.42046 -0.02729 0.07214  -0.00409 77  ARG A CB    
281  C  CG    . ARG A 47  ? 0.44465 0.20919 0.44031 -0.02848 0.07711  -0.00234 77  ARG A CG    
282  C  CD    . ARG A 47  ? 0.52118 0.28055 0.50557 -0.02704 0.07754  -0.00359 77  ARG A CD    
283  N  NE    . ARG A 47  ? 0.47469 0.24300 0.46277 -0.02733 0.08354  -0.00287 77  ARG A NE    
284  C  CZ    . ARG A 47  ? 0.59538 0.36843 0.57891 -0.02428 0.08898  -0.00523 77  ARG A CZ    
285  N  NH1   . ARG A 47  ? 0.47048 0.24167 0.44622 -0.01908 0.08972  -0.00914 77  ARG A NH1   
286  N  NH2   . ARG A 47  ? 0.45662 0.23648 0.44250 -0.02645 0.09324  -0.00355 77  ARG A NH2   
287  N  N     . GLN A 48  ? 0.47000 0.20309 0.44912 -0.02989 0.05904  -0.00411 78  GLN A N     
288  C  CA    . GLN A 48  ? 0.47849 0.19603 0.44775 -0.03381 0.04961  -0.00273 78  GLN A CA    
289  C  C     . GLN A 48  ? 0.59307 0.31591 0.57239 -0.03879 0.04813  0.00087  78  GLN A C     
290  O  O     . GLN A 48  ? 0.59214 0.30634 0.56721 -0.04561 0.03999  0.00446  78  GLN A O     
291  C  CB    . GLN A 48  ? 0.60294 0.30401 0.55339 -0.02643 0.04699  -0.00845 78  GLN A CB    
292  C  CG    . GLN A 48  ? 0.73345 0.42805 0.67173 -0.02200 0.04658  -0.01137 78  GLN A CG    
293  C  CD    . GLN A 48  ? 0.74744 0.43882 0.67362 -0.01110 0.04994  -0.01797 78  GLN A CD    
294  O  OE1   . GLN A 48  ? 0.73774 0.42662 0.66063 -0.00636 0.05039  -0.02102 78  GLN A OE1   
295  N  NE2   . GLN A 48  ? 0.86229 0.55495 0.78147 -0.00664 0.05236  -0.02022 78  GLN A NE2   
296  N  N     . THR A 49  ? 0.47319 0.21054 0.46558 -0.03630 0.05539  0.00054  79  THR A N     
297  C  CA    . THR A 49  ? 0.48168 0.22431 0.48281 -0.03993 0.05438  0.00360  79  THR A CA    
298  C  C     . THR A 49  ? 0.44741 0.20955 0.46673 -0.04390 0.05753  0.00841  79  THR A C     
299  O  O     . THR A 49  ? 0.50289 0.26821 0.52467 -0.04964 0.05342  0.01259  79  THR A O     
300  C  CB    . THR A 49  ? 0.53024 0.27174 0.52954 -0.03280 0.05889  -0.00113 79  THR A CB    
301  O  OG1   . THR A 49  ? 0.51980 0.27437 0.52709 -0.02731 0.06770  -0.00389 79  THR A OG1   
302  C  CG2   . THR A 49  ? 0.44006 0.16149 0.41938 -0.02786 0.05420  -0.00597 79  THR A CG2   
303  N  N     . TRP A 50  ? 0.40927 0.18413 0.44019 -0.04032 0.06415  0.00763  80  TRP A N     
304  C  CA    . TRP A 50  ? 0.50836 0.30155 0.55562 -0.04251 0.06656  0.01185  80  TRP A CA    
305  C  C     . TRP A 50  ? 0.37032 0.17148 0.42225 -0.04134 0.06929  0.01228  80  TRP A C     
306  O  O     . TRP A 50  ? 0.43083 0.24570 0.49387 -0.04230 0.06990  0.01559  80  TRP A O     
307  C  CB    . TRP A 50  ? 0.39989 0.20218 0.45654 -0.03841 0.07205  0.01056  80  TRP A CB    
308  C  CG    . TRP A 50  ? 0.48728 0.28789 0.54161 -0.03122 0.07852  0.00481  80  TRP A CG    
309  C  CD1   . TRP A 50  ? 0.44861 0.24014 0.49459 -0.02709 0.07934  0.00047  80  TRP A CD1   
310  C  CD2   . TRP A 50  ? 0.34705 0.15644 0.40729 -0.02750 0.08473  0.00302  80  TRP A CD2   
311  N  NE1   . TRP A 50  ? 0.35819 0.15476 0.40554 -0.02115 0.08603  -0.00381 80  TRP A NE1   
312  C  CE2   . TRP A 50  ? 0.36553 0.17253 0.42153 -0.02207 0.08932  -0.00203 80  TRP A CE2   
313  C  CE3   . TRP A 50  ? 0.42885 0.24715 0.49626 -0.02823 0.08624  0.00522  80  TRP A CE3   
314  C  CZ2   . TRP A 50  ? 0.43654 0.25098 0.49617 -0.01890 0.09540  -0.00424 80  TRP A CZ2   
315  C  CZ3   . TRP A 50  ? 0.33378 0.15627 0.40326 -0.02488 0.09168  0.00287  80  TRP A CZ3   
316  C  CH2   . TRP A 50  ? 0.40937 0.23050 0.47543 -0.02100 0.09626  -0.00148 80  TRP A CH2   
317  N  N     . GLY A 51  ? 0.39488 0.18758 0.43757 -0.03900 0.07041  0.00913  81  GLY A N     
318  C  CA    . GLY A 51  ? 0.45259 0.25010 0.49725 -0.03833 0.07237  0.00962  81  GLY A CA    
319  C  C     . GLY A 51  ? 0.42071 0.21383 0.46030 -0.04277 0.06627  0.01234  81  GLY A C     
320  O  O     . GLY A 51  ? 0.50524 0.30191 0.54597 -0.04226 0.06706  0.01305  81  GLY A O     
321  N  N     . LYS A 52  ? 0.50037 0.28488 0.53344 -0.04712 0.05988  0.01380  82  LYS A N     
322  C  CA    . LYS A 52  ? 0.49976 0.27992 0.52768 -0.05227 0.05307  0.01667  82  LYS A CA    
323  C  C     . LYS A 52  ? 0.55504 0.35216 0.59529 -0.05481 0.05220  0.02121  82  LYS A C     
324  O  O     . LYS A 52  ? 0.61158 0.42009 0.66131 -0.05713 0.05156  0.02441  82  LYS A O     
325  C  CB    . LYS A 52  ? 0.49896 0.26745 0.51830 -0.05803 0.04517  0.01844  82  LYS A CB    
326  C  CG    . LYS A 52  ? 0.75139 0.51459 0.76455 -0.06369 0.03773  0.02122  82  LYS A CG    
327  C  CD    . LYS A 52  ? 1.11969 0.87082 1.12410 -0.07096 0.02876  0.02383  82  LYS A CD    
328  C  CE    . LYS A 52  ? 1.15678 0.89856 1.15180 -0.07582 0.02110  0.02543  82  LYS A CE    
329  N  NZ    . LYS A 52  ? 0.99319 0.75234 0.99905 -0.07922 0.02055  0.02953  82  LYS A NZ    
330  N  N     . GLU A 53  ? 0.57816 0.37696 0.61725 -0.05370 0.05208  0.02128  83  GLU A N     
331  C  CA    . GLU A 53  ? 0.63641 0.45137 0.68542 -0.05416 0.05090  0.02485  83  GLU A CA    
332  C  C     . GLU A 53  ? 0.66804 0.48895 0.71917 -0.06148 0.04368  0.02971  83  GLU A C     
333  O  O     . GLU A 53  ? 0.61259 0.42097 0.65388 -0.06615 0.03836  0.02999  83  GLU A O     
334  C  CB    . GLU A 53  ? 0.65153 0.46329 0.69581 -0.05074 0.05207  0.02315  83  GLU A CB    
335  C  CG    . GLU A 53  ? 0.65069 0.45939 0.69427 -0.04513 0.05907  0.01956  83  GLU A CG    
336  C  CD    . GLU A 53  ? 0.91719 0.72424 0.95695 -0.04225 0.05998  0.01885  83  GLU A CD    
337  O  OE1   . GLU A 53  ? 0.88865 0.69379 0.92398 -0.04390 0.05542  0.02016  83  GLU A OE1   
338  O  OE2   . GLU A 53  ? 0.83624 0.64323 0.87670 -0.03875 0.06475  0.01715  83  GLU A OE2   
339  N  N     . ARG A 54  ? 0.59873 0.43859 0.66181 -0.06243 0.04329  0.03353  84  ARG A N     
340  C  CA    . ARG A 54  ? 0.58823 0.43738 0.65446 -0.07071 0.03657  0.03914  84  ARG A CA    
341  C  C     . ARG A 54  ? 0.54443 0.41946 0.62466 -0.06927 0.03731  0.04301  84  ARG A C     
342  O  O     . ARG A 54  ? 0.53939 0.42152 0.62562 -0.06139 0.04280  0.04079  84  ARG A O     
343  C  CB    . ARG A 54  ? 0.55758 0.39697 0.62002 -0.07615 0.03458  0.04007  84  ARG A CB    
344  C  CG    . ARG A 54  ? 0.58984 0.43299 0.65869 -0.07202 0.04039  0.03862  84  ARG A CG    
345  C  CD    . ARG A 54  ? 0.64609 0.48191 0.71106 -0.07891 0.03634  0.04106  84  ARG A CD    
346  N  NE    . ARG A 54  ? 0.77813 0.61117 0.84527 -0.07422 0.04170  0.03823  84  ARG A NE    
347  C  CZ    . ARG A 54  ? 0.67409 0.51952 0.75000 -0.07608 0.04246  0.04156  84  ARG A CZ    
348  N  NH1   . ARG A 54  ? 0.52455 0.38162 0.60452 -0.08474 0.03686  0.04826  84  ARG A NH1   
349  N  NH2   . ARG A 54  ? 0.82020 0.66748 0.90089 -0.06952 0.04877  0.03843  84  ARG A NH2   
350  N  N     . MET A 55  ? 0.55799 0.44685 0.64240 -0.07667 0.03146  0.04873  85  MET A N     
351  C  CA    . MET A 55  ? 0.63291 0.54982 0.73073 -0.07520 0.03194  0.05292  85  MET A CA    
352  C  C     . MET A 55  ? 0.65570 0.57657 0.75838 -0.07964 0.03275  0.05578  85  MET A C     
353  O  O     . MET A 55  ? 0.69347 0.60467 0.79039 -0.08933 0.02791  0.05862  85  MET A O     
354  C  CB    . MET A 55  ? 0.51978 0.45482 0.62077 -0.08052 0.02557  0.05805  85  MET A CB    
355  C  CG    . MET A 55  ? 0.69318 0.62637 0.78982 -0.07482 0.02477  0.05515  85  MET A CG    
356  S  SD    . MET A 55  ? 0.96240 0.91364 1.06678 -0.06083 0.02943  0.05273  85  MET A SD    
357  C  CE    . MET A 55  ? 0.74119 0.69254 0.83896 -0.05778 0.02509  0.05144  85  MET A CE    
358  N  N     . VAL A 56  ? 0.76395 0.69602 0.87528 -0.07248 0.03827  0.05474  86  VAL A N     
359  C  CA    . VAL A 56  ? 0.75576 0.69240 0.87213 -0.07525 0.03977  0.05710  86  VAL A CA    
360  C  C     . VAL A 56  ? 0.75288 0.72117 0.88202 -0.07468 0.03908  0.06256  86  VAL A C     
361  O  O     . VAL A 56  ? 0.76995 0.75175 0.90584 -0.06445 0.04290  0.06062  86  VAL A O     
362  C  CB    . VAL A 56  ? 0.67335 0.59816 0.78937 -0.06701 0.04681  0.05135  86  VAL A CB    
363  C  CG1   . VAL A 56  ? 0.61163 0.53996 0.73198 -0.06970 0.04808  0.05358  86  VAL A CG1   
364  C  CG2   . VAL A 56  ? 0.52879 0.42643 0.63227 -0.06609 0.04785  0.04574  86  VAL A CG2   
365  N  N     . LYS A 57  ? 0.89964 0.88019 1.03118 -0.08561 0.03364  0.06957  87  LYS A N     
366  C  CA    . LYS A 57  ? 0.82206 0.83679 0.96571 -0.08607 0.03246  0.07570  87  LYS A CA    
367  C  C     . LYS A 57  ? 0.80287 0.83405 0.94982 -0.07825 0.03190  0.07458  87  LYS A C     
368  O  O     . LYS A 57  ? 0.77259 0.82879 0.92864 -0.06991 0.03390  0.07551  87  LYS A O     
369  C  CB    . LYS A 57  ? 0.82432 0.85102 0.97670 -0.07950 0.03791  0.07563  87  LYS A CB    
370  C  CG    . LYS A 57  ? 0.96470 0.97709 1.11385 -0.08674 0.03818  0.07701  87  LYS A CG    
371  C  CD    . LYS A 57  ? 0.89179 0.91316 1.04045 -0.10217 0.03122  0.08568  87  LYS A CD    
372  C  CE    . LYS A 57  ? 1.10273 1.10819 1.24636 -0.10892 0.03077  0.08710  87  LYS A CE    
373  N  NZ    . LYS A 57  ? 0.96770 0.97924 1.10887 -0.12544 0.02296  0.09617  87  LYS A NZ    
374  N  N     . GLY A 58  ? 0.66643 0.68282 0.80481 -0.08012 0.02881  0.07231  88  GLY A N     
375  C  CA    . GLY A 58  ? 0.67225 0.70003 0.81127 -0.07268 0.02768  0.07068  88  GLY A CA    
376  C  C     . GLY A 58  ? 0.63989 0.65822 0.77667 -0.05846 0.03293  0.06362  88  GLY A C     
377  O  O     . GLY A 58  ? 0.62422 0.65265 0.76092 -0.05060 0.03176  0.06214  88  GLY A O     
378  N  N     . LYS A 59  ? 0.68707 0.68623 0.82120 -0.05506 0.03813  0.05932  89  LYS A N     
379  C  CA    . LYS A 59  ? 0.55733 0.54661 0.68886 -0.04312 0.04275  0.05319  89  LYS A CA    
380  C  C     . LYS A 59  ? 0.45392 0.41303 0.57400 -0.04460 0.04424  0.04833  89  LYS A C     
381  O  O     . LYS A 59  ? 0.50988 0.45364 0.62568 -0.05178 0.04449  0.04821  89  LYS A O     
382  C  CB    . LYS A 59  ? 0.43199 0.42612 0.57021 -0.03746 0.04774  0.05218  89  LYS A CB    
383  C  CG    . LYS A 59  ? 0.45344 0.47865 0.60304 -0.03550 0.04676  0.05715  89  LYS A CG    
384  C  CD    . LYS A 59  ? 0.56086 0.60701 0.71259 -0.02708 0.04381  0.05771  89  LYS A CD    
385  C  CE    . LYS A 59  ? 0.64683 0.72631 0.80982 -0.02357 0.04338  0.06240  89  LYS A CE    
386  N  NZ    . LYS A 59  ? 0.76890 0.86348 0.93767 -0.03718 0.04067  0.06981  89  LYS A NZ    
387  N  N     . GLN A 60  ? 0.40562 0.35597 0.51960 -0.03758 0.04489  0.04435  90  GLN A N     
388  C  CA    . GLN A 60  ? 0.50200 0.42648 0.60489 -0.03940 0.04614  0.04039  90  GLN A CA    
389  C  C     . GLN A 60  ? 0.45270 0.36280 0.55406 -0.03634 0.05219  0.03641  90  GLN A C     
390  O  O     . GLN A 60  ? 0.41699 0.33159 0.52198 -0.02873 0.05528  0.03462  90  GLN A O     
391  C  CB    . GLN A 60  ? 0.46448 0.38374 0.56012 -0.03414 0.04436  0.03805  90  GLN A CB    
392  C  CG    . GLN A 60  ? 0.50551 0.39933 0.58945 -0.03624 0.04598  0.03434  90  GLN A CG    
393  C  CD    . GLN A 60  ? 0.65909 0.54475 0.73734 -0.04486 0.04203  0.03586  90  GLN A CD    
394  O  OE1   . GLN A 60  ? 0.75395 0.64867 0.83238 -0.04739 0.03684  0.03852  90  GLN A OE1   
395  N  NE2   . GLN A 60  ? 0.73781 0.60638 0.81022 -0.04890 0.04398  0.03399  90  GLN A NE2   
396  N  N     . LEU A 61  ? 0.51353 0.40649 0.60867 -0.04183 0.05333  0.03489  91  LEU A N     
397  C  CA    . LEU A 61  ? 0.41840 0.29706 0.51019 -0.03934 0.05885  0.03070  91  LEU A CA    
398  C  C     . LEU A 61  ? 0.42584 0.28732 0.50653 -0.03854 0.05976  0.02725  91  LEU A C     
399  O  O     . LEU A 61  ? 0.50898 0.36258 0.58243 -0.04285 0.05620  0.02772  91  LEU A O     
400  C  CB    . LEU A 61  ? 0.41812 0.29032 0.50920 -0.04473 0.05923  0.03103  91  LEU A CB    
401  C  CG    . LEU A 61  ? 0.48161 0.33938 0.56777 -0.04219 0.06447  0.02635  91  LEU A CG    
402  C  CD1   . LEU A 61  ? 0.37729 0.24434 0.47234 -0.03663 0.06914  0.02541  91  LEU A CD1   
403  C  CD2   . LEU A 61  ? 0.55428 0.40056 0.63430 -0.04714 0.06285  0.02597  91  LEU A CD2   
404  N  N     . LYS A 62  ? 0.45389 0.30979 0.53279 -0.03343 0.06416  0.02411  92  LYS A N     
405  C  CA    . LYS A 62  ? 0.41495 0.25548 0.48327 -0.03330 0.06588  0.02120  92  LYS A CA    
406  C  C     . LYS A 62  ? 0.46945 0.30323 0.53678 -0.03216 0.07169  0.01809  92  LYS A C     
407  O  O     . LYS A 62  ? 0.43085 0.27156 0.50566 -0.02932 0.07452  0.01777  92  LYS A O     
408  C  CB    . LYS A 62  ? 0.52635 0.36602 0.59097 -0.02910 0.06478  0.02089  92  LYS A CB    
409  C  CG    . LYS A 62  ? 0.57361 0.42193 0.63891 -0.02830 0.05903  0.02341  92  LYS A CG    
410  C  CD    . LYS A 62  ? 0.55511 0.39513 0.61241 -0.03300 0.05569  0.02379  92  LYS A CD    
411  C  CE    . LYS A 62  ? 0.59957 0.42370 0.64537 -0.03232 0.05733  0.02126  92  LYS A CE    
412  N  NZ    . LYS A 62  ? 0.66484 0.47917 0.70244 -0.03686 0.05496  0.02106  92  LYS A NZ    
413  N  N     . THR A 63  ? 0.42208 0.24364 0.48004 -0.03385 0.07340  0.01577  93  THR A N     
414  C  CA    . THR A 63  ? 0.54695 0.36426 0.60329 -0.03275 0.07883  0.01273  93  THR A CA    
415  C  C     . THR A 63  ? 0.43249 0.24170 0.47971 -0.03263 0.08136  0.01100  93  THR A C     
416  O  O     . THR A 63  ? 0.53478 0.33635 0.57314 -0.03433 0.07922  0.01090  93  THR A O     
417  C  CB    . THR A 63  ? 0.59119 0.40357 0.64439 -0.03449 0.07845  0.01139  93  THR A CB    
418  O  OG1   . THR A 63  ? 0.60530 0.42499 0.66651 -0.03573 0.07606  0.01361  93  THR A OG1   
419  C  CG2   . THR A 63  ? 0.38073 0.19072 0.43177 -0.03201 0.08405  0.00778  93  THR A CG2   
420  N  N     . PHE A 64  ? 0.41319 0.22429 0.46221 -0.03108 0.08569  0.00991  94  PHE A N     
421  C  CA    . PHE A 64  ? 0.42624 0.23147 0.46692 -0.03222 0.08830  0.00907  94  PHE A CA    
422  C  C     . PHE A 64  ? 0.45995 0.26853 0.50199 -0.03180 0.09407  0.00681  94  PHE A C     
423  O  O     . PHE A 64  ? 0.45293 0.26800 0.50348 -0.02992 0.09591  0.00609  94  PHE A O     
424  C  CB    . PHE A 64  ? 0.44135 0.24473 0.48057 -0.03196 0.08638  0.01095  94  PHE A CB    
425  C  CG    . PHE A 64  ? 0.45781 0.26134 0.49739 -0.03064 0.08061  0.01288  94  PHE A CG    
426  C  CD1   . PHE A 64  ? 0.44186 0.23920 0.47364 -0.03233 0.07749  0.01341  94  PHE A CD1   
427  C  CD2   . PHE A 64  ? 0.51922 0.33040 0.56672 -0.02719 0.07819  0.01405  94  PHE A CD2   
428  C  CE1   . PHE A 64  ? 0.40764 0.20704 0.44001 -0.03104 0.07208  0.01512  94  PHE A CE1   
429  C  CE2   . PHE A 64  ? 0.50301 0.31745 0.55087 -0.02531 0.07288  0.01578  94  PHE A CE2   
430  C  CZ    . PHE A 64  ? 0.51999 0.32883 0.56052 -0.02746 0.06986  0.01632  94  PHE A CZ    
431  N  N     . PHE A 65  ? 0.46189 0.26732 0.49541 -0.03341 0.09688  0.00579  95  PHE A N     
432  C  CA    . PHE A 65  ? 0.36371 0.17468 0.39721 -0.03316 0.10247  0.00370  95  PHE A CA    
433  C  C     . PHE A 65  ? 0.44426 0.25623 0.47524 -0.03660 0.10468  0.00538  95  PHE A C     
434  O  O     . PHE A 65  ? 0.39718 0.20307 0.41983 -0.03952 0.10315  0.00723  95  PHE A O     
435  C  CB    . PHE A 65  ? 0.38174 0.19102 0.40667 -0.03185 0.10393  0.00122  95  PHE A CB    
436  C  CG    . PHE A 65  ? 0.47481 0.28060 0.50013 -0.02901 0.10092  -0.00046 95  PHE A CG    
437  C  CD1   . PHE A 65  ? 0.36605 0.17620 0.39598 -0.02585 0.10289  -0.00297 95  PHE A CD1   
438  C  CD2   . PHE A 65  ? 0.46573 0.26325 0.48646 -0.02998 0.09549  0.00075  95  PHE A CD2   
439  C  CE1   . PHE A 65  ? 0.40552 0.21022 0.43414 -0.02410 0.09916  -0.00404 95  PHE A CE1   
440  C  CE2   . PHE A 65  ? 0.50716 0.30019 0.52726 -0.02885 0.09163  -0.00009 95  PHE A CE2   
441  C  CZ    . PHE A 65  ? 0.39715 0.19306 0.42074 -0.02611 0.09334  -0.00238 95  PHE A CZ    
442  N  N     . LEU A 66  ? 0.51382 0.33281 0.55117 -0.03671 0.10792  0.00489  96  LEU A N     
443  C  CA    . LEU A 66  ? 0.36313 0.18248 0.39834 -0.04110 0.10910  0.00698  96  LEU A CA    
444  C  C     . LEU A 66  ? 0.37682 0.20378 0.40723 -0.04392 0.11433  0.00626  96  LEU A C     
445  O  O     . LEU A 66  ? 0.41599 0.25240 0.45061 -0.04111 0.11826  0.00343  96  LEU A O     
446  C  CB    . LEU A 66  ? 0.35451 0.17739 0.39900 -0.03978 0.10902  0.00699  96  LEU A CB    
447  C  CG    . LEU A 66  ? 0.34917 0.16860 0.39950 -0.03567 0.10434  0.00754  96  LEU A CG    
448  C  CD1   . LEU A 66  ? 0.34119 0.16493 0.40005 -0.03345 0.10459  0.00721  96  LEU A CD1   
449  C  CD2   . LEU A 66  ? 0.40297 0.21212 0.44562 -0.03686 0.09898  0.01012  96  LEU A CD2   
450  N  N     . LEU A 67  ? 0.37786 0.20170 0.39897 -0.04918 0.11429  0.00886  97  LEU A N     
451  C  CA    . LEU A 67  ? 0.38266 0.21664 0.39892 -0.05236 0.11929  0.00892  97  LEU A CA    
452  C  C     . LEU A 67  ? 0.43516 0.26785 0.44644 -0.06083 0.11894  0.01327  97  LEU A C     
453  O  O     . LEU A 67  ? 0.51584 0.33551 0.52206 -0.06372 0.11409  0.01608  97  LEU A O     
454  C  CB    . LEU A 67  ? 0.39068 0.22356 0.39763 -0.05054 0.11984  0.00794  97  LEU A CB    
455  C  CG    . LEU A 67  ? 0.41858 0.25400 0.42733 -0.04274 0.12061  0.00335  97  LEU A CG    
456  C  CD1   . LEU A 67  ? 0.40626 0.23459 0.40472 -0.04069 0.11853  0.00274  97  LEU A CD1   
457  C  CD2   . LEU A 67  ? 0.41778 0.26874 0.42870 -0.04020 0.12625  0.00054  97  LEU A CD2   
458  N  N     . GLY A 68  ? 0.39078 0.23697 0.40278 -0.06482 0.12360  0.01386  98  GLY A N     
459  C  CA    . GLY A 68  ? 0.50427 0.35114 0.50889 -0.07461 0.12363  0.01867  98  GLY A CA    
460  C  C     . GLY A 68  ? 0.56524 0.42002 0.56063 -0.07705 0.12696  0.01982  98  GLY A C     
461  O  O     . GLY A 68  ? 0.47901 0.33127 0.47064 -0.07121 0.12701  0.01742  98  GLY A O     
462  N  N     . THR A 69  ? 0.48673 0.35216 0.47811 -0.08582 0.12961  0.02367  99  THR A N     
463  C  CA    . THR A 69  ? 0.51386 0.39078 0.49654 -0.08873 0.13335  0.02543  99  THR A CA    
464  C  C     . THR A 69  ? 0.56224 0.46515 0.54999 -0.08747 0.14010  0.02360  99  THR A C     
465  O  O     . THR A 69  ? 0.54006 0.45096 0.53753 -0.08633 0.14163  0.02175  99  THR A O     
466  C  CB    . THR A 69  ? 0.54133 0.41098 0.51312 -0.10088 0.13066  0.03233  99  THR A CB    
467  O  OG1   . THR A 69  ? 0.51151 0.38012 0.48610 -0.10946 0.12874  0.03580  99  THR A OG1   
468  C  CG2   . THR A 69  ? 0.47000 0.31561 0.43409 -0.09966 0.12440  0.03319  99  THR A CG2   
469  N  N     . THR A 70  ? 0.61415 0.53111 0.59481 -0.08668 0.14407  0.02384  100 THR A N     
470  C  CA    . THR A 70  ? 0.66124 0.60558 0.64488 -0.08410 0.15051  0.02189  100 THR A CA    
471  C  C     . THR A 70  ? 0.69088 0.65134 0.66506 -0.09168 0.15376  0.02687  100 THR A C     
472  O  O     . THR A 70  ? 0.74456 0.69351 0.70886 -0.09574 0.15133  0.03032  100 THR A O     
473  C  CB    . THR A 70  ? 0.63520 0.58335 0.62020 -0.06920 0.15232  0.01432  100 THR A CB    
474  O  OG1   . THR A 70  ? 0.68860 0.66436 0.67413 -0.06542 0.15833  0.01217  100 THR A OG1   
475  C  CG2   . THR A 70  ? 0.68027 0.61507 0.65505 -0.06399 0.14978  0.01319  100 THR A CG2   
476  N  N     . SER A 71  ? 0.70244 0.69118 0.67974 -0.09357 0.15934  0.02736  101 SER A N     
477  C  CA    . SER A 71  ? 0.78984 0.79992 0.75889 -0.10022 0.16327  0.03216  101 SER A CA    
478  C  C     . SER A 71  ? 0.81304 0.82892 0.77362 -0.08844 0.16550  0.02808  101 SER A C     
479  O  O     . SER A 71  ? 0.84073 0.86110 0.79111 -0.09305 0.16632  0.03231  101 SER A O     
480  C  CB    . SER A 71  ? 0.69036 0.73232 0.66580 -0.10511 0.16857  0.03375  101 SER A CB    
481  O  OG    . SER A 71  ? 0.98123 1.04367 0.95994 -0.09082 0.17331  0.02657  101 SER A OG    
482  N  N     . SER A 72  ? 0.79251 0.80688 0.75595 -0.07336 0.16590  0.02005  102 SER A N     
483  C  CA    . SER A 72  ? 0.75394 0.77165 0.70802 -0.06062 0.16693  0.01529  102 SER A CA    
484  C  C     . SER A 72  ? 0.72868 0.72229 0.67321 -0.06175 0.16236  0.01718  102 SER A C     
485  O  O     . SER A 72  ? 0.78759 0.75456 0.73451 -0.06136 0.15702  0.01616  102 SER A O     
486  C  CB    . SER A 72  ? 0.77927 0.79254 0.73721 -0.04544 0.16614  0.00656  102 SER A CB    
487  O  OG    . SER A 72  ? 0.86062 0.86684 0.80771 -0.03321 0.16449  0.00181  102 SER A OG    
488  N  N     . ALA A 73  ? 0.91052 0.91489 0.84407 -0.06265 0.16447  0.01987  103 ALA A N     
489  C  CA    . ALA A 73  ? 0.95134 0.93411 0.87478 -0.06236 0.16031  0.02109  103 ALA A CA    
490  C  C     . ALA A 73  ? 0.87445 0.84130 0.79431 -0.04722 0.15684  0.01341  103 ALA A C     
491  O  O     . ALA A 73  ? 0.89167 0.83302 0.80820 -0.04688 0.15144  0.01323  103 ALA A O     
492  C  CB    . ALA A 73  ? 0.72097 0.72098 0.63318 -0.06656 0.16372  0.02586  103 ALA A CB    
493  N  N     . ALA A 74  ? 0.83444 0.81556 0.75420 -0.03473 0.15929  0.00706  104 ALA A N     
494  C  CA    . ALA A 74  ? 0.87354 0.83795 0.78837 -0.02078 0.15501  -0.00020 104 ALA A CA    
495  C  C     . ALA A 74  ? 0.92737 0.86707 0.85145 -0.02211 0.14984  -0.00171 104 ALA A C     
496  O  O     . ALA A 74  ? 0.86721 0.78361 0.78727 -0.01923 0.14419  -0.00320 104 ALA A O     
497  C  CB    . ALA A 74  ? 0.73683 0.72084 0.64857 -0.00707 0.15808  -0.00677 104 ALA A CB    
498  N  N     . GLU A 75  ? 0.82760 0.77339 0.76411 -0.02636 0.15162  -0.00126 105 GLU A N     
499  C  CA    . GLU A 75  ? 0.75173 0.67697 0.69750 -0.02750 0.14712  -0.00235 105 GLU A CA    
500  C  C     . GLU A 75  ? 0.77133 0.67715 0.71748 -0.03724 0.14296  0.00287  105 GLU A C     
501  O  O     . GLU A 75  ? 0.79774 0.68294 0.74560 -0.03527 0.13763  0.00151  105 GLU A O     
502  C  CB    . GLU A 75  ? 0.75136 0.68862 0.70974 -0.03024 0.15015  -0.00257 105 GLU A CB    
503  C  CG    . GLU A 75  ? 0.80716 0.76282 0.76541 -0.01941 0.15377  -0.00847 105 GLU A CG    
504  C  CD    . GLU A 75  ? 1.05938 1.02694 1.03038 -0.02235 0.15668  -0.00865 105 GLU A CD    
505  O  OE1   . GLU A 75  ? 1.03335 0.99631 1.01263 -0.03336 0.15610  -0.00379 105 GLU A OE1   
506  O  OE2   . GLU A 75  ? 1.23411 1.21485 1.20590 -0.01303 0.15910  -0.01392 105 GLU A OE2   
507  N  N     . THR A 76  ? 0.75782 0.67023 0.70167 -0.04786 0.14492  0.00902  106 THR A N     
508  C  CA    . THR A 76  ? 0.69764 0.59063 0.63883 -0.05605 0.14043  0.01371  106 THR A CA    
509  C  C     . THR A 76  ? 0.77332 0.64971 0.70529 -0.04991 0.13615  0.01162  106 THR A C     
510  O  O     . THR A 76  ? 0.82817 0.68447 0.76165 -0.05044 0.13074  0.01172  106 THR A O     
511  C  CB    . THR A 76  ? 0.79612 0.69842 0.73225 -0.06801 0.14283  0.02067  106 THR A CB    
512  O  OG1   . THR A 76  ? 0.73268 0.65100 0.67710 -0.07449 0.14630  0.02283  106 THR A OG1   
513  C  CG2   . THR A 76  ? 0.58649 0.46616 0.51845 -0.07579 0.13730  0.02513  106 THR A CG2   
514  N  N     . LYS A 77  ? 0.74998 0.63553 0.67191 -0.04359 0.13828  0.00964  107 LYS A N     
515  C  CA    . LYS A 77  ? 0.85274 0.72235 0.76459 -0.03780 0.13385  0.00768  107 LYS A CA    
516  C  C     . LYS A 77  ? 0.88225 0.73714 0.79715 -0.02906 0.12905  0.00209  107 LYS A C     
517  O  O     . LYS A 77  ? 0.79307 0.62859 0.70545 -0.02866 0.12334  0.00194  107 LYS A O     
518  C  CB    . LYS A 77  ? 0.83480 0.71859 0.73437 -0.03196 0.13711  0.00657  107 LYS A CB    
519  C  CG    . LYS A 77  ? 0.90847 0.77589 0.79628 -0.02509 0.13228  0.00416  107 LYS A CG    
520  C  CD    . LYS A 77  ? 1.06796 0.91780 0.95294 -0.03352 0.12843  0.00893  107 LYS A CD    
521  C  CE    . LYS A 77  ? 1.27489 1.11056 1.14749 -0.02686 0.12392  0.00670  107 LYS A CE    
522  N  NZ    . LYS A 77  ? 1.22829 1.04587 1.09829 -0.03399 0.11957  0.01067  107 LYS A NZ    
523  N  N     . GLU A 78  ? 0.77337 0.63749 0.69309 -0.02239 0.13098  -0.00232 108 GLU A N     
524  C  CA    . GLU A 78  ? 0.63667 0.48649 0.55904 -0.01549 0.12610  -0.00698 108 GLU A CA    
525  C  C     . GLU A 78  ? 0.75103 0.58585 0.68342 -0.02220 0.12203  -0.00434 108 GLU A C     
526  O  O     . GLU A 78  ? 0.68139 0.49928 0.61211 -0.02030 0.11612  -0.00541 108 GLU A O     
527  C  CB    . GLU A 78  ? 0.80963 0.67225 0.73640 -0.00876 0.12915  -0.01140 108 GLU A CB    
528  C  CG    . GLU A 78  ? 0.80106 0.67933 0.71691 0.00075  0.13245  -0.01521 108 GLU A CG    
529  C  CD    . GLU A 78  ? 1.05558 0.95198 0.97699 0.00572  0.13688  -0.01858 108 GLU A CD    
530  O  OE1   . GLU A 78  ? 1.02547 0.91952 0.95890 0.00244  0.13683  -0.01847 108 GLU A OE1   
531  O  OE2   . GLU A 78  ? 1.05908 0.97334 0.97258 0.01346  0.14044  -0.02143 108 GLU A OE2   
532  N  N     . VAL A 79  ? 0.72782 0.56938 0.67017 -0.02997 0.12477  -0.00079 109 VAL A N     
533  C  CA    . VAL A 79  ? 0.69652 0.52596 0.64825 -0.03476 0.12098  0.00130  109 VAL A CA    
534  C  C     . VAL A 79  ? 0.74812 0.56314 0.69426 -0.03921 0.11658  0.00467  109 VAL A C     
535  O  O     . VAL A 79  ? 0.70463 0.50667 0.65429 -0.03903 0.11143  0.00470  109 VAL A O     
536  C  CB    . VAL A 79  ? 0.71952 0.55914 0.68145 -0.04086 0.12449  0.00380  109 VAL A CB    
537  C  CG1   . VAL A 79  ? 0.78936 0.61653 0.75691 -0.04655 0.12037  0.00712  109 VAL A CG1   
538  C  CG2   . VAL A 79  ? 0.57120 0.41945 0.54135 -0.03533 0.12670  -0.00025 109 VAL A CG2   
539  N  N     . ASP A 80  ? 0.75111 0.56907 0.68817 -0.04315 0.11840  0.00766  110 ASP A N     
540  C  CA    . ASP A 80  ? 0.78504 0.58844 0.71470 -0.04611 0.11397  0.01027  110 ASP A CA    
541  C  C     . ASP A 80  ? 0.75750 0.54888 0.68253 -0.03927 0.10901  0.00683  110 ASP A C     
542  O  O     . ASP A 80  ? 0.76034 0.53835 0.68687 -0.04020 0.10357  0.00756  110 ASP A O     
543  C  CB    . ASP A 80  ? 0.75280 0.56241 0.67178 -0.05066 0.11706  0.01374  110 ASP A CB    
544  C  CG    . ASP A 80  ? 1.08759 0.90637 1.00980 -0.05989 0.12046  0.01836  110 ASP A CG    
545  O  OD1   . ASP A 80  ? 0.92710 0.74255 0.85864 -0.06293 0.11908  0.01914  110 ASP A OD1   
546  O  OD2   . ASP A 80  ? 1.20318 1.03260 1.11803 -0.06444 0.12416  0.02151  110 ASP A OD2   
547  N  N     . GLN A 81  ? 0.67579 0.47183 0.59462 -0.03204 0.11021  0.00297  111 GLN A N     
548  C  CA    . GLN A 81  ? 0.77190 0.55471 0.68429 -0.02565 0.10449  -0.00039 111 GLN A CA    
549  C  C     . GLN A 81  ? 0.77402 0.54860 0.69602 -0.02484 0.10001  -0.00189 111 GLN A C     
550  O  O     . GLN A 81  ? 0.70309 0.46449 0.62325 -0.02485 0.09390  -0.00180 111 GLN A O     
551  C  CB    . GLN A 81  ? 0.80662 0.59606 0.70949 -0.01694 0.10633  -0.00474 111 GLN A CB    
552  C  CG    . GLN A 81  ? 0.95477 0.75352 0.84641 -0.01629 0.11020  -0.00346 111 GLN A CG    
553  C  CD    . GLN A 81  ? 1.02916 0.84027 0.91291 -0.00671 0.11323  -0.00788 111 GLN A CD    
554  O  OE1   . GLN A 81  ? 0.99233 0.81419 0.86640 -0.00436 0.11658  -0.00740 111 GLN A OE1   
555  N  NE2   . GLN A 81  ? 0.90023 0.71040 0.78716 -0.00046 0.11185  -0.01232 111 GLN A NE2   
556  N  N     . GLU A 82  ? 0.75235 0.53562 0.68416 -0.02441 0.10294  -0.00299 112 GLU A N     
557  C  CA    . GLU A 82  ? 0.64753 0.42501 0.58899 -0.02409 0.09920  -0.00392 112 GLU A CA    
558  C  C     . GLU A 82  ? 0.67039 0.44125 0.61861 -0.02997 0.09571  -0.00012 112 GLU A C     
559  O  O     . GLU A 82  ? 0.66761 0.42953 0.61751 -0.02965 0.09002  -0.00024 112 GLU A O     
560  C  CB    . GLU A 82  ? 0.65531 0.44491 0.60556 -0.02275 0.10393  -0.00546 112 GLU A CB    
561  C  CG    . GLU A 82  ? 0.69208 0.47741 0.65152 -0.02177 0.10075  -0.00659 112 GLU A CG    
562  C  CD    . GLU A 82  ? 0.67447 0.47184 0.64274 -0.02050 0.10565  -0.00800 112 GLU A CD    
563  O  OE1   . GLU A 82  ? 0.67731 0.48648 0.64277 -0.01882 0.11103  -0.00917 112 GLU A OE1   
564  O  OE2   . GLU A 82  ? 0.67712 0.47333 0.65506 -0.02122 0.10412  -0.00779 112 GLU A OE2   
565  N  N     . SER A 83  ? 0.62702 0.40219 0.57778 -0.03506 0.09849  0.00317  113 SER A N     
566  C  CA    . SER A 83  ? 0.63226 0.40055 0.58725 -0.03911 0.09461  0.00633  113 SER A CA    
567  C  C     . SER A 83  ? 0.66854 0.42526 0.61534 -0.03853 0.08909  0.00671  113 SER A C     
568  O  O     . SER A 83  ? 0.66233 0.41388 0.61370 -0.03905 0.08419  0.00764  113 SER A O     
569  C  CB    . SER A 83  ? 0.65402 0.42532 0.60899 -0.04434 0.09734  0.00963  113 SER A CB    
570  O  OG    . SER A 83  ? 0.74448 0.51073 0.70533 -0.04622 0.09363  0.01165  113 SER A OG    
571  N  N     . GLN A 84  ? 0.81844 0.57265 0.75346 -0.03712 0.08989  0.00597  114 GLN A N     
572  C  CA    . GLN A 84  ? 0.80881 0.55149 0.73489 -0.03638 0.08456  0.00619  114 GLN A CA    
573  C  C     . GLN A 84  ? 0.67197 0.40843 0.59929 -0.03310 0.07908  0.00375  114 GLN A C     
574  O  O     . GLN A 84  ? 0.87093 0.59980 0.79794 -0.03426 0.07338  0.00482  114 GLN A O     
575  C  CB    . GLN A 84  ? 0.91157 0.65392 0.82435 -0.03530 0.08702  0.00607  114 GLN A CB    
576  C  CG    . GLN A 84  ? 0.90251 0.64667 0.81160 -0.04072 0.08994  0.00992  114 GLN A CG    
577  C  CD    . GLN A 84  ? 1.19118 0.94586 1.09314 -0.04104 0.09611  0.01035  114 GLN A CD    
578  O  OE1   . GLN A 84  ? 1.33253 1.09124 1.22857 -0.03547 0.09751  0.00735  114 GLN A OE1   
579  N  NE2   . GLN A 84  ? 0.99663 0.75619 0.89821 -0.04752 0.09939  0.01423  114 GLN A NE2   
580  N  N     . ARG A 85  ? 0.66419 0.40375 0.59228 -0.02945 0.08034  0.00078  115 ARG A N     
581  C  CA    . ARG A 85  ? 0.66015 0.39164 0.58752 -0.02731 0.07422  -0.00115 115 ARG A CA    
582  C  C     . ARG A 85  ? 0.76267 0.49701 0.70365 -0.03052 0.07193  0.00057  115 ARG A C     
583  O  O     . ARG A 85  ? 0.80367 0.53140 0.74506 -0.03204 0.06542  0.00132  115 ARG A O     
584  C  CB    . ARG A 85  ? 0.73703 0.46857 0.65831 -0.02151 0.07533  -0.00522 115 ARG A CB    
585  C  CG    . ARG A 85  ? 0.90529 0.63726 0.81275 -0.01626 0.07795  -0.00763 115 ARG A CG    
586  C  CD    . ARG A 85  ? 0.83289 0.56507 0.73380 -0.00886 0.07818  -0.01225 115 ARG A CD    
587  N  NE    . ARG A 85  ? 1.07217 0.81971 0.97214 -0.00549 0.08608  -0.01356 115 ARG A NE    
588  C  CZ    . ARG A 85  ? 1.04873 0.80814 0.95809 -0.00549 0.09100  -0.01411 115 ARG A CZ    
589  N  NH1   . ARG A 85  ? 1.01383 0.77037 0.93340 -0.00775 0.08884  -0.01383 115 ARG A NH1   
590  N  NH2   . ARG A 85  ? 0.98647 0.76170 0.89501 -0.00345 0.09801  -0.01470 115 ARG A NH2   
591  N  N     . HIS A 86  ? 0.67578 0.42030 0.62731 -0.03176 0.07674  0.00145  116 HIS A N     
592  C  CA    . HIS A 86  ? 0.65536 0.40391 0.61952 -0.03363 0.07477  0.00276  116 HIS A CA    
593  C  C     . HIS A 86  ? 0.50922 0.26234 0.48163 -0.03660 0.07453  0.00599  116 HIS A C     
594  O  O     . HIS A 86  ? 0.63602 0.39157 0.61646 -0.03787 0.07075  0.00757  116 HIS A O     
595  C  CB    . HIS A 86  ? 0.61390 0.36925 0.58335 -0.03132 0.07905  0.00062  116 HIS A CB    
596  C  CG    . HIS A 86  ? 0.65230 0.40189 0.61224 -0.02697 0.07798  -0.00302 116 HIS A CG    
597  N  ND1   . HIS A 86  ? 0.66531 0.40537 0.62179 -0.02685 0.07138  -0.00367 116 HIS A ND1   
598  C  CD2   . HIS A 86  ? 0.63232 0.38419 0.58446 -0.02228 0.08196  -0.00621 116 HIS A CD2   
599  C  CE1   . HIS A 86  ? 0.63152 0.36573 0.57709 -0.02159 0.07092  -0.00751 116 HIS A CE1   
600  N  NE2   . HIS A 86  ? 0.77131 0.51373 0.71438 -0.01808 0.07755  -0.00932 116 HIS A NE2   
601  N  N     . GLY A 87  ? 0.62228 0.37667 0.59194 -0.03756 0.07795  0.00705  117 GLY A N     
602  C  CA    . GLY A 87  ? 0.71518 0.47064 0.68919 -0.03933 0.07652  0.00974  117 GLY A CA    
603  C  C     . GLY A 87  ? 0.65129 0.41506 0.63796 -0.03897 0.07735  0.01039  117 GLY A C     
604  O  O     . GLY A 87  ? 0.64937 0.41456 0.64064 -0.03869 0.07376  0.01213  117 GLY A O     
605  N  N     . ASP A 88  ? 0.55960 0.32938 0.55126 -0.03821 0.08181  0.00884  118 ASP A N     
606  C  CA    . ASP A 88  ? 0.56623 0.34389 0.56992 -0.03741 0.08257  0.00926  118 ASP A CA    
607  C  C     . ASP A 88  ? 0.53005 0.31312 0.53652 -0.03766 0.08832  0.00863  118 ASP A C     
608  O  O     . ASP A 88  ? 0.54553 0.33539 0.56108 -0.03633 0.09022  0.00792  118 ASP A O     
609  C  CB    . ASP A 88  ? 0.53288 0.31303 0.54208 -0.03636 0.08074  0.00824  118 ASP A CB    
610  C  CG    . ASP A 88  ? 0.61673 0.39399 0.61975 -0.03491 0.08304  0.00524  118 ASP A CG    
611  O  OD1   . ASP A 88  ? 0.56295 0.34006 0.55944 -0.03425 0.08715  0.00387  118 ASP A OD1   
612  O  OD2   . ASP A 88  ? 0.71386 0.48923 0.71775 -0.03427 0.08039  0.00431  118 ASP A OD2   
613  N  N     . ILE A 89  ? 0.47428 0.25495 0.47296 -0.03986 0.09088  0.00924  119 ILE A N     
614  C  CA    . ILE A 89  ? 0.44281 0.22945 0.44307 -0.04163 0.09598  0.00930  119 ILE A CA    
615  C  C     . ILE A 89  ? 0.46977 0.25245 0.46890 -0.04441 0.09420  0.01212  119 ILE A C     
616  O  O     . ILE A 89  ? 0.61579 0.38989 0.60659 -0.04595 0.09086  0.01390  119 ILE A O     
617  C  CB    . ILE A 89  ? 0.40661 0.19555 0.39810 -0.04281 0.10017  0.00837  119 ILE A CB    
618  C  CG1   . ILE A 89  ? 0.48179 0.27415 0.47358 -0.03832 0.10151  0.00477  119 ILE A CG1   
619  C  CG2   . ILE A 89  ? 0.46989 0.26630 0.46226 -0.04642 0.10486  0.00955  119 ILE A CG2   
620  C  CD1   . ILE A 89  ? 0.58832 0.38532 0.57123 -0.03730 0.10556  0.00317  119 ILE A CD1   
621  N  N     . ILE A 90  ? 0.49279 0.28035 0.49935 -0.04451 0.09568  0.01233  120 ILE A N     
622  C  CA    . ILE A 90  ? 0.43835 0.22099 0.44227 -0.04717 0.09383  0.01472  120 ILE A CA    
623  C  C     . ILE A 90  ? 0.41976 0.20711 0.42089 -0.05240 0.09869  0.01555  120 ILE A C     
624  O  O     . ILE A 90  ? 0.54365 0.34148 0.55224 -0.05161 0.10310  0.01377  120 ILE A O     
625  C  CB    . ILE A 90  ? 0.38925 0.17422 0.40273 -0.04333 0.09149  0.01440  120 ILE A CB    
626  C  CG1   . ILE A 90  ? 0.38569 0.17023 0.40288 -0.03843 0.08690  0.01403  120 ILE A CG1   
627  C  CG2   . ILE A 90  ? 0.49551 0.27298 0.50395 -0.04564 0.08873  0.01655  120 ILE A CG2   
628  C  CD1   . ILE A 90  ? 0.43129 0.22354 0.46021 -0.03380 0.08602  0.01335  120 ILE A CD1   
629  N  N     . GLN A 91  ? 0.46724 0.24766 0.45747 -0.05802 0.09771  0.01846  121 GLN A N     
630  C  CA    . GLN A 91  ? 0.44834 0.23557 0.43529 -0.06442 0.10226  0.02011  121 GLN A CA    
631  C  C     . GLN A 91  ? 0.53468 0.31208 0.51327 -0.07127 0.09883  0.02416  121 GLN A C     
632  O  O     . GLN A 91  ? 0.62257 0.38579 0.59164 -0.07195 0.09348  0.02599  121 GLN A O     
633  C  CB    . GLN A 91  ? 0.53229 0.32412 0.51171 -0.06612 0.10577  0.02015  121 GLN A CB    
634  C  CG    . GLN A 91  ? 0.53201 0.33688 0.50976 -0.07196 0.11142  0.02167  121 GLN A CG    
635  C  CD    . GLN A 91  ? 0.57882 0.38938 0.54786 -0.07257 0.11462  0.02182  121 GLN A CD    
636  O  OE1   . GLN A 91  ? 0.69273 0.49302 0.65199 -0.07403 0.11175  0.02361  121 GLN A OE1   
637  N  NE2   . GLN A 91  ? 0.57043 0.39768 0.54243 -0.07053 0.12038  0.01965  121 GLN A NE2   
638  N  N     . LYS A 92  ? 0.51949 0.30391 0.50065 -0.07647 0.10146  0.02555  122 LYS A N     
639  C  CA    . LYS A 92  ? 0.47710 0.25299 0.44838 -0.08549 0.09847  0.03013  122 LYS A CA    
640  C  C     . LYS A 92  ? 0.62256 0.41384 0.59342 -0.09351 0.10452  0.03229  122 LYS A C     
641  O  O     . LYS A 92  ? 0.57447 0.38325 0.55406 -0.09037 0.11076  0.02945  122 LYS A O     
642  C  CB    . LYS A 92  ? 0.46649 0.23353 0.44030 -0.08451 0.09343  0.03036  122 LYS A CB    
643  C  CG    . LYS A 92  ? 0.56842 0.32053 0.53969 -0.07693 0.08645  0.02903  122 LYS A CG    
644  C  CD    . LYS A 92  ? 0.44734 0.19014 0.41873 -0.07492 0.08080  0.02918  122 LYS A CD    
645  C  CE    . LYS A 92  ? 0.62563 0.35401 0.58240 -0.08442 0.07595  0.03368  122 LYS A CE    
646  N  NZ    . LYS A 92  ? 0.71974 0.43318 0.67207 -0.08065 0.06798  0.03351  122 LYS A NZ    
647  N  N     . ASP A 93  ? 0.57611 0.36106 0.53576 -0.10401 0.10220  0.03752  123 ASP A N     
648  C  CA    . ASP A 93  ? 0.61012 0.41153 0.56784 -0.11334 0.10757  0.04080  123 ASP A CA    
649  C  C     . ASP A 93  ? 0.70497 0.51588 0.67062 -0.11755 0.10884  0.04140  123 ASP A C     
650  O  O     . ASP A 93  ? 0.81697 0.62012 0.77582 -0.12734 0.10477  0.04603  123 ASP A O     
651  C  CB    . ASP A 93  ? 0.74491 0.53603 0.68619 -0.12419 0.10435  0.04700  123 ASP A CB    
652  C  CG    . ASP A 93  ? 0.88385 0.69557 0.82285 -0.13372 0.11042  0.05086  123 ASP A CG    
653  O  OD1   . ASP A 93  ? 1.06373 0.89830 1.01366 -0.13025 0.11730  0.04796  123 ASP A OD1   
654  O  OD2   . ASP A 93  ? 1.18375 0.98949 1.10943 -0.14450 0.10814  0.05687  123 ASP A OD2   
655  N  N     . PHE A 94  ? 0.55494 0.38221 0.53425 -0.11025 0.11416  0.03668  124 PHE A N     
656  C  CA    . PHE A 94  ? 0.44950 0.29078 0.43722 -0.11374 0.11694  0.03675  124 PHE A CA    
657  C  C     . PHE A 94  ? 0.53823 0.40426 0.53462 -0.10840 0.12523  0.03293  124 PHE A C     
658  O  O     . PHE A 94  ? 0.45623 0.32338 0.45535 -0.09861 0.12722  0.02852  124 PHE A O     
659  C  CB    . PHE A 94  ? 0.42821 0.25931 0.42372 -0.10812 0.11283  0.03410  124 PHE A CB    
660  C  CG    . PHE A 94  ? 0.41248 0.24538 0.41826 -0.09492 0.11459  0.02808  124 PHE A CG    
661  C  CD1   . PHE A 94  ? 0.50017 0.31754 0.50288 -0.08853 0.11014  0.02680  124 PHE A CD1   
662  C  CD2   . PHE A 94  ? 0.39798 0.24845 0.41560 -0.08932 0.12036  0.02394  124 PHE A CD2   
663  C  CE1   . PHE A 94  ? 0.45926 0.27925 0.47113 -0.07791 0.11139  0.02205  124 PHE A CE1   
664  C  CE2   . PHE A 94  ? 0.38570 0.23635 0.41123 -0.07836 0.12131  0.01900  124 PHE A CE2   
665  C  CZ    . PHE A 94  ? 0.44783 0.28354 0.47064 -0.07331 0.11680  0.01838  124 PHE A CZ    
666  N  N     . LEU A 95  ? 0.48580 0.37149 0.48539 -0.11485 0.12949  0.03466  125 LEU A N     
667  C  CA    . LEU A 95  ? 0.45456 0.36513 0.46098 -0.10893 0.13705  0.03076  125 LEU A CA    
668  C  C     . LEU A 95  ? 0.52272 0.43276 0.54043 -0.09614 0.13805  0.02392  125 LEU A C     
669  O  O     . LEU A 95  ? 0.41032 0.31754 0.43579 -0.09553 0.13638  0.02290  125 LEU A O     
670  C  CB    . LEU A 95  ? 0.45099 0.38427 0.45991 -0.11809 0.14090  0.03388  125 LEU A CB    
671  C  CG    . LEU A 95  ? 0.56126 0.52287 0.57606 -0.11082 0.14870  0.02951  125 LEU A CG    
672  C  CD1   . LEU A 95  ? 0.47824 0.44626 0.48442 -0.10716 0.15162  0.02912  125 LEU A CD1   
673  C  CD2   . LEU A 95  ? 0.48051 0.46717 0.49955 -0.11926 0.15239  0.03227  125 LEU A CD2   
674  N  N     . ASP A 96  ? 0.47179 0.38377 0.48949 -0.08613 0.14032  0.01941  126 ASP A N     
675  C  CA    . ASP A 96  ? 0.38066 0.28877 0.40685 -0.07474 0.14020  0.01354  126 ASP A CA    
676  C  C     . ASP A 96  ? 0.50171 0.43129 0.53520 -0.06999 0.14583  0.00959  126 ASP A C     
677  O  O     . ASP A 96  ? 0.48424 0.42635 0.51497 -0.06389 0.14973  0.00636  126 ASP A O     
678  C  CB    . ASP A 96  ? 0.48872 0.38676 0.50979 -0.06729 0.13876  0.01096  126 ASP A CB    
679  C  CG    . ASP A 96  ? 0.51795 0.40693 0.54624 -0.05806 0.13661  0.00655  126 ASP A CG    
680  O  OD1   . ASP A 96  ? 0.40604 0.30132 0.44346 -0.05516 0.13808  0.00420  126 ASP A OD1   
681  O  OD2   . ASP A 96  ? 0.49038 0.36652 0.51499 -0.05420 0.13332  0.00572  126 ASP A OD2   
682  N  N     . VAL A 97  ? 0.46125 0.39470 0.50333 -0.07196 0.14584  0.00952  127 VAL A N     
683  C  CA    . VAL A 97  ? 0.38996 0.34298 0.43970 -0.06712 0.15068  0.00553  127 VAL A CA    
684  C  C     . VAL A 97  ? 0.45628 0.40119 0.51605 -0.06292 0.14849  0.00306  127 VAL A C     
685  O  O     . VAL A 97  ? 0.43318 0.36065 0.49379 -0.06563 0.14343  0.00539  127 VAL A O     
686  C  CB    . VAL A 97  ? 0.40530 0.37978 0.45496 -0.07665 0.15418  0.00908  127 VAL A CB    
687  C  CG1   . VAL A 97  ? 0.37090 0.35822 0.41108 -0.07973 0.15727  0.01132  127 VAL A CG1   
688  C  CG2   . VAL A 97  ? 0.36612 0.32991 0.41590 -0.08854 0.14960  0.01484  127 VAL A CG2   
689  N  N     . TYR A 98  ? 0.46808 0.42554 0.53486 -0.05546 0.15202  -0.00184 128 TYR A N     
690  C  CA    . TYR A 98  ? 0.42398 0.37389 0.50019 -0.05023 0.15017  -0.00454 128 TYR A CA    
691  C  C     . TYR A 98  ? 0.37468 0.31771 0.45435 -0.05841 0.14660  -0.00044 128 TYR A C     
692  O  O     . TYR A 98  ? 0.34889 0.27703 0.43241 -0.05552 0.14253  -0.00067 128 TYR A O     
693  C  CB    . TYR A 98  ? 0.32883 0.29501 0.41127 -0.04235 0.15462  -0.01000 128 TYR A CB    
694  C  CG    . TYR A 98  ? 0.44897 0.40548 0.53901 -0.03429 0.15286  -0.01363 128 TYR A CG    
695  C  CD1   . TYR A 98  ? 0.35644 0.30233 0.44435 -0.02589 0.15145  -0.01683 128 TYR A CD1   
696  C  CD2   . TYR A 98  ? 0.44692 0.40477 0.54560 -0.03555 0.15223  -0.01354 128 TYR A CD2   
697  C  CE1   . TYR A 98  ? 0.40335 0.34141 0.49776 -0.01960 0.14976  -0.01936 128 TYR A CE1   
698  C  CE2   . TYR A 98  ? 0.49957 0.44963 0.60495 -0.02812 0.15079  -0.01653 128 TYR A CE2   
699  C  CZ    . TYR A 98  ? 0.51208 0.45279 0.61544 -0.02044 0.14970  -0.01923 128 TYR A CZ    
700  O  OH    . TYR A 98  ? 0.58159 0.51565 0.69111 -0.01405 0.14824  -0.02149 128 TYR A OH    
701  N  N     . TYR A 99  ? 0.33362 0.28785 0.41148 -0.06824 0.14773  0.00328  129 TYR A N     
702  C  CA    . TYR A 99  ? 0.39301 0.33925 0.47261 -0.07644 0.14330  0.00713  129 TYR A CA    
703  C  C     . TYR A 99  ? 0.41789 0.34193 0.48857 -0.08262 0.13678  0.01197  129 TYR A C     
704  O  O     . TYR A 99  ? 0.48646 0.40043 0.55528 -0.08932 0.13180  0.01534  129 TYR A O     
705  C  CB    . TYR A 99  ? 0.45016 0.41743 0.53181 -0.08474 0.14644  0.00911  129 TYR A CB    
706  C  CG    . TYR A 99  ? 0.62411 0.60826 0.71590 -0.07581 0.15122  0.00322  129 TYR A CG    
707  C  CD1   . TYR A 99  ? 0.51682 0.49083 0.61604 -0.06675 0.14960  -0.00083 129 TYR A CD1   
708  C  CD2   . TYR A 99  ? 0.65316 0.66399 0.74632 -0.07564 0.15728  0.00160  129 TYR A CD2   
709  C  CE1   . TYR A 99  ? 0.70237 0.69012 0.80968 -0.05833 0.15364  -0.00627 129 TYR A CE1   
710  C  CE2   . TYR A 99  ? 0.67241 0.69780 0.77347 -0.06640 0.16123  -0.00425 129 TYR A CE2   
711  C  CZ    . TYR A 99  ? 0.78910 0.80187 0.89701 -0.05794 0.15932  -0.00819 129 TYR A CZ    
712  O  OH    . TYR A 99  ? 0.66957 0.69575 0.78416 -0.04883 0.16300  -0.01395 129 TYR A OH    
713  N  N     . ASN A 100 ? 0.37401 0.29015 0.43821 -0.08025 0.13630  0.01217  130 ASN A N     
714  C  CA    . ASN A 100 ? 0.36146 0.25550 0.41737 -0.08336 0.12984  0.01564  130 ASN A CA    
715  C  C     . ASN A 100 ? 0.39199 0.27243 0.45100 -0.07291 0.12709  0.01241  130 ASN A C     
716  O  O     . ASN A 100 ? 0.37717 0.24130 0.42928 -0.07334 0.12216  0.01446  130 ASN A O     
717  C  CB    . ASN A 100 ? 0.37346 0.26779 0.41828 -0.09007 0.13045  0.01929  130 ASN A CB    
718  C  CG    . ASN A 100 ? 0.45365 0.34518 0.49009 -0.10404 0.12733  0.02575  130 ASN A CG    
719  O  OD1   . ASN A 100 ? 0.48295 0.36496 0.51966 -0.10797 0.12259  0.02753  130 ASN A OD1   
720  N  ND2   . ASN A 100 ? 0.50921 0.40821 0.53724 -0.11162 0.12944  0.02943  130 ASN A ND2   
721  N  N     . LEU A 101 ? 0.38877 0.27609 0.45761 -0.06372 0.12991  0.00761  131 LEU A N     
722  C  CA    . LEU A 101 ? 0.35168 0.22819 0.42374 -0.05507 0.12719  0.00532  131 LEU A CA    
723  C  C     . LEU A 101 ? 0.33831 0.19873 0.40911 -0.05507 0.12040  0.00753  131 LEU A C     
724  O  O     . LEU A 101 ? 0.33792 0.18849 0.40757 -0.05031 0.11700  0.00737  131 LEU A O     
725  C  CB    . LEU A 101 ? 0.35824 0.24443 0.44041 -0.04661 0.13081  0.00048  131 LEU A CB    
726  C  CG    . LEU A 101 ? 0.32085 0.21725 0.40102 -0.04315 0.13560  -0.00252 131 LEU A CG    
727  C  CD1   . LEU A 101 ? 0.35390 0.25812 0.44205 -0.03469 0.13855  -0.00748 131 LEU A CD1   
728  C  CD2   . LEU A 101 ? 0.32614 0.21198 0.39937 -0.04162 0.13318  -0.00187 131 LEU A CD2   
729  N  N     . THR A 102 ? 0.34290 0.20040 0.41297 -0.06000 0.11776  0.00958  132 THR A N     
730  C  CA    . THR A 102 ? 0.34869 0.18927 0.41510 -0.05841 0.11034  0.01121  132 THR A CA    
731  C  C     . THR A 102 ? 0.36243 0.18834 0.41632 -0.06201 0.10553  0.01448  132 THR A C     
732  O  O     . THR A 102 ? 0.39312 0.20828 0.44504 -0.05591 0.10093  0.01413  132 THR A O     
733  C  CB    . THR A 102 ? 0.35378 0.19162 0.41964 -0.06315 0.10737  0.01273  132 THR A CB    
734  O  OG1   . THR A 102 ? 0.33998 0.18983 0.41809 -0.05751 0.11109  0.00910  132 THR A OG1   
735  C  CG2   . THR A 102 ? 0.36466 0.18203 0.42250 -0.06137 0.09831  0.01454  132 THR A CG2   
736  N  N     . LEU A 103 ? 0.37296 0.20008 0.41839 -0.07146 0.10682  0.01762  133 LEU A N     
737  C  CA    . LEU A 103 ? 0.38598 0.19968 0.41917 -0.07460 0.10282  0.02050  133 LEU A CA    
738  C  C     . LEU A 103 ? 0.40762 0.22193 0.44354 -0.06662 0.10416  0.01790  133 LEU A C     
739  O  O     . LEU A 103 ? 0.41038 0.21154 0.44032 -0.06352 0.09893  0.01861  133 LEU A O     
740  C  CB    . LEU A 103 ? 0.39672 0.21562 0.42164 -0.08578 0.10541  0.02422  133 LEU A CB    
741  C  CG    . LEU A 103 ? 0.47522 0.29330 0.49532 -0.09669 0.10325  0.02819  133 LEU A CG    
742  C  CD1   . LEU A 103 ? 0.50101 0.32555 0.51211 -0.10830 0.10567  0.03272  133 LEU A CD1   
743  C  CD2   . LEU A 103 ? 0.44860 0.24343 0.45981 -0.09706 0.09365  0.03013  133 LEU A CD2   
744  N  N     . LYS A 104 ? 0.36683 0.19602 0.41113 -0.06288 0.11056  0.01477  134 LYS A N     
745  C  CA    . LYS A 104 ? 0.36340 0.19189 0.40864 -0.05674 0.11110  0.01276  134 LYS A CA    
746  C  C     . LYS A 104 ? 0.38483 0.20646 0.43514 -0.04907 0.10669  0.01152  134 LYS A C     
747  O  O     . LYS A 104 ? 0.37904 0.19246 0.42513 -0.04652 0.10292  0.01216  134 LYS A O     
748  C  CB    . LYS A 104 ? 0.35318 0.19649 0.40457 -0.05351 0.11760  0.00934  134 LYS A CB    
749  C  CG    . LYS A 104 ? 0.35118 0.19165 0.40175 -0.04813 0.11714  0.00754  134 LYS A CG    
750  C  CD    . LYS A 104 ? 0.37371 0.22550 0.42592 -0.04494 0.12242  0.00414  134 LYS A CD    
751  C  CE    . LYS A 104 ? 0.35617 0.21410 0.39974 -0.04998 0.12567  0.00531  134 LYS A CE    
752  N  NZ    . LYS A 104 ? 0.45221 0.31711 0.49354 -0.04459 0.12895  0.00166  134 LYS A NZ    
753  N  N     . THR A 105 ? 0.36633 0.19248 0.42561 -0.04521 0.10700  0.00988  135 THR A N     
754  C  CA    . THR A 105 ? 0.37595 0.19860 0.44052 -0.03745 0.10310  0.00893  135 THR A CA    
755  C  C     . THR A 105 ? 0.35334 0.16144 0.40864 -0.03735 0.09579  0.01135  135 THR A C     
756  O  O     . THR A 105 ? 0.35339 0.15767 0.40792 -0.03195 0.09199  0.01136  135 THR A O     
757  C  CB    . THR A 105 ? 0.39830 0.22852 0.47318 -0.03351 0.10487  0.00687  135 THR A CB    
758  O  OG1   . THR A 105 ? 0.45632 0.29848 0.53931 -0.03088 0.11055  0.00405  135 THR A OG1   
759  C  CG2   . THR A 105 ? 0.32789 0.15418 0.40639 -0.02594 0.09988  0.00667  135 THR A CG2   
760  N  N     . MET A 106 ? 0.36500 0.16474 0.41197 -0.04350 0.09326  0.01355  136 MET A N     
761  C  CA    . MET A 106 ? 0.37871 0.16187 0.41466 -0.04234 0.08516  0.01545  136 MET A CA    
762  C  C     . MET A 106 ? 0.38768 0.16343 0.41414 -0.04397 0.08317  0.01694  136 MET A C     
763  O  O     . MET A 106 ? 0.41779 0.18397 0.43837 -0.03857 0.07708  0.01711  136 MET A O     
764  C  CB    . MET A 106 ? 0.39183 0.16497 0.41921 -0.04934 0.08164  0.01779  136 MET A CB    
765  C  CG    . MET A 106 ? 0.43244 0.20818 0.46702 -0.04541 0.08065  0.01617  136 MET A CG    
766  S  SD    . MET A 106 ? 0.52381 0.29792 0.56346 -0.03079 0.07580  0.01346  136 MET A SD    
767  C  CE    . MET A 106 ? 0.49596 0.24881 0.51717 -0.02901 0.06600  0.01547  136 MET A CE    
768  N  N     . MET A 107 ? 0.41259 0.19443 0.43809 -0.04990 0.08839  0.01754  137 MET A N     
769  C  CA    . MET A 107 ? 0.40311 0.17882 0.42049 -0.05057 0.08682  0.01856  137 MET A CA    
770  C  C     . MET A 107 ? 0.44719 0.22650 0.47109 -0.04184 0.08550  0.01646  137 MET A C     
771  O  O     . MET A 107 ? 0.39303 0.16354 0.41019 -0.03859 0.08010  0.01712  137 MET A O     
772  C  CB    . MET A 107 ? 0.39501 0.17865 0.41091 -0.05698 0.09297  0.01909  137 MET A CB    
773  C  CG    . MET A 107 ? 0.45020 0.23009 0.46000 -0.05618 0.09234  0.01928  137 MET A CG    
774  S  SD    . MET A 107 ? 0.62562 0.41533 0.63261 -0.06167 0.09917  0.01942  137 MET A SD    
775  C  CE    . MET A 107 ? 0.49688 0.30295 0.51866 -0.05529 0.10494  0.01498  137 MET A CE    
776  N  N     . GLY A 108 ? 0.37505 0.16758 0.41170 -0.03802 0.08990  0.01408  138 GLY A N     
777  C  CA    . GLY A 108 ? 0.36277 0.15991 0.40559 -0.03140 0.08841  0.01290  138 GLY A CA    
778  C  C     . GLY A 108 ? 0.37541 0.16852 0.41801 -0.02480 0.08225  0.01320  138 GLY A C     
779  O  O     . GLY A 108 ? 0.38899 0.18042 0.42909 -0.02080 0.07813  0.01361  138 GLY A O     
780  N  N     . ILE A 109 ? 0.39016 0.18148 0.43407 -0.02325 0.08101  0.01294  139 ILE A N     
781  C  CA    . ILE A 109 ? 0.36659 0.15471 0.40954 -0.01510 0.07481  0.01272  139 ILE A CA    
782  C  C     . ILE A 109 ? 0.41459 0.18705 0.44221 -0.01487 0.06789  0.01415  139 ILE A C     
783  O  O     . ILE A 109 ? 0.44640 0.21822 0.47149 -0.00737 0.06272  0.01386  139 ILE A O     
784  C  CB    . ILE A 109 ? 0.41427 0.20265 0.46104 -0.01314 0.07464  0.01185  139 ILE A CB    
785  C  CG1   . ILE A 109 ? 0.35535 0.16035 0.41793 -0.00951 0.07995  0.01006  139 ILE A CG1   
786  C  CG2   . ILE A 109 ? 0.44194 0.21943 0.48021 -0.00600 0.06635  0.01188  139 ILE A CG2   
787  C  CD1   . ILE A 109 ? 0.46288 0.26992 0.53057 -0.00949 0.08187  0.00891  139 ILE A CD1   
788  N  N     . GLU A 110 ? 0.40599 0.16689 0.42280 -0.02337 0.06791  0.01587  140 GLU A N     
789  C  CA    . GLU A 110 ? 0.48599 0.22969 0.48628 -0.02407 0.06110  0.01745  140 GLU A CA    
790  C  C     . GLU A 110 ? 0.52389 0.27034 0.52317 -0.02155 0.06059  0.01729  140 GLU A C     
791  O  O     . GLU A 110 ? 0.51020 0.24893 0.50105 -0.01545 0.05396  0.01715  140 GLU A O     
792  C  CB    . GLU A 110 ? 0.51100 0.24384 0.50054 -0.03534 0.06191  0.02007  140 GLU A CB    
793  C  CG    . GLU A 110 ? 0.65786 0.37068 0.62830 -0.03726 0.05462  0.02214  140 GLU A CG    
794  C  CD    . GLU A 110 ? 0.77144 0.47565 0.73132 -0.05007 0.05596  0.02564  140 GLU A CD    
795  O  OE1   . GLU A 110 ? 0.67763 0.39337 0.64559 -0.05690 0.06268  0.02629  140 GLU A OE1   
796  O  OE2   . GLU A 110 ? 0.73198 0.41886 0.67517 -0.05320 0.05023  0.02784  140 GLU A OE2   
797  N  N     . TRP A 111 ? 0.40344 0.16141 0.41122 -0.02526 0.06711  0.01699  141 TRP A N     
798  C  CA    . TRP A 111 ? 0.40349 0.16353 0.41007 -0.02371 0.06629  0.01695  141 TRP A CA    
799  C  C     . TRP A 111 ? 0.43125 0.19934 0.44400 -0.01418 0.06234  0.01589  141 TRP A C     
800  O  O     . TRP A 111 ? 0.49101 0.25443 0.49640 -0.00992 0.05688  0.01608  141 TRP A O     
801  C  CB    . TRP A 111 ? 0.39420 0.16404 0.40791 -0.02860 0.07316  0.01651  141 TRP A CB    
802  C  CG    . TRP A 111 ? 0.48440 0.25509 0.49621 -0.02731 0.07148  0.01653  141 TRP A CG    
803  C  CD1   . TRP A 111 ? 0.54530 0.30627 0.54560 -0.03062 0.06982  0.01756  141 TRP A CD1   
804  C  CD2   . TRP A 111 ? 0.46654 0.24832 0.48768 -0.02263 0.07057  0.01582  141 TRP A CD2   
805  N  NE1   . TRP A 111 ? 0.53986 0.30498 0.54206 -0.02789 0.06792  0.01715  141 TRP A NE1   
806  C  CE2   . TRP A 111 ? 0.43575 0.21392 0.45069 -0.02353 0.06820  0.01633  141 TRP A CE2   
807  C  CE3   . TRP A 111 ? 0.41992 0.21483 0.45389 -0.01843 0.07148  0.01516  141 TRP A CE3   
808  C  CZ2   . TRP A 111 ? 0.48450 0.27186 0.50565 -0.02101 0.06633  0.01635  141 TRP A CZ2   
809  C  CZ3   . TRP A 111 ? 0.48043 0.28489 0.52040 -0.01626 0.06975  0.01555  141 TRP A CZ3   
810  C  CH2   . TRP A 111 ? 0.53049 0.33118 0.56405 -0.01787 0.06703  0.01621  141 TRP A CH2   
811  N  N     . VAL A 112 ? 0.41377 0.19462 0.43941 -0.01030 0.06468  0.01485  142 VAL A N     
812  C  CA    . VAL A 112 ? 0.45575 0.24766 0.48796 -0.00151 0.06127  0.01438  142 VAL A CA    
813  C  C     . VAL A 112 ? 0.45119 0.23317 0.47207 0.00594  0.05343  0.01411  142 VAL A C     
814  O  O     . VAL A 112 ? 0.57237 0.35769 0.59027 0.01212  0.04870  0.01406  142 VAL A O     
815  C  CB    . VAL A 112 ? 0.37173 0.17785 0.41823 0.00137  0.06486  0.01362  142 VAL A CB    
816  C  CG1   . VAL A 112 ? 0.35668 0.17593 0.40916 0.01074  0.06096  0.01369  142 VAL A CG1   
817  C  CG2   . VAL A 112 ? 0.49540 0.31020 0.55133 -0.00482 0.07152  0.01358  142 VAL A CG2   
818  N  N     . HIS A 113 ? 0.49605 0.26499 0.50916 0.00543  0.05139  0.01390  143 HIS A N     
819  C  CA    . HIS A 113 ? 0.46385 0.22041 0.46387 0.01352  0.04275  0.01326  143 HIS A CA    
820  C  C     . HIS A 113 ? 0.57935 0.32336 0.56478 0.01324  0.03779  0.01385  143 HIS A C     
821  O  O     . HIS A 113 ? 0.60361 0.34752 0.58291 0.02292  0.03133  0.01282  143 HIS A O     
822  C  CB    . HIS A 113 ? 0.52050 0.26191 0.51264 0.01080  0.04075  0.01338  143 HIS A CB    
823  C  CG    . HIS A 113 ? 0.57594 0.29661 0.54867 0.01635  0.03076  0.01307  143 HIS A CG    
824  N  ND1   . HIS A 113 ? 0.60071 0.32265 0.56974 0.03010  0.02382  0.01104  143 HIS A ND1   
825  C  CD2   . HIS A 113 ? 0.58778 0.28533 0.54244 0.01024  0.02603  0.01458  143 HIS A CD2   
826  C  CE1   . HIS A 113 ? 0.55213 0.25076 0.50051 0.03306  0.01472  0.01083  143 HIS A CE1   
827  N  NE2   . HIS A 113 ? 0.50920 0.19200 0.44845 0.02050  0.01578  0.01320  143 HIS A NE2   
828  N  N     . ARG A 114 ? 0.55135 0.28658 0.53133 0.00287  0.04090  0.01541  144 ARG A N     
829  C  CA    . ARG A 114 ? 0.52546 0.24503 0.48890 0.00226  0.03555  0.01611  144 ARG A CA    
830  C  C     . ARG A 114 ? 0.60346 0.33383 0.57127 0.00440  0.03628  0.01581  144 ARG A C     
831  O  O     . ARG A 114 ? 0.54659 0.26950 0.50318 0.00968  0.03004  0.01535  144 ARG A O     
832  C  CB    . ARG A 114 ? 0.49535 0.20063 0.44921 -0.00989 0.03798  0.01840  144 ARG A CB    
833  C  CG    . ARG A 114 ? 0.67383 0.36415 0.61851 -0.01410 0.03527  0.01961  144 ARG A CG    
834  C  CD    . ARG A 114 ? 0.72656 0.40538 0.66106 -0.02694 0.03740  0.02270  144 ARG A CD    
835  N  NE    . ARG A 114 ? 0.86826 0.53468 0.79487 -0.03334 0.03508  0.02465  144 ARG A NE    
836  C  CZ    . ARG A 114 ? 0.94893 0.59249 0.85667 -0.03271 0.02575  0.02575  144 ARG A CZ    
837  N  NH1   . ARG A 114 ? 1.00619 0.63633 0.90005 -0.02533 0.01801  0.02482  144 ARG A NH1   
838  N  NH2   . ARG A 114 ? 0.89851 0.53178 0.80020 -0.03950 0.02349  0.02778  144 ARG A NH2   
839  N  N     . PHE A 115 ? 0.54751 0.29443 0.53038 0.00045  0.04316  0.01600  145 PHE A N     
840  C  CA    . PHE A 115 ? 0.51421 0.26859 0.49972 -0.00024 0.04378  0.01621  145 PHE A CA    
841  C  C     . PHE A 115 ? 0.55881 0.33495 0.55990 0.00416  0.04510  0.01588  145 PHE A C     
842  O  O     . PHE A 115 ? 0.67375 0.45665 0.67620 0.00461  0.04371  0.01624  145 PHE A O     
843  C  CB    . PHE A 115 ? 0.51431 0.26491 0.49920 -0.01061 0.04962  0.01721  145 PHE A CB    
844  C  CG    . PHE A 115 ? 0.59631 0.32805 0.56595 -0.01642 0.04864  0.01842  145 PHE A CG    
845  C  CD1   . PHE A 115 ? 0.77492 0.49235 0.72907 -0.01515 0.04287  0.01890  145 PHE A CD1   
846  C  CD2   . PHE A 115 ? 0.60658 0.33531 0.57672 -0.02347 0.05318  0.01935  145 PHE A CD2   
847  C  CE1   . PHE A 115 ? 0.62721 0.32666 0.56625 -0.02151 0.04155  0.02068  145 PHE A CE1   
848  C  CE2   . PHE A 115 ? 0.62491 0.33782 0.58080 -0.03029 0.05206  0.02134  145 PHE A CE2   
849  C  CZ    . PHE A 115 ? 0.58261 0.28026 0.52262 -0.02966 0.04617  0.02222  145 PHE A CZ    
850  N  N     . CYS A 116 ? 0.63692 0.42419 0.64917 0.00704  0.04730  0.01550  146 CYS A N     
851  C  CA    . CYS A 116 ? 0.43430 0.24273 0.46065 0.01019  0.04829  0.01594  146 CYS A CA    
852  C  C     . CYS A 116 ? 0.55614 0.37493 0.58872 0.01890  0.04651  0.01533  146 CYS A C     
853  O  O     . CYS A 116 ? 0.58206 0.41435 0.62770 0.01816  0.05056  0.01576  146 CYS A O     
854  C  CB    . CYS A 116 ? 0.48805 0.30303 0.52480 0.00193  0.05504  0.01659  146 CYS A CB    
855  S  SG    . CYS A 116 ? 0.68613 0.52193 0.73551 0.00147  0.05497  0.01827  146 CYS A SG    
856  N  N     . PRO A 117 ? 0.55211 0.36440 0.57463 0.02791  0.04009  0.01418  147 PRO A N     
857  C  CA    . PRO A 117 ? 0.59863 0.42186 0.62613 0.03803  0.03773  0.01332  147 PRO A CA    
858  C  C     . PRO A 117 ? 0.61836 0.46785 0.65821 0.04313  0.03745  0.01446  147 PRO A C     
859  O  O     . PRO A 117 ? 0.56561 0.42891 0.61258 0.05069  0.03693  0.01425  147 PRO A O     
860  C  CB    . PRO A 117 ? 0.61868 0.42544 0.62844 0.04690  0.02950  0.01155  147 PRO A CB    
861  C  CG    . PRO A 117 ? 0.57884 0.37746 0.57870 0.04420  0.02683  0.01191  147 PRO A CG    
862  C  CD    . PRO A 117 ? 0.55520 0.35013 0.56018 0.03046  0.03391  0.01349  147 PRO A CD    
863  N  N     . GLN A 118 ? 0.65555 0.51289 0.69817 0.03852  0.03779  0.01600  148 GLN A N     
864  C  CA    . GLN A 118 ? 0.60615 0.48978 0.66065 0.04091  0.03734  0.01802  148 GLN A CA    
865  C  C     . GLN A 118 ? 0.65106 0.54773 0.72103 0.03369  0.04350  0.02008  148 GLN A C     
866  O  O     . GLN A 118 ? 0.59703 0.51680 0.67771 0.03564  0.04322  0.02232  148 GLN A O     
867  C  CB    . GLN A 118 ? 0.69325 0.57914 0.74414 0.03755  0.03471  0.01911  148 GLN A CB    
868  C  CG    . GLN A 118 ? 0.72334 0.59805 0.75842 0.04566  0.02792  0.01706  148 GLN A CG    
869  C  CD    . GLN A 118 ? 0.77766 0.62296 0.79819 0.04071  0.02799  0.01555  148 GLN A CD    
870  O  OE1   . GLN A 118 ? 0.81052 0.64533 0.83320 0.03121  0.03348  0.01599  148 GLN A OE1   
871  N  NE2   . GLN A 118 ? 0.76374 0.59630 0.76864 0.04729  0.02162  0.01386  148 GLN A NE2   
872  N  N     . ALA A 119 ? 0.60818 0.49133 0.67894 0.02559  0.04878  0.01949  149 ALA A N     
873  C  CA    . ALA A 119 ? 0.44650 0.33935 0.52982 0.01921  0.05413  0.02099  149 ALA A CA    
874  C  C     . ALA A 119 ? 0.36316 0.27338 0.45628 0.02616  0.05443  0.02161  149 ALA A C     
875  O  O     . ALA A 119 ? 0.37836 0.28390 0.46843 0.03360  0.05349  0.01962  149 ALA A O     
876  C  CB    . ALA A 119 ? 0.51341 0.38912 0.59433 0.01224  0.05937  0.01936  149 ALA A CB    
877  N  N     . ALA A 120 ? 0.36812 0.29823 0.47244 0.02348  0.05535  0.02464  150 ALA A N     
878  C  CA    . ALA A 120 ? 0.30750 0.25523 0.42160 0.02942  0.05629  0.02564  150 ALA A CA    
879  C  C     . ALA A 120 ? 0.37526 0.31325 0.49271 0.02710  0.06156  0.02391  150 ALA A C     
880  O  O     . ALA A 120 ? 0.36235 0.30235 0.48129 0.03488  0.06172  0.02241  150 ALA A O     
881  C  CB    . ALA A 120 ? 0.29482 0.26642 0.41966 0.02538  0.05598  0.03011  150 ALA A CB    
882  N  N     . PHE A 121 ? 0.35078 0.27812 0.46849 0.01722  0.06541  0.02385  151 PHE A N     
883  C  CA    . PHE A 121 ? 0.34858 0.26866 0.46979 0.01495  0.07059  0.02208  151 PHE A CA    
884  C  C     . PHE A 121 ? 0.30445 0.20513 0.41825 0.00774  0.07328  0.02005  151 PHE A C     
885  O  O     . PHE A 121 ? 0.32815 0.22346 0.43677 0.00252  0.07191  0.02079  151 PHE A O     
886  C  CB    . PHE A 121 ? 0.28063 0.21520 0.41268 0.01158  0.07290  0.02465  151 PHE A CB    
887  C  CG    . PHE A 121 ? 0.36364 0.32013 0.50402 0.01882  0.07113  0.02697  151 PHE A CG    
888  C  CD1   . PHE A 121 ? 0.34160 0.30073 0.48514 0.02680  0.07253  0.02515  151 PHE A CD1   
889  C  CD2   . PHE A 121 ? 0.37333 0.34896 0.51817 0.01759  0.06790  0.03114  151 PHE A CD2   
890  C  CE1   . PHE A 121 ? 0.34312 0.32345 0.49374 0.03435  0.07093  0.02722  151 PHE A CE1   
891  C  CE2   . PHE A 121 ? 0.28031 0.27905 0.43281 0.02448  0.06651  0.03357  151 PHE A CE2   
892  C  CZ    . PHE A 121 ? 0.36762 0.36862 0.52283 0.03329  0.06813  0.03149  151 PHE A CZ    
893  N  N     . VAL A 122 ? 0.32388 0.21540 0.43714 0.00779  0.07700  0.01754  152 VAL A N     
894  C  CA    . VAL A 122 ? 0.34609 0.22194 0.45251 0.00140  0.08015  0.01559  152 VAL A CA    
895  C  C     . VAL A 122 ? 0.29266 0.16897 0.40485 -0.00059 0.08542  0.01401  152 VAL A C     
896  O  O     . VAL A 122 ? 0.33347 0.21435 0.45090 0.00407  0.08658  0.01316  152 VAL A O     
897  C  CB    . VAL A 122 ? 0.38918 0.25120 0.48547 0.00265  0.07872  0.01406  152 VAL A CB    
898  C  CG1   . VAL A 122 ? 0.34512 0.19477 0.43468 -0.00446 0.08212  0.01280  152 VAL A CG1   
899  C  CG2   . VAL A 122 ? 0.33456 0.19524 0.42393 0.00665  0.07276  0.01513  152 VAL A CG2   
900  N  N     . MET A 123 ? 0.33465 0.20609 0.44492 -0.00653 0.08800  0.01340  153 MET A N     
901  C  CA    . MET A 123 ? 0.36789 0.23861 0.48161 -0.00763 0.09282  0.01121  153 MET A CA    
902  C  C     . MET A 123 ? 0.29490 0.15481 0.40108 -0.01082 0.09602  0.00863  153 MET A C     
903  O  O     . MET A 123 ? 0.37365 0.22693 0.47251 -0.01460 0.09524  0.00876  153 MET A O     
904  C  CB    . MET A 123 ? 0.28705 0.16117 0.40358 -0.01080 0.09298  0.01215  153 MET A CB    
905  C  CG    . MET A 123 ? 0.33940 0.21064 0.45684 -0.01113 0.09739  0.00927  153 MET A CG    
906  S  SD    . MET A 123 ? 0.41926 0.29248 0.53862 -0.01396 0.09619  0.01060  153 MET A SD    
907  C  CE    . MET A 123 ? 0.37906 0.25667 0.50532 -0.00942 0.10078  0.00796  153 MET A CE    
908  N  N     . LYS A 124 ? 0.29212 0.15151 0.39997 -0.00929 0.09920  0.00663  154 LYS A N     
909  C  CA    . LYS A 124 ? 0.29693 0.15014 0.39877 -0.01281 0.10285  0.00450  154 LYS A CA    
910  C  C     . LYS A 124 ? 0.29266 0.14919 0.39743 -0.01270 0.10682  0.00205  154 LYS A C     
911  O  O     . LYS A 124 ? 0.32923 0.19167 0.44144 -0.00946 0.10834  0.00115  154 LYS A O     
912  C  CB    . LYS A 124 ? 0.29825 0.14922 0.39907 -0.01250 0.10359  0.00399  154 LYS A CB    
913  C  CG    . LYS A 124 ? 0.42283 0.27155 0.51879 -0.01689 0.10769  0.00241  154 LYS A CG    
914  C  CD    . LYS A 124 ? 0.34236 0.19814 0.44453 -0.01548 0.11230  -0.00023 154 LYS A CD    
915  C  CE    . LYS A 124 ? 0.56928 0.42602 0.66656 -0.01989 0.11608  -0.00136 154 LYS A CE    
916  N  NZ    . LYS A 124 ? 0.52259 0.38742 0.62349 -0.01811 0.12097  -0.00466 154 LYS A NZ    
917  N  N     . THR A 125 ? 0.30227 0.15444 0.40023 -0.01538 0.10806  0.00080  155 THR A N     
918  C  CA    . THR A 125 ? 0.38049 0.23394 0.47876 -0.01398 0.11065  -0.00193 155 THR A CA    
919  C  C     . THR A 125 ? 0.31369 0.16545 0.40463 -0.01487 0.11425  -0.00480 155 THR A C     
920  O  O     . THR A 125 ? 0.30938 0.15846 0.39439 -0.01782 0.11441  -0.00399 155 THR A O     
921  C  CB    . THR A 125 ? 0.32914 0.17937 0.42574 -0.01475 0.10699  -0.00068 155 THR A CB    
922  O  OG1   . THR A 125 ? 0.39925 0.24876 0.49486 -0.01263 0.10888  -0.00358 155 THR A OG1   
923  C  CG2   . THR A 125 ? 0.37470 0.21720 0.46192 -0.01804 0.10418  0.00022  155 THR A CG2   
924  N  N     . ASP A 126 ? 0.34109 0.19493 0.43186 -0.01193 0.11683  -0.00806 156 ASP A N     
925  C  CA    . ASP A 126 ? 0.30840 0.16338 0.39173 -0.01109 0.12033  -0.01137 156 ASP A CA    
926  C  C     . ASP A 126 ? 0.35900 0.20558 0.43210 -0.01023 0.11766  -0.01262 156 ASP A C     
927  O  O     . ASP A 126 ? 0.32611 0.16605 0.39888 -0.01152 0.11307  -0.01050 156 ASP A O     
928  C  CB    . ASP A 126 ? 0.45829 0.32162 0.54673 -0.00744 0.12458  -0.01457 156 ASP A CB    
929  C  CG    . ASP A 126 ? 0.56606 0.43651 0.66159 -0.00946 0.12687  -0.01332 156 ASP A CG    
930  O  OD1   . ASP A 126 ? 0.59293 0.46091 0.68684 -0.01380 0.12539  -0.01031 156 ASP A OD1   
931  O  OD2   . ASP A 126 ? 0.46939 0.34664 0.57095 -0.00667 0.12959  -0.01541 156 ASP A OD2   
932  N  N     . SER A 127 ? 0.36025 0.20780 0.42479 -0.00805 0.12012  -0.01584 157 SER A N     
933  C  CA    . SER A 127 ? 0.33846 0.17647 0.39070 -0.00635 0.11697  -0.01744 157 SER A CA    
934  C  C     . SER A 127 ? 0.44045 0.27336 0.48808 -0.00079 0.11540  -0.02115 157 SER A C     
935  O  O     . SER A 127 ? 0.43936 0.26015 0.47744 -0.00021 0.11036  -0.02150 157 SER A O     
936  C  CB    . SER A 127 ? 0.34555 0.18761 0.38964 -0.00604 0.11991  -0.01883 157 SER A CB    
937  O  OG    . SER A 127 ? 0.51563 0.37099 0.56307 -0.00401 0.12561  -0.02110 157 SER A OG    
938  N  N     . ASP A 128 ? 0.33611 0.17668 0.38927 0.00300  0.11894  -0.02375 158 ASP A N     
939  C  CA    . ASP A 128 ? 0.41516 0.25026 0.46279 0.00909  0.11742  -0.02771 158 ASP A CA    
940  C  C     . ASP A 128 ? 0.33857 0.16947 0.39429 0.00655  0.11432  -0.02472 158 ASP A C     
941  O  O     . ASP A 128 ? 0.32807 0.16383 0.39000 0.00955  0.11645  -0.02624 158 ASP A O     
942  C  CB    . ASP A 128 ? 0.33945 0.18586 0.38679 0.01540  0.12281  -0.03262 158 ASP A CB    
943  C  CG    . ASP A 128 ? 0.52569 0.38615 0.58715 0.01365  0.12784  -0.03160 158 ASP A CG    
944  O  OD1   . ASP A 128 ? 0.31744 0.18027 0.38709 0.00745  0.12798  -0.02717 158 ASP A OD1   
945  O  OD2   . ASP A 128 ? 0.60168 0.46961 0.66473 0.01901  0.13097  -0.03547 158 ASP A OD2   
946  N  N     . MET A 129 ? 0.33772 0.16096 0.39302 0.00119  0.10937  -0.02045 159 MET A N     
947  C  CA    . MET A 129 ? 0.33061 0.15411 0.39498 -0.00200 0.10677  -0.01661 159 MET A CA    
948  C  C     . MET A 129 ? 0.36372 0.17585 0.42225 -0.00662 0.09960  -0.01320 159 MET A C     
949  O  O     . MET A 129 ? 0.39315 0.19796 0.44321 -0.00883 0.09653  -0.01264 159 MET A O     
950  C  CB    . MET A 129 ? 0.31775 0.15194 0.39494 -0.00546 0.10888  -0.01275 159 MET A CB    
951  C  CG    . MET A 129 ? 0.31195 0.15710 0.39629 -0.00292 0.11486  -0.01471 159 MET A CG    
952  S  SD    . MET A 129 ? 0.35935 0.21257 0.45569 0.00028  0.11714  -0.01503 159 MET A SD    
953  C  CE    . MET A 129 ? 0.29364 0.14504 0.39517 -0.00320 0.11175  -0.00966 159 MET A CE    
954  N  N     . PHE A 130 ? 0.34729 0.15748 0.40882 -0.00794 0.09680  -0.01125 160 PHE A N     
955  C  CA    . PHE A 130 ? 0.35836 0.16198 0.41781 -0.01454 0.08995  -0.00627 160 PHE A CA    
956  C  C     . PHE A 130 ? 0.33451 0.15232 0.40906 -0.01831 0.09079  -0.00101 160 PHE A C     
957  O  O     . PHE A 130 ? 0.36999 0.19782 0.45470 -0.01561 0.09451  -0.00105 160 PHE A O     
958  C  CB    . PHE A 130 ? 0.35554 0.14799 0.40729 -0.01470 0.08541  -0.00654 160 PHE A CB    
959  C  CG    . PHE A 130 ? 0.35948 0.14975 0.41257 -0.02337 0.07870  0.00016  160 PHE A CG    
960  C  CD1   . PHE A 130 ? 0.37442 0.15207 0.41636 -0.02876 0.07166  0.00223  160 PHE A CD1   
961  C  CD2   . PHE A 130 ? 0.39853 0.20066 0.46389 -0.02592 0.07951  0.00435  160 PHE A CD2   
962  C  CE1   . PHE A 130 ? 0.41041 0.18797 0.45376 -0.03801 0.06516  0.00898  160 PHE A CE1   
963  C  CE2   . PHE A 130 ? 0.37976 0.18322 0.44669 -0.03435 0.07358  0.01100  160 PHE A CE2   
964  C  CZ    . PHE A 130 ? 0.36746 0.15885 0.42342 -0.04097 0.06629  0.01349  160 PHE A CZ    
965  N  N     . ILE A 131 ? 0.33295 0.15194 0.40837 -0.02381 0.08696  0.00331  161 ILE A N     
966  C  CA    A ILE A 131 ? 0.33443 0.16780 0.42253 -0.02641 0.08682  0.00823  161 ILE A CA    
967  C  CA    B ILE A 131 ? 0.32156 0.15494 0.40970 -0.02637 0.08684  0.00821  161 ILE A CA    
968  C  C     . ILE A 131 ? 0.32851 0.16094 0.41519 -0.03372 0.07996  0.01373  161 ILE A C     
969  O  O     . ILE A 131 ? 0.39587 0.21738 0.47251 -0.03788 0.07508  0.01441  161 ILE A O     
970  C  CB    A ILE A 131 ? 0.38055 0.21919 0.47144 -0.02579 0.08853  0.00848  161 ILE A CB    
971  C  CB    B ILE A 131 ? 0.35901 0.19813 0.45041 -0.02544 0.08890  0.00833  161 ILE A CB    
972  C  CG1   A ILE A 131 ? 0.35819 0.19754 0.44935 -0.02046 0.09468  0.00386  161 ILE A CG1   
973  C  CG1   B ILE A 131 ? 0.36157 0.20306 0.45503 -0.01980 0.09532  0.00390  161 ILE A CG1   
974  C  CG2   A ILE A 131 ? 0.30714 0.16066 0.40961 -0.02664 0.08761  0.01305  161 ILE A CG2   
975  C  CG2   B ILE A 131 ? 0.33564 0.18892 0.43786 -0.02686 0.08739  0.01316  161 ILE A CG2   
976  C  CD1   A ILE A 131 ? 0.35513 0.20342 0.45580 -0.01618 0.09896  0.00263  161 ILE A CD1   
977  C  CD1   B ILE A 131 ? 0.35304 0.19663 0.44661 -0.01957 0.09686  0.00387  161 ILE A CD1   
978  N  N     . ASN A 132 ? 0.32068 0.16509 0.41699 -0.03548 0.07937  0.01783  162 ASN A N     
979  C  CA    . ASN A 132 ? 0.32623 0.17393 0.42269 -0.04365 0.07292  0.02417  162 ASN A CA    
980  C  C     . ASN A 132 ? 0.31641 0.18222 0.42342 -0.04411 0.07297  0.02802  162 ASN A C     
981  O  O     . ASN A 132 ? 0.30488 0.18739 0.42319 -0.04153 0.07514  0.03028  162 ASN A O     
982  C  CB    . ASN A 132 ? 0.32594 0.17661 0.42513 -0.04588 0.07177  0.02689  162 ASN A CB    
983  C  CG    . ASN A 132 ? 0.33432 0.18787 0.43202 -0.05627 0.06440  0.03417  162 ASN A CG    
984  O  OD1   . ASN A 132 ? 0.39722 0.25811 0.49700 -0.06050 0.06140  0.03764  162 ASN A OD1   
985  N  ND2   . ASN A 132 ? 0.40440 0.25226 0.49795 -0.06079 0.06115  0.03668  162 ASN A ND2   
986  N  N     . VAL A 133 ? 0.38481 0.24670 0.48696 -0.04631 0.07040  0.02826  163 VAL A N     
987  C  CA    . VAL A 133 ? 0.38167 0.25882 0.49154 -0.04538 0.07006  0.03095  163 VAL A CA    
988  C  C     . VAL A 133 ? 0.37813 0.27221 0.49522 -0.05101 0.06572  0.03782  163 VAL A C     
989  O  O     . VAL A 133 ? 0.41527 0.32822 0.54201 -0.04764 0.06657  0.04013  163 VAL A O     
990  C  CB    . VAL A 133 ? 0.39875 0.26612 0.50026 -0.04659 0.06798  0.02946  163 VAL A CB    
991  C  CG1   . VAL A 133 ? 0.52267 0.40523 0.63034 -0.04644 0.06584  0.03284  163 VAL A CG1   
992  C  CG2   . VAL A 133 ? 0.32265 0.17869 0.41893 -0.04049 0.07322  0.02329  163 VAL A CG2   
993  N  N     . ASP A 134 ? 0.34488 0.23293 0.45655 -0.05965 0.06050  0.04140  164 ASP A N     
994  C  CA    . ASP A 134 ? 0.38734 0.29331 0.50567 -0.06686 0.05601  0.04892  164 ASP A CA    
995  C  C     . ASP A 134 ? 0.42552 0.34998 0.55569 -0.06269 0.05986  0.05080  164 ASP A C     
996  O  O     . ASP A 134 ? 0.44538 0.39360 0.58582 -0.06138 0.05973  0.05484  164 ASP A O     
997  C  CB    . ASP A 134 ? 0.46829 0.36046 0.57632 -0.07801 0.04902  0.05249  164 ASP A CB    
998  C  CG    . ASP A 134 ? 0.68677 0.55867 0.78151 -0.08127 0.04463  0.05018  164 ASP A CG    
999  O  OD1   . ASP A 134 ? 0.67815 0.52868 0.76238 -0.07727 0.04611  0.04428  164 ASP A OD1   
1000 O  OD2   . ASP A 134 ? 0.65880 0.53715 0.75342 -0.08727 0.03966  0.05414  164 ASP A OD2   
1001 N  N     . TYR A 135 ? 0.30854 0.22304 0.43705 -0.05935 0.06339  0.04747  165 TYR A N     
1002 C  CA    . TYR A 135 ? 0.37894 0.30924 0.51785 -0.05508 0.06701  0.04893  165 TYR A CA    
1003 C  C     . TYR A 135 ? 0.36373 0.30624 0.51142 -0.04407 0.07227  0.04563  165 TYR A C     
1004 O  O     . TYR A 135 ? 0.39934 0.36270 0.55718 -0.04029 0.07347  0.04851  165 TYR A O     
1005 C  CB    . TYR A 135 ? 0.41539 0.33021 0.54906 -0.05392 0.06911  0.04568  165 TYR A CB    
1006 C  CG    . TYR A 135 ? 0.29196 0.22154 0.43477 -0.05175 0.07155  0.04832  165 TYR A CG    
1007 C  CD1   . TYR A 135 ? 0.29264 0.23937 0.44056 -0.05916 0.06777  0.05628  165 TYR A CD1   
1008 C  CD2   . TYR A 135 ? 0.28377 0.21096 0.42980 -0.04282 0.07736  0.04321  165 TYR A CD2   
1009 C  CE1   . TYR A 135 ? 0.35701 0.31797 0.51284 -0.05710 0.07005  0.05897  165 TYR A CE1   
1010 C  CE2   . TYR A 135 ? 0.27617 0.21628 0.43010 -0.04030 0.07952  0.04543  165 TYR A CE2   
1011 C  CZ    . TYR A 135 ? 0.39939 0.35632 0.55808 -0.04728 0.07594  0.05335  165 TYR A CZ    
1012 O  OH    . TYR A 135 ? 0.48412 0.45488 0.65040 -0.04458 0.07820  0.05582  165 TYR A OH    
1013 N  N     . LEU A 136 ? 0.32041 0.24956 0.46328 -0.03869 0.07511  0.03962  166 LEU A N     
1014 C  CA    . LEU A 136 ? 0.34418 0.28168 0.49290 -0.02928 0.07872  0.03678  166 LEU A CA    
1015 C  C     . LEU A 136 ? 0.39658 0.35290 0.55055 -0.02849 0.07549  0.04090  166 LEU A C     
1016 O  O     . LEU A 136 ? 0.34338 0.31556 0.50488 -0.02104 0.07679  0.04137  166 LEU A O     
1017 C  CB    . LEU A 136 ? 0.33203 0.25218 0.47308 -0.02634 0.08104  0.03102  166 LEU A CB    
1018 C  CG    . LEU A 136 ? 0.36358 0.28848 0.50771 -0.01807 0.08333  0.02846  166 LEU A CG    
1019 C  CD1   . LEU A 136 ? 0.27162 0.20543 0.42364 -0.01083 0.08674  0.02728  166 LEU A CD1   
1020 C  CD2   . LEU A 136 ? 0.29561 0.20308 0.43120 -0.01750 0.08544  0.02370  166 LEU A CD2   
1021 N  N     . THR A 137 ? 0.30382 0.25798 0.45286 -0.03505 0.07102  0.04334  167 THR A N     
1022 C  CA    . THR A 137 ? 0.37158 0.34464 0.52492 -0.03433 0.06751  0.04714  167 THR A CA    
1023 C  C     . THR A 137 ? 0.47951 0.47829 0.64290 -0.03508 0.06630  0.05300  167 THR A C     
1024 O  O     . THR A 137 ? 0.42795 0.44689 0.59793 -0.02757 0.06624  0.05412  167 THR A O     
1025 C  CB    . THR A 137 ? 0.32622 0.29189 0.47227 -0.04283 0.06252  0.04910  167 THR A CB    
1026 O  OG1   . THR A 137 ? 0.42117 0.36668 0.55842 -0.04023 0.06392  0.04370  167 THR A OG1   
1027 C  CG2   . THR A 137 ? 0.36546 0.35405 0.51657 -0.04328 0.05827  0.05384  167 THR A CG2   
1028 N  N     . GLU A 138 ? 0.41369 0.41217 0.57724 -0.04397 0.06482  0.05698  168 GLU A N     
1029 C  CA    . GLU A 138 ? 0.36787 0.39136 0.54072 -0.04582 0.06395  0.06322  168 GLU A CA    
1030 C  C     . GLU A 138 ? 0.37353 0.40859 0.55427 -0.03383 0.06888  0.06077  168 GLU A C     
1031 O  O     . GLU A 138 ? 0.50379 0.56504 0.69274 -0.02856 0.06846  0.06402  168 GLU A O     
1032 C  CB    . GLU A 138 ? 0.33691 0.35203 0.50599 -0.05764 0.06149  0.06730  168 GLU A CB    
1033 C  CG    . GLU A 138 ? 0.46936 0.50437 0.64674 -0.05887 0.06228  0.07257  168 GLU A CG    
1034 C  CD    . GLU A 138 ? 0.67972 0.70234 0.85063 -0.07135 0.05885  0.07666  168 GLU A CD    
1035 O  OE1   . GLU A 138 ? 0.64264 0.64468 0.80276 -0.07978 0.05446  0.07645  168 GLU A OE1   
1036 O  OE2   . GLU A 138 ? 0.67651 0.70858 0.85185 -0.07238 0.06009  0.07996  168 GLU A OE2   
1037 N  N     . LEU A 139 ? 0.38425 0.40066 0.56216 -0.02865 0.07336  0.05481  169 LEU A N     
1038 C  CA    . LEU A 139 ? 0.45332 0.47857 0.63792 -0.01760 0.07753  0.05230  169 LEU A CA    
1039 C  C     . LEU A 139 ? 0.46158 0.49478 0.64768 -0.00656 0.07755  0.04951  169 LEU A C     
1040 O  O     . LEU A 139 ? 0.47809 0.52973 0.67074 0.00236  0.07816  0.05028  169 LEU A O     
1041 C  CB    . LEU A 139 ? 0.39828 0.40183 0.57911 -0.01533 0.08193  0.04653  169 LEU A CB    
1042 C  CG    . LEU A 139 ? 0.44567 0.44123 0.62419 -0.02338 0.08186  0.04857  169 LEU A CG    
1043 C  CD1   . LEU A 139 ? 0.32217 0.29820 0.49690 -0.01897 0.08643  0.04197  169 LEU A CD1   
1044 C  CD2   . LEU A 139 ? 0.41237 0.43055 0.59927 -0.02440 0.08122  0.05467  169 LEU A CD2   
1045 N  N     . LEU A 140 ? 0.40951 0.42825 0.58836 -0.00656 0.07639  0.04624  170 LEU A N     
1046 C  CA    . LEU A 140 ? 0.47917 0.50207 0.65682 0.00356  0.07535  0.04359  170 LEU A CA    
1047 C  C     . LEU A 140 ? 0.50514 0.55510 0.68765 0.00610  0.07131  0.04842  170 LEU A C     
1048 O  O     . LEU A 140 ? 0.58922 0.65297 0.77430 0.01753  0.07065  0.04751  170 LEU A O     
1049 C  CB    . LEU A 140 ? 0.37148 0.37281 0.53937 0.00148  0.07465  0.03979  170 LEU A CB    
1050 C  CG    . LEU A 140 ? 0.31711 0.29421 0.47946 0.00113  0.07870  0.03440  170 LEU A CG    
1051 C  CD1   . LEU A 140 ? 0.26437 0.22406 0.41714 -0.00312 0.07750  0.03228  170 LEU A CD1   
1052 C  CD2   . LEU A 140 ? 0.25557 0.23111 0.41914 0.01165  0.08098  0.03054  170 LEU A CD2   
1053 N  N     . LEU A 141 ? 0.51736 0.57541 0.70037 -0.00422 0.06809  0.05352  171 LEU A N     
1054 C  CA    . LEU A 141 ? 0.42350 0.51097 0.61195 -0.00315 0.06423  0.05882  171 LEU A CA    
1055 C  C     . LEU A 141 ? 0.42757 0.54090 0.62569 0.00169  0.06557  0.06243  171 LEU A C     
1056 O  O     . LEU A 141 ? 0.60327 0.74342 0.80600 0.00927  0.06345  0.06481  171 LEU A O     
1057 C  CB    . LEU A 141 ? 0.41264 0.50275 0.59978 -0.01740 0.06032  0.06416  171 LEU A CB    
1058 C  CG    . LEU A 141 ? 0.50818 0.57936 0.68608 -0.02005 0.05794  0.06112  171 LEU A CG    
1059 C  CD1   . LEU A 141 ? 0.41145 0.48030 0.58671 -0.03491 0.05380  0.06598  171 LEU A CD1   
1060 C  CD2   . LEU A 141 ? 0.39798 0.48218 0.57505 -0.00936 0.05549  0.05953  171 LEU A CD2   
1061 N  N     . LYS A 142 ? 0.42808 0.53431 0.62874 -0.00170 0.06899  0.06267  172 LYS A N     
1062 C  CA    . LYS A 142 ? 0.49890 0.62808 0.70827 0.00305  0.07066  0.06593  172 LYS A CA    
1063 C  C     . LYS A 142 ? 0.62319 0.75161 0.83356 0.01899  0.07344  0.06041  172 LYS A C     
1064 O  O     . LYS A 142 ? 0.68421 0.83580 0.90141 0.02642  0.07408  0.06273  172 LYS A O     
1065 C  CB    . LYS A 142 ? 0.66473 0.78575 0.87533 -0.00769 0.07257  0.06880  172 LYS A CB    
1066 C  CG    . LYS A 142 ? 0.73331 0.87494 0.95216 -0.00333 0.07481  0.07199  172 LYS A CG    
1067 C  CD    . LYS A 142 ? 0.71745 0.83941 0.93448 -0.00817 0.07803  0.07052  172 LYS A CD    
1068 C  CE    . LYS A 142 ? 0.92390 1.02549 1.13345 -0.02353 0.07557  0.07245  172 LYS A CE    
1069 N  NZ    . LYS A 142 ? 0.97397 1.06568 1.18213 -0.03002 0.07691  0.07408  172 LYS A NZ    
1070 N  N     . LYS A 143 ? 0.73042 0.83311 0.93368 0.02411  0.07478  0.05346  173 LYS A N     
1071 C  CA    . LYS A 143 ? 0.77988 0.87823 0.98307 0.03736  0.07689  0.04844  173 LYS A CA    
1072 C  C     . LYS A 143 ? 0.64433 0.76035 0.84698 0.05151  0.07345  0.04765  173 LYS A C     
1073 O  O     . LYS A 143 ? 0.68157 0.80282 0.88566 0.06346  0.07410  0.04529  173 LYS A O     
1074 C  CB    . LYS A 143 ? 0.69470 0.76062 0.88998 0.03686  0.07901  0.04193  173 LYS A CB    
1075 C  CG    . LYS A 143 ? 0.51373 0.57095 0.70910 0.04637  0.08166  0.03719  173 LYS A CG    
1076 C  CD    . LYS A 143 ? 0.40807 0.46659 0.60959 0.04277  0.08571  0.03826  173 LYS A CD    
1077 C  CE    . LYS A 143 ? 0.45776 0.50331 0.65837 0.05088  0.08843  0.03276  173 LYS A CE    
1078 N  NZ    . LYS A 143 ? 0.39811 0.45260 0.60594 0.05174  0.09159  0.03417  173 LYS A NZ    
1079 N  N     . ASN A 144 ? 0.62027 0.74582 0.82020 0.05110  0.06937  0.04944  174 ASN A N     
1080 C  CA    . ASN A 144 ? 0.85724 0.99739 1.05402 0.06559  0.06521  0.04791  174 ASN A CA    
1081 C  C     . ASN A 144 ? 0.86551 0.98215 1.05310 0.07712  0.06452  0.04071  174 ASN A C     
1082 O  O     . ASN A 144 ? 1.06282 1.18885 1.24822 0.09206  0.06196  0.03857  174 ASN A O     
1083 C  CB    . ASN A 144 ? 0.83924 1.01539 1.04453 0.07393  0.06455  0.05208  174 ASN A CB    
1084 C  CG    . ASN A 144 ? 0.88924 1.09016 1.10383 0.06113  0.06506  0.06023  174 ASN A CG    
1085 O  OD1   . ASN A 144 ? 0.86978 1.06940 1.08330 0.04958  0.06326  0.06315  174 ASN A OD1   
1086 N  ND2   . ASN A 144 ? 0.88472 1.10802 1.10786 0.06279  0.06713  0.06421  174 ASN A ND2   
1087 N  N     . ARG A 145 ? 0.88415 0.97004 1.06540 0.07011  0.06631  0.03710  175 ARG A N     
1088 C  CA    . ARG A 145 ? 0.71237 0.77366 0.88389 0.07791  0.06529  0.03097  175 ARG A CA    
1089 C  C     . ARG A 145 ? 0.65750 0.69874 0.81890 0.07273  0.06301  0.02908  175 ARG A C     
1090 O  O     . ARG A 145 ? 0.81383 0.83922 0.97452 0.06070  0.06604  0.02906  175 ARG A O     
1091 C  CB    . ARG A 145 ? 0.60929 0.65405 0.78311 0.07444  0.07019  0.02851  175 ARG A CB    
1092 C  CG    . ARG A 145 ? 0.65679 0.71908 0.84011 0.07953  0.07272  0.03009  175 ARG A CG    
1093 C  CD    . ARG A 145 ? 0.60849 0.67370 0.78802 0.09620  0.06952  0.02679  175 ARG A CD    
1094 N  NE    . ARG A 145 ? 0.74254 0.77918 0.91345 0.09821  0.06921  0.02137  175 ARG A NE    
1095 C  CZ    . ARG A 145 ? 0.69404 0.71308 0.85276 0.10197  0.06460  0.01824  175 ARG A CZ    
1096 N  NH1   . ARG A 145 ? 0.59168 0.61831 0.74481 0.10650  0.05972  0.01914  175 ARG A NH1   
1097 N  NH2   . ARG A 145 ? 0.72721 0.72065 0.87866 0.10087  0.06461  0.01428  175 ARG A NH2   
1098 N  N     . THR A 146 ? 0.62556 0.66726 0.77815 0.08258  0.05740  0.02731  176 THR A N     
1099 C  CA    . THR A 146 ? 0.50563 0.52998 0.64771 0.07885  0.05453  0.02577  176 THR A CA    
1100 C  C     . THR A 146 ? 0.58734 0.58379 0.71576 0.08448  0.05180  0.02073  176 THR A C     
1101 O  O     . THR A 146 ? 0.48062 0.45945 0.59944 0.08011  0.04990  0.01949  176 THR A O     
1102 C  CB    . THR A 146 ? 0.56557 0.61025 0.70594 0.08475  0.04935  0.02777  176 THR A CB    
1103 O  OG1   . THR A 146 ? 0.79842 0.82783 0.93036 0.07845  0.04734  0.02709  176 THR A OG1   
1104 C  CG2   . THR A 146 ? 0.48863 0.53885 0.62130 0.10292  0.04372  0.02478  176 THR A CG2   
1105 N  N     . THR A 147 ? 0.49307 0.48472 0.61944 0.09380  0.05096  0.01806  177 THR A N     
1106 C  CA    . THR A 147 ? 0.45579 0.42051 0.56793 0.09861  0.04712  0.01383  177 THR A CA    
1107 C  C     . THR A 147 ? 0.45041 0.40440 0.56526 0.09813  0.05035  0.01190  177 THR A C     
1108 O  O     . THR A 147 ? 0.42139 0.39178 0.54689 0.10137  0.05333  0.01289  177 THR A O     
1109 C  CB    . THR A 147 ? 0.52616 0.49295 0.62653 0.11541  0.03868  0.01156  177 THR A CB    
1110 O  OG1   . THR A 147 ? 0.58564 0.57522 0.69349 0.12680  0.03838  0.01199  177 THR A OG1   
1111 C  CG2   . THR A 147 ? 0.50527 0.48126 0.60118 0.11680  0.03487  0.01284  177 THR A CG2   
1112 N  N     . ARG A 148 ? 0.50140 0.42832 0.60608 0.09403  0.04941  0.00933  178 ARG A N     
1113 C  CA    . ARG A 148 ? 0.50133 0.41618 0.60701 0.09297  0.05174  0.00729  178 ARG A CA    
1114 C  C     . ARG A 148 ? 0.38199 0.31089 0.50373 0.08617  0.05973  0.00890  178 ARG A C     
1115 O  O     . ARG A 148 ? 0.32309 0.25755 0.45067 0.09126  0.06128  0.00798  178 ARG A O     
1116 C  CB    . ARG A 148 ? 0.42801 0.34085 0.52652 0.10822  0.04537  0.00476  178 ARG A CB    
1117 C  CG    . ARG A 148 ? 0.45672 0.35080 0.53611 0.11522  0.03630  0.00272  178 ARG A CG    
1118 C  CD    . ARG A 148 ? 0.38591 0.27863 0.45627 0.13254  0.02864  -0.00003 178 ARG A CD    
1119 N  NE    . ARG A 148 ? 0.56338 0.44655 0.63518 0.13327  0.02956  -0.00180 178 ARG A NE    
1120 C  CZ    . ARG A 148 ? 0.60760 0.46307 0.66788 0.12877  0.02630  -0.00357 178 ARG A CZ    
1121 N  NH1   . ARG A 148 ? 0.51515 0.34890 0.56192 0.12170  0.02266  -0.00348 178 ARG A NH1   
1122 N  NH2   . ARG A 148 ? 0.57514 0.42496 0.63733 0.13081  0.02654  -0.00518 178 ARG A NH2   
1123 N  N     . PHE A 149 ? 0.44619 0.37976 0.57396 0.07492  0.06431  0.01123  179 PHE A N     
1124 C  CA    . PHE A 149 ? 0.40922 0.35430 0.54995 0.06785  0.07095  0.01299  179 PHE A CA    
1125 C  C     . PHE A 149 ? 0.29610 0.22441 0.43572 0.05647  0.07572  0.01161  179 PHE A C     
1126 O  O     . PHE A 149 ? 0.32741 0.24337 0.45959 0.05010  0.07504  0.01147  179 PHE A O     
1127 C  CB    . PHE A 149 ? 0.36423 0.32818 0.51155 0.06396  0.07148  0.01700  179 PHE A CB    
1128 C  CG    . PHE A 149 ? 0.37284 0.34541 0.53072 0.05566  0.07701  0.01919  179 PHE A CG    
1129 C  CD1   . PHE A 149 ? 0.41058 0.39589 0.57715 0.05993  0.07932  0.01983  179 PHE A CD1   
1130 C  CD2   . PHE A 149 ? 0.30375 0.27008 0.46136 0.04398  0.07936  0.02046  179 PHE A CD2   
1131 C  CE1   . PHE A 149 ? 0.39761 0.38891 0.57214 0.05224  0.08373  0.02193  179 PHE A CE1   
1132 C  CE2   . PHE A 149 ? 0.40221 0.37377 0.56703 0.03679  0.08328  0.02232  179 PHE A CE2   
1133 C  CZ    . PHE A 149 ? 0.45676 0.44033 0.62983 0.04068  0.08541  0.02311  179 PHE A CZ    
1134 N  N     . PHE A 150 ? 0.28208 0.21114 0.42875 0.05457  0.08048  0.01054  180 PHE A N     
1135 C  CA    . PHE A 150 ? 0.32064 0.23665 0.46640 0.04518  0.08517  0.00885  180 PHE A CA    
1136 C  C     . PHE A 150 ? 0.34929 0.27422 0.50521 0.04303  0.09045  0.00892  180 PHE A C     
1137 O  O     . PHE A 150 ? 0.26012 0.19239 0.42160 0.04967  0.09094  0.00827  180 PHE A O     
1138 C  CB    . PHE A 150 ? 0.26673 0.16620 0.40491 0.04618  0.08384  0.00593  180 PHE A CB    
1139 C  CG    . PHE A 150 ? 0.27014 0.15720 0.40470 0.03602  0.08765  0.00472  180 PHE A CG    
1140 C  CD1   . PHE A 150 ? 0.26183 0.15079 0.40273 0.03208  0.09340  0.00318  180 PHE A CD1   
1141 C  CD2   . PHE A 150 ? 0.32119 0.19553 0.44528 0.03115  0.08524  0.00506  180 PHE A CD2   
1142 C  CE1   . PHE A 150 ? 0.29703 0.17740 0.43423 0.02388  0.09688  0.00190  180 PHE A CE1   
1143 C  CE2   . PHE A 150 ? 0.29565 0.16110 0.41620 0.02209  0.08887  0.00426  180 PHE A CE2   
1144 C  CZ    . PHE A 150 ? 0.33418 0.20355 0.46138 0.01876  0.09470  0.00263  180 PHE A CZ    
1145 N  N     . THR A 151 ? 0.27436 0.19751 0.43151 0.03433  0.09396  0.00951  181 THR A N     
1146 C  CA    . THR A 151 ? 0.30723 0.23708 0.47197 0.03245  0.09807  0.00962  181 THR A CA    
1147 C  C     . THR A 151 ? 0.26062 0.17974 0.42217 0.02454  0.10194  0.00763  181 THR A C     
1148 O  O     . THR A 151 ? 0.33256 0.24131 0.48691 0.02011  0.10171  0.00670  181 THR A O     
1149 C  CB    . THR A 151 ? 0.27756 0.22296 0.44790 0.03182  0.09669  0.01390  181 THR A CB    
1150 O  OG1   . THR A 151 ? 0.39067 0.34151 0.56739 0.03077  0.10000  0.01420  181 THR A OG1   
1151 C  CG2   . THR A 151 ? 0.23908 0.18133 0.40496 0.02396  0.09519  0.01605  181 THR A CG2   
1152 N  N     . GLY A 152 ? 0.31462 0.23656 0.48074 0.02346  0.10527  0.00691  182 GLY A N     
1153 C  CA    . GLY A 152 ? 0.23659 0.14938 0.39887 0.01801  0.10868  0.00438  182 GLY A CA    
1154 C  C     . GLY A 152 ? 0.28084 0.19641 0.44815 0.02063  0.11214  0.00226  182 GLY A C     
1155 O  O     . GLY A 152 ? 0.33025 0.25518 0.50378 0.02394  0.11165  0.00418  182 GLY A O     
1156 N  N     . PHE A 153 ? 0.27140 0.17984 0.43565 0.01931  0.11566  -0.00168 183 PHE A N     
1157 C  CA    . PHE A 153 ? 0.23889 0.14964 0.40742 0.02299  0.11898  -0.00457 183 PHE A CA    
1158 C  C     . PHE A 153 ? 0.33314 0.24574 0.50521 0.02765  0.11948  -0.00630 183 PHE A C     
1159 O  O     . PHE A 153 ? 0.30710 0.21434 0.47532 0.02562  0.12033  -0.00826 183 PHE A O     
1160 C  CB    . PHE A 153 ? 0.23045 0.13458 0.39358 0.02062  0.12224  -0.00840 183 PHE A CB    
1161 C  CG    . PHE A 153 ? 0.22545 0.13241 0.39230 0.02506  0.12533  -0.01169 183 PHE A CG    
1162 C  CD1   . PHE A 153 ? 0.25479 0.16357 0.42263 0.02621  0.12463  -0.01075 183 PHE A CD1   
1163 C  CD2   . PHE A 153 ? 0.31151 0.22282 0.47645 0.02538  0.12551  -0.01419 183 PHE A CD2   
1164 C  CE1   . PHE A 153 ? 0.30234 0.21705 0.46775 0.02794  0.12347  -0.01249 183 PHE A CE1   
1165 C  CE2   . PHE A 153 ? 0.22913 0.14699 0.39236 0.02697  0.12421  -0.01581 183 PHE A CE2   
1166 C  CZ    . PHE A 153 ? 0.27445 0.19382 0.43710 0.02839  0.12283  -0.01506 183 PHE A CZ    
1167 N  N     . LEU A 154 ? 0.28958 0.20990 0.46778 0.03341  0.11825  -0.00522 184 LEU A N     
1168 C  CA    . LEU A 154 ? 0.36820 0.29102 0.54431 0.03636  0.11477  -0.00592 184 LEU A CA    
1169 C  C     . LEU A 154 ? 0.27456 0.19853 0.44732 0.03455  0.11517  -0.00894 184 LEU A C     
1170 O  O     . LEU A 154 ? 0.35056 0.27920 0.52292 0.03409  0.11565  -0.00967 184 LEU A O     
1171 C  CB    . LEU A 154 ? 0.27028 0.20316 0.44926 0.04247  0.11072  -0.00352 184 LEU A CB    
1172 C  CG    . LEU A 154 ? 0.42180 0.35563 0.60343 0.04692  0.10880  -0.00089 184 LEU A CG    
1173 C  CD1   . LEU A 154 ? 0.32747 0.26270 0.50994 0.04186  0.10979  0.00198  184 LEU A CD1   
1174 C  CD2   . LEU A 154 ? 0.44997 0.39607 0.63268 0.05436  0.10425  0.00081  184 LEU A CD2   
1175 N  N     . LYS A 155 ? 0.28611 0.20489 0.45649 0.03361  0.11497  -0.01060 185 LYS A N     
1176 C  CA    . LYS A 155 ? 0.35390 0.27438 0.52290 0.03216  0.11582  -0.01338 185 LYS A CA    
1177 C  C     . LYS A 155 ? 0.47777 0.39761 0.64570 0.03581  0.11107  -0.01312 185 LYS A C     
1178 O  O     . LYS A 155 ? 0.45885 0.36935 0.62523 0.03518  0.11055  -0.01315 185 LYS A O     
1179 C  CB    . LYS A 155 ? 0.27152 0.18584 0.43977 0.02737  0.12130  -0.01572 185 LYS A CB    
1180 C  CG    . LYS A 155 ? 0.34346 0.25643 0.51042 0.02512  0.12490  -0.01627 185 LYS A CG    
1181 C  CD    . LYS A 155 ? 0.33194 0.23786 0.49662 0.02110  0.12990  -0.01834 185 LYS A CD    
1182 C  CE    . LYS A 155 ? 0.37779 0.28872 0.54294 0.02032  0.13391  -0.02200 185 LYS A CE    
1183 N  NZ    . LYS A 155 ? 0.39807 0.31712 0.56096 0.02236  0.13251  -0.02332 185 LYS A NZ    
1184 N  N     . LEU A 156 ? 0.40388 0.33136 0.57101 0.03946  0.10725  -0.01304 186 LEU A N     
1185 C  CA    . LEU A 156 ? 0.46832 0.39505 0.63279 0.04460  0.10158  -0.01284 186 LEU A CA    
1186 C  C     . LEU A 156 ? 0.55061 0.47707 0.71380 0.04442  0.10036  -0.01520 186 LEU A C     
1187 O  O     . LEU A 156 ? 0.64439 0.56615 0.80443 0.04818  0.09572  -0.01557 186 LEU A O     
1188 C  CB    . LEU A 156 ? 0.36404 0.29970 0.52765 0.05032  0.09738  -0.01103 186 LEU A CB    
1189 C  CG    . LEU A 156 ? 0.45749 0.39522 0.62432 0.05118  0.09876  -0.00833 186 LEU A CG    
1190 C  CD1   . LEU A 156 ? 0.38557 0.33413 0.55288 0.05696  0.09538  -0.00646 186 LEU A CD1   
1191 C  CD2   . LEU A 156 ? 0.31161 0.24029 0.47733 0.05239  0.09795  -0.00769 186 LEU A CD2   
1192 N  N     . ASN A 157 ? 0.53040 0.46142 0.69515 0.04103  0.10365  -0.01691 187 ASN A N     
1193 C  CA    . ASN A 157 ? 0.67082 0.60165 0.83568 0.04084  0.10299  -0.01921 187 ASN A CA    
1194 C  C     . ASN A 157 ? 0.68627 0.61631 0.85506 0.03517  0.10992  -0.02138 187 ASN A C     
1195 O  O     . ASN A 157 ? 0.89875 0.83582 1.06706 0.03435  0.11126  -0.02291 187 ASN A O     
1196 C  CB    . ASN A 157 ? 0.93616 0.87505 1.09752 0.04482  0.09826  -0.01953 187 ASN A CB    
1197 C  CG    . ASN A 157 ? 1.16270 1.10252 1.32466 0.04429  0.09813  -0.02206 187 ASN A CG    
1198 O  OD1   . ASN A 157 ? 1.14547 1.07833 1.30950 0.04381  0.09826  -0.02305 187 ASN A OD1   
1199 N  ND2   . ASN A 157 ? 1.02874 0.97587 1.18869 0.04444  0.09767  -0.02319 187 ASN A ND2   
1200 N  N     . GLU A 158 ? 0.55533 0.47647 0.72658 0.03183  0.11384  -0.02163 188 GLU A N     
1201 C  CA    . GLU A 158 ? 0.36809 0.28969 0.54302 0.02681  0.12164  -0.02406 188 GLU A CA    
1202 C  C     . GLU A 158 ? 0.42068 0.33741 0.60009 0.02424  0.12467  -0.02639 188 GLU A C     
1203 O  O     . GLU A 158 ? 0.42165 0.32672 0.59861 0.02383  0.12021  -0.02494 188 GLU A O     
1204 C  CB    . GLU A 158 ? 0.39212 0.30718 0.56619 0.02410  0.12533  -0.02311 188 GLU A CB    
1205 C  CG    . GLU A 158 ? 0.55869 0.47854 0.72986 0.02581  0.12365  -0.02140 188 GLU A CG    
1206 C  CD    . GLU A 158 ? 0.51497 0.44294 0.68460 0.02529  0.12597  -0.02344 188 GLU A CD    
1207 O  OE1   . GLU A 158 ? 0.50708 0.43765 0.67790 0.02307  0.13086  -0.02634 188 GLU A OE1   
1208 O  OE2   . GLU A 158 ? 0.72522 0.65656 0.89189 0.02738  0.12277  -0.02228 188 GLU A OE2   
1209 N  N     . PHE A 159 ? 0.34299 0.26919 0.52655 0.02211  0.13045  -0.02955 189 PHE A N     
1210 C  CA    . PHE A 159 ? 0.37116 0.29977 0.55450 0.01557  0.12993  -0.02977 189 PHE A CA    
1211 C  C     . PHE A 159 ? 0.32157 0.25614 0.49993 0.00573  0.13256  -0.02818 189 PHE A C     
1212 O  O     . PHE A 159 ? 0.25514 0.19760 0.43386 0.00698  0.13762  -0.02987 189 PHE A O     
1213 C  CB    . PHE A 159 ? 0.31608 0.25500 0.50728 0.02110  0.13315  -0.03416 189 PHE A CB    
1214 C  CG    . PHE A 159 ? 0.54418 0.48080 0.73053 0.02648  0.12374  -0.03223 189 PHE A CG    
1215 C  CD1   . PHE A 159 ? 0.56014 0.48879 0.74827 0.02774  0.12015  -0.03244 189 PHE A CD1   
1216 C  CD2   . PHE A 159 ? 0.54273 0.48472 0.72155 0.03008  0.11826  -0.03034 189 PHE A CD2   
1217 C  CE1   . PHE A 159 ? 0.63886 0.56819 0.82074 0.03328  0.11146  -0.03087 189 PHE A CE1   
1218 C  CE2   . PHE A 159 ? 0.54746 0.48998 0.72137 0.03482  0.11066  -0.02886 189 PHE A CE2   
1219 C  CZ    . PHE A 159 ? 0.61696 0.55432 0.79203 0.03678  0.10732  -0.02920 189 PHE A CZ    
1220 N  N     . PRO A 160 ? 0.30413 0.23397 0.47637 -0.00420 0.12857  -0.02463 190 PRO A N     
1221 C  CA    . PRO A 160 ? 0.29665 0.23416 0.46388 -0.01467 0.13104  -0.02244 190 PRO A CA    
1222 C  C     . PRO A 160 ? 0.33195 0.29044 0.50476 -0.01399 0.13822  -0.02622 190 PRO A C     
1223 O  O     . PRO A 160 ? 0.29321 0.25967 0.47227 -0.01095 0.13930  -0.02913 190 PRO A O     
1224 C  CB    . PRO A 160 ? 0.26626 0.19354 0.42639 -0.02479 0.12422  -0.01796 190 PRO A CB    
1225 C  CG    . PRO A 160 ? 0.31602 0.23550 0.47925 -0.01929 0.11948  -0.01937 190 PRO A CG    
1226 C  CD    . PRO A 160 ? 0.27477 0.19013 0.44256 -0.00638 0.12057  -0.02205 190 PRO A CD    
1227 N  N     . ILE A 161 ? 0.31360 0.28067 0.48358 -0.01545 0.14276  -0.02660 191 ILE A N     
1228 C  CA    . ILE A 161 ? 0.24417 0.23223 0.41729 -0.01366 0.14929  -0.03052 191 ILE A CA    
1229 C  C     . ILE A 161 ? 0.27211 0.27373 0.44381 -0.02535 0.14950  -0.02772 191 ILE A C     
1230 O  O     . ILE A 161 ? 0.28028 0.28006 0.44515 -0.03497 0.14805  -0.02311 191 ILE A O     
1231 C  CB    . ILE A 161 ? 0.40589 0.39717 0.57500 -0.00919 0.15332  -0.03244 191 ILE A CB    
1232 C  CG1   . ILE A 161 ? 0.23323 0.21333 0.40420 0.00165  0.15303  -0.03521 191 ILE A CG1   
1233 C  CG2   . ILE A 161 ? 0.23903 0.25261 0.40835 -0.00802 0.15916  -0.03602 191 ILE A CG2   
1234 C  CD1   . ILE A 161 ? 0.37868 0.35470 0.54340 0.00420  0.15439  -0.03557 191 ILE A CD1   
1235 N  N     . ARG A 162 ? 0.25555 0.27045 0.43345 -0.02467 0.15100  -0.03025 192 ARG A N     
1236 C  CA    . ARG A 162 ? 0.36742 0.39784 0.54507 -0.03635 0.15097  -0.02739 192 ARG A CA    
1237 C  C     . ARG A 162 ? 0.41550 0.47406 0.59568 -0.03434 0.15812  -0.03096 192 ARG A C     
1238 O  O     . ARG A 162 ? 0.27712 0.35417 0.45910 -0.04281 0.15895  -0.02929 192 ARG A O     
1239 C  CB    . ARG A 162 ? 0.36772 0.39406 0.54987 -0.03868 0.14641  -0.02703 192 ARG A CB    
1240 C  CG    . ARG A 162 ? 0.34304 0.34197 0.52238 -0.03675 0.13904  -0.02494 192 ARG A CG    
1241 C  CD    . ARG A 162 ? 0.34667 0.33069 0.51571 -0.04762 0.13366  -0.01848 192 ARG A CD    
1242 N  NE    . ARG A 162 ? 0.45833 0.41828 0.62334 -0.04675 0.12524  -0.01649 192 ARG A NE    
1243 C  CZ    . ARG A 162 ? 0.29549 0.23676 0.45003 -0.05402 0.11841  -0.01141 192 ARG A CZ    
1244 N  NH1   . ARG A 162 ? 0.31231 0.25521 0.45986 -0.06317 0.11925  -0.00747 192 ARG A NH1   
1245 N  NH2   . ARG A 162 ? 0.29650 0.21671 0.44655 -0.05136 0.11025  -0.01048 192 ARG A NH2   
1246 N  N     . GLN A 163 ? 0.42369 0.48588 0.60244 -0.02407 0.16270  -0.03530 193 GLN A N     
1247 C  CA    . GLN A 163 ? 0.39742 0.48591 0.57578 -0.02040 0.16903  -0.03912 193 GLN A CA    
1248 C  C     . GLN A 163 ? 0.39047 0.48806 0.56179 -0.03075 0.17002  -0.03418 193 GLN A C     
1249 O  O     . GLN A 163 ? 0.42651 0.51042 0.59142 -0.02964 0.16927  -0.03281 193 GLN A O     
1250 C  CB    . GLN A 163 ? 0.42821 0.51278 0.60266 -0.00479 0.16952  -0.04523 193 GLN A CB    
1251 C  CG    . GLN A 163 ? 0.82222 0.91682 0.99461 0.00474  0.16509  -0.04943 193 GLN A CG    
1252 C  CD    . GLN A 163 ? 1.03896 1.13977 1.19986 0.01660  0.16264  -0.05331 193 GLN A CD    
1253 O  OE1   . GLN A 163 ? 1.09121 1.17793 1.24551 0.02142  0.16150  -0.05404 193 GLN A OE1   
1254 N  NE2   . GLN A 163 ? 0.99537 1.11744 1.15346 0.02159  0.16172  -0.05565 193 GLN A NE2   
1255 N  N     . PRO A 164 ? 0.33066 0.45232 0.50285 -0.04045 0.17185  -0.03153 194 PRO A N     
1256 C  CA    . PRO A 164 ? 0.34179 0.47325 0.50720 -0.05288 0.17230  -0.02536 194 PRO A CA    
1257 C  C     . PRO A 164 ? 0.40579 0.54016 0.56375 -0.04658 0.17590  -0.02704 194 PRO A C     
1258 O  O     . PRO A 164 ? 0.40373 0.53253 0.55492 -0.05593 0.17435  -0.02138 194 PRO A O     
1259 C  CB    . PRO A 164 ? 0.26923 0.43241 0.43887 -0.06105 0.17484  -0.02393 194 PRO A CB    
1260 C  CG    . PRO A 164 ? 0.43399 0.60831 0.61140 -0.04819 0.17775  -0.03163 194 PRO A CG    
1261 C  CD    . PRO A 164 ? 0.45142 0.59517 0.63124 -0.04108 0.17361  -0.03380 194 PRO A CD    
1262 N  N     . PHE A 165 ? 0.31085 0.45158 0.46852 -0.03149 0.17982  -0.03436 195 PHE A N     
1263 C  CA    . PHE A 165 ? 0.31668 0.46096 0.46546 -0.02551 0.18259  -0.03603 195 PHE A CA    
1264 C  C     . PHE A 165 ? 0.32832 0.44397 0.47285 -0.01593 0.18013  -0.03873 195 PHE A C     
1265 O  O     . PHE A 165 ? 0.43639 0.55222 0.57286 -0.00955 0.18168  -0.04090 195 PHE A O     
1266 C  CB    . PHE A 165 ? 0.31469 0.48990 0.46192 -0.01684 0.18617  -0.04084 195 PHE A CB    
1267 C  CG    . PHE A 165 ? 0.34026 0.54343 0.49224 -0.02804 0.18692  -0.03655 195 PHE A CG    
1268 C  CD1   . PHE A 165 ? 0.27633 0.49486 0.42634 -0.04242 0.18946  -0.03018 195 PHE A CD1   
1269 C  CD2   . PHE A 165 ? 0.32931 0.54244 0.48695 -0.02501 0.18432  -0.03813 195 PHE A CD2   
1270 C  CE1   . PHE A 165 ? 0.39303 0.63653 0.54651 -0.05384 0.18878  -0.02501 195 PHE A CE1   
1271 C  CE2   . PHE A 165 ? 0.32644 0.56463 0.48855 -0.03600 0.18464  -0.03352 195 PHE A CE2   
1272 C  CZ    . PHE A 165 ? 0.33674 0.59000 0.49675 -0.05068 0.18656  -0.02671 195 PHE A CZ    
1273 N  N     . SER A 166 ? 0.33101 0.42376 0.48021 -0.01539 0.17610  -0.03821 196 SER A N     
1274 C  CA    . SER A 166 ? 0.31341 0.38038 0.45930 -0.00816 0.17333  -0.03959 196 SER A CA    
1275 C  C     . SER A 166 ? 0.36672 0.41929 0.50620 -0.01647 0.17039  -0.03379 196 SER A C     
1276 O  O     . SER A 166 ? 0.41684 0.47156 0.55630 -0.02870 0.16876  -0.02805 196 SER A O     
1277 C  CB    . SER A 166 ? 0.33226 0.38344 0.48537 -0.00486 0.17026  -0.04053 196 SER A CB    
1278 O  OG    . SER A 166 ? 0.50011 0.52917 0.65060 0.00078  0.16748  -0.04097 196 SER A OG    
1279 N  N     . LYS A 167 ? 0.35284 0.39057 0.48636 -0.01029 0.16925  -0.03517 197 LYS A N     
1280 C  CA    . LYS A 167 ? 0.45444 0.47756 0.58155 -0.01692 0.16625  -0.03018 197 LYS A CA    
1281 C  C     . LYS A 167 ? 0.41423 0.41967 0.54513 -0.02409 0.16117  -0.02537 197 LYS A C     
1282 O  O     . LYS A 167 ? 0.47550 0.47419 0.60164 -0.03324 0.15864  -0.02011 197 LYS A O     
1283 C  CB    . LYS A 167 ? 0.43526 0.44592 0.55608 -0.00753 0.16555  -0.03347 197 LYS A CB    
1284 C  CG    . LYS A 167 ? 0.67295 0.66967 0.78627 -0.01199 0.16279  -0.02958 197 LYS A CG    
1285 C  CD    . LYS A 167 ? 0.69357 0.67026 0.80491 -0.00535 0.15942  -0.03109 197 LYS A CD    
1286 C  CE    . LYS A 167 ? 0.67754 0.65364 0.77961 0.00255  0.16022  -0.03505 197 LYS A CE    
1287 N  NZ    . LYS A 167 ? 0.60384 0.56795 0.69814 -0.00073 0.15752  -0.03204 197 LYS A NZ    
1288 N  N     . TRP A 168 ? 0.35417 0.35276 0.49237 -0.01941 0.15955  -0.02731 198 TRP A N     
1289 C  CA    . TRP A 168 ? 0.36422 0.34575 0.50506 -0.02357 0.15419  -0.02354 198 TRP A CA    
1290 C  C     . TRP A 168 ? 0.35567 0.34382 0.50134 -0.02996 0.15303  -0.02185 198 TRP A C     
1291 O  O     . TRP A 168 ? 0.29932 0.27470 0.44795 -0.02994 0.14864  -0.02056 198 TRP A O     
1292 C  CB    . TRP A 168 ? 0.55843 0.52740 0.70325 -0.01364 0.15259  -0.02639 198 TRP A CB    
1293 C  CG    . TRP A 168 ? 0.67783 0.63899 0.81719 -0.00880 0.15266  -0.02743 198 TRP A CG    
1294 C  CD1   . TRP A 168 ? 0.57142 0.52614 0.70322 -0.01327 0.15128  -0.02441 198 TRP A CD1   
1295 C  CD2   . TRP A 168 ? 0.74359 0.70147 0.88367 0.00099  0.15356  -0.03162 198 TRP A CD2   
1296 N  NE1   . TRP A 168 ? 0.53495 0.48285 0.66309 -0.00695 0.15111  -0.02652 198 TRP A NE1   
1297 C  CE2   . TRP A 168 ? 0.77088 0.72003 0.90351 0.00139  0.15224  -0.03072 198 TRP A CE2   
1298 C  CE3   . TRP A 168 ? 0.78744 0.74793 0.93285 0.00905  0.15489  -0.03582 198 TRP A CE3   
1299 C  CZ2   . TRP A 168 ? 0.85933 0.80162 0.98921 0.00877  0.15168  -0.03360 198 TRP A CZ2   
1300 C  CZ3   . TRP A 168 ? 0.94392 0.89746 1.08629 0.01647  0.15455  -0.03861 198 TRP A CZ3   
1301 C  CH2   . TRP A 168 ? 0.90492 0.84912 1.03939 0.01592  0.15270  -0.03735 198 TRP A CH2   
1302 N  N     . PHE A 169 ? 0.27742 0.28561 0.42309 -0.03548 0.15646  -0.02163 199 PHE A N     
1303 C  CA    . PHE A 169 ? 0.26948 0.28514 0.41899 -0.04368 0.15483  -0.01931 199 PHE A CA    
1304 C  C     . PHE A 169 ? 0.28078 0.28116 0.42430 -0.05585 0.14850  -0.01246 199 PHE A C     
1305 O  O     . PHE A 169 ? 0.28937 0.28756 0.42515 -0.06268 0.14803  -0.00862 199 PHE A O     
1306 C  CB    . PHE A 169 ? 0.27046 0.31438 0.42128 -0.04779 0.15994  -0.02003 199 PHE A CB    
1307 C  CG    . PHE A 169 ? 0.30140 0.35267 0.45430 -0.06011 0.15726  -0.01576 199 PHE A CG    
1308 C  CD1   . PHE A 169 ? 0.34812 0.39840 0.50830 -0.05773 0.15537  -0.01785 199 PHE A CD1   
1309 C  CD2   . PHE A 169 ? 0.28745 0.34521 0.43418 -0.07460 0.15599  -0.00930 199 PHE A CD2   
1310 C  CE1   . PHE A 169 ? 0.28248 0.33770 0.44354 -0.06960 0.15193  -0.01376 199 PHE A CE1   
1311 C  CE2   . PHE A 169 ? 0.29448 0.35727 0.44188 -0.08726 0.15250  -0.00477 199 PHE A CE2   
1312 C  CZ    . PHE A 169 ? 0.28954 0.35069 0.44399 -0.08478 0.15027  -0.00707 199 PHE A CZ    
1313 N  N     . VAL A 170 ? 0.35081 0.33921 0.49670 -0.05750 0.14322  -0.01128 200 VAL A N     
1314 C  CA    . VAL A 170 ? 0.35495 0.32769 0.49327 -0.06894 0.13596  -0.00511 200 VAL A CA    
1315 C  C     . VAL A 170 ? 0.29908 0.27876 0.44031 -0.07635 0.13350  -0.00372 200 VAL A C     
1316 O  O     . VAL A 170 ? 0.29069 0.27177 0.43960 -0.06896 0.13355  -0.00765 200 VAL A O     
1317 C  CB    . VAL A 170 ? 0.29776 0.24357 0.43238 -0.06335 0.12950  -0.00453 200 VAL A CB    
1318 C  CG1   . VAL A 170 ? 0.29563 0.23580 0.42689 -0.05803 0.13151  -0.00512 200 VAL A CG1   
1319 C  CG2   . VAL A 170 ? 0.31480 0.25680 0.45776 -0.05233 0.12866  -0.00894 200 VAL A CG2   
1320 N  N     . SER A 171 ? 0.31212 0.29671 0.44693 -0.09138 0.13124  0.00209  201 SER A N     
1321 C  CA    . SER A 171 ? 0.35947 0.34835 0.49507 -0.10126 0.12729  0.00475  201 SER A CA    
1322 C  C     . SER A 171 ? 0.32695 0.28711 0.45788 -0.10025 0.11768  0.00589  201 SER A C     
1323 O  O     . SER A 171 ? 0.35463 0.29264 0.48002 -0.09419 0.11375  0.00586  201 SER A O     
1324 C  CB    . SER A 171 ? 0.39653 0.39554 0.52452 -0.11934 0.12610  0.01193  201 SER A CB    
1325 O  OG    . SER A 171 ? 0.45164 0.42482 0.56640 -0.12753 0.11834  0.01765  201 SER A OG    
1326 N  N     . LYS A 172 ? 0.34125 0.30244 0.47390 -0.10572 0.11352  0.00676  202 LYS A N     
1327 C  CA    . LYS A 172 ? 0.43049 0.36362 0.55643 -0.10500 0.10323  0.00798  202 LYS A CA    
1328 C  C     . LYS A 172 ? 0.39644 0.30633 0.50600 -0.11636 0.09457  0.01471  202 LYS A C     
1329 O  O     . LYS A 172 ? 0.43338 0.31612 0.53477 -0.11081 0.08673  0.01473  202 LYS A O     
1330 C  CB    . LYS A 172 ? 0.40291 0.34205 0.53317 -0.10934 0.10008  0.00763  202 LYS A CB    
1331 C  CG    . LYS A 172 ? 0.44793 0.40742 0.59352 -0.09638 0.10802  0.00040  202 LYS A CG    
1332 C  CD    . LYS A 172 ? 0.55929 0.50528 0.70777 -0.08814 0.10248  -0.00285 202 LYS A CD    
1333 C  CE    . LYS A 172 ? 0.62838 0.59621 0.79134 -0.07729 0.11030  -0.00952 202 LYS A CE    
1334 N  NZ    . LYS A 172 ? 0.79151 0.77571 0.96041 -0.06911 0.12024  -0.01308 202 LYS A NZ    
1335 N  N     . SER A 173 ? 0.37432 0.29445 0.47799 -0.13154 0.09568  0.02039  203 SER A N     
1336 C  CA    A SER A 173 ? 0.39605 0.29261 0.48282 -0.14208 0.08742  0.02682  203 SER A CA    
1337 C  CA    B SER A 173 ? 0.39601 0.29258 0.48281 -0.14204 0.08744  0.02681  203 SER A CA    
1338 C  C     . SER A 173 ? 0.39235 0.27639 0.47542 -0.13207 0.08894  0.02511  203 SER A C     
1339 O  O     . SER A 173 ? 0.43870 0.29515 0.50831 -0.13293 0.08039  0.02773  203 SER A O     
1340 C  CB    A SER A 173 ? 0.40825 0.32057 0.48957 -0.16158 0.08851  0.03394  203 SER A CB    
1341 C  CB    B SER A 173 ? 0.40793 0.32059 0.48949 -0.16141 0.08864  0.03385  203 SER A CB    
1342 O  OG    A SER A 173 ? 0.45448 0.38775 0.54003 -0.16022 0.09813  0.03345  203 SER A OG    
1343 O  OG    B SER A 173 ? 0.50544 0.42791 0.58912 -0.17223 0.08562  0.03628  203 SER A OG    
1344 N  N     . GLU A 174 ? 0.37324 0.27659 0.46713 -0.12232 0.09913  0.02062  204 GLU A N     
1345 C  CA    . GLU A 174 ? 0.36878 0.26198 0.46022 -0.11279 0.10074  0.01881  204 GLU A CA    
1346 C  C     . GLU A 174 ? 0.38609 0.26064 0.47933 -0.09795 0.09662  0.01452  204 GLU A C     
1347 O  O     . GLU A 174 ? 0.45005 0.30491 0.53494 -0.09373 0.09188  0.01531  204 GLU A O     
1348 C  CB    . GLU A 174 ? 0.35206 0.27021 0.45321 -0.10690 0.11187  0.01524  204 GLU A CB    
1349 C  CG    . GLU A 174 ? 0.42329 0.35763 0.51971 -0.11921 0.11583  0.01971  204 GLU A CG    
1350 C  CD    . GLU A 174 ? 0.49936 0.46079 0.60498 -0.11217 0.12646  0.01536  204 GLU A CD    
1351 O  OE1   . GLU A 174 ? 0.42882 0.40361 0.54547 -0.10274 0.13100  0.00981  204 GLU A OE1   
1352 O  OE2   . GLU A 174 ? 0.43626 0.40453 0.53684 -0.11557 0.12977  0.01738  204 GLU A OE2   
1353 N  N     . TYR A 175 ? 0.35072 0.23280 0.45485 -0.08935 0.09858  0.00991  205 TYR A N     
1354 C  CA    . TYR A 175 ? 0.34457 0.21242 0.45161 -0.07477 0.09498  0.00586  205 TYR A CA    
1355 C  C     . TYR A 175 ? 0.34330 0.21381 0.45555 -0.07414 0.09260  0.00410  205 TYR A C     
1356 O  O     . TYR A 175 ? 0.32901 0.22009 0.45325 -0.07097 0.09964  0.00059  205 TYR A O     
1357 C  CB    . TYR A 175 ? 0.32585 0.20201 0.44281 -0.06058 0.10188  0.00090  205 TYR A CB    
1358 C  CG    . TYR A 175 ? 0.32279 0.18401 0.44047 -0.04737 0.09711  -0.00168 205 TYR A CG    
1359 C  CD1   . TYR A 175 ? 0.33278 0.17468 0.44041 -0.04442 0.09065  0.00024  205 TYR A CD1   
1360 C  CD2   . TYR A 175 ? 0.31072 0.17835 0.43861 -0.03765 0.09891  -0.00597 205 TYR A CD2   
1361 C  CE1   . TYR A 175 ? 0.33043 0.16179 0.43849 -0.03172 0.08631  -0.00201 205 TYR A CE1   
1362 C  CE2   . TYR A 175 ? 0.30828 0.16463 0.43670 -0.02547 0.09470  -0.00795 205 TYR A CE2   
1363 C  CZ    . TYR A 175 ? 0.31805 0.15724 0.43668 -0.02239 0.08845  -0.00594 205 TYR A CZ    
1364 O  OH    . TYR A 175 ? 0.34524 0.17622 0.46412 -0.00977 0.08433  -0.00779 205 TYR A OH    
1365 N  N     . PRO A 176 ? 0.39563 0.24448 0.49799 -0.07651 0.08213  0.00623  206 PRO A N     
1366 C  CA    . PRO A 176 ? 0.36812 0.21847 0.47333 -0.07894 0.07869  0.00549  206 PRO A CA    
1367 C  C     . PRO A 176 ? 0.35116 0.19800 0.46400 -0.06320 0.07783  0.00002  206 PRO A C     
1368 O  O     . PRO A 176 ? 0.41364 0.26087 0.52862 -0.06449 0.07463  -0.00089 206 PRO A O     
1369 C  CB    . PRO A 176 ? 0.38933 0.21452 0.47649 -0.09076 0.06626  0.01119  206 PRO A CB    
1370 C  CG    . PRO A 176 ? 0.39776 0.20211 0.47384 -0.08513 0.06161  0.01215  206 PRO A CG    
1371 C  CD    . PRO A 176 ? 0.38042 0.20290 0.46555 -0.08103 0.07245  0.01054  206 PRO A CD    
1372 N  N     . TRP A 177 ? 0.38707 0.23216 0.50414 -0.04929 0.08075  -0.00326 207 TRP A N     
1373 C  CA    . TRP A 177 ? 0.33081 0.17196 0.45389 -0.03404 0.07926  -0.00780 207 TRP A CA    
1374 C  C     . TRP A 177 ? 0.33227 0.19623 0.47176 -0.02539 0.08994  -0.01263 207 TRP A C     
1375 O  O     . TRP A 177 ? 0.34187 0.22160 0.48635 -0.02904 0.09788  -0.01278 207 TRP A O     
1376 C  CB    . TRP A 177 ? 0.33839 0.15913 0.45230 -0.02434 0.07236  -0.00750 207 TRP A CB    
1377 C  CG    . TRP A 177 ? 0.36419 0.15968 0.45974 -0.03169 0.06042  -0.00340 207 TRP A CG    
1378 C  CD1   . TRP A 177 ? 0.43687 0.21672 0.52375 -0.03412 0.05088  -0.00266 207 TRP A CD1   
1379 C  CD2   . TRP A 177 ? 0.39725 0.17869 0.47933 -0.03801 0.05612  0.00060  207 TRP A CD2   
1380 N  NE1   . TRP A 177 ? 0.40510 0.16064 0.47296 -0.04146 0.04039  0.00156  207 TRP A NE1   
1381 C  CE2   . TRP A 177 ? 0.44853 0.20491 0.51325 -0.04394 0.04359  0.00361  207 TRP A CE2   
1382 C  CE3   . TRP A 177 ? 0.37435 0.16076 0.45642 -0.03914 0.06107  0.00185  207 TRP A CE3   
1383 C  CZ2   . TRP A 177 ? 0.42570 0.16179 0.47285 -0.05066 0.03608  0.00777  207 TRP A CZ2   
1384 C  CZ3   . TRP A 177 ? 0.39382 0.16157 0.45969 -0.04564 0.05411  0.00587  207 TRP A CZ3   
1385 C  CH2   . TRP A 177 ? 0.41922 0.16207 0.46771 -0.05126 0.04186  0.00878  207 TRP A CH2   
1386 N  N     . ASP A 178 ? 0.29918 0.16372 0.44547 -0.01386 0.08958  -0.01651 208 ASP A N     
1387 C  CA    . ASP A 178 ? 0.39563 0.28006 0.55628 -0.00583 0.09879  -0.02122 208 ASP A CA    
1388 C  C     . ASP A 178 ? 0.37347 0.26238 0.53868 0.00324  0.10419  -0.02272 208 ASP A C     
1389 O  O     . ASP A 178 ? 0.41810 0.32302 0.59189 0.00580  0.11224  -0.02552 208 ASP A O     
1390 C  CB    . ASP A 178 ? 0.45387 0.33653 0.61937 0.00298  0.09610  -0.02452 208 ASP A CB    
1391 C  CG    . ASP A 178 ? 0.61034 0.49114 0.77328 -0.00547 0.09126  -0.02375 208 ASP A CG    
1392 O  OD1   . ASP A 178 ? 0.70821 0.59536 0.86832 -0.01929 0.09203  -0.02083 208 ASP A OD1   
1393 O  OD2   . ASP A 178 ? 0.53833 0.41191 0.70190 0.00172  0.08651  -0.02587 208 ASP A OD2   
1394 N  N     . ARG A 179 ? 0.34474 0.21975 0.50352 0.00805  0.09927  -0.02094 209 ARG A N     
1395 C  CA    . ARG A 179 ? 0.37064 0.24994 0.53355 0.01610  0.10339  -0.02175 209 ARG A CA    
1396 C  C     . ARG A 179 ? 0.38045 0.25004 0.53392 0.01128  0.10044  -0.01809 209 ARG A C     
1397 O  O     . ARG A 179 ? 0.31001 0.16550 0.45281 0.00546  0.09339  -0.01530 209 ARG A O     
1398 C  CB    . ARG A 179 ? 0.42406 0.29965 0.59021 0.02970  0.10051  -0.02355 209 ARG A CB    
1399 C  CG    . ARG A 179 ? 0.63693 0.52943 0.80842 0.03378  0.10176  -0.02602 209 ARG A CG    
1400 C  CD    . ARG A 179 ? 0.72050 0.62591 0.88742 0.04068  0.09750  -0.02469 209 ARG A CD    
1401 N  NE    . ARG A 179 ? 0.95782 0.85594 1.11577 0.04737  0.08836  -0.02328 209 ARG A NE    
1402 C  CZ    . ARG A 179 ? 1.08320 0.98978 1.23622 0.05370  0.08400  -0.02215 209 ARG A CZ    
1403 N  NH1   . ARG A 179 ? 0.90100 0.81518 1.05574 0.05281  0.08706  -0.02056 209 ARG A NH1   
1404 N  NH2   . ARG A 179 ? 1.06432 0.97104 1.21041 0.06084  0.07659  -0.02276 209 ARG A NH2   
1405 N  N     . TYR A 180 ? 0.26349 0.14009 0.42024 0.01323  0.10553  -0.01818 210 TYR A N     
1406 C  CA    . TYR A 180 ? 0.31757 0.18591 0.46617 0.01003  0.10305  -0.01504 210 TYR A CA    
1407 C  C     . TYR A 180 ? 0.36109 0.22226 0.50828 0.02068  0.09820  -0.01480 210 TYR A C     
1408 O  O     . TYR A 180 ? 0.40786 0.27373 0.56187 0.03025  0.09856  -0.01698 210 TYR A O     
1409 C  CB    . TYR A 180 ? 0.26258 0.14222 0.41529 0.00772  0.11043  -0.01550 210 TYR A CB    
1410 C  CG    . TYR A 180 ? 0.26557 0.15242 0.41641 -0.00296 0.11463  -0.01498 210 TYR A CG    
1411 C  CD1   . TYR A 180 ? 0.27923 0.15891 0.42142 -0.01316 0.11064  -0.01185 210 TYR A CD1   
1412 C  CD2   . TYR A 180 ? 0.25618 0.15712 0.41277 -0.00259 0.12212  -0.01745 210 TYR A CD2   
1413 C  CE1   . TYR A 180 ? 0.28207 0.17134 0.42274 -0.02313 0.11467  -0.01082 210 TYR A CE1   
1414 C  CE2   . TYR A 180 ? 0.25930 0.16928 0.41374 -0.01095 0.12598  -0.01715 210 TYR A CE2   
1415 C  CZ    . TYR A 180 ? 0.27151 0.17716 0.41871 -0.02141 0.12259  -0.01365 210 TYR A CZ    
1416 O  OH    . TYR A 180 ? 0.32382 0.24116 0.46907 -0.02997 0.12653  -0.01279 210 TYR A OH    
1417 N  N     . PRO A 181 ? 0.33025 0.18088 0.46826 0.02003  0.09332  -0.01215 211 PRO A N     
1418 C  CA    . PRO A 181 ? 0.28096 0.12882 0.41807 0.03110  0.08922  -0.01197 211 PRO A CA    
1419 C  C     . PRO A 181 ? 0.31911 0.18165 0.46604 0.03498  0.09565  -0.01250 211 PRO A C     
1420 O  O     . PRO A 181 ? 0.28516 0.15555 0.43670 0.02885  0.10223  -0.01305 211 PRO A O     
1421 C  CB    . PRO A 181 ? 0.32132 0.15509 0.44526 0.02728  0.08309  -0.00914 211 PRO A CB    
1422 C  CG    . PRO A 181 ? 0.37032 0.20600 0.49261 0.01449  0.08771  -0.00762 211 PRO A CG    
1423 C  CD    . PRO A 181 ? 0.37097 0.21276 0.49850 0.00927  0.09127  -0.00910 211 PRO A CD    
1424 N  N     . PRO A 182 ? 0.43325 0.30421 0.57963 0.04324  0.09176  -0.01169 212 PRO A N     
1425 C  CA    . PRO A 182 ? 0.31663 0.20079 0.46928 0.04372  0.09616  -0.01083 212 PRO A CA    
1426 C  C     . PRO A 182 ? 0.30756 0.18315 0.45932 0.03768  0.09996  -0.00961 212 PRO A C     
1427 O  O     . PRO A 182 ? 0.26649 0.13140 0.40853 0.03547  0.09488  -0.00794 212 PRO A O     
1428 C  CB    . PRO A 182 ? 0.32333 0.21433 0.47415 0.05294  0.09047  -0.00951 212 PRO A CB    
1429 C  CG    . PRO A 182 ? 0.25699 0.14105 0.40015 0.05880  0.08287  -0.01069 212 PRO A CG    
1430 C  CD    . PRO A 182 ? 0.35239 0.21857 0.49091 0.05210  0.08284  -0.01127 212 PRO A CD    
1431 N  N     . PHE A 183 ? 0.27137 0.15510 0.42836 0.03389  0.10590  -0.00990 213 PHE A N     
1432 C  CA    . PHE A 183 ? 0.26717 0.14817 0.41895 0.02687  0.10681  -0.00818 213 PHE A CA    
1433 C  C     . PHE A 183 ? 0.29180 0.18186 0.44936 0.02676  0.11127  -0.00823 213 PHE A C     
1434 O  O     . PHE A 183 ? 0.23402 0.13165 0.39894 0.03079  0.11410  -0.00966 213 PHE A O     
1435 C  CB    . PHE A 183 ? 0.28999 0.16501 0.43591 0.01793  0.10822  -0.00860 213 PHE A CB    
1436 C  CG    . PHE A 183 ? 0.33793 0.22083 0.48893 0.01470  0.11460  -0.01126 213 PHE A CG    
1437 C  CD1   . PHE A 183 ? 0.26061 0.14639 0.41591 0.01651  0.11554  -0.01343 213 PHE A CD1   
1438 C  CD2   . PHE A 183 ? 0.33876 0.22599 0.48918 0.01053  0.11913  -0.01183 213 PHE A CD2   
1439 C  CE1   . PHE A 183 ? 0.26894 0.16333 0.42847 0.01437  0.12121  -0.01616 213 PHE A CE1   
1440 C  CE2   . PHE A 183 ? 0.31122 0.20619 0.46486 0.00917  0.12447  -0.01475 213 PHE A CE2   
1441 C  CZ    . PHE A 183 ? 0.38984 0.28911 0.54830 0.01115  0.12565  -0.01693 213 PHE A CZ    
1442 N  N     . CYS A 184 ? 0.24654 0.13438 0.39959 0.02201  0.11124  -0.00657 214 CYS A N     
1443 C  CA    . CYS A 184 ? 0.32484 0.21826 0.48093 0.02069  0.11446  -0.00653 214 CYS A CA    
1444 C  C     . CYS A 184 ? 0.27816 0.16865 0.42956 0.01420  0.11811  -0.00812 214 CYS A C     
1445 O  O     . CYS A 184 ? 0.37701 0.26172 0.52180 0.00932  0.11737  -0.00760 214 CYS A O     
1446 C  CB    . CYS A 184 ? 0.29600 0.19074 0.45076 0.02097  0.11112  -0.00329 214 CYS A CB    
1447 S  SG    . CYS A 184 ? 0.38564 0.28975 0.54674 0.02975  0.10737  -0.00112 214 CYS A SG    
1448 N  N     . SER A 185 ? 0.30520 0.19934 0.45859 0.01426  0.12171  -0.01001 215 SER A N     
1449 C  CA    . SER A 185 ? 0.29147 0.18376 0.43903 0.00980  0.12488  -0.01198 215 SER A CA    
1450 C  C     . SER A 185 ? 0.31400 0.20013 0.45372 0.00469  0.12272  -0.00971 215 SER A C     
1451 O  O     . SER A 185 ? 0.34214 0.22616 0.48132 0.00485  0.11930  -0.00701 215 SER A O     
1452 C  CB    . SER A 185 ? 0.27252 0.16686 0.42057 0.01191  0.12737  -0.01430 215 SER A CB    
1453 O  OG    . SER A 185 ? 0.33513 0.22803 0.47623 0.00943  0.12989  -0.01669 215 SER A OG    
1454 N  N     . GLY A 186 ? 0.26050 0.14530 0.39438 0.00033  0.12480  -0.01072 216 GLY A N     
1455 C  CA    . GLY A 186 ? 0.26915 0.14808 0.39480 -0.00455 0.12316  -0.00876 216 GLY A CA    
1456 C  C     . GLY A 186 ? 0.36963 0.24666 0.49107 -0.00462 0.12353  -0.00949 216 GLY A C     
1457 O  O     . GLY A 186 ? 0.45724 0.32898 0.57198 -0.00802 0.12169  -0.00781 216 GLY A O     
1458 N  N     . THR A 187 ? 0.26825 0.14797 0.39226 -0.00098 0.12523  -0.01190 217 THR A N     
1459 C  CA    . THR A 187 ? 0.34579 0.22071 0.46419 -0.00083 0.12399  -0.01242 217 THR A CA    
1460 C  C     . THR A 187 ? 0.27979 0.15005 0.39735 -0.00328 0.11922  -0.00841 217 THR A C     
1461 O  O     . THR A 187 ? 0.40887 0.27331 0.51864 -0.00602 0.11768  -0.00796 217 THR A O     
1462 C  CB    . THR A 187 ? 0.26953 0.14634 0.39090 0.00370  0.12523  -0.01501 217 THR A CB    
1463 O  OG1   . THR A 187 ? 0.34348 0.22468 0.47425 0.00580  0.12437  -0.01322 217 THR A OG1   
1464 C  CG2   . THR A 187 ? 0.26940 0.15119 0.38937 0.00668  0.12980  -0.01965 217 THR A CG2   
1465 N  N     . GLY A 188 ? 0.26940 0.14314 0.39426 -0.00178 0.11687  -0.00579 218 GLY A N     
1466 C  CA    . GLY A 188 ? 0.32691 0.20010 0.45219 -0.00338 0.11233  -0.00182 218 GLY A CA    
1467 C  C     . GLY A 188 ? 0.27076 0.15064 0.40383 0.00019  0.11086  0.00006  218 GLY A C     
1468 O  O     . GLY A 188 ? 0.37223 0.25798 0.51213 0.00387  0.11218  -0.00057 218 GLY A O     
1469 N  N     . TYR A 189 ? 0.32449 0.20291 0.45551 -0.00003 0.10799  0.00197  219 TYR A N     
1470 C  CA    . TYR A 189 ? 0.29457 0.17891 0.43106 0.00503  0.10538  0.00359  219 TYR A CA    
1471 C  C     . TYR A 189 ? 0.27334 0.15838 0.40695 0.00468  0.10061  0.00671  219 TYR A C     
1472 O  O     . TYR A 189 ? 0.27530 0.15324 0.40164 0.00052  0.09952  0.00709  219 TYR A O     
1473 C  CB    . TYR A 189 ? 0.26226 0.14398 0.39869 0.00771  0.10600  0.00186  219 TYR A CB    
1474 C  CG    . TYR A 189 ? 0.32068 0.19281 0.44868 0.00354  0.10585  0.00124  219 TYR A CG    
1475 C  CD1   . TYR A 189 ? 0.27938 0.14507 0.40026 0.00262  0.10150  0.00319  219 TYR A CD1   
1476 C  CD2   . TYR A 189 ? 0.31583 0.18630 0.44269 0.00055  0.10984  -0.00109 219 TYR A CD2   
1477 C  CE1   . TYR A 189 ? 0.32071 0.17692 0.43295 -0.00197 0.10103  0.00318  219 TYR A CE1   
1478 C  CE2   . TYR A 189 ? 0.32771 0.19121 0.44686 -0.00441 0.10966  -0.00085 219 TYR A CE2   
1479 C  CZ    . TYR A 189 ? 0.31636 0.17190 0.42790 -0.00603 0.10515  0.00148  219 TYR A CZ    
1480 O  OH    . TYR A 189 ? 0.38394 0.23187 0.48693 -0.01172 0.10464  0.00226  219 TYR A OH    
1481 N  N     . VAL A 190 ? 0.32334 0.21831 0.46267 0.00944  0.09790  0.00886  220 VAL A N     
1482 C  CA    . VAL A 190 ? 0.27707 0.17646 0.41452 0.01007  0.09315  0.01188  220 VAL A CA    
1483 C  C     . VAL A 190 ? 0.26934 0.17212 0.40664 0.01801  0.08964  0.01203  220 VAL A C     
1484 O  O     . VAL A 190 ? 0.29118 0.19941 0.43379 0.02364  0.09043  0.01117  220 VAL A O     
1485 C  CB    . VAL A 190 ? 0.26636 0.17738 0.40941 0.00796  0.09203  0.01513  220 VAL A CB    
1486 C  CG1   . VAL A 190 ? 0.30984 0.22659 0.45069 0.00747  0.08724  0.01823  220 VAL A CG1   
1487 C  CG2   . VAL A 190 ? 0.26297 0.16801 0.40452 0.00126  0.09458  0.01455  220 VAL A CG2   
1488 N  N     . PHE A 191 ? 0.27470 0.17318 0.40483 0.01888  0.08548  0.01282  221 PHE A N     
1489 C  CA    . PHE A 191 ? 0.33098 0.23058 0.45796 0.02769  0.08078  0.01259  221 PHE A CA    
1490 C  C     . PHE A 191 ? 0.36411 0.26924 0.48739 0.02993  0.07589  0.01469  221 PHE A C     
1491 O  O     . PHE A 191 ? 0.30590 0.20737 0.42570 0.02352  0.07574  0.01576  221 PHE A O     
1492 C  CB    . PHE A 191 ? 0.28817 0.17034 0.40559 0.02784  0.07959  0.01022  221 PHE A CB    
1493 C  CG    . PHE A 191 ? 0.29651 0.16437 0.40521 0.01939  0.08065  0.00987  221 PHE A CG    
1494 C  CD1   . PHE A 191 ? 0.36917 0.23320 0.47954 0.01215  0.08616  0.00875  221 PHE A CD1   
1495 C  CD2   . PHE A 191 ? 0.33865 0.19738 0.43669 0.01948  0.07596  0.01054  221 PHE A CD2   
1496 C  CE1   . PHE A 191 ? 0.30988 0.16314 0.41211 0.00513  0.08725  0.00859  221 PHE A CE1   
1497 C  CE2   . PHE A 191 ? 0.32392 0.17025 0.41374 0.01177  0.07706  0.01051  221 PHE A CE2   
1498 C  CZ    . PHE A 191 ? 0.36101 0.20541 0.45319 0.00460  0.08282  0.00966  221 PHE A CZ    
1499 N  N     . SER A 192 ? 0.34136 0.25684 0.46551 0.03968  0.07178  0.01517  222 SER A N     
1500 C  CA    . SER A 192 ? 0.39425 0.31460 0.51293 0.04367  0.06637  0.01647  222 SER A CA    
1501 C  C     . SER A 192 ? 0.35035 0.24955 0.45494 0.04258  0.06322  0.01461  222 SER A C     
1502 O  O     . SER A 192 ? 0.37348 0.25684 0.47168 0.04281  0.06314  0.01243  222 SER A O     
1503 C  CB    . SER A 192 ? 0.34231 0.27874 0.46322 0.05634  0.06223  0.01681  222 SER A CB    
1504 O  OG    . SER A 192 ? 0.49587 0.42356 0.61295 0.06395  0.06087  0.01403  222 SER A OG    
1505 N  N     . GLY A 193 ? 0.31506 0.21418 0.41439 0.04083  0.06028  0.01579  223 GLY A N     
1506 C  CA    . GLY A 193 ? 0.34200 0.22084 0.42800 0.03745  0.05799  0.01461  223 GLY A CA    
1507 C  C     . GLY A 193 ? 0.47622 0.34000 0.54968 0.04507  0.05258  0.01245  223 GLY A C     
1508 O  O     . GLY A 193 ? 0.48670 0.33056 0.54975 0.04004  0.05207  0.01159  223 GLY A O     
1509 N  N     . ASP A 194 ? 0.43469 0.30757 0.50777 0.05725  0.04795  0.01173  224 ASP A N     
1510 C  CA    . ASP A 194 ? 0.46609 0.32237 0.52510 0.06575  0.04139  0.00937  224 ASP A CA    
1511 C  C     . ASP A 194 ? 0.53277 0.37357 0.59017 0.06107  0.04374  0.00818  224 ASP A C     
1512 O  O     . ASP A 194 ? 0.54272 0.36212 0.58570 0.06208  0.03871  0.00690  224 ASP A O     
1513 C  CB    . ASP A 194 ? 0.38173 0.25334 0.44209 0.08077  0.03666  0.00850  224 ASP A CB    
1514 C  CG    . ASP A 194 ? 0.55667 0.44696 0.63288 0.08199  0.04184  0.00925  224 ASP A CG    
1515 O  OD1   . ASP A 194 ? 0.56088 0.46479 0.64994 0.07343  0.04804  0.01159  224 ASP A OD1   
1516 O  OD2   . ASP A 194 ? 0.58549 0.47531 0.66055 0.09105  0.03955  0.00751  224 ASP A OD2   
1517 N  N     . VAL A 195 ? 0.51381 0.36547 0.58537 0.05618  0.05077  0.00868  225 VAL A N     
1518 C  CA    . VAL A 195 ? 0.40818 0.24849 0.47992 0.05140  0.05363  0.00754  225 VAL A CA    
1519 C  C     . VAL A 195 ? 0.50678 0.32735 0.56834 0.04063  0.05421  0.00784  225 VAL A C     
1520 O  O     . VAL A 195 ? 0.48365 0.28936 0.53808 0.03815  0.05266  0.00710  225 VAL A O     
1521 C  CB    . VAL A 195 ? 0.47778 0.33383 0.56611 0.04760  0.06142  0.00793  225 VAL A CB    
1522 C  CG1   . VAL A 195 ? 0.39326 0.23885 0.48211 0.04136  0.06511  0.00664  225 VAL A CG1   
1523 C  CG2   . VAL A 195 ? 0.33145 0.20566 0.42835 0.05830  0.06034  0.00794  225 VAL A CG2   
1524 N  N     . ALA A 196 ? 0.45990 0.28063 0.52054 0.03355  0.05641  0.00919  226 ALA A N     
1525 C  CA    . ALA A 196 ? 0.36081 0.16481 0.41172 0.02342  0.05732  0.00979  226 ALA A CA    
1526 C  C     . ALA A 196 ? 0.48427 0.26747 0.51726 0.02590  0.04931  0.00961  226 ALA A C     
1527 O  O     . ALA A 196 ? 0.50682 0.27504 0.53180 0.01866  0.04900  0.01013  226 ALA A O     
1528 C  CB    . ALA A 196 ? 0.42766 0.23499 0.47915 0.01726  0.06000  0.01107  226 ALA A CB    
1529 N  N     . SER A 197 ? 0.46680 0.24839 0.49226 0.03646  0.04206  0.00889  227 SER A N     
1530 C  CA    . SER A 197 ? 0.54153 0.29946 0.54662 0.03891  0.03325  0.00856  227 SER A CA    
1531 C  C     . SER A 197 ? 0.52986 0.27645 0.52969 0.04212  0.02934  0.00745  227 SER A C     
1532 O  O     . SER A 197 ? 0.56109 0.28571 0.54641 0.03614  0.02509  0.00826  227 SER A O     
1533 C  CB    . SER A 197 ? 0.58420 0.34288 0.58074 0.05029  0.02604  0.00761  227 SER A CB    
1534 O  OG    . SER A 197 ? 0.76732 0.53197 0.76555 0.04578  0.02849  0.00883  227 SER A OG    
1535 N  N     . GLN A 198 ? 0.46376 0.22493 0.47475 0.05056  0.03057  0.00597  228 GLN A N     
1536 C  CA    . GLN A 198 ? 0.42108 0.17202 0.42726 0.05500  0.02634  0.00458  228 GLN A CA    
1537 C  C     . GLN A 198 ? 0.53957 0.28393 0.54917 0.04130  0.03165  0.00580  228 GLN A C     
1538 O  O     . GLN A 198 ? 0.48974 0.21573 0.48787 0.03955  0.02617  0.00576  228 GLN A O     
1539 C  CB    . GLN A 198 ? 0.41131 0.18214 0.42962 0.06754  0.02716  0.00284  228 GLN A CB    
1540 C  CG    . GLN A 198 ? 0.60013 0.38421 0.61772 0.08026  0.02326  0.00215  228 GLN A CG    
1541 C  CD    . GLN A 198 ? 0.78280 0.59276 0.81598 0.08984  0.02640  0.00156  228 GLN A CD    
1542 O  OE1   . GLN A 198 ? 0.73733 0.54674 0.76844 0.10005  0.02251  -0.00031 228 GLN A OE1   
1543 N  NE2   . GLN A 198 ? 0.63725 0.46973 0.68550 0.08631  0.03309  0.00338  228 GLN A NE2   
1544 N  N     . VAL A 199 ? 0.47338 0.23240 0.49734 0.03217  0.04140  0.00685  229 VAL A N     
1545 C  CA    . VAL A 199 ? 0.39273 0.14958 0.42082 0.02003  0.04707  0.00774  229 VAL A CA    
1546 C  C     . VAL A 199 ? 0.44546 0.18273 0.45772 0.00931  0.04392  0.01008  229 VAL A C     
1547 O  O     . VAL A 199 ? 0.49905 0.22395 0.50422 0.00323  0.04139  0.01099  229 VAL A O     
1548 C  CB    . VAL A 199 ? 0.37123 0.14843 0.41716 0.01489  0.05766  0.00765  229 VAL A CB    
1549 C  CG1   . VAL A 199 ? 0.37052 0.14586 0.41777 0.00241  0.06312  0.00858  229 VAL A CG1   
1550 C  CG2   . VAL A 199 ? 0.38654 0.18061 0.44690 0.02355  0.06049  0.00584  229 VAL A CG2   
1551 N  N     . TYR A 200 ? 0.41612 0.15089 0.42269 0.00698  0.04363  0.01126  230 TYR A N     
1552 C  CA    . TYR A 200 ? 0.52445 0.24160 0.51578 -0.00368 0.04108  0.01391  230 TYR A CA    
1553 C  C     . TYR A 200 ? 0.58864 0.28173 0.56132 -0.00186 0.03045  0.01440  230 TYR A C     
1554 O  O     . TYR A 200 ? 0.75752 0.43641 0.71992 -0.01291 0.02850  0.01700  230 TYR A O     
1555 C  CB    . TYR A 200 ? 0.43694 0.15376 0.42355 -0.00335 0.04077  0.01456  230 TYR A CB    
1556 C  CG    . TYR A 200 ? 0.58779 0.28690 0.55821 -0.01376 0.03816  0.01746  230 TYR A CG    
1557 C  CD1   . TYR A 200 ? 0.60577 0.30737 0.57826 -0.02704 0.04434  0.01981  230 TYR A CD1   
1558 C  CD2   . TYR A 200 ? 0.68425 0.36508 0.63675 -0.00989 0.02940  0.01788  230 TYR A CD2   
1559 C  CE1   . TYR A 200 ? 0.70381 0.39112 0.66158 -0.03701 0.04218  0.02302  230 TYR A CE1   
1560 C  CE2   . TYR A 200 ? 0.73260 0.39664 0.66952 -0.01975 0.02685  0.02086  230 TYR A CE2   
1561 C  CZ    . TYR A 200 ? 0.84953 0.51722 0.78935 -0.03378 0.03339  0.02371  230 TYR A CZ    
1562 O  OH    . TYR A 200 ? 0.93503 0.58791 0.85953 -0.04404 0.03109  0.02721  230 TYR A OH    
1563 N  N     . ASN A 201 ? 0.50586 0.19463 0.47343 0.01211  0.02313  0.01204  231 ASN A N     
1564 C  CA    . ASN A 201 ? 0.57003 0.23301 0.51688 0.01665  0.01106  0.01180  231 ASN A CA    
1565 C  C     . ASN A 201 ? 0.60384 0.25993 0.55070 0.01076  0.01017  0.01241  231 ASN A C     
1566 O  O     . ASN A 201 ? 0.64596 0.28060 0.57691 0.00073  0.00461  0.01512  231 ASN A O     
1567 C  CB    . ASN A 201 ? 0.55279 0.21661 0.49534 0.03511  0.00395  0.00848  231 ASN A CB    
1568 C  CG    . ASN A 201 ? 0.80234 0.43684 0.72004 0.04131  -0.00974 0.00775  231 ASN A CG    
1569 O  OD1   . ASN A 201 ? 0.93224 0.56535 0.84656 0.05548  -0.01593 0.00481  231 ASN A OD1   
1570 N  ND2   . ASN A 201 ? 0.84565 0.45594 0.74467 0.03112  -0.01508 0.01046  231 ASN A ND2   
1571 N  N     . VAL A 202 ? 0.47345 0.14705 0.43706 0.01596  0.01524  0.01032  232 VAL A N     
1572 C  CA    . VAL A 202 ? 0.47668 0.14433 0.44057 0.01191  0.01378  0.01043  232 VAL A CA    
1573 C  C     . VAL A 202 ? 0.57444 0.25058 0.54743 -0.00489 0.02251  0.01314  232 VAL A C     
1574 O  O     . VAL A 202 ? 0.53972 0.20907 0.51037 -0.01134 0.02060  0.01410  232 VAL A O     
1575 C  CB    . VAL A 202 ? 0.45972 0.14412 0.43775 0.02587  0.01580  0.00687  232 VAL A CB    
1576 C  CG1   . VAL A 202 ? 0.51407 0.22779 0.51531 0.02574  0.02803  0.00617  232 VAL A CG1   
1577 C  CG2   . VAL A 202 ? 0.68588 0.36216 0.66216 0.02608  0.01205  0.00606  232 VAL A CG2   
1578 N  N     . SER A 203 ? 0.45614 0.14573 0.43735 -0.01148 0.03082  0.01437  233 SER A N     
1579 C  CA    . SER A 203 ? 0.48953 0.19111 0.47994 -0.02558 0.03985  0.01646  233 SER A CA    
1580 C  C     . SER A 203 ? 0.55800 0.24315 0.53507 -0.03867 0.03499  0.02003  233 SER A C     
1581 O  O     . SER A 203 ? 0.56184 0.25635 0.54734 -0.04538 0.03927  0.02047  233 SER A O     
1582 C  CB    . SER A 203 ? 0.43995 0.15072 0.43354 -0.03022 0.04614  0.01758  233 SER A CB    
1583 O  OG    . SER A 203 ? 0.62678 0.31878 0.60212 -0.03635 0.04018  0.02056  233 SER A OG    
1584 N  N     . LYS A 204 ? 0.52702 0.18856 0.48342 -0.04223 0.02594  0.02262  234 LYS A N     
1585 C  CA    . LYS A 204 ? 0.56120 0.20583 0.50283 -0.05711 0.02059  0.02717  234 LYS A CA    
1586 C  C     . LYS A 204 ? 0.56804 0.20145 0.50540 -0.05572 0.01350  0.02657  234 LYS A C     
1587 O  O     . LYS A 204 ? 0.69654 0.32283 0.62713 -0.06971 0.01117  0.03044  234 LYS A O     
1588 C  CB    . LYS A 204 ? 0.65390 0.27459 0.57328 -0.06017 0.01217  0.02995  234 LYS A CB    
1589 C  CG    . LYS A 204 ? 0.89363 0.52518 0.81643 -0.06497 0.01947  0.03140  234 LYS A CG    
1590 C  CD    . LYS A 204 ? 1.12152 0.72844 1.02104 -0.07044 0.01120  0.03483  234 LYS A CD    
1591 C  CE    . LYS A 204 ? 1.28514 0.87333 1.17124 -0.05559 0.00124  0.03181  234 LYS A CE    
1592 N  NZ    . LYS A 204 ? 1.41204 0.98002 1.27725 -0.05997 -0.00605 0.03460  234 LYS A NZ    
1593 N  N     . SER A 205 ? 0.51594 0.14969 0.45769 -0.03993 0.01047  0.02212  235 SER A N     
1594 C  CA    . SER A 205 ? 0.57065 0.19108 0.50597 -0.03883 0.00270  0.02165  235 SER A CA    
1595 C  C     . SER A 205 ? 0.54031 0.18405 0.49729 -0.03640 0.01115  0.01907  235 SER A C     
1596 O  O     . SER A 205 ? 0.63822 0.27369 0.59223 -0.03562 0.00576  0.01844  235 SER A O     
1597 C  CB    . SER A 205 ? 0.73463 0.33394 0.65457 -0.02246 -0.00946 0.01858  235 SER A CB    
1598 O  OG    . SER A 205 ? 0.71646 0.33475 0.65127 -0.00577 -0.00453 0.01399  235 SER A OG    
1599 N  N     . VAL A 206 ? 0.50153 0.17266 0.47889 -0.03527 0.02364  0.01754  236 VAL A N     
1600 C  CA    . VAL A 206 ? 0.47268 0.16656 0.47051 -0.03228 0.03224  0.01481  236 VAL A CA    
1601 C  C     . VAL A 206 ? 0.48660 0.19222 0.49058 -0.04846 0.03901  0.01765  236 VAL A C     
1602 O  O     . VAL A 206 ? 0.47494 0.18404 0.47620 -0.05866 0.04278  0.02067  236 VAL A O     
1603 C  CB    . VAL A 206 ? 0.46358 0.17893 0.47790 -0.02179 0.04097  0.01167  236 VAL A CB    
1604 C  CG1   . VAL A 206 ? 0.40539 0.14361 0.43964 -0.02024 0.05036  0.00920  236 VAL A CG1   
1605 C  CG2   . VAL A 206 ? 0.54376 0.25124 0.55260 -0.00529 0.03409  0.00912  236 VAL A CG2   
1606 N  N     . PRO A 207 ? 0.44315 0.15633 0.45510 -0.05094 0.04069  0.01680  237 PRO A N     
1607 C  CA    . PRO A 207 ? 0.51092 0.23938 0.52956 -0.06575 0.04756  0.01936  237 PRO A CA    
1608 C  C     . PRO A 207 ? 0.46372 0.21582 0.49549 -0.06704 0.05955  0.01858  237 PRO A C     
1609 O  O     . PRO A 207 ? 0.39980 0.16532 0.44451 -0.05603 0.06562  0.01465  237 PRO A O     
1610 C  CB    . PRO A 207 ? 0.42926 0.16627 0.45841 -0.06256 0.04868  0.01669  237 PRO A CB    
1611 C  CG    . PRO A 207 ? 0.48352 0.19986 0.50357 -0.05045 0.03827  0.01457  237 PRO A CG    
1612 C  CD    . PRO A 207 ? 0.53707 0.24804 0.55332 -0.03951 0.03703  0.01321  237 PRO A CD    
1613 N  N     . TYR A 208 ? 0.44786 0.20475 0.47524 -0.08080 0.06248  0.02259  238 TYR A N     
1614 C  CA    . TYR A 208 ? 0.41012 0.18835 0.44760 -0.08211 0.07308  0.02186  238 TYR A CA    
1615 C  C     . TYR A 208 ? 0.38980 0.19300 0.44471 -0.07992 0.08223  0.01851  238 TYR A C     
1616 O  O     . TYR A 208 ? 0.43099 0.23881 0.48864 -0.08495 0.08156  0.01893  238 TYR A O     
1617 C  CB    . TYR A 208 ? 0.42397 0.20194 0.45126 -0.09725 0.07348  0.02723  238 TYR A CB    
1618 C  CG    . TYR A 208 ? 0.48897 0.28971 0.52538 -0.09848 0.08413  0.02638  238 TYR A CG    
1619 C  CD1   . TYR A 208 ? 0.40549 0.20468 0.44106 -0.09217 0.08629  0.02512  238 TYR A CD1   
1620 C  CD2   . TYR A 208 ? 0.44880 0.27310 0.49417 -0.10509 0.09167  0.02654  238 TYR A CD2   
1621 C  CE1   . TYR A 208 ? 0.40346 0.22126 0.44562 -0.09255 0.09500  0.02407  238 TYR A CE1   
1622 C  CE2   . TYR A 208 ? 0.42384 0.26804 0.47560 -0.10454 0.10062  0.02526  238 TYR A CE2   
1623 C  CZ    . TYR A 208 ? 0.46074 0.30043 0.51036 -0.09825 0.10200  0.02402  238 TYR A CZ    
1624 O  OH    . TYR A 208 ? 0.54463 0.40226 0.59902 -0.09700 0.11008  0.02248  238 TYR A OH    
1625 N  N     . ILE A 209 ? 0.44467 0.26310 0.51039 -0.07235 0.09022  0.01514  239 ILE A N     
1626 C  CA    . ILE A 209 ? 0.35533 0.19774 0.43498 -0.07103 0.09940  0.01206  239 ILE A CA    
1627 C  C     . ILE A 209 ? 0.34761 0.20169 0.42987 -0.06966 0.10639  0.01107  239 ILE A C     
1628 O  O     . ILE A 209 ? 0.36965 0.21494 0.44861 -0.06442 0.10492  0.01082  239 ILE A O     
1629 C  CB    . ILE A 209 ? 0.34083 0.18757 0.43214 -0.05905 0.10056  0.00729  239 ILE A CB    
1630 C  CG1   . ILE A 209 ? 0.32697 0.19677 0.43026 -0.05892 0.10897  0.00428  239 ILE A CG1   
1631 C  CG2   . ILE A 209 ? 0.33187 0.17452 0.42664 -0.04676 0.10070  0.00467  239 ILE A CG2   
1632 C  CD1   . ILE A 209 ? 0.31378 0.18816 0.42802 -0.04825 0.11021  -0.00019 239 ILE A CD1   
1633 N  N     . LYS A 210 ? 0.34221 0.21636 0.42938 -0.07436 0.11352  0.01056  240 LYS A N     
1634 C  CA    . LYS A 210 ? 0.33827 0.22320 0.42540 -0.07375 0.11950  0.00980  240 LYS A CA    
1635 C  C     . LYS A 210 ? 0.32330 0.21310 0.41905 -0.06113 0.12352  0.00466  240 LYS A C     
1636 O  O     . LYS A 210 ? 0.32136 0.21630 0.41569 -0.05921 0.12719  0.00366  240 LYS A O     
1637 C  CB    . LYS A 210 ? 0.35726 0.26389 0.44604 -0.08147 0.12545  0.01060  240 LYS A CB    
1638 C  CG    . LYS A 210 ? 0.32591 0.24963 0.42627 -0.07659 0.13002  0.00639  240 LYS A CG    
1639 C  CD    . LYS A 210 ? 0.35513 0.30281 0.45652 -0.08447 0.13539  0.00749  240 LYS A CD    
1640 C  CE    . LYS A 210 ? 0.37709 0.34271 0.48972 -0.07777 0.14020  0.00244  240 LYS A CE    
1641 N  NZ    . LYS A 210 ? 0.45749 0.44570 0.57191 -0.08710 0.14315  0.00435  240 LYS A NZ    
1642 N  N     . LEU A 211 ? 0.31385 0.20222 0.41772 -0.05293 0.12268  0.00157  241 LEU A N     
1643 C  CA    . LEU A 211 ? 0.30143 0.19205 0.41237 -0.04176 0.12532  -0.00247 241 LEU A CA    
1644 C  C     . LEU A 211 ? 0.32790 0.20219 0.43472 -0.03796 0.11962  -0.00090 241 LEU A C     
1645 O  O     . LEU A 211 ? 0.39626 0.26045 0.50217 -0.03622 0.11421  0.00008  241 LEU A O     
1646 C  CB    . LEU A 211 ? 0.33934 0.23800 0.46064 -0.03515 0.12748  -0.00620 241 LEU A CB    
1647 C  CG    . LEU A 211 ? 0.36887 0.28481 0.49425 -0.03844 0.13255  -0.00796 241 LEU A CG    
1648 C  CD1   . LEU A 211 ? 0.30002 0.22133 0.43498 -0.03138 0.13372  -0.01164 241 LEU A CD1   
1649 C  CD2   . LEU A 211 ? 0.29864 0.22769 0.42296 -0.03754 0.13858  -0.01004 241 LEU A CD2   
1650 N  N     . GLU A 212 ? 0.38068 0.25311 0.48484 -0.03593 0.12051  -0.00093 242 GLU A N     
1651 C  CA    . GLU A 212 ? 0.32721 0.18570 0.42603 -0.03379 0.11483  0.00112  242 GLU A CA    
1652 C  C     . GLU A 212 ? 0.30157 0.15812 0.40741 -0.02433 0.11239  -0.00049 242 GLU A C     
1653 O  O     . GLU A 212 ? 0.31329 0.15930 0.41519 -0.02171 0.10638  0.00109  242 GLU A O     
1654 C  CB    . GLU A 212 ? 0.34088 0.19873 0.43475 -0.03491 0.11630  0.00168  242 GLU A CB    
1655 C  CG    . GLU A 212 ? 0.34140 0.20828 0.44137 -0.02931 0.12089  -0.00158 242 GLU A CG    
1656 C  CD    . GLU A 212 ? 0.55677 0.42026 0.66179 -0.02186 0.11820  -0.00220 242 GLU A CD    
1657 O  OE1   . GLU A 212 ? 0.47597 0.33060 0.57758 -0.02096 0.11306  0.00005  242 GLU A OE1   
1658 O  OE2   . GLU A 212 ? 0.47862 0.34889 0.59047 -0.01693 0.12098  -0.00480 242 GLU A OE2   
1659 N  N     . ASP A 213 ? 0.31417 0.18087 0.42943 -0.01880 0.11656  -0.00356 243 ASP A N     
1660 C  CA    . ASP A 213 ? 0.28103 0.14830 0.40350 -0.01010 0.11474  -0.00466 243 ASP A CA    
1661 C  C     . ASP A 213 ? 0.31456 0.17846 0.43879 -0.00754 0.11129  -0.00473 243 ASP A C     
1662 O  O     . ASP A 213 ? 0.28958 0.14913 0.41445 -0.00128 0.10686  -0.00414 243 ASP A O     
1663 C  CB    . ASP A 213 ? 0.36241 0.23955 0.49251 -0.00578 0.11961  -0.00747 243 ASP A CB    
1664 C  CG    . ASP A 213 ? 0.38160 0.26814 0.51535 -0.00668 0.12499  -0.01052 243 ASP A CG    
1665 O  OD1   . ASP A 213 ? 0.40294 0.29105 0.53392 -0.01216 0.12578  -0.01014 243 ASP A OD1   
1666 O  OD2   . ASP A 213 ? 0.50927 0.40175 0.64795 -0.00205 0.12805  -0.01312 243 ASP A OD2   
1667 N  N     . VAL A 214 ? 0.28383 0.15025 0.40819 -0.01211 0.11287  -0.00536 244 VAL A N     
1668 C  CA    . VAL A 214 ? 0.29634 0.15704 0.42041 -0.01068 0.10844  -0.00523 244 VAL A CA    
1669 C  C     . VAL A 214 ? 0.30301 0.14741 0.41498 -0.01376 0.10080  -0.00196 244 VAL A C     
1670 O  O     . VAL A 214 ? 0.31145 0.14731 0.42116 -0.00793 0.09489  -0.00194 244 VAL A O     
1671 C  CB    . VAL A 214 ? 0.28653 0.15471 0.41368 -0.01576 0.11155  -0.00644 244 VAL A CB    
1672 C  CG1   . VAL A 214 ? 0.29278 0.15262 0.41793 -0.01517 0.10580  -0.00600 244 VAL A CG1   
1673 C  CG2   . VAL A 214 ? 0.27254 0.15582 0.41017 -0.01118 0.11854  -0.01024 244 VAL A CG2   
1674 N  N     . PHE A 215 ? 0.31242 0.15238 0.41594 -0.02201 0.10068  0.00052  245 PHE A N     
1675 C  CA    . PHE A 215 ? 0.32926 0.15178 0.41958 -0.02508 0.09282  0.00357  245 PHE A CA    
1676 C  C     . PHE A 215 ? 0.38830 0.20400 0.47664 -0.01537 0.08802  0.00333  245 PHE A C     
1677 O  O     . PHE A 215 ? 0.33997 0.14272 0.42070 -0.01102 0.08035  0.00388  245 PHE A O     
1678 C  CB    . PHE A 215 ? 0.33963 0.15892 0.42082 -0.03567 0.09368  0.00655  245 PHE A CB    
1679 C  CG    . PHE A 215 ? 0.35906 0.15831 0.42482 -0.03917 0.08506  0.00981  245 PHE A CG    
1680 C  CD1   . PHE A 215 ? 0.39290 0.18009 0.45039 -0.04419 0.07891  0.01165  245 PHE A CD1   
1681 C  CD2   . PHE A 215 ? 0.39565 0.18700 0.45440 -0.03690 0.08232  0.01086  245 PHE A CD2   
1682 C  CE1   . PHE A 215 ? 0.39376 0.15919 0.43452 -0.04689 0.06965  0.01453  245 PHE A CE1   
1683 C  CE2   . PHE A 215 ? 0.52830 0.29979 0.57133 -0.03907 0.07379  0.01348  245 PHE A CE2   
1684 C  CZ    . PHE A 215 ? 0.39936 0.15691 0.43267 -0.04396 0.06721  0.01530  245 PHE A CZ    
1685 N  N     . VAL A 216 ? 0.37165 0.19635 0.46606 -0.01159 0.09198  0.00249  246 VAL A N     
1686 C  CA    . VAL A 216 ? 0.31840 0.14113 0.41259 -0.00260 0.08794  0.00251  246 VAL A CA    
1687 C  C     . VAL A 216 ? 0.32608 0.15178 0.42627 0.00723  0.08552  0.00077  246 VAL A C     
1688 O  O     . VAL A 216 ? 0.35150 0.17068 0.44647 0.01480  0.07902  0.00105  246 VAL A O     
1689 C  CB    . VAL A 216 ? 0.36688 0.20013 0.46733 -0.00178 0.09266  0.00228  246 VAL A CB    
1690 C  CG1   . VAL A 216 ? 0.35534 0.19168 0.45830 0.00746  0.08904  0.00254  246 VAL A CG1   
1691 C  CG2   . VAL A 216 ? 0.37121 0.19934 0.46347 -0.00989 0.09355  0.00402  246 VAL A CG2   
1692 N  N     . GLY A 217 ? 0.38268 0.21862 0.49317 0.00817  0.09050  -0.00126 247 GLY A N     
1693 C  CA    . GLY A 217 ? 0.29649 0.13498 0.41222 0.01738  0.08827  -0.00293 247 GLY A CA    
1694 C  C     . GLY A 217 ? 0.33440 0.15754 0.43971 0.01880  0.08034  -0.00259 247 GLY A C     
1695 O  O     . GLY A 217 ? 0.37756 0.19735 0.48079 0.02895  0.07478  -0.00328 247 GLY A O     
1696 N  N     . LEU A 218 ? 0.32203 0.13576 0.41982 0.00878  0.07919  -0.00140 248 LEU A N     
1697 C  CA    . LEU A 218 ? 0.41753 0.21274 0.50224 0.00867  0.07003  -0.00048 248 LEU A CA    
1698 C  C     . LEU A 218 ? 0.38979 0.17160 0.46195 0.01456  0.06206  0.00065  248 LEU A C     
1699 O  O     . LEU A 218 ? 0.39671 0.16679 0.46053 0.02289  0.05384  -0.00013 248 LEU A O     
1700 C  CB    . LEU A 218 ? 0.36320 0.15110 0.44082 -0.00537 0.06983  0.00175  248 LEU A CB    
1701 C  CG    . LEU A 218 ? 0.36561 0.16542 0.45299 -0.01104 0.07572  0.00061  248 LEU A CG    
1702 C  CD1   . LEU A 218 ? 0.35319 0.15008 0.43362 -0.02621 0.07620  0.00373  248 LEU A CD1   
1703 C  CD2   . LEU A 218 ? 0.36769 0.16222 0.45582 -0.00427 0.07075  -0.00131 248 LEU A CD2   
1704 N  N     . CYS A 219 ? 0.37533 0.15837 0.44502 0.01099  0.06395  0.00222  249 CYS A N     
1705 C  CA    . CYS A 219 ? 0.36699 0.13835 0.42458 0.01693  0.05646  0.00304  249 CYS A CA    
1706 C  C     . CYS A 219 ? 0.37935 0.16036 0.44291 0.03193  0.05469  0.00107  249 CYS A C     
1707 O  O     . CYS A 219 ? 0.46572 0.23594 0.51844 0.04131  0.04607  0.00046  249 CYS A O     
1708 C  CB    . CYS A 219 ? 0.42982 0.20194 0.48445 0.01003  0.05929  0.00502  249 CYS A CB    
1709 S  SG    . CYS A 219 ? 0.40235 0.16318 0.44689 -0.00664 0.06005  0.00806  249 CYS A SG    
1710 N  N     . LEU A 220 ? 0.41015 0.21164 0.48970 0.03445  0.06236  0.00025  250 LEU A N     
1711 C  CA    . LEU A 220 ? 0.37424 0.18839 0.46064 0.04745  0.06133  -0.00084 250 LEU A CA    
1712 C  C     . LEU A 220 ? 0.39380 0.20362 0.47818 0.05695  0.05629  -0.00280 250 LEU A C     
1713 O  O     . LEU A 220 ? 0.38238 0.19332 0.46275 0.06950  0.05047  -0.00361 250 LEU A O     
1714 C  CB    . LEU A 220 ? 0.38125 0.21624 0.48438 0.04632  0.07020  -0.00090 250 LEU A CB    
1715 C  CG    . LEU A 220 ? 0.36702 0.20749 0.47260 0.03854  0.07483  0.00077  250 LEU A CG    
1716 C  CD1   . LEU A 220 ? 0.28748 0.14480 0.40773 0.03742  0.08254  0.00033  250 LEU A CD1   
1717 C  CD2   . LEU A 220 ? 0.35255 0.19486 0.45325 0.04390  0.07031  0.00217  250 LEU A CD2   
1718 N  N     . GLU A 221 ? 0.36387 0.17006 0.45100 0.05180  0.05838  -0.00373 251 GLU A N     
1719 C  CA    . GLU A 221 ? 0.38951 0.18939 0.47363 0.06021  0.05299  -0.00569 251 GLU A CA    
1720 C  C     . GLU A 221 ? 0.44542 0.22232 0.50960 0.06462  0.04124  -0.00564 251 GLU A C     
1721 O  O     . GLU A 221 ? 0.50345 0.27702 0.56224 0.07808  0.03449  -0.00744 251 GLU A O     
1722 C  CB    . GLU A 221 ? 0.37343 0.17308 0.46339 0.05182  0.05725  -0.00645 251 GLU A CB    
1723 C  CG    . GLU A 221 ? 0.49929 0.28815 0.58381 0.05780  0.05072  -0.00827 251 GLU A CG    
1724 C  CD    . GLU A 221 ? 0.50105 0.29321 0.59306 0.04853  0.05587  -0.00887 251 GLU A CD    
1725 O  OE1   . GLU A 221 ? 0.45799 0.23909 0.54238 0.03620  0.05440  -0.00710 251 GLU A OE1   
1726 O  OE2   . GLU A 221 ? 0.42970 0.23852 0.53424 0.05269  0.06108  -0.01079 251 GLU A OE2   
1727 N  N     . ARG A 222 ? 0.49771 0.25810 0.54955 0.05396  0.03819  -0.00361 252 ARG A N     
1728 C  CA    . ARG A 222 ? 0.40376 0.13921 0.43406 0.05781  0.02600  -0.00342 252 ARG A CA    
1729 C  C     . ARG A 222 ? 0.56234 0.30071 0.58723 0.07199  0.02117  -0.00442 252 ARG A C     
1730 O  O     . ARG A 222 ? 0.66560 0.38905 0.67532 0.08330  0.01063  -0.00601 252 ARG A O     
1731 C  CB    . ARG A 222 ? 0.48718 0.20558 0.50530 0.04251  0.02414  -0.00038 252 ARG A CB    
1732 C  CG    . ARG A 222 ? 0.51709 0.20660 0.51001 0.04486  0.01095  0.00037  252 ARG A CG    
1733 C  CD    . ARG A 222 ? 0.50795 0.17469 0.48680 0.04379  0.00129  0.00015  252 ARG A CD    
1734 N  NE    . ARG A 222 ? 0.73897 0.41087 0.72722 0.03017  0.00709  0.00158  252 ARG A NE    
1735 C  CZ    . ARG A 222 ? 0.70284 0.36387 0.68372 0.01314  0.00650  0.00521  252 ARG A CZ    
1736 N  NH1   . ARG A 222 ? 0.54456 0.18674 0.50785 0.00658  0.00034  0.00805  252 ARG A NH1   
1737 N  NH2   . ARG A 222 ? 0.54982 0.22020 0.54102 0.00240  0.01220  0.00615  252 ARG A NH2   
1738 N  N     . LEU A 223 ? 0.52387 0.28208 0.56068 0.07207  0.02837  -0.00364 253 LEU A N     
1739 C  CA    . LEU A 223 ? 0.47096 0.23744 0.50534 0.08367  0.02528  -0.00402 253 LEU A CA    
1740 C  C     . LEU A 223 ? 0.46457 0.25112 0.50941 0.09851  0.02608  -0.00582 253 LEU A C     
1741 O  O     . LEU A 223 ? 0.50419 0.30054 0.54696 0.10982  0.02283  -0.00616 253 LEU A O     
1742 C  CB    . LEU A 223 ? 0.48130 0.25998 0.52386 0.07484  0.03258  -0.00183 253 LEU A CB    
1743 C  CG    . LEU A 223 ? 0.51810 0.27834 0.54781 0.06314  0.03054  0.00008  253 LEU A CG    
1744 C  CD1   . LEU A 223 ? 0.40932 0.18298 0.44886 0.05418  0.03876  0.00198  253 LEU A CD1   
1745 C  CD2   . LEU A 223 ? 0.46307 0.20452 0.47206 0.07168  0.01904  -0.00054 253 LEU A CD2   
1746 N  N     . ASN A 224 ? 0.42112 0.21509 0.47683 0.09882  0.03026  -0.00685 254 ASN A N     
1747 C  CA    . ASN A 224 ? 0.52811 0.34270 0.59525 0.11147  0.03225  -0.00812 254 ASN A CA    
1748 C  C     . ASN A 224 ? 0.65087 0.49227 0.73328 0.11122  0.03985  -0.00614 254 ASN A C     
1749 O  O     . ASN A 224 ? 0.65310 0.51335 0.74149 0.12310  0.03951  -0.00624 254 ASN A O     
1750 C  CB    . ASN A 224 ? 0.59378 0.40113 0.64702 0.12918  0.02143  -0.01045 254 ASN A CB    
1751 C  CG    . ASN A 224 ? 0.65646 0.44066 0.69658 0.12766  0.01262  -0.01262 254 ASN A CG    
1752 O  OD1   . ASN A 224 ? 0.83326 0.59463 0.85484 0.12707  0.00415  -0.01257 254 ASN A OD1   
1753 N  ND2   . ASN A 224 ? 0.74367 0.53531 0.79281 0.12511  0.01403  -0.01428 254 ASN A ND2   
1754 N  N     . ILE A 225 ? 0.55519 0.39887 0.64360 0.09744  0.04647  -0.00412 255 ILE A N     
1755 C  CA    . ILE A 225 ? 0.34822 0.21423 0.45061 0.09422  0.05365  -0.00196 255 ILE A CA    
1756 C  C     . ILE A 225 ? 0.40012 0.27795 0.51768 0.08996  0.06176  -0.00209 255 ILE A C     
1757 O  O     . ILE A 225 ? 0.48696 0.35528 0.60568 0.08087  0.06532  -0.00295 255 ILE A O     
1758 C  CB    . ILE A 225 ? 0.41601 0.27624 0.51530 0.08240  0.05583  -0.00011 255 ILE A CB    
1759 C  CG1   . ILE A 225 ? 0.40020 0.24955 0.48403 0.08802  0.04741  -0.00009 255 ILE A CG1   
1760 C  CG2   . ILE A 225 ? 0.44732 0.32756 0.56059 0.07684  0.06321  0.00213  255 ILE A CG2   
1761 C  CD1   . ILE A 225 ? 0.48649 0.32506 0.56356 0.07698  0.04801  0.00141  255 ILE A CD1   
1762 N  N     . ARG A 226 ? 0.44003 0.33932 0.56869 0.09670  0.06444  -0.00115 256 ARG A N     
1763 C  CA    . ARG A 226 ? 0.52034 0.43039 0.66208 0.09440  0.07125  -0.00136 256 ARG A CA    
1764 C  C     . ARG A 226 ? 0.44655 0.36691 0.59761 0.08374  0.07823  0.00102  256 ARG A C     
1765 O  O     . ARG A 226 ? 0.45129 0.38123 0.60318 0.08272  0.07768  0.00361  256 ARG A O     
1766 C  CB    . ARG A 226 ? 0.59664 0.52554 0.73975 0.10500  0.06759  -0.00160 256 ARG A CB    
1767 C  CG    . ARG A 226 ? 0.75200 0.67259 0.88100 0.11602  0.05753  -0.00463 256 ARG A CG    
1768 C  CD    . ARG A 226 ? 0.92641 0.84531 1.05136 0.11555  0.05456  -0.00772 256 ARG A CD    
1769 N  NE    . ARG A 226 ? 1.22642 1.14074 1.33925 0.12755  0.04394  -0.01116 256 ARG A NE    
1770 C  CZ    . ARG A 226 ? 1.19416 1.11503 1.30484 0.13191  0.03929  -0.01433 256 ARG A CZ    
1771 N  NH1   . ARG A 226 ? 0.98244 0.91425 1.10010 0.12573  0.04452  -0.01391 256 ARG A NH1   
1772 N  NH2   . ARG A 226 ? 1.17694 1.09306 1.28053 0.14189  0.02854  -0.01853 256 ARG A NH2   
1773 N  N     . LEU A 227 ? 0.52962 0.44729 0.68656 0.07607  0.08418  -0.00005 257 LEU A N     
1774 C  CA    . LEU A 227 ? 0.58198 0.50757 0.74612 0.06728  0.09002  0.00171  257 LEU A CA    
1775 C  C     . LEU A 227 ? 0.47313 0.41870 0.64692 0.07184  0.09161  0.00415  257 LEU A C     
1776 O  O     . LEU A 227 ? 0.50511 0.45912 0.68046 0.07880  0.08989  0.00352  257 LEU A O     
1777 C  CB    . LEU A 227 ? 0.33241 0.25119 0.49953 0.06005  0.09563  -0.00062 257 LEU A CB    
1778 C  CG    . LEU A 227 ? 0.36121 0.26320 0.52024 0.05514  0.09470  -0.00284 257 LEU A CG    
1779 C  CD1   . LEU A 227 ? 0.41350 0.31496 0.57630 0.04831  0.10053  -0.00490 257 LEU A CD1   
1780 C  CD2   . LEU A 227 ? 0.44272 0.33632 0.59303 0.04941  0.09222  -0.00131 257 LEU A CD2   
1781 N  N     . GLU A 228 ? 0.39063 0.34443 0.56740 0.06559  0.09321  0.00725  258 GLU A N     
1782 C  CA    . GLU A 228 ? 0.41684 0.39006 0.60271 0.06722  0.09484  0.01054  258 GLU A CA    
1783 C  C     . GLU A 228 ? 0.37538 0.34838 0.56420 0.05618  0.09879  0.01230  258 GLU A C     
1784 O  O     . GLU A 228 ? 0.35376 0.31619 0.53718 0.04867  0.09885  0.01201  258 GLU A O     
1785 C  CB    . GLU A 228 ? 0.40052 0.39070 0.58706 0.07314  0.09053  0.01408  258 GLU A CB    
1786 C  CG    . GLU A 228 ? 0.61245 0.59650 0.79066 0.07188  0.08629  0.01446  258 GLU A CG    
1787 C  CD    . GLU A 228 ? 0.87877 0.88081 1.05690 0.08179  0.08143  0.01674  258 GLU A CD    
1788 O  OE1   . GLU A 228 ? 0.84080 0.86319 1.02588 0.07987  0.08202  0.02108  258 GLU A OE1   
1789 O  OE2   . GLU A 228 ? 0.79650 0.79261 0.96690 0.09150  0.07663  0.01428  258 GLU A OE2   
1790 N  N     . GLU A 229 ? 0.35524 0.33815 0.55110 0.05575  0.10153  0.01388  259 GLU A N     
1791 C  CA    . GLU A 229 ? 0.40932 0.39141 0.60620 0.04604  0.10382  0.01598  259 GLU A CA    
1792 C  C     . GLU A 229 ? 0.32089 0.31261 0.51727 0.04080  0.10065  0.02104  259 GLU A C     
1793 O  O     . GLU A 229 ? 0.31381 0.32221 0.51344 0.04584  0.09781  0.02423  259 GLU A O     
1794 C  CB    . GLU A 229 ? 0.35237 0.34244 0.55564 0.04750  0.10653  0.01688  259 GLU A CB    
1795 C  CG    . GLU A 229 ? 0.42999 0.41222 0.63444 0.05318  0.10957  0.01183  259 GLU A CG    
1796 C  CD    . GLU A 229 ? 0.51409 0.48047 0.71445 0.04705  0.11291  0.00807  259 GLU A CD    
1797 O  OE1   . GLU A 229 ? 0.47390 0.43433 0.66985 0.03896  0.11270  0.00930  259 GLU A OE1   
1798 O  OE2   . GLU A 229 ? 0.64491 0.60619 0.83941 0.04769  0.11185  0.00443  259 GLU A OE2   
1799 N  N     . LEU A 230 ? 0.40958 0.39135 0.60133 0.03105  0.10082  0.02165  260 LEU A N     
1800 C  CA    . LEU A 230 ? 0.37218 0.36141 0.56266 0.02520  0.09728  0.02630  260 LEU A CA    
1801 C  C     . LEU A 230 ? 0.34844 0.35583 0.54519 0.02241  0.09628  0.03208  260 LEU A C     
1802 O  O     . LEU A 230 ? 0.32868 0.35291 0.52807 0.02196  0.09304  0.03672  260 LEU A O     
1803 C  CB    . LEU A 230 ? 0.31230 0.28470 0.49508 0.01587  0.09720  0.02525  260 LEU A CB    
1804 C  CG    . LEU A 230 ? 0.36641 0.34332 0.54670 0.00846  0.09320  0.02977  260 LEU A CG    
1805 C  CD1   . LEU A 230 ? 0.26214 0.24819 0.44227 0.01327  0.08995  0.03079  260 LEU A CD1   
1806 C  CD2   . LEU A 230 ? 0.25139 0.20945 0.42294 0.00024  0.09308  0.02807  260 LEU A CD2   
1807 N  N     . HIS A 231 ? 0.32056 0.32567 0.51945 0.02061  0.09890  0.03199  261 HIS A N     
1808 C  CA    . HIS A 231 ? 0.37748 0.39561 0.58011 0.01493  0.09773  0.03796  261 HIS A CA    
1809 C  C     . HIS A 231 ? 0.46531 0.48558 0.67225 0.01972  0.10105  0.03671  261 HIS A C     
1810 O  O     . HIS A 231 ? 0.47630 0.48495 0.68240 0.02572  0.10422  0.03084  261 HIS A O     
1811 C  CB    . HIS A 231 ? 0.46492 0.47006 0.66035 0.00251  0.09557  0.04003  261 HIS A CB    
1812 C  CG    . HIS A 231 ? 0.52034 0.53696 0.71757 -0.00586 0.09291  0.04721  261 HIS A CG    
1813 N  ND1   . HIS A 231 ? 0.56424 0.57166 0.75841 -0.01038 0.09351  0.04778  261 HIS A ND1   
1814 C  CD2   . HIS A 231 ? 0.36964 0.40626 0.57061 -0.01116 0.08920  0.05443  261 HIS A CD2   
1815 C  CE1   . HIS A 231 ? 0.56488 0.58487 0.76037 -0.01887 0.09006  0.05543  261 HIS A CE1   
1816 N  NE2   . HIS A 231 ? 0.51541 0.55451 0.71563 -0.01986 0.08757  0.05977  261 HIS A NE2   
1817 N  N     . SER A 232 ? 0.41172 0.44789 0.62325 0.01662  0.10013  0.04262  262 SER A N     
1818 C  CA    . SER A 232 ? 0.48395 0.52266 0.69912 0.02058  0.10303  0.04210  262 SER A CA    
1819 C  C     . SER A 232 ? 0.49360 0.50929 0.70183 0.01593  0.10477  0.03833  262 SER A C     
1820 O  O     . SER A 232 ? 0.53950 0.55214 0.74944 0.02114  0.10780  0.03547  262 SER A O     
1821 C  CB    . SER A 232 ? 0.48307 0.54469 0.70371 0.01673  0.10129  0.05025  262 SER A CB    
1822 O  OG    . SER A 232 ? 0.63186 0.69509 0.84881 0.00399  0.09719  0.05618  262 SER A OG    
1823 N  N     . GLN A 233 ? 0.60925 0.60895 0.80899 0.00707  0.10261  0.03806  263 GLN A N     
1824 C  CA    . GLN A 233 ? 0.54953 0.52639 0.74029 0.00376  0.10346  0.03383  263 GLN A CA    
1825 C  C     . GLN A 233 ? 0.45231 0.41370 0.63792 0.00622  0.10500  0.02727  263 GLN A C     
1826 O  O     . GLN A 233 ? 0.58228 0.54705 0.76845 0.00593  0.10369  0.02777  263 GLN A O     
1827 C  CB    . GLN A 233 ? 0.61130 0.58017 0.79373 -0.00837 0.09869  0.03880  263 GLN A CB    
1828 C  CG    . GLN A 233 ? 0.69279 0.67759 0.87925 -0.01362 0.09639  0.04676  263 GLN A CG    
1829 C  CD    . GLN A 233 ? 0.72213 0.70621 0.91036 -0.00846 0.09943  0.04514  263 GLN A CD    
1830 O  OE1   . GLN A 233 ? 0.65815 0.62219 0.83858 -0.00704 0.10056  0.03984  263 GLN A OE1   
1831 N  NE2   . GLN A 233 ? 0.74196 0.74867 0.94010 -0.00463 0.10077  0.04937  263 GLN A NE2   
1832 N  N     . PRO A 234 ? 0.43893 0.38458 0.61930 0.00889  0.10774  0.02118  264 PRO A N     
1833 C  CA    . PRO A 234 ? 0.43977 0.37250 0.61465 0.01013  0.10922  0.01557  264 PRO A CA    
1834 C  C     . PRO A 234 ? 0.45195 0.37528 0.61813 0.00188  0.10529  0.01750  264 PRO A C     
1835 O  O     . PRO A 234 ? 0.39178 0.30887 0.55157 -0.00501 0.10162  0.02069  264 PRO A O     
1836 C  CB    . PRO A 234 ? 0.35959 0.28020 0.52994 0.01387  0.11237  0.00960  264 PRO A CB    
1837 C  CG    . PRO A 234 ? 0.45524 0.37580 0.62417 0.01153  0.11073  0.01271  264 PRO A CG    
1838 C  CD    . PRO A 234 ? 0.36348 0.30360 0.54228 0.01113  0.10953  0.01921  264 PRO A CD    
1839 N  N     . THR A 235 ? 0.31375 0.23469 0.47860 0.00243  0.10560  0.01557  265 THR A N     
1840 C  CA    . THR A 235 ? 0.27696 0.18916 0.43368 -0.00438 0.10205  0.01691  265 THR A CA    
1841 C  C     . THR A 235 ? 0.25546 0.15547 0.40550 -0.00278 0.10409  0.01142  265 THR A C     
1842 O  O     . THR A 235 ? 0.28304 0.17335 0.42456 -0.00776 0.10129  0.01169  265 THR A O     
1843 C  CB    . THR A 235 ? 0.37566 0.30125 0.53737 -0.00709 0.09890  0.02232  265 THR A CB    
1844 O  OG1   . THR A 235 ? 0.24400 0.17868 0.41245 0.00020  0.10126  0.02063  265 THR A OG1   
1845 C  CG2   . THR A 235 ? 0.30648 0.24589 0.47343 -0.01077 0.09619  0.02885  265 THR A CG2   
1846 N  N     . PHE A 236 ? 0.33017 0.23095 0.48347 0.00361  0.10860  0.00678  266 PHE A N     
1847 C  CA    . PHE A 236 ? 0.25205 0.14400 0.39954 0.00478  0.11107  0.00191  266 PHE A CA    
1848 C  C     . PHE A 236 ? 0.25251 0.13915 0.39736 0.00882  0.11460  -0.00330 266 PHE A C     
1849 O  O     . PHE A 236 ? 0.24486 0.13785 0.39654 0.01341  0.11698  -0.00433 266 PHE A O     
1850 C  CB    . PHE A 236 ? 0.24542 0.14355 0.39822 0.00795  0.11276  0.00131  266 PHE A CB    
1851 C  CG    . PHE A 236 ? 0.24619 0.14889 0.40002 0.00557  0.10917  0.00548  266 PHE A CG    
1852 C  CD1   . PHE A 236 ? 0.24079 0.15595 0.40191 0.00721  0.10691  0.00968  266 PHE A CD1   
1853 C  CD2   . PHE A 236 ? 0.25264 0.14846 0.39984 0.00235  0.10804  0.00511  266 PHE A CD2   
1854 C  CE1   . PHE A 236 ? 0.24194 0.16287 0.40355 0.00622  0.10347  0.01305  266 PHE A CE1   
1855 C  CE2   . PHE A 236 ? 0.25402 0.15377 0.40146 0.00087  0.10450  0.00856  266 PHE A CE2   
1856 C  CZ    . PHE A 236 ? 0.24876 0.16132 0.40335 0.00299  0.10210  0.01242  266 PHE A CZ    
1857 N  N     . PHE A 237 ? 0.26167 0.13760 0.39639 0.00806  0.11491  -0.00690 267 PHE A N     
1858 C  CA    . PHE A 237 ? 0.26461 0.13547 0.39465 0.01256  0.11740  -0.01207 267 PHE A CA    
1859 C  C     . PHE A 237 ? 0.26744 0.13642 0.39227 0.01474  0.12068  -0.01700 267 PHE A C     
1860 O  O     . PHE A 237 ? 0.27853 0.13841 0.39206 0.01443  0.11939  -0.01937 267 PHE A O     
1861 C  CB    . PHE A 237 ? 0.27656 0.13585 0.39671 0.01039  0.11306  -0.01133 267 PHE A CB    
1862 C  CG    . PHE A 237 ? 0.27371 0.13735 0.39949 0.00749  0.11026  -0.00598 267 PHE A CG    
1863 C  CD1   . PHE A 237 ? 0.34443 0.21231 0.47525 0.01167  0.11223  -0.00684 267 PHE A CD1   
1864 C  CD2   . PHE A 237 ? 0.35859 0.22425 0.48524 0.00059  0.10579  0.00019  267 PHE A CD2   
1865 C  CE1   . PHE A 237 ? 0.26543 0.13955 0.40170 0.00884  0.10990  -0.00136 267 PHE A CE1   
1866 C  CE2   . PHE A 237 ? 0.28569 0.15888 0.41803 -0.00257 0.10335  0.00578  267 PHE A CE2   
1867 C  CZ    . PHE A 237 ? 0.26807 0.14574 0.40524 0.00155  0.10554  0.00512  267 PHE A CZ    
1868 N  N     . PRO A 238 ? 0.26738 0.14534 0.39966 0.01708  0.12470  -0.01856 268 PRO A N     
1869 C  CA    . PRO A 238 ? 0.28812 0.16784 0.41663 0.01808  0.12819  -0.02248 268 PRO A CA    
1870 C  C     . PRO A 238 ? 0.26588 0.14344 0.38754 0.02325  0.13025  -0.02804 268 PRO A C     
1871 O  O     . PRO A 238 ? 0.36190 0.24018 0.47673 0.02437  0.13220  -0.03136 268 PRO A O     
1872 C  CB    . PRO A 238 ? 0.25051 0.13952 0.38897 0.01856  0.13065  -0.02182 268 PRO A CB    
1873 C  CG    . PRO A 238 ? 0.27123 0.16196 0.41674 0.01767  0.12758  -0.01712 268 PRO A CG    
1874 C  CD    . PRO A 238 ? 0.28225 0.16964 0.42633 0.01876  0.12571  -0.01646 268 PRO A CD    
1875 N  N     . GLY A 239 ? 0.26513 0.14041 0.38762 0.02681  0.12955  -0.02905 269 GLY A N     
1876 C  CA    . GLY A 239 ? 0.27083 0.14625 0.38386 0.03175  0.12852  -0.03359 269 GLY A CA    
1877 C  C     . GLY A 239 ? 0.28917 0.14788 0.38876 0.03321  0.12579  -0.03561 269 GLY A C     
1878 O  O     . GLY A 239 ? 0.29479 0.15156 0.38362 0.03857  0.12425  -0.04008 269 GLY A O     
1879 N  N     . GLY A 240 ? 0.31242 0.16226 0.40928 0.02738  0.12181  -0.03119 270 GLY A N     
1880 C  CA    . GLY A 240 ? 0.35895 0.19255 0.44049 0.02682  0.11618  -0.03169 270 GLY A CA    
1881 C  C     . GLY A 240 ? 0.37669 0.20136 0.45573 0.02593  0.11193  -0.02955 270 GLY A C     
1882 O  O     . GLY A 240 ? 0.36299 0.19523 0.45219 0.02705  0.11410  -0.02837 270 GLY A O     
1883 N  N     . LEU A 241 ? 0.33565 0.14334 0.40012 0.02350  0.10529  -0.02872 271 LEU A N     
1884 C  CA    . LEU A 241 ? 0.33946 0.13631 0.39909 0.02016  0.09975  -0.02535 271 LEU A CA    
1885 C  C     . LEU A 241 ? 0.39695 0.17138 0.43471 0.02233  0.09294  -0.02853 271 LEU A C     
1886 O  O     . LEU A 241 ? 0.42303 0.18933 0.45000 0.02280  0.09047  -0.03050 271 LEU A O     
1887 C  CB    . LEU A 241 ? 0.36071 0.16007 0.42689 0.00965  0.09591  -0.01692 271 LEU A CB    
1888 C  CG    . LEU A 241 ? 0.43142 0.25056 0.51705 0.00702  0.10010  -0.01231 271 LEU A CG    
1889 C  CD1   . LEU A 241 ? 0.37470 0.19563 0.46284 -0.00268 0.09524  -0.00470 271 LEU A CD1   
1890 C  CD2   . LEU A 241 ? 0.36901 0.19364 0.46134 0.01021  0.10211  -0.01212 271 LEU A CD2   
1891 N  N     . ARG A 242 ? 0.37273 0.13579 0.40328 0.02241  0.08875  -0.02790 272 ARG A N     
1892 C  CA    . ARG A 242 ? 0.39926 0.13657 0.40654 0.02276  0.07983  -0.02954 272 ARG A CA    
1893 C  C     . ARG A 242 ? 0.40682 0.13688 0.41178 0.01040  0.07298  -0.02174 272 ARG A C     
1894 O  O     . ARG A 242 ? 0.39638 0.13679 0.41422 0.00209  0.07315  -0.01459 272 ARG A O     
1895 C  CB    . ARG A 242 ? 0.40902 0.13474 0.40790 0.02600  0.07676  -0.03088 272 ARG A CB    
1896 C  CG    . ARG A 242 ? 0.43857 0.13484 0.41287 0.02381  0.06563  -0.03052 272 ARG A CG    
1897 C  CD    . ARG A 242 ? 0.44373 0.13271 0.41482 0.02372  0.06330  -0.02916 272 ARG A CD    
1898 N  NE    . ARG A 242 ? 0.71744 0.37845 0.66159 0.02874  0.05387  -0.03349 272 ARG A NE    
1899 C  CZ    . ARG A 242 ? 0.64256 0.30041 0.58002 0.03475  0.05089  -0.03655 272 ARG A CZ    
1900 N  NH1   . ARG A 242 ? 0.72695 0.40066 0.68040 0.03476  0.05709  -0.03465 272 ARG A NH1   
1901 N  NH2   . ARG A 242 ? 0.53952 0.17930 0.45475 0.04096  0.04147  -0.04154 272 ARG A NH2   
1902 N  N     . PHE A 243 ? 0.42418 0.13871 0.41348 0.00980  0.06727  -0.02322 273 PHE A N     
1903 C  CA    . PHE A 243 ? 0.43150 0.13996 0.41850 -0.00174 0.06078  -0.01629 273 PHE A CA    
1904 C  C     . PHE A 243 ? 0.47886 0.17014 0.45500 -0.01090 0.05117  -0.01042 273 PHE A C     
1905 O  O     . PHE A 243 ? 0.46993 0.13950 0.42716 -0.00719 0.04513  -0.01365 273 PHE A O     
1906 C  CB    . PHE A 243 ? 0.44676 0.14199 0.41855 0.00088  0.05689  -0.01996 273 PHE A CB    
1907 C  CG    . PHE A 243 ? 0.45612 0.14354 0.42415 -0.01094 0.04941  -0.01314 273 PHE A CG    
1908 C  CD1   . PHE A 243 ? 0.43847 0.14491 0.42381 -0.01749 0.05335  -0.00817 273 PHE A CD1   
1909 C  CD2   . PHE A 243 ? 0.55178 0.21234 0.49827 -0.01580 0.03773  -0.01149 273 PHE A CD2   
1910 C  CE1   . PHE A 243 ? 0.44621 0.14775 0.42900 -0.02801 0.04672  -0.00204 273 PHE A CE1   
1911 C  CE2   . PHE A 243 ? 0.49222 0.14699 0.43606 -0.02767 0.03060  -0.00478 273 PHE A CE2   
1912 C  CZ    . PHE A 243 ? 0.47293 0.14907 0.43532 -0.03363 0.03531  -0.00015 273 PHE A CZ    
1913 N  N     . SER A 244 ? 0.44228 0.14348 0.42949 -0.02312 0.04925  -0.00154 274 SER A N     
1914 C  CA    . SER A 244 ? 0.46214 0.14719 0.43749 -0.03520 0.03851  0.00552  274 SER A CA    
1915 C  C     . SER A 244 ? 0.45293 0.15301 0.44074 -0.04641 0.03766  0.01330  274 SER A C     
1916 O  O     . SER A 244 ? 0.42881 0.15415 0.43709 -0.04514 0.04578  0.01451  274 SER A O     
1917 C  CB    . SER A 244 ? 0.46443 0.14845 0.44046 -0.03902 0.03671  0.00955  274 SER A CB    
1918 O  OG    . SER A 244 ? 0.51462 0.22747 0.51468 -0.04254 0.04379  0.01492  274 SER A OG    
1919 N  N     . VAL A 245 ? 0.47366 0.15733 0.44790 -0.05704 0.02720  0.01834  275 VAL A N     
1920 C  CA    . VAL A 245 ? 0.53055 0.22820 0.51512 -0.06831 0.02522  0.02599  275 VAL A CA    
1921 C  C     . VAL A 245 ? 0.44555 0.17225 0.45242 -0.07361 0.03049  0.03297  275 VAL A C     
1922 O  O     . VAL A 245 ? 0.48415 0.23438 0.50843 -0.07398 0.03597  0.03515  275 VAL A O     
1923 C  CB    . VAL A 245 ? 0.49567 0.17009 0.46099 -0.08057 0.01181  0.03128  275 VAL A CB    
1924 C  CG1   . VAL A 245 ? 0.61474 0.30779 0.59260 -0.09483 0.00909  0.04141  275 VAL A CG1   
1925 C  CG2   . VAL A 245 ? 0.53126 0.18212 0.47749 -0.07484 0.00706  0.02468  275 VAL A CG2   
1926 N  N     . CYS A 246 ? 0.44994 0.17506 0.45545 -0.07731 0.02846  0.03658  276 CYS A N     
1927 C  CA    . CYS A 246 ? 0.43264 0.18553 0.45738 -0.08369 0.03183  0.04449  276 CYS A CA    
1928 C  C     . CYS A 246 ? 0.49565 0.27280 0.54050 -0.07219 0.04379  0.04030  276 CYS A C     
1929 O  O     . CYS A 246 ? 0.49080 0.29432 0.55340 -0.07433 0.04775  0.04499  276 CYS A O     
1930 C  CB    . CYS A 246 ? 0.50404 0.24884 0.52112 -0.09141 0.02617  0.05007  276 CYS A CB    
1931 S  SG    . CYS A 246 ? 0.77667 0.49702 0.77204 -0.10951 0.01039  0.05817  276 CYS A SG    
1932 N  N     . LEU A 247 ? 0.41994 0.18859 0.46143 -0.05977 0.04907  0.03146  277 LEU A N     
1933 C  CA    . LEU A 247 ? 0.40924 0.19850 0.46820 -0.04929 0.05966  0.02707  277 LEU A CA    
1934 C  C     . LEU A 247 ? 0.38078 0.18036 0.44734 -0.04799 0.06266  0.02598  277 LEU A C     
1935 O  O     . LEU A 247 ? 0.42149 0.24385 0.50497 -0.04626 0.06801  0.02795  277 LEU A O     
1936 C  CB    . LEU A 247 ? 0.37784 0.15569 0.43027 -0.03710 0.06400  0.01782  277 LEU A CB    
1937 C  CG    . LEU A 247 ? 0.45287 0.24993 0.52170 -0.02711 0.07417  0.01312  277 LEU A CG    
1938 C  CD1   . LEU A 247 ? 0.35773 0.17763 0.44432 -0.02814 0.07804  0.01826  277 LEU A CD1   
1939 C  CD2   . LEU A 247 ? 0.35648 0.14381 0.41840 -0.01564 0.07816  0.00392  277 LEU A CD2   
1940 N  N     . PHE A 248 ? 0.38036 0.16266 0.43348 -0.04806 0.05895  0.02260  278 PHE A N     
1941 C  CA    . PHE A 248 ? 0.37079 0.16181 0.43030 -0.04547 0.06257  0.02065  278 PHE A CA    
1942 C  C     . PHE A 248 ? 0.37451 0.18050 0.44314 -0.05456 0.05980  0.02832  278 PHE A C     
1943 O  O     . PHE A 248 ? 0.40619 0.22470 0.48396 -0.05190 0.06375  0.02761  278 PHE A O     
1944 C  CB    . PHE A 248 ? 0.38620 0.15660 0.42913 -0.04216 0.05983  0.01486  278 PHE A CB    
1945 C  CG    . PHE A 248 ? 0.38175 0.14956 0.42268 -0.03000 0.06645  0.00616  278 PHE A CG    
1946 C  CD1   . PHE A 248 ? 0.37863 0.14675 0.42084 -0.02456 0.06937  0.00351  278 PHE A CD1   
1947 C  CD2   . PHE A 248 ? 0.37974 0.14756 0.41875 -0.02450 0.06999  0.00122  278 PHE A CD2   
1948 C  CE1   . PHE A 248 ? 0.37441 0.14254 0.41539 -0.01368 0.07533  -0.00427 278 PHE A CE1   
1949 C  CE2   . PHE A 248 ? 0.37525 0.14425 0.41326 -0.01384 0.07637  -0.00634 278 PHE A CE2   
1950 C  CZ    . PHE A 248 ? 0.44701 0.21683 0.48645 -0.00869 0.07890  -0.00893 278 PHE A CZ    
1951 N  N     . ARG A 249 ? 0.37512 0.18100 0.44124 -0.06522 0.05299  0.03577  279 ARG A N     
1952 C  CA    . ARG A 249 ? 0.40725 0.23359 0.48465 -0.07322 0.05116  0.04345  279 ARG A CA    
1953 C  C     . ARG A 249 ? 0.40823 0.26280 0.50510 -0.06878 0.05796  0.04562  279 ARG A C     
1954 O  O     . ARG A 249 ? 0.45193 0.32658 0.55898 -0.07253 0.05739  0.05086  279 ARG A O     
1955 C  CB    . ARG A 249 ? 0.40965 0.23120 0.47963 -0.08704 0.04188  0.05175  279 ARG A CB    
1956 C  CG    . ARG A 249 ? 0.47851 0.27618 0.53044 -0.09445 0.03278  0.05218  279 ARG A CG    
1957 C  CD    . ARG A 249 ? 0.49989 0.29489 0.54568 -0.10927 0.02357  0.06144  279 ARG A CD    
1958 N  NE    . ARG A 249 ? 0.69187 0.46008 0.71750 -0.11778 0.01285  0.06257  279 ARG A NE    
1959 C  CZ    . ARG A 249 ? 0.92285 0.68361 0.93937 -0.13234 0.00296  0.07073  279 ARG A CZ    
1960 N  NH1   . ARG A 249 ? 0.83549 0.61489 0.86154 -0.14013 0.00290  0.07862  279 ARG A NH1   
1961 N  NH2   . ARG A 249 ? 0.83325 0.56715 0.82993 -0.13943 -0.00750 0.07117  279 ARG A NH2   
1962 N  N     . ARG A 250 ? 0.39716 0.25428 0.49884 -0.06066 0.06372  0.04189  280 ARG A N     
1963 C  CA    . ARG A 250 ? 0.41351 0.29607 0.53219 -0.05607 0.06920  0.04408  280 ARG A CA    
1964 C  C     . ARG A 250 ? 0.31786 0.20220 0.44252 -0.04350 0.07712  0.03640  280 ARG A C     
1965 O  O     . ARG A 250 ? 0.41061 0.30709 0.54488 -0.03741 0.08174  0.03575  280 ARG A O     
1966 C  CB    . ARG A 250 ? 0.33275 0.22134 0.45347 -0.06006 0.06777  0.04912  280 ARG A CB    
1967 C  CG    . ARG A 250 ? 0.53440 0.40318 0.64524 -0.05597 0.06856  0.04409  280 ARG A CG    
1968 C  CD    . ARG A 250 ? 0.64504 0.52014 0.75770 -0.06035 0.06696  0.04970  280 ARG A CD    
1969 N  NE    . ARG A 250 ? 0.79294 0.65599 0.90113 -0.05241 0.07024  0.04385  280 ARG A NE    
1970 C  CZ    . ARG A 250 ? 0.91580 0.75360 1.00711 -0.05417 0.06571  0.04151  280 ARG A CZ    
1971 N  NH1   . ARG A 250 ? 0.66615 0.48528 0.74209 -0.06368 0.05723  0.04429  280 ARG A NH1   
1972 N  NH2   . ARG A 250 ? 0.88410 0.71449 0.97288 -0.04582 0.06917  0.03614  280 ARG A NH2   
1973 N  N     . ILE A 251 ? 0.35858 0.23098 0.47710 -0.03994 0.07843  0.03080  281 ILE A N     
1974 C  CA    . ILE A 251 ? 0.31087 0.18651 0.43500 -0.02993 0.08533  0.02449  281 ILE A CA    
1975 C  C     . ILE A 251 ? 0.32323 0.20147 0.44814 -0.03012 0.08527  0.02412  281 ILE A C     
1976 O  O     . ILE A 251 ? 0.33839 0.21217 0.45751 -0.03692 0.08023  0.02720  281 ILE A O     
1977 C  CB    . ILE A 251 ? 0.30131 0.15987 0.41600 -0.02433 0.08788  0.01715  281 ILE A CB    
1978 C  CG1   . ILE A 251 ? 0.37737 0.21779 0.47756 -0.02703 0.08419  0.01467  281 ILE A CG1   
1979 C  CG2   . ILE A 251 ? 0.30533 0.15877 0.41710 -0.02370 0.08725  0.01712  281 ILE A CG2   
1980 C  CD1   . ILE A 251 ? 0.36302 0.18974 0.45353 -0.01967 0.08714  0.00671  281 ILE A CD1   
1981 N  N     . VAL A 252 ? 0.29560 0.18024 0.42695 -0.02290 0.09045  0.02046  282 VAL A N     
1982 C  CA    . VAL A 252 ? 0.29785 0.18257 0.42837 -0.02234 0.09066  0.01944  282 VAL A CA    
1983 C  C     . VAL A 252 ? 0.33961 0.20942 0.46093 -0.01973 0.09313  0.01335  282 VAL A C     
1984 O  O     . VAL A 252 ? 0.34137 0.20316 0.45516 -0.02259 0.09094  0.01296  282 VAL A O     
1985 C  CB    . VAL A 252 ? 0.30009 0.20050 0.44165 -0.01663 0.09349  0.01996  282 VAL A CB    
1986 C  CG1   . VAL A 252 ? 0.36276 0.25912 0.50101 -0.01537 0.09395  0.01787  282 VAL A CG1   
1987 C  CG2   . VAL A 252 ? 0.26539 0.18362 0.41492 -0.01899 0.09018  0.02649  282 VAL A CG2   
1988 N  N     . ALA A 253 ? 0.28470 0.15199 0.40642 -0.01408 0.09772  0.00857  283 ALA A N     
1989 C  CA    . ALA A 253 ? 0.28865 0.14715 0.40331 -0.01108 0.10074  0.00313  283 ALA A CA    
1990 C  C     . ALA A 253 ? 0.29117 0.14363 0.40159 -0.00665 0.10337  -0.00167 283 ALA A C     
1991 O  O     . ALA A 253 ? 0.28344 0.14224 0.40084 -0.00342 0.10559  -0.00200 283 ALA A O     
1992 C  CB    . ALA A 253 ? 0.27962 0.14602 0.40076 -0.00774 0.10471  0.00181  283 ALA A CB    
1993 N  N     . CYS A 254 ? 0.30236 0.14286 0.40061 -0.00576 0.10282  -0.00555 284 CYS A N     
1994 C  CA    . CYS A 254 ? 0.30639 0.14145 0.39862 -0.00004 0.10516  -0.01105 284 CYS A CA    
1995 C  C     . CYS A 254 ? 0.31012 0.14372 0.39587 0.00345  0.10843  -0.01589 284 CYS A C     
1996 O  O     . CYS A 254 ? 0.31940 0.14597 0.39650 0.00115  0.10595  -0.01574 284 CYS A O     
1997 C  CB    . CYS A 254 ? 0.32137 0.14147 0.40133 -0.00150 0.09939  -0.01097 284 CYS A CB    
1998 S  SG    . CYS A 254 ? 0.32859 0.14072 0.39910 0.00717  0.10117  -0.01815 284 CYS A SG    
1999 N  N     . HIS A 255 ? 0.30410 0.14454 0.39315 0.00910  0.11367  -0.02019 285 HIS A N     
2000 C  CA    . HIS A 255 ? 0.30725 0.15085 0.39144 0.01244  0.11760  -0.02460 285 HIS A CA    
2001 C  C     . HIS A 255 ? 0.31895 0.15469 0.38979 0.01877  0.11696  -0.03026 285 HIS A C     
2002 O  O     . HIS A 255 ? 0.32658 0.15171 0.39122 0.02002  0.11286  -0.03059 285 HIS A O     
2003 C  CB    . HIS A 255 ? 0.29305 0.15081 0.38905 0.01413  0.12330  -0.02548 285 HIS A CB    
2004 C  CG    . HIS A 255 ? 0.34727 0.21282 0.44194 0.01487  0.12762  -0.02799 285 HIS A CG    
2005 N  ND1   . HIS A 255 ? 0.31195 0.18813 0.41137 0.01862  0.13238  -0.03135 285 HIS A ND1   
2006 C  CD2   . HIS A 255 ? 0.41749 0.28316 0.50703 0.01188  0.12792  -0.02726 285 HIS A CD2   
2007 C  CE1   . HIS A 255 ? 0.28837 0.17175 0.38559 0.01720  0.13536  -0.03222 285 HIS A CE1   
2008 N  NE2   . HIS A 255 ? 0.38183 0.25872 0.47286 0.01323  0.13283  -0.02975 285 HIS A NE2   
2009 N  N     . PHE A 256 ? 0.40871 0.24991 0.47448 0.02270  0.12055  -0.03441 286 PHE A N     
2010 C  CA    . PHE A 256 ? 0.33450 0.17107 0.38651 0.03093  0.12029  -0.04072 286 PHE A CA    
2011 C  C     . PHE A 256 ? 0.36095 0.17932 0.39707 0.03073  0.11338  -0.04071 286 PHE A C     
2012 O  O     . PHE A 256 ? 0.53633 0.34256 0.55992 0.03635  0.10949  -0.04432 286 PHE A O     
2013 C  CB    . PHE A 256 ? 0.34892 0.18803 0.40370 0.03690  0.12195  -0.04415 286 PHE A CB    
2014 C  CG    . PHE A 256 ? 0.39571 0.25355 0.46443 0.03765  0.12879  -0.04495 286 PHE A CG    
2015 C  CD1   . PHE A 256 ? 0.45742 0.32860 0.52760 0.03759  0.13339  -0.04627 286 PHE A CD1   
2016 C  CD2   . PHE A 256 ? 0.40426 0.26628 0.48402 0.03789  0.13019  -0.04401 286 PHE A CD2   
2017 C  CE1   . PHE A 256 ? 0.39651 0.28373 0.47843 0.03698  0.13869  -0.04650 286 PHE A CE1   
2018 C  CE2   . PHE A 256 ? 0.43353 0.31109 0.52496 0.03844  0.13558  -0.04478 286 PHE A CE2   
2019 C  CZ    . PHE A 256 ? 0.33076 0.22040 0.42309 0.03755  0.13955  -0.04592 286 PHE A CZ    
2020 N  N     . ILE A 257 ? 0.35421 0.16969 0.38954 0.02466  0.11138  -0.03695 287 ILE A N     
2021 C  CA    . ILE A 257 ? 0.39839 0.19539 0.41882 0.02329  0.10385  -0.03627 287 ILE A CA    
2022 C  C     . ILE A 257 ? 0.37980 0.17712 0.39107 0.02488  0.10437  -0.03799 287 ILE A C     
2023 O  O     . ILE A 257 ? 0.42245 0.22626 0.44063 0.01905  0.10618  -0.03430 287 ILE A O     
2024 C  CB    . ILE A 257 ? 0.36927 0.15951 0.39549 0.01412  0.09882  -0.02957 287 ILE A CB    
2025 C  CG1   . ILE A 257 ? 0.36948 0.15428 0.39714 0.01417  0.09618  -0.02880 287 ILE A CG1   
2026 C  CG2   . ILE A 257 ? 0.38480 0.15983 0.39838 0.01033  0.09176  -0.02771 287 ILE A CG2   
2027 C  CD1   . ILE A 257 ? 0.40224 0.19063 0.44197 0.00560  0.09412  -0.02176 287 ILE A CD1   
2028 N  N     . LYS A 258 ? 0.39574 0.18520 0.39045 0.03323  0.10220  -0.04357 288 LYS A N     
2029 C  CA    . LYS A 258 ? 0.44534 0.23538 0.42919 0.03641  0.10243  -0.04576 288 LYS A CA    
2030 C  C     . LYS A 258 ? 0.42139 0.19418 0.39616 0.03111  0.09501  -0.04248 288 LYS A C     
2031 O  O     . LYS A 258 ? 0.43668 0.19550 0.41008 0.02633  0.08877  -0.03951 288 LYS A O     
2032 C  CB    . LYS A 258 ? 0.41875 0.20842 0.38775 0.04906  0.10263  -0.05341 288 LYS A CB    
2033 C  CG    . LYS A 258 ? 0.51771 0.28305 0.46544 0.05502  0.09340  -0.05681 288 LYS A CG    
2034 C  CD    . LYS A 258 ? 0.51870 0.28603 0.45007 0.06939  0.09381  -0.06493 288 LYS A CD    
2035 C  CE    . LYS A 258 ? 0.63770 0.38772 0.55478 0.07743  0.08768  -0.06959 288 LYS A CE    
2036 N  NZ    . LYS A 258 ? 0.63720 0.39949 0.54703 0.09138  0.09153  -0.07731 288 LYS A NZ    
2037 N  N     . PRO A 259 ? 0.45346 0.22787 0.42214 0.03134  0.09550  -0.04261 289 PRO A N     
2038 C  CA    . PRO A 259 ? 0.48258 0.24173 0.44317 0.02611  0.08865  -0.03945 289 PRO A CA    
2039 C  C     . PRO A 259 ? 0.47151 0.20643 0.41554 0.02791  0.07867  -0.04079 289 PRO A C     
2040 O  O     . PRO A 259 ? 0.52091 0.24520 0.46695 0.01922  0.07281  -0.03574 289 PRO A O     
2041 C  CB    . PRO A 259 ? 0.43898 0.20555 0.39294 0.02988  0.09188  -0.04147 289 PRO A CB    
2042 C  CG    . PRO A 259 ? 0.42272 0.21288 0.38967 0.03074  0.10150  -0.04200 289 PRO A CG    
2043 C  CD    . PRO A 259 ? 0.41970 0.21200 0.38887 0.03600  0.10266  -0.04535 289 PRO A CD    
2044 N  N     . ARG A 260 ? 0.47064 0.19691 0.39785 0.03871  0.07614  -0.04721 290 ARG A N     
2045 C  CA    . ARG A 260 ? 0.52782 0.22700 0.43503 0.04106  0.06513  -0.04891 290 ARG A CA    
2046 C  C     . ARG A 260 ? 0.52893 0.22081 0.44294 0.03412  0.06173  -0.04514 290 ARG A C     
2047 O  O     . ARG A 260 ? 0.57703 0.25043 0.48370 0.02705  0.05283  -0.04139 290 ARG A O     
2048 C  CB    . ARG A 260 ? 0.54981 0.24299 0.43703 0.05620  0.06359  -0.05738 290 ARG A CB    
2049 C  CG    . ARG A 260 ? 0.71244 0.37564 0.57620 0.06072  0.05172  -0.06029 290 ARG A CG    
2050 C  CD    . ARG A 260 ? 0.77237 0.41530 0.61924 0.05912  0.04263  -0.05946 290 ARG A CD    
2051 N  NE    . ARG A 260 ? 1.07287 0.70453 0.92617 0.04406  0.03666  -0.05161 290 ARG A NE    
2052 C  CZ    . ARG A 260 ? 0.95141 0.57655 0.80257 0.03726  0.03251  -0.04792 290 ARG A CZ    
2053 N  NH1   . ARG A 260 ? 0.87585 0.50867 0.72368 0.04263  0.03589  -0.05037 290 ARG A NH1   
2054 N  NH2   . ARG A 260 ? 0.90403 0.51595 0.75623 0.02494  0.02489  -0.04159 290 ARG A NH2   
2055 N  N     . THR A 261 ? 0.47472 0.18145 0.40207 0.03578  0.06848  -0.04587 291 THR A N     
2056 C  CA    . THR A 261 ? 0.46881 0.17211 0.40443 0.02953  0.06650  -0.04206 291 THR A CA    
2057 C  C     . THR A 261 ? 0.45785 0.16470 0.40746 0.01604  0.06514  -0.03370 291 THR A C     
2058 O  O     . THR A 261 ? 0.49163 0.18678 0.43915 0.00921  0.05855  -0.02958 291 THR A O     
2059 C  CB    . THR A 261 ? 0.45160 0.17378 0.40030 0.03485  0.07537  -0.04485 291 THR A CB    
2060 O  OG1   . THR A 261 ? 0.49753 0.21477 0.43017 0.04788  0.07494  -0.05278 291 THR A OG1   
2061 C  CG2   . THR A 261 ? 0.44315 0.16521 0.40203 0.02952  0.07476  -0.04117 291 THR A CG2   
2062 N  N     . LEU A 262 ? 0.44324 0.16570 0.40554 0.01233  0.07066  -0.03115 292 LEU A N     
2063 C  CA    . LEU A 262 ? 0.43244 0.16062 0.40812 0.00098  0.06963  -0.02367 292 LEU A CA    
2064 C  C     . LEU A 262 ? 0.45118 0.16013 0.41333 -0.00480 0.05953  -0.02087 292 LEU A C     
2065 O  O     . LEU A 262 ? 0.53293 0.23997 0.50049 -0.01404 0.05498  -0.01490 292 LEU A O     
2066 C  CB    . LEU A 262 ? 0.41583 0.16245 0.40483 -0.00015 0.07715  -0.02248 292 LEU A CB    
2067 C  CG    . LEU A 262 ? 0.51374 0.26650 0.51432 -0.00970 0.07592  -0.01577 292 LEU A CG    
2068 C  CD1   . LEU A 262 ? 0.45903 0.22154 0.47457 -0.01405 0.07715  -0.01164 292 LEU A CD1   
2069 C  CD2   . LEU A 262 ? 0.39640 0.16192 0.40390 -0.00916 0.08206  -0.01584 292 LEU A CD2   
2070 N  N     . LEU A 263 ? 0.46873 0.16459 0.41327 0.00085  0.05593  -0.02513 293 LEU A N     
2071 C  CA    . LEU A 263 ? 0.52077 0.19560 0.44981 -0.00398 0.04529  -0.02308 293 LEU A CA    
2072 C  C     . LEU A 263 ? 0.50719 0.16177 0.42356 -0.00617 0.03618  -0.02239 293 LEU A C     
2073 O  O     . LEU A 263 ? 0.53113 0.17577 0.44522 -0.01648 0.02829  -0.01668 293 LEU A O     
2074 C  CB    . LEU A 263 ? 0.50390 0.17082 0.41681 0.00453  0.04429  -0.02852 293 LEU A CB    
2075 C  CG    . LEU A 263 ? 0.51160 0.19715 0.43535 0.00526  0.05250  -0.02836 293 LEU A CG    
2076 C  CD1   . LEU A 263 ? 0.57689 0.26069 0.48609 0.01666  0.05430  -0.03497 293 LEU A CD1   
2077 C  CD2   . LEU A 263 ? 0.48705 0.17176 0.41585 -0.00465 0.04903  -0.02251 293 LEU A CD2   
2078 N  N     . ASP A 264 ? 0.51194 0.16240 0.42142 0.00261  0.03751  -0.02759 294 ASP A N     
2079 C  CA    . ASP A 264 ? 0.59113 0.22068 0.48693 0.00108  0.02870  -0.02720 294 ASP A CA    
2080 C  C     . ASP A 264 ? 0.51562 0.15534 0.42883 -0.01047 0.02950  -0.01962 294 ASP A C     
2081 O  O     . ASP A 264 ? 0.54044 0.16392 0.44490 -0.01901 0.02006  -0.01506 294 ASP A O     
2082 C  CB    . ASP A 264 ? 0.53978 0.16270 0.42275 0.01492  0.02994  -0.03536 294 ASP A CB    
2083 C  CG    . ASP A 264 ? 0.59247 0.20556 0.45559 0.02783  0.02812  -0.04316 294 ASP A CG    
2084 O  OD1   . ASP A 264 ? 0.62592 0.22948 0.47998 0.02561  0.02305  -0.04223 294 ASP A OD1   
2085 O  OD2   . ASP A 264 ? 0.60040 0.21664 0.45724 0.04049  0.03178  -0.05016 294 ASP A OD2   
2086 N  N     . TYR A 265 ? 0.48830 0.15411 0.42449 -0.01079 0.03997  -0.01814 295 TYR A N     
2087 C  CA    . TYR A 265 ? 0.49768 0.17529 0.45041 -0.02051 0.04087  -0.01104 295 TYR A CA    
2088 C  C     . TYR A 265 ? 0.47296 0.15388 0.43176 -0.03272 0.03638  -0.00344 295 TYR A C     
2089 O  O     . TYR A 265 ? 0.47588 0.15551 0.43729 -0.04288 0.03097  0.00321  295 TYR A O     
2090 C  CB    . TYR A 265 ? 0.44686 0.15047 0.42135 -0.01682 0.05244  -0.01168 295 TYR A CB    
2091 C  CG    . TYR A 265 ? 0.44393 0.14933 0.41727 -0.00666 0.05745  -0.01775 295 TYR A CG    
2092 C  CD1   . TYR A 265 ? 0.46496 0.14992 0.41825 -0.00008 0.05198  -0.02277 295 TYR A CD1   
2093 C  CD2   . TYR A 265 ? 0.45054 0.17815 0.44252 -0.00339 0.06726  -0.01851 295 TYR A CD2   
2094 C  CE1   . TYR A 265 ? 0.49748 0.18589 0.45015 0.00994  0.05676  -0.02862 295 TYR A CE1   
2095 C  CE2   . TYR A 265 ? 0.44381 0.17489 0.43588 0.00555  0.07196  -0.02394 295 TYR A CE2   
2096 C  CZ    . TYR A 265 ? 0.52578 0.23817 0.49863 0.01238  0.06698  -0.02907 295 TYR A CZ    
2097 O  OH    . TYR A 265 ? 0.52120 0.23837 0.49424 0.02194  0.07169  -0.03475 295 TYR A OH    
2098 N  N     . TRP A 266 ? 0.48187 0.16868 0.44325 -0.03206 0.03867  -0.00407 296 TRP A N     
2099 C  CA    . TRP A 266 ? 0.46773 0.15829 0.43429 -0.04263 0.03436  0.00254  296 TRP A CA    
2100 C  C     . TRP A 266 ? 0.49403 0.16038 0.44183 -0.04988 0.02167  0.00524  296 TRP A C     
2101 O  O     . TRP A 266 ? 0.49550 0.16446 0.44785 -0.06165 0.01616  0.01268  296 TRP A O     
2102 C  CB    . TRP A 266 ? 0.46061 0.15912 0.43065 -0.03933 0.03885  0.00050  296 TRP A CB    
2103 C  CG    . TRP A 266 ? 0.62706 0.33725 0.60832 -0.04848 0.03743  0.00697  296 TRP A CG    
2104 C  CD1   . TRP A 266 ? 0.46452 0.16566 0.43772 -0.05413 0.03046  0.00940  296 TRP A CD1   
2105 C  CD2   . TRP A 266 ? 0.49763 0.23131 0.49957 -0.05205 0.04281  0.01152  296 TRP A CD2   
2106 N  NE1   . TRP A 266 ? 0.45134 0.16994 0.43937 -0.06109 0.03138  0.01517  296 TRP A NE1   
2107 C  CE2   . TRP A 266 ? 0.49499 0.23365 0.50033 -0.05951 0.03877  0.01649  296 TRP A CE2   
2108 C  CE3   . TRP A 266 ? 0.58833 0.33898 0.60535 -0.04898 0.05016  0.01165  296 TRP A CE3   
2109 C  CZ2   . TRP A 266 ? 0.49846 0.25928 0.52133 -0.06305 0.04195  0.02127  296 TRP A CZ2   
2110 C  CZ3   . TRP A 266 ? 0.59424 0.36558 0.62827 -0.05260 0.05305  0.01648  296 TRP A CZ3   
2111 C  CH2   . TRP A 266 ? 0.62097 0.39745 0.65745 -0.05917 0.04892  0.02110  296 TRP A CH2   
2112 N  N     . GLN A 267 ? 0.53383 0.17677 0.45963 -0.04286 0.01645  -0.00066 297 GLN A N     
2113 C  CA    . GLN A 267 ? 0.54525 0.16061 0.44968 -0.04905 0.00298  0.00134  297 GLN A CA    
2114 C  C     . GLN A 267 ? 0.55844 0.16783 0.46175 -0.05693 -0.00221 0.00621  297 GLN A C     
2115 O  O     . GLN A 267 ? 0.58773 0.18674 0.48488 -0.06953 -0.01210 0.01295  297 GLN A O     
2116 C  CB    . GLN A 267 ? 0.66692 0.25811 0.54654 -0.03715 -0.00144 -0.00702 297 GLN A CB    
2117 C  CG    . GLN A 267 ? 0.75431 0.31283 0.60811 -0.04232 -0.01679 -0.00576 297 GLN A CG    
2118 C  CD    . GLN A 267 ? 0.96421 0.52263 0.81947 -0.05220 -0.02187 -0.00063 297 GLN A CD    
2119 O  OE1   . GLN A 267 ? 1.20891 0.77362 1.06582 -0.04662 -0.01781 -0.00376 297 GLN A OE1   
2120 N  NE2   . GLN A 267 ? 0.95213 0.50570 0.80763 -0.06731 -0.03060 0.00763  297 GLN A NE2   
2121 N  N     . ALA A 268 ? 0.54190 0.15790 0.45067 -0.05018 0.00407  0.00318  298 ALA A N     
2122 C  CA    . ALA A 268 ? 0.54699 0.15845 0.45518 -0.05721 -0.00008 0.00784  298 ALA A CA    
2123 C  C     . ALA A 268 ? 0.60463 0.23667 0.53187 -0.07152 0.00019  0.01791  298 ALA A C     
2124 O  O     . ALA A 268 ? 0.54599 0.16922 0.46731 -0.08348 -0.00858 0.02479  298 ALA A O     
2125 C  CB    . ALA A 268 ? 0.53382 0.15449 0.44897 -0.04682 0.00862  0.00283  298 ALA A CB    
2126 N  N     . LEU A 269 ? 0.51609 0.17667 0.46601 -0.07013 0.01019  0.01895  299 LEU A N     
2127 C  CA    . LEU A 269 ? 0.53054 0.21381 0.49883 -0.08146 0.01095  0.02786  299 LEU A CA    
2128 C  C     . LEU A 269 ? 0.52401 0.20048 0.48559 -0.09336 0.00134  0.03375  299 LEU A C     
2129 O  O     . LEU A 269 ? 0.59128 0.27486 0.55730 -0.10616 -0.00402 0.04227  299 LEU A O     
2130 C  CB    . LEU A 269 ? 0.46015 0.17265 0.45132 -0.07540 0.02294  0.02666  299 LEU A CB    
2131 C  CG    . LEU A 269 ? 0.55800 0.27921 0.55743 -0.06538 0.03194  0.02195  299 LEU A CG    
2132 C  CD1   . LEU A 269 ? 0.50905 0.25200 0.52553 -0.05771 0.04267  0.01894  299 LEU A CD1   
2133 C  CD2   . LEU A 269 ? 0.44144 0.17118 0.44831 -0.07143 0.03106  0.02769  299 LEU A CD2   
2134 N  N     . GLU A 270 ? 0.51422 0.17780 0.46487 -0.08962 -0.00119 0.02960  300 GLU A N     
2135 C  CA    . GLU A 270 ? 0.57841 0.23178 0.51991 -0.10076 -0.01162 0.03471  300 GLU A CA    
2136 C  C     . GLU A 270 ? 0.66618 0.29266 0.58710 -0.10995 -0.02468 0.03823  300 GLU A C     
2137 O  O     . GLU A 270 ? 0.78101 0.40939 0.70213 -0.12462 -0.03273 0.04673  300 GLU A O     
2138 C  CB    . GLU A 270 ? 0.64548 0.28742 0.57685 -0.09368 -0.01218 0.02887  300 GLU A CB    
2139 C  CG    . GLU A 270 ? 0.88391 0.55098 0.83390 -0.09099 -0.00342 0.02889  300 GLU A CG    
2140 C  CD    . GLU A 270 ? 1.15876 0.84339 1.12106 -0.10383 -0.00683 0.03768  300 GLU A CD    
2141 O  OE1   . GLU A 270 ? 1.02947 0.70136 0.98102 -0.11526 -0.01795 0.04294  300 GLU A OE1   
2142 O  OE2   . GLU A 270 ? 1.19233 0.90356 1.17425 -0.10232 0.00115  0.03930  300 GLU A OE2   
2143 N  N     . ASN A 271 ? 0.63158 0.23315 0.53375 -0.10147 -0.02742 0.03185  301 ASN A N     
2144 C  CA    . ASN A 271 ? 0.62946 0.21342 0.51357 -0.10583 -0.03932 0.03342  301 ASN A CA    
2145 C  C     . ASN A 271 ? 0.60046 0.19706 0.49381 -0.11805 -0.04128 0.04210  301 ASN A C     
2146 O  O     . ASN A 271 ? 0.71437 0.30331 0.59695 -0.12768 -0.05183 0.04705  301 ASN A O     
2147 C  CB    . ASN A 271 ? 0.63272 0.19500 0.49779 -0.09139 -0.04051 0.02412  301 ASN A CB    
2148 C  CG    . ASN A 271 ? 0.75832 0.30567 0.60869 -0.07966 -0.04165 0.01589  301 ASN A CG    
2149 O  OD1   . ASN A 271 ? 0.92696 0.47658 0.77904 -0.08326 -0.04308 0.01738  301 ASN A OD1   
2150 N  ND2   . ASN A 271 ? 0.76588 0.29875 0.60118 -0.06507 -0.04114 0.00709  301 ASN A ND2   
2151 N  N     . SER A 272 ? 0.66175 0.27715 0.57354 -0.11776 -0.03158 0.04410  302 SER A N     
2152 C  CA    . SER A 272 ? 0.67455 0.30241 0.59460 -0.12744 -0.03249 0.05172  302 SER A CA    
2153 C  C     . SER A 272 ? 0.61195 0.26987 0.55383 -0.13988 -0.02968 0.06140  302 SER A C     
2154 O  O     . SER A 272 ? 0.72644 0.40087 0.67871 -0.14763 -0.02874 0.06834  302 SER A O     
2155 C  CB    . SER A 272 ? 0.56251 0.19078 0.48687 -0.11791 -0.02423 0.04739  302 SER A CB    
2156 O  OG    . SER A 272 ? 0.68023 0.32960 0.62241 -0.10655 -0.01148 0.04206  302 SER A OG    
2157 N  N     . ARG A 273 ? 0.62329 0.29104 0.57279 -0.14073 -0.02788 0.06171  303 ARG A N     
2158 C  CA    . ARG A 273 ? 0.66830 0.36853 0.63812 -0.15032 -0.02581 0.07001  303 ARG A CA    
2159 C  C     . ARG A 273 ? 0.75728 0.45855 0.72126 -0.16662 -0.03655 0.07940  303 ARG A C     
2160 O  O     . ARG A 273 ? 0.94464 0.62415 0.88900 -0.16927 -0.04654 0.07815  303 ARG A O     
2161 C  CB    . ARG A 273 ? 0.71723 0.42402 0.69149 -0.14679 -0.02390 0.06730  303 ARG A CB    
2162 C  CG    . ARG A 273 ? 1.00569 0.73922 0.99429 -0.15794 -0.02570 0.07575  303 ARG A CG    
2163 C  CD    . ARG A 273 ? 1.09589 0.82692 1.08270 -0.15427 -0.02602 0.07212  303 ARG A CD    
2164 N  NE    . ARG A 273 ? 1.07946 0.77454 1.04324 -0.14914 -0.03160 0.06524  303 ARG A NE    
2165 C  CZ    . ARG A 273 ? 1.21839 0.88966 1.16277 -0.15769 -0.04408 0.06735  303 ARG A CZ    
2166 N  NH1   . ARG A 273 ? 1.24096 0.92320 1.18688 -0.17156 -0.05181 0.07575  303 ARG A NH1   
2167 N  NH2   . ARG A 273 ? 1.18223 0.82565 1.10677 -0.14838 -0.04761 0.05931  303 ARG A NH2   
2168 N  N     . GLY A 274 ? 0.68706 0.41691 0.66796 -0.17549 -0.03413 0.08802  304 GLY A N     
2169 C  CA    . GLY A 274 ? 0.86683 0.60348 0.84327 -0.18936 -0.04306 0.09633  304 GLY A CA    
2170 C  C     . GLY A 274 ? 0.97206 0.69840 0.93923 -0.19061 -0.04567 0.09731  304 GLY A C     
2171 O  O     . GLY A 274 ? 1.22572 0.96022 1.19024 -0.20284 -0.05260 0.10512  304 GLY A O     
2172 N  N     . GLU A 275 ? 0.76094 0.46784 0.72116 -0.17820 -0.04116 0.08928  305 GLU A N     
2173 C  CA    . GLU A 275 ? 0.80151 0.49975 0.75427 -0.17822 -0.04260 0.08995  305 GLU A CA    
2174 C  C     . GLU A 275 ? 0.78355 0.51172 0.75957 -0.17815 -0.03225 0.09436  305 GLU A C     
2175 O  O     . GLU A 275 ? 0.82243 0.56747 0.81541 -0.17281 -0.02362 0.09308  305 GLU A O     
2176 C  CB    . GLU A 275 ? 0.90929 0.57459 0.84332 -0.16456 -0.04317 0.07941  305 GLU A CB    
2177 C  CG    . GLU A 275 ? 0.96074 0.59769 0.87105 -0.16334 -0.05386 0.07499  305 GLU A CG    
2178 C  CD    . GLU A 275 ? 0.98548 0.59465 0.87292 -0.15914 -0.06109 0.07109  305 GLU A CD    
2179 O  OE1   . GLU A 275 ? 0.93485 0.54603 0.82606 -0.15498 -0.05609 0.07025  305 GLU A OE1   
2180 O  OE2   . GLU A 275 ? 1.08119 0.66676 0.94660 -0.15979 -0.07198 0.06892  305 GLU A OE2   
2181 N  N     . ASP A 276 ? 0.84858 0.58355 0.82487 -0.18422 -0.03381 0.09987  306 ASP A N     
2182 C  CA    . ASP A 276 ? 0.88781 0.65368 0.88632 -0.18432 -0.02451 0.10488  306 ASP A CA    
2183 C  C     . ASP A 276 ? 0.89644 0.64720 0.89263 -0.17189 -0.01808 0.09786  306 ASP A C     
2184 O  O     . ASP A 276 ? 0.91186 0.63017 0.88750 -0.16550 -0.02239 0.09065  306 ASP A O     
2185 C  CB    . ASP A 276 ? 1.03774 0.82485 1.04011 -0.19799 -0.02900 0.11552  306 ASP A CB    
2186 C  CG    . ASP A 276 ? 1.30975 1.11932 1.31835 -0.21010 -0.03413 0.12316  306 ASP A CG    
2187 O  OD1   . ASP A 276 ? 1.25051 1.05979 1.26171 -0.20775 -0.03373 0.12028  306 ASP A OD1   
2188 O  OD2   . ASP A 276 ? 1.18469 1.01224 1.19513 -0.22176 -0.03866 0.13197  306 ASP A OD2   
2189 N  N     . CYS A 277 ? 0.87161 0.65172 0.88935 -0.16375 -0.00690 0.09735  307 CYS A N     
2190 C  CA    . CYS A 277 ? 0.98071 0.75368 0.99895 -0.14862 0.00085  0.08891  307 CYS A CA    
2191 C  C     . CYS A 277 ? 0.98156 0.77781 1.01211 -0.15213 0.00438  0.09574  307 CYS A C     
2192 O  O     . CYS A 277 ? 0.96508 0.79564 1.01360 -0.15785 0.00710  0.10329  307 CYS A O     
2193 C  CB    . CYS A 277 ? 0.80171 0.58633 0.83330 -0.13172 0.01190  0.07928  307 CYS A CB    
2194 S  SG    . CYS A 277 ? 0.86377 0.61615 0.87744 -0.12355 0.00914  0.06889  307 CYS A SG    
2195 N  N     . PRO A 278 ? 1.07917 0.85895 1.10015 -0.14865 0.00411  0.09350  308 PRO A N     
2196 C  CA    . PRO A 278 ? 1.06912 0.87145 1.10218 -0.15021 0.00841  0.09928  308 PRO A CA    
2197 C  C     . PRO A 278 ? 0.88627 0.73063 0.94643 -0.14387 0.01858  0.10053  308 PRO A C     
2198 O  O     . PRO A 278 ? 1.11060 0.95787 1.17901 -0.12792 0.02726  0.09095  308 PRO A O     
2199 C  CB    . PRO A 278 ? 1.17719 0.95791 1.20111 -0.13707 0.01188  0.09018  308 PRO A CB    
2200 C  CG    . PRO A 278 ? 1.04911 0.78744 1.04600 -0.13817 0.00239  0.08505  308 PRO A CG    
2201 C  CD    . PRO A 278 ? 0.98126 0.72026 0.97850 -0.14186 -0.00039 0.08502  308 PRO A CD    
2202 N  N     . ASN B 13  ? 1.25535 0.86486 0.78233 -0.28779 0.05644  0.17561  43  ASN B N     
2203 C  CA    . ASN B 13  ? 1.23017 0.83284 0.75263 -0.27383 0.06210  0.17098  43  ASN B CA    
2204 C  C     . ASN B 13  ? 1.37143 1.00411 0.91042 -0.26656 0.07528  0.16823  43  ASN B C     
2205 O  O     . ASN B 13  ? 1.32313 0.96163 0.87815 -0.26362 0.07684  0.16409  43  ASN B O     
2206 C  CB    . ASN B 13  ? 1.26807 0.87176 0.77298 -0.27709 0.06343  0.17645  43  ASN B CB    
2207 C  CG    . ASN B 13  ? 1.47689 1.03825 0.96190 -0.27293 0.05180  0.17383  43  ASN B CG    
2208 O  OD1   . ASN B 13  ? 1.49698 1.02933 0.98159 -0.26471 0.04363  0.16685  43  ASN B OD1   
2209 N  ND2   . ASN B 13  ? 1.45379 1.01280 0.92218 -0.27771 0.05101  0.17912  43  ASN B ND2   
2210 N  N     . PHE B 14  ? 1.31054 0.96224 0.84443 -0.26298 0.08461  0.17016  44  PHE B N     
2211 C  CA    . PHE B 14  ? 1.28260 0.96530 0.83871 -0.24559 0.09377  0.16111  44  PHE B CA    
2212 C  C     . PHE B 14  ? 1.22070 0.94993 0.78715 -0.25361 0.10408  0.16684  44  PHE B C     
2213 O  O     . PHE B 14  ? 1.28715 1.03153 0.84113 -0.26873 0.10665  0.17764  44  PHE B O     
2214 C  CB    . PHE B 14  ? 1.11659 0.79578 0.66740 -0.22955 0.09526  0.15523  44  PHE B CB    
2215 C  CG    . PHE B 14  ? 1.08981 0.72851 0.63458 -0.21818 0.08597  0.14759  44  PHE B CG    
2216 C  CD1   . PHE B 14  ? 1.21549 0.81915 0.73724 -0.22619 0.07692  0.15243  44  PHE B CD1   
2217 C  CD2   . PHE B 14  ? 1.11945 0.75607 0.68103 -0.19946 0.08604  0.13568  44  PHE B CD2   
2218 C  CE1   . PHE B 14  ? 1.23880 0.80758 0.75483 -0.21467 0.06834  0.14507  44  PHE B CE1   
2219 C  CE2   . PHE B 14  ? 1.16929 0.77244 0.72602 -0.18922 0.07766  0.12897  44  PHE B CE2   
2220 C  CZ    . PHE B 14  ? 1.19836 0.76839 0.73256 -0.19624 0.06894  0.13341  44  PHE B CZ    
2221 N  N     . LEU B 15  ? 1.35913 1.11166 0.94812 -0.24317 0.10980  0.15955  45  LEU B N     
2222 C  CA    . LEU B 15  ? 1.35782 1.15657 0.95920 -0.24722 0.11969  0.16286  45  LEU B CA    
2223 C  C     . LEU B 15  ? 1.39915 1.22769 1.00361 -0.23231 0.12818  0.15873  45  LEU B C     
2224 O  O     . LEU B 15  ? 1.26695 1.13365 0.87171 -0.23813 0.13593  0.16483  45  LEU B O     
2225 C  CB    . LEU B 15  ? 1.28148 1.08916 0.90445 -0.24270 0.12106  0.15671  45  LEU B CB    
2226 C  CG    . LEU B 15  ? 1.34802 1.12102 0.97031 -0.25032 0.11162  0.15677  45  LEU B CG    
2227 C  CD1   . LEU B 15  ? 1.27155 1.06035 0.91538 -0.24740 0.11444  0.15206  45  LEU B CD1   
2228 C  CD2   . LEU B 15  ? 1.26104 1.01782 0.86371 -0.27363 0.10531  0.16937  45  LEU B CD2   
2229 N  N     . LYS B 16  ? 1.27448 1.08699 0.88103 -0.21282 0.12648  0.14836  46  LYS B N     
2230 C  CA    . LYS B 16  ? 1.19275 1.02541 0.79817 -0.19747 0.13236  0.14390  46  LYS B CA    
2231 C  C     . LYS B 16  ? 1.10658 0.90498 0.69841 -0.18887 0.12595  0.14011  46  LYS B C     
2232 O  O     . LYS B 16  ? 1.22904 0.99469 0.82338 -0.18312 0.11868  0.13387  46  LYS B O     
2233 C  CB    . LYS B 16  ? 1.25723 1.11000 0.88207 -0.17922 0.13723  0.13311  46  LYS B CB    
2234 C  CG    . LYS B 16  ? 1.17577 1.06788 0.81400 -0.18447 0.14467  0.13577  46  LYS B CG    
2235 C  CD    . LYS B 16  ? 1.21343 1.12379 0.86688 -0.16393 0.14907  0.12453  46  LYS B CD    
2236 C  CE    . LYS B 16  ? 1.32495 1.27723 0.99068 -0.16692 0.15685  0.12649  46  LYS B CE    
2237 N  NZ    . LYS B 16  ? 1.34668 1.29294 1.02358 -0.17968 0.15459  0.12895  46  LYS B NZ    
2238 N  N     . LEU B 17  ? 1.11478 0.92168 0.69213 -0.18786 0.12853  0.14396  47  LEU B N     
2239 C  CA    . LEU B 17  ? 1.23745 1.01492 0.80114 -0.17912 0.12303  0.14047  47  LEU B CA    
2240 C  C     . LEU B 17  ? 1.26109 1.05915 0.82456 -0.16138 0.12849  0.13470  47  LEU B C     
2241 O  O     . LEU B 17  ? 1.19474 1.02826 0.75588 -0.16327 0.13616  0.13965  47  LEU B O     
2242 C  CB    . LEU B 17  ? 1.18493 0.94479 0.72605 -0.19597 0.11891  0.15146  47  LEU B CB    
2243 C  CG    . LEU B 17  ? 1.22641 0.94526 0.75960 -0.20687 0.10873  0.15379  47  LEU B CG    
2244 C  CD1   . LEU B 17  ? 1.14146 0.84365 0.64970 -0.22285 0.10459  0.16479  47  LEU B CD1   
2245 C  CD2   . LEU B 17  ? 1.22978 0.91666 0.76686 -0.19028 0.10189  0.14235  47  LEU B CD2   
2246 N  N     . PRO B 18  ? 1.32063 1.09841 0.88594 -0.14388 0.12444  0.12438  48  PRO B N     
2247 C  CA    . PRO B 18  ? 1.26890 1.06108 0.83005 -0.12720 0.12800  0.11921  48  PRO B CA    
2248 C  C     . PRO B 18  ? 1.37578 1.16854 0.91606 -0.13322 0.12880  0.12711  48  PRO B C     
2249 O  O     . PRO B 18  ? 1.32034 1.08652 0.84752 -0.14490 0.12324  0.13287  48  PRO B O     
2250 C  CB    . PRO B 18  ? 1.36740 1.12990 0.93310 -0.11120 0.12111  0.10781  48  PRO B CB    
2251 C  CG    . PRO B 18  ? 1.25939 0.98750 0.82346 -0.12152 0.11322  0.10958  48  PRO B CG    
2252 C  CD    . PRO B 18  ? 1.28490 1.02586 0.85495 -0.13874 0.11587  0.11732  48  PRO B CD    
2253 N  N     . ASP B 19  ? 1.35136 1.17481 0.88773 -0.12458 0.13554  0.12726  49  ASP B N     
2254 C  CA    . ASP B 19  ? 1.35482 1.18663 0.87204 -0.12944 0.13787  0.13519  49  ASP B CA    
2255 C  C     . ASP B 19  ? 1.30632 1.10827 0.81187 -0.11587 0.13192  0.12878  49  ASP B C     
2256 O  O     . ASP B 19  ? 1.20414 1.01607 0.70835 -0.09795 0.13375  0.12188  49  ASP B O     
2257 C  CB    . ASP B 19  ? 1.38038 1.26027 0.89876 -0.12413 0.14759  0.13749  49  ASP B CB    
2258 C  CG    . ASP B 19  ? 1.30782 1.20594 0.80908 -0.13697 0.15161  0.14977  49  ASP B CG    
2259 O  OD1   . ASP B 19  ? 1.31022 1.17979 0.79616 -0.14663 0.14632  0.15512  49  ASP B OD1   
2260 O  OD2   . ASP B 19  ? 1.21415 1.15616 0.71690 -0.13741 0.15997  0.15424  49  ASP B OD2   
2261 N  N     . THR B 20  ? 1.28608 1.05030 0.78222 -0.12399 0.12413  0.13082  50  THR B N     
2262 C  CA    . THR B 20  ? 1.33433 1.06794 0.82049 -0.11163 0.11756  0.12431  50  THR B CA    
2263 C  C     . THR B 20  ? 1.30731 1.01623 0.77271 -0.12460 0.11285  0.13263  50  THR B C     
2264 O  O     . THR B 20  ? 1.28173 0.98541 0.74220 -0.14351 0.11170  0.14179  50  THR B O     
2265 C  CB    . THR B 20  ? 1.44762 1.15355 0.94663 -0.10224 0.11046  0.11381  50  THR B CB    
2266 O  OG1   . THR B 20  ? 1.43489 1.11734 0.92527 -0.08846 0.10480  0.10692  50  THR B OG1   
2267 C  CG2   . THR B 20  ? 1.29026 0.97083 0.78989 -0.11725 0.10460  0.11783  50  THR B CG2   
2268 N  N     . ASP B 21  ? 1.30439 0.99641 0.75652 -0.11387 0.10943  0.12910  51  ASP B N     
2269 C  CA    . ASP B 21  ? 1.31241 0.97700 0.74305 -0.12280 0.10398  0.13531  51  ASP B CA    
2270 C  C     . ASP B 21  ? 1.45663 1.08741 0.88435 -0.10780 0.09578  0.12520  51  ASP B C     
2271 O  O     . ASP B 21  ? 1.39548 1.02737 0.81627 -0.09397 0.09608  0.12068  51  ASP B O     
2272 C  CB    . ASP B 21  ? 1.36803 1.05422 0.78194 -0.12702 0.10979  0.14396  51  ASP B CB    
2273 C  CG    . ASP B 21  ? 1.57161 1.23067 0.96224 -0.14040 0.10441  0.15258  51  ASP B CG    
2274 O  OD1   . ASP B 21  ? 1.52688 1.14757 0.91054 -0.13611 0.09561  0.14769  51  ASP B OD1   
2275 O  OD2   . ASP B 21  ? 1.71437 1.39115 1.09316 -0.15533 0.10877  0.16442  51  ASP B OD2   
2276 N  N     . CYS B 22  ? 1.43747 1.03919 0.87037 -0.11020 0.08820  0.12160  52  CYS B N     
2277 C  CA    . CYS B 22  ? 1.33969 0.91149 0.77156 -0.09675 0.08008  0.11209  52  CYS B CA    
2278 C  C     . CYS B 22  ? 1.35882 0.90488 0.76704 -0.09808 0.07469  0.11521  52  CYS B C     
2279 O  O     . CYS B 22  ? 1.32684 0.85362 0.73177 -0.08489 0.06913  0.10749  52  CYS B O     
2280 C  CB    . CYS B 22  ? 1.28469 0.83643 0.72902 -0.09875 0.07379  0.10770  52  CYS B CB    
2281 S  SG    . CYS B 22  ? 1.45178 1.02732 0.92545 -0.09300 0.07822  0.10103  52  CYS B SG    
2282 N  N     . ARG B 23  ? 1.40458 0.94970 0.79574 -0.11407 0.07584  0.12650  53  ARG B N     
2283 C  CA    . ARG B 23  ? 1.37420 0.89382 0.74101 -0.11593 0.07054  0.12999  53  ARG B CA    
2284 C  C     . ARG B 23  ? 1.50710 1.04002 0.86641 -0.10310 0.07448  0.12769  53  ARG B C     
2285 O  O     . ARG B 23  ? 1.43063 0.94034 0.77898 -0.09297 0.06870  0.12272  53  ARG B O     
2286 C  CB    . ARG B 23  ? 1.46114 0.97663 0.81063 -0.13769 0.07046  0.14348  53  ARG B CB    
2287 C  CG    . ARG B 23  ? 1.48423 0.96652 0.80677 -0.14152 0.06310  0.14739  53  ARG B CG    
2288 C  CD    . ARG B 23  ? 1.67833 1.14015 0.98647 -0.16231 0.05777  0.15740  53  ARG B CD    
2289 N  NE    . ARG B 23  ? 1.89814 1.39030 1.20800 -0.17988 0.06534  0.16879  53  ARG B NE    
2290 C  CZ    . ARG B 23  ? 1.71215 1.19657 1.01722 -0.19903 0.06239  0.17727  53  ARG B CZ    
2291 N  NH1   . ARG B 23  ? 1.54961 0.99599 0.84720 -0.20242 0.05188  0.17544  53  ARG B NH1   
2292 N  NH2   . ARG B 23  ? 1.61456 1.13081 0.92194 -0.21479 0.06980  0.18778  53  ARG B NH2   
2293 N  N     . GLN B 24  ? 1.62957 1.20027 0.99413 -0.10267 0.08402  0.13105  54  GLN B N     
2294 C  CA    . GLN B 24  ? 1.55087 1.13675 0.90895 -0.08836 0.08785  0.12805  54  GLN B CA    
2295 C  C     . GLN B 24  ? 1.57457 1.15505 0.94579 -0.06733 0.08482  0.11432  54  GLN B C     
2296 O  O     . GLN B 24  ? 1.56737 1.13286 0.92891 -0.05464 0.08080  0.10890  54  GLN B O     
2297 C  CB    . GLN B 24  ? 1.51566 1.14583 0.87613 -0.09237 0.09863  0.13490  54  GLN B CB    
2298 C  CG    . GLN B 24  ? 1.65375 1.30403 1.00761 -0.07578 0.10309  0.13151  54  GLN B CG    
2299 C  CD    . GLN B 24  ? 1.71951 1.36071 1.04860 -0.07907 0.10229  0.13833  54  GLN B CD    
2300 O  OE1   . GLN B 24  ? 1.63861 1.27336 0.95468 -0.09771 0.10195  0.14942  54  GLN B OE1   
2301 N  NE2   . GLN B 24  ? 1.57858 1.21836 0.90004 -0.06103 0.10151  0.13181  54  GLN B NE2   
2302 N  N     . THR B 25  ? 1.50745 1.09936 0.90018 -0.06384 0.08624  0.10875  55  THR B N     
2303 C  CA    . THR B 25  ? 1.41767 1.00481 0.82358 -0.04585 0.08290  0.09638  55  THR B CA    
2304 C  C     . THR B 25  ? 1.42707 0.99227 0.84669 -0.04865 0.07638  0.09164  55  THR B C     
2305 O  O     . THR B 25  ? 1.50149 1.08028 0.93898 -0.05099 0.07901  0.09008  55  THR B O     
2306 C  CB    . THR B 25  ? 1.53486 1.15656 0.95303 -0.03664 0.09017  0.09313  55  THR B CB    
2307 O  OG1   . THR B 25  ? 1.65062 1.29756 1.05576 -0.03621 0.09713  0.09928  55  THR B OG1   
2308 C  CG2   . THR B 25  ? 1.34000 0.95346 0.76594 -0.01717 0.08550  0.08075  55  THR B CG2   
2309 N  N     . PRO B 26  ? 1.31777 0.85011 0.72928 -0.04794 0.06782  0.08920  56  PRO B N     
2310 C  CA    . PRO B 26  ? 1.28357 0.79678 0.70788 -0.04819 0.06123  0.08388  56  PRO B CA    
2311 C  C     . PRO B 26  ? 1.27303 0.79383 0.71592 -0.03425 0.06037  0.07369  56  PRO B C     
2312 O  O     . PRO B 26  ? 1.21863 0.73546 0.65831 -0.02063 0.05773  0.06727  56  PRO B O     
2313 C  CB    . PRO B 26  ? 1.22565 0.70513 0.63414 -0.04640 0.05231  0.08250  56  PRO B CB    
2314 C  CG    . PRO B 26  ? 1.25131 0.73280 0.64331 -0.03915 0.05380  0.08318  56  PRO B CG    
2315 C  CD    . PRO B 26  ? 1.24991 0.76196 0.63951 -0.04630 0.06366  0.09114  56  PRO B CD    
2316 N  N     . PRO B 27  ? 1.14426 0.67522 0.60596 -0.03747 0.06207  0.07210  57  PRO B N     
2317 C  CA    . PRO B 27  ? 1.14856 0.68444 0.62725 -0.02535 0.06038  0.06276  57  PRO B CA    
2318 C  C     . PRO B 27  ? 1.13253 0.64215 0.61420 -0.01941 0.05073  0.05600  57  PRO B C     
2319 O  O     . PRO B 27  ? 1.05762 0.54760 0.53408 -0.02597 0.04579  0.05815  57  PRO B O     
2320 C  CB    . PRO B 27  ? 1.11000 0.66392 0.60629 -0.03276 0.06524  0.06448  57  PRO B CB    
2321 C  CG    . PRO B 27  ? 1.06299 0.60922 0.55295 -0.04886 0.06540  0.07297  57  PRO B CG    
2322 C  CD    . PRO B 27  ? 1.09014 0.62935 0.55757 -0.05269 0.06565  0.07915  57  PRO B CD    
2323 N  N     . PHE B 28  ? 1.03994 0.54935 0.52894 -0.00658 0.04748  0.04777  58  PHE B N     
2324 C  CA    . PHE B 28  ? 0.91551 0.40507 0.41079 -0.00152 0.03856  0.04134  58  PHE B CA    
2325 C  C     . PHE B 28  ? 0.98535 0.47945 0.50094 -0.00537 0.03794  0.03934  58  PHE B C     
2326 O  O     . PHE B 28  ? 0.93596 0.41531 0.45570 -0.00753 0.03202  0.03786  58  PHE B O     
2327 C  CB    . PHE B 28  ? 0.91623 0.40198 0.41020 0.01236  0.03409  0.03385  58  PHE B CB    
2328 C  CG    . PHE B 28  ? 0.98299 0.45367 0.48645 0.01694  0.02520  0.02733  58  PHE B CG    
2329 C  CD1   . PHE B 28  ? 0.98407 0.43400 0.47821 0.01813  0.01811  0.02622  58  PHE B CD1   
2330 C  CD2   . PHE B 28  ? 0.89207 0.37033 0.41340 0.01983  0.02378  0.02254  58  PHE B CD2   
2331 C  CE1   . PHE B 28  ? 0.97709 0.41666 0.48039 0.02223  0.01004  0.02052  58  PHE B CE1   
2332 C  CE2   . PHE B 28  ? 0.88231 0.34933 0.41263 0.02294  0.01564  0.01732  58  PHE B CE2   
2333 C  CZ    . PHE B 28  ? 0.91958 0.36857 0.44137 0.02419  0.00888  0.01633  58  PHE B CZ    
2334 N  N     . LEU B 29  ? 1.00630 0.52132 0.53421 -0.00538 0.04381  0.03900  59  LEU B N     
2335 C  CA    . LEU B 29  ? 0.86219 0.38279 0.40941 -0.00889 0.04374  0.03723  59  LEU B CA    
2336 C  C     . LEU B 29  ? 0.89121 0.43331 0.44429 -0.01695 0.05247  0.04252  59  LEU B C     
2337 O  O     . LEU B 29  ? 0.91043 0.47080 0.46137 -0.01339 0.05835  0.04306  59  LEU B O     
2338 C  CB    . LEU B 29  ? 0.84951 0.37165 0.40886 0.00121  0.03981  0.02932  59  LEU B CB    
2339 C  CG    . LEU B 29  ? 0.89242 0.42026 0.47199 -0.00168 0.03923  0.02714  59  LEU B CG    
2340 C  CD1   . LEU B 29  ? 0.82673 0.34102 0.41016 -0.00791 0.03454  0.02840  59  LEU B CD1   
2341 C  CD2   . LEU B 29  ? 0.85273 0.38029 0.44109 0.00772  0.03450  0.01993  59  LEU B CD2   
2342 N  N     . VAL B 30  ? 0.86511 0.40536 0.42475 -0.02733 0.05295  0.04632  60  VAL B N     
2343 C  CA    . VAL B 30  ? 0.94427 0.50440 0.51175 -0.03602 0.06038  0.05115  60  VAL B CA    
2344 C  C     . VAL B 30  ? 0.87607 0.44119 0.46401 -0.03502 0.05953  0.04689  60  VAL B C     
2345 O  O     . VAL B 30  ? 0.95913 0.50940 0.55294 -0.03585 0.05358  0.04475  60  VAL B O     
2346 C  CB    . VAL B 30  ? 0.89783 0.45188 0.45543 -0.04999 0.06142  0.05966  60  VAL B CB    
2347 C  CG1   . VAL B 30  ? 0.94479 0.52004 0.51228 -0.05962 0.06845  0.06448  60  VAL B CG1   
2348 C  CG2   . VAL B 30  ? 0.87700 0.42693 0.41349 -0.05196 0.06249  0.06466  60  VAL B CG2   
2349 N  N     . LEU B 31  ? 0.90699 0.49375 0.50520 -0.03279 0.06539  0.04568  61  LEU B N     
2350 C  CA    . LEU B 31  ? 0.87065 0.46423 0.48783 -0.03202 0.06542  0.04203  61  LEU B CA    
2351 C  C     . LEU B 31  ? 0.87396 0.48233 0.49743 -0.04326 0.07165  0.04790  61  LEU B C     
2352 O  O     . LEU B 31  ? 0.86146 0.48882 0.48064 -0.04629 0.07860  0.05199  61  LEU B O     
2353 C  CB    . LEU B 31  ? 0.81029 0.41532 0.43336 -0.02069 0.06648  0.03584  61  LEU B CB    
2354 C  CG    . LEU B 31  ? 0.83452 0.42578 0.45085 -0.00939 0.05988  0.02986  61  LEU B CG    
2355 C  CD1   . LEU B 31  ? 0.78438 0.38630 0.40405 0.00124  0.06061  0.02428  61  LEU B CD1   
2356 C  CD2   . LEU B 31  ? 0.83797 0.40989 0.46057 -0.00925 0.05155  0.02666  61  LEU B CD2   
2357 N  N     . LEU B 32  ? 0.82945 0.42984 0.46249 -0.04932 0.06886  0.04846  62  LEU B N     
2358 C  CA    . LEU B 32  ? 0.76947 0.38175 0.40981 -0.05985 0.07354  0.05339  62  LEU B CA    
2359 C  C     . LEU B 32  ? 0.82688 0.44770 0.48686 -0.05591 0.07395  0.04837  62  LEU B C     
2360 O  O     . LEU B 32  ? 0.86059 0.46832 0.52842 -0.05335 0.06812  0.04467  62  LEU B O     
2361 C  CB    . LEU B 32  ? 0.77964 0.37381 0.41251 -0.07005 0.06931  0.05843  62  LEU B CB    
2362 C  CG    . LEU B 32  ? 0.83704 0.41793 0.44853 -0.07378 0.06736  0.06319  62  LEU B CG    
2363 C  CD1   . LEU B 32  ? 0.81476 0.37283 0.41707 -0.08197 0.06113  0.06695  62  LEU B CD1   
2364 C  CD2   . LEU B 32  ? 0.86825 0.46909 0.47177 -0.08017 0.07512  0.06959  62  LEU B CD2   
2365 N  N     . VAL B 33  ? 0.79060 0.43429 0.45812 -0.05514 0.08072  0.04828  63  VAL B N     
2366 C  CA    . VAL B 33  ? 0.84352 0.49647 0.52780 -0.04966 0.08148  0.04298  63  VAL B CA    
2367 C  C     . VAL B 33  ? 0.82958 0.49494 0.52441 -0.05891 0.08585  0.04668  63  VAL B C     
2368 O  O     . VAL B 33  ? 0.91718 0.59950 0.60858 -0.06541 0.09211  0.05179  63  VAL B O     
2369 C  CB    . VAL B 33  ? 0.75658 0.42480 0.44011 -0.03923 0.08490  0.03877  63  VAL B CB    
2370 C  CG1   . VAL B 33  ? 0.70310 0.37944 0.40238 -0.03413 0.08529  0.03358  63  VAL B CG1   
2371 C  CG2   . VAL B 33  ? 0.84798 0.50209 0.52012 -0.02983 0.07968  0.03492  63  VAL B CG2   
2372 N  N     . THR B 34  ? 0.79086 0.44939 0.49869 -0.05952 0.08254  0.04422  64  THR B N     
2373 C  CA    . THR B 34  ? 0.82014 0.48921 0.53890 -0.06723 0.08599  0.04692  64  THR B CA    
2374 C  C     . THR B 34  ? 0.92958 0.61886 0.66100 -0.06148 0.09089  0.04297  64  THR B C     
2375 O  O     . THR B 34  ? 0.87412 0.56084 0.61093 -0.05171 0.08833  0.03678  64  THR B O     
2376 C  CB    . THR B 34  ? 0.81947 0.47190 0.54528 -0.06977 0.07993  0.04613  64  THR B CB    
2377 O  OG1   . THR B 34  ? 0.87951 0.52537 0.61374 -0.06020 0.07537  0.03955  64  THR B OG1   
2378 C  CG2   . THR B 34  ? 0.89827 0.53014 0.60953 -0.07520 0.07468  0.05007  64  THR B CG2   
2379 N  N     . SER B 35  ? 0.95341 0.66250 0.68839 -0.06769 0.09748  0.04667  65  SER B N     
2380 C  CA    . SER B 35  ? 0.91523 0.64401 0.66191 -0.06233 0.10213  0.04297  65  SER B CA    
2381 C  C     . SER B 35  ? 0.94788 0.69496 0.70020 -0.07245 0.10799  0.04813  65  SER B C     
2382 O  O     . SER B 35  ? 0.97894 0.72778 0.72299 -0.08324 0.10955  0.05513  65  SER B O     
2383 C  CB    . SER B 35  ? 0.87787 0.61916 0.61759 -0.05171 0.10501  0.03948  65  SER B CB    
2384 O  OG    . SER B 35  ? 0.93435 0.69316 0.66418 -0.05621 0.11087  0.04484  65  SER B OG    
2385 N  N     . SER B 36  ? 0.97873 0.73883 0.74464 -0.06923 0.11074  0.04475  66  SER B N     
2386 C  CA    . SER B 36  ? 0.94227 0.72202 0.71541 -0.07750 0.11634  0.04865  66  SER B CA    
2387 C  C     . SER B 36  ? 1.04395 0.85149 0.81179 -0.07579 0.12362  0.05030  66  SER B C     
2388 O  O     . SER B 36  ? 1.04909 0.86093 0.80904 -0.06571 0.12432  0.04701  66  SER B O     
2389 C  CB    . SER B 36  ? 0.91421 0.69723 0.70378 -0.07379 0.11635  0.04400  66  SER B CB    
2390 O  OG    . SER B 36  ? 1.02767 0.78797 0.82261 -0.07273 0.10965  0.04153  66  SER B OG    
2391 N  N     . HIS B 37  ? 1.08984 0.91751 0.86194 -0.08540 0.12883  0.05538  67  HIS B N     
2392 C  CA    . HIS B 37  ? 1.05588 0.91481 0.82419 -0.08420 0.13618  0.05737  67  HIS B CA    
2393 C  C     . HIS B 37  ? 1.05885 0.93144 0.83211 -0.06809 0.13847  0.04910  67  HIS B C     
2394 O  O     . HIS B 37  ? 1.03768 0.92470 0.80194 -0.05917 0.14131  0.04737  67  HIS B O     
2395 C  CB    . HIS B 37  ? 1.06362 0.94218 0.83735 -0.09834 0.14070  0.06433  67  HIS B CB    
2396 C  CG    . HIS B 37  ? 1.12902 0.99549 0.89377 -0.11485 0.13819  0.07336  67  HIS B CG    
2397 N  ND1   . HIS B 37  ? 1.02053 0.90533 0.77522 -0.12536 0.14226  0.08159  67  HIS B ND1   
2398 C  CD2   . HIS B 37  ? 1.10940 0.94651 0.87219 -0.12238 0.13141  0.07550  67  HIS B CD2   
2399 C  CE1   . HIS B 37  ? 0.99934 0.86454 0.74567 -0.13942 0.13773  0.08859  67  HIS B CE1   
2400 N  NE2   . HIS B 37  ? 1.07920 0.91482 0.82981 -0.13719 0.13096  0.08472  67  HIS B NE2   
2401 N  N     . LYS B 38  ? 1.05623 0.92366 0.84248 -0.06365 0.13681  0.04385  68  LYS B N     
2402 C  CA    . LYS B 38  ? 1.17578 1.05409 0.96574 -0.04894 0.13821  0.03608  68  LYS B CA    
2403 C  C     . LYS B 38  ? 1.15577 1.01650 0.93704 -0.03549 0.13301  0.02975  68  LYS B C     
2404 O  O     . LYS B 38  ? 1.07788 0.94686 0.85707 -0.02222 0.13351  0.02348  68  LYS B O     
2405 C  CB    . LYS B 38  ? 1.15345 1.02869 0.95896 -0.04893 0.13727  0.03271  68  LYS B CB    
2406 C  CG    . LYS B 38  ? 1.18779 1.03303 0.99886 -0.05150 0.13019  0.03148  68  LYS B CG    
2407 C  CD    . LYS B 38  ? 1.22961 1.07509 1.05603 -0.05232 0.13001  0.02905  68  LYS B CD    
2408 C  CE    . LYS B 38  ? 1.18486 1.00446 1.01699 -0.05618 0.12348  0.02904  68  LYS B CE    
2409 N  NZ    . LYS B 38  ? 1.45270 1.27325 1.29961 -0.05627 0.12332  0.02665  68  LYS B NZ    
2410 N  N     . GLN B 39  ? 1.22041 1.05675 0.99555 -0.03834 0.12751  0.03112  69  GLN B N     
2411 C  CA    . GLN B 39  ? 1.10022 0.91767 0.86801 -0.02683 0.12151  0.02528  69  GLN B CA    
2412 C  C     . GLN B 39  ? 1.00553 0.83173 0.75736 -0.01922 0.12318  0.02503  69  GLN B C     
2413 O  O     . GLN B 39  ? 1.08004 0.88851 0.82194 -0.01649 0.11851  0.02448  69  GLN B O     
2414 C  CB    . GLN B 39  ? 1.03364 0.82284 0.80219 -0.03239 0.11466  0.02646  69  GLN B CB    
2415 C  CG    . GLN B 39  ? 1.02231 0.80209 0.80597 -0.03728 0.11207  0.02571  69  GLN B CG    
2416 C  CD    . GLN B 39  ? 1.07957 0.83322 0.86363 -0.03946 0.10460  0.02548  69  GLN B CD    
2417 O  OE1   . GLN B 39  ? 1.09828 0.84278 0.87779 -0.04773 0.10322  0.03032  69  GLN B OE1   
2418 N  NE2   . GLN B 39  ? 1.01289 0.75475 0.80165 -0.03205 0.09935  0.01994  69  GLN B NE2   
2419 N  N     . LEU B 40  ? 1.02801 0.88263 0.77709 -0.01502 0.12972  0.02523  70  LEU B N     
2420 C  CA    . LEU B 40  ? 0.98183 0.84820 0.71545 -0.00583 0.13160  0.02453  70  LEU B CA    
2421 C  C     . LEU B 40  ? 0.97923 0.82661 0.70405 0.00989  0.12476  0.01641  70  LEU B C     
2422 O  O     . LEU B 40  ? 1.02198 0.86310 0.73289 0.01547  0.12266  0.01609  70  LEU B O     
2423 C  CB    . LEU B 40  ? 0.94996 0.85285 0.68350 -0.00195 0.13949  0.02506  70  LEU B CB    
2424 C  CG    . LEU B 40  ? 1.13926 1.06055 0.85681 0.00874  0.14236  0.02445  70  LEU B CG    
2425 C  CD1   . LEU B 40  ? 1.15736 1.07744 0.86596 -0.00194 0.14371  0.03245  70  LEU B CD1   
2426 C  CD2   . LEU B 40  ? 1.08029 1.04015 0.79927 0.01386  0.14990  0.02420  70  LEU B CD2   
2427 N  N     . ALA B 41  ? 0.95902 0.79630 0.69100 0.01680  0.12076  0.01000  71  ALA B N     
2428 C  CA    . ALA B 41  ? 1.05931 0.87652 0.78204 0.03053  0.11305  0.00260  71  ALA B CA    
2429 C  C     . ALA B 41  ? 1.06045 0.84970 0.77904 0.02650  0.10621  0.00371  71  ALA B C     
2430 O  O     . ALA B 41  ? 1.11589 0.89402 0.82059 0.03570  0.10163  0.00062  71  ALA B O     
2431 C  CB    . ALA B 41  ? 0.90335 0.71313 0.63482 0.03593  0.10947  -0.00335 71  ALA B CB    
2432 N  N     . GLU B 42  ? 1.04599 0.82387 0.77588 0.01345  0.10510  0.00790  72  GLU B N     
2433 C  CA    . GLU B 42  ? 1.04041 0.79400 0.76673 0.00936  0.09886  0.00922  72  GLU B CA    
2434 C  C     . GLU B 42  ? 0.95400 0.70986 0.66547 0.00943  0.10049  0.01268  72  GLU B C     
2435 O  O     . GLU B 42  ? 1.12113 0.86065 0.82179 0.01583  0.09481  0.01008  72  GLU B O     
2436 C  CB    . GLU B 42  ? 0.96355 0.70906 0.70305 -0.00411 0.09839  0.01363  72  GLU B CB    
2437 C  CG    . GLU B 42  ? 1.09444 0.82914 0.84732 -0.00392 0.09389  0.01000  72  GLU B CG    
2438 C  CD    . GLU B 42  ? 1.13326 0.88543 0.89585 -0.00210 0.09856  0.00814  72  GLU B CD    
2439 O  OE1   . GLU B 42  ? 1.04048 0.81457 0.79968 -0.00067 0.10533  0.00949  72  GLU B OE1   
2440 O  OE2   . GLU B 42  ? 0.99698 0.74188 0.77048 -0.00216 0.09540  0.00549  72  GLU B OE2   
2441 N  N     . ARG B 43  ? 0.85447 0.63022 0.56503 0.00142  0.10791  0.01902  73  ARG B N     
2442 C  CA    . ARG B 43  ? 0.90044 0.67850 0.59695 -0.00048 0.10961  0.02346  73  ARG B CA    
2443 C  C     . ARG B 43  ? 1.03166 0.81802 0.71374 0.01458  0.10973  0.01907  73  ARG B C     
2444 O  O     . ARG B 43  ? 0.99399 0.76947 0.66303 0.01835  0.10672  0.01914  73  ARG B O     
2445 C  CB    . ARG B 43  ? 0.94141 0.74013 0.63966 -0.01365 0.11719  0.03191  73  ARG B CB    
2446 C  CG    . ARG B 43  ? 0.92131 0.70666 0.62868 -0.02866 0.11555  0.03693  73  ARG B CG    
2447 C  CD    . ARG B 43  ? 0.99421 0.79691 0.70012 -0.04278 0.12170  0.04593  73  ARG B CD    
2448 N  NE    . ARG B 43  ? 0.96476 0.79792 0.67790 -0.04290 0.12882  0.04662  73  ARG B NE    
2449 C  CZ    . ARG B 43  ? 0.96941 0.80830 0.69686 -0.04863 0.13034  0.04682  73  ARG B CZ    
2450 N  NH1   . ARG B 43  ? 0.87662 0.69360 0.61275 -0.05450 0.12540  0.04649  73  ARG B NH1   
2451 N  NH2   . ARG B 43  ? 0.86679 0.73509 0.59970 -0.04773 0.13687  0.04718  73  ARG B NH2   
2452 N  N     . MET B 44  ? 0.93341 0.73826 0.61662 0.02429  0.11271  0.01483  74  MET B N     
2453 C  CA    . MET B 44  ? 0.98138 0.79285 0.64928 0.04082  0.11178  0.00971  74  MET B CA    
2454 C  C     . MET B 44  ? 0.95946 0.74044 0.61995 0.05061  0.10160  0.00306  74  MET B C     
2455 O  O     . MET B 44  ? 0.97694 0.75200 0.62179 0.05968  0.09871  0.00118  74  MET B O     
2456 C  CB    . MET B 44  ? 1.07600 0.91213 0.74620 0.05020  0.11614  0.00583  74  MET B CB    
2457 C  CG    . MET B 44  ? 1.05438 0.92547 0.72981 0.04176  0.12638  0.01246  74  MET B CG    
2458 S  SD    . MET B 44  ? 1.22455 1.11125 0.88689 0.03551  0.13164  0.02082  74  MET B SD    
2459 C  CE    . MET B 44  ? 0.91103 0.79315 0.55234 0.05776  0.12712  0.01336  74  MET B CE    
2460 N  N     . ALA B 45  ? 0.90716 0.66913 0.57848 0.04846  0.09585  -0.00021 75  ALA B N     
2461 C  CA    . ALA B 45  ? 0.86034 0.59373 0.52540 0.05560  0.08554  -0.00572 75  ALA B CA    
2462 C  C     . ALA B 45  ? 0.93870 0.65514 0.59780 0.05008  0.08208  -0.00247 75  ALA B C     
2463 O  O     . ALA B 45  ? 0.90601 0.60660 0.55205 0.05891  0.07551  -0.00616 75  ALA B O     
2464 C  CB    . ALA B 45  ? 0.81388 0.53314 0.49307 0.05176  0.08063  -0.00836 75  ALA B CB    
2465 N  N     . ILE B 46  ? 0.85943 0.57819 0.52655 0.03602  0.08594  0.00425  76  ILE B N     
2466 C  CA    . ILE B 46  ? 0.88550 0.58652 0.54647 0.03067  0.08215  0.00727  76  ILE B CA    
2467 C  C     . ILE B 46  ? 0.91524 0.62474 0.55852 0.03688  0.08492  0.00874  76  ILE B C     
2468 O  O     . ILE B 46  ? 0.84065 0.53258 0.47287 0.04193  0.07900  0.00680  76  ILE B O     
2469 C  CB    . ILE B 46  ? 0.79371 0.49371 0.46564 0.01493  0.08484  0.01382  76  ILE B CB    
2470 C  CG1   . ILE B 46  ? 0.71038 0.39915 0.39823 0.01047  0.08066  0.01183  76  ILE B CG1   
2471 C  CG2   . ILE B 46  ? 0.83475 0.52099 0.49687 0.00989  0.08253  0.01773  76  ILE B CG2   
2472 C  CD1   . ILE B 46  ? 0.82022 0.51353 0.51962 -0.00313 0.08443  0.01759  76  ILE B CD1   
2473 N  N     . ARG B 47  ? 0.86645 0.60325 0.50732 0.03683  0.09347  0.01199  77  ARG B N     
2474 C  CA    . ARG B 47  ? 0.95447 0.70413 0.57882 0.04226  0.09713  0.01428  77  ARG B CA    
2475 C  C     . ARG B 47  ? 0.95322 0.69544 0.56322 0.06068  0.09154  0.00657  77  ARG B C     
2476 O  O     . ARG B 47  ? 0.99291 0.73288 0.58786 0.06599  0.09075  0.00726  77  ARG B O     
2477 C  CB    . ARG B 47  ? 0.95113 0.73586 0.57729 0.03907  0.10732  0.01898  77  ARG B CB    
2478 C  CG    . ARG B 47  ? 1.02024 0.81447 0.65301 0.02056  0.11314  0.02853  77  ARG B CG    
2479 C  CD    . ARG B 47  ? 1.04001 0.87033 0.67710 0.01744  0.12241  0.03241  77  ARG B CD    
2480 N  NE    . ARG B 47  ? 1.07168 0.91002 0.71518 -0.00166 0.12708  0.04182  77  ARG B NE    
2481 C  CZ    . ARG B 47  ? 1.09821 0.95000 0.75565 -0.01070 0.13097  0.04432  77  ARG B CZ    
2482 N  NH1   . ARG B 47  ? 1.13210 0.99465 0.79844 -0.00194 0.13195  0.03835  77  ARG B NH1   
2483 N  NH2   . ARG B 47  ? 1.14207 0.99516 0.80330 -0.02832 0.13329  0.05272  77  ARG B NH2   
2484 N  N     . GLN B 48  ? 0.91894 0.65620 0.53230 0.06998  0.08730  -0.00038 78  GLN B N     
2485 C  CA    . GLN B 48  ? 0.92845 0.65611 0.52622 0.08813  0.08061  -0.00817 78  GLN B CA    
2486 C  C     . GLN B 48  ? 0.91345 0.60645 0.50972 0.08875  0.06930  -0.01204 78  GLN B C     
2487 O  O     . GLN B 48  ? 1.04695 0.72643 0.62842 0.10218  0.06206  -0.01790 78  GLN B O     
2488 C  CB    . GLN B 48  ? 0.97149 0.71304 0.57128 0.09793  0.08185  -0.01330 78  GLN B CB    
2489 C  CG    . GLN B 48  ? 1.07944 0.85854 0.68089 0.09772  0.09301  -0.00953 78  GLN B CG    
2490 C  CD    . GLN B 48  ? 1.14814 0.94042 0.75905 0.10119  0.09516  -0.01300 78  GLN B CD    
2491 O  OE1   . GLN B 48  ? 1.14422 0.91681 0.76146 0.10222  0.08861  -0.01763 78  GLN B OE1   
2492 N  NE2   . GLN B 48  ? 1.19888 1.02561 0.81072 0.10265  0.10430  -0.01052 78  GLN B NE2   
2493 N  N     . THR B 49  ? 0.89238 0.57240 0.50290 0.07514  0.06748  -0.00897 79  THR B N     
2494 C  CA    . THR B 49  ? 0.96662 0.61694 0.57660 0.07424  0.05708  -0.01169 79  THR B CA    
2495 C  C     . THR B 49  ? 0.92721 0.56791 0.53607 0.06507  0.05679  -0.00672 79  THR B C     
2496 O  O     . THR B 49  ? 0.92083 0.56512 0.51599 0.06868  0.05894  -0.00485 79  THR B O     
2497 C  CB    . THR B 49  ? 0.91764 0.55983 0.54419 0.06808  0.05352  -0.01327 79  THR B CB    
2498 O  OG1   . THR B 49  ? 0.88757 0.54348 0.52900 0.05487  0.06119  -0.00723 79  THR B OG1   
2499 C  CG2   . THR B 49  ? 0.91045 0.55713 0.53557 0.07811  0.05196  -0.01889 79  THR B CG2   
2500 N  N     . TRP B 50  ? 0.85422 0.48345 0.47636 0.05381  0.05416  -0.00452 80  TRP B N     
2501 C  CA    . TRP B 50  ? 0.91468 0.53103 0.53433 0.04659  0.05200  -0.00084 80  TRP B CA    
2502 C  C     . TRP B 50  ? 0.93907 0.56932 0.55547 0.03876  0.06049  0.00625  80  TRP B C     
2503 O  O     . TRP B 50  ? 0.84843 0.46710 0.45920 0.03413  0.05850  0.00915  80  TRP B O     
2504 C  CB    . TRP B 50  ? 0.85297 0.45555 0.48728 0.03788  0.04673  -0.00067 80  TRP B CB    
2505 C  CG    . TRP B 50  ? 0.88390 0.49775 0.53568 0.02952  0.05125  0.00149  80  TRP B CG    
2506 C  CD1   . TRP B 50  ? 0.85948 0.47629 0.52154 0.03138  0.04990  -0.00186 80  TRP B CD1   
2507 C  CD2   . TRP B 50  ? 0.81559 0.43693 0.47569 0.01785  0.05691  0.00749  80  TRP B CD2   
2508 N  NE1   . TRP B 50  ? 0.82139 0.44866 0.49837 0.02210  0.05500  0.00156  80  TRP B NE1   
2509 C  CE2   . TRP B 50  ? 0.76616 0.39592 0.44207 0.01374  0.05906  0.00722  80  TRP B CE2   
2510 C  CE3   . TRP B 50  ? 0.75499 0.37526 0.40933 0.01051  0.05976  0.01307  80  TRP B CE3   
2511 C  CZ2   . TRP B 50  ? 0.73015 0.36737 0.41637 0.00300  0.06383  0.01213  80  TRP B CZ2   
2512 C  CZ3   . TRP B 50  ? 0.75228 0.37858 0.41586 -0.00049 0.06395  0.01804  80  TRP B CZ3   
2513 C  CH2   . TRP B 50  ? 0.72300 0.35774 0.40241 -0.00398 0.06589  0.01747  80  TRP B CH2   
2514 N  N     . GLY B 51  ? 0.92213 0.57603 0.54109 0.03708  0.06912  0.00909  81  GLY B N     
2515 C  CA    . GLY B 51  ? 0.92477 0.59203 0.54110 0.02706  0.07667  0.01689  81  GLY B CA    
2516 C  C     . GLY B 51  ? 1.05819 0.73825 0.65757 0.03398  0.08067  0.01841  81  GLY B C     
2517 O  O     . GLY B 51  ? 1.06026 0.74841 0.65413 0.02538  0.08571  0.02540  81  GLY B O     
2518 N  N     . LYS B 52  ? 1.06026 0.74199 0.65064 0.04901  0.07815  0.01226  82  LYS B N     
2519 C  CA    . LYS B 52  ? 1.10249 0.79668 0.67518 0.05797  0.08136  0.01303  82  LYS B CA    
2520 C  C     . LYS B 52  ? 1.14132 0.82023 0.70346 0.05315  0.07909  0.01692  82  LYS B C     
2521 O  O     . LYS B 52  ? 1.10728 0.76055 0.66645 0.05662  0.07050  0.01290  82  LYS B O     
2522 C  CB    . LYS B 52  ? 1.06902 0.75871 0.63098 0.07651  0.07592  0.00462  82  LYS B CB    
2523 C  CG    . LYS B 52  ? 1.11417 0.82740 0.66122 0.08816  0.08128  0.00454  82  LYS B CG    
2524 C  CD    . LYS B 52  ? 1.18447 0.89335 0.72176 0.10729  0.07534  -0.00461 82  LYS B CD    
2525 C  CE    . LYS B 52  ? 1.03530 0.75378 0.58419 0.10901  0.07649  -0.00795 82  LYS B CE    
2526 N  NZ    . LYS B 52  ? 1.32629 1.08079 0.87933 0.10626  0.08761  -0.00335 82  LYS B NZ    
2527 N  N     . GLU B 53  ? 1.20690 0.90142 0.76329 0.04501  0.08627  0.02466  83  GLU B N     
2528 C  CA    . GLU B 53  ? 1.20548 0.88562 0.75028 0.04001  0.08436  0.02887  83  GLU B CA    
2529 C  C     . GLU B 53  ? 1.11931 0.79196 0.64672 0.05500  0.08023  0.02432  83  GLU B C     
2530 O  O     . GLU B 53  ? 1.15029 0.83819 0.67085 0.06809  0.08198  0.02056  83  GLU B O     
2531 C  CB    . GLU B 53  ? 1.08488 0.78416 0.62611 0.02704  0.09277  0.03884  83  GLU B CB    
2532 C  CG    . GLU B 53  ? 1.16876 0.87265 0.72528 0.01135  0.09591  0.04381  83  GLU B CG    
2533 C  CD    . GLU B 53  ? 1.24147 0.96056 0.79253 -0.00323 0.10267  0.05433  83  GLU B CD    
2534 O  OE1   . GLU B 53  ? 1.24817 0.98102 0.78501 -0.00047 0.10652  0.05788  83  GLU B OE1   
2535 O  OE2   . GLU B 53  ? 1.10321 0.82022 0.66336 -0.01761 0.10372  0.05926  83  GLU B OE2   
2536 N  N     . ARG B 54  ? 1.11857 0.76729 0.63802 0.05391  0.07427  0.02433  84  ARG B N     
2537 C  CA    . ARG B 54  ? 1.08541 0.72251 0.58919 0.06844  0.06865  0.01905  84  ARG B CA    
2538 C  C     . ARG B 54  ? 1.10923 0.71988 0.60618 0.06450  0.06236  0.01994  84  ARG B C     
2539 O  O     . ARG B 54  ? 1.16226 0.76262 0.66651 0.05164  0.06172  0.02393  84  ARG B O     
2540 C  CB    . ARG B 54  ? 1.02048 0.64857 0.52735 0.08145  0.06165  0.00975  84  ARG B CB    
2541 C  CG    . ARG B 54  ? 1.01581 0.62484 0.53863 0.07479  0.05518  0.00695  84  ARG B CG    
2542 C  CD    . ARG B 54  ? 1.14884 0.74997 0.67399 0.08602  0.04827  -0.00129 84  ARG B CD    
2543 N  NE    . ARG B 54  ? 1.22008 0.80861 0.76225 0.07817  0.04347  -0.00286 84  ARG B NE    
2544 C  CZ    . ARG B 54  ? 1.34029 0.90516 0.88394 0.07828  0.03379  -0.00636 84  ARG B CZ    
2545 N  NH1   . ARG B 54  ? 1.22152 0.77049 0.75075 0.08580  0.02727  -0.00906 84  ARG B NH1   
2546 N  NH2   . ARG B 54  ? 1.35725 0.91547 0.91719 0.07068  0.03050  -0.00702 84  ARG B NH2   
2547 N  N     . MET B 55  ? 1.13617 0.73560 0.61797 0.07679  0.05723  0.01577  85  MET B N     
2548 C  CA    . MET B 55  ? 1.19755 0.77055 0.67202 0.07631  0.04976  0.01473  85  MET B CA    
2549 C  C     . MET B 55  ? 1.29553 0.84738 0.77754 0.08168  0.03943  0.00692  85  MET B C     
2550 O  O     . MET B 55  ? 1.25406 0.80645 0.73466 0.09305  0.03584  0.00076  85  MET B O     
2551 C  CB    . MET B 55  ? 1.24693 0.81916 0.70038 0.08634  0.04955  0.01473  85  MET B CB    
2552 C  CG    . MET B 55  ? 1.31446 0.90162 0.75874 0.07775  0.05808  0.02389  85  MET B CG    
2553 S  SD    . MET B 55  ? 1.55111 1.11719 0.99561 0.06140  0.05592  0.03004  85  MET B SD    
2554 C  CE    . MET B 55  ? 1.39700 0.98462 0.82857 0.05194  0.06619  0.04118  85  MET B CE    
2555 N  N     . VAL B 56  ? 1.56767 1.10122 1.05676 0.07340  0.03428  0.00740  86  VAL B N     
2556 C  CA    . VAL B 56  ? 1.63182 1.14689 1.12955 0.07552  0.02446  0.00137  86  VAL B CA    
2557 C  C     . VAL B 56  ? 1.57646 1.07017 1.06422 0.07673  0.01739  0.00045  86  VAL B C     
2558 O  O     . VAL B 56  ? 1.54801 1.03537 1.03737 0.06756  0.01796  0.00452  86  VAL B O     
2559 C  CB    . VAL B 56  ? 1.52215 1.03935 1.04015 0.06427  0.02516  0.00286  86  VAL B CB    
2560 C  CG1   . VAL B 56  ? 1.38482 0.88662 0.91203 0.06647  0.01518  -0.00300 86  VAL B CG1   
2561 C  CG2   . VAL B 56  ? 1.40182 0.94181 0.92886 0.06177  0.03350  0.00491  86  VAL B CG2   
2562 N  N     . LYS B 57  ? 1.60314 1.08503 1.07942 0.08851  0.01025  -0.00507 87  LYS B N     
2563 C  CA    . LYS B 57  ? 1.51691 0.97920 0.98203 0.09127  0.00333  -0.00645 87  LYS B CA    
2564 C  C     . LYS B 57  ? 1.42841 0.89362 0.88160 0.08707  0.00962  -0.00018 87  LYS B C     
2565 O  O     . LYS B 57  ? 1.49016 0.94119 0.93981 0.08265  0.00625  0.00129  87  LYS B O     
2566 C  CB    . LYS B 57  ? 1.55330 1.00071 1.03081 0.08494  -0.00454 -0.00840 87  LYS B CB    
2567 C  CG    . LYS B 57  ? 1.49850 0.94350 0.98878 0.08648  -0.01097 -0.01345 87  LYS B CG    
2568 C  CD    . LYS B 57  ? 1.35816 0.78698 0.83825 0.09688  -0.02164 -0.01971 87  LYS B CD    
2569 C  CE    . LYS B 57  ? 1.45377 0.87886 0.94593 0.09626  -0.02881 -0.02382 87  LYS B CE    
2570 N  NZ    . LYS B 57  ? 1.42506 0.83136 0.90863 0.10329  -0.04127 -0.02932 87  LYS B NZ    
2571 N  N     . GLY B 58  ? 1.40999 0.89428 0.85620 0.08834  0.01860  0.00376  88  GLY B N     
2572 C  CA    . GLY B 58  ? 1.39524 0.88459 0.82942 0.08305  0.02498  0.01076  88  GLY B CA    
2573 C  C     . GLY B 58  ? 1.41974 0.91380 0.86257 0.06723  0.03034  0.01790  88  GLY B C     
2574 O  O     . GLY B 58  ? 1.32002 0.81380 0.75160 0.06096  0.03409  0.02422  88  GLY B O     
2575 N  N     . LYS B 59  ? 1.42863 0.92598 0.88988 0.06046  0.03034  0.01727  89  LYS B N     
2576 C  CA    . LYS B 59  ? 1.22589 0.72636 0.69563 0.04605  0.03441  0.02343  89  LYS B CA    
2577 C  C     . LYS B 59  ? 1.12881 0.65450 0.60853 0.04116  0.04318  0.02681  89  LYS B C     
2578 O  O     . LYS B 59  ? 1.24593 0.78190 0.73383 0.04813  0.04351  0.02223  89  LYS B O     
2579 C  CB    . LYS B 59  ? 1.19544 0.68029 0.67867 0.04210  0.02725  0.02019  89  LYS B CB    
2580 C  CG    . LYS B 59  ? 1.22601 0.68739 0.69996 0.04365  0.01926  0.01852  89  LYS B CG    
2581 C  CD    . LYS B 59  ? 1.29818 0.74945 0.76454 0.05642  0.01234  0.01191  89  LYS B CD    
2582 C  CE    . LYS B 59  ? 1.41963 0.84917 0.87647 0.05793  0.00468  0.01040  89  LYS B CE    
2583 N  NZ    . LYS B 59  ? 1.33571 0.75508 0.78370 0.07002  -0.00228 0.00431  89  LYS B NZ    
2584 N  N     . GLN B 60  ? 1.13637 0.67119 0.61476 0.02894  0.04965  0.03483  90  GLN B N     
2585 C  CA    . GLN B 60  ? 1.20972 0.77101 0.69586 0.02359  0.05851  0.03895  90  GLN B CA    
2586 C  C     . GLN B 60  ? 1.11748 0.68072 0.62370 0.01669  0.05829  0.03794  90  GLN B C     
2587 O  O     . GLN B 60  ? 1.15822 0.70632 0.66911 0.00832  0.05463  0.03948  90  GLN B O     
2588 C  CB    . GLN B 60  ? 1.26841 0.83978 0.74347 0.01214  0.06523  0.04884  90  GLN B CB    
2589 C  CG    . GLN B 60  ? 1.17027 0.77130 0.65307 0.00516  0.07447  0.05400  90  GLN B CG    
2590 C  CD    . GLN B 60  ? 1.18567 0.81015 0.66758 0.01809  0.07882  0.05029  90  GLN B CD    
2591 O  OE1   . GLN B 60  ? 1.29898 0.92925 0.76584 0.02594  0.08024  0.05073  90  GLN B OE1   
2592 N  NE2   . GLN B 60  ? 1.16753 0.80487 0.66459 0.02123  0.08050  0.04632  90  GLN B NE2   
2593 N  N     . LEU B 61  ? 1.08861 0.67051 0.60568 0.02102  0.06200  0.03516  91  LEU B N     
2594 C  CA    . LEU B 61  ? 0.98886 0.57655 0.52487 0.01487  0.06305  0.03454  91  LEU B CA    
2595 C  C     . LEU B 61  ? 1.01703 0.63052 0.55664 0.00621  0.07262  0.04111  91  LEU B C     
2596 O  O     . LEU B 61  ? 1.02335 0.65790 0.55703 0.01163  0.07835  0.04196  91  LEU B O     
2597 C  CB    . LEU B 61  ? 0.89204 0.48015 0.43811 0.02569  0.05928  0.02631  91  LEU B CB    
2598 C  CG    . LEU B 61  ? 0.96959 0.56801 0.53466 0.02009  0.06175  0.02596  91  LEU B CG    
2599 C  CD1   . LEU B 61  ? 0.99785 0.57875 0.57371 0.01246  0.05622  0.02576  91  LEU B CD1   
2600 C  CD2   . LEU B 61  ? 1.01788 0.62382 0.58891 0.03112  0.06054  0.01920  91  LEU B CD2   
2601 N  N     . LYS B 62  ? 1.01071 0.62327 0.55975 -0.00677 0.07396  0.04558  92  LYS B N     
2602 C  CA    . LYS B 62  ? 1.01988 0.65589 0.57392 -0.01688 0.08219  0.05209  92  LYS B CA    
2603 C  C     . LYS B 62  ? 0.96333 0.60212 0.53689 -0.02058 0.08202  0.04979  92  LYS B C     
2604 O  O     . LYS B 62  ? 0.89501 0.51411 0.47578 -0.02159 0.07565  0.04674  92  LYS B O     
2605 C  CB    . LYS B 62  ? 0.92975 0.56119 0.47291 -0.03136 0.08385  0.06147  92  LYS B CB    
2606 C  CG    . LYS B 62  ? 1.08875 0.71899 0.61173 -0.02908 0.08469  0.06490  92  LYS B CG    
2607 C  CD    . LYS B 62  ? 1.05305 0.71474 0.57179 -0.02379 0.09276  0.06664  92  LYS B CD    
2608 C  CE    . LYS B 62  ? 1.09987 0.78678 0.62216 -0.03795 0.10069  0.07550  92  LYS B CE    
2609 N  NZ    . LYS B 62  ? 1.15028 0.87157 0.66859 -0.03218 0.10873  0.07726  92  LYS B NZ    
2610 N  N     . THR B 63  ? 0.91973 0.58406 0.50182 -0.02205 0.08893  0.05113  93  THR B N     
2611 C  CA    . THR B 63  ? 0.95139 0.61993 0.55193 -0.02442 0.08915  0.04856  93  THR B CA    
2612 C  C     . THR B 63  ? 0.94950 0.64026 0.55544 -0.03641 0.09668  0.05557  93  THR B C     
2613 O  O     . THR B 63  ? 0.96851 0.68461 0.57020 -0.03535 0.10352  0.05835  93  THR B O     
2614 C  CB    . THR B 63  ? 0.96466 0.64042 0.57240 -0.01041 0.08833  0.04028  93  THR B CB    
2615 O  OG1   . THR B 63  ? 0.98200 0.63576 0.58496 -0.00059 0.08026  0.03404  93  THR B OG1   
2616 C  CG2   . THR B 63  ? 0.90575 0.58635 0.53225 -0.01356 0.08886  0.03816  93  THR B CG2   
2617 N  N     . PHE B 64  ? 0.90896 0.59120 0.52427 -0.04729 0.09510  0.05822  94  PHE B N     
2618 C  CA    . PHE B 64  ? 0.97767 0.67775 0.59866 -0.06010 0.10093  0.06496  94  PHE B CA    
2619 C  C     . PHE B 64  ? 0.81705 0.51581 0.45647 -0.06149 0.09969  0.06157  94  PHE B C     
2620 O  O     . PHE B 64  ? 0.81089 0.49002 0.45676 -0.05669 0.09334  0.05618  94  PHE B O     
2621 C  CB    . PHE B 64  ? 0.91171 0.60019 0.52077 -0.07509 0.09968  0.07386  94  PHE B CB    
2622 C  CG    . PHE B 64  ? 1.05810 0.74223 0.64790 -0.07401 0.09950  0.07716  94  PHE B CG    
2623 C  CD1   . PHE B 64  ? 1.04981 0.76047 0.63202 -0.07422 0.10669  0.08148  94  PHE B CD1   
2624 C  CD2   . PHE B 64  ? 1.08777 0.74270 0.66688 -0.07217 0.09216  0.07585  94  PHE B CD2   
2625 C  CE1   . PHE B 64  ? 1.07788 0.78532 0.64214 -0.07292 0.10666  0.08467  94  PHE B CE1   
2626 C  CE2   . PHE B 64  ? 1.11259 0.76295 0.67354 -0.07089 0.09193  0.07880  94  PHE B CE2   
2627 C  CZ    . PHE B 64  ? 1.08097 0.75741 0.63454 -0.07138 0.09926  0.08331  94  PHE B CZ    
2628 N  N     . PHE B 65  ? 0.80939 0.53073 0.45724 -0.06835 0.10586  0.06505  95  PHE B N     
2629 C  CA    . PHE B 65  ? 0.92986 0.65359 0.59512 -0.07021 0.10577  0.06249  95  PHE B CA    
2630 C  C     . PHE B 65  ? 0.94333 0.66496 0.60945 -0.08668 0.10620  0.07019  95  PHE B C     
2631 O  O     . PHE B 65  ? 0.94541 0.68461 0.60588 -0.09659 0.11140  0.07752  95  PHE B O     
2632 C  CB    . PHE B 65  ? 0.97517 0.72683 0.64979 -0.06290 0.11204  0.05907  95  PHE B CB    
2633 C  CG    . PHE B 65  ? 0.93508 0.68652 0.60725 -0.04610 0.11045  0.05109  95  PHE B CG    
2634 C  CD1   . PHE B 65  ? 0.90205 0.64044 0.58407 -0.03744 0.10543  0.04347  95  PHE B CD1   
2635 C  CD2   . PHE B 65  ? 0.96394 0.72790 0.62288 -0.03913 0.11345  0.05145  95  PHE B CD2   
2636 C  CE1   . PHE B 65  ? 0.86726 0.60287 0.54524 -0.02287 0.10275  0.03643  95  PHE B CE1   
2637 C  CE2   . PHE B 65  ? 0.93666 0.69815 0.59145 -0.02306 0.11092  0.04384  95  PHE B CE2   
2638 C  CZ    . PHE B 65  ? 0.89820 0.64444 0.56212 -0.01530 0.10524  0.03637  95  PHE B CZ    
2639 N  N     . LEU B 66  ? 0.99258 0.69326 0.66526 -0.08952 0.10031  0.06862  96  LEU B N     
2640 C  CA    . LEU B 66  ? 0.98087 0.67435 0.65334 -0.10377 0.09878  0.07492  96  LEU B CA    
2641 C  C     . LEU B 66  ? 1.03045 0.74380 0.71899 -0.10726 0.10344  0.07490  96  LEU B C     
2642 O  O     . LEU B 66  ? 0.97724 0.69228 0.68008 -0.09863 0.10294  0.06817  96  LEU B O     
2643 C  CB    . LEU B 66  ? 0.93654 0.59896 0.60748 -0.10309 0.08985  0.07257  96  LEU B CB    
2644 C  CG    . LEU B 66  ? 0.91077 0.55290 0.56779 -0.09697 0.08452  0.07075  96  LEU B CG    
2645 C  CD1   . LEU B 66  ? 0.82384 0.43912 0.48125 -0.09480 0.07578  0.06764  96  LEU B CD1   
2646 C  CD2   . LEU B 66  ? 0.93125 0.57164 0.56905 -0.10636 0.08572  0.07872  96  LEU B CD2   
2647 N  N     . LEU B 67  ? 1.02141 0.74977 0.70715 -0.12045 0.10765  0.08271  97  LEU B N     
2648 C  CA    . LEU B 67  ? 1.06226 0.81068 0.76205 -0.12540 0.11213  0.08366  97  LEU B CA    
2649 C  C     . LEU B 67  ? 1.05948 0.79939 0.75453 -0.14258 0.10957  0.09182  97  LEU B C     
2650 O  O     . LEU B 67  ? 1.02079 0.74973 0.69954 -0.15265 0.10708  0.09879  97  LEU B O     
2651 C  CB    . LEU B 67  ? 0.91854 0.70310 0.62098 -0.12325 0.12112  0.08474  97  LEU B CB    
2652 C  CG    . LEU B 67  ? 0.93501 0.73208 0.64631 -0.10570 0.12386  0.07557  97  LEU B CG    
2653 C  CD1   . LEU B 67  ? 0.97826 0.81042 0.68757 -0.10278 0.13206  0.07712  97  LEU B CD1   
2654 C  CD2   . LEU B 67  ? 1.03334 0.82823 0.76216 -0.10121 0.12265  0.06968  97  LEU B CD2   
2655 N  N     . GLY B 68  ? 1.11687 0.86024 0.82520 -0.14580 0.10958  0.09089  98  GLY B N     
2656 C  CA    . GLY B 68  ? 1.20139 0.94280 0.90705 -0.16217 0.10810  0.09856  98  GLY B CA    
2657 C  C     . GLY B 68  ? 1.15638 0.93305 0.86927 -0.16950 0.11628  0.10287  98  GLY B C     
2658 O  O     . GLY B 68  ? 1.16167 0.96424 0.87393 -0.16543 0.12308  0.10311  98  GLY B O     
2659 N  N     . THR B 69  ? 1.11732 0.89617 0.83708 -0.17961 0.11544  0.10603  99  THR B N     
2660 C  CA    . THR B 69  ? 0.99604 0.80881 0.72406 -0.18734 0.12263  0.11010  99  THR B CA    
2661 C  C     . THR B 69  ? 1.08535 0.90685 0.83320 -0.17943 0.12446  0.10316  99  THR B C     
2662 O  O     . THR B 69  ? 1.13051 0.92939 0.88447 -0.17183 0.11923  0.09713  99  THR B O     
2663 C  CB    . THR B 69  ? 0.91299 0.72299 0.63054 -0.20885 0.11997  0.12130  99  THR B CB    
2664 O  OG1   . THR B 69  ? 1.13303 0.91221 0.85016 -0.21310 0.11147  0.12083  99  THR B OG1   
2665 C  CG2   . THR B 69  ? 0.99879 0.79979 0.69559 -0.21719 0.11803  0.12861  99  THR B CG2   
2666 N  N     . THR B 70  ? 1.04574 0.90177 0.80334 -0.18104 0.13199  0.10415  100 THR B N     
2667 C  CA    . THR B 70  ? 1.12673 0.99435 0.90265 -0.17307 0.13454  0.09757  100 THR B CA    
2668 C  C     . THR B 70  ? 1.19525 1.08976 0.97741 -0.18584 0.13891  0.10352  100 THR B C     
2669 O  O     . THR B 70  ? 1.14873 1.06449 0.92323 -0.19708 0.14266  0.11145  100 THR B O     
2670 C  CB    . THR B 70  ? 1.15852 1.04255 0.94197 -0.15430 0.13961  0.08869  100 THR B CB    
2671 O  OG1   . THR B 70  ? 1.24698 1.14138 1.04709 -0.14739 0.14175  0.08272  100 THR B OG1   
2672 C  CG2   . THR B 70  ? 1.14127 1.05831 0.91868 -0.15411 0.14699  0.09195  100 THR B CG2   
2673 N  N     . SER B 71  ? 1.36666 1.26095 1.16288 -0.18427 0.13825  0.09983  101 SER B N     
2674 C  CA    . SER B 71  ? 1.29253 1.21368 1.09670 -0.19484 0.14242  0.10431  101 SER B CA    
2675 C  C     . SER B 71  ? 1.33859 1.30004 1.15106 -0.18566 0.15174  0.10099  101 SER B C     
2676 O  O     . SER B 71  ? 1.31455 1.30690 1.12884 -0.19570 0.15669  0.10685  101 SER B O     
2677 C  CB    . SER B 71  ? 1.08864 0.99562 0.90469 -0.19493 0.13845  0.10096  101 SER B CB    
2678 O  OG    . SER B 71  ? 1.19820 1.10222 1.02628 -0.17667 0.13954  0.09046  101 SER B OG    
2679 N  N     . SER B 72  ? 1.32631 1.28839 1.14296 -0.16667 0.15373  0.09173  102 SER B N     
2680 C  CA    . SER B 72  ? 1.30042 1.29762 1.12338 -0.15519 0.16144  0.08719  102 SER B CA    
2681 C  C     . SER B 72  ? 1.20279 1.22833 1.01499 -0.16017 0.16677  0.09361  102 SER B C     
2682 O  O     . SER B 72  ? 1.17063 1.18542 0.97014 -0.15832 0.16532  0.09507  102 SER B O     
2683 C  CB    . SER B 72  ? 1.28620 1.27188 1.11197 -0.13432 0.16056  0.07633  102 SER B CB    
2684 O  OG    . SER B 72  ? 1.24585 1.26254 1.07231 -0.12192 0.16697  0.07206  102 SER B OG    
2685 N  N     . ALA B 73  ? 1.16445 1.22790 0.98180 -0.16632 0.17301  0.09753  103 ALA B N     
2686 C  CA    . ALA B 73  ? 1.05125 1.14863 0.85972 -0.16978 0.17899  0.10344  103 ALA B CA    
2687 C  C     . ALA B 73  ? 1.13398 1.24021 0.93759 -0.14866 0.18205  0.09552  103 ALA B C     
2688 O  O     . ALA B 73  ? 1.12774 1.24091 0.91860 -0.14860 0.18355  0.09917  103 ALA B O     
2689 C  CB    . ALA B 73  ? 0.92401 1.06391 0.74100 -0.17803 0.18523  0.10785  103 ALA B CB    
2690 N  N     . ALA B 74  ? 1.21361 1.31852 1.02615 -0.13052 0.18246  0.08470  104 ALA B N     
2691 C  CA    . ALA B 74  ? 1.29922 1.40957 1.10579 -0.10954 0.18405  0.07647  104 ALA B CA    
2692 C  C     . ALA B 74  ? 1.32461 1.40002 1.11977 -0.10548 0.17836  0.07511  104 ALA B C     
2693 O  O     . ALA B 74  ? 1.21889 1.30230 1.00226 -0.09743 0.17993  0.07463  104 ALA B O     
2694 C  CB    . ALA B 74  ? 1.21962 1.32936 1.03681 -0.09266 0.18395  0.06552  104 ALA B CB    
2695 N  N     . GLU B 75  ? 1.34106 1.37844 1.13927 -0.11039 0.17156  0.07434  105 GLU B N     
2696 C  CA    . GLU B 75  ? 1.31350 1.31782 1.10139 -0.10697 0.16574  0.07306  105 GLU B CA    
2697 C  C     . GLU B 75  ? 1.29088 1.29602 1.06492 -0.12038 0.16592  0.08279  105 GLU B C     
2698 O  O     . GLU B 75  ? 1.25735 1.25354 1.01940 -0.11384 0.16459  0.08191  105 GLU B O     
2699 C  CB    . GLU B 75  ? 1.18348 1.15065 0.97821 -0.10927 0.15853  0.07032  105 GLU B CB    
2700 C  CG    . GLU B 75  ? 1.20768 1.16751 1.01330 -0.09404 0.15700  0.06010  105 GLU B CG    
2701 C  CD    . GLU B 75  ? 1.32765 1.25426 1.14029 -0.09687 0.15016  0.05816  105 GLU B CD    
2702 O  OE1   . GLU B 75  ? 1.41177 1.32241 1.22112 -0.11031 0.14673  0.06448  105 GLU B OE1   
2703 O  OE2   . GLU B 75  ? 1.41079 1.32747 1.23130 -0.08551 0.14789  0.05044  105 GLU B OE2   
2704 N  N     . THR B 76  ? 1.23597 1.25057 1.01048 -0.13958 0.16704  0.09233  106 THR B N     
2705 C  CA    . THR B 76  ? 1.19555 1.21265 0.95564 -0.15372 0.16718  0.10249  106 THR B CA    
2706 C  C     . THR B 76  ? 1.28811 1.33968 1.04041 -0.14612 0.17397  0.10337  106 THR B C     
2707 O  O     . THR B 76  ? 1.32761 1.37230 1.06601 -0.14542 0.17310  0.10601  106 THR B O     
2708 C  CB    . THR B 76  ? 1.10401 1.12879 0.86573 -0.17620 0.16708  0.11284  106 THR B CB    
2709 O  OG1   . THR B 76  ? 1.09954 1.09110 0.86713 -0.18147 0.16015  0.11143  106 THR B OG1   
2710 C  CG2   . THR B 76  ? 1.10207 1.12623 0.84709 -0.19213 0.16623  0.12399  106 THR B CG2   
2711 N  N     . LYS B 77  ? 1.27617 1.36572 1.03674 -0.13950 0.18065  0.10095  107 LYS B N     
2712 C  CA    . LYS B 77  ? 1.32576 1.45132 1.07897 -0.12951 0.18714  0.10076  107 LYS B CA    
2713 C  C     . LYS B 77  ? 1.34423 1.45193 1.08886 -0.10886 0.18460  0.09180  107 LYS B C     
2714 O  O     . LYS B 77  ? 1.31397 1.42906 1.04510 -0.10572 0.18605  0.09438  107 LYS B O     
2715 C  CB    . LYS B 77  ? 1.26372 1.43015 1.02803 -0.12268 0.19371  0.09757  107 LYS B CB    
2716 C  CG    . LYS B 77  ? 1.34680 1.55470 1.10375 -0.11019 0.20052  0.09659  107 LYS B CG    
2717 C  CD    . LYS B 77  ? 1.40247 1.62712 1.14673 -0.12438 0.20319  0.10821  107 LYS B CD    
2718 C  CE    . LYS B 77  ? 1.26432 1.49630 1.01269 -0.15173 0.20350  0.12061  107 LYS B CE    
2719 N  NZ    . LYS B 77  ? 1.02533 1.27022 0.75988 -0.16715 0.20521  0.13266  107 LYS B NZ    
2720 N  N     . GLU B 78  ? 1.36843 1.45270 1.12038 -0.09498 0.18048  0.08145  108 GLU B N     
2721 C  CA    . GLU B 78  ? 1.43348 1.49902 1.17757 -0.07574 0.17697  0.07261  108 GLU B CA    
2722 C  C     . GLU B 78  ? 1.48781 1.52449 1.21926 -0.08122 0.17217  0.07644  108 GLU B C     
2723 O  O     . GLU B 78  ? 1.49776 1.53615 1.21664 -0.07085 0.17229  0.07462  108 GLU B O     
2724 C  CB    . GLU B 78  ? 1.29383 1.33524 1.04836 -0.06449 0.17219  0.06261  108 GLU B CB    
2725 C  CG    . GLU B 78  ? 1.42164 1.48962 1.18600 -0.05437 0.17638  0.05681  108 GLU B CG    
2726 C  CD    . GLU B 78  ? 1.57412 1.61856 1.35113 -0.05017 0.17189  0.04989  108 GLU B CD    
2727 O  OE1   . GLU B 78  ? 1.59493 1.60332 1.37285 -0.05285 0.16538  0.04870  108 GLU B OE1   
2728 O  OE2   . GLU B 78  ? 1.56939 1.63268 1.35530 -0.04398 0.17488  0.04568  108 GLU B OE2   
2729 N  N     . VAL B 79  ? 1.29792 1.30752 1.03152 -0.09681 0.16753  0.08155  109 VAL B N     
2730 C  CA    . VAL B 79  ? 1.26863 1.24832 0.98976 -0.10156 0.16220  0.08469  109 VAL B CA    
2731 C  C     . VAL B 79  ? 1.25933 1.25829 0.96668 -0.11153 0.16609  0.09433  109 VAL B C     
2732 O  O     . VAL B 79  ? 1.23340 1.21920 0.92735 -0.10770 0.16388  0.09480  109 VAL B O     
2733 C  CB    . VAL B 79  ? 1.15626 1.10197 0.88199 -0.11427 0.15560  0.08715  109 VAL B CB    
2734 C  CG1   . VAL B 79  ? 1.05190 0.97383 0.76250 -0.12384 0.15112  0.09345  109 VAL B CG1   
2735 C  CG2   . VAL B 79  ? 1.07398 0.99434 0.80929 -0.10174 0.15034  0.07713  109 VAL B CG2   
2736 N  N     . ASP B 80  ? 1.23186 1.26293 0.94192 -0.12479 0.17179  0.10244  110 ASP B N     
2737 C  CA    . ASP B 80  ? 1.29294 1.34678 0.98994 -0.13475 0.17592  0.11228  110 ASP B CA    
2738 C  C     . ASP B 80  ? 1.36884 1.44492 1.05748 -0.11625 0.18016  0.10755  110 ASP B C     
2739 O  O     . ASP B 80  ? 1.22770 1.29789 0.90164 -0.11554 0.17941  0.11060  110 ASP B O     
2740 C  CB    . ASP B 80  ? 1.35713 1.44598 1.06007 -0.15190 0.18139  0.12155  110 ASP B CB    
2741 C  CG    . ASP B 80  ? 1.51044 1.57747 1.22132 -0.16900 0.17665  0.12556  110 ASP B CG    
2742 O  OD1   . ASP B 80  ? 1.51916 1.54445 1.22526 -0.17310 0.16909  0.12527  110 ASP B OD1   
2743 O  OD2   . ASP B 80  ? 1.44189 1.53375 1.16337 -0.17751 0.18019  0.12868  110 ASP B OD2   
2744 N  N     . GLN B 81  ? 1.57779 1.67859 1.27454 -0.10019 0.18416  0.09971  111 GLN B N     
2745 C  CA    . GLN B 81  ? 1.56321 1.68513 1.25060 -0.08060 0.18747  0.09440  111 GLN B CA    
2746 C  C     . GLN B 81  ? 1.61258 1.69735 1.29105 -0.06570 0.18078  0.08638  111 GLN B C     
2747 O  O     . GLN B 81  ? 1.38975 1.48040 1.05432 -0.05608 0.18154  0.08585  111 GLN B O     
2748 C  CB    . GLN B 81  ? 1.59977 1.75290 1.29641 -0.06571 0.19200  0.08702  111 GLN B CB    
2749 C  CG    . GLN B 81  ? 1.61612 1.81506 1.31967 -0.07820 0.19965  0.09503  111 GLN B CG    
2750 C  CD    . GLN B 81  ? 1.62057 1.85085 1.33251 -0.06209 0.20391  0.08713  111 GLN B CD    
2751 O  OE1   . GLN B 81  ? 1.63839 1.84951 1.35898 -0.05161 0.20038  0.07782  111 GLN B OE1   
2752 N  NE2   . GLN B 81  ? 1.40891 1.68864 1.11762 -0.05982 0.21140  0.09092  111 GLN B NE2   
2753 N  N     . GLU B 82  ? 1.36005 1.40747 1.04616 -0.06392 0.17405  0.08039  112 GLU B N     
2754 C  CA    . GLU B 82  ? 1.30325 1.31484 0.98174 -0.05197 0.16702  0.07348  112 GLU B CA    
2755 C  C     . GLU B 82  ? 1.26469 1.25837 0.92973 -0.06207 0.16448  0.08056  112 GLU B C     
2756 O  O     . GLU B 82  ? 1.17305 1.15701 0.82554 -0.05081 0.16220  0.07738  112 GLU B O     
2757 C  CB    . GLU B 82  ? 1.26711 1.24587 0.95779 -0.05092 0.16059  0.06717  112 GLU B CB    
2758 C  CG    . GLU B 82  ? 1.23206 1.17455 0.91681 -0.03956 0.15275  0.06000  112 GLU B CG    
2759 C  CD    . GLU B 82  ? 1.39873 1.31367 1.09649 -0.03961 0.14690  0.05465  112 GLU B CD    
2760 O  OE1   . GLU B 82  ? 1.44334 1.36845 1.15445 -0.04568 0.14927  0.05530  112 GLU B OE1   
2761 O  OE2   . GLU B 82  ? 1.36202 1.24642 1.05671 -0.03367 0.13992  0.04995  112 GLU B OE2   
2762 N  N     . SER B 83  ? 1.25785 1.24548 0.92413 -0.08315 0.16423  0.09011  113 SER B N     
2763 C  CA    . SER B 83  ? 1.18882 1.15945 0.84064 -0.09392 0.16161  0.09757  113 SER B CA    
2764 C  C     . SER B 83  ? 1.17592 1.17718 0.81425 -0.09160 0.16750  0.10260  113 SER B C     
2765 O  O     . SER B 83  ? 1.12145 1.10859 0.74553 -0.08779 0.16506  0.10324  113 SER B O     
2766 C  CB    . SER B 83  ? 1.11902 1.07942 0.77300 -0.11729 0.15991  0.10726  113 SER B CB    
2767 O  OG    . SER B 83  ? 1.08954 1.03172 0.72762 -0.12790 0.15673  0.11462  113 SER B OG    
2768 N  N     . GLN B 84  ? 1.17673 1.22142 0.81923 -0.09343 0.17527  0.10619  114 GLN B N     
2769 C  CA    . GLN B 84  ? 1.18235 1.26088 0.81234 -0.09056 0.18133  0.11119  114 GLN B CA    
2770 C  C     . GLN B 84  ? 1.13911 1.21721 0.76089 -0.06520 0.18052  0.10106  114 GLN B C     
2771 O  O     . GLN B 84  ? 1.00156 1.08435 0.60825 -0.06105 0.18140  0.10363  114 GLN B O     
2772 C  CB    . GLN B 84  ? 1.37576 1.50405 1.01303 -0.09723 0.18974  0.11685  114 GLN B CB    
2773 C  CG    . GLN B 84  ? 1.48212 1.61755 1.11966 -0.12515 0.19110  0.13072  114 GLN B CG    
2774 C  CD    . GLN B 84  ? 1.39488 1.57892 1.04188 -0.13297 0.19873  0.13611  114 GLN B CD    
2775 O  OE1   . GLN B 84  ? 1.29721 1.51516 0.94840 -0.11648 0.20407  0.13013  114 GLN B OE1   
2776 N  NE2   . GLN B 84  ? 1.25633 1.44371 0.90584 -0.15798 0.19871  0.14737  114 GLN B NE2   
2777 N  N     . ARG B 85  ? 1.34651 1.41751 0.97684 -0.04808 0.17823  0.08956  115 ARG B N     
2778 C  CA    . ARG B 85  ? 1.26028 1.32890 0.88121 -0.02367 0.17625  0.07963  115 ARG B CA    
2779 C  C     . ARG B 85  ? 1.26287 1.28796 0.87435 -0.01910 0.16817  0.07598  115 ARG B C     
2780 O  O     . ARG B 85  ? 1.25514 1.27978 0.85271 -0.00466 0.16700  0.07239  115 ARG B O     
2781 C  CB    . ARG B 85  ? 1.27681 1.34847 0.90783 -0.00746 0.17519  0.06871  115 ARG B CB    
2782 C  CG    . ARG B 85  ? 1.16865 1.23657 0.78809 0.01818  0.17203  0.05818  115 ARG B CG    
2783 C  CD    . ARG B 85  ? 1.29174 1.34881 0.92014 0.03175  0.16817  0.04734  115 ARG B CD    
2784 N  NE    . ARG B 85  ? 1.40347 1.48557 1.04709 0.02357  0.17352  0.04962  115 ARG B NE    
2785 C  CZ    . ARG B 85  ? 1.47105 1.54049 1.12725 0.02638  0.17065  0.04339  115 ARG B CZ    
2786 N  NH1   . ARG B 85  ? 1.31512 1.34789 0.97095 0.03622  0.16243  0.03491  115 ARG B NH1   
2787 N  NH2   . ARG B 85  ? 1.42577 1.52049 1.09514 0.01851  0.17599  0.04607  115 ARG B NH2   
2788 N  N     . HIS B 86  ? 1.31003 1.29901 0.92832 -0.03047 0.16228  0.07664  116 HIS B N     
2789 C  CA    . HIS B 86  ? 1.20962 1.15772 0.82083 -0.02496 0.15406  0.07203  116 HIS B CA    
2790 C  C     . HIS B 86  ? 1.10386 1.03113 0.70692 -0.04150 0.15156  0.08061  116 HIS B C     
2791 O  O     . HIS B 86  ? 1.11783 1.01924 0.71024 -0.03554 0.14614  0.07800  116 HIS B O     
2792 C  CB    . HIS B 86  ? 1.21866 1.13812 0.84286 -0.02043 0.14757  0.06371  116 HIS B CB    
2793 C  CG    . HIS B 86  ? 1.26261 1.19433 0.89234 -0.00285 0.14798  0.05421  116 HIS B CG    
2794 N  ND1   . HIS B 86  ? 1.15184 1.08091 0.77051 0.01724  0.14511  0.04628  116 HIS B ND1   
2795 C  CD2   . HIS B 86  ? 1.29016 1.23506 0.93388 -0.00207 0.15025  0.05126  116 HIS B CD2   
2796 C  CE1   . HIS B 86  ? 1.24304 1.18237 0.86771 0.02965  0.14528  0.03888  116 HIS B CE1   
2797 N  NE2   . HIS B 86  ? 1.27437 1.22383 0.91461 0.01833  0.14862  0.04169  116 HIS B NE2   
2798 N  N     . GLY B 87  ? 1.05401 0.99006 0.66067 -0.06183 0.15459  0.09054  117 GLY B N     
2799 C  CA    . GLY B 87  ? 1.16669 1.08244 0.76264 -0.07772 0.15166  0.09916  117 GLY B CA    
2800 C  C     . GLY B 87  ? 1.23949 1.10935 0.83470 -0.07725 0.14241  0.09484  117 GLY B C     
2801 O  O     . GLY B 87  ? 1.19005 1.03943 0.77177 -0.08298 0.13878  0.09903  117 GLY B O     
2802 N  N     . ASP B 88  ? 1.21749 1.07140 0.82657 -0.07085 0.13839  0.08682  118 ASP B N     
2803 C  CA    . ASP B 88  ? 1.04542 0.85947 0.65500 -0.06834 0.12960  0.08185  118 ASP B CA    
2804 C  C     . ASP B 88  ? 1.06903 0.86760 0.69154 -0.07940 0.12633  0.08276  118 ASP B C     
2805 O  O     . ASP B 88  ? 1.22853 0.99995 0.85624 -0.07461 0.11960  0.07684  118 ASP B O     
2806 C  CB    . ASP B 88  ? 1.07709 0.88218 0.68910 -0.04815 0.12599  0.07051  118 ASP B CB    
2807 C  CG    . ASP B 88  ? 1.19930 1.02393 0.82544 -0.03952 0.12913  0.06451  118 ASP B CG    
2808 O  OD1   . ASP B 88  ? 1.09670 0.94035 0.73294 -0.04905 0.13392  0.06852  118 ASP B OD1   
2809 O  OD2   . ASP B 88  ? 1.12801 0.94783 0.75419 -0.02311 0.12626  0.05570  118 ASP B OD2   
2810 N  N     . ILE B 89  ? 1.07844 0.89365 0.70569 -0.09420 0.13051  0.09022  119 ILE B N     
2811 C  CA    . ILE B 89  ? 1.03662 0.83987 0.67617 -0.10389 0.12769  0.09092  119 ILE B CA    
2812 C  C     . ILE B 89  ? 1.04995 0.83361 0.67882 -0.12147 0.12372  0.09987  119 ILE B C     
2813 O  O     . ILE B 89  ? 0.97377 0.77007 0.59098 -0.13280 0.12692  0.10889  119 ILE B O     
2814 C  CB    . ILE B 89  ? 0.97381 0.80870 0.62721 -0.10709 0.13435  0.09194  119 ILE B CB    
2815 C  CG1   . ILE B 89  ? 1.13691 0.98484 0.80001 -0.08842 0.13647  0.08186  119 ILE B CG1   
2816 C  CG2   . ILE B 89  ? 1.01688 0.83920 0.68087 -0.11893 0.13131  0.09402  119 ILE B CG2   
2817 C  CD1   . ILE B 89  ? 1.13581 1.01448 0.81232 -0.08903 0.14271  0.08151  119 ILE B CD1   
2818 N  N     . ILE B 90  ? 1.07492 0.82749 0.70668 -0.12347 0.11625  0.09743  120 ILE B N     
2819 C  CA    . ILE B 90  ? 1.04125 0.77073 0.66298 -0.13893 0.11078  0.10467  120 ILE B CA    
2820 C  C     . ILE B 90  ? 1.05292 0.78355 0.68787 -0.14744 0.11015  0.10575  120 ILE B C     
2821 O  O     . ILE B 90  ? 1.01873 0.74024 0.66717 -0.13910 0.10741  0.09835  120 ILE B O     
2822 C  CB    . ILE B 90  ? 0.99208 0.68447 0.60495 -0.13324 0.10186  0.10069  120 ILE B CB    
2823 C  CG1   . ILE B 90  ? 1.00859 0.69949 0.60903 -0.12350 0.10224  0.09877  120 ILE B CG1   
2824 C  CG2   . ILE B 90  ? 0.94850 0.61509 0.54912 -0.14811 0.09522  0.10767  120 ILE B CG2   
2825 C  CD1   . ILE B 90  ? 0.96802 0.62750 0.56407 -0.11356 0.09408  0.09223  120 ILE B CD1   
2826 N  N     . GLN B 91  ? 1.14528 0.88690 0.77589 -0.16447 0.11228  0.11527  121 GLN B N     
2827 C  CA    . GLN B 91  ? 1.12199 0.86842 0.76475 -0.17317 0.11227  0.11688  121 GLN B CA    
2828 C  C     . GLN B 91  ? 1.07832 0.80422 0.70766 -0.19192 0.10625  0.12615  121 GLN B C     
2829 O  O     . GLN B 91  ? 1.14259 0.86444 0.75399 -0.20239 0.10532  0.13423  121 GLN B O     
2830 C  CB    . GLN B 91  ? 1.09406 0.88222 0.74818 -0.17527 0.12173  0.11889  121 GLN B CB    
2831 C  CG    . GLN B 91  ? 1.14160 0.93678 0.81004 -0.18256 0.12212  0.11951  121 GLN B CG    
2832 C  CD    . GLN B 91  ? 1.15511 0.99310 0.83385 -0.18451 0.13140  0.12161  121 GLN B CD    
2833 O  OE1   . GLN B 91  ? 1.10096 0.96261 0.77124 -0.19220 0.13637  0.12889  121 GLN B OE1   
2834 N  NE2   . GLN B 91  ? 1.06449 0.91362 0.76117 -0.17702 0.13372  0.11517  121 GLN B NE2   
2835 N  N     . LYS B 92  ? 1.08212 0.79357 0.71917 -0.19578 0.10154  0.12487  122 LYS B N     
2836 C  CA    . LYS B 92  ? 1.13838 0.83268 0.76449 -0.21388 0.09557  0.13338  122 LYS B CA    
2837 C  C     . LYS B 92  ? 1.26204 0.96878 0.90490 -0.21800 0.09713  0.13264  122 LYS B C     
2838 O  O     . LYS B 92  ? 1.26113 0.98457 0.92316 -0.20573 0.10180  0.12485  122 LYS B O     
2839 C  CB    . LYS B 92  ? 1.11480 0.76517 0.72644 -0.21249 0.08434  0.13184  122 LYS B CB    
2840 C  CG    . LYS B 92  ? 1.15381 0.78934 0.74549 -0.21175 0.08185  0.13434  122 LYS B CG    
2841 C  CD    . LYS B 92  ? 1.19221 0.78418 0.76762 -0.21087 0.07012  0.13319  122 LYS B CD    
2842 C  CE    . LYS B 92  ? 1.20075 0.77264 0.76183 -0.22880 0.06277  0.14171  122 LYS B CE    
2843 N  NZ    . LYS B 92  ? 1.26546 0.79416 0.80616 -0.22708 0.05085  0.14085  122 LYS B NZ    
2844 N  N     . ASP B 93  ? 1.32291 1.02030 0.95744 -0.23569 0.09265  0.14095  123 ASP B N     
2845 C  CA    . ASP B 93  ? 1.22849 0.93991 0.87709 -0.24246 0.09424  0.14196  123 ASP B CA    
2846 C  C     . ASP B 93  ? 1.29998 0.98285 0.95459 -0.23492 0.08651  0.13507  123 ASP B C     
2847 O  O     . ASP B 93  ? 1.50476 1.16007 1.14778 -0.24454 0.07756  0.13897  123 ASP B O     
2848 C  CB    . ASP B 93  ? 1.28503 1.00197 0.92224 -0.26529 0.09254  0.15426  123 ASP B CB    
2849 C  CG    . ASP B 93  ? 1.42481 1.16320 1.08010 -0.27046 0.09403  0.15436  123 ASP B CG    
2850 O  OD1   . ASP B 93  ? 1.45133 1.20099 1.12304 -0.26015 0.09963  0.14749  123 ASP B OD1   
2851 O  OD2   . ASP B 93  ? 1.36304 1.10776 1.01787 -0.28286 0.08858  0.16006  123 ASP B OD2   
2852 N  N     . PHE B 94  ? 1.14672 0.83651 0.81902 -0.21714 0.08963  0.12470  124 PHE B N     
2853 C  CA    . PHE B 94  ? 1.07813 0.74870 0.75982 -0.20912 0.08391  0.11796  124 PHE B CA    
2854 C  C     . PHE B 94  ? 1.10450 0.80044 0.81015 -0.19668 0.09114  0.11007  124 PHE B C     
2855 O  O     . PHE B 94  ? 1.13434 0.85144 0.84655 -0.18759 0.09812  0.10651  124 PHE B O     
2856 C  CB    . PHE B 94  ? 1.09181 0.72873 0.76348 -0.19875 0.07561  0.11294  124 PHE B CB    
2857 C  CG    . PHE B 94  ? 1.19812 0.84199 0.87522 -0.18302 0.07940  0.10585  124 PHE B CG    
2858 C  CD1   . PHE B 94  ? 1.16454 0.81310 0.82952 -0.18402 0.08210  0.10892  124 PHE B CD1   
2859 C  CD2   . PHE B 94  ? 1.09354 0.73852 0.78699 -0.16767 0.07970  0.09640  124 PHE B CD2   
2860 C  CE1   . PHE B 94  ? 1.08128 0.73466 0.75015 -0.16941 0.08478  0.10228  124 PHE B CE1   
2861 C  CE2   . PHE B 94  ? 1.05593 0.70558 0.75317 -0.15425 0.08211  0.09024  124 PHE B CE2   
2862 C  CZ    . PHE B 94  ? 1.12402 0.77719 0.80876 -0.15484 0.08445  0.09297  124 PHE B CZ    
2863 N  N     . LEU B 95  ? 1.09129 0.78443 0.80867 -0.19629 0.08906  0.10747  125 LEU B N     
2864 C  CA    . LEU B 95  ? 1.11267 0.82746 0.85202 -0.18535 0.09511  0.10027  125 LEU B CA    
2865 C  C     . LEU B 95  ? 1.13188 0.84111 0.87724 -0.16755 0.09511  0.09130  125 LEU B C     
2866 O  O     . LEU B 95  ? 1.07167 0.75632 0.81543 -0.16079 0.08814  0.08725  125 LEU B O     
2867 C  CB    . LEU B 95  ? 1.12231 0.82994 0.87119 -0.18764 0.09145  0.09903  125 LEU B CB    
2868 C  CG    . LEU B 95  ? 1.17464 0.90273 0.94587 -0.17709 0.09708  0.09187  125 LEU B CG    
2869 C  CD1   . LEU B 95  ? 1.07376 0.83832 0.85308 -0.18062 0.10680  0.09395  125 LEU B CD1   
2870 C  CD2   . LEU B 95  ? 1.12640 0.84256 0.90488 -0.17848 0.09213  0.09054  125 LEU B CD2   
2871 N  N     . ASP B 96  ? 1.12899 0.86135 0.88049 -0.15983 0.10242  0.08826  126 ASP B N     
2872 C  CA    . ASP B 96  ? 1.11270 0.83984 0.86746 -0.14420 0.10201  0.08052  126 ASP B CA    
2873 C  C     . ASP B 96  ? 1.01789 0.74700 0.79081 -0.13387 0.10189  0.07292  126 ASP B C     
2874 O  O     . ASP B 96  ? 1.01160 0.76260 0.79649 -0.12768 0.10786  0.06917  126 ASP B O     
2875 C  CB    . ASP B 96  ? 1.09935 0.84847 0.85144 -0.13941 0.10884  0.08011  126 ASP B CB    
2876 C  CG    . ASP B 96  ? 1.06783 0.80539 0.81703 -0.12587 0.10644  0.07381  126 ASP B CG    
2877 O  OD1   . ASP B 96  ? 1.05420 0.77050 0.80639 -0.12001 0.10023  0.06943  126 ASP B OD1   
2878 O  OD2   . ASP B 96  ? 1.01816 0.76847 0.76171 -0.12104 0.11045  0.07336  126 ASP B OD2   
2879 N  N     . VAL B 97  ? 0.97387 0.67982 0.74784 -0.13156 0.09468  0.07064  127 VAL B N     
2880 C  CA    . VAL B 97  ? 1.02553 0.73128 0.81565 -0.12218 0.09361  0.06398  127 VAL B CA    
2881 C  C     . VAL B 97  ? 0.98387 0.66642 0.77049 -0.11404 0.08621  0.06000  127 VAL B C     
2882 O  O     . VAL B 97  ? 0.94077 0.60477 0.71232 -0.11684 0.08107  0.06271  127 VAL B O     
2883 C  CB    . VAL B 97  ? 1.08407 0.79088 0.88229 -0.12862 0.09273  0.06574  127 VAL B CB    
2884 C  CG1   . VAL B 97  ? 0.99758 0.73081 0.80132 -0.13597 0.10034  0.06912  127 VAL B CG1   
2885 C  CG2   . VAL B 97  ? 1.00575 0.68784 0.78995 -0.13731 0.08488  0.07068  127 VAL B CG2   
2886 N  N     . TYR B 98  ? 0.86960 0.55399 0.67001 -0.10406 0.08547  0.05369  128 TYR B N     
2887 C  CA    . TYR B 98  ? 0.89422 0.56186 0.69296 -0.09563 0.07908  0.04966  128 TYR B CA    
2888 C  C     . TYR B 98  ? 0.91914 0.56378 0.70586 -0.09949 0.07135  0.05248  128 TYR B C     
2889 O  O     . TYR B 98  ? 0.94854 0.57796 0.72335 -0.09686 0.06658  0.05231  128 TYR B O     
2890 C  CB    . TYR B 98  ? 0.82806 0.50158 0.64394 -0.08694 0.07875  0.04380  128 TYR B CB    
2891 C  CG    . TYR B 98  ? 0.91758 0.58028 0.73309 -0.07815 0.07336  0.03960  128 TYR B CG    
2892 C  CD1   . TYR B 98  ? 0.89935 0.56665 0.71422 -0.07223 0.07483  0.03659  128 TYR B CD1   
2893 C  CD2   . TYR B 98  ? 0.97839 0.62664 0.79323 -0.07548 0.06630  0.03867  128 TYR B CD2   
2894 C  CE1   . TYR B 98  ? 0.98292 0.64075 0.79732 -0.06523 0.06940  0.03313  128 TYR B CE1   
2895 C  CE2   . TYR B 98  ? 0.90923 0.55035 0.72414 -0.06786 0.06133  0.03512  128 TYR B CE2   
2896 C  CZ    . TYR B 98  ? 0.94450 0.59042 0.75948 -0.06345 0.06290  0.03257  128 TYR B CZ    
2897 O  OH    . TYR B 98  ? 1.14326 0.78250 0.95827 -0.05685 0.05747  0.02938  128 TYR B OH    
2898 N  N     . TYR B 99  ? 0.93382 0.57479 0.72195 -0.10543 0.06956  0.05503  129 TYR B N     
2899 C  CA    . TYR B 99  ? 0.91752 0.53470 0.69384 -0.10685 0.06086  0.05661  129 TYR B CA    
2900 C  C     . TYR B 99  ? 1.00798 0.61033 0.76290 -0.11650 0.05799  0.06285  129 TYR B C     
2901 O  O     . TYR B 99  ? 1.02125 0.60122 0.76281 -0.11851 0.05001  0.06468  129 TYR B O     
2902 C  CB    . TYR B 99  ? 0.91469 0.53139 0.69908 -0.10861 0.05896  0.05664  129 TYR B CB    
2903 C  CG    . TYR B 99  ? 1.00435 0.62976 0.80661 -0.09753 0.05929  0.05031  129 TYR B CG    
2904 C  CD1   . TYR B 99  ? 1.01143 0.63076 0.81421 -0.08766 0.05540  0.04603  129 TYR B CD1   
2905 C  CD2   . TYR B 99  ? 0.97008 0.61107 0.78870 -0.09728 0.06359  0.04882  129 TYR B CD2   
2906 C  CE1   . TYR B 99  ? 1.13059 0.75904 0.94922 -0.07886 0.05543  0.04106  129 TYR B CE1   
2907 C  CE2   . TYR B 99  ? 1.10069 0.74968 0.93496 -0.08779 0.06378  0.04353  129 TYR B CE2   
2908 C  CZ    . TYR B 99  ? 1.16209 0.80500 0.99618 -0.07911 0.05965  0.03997  129 TYR B CZ    
2909 O  OH    . TYR B 99  ? 1.10015 0.75195 0.94930 -0.07101 0.05946  0.03553  129 TYR B OH    
2910 N  N     . ASN B 100 ? 1.02421 0.63811 0.77443 -0.12182 0.06385  0.06606  130 ASN B N     
2911 C  CA    . ASN B 100 ? 0.96498 0.56583 0.69435 -0.13023 0.06140  0.07196  130 ASN B CA    
2912 C  C     . ASN B 100 ? 0.94677 0.54468 0.66924 -0.12331 0.06160  0.06970  130 ASN B C     
2913 O  O     . ASN B 100 ? 0.96730 0.55916 0.67357 -0.12978 0.06141  0.07455  130 ASN B O     
2914 C  CB    . ASN B 100 ? 1.02178 0.63902 0.74869 -0.14352 0.06759  0.07885  130 ASN B CB    
2915 C  CG    . ASN B 100 ? 1.11623 0.71998 0.83322 -0.15600 0.06253  0.08497  130 ASN B CG    
2916 O  OD1   . ASN B 100 ? 1.16065 0.73797 0.86686 -0.15507 0.05336  0.08475  130 ASN B OD1   
2917 N  ND2   . ASN B 100 ? 1.25692 0.87890 0.97662 -0.16763 0.06796  0.09048  130 ASN B ND2   
2918 N  N     . LEU B 101 ? 0.87857 0.48024 0.61237 -0.11080 0.06157  0.06273  131 LEU B N     
2919 C  CA    . LEU B 101 ? 0.84672 0.44560 0.57430 -0.10404 0.06133  0.06030  131 LEU B CA    
2920 C  C     . LEU B 101 ? 0.88844 0.46167 0.59591 -0.10500 0.05358  0.06233  131 LEU B C     
2921 O  O     . LEU B 101 ? 0.89208 0.46217 0.58780 -0.10512 0.05424  0.06377  131 LEU B O     
2922 C  CB    . LEU B 101 ? 0.81102 0.41630 0.55384 -0.09163 0.06107  0.05283  131 LEU B CB    
2923 C  CG    . LEU B 101 ? 0.74943 0.37902 0.50721 -0.08927 0.06899  0.05054  131 LEU B CG    
2924 C  CD1   . LEU B 101 ? 0.77654 0.40953 0.54756 -0.07835 0.06745  0.04378  131 LEU B CD1   
2925 C  CD2   . LEU B 101 ? 0.75964 0.39991 0.50892 -0.09149 0.07458  0.05298  131 LEU B CD2   
2926 N  N     . THR B 102 ? 0.89138 0.44558 0.59322 -0.10500 0.04588  0.06234  132 THR B N     
2927 C  CA    . THR B 102 ? 0.79289 0.32112 0.47289 -0.10584 0.03794  0.06437  132 THR B CA    
2928 C  C     . THR B 102 ? 0.86423 0.38946 0.52737 -0.11831 0.04021  0.07202  132 THR B C     
2929 O  O     . THR B 102 ? 0.95229 0.46879 0.60140 -0.11774 0.03895  0.07321  132 THR B O     
2930 C  CB    . THR B 102 ? 0.84111 0.34908 0.51478 -0.10467 0.02900  0.06388  132 THR B CB    
2931 O  OG1   . THR B 102 ? 0.81406 0.32710 0.50311 -0.09256 0.02690  0.05701  132 THR B OG1   
2932 C  CG2   . THR B 102 ? 0.79040 0.26975 0.43903 -0.10465 0.02009  0.06565  132 THR B CG2   
2933 N  N     . LEU B 103 ? 0.90355 0.43848 0.56870 -0.12996 0.04404  0.07747  133 LEU B N     
2934 C  CA    . LEU B 103 ? 0.86303 0.40070 0.51413 -0.14333 0.04714  0.08561  133 LEU B CA    
2935 C  C     . LEU B 103 ? 0.89386 0.44922 0.54678 -0.13971 0.05435  0.08490  133 LEU B C     
2936 O  O     . LEU B 103 ? 0.99690 0.54258 0.63258 -0.14273 0.05293  0.08837  133 LEU B O     
2937 C  CB    . LEU B 103 ? 0.94715 0.50004 0.60506 -0.15557 0.05146  0.09087  133 LEU B CB    
2938 C  CG    . LEU B 103 ? 1.11548 0.65180 0.77225 -0.15906 0.04432  0.09145  133 LEU B CG    
2939 C  CD1   . LEU B 103 ? 1.05550 0.60579 0.71563 -0.17368 0.04811  0.09804  133 LEU B CD1   
2940 C  CD2   . LEU B 103 ? 0.94694 0.44752 0.57986 -0.16036 0.03283  0.09330  133 LEU B CD2   
2941 N  N     . LYS B 104 ? 0.89851 0.47829 0.57101 -0.13224 0.06146  0.08005  134 LYS B N     
2942 C  CA    . LYS B 104 ? 0.85272 0.44844 0.52583 -0.12721 0.06756  0.07872  134 LYS B CA    
2943 C  C     . LYS B 104 ? 0.88730 0.46360 0.54788 -0.11946 0.06205  0.07594  134 LYS B C     
2944 O  O     . LYS B 104 ? 0.88741 0.46256 0.53392 -0.12217 0.06337  0.07943  134 LYS B O     
2945 C  CB    . LYS B 104 ? 0.80341 0.42198 0.49763 -0.11774 0.07353  0.07240  134 LYS B CB    
2946 C  CG    . LYS B 104 ? 0.83687 0.47045 0.53007 -0.11118 0.07889  0.07045  134 LYS B CG    
2947 C  CD    . LYS B 104 ? 0.96548 0.62236 0.67649 -0.10391 0.08492  0.06549  134 LYS B CD    
2948 C  CE    . LYS B 104 ? 0.84349 0.52338 0.56020 -0.11285 0.09186  0.07010  134 LYS B CE    
2949 N  NZ    . LYS B 104 ? 0.93918 0.64353 0.66825 -0.10436 0.09837  0.06542  134 LYS B NZ    
2950 N  N     . THR B 105 ? 0.76373 0.32464 0.42828 -0.11019 0.05545  0.07007  135 THR B N     
2951 C  CA    . THR B 105 ? 0.85865 0.40273 0.51205 -0.10233 0.05005  0.06706  135 THR B CA    
2952 C  C     . THR B 105 ? 0.90315 0.42627 0.53233 -0.11065 0.04539  0.07329  135 THR B C     
2953 O  O     . THR B 105 ? 0.96448 0.48425 0.58106 -0.11006 0.04601  0.07478  135 THR B O     
2954 C  CB    . THR B 105 ? 0.79416 0.32745 0.45575 -0.09188 0.04338  0.06036  135 THR B CB    
2955 O  OG1   . THR B 105 ? 0.81400 0.36534 0.49467 -0.08332 0.04730  0.05454  135 THR B OG1   
2956 C  CG2   . THR B 105 ? 0.77593 0.28726 0.42187 -0.08599 0.03578  0.05854  135 THR B CG2   
2957 N  N     . MET B 106 ? 0.87657 0.38506 0.49777 -0.11905 0.04055  0.07740  136 MET B N     
2958 C  CA    . MET B 106 ? 0.90166 0.38712 0.49753 -0.12776 0.03495  0.08370  136 MET B CA    
2959 C  C     . MET B 106 ? 1.01878 0.51816 0.60656 -0.13888 0.04186  0.09115  136 MET B C     
2960 O  O     . MET B 106 ? 1.02910 0.51630 0.59811 -0.14145 0.03976  0.09454  136 MET B O     
2961 C  CB    . MET B 106 ? 0.96634 0.43215 0.55376 -0.13488 0.02758  0.08677  136 MET B CB    
2962 C  CG    . MET B 106 ? 1.01205 0.45743 0.59846 -0.12293 0.01825  0.08010  136 MET B CG    
2963 S  SD    . MET B 106 ? 1.04681 0.47255 0.61819 -0.11106 0.01171  0.07555  136 MET B SD    
2964 C  CE    . MET B 106 ? 1.02409 0.42816 0.56429 -0.12495 0.00840  0.08495  136 MET B CE    
2965 N  N     . MET B 107 ? 0.95678 0.48390 0.55887 -0.14456 0.05045  0.09348  137 MET B N     
2966 C  CA    . MET B 107 ? 0.95274 0.49874 0.54884 -0.15308 0.05780  0.09993  137 MET B CA    
2967 C  C     . MET B 107 ? 0.97989 0.52661 0.56989 -0.14343 0.05929  0.09684  137 MET B C     
2968 O  O     . MET B 107 ? 0.98186 0.51843 0.55249 -0.14887 0.05772  0.10201  137 MET B O     
2969 C  CB    . MET B 107 ? 0.97331 0.55326 0.58850 -0.15544 0.06732  0.10034  137 MET B CB    
2970 C  CG    . MET B 107 ? 0.84158 0.44612 0.45170 -0.16192 0.07549  0.10628  137 MET B CG    
2971 S  SD    . MET B 107 ? 0.96747 0.61401 0.59853 -0.16319 0.08651  0.10634  137 MET B SD    
2972 C  CE    . MET B 107 ? 0.91820 0.57122 0.56835 -0.14213 0.08814  0.09378  137 MET B CE    
2973 N  N     . GLY B 108 ? 0.96391 0.52016 0.56930 -0.12897 0.06133  0.08829  138 GLY B N     
2974 C  CA    . GLY B 108 ? 0.88697 0.44392 0.48706 -0.11916 0.06228  0.08483  138 GLY B CA    
2975 C  C     . GLY B 108 ? 0.92421 0.45168 0.50397 -0.11841 0.05414  0.08567  138 GLY B C     
2976 O  O     . GLY B 108 ? 0.93061 0.45586 0.49554 -0.11952 0.05512  0.08875  138 GLY B O     
2977 N  N     . ILE B 109 ? 0.90279 0.40740 0.48057 -0.11625 0.04580  0.08303  139 ILE B N     
2978 C  CA    . ILE B 109 ? 0.97194 0.44781 0.52988 -0.11365 0.03730  0.08283  139 ILE B CA    
2979 C  C     . ILE B 109 ? 1.01524 0.47978 0.55026 -0.12776 0.03625  0.09241  139 ILE B C     
2980 O  O     . ILE B 109 ? 1.09831 0.55302 0.61651 -0.12733 0.03488  0.09439  139 ILE B O     
2981 C  CB    . ILE B 109 ? 0.98310 0.43895 0.54306 -0.10764 0.02838  0.07797  139 ILE B CB    
2982 C  CG1   . ILE B 109 ? 1.00186 0.46735 0.58070 -0.09295 0.02848  0.06874  139 ILE B CG1   
2983 C  CG2   . ILE B 109 ? 1.00908 0.43280 0.54419 -0.10787 0.01870  0.07951  139 ILE B CG2   
2984 C  CD1   . ILE B 109 ? 0.97916 0.43380 0.56494 -0.08653 0.02144  0.06385  139 ILE B CD1   
2985 N  N     . GLU B 110 ? 1.02580 0.49316 0.56004 -0.14120 0.03715  0.09892  140 GLU B N     
2986 C  CA    . GLU B 110 ? 0.98995 0.44913 0.50285 -0.15705 0.03635  0.10923  140 GLU B CA    
2987 C  C     . GLU B 110 ? 1.16070 0.63941 0.66934 -0.15853 0.04412  0.11273  140 GLU B C     
2988 O  O     . GLU B 110 ? 1.16902 0.63321 0.65615 -0.16328 0.04132  0.11764  140 GLU B O     
2989 C  CB    . GLU B 110 ? 1.09483 0.56261 0.61192 -0.17181 0.03805  0.11580  140 GLU B CB    
2990 C  CG    . GLU B 110 ? 1.19071 0.65018 0.68532 -0.19071 0.03643  0.12760  140 GLU B CG    
2991 C  CD    . GLU B 110 ? 1.30657 0.77724 0.80625 -0.20632 0.03821  0.13446  140 GLU B CD    
2992 O  OE1   . GLU B 110 ? 1.27780 0.76144 0.79835 -0.20157 0.04063  0.12958  140 GLU B OE1   
2993 O  OE2   . GLU B 110 ? 1.35528 0.82761 0.84287 -0.22157 0.03640  0.14301  140 GLU B OE2   
2994 N  N     . TRP B 111 ? 1.19413 0.70528 0.72223 -0.15313 0.05354  0.10978  141 TRP B N     
2995 C  CA    . TRP B 111 ? 1.15421 0.68630 0.67808 -0.15298 0.06100  0.11272  141 TRP B CA    
2996 C  C     . TRP B 111 ? 1.09893 0.61346 0.60965 -0.14246 0.05697  0.10889  141 TRP B C     
2997 O  O     . TRP B 111 ? 1.07482 0.58445 0.56655 -0.14841 0.05706  0.11501  141 TRP B O     
2998 C  CB    . TRP B 111 ? 1.14768 0.71450 0.69378 -0.14544 0.07029  0.10830  141 TRP B CB    
2999 C  CG    . TRP B 111 ? 1.26796 0.85972 0.80978 -0.14438 0.07821  0.11124  141 TRP B CG    
3000 C  CD1   . TRP B 111 ? 1.25223 0.86938 0.79104 -0.15642 0.08525  0.11986  141 TRP B CD1   
3001 C  CD2   . TRP B 111 ? 1.23240 0.82743 0.77210 -0.13006 0.07963  0.10555  141 TRP B CD2   
3002 N  NE1   . TRP B 111 ? 1.26462 0.90162 0.79945 -0.14953 0.09122  0.11971  141 TRP B NE1   
3003 C  CE2   . TRP B 111 ? 1.26696 0.88947 0.80181 -0.13317 0.08768  0.11084  141 TRP B CE2   
3004 C  CE3   . TRP B 111 ? 1.11606 0.69412 0.65720 -0.11502 0.07455  0.09663  141 TRP B CE3   
3005 C  CZ2   . TRP B 111 ? 1.25545 0.88718 0.78594 -0.12070 0.09052  0.10709  141 TRP B CZ2   
3006 C  CZ3   . TRP B 111 ? 1.19920 0.78551 0.73630 -0.10387 0.07712  0.09316  141 TRP B CZ3   
3007 C  CH2   . TRP B 111 ? 1.19803 0.81001 0.72939 -0.10626 0.08490  0.09818  141 TRP B CH2   
3008 N  N     . VAL B 112 ? 1.08759 0.59163 0.60733 -0.12748 0.05279  0.09917  142 VAL B N     
3009 C  CA    . VAL B 112 ? 0.99485 0.48236 0.50247 -0.11736 0.04845  0.09524  142 VAL B CA    
3010 C  C     . VAL B 112 ? 1.12595 0.58358 0.60794 -0.12562 0.04089  0.10102  142 VAL B C     
3011 O  O     . VAL B 112 ? 1.02964 0.47917 0.49467 -0.12472 0.04007  0.10319  142 VAL B O     
3012 C  CB    . VAL B 112 ? 0.96534 0.44504 0.48640 -0.10194 0.04375  0.08459  142 VAL B CB    
3013 C  CG1   . VAL B 112 ? 0.91858 0.37966 0.42585 -0.09239 0.03827  0.08086  142 VAL B CG1   
3014 C  CG2   . VAL B 112 ? 0.87960 0.38672 0.42324 -0.09411 0.05060  0.07924  142 VAL B CG2   
3015 N  N     . HIS B 113 ? 1.11660 0.55632 0.59393 -0.13363 0.03480  0.10366  143 HIS B N     
3016 C  CA    . HIS B 113 ? 1.11995 0.52713 0.57075 -0.14069 0.02595  0.10859  143 HIS B CA    
3017 C  C     . HIS B 113 ? 1.14274 0.55436 0.57585 -0.15685 0.02947  0.12000  143 HIS B C     
3018 O  O     . HIS B 113 ? 1.08840 0.47824 0.49767 -0.16018 0.02443  0.12392  143 HIS B O     
3019 C  CB    . HIS B 113 ? 1.15287 0.53937 0.60195 -0.14449 0.01787  0.10834  143 HIS B CB    
3020 C  CG    . HIS B 113 ? 1.20341 0.55601 0.62306 -0.15426 0.00836  0.11474  143 HIS B CG    
3021 N  ND1   . HIS B 113 ? 1.15519 0.48005 0.55467 -0.14703 0.00041  0.11228  143 HIS B ND1   
3022 C  CD2   . HIS B 113 ? 1.19288 0.53639 0.60100 -0.17009 0.00463  0.12261  143 HIS B CD2   
3023 C  CE1   . HIS B 113 ? 1.29581 0.60021 0.67576 -0.15639 -0.00802 0.11667  143 HIS B CE1   
3024 N  NE2   . HIS B 113 ? 1.21515 0.53406 0.60307 -0.16971 -0.00600 0.12184  143 HIS B NE2   
3025 N  N     . ARG B 114 ? 1.18356 0.62419 0.62769 -0.16715 0.03800  0.12564  144 ARG B N     
3026 C  CA    . ARG B 114 ? 1.15734 0.60537 0.58552 -0.18444 0.04125  0.13753  144 ARG B CA    
3027 C  C     . ARG B 114 ? 1.18644 0.65856 0.61364 -0.18034 0.04964  0.13883  144 ARG B C     
3028 O  O     . ARG B 114 ? 1.28684 0.75088 0.69265 -0.18793 0.04863  0.14595  144 ARG B O     
3029 C  CB    . ARG B 114 ? 1.19463 0.66386 0.63362 -0.19899 0.04596  0.14400  144 ARG B CB    
3030 C  CG    . ARG B 114 ? 1.17556 0.61917 0.61013 -0.20676 0.03698  0.14530  144 ARG B CG    
3031 C  CD    . ARG B 114 ? 1.31349 0.77852 0.75503 -0.22407 0.04105  0.15353  144 ARG B CD    
3032 N  NE    . ARG B 114 ? 1.50321 0.95610 0.95324 -0.22539 0.03256  0.14991  144 ARG B NE    
3033 C  CZ    . ARG B 114 ? 1.47219 0.90138 0.91027 -0.22957 0.02033  0.14979  144 ARG B CZ    
3034 N  NH1   . ARG B 114 ? 1.30504 0.71871 0.72263 -0.23350 0.01481  0.15305  144 ARG B NH1   
3035 N  NH2   . ARG B 114 ? 1.59420 1.01458 1.03987 -0.22925 0.01333  0.14607  144 ARG B NH2   
3036 N  N     . PHE B 115 ? 1.24489 0.74552 0.69350 -0.16806 0.05739  0.13205  145 PHE B N     
3037 C  CA    . PHE B 115 ? 1.13873 0.66764 0.58755 -0.16468 0.06616  0.13381  145 PHE B CA    
3038 C  C     . PHE B 115 ? 1.16830 0.69582 0.62106 -0.14478 0.06619  0.12390  145 PHE B C     
3039 O  O     . PHE B 115 ? 1.26518 0.81356 0.71581 -0.13994 0.07254  0.12465  145 PHE B O     
3040 C  CB    . PHE B 115 ? 1.15049 0.71916 0.61814 -0.16859 0.07604  0.13587  145 PHE B CB    
3041 C  CG    . PHE B 115 ? 1.30615 0.87822 0.77271 -0.18804 0.07588  0.14502  145 PHE B CG    
3042 C  CD1   . PHE B 115 ? 1.42567 0.99585 0.87225 -0.20615 0.07542  0.15724  145 PHE B CD1   
3043 C  CD2   . PHE B 115 ? 1.28082 0.85705 0.76549 -0.18886 0.07564  0.14174  145 PHE B CD2   
3044 C  CE1   . PHE B 115 ? 1.43845 1.01035 0.88292 -0.22528 0.07426  0.16613  145 PHE B CE1   
3045 C  CE2   . PHE B 115 ? 1.27950 0.85786 0.76260 -0.20686 0.07486  0.15011  145 PHE B CE2   
3046 C  CZ    . PHE B 115 ? 1.31357 0.88942 0.77637 -0.22538 0.07391  0.16237  145 PHE B CZ    
3047 N  N     . CYS B 116 ? 1.11962 0.62419 0.57727 -0.13323 0.05905  0.11495  146 CYS B N     
3048 C  CA    . CYS B 116 ? 1.09967 0.60323 0.56007 -0.11579 0.05856  0.10628  146 CYS B CA    
3049 C  C     . CYS B 116 ? 1.16033 0.63043 0.61482 -0.10743 0.04824  0.09982  146 CYS B C     
3050 O  O     . CYS B 116 ? 1.14455 0.61409 0.61252 -0.09372 0.04621  0.09047  146 CYS B O     
3051 C  CB    . CYS B 116 ? 1.04600 0.57559 0.53030 -0.10499 0.06436  0.09903  146 CYS B CB    
3052 S  SG    . CYS B 116 ? 1.44618 0.98622 0.93089 -0.08672 0.06686  0.09157  146 CYS B SG    
3053 N  N     . PRO B 117 ? 1.13494 0.57692 0.56857 -0.11511 0.04110  0.10455  147 PRO B N     
3054 C  CA    . PRO B 117 ? 1.07501 0.48619 0.50151 -0.10574 0.03095  0.09805  147 PRO B CA    
3055 C  C     . PRO B 117 ? 1.18447 0.59096 0.60514 -0.09220 0.02961  0.09238  147 PRO B C     
3056 O  O     . PRO B 117 ? 1.11559 0.50058 0.53267 -0.08267 0.02159  0.08600  147 PRO B O     
3057 C  CB    . PRO B 117 ? 1.13361 0.51682 0.53577 -0.11840 0.02399  0.10568  147 PRO B CB    
3058 C  CG    . PRO B 117 ? 1.08019 0.47865 0.47139 -0.13255 0.03082  0.11643  147 PRO B CG    
3059 C  CD    . PRO B 117 ? 1.14132 0.57817 0.55566 -0.13281 0.04140  0.11622  147 PRO B CD    
3060 N  N     . GLN B 118 ? 1.23068 0.65690 0.64967 -0.09066 0.03679  0.09445  148 GLN B N     
3061 C  CA    . GLN B 118 ? 1.14618 0.56923 0.56027 -0.07704 0.03560  0.08870  148 GLN B CA    
3062 C  C     . GLN B 118 ? 1.18699 0.62218 0.62273 -0.06278 0.03619  0.07862  148 GLN B C     
3063 O  O     . GLN B 118 ? 1.17254 0.60190 0.60553 -0.05066 0.03333  0.07263  148 GLN B O     
3064 C  CB    . GLN B 118 ? 1.12878 0.56868 0.53132 -0.07992 0.04277  0.09478  148 GLN B CB    
3065 C  CG    . GLN B 118 ? 1.21483 0.64499 0.59467 -0.09578 0.04256  0.10612  148 GLN B CG    
3066 C  CD    . GLN B 118 ? 1.24695 0.69354 0.63262 -0.11208 0.04755  0.11442  148 GLN B CD    
3067 O  OE1   . GLN B 118 ? 1.28823 0.75456 0.69526 -0.11093 0.05174  0.11151  148 GLN B OE1   
3068 N  NE2   . GLN B 118 ? 1.25173 0.68960 0.61763 -0.12794 0.04666  0.12508  148 GLN B NE2   
3069 N  N     . ALA B 119 ? 1.10074 0.55168 0.55708 -0.06426 0.03930  0.07676  149 ALA B N     
3070 C  CA    . ALA B 119 ? 1.06825 0.53076 0.54444 -0.05206 0.03970  0.06791  149 ALA B CA    
3071 C  C     . ALA B 119 ? 1.08419 0.52501 0.56121 -0.04248 0.03035  0.06047  149 ALA B C     
3072 O  O     . ALA B 119 ? 1.08723 0.51090 0.56217 -0.04575 0.02438  0.06055  149 ALA B O     
3073 C  CB    . ALA B 119 ? 0.98755 0.46799 0.48416 -0.05671 0.04399  0.06791  149 ALA B CB    
3074 N  N     . ALA B 120 ? 0.97809 0.41981 0.45712 -0.03027 0.02855  0.05400  150 ALA B N     
3075 C  CA    . ALA B 120 ? 0.93552 0.35980 0.41629 -0.02147 0.01964  0.04707  150 ALA B CA    
3076 C  C     . ALA B 120 ? 0.99783 0.42694 0.49938 -0.02085 0.01746  0.04299  150 ALA B C     
3077 O  O     . ALA B 120 ? 0.97336 0.38779 0.47511 -0.01912 0.01036  0.04041  150 ALA B O     
3078 C  CB    . ALA B 120 ? 0.93613 0.36118 0.41518 -0.00940 0.01779  0.04124  150 ALA B CB    
3079 N  N     . PHE B 121 ? 0.90115 0.35141 0.41960 -0.02173 0.02343  0.04236  151 PHE B N     
3080 C  CA    . PHE B 121 ? 0.91167 0.36841 0.45041 -0.02111 0.02196  0.03866  151 PHE B CA    
3081 C  C     . PHE B 121 ? 0.91350 0.39078 0.46414 -0.02803 0.03008  0.04209  151 PHE B C     
3082 O  O     . PHE B 121 ? 0.94587 0.43757 0.49340 -0.02928 0.03684  0.04482  151 PHE B O     
3083 C  CB    . PHE B 121 ? 0.86561 0.32465 0.41551 -0.01038 0.01769  0.03090  151 PHE B CB    
3084 C  CG    . PHE B 121 ? 0.87463 0.31546 0.41515 -0.00366 0.00917  0.02716  151 PHE B CG    
3085 C  CD1   . PHE B 121 ? 0.87231 0.30288 0.41638 -0.00300 0.00247  0.02508  151 PHE B CD1   
3086 C  CD2   . PHE B 121 ? 0.88782 0.32243 0.41513 0.00261  0.00771  0.02565  151 PHE B CD2   
3087 C  CE1   . PHE B 121 ? 0.88254 0.29802 0.41762 0.00372  -0.00550 0.02149  151 PHE B CE1   
3088 C  CE2   . PHE B 121 ? 0.89792 0.31611 0.41641 0.00889  -0.00030 0.02209  151 PHE B CE2   
3089 C  CZ    . PHE B 121 ? 0.95971 0.36883 0.48222 0.00942  -0.00688 0.01998  151 PHE B CZ    
3090 N  N     . VAL B 122 ? 0.85016 0.32933 0.41403 -0.03199 0.02917  0.04183  152 VAL B N     
3091 C  CA    . VAL B 122 ? 0.83702 0.33453 0.41350 -0.03863 0.03601  0.04465  152 VAL B CA    
3092 C  C     . VAL B 122 ? 0.81544 0.31985 0.41271 -0.03407 0.03409  0.03906  152 VAL B C     
3093 O  O     . VAL B 122 ? 0.82741 0.32042 0.42838 -0.03146 0.02742  0.03610  152 VAL B O     
3094 C  CB    . VAL B 122 ? 0.84697 0.33853 0.41660 -0.05062 0.03681  0.05155  152 VAL B CB    
3095 C  CG1   . VAL B 122 ? 0.85929 0.37141 0.44270 -0.05763 0.04395  0.05442  152 VAL B CG1   
3096 C  CG2   . VAL B 122 ? 0.88851 0.37078 0.43575 -0.05641 0.03753  0.05778  152 VAL B CG2   
3097 N  N     . MET B 123 ? 0.80130 0.32469 0.41129 -0.03270 0.03962  0.03762  153 MET B N     
3098 C  CA    . MET B 123 ? 0.83259 0.36398 0.46222 -0.03028 0.03869  0.03346  153 MET B CA    
3099 C  C     . MET B 123 ? 0.80169 0.34877 0.44113 -0.03775 0.04550  0.03699  153 MET B C     
3100 O  O     . MET B 123 ? 0.80172 0.36326 0.43890 -0.03975 0.05231  0.03956  153 MET B O     
3101 C  CB    . MET B 123 ? 0.77381 0.31154 0.40996 -0.02108 0.03767  0.02768  153 MET B CB    
3102 C  CG    . MET B 123 ? 0.82476 0.37214 0.48037 -0.01994 0.03743  0.02430  153 MET B CG    
3103 S  SD    . MET B 123 ? 0.89142 0.43987 0.55184 -0.00987 0.03318  0.01754  153 MET B SD    
3104 C  CE    . MET B 123 ? 0.97590 0.53169 0.65832 -0.01166 0.03138  0.01520  153 MET B CE    
3105 N  N     . LYS B 124 ? 0.80505 0.35028 0.45508 -0.04133 0.04349  0.03703  154 LYS B N     
3106 C  CA    . LYS B 124 ? 0.77593 0.33588 0.43792 -0.04750 0.04907  0.03936  154 LYS B CA    
3107 C  C     . LYS B 124 ? 0.78149 0.35162 0.46199 -0.04159 0.04881  0.03387  154 LYS B C     
3108 O  O     . LYS B 124 ? 0.78437 0.34687 0.47149 -0.03735 0.04271  0.03014  154 LYS B O     
3109 C  CB    . LYS B 124 ? 0.77522 0.32514 0.43524 -0.05524 0.04654  0.04315  154 LYS B CB    
3110 C  CG    . LYS B 124 ? 0.85328 0.41665 0.52660 -0.06148 0.05111  0.04515  154 LYS B CG    
3111 C  CD    . LYS B 124 ? 0.81218 0.37496 0.50128 -0.05680 0.04708  0.04049  154 LYS B CD    
3112 C  CE    . LYS B 124 ? 0.86827 0.44839 0.57387 -0.05953 0.05239  0.04043  154 LYS B CE    
3113 N  NZ    . LYS B 124 ? 0.98495 0.56412 0.70477 -0.05488 0.04808  0.03623  154 LYS B NZ    
3114 N  N     . THR B 125 ? 0.72977 0.31766 0.41778 -0.04132 0.05519  0.03356  155 THR B N     
3115 C  CA    . THR B 125 ? 0.83519 0.43157 0.53774 -0.03522 0.05479  0.02833  155 THR B CA    
3116 C  C     . THR B 125 ? 0.76986 0.38424 0.48400 -0.03869 0.06146  0.02943  155 THR B C     
3117 O  O     . THR B 125 ? 0.72828 0.35290 0.43792 -0.04427 0.06755  0.03381  155 THR B O     
3118 C  CB    . THR B 125 ? 0.85976 0.45625 0.55600 -0.02641 0.05360  0.02434  155 THR B CB    
3119 O  OG1   . THR B 125 ? 0.87793 0.47763 0.58632 -0.02101 0.05093  0.01929  155 THR B OG1   
3120 C  CG2   . THR B 125 ? 0.74890 0.35919 0.43702 -0.02608 0.06083  0.02652  155 THR B CG2   
3121 N  N     . ASP B 126 ? 0.79176 0.41060 0.52014 -0.03505 0.06001  0.02536  156 ASP B N     
3122 C  CA    . ASP B 126 ? 0.76719 0.40281 0.50713 -0.03678 0.06584  0.02539  156 ASP B CA    
3123 C  C     . ASP B 126 ? 0.79566 0.44227 0.53128 -0.03016 0.06947  0.02285  156 ASP B C     
3124 O  O     . ASP B 126 ? 0.82650 0.46592 0.55146 -0.02412 0.06652  0.02075  156 ASP B O     
3125 C  CB    . ASP B 126 ? 0.87091 0.50600 0.62687 -0.03620 0.06261  0.02264  156 ASP B CB    
3126 C  CG    . ASP B 126 ? 0.89023 0.51741 0.65012 -0.04173 0.05963  0.02513  156 ASP B CG    
3127 O  OD1   . ASP B 126 ? 0.88184 0.50295 0.63155 -0.04708 0.06019  0.02933  156 ASP B OD1   
3128 O  OD2   . ASP B 126 ? 0.97898 0.60605 0.75113 -0.04049 0.05644  0.02296  156 ASP B OD2   
3129 N  N     . SER B 127 ? 0.88305 0.54633 0.62616 -0.03041 0.07518  0.02267  157 SER B N     
3130 C  CA    . SER B 127 ? 0.87823 0.55413 0.61614 -0.02313 0.07894  0.02017  157 SER B CA    
3131 C  C     . SER B 127 ? 0.93650 0.60875 0.67916 -0.01411 0.07465  0.01376  157 SER B C     
3132 O  O     . SER B 127 ? 0.92772 0.60240 0.66135 -0.00537 0.07442  0.01042  157 SER B O     
3133 C  CB    . SER B 127 ? 0.77849 0.47618 0.52073 -0.02738 0.08727  0.02317  157 SER B CB    
3134 O  OG    . SER B 127 ? 0.89162 0.59356 0.64935 -0.03046 0.08795  0.02236  157 SER B OG    
3135 N  N     . ASP B 128 ? 0.78238 0.44859 0.53784 -0.01583 0.07079  0.01205  158 ASP B N     
3136 C  CA    . ASP B 128 ? 0.86300 0.52400 0.62217 -0.00889 0.06572  0.00668  158 ASP B CA    
3137 C  C     . ASP B 128 ? 0.83529 0.47804 0.58932 -0.00656 0.05705  0.00480  158 ASP B C     
3138 O  O     . ASP B 128 ? 0.75119 0.38644 0.51415 -0.00824 0.05143  0.00363  158 ASP B O     
3139 C  CB    . ASP B 128 ? 0.88739 0.55365 0.66300 -0.01227 0.06629  0.00618  158 ASP B CB    
3140 C  CG    . ASP B 128 ? 0.90569 0.56720 0.69060 -0.02014 0.06467  0.00942  158 ASP B CG    
3141 O  OD1   . ASP B 128 ? 0.87901 0.53836 0.65823 -0.02483 0.06625  0.01323  158 ASP B OD1   
3142 O  OD2   . ASP B 128 ? 0.92768 0.58733 0.72445 -0.02130 0.06141  0.00820  158 ASP B OD2   
3143 N  N     . MET B 129 ? 0.71386 0.35093 0.45302 -0.00261 0.05603  0.00470  159 MET B N     
3144 C  CA    . MET B 129 ? 0.75072 0.37121 0.48308 -0.00093 0.04841  0.00357  159 MET B CA    
3145 C  C     . MET B 129 ? 0.71628 0.33062 0.43347 0.00841  0.04530  -0.00001 159 MET B C     
3146 O  O     . MET B 129 ? 0.78130 0.40521 0.48976 0.01315  0.05043  -0.00026 159 MET B O     
3147 C  CB    . MET B 129 ? 0.77577 0.39169 0.50314 -0.00651 0.04941  0.00788  159 MET B CB    
3148 C  CG    . MET B 129 ? 0.84741 0.46477 0.58646 -0.01478 0.05037  0.01118  159 MET B CG    
3149 S  SD    . MET B 129 ? 0.87256 0.48028 0.62298 -0.01554 0.04173  0.00911  159 MET B SD    
3150 C  CE    . MET B 129 ? 0.82268 0.41441 0.55975 -0.01363 0.03530  0.00917  159 MET B CE    
3151 N  N     . PHE B 130 ? 0.73848 0.33752 0.45227 0.01121  0.03651  -0.00276 160 PHE B N     
3152 C  CA    . PHE B 130 ? 0.71766 0.30635 0.41491 0.01913  0.03205  -0.00549 160 PHE B CA    
3153 C  C     . PHE B 130 ? 0.71946 0.29847 0.41133 0.01616  0.02934  -0.00324 160 PHE B C     
3154 O  O     . PHE B 130 ? 0.71280 0.28568 0.41325 0.01102  0.02484  -0.00241 160 PHE B O     
3155 C  CB    . PHE B 130 ? 0.71869 0.29500 0.41380 0.02429  0.02278  -0.01027 160 PHE B CB    
3156 C  CG    . PHE B 130 ? 0.78456 0.34619 0.46287 0.03150  0.01593  -0.01304 160 PHE B CG    
3157 C  CD1   . PHE B 130 ? 0.75292 0.31446 0.41568 0.04176  0.01660  -0.01607 160 PHE B CD1   
3158 C  CD2   . PHE B 130 ? 0.74119 0.28993 0.41889 0.02869  0.00864  -0.01279 160 PHE B CD2   
3159 C  CE1   . PHE B 130 ? 0.77040 0.31765 0.41675 0.04913  0.00993  -0.01880 160 PHE B CE1   
3160 C  CE2   . PHE B 130 ? 0.83852 0.37344 0.50066 0.03527  0.00210  -0.01539 160 PHE B CE2   
3161 C  CZ    . PHE B 130 ? 0.82029 0.35370 0.46658 0.04549  0.00267  -0.01841 160 PHE B CZ    
3162 N  N     . ILE B 131 ? 0.78897 0.36750 0.46628 0.01986  0.03198  -0.00228 161 ILE B N     
3163 C  CA    . ILE B 131 ? 0.74172 0.30938 0.41082 0.01839  0.02905  -0.00055 161 ILE B CA    
3164 C  C     . ILE B 131 ? 0.75914 0.31608 0.41205 0.02769  0.02384  -0.00409 161 ILE B C     
3165 O  O     . ILE B 131 ? 0.83641 0.39957 0.47899 0.03462  0.02727  -0.00531 161 ILE B O     
3166 C  CB    . ILE B 131 ? 0.74365 0.31871 0.40852 0.01284  0.03665  0.00487  161 ILE B CB    
3167 C  CG1   . ILE B 131 ? 0.76966 0.35464 0.44906 0.00385  0.04153  0.00838  161 ILE B CG1   
3168 C  CG2   . ILE B 131 ? 0.77380 0.33480 0.42885 0.01176  0.03252  0.00632  161 ILE B CG2   
3169 C  CD1   . ILE B 131 ? 0.78112 0.35707 0.47040 -0.00107 0.03609  0.00866  161 ILE B CD1   
3170 N  N     . ASN B 132 ? 0.79965 0.34146 0.45008 0.02826  0.01538  -0.00578 162 ASN B N     
3171 C  CA    . ASN B 132 ? 0.81693 0.34595 0.45122 0.03644  0.00936  -0.00891 162 ASN B CA    
3172 C  C     . ASN B 132 ? 0.82311 0.34829 0.44729 0.03521  0.01153  -0.00582 162 ASN B C     
3173 O  O     . ASN B 132 ? 0.82046 0.33617 0.44614 0.03185  0.00678  -0.00520 162 ASN B O     
3174 C  CB    . ASN B 132 ? 0.78405 0.29913 0.42129 0.03709  -0.00179 -0.01238 162 ASN B CB    
3175 C  CG    . ASN B 132 ? 0.83142 0.33218 0.45140 0.04614  -0.00901 -0.01620 162 ASN B CG    
3176 O  OD1   . ASN B 132 ? 0.85942 0.35947 0.46516 0.05166  -0.00588 -0.01588 162 ASN B OD1   
3177 N  ND2   . ASN B 132 ? 0.80765 0.29690 0.42828 0.04733  -0.01907 -0.01956 162 ASN B ND2   
3178 N  N     . VAL B 133 ? 0.80773 0.34113 0.42081 0.03817  0.01863  -0.00378 163 VAL B N     
3179 C  CA    . VAL B 133 ? 0.93259 0.46279 0.53448 0.03629  0.02124  -0.00010 163 VAL B CA    
3180 C  C     . VAL B 133 ? 0.92067 0.43411 0.50889 0.04328  0.01344  -0.00321 163 VAL B C     
3181 O  O     . VAL B 133 ? 0.93149 0.43619 0.51323 0.04084  0.01202  -0.00112 163 VAL B O     
3182 C  CB    . VAL B 133 ? 0.88977 0.43615 0.48372 0.03683  0.03099  0.00352  163 VAL B CB    
3183 C  CG1   . VAL B 133 ? 1.00621 0.54829 0.58633 0.03456  0.03317  0.00779  163 VAL B CG1   
3184 C  CG2   . VAL B 133 ? 0.79937 0.36208 0.40713 0.02859  0.03834  0.00706  163 VAL B CG2   
3185 N  N     . ASP B 134 ? 0.92321 0.43071 0.50575 0.05220  0.00773  -0.00831 164 ASP B N     
3186 C  CA    . ASP B 134 ? 0.91329 0.40395 0.48286 0.05886  -0.00060 -0.01155 164 ASP B CA    
3187 C  C     . ASP B 134 ? 0.85308 0.33187 0.43084 0.05352  -0.00845 -0.01217 164 ASP B C     
3188 O  O     . ASP B 134 ? 0.94177 0.41088 0.51169 0.05374  -0.01135 -0.01154 164 ASP B O     
3189 C  CB    . ASP B 134 ? 0.98058 0.46571 0.54190 0.06926  -0.00629 -0.01702 164 ASP B CB    
3190 C  CG    . ASP B 134 ? 1.31233 0.81186 0.86564 0.07617  0.00132  -0.01699 164 ASP B CG    
3191 O  OD1   . ASP B 134 ? 1.27279 0.77467 0.81093 0.08234  0.00453  -0.01616 164 ASP B OD1   
3192 O  OD2   . ASP B 134 ? 1.35275 0.86279 0.91503 0.07553  0.00431  -0.01764 164 ASP B OD2   
3193 N  N     . TYR B 135 ? 0.82987 0.31053 0.42331 0.04880  -0.01189 -0.01325 165 TYR B N     
3194 C  CA    . TYR B 135 ? 0.85779 0.33125 0.45995 0.04383  -0.01910 -0.01357 165 TYR B CA    
3195 C  C     . TYR B 135 ? 0.90329 0.38060 0.51003 0.03726  -0.01449 -0.00940 165 TYR B C     
3196 O  O     . TYR B 135 ? 0.89841 0.36746 0.50335 0.03651  -0.01974 -0.00962 165 TYR B O     
3197 C  CB    . TYR B 135 ? 0.81193 0.28862 0.42960 0.03988  -0.02361 -0.01509 165 TYR B CB    
3198 C  CG    . TYR B 135 ? 0.80907 0.27964 0.43437 0.03614  -0.03301 -0.01609 165 TYR B CG    
3199 C  CD1   . TYR B 135 ? 0.82342 0.28048 0.43830 0.04039  -0.04212 -0.01889 165 TYR B CD1   
3200 C  CD2   . TYR B 135 ? 0.80424 0.28404 0.44722 0.02859  -0.03300 -0.01424 165 TYR B CD2   
3201 C  CE1   . TYR B 135 ? 0.92471 0.37900 0.54706 0.03653  -0.05080 -0.01953 165 TYR B CE1   
3202 C  CE2   . TYR B 135 ? 0.86009 0.33807 0.51052 0.02533  -0.04141 -0.01489 165 TYR B CE2   
3203 C  CZ    . TYR B 135 ? 0.95180 0.41762 0.59210 0.02901  -0.05031 -0.01744 165 TYR B CZ    
3204 O  OH    . TYR B 135 ? 1.04336 0.51003 0.69156 0.02529  -0.05879 -0.01781 165 TYR B OH    
3205 N  N     . LEU B 136 ? 0.87895 0.36818 0.49086 0.03260  -0.00539 -0.00570 166 LEU B N     
3206 C  CA    . LEU B 136 ? 0.80571 0.29579 0.41939 0.02631  -0.00196 -0.00163 166 LEU B CA    
3207 C  C     . LEU B 136 ? 0.90898 0.38842 0.50499 0.02902  -0.00244 -0.00038 166 LEU B C     
3208 O  O     . LEU B 136 ? 0.82589 0.29703 0.41966 0.02707  -0.00592 0.00045  166 LEU B O     
3209 C  CB    . LEU B 136 ? 0.79633 0.30004 0.41630 0.02050  0.00751  0.00244  166 LEU B CB    
3210 C  CG    . LEU B 136 ? 0.79699 0.29880 0.41514 0.01377  0.01048  0.00706  166 LEU B CG    
3211 C  CD1   . LEU B 136 ? 0.78983 0.28589 0.41717 0.01164  0.00399  0.00590  166 LEU B CD1   
3212 C  CD2   . LEU B 136 ? 0.80370 0.31882 0.42749 0.00724  0.01926  0.01134  166 LEU B CD2   
3213 N  N     . THR B 137 ? 0.94536 0.42544 0.52780 0.03407  0.00107  -0.00020 167 THR B N     
3214 C  CA    . THR B 137 ? 0.99659 0.46654 0.56092 0.03732  0.00048  0.00094  167 THR B CA    
3215 C  C     . THR B 137 ? 0.99150 0.44606 0.55148 0.04205  -0.00961 -0.00311 167 THR B C     
3216 O  O     . THR B 137 ? 0.96424 0.40877 0.51645 0.04124  -0.01212 -0.00196 167 THR B O     
3217 C  CB    . THR B 137 ? 0.91063 0.38621 0.46208 0.04366  0.00517  0.00101  167 THR B CB    
3218 O  OG1   . THR B 137 ? 1.00015 0.49186 0.55415 0.03839  0.01498  0.00572  167 THR B OG1   
3219 C  CG2   . THR B 137 ? 1.03942 0.50372 0.57161 0.04822  0.00350  0.00161  167 THR B CG2   
3220 N  N     . GLU B 138 ? 0.96627 0.41824 0.52994 0.04701  -0.01598 -0.00782 168 GLU B N     
3221 C  CA    . GLU B 138 ? 0.87911 0.31798 0.43964 0.05064  -0.02621 -0.01154 168 GLU B CA    
3222 C  C     . GLU B 138 ? 0.92636 0.36416 0.49691 0.04507  -0.02975 -0.01069 168 GLU B C     
3223 O  O     . GLU B 138 ? 0.99772 0.42536 0.56043 0.04719  -0.03479 -0.01155 168 GLU B O     
3224 C  CB    . GLU B 138 ? 0.91335 0.35033 0.47815 0.05435  -0.03297 -0.01594 168 GLU B CB    
3225 C  CG    . GLU B 138 ? 0.99918 0.42509 0.56426 0.05588  -0.04454 -0.01944 168 GLU B CG    
3226 C  CD    . GLU B 138 ? 1.34917 0.77143 0.91638 0.05828  -0.05179 -0.02309 168 GLU B CD    
3227 O  OE1   . GLU B 138 ? 1.45052 0.87428 1.01203 0.06268  -0.04859 -0.02403 168 GLU B OE1   
3228 O  OE2   . GLU B 138 ? 1.37691 0.79499 0.95076 0.05570  -0.06108 -0.02491 168 GLU B OE2   
3229 N  N     . LEU B 139 ? 0.97728 0.42598 0.56433 0.03869  -0.02710 -0.00910 169 LEU B N     
3230 C  CA    . LEU B 139 ? 0.83230 0.28190 0.42909 0.03476  -0.03089 -0.00872 169 LEU B CA    
3231 C  C     . LEU B 139 ? 0.83885 0.28329 0.42655 0.03301  -0.02748 -0.00547 169 LEU B C     
3232 O  O     . LEU B 139 ? 0.91082 0.34941 0.49711 0.03389  -0.03288 -0.00635 169 LEU B O     
3233 C  CB    . LEU B 139 ? 0.87522 0.33821 0.49167 0.02907  -0.02917 -0.00796 169 LEU B CB    
3234 C  CG    . LEU B 139 ? 0.85388 0.32048 0.48043 0.02931  -0.03484 -0.01094 169 LEU B CG    
3235 C  CD1   . LEU B 139 ? 0.90760 0.38780 0.55285 0.02332  -0.03219 -0.00959 169 LEU B CD1   
3236 C  CD2   . LEU B 139 ? 0.84283 0.30324 0.46901 0.03124  -0.04529 -0.01375 169 LEU B CD2   
3237 N  N     . LEU B 140 ? 0.84245 0.28904 0.42312 0.03044  -0.01911 -0.00162 170 LEU B N     
3238 C  CA    . LEU B 140 ? 0.94781 0.38703 0.51746 0.02758  -0.01668 0.00211  170 LEU B CA    
3239 C  C     . LEU B 140 ? 0.96291 0.38700 0.51409 0.03312  -0.02112 0.00094  170 LEU B C     
3240 O  O     . LEU B 140 ? 0.93748 0.35113 0.48103 0.03319  -0.02474 0.00146  170 LEU B O     
3241 C  CB    . LEU B 140 ? 0.85255 0.29885 0.41847 0.02219  -0.00700 0.00722  170 LEU B CB    
3242 C  CG    . LEU B 140 ? 0.85120 0.31140 0.43384 0.01574  -0.00204 0.00918  170 LEU B CG    
3243 C  CD1   . LEU B 140 ? 0.83661 0.30626 0.41510 0.01153  0.00717  0.01362  170 LEU B CD1   
3244 C  CD2   . LEU B 140 ? 0.83103 0.28696 0.41795 0.01139  -0.00451 0.01069  170 LEU B CD2   
3245 N  N     . LEU B 141 ? 0.91438 0.33640 0.45721 0.03860  -0.02136 -0.00095 171 LEU B N     
3246 C  CA    . LEU B 141 ? 0.95682 0.36446 0.48260 0.04476  -0.02621 -0.00266 171 LEU B CA    
3247 C  C     . LEU B 141 ? 0.89676 0.29757 0.42682 0.04812  -0.03617 -0.00700 171 LEU B C     
3248 O  O     . LEU B 141 ? 0.94125 0.33047 0.46041 0.05037  -0.04019 -0.00730 171 LEU B O     
3249 C  CB    . LEU B 141 ? 0.90621 0.31414 0.42329 0.05100  -0.02510 -0.00440 171 LEU B CB    
3250 C  CG    . LEU B 141 ? 0.95386 0.37007 0.46346 0.04856  -0.01511 0.00035  171 LEU B CG    
3251 C  CD1   . LEU B 141 ? 1.05737 0.47844 0.56156 0.05583  -0.01374 -0.00199 171 LEU B CD1   
3252 C  CD2   . LEU B 141 ? 0.92708 0.33365 0.41875 0.04690  -0.01289 0.00453  171 LEU B CD2   
3253 N  N     . LYS B 142 ? 0.88435 0.29251 0.42955 0.04840  -0.04072 -0.01028 172 LYS B N     
3254 C  CA    . LYS B 142 ? 0.88313 0.28836 0.43348 0.05075  -0.05036 -0.01392 172 LYS B CA    
3255 C  C     . LYS B 142 ? 0.98546 0.39230 0.54048 0.04792  -0.05113 -0.01254 172 LYS B C     
3256 O  O     . LYS B 142 ? 1.01825 0.41721 0.56620 0.05197  -0.05748 -0.01458 172 LYS B O     
3257 C  CB    . LYS B 142 ? 0.95317 0.36735 0.51937 0.04966  -0.05542 -0.01672 172 LYS B CB    
3258 C  CG    . LYS B 142 ? 1.23697 0.65717 0.81549 0.04819  -0.06273 -0.01841 172 LYS B CG    
3259 C  CD    . LYS B 142 ? 1.31223 0.73884 0.90279 0.04675  -0.06998 -0.02093 172 LYS B CD    
3260 C  CE    . LYS B 142 ? 1.44778 0.88761 1.05475 0.04303  -0.07433 -0.02097 172 LYS B CE    
3261 N  NZ    . LYS B 142 ? 1.35364 0.79721 0.96203 0.04237  -0.06970 -0.01888 172 LYS B NZ    
3262 N  N     . LYS B 143 ? 0.99354 0.41008 0.55950 0.04203  -0.04551 -0.00960 173 LYS B N     
3263 C  CA    . LYS B 143 ? 0.86103 0.27860 0.43075 0.04038  -0.04702 -0.00868 173 LYS B CA    
3264 C  C     . LYS B 143 ? 0.91609 0.31737 0.46557 0.04281  -0.04763 -0.00729 173 LYS B C     
3265 O  O     . LYS B 143 ? 0.88585 0.28213 0.43196 0.04604  -0.05339 -0.00889 173 LYS B O     
3266 C  CB    . LYS B 143 ? 0.88639 0.31513 0.46871 0.03368  -0.04028 -0.00540 173 LYS B CB    
3267 C  CG    . LYS B 143 ? 0.89144 0.32134 0.47770 0.03269  -0.04229 -0.00469 173 LYS B CG    
3268 C  CD    . LYS B 143 ? 0.93903 0.37834 0.53807 0.03607  -0.05008 -0.00845 173 LYS B CD    
3269 C  CE    . LYS B 143 ? 1.04600 0.49259 0.65371 0.03513  -0.05076 -0.00776 173 LYS B CE    
3270 N  NZ    . LYS B 143 ? 1.13470 0.59626 0.75775 0.03761  -0.05733 -0.01081 173 LYS B NZ    
3271 N  N     . ASN B 144 ? 0.89253 0.28531 0.42705 0.04195  -0.04243 -0.00446 174 ASN B N     
3272 C  CA    . ASN B 144 ? 0.91372 0.28875 0.42617 0.04390  -0.04363 -0.00276 174 ASN B CA    
3273 C  C     . ASN B 144 ? 0.91635 0.28569 0.42554 0.04077  -0.04429 -0.00039 174 ASN B C     
3274 O  O     . ASN B 144 ? 0.94278 0.29758 0.43764 0.04503  -0.05003 -0.00153 174 ASN B O     
3275 C  CB    . ASN B 144 ? 0.92564 0.29074 0.42840 0.05209  -0.05147 -0.00722 174 ASN B CB    
3276 C  CG    . ASN B 144 ? 0.94898 0.29535 0.42741 0.05461  -0.05205 -0.00553 174 ASN B CG    
3277 O  OD1   . ASN B 144 ? 0.99055 0.33341 0.45797 0.05169  -0.04579 -0.00158 174 ASN B OD1   
3278 N  ND2   . ASN B 144 ? 0.95922 0.29456 0.42893 0.06011  -0.05967 -0.00839 174 ASN B ND2   
3279 N  N     . ARG B 145 ? 0.94538 0.32477 0.46630 0.03416  -0.03916 0.00256  175 ARG B N     
3280 C  CA    . ARG B 145 ? 0.90785 0.28021 0.42398 0.03092  -0.03989 0.00514  175 ARG B CA    
3281 C  C     . ARG B 145 ? 0.93856 0.30817 0.44613 0.02220  -0.03191 0.01164  175 ARG B C     
3282 O  O     . ARG B 145 ? 1.00655 0.39064 0.52746 0.01645  -0.02530 0.01390  175 ARG B O     
3283 C  CB    . ARG B 145 ? 0.96735 0.35396 0.50392 0.03051  -0.04137 0.00325  175 ARG B CB    
3284 C  CG    . ARG B 145 ? 0.98689 0.37843 0.53126 0.03838  -0.04968 -0.00242 175 ARG B CG    
3285 C  CD    . ARG B 145 ? 0.96725 0.34611 0.49900 0.04370  -0.05666 -0.00384 175 ARG B CD    
3286 N  NE    . ARG B 145 ? 1.13626 0.51501 0.67018 0.03991  -0.05504 -0.00122 175 ARG B NE    
3287 C  CZ    . ARG B 145 ? 1.11054 0.47323 0.62802 0.03523  -0.05294 0.00316  175 ARG B CZ    
3288 N  NH1   . ARG B 145 ? 1.05305 0.39928 0.55055 0.03343  -0.05179 0.00581  175 ARG B NH1   
3289 N  NH2   . ARG B 145 ? 1.05726 0.42035 0.57795 0.03185  -0.05231 0.00520  175 ARG B NH2   
3290 N  N     . THR B 146 ? 1.02997 0.38149 0.51481 0.02093  -0.03275 0.01485  176 THR B N     
3291 C  CA    . THR B 146 ? 0.97752 0.32723 0.45171 0.01209  -0.02544 0.02170  176 THR B CA    
3292 C  C     . THR B 146 ? 1.05196 0.39006 0.51598 0.00430  -0.02588 0.02684  176 THR B C     
3293 O  O     . THR B 146 ? 0.99287 0.33122 0.44901 -0.00501 -0.01991 0.03343  176 THR B O     
3294 C  CB    . THR B 146 ? 1.11337 0.45164 0.56749 0.01459  -0.02551 0.02292  176 THR B CB    
3295 O  OG1   . THR B 146 ? 1.07175 0.38808 0.50796 0.01933  -0.03376 0.02132  176 THR B OG1   
3296 C  CG2   . THR B 146 ? 0.97785 0.32655 0.44057 0.02217  -0.02529 0.01804  176 THR B CG2   
3297 N  N     . THR B 147 ? 0.96004 0.28831 0.42308 0.00786  -0.03314 0.02418  177 THR B N     
3298 C  CA    . THR B 147 ? 0.98268 0.29867 0.43614 0.00109  -0.03473 0.02853  177 THR B CA    
3299 C  C     . THR B 147 ? 1.06918 0.39141 0.53783 0.00510  -0.03886 0.02457  177 THR B C     
3300 O  O     . THR B 147 ? 0.96680 0.29561 0.44571 0.01468  -0.04357 0.01826  177 THR B O     
3301 C  CB    . THR B 147 ? 1.10357 0.39054 0.52749 0.00206  -0.04177 0.03035  177 THR B CB    
3302 O  OG1   . THR B 147 ? 1.05010 0.32858 0.47074 0.01451  -0.05079 0.02338  177 THR B OG1   
3303 C  CG2   . THR B 147 ? 1.01775 0.29894 0.42584 -0.00172 -0.03788 0.03453  177 THR B CG2   
3304 N  N     . ARG B 148 ? 1.06026 0.38071 0.52953 -0.00246 -0.03742 0.02857  178 ARG B N     
3305 C  CA    . ARG B 148 ? 1.02598 0.35136 0.50759 0.00099  -0.04123 0.02553  178 ARG B CA    
3306 C  C     . ARG B 148 ? 1.01839 0.36903 0.52720 0.00664  -0.03905 0.02030  178 ARG B C     
3307 O  O     . ARG B 148 ? 0.95597 0.31095 0.47266 0.01523  -0.04499 0.01512  178 ARG B O     
3308 C  CB    . ARG B 148 ? 1.03372 0.33734 0.49733 0.00951  -0.05222 0.02233  178 ARG B CB    
3309 C  CG    . ARG B 148 ? 1.15336 0.42927 0.58948 0.00270  -0.05580 0.02796  178 ARG B CG    
3310 C  CD    . ARG B 148 ? 1.18347 0.43521 0.59835 0.01284  -0.06757 0.02414  178 ARG B CD    
3311 N  NE    . ARG B 148 ? 1.13692 0.39535 0.56254 0.02208  -0.07314 0.01878  178 ARG B NE    
3312 C  CZ    . ARG B 148 ? 1.17475 0.42607 0.59748 0.01959  -0.07595 0.02044  178 ARG B CZ    
3313 N  NH1   . ARG B 148 ? 1.10028 0.34155 0.51340 0.00663  -0.07320 0.02742  178 ARG B NH1   
3314 N  NH2   . ARG B 148 ? 1.11587 0.37336 0.54632 0.03035  -0.08183 0.01491  178 ARG B NH2   
3315 N  N     . PHE B 149 ? 0.99336 0.36122 0.51572 0.00169  -0.03072 0.02187  179 PHE B N     
3316 C  CA    . PHE B 149 ? 0.96751 0.35721 0.51332 0.00566  -0.02866 0.01760  179 PHE B CA    
3317 C  C     . PHE B 149 ? 0.93751 0.34476 0.50183 -0.00131 -0.02150 0.01994  179 PHE B C     
3318 O  O     . PHE B 149 ? 0.86599 0.27512 0.42708 -0.00955 -0.01469 0.02489  179 PHE B O     
3319 C  CB    . PHE B 149 ? 0.88068 0.27388 0.42494 0.00807  -0.02644 0.01625  179 PHE B CB    
3320 C  CG    . PHE B 149 ? 0.86329 0.27586 0.42902 0.01139  -0.02541 0.01216  179 PHE B CG    
3321 C  CD1   . PHE B 149 ? 0.96927 0.38755 0.54539 0.01813  -0.03206 0.00718  179 PHE B CD1   
3322 C  CD2   . PHE B 149 ? 0.84622 0.27119 0.42028 0.00777  -0.01830 0.01347  179 PHE B CD2   
3323 C  CE1   . PHE B 149 ? 0.98555 0.42039 0.58010 0.01961  -0.03189 0.00418  179 PHE B CE1   
3324 C  CE2   . PHE B 149 ? 0.90772 0.34727 0.49899 0.01060  -0.01847 0.00981  179 PHE B CE2   
3325 C  CZ    . PHE B 149 ? 0.88243 0.32607 0.48367 0.01575  -0.02542 0.00547  179 PHE B CZ    
3326 N  N     . PHE B 150 ? 0.88802 0.30946 0.47167 0.00204  -0.02305 0.01646  180 PHE B N     
3327 C  CA    . PHE B 150 ? 0.81819 0.25645 0.42029 -0.00355 -0.01686 0.01804  180 PHE B CA    
3328 C  C     . PHE B 150 ? 0.79737 0.25362 0.42064 0.00106  -0.01800 0.01354  180 PHE B C     
3329 O  O     . PHE B 150 ? 0.92932 0.38693 0.55651 0.00754  -0.02472 0.00993  180 PHE B O     
3330 C  CB    . PHE B 150 ? 0.82050 0.25320 0.42079 -0.00664 -0.01828 0.02029  180 PHE B CB    
3331 C  CG    . PHE B 150 ? 0.87271 0.31851 0.48616 -0.01467 -0.01081 0.02356  180 PHE B CG    
3332 C  CD1   . PHE B 150 ? 0.85451 0.31951 0.49065 -0.01329 -0.00881 0.02105  180 PHE B CD1   
3333 C  CD2   . PHE B 150 ? 0.81642 0.25660 0.41976 -0.02392 -0.00582 0.02932  180 PHE B CD2   
3334 C  CE1   . PHE B 150 ? 0.80162 0.27882 0.44985 -0.02008 -0.00196 0.02371  180 PHE B CE1   
3335 C  CE2   . PHE B 150 ? 0.82217 0.27616 0.43814 -0.03113 0.00104  0.03217  180 PHE B CE2   
3336 C  CZ    . PHE B 150 ? 0.84100 0.31304 0.47931 -0.02873 0.00302  0.02909  180 PHE B CZ    
3337 N  N     . THR B 151 ? 0.83091 0.30132 0.46702 -0.00223 -0.01189 0.01388  181 THR B N     
3338 C  CA    . THR B 151 ? 0.77067 0.25602 0.42480 0.00087  -0.01347 0.01020  181 THR B CA    
3339 C  C     . THR B 151 ? 0.74993 0.25028 0.41941 -0.00426 -0.00645 0.01154  181 THR B C     
3340 O  O     . THR B 151 ? 0.82433 0.32500 0.49016 -0.00964 0.00015  0.01504  181 THR B O     
3341 C  CB    . THR B 151 ? 0.86144 0.34406 0.51085 0.00530  -0.01651 0.00736  181 THR B CB    
3342 O  OG1   . THR B 151 ? 0.78426 0.27914 0.44959 0.00784  -0.02057 0.00400  181 THR B OG1   
3343 C  CG2   . THR B 151 ? 0.79955 0.28333 0.44478 0.00246  -0.00994 0.00908  181 THR B CG2   
3344 N  N     . GLY B 152 ? 0.75380 0.26702 0.43987 -0.00265 -0.00828 0.00882  182 GLY B N     
3345 C  CA    . GLY B 152 ? 0.82769 0.35446 0.52817 -0.00629 -0.00285 0.00925  182 GLY B CA    
3346 C  C     . GLY B 152 ? 0.76046 0.29954 0.47841 -0.00509 -0.00685 0.00694  182 GLY B C     
3347 O  O     . GLY B 152 ? 0.84022 0.37901 0.55880 -0.00130 -0.01369 0.00447  182 GLY B O     
3348 N  N     . PHE B 153 ? 0.78739 0.33819 0.51946 -0.00857 -0.00291 0.00796  183 PHE B N     
3349 C  CA    . PHE B 153 ? 0.77323 0.33683 0.52181 -0.00812 -0.00650 0.00666  183 PHE B CA    
3350 C  C     . PHE B 153 ? 0.71625 0.28010 0.46524 -0.00633 -0.00878 0.00731  183 PHE B C     
3351 O  O     . PHE B 153 ? 0.80612 0.37046 0.55654 -0.00894 -0.00454 0.00937  183 PHE B O     
3352 C  CB    . PHE B 153 ? 0.72575 0.30126 0.48857 -0.01208 -0.00157 0.00722  183 PHE B CB    
3353 C  CG    . PHE B 153 ? 0.77499 0.36437 0.55464 -0.01247 -0.00518 0.00645  183 PHE B CG    
3354 C  CD1   . PHE B 153 ? 0.75816 0.35190 0.54321 -0.01239 -0.01053 0.00484  183 PHE B CD1   
3355 C  CD2   . PHE B 153 ? 0.73125 0.32938 0.52060 -0.01323 -0.00365 0.00764  183 PHE B CD2   
3356 C  CE1   . PHE B 153 ? 0.71661 0.32468 0.51695 -0.01397 -0.01392 0.00497  183 PHE B CE1   
3357 C  CE2   . PHE B 153 ? 0.69813 0.31087 0.50276 -0.01349 -0.00672 0.00732  183 PHE B CE2   
3358 C  CZ    . PHE B 153 ? 0.77465 0.39319 0.58511 -0.01432 -0.01168 0.00625  183 PHE B CZ    
3359 N  N     . LEU B 154 ? 0.75261 0.31627 0.49966 -0.00137 -0.01600 0.00538  184 LEU B N     
3360 C  CA    . LEU B 154 ? 0.77167 0.33368 0.51539 0.00265  -0.01944 0.00527  184 LEU B CA    
3361 C  C     . LEU B 154 ? 0.75968 0.33880 0.52089 0.00238  -0.01913 0.00546  184 LEU B C     
3362 O  O     . LEU B 154 ? 0.81981 0.41435 0.59558 0.00164  -0.02084 0.00466  184 LEU B O     
3363 C  CB    . LEU B 154 ? 0.78410 0.34196 0.51929 0.00939  -0.02745 0.00270  184 LEU B CB    
3364 C  CG    . LEU B 154 ? 0.87921 0.41643 0.59290 0.01126  -0.02859 0.00266  184 LEU B CG    
3365 C  CD1   . LEU B 154 ? 0.86939 0.40170 0.57946 0.00731  -0.02462 0.00328  184 LEU B CD1   
3366 C  CD2   . LEU B 154 ? 0.96542 0.49927 0.67084 0.01908  -0.03706 -0.00032 184 LEU B CD2   
3367 N  N     . LYS B 155 ? 0.78675 0.36243 0.54555 0.00262  -0.01732 0.00679  185 LYS B N     
3368 C  CA    . LYS B 155 ? 0.70471 0.29478 0.47764 0.00356  -0.01713 0.00697  185 LYS B CA    
3369 C  C     . LYS B 155 ? 0.77649 0.36102 0.53974 0.01135  -0.02331 0.00565  185 LYS B C     
3370 O  O     . LYS B 155 ? 0.81859 0.38767 0.56876 0.01144  -0.02290 0.00684  185 LYS B O     
3371 C  CB    . LYS B 155 ? 0.73996 0.33024 0.51806 -0.00272 -0.00963 0.00949  185 LYS B CB    
3372 C  CG    . LYS B 155 ? 0.78845 0.38271 0.57299 -0.00878 -0.00392 0.01027  185 LYS B CG    
3373 C  CD    . LYS B 155 ? 0.75004 0.34285 0.53573 -0.01456 0.00365  0.01271  185 LYS B CD    
3374 C  CE    . LYS B 155 ? 0.91758 0.52322 0.71825 -0.01521 0.00544  0.01318  185 LYS B CE    
3375 N  NZ    . LYS B 155 ? 0.93084 0.55331 0.74865 -0.01525 0.00482  0.01195  185 LYS B NZ    
3376 N  N     . LEU B 156 ? 0.81242 0.40966 0.58118 0.01789  -0.02952 0.00328  186 LEU B N     
3377 C  CA    . LEU B 156 ? 0.81495 0.40665 0.57161 0.02754  -0.03671 0.00106  186 LEU B CA    
3378 C  C     . LEU B 156 ? 0.95929 0.56502 0.72446 0.03345  -0.03903 0.00031  186 LEU B C     
3379 O  O     . LEU B 156 ? 0.99966 0.59748 0.75193 0.04234  -0.04483 -0.00160 186 LEU B O     
3380 C  CB    . LEU B 156 ? 0.75893 0.35618 0.51337 0.03271  -0.04297 -0.00152 186 LEU B CB    
3381 C  CG    . LEU B 156 ? 0.96608 0.54891 0.71065 0.02843  -0.04172 -0.00126 186 LEU B CG    
3382 C  CD1   . LEU B 156 ? 0.88204 0.47055 0.62466 0.03347  -0.04846 -0.00394 186 LEU B CD1   
3383 C  CD2   . LEU B 156 ? 0.85189 0.40829 0.57517 0.02782  -0.04033 -0.00014 186 LEU B CD2   
3384 N  N     . ASN B 157 ? 1.06808 0.69375 0.85322 0.02957  -0.03519 0.00157  187 ASN B N     
3385 C  CA    . ASN B 157 ? 1.13986 0.78060 0.93356 0.03562  -0.03715 0.00097  187 ASN B CA    
3386 C  C     . ASN B 157 ? 1.01188 0.65517 0.81627 0.02885  -0.03012 0.00346  187 ASN B C     
3387 O  O     . ASN B 157 ? 1.09869 0.76276 0.92157 0.02656  -0.02769 0.00436  187 ASN B O     
3388 C  CB    . ASN B 157 ? 1.29906 0.96774 1.10799 0.03920  -0.04095 -0.00005 187 ASN B CB    
3389 C  CG    . ASN B 157 ? 1.43611 1.11993 1.24805 0.04959  -0.04532 -0.00161 187 ASN B CG    
3390 O  OD1   . ASN B 157 ? 1.46146 1.13419 1.25716 0.05969  -0.05093 -0.00415 187 ASN B OD1   
3391 N  ND2   . ASN B 157 ? 1.19011 0.89901 1.02169 0.04769  -0.04319 -0.00014 187 ASN B ND2   
3392 N  N     . GLU B 158 ? 0.89576 0.51779 0.68791 0.02513  -0.02699 0.00484  188 GLU B N     
3393 C  CA    . GLU B 158 ? 0.87255 0.49540 0.67320 0.01798  -0.02007 0.00726  188 GLU B CA    
3394 C  C     . GLU B 158 ? 0.82892 0.44826 0.62576 0.02322  -0.02229 0.00703  188 GLU B C     
3395 O  O     . GLU B 158 ? 0.86448 0.46815 0.64363 0.03005  -0.02841 0.00569  188 GLU B O     
3396 C  CB    . GLU B 158 ? 0.87947 0.48447 0.67044 0.00927  -0.01472 0.00951  188 GLU B CB    
3397 C  CG    . GLU B 158 ? 0.95601 0.56566 0.75245 0.00398  -0.01153 0.00973  188 GLU B CG    
3398 C  CD    . GLU B 158 ? 1.03912 0.66886 0.85662 -0.00022 -0.00725 0.01022  188 GLU B CD    
3399 O  OE1   . GLU B 158 ? 1.01418 0.64899 0.84020 -0.00334 -0.00265 0.01154  188 GLU B OE1   
3400 O  OE2   . GLU B 158 ? 1.16373 0.80323 0.98837 -0.00063 -0.00901 0.00936  188 GLU B OE2   
3401 N  N     . PHE B 159 ? 0.78971 0.42226 0.60196 0.02035  -0.01783 0.00818  189 PHE B N     
3402 C  CA    . PHE B 159 ? 0.75642 0.38643 0.56657 0.02484  -0.01950 0.00804  189 PHE B CA    
3403 C  C     . PHE B 159 ? 0.75491 0.37784 0.56786 0.01547  -0.01257 0.01081  189 PHE B C     
3404 O  O     . PHE B 159 ? 0.66143 0.29419 0.48760 0.00759  -0.00571 0.01228  189 PHE B O     
3405 C  CB    . PHE B 159 ? 0.71459 0.37029 0.54130 0.03177  -0.02126 0.00668  189 PHE B CB    
3406 C  CG    . PHE B 159 ? 0.86072 0.52932 0.68746 0.04036  -0.02761 0.00430  189 PHE B CG    
3407 C  CD1   . PHE B 159 ? 0.98229 0.64283 0.79311 0.05223  -0.03571 0.00155  189 PHE B CD1   
3408 C  CD2   . PHE B 159 ? 0.89878 0.58712 0.74029 0.03663  -0.02614 0.00482  189 PHE B CD2   
3409 C  CE1   . PHE B 159 ? 0.97668 0.65125 0.78746 0.06077  -0.04162 -0.00083 189 PHE B CE1   
3410 C  CE2   . PHE B 159 ? 0.96217 0.66433 0.80407 0.04378  -0.03224 0.00297  189 PHE B CE2   
3411 C  CZ    . PHE B 159 ? 1.00769 0.70425 0.83477 0.05613  -0.03968 0.00005  189 PHE B CZ    
3412 N  N     . PRO B 160 ? 0.68412 0.28975 0.48396 0.01606  -0.01465 0.01158  190 PRO B N     
3413 C  CA    . PRO B 160 ? 0.70365 0.30405 0.50621 0.00655  -0.00831 0.01450  190 PRO B CA    
3414 C  C     . PRO B 160 ? 0.70917 0.33206 0.53445 0.00514  -0.00288 0.01455  190 PRO B C     
3415 O  O     . PRO B 160 ? 0.66361 0.30108 0.49816 0.01296  -0.00580 0.01272  190 PRO B O     
3416 C  CB    . PRO B 160 ? 0.74858 0.32746 0.53261 0.00939  -0.01419 0.01495  190 PRO B CB    
3417 C  CG    . PRO B 160 ? 0.79320 0.37054 0.56829 0.02309  -0.02356 0.01137  190 PRO B CG    
3418 C  CD    . PRO B 160 ? 0.65033 0.23857 0.43007 0.02530  -0.02368 0.00983  190 PRO B CD    
3419 N  N     . ILE B 161 ? 0.60747 0.23388 0.44112 -0.00449 0.00496  0.01668  191 ILE B N     
3420 C  CA    . ILE B 161 ? 0.64990 0.29581 0.50400 -0.00666 0.01051  0.01681  191 ILE B CA    
3421 C  C     . ILE B 161 ? 0.74058 0.38204 0.59424 -0.00716 0.01109  0.01774  191 ILE B C     
3422 O  O     . ILE B 161 ? 0.73597 0.36337 0.57998 -0.01388 0.01316  0.01995  191 ILE B O     
3423 C  CB    . ILE B 161 ? 0.77760 0.42930 0.63971 -0.01532 0.01807  0.01803  191 ILE B CB    
3424 C  CG1   . ILE B 161 ? 0.71134 0.36851 0.57528 -0.01416 0.01659  0.01682  191 ILE B CG1   
3425 C  CG2   . ILE B 161 ? 0.66837 0.33588 0.54848 -0.01812 0.02385  0.01833  191 ILE B CG2   
3426 C  CD1   . ILE B 161 ? 0.86558 0.52432 0.73274 -0.02121 0.02264  0.01757  191 ILE B CD1   
3427 N  N     . ARG B 162 ? 0.79315 0.44760 0.65734 -0.00048 0.00922  0.01633  192 ARG B N     
3428 C  CA    . ARG B 162 ? 0.78652 0.43663 0.64971 0.00106  0.00836  0.01666  192 ARG B CA    
3429 C  C     . ARG B 162 ? 0.81706 0.48320 0.69905 -0.00344 0.01554  0.01740  192 ARG B C     
3430 O  O     . ARG B 162 ? 0.78804 0.45347 0.67172 -0.00155 0.01498  0.01743  192 ARG B O     
3431 C  CB    . ARG B 162 ? 0.63901 0.29096 0.49793 0.01379  0.00026  0.01420  192 ARG B CB    
3432 C  CG    . ARG B 162 ? 0.68337 0.31972 0.52266 0.02038  -0.00784 0.01276  192 ARG B CG    
3433 C  CD    . ARG B 162 ? 0.60457 0.21164 0.42176 0.01526  -0.01058 0.01452  192 ARG B CD    
3434 N  NE    . ARG B 162 ? 0.74933 0.34016 0.54618 0.02386  -0.01982 0.01261  192 ARG B NE    
3435 C  CZ    . ARG B 162 ? 0.80362 0.36687 0.57751 0.02092  -0.02443 0.01396  192 ARG B CZ    
3436 N  NH1   . ARG B 162 ? 0.81697 0.36732 0.58569 0.00850  -0.02033 0.01775  192 ARG B NH1   
3437 N  NH2   . ARG B 162 ? 0.81290 0.36198 0.56820 0.03048  -0.03351 0.01162  192 ARG B NH2   
3438 N  N     . GLN B 163 ? 0.88178 0.56116 0.77677 -0.00879 0.02165  0.01778  193 GLN B N     
3439 C  CA    . GLN B 163 ? 0.66924 0.36260 0.58070 -0.01278 0.02823  0.01824  193 GLN B CA    
3440 C  C     . GLN B 163 ? 0.78333 0.46716 0.69026 -0.02136 0.03352  0.02007  193 GLN B C     
3441 O  O     . GLN B 163 ? 0.81134 0.48987 0.71270 -0.02732 0.03661  0.02106  193 GLN B O     
3442 C  CB    . GLN B 163 ? 0.78059 0.48923 0.70497 -0.01491 0.03147  0.01785  193 GLN B CB    
3443 C  CG    . GLN B 163 ? 0.83426 0.55385 0.76261 -0.00864 0.02614  0.01682  193 GLN B CG    
3444 C  CD    . GLN B 163 ? 0.99845 0.72621 0.93367 -0.01289 0.02784  0.01697  193 GLN B CD    
3445 O  OE1   . GLN B 163 ? 1.03581 0.77865 0.98502 -0.01434 0.02973  0.01732  193 GLN B OE1   
3446 N  NE2   . GLN B 163 ? 0.91468 0.63126 0.83884 -0.01491 0.02654  0.01682  193 GLN B NE2   
3447 N  N     . PRO B 164 ? 0.86658 0.54920 0.77557 -0.02217 0.03460  0.02066  194 PRO B N     
3448 C  CA    . PRO B 164 ? 0.72988 0.40366 0.63279 -0.03105 0.03877  0.02293  194 PRO B CA    
3449 C  C     . PRO B 164 ? 0.67549 0.36010 0.58761 -0.03770 0.04699  0.02337  194 PRO B C     
3450 O  O     . PRO B 164 ? 0.67983 0.35931 0.58557 -0.04515 0.05059  0.02545  194 PRO B O     
3451 C  CB    . PRO B 164 ? 0.68272 0.35569 0.58839 -0.02944 0.03752  0.02305  194 PRO B CB    
3452 C  CG    . PRO B 164 ? 0.69539 0.37993 0.61107 -0.01945 0.03423  0.02064  194 PRO B CG    
3453 C  CD    . PRO B 164 ? 0.70521 0.39098 0.61743 -0.01441 0.03026  0.01949  194 PRO B CD    
3454 N  N     . PHE B 165 ? 0.75033 0.44971 0.67603 -0.03529 0.04963  0.02161  195 PHE B N     
3455 C  CA    . PHE B 165 ? 0.76914 0.47636 0.70063 -0.04010 0.05624  0.02144  195 PHE B CA    
3456 C  C     . PHE B 165 ? 0.81148 0.51287 0.73367 -0.04201 0.05613  0.02159  195 PHE B C     
3457 O  O     . PHE B 165 ? 0.89768 0.60324 0.82079 -0.04550 0.06118  0.02143  195 PHE B O     
3458 C  CB    . PHE B 165 ? 0.75660 0.47921 0.70428 -0.03712 0.05812  0.01964  195 PHE B CB    
3459 C  CG    . PHE B 165 ? 0.78256 0.50940 0.73356 -0.03194 0.05292  0.01876  195 PHE B CG    
3460 C  CD1   . PHE B 165 ? 0.85077 0.57684 0.79895 -0.03263 0.05175  0.01828  195 PHE B CD1   
3461 C  CD2   . PHE B 165 ? 0.84318 0.57575 0.79969 -0.02618 0.04885  0.01848  195 PHE B CD2   
3462 C  CE1   . PHE B 165 ? 0.84666 0.57817 0.79813 -0.02880 0.04660  0.01787  195 PHE B CE1   
3463 C  CE2   . PHE B 165 ? 0.80503 0.54497 0.76502 -0.02164 0.04409  0.01803  195 PHE B CE2   
3464 C  CZ    . PHE B 165 ? 0.74883 0.48849 0.70661 -0.02356 0.04299  0.01789  195 PHE B CZ    
3465 N  N     . SER B 166 ? 0.83172 0.52379 0.74434 -0.03895 0.05029  0.02160  196 SER B N     
3466 C  CA    . SER B 166 ? 0.72633 0.41242 0.62989 -0.04002 0.04957  0.02154  196 SER B CA    
3467 C  C     . SER B 166 ? 0.73901 0.41451 0.62881 -0.04608 0.05209  0.02389  196 SER B C     
3468 O  O     . SER B 166 ? 0.74275 0.40857 0.62395 -0.04854 0.05035  0.02594  196 SER B O     
3469 C  CB    . SER B 166 ? 0.66365 0.34383 0.56120 -0.03440 0.04223  0.02072  196 SER B CB    
3470 O  OG    . SER B 166 ? 0.74049 0.41365 0.62836 -0.03540 0.04127  0.02063  196 SER B OG    
3471 N  N     . LYS B 167 ? 0.70553 0.38255 0.59206 -0.04854 0.05564  0.02379  197 LYS B N     
3472 C  CA    . LYS B 167 ? 0.86554 0.53430 0.73813 -0.05420 0.05779  0.02648  197 LYS B CA    
3473 C  C     . LYS B 167 ? 0.76499 0.41697 0.62214 -0.05348 0.05147  0.02780  197 LYS B C     
3474 O  O     . LYS B 167 ? 0.87671 0.51899 0.72070 -0.05904 0.05176  0.03094  197 LYS B O     
3475 C  CB    . LYS B 167 ? 0.79560 0.47010 0.66659 -0.05519 0.06237  0.02575  197 LYS B CB    
3476 C  CG    . LYS B 167 ? 0.93651 0.60472 0.80116 -0.05121 0.05845  0.02412  197 LYS B CG    
3477 C  CD    . LYS B 167 ? 0.92590 0.59884 0.78735 -0.05136 0.06264  0.02317  197 LYS B CD    
3478 C  CE    . LYS B 167 ? 1.02727 0.70299 0.88112 -0.05711 0.06842  0.02612  197 LYS B CE    
3479 N  NZ    . LYS B 167 ? 1.03200 0.71381 0.88134 -0.05564 0.07239  0.02496  197 LYS B NZ    
3480 N  N     . TRP B 168 ? 0.73545 0.38477 0.59398 -0.04684 0.04557  0.02560  198 TRP B N     
3481 C  CA    . TRP B 168 ? 0.80447 0.43790 0.64782 -0.04427 0.03877  0.02605  198 TRP B CA    
3482 C  C     . TRP B 168 ? 0.73347 0.36153 0.57585 -0.03986 0.03301  0.02567  198 TRP B C     
3483 O  O     . TRP B 168 ? 0.72664 0.34517 0.55974 -0.03427 0.02621  0.02460  198 TRP B O     
3484 C  CB    . TRP B 168 ? 0.84061 0.47555 0.68421 -0.03921 0.03574  0.02362  198 TRP B CB    
3485 C  CG    . TRP B 168 ? 0.87221 0.51097 0.71540 -0.04202 0.04030  0.02344  198 TRP B CG    
3486 C  CD1   . TRP B 168 ? 0.85564 0.49061 0.68961 -0.04753 0.04482  0.02565  198 TRP B CD1   
3487 C  CD2   . TRP B 168 ? 0.96261 0.60969 0.81385 -0.03894 0.03999  0.02090  198 TRP B CD2   
3488 N  NE1   . TRP B 168 ? 0.92635 0.56693 0.76192 -0.04670 0.04749  0.02414  198 TRP B NE1   
3489 C  CE2   . TRP B 168 ? 0.97010 0.61644 0.81554 -0.04172 0.04421  0.02120  198 TRP B CE2   
3490 C  CE3   . TRP B 168 ? 1.01560 0.67097 0.87764 -0.03450 0.03617  0.01874  198 TRP B CE3   
3491 C  CZ2   . TRP B 168 ? 1.06363 0.71434 0.91246 -0.03950 0.04401  0.01895  198 TRP B CZ2   
3492 C  CZ3   . TRP B 168 ? 1.26319 0.92322 1.12911 -0.03396 0.03600  0.01713  198 TRP B CZ3   
3493 C  CH2   . TRP B 168 ? 1.28215 0.93835 1.14083 -0.03609 0.03950  0.01702  198 TRP B CH2   
3494 N  N     . PHE B 169 ? 0.69929 0.33314 0.55004 -0.04146 0.03527  0.02625  199 PHE B N     
3495 C  CA    . PHE B 169 ? 0.75116 0.37865 0.59919 -0.03685 0.02957  0.02586  199 PHE B CA    
3496 C  C     . PHE B 169 ? 0.66575 0.27060 0.49231 -0.03984 0.02447  0.02836  199 PHE B C     
3497 O  O     . PHE B 169 ? 0.75778 0.35627 0.57654 -0.04904 0.02783  0.03175  199 PHE B O     
3498 C  CB    . PHE B 169 ? 0.76109 0.39949 0.62256 -0.03874 0.03369  0.02609  199 PHE B CB    
3499 C  CG    . PHE B 169 ? 0.73421 0.36221 0.58909 -0.03603 0.02819  0.02649  199 PHE B CG    
3500 C  CD1   . PHE B 169 ? 0.63509 0.26495 0.49208 -0.02568 0.02209  0.02384  199 PHE B CD1   
3501 C  CD2   . PHE B 169 ? 0.68656 0.30352 0.53249 -0.04369 0.02868  0.02958  199 PHE B CD2   
3502 C  CE1   . PHE B 169 ? 0.63262 0.25187 0.48189 -0.02172 0.01631  0.02374  199 PHE B CE1   
3503 C  CE2   . PHE B 169 ? 0.66602 0.27094 0.50419 -0.04112 0.02253  0.02986  199 PHE B CE2   
3504 C  CZ    . PHE B 169 ? 0.64022 0.24549 0.47957 -0.02944 0.01620  0.02665  199 PHE B CZ    
3505 N  N     . VAL B 170 ? 0.66823 0.26112 0.48420 -0.03201 0.01593  0.02684  200 VAL B N     
3506 C  CA    . VAL B 170 ? 0.84891 0.41725 0.64277 -0.03377 0.00922  0.02894  200 VAL B CA    
3507 C  C     . VAL B 170 ? 0.76775 0.33052 0.55901 -0.02519 0.00206  0.02696  200 VAL B C     
3508 O  O     . VAL B 170 ? 0.81657 0.38818 0.61388 -0.01405 -0.00157 0.02332  200 VAL B O     
3509 C  CB    . VAL B 170 ? 0.83810 0.39068 0.61390 -0.03170 0.00406  0.02887  200 VAL B CB    
3510 C  CG1   . VAL B 170 ? 0.74911 0.30388 0.52364 -0.04078 0.01060  0.03146  200 VAL B CG1   
3511 C  CG2   . VAL B 170 ? 0.80566 0.36661 0.58664 -0.01955 -0.00019 0.02446  200 VAL B CG2   
3512 N  N     . SER B 171 ? 0.77435 0.32281 0.55571 -0.03019 -0.00047 0.02945  201 SER B N     
3513 C  CA    . SER B 171 ? 0.80867 0.34804 0.58385 -0.02143 -0.00848 0.02748  201 SER B CA    
3514 C  C     . SER B 171 ? 0.84684 0.36634 0.60067 -0.01168 -0.01922 0.02537  201 SER B C     
3515 O  O     . SER B 171 ? 0.90422 0.41316 0.64576 -0.01398 -0.02062 0.02628  201 SER B O     
3516 C  CB    . SER B 171 ? 0.79325 0.31854 0.56001 -0.03018 -0.00979 0.03099  201 SER B CB    
3517 O  OG    . SER B 171 ? 0.93076 0.42815 0.67171 -0.03633 -0.01626 0.03426  201 SER B OG    
3518 N  N     . LYS B 172 ? 0.82314 0.33753 0.57167 0.00021  -0.02718 0.02229  202 LYS B N     
3519 C  CA    . LYS B 172 ? 0.94426 0.43925 0.67068 0.01120  -0.03826 0.01972  202 LYS B CA    
3520 C  C     . LYS B 172 ? 0.95431 0.41439 0.65205 0.00397  -0.04540 0.02308  202 LYS B C     
3521 O  O     . LYS B 172 ? 1.01665 0.45771 0.69362 0.00942  -0.05324 0.02193  202 LYS B O     
3522 C  CB    . LYS B 172 ? 0.89423 0.39439 0.62148 0.02739  -0.04523 0.01521  202 LYS B CB    
3523 C  CG    . LYS B 172 ? 0.84882 0.38328 0.60141 0.03530  -0.03982 0.01218  202 LYS B CG    
3524 C  CD    . LYS B 172 ? 1.00945 0.54829 0.75567 0.05377  -0.04869 0.00731  202 LYS B CD    
3525 C  CE    . LYS B 172 ? 1.01829 0.59401 0.79097 0.05977  -0.04315 0.00534  202 LYS B CE    
3526 N  NZ    . LYS B 172 ? 1.34041 0.92499 1.10814 0.07829  -0.05157 0.00086  202 LYS B NZ    
3527 N  N     . SER B 173 ? 0.96358 0.41517 0.65934 -0.00874 -0.04305 0.02746  203 SER B N     
3528 C  CA    . SER B 173 ? 1.01911 0.44803 0.69263 -0.01879 -0.04844 0.03146  203 SER B CA    
3529 C  C     . SER B 173 ? 0.97749 0.40849 0.65062 -0.03106 -0.04150 0.03540  203 SER B C     
3530 O  O     . SER B 173 ? 1.12016 0.53611 0.77438 -0.03606 -0.04657 0.03764  203 SER B O     
3531 C  CB    . SER B 173 ? 0.95856 0.38747 0.63377 -0.02788 -0.04881 0.03443  203 SER B CB    
3532 O  OG    . SER B 173 ? 1.04454 0.49222 0.74056 -0.03917 -0.03705 0.03752  203 SER B OG    
3533 N  N     . GLU B 174 ? 0.93865 0.39021 0.63245 -0.03537 -0.03016 0.03597  204 GLU B N     
3534 C  CA    . GLU B 174 ? 0.94241 0.39804 0.63601 -0.04432 -0.02375 0.03880  204 GLU B CA    
3535 C  C     . GLU B 174 ? 0.93328 0.38431 0.61877 -0.03437 -0.02792 0.03539  204 GLU B C     
3536 O  O     . GLU B 174 ? 0.76702 0.20384 0.43665 -0.03974 -0.02920 0.03792  204 GLU B O     
3537 C  CB    . GLU B 174 ? 0.90446 0.39084 0.62509 -0.05000 -0.01091 0.03922  204 GLU B CB    
3538 C  CG    . GLU B 174 ? 0.91434 0.40572 0.64070 -0.06302 -0.00531 0.04373  204 GLU B CG    
3539 C  CD    . GLU B 174 ? 1.05884 0.58091 0.81178 -0.06556 0.00647  0.04291  204 GLU B CD    
3540 O  OE1   . GLU B 174 ? 1.03770 0.57656 0.80763 -0.05571 0.00849  0.03833  204 GLU B OE1   
3541 O  OE2   . GLU B 174 ? 1.18290 0.71252 0.93879 -0.07743 0.01338  0.04699  204 GLU B OE2   
3542 N  N     . TYR B 175 ? 0.94342 0.40745 0.63953 -0.02011 -0.03009 0.02987  205 TYR B N     
3543 C  CA    . TYR B 175 ? 0.82413 0.28471 0.51218 -0.00931 -0.03533 0.02621  205 TYR B CA    
3544 C  C     . TYR B 175 ? 0.90672 0.37172 0.59633 0.00704  -0.04264 0.02096  205 TYR B C     
3545 O  O     . TYR B 175 ? 0.77052 0.26198 0.48293 0.01242  -0.03814 0.01844  205 TYR B O     
3546 C  CB    . TYR B 175 ? 0.77758 0.26083 0.48331 -0.01073 -0.02693 0.02532  205 TYR B CB    
3547 C  CG    . TYR B 175 ? 0.80234 0.28070 0.49822 -0.00124 -0.03251 0.02208  205 TYR B CG    
3548 C  CD1   . TYR B 175 ? 0.75486 0.21217 0.42983 -0.00540 -0.03544 0.02410  205 TYR B CD1   
3549 C  CD2   . TYR B 175 ? 0.77001 0.26553 0.47701 0.01175  -0.03512 0.01721  205 TYR B CD2   
3550 C  CE1   . TYR B 175 ? 0.76415 0.21652 0.42954 0.00368  -0.04080 0.02090  205 TYR B CE1   
3551 C  CE2   . TYR B 175 ? 0.81883 0.31127 0.51685 0.02047  -0.04052 0.01421  205 TYR B CE2   
3552 C  CZ    . TYR B 175 ? 0.83051 0.30045 0.50741 0.01666  -0.04341 0.01584  205 TYR B CZ    
3553 O  OH    . TYR B 175 ? 0.83311 0.29945 0.50052 0.02554  -0.04889 0.01267  205 TYR B OH    
3554 N  N     . PRO B 176 ? 0.89509 0.33484 0.55983 0.01555  -0.05429 0.01928  206 PRO B N     
3555 C  CA    . PRO B 176 ? 0.89340 0.33605 0.55688 0.03179  -0.06203 0.01443  206 PRO B CA    
3556 C  C     . PRO B 176 ? 0.87278 0.33160 0.54109 0.04718  -0.06519 0.00914  206 PRO B C     
3557 O  O     . PRO B 176 ? 0.98106 0.44672 0.64967 0.06143  -0.07109 0.00512  206 PRO B O     
3558 C  CB    . PRO B 176 ? 0.83623 0.24062 0.46690 0.03369  -0.07420 0.01516  206 PRO B CB    
3559 C  CG    . PRO B 176 ? 0.92956 0.31598 0.54372 0.02325  -0.07446 0.01867  206 PRO B CG    
3560 C  CD    . PRO B 176 ? 0.92064 0.32574 0.55568 0.00884  -0.06108 0.02263  206 PRO B CD    
3561 N  N     . TRP B 177 ? 0.88193 0.34786 0.55343 0.04538  -0.06198 0.00894  207 TRP B N     
3562 C  CA    . TRP B 177 ? 0.86391 0.34414 0.53779 0.05968  -0.06619 0.00411  207 TRP B CA    
3563 C  C     . TRP B 177 ? 0.84598 0.36353 0.55100 0.05846  -0.05719 0.00354  207 TRP B C     
3564 O  O     . TRP B 177 ? 0.81516 0.34427 0.53757 0.04617  -0.04753 0.00673  207 TRP B O     
3565 C  CB    . TRP B 177 ? 0.86308 0.32380 0.51618 0.06073  -0.07109 0.00362  207 TRP B CB    
3566 C  CG    . TRP B 177 ? 0.92400 0.34622 0.54381 0.06321  -0.08175 0.00397  207 TRP B CG    
3567 C  CD1   . TRP B 177 ? 0.94271 0.35077 0.54346 0.07880  -0.09358 -0.00020 207 TRP B CD1   
3568 C  CD2   . TRP B 177 ? 0.93972 0.33253 0.54041 0.04949  -0.08209 0.00898  207 TRP B CD2   
3569 N  NE1   . TRP B 177 ? 0.93780 0.30638 0.50742 0.07535  -0.10192 0.00184  207 TRP B NE1   
3570 C  CE2   . TRP B 177 ? 0.93916 0.29848 0.50874 0.05660  -0.09489 0.00787  207 TRP B CE2   
3571 C  CE3   . TRP B 177 ? 0.90757 0.29985 0.51375 0.03206  -0.07311 0.01445  207 TRP B CE3   
3572 C  CZ2   . TRP B 177 ? 0.95628 0.29792 0.50827 0.04414  -0.09734 0.01191  207 TRP B CZ2   
3573 C  CZ3   . TRP B 177 ? 0.96791 0.33230 0.55145 0.02114  -0.07630 0.01903  207 TRP B CZ3   
3574 C  CH2   . TRP B 177 ? 0.88336 0.22849 0.44315 0.02638  -0.08785 0.01766  207 TRP B CH2   
3575 N  N     . ASP B 178 ? 1.07280 0.60928 0.78366 0.07168  -0.06113 -0.00054 208 ASP B N     
3576 C  CA    . ASP B 178 ? 0.94752 0.52006 0.68655 0.07167  -0.05468 -0.00100 208 ASP B CA    
3577 C  C     . ASP B 178 ? 0.89869 0.47896 0.64733 0.06177  -0.04831 0.00074  208 ASP B C     
3578 O  O     . ASP B 178 ? 0.88872 0.49356 0.66042 0.05641  -0.04141 0.00185  208 ASP B O     
3579 C  CB    . ASP B 178 ? 0.95365 0.54573 0.69476 0.08837  -0.06150 -0.00539 208 ASP B CB    
3580 C  CG    . ASP B 178 ? 1.38900 0.97859 1.12295 0.10035  -0.06771 -0.00767 208 ASP B CG    
3581 O  OD1   . ASP B 178 ? 1.46006 1.03740 1.19285 0.09443  -0.06558 -0.00558 208 ASP B OD1   
3582 O  OD2   . ASP B 178 ? 1.53003 1.13077 1.25915 0.11629  -0.07506 -0.01170 208 ASP B OD2   
3583 N  N     . ARG B 179 ? 0.92759 0.48690 0.65809 0.05980  -0.05110 0.00091  209 ARG B N     
3584 C  CA    . ARG B 179 ? 0.83681 0.40294 0.57400 0.05316  -0.04669 0.00176  209 ARG B CA    
3585 C  C     . ARG B 179 ? 0.81874 0.35957 0.54119 0.04205  -0.04384 0.00499  209 ARG B C     
3586 O  O     . ARG B 179 ? 0.82960 0.34422 0.53070 0.04189  -0.04839 0.00596  209 ARG B O     
3587 C  CB    . ARG B 179 ? 0.84223 0.41440 0.57341 0.06425  -0.05360 -0.00194 209 ARG B CB    
3588 C  CG    . ARG B 179 ? 1.01583 0.61695 0.76154 0.07534  -0.05660 -0.00476 209 ARG B CG    
3589 C  CD    . ARG B 179 ? 1.37622 0.98175 1.11216 0.08781  -0.06476 -0.00866 209 ARG B CD    
3590 N  NE    . ARG B 179 ? 1.56524 1.17298 1.30378 0.08181  -0.06271 -0.00815 209 ARG B NE    
3591 C  CZ    . ARG B 179 ? 1.48286 1.11783 1.24152 0.07883  -0.05981 -0.00778 209 ARG B CZ    
3592 N  NH1   . ARG B 179 ? 1.32290 0.98694 1.10188 0.08042  -0.05808 -0.00741 209 ARG B NH1   
3593 N  NH2   . ARG B 179 ? 1.31316 0.94556 1.07068 0.07387  -0.05911 -0.00754 209 ARG B NH2   
3594 N  N     . TYR B 180 ? 0.78983 0.33898 0.52330 0.03255  -0.03656 0.00690  210 TYR B N     
3595 C  CA    . TYR B 180 ? 0.70378 0.23370 0.42409 0.02316  -0.03367 0.00979  210 TYR B CA    
3596 C  C     . TYR B 180 ? 0.74053 0.25950 0.44532 0.02883  -0.03948 0.00771  210 TYR B C     
3597 O  O     . TYR B 180 ? 0.71805 0.25031 0.42797 0.03813  -0.04377 0.00420  210 TYR B O     
3598 C  CB    . TYR B 180 ? 0.68478 0.22892 0.42252 0.01241  -0.02379 0.01217  210 TYR B CB    
3599 C  CG    . TYR B 180 ? 0.75409 0.30155 0.50084 0.00424  -0.01739 0.01510  210 TYR B CG    
3600 C  CD1   . TYR B 180 ? 0.69000 0.21913 0.42272 0.00175  -0.01967 0.01723  210 TYR B CD1   
3601 C  CD2   . TYR B 180 ? 0.75274 0.32082 0.52100 -0.00098 -0.00973 0.01572  210 TYR B CD2   
3602 C  CE1   . TYR B 180 ? 0.75887 0.29191 0.50000 -0.00601 -0.01403 0.01995  210 TYR B CE1   
3603 C  CE2   . TYR B 180 ? 0.70577 0.27740 0.48194 -0.00787 -0.00394 0.01810  210 TYR B CE2   
3604 C  CZ    . TYR B 180 ? 0.68615 0.24136 0.44950 -0.01038 -0.00592 0.02019  210 TYR B CZ    
3605 O  OH    . TYR B 180 ? 0.72430 0.28428 0.49600 -0.01754 -0.00028 0.02259  210 TYR B OH    
3606 N  N     . PRO B 181 ? 0.86286 0.35855 0.54830 0.02335  -0.03993 0.00999  211 PRO B N     
3607 C  CA    . PRO B 181 ? 0.88824 0.37480 0.56069 0.02744  -0.04406 0.00826  211 PRO B CA    
3608 C  C     . PRO B 181 ? 0.73484 0.24057 0.42447 0.02373  -0.03819 0.00792  211 PRO B C     
3609 O  O     . PRO B 181 ? 0.75605 0.27805 0.46452 0.01680  -0.03073 0.00957  211 PRO B O     
3610 C  CB    . PRO B 181 ? 0.88588 0.34407 0.53517 0.01961  -0.04429 0.01208  211 PRO B CB    
3611 C  CG    . PRO B 181 ? 0.85204 0.31541 0.51165 0.00753  -0.03587 0.01643  211 PRO B CG    
3612 C  CD    . PRO B 181 ? 0.83106 0.31102 0.50776 0.01147  -0.03551 0.01485  211 PRO B CD    
3613 N  N     . PRO B 182 ? 0.83336 0.33658 0.51615 0.02820  -0.04175 0.00576  212 PRO B N     
3614 C  CA    . PRO B 182 ? 0.76982 0.28444 0.46385 0.02292  -0.03651 0.00611  212 PRO B CA    
3615 C  C     . PRO B 182 ? 0.75315 0.25765 0.44252 0.01168  -0.02914 0.01030  212 PRO B C     
3616 O  O     . PRO B 182 ? 0.78593 0.26921 0.45607 0.00861  -0.03019 0.01275  212 PRO B O     
3617 C  CB    . PRO B 182 ? 0.80224 0.30898 0.48320 0.03009  -0.04304 0.00323  212 PRO B CB    
3618 C  CG    . PRO B 182 ? 0.76016 0.25682 0.42673 0.04072  -0.05179 0.00066  212 PRO B CG    
3619 C  CD    . PRO B 182 ? 0.76528 0.25093 0.42627 0.03760  -0.05084 0.00314  212 PRO B CD    
3620 N  N     . PHE B 183 ? 0.71585 0.23587 0.42201 0.00548  -0.02201 0.01131  213 PHE B N     
3621 C  CA    . PHE B 183 ? 0.71923 0.23295 0.42070 -0.00361 -0.01510 0.01476  213 PHE B CA    
3622 C  C     . PHE B 183 ? 0.71544 0.24456 0.43131 -0.00561 -0.01067 0.01374  213 PHE B C     
3623 O  O     . PHE B 183 ? 0.83372 0.37700 0.56297 -0.00150 -0.01319 0.01097  213 PHE B O     
3624 C  CB    . PHE B 183 ? 0.71667 0.22924 0.41997 -0.01100 -0.01000 0.01841  213 PHE B CB    
3625 C  CG    . PHE B 183 ? 0.69347 0.22655 0.41930 -0.01211 -0.00589 0.01781  213 PHE B CG    
3626 C  CD1   . PHE B 183 ? 0.74016 0.28097 0.47435 -0.00577 -0.01027 0.01559  213 PHE B CD1   
3627 C  CD2   . PHE B 183 ? 0.79727 0.34200 0.53483 -0.01879 0.00209  0.01937  213 PHE B CD2   
3628 C  CE1   . PHE B 183 ? 0.80968 0.36938 0.56420 -0.00693 -0.00650 0.01531  213 PHE B CE1   
3629 C  CE2   . PHE B 183 ? 0.78840 0.35073 0.54568 -0.01971 0.00560  0.01878  213 PHE B CE2   
3630 C  CZ    . PHE B 183 ? 0.78308 0.35262 0.54895 -0.01417 0.00135  0.01692  213 PHE B CZ    
3631 N  N     . CYS B 184 ? 0.70720 0.23325 0.41892 -0.01191 -0.00464 0.01614  214 CYS B N     
3632 C  CA    . CYS B 184 ? 0.78919 0.32648 0.51087 -0.01350 -0.00059 0.01518  214 CYS B CA    
3633 C  C     . CYS B 184 ? 0.84902 0.39726 0.58193 -0.01976 0.00725  0.01728  214 CYS B C     
3634 O  O     . CYS B 184 ? 0.87990 0.42302 0.60612 -0.02509 0.01126  0.02066  214 CYS B O     
3635 C  CB    . CYS B 184 ? 0.81168 0.33806 0.51830 -0.01380 -0.00003 0.01565  214 CYS B CB    
3636 S  SG    . CYS B 184 ? 0.87112 0.38504 0.56427 -0.00602 -0.00902 0.01264  214 CYS B SG    
3637 N  N     . SER B 185 ? 0.79786 0.36017 0.54581 -0.01960 0.00931  0.01550  215 SER B N     
3638 C  CA    . SER B 185 ? 0.82505 0.39828 0.58330 -0.02444 0.01666  0.01686  215 SER B CA    
3639 C  C     . SER B 185 ? 0.75678 0.32493 0.50324 -0.02906 0.02262  0.01984  215 SER B C     
3640 O  O     . SER B 185 ? 0.75402 0.31442 0.48816 -0.02768 0.02192  0.01973  215 SER B O     
3641 C  CB    . SER B 185 ? 0.69207 0.27638 0.46267 -0.02302 0.01684  0.01433  215 SER B CB    
3642 O  OG    . SER B 185 ? 0.85351 0.44632 0.63048 -0.02646 0.02369  0.01516  215 SER B OG    
3643 N  N     . GLY B 186 ? 0.82710 0.40123 0.57774 -0.03439 0.02834  0.02250  216 GLY B N     
3644 C  CA    . GLY B 186 ? 0.72759 0.30181 0.46892 -0.03972 0.03462  0.02592  216 GLY B CA    
3645 C  C     . GLY B 186 ? 0.76205 0.34700 0.50744 -0.03803 0.03918  0.02425  216 GLY B C     
3646 O  O     . GLY B 186 ? 0.84581 0.43319 0.58259 -0.04095 0.04427  0.02673  216 GLY B O     
3647 N  N     . THR B 187 ? 0.68196 0.27332 0.43893 -0.03351 0.03712  0.02039  217 THR B N     
3648 C  CA    . THR B 187 ? 0.76597 0.36352 0.52318 -0.03047 0.03965  0.01818  217 THR B CA    
3649 C  C     . THR B 187 ? 0.83714 0.42624 0.57702 -0.02930 0.03986  0.01927  217 THR B C     
3650 O  O     . THR B 187 ? 0.83613 0.43151 0.57107 -0.02854 0.04473  0.01954  217 THR B O     
3651 C  CB    . THR B 187 ? 0.81154 0.41032 0.57803 -0.02597 0.03429  0.01416  217 THR B CB    
3652 O  OG1   . THR B 187 ? 0.89033 0.47889 0.65162 -0.02361 0.02728  0.01330  217 THR B OG1   
3653 C  CG2   . THR B 187 ? 0.70397 0.31292 0.48760 -0.02766 0.03485  0.01364  217 THR B CG2   
3654 N  N     . GLY B 188 ? 0.80382 0.37972 0.53418 -0.02844 0.03458  0.01972  218 GLY B N     
3655 C  CA    . GLY B 188 ? 0.88702 0.45364 0.59941 -0.02837 0.03501  0.02163  218 GLY B CA    
3656 C  C     . GLY B 188 ? 0.82596 0.37796 0.52984 -0.02465 0.02742  0.02012  218 GLY B C     
3657 O  O     . GLY B 188 ? 0.83534 0.38707 0.54645 -0.02013 0.02198  0.01641  218 GLY B O     
3658 N  N     . TYR B 189 ? 0.77825 0.31872 0.46666 -0.02699 0.02684  0.02319  219 TYR B N     
3659 C  CA    . TYR B 189 ? 0.79293 0.31826 0.47133 -0.02299 0.01932  0.02172  219 TYR B CA    
3660 C  C     . TYR B 189 ? 0.75467 0.26979 0.41360 -0.02342 0.02032  0.02406  219 TYR B C     
3661 O  O     . TYR B 189 ? 0.83465 0.35488 0.48806 -0.02829 0.02678  0.02784  219 TYR B O     
3662 C  CB    . TYR B 189 ? 0.77619 0.29630 0.45659 -0.02527 0.01618  0.02301  219 TYR B CB    
3663 C  CG    . TYR B 189 ? 0.84833 0.36842 0.52529 -0.03334 0.02097  0.02802  219 TYR B CG    
3664 C  CD1   . TYR B 189 ? 0.79448 0.30432 0.45346 -0.03846 0.02264  0.03256  219 TYR B CD1   
3665 C  CD2   . TYR B 189 ? 0.85721 0.38728 0.54839 -0.03640 0.02333  0.02853  219 TYR B CD2   
3666 C  CE1   . TYR B 189 ? 0.90348 0.41319 0.55874 -0.04726 0.02622  0.03775  219 TYR B CE1   
3667 C  CE2   . TYR B 189 ? 0.83111 0.36074 0.51890 -0.04429 0.02701  0.03319  219 TYR B CE2   
3668 C  CZ    . TYR B 189 ? 0.90620 0.42562 0.57596 -0.05016 0.02825  0.03796  219 TYR B CZ    
3669 O  OH    . TYR B 189 ? 0.99035 0.50921 0.65599 -0.05935 0.03118  0.04319  219 TYR B OH    
3670 N  N     . VAL B 190 ? 0.76588 0.26818 0.41467 -0.01832 0.01399  0.02194  220 VAL B N     
3671 C  CA    . VAL B 190 ? 0.78530 0.27699 0.41454 -0.01793 0.01448  0.02393  220 VAL B CA    
3672 C  C     . VAL B 190 ? 0.80137 0.27439 0.41583 -0.01799 0.00854  0.02521  220 VAL B C     
3673 O  O     . VAL B 190 ? 0.89001 0.35821 0.50861 -0.01343 0.00189  0.02190  220 VAL B O     
3674 C  CB    . VAL B 190 ? 0.78782 0.27969 0.41463 -0.01073 0.01249  0.02000  220 VAL B CB    
3675 C  CG1   . VAL B 190 ? 0.80727 0.29034 0.41425 -0.01017 0.01398  0.02234  220 VAL B CG1   
3676 C  CG2   . VAL B 190 ? 0.86516 0.37273 0.50542 -0.00930 0.01646  0.01787  220 VAL B CG2   
3677 N  N     . PHE B 191 ? 0.81885 0.28251 0.41592 -0.02296 0.01076  0.03002  221 PHE B N     
3678 C  CA    . PHE B 191 ? 0.83802 0.28062 0.41742 -0.02288 0.00440  0.03135  221 PHE B CA    
3679 C  C     . PHE B 191 ? 0.89857 0.33124 0.45781 -0.02402 0.00555  0.03437  221 PHE B C     
3680 O  O     . PHE B 191 ? 0.85869 0.30205 0.41666 -0.02815 0.01270  0.03764  221 PHE B O     
3681 C  CB    . PHE B 191 ? 0.84098 0.27844 0.41844 -0.03048 0.00441  0.03552  221 PHE B CB    
3682 C  CG    . PHE B 191 ? 0.84015 0.28785 0.41827 -0.04101 0.01266  0.04164  221 PHE B CG    
3683 C  CD1   . PHE B 191 ? 0.87753 0.34547 0.47525 -0.04323 0.01855  0.04120  221 PHE B CD1   
3684 C  CD2   . PHE B 191 ? 0.87866 0.31648 0.43748 -0.04897 0.01427  0.04803  221 PHE B CD2   
3685 C  CE1   . PHE B 191 ? 0.85850 0.33779 0.45703 -0.05252 0.02599  0.04665  221 PHE B CE1   
3686 C  CE2   . PHE B 191 ? 0.86009 0.31025 0.42009 -0.05929 0.02172  0.05406  221 PHE B CE2   
3687 C  CZ    . PHE B 191 ? 0.84153 0.31293 0.42159 -0.06074 0.02760  0.05319  221 PHE B CZ    
3688 N  N     . SER B 192 ? 0.99154 0.40528 0.53514 -0.01948 -0.00149 0.03298  222 SER B N     
3689 C  CA    . SER B 192 ? 0.89708 0.29879 0.41906 -0.02136 -0.00088 0.03659  222 SER B CA    
3690 C  C     . SER B 192 ? 0.90943 0.30731 0.42020 -0.03343 0.00315  0.04460  222 SER B C     
3691 O  O     . SER B 192 ? 0.93438 0.32895 0.44794 -0.03883 0.00182  0.04665  222 SER B O     
3692 C  CB    . SER B 192 ? 0.91403 0.29430 0.42022 -0.01417 -0.00994 0.03353  222 SER B CB    
3693 O  OG    . SER B 192 ? 1.01207 0.37983 0.51542 -0.01340 -0.01664 0.03260  222 SER B OG    
3694 N  N     . GLY B 193 ? 0.94024 0.34030 0.43872 -0.03804 0.00820  0.04942  223 GLY B N     
3695 C  CA    . GLY B 193 ? 0.97040 0.37274 0.46054 -0.05114 0.01321  0.05789  223 GLY B CA    
3696 C  C     . GLY B 193 ? 1.00020 0.37891 0.47394 -0.05817 0.00675  0.06201  223 GLY B C     
3697 O  O     . GLY B 193 ? 1.02638 0.40738 0.50036 -0.06906 0.00898  0.06759  223 GLY B O     
3698 N  N     . ASP B 194 ? 1.07725 0.43209 0.53552 -0.05182 -0.00200 0.05920  224 ASP B N     
3699 C  CA    . ASP B 194 ? 1.12379 0.45259 0.56332 -0.05679 -0.00972 0.06239  224 ASP B CA    
3700 C  C     . ASP B 194 ? 1.23963 0.56974 0.69182 -0.05805 -0.01221 0.06092  224 ASP B C     
3701 O  O     . ASP B 194 ? 1.11752 0.43155 0.55668 -0.06643 -0.01614 0.06576  224 ASP B O     
3702 C  CB    . ASP B 194 ? 1.11222 0.41767 0.53557 -0.04631 -0.01909 0.05761  224 ASP B CB    
3703 C  CG    . ASP B 194 ? 1.27494 0.58855 0.71603 -0.03231 -0.02246 0.04816  224 ASP B CG    
3704 O  OD1   . ASP B 194 ? 1.20100 0.53689 0.66136 -0.02858 -0.01670 0.04502  224 ASP B OD1   
3705 O  OD2   . ASP B 194 ? 1.31468 0.61283 0.74995 -0.02496 -0.03132 0.04392  224 ASP B OD2   
3706 N  N     . VAL B 195 ? 1.06869 0.41656 0.54500 -0.04983 -0.01068 0.05439  225 VAL B N     
3707 C  CA    . VAL B 195 ? 0.93810 0.28888 0.42735 -0.04978 -0.01293 0.05258  225 VAL B CA    
3708 C  C     . VAL B 195 ? 1.07332 0.43286 0.56626 -0.06331 -0.00695 0.05948  225 VAL B C     
3709 O  O     . VAL B 195 ? 1.00602 0.35760 0.49841 -0.06687 -0.01066 0.06071  225 VAL B O     
3710 C  CB    . VAL B 195 ? 0.97048 0.34145 0.48553 -0.03975 -0.01156 0.04514  225 VAL B CB    
3711 C  CG1   . VAL B 195 ? 0.94303 0.32040 0.47265 -0.04051 -0.01251 0.04400  225 VAL B CG1   
3712 C  CG2   . VAL B 195 ? 1.01220 0.37396 0.52302 -0.02709 -0.01903 0.03857  225 VAL B CG2   
3713 N  N     . ALA B 196 ? 1.01644 0.39350 0.51320 -0.07053 0.00212  0.06392  226 ALA B N     
3714 C  CA    . ALA B 196 ? 0.92957 0.31767 0.42992 -0.08387 0.00799  0.07081  226 ALA B CA    
3715 C  C     . ALA B 196 ? 0.97702 0.34022 0.45434 -0.09458 0.00184  0.07756  226 ALA B C     
3716 O  O     . ALA B 196 ? 1.05776 0.41848 0.53783 -0.10146 0.00034  0.08012  226 ALA B O     
3717 C  CB    . ALA B 196 ? 0.92561 0.33572 0.42894 -0.08918 0.01791  0.07491  226 ALA B CB    
3718 N  N     . SER B 197 ? 1.10391 0.44702 0.55697 -0.09632 -0.00233 0.08067  227 SER B N     
3719 C  CA    . SER B 197 ? 1.12287 0.43899 0.55069 -0.10721 -0.00928 0.08756  227 SER B CA    
3720 C  C     . SER B 197 ? 1.07604 0.36859 0.49821 -0.10024 -0.02016 0.08287  227 SER B C     
3721 O  O     . SER B 197 ? 1.07252 0.35581 0.48818 -0.10831 -0.02490 0.08612  227 SER B O     
3722 C  CB    . SER B 197 ? 1.15262 0.45176 0.55491 -0.10988 -0.01164 0.09169  227 SER B CB    
3723 O  OG    . SER B 197 ? 1.24121 0.56204 0.64533 -0.11936 -0.00182 0.09822  227 SER B OG    
3724 N  N     . GLN B 198 ? 1.16312 0.45275 0.59145 -0.08416 -0.02456 0.07390  228 GLN B N     
3725 C  CA    . GLN B 198 ? 1.09315 0.36310 0.51542 -0.07583 -0.03522 0.06900  228 GLN B CA    
3726 C  C     . GLN B 198 ? 1.04779 0.33157 0.48960 -0.07764 -0.03367 0.06795  228 GLN B C     
3727 O  O     . GLN B 198 ? 1.02486 0.30140 0.46158 -0.07899 -0.04090 0.06739  228 GLN B O     
3728 C  CB    . GLN B 198 ? 1.06895 0.33691 0.49477 -0.05850 -0.03977 0.06000  228 GLN B CB    
3729 C  CG    . GLN B 198 ? 1.14129 0.38713 0.54186 -0.05496 -0.04544 0.06009  228 GLN B CG    
3730 C  CD    . GLN B 198 ? 1.41459 0.66173 0.82012 -0.03824 -0.04948 0.05125  228 GLN B CD    
3731 O  OE1   . GLN B 198 ? 1.47116 0.71387 0.87937 -0.02745 -0.05672 0.04513  228 GLN B OE1   
3732 N  NE2   . GLN B 198 ? 1.37243 0.62848 0.77989 -0.03578 -0.04495 0.05036  228 GLN B NE2   
3733 N  N     . VAL B 199 ? 0.97998 0.29290 0.44905 -0.07618 -0.02450 0.06578  229 VAL B N     
3734 C  CA    . VAL B 199 ? 0.94931 0.27593 0.43720 -0.07815 -0.02220 0.06509  229 VAL B CA    
3735 C  C     . VAL B 199 ? 1.09405 0.41585 0.57314 -0.09473 -0.02056 0.07383  229 VAL B C     
3736 O  O     . VAL B 199 ? 1.07229 0.39204 0.55415 -0.09626 -0.02521 0.07329  229 VAL B O     
3737 C  CB    . VAL B 199 ? 0.94739 0.30771 0.46568 -0.07388 -0.01255 0.06114  229 VAL B CB    
3738 C  CG1   . VAL B 199 ? 0.89780 0.27339 0.43331 -0.08015 -0.00817 0.06282  229 VAL B CG1   
3739 C  CG2   . VAL B 199 ? 0.92992 0.29434 0.45904 -0.05827 -0.01631 0.05244  229 VAL B CG2   
3740 N  N     . TYR B 200 ? 1.03205 0.36252 0.50626 -0.10637 -0.01359 0.08070  230 TYR B N     
3741 C  CA    . TYR B 200 ? 1.09122 0.42192 0.55866 -0.12321 -0.01207 0.08930  230 TYR B CA    
3742 C  C     . TYR B 200 ? 1.11775 0.42845 0.56719 -0.12529 -0.02414 0.08924  230 TYR B C     
3743 O  O     . TYR B 200 ? 1.21322 0.52584 0.66463 -0.13297 -0.02708 0.09145  230 TYR B O     
3744 C  CB    . TYR B 200 ? 1.08922 0.43356 0.55184 -0.13472 -0.00325 0.09694  230 TYR B CB    
3745 C  CG    . TYR B 200 ? 1.20799 0.55672 0.66390 -0.15295 -0.00227 0.10606  230 TYR B CG    
3746 C  CD1   . TYR B 200 ? 1.25599 0.62724 0.72912 -0.16121 0.00507  0.10926  230 TYR B CD1   
3747 C  CD2   . TYR B 200 ? 1.21270 0.54702 0.64752 -0.16127 -0.00919 0.11045  230 TYR B CD2   
3748 C  CE1   . TYR B 200 ? 1.21123 0.59221 0.68187 -0.17724 0.00551  0.11666  230 TYR B CE1   
3749 C  CE2   . TYR B 200 ? 1.26883 0.61172 0.70066 -0.17786 -0.00898 0.11804  230 TYR B CE2   
3750 C  CZ    . TYR B 200 ? 1.28044 0.64740 0.73072 -0.18575 -0.00168 0.12113  230 TYR B CZ    
3751 O  OH    . TYR B 200 ? 1.28664 0.66411 0.73511 -0.20226 -0.00178 0.12861  230 TYR B OH    
3752 N  N     . ASN B 201 ? 1.25652 0.54708 0.68748 -0.11793 -0.03166 0.08634  231 ASN B N     
3753 C  CA    . ASN B 201 ? 1.27271 0.54145 0.68360 -0.11814 -0.04396 0.08538  231 ASN B CA    
3754 C  C     . ASN B 201 ? 1.16923 0.43454 0.58726 -0.10894 -0.05127 0.07911  231 ASN B C     
3755 O  O     . ASN B 201 ? 1.29723 0.55511 0.70782 -0.11522 -0.05768 0.08085  231 ASN B O     
3756 C  CB    . ASN B 201 ? 1.34689 0.59592 0.73789 -0.10948 -0.05012 0.08226  231 ASN B CB    
3757 C  CG    . ASN B 201 ? 1.63156 0.85601 0.99801 -0.11018 -0.06295 0.08151  231 ASN B CG    
3758 O  OD1   . ASN B 201 ? 1.72156 0.93378 1.08297 -0.09774 -0.07224 0.07457  231 ASN B OD1   
3759 N  ND2   . ASN B 201 ? 1.61395 0.83142 0.96404 -0.12475 -0.06373 0.08879  231 ASN B ND2   
3760 N  N     . VAL B 202 ? 1.15708 0.42798 0.58898 -0.09393 -0.05071 0.07185  232 VAL B N     
3761 C  CA    . VAL B 202 ? 1.07956 0.34696 0.51608 -0.08321 -0.05833 0.06562  232 VAL B CA    
3762 C  C     . VAL B 202 ? 1.12755 0.41280 0.58527 -0.08803 -0.05316 0.06684  232 VAL B C     
3763 O  O     . VAL B 202 ? 1.00174 0.28373 0.46160 -0.08129 -0.05965 0.06292  232 VAL B O     
3764 C  CB    . VAL B 202 ? 1.16928 0.43653 0.61139 -0.06493 -0.06082 0.05739  232 VAL B CB    
3765 C  CG1   . VAL B 202 ? 0.97629 0.26605 0.44452 -0.06260 -0.05014 0.05615  232 VAL B CG1   
3766 C  CG2   . VAL B 202 ? 1.14560 0.40431 0.58376 -0.05257 -0.07127 0.05118  232 VAL B CG2   
3767 N  N     . SER B 203 ? 1.03216 0.33597 0.50423 -0.09920 -0.04190 0.07220  233 SER B N     
3768 C  CA    . SER B 203 ? 1.05624 0.37962 0.55172 -0.10089 -0.03566 0.07194  233 SER B CA    
3769 C  C     . SER B 203 ? 1.13910 0.45864 0.63208 -0.10647 -0.04170 0.07342  233 SER B C     
3770 O  O     . SER B 203 ? 1.09379 0.42076 0.60108 -0.10025 -0.04235 0.06966  233 SER B O     
3771 C  CB    . SER B 203 ? 0.98255 0.32569 0.49039 -0.11197 -0.02272 0.07766  233 SER B CB    
3772 O  OG    . SER B 203 ? 1.00553 0.34718 0.50028 -0.12751 -0.02146 0.08572  233 SER B OG    
3773 N  N     . LYS B 204 ? 1.17684 0.48487 0.65162 -0.11838 -0.04637 0.07894  234 LYS B N     
3774 C  CA    . LYS B 204 ? 1.11323 0.41781 0.58568 -0.12472 -0.05212 0.08065  234 LYS B CA    
3775 C  C     . LYS B 204 ? 1.09318 0.37786 0.55303 -0.11184 -0.06509 0.07421  234 LYS B C     
3776 O  O     . LYS B 204 ? 1.09966 0.37979 0.55696 -0.11471 -0.07086 0.07459  234 LYS B O     
3777 C  CB    . LYS B 204 ? 1.23590 0.53551 0.69315 -0.14272 -0.05344 0.08892  234 LYS B CB    
3778 C  CG    . LYS B 204 ? 1.18862 0.51353 0.66203 -0.15741 -0.04146 0.09599  234 LYS B CG    
3779 C  CD    . LYS B 204 ? 1.20603 0.52863 0.66374 -0.17457 -0.04173 0.10456  234 LYS B CD    
3780 C  CE    . LYS B 204 ? 1.51208 0.85033 0.97808 -0.19020 -0.03903 0.11093  234 LYS B CE    
3781 N  NZ    . LYS B 204 ? 1.33182 0.65391 0.78873 -0.19085 -0.05075 0.10931  234 LYS B NZ    
3782 N  N     . SER B 205 ? 1.15001 0.42336 0.60151 -0.09733 -0.07000 0.06826  235 SER B N     
3783 C  CA    . SER B 205 ? 1.13548 0.39362 0.57663 -0.08263 -0.08153 0.06147  235 SER B CA    
3784 C  C     . SER B 205 ? 1.07211 0.34461 0.53419 -0.06772 -0.07862 0.05499  235 SER B C     
3785 O  O     . SER B 205 ? 1.05389 0.31743 0.50962 -0.05416 -0.08751 0.04918  235 SER B O     
3786 C  CB    . SER B 205 ? 1.05455 0.28969 0.46966 -0.07531 -0.09080 0.05873  235 SER B CB    
3787 O  OG    . SER B 205 ? 1.18828 0.42918 0.61075 -0.06247 -0.08776 0.05381  235 SER B OG    
3788 N  N     . VAL B 206 ? 1.07382 0.36816 0.55945 -0.06967 -0.06683 0.05583  236 VAL B N     
3789 C  CA    . VAL B 206 ? 1.06048 0.36946 0.56667 -0.05684 -0.06343 0.05007  236 VAL B CA    
3790 C  C     . VAL B 206 ? 1.03154 0.35673 0.55773 -0.06140 -0.05837 0.05128  236 VAL B C     
3791 O  O     . VAL B 206 ? 0.93648 0.27172 0.47014 -0.07569 -0.05104 0.05708  236 VAL B O     
3792 C  CB    . VAL B 206 ? 1.00713 0.32781 0.52479 -0.05522 -0.05459 0.04953  236 VAL B CB    
3793 C  CG1   . VAL B 206 ? 1.03782 0.37571 0.57873 -0.04491 -0.05030 0.04450  236 VAL B CG1   
3794 C  CG2   . VAL B 206 ? 0.96186 0.26619 0.45999 -0.04827 -0.06055 0.04729  236 VAL B CG2   
3795 N  N     . PRO B 207 ? 0.93403 0.26306 0.46911 -0.04945 -0.06194 0.04602  237 PRO B N     
3796 C  CA    . PRO B 207 ? 0.89580 0.23955 0.44943 -0.05320 -0.05744 0.04694  237 PRO B CA    
3797 C  C     . PRO B 207 ? 0.98912 0.35496 0.56534 -0.06156 -0.04390 0.04978  237 PRO B C     
3798 O  O     . PRO B 207 ? 0.92714 0.30117 0.51257 -0.05641 -0.03871 0.04750  237 PRO B O     
3799 C  CB    . PRO B 207 ? 0.99147 0.33641 0.55057 -0.03604 -0.06304 0.04003  237 PRO B CB    
3800 C  CG    . PRO B 207 ? 1.01397 0.33949 0.55031 -0.02466 -0.07387 0.03615  237 PRO B CG    
3801 C  CD    . PRO B 207 ? 0.99045 0.31138 0.51859 -0.03145 -0.07036 0.03901  237 PRO B CD    
3802 N  N     . TYR B 208 ? 0.87827 0.25336 0.46228 -0.07435 -0.03869 0.05466  238 TYR B N     
3803 C  CA    . TYR B 208 ? 0.90152 0.29726 0.50440 -0.08311 -0.02606 0.05776  238 TYR B CA    
3804 C  C     . TYR B 208 ? 0.90541 0.31784 0.53160 -0.07509 -0.02098 0.05339  238 TYR B C     
3805 O  O     . TYR B 208 ? 0.94466 0.35633 0.57516 -0.06765 -0.02596 0.05011  238 TYR B O     
3806 C  CB    . TYR B 208 ? 0.89552 0.29659 0.49790 -0.09938 -0.02273 0.06452  238 TYR B CB    
3807 C  CG    . TYR B 208 ? 0.84433 0.26871 0.46686 -0.10751 -0.01002 0.06731  238 TYR B CG    
3808 C  CD1   . TYR B 208 ? 0.91502 0.35383 0.55693 -0.10550 -0.00619 0.06528  238 TYR B CD1   
3809 C  CD2   . TYR B 208 ? 0.86591 0.29772 0.48680 -0.11679 -0.00193 0.07194  238 TYR B CD2   
3810 C  CE1   . TYR B 208 ? 1.05246 0.51197 0.71137 -0.11229 0.00520  0.06739  238 TYR B CE1   
3811 C  CE2   . TYR B 208 ? 0.86925 0.32346 0.50710 -0.12309 0.00949  0.07403  238 TYR B CE2   
3812 C  CZ    . TYR B 208 ? 0.98949 0.46026 0.64800 -0.12007 0.01289  0.07110  238 TYR B CZ    
3813 O  OH    . TYR B 208 ? 1.07148 0.57149 0.75016 -0.12372 0.02368  0.07146  238 TYR B OH    
3814 N  N     . ILE B 209 ? 0.89311 0.32394 0.53528 -0.07596 -0.01115 0.05293  239 ILE B N     
3815 C  CA    . ILE B 209 ? 0.87419 0.33227 0.54417 -0.06999 -0.00468 0.04870  239 ILE B CA    
3816 C  C     . ILE B 209 ? 0.80592 0.28661 0.49045 -0.07867 0.00683  0.05128  239 ILE B C     
3817 O  O     . ILE B 209 ? 0.83932 0.31935 0.51612 -0.08322 0.00985  0.05367  239 ILE B O     
3818 C  CB    . ILE B 209 ? 0.89180 0.35735 0.57045 -0.05523 -0.00720 0.04203  239 ILE B CB    
3819 C  CG1   . ILE B 209 ? 0.84787 0.33884 0.55326 -0.04988 -0.00221 0.03835  239 ILE B CG1   
3820 C  CG2   . ILE B 209 ? 0.82842 0.29855 0.50576 -0.05484 -0.00370 0.04155  239 ILE B CG2   
3821 C  CD1   . ILE B 209 ? 0.89720 0.39542 0.61036 -0.03606 -0.00644 0.03252  239 ILE B CD1   
3822 N  N     . LYS B 210 ? 0.86158 0.36248 0.56639 -0.08016 0.01307  0.05058  240 LYS B N     
3823 C  CA    . LYS B 210 ? 0.80807 0.33066 0.52562 -0.08757 0.02356  0.05274  240 LYS B CA    
3824 C  C     . LYS B 210 ? 0.87240 0.41154 0.60287 -0.08030 0.02851  0.04852  240 LYS B C     
3825 O  O     . LYS B 210 ? 0.79504 0.35164 0.53461 -0.08433 0.03666  0.04948  240 LYS B O     
3826 C  CB    . LYS B 210 ? 0.90186 0.43950 0.63561 -0.09117 0.02808  0.05317  240 LYS B CB    
3827 C  CG    . LYS B 210 ? 0.88376 0.43423 0.63711 -0.08020 0.02828  0.04723  240 LYS B CG    
3828 C  CD    . LYS B 210 ? 0.92153 0.48404 0.68865 -0.08377 0.03195  0.04785  240 LYS B CD    
3829 C  CE    . LYS B 210 ? 1.03297 0.60742 0.81826 -0.07311 0.03164  0.04244  240 LYS B CE    
3830 N  NZ    . LYS B 210 ? 1.03490 0.61798 0.83165 -0.07561 0.03396  0.04285  240 LYS B NZ    
3831 N  N     . LEU B 211 ? 0.82176 0.35632 0.55286 -0.06954 0.02336  0.04383  241 LEU B N     
3832 C  CA    . LEU B 211 ? 0.78794 0.33497 0.52874 -0.06325 0.02632  0.04010  241 LEU B CA    
3833 C  C     . LEU B 211 ? 0.72486 0.25800 0.44756 -0.06345 0.02367  0.04127  241 LEU B C     
3834 O  O     . LEU B 211 ? 0.71192 0.22781 0.42138 -0.05846 0.01582  0.04013  241 LEU B O     
3835 C  CB    . LEU B 211 ? 0.76444 0.31728 0.51745 -0.05240 0.02215  0.03481  241 LEU B CB    
3836 C  CG    . LEU B 211 ? 0.83771 0.40452 0.60853 -0.05182 0.02471  0.03374  241 LEU B CG    
3837 C  CD1   . LEU B 211 ? 0.80119 0.37427 0.58234 -0.04149 0.02000  0.02930  241 LEU B CD1   
3838 C  CD2   . LEU B 211 ? 0.66964 0.25552 0.45512 -0.05638 0.03379  0.03413  241 LEU B CD2   
3839 N  N     . GLU B 212 ? 0.76502 0.30622 0.48672 -0.06825 0.03005  0.04325  242 GLU B N     
3840 C  CA    . GLU B 212 ? 0.83360 0.36123 0.53591 -0.07086 0.02839  0.04586  242 GLU B CA    
3841 C  C     . GLU B 212 ? 0.79130 0.31042 0.48888 -0.06092 0.02255  0.04146  242 GLU B C     
3842 O  O     . GLU B 212 ? 0.83461 0.33431 0.51329 -0.06030 0.01668  0.04259  242 GLU B O     
3843 C  CB    . GLU B 212 ? 0.72062 0.26215 0.42377 -0.07700 0.03689  0.04874  242 GLU B CB    
3844 C  CG    . GLU B 212 ? 0.76604 0.32694 0.48535 -0.07073 0.04214  0.04435  242 GLU B CG    
3845 C  CD    . GLU B 212 ? 1.01148 0.56648 0.72402 -0.06367 0.03933  0.04134  242 GLU B CD    
3846 O  OE1   . GLU B 212 ? 1.00026 0.54057 0.69473 -0.06547 0.03644  0.04379  242 GLU B OE1   
3847 O  OE2   . GLU B 212 ? 1.05720 0.62146 0.78188 -0.05658 0.03953  0.03664  242 GLU B OE2   
3848 N  N     . ASP B 213 ? 0.76685 0.29976 0.48059 -0.05336 0.02349  0.03656  243 ASP B N     
3849 C  CA    . ASP B 213 ? 0.76849 0.29535 0.47829 -0.04480 0.01787  0.03269  243 ASP B CA    
3850 C  C     . ASP B 213 ? 0.72069 0.23429 0.42364 -0.03873 0.00903  0.03085  243 ASP B C     
3851 O  O     . ASP B 213 ? 0.78177 0.28100 0.47018 -0.03417 0.00300  0.02974  243 ASP B O     
3852 C  CB    . ASP B 213 ? 0.80864 0.35308 0.53640 -0.03961 0.02025  0.02852  243 ASP B CB    
3853 C  CG    . ASP B 213 ? 0.92419 0.48459 0.67211 -0.03929 0.02279  0.02714  243 ASP B CG    
3854 O  OD1   . ASP B 213 ? 0.76070 0.31928 0.51009 -0.04147 0.02217  0.02864  243 ASP B OD1   
3855 O  OD2   . ASP B 213 ? 0.91902 0.49306 0.68067 -0.03679 0.02500  0.02451  243 ASP B OD2   
3856 N  N     . VAL B 214 ? 0.73176 0.24929 0.44336 -0.03803 0.00786  0.03047  244 VAL B N     
3857 C  CA    . VAL B 214 ? 0.76263 0.26694 0.46518 -0.03136 -0.00093 0.02876  244 VAL B CA    
3858 C  C     . VAL B 214 ? 0.81493 0.29356 0.49188 -0.03546 -0.00566 0.03229  244 VAL B C     
3859 O  O     . VAL B 214 ? 0.84418 0.30644 0.50570 -0.02868 -0.01383 0.03045  244 VAL B O     
3860 C  CB    . VAL B 214 ? 0.77549 0.28895 0.49131 -0.02965 -0.00114 0.02788  244 VAL B CB    
3861 C  CG1   . VAL B 214 ? 0.71808 0.21787 0.42254 -0.02089 -0.01088 0.02563  244 VAL B CG1   
3862 C  CG2   . VAL B 214 ? 0.78920 0.32749 0.52957 -0.02636 0.00318  0.02488  244 VAL B CG2   
3863 N  N     . PHE B 215 ? 0.75254 0.22733 0.42385 -0.04678 -0.00109 0.03759  245 PHE B N     
3864 C  CA    . PHE B 215 ? 0.78090 0.23042 0.42682 -0.05262 -0.00612 0.04191  245 PHE B CA    
3865 C  C     . PHE B 215 ? 0.82383 0.26114 0.45371 -0.05030 -0.00879 0.04172  245 PHE B C     
3866 O  O     . PHE B 215 ? 0.85115 0.26520 0.46008 -0.04684 -0.01735 0.04157  245 PHE B O     
3867 C  CB    . PHE B 215 ? 0.80603 0.25772 0.44998 -0.06681 0.00000  0.04841  245 PHE B CB    
3868 C  CG    . PHE B 215 ? 0.83320 0.25876 0.45026 -0.07491 -0.00551 0.05389  245 PHE B CG    
3869 C  CD1   . PHE B 215 ? 0.92305 0.32618 0.52526 -0.07330 -0.01505 0.05411  245 PHE B CD1   
3870 C  CD2   . PHE B 215 ? 0.87582 0.29820 0.48088 -0.08345 -0.00199 0.05870  245 PHE B CD2   
3871 C  CE1   . PHE B 215 ? 0.98147 0.36227 0.55916 -0.08068 -0.02132 0.05876  245 PHE B CE1   
3872 C  CE2   . PHE B 215 ? 0.96421 0.36172 0.54332 -0.09195 -0.00760 0.06438  245 PHE B CE2   
3873 C  CZ    . PHE B 215 ? 0.97877 0.35642 0.54496 -0.09068 -0.01752 0.06418  245 PHE B CZ    
3874 N  N     . VAL B 216 ? 0.78640 0.23821 0.42463 -0.05168 -0.00191 0.04156  246 VAL B N     
3875 C  CA    . VAL B 216 ? 0.80032 0.24178 0.42446 -0.04854 -0.00432 0.04091  246 VAL B CA    
3876 C  C     . VAL B 216 ? 0.80340 0.23712 0.42441 -0.03577 -0.01292 0.03517  246 VAL B C     
3877 O  O     . VAL B 216 ? 0.82505 0.23868 0.42571 -0.03250 -0.01950 0.03497  246 VAL B O     
3878 C  CB    . VAL B 216 ? 0.82728 0.28718 0.46256 -0.05003 0.00394  0.04066  246 VAL B CB    
3879 C  CG1   . VAL B 216 ? 0.79835 0.24915 0.42170 -0.04422 0.00071  0.03858  246 VAL B CG1   
3880 C  CG2   . VAL B 216 ? 0.81374 0.27952 0.44638 -0.06225 0.01154  0.04690  246 VAL B CG2   
3881 N  N     . GLY B 217 ? 0.78228 0.23294 0.42310 -0.02836 -0.01305 0.03055  247 GLY B N     
3882 C  CA    . GLY B 217 ? 0.78442 0.23179 0.42349 -0.01619 -0.02126 0.02535  247 GLY B CA    
3883 C  C     . GLY B 217 ? 0.86212 0.28586 0.48027 -0.01232 -0.03050 0.02545  247 GLY B C     
3884 O  O     . GLY B 217 ? 0.82266 0.23350 0.42658 -0.00374 -0.03817 0.02251  247 GLY B O     
3885 N  N     . LEU B 218 ? 0.88239 0.29952 0.49760 -0.01807 -0.03055 0.02858  248 LEU B N     
3886 C  CA    . LEU B 218 ? 0.93416 0.32516 0.52650 -0.01469 -0.04044 0.02886  248 LEU B CA    
3887 C  C     . LEU B 218 ? 0.88431 0.24867 0.44888 -0.01865 -0.04468 0.03194  248 LEU B C     
3888 O  O     . LEU B 218 ? 0.89688 0.24028 0.44112 -0.01021 -0.05452 0.02949  248 LEU B O     
3889 C  CB    . LEU B 218 ? 0.90688 0.29434 0.50025 -0.02212 -0.03964 0.03240  248 LEU B CB    
3890 C  CG    . LEU B 218 ? 0.81540 0.22242 0.43046 -0.01684 -0.03819 0.02938  248 LEU B CG    
3891 C  CD1   . LEU B 218 ? 0.84679 0.25083 0.46305 -0.02717 -0.03560 0.03389  248 LEU B CD1   
3892 C  CD2   . LEU B 218 ? 0.83272 0.23359 0.44126 -0.00162 -0.04822 0.02393  248 LEU B CD2   
3893 N  N     . CYS B 219 ? 0.96279 0.32816 0.52541 -0.03112 -0.03749 0.03735  249 CYS B N     
3894 C  CA    . CYS B 219 ? 0.95322 0.29547 0.49010 -0.03587 -0.04067 0.04094  249 CYS B CA    
3895 C  C     . CYS B 219 ? 0.91797 0.25722 0.44929 -0.02476 -0.04454 0.03603  249 CYS B C     
3896 O  O     . CYS B 219 ? 0.99287 0.30703 0.49978 -0.02026 -0.05326 0.03543  249 CYS B O     
3897 C  CB    . CYS B 219 ? 0.90417 0.25515 0.44357 -0.05044 -0.03097 0.04750  249 CYS B CB    
3898 S  SG    . CYS B 219 ? 0.90021 0.25374 0.44289 -0.06513 -0.02696 0.05418  249 CYS B SG    
3899 N  N     . LEU B 220 ? 0.87644 0.24023 0.42924 -0.02044 -0.03860 0.03252  250 LEU B N     
3900 C  CA    . LEU B 220 ? 0.92469 0.28801 0.47422 -0.01042 -0.04219 0.02783  250 LEU B CA    
3901 C  C     . LEU B 220 ? 1.01426 0.36746 0.55522 0.00303  -0.05287 0.02246  250 LEU B C     
3902 O  O     . LEU B 220 ? 0.99986 0.33731 0.52304 0.01011  -0.05961 0.02014  250 LEU B O     
3903 C  CB    . LEU B 220 ? 0.85023 0.24203 0.42573 -0.00818 -0.03527 0.02482  250 LEU B CB    
3904 C  CG    . LEU B 220 ? 0.94531 0.34879 0.52864 -0.01822 -0.02523 0.02873  250 LEU B CG    
3905 C  CD1   . LEU B 220 ? 0.84241 0.27147 0.45043 -0.01440 -0.02054 0.02492  250 LEU B CD1   
3906 C  CD2   . LEU B 220 ? 0.89053 0.27797 0.45294 -0.02117 -0.02558 0.03142  250 LEU B CD2   
3907 N  N     . GLU B 221 ? 0.89498 0.25837 0.44839 0.00759  -0.05456 0.02018  251 GLU B N     
3908 C  CA    . GLU B 221 ? 0.96073 0.31649 0.50545 0.02143  -0.06486 0.01506  251 GLU B CA    
3909 C  C     . GLU B 221 ? 1.03209 0.35218 0.54365 0.02228  -0.07423 0.01670  251 GLU B C     
3910 O  O     . GLU B 221 ? 1.02844 0.33444 0.52289 0.03375  -0.08329 0.01262  251 GLU B O     
3911 C  CB    . GLU B 221 ? 0.94963 0.32350 0.51347 0.02482  -0.06403 0.01328  251 GLU B CB    
3912 C  CG    . GLU B 221 ? 0.96217 0.33331 0.51945 0.04013  -0.07404 0.00787  251 GLU B CG    
3913 C  CD    . GLU B 221 ? 1.10259 0.49330 0.67953 0.04255  -0.07218 0.00677  251 GLU B CD    
3914 O  OE1   . GLU B 221 ? 1.03354 0.41371 0.60603 0.03604  -0.07164 0.01009  251 GLU B OE1   
3915 O  OE2   . GLU B 221 ? 1.13376 0.55102 0.73080 0.05019  -0.07119 0.00295  251 GLU B OE2   
3916 N  N     . ARG B 222 ? 1.02362 0.32936 0.52534 0.01000  -0.07262 0.02270  252 ARG B N     
3917 C  CA    . ARG B 222 ? 1.12773 0.41222 0.60339 0.00807  -0.08081 0.02430  252 ARG B CA    
3918 C  C     . ARG B 222 ? 1.02994 0.30103 0.48768 0.00842  -0.08299 0.02454  252 ARG B C     
3919 O  O     . ARG B 222 ? 1.09920 0.35246 0.53446 0.01538  -0.09283 0.02210  252 ARG B O     
3920 C  CB    . ARG B 222 ? 1.07756 0.36038 0.55199 -0.00805 -0.07701 0.03107  252 ARG B CB    
3921 C  CG    . ARG B 222 ? 1.17336 0.43321 0.61987 -0.01337 -0.08521 0.03381  252 ARG B CG    
3922 C  CD    . ARG B 222 ? 1.12537 0.37296 0.55845 -0.00198 -0.09722 0.02912  252 ARG B CD    
3923 N  NE    . ARG B 222 ? 1.23658 0.49623 0.68594 -0.00153 -0.09570 0.02865  252 ARG B NE    
3924 C  CZ    . ARG B 222 ? 1.30344 0.56199 0.75294 -0.01354 -0.09461 0.03335  252 ARG B CZ    
3925 N  NH1   . ARG B 222 ? 1.16141 0.40774 0.59556 -0.02757 -0.09515 0.03916  252 ARG B NH1   
3926 N  NH2   . ARG B 222 ? 1.20370 0.47426 0.66927 -0.01157 -0.09305 0.03229  252 ARG B NH2   
3927 N  N     . LEU B 223 ? 1.09716 0.37603 0.56347 0.00182  -0.07427 0.02715  253 LEU B N     
3928 C  CA    . LEU B 223 ? 1.04262 0.30967 0.49288 0.00142  -0.07524 0.02787  253 LEU B CA    
3929 C  C     . LEU B 223 ? 1.08461 0.35173 0.53417 0.01687  -0.08013 0.02095  253 LEU B C     
3930 O  O     . LEU B 223 ? 1.13693 0.39315 0.57185 0.01853  -0.08222 0.02066  253 LEU B O     
3931 C  CB    . LEU B 223 ? 1.04835 0.32347 0.50658 -0.01135 -0.06406 0.03360  253 LEU B CB    
3932 C  CG    . LEU B 223 ? 1.00599 0.28001 0.46072 -0.02775 -0.05951 0.04131  253 LEU B CG    
3933 C  CD1   . LEU B 223 ? 0.97093 0.25892 0.43801 -0.03805 -0.04747 0.04621  253 LEU B CD1   
3934 C  CD2   . LEU B 223 ? 1.01507 0.26721 0.44185 -0.03299 -0.06635 0.04452  253 LEU B CD2   
3935 N  N     . ASN B 224 ? 1.02852 0.30944 0.49346 0.02819  -0.08231 0.01538  254 ASN B N     
3936 C  CA    . ASN B 224 ? 1.06334 0.35598 0.53420 0.04187  -0.08601 0.00863  254 ASN B CA    
3937 C  C     . ASN B 224 ? 1.04809 0.35994 0.53542 0.03770  -0.07775 0.00886  254 ASN B C     
3938 O  O     . ASN B 224 ? 1.17118 0.48583 0.65674 0.04627  -0.08111 0.00462  254 ASN B O     
3939 C  CB    . ASN B 224 ? 0.99452 0.25860 0.43458 0.05210  -0.09746 0.00569  254 ASN B CB    
3940 C  CG    . ASN B 224 ? 1.20833 0.46046 0.63321 0.05704  -0.10644 0.00451  254 ASN B CG    
3941 O  OD1   . ASN B 224 ? 1.46724 0.72881 0.90284 0.06324  -0.10823 0.00202  254 ASN B OD1   
3942 N  ND2   . ASN B 224 ? 1.25751 0.48844 0.65634 0.05444  -0.11249 0.00621  254 ASN B ND2   
3943 N  N     . ILE B 225 ? 1.05526 0.38009 0.55757 0.02531  -0.06756 0.01350  255 ILE B N     
3944 C  CA    . ILE B 225 ? 0.95546 0.29876 0.47348 0.02214  -0.06004 0.01341  255 ILE B CA    
3945 C  C     . ILE B 225 ? 0.94122 0.31420 0.48805 0.02694  -0.05767 0.00935  255 ILE B C     
3946 O  O     . ILE B 225 ? 1.01291 0.40008 0.57647 0.02220  -0.05289 0.01085  255 ILE B O     
3947 C  CB    . ILE B 225 ? 0.90780 0.25240 0.42723 0.00794  -0.05059 0.01995  255 ILE B CB    
3948 C  CG1   . ILE B 225 ? 1.02134 0.33836 0.51178 0.00231  -0.05299 0.02461  255 ILE B CG1   
3949 C  CG2   . ILE B 225 ? 0.88729 0.25368 0.42537 0.00645  -0.04312 0.01898  255 ILE B CG2   
3950 C  CD1   . ILE B 225 ? 1.05569 0.37418 0.54496 -0.01247 -0.04451 0.03206  255 ILE B CD1   
3951 N  N     . ARG B 226 ? 1.00205 0.38462 0.55443 0.03586  -0.06130 0.00444  256 ARG B N     
3952 C  CA    . ARG B 226 ? 1.02972 0.44036 0.60813 0.03959  -0.06010 0.00112  256 ARG B CA    
3953 C  C     . ARG B 226 ? 0.93720 0.36385 0.53304 0.03157  -0.05157 0.00289  256 ARG B C     
3954 O  O     . ARG B 226 ? 0.98532 0.40415 0.57278 0.02839  -0.04910 0.00418  256 ARG B O     
3955 C  CB    . ARG B 226 ? 1.07387 0.48994 0.65105 0.05177  -0.06819 -0.00451 256 ARG B CB    
3956 C  CG    . ARG B 226 ? 1.36085 0.76237 0.91989 0.06238  -0.07759 -0.00731 256 ARG B CG    
3957 C  CD    . ARG B 226 ? 1.49460 0.90659 1.06383 0.06472  -0.07839 -0.00761 256 ARG B CD    
3958 N  NE    . ARG B 226 ? 1.70484 1.10259 1.25510 0.07676  -0.08833 -0.01094 256 ARG B NE    
3959 C  CZ    . ARG B 226 ? 1.74192 1.14917 1.29773 0.08384  -0.09188 -0.01298 256 ARG B CZ    
3960 N  NH1   . ARG B 226 ? 1.56422 0.99584 1.14491 0.07961  -0.08612 -0.01183 256 ARG B NH1   
3961 N  NH2   . ARG B 226 ? 1.62434 1.01613 1.15939 0.09627  -0.10180 -0.01648 256 ARG B NH2   
3962 N  N     . LEU B 227 ? 0.80837 0.25678 0.42731 0.02884  -0.04740 0.00289  257 LEU B N     
3963 C  CA    . LEU B 227 ? 0.81829 0.28196 0.45363 0.02272  -0.04060 0.00380  257 LEU B CA    
3964 C  C     . LEU B 227 ? 0.92278 0.39428 0.56271 0.02779  -0.04446 0.00017  257 LEU B C     
3965 O  O     . LEU B 227 ? 0.95085 0.42918 0.59355 0.03545  -0.05123 -0.00330 257 LEU B O     
3966 C  CB    . LEU B 227 ? 0.78937 0.27322 0.44720 0.01917  -0.03631 0.00444  257 LEU B CB    
3967 C  CG    . LEU B 227 ? 0.89669 0.37619 0.55349 0.01443  -0.03295 0.00764  257 LEU B CG    
3968 C  CD1   . LEU B 227 ? 0.81064 0.31188 0.49123 0.01118  -0.02826 0.00792  257 LEU B CD1   
3969 C  CD2   . LEU B 227 ? 0.80149 0.26595 0.44432 0.00621  -0.02768 0.01209  257 LEU B CD2   
3970 N  N     . GLU B 228 ? 0.90606 0.37761 0.54664 0.02374  -0.04048 0.00093  258 GLU B N     
3971 C  CA    . GLU B 228 ? 0.91686 0.39540 0.56243 0.02719  -0.04414 -0.00219 258 GLU B CA    
3972 C  C     . GLU B 228 ? 0.90184 0.39346 0.56293 0.02154  -0.03905 -0.00150 258 GLU B C     
3973 O  O     . GLU B 228 ? 0.87551 0.36487 0.53585 0.01584  -0.03198 0.00132  258 GLU B O     
3974 C  CB    . GLU B 228 ? 0.93970 0.40033 0.56516 0.03032  -0.04677 -0.00295 258 GLU B CB    
3975 C  CG    . GLU B 228 ? 1.06285 0.50689 0.66930 0.03647  -0.05266 -0.00391 258 GLU B CG    
3976 C  CD    . GLU B 228 ? 1.15329 0.57887 0.73938 0.03850  -0.05427 -0.00405 258 GLU B CD    
3977 O  OE1   . GLU B 228 ? 1.15286 0.58268 0.74194 0.04046  -0.05582 -0.00628 258 GLU B OE1   
3978 O  OE2   . GLU B 228 ? 1.06803 0.47428 0.63456 0.03763  -0.05420 -0.00166 258 GLU B OE2   
3979 N  N     . GLU B 229 ? 0.94526 0.45042 0.61926 0.02316  -0.04321 -0.00401 259 GLU B N     
3980 C  CA    . GLU B 229 ? 1.00422 0.51710 0.68851 0.01882  -0.04069 -0.00394 259 GLU B CA    
3981 C  C     . GLU B 229 ? 0.97719 0.47599 0.64674 0.01959  -0.03986 -0.00429 259 GLU B C     
3982 O  O     . GLU B 229 ? 0.77715 0.26446 0.43262 0.02436  -0.04426 -0.00579 259 GLU B O     
3983 C  CB    . GLU B 229 ? 0.88170 0.41027 0.58068 0.01955  -0.04697 -0.00606 259 GLU B CB    
3984 C  CG    . GLU B 229 ? 1.15214 0.69799 0.86634 0.01954  -0.04828 -0.00573 259 GLU B CG    
3985 C  CD    . GLU B 229 ? 1.24576 0.80241 0.97503 0.01321  -0.04220 -0.00349 259 GLU B CD    
3986 O  OE1   . GLU B 229 ? 1.23334 0.78518 0.96191 0.00911  -0.03759 -0.00257 259 GLU B OE1   
3987 O  OE2   . GLU B 229 ? 1.32115 0.89132 1.06226 0.01313  -0.04216 -0.00285 259 GLU B OE2   
3988 N  N     . LEU B 230 ? 0.89384 0.39383 0.56592 0.01568  -0.03432 -0.00310 260 LEU B N     
3989 C  CA    . LEU B 230 ? 0.88951 0.37786 0.54738 0.01728  -0.03306 -0.00343 260 LEU B CA    
3990 C  C     . LEU B 230 ? 0.86864 0.35546 0.52586 0.02083  -0.04062 -0.00680 260 LEU B C     
3991 O  O     . LEU B 230 ? 0.91990 0.39444 0.56220 0.02468  -0.04263 -0.00795 260 LEU B O     
3992 C  CB    . LEU B 230 ? 0.87873 0.37084 0.53912 0.01354  -0.02538 -0.00163 260 LEU B CB    
3993 C  CG    . LEU B 230 ? 0.78247 0.26550 0.42869 0.01629  -0.02383 -0.00217 260 LEU B CG    
3994 C  CD1   . LEU B 230 ? 0.81191 0.28193 0.43966 0.01793  -0.02253 -0.00040 260 LEU B CD1   
3995 C  CD2   . LEU B 230 ? 0.77548 0.26534 0.42482 0.01391  -0.01654 -0.00083 260 LEU B CD2   
3996 N  N     . HIS B 231 ? 0.85597 0.35500 0.52854 0.01920  -0.04526 -0.00810 261 HIS B N     
3997 C  CA    . HIS B 231 ? 0.83803 0.33625 0.51108 0.02045  -0.05261 -0.01065 261 HIS B CA    
3998 C  C     . HIS B 231 ? 0.98258 0.49638 0.67190 0.01813  -0.05880 -0.01113 261 HIS B C     
3999 O  O     . HIS B 231 ? 1.05881 0.58496 0.76025 0.01567  -0.05628 -0.00957 261 HIS B O     
4000 C  CB    . HIS B 231 ? 0.90310 0.39818 0.57527 0.01876  -0.05024 -0.01084 261 HIS B CB    
4001 C  CG    . HIS B 231 ? 1.03978 0.53031 0.70962 0.01985  -0.05862 -0.01338 261 HIS B CG    
4002 N  ND1   . HIS B 231 ? 1.01117 0.50812 0.69191 0.01552  -0.06243 -0.01359 261 HIS B ND1   
4003 C  CD2   . HIS B 231 ? 1.03360 0.51255 0.69047 0.02443  -0.06451 -0.01567 261 HIS B CD2   
4004 C  CE1   . HIS B 231 ? 0.98305 0.47190 0.65722 0.01695  -0.07080 -0.01577 261 HIS B CE1   
4005 N  NE2   . HIS B 231 ? 0.98676 0.46514 0.64691 0.02263  -0.07207 -0.01723 261 HIS B NE2   
4006 N  N     . SER B 232 ? 0.94910 0.46297 0.63820 0.01884  -0.06722 -0.01312 262 SER B N     
4007 C  CA    . SER B 232 ? 1.02786 0.55877 0.73210 0.01567  -0.07386 -0.01305 262 SER B CA    
4008 C  C     . SER B 232 ? 1.08394 0.62614 0.80358 0.00846  -0.07235 -0.01106 262 SER B C     
4009 O  O     . SER B 232 ? 1.11796 0.67775 0.85231 0.00477  -0.07565 -0.00985 262 SER B O     
4010 C  CB    . SER B 232 ? 1.13686 0.66453 0.83619 0.01686  -0.08359 -0.01521 262 SER B CB    
4011 O  OG    . SER B 232 ? 1.17389 0.68822 0.86550 0.01560  -0.08510 -0.01603 262 SER B OG    
4012 N  N     . GLN B 233 ? 1.00237 0.53566 0.71837 0.00679  -0.06764 -0.01069 263 GLN B N     
4013 C  CA    . GLN B 233 ? 0.98081 0.52232 0.70922 0.00076  -0.06566 -0.00903 263 GLN B CA    
4014 C  C     . GLN B 233 ? 0.90781 0.45026 0.63798 0.00085  -0.05521 -0.00756 263 GLN B C     
4015 O  O     . GLN B 233 ? 0.90813 0.44076 0.62649 0.00485  -0.04978 -0.00776 263 GLN B O     
4016 C  CB    . GLN B 233 ? 1.06674 0.59710 0.78893 -0.00086 -0.07005 -0.01021 263 GLN B CB    
4017 C  CG    . GLN B 233 ? 1.00796 0.53659 0.72850 -0.00261 -0.08141 -0.01126 263 GLN B CG    
4018 C  CD    . GLN B 233 ? 1.31285 0.86141 1.05064 -0.00927 -0.08652 -0.00902 263 GLN B CD    
4019 O  OE1   . GLN B 233 ? 1.43273 0.98989 1.18189 -0.01563 -0.08623 -0.00690 263 GLN B OE1   
4020 N  NE2   . GLN B 233 ? 1.25849 0.81558 0.99795 -0.00757 -0.09134 -0.00941 263 GLN B NE2   
4021 N  N     . PRO B 234 ? 0.93596 0.49046 0.68045 -0.00403 -0.05238 -0.00576 264 PRO B N     
4022 C  CA    . PRO B 234 ? 0.88529 0.44124 0.63185 -0.00433 -0.04273 -0.00439 264 PRO B CA    
4023 C  C     . PRO B 234 ? 0.86802 0.41152 0.60275 -0.00231 -0.03839 -0.00532 264 PRO B C     
4024 O  O     . PRO B 234 ? 0.81665 0.35393 0.54766 -0.00248 -0.04250 -0.00676 264 PRO B O     
4025 C  CB    . PRO B 234 ? 0.88040 0.45155 0.64472 -0.00996 -0.04240 -0.00267 264 PRO B CB    
4026 C  CG    . PRO B 234 ? 0.97753 0.55024 0.74533 -0.01353 -0.05161 -0.00308 264 PRO B CG    
4027 C  CD    . PRO B 234 ? 0.80390 0.37143 0.56288 -0.01004 -0.05812 -0.00460 264 PRO B CD    
4028 N  N     . THR B 235 ? 0.81317 0.35322 0.54095 -0.00027 -0.03056 -0.00437 265 THR B N     
4029 C  CA    . THR B 235 ? 0.80560 0.33785 0.52233 0.00214  -0.02544 -0.00486 265 THR B CA    
4030 C  C     . THR B 235 ? 0.77624 0.31579 0.49759 -0.00003 -0.01588 -0.00277 265 THR B C     
4031 O  O     . THR B 235 ? 0.78737 0.32461 0.50163 0.00193  -0.01137 -0.00316 265 THR B O     
4032 C  CB    . THR B 235 ? 0.86156 0.38131 0.56050 0.00699  -0.02559 -0.00550 265 THR B CB    
4033 O  OG1   . THR B 235 ? 0.74245 0.26235 0.43955 0.00658  -0.02314 -0.00360 265 THR B OG1   
4034 C  CG2   . THR B 235 ? 0.78282 0.29414 0.47564 0.00980  -0.03531 -0.00812 265 THR B CG2   
4035 N  N     . PHE B 236 ? 0.79028 0.33897 0.52246 -0.00345 -0.01293 -0.00067 266 PHE B N     
4036 C  CA    . PHE B 236 ? 0.79685 0.35320 0.53485 -0.00629 -0.00458 0.00140  266 PHE B CA    
4037 C  C     . PHE B 236 ? 0.74600 0.31423 0.50151 -0.00982 -0.00524 0.00150  266 PHE B C     
4038 O  O     . PHE B 236 ? 0.74048 0.31418 0.50519 -0.01113 -0.01039 0.00155  266 PHE B O     
4039 C  CB    . PHE B 236 ? 0.68846 0.24374 0.42299 -0.00755 -0.00090 0.00397  266 PHE B CB    
4040 C  CG    . PHE B 236 ? 0.71837 0.26173 0.43478 -0.00523 0.00025  0.00469  266 PHE B CG    
4041 C  CD1   . PHE B 236 ? 0.76352 0.29705 0.47066 -0.00167 -0.00619 0.00328  266 PHE B CD1   
4042 C  CD2   . PHE B 236 ? 0.78599 0.32913 0.49455 -0.00688 0.00776  0.00707  266 PHE B CD2   
4043 C  CE1   . PHE B 236 ? 0.73207 0.25400 0.42182 0.00042  -0.00521 0.00412  266 PHE B CE1   
4044 C  CE2   . PHE B 236 ? 0.72563 0.25876 0.41715 -0.00555 0.00886  0.00843  266 PHE B CE2   
4045 C  CZ    . PHE B 236 ? 0.73702 0.25865 0.41886 -0.00178 0.00233  0.00690  266 PHE B CZ    
4046 N  N     . PHE B 237 ? 0.70486 0.27826 0.46473 -0.01108 -0.00003 0.00161  267 PHE B N     
4047 C  CA    . PHE B 237 ? 0.76734 0.35045 0.54224 -0.01425 -0.00088 0.00156  267 PHE B CA    
4048 C  C     . PHE B 237 ? 0.74089 0.33302 0.52304 -0.01642 0.00747  0.00312  267 PHE B C     
4049 O  O     . PHE B 237 ? 0.72771 0.32156 0.50914 -0.01562 0.01111  0.00219  267 PHE B O     
4050 C  CB    . PHE B 237 ? 0.70309 0.28093 0.47515 -0.01310 -0.00604 -0.00080 267 PHE B CB    
4051 C  CG    . PHE B 237 ? 0.73196 0.30181 0.49858 -0.01221 -0.01532 -0.00205 267 PHE B CG    
4052 C  CD1   . PHE B 237 ? 0.84569 0.40327 0.59635 -0.00754 -0.01726 -0.00368 267 PHE B CD1   
4053 C  CD2   . PHE B 237 ? 0.73689 0.31290 0.51438 -0.01621 -0.02211 -0.00134 267 PHE B CD2   
4054 C  CE1   . PHE B 237 ? 0.76956 0.31970 0.51513 -0.00675 -0.02614 -0.00493 267 PHE B CE1   
4055 C  CE2   . PHE B 237 ? 0.71384 0.28420 0.48672 -0.01608 -0.03093 -0.00223 267 PHE B CE2   
4056 C  CZ    . PHE B 237 ? 0.68725 0.24396 0.44409 -0.01126 -0.03307 -0.00419 267 PHE B CZ    
4057 N  N     . PRO B 238 ? 0.71840 0.31623 0.50690 -0.01867 0.01017  0.00528  268 PRO B N     
4058 C  CA    . PRO B 238 ? 0.70720 0.31387 0.50356 -0.02135 0.01744  0.00689  268 PRO B CA    
4059 C  C     . PRO B 238 ? 0.69907 0.31487 0.50895 -0.02306 0.01742  0.00613  268 PRO B C     
4060 O  O     . PRO B 238 ? 0.70139 0.32358 0.51580 -0.02426 0.02357  0.00661  268 PRO B O     
4061 C  CB    . PRO B 238 ? 0.71760 0.32593 0.51715 -0.02274 0.01736  0.00894  268 PRO B CB    
4062 C  CG    . PRO B 238 ? 0.78580 0.38410 0.57456 -0.01988 0.01143  0.00835  268 PRO B CG    
4063 C  CD    . PRO B 238 ? 0.70062 0.29650 0.48842 -0.01814 0.00593  0.00602  268 PRO B CD    
4064 N  N     . GLY B 239 ? 0.66383 0.28093 0.48009 -0.02371 0.01048  0.00527  269 GLY B N     
4065 C  CA    . GLY B 239 ? 0.65514 0.27948 0.48284 -0.02614 0.00949  0.00501  269 GLY B CA    
4066 C  C     . GLY B 239 ? 0.71606 0.33356 0.53702 -0.02456 0.00816  0.00278  269 GLY B C     
4067 O  O     . GLY B 239 ? 0.78137 0.40274 0.60981 -0.02651 0.00722  0.00249  269 GLY B O     
4068 N  N     . GLY B 240 ? 0.75557 0.36248 0.56155 -0.02054 0.00772  0.00110  270 GLY B N     
4069 C  CA    . GLY B 240 ? 0.69244 0.29133 0.48904 -0.01710 0.00571  -0.00160 270 GLY B CA    
4070 C  C     . GLY B 240 ? 0.72869 0.31768 0.52113 -0.01771 -0.00477 -0.00284 270 GLY B C     
4071 O  O     . GLY B 240 ? 0.77715 0.36850 0.57628 -0.02161 -0.01026 -0.00132 270 GLY B O     
4072 N  N     . LEU B 241 ? 0.75837 0.33629 0.53868 -0.01353 -0.00810 -0.00568 271 LEU B N     
4073 C  CA    . LEU B 241 ? 0.78409 0.34912 0.55676 -0.01394 -0.01901 -0.00698 271 LEU B CA    
4074 C  C     . LEU B 241 ? 0.79964 0.35413 0.56345 -0.01102 -0.02326 -0.00973 271 LEU B C     
4075 O  O     . LEU B 241 ? 0.87326 0.42758 0.63021 -0.00491 -0.01770 -0.01193 271 LEU B O     
4076 C  CB    . LEU B 241 ? 0.76578 0.32038 0.52412 -0.00933 -0.02180 -0.00836 271 LEU B CB    
4077 C  CG    . LEU B 241 ? 0.85570 0.41324 0.61703 -0.01148 -0.02298 -0.00652 271 LEU B CG    
4078 C  CD1   . LEU B 241 ? 0.87143 0.41599 0.61523 -0.00536 -0.02545 -0.00867 271 LEU B CD1   
4079 C  CD2   . LEU B 241 ? 0.74545 0.30647 0.51711 -0.01814 -0.03137 -0.00481 271 LEU B CD2   
4080 N  N     . ARG B 242 ? 0.72379 0.26931 0.48657 -0.01536 -0.03384 -0.00954 272 ARG B N     
4081 C  CA    . ARG B 242 ? 0.73017 0.25931 0.47944 -0.01230 -0.04126 -0.01243 272 ARG B CA    
4082 C  C     . ARG B 242 ? 0.75030 0.26459 0.47937 -0.00338 -0.04418 -0.01601 272 ARG B C     
4083 O  O     . ARG B 242 ? 0.84856 0.35792 0.57351 -0.00408 -0.04866 -0.01560 272 ARG B O     
4084 C  CB    . ARG B 242 ? 0.78003 0.30306 0.53301 -0.02126 -0.05278 -0.01028 272 ARG B CB    
4085 C  CG    . ARG B 242 ? 0.84965 0.35119 0.58603 -0.01937 -0.06327 -0.01290 272 ARG B CG    
4086 C  CD    . ARG B 242 ? 0.80867 0.30455 0.54815 -0.03037 -0.07557 -0.00964 272 ARG B CD    
4087 N  NE    . ARG B 242 ? 1.01692 0.49980 0.74994 -0.03346 -0.08317 -0.00983 272 ARG B NE    
4088 C  CZ    . ARG B 242 ? 0.96576 0.44197 0.69950 -0.04416 -0.09462 -0.00653 272 ARG B CZ    
4089 N  NH1   . ARG B 242 ? 1.02336 0.50704 0.76521 -0.05274 -0.09972 -0.00282 272 ARG B NH1   
4090 N  NH2   . ARG B 242 ? 0.98919 0.45115 0.71461 -0.04648 -0.10149 -0.00682 272 ARG B NH2   
4091 N  N     . PHE B 243 ? 0.78815 0.29627 0.50427 0.00571  -0.04171 -0.01966 273 PHE B N     
4092 C  CA    . PHE B 243 ? 0.78843 0.28637 0.48581 0.01565  -0.04251 -0.02299 273 PHE B CA    
4093 C  C     . PHE B 243 ? 0.87414 0.34929 0.55529 0.01735  -0.05646 -0.02534 273 PHE B C     
4094 O  O     . PHE B 243 ? 0.89547 0.35849 0.57216 0.01525  -0.06511 -0.02625 273 PHE B O     
4095 C  CB    . PHE B 243 ? 0.84211 0.34352 0.53000 0.02611  -0.03535 -0.02629 273 PHE B CB    
4096 C  CG    . PHE B 243 ? 0.86186 0.35336 0.52911 0.03732  -0.03703 -0.02987 273 PHE B CG    
4097 C  CD1   . PHE B 243 ? 0.81031 0.31067 0.47638 0.03965  -0.02974 -0.02861 273 PHE B CD1   
4098 C  CD2   . PHE B 243 ? 0.88579 0.35783 0.53350 0.04560  -0.04672 -0.03440 273 PHE B CD2   
4099 C  CE1   . PHE B 243 ? 0.78927 0.28171 0.43627 0.05009  -0.03113 -0.03163 273 PHE B CE1   
4100 C  CE2   . PHE B 243 ? 0.94147 0.40465 0.56931 0.05709  -0.04862 -0.03793 273 PHE B CE2   
4101 C  CZ    . PHE B 243 ? 0.95725 0.43176 0.58537 0.05930  -0.04043 -0.03644 273 PHE B CZ    
4102 N  N     . SER B 244 ? 0.83222 0.30053 0.50355 0.02095  -0.05907 -0.02619 274 SER B N     
4103 C  CA    . SER B 244 ? 0.88365 0.32908 0.53421 0.02674  -0.07091 -0.02967 274 SER B CA    
4104 C  C     . SER B 244 ? 0.93164 0.37591 0.57041 0.03552  -0.06732 -0.03144 274 SER B C     
4105 O  O     . SER B 244 ? 0.95276 0.41090 0.60116 0.03297  -0.05919 -0.02881 274 SER B O     
4106 C  CB    . SER B 244 ? 0.83946 0.27412 0.49281 0.01657  -0.08368 -0.02753 274 SER B CB    
4107 O  OG    . SER B 244 ? 0.87507 0.31774 0.53691 0.01177  -0.08257 -0.02492 274 SER B OG    
4108 N  N     . VAL B 245 ? 0.89657 0.32345 0.51312 0.04635  -0.07378 -0.03596 275 VAL B N     
4109 C  CA    . VAL B 245 ? 0.93552 0.36039 0.53883 0.05554  -0.07119 -0.03779 275 VAL B CA    
4110 C  C     . VAL B 245 ? 0.89799 0.32181 0.50708 0.04856  -0.07437 -0.03513 275 VAL B C     
4111 O  O     . VAL B 245 ? 0.97938 0.41368 0.59126 0.04965  -0.06635 -0.03354 275 VAL B O     
4112 C  CB    . VAL B 245 ? 0.98343 0.38694 0.56067 0.06847  -0.08047 -0.04339 275 VAL B CB    
4113 C  CG1   . VAL B 245 ? 1.12796 0.52405 0.69113 0.07563  -0.08243 -0.04493 275 VAL B CG1   
4114 C  CG2   . VAL B 245 ? 0.96714 0.37780 0.53695 0.07929  -0.07363 -0.04644 275 VAL B CG2   
4115 N  N     . CYS B 246 ? 0.94366 0.35535 0.55441 0.04082  -0.08641 -0.03436 276 CYS B N     
4116 C  CA    . CYS B 246 ? 1.02043 0.43070 0.63472 0.03539  -0.09092 -0.03248 276 CYS B CA    
4117 C  C     . CYS B 246 ? 0.98719 0.41925 0.62312 0.02702  -0.08158 -0.02803 276 CYS B C     
4118 O  O     . CYS B 246 ? 0.98199 0.41789 0.61855 0.02747  -0.07906 -0.02710 276 CYS B O     
4119 C  CB    . CYS B 246 ? 1.12639 0.52071 0.73769 0.02813  -0.10638 -0.03227 276 CYS B CB    
4120 S  SG    . CYS B 246 ? 1.53962 0.90272 1.12049 0.03916  -0.12000 -0.03792 276 CYS B SG    
4121 N  N     . LEU B 247 ? 0.96970 0.41512 0.62212 0.02011  -0.07675 -0.02546 277 LEU B N     
4122 C  CA    . LEU B 247 ? 0.85159 0.31696 0.52302 0.01358  -0.06805 -0.02162 277 LEU B CA    
4123 C  C     . LEU B 247 ? 0.88953 0.36399 0.55850 0.01985  -0.05572 -0.02158 277 LEU B C     
4124 O  O     . LEU B 247 ? 0.81065 0.29164 0.48370 0.01837  -0.05187 -0.01971 277 LEU B O     
4125 C  CB    . LEU B 247 ? 0.87704 0.35419 0.56555 0.00563  -0.06584 -0.01908 277 LEU B CB    
4126 C  CG    . LEU B 247 ? 0.82883 0.32635 0.53626 0.00002  -0.05698 -0.01544 277 LEU B CG    
4127 C  CD1   . LEU B 247 ? 0.93406 0.43488 0.64708 -0.00464 -0.06194 -0.01360 277 LEU B CD1   
4128 C  CD2   . LEU B 247 ? 0.75091 0.25939 0.47375 -0.00658 -0.05481 -0.01331 277 LEU B CD2   
4129 N  N     . PHE B 248 ? 0.80133 0.27667 0.46288 0.02675  -0.04977 -0.02347 278 PHE B N     
4130 C  CA    . PHE B 248 ? 0.78038 0.26746 0.44102 0.03072  -0.03773 -0.02241 278 PHE B CA    
4131 C  C     . PHE B 248 ? 0.81239 0.29192 0.45721 0.03763  -0.03794 -0.02360 278 PHE B C     
4132 O  O     . PHE B 248 ? 0.92968 0.41865 0.57364 0.03892  -0.02871 -0.02166 278 PHE B O     
4133 C  CB    . PHE B 248 ? 0.81197 0.30584 0.47008 0.03598  -0.03101 -0.02384 278 PHE B CB    
4134 C  CG    . PHE B 248 ? 0.75845 0.26741 0.43522 0.02875  -0.02465 -0.02122 278 PHE B CG    
4135 C  CD1   . PHE B 248 ? 0.75263 0.26167 0.44314 0.02010  -0.03012 -0.01962 278 PHE B CD1   
4136 C  CD2   . PHE B 248 ? 0.74927 0.27316 0.42959 0.03043  -0.01348 -0.02013 278 PHE B CD2   
4137 C  CE1   . PHE B 248 ? 0.84862 0.37147 0.55579 0.01413  -0.02439 -0.01730 278 PHE B CE1   
4138 C  CE2   . PHE B 248 ? 0.76681 0.30379 0.46384 0.02407  -0.00802 -0.01789 278 PHE B CE2   
4139 C  CZ    . PHE B 248 ? 0.78127 0.31710 0.49148 0.01638  -0.01351 -0.01666 278 PHE B CZ    
4140 N  N     . ARG B 249 ? 0.88459 0.34705 0.51632 0.04165  -0.04844 -0.02645 279 ARG B N     
4141 C  CA    . ARG B 249 ? 0.83921 0.29469 0.45734 0.04741  -0.04902 -0.02726 279 ARG B CA    
4142 C  C     . ARG B 249 ? 0.87338 0.33305 0.50048 0.04074  -0.04842 -0.02424 279 ARG B C     
4143 O  O     . ARG B 249 ? 0.89343 0.35110 0.51144 0.04449  -0.04567 -0.02389 279 ARG B O     
4144 C  CB    . ARG B 249 ? 0.84811 0.28307 0.44923 0.05375  -0.06124 -0.03133 279 ARG B CB    
4145 C  CG    . ARG B 249 ? 0.95661 0.38410 0.54083 0.06504  -0.06219 -0.03537 279 ARG B CG    
4146 C  CD    . ARG B 249 ? 0.98649 0.39087 0.55328 0.07060  -0.07603 -0.03928 279 ARG B CD    
4147 N  NE    . ARG B 249 ? 1.25672 0.65078 0.80425 0.08316  -0.07911 -0.04391 279 ARG B NE    
4148 C  CZ    . ARG B 249 ? 1.37526 0.74777 0.90284 0.09119  -0.09069 -0.04802 279 ARG B CZ    
4149 N  NH1   . ARG B 249 ? 1.32043 0.67983 0.84533 0.08722  -0.10018 -0.04791 279 ARG B NH1   
4150 N  NH2   . ARG B 249 ? 1.25568 0.61973 0.76490 0.10407  -0.09319 -0.05256 279 ARG B NH2   
4151 N  N     . ARG B 250 ? 0.89485 0.36030 0.53846 0.03158  -0.05137 -0.02216 280 ARG B N     
4152 C  CA    . ARG B 250 ? 0.87071 0.34023 0.52189 0.02664  -0.05226 -0.01996 280 ARG B CA    
4153 C  C     . ARG B 250 ? 0.80359 0.28981 0.47250 0.01981  -0.04461 -0.01644 280 ARG B C     
4154 O  O     . ARG B 250 ? 0.76630 0.25849 0.44673 0.01416  -0.04774 -0.01483 280 ARG B O     
4155 C  CB    . ARG B 250 ? 0.96944 0.43135 0.62248 0.02286  -0.06469 -0.02085 280 ARG B CB    
4156 C  CG    . ARG B 250 ? 1.08971 0.55420 0.75368 0.01612  -0.07021 -0.02026 280 ARG B CG    
4157 C  CD    . ARG B 250 ? 1.17049 0.62806 0.83489 0.01129  -0.08318 -0.02048 280 ARG B CD    
4158 N  NE    . ARG B 250 ? 1.21203 0.67767 0.89116 0.00187  -0.08737 -0.01815 280 ARG B NE    
4159 C  CZ    . ARG B 250 ? 1.33451 0.79098 1.01003 -0.00038 -0.09380 -0.01885 280 ARG B CZ    
4160 N  NH1   . ARG B 250 ? 1.50149 0.93961 1.15845 0.00713  -0.09752 -0.02238 280 ARG B NH1   
4161 N  NH2   . ARG B 250 ? 1.23816 0.70368 0.92786 -0.00994 -0.09696 -0.01596 280 ARG B NH2   
4162 N  N     . ILE B 251 ? 0.76832 0.26297 0.43913 0.02069  -0.03482 -0.01528 281 ILE B N     
4163 C  CA    . ILE B 251 ? 0.75113 0.25977 0.43564 0.01518  -0.02704 -0.01193 281 ILE B CA    
4164 C  C     . ILE B 251 ? 0.78574 0.29745 0.46186 0.01800  -0.01745 -0.01031 281 ILE B C     
4165 O  O     . ILE B 251 ? 0.81880 0.32610 0.48123 0.02418  -0.01540 -0.01172 281 ILE B O     
4166 C  CB    . ILE B 251 ? 0.73677 0.25550 0.43577 0.01067  -0.02482 -0.01120 281 ILE B CB    
4167 C  CG1   . ILE B 251 ? 0.74871 0.26830 0.44091 0.01545  -0.01947 -0.01263 281 ILE B CG1   
4168 C  CG2   . ILE B 251 ? 0.73598 0.25167 0.44205 0.00675  -0.03477 -0.01209 281 ILE B CG2   
4169 C  CD1   . ILE B 251 ? 0.80341 0.33475 0.50924 0.01152  -0.01456 -0.01152 281 ILE B CD1   
4170 N  N     . VAL B 252 ? 0.74372 0.26338 0.42744 0.01332  -0.01195 -0.00710 282 VAL B N     
4171 C  CA    . VAL B 252 ? 0.74639 0.26952 0.42296 0.01350  -0.00321 -0.00445 282 VAL B CA    
4172 C  C     . VAL B 252 ? 0.73436 0.27084 0.42002 0.01033  0.00503  -0.00260 282 VAL B C     
4173 O  O     . VAL B 252 ? 0.74770 0.28896 0.42577 0.01247  0.01161  -0.00169 282 VAL B O     
4174 C  CB    . VAL B 252 ? 0.74721 0.26719 0.42239 0.01053  -0.00331 -0.00195 282 VAL B CB    
4175 C  CG1   . VAL B 252 ? 0.82575 0.34987 0.49523 0.00800  0.00549  0.00186  282 VAL B CG1   
4176 C  CG2   . VAL B 252 ? 0.76201 0.26872 0.42465 0.01502  -0.01034 -0.00388 282 VAL B CG2   
4177 N  N     . ALA B 253 ? 0.80284 0.34693 0.50463 0.00539  0.00492  -0.00194 283 ALA B N     
4178 C  CA    . ALA B 253 ? 0.79686 0.35354 0.50731 0.00200  0.01297  0.00009  283 ALA B CA    
4179 C  C     . ALA B 253 ? 0.72422 0.28710 0.45009 -0.00042 0.01069  -0.00112 283 ALA B C     
4180 O  O     . ALA B 253 ? 0.70672 0.26867 0.44143 -0.00312 0.00497  -0.00124 283 ALA B O     
4181 C  CB    . ALA B 253 ? 0.70317 0.26322 0.41581 -0.00330 0.01768  0.00411  283 ALA B CB    
4182 N  N     . CYS B 254 ? 0.71391 0.28417 0.44258 0.00069  0.01516  -0.00190 284 CYS B N     
4183 C  CA    . CYS B 254 ? 0.75500 0.33097 0.49741 -0.00179 0.01364  -0.00278 284 CYS B CA    
4184 C  C     . CYS B 254 ? 0.73728 0.32643 0.48693 -0.00381 0.02253  -0.00121 284 CYS B C     
4185 O  O     . CYS B 254 ? 0.73608 0.32951 0.47769 -0.00026 0.02802  -0.00157 284 CYS B O     
4186 C  CB    . CYS B 254 ? 0.75688 0.32470 0.49361 0.00273  0.00704  -0.00650 284 CYS B CB    
4187 S  SG    . CYS B 254 ? 0.82514 0.39790 0.57679 -0.00106 0.00424  -0.00719 284 CYS B SG    
4188 N  N     . HIS B 255 ? 0.71004 0.30676 0.47476 -0.00916 0.02372  0.00050  285 HIS B N     
4189 C  CA    . HIS B 255 ? 0.74069 0.34990 0.51438 -0.01215 0.03144  0.00226  285 HIS B CA    
4190 C  C     . HIS B 255 ? 0.79907 0.41312 0.57901 -0.01036 0.03159  -0.00017 285 HIS B C     
4191 O  O     . HIS B 255 ? 0.75715 0.36350 0.53465 -0.00773 0.02489  -0.00286 285 HIS B O     
4192 C  CB    . HIS B 255 ? 0.73340 0.34648 0.51865 -0.01782 0.03159  0.00504  285 HIS B CB    
4193 C  CG    . HIS B 255 ? 0.73849 0.36237 0.53090 -0.02155 0.03921  0.00746  285 HIS B CG    
4194 N  ND1   . HIS B 255 ? 0.68826 0.31803 0.49412 -0.02533 0.03937  0.00881  285 HIS B ND1   
4195 C  CD2   . HIS B 255 ? 0.71725 0.34785 0.50500 -0.02223 0.04656  0.00894  285 HIS B CD2   
4196 C  CE1   . HIS B 255 ? 0.70586 0.34368 0.51474 -0.02827 0.04619  0.01085  285 HIS B CE1   
4197 N  NE2   . HIS B 255 ? 0.85612 0.49531 0.65453 -0.02696 0.05070  0.01115  285 HIS B NE2   
4198 N  N     . PHE B 256 ? 0.78723 0.41323 0.57416 -0.01200 0.03883  0.00087  286 PHE B N     
4199 C  CA    . PHE B 256 ? 0.76039 0.39206 0.55421 -0.01048 0.03973  -0.00127 286 PHE B CA    
4200 C  C     . PHE B 256 ? 0.82590 0.45298 0.60670 -0.00256 0.03822  -0.00512 286 PHE B C     
4201 O  O     . PHE B 256 ? 0.88959 0.51100 0.67046 -0.00004 0.03307  -0.00794 286 PHE B O     
4202 C  CB    . PHE B 256 ? 0.75237 0.38146 0.55808 -0.01395 0.03351  -0.00143 286 PHE B CB    
4203 C  CG    . PHE B 256 ? 0.75010 0.38659 0.56936 -0.01996 0.03544  0.00176  286 PHE B CG    
4204 C  CD1   . PHE B 256 ? 0.84051 0.48732 0.66530 -0.02231 0.04318  0.00376  286 PHE B CD1   
4205 C  CD2   . PHE B 256 ? 0.77374 0.40734 0.59929 -0.02286 0.02910  0.00275  286 PHE B CD2   
4206 C  CE1   . PHE B 256 ? 0.90964 0.56131 0.74502 -0.02686 0.04407  0.00638  286 PHE B CE1   
4207 C  CE2   . PHE B 256 ? 0.73345 0.37417 0.56995 -0.02664 0.03042  0.00526  286 PHE B CE2   
4208 C  CZ    . PHE B 256 ? 0.79376 0.44225 0.63463 -0.02832 0.03765  0.00690  286 PHE B CZ    
4209 N  N     . ILE B 257 ? 0.86701 0.49684 0.63578 0.00154  0.04257  -0.00513 287 ILE B N     
4210 C  CA    . ILE B 257 ? 0.80774 0.43433 0.56201 0.01088  0.04127  -0.00902 287 ILE B CA    
4211 C  C     . ILE B 257 ? 0.86531 0.50922 0.61781 0.01366  0.05070  -0.00860 287 ILE B C     
4212 O  O     . ILE B 257 ? 0.81935 0.47193 0.56923 0.01091  0.05675  -0.00521 287 ILE B O     
4213 C  CB    . ILE B 257 ? 0.80090 0.41540 0.54010 0.01491  0.03662  -0.00979 287 ILE B CB    
4214 C  CG1   . ILE B 257 ? 0.83153 0.42982 0.57213 0.01285  0.02621  -0.01087 287 ILE B CG1   
4215 C  CG2   . ILE B 257 ? 0.81557 0.42992 0.53824 0.02569  0.03697  -0.01345 287 ILE B CG2   
4216 C  CD1   . ILE B 257 ? 0.93763 0.52315 0.66470 0.01609  0.02080  -0.01160 287 ILE B CD1   
4217 N  N     . LYS B 258 ? 0.83739 0.48678 0.59085 0.01880  0.05165  -0.01184 288 LYS B N     
4218 C  CA    . LYS B 258 ? 0.88363 0.55187 0.63558 0.02248  0.06021  -0.01201 288 LYS B CA    
4219 C  C     . LYS B 258 ? 0.92922 0.59939 0.66264 0.03295  0.06071  -0.01457 288 LYS B C     
4220 O  O     . LYS B 258 ? 1.00104 0.65506 0.72219 0.03899  0.05322  -0.01750 288 LYS B O     
4221 C  CB    . LYS B 258 ? 0.89318 0.56619 0.65223 0.02521  0.06049  -0.01503 288 LYS B CB    
4222 C  CG    . LYS B 258 ? 1.28595 0.94651 1.03171 0.03625  0.05317  -0.02101 288 LYS B CG    
4223 C  CD    . LYS B 258 ? 1.38799 1.05288 1.13934 0.03919  0.05356  -0.02398 288 LYS B CD    
4224 C  CE    . LYS B 258 ? 1.36817 1.02064 1.10214 0.05191  0.04641  -0.03026 288 LYS B CE    
4225 N  NZ    . LYS B 258 ? 1.42955 1.08977 1.16564 0.05713  0.04847  -0.03354 288 LYS B NZ    
4226 N  N     . PRO B 259 ? 0.94781 0.63873 0.67864 0.03546  0.06925  -0.01346 289 PRO B N     
4227 C  CA    . PRO B 259 ? 0.98666 0.68306 0.69978 0.04545  0.07056  -0.01517 289 PRO B CA    
4228 C  C     . PRO B 259 ? 0.95428 0.63705 0.65251 0.05926  0.06261  -0.02207 289 PRO B C     
4229 O  O     . PRO B 259 ? 0.96858 0.63944 0.65235 0.06525  0.05765  -0.02366 289 PRO B O     
4230 C  CB    . PRO B 259 ? 0.98654 0.71146 0.70275 0.04542  0.08097  -0.01306 289 PRO B CB    
4231 C  CG    . PRO B 259 ? 0.89258 0.62356 0.62700 0.03134  0.08537  -0.00786 289 PRO B CG    
4232 C  CD    . PRO B 259 ? 0.85058 0.56220 0.59436 0.02870  0.07803  -0.01007 289 PRO B CD    
4233 N  N     . ARG B 260 ? 0.96267 0.64565 0.66248 0.06493  0.06074  -0.02634 290 ARG B N     
4234 C  CA    . ARG B 260 ? 1.00198 0.66845 0.68546 0.07806  0.05171  -0.03304 290 ARG B CA    
4235 C  C     . ARG B 260 ? 0.98153 0.62030 0.66000 0.07556  0.04087  -0.03364 290 ARG B C     
4236 O  O     . ARG B 260 ? 0.98358 0.60895 0.64404 0.08510  0.03428  -0.03712 290 ARG B O     
4237 C  CB    . ARG B 260 ? 1.17021 0.83660 0.85800 0.08161  0.05006  -0.03681 290 ARG B CB    
4238 C  CG    . ARG B 260 ? 1.29515 0.93932 0.96515 0.09393  0.03874  -0.04365 290 ARG B CG    
4239 C  CD    . ARG B 260 ? 1.28365 0.93648 0.93335 0.11106  0.03972  -0.04855 290 ARG B CD    
4240 N  NE    . ARG B 260 ? 1.44245 1.08231 1.07553 0.11709  0.03424  -0.04965 290 ARG B NE    
4241 C  CZ    . ARG B 260 ? 1.47085 1.12619 1.09252 0.12580  0.03934  -0.04991 290 ARG B CZ    
4242 N  NH1   . ARG B 260 ? 1.44794 1.13413 1.07383 0.12826  0.05034  -0.04850 290 ARG B NH1   
4243 N  NH2   . ARG B 260 ? 1.32643 0.96703 0.93221 0.13183  0.03319  -0.05134 290 ARG B NH2   
4244 N  N     . THR B 261 ? 0.91839 0.54935 0.61248 0.06302  0.03871  -0.03026 291 THR B N     
4245 C  CA    . THR B 261 ? 0.85556 0.46329 0.54695 0.05933  0.02848  -0.03031 291 THR B CA    
4246 C  C     . THR B 261 ? 0.96583 0.56968 0.64744 0.06043  0.02809  -0.02880 291 THR B C     
4247 O  O     . THR B 261 ? 0.94750 0.53218 0.61635 0.06494  0.01884  -0.03138 291 THR B O     
4248 C  CB    . THR B 261 ? 0.78489 0.39107 0.49611 0.04576  0.02786  -0.02631 291 THR B CB    
4249 O  OG1   . THR B 261 ? 0.95369 0.56446 0.67405 0.04478  0.02878  -0.02750 291 THR B OG1   
4250 C  CG2   . THR B 261 ? 0.85131 0.43604 0.56006 0.04203  0.01675  -0.02643 291 THR B CG2   
4251 N  N     . LEU B 262 ? 0.80549 0.42637 0.49230 0.05580  0.03754  -0.02441 292 LEU B N     
4252 C  CA    . LEU B 262 ? 0.79009 0.40763 0.46744 0.05617  0.03766  -0.02245 292 LEU B CA    
4253 C  C     . LEU B 262 ? 0.89351 0.50894 0.54974 0.07043  0.03556  -0.02674 292 LEU B C     
4254 O  O     . LEU B 262 ? 0.94804 0.54858 0.59201 0.07430  0.02932  -0.02800 292 LEU B O     
4255 C  CB    . LEU B 262 ? 0.85269 0.48881 0.53833 0.04779  0.04808  -0.01648 292 LEU B CB    
4256 C  CG    . LEU B 262 ? 0.88149 0.51649 0.55653 0.04756  0.04961  -0.01366 292 LEU B CG    
4257 C  CD1   . LEU B 262 ? 0.86113 0.47431 0.53451 0.04452  0.04084  -0.01382 292 LEU B CD1   
4258 C  CD2   . LEU B 262 ? 0.80806 0.46023 0.49063 0.03778  0.05923  -0.00721 292 LEU B CD2   
4259 N  N     . LEU B 263 ? 0.83002 0.46134 0.48131 0.07907  0.04070  -0.02914 293 LEU B N     
4260 C  CA    . LEU B 263 ? 0.89685 0.52724 0.52684 0.09472  0.03821  -0.03388 293 LEU B CA    
4261 C  C     . LEU B 263 ? 0.98116 0.58326 0.59815 0.10256  0.02468  -0.03970 293 LEU B C     
4262 O  O     . LEU B 263 ? 1.05473 0.64483 0.65386 0.11183  0.01888  -0.04253 293 LEU B O     
4263 C  CB    . LEU B 263 ? 0.84690 0.50112 0.47481 0.10316  0.04568  -0.03581 293 LEU B CB    
4264 C  CG    . LEU B 263 ? 0.93853 0.62194 0.57686 0.09510  0.05863  -0.02952 293 LEU B CG    
4265 C  CD1   . LEU B 263 ? 0.93844 0.64717 0.57861 0.10133  0.06581  -0.03113 293 LEU B CD1   
4266 C  CD2   . LEU B 263 ? 0.93455 0.62418 0.56090 0.09745  0.06164  -0.02679 293 LEU B CD2   
4267 N  N     . ASP B 264 ? 0.89878 0.48910 0.52428 0.09803  0.01900  -0.04111 294 ASP B N     
4268 C  CA    . ASP B 264 ? 0.97534 0.53737 0.58830 0.10317  0.00514  -0.04578 294 ASP B CA    
4269 C  C     . ASP B 264 ? 1.00575 0.54941 0.61774 0.09639  -0.00219 -0.04376 294 ASP B C     
4270 O  O     . ASP B 264 ? 0.95190 0.47489 0.54623 0.10408  -0.01249 -0.04751 294 ASP B O     
4271 C  CB    . ASP B 264 ? 0.99727 0.55226 0.62002 0.09815  0.00103  -0.04677 294 ASP B CB    
4272 C  CG    . ASP B 264 ? 1.07628 0.64227 0.69344 0.10882  0.00442  -0.05091 294 ASP B CG    
4273 O  OD1   . ASP B 264 ? 1.08052 0.65204 0.68023 0.12340  0.00546  -0.05487 294 ASP B OD1   
4274 O  OD2   . ASP B 264 ? 1.06764 0.63758 0.69755 0.10320  0.00600  -0.05031 294 ASP B OD2   
4275 N  N     . TYR B 265 ? 0.90705 0.45724 0.53703 0.08250  0.00228  -0.03811 295 TYR B N     
4276 C  CA    . TYR B 265 ? 0.90335 0.43859 0.53293 0.07647  -0.00423 -0.03623 295 TYR B CA    
4277 C  C     . TYR B 265 ? 0.86855 0.40270 0.48180 0.08473  -0.00338 -0.03702 295 TYR B C     
4278 O  O     . TYR B 265 ? 0.85536 0.37017 0.45645 0.08803  -0.01288 -0.03910 295 TYR B O     
4279 C  CB    . TYR B 265 ? 0.93698 0.48165 0.58778 0.06183  0.00102  -0.03038 295 TYR B CB    
4280 C  CG    . TYR B 265 ? 0.89380 0.43634 0.56104 0.05235  -0.00211 -0.02908 295 TYR B CG    
4281 C  CD1   . TYR B 265 ? 0.93306 0.46476 0.59625 0.05553  -0.00935 -0.03257 295 TYR B CD1   
4282 C  CD2   . TYR B 265 ? 0.89587 0.44706 0.58167 0.04051  0.00187  -0.02428 295 TYR B CD2   
4283 C  CE1   . TYR B 265 ? 0.84936 0.38023 0.52756 0.04619  -0.01202 -0.03077 295 TYR B CE1   
4284 C  CE2   . TYR B 265 ? 0.84183 0.39329 0.54279 0.03232  -0.00067 -0.02287 295 TYR B CE2   
4285 C  CZ    . TYR B 265 ? 0.89886 0.44087 0.59649 0.03473  -0.00733 -0.02587 295 TYR B CZ    
4286 O  OH    . TYR B 265 ? 0.98604 0.52918 0.69849 0.02610  -0.00978 -0.02397 295 TYR B OH    
4287 N  N     . TRP B 266 ? 0.93682 0.49212 0.54944 0.08761  0.00776  -0.03505 296 TRP B N     
4288 C  CA    . TRP B 266 ? 0.88480 0.44167 0.48152 0.09561  0.00939  -0.03535 296 TRP B CA    
4289 C  C     . TRP B 266 ? 0.95839 0.50108 0.53257 0.11166  0.00078  -0.04200 296 TRP B C     
4290 O  O     . TRP B 266 ? 0.94213 0.46936 0.50207 0.11703  -0.00605 -0.04378 296 TRP B O     
4291 C  CB    . TRP B 266 ? 0.83945 0.42409 0.43927 0.09534  0.02279  -0.03165 296 TRP B CB    
4292 C  CG    . TRP B 266 ? 0.94101 0.52900 0.53003 0.09751  0.02588  -0.02924 296 TRP B CG    
4293 C  CD1   . TRP B 266 ? 0.93634 0.53361 0.50805 0.11003  0.02855  -0.03107 296 TRP B CD1   
4294 C  CD2   . TRP B 266 ? 0.97379 0.55593 0.56745 0.08751  0.02632  -0.02461 296 TRP B CD2   
4295 N  NE1   . TRP B 266 ? 1.00676 0.60421 0.57242 0.10757  0.03088  -0.02744 296 TRP B NE1   
4296 C  CE2   . TRP B 266 ? 0.99320 0.58047 0.57169 0.09388  0.02940  -0.02358 296 TRP B CE2   
4297 C  CE3   . TRP B 266 ? 0.93735 0.51088 0.54566 0.07456  0.02421  -0.02137 296 TRP B CE3   
4298 C  CZ2   . TRP B 266 ? 1.03178 0.61404 0.60900 0.08715  0.03027  -0.01938 296 TRP B CZ2   
4299 C  CZ3   . TRP B 266 ? 1.03309 0.60205 0.63973 0.06887  0.02487  -0.01764 296 TRP B CZ3   
4300 C  CH2   . TRP B 266 ? 1.10462 0.67696 0.69559 0.07495  0.02776  -0.01668 296 TRP B CH2   
4301 N  N     . GLN B 267 ? 0.94300 0.48970 0.51261 0.12014  0.00040  -0.04603 297 GLN B N     
4302 C  CA    . GLN B 267 ? 0.99127 0.52180 0.53763 0.13644  -0.00924 -0.05299 297 GLN B CA    
4303 C  C     . GLN B 267 ? 0.98554 0.48351 0.52514 0.13413  -0.02430 -0.05531 297 GLN B C     
4304 O  O     . GLN B 267 ? 0.98214 0.46276 0.50144 0.14454  -0.03298 -0.05921 297 GLN B O     
4305 C  CB    . GLN B 267 ? 0.97729 0.51589 0.52117 0.14476  -0.00795 -0.05693 297 GLN B CB    
4306 C  CG    . GLN B 267 ? 1.08598 0.61240 0.60278 0.16487  -0.01625 -0.06454 297 GLN B CG    
4307 C  CD    . GLN B 267 ? 1.30284 0.84318 0.80445 0.17726  -0.01119 -0.06531 297 GLN B CD    
4308 O  OE1   . GLN B 267 ? 1.46750 1.03847 0.97446 0.17878  0.00136  -0.06271 297 GLN B OE1   
4309 N  NE2   . GLN B 267 ? 1.18780 0.70620 0.67010 0.18576  -0.02118 -0.06860 297 GLN B NE2   
4310 N  N     . ALA B 268 ? 0.89838 0.38860 0.45439 0.12053  -0.02782 -0.05282 298 ALA B N     
4311 C  CA    . ALA B 268 ? 0.88170 0.34391 0.43317 0.11589  -0.04203 -0.05392 298 ALA B CA    
4312 C  C     . ALA B 268 ? 0.95078 0.40461 0.49617 0.11500  -0.04512 -0.05264 298 ALA B C     
4313 O  O     . ALA B 268 ? 1.03397 0.46455 0.56211 0.12097  -0.05720 -0.05613 298 ALA B O     
4314 C  CB    . ALA B 268 ? 0.86197 0.32447 0.43554 0.09960  -0.04281 -0.04990 298 ALA B CB    
4315 N  N     . LEU B 269 ? 1.00047 0.47197 0.55880 0.10765  -0.03478 -0.04767 299 LEU B N     
4316 C  CA    . LEU B 269 ? 0.90889 0.37297 0.46205 0.10636  -0.03719 -0.04622 299 LEU B CA    
4317 C  C     . LEU B 269 ? 1.06433 0.52413 0.59370 0.12227  -0.03862 -0.05015 299 LEU B C     
4318 O  O     . LEU B 269 ? 0.97803 0.41942 0.49450 0.12594  -0.04755 -0.05205 299 LEU B O     
4319 C  CB    . LEU B 269 ? 0.85736 0.34031 0.42795 0.09537  -0.02596 -0.04006 299 LEU B CB    
4320 C  CG    . LEU B 269 ? 0.95957 0.44346 0.55193 0.08039  -0.02685 -0.03647 299 LEU B CG    
4321 C  CD1   . LEU B 269 ? 0.83482 0.34121 0.44438 0.07168  -0.01394 -0.03114 299 LEU B CD1   
4322 C  CD2   . LEU B 269 ? 0.87897 0.34575 0.47159 0.07451  -0.03694 -0.03594 299 LEU B CD2   
4323 N  N     . GLU B 270 ? 1.06713 0.54477 0.59016 0.13223  -0.03014 -0.05146 300 GLU B N     
4324 C  CA    . GLU B 270 ? 1.18580 0.66103 0.68502 0.14921  -0.03195 -0.05567 300 GLU B CA    
4325 C  C     . GLU B 270 ? 1.16564 0.61215 0.64477 0.16007  -0.04754 -0.06243 300 GLU B C     
4326 O  O     . GLU B 270 ? 1.27067 0.69946 0.73295 0.16720  -0.05593 -0.06504 300 GLU B O     
4327 C  CB    . GLU B 270 ? 1.09590 0.59888 0.59288 0.15795  -0.02018 -0.05579 300 GLU B CB    
4328 C  CG    . GLU B 270 ? 1.26810 0.79868 0.78016 0.14808  -0.00547 -0.04878 300 GLU B CG    
4329 C  CD    . GLU B 270 ? 1.62062 1.15139 1.12378 0.14924  -0.00350 -0.04628 300 GLU B CD    
4330 O  OE1   . GLU B 270 ? 1.54611 1.06025 1.02963 0.16098  -0.01195 -0.05063 300 GLU B OE1   
4331 O  OE2   . GLU B 270 ? 1.58805 1.13442 1.10281 0.13845  0.00604  -0.03995 300 GLU B OE2   
4332 N  N     . ASN B 271 ? 1.07931 0.51912 0.55922 0.16096  -0.05234 -0.06522 301 ASN B N     
4333 C  CA    . ASN B 271 ? 1.10639 0.51744 0.56472 0.17157  -0.06780 -0.07168 301 ASN B CA    
4334 C  C     . ASN B 271 ? 1.07063 0.45323 0.52500 0.16425  -0.08146 -0.07146 301 ASN B C     
4335 O  O     . ASN B 271 ? 1.11260 0.46977 0.54377 0.17482  -0.09472 -0.07657 301 ASN B O     
4336 C  CB    . ASN B 271 ? 1.05559 0.46342 0.51833 0.17002  -0.07059 -0.07349 301 ASN B CB    
4337 C  CG    . ASN B 271 ? 1.06117 0.49452 0.52348 0.18029  -0.05946 -0.07520 301 ASN B CG    
4338 O  OD1   . ASN B 271 ? 1.21908 0.67162 0.67431 0.19056  -0.05100 -0.07565 301 ASN B OD1   
4339 N  ND2   . ASN B 271 ? 1.03961 0.47452 0.50949 0.17740  -0.05945 -0.07598 301 ASN B ND2   
4340 N  N     . SER B 272 ? 1.10315 0.48951 0.57907 0.14664  -0.07917 -0.06577 302 SER B N     
4341 C  CA    . SER B 272 ? 1.08619 0.44977 0.56129 0.13804  -0.09154 -0.06492 302 SER B CA    
4342 C  C     . SER B 272 ? 1.06732 0.43303 0.54075 0.13787  -0.08914 -0.06307 302 SER B C     
4343 O  O     . SER B 272 ? 1.14105 0.49078 0.61481 0.13070  -0.09849 -0.06214 302 SER B O     
4344 C  CB    . SER B 272 ? 0.98647 0.35297 0.48552 0.11937  -0.09199 -0.06009 302 SER B CB    
4345 O  OG    . SER B 272 ? 1.07619 0.47072 0.59736 0.11132  -0.07672 -0.05514 302 SER B OG    
4346 N  N     . ARG B 273 ? 1.22551 0.61149 0.69732 0.14496  -0.07686 -0.06220 303 ARG B N     
4347 C  CA    . ARG B 273 ? 1.17819 0.56459 0.64380 0.14737  -0.07494 -0.06102 303 ARG B CA    
4348 C  C     . ARG B 273 ? 1.27392 0.63182 0.71602 0.15728  -0.09001 -0.06612 303 ARG B C     
4349 O  O     . ARG B 273 ? 1.42410 0.77106 0.84547 0.17203  -0.09621 -0.07164 303 ARG B O     
4350 C  CB    . ARG B 273 ? 1.16279 0.57356 0.62398 0.15658  -0.06120 -0.06014 303 ARG B CB    
4351 C  CG    . ARG B 273 ? 1.51112 0.93075 0.97358 0.15389  -0.05433 -0.05629 303 ARG B CG    
4352 C  CD    . ARG B 273 ? 1.63781 1.08030 1.09148 0.16448  -0.04266 -0.05573 303 ARG B CD    
4353 N  NE    . ARG B 273 ? 1.68833 1.12598 1.12115 0.18252  -0.04770 -0.06212 303 ARG B NE    
4354 C  CZ    . ARG B 273 ? 1.82207 1.24298 1.23140 0.19686  -0.05655 -0.06699 303 ARG B CZ    
4355 N  NH1   . ARG B 273 ? 1.86221 1.27043 1.26589 0.19540  -0.06087 -0.06617 303 ARG B NH1   
4356 N  NH2   . ARG B 273 ? 1.76748 1.18359 1.15744 0.21396  -0.06171 -0.07318 303 ARG B NH2   
4357 N  N     . GLY B 274 ? 1.29112 0.63631 0.73563 0.14962  -0.09670 -0.06454 304 GLY B N     
4358 C  CA    . GLY B 274 ? 1.47887 0.79617 0.90188 0.15749  -0.11176 -0.06901 304 GLY B CA    
4359 C  C     . GLY B 274 ? 1.33346 0.62629 0.75514 0.15001  -0.12756 -0.07034 304 GLY B C     
4360 O  O     . GLY B 274 ? 1.28656 0.55379 0.68918 0.15573  -0.14169 -0.07399 304 GLY B O     
4361 N  N     . GLU B 275 ? 1.25788 0.55728 0.69802 0.13738  -0.12617 -0.06734 305 GLU B N     
4362 C  CA    . GLU B 275 ? 1.18020 0.46068 0.62406 0.12545  -0.14005 -0.06643 305 GLU B CA    
4363 C  C     . GLU B 275 ? 1.30747 0.59677 0.77192 0.10975  -0.13852 -0.06113 305 GLU B C     
4364 O  O     . GLU B 275 ? 1.39614 0.70673 0.87431 0.10701  -0.12573 -0.05794 305 GLU B O     
4365 C  CB    . GLU B 275 ? 1.20683 0.49029 0.65964 0.11974  -0.13977 -0.06567 305 GLU B CB    
4366 C  CG    . GLU B 275 ? 1.27725 0.56255 0.71535 0.13544  -0.13587 -0.07030 305 GLU B CG    
4367 C  CD    . GLU B 275 ? 1.38417 0.63837 0.79748 0.14362  -0.15262 -0.07564 305 GLU B CD    
4368 O  OE1   . GLU B 275 ? 1.48323 0.73212 0.90543 0.12999  -0.16230 -0.07226 305 GLU B OE1   
4369 O  OE2   . GLU B 275 ? 1.52834 0.77671 0.91909 0.16162  -0.15496 -0.08084 305 GLU B OE2   
4370 N  N     . ASP B 276 ? 1.46834 0.74112 0.93397 0.09936  -0.15225 -0.06009 306 ASP B N     
4371 C  CA    . ASP B 276 ? 1.58215 0.86274 1.06534 0.08549  -0.15298 -0.05561 306 ASP B CA    
4372 C  C     . ASP B 276 ? 1.57873 0.87324 1.08609 0.06933  -0.15089 -0.05066 306 ASP B C     
4373 O  O     . ASP B 276 ? 1.55928 0.84941 1.06681 0.06691  -0.15387 -0.05081 306 ASP B O     
4374 C  CB    . ASP B 276 ? 1.77935 1.03620 1.24872 0.08403  -0.16970 -0.05717 306 ASP B CB    
4375 C  CG    . ASP B 276 ? 1.94542 1.19351 1.39485 0.09868  -0.17065 -0.06113 306 ASP B CG    
4376 O  OD1   . ASP B 276 ? 1.91076 1.16770 1.35433 0.11060  -0.15898 -0.06304 306 ASP B OD1   
4377 O  OD2   . ASP B 276 ? 2.04435 1.28191 1.48582 0.09763  -0.18249 -0.06152 306 ASP B OD2   
4378 N  N     . CYS B 277 ? 1.57736 0.88878 1.10437 0.05892  -0.14595 -0.04637 307 CYS B N     
4379 C  CA    . CYS B 277 ? 1.58644 0.91451 1.13763 0.04394  -0.14345 -0.04137 307 CYS B CA    
4380 C  C     . CYS B 277 ? 1.56868 0.89849 1.12855 0.03366  -0.15093 -0.03860 307 CYS B C     
4381 O  O     . CYS B 277 ? 1.46748 0.79605 1.02191 0.03839  -0.15045 -0.03973 307 CYS B O     
4382 C  CB    . CYS B 277 ? 1.64158 0.99584 1.21045 0.04345  -0.12607 -0.03884 307 CYS B CB    
4383 S  SG    . CYS B 277 ? 1.76174 1.12157 1.32632 0.05273  -0.11571 -0.04097 307 CYS B SG    
4384 N  N     . PRO B 278 ? 1.57915 0.91311 1.15232 0.01969  -0.15790 -0.03486 308 PRO B N     
4385 C  CA    . PRO B 278 ? 1.46346 0.80212 1.04572 0.00908  -0.16594 -0.03190 308 PRO B CA    
4386 C  C     . PRO B 278 ? 1.54301 0.90218 1.13847 0.00965  -0.15589 -0.03045 308 PRO B C     
4387 O  O     . PRO B 278 ? 1.38525 0.75496 0.99237 0.00078  -0.16030 -0.02764 308 PRO B O     
4388 C  CB    . PRO B 278 ? 1.41899 0.76708 1.01726 -0.00568 -0.17013 -0.02724 308 PRO B CB    
4389 C  CG    . PRO B 278 ? 1.51751 0.85277 1.10617 -0.00201 -0.17059 -0.02901 308 PRO B CG    
4390 C  CD    . PRO B 278 ? 1.50418 0.84081 1.08495 0.01310  -0.15804 -0.03295 308 PRO B CD    
4391 C  C1    . NAG C .   ? 0.53612 0.43234 0.55496 -0.12650 0.12608  0.03643  1   NAG E C1    
4392 C  C2    . NAG C .   ? 0.54510 0.46836 0.56666 -0.13533 0.13143  0.03900  1   NAG E C2    
4393 C  C3    . NAG C .   ? 0.53977 0.45731 0.54998 -0.15279 0.12663  0.04745  1   NAG E C3    
4394 C  C4    . NAG C .   ? 0.67524 0.57534 0.67102 -0.15727 0.12288  0.05152  1   NAG E C4    
4395 C  C5    . NAG C .   ? 0.53970 0.41322 0.53390 -0.14603 0.11782  0.04757  1   NAG E C5    
4396 C  C6    . NAG C .   ? 0.54750 0.40488 0.52819 -0.14815 0.11458  0.05045  1   NAG E C6    
4397 C  C7    . NAG C .   ? 0.55234 0.51447 0.59493 -0.12621 0.14109  0.03160  1   NAG E C7    
4398 C  C8    . NAG C .   ? 0.52951 0.49998 0.58372 -0.12241 0.14211  0.02807  1   NAG E C8    
4399 N  N2    . NAG C .   ? 0.53386 0.46909 0.56780 -0.13108 0.13368  0.03526  1   NAG E N2    
4400 O  O3    . NAG C .   ? 0.68283 0.62972 0.69557 -0.16163 0.13218  0.05045  1   NAG E O3    
4401 O  O4    . NAG C .   ? 0.86755 0.75655 0.85116 -0.17351 0.11661  0.05943  1   NAG E O4    
4402 O  O5    . NAG C .   ? 0.51399 0.39727 0.51987 -0.13121 0.12317  0.04027  1   NAG E O5    
4403 O  O6    . NAG C .   ? 0.59492 0.46945 0.57684 -0.14376 0.12158  0.04864  1   NAG E O6    
4404 O  O7    . NAG C .   ? 0.55936 0.53794 0.59976 -0.12391 0.14644  0.03081  1   NAG E O7    
4405 C  C1    . NAG C .   ? 0.87239 0.77303 0.84655 -0.18363 0.11939  0.06510  2   NAG E C1    
4406 C  C2    . NAG C .   ? 0.91320 0.79610 0.87152 -0.20120 0.11123  0.07398  2   NAG E C2    
4407 C  C3    . NAG C .   ? 1.08937 0.98886 1.03850 -0.21362 0.11474  0.08088  2   NAG E C3    
4408 C  C4    . NAG C .   ? 1.16237 1.10369 1.12294 -0.21415 0.12493  0.08025  2   NAG E C4    
4409 C  C5    . NAG C .   ? 1.17450 1.12744 1.14899 -0.19415 0.13173  0.07029  2   NAG E C5    
4410 C  C6    . NAG C .   ? 1.17846 1.17143 1.16351 -0.19133 0.14123  0.06812  2   NAG E C6    
4411 C  C7    . NAG C .   ? 0.81771 0.64325 0.76707 -0.18984 0.09619  0.06987  2   NAG E C7    
4412 C  C8    . NAG C .   ? 0.77450 0.56550 0.70999 -0.18604 0.08708  0.07000  2   NAG E C8    
4413 N  N2    . NAG C .   ? 0.81028 0.65676 0.75738 -0.19757 0.10230  0.07367  2   NAG E N2    
4414 O  O3    . NAG C .   ? 1.18782 1.07280 1.12250 -0.23204 0.10687  0.08985  2   NAG E O3    
4415 O  O4    . NAG C .   ? 1.35544 1.31260 1.30728 -0.22257 0.12859  0.08587  2   NAG E O4    
4416 O  O5    . NAG C .   ? 1.03402 0.97073 1.01675 -0.18581 0.12797  0.06508  2   NAG E O5    
4417 O  O6    . NAG C .   ? 0.93190 0.92995 0.92841 -0.17282 0.14565  0.05862  2   NAG E O6    
4418 O  O7    . NAG C .   ? 1.00699 0.84189 0.96877 -0.18524 0.09793  0.06626  2   NAG E O7    
4419 C  C1    . NAG D .   ? 0.90816 1.15416 1.13996 0.04945  0.06776  0.07274  1   NAG F C1    
4420 C  C2    . NAG D .   ? 0.90597 1.16090 1.14469 0.04955  0.07156  0.07529  1   NAG F C2    
4421 C  C3    . NAG D .   ? 1.01226 1.29237 1.25858 0.03493  0.07108  0.08515  1   NAG F C3    
4422 C  C4    . NAG D .   ? 0.95193 1.27006 1.20246 0.03666  0.06712  0.09077  1   NAG F C4    
4423 C  C5    . NAG D .   ? 0.96357 1.26962 1.20689 0.03811  0.06352  0.08687  1   NAG F C5    
4424 C  C6    . NAG D .   ? 0.85729 1.20087 1.10371 0.04361  0.05941  0.09076  1   NAG F C6    
4425 C  C7    . NAG D .   ? 0.93568 1.14664 1.17002 0.05780  0.07778  0.06512  1   NAG F C7    
4426 C  C8    . NAG D .   ? 0.77994 0.95249 1.00703 0.05676  0.07987  0.05790  1   NAG F C8    
4427 N  N2    . NAG D .   ? 0.84486 1.06572 1.08001 0.04586  0.07524  0.07053  1   NAG F N2    
4428 O  O3    . NAG D .   ? 0.94712 1.23794 1.19938 0.03666  0.07437  0.08768  1   NAG F O3    
4429 O  O4    . NAG D .   ? 0.82903 1.16516 1.08523 0.01901  0.06610  0.10042  1   NAG F O4    
4430 O  O5    . NAG D .   ? 0.97559 1.25747 1.21126 0.05325  0.06413  0.07749  1   NAG F O5    
4431 O  O6    . NAG D .   ? 1.02665 1.39963 1.27748 0.06029  0.06000  0.09079  1   NAG F O6    
4432 O  O7    . NAG D .   ? 0.86303 1.09609 1.10207 0.06904  0.07816  0.06610  1   NAG F O7    
4433 C  C1    . FUC D .   ? 0.98243 1.37485 1.23005 0.07630  0.05620  0.08804  2   FUC F C1    
4434 C  C2    . FUC D .   ? 1.00964 1.43417 1.26185 0.09323  0.05688  0.08873  2   FUC F C2    
4435 C  C3    . FUC D .   ? 1.04596 1.44336 1.29343 0.10534  0.05956  0.08137  2   FUC F C3    
4436 C  C4    . FUC D .   ? 1.08814 1.44769 1.32280 0.11389  0.05721  0.07194  2   FUC F C4    
4437 C  C5    . FUC D .   ? 1.11190 1.44314 1.34352 0.09566  0.05739  0.07214  2   FUC F C5    
4438 C  C6    . FUC D .   ? 0.75002 1.04605 0.96883 0.10222  0.05495  0.06387  2   FUC F C6    
4439 O  O2    . FUC D .   ? 0.85803 1.31221 1.11920 0.08163  0.05825  0.09774  2   FUC F O2    
4440 O  O3    . FUC D .   ? 1.10297 1.51340 1.34279 0.11851  0.05689  0.07830  2   FUC F O3    
4441 O  O4    . FUC D .   ? 1.12966 1.50593 1.35795 0.13104  0.05197  0.06892  2   FUC F O4    
4442 O  O5    . FUC D .   ? 1.10042 1.45799 1.33645 0.08579  0.05472  0.07877  2   FUC F O5    
4443 C  C1    . NAG E .   ? 1.12734 0.74131 0.83875 -0.18170 0.06417  0.09718  1   NAG G C1    
4444 C  C2    . NAG E .   ? 1.11688 0.73864 0.84402 -0.18132 0.06466  0.09492  1   NAG G C2    
4445 C  C3    . NAG E .   ? 1.26853 0.87975 0.98419 -0.19766 0.05961  0.10276  1   NAG G C3    
4446 C  C4    . NAG E .   ? 1.35841 0.98409 1.06430 -0.21346 0.06407  0.11178  1   NAG G C4    
4447 C  C5    . NAG E .   ? 1.20647 0.82151 0.89652 -0.21206 0.06294  0.11332  1   NAG G C5    
4448 C  C6    . NAG E .   ? 1.16103 0.79179 0.84074 -0.22737 0.06749  0.12261  1   NAG G C6    
4449 C  C7    . NAG E .   ? 1.00268 0.62507 0.75727 -0.15861 0.06337  0.08146  1   NAG G C7    
4450 C  C8    . NAG E .   ? 0.98600 0.59312 0.74527 -0.14527 0.05729  0.07473  1   NAG G C8    
4451 N  N2    . NAG E .   ? 1.03609 0.64296 0.76999 -0.16784 0.05933  0.08752  1   NAG G N2    
4452 O  O3    . NAG E .   ? 1.25948 0.88233 0.99108 -0.19749 0.06140  0.10075  1   NAG G O3    
4453 O  O4    . NAG E .   ? 1.53402 1.15227 1.23154 -0.22478 0.05567  0.11707  1   NAG G O4    
4454 O  O5    . NAG E .   ? 1.20699 0.83527 0.91002 -0.19577 0.06873  0.10534  1   NAG G O5    
4455 O  O6    . NAG E .   ? 1.25307 0.92194 0.94993 -0.23017 0.07773  0.12342  1   NAG G O6    
4456 O  O7    . NAG E .   ? 0.91591 0.56430 0.68434 -0.16077 0.07145  0.08151  1   NAG G O7    
4457 C  C1    . NAG E .   ? 1.59169 1.22473 1.29839 -0.23308 0.05520  0.11968  2   NAG G C1    
4458 C  C2    . NAG E .   ? 1.58436 1.25228 1.29730 -0.24547 0.06465  0.12615  2   NAG G C2    
4459 C  C3    . NAG E .   ? 1.62281 1.28942 1.32297 -0.25984 0.05751  0.13381  2   NAG G C3    
4460 C  C4    . NAG E .   ? 1.64098 1.27432 1.32030 -0.25785 0.04721  0.13389  2   NAG G C4    
4461 C  C5    . NAG E .   ? 1.66383 1.26722 1.34092 -0.24745 0.03677  0.12740  2   NAG G C5    
4462 C  C6    . NAG E .   ? 1.53761 1.11088 1.19854 -0.23829 0.02963  0.12404  2   NAG G C6    
4463 C  C7    . NAG E .   ? 1.51687 1.20938 1.26140 -0.23353 0.07697  0.11728  2   NAG G C7    
4464 C  C8    . NAG E .   ? 1.36495 1.05083 1.12139 -0.22817 0.07287  0.11252  2   NAG G C8    
4465 N  N2    . NAG E .   ? 1.52130 1.21134 1.25332 -0.24499 0.07084  0.12405  2   NAG G N2    
4466 O  O3    . NAG E .   ? 1.63208 1.33039 1.33406 -0.26978 0.06636  0.14015  2   NAG G O3    
4467 O  O4    . NAG E .   ? 1.67758 1.31005 1.34329 -0.27209 0.04132  0.14134  2   NAG G O4    
4468 O  O5    . NAG E .   ? 1.67353 1.28496 1.36920 -0.23674 0.04240  0.12097  2   NAG G O5    
4469 O  O6    . NAG E .   ? 1.61693 1.17015 1.28061 -0.22454 0.02326  0.11647  2   NAG G O6    
4470 O  O7    . NAG E .   ? 1.55839 1.26349 1.30897 -0.22306 0.08374  0.11287  2   NAG G O7    
4471 C  C1    . NAG F .   ? 0.98175 0.29874 0.42894 0.06501  -0.06282 -0.00870 1   NAG H C1    
4472 C  C2    . NAG F .   ? 0.98487 0.30130 0.43106 0.07232  -0.06779 -0.01349 1   NAG H C2    
4473 C  C3    . NAG F .   ? 1.00774 0.30472 0.43156 0.07897  -0.07324 -0.01504 1   NAG H C3    
4474 C  C4    . NAG F .   ? 1.01200 0.30249 0.43241 0.08171  -0.07948 -0.01675 1   NAG H C4    
4475 C  C5    . NAG F .   ? 1.05581 0.34390 0.47423 0.07418  -0.07437 -0.01148 1   NAG H C5    
4476 C  C6    . NAG F .   ? 1.14243 0.42375 0.55679 0.07756  -0.08079 -0.01327 1   NAG H C6    
4477 C  C7    . NAG F .   ? 0.97030 0.30397 0.43177 0.07201  -0.06299 -0.01492 1   NAG H C7    
4478 C  C8    . NAG F .   ? 1.03559 0.38098 0.51690 0.07180  -0.06883 -0.01849 1   NAG H C8    
4479 N  N2    . NAG F .   ? 0.98253 0.30474 0.43011 0.07083  -0.06207 -0.01210 1   NAG H N2    
4480 O  O3    . NAG F .   ? 1.01075 0.30707 0.43396 0.08595  -0.07868 -0.01980 1   NAG H O3    
4481 O  O4    . NAG F .   ? 1.03443 0.30594 0.43296 0.08866  -0.08500 -0.01861 1   NAG H O4    
4482 O  O5    . NAG F .   ? 1.11938 0.42695 0.55992 0.06761  -0.06865 -0.00984 1   NAG H O5    
4483 O  O6    . NAG F .   ? 1.28388 0.58291 0.71882 0.08130  -0.08530 -0.01800 1   NAG H O6    
4484 O  O7    . NAG F .   ? 1.09623 0.43094 0.55348 0.07323  -0.05946 -0.01442 1   NAG H O7    
4497 C  C1    . NAG F .   ? 1.03873 0.30681 0.43512 0.09641  -0.09410 -0.02360 2   NAG H C1    
4498 C  C2    . NAG F .   ? 1.06852 0.31439 0.43898 0.10342  -0.09885 -0.02499 2   NAG H C2    
4499 C  C3    . NAG F .   ? 1.07002 0.31338 0.43762 0.11292  -0.10900 -0.03086 2   NAG H C3    
4500 C  C4    . NAG F .   ? 1.05860 0.32444 0.44961 0.11568  -0.11323 -0.03573 2   NAG H C4    
4501 C  C5    . NAG F .   ? 1.02513 0.31172 0.44054 0.10729  -0.10759 -0.03322 2   NAG H C5    
4502 C  C6    . NAG F .   ? 1.07249 0.38108 0.51066 0.10796  -0.11168 -0.03695 2   NAG H C6    
4503 C  C7    . NAG F .   ? 1.08949 0.31306 0.43105 0.09255  -0.08721 -0.01396 2   NAG H C7    
4504 C  C8    . NAG F .   ? 1.10562 0.31405 0.42956 0.08510  -0.08360 -0.00722 2   NAG H C8    
4505 N  N2    . NAG F .   ? 1.08426 0.31092 0.43294 0.09920  -0.09511 -0.01949 2   NAG H N2    
4506 O  O3    . NAG F .   ? 1.09405 0.31702 0.43791 0.12017  -0.11378 -0.03274 2   NAG H O3    
4507 O  O4    . NAG F .   ? 1.05278 0.32126 0.44319 0.12412  -0.12213 -0.04075 2   NAG H O4    
4508 O  O5    . NAG F .   ? 1.02298 0.30802 0.43816 0.09980  -0.09873 -0.02847 2   NAG H O5    
4509 O  O6    . NAG F .   ? 1.03819 0.34627 0.47694 0.10780  -0.11162 -0.03788 2   NAG H O6    
4510 O  O7    . NAG F .   ? 1.08273 0.31546 0.43092 0.09254  -0.08357 -0.01422 2   NAG H O7    
4524 C  C1    . BMA F .   ? 1.05652 0.32805 0.44659 0.13188  -0.12975 -0.04614 3   BMA H C1    
4525 C  C2    . BMA F .   ? 1.04429 0.33606 0.44994 0.13656  -0.13672 -0.05050 3   BMA H C2    
4526 C  C3    . BMA F .   ? 1.05166 0.34574 0.45394 0.14529  -0.14573 -0.05621 3   BMA H C3    
4527 C  C4    . BMA F .   ? 1.07906 0.34643 0.45236 0.15355  -0.14905 -0.05789 3   BMA H C4    
4528 C  C5    . BMA F .   ? 1.08989 0.33717 0.44885 0.14785  -0.14139 -0.05298 3   BMA H C5    
4529 C  C6    . BMA F .   ? 1.11828 0.33780 0.44712 0.15454  -0.14404 -0.05344 3   BMA H C6    
4530 O  O2    . BMA F .   ? 1.05074 0.33743 0.44829 0.14045  -0.13856 -0.05063 3   BMA H O2    
4531 O  O3    . BMA F .   ? 1.17342 0.48762 0.58789 0.15045  -0.15243 -0.06001 3   BMA H O3    
4532 O  O4    . BMA F .   ? 1.08562 0.35512 0.45618 0.16128  -0.15700 -0.06317 3   BMA H O4    
4533 O  O5    . BMA F .   ? 1.11712 0.36461 0.48031 0.13902  -0.13335 -0.04738 3   BMA H O5    
4534 O  O6    . BMA F .   ? 1.12854 0.33927 0.44602 0.15886  -0.14751 -0.05401 3   BMA H O6    
4544 C  C1    . MAN F .   ? 1.15393 0.49378 0.59223 0.14648  -0.15483 -0.06113 4   MAN H C1    
4545 C  C2    . MAN F .   ? 1.23970 0.59785 0.68360 0.15483  -0.16335 -0.06575 4   MAN H C2    
4546 C  C3    . MAN F .   ? 1.14863 0.51355 0.59543 0.15649  -0.16161 -0.06477 4   MAN H C3    
4547 C  C4    . MAN F .   ? 1.16649 0.54362 0.63302 0.14466  -0.15350 -0.05967 4   MAN H C4    
4548 C  C5    . MAN F .   ? 1.05013 0.40926 0.51149 0.13591  -0.14535 -0.05527 4   MAN H C5    
4549 C  C6    . MAN F .   ? 1.17990 0.55349 0.66231 0.12455  -0.13811 -0.05091 4   MAN H C6    
4550 O  O2    . MAN F .   ? 1.31333 0.69769 0.77930 0.15077  -0.16746 -0.06685 4   MAN H O2    
4551 O  O3    . MAN F .   ? 1.26984 0.65753 0.72461 0.16465  -0.16954 -0.06915 4   MAN H O3    
4552 O  O4    . MAN F .   ? 1.15997 0.53618 0.62380 0.14672  -0.15148 -0.05853 4   MAN H O4    
4553 O  O5    . MAN F .   ? 1.06312 0.41721 0.52127 0.13605  -0.14807 -0.05690 4   MAN H O5    
4554 O  O6    . MAN F .   ? 1.27779 0.63443 0.75247 0.11810  -0.13015 -0.04688 4   MAN H O6    
4566 C  C1    . MAN F .   ? 1.18994 0.37714 0.47952 0.16502  -0.15128 -0.05424 5   MAN H C1    
4567 C  C2    . MAN F .   ? 1.26773 0.45111 0.54926 0.16887  -0.15541 -0.05461 5   MAN H C2    
4568 C  C3    . MAN F .   ? 1.37799 0.57452 0.66758 0.18066  -0.16464 -0.06245 5   MAN H C3    
4569 C  C4    . MAN F .   ? 1.28419 0.48129 0.56757 0.19025  -0.17164 -0.06791 5   MAN H C4    
4570 C  C5    . MAN F .   ? 1.29933 0.49961 0.59214 0.18425  -0.16721 -0.06688 5   MAN H C5    
4571 C  C6    . MAN F .   ? 1.16831 0.36729 0.45359 0.19273  -0.17386 -0.07155 5   MAN H C6    
4572 O  O2    . MAN F .   ? 1.21382 0.37732 0.46883 0.17057  -0.15734 -0.05198 5   MAN H O2    
4573 O  O3    . MAN F .   ? 1.33407 0.52484 0.61163 0.18642  -0.16937 -0.06306 5   MAN H O3    
4574 O  O4    . MAN F .   ? 1.30228 0.51908 0.59759 0.19967  -0.17949 -0.07470 5   MAN H O4    
4575 O  O5    . MAN F .   ? 1.18084 0.36799 0.46412 0.17464  -0.15852 -0.05954 5   MAN H O5    
4576 O  O6    . MAN F .   ? 1.26136 0.44248 0.52301 0.19441  -0.17355 -0.06837 5   MAN H O6    
4588 C  C1    . FUC F .   ? 1.63047 0.92516 1.06039 0.08860  -0.09337 -0.02166 6   FUC H C1    
4589 C  C2    . FUC F .   ? 1.51183 0.83010 0.96558 0.09137  -0.09720 -0.02590 6   FUC H C2    
4590 C  C3    . FUC F .   ? 1.59007 0.92593 1.06472 0.08393  -0.09172 -0.02324 6   FUC H C3    
4591 C  C4    . FUC F .   ? 1.64537 0.97104 1.11091 0.08153  -0.08995 -0.02003 6   FUC H C4    
4592 C  C5    . FUC F .   ? 1.61131 0.91350 1.05325 0.07771  -0.08626 -0.01558 6   FUC H C5    
4593 C  C6    . FUC F .   ? 1.60137 0.88921 1.03033 0.07449  -0.08601 -0.01196 6   FUC H C6    
4594 O  O2    . FUC F .   ? 1.47313 0.79884 0.93414 0.09245  -0.09833 -0.02825 6   FUC H O2    
4595 O  O3    . FUC F .   ? 1.43828 0.79563 0.93290 0.08691  -0.09644 -0.02695 6   FUC H O3    
4596 O  O4    . FUC F .   ? 1.88561 1.20809 1.34461 0.09046  -0.09825 -0.02386 6   FUC H O4    
4597 O  O5    . FUC F .   ? 1.64042 0.92617 1.06265 0.08551  -0.09230 -0.01846 6   FUC H O5    
4609 C  C2    . BGC G .   ? 1.48320 1.51467 1.59668 0.04646  0.15669  -0.06080 1   BGC D C2    
4610 C  C3    . BGC G .   ? 1.38129 1.39718 1.50479 0.03853  0.15651  -0.05611 1   BGC D C3    
4611 C  C4    . BGC G .   ? 1.36569 1.36377 1.48754 0.03626  0.15809  -0.05418 1   BGC D C4    
4612 C  C5    . BGC G .   ? 1.37269 1.35973 1.48236 0.04465  0.15389  -0.05727 1   BGC D C5    
4613 C  C6    . BGC G .   ? 1.30446 1.27517 1.41159 0.04244  0.15593  -0.05573 1   BGC D C6    
4614 C  C1    . BGC G .   ? 1.57759 1.59560 1.67851 0.05542  0.15249  -0.06407 1   BGC D C1    
4615 O  O1    . BGC G .   ? 1.40740 1.44036 1.49851 0.06352  0.15309  -0.06875 1   BGC D O1    
4616 O  O2    . BGC G .   ? 1.50344 1.55035 1.61763 0.05024  0.15397  -0.06274 1   BGC D O2    
4617 O  O3    . BGC G .   ? 1.18339 1.21058 1.31707 0.02971  0.16128  -0.05340 1   BGC D O3    
4618 O  O4    . BGC G .   ? 1.42160 1.40583 1.55137 0.03168  0.15615  -0.05030 1   BGC D O4    
4619 O  O5    . BGC G .   ? 1.46930 1.47044 1.56959 0.05163  0.15479  -0.06191 1   BGC D O5    
4620 O  O6    . BGC G .   ? 1.35625 1.33534 1.46310 0.03854  0.16263  -0.05541 1   BGC D O6    
4621 C  C1    . GAL G .   ? 1.29845 1.27819 1.42851 0.03502  0.14956  -0.05012 2   GAL D C1    
4622 C  C2    . GAL G .   ? 1.28082 1.26173 1.42155 0.02976  0.14950  -0.04718 2   GAL D C2    
4623 C  C3    . GAL G .   ? 1.16792 1.14429 1.30782 0.03337  0.14231  -0.04661 2   GAL D C3    
4624 C  C4    . GAL G .   ? 1.06772 1.02965 1.20339 0.03507  0.13853  -0.04476 2   GAL D C4    
4625 C  C5    . GAL G .   ? 1.13875 1.09855 1.26428 0.03964  0.13896  -0.04791 2   GAL D C5    
4626 C  C6    . GAL G .   ? 1.13665 1.08149 1.25802 0.04047  0.13593  -0.04619 2   GAL D C6    
4627 O  O2    . GAL G .   ? 1.19319 1.19059 1.33838 0.02653  0.15371  -0.04819 2   GAL D O2    
4628 O  O3    . GAL G .   ? 1.00600 0.98255 1.15478 0.02948  0.14198  -0.04426 2   GAL D O3    
4629 O  O4    . GAL G .   ? 1.05403 1.00695 1.19564 0.03012  0.14096  -0.04127 2   GAL D O4    
4630 O  O5    . GAL G .   ? 1.19582 1.15923 1.32179 0.03709  0.14546  -0.04883 2   GAL D O5    
4631 O  O6    . GAL G .   ? 1.33157 1.26847 1.45391 0.03715  0.13996  -0.04488 2   GAL D O6    
4632 C  C1    . GLA G .   ? 0.88980 0.83469 1.03488 0.02911  0.13700  -0.03755 3   GLA D C1    
4633 C  C2    . GLA G .   ? 0.92494 0.86098 1.07371 0.02551  0.13992  -0.03490 3   GLA D C2    
4634 C  C3    . GLA G .   ? 0.88864 0.82696 1.04441 0.02139  0.14502  -0.03458 3   GLA D C3    
4635 C  C4    . GLA G .   ? 0.79181 0.73381 0.95314 0.02117  0.14237  -0.03367 3   GLA D C4    
4636 C  C5    . GLA G .   ? 0.90593 0.85775 1.06382 0.02419  0.13984  -0.03633 3   GLA D C5    
4637 C  C6    . GLA G .   ? 0.75524 0.71019 0.91776 0.02438  0.13685  -0.03574 3   GLA D C6    
4638 O  O2    . GLA G .   ? 0.90300 0.83369 1.04551 0.02640  0.14210  -0.03636 3   GLA D O2    
4639 O  O3    . GLA G .   ? 0.83324 0.76183 0.99013 0.01838  0.14534  -0.03156 3   GLA D O3    
4640 O  O4    . GLA G .   ? 0.49976 0.43562 0.66211 0.02256  0.13668  -0.03031 3   GLA D O4    
4641 O  O5    . GLA G .   ? 0.94517 0.89438 1.09593 0.02824  0.13488  -0.03636 3   GLA D O5    
4642 O  O6    . GLA G .   ? 0.95988 0.91841 1.11718 0.02863  0.13101  -0.03646 3   GLA D O6    
4643 C  C1    . NGA G .   ? 0.73523 0.66749 0.88749 0.01009  0.14583  -0.02950 4   NGA D C1    
4644 C  C2    . NGA G .   ? 0.78556 0.70653 0.93326 0.00766  0.14220  -0.02581 4   NGA D C2    
4645 C  C3    . NGA G .   ? 0.72414 0.64238 0.86710 -0.00039 0.14036  -0.02209 4   NGA D C3    
4646 C  C4    . NGA G .   ? 0.68967 0.60813 0.83622 -0.00343 0.13843  -0.02050 4   NGA D C4    
4647 C  C5    . NGA G .   ? 0.63818 0.56868 0.79004 -0.00152 0.14215  -0.02401 4   NGA D C5    
4648 C  C6    . NGA G .   ? 0.48084 0.41018 0.63624 -0.00405 0.13942  -0.02264 4   NGA D C6    
4649 C  C7    . NGA G .   ? 0.88397 0.79530 1.02612 0.01342  0.14072  -0.02683 4   NGA D C7    
4650 C  C8    . NGA G .   ? 0.65122 0.55838 0.78535 0.01543  0.14076  -0.02874 4   NGA D C8    
4651 N  N2    . NGA G .   ? 0.93756 0.85618 1.07939 0.00998  0.14304  -0.02739 4   NGA D N2    
4652 O  O3    . NGA G .   ? 0.70028 0.60802 0.83975 -0.00134 0.13658  -0.01900 4   NGA D O3    
4653 O  O4    . NGA G .   ? 0.70596 0.61641 0.85639 0.00080  0.13441  -0.01919 4   NGA D O4    
4654 O  O5    . NGA G .   ? 0.79457 0.72700 0.95140 0.00717  0.14394  -0.02763 4   NGA D O5    
4655 O  O6    . NGA G .   ? 0.41574 0.35777 0.57589 -0.00323 0.14292  -0.02577 4   NGA D O6    
4656 O  O7    . NGA G .   ? 0.74831 0.65676 0.89625 0.01484  0.13826  -0.02473 4   NGA D O7    
4657 C  C1    . GAL H .   ? 1.45958 1.15359 1.36540 -0.03393 0.03520  0.01484  1   GAL I C1    
4658 C  C2    . GAL H .   ? 1.58991 1.28280 1.49275 -0.03044 0.03023  0.01536  1   GAL I C2    
4659 C  C3    . GAL H .   ? 1.59274 1.29087 1.49843 -0.02887 0.02370  0.01493  1   GAL I C3    
4660 C  C4    . GAL H .   ? 1.53222 1.21902 1.42629 -0.02973 0.02208  0.01402  1   GAL I C4    
4661 C  C5    . GAL H .   ? 1.48327 1.16729 1.37696 -0.03292 0.02657  0.01339  1   GAL I C5    
4662 C  C6    . GAL H .   ? 1.51030 1.18135 1.38930 -0.03262 0.02704  0.01247  1   GAL I C6    
4663 O  O2    . GAL H .   ? 1.69326 1.39360 1.60394 -0.02863 0.03078  0.01604  1   GAL I O2    
4664 O  O3    . GAL H .   ? 1.66978 1.37013 1.57374 -0.02422 0.01902  0.01501  1   GAL I O3    
4665 O  O4    . GAL H .   ? 1.63073 1.30494 1.51091 -0.02806 0.02258  0.01409  1   GAL I O4    
4666 O  O5    . GAL H .   ? 1.58336 1.26965 1.48039 -0.03438 0.03352  0.01379  1   GAL I O5    
4667 O  O6    . GAL H .   ? 1.54749 1.21708 1.42416 -0.03396 0.03319  0.01201  1   GAL I O6    
4668 C  C1    . GLA H .   ? 1.50699 1.17610 1.37921 -0.02506 0.01639  0.01338  2   GLA I C1    
4669 C  C2    . GLA H .   ? 1.49855 1.15140 1.35365 -0.02474 0.01747  0.01343  2   GLA I C2    
4670 C  C3    . GLA H .   ? 1.39545 1.04211 1.24440 -0.02392 0.01885  0.01467  2   GLA I C3    
4671 C  C4    . GLA H .   ? 1.35659 1.00776 1.20822 -0.01863 0.01312  0.01410  2   GLA I C4    
4672 C  C5    . GLA H .   ? 1.37014 1.04001 1.24001 -0.01814 0.01284  0.01392  2   GLA I C5    
4673 C  C6    . GLA H .   ? 1.31992 0.99762 1.19240 -0.01167 0.00705  0.01326  2   GLA I C6    
4674 O  O2    . GLA H .   ? 1.30191 0.95077 1.15344 -0.02802 0.02246  0.01338  2   GLA I O2    
4675 O  O3    . GLA H .   ? 1.43810 1.06924 1.26994 -0.02464 0.01921  0.01534  2   GLA I O3    
4676 O  O4    . GLA H .   ? 1.35131 0.99852 1.19539 -0.01473 0.00695  0.01279  2   GLA I O4    
4677 O  O5    . GLA H .   ? 1.29957 0.97688 1.17664 -0.02069 0.01175  0.01344  2   GLA I O5    
4678 O  O6    . GLA H .   ? 1.33915 1.03484 1.22830 -0.01190 0.00802  0.01378  2   GLA I O6    
4679 C  C1    . NGA H .   ? 1.23331 0.85802 1.05894 -0.02818 0.02363  0.01751  3   NGA I C1    
4680 C  C2    . NGA H .   ? 1.21372 0.82859 1.02583 -0.03176 0.02714  0.01890  3   NGA I C2    
4681 C  C3    . NGA H .   ? 1.12803 0.73865 0.93454 -0.03712 0.03164  0.02205  3   NGA I C3    
4682 C  C4    . NGA H .   ? 1.06017 0.66096 0.85998 -0.03568 0.02671  0.02303  3   NGA I C4    
4683 C  C5    . NGA H .   ? 1.13047 0.74145 0.94422 -0.03040 0.02331  0.02077  3   NGA I C5    
4684 C  C6    . NGA H .   ? 1.04033 0.64181 0.84632 -0.02639 0.01726  0.02086  3   NGA I C6    
4685 C  C7    . NGA H .   ? 1.10267 0.72163 0.91582 -0.03009 0.02748  0.01589  3   NGA I C7    
4686 C  C8    . NGA H .   ? 1.06375 0.68866 0.88125 -0.03055 0.03049  0.01448  3   NGA I C8    
4687 N  N2    . NGA H .   ? 1.20106 0.82281 1.01803 -0.03274 0.03066  0.01774  3   NGA I N2    
4688 O  O3    . NGA H .   ? 1.06806 0.67156 0.86139 -0.04075 0.03474  0.02398  3   NGA I O3    
4689 O  O4    . NGA H .   ? 1.08576 0.67207 0.86992 -0.03260 0.02103  0.02275  3   NGA I O4    
4690 O  O5    . NGA H .   ? 1.21858 0.83540 1.03716 -0.02568 0.01961  0.01816  3   NGA I O5    
4691 O  O6    . NGA H .   ? 0.95331 0.56746 0.77354 -0.02219 0.01587  0.01938  3   NGA I O6    
4692 O  O7    . NGA H .   ? 0.97201 0.58335 0.77766 -0.02697 0.02186  0.01516  3   NGA I O7    
4693 MN MN    . MN  I .   ? 0.50409 0.39043 0.58974 0.00875  0.13645  -0.02919 401 MN  A MN    
4694 N  N1    . UDP J .   ? 0.38800 0.28802 0.45108 -0.02580 0.14023  -0.01207 402 UDP A N1    
4695 C  C2    . UDP J .   ? 0.49125 0.38505 0.54800 -0.03212 0.13826  -0.00802 402 UDP A C2    
4696 N  N3    . UDP J .   ? 0.45718 0.36229 0.50945 -0.03752 0.14148  -0.00616 402 UDP A N3    
4697 C  C4    . UDP J .   ? 0.48039 0.40413 0.53460 -0.03727 0.14645  -0.00783 402 UDP A C4    
4698 C  C5    . UDP J .   ? 0.34482 0.27433 0.40580 -0.02961 0.14821  -0.01260 402 UDP A C5    
4699 C  C6    . UDP J .   ? 0.43056 0.34718 0.49533 -0.02432 0.14502  -0.01448 402 UDP A C6    
4700 O  O2    . UDP J .   ? 0.52252 0.40270 0.57751 -0.03300 0.13391  -0.00607 402 UDP A O2    
4701 O  O4    . UDP J .   ? 0.49847 0.43303 0.54813 -0.04336 0.14889  -0.00515 402 UDP A O4    
4702 C  "C1'" . UDP J .   ? 0.36985 0.25910 0.43751 -0.02088 0.13684  -0.01347 402 UDP A "C1'" 
4703 C  "C2'" . UDP J .   ? 0.42726 0.31611 0.49096 -0.01281 0.13721  -0.01824 402 UDP A "C2'" 
4704 O  "O2'" . UDP J .   ? 0.47126 0.35149 0.52487 -0.01185 0.13465  -0.01829 402 UDP A "O2'" 
4705 C  "C3'" . UDP J .   ? 0.52150 0.40334 0.59336 -0.01028 0.13449  -0.01844 402 UDP A "C3'" 
4706 C  "C4'" . UDP J .   ? 0.54939 0.43791 0.63092 -0.01381 0.13612  -0.01652 402 UDP A "C4'" 
4707 O  "O4'" . UDP J .   ? 0.42019 0.31289 0.49788 -0.02044 0.13740  -0.01366 402 UDP A "O4'" 
4708 O  "O3'" . UDP J .   ? 0.34460 0.21387 0.41501 -0.01226 0.12956  -0.01561 402 UDP A "O3'" 
4709 C  "C5'" . UDP J .   ? 0.39956 0.29888 0.48732 -0.00979 0.13973  -0.01993 402 UDP A "C5'" 
4710 O  "O5'" . UDP J .   ? 0.48415 0.39544 0.56635 -0.00772 0.14388  -0.02297 402 UDP A "O5'" 
4711 P  PA    . UDP J .   ? 0.50890 0.42523 0.58887 0.00173  0.14584  -0.02899 402 UDP A PA    
4712 O  O1A   . UDP J .   ? 0.52995 0.45936 0.60200 0.00413  0.14945  -0.03162 402 UDP A O1A   
4713 O  O2A   . UDP J .   ? 0.53933 0.44031 0.61569 0.00606  0.14148  -0.03008 402 UDP A O2A   
4714 O  O3A   . UDP J .   ? 0.51214 0.43738 0.60336 0.00247  0.14820  -0.03001 402 UDP A O3A   
4715 P  PB    . UDP J .   ? 0.70815 0.62886 0.80893 0.00577  0.14691  -0.03083 402 UDP A PB    
4716 O  O1B   . UDP J .   ? 0.98548 0.91849 1.08850 0.01178  0.15066  -0.03568 402 UDP A O1B   
4717 O  O2B   . UDP J .   ? 0.67073 0.58993 0.77924 -0.00086 0.14554  -0.02631 402 UDP A O2B   
4718 O  O3B   . UDP J .   ? 0.55370 0.45959 0.65048 0.00906  0.14275  -0.03098 402 UDP A O3B   
4719 C  C1    . B3P K .   ? 0.45334 0.20625 0.52817 0.00303  0.04118  -0.00700 403 B3P A C1    
4720 C  C2    . B3P K .   ? 0.40284 0.18175 0.49571 0.00653  0.05435  -0.00887 403 B3P A C2    
4721 C  C3    . B3P K .   ? 0.47168 0.20662 0.52958 -0.00465 0.03481  -0.00295 403 B3P A C3    
4722 N  N1    . B3P K .   ? 0.40554 0.13158 0.45699 0.00987  0.03022  -0.00442 403 B3P A N1    
4723 C  C4    . B3P K .   ? 0.53317 0.23956 0.56659 0.00585  0.02274  -0.00133 403 B3P A C4    
4724 C  C5    . B3P K .   ? 0.45731 0.13407 0.46934 0.00088  0.00871  0.00065  403 B3P A C5    
4725 C  C6    . B3P K .   ? 0.44378 0.15177 0.47713 0.02285  0.02163  -0.00378 403 B3P A C6    
4726 C  C7    . B3P K .   ? 0.51659 0.23035 0.55135 -0.00963 0.02925  0.00238  403 B3P A C7    
4727 N  N2    . B3P K .   ? 0.40438 0.18405 0.49889 0.02181  0.05386  -0.01078 403 B3P A N2    
4728 C  C8    . B3P K .   ? 0.43631 0.23549 0.54352 0.02406  0.06406  -0.01145 403 B3P A C8    
4729 C  C9    . B3P K .   ? 0.34762 0.14913 0.45713 0.04018  0.06233  -0.01322 403 B3P A C9    
4730 C  C10   . B3P K .   ? 0.36642 0.18588 0.48928 0.02109  0.07411  -0.01357 403 B3P A C10   
4731 C  C11   . B3P K .   ? 0.42400 0.22050 0.52497 0.01423  0.06542  -0.00825 403 B3P A C11   
4732 O  O1    . B3P K .   ? 0.48379 0.30521 0.60448 0.04189  0.07065  -0.01355 403 B3P A O1    
4733 O  O2    . B3P K .   ? 0.41217 0.23407 0.54078 0.03035  0.07300  -0.01657 403 B3P A O2    
4734 O  O3    . B3P K .   ? 0.44796 0.22356 0.53240 0.01563  0.05537  -0.00631 403 B3P A O3    
4735 O  O4    . B3P K .   ? 0.51084 0.17788 0.51870 0.01532  0.00122  -0.00282 403 B3P A O4    
4736 O  O5    . B3P K .   ? 0.57770 0.26649 0.59313 0.02295  0.01354  -0.00185 403 B3P A O5    
4737 O  O6    . B3P K .   ? 0.42319 0.16199 0.47568 -0.00687 0.04147  0.00078  403 B3P A O6    
4764 C  C1    . PEG L .   ? 0.98993 0.68773 0.89010 -0.07482 0.07360  0.03336  404 PEG A C1    
4765 O  O1    . PEG L .   ? 1.06773 0.75848 0.95692 -0.07484 0.07229  0.03395  404 PEG A O1    
4766 C  C2    . PEG L .   ? 0.85658 0.55003 0.76293 -0.06716 0.06819  0.03087  404 PEG A C2    
4767 O  O2    . PEG L .   ? 0.98204 0.68377 0.89787 -0.06042 0.06891  0.02746  404 PEG A O2    
4768 C  C3    . PEG L .   ? 0.90627 0.62286 0.83204 -0.06099 0.07562  0.02591  404 PEG A C3    
4769 C  C4    . PEG L .   ? 0.89588 0.61761 0.82885 -0.05493 0.07488  0.02283  404 PEG A C4    
4770 O  O4    . PEG L .   ? 0.80077 0.52994 0.73442 -0.05546 0.07965  0.02153  404 PEG A O4    
4771 C  C1    . PEG M .   ? 0.84148 0.62727 0.88381 -0.08612 0.03245  0.04074  405 PEG A C1    
4772 O  O1    . PEG M .   ? 1.00821 0.77977 1.04166 -0.07733 0.03538  0.03307  405 PEG A O1    
4773 C  C2    . PEG M .   ? 0.83550 0.63923 0.89232 -0.08090 0.03995  0.04072  405 PEG A C2    
4774 O  O2    . PEG M .   ? 0.82206 0.64944 0.89237 -0.08761 0.03901  0.04840  405 PEG A O2    
4775 C  C3    . PEG M .   ? 0.64097 0.47499 0.71582 -0.08964 0.03957  0.05161  405 PEG A C3    
4776 C  C4    . PEG M .   ? 0.68086 0.54621 0.77404 -0.09005 0.04303  0.05694  405 PEG A C4    
4777 O  O4    . PEG M .   ? 0.72228 0.59740 0.82485 -0.08141 0.05027  0.05429  405 PEG A O4    
4778 C  C1    . GAL N .   ? 0.65798 0.56384 0.78507 -0.00643 0.13779  -0.01822 406 GAL A C1    
4779 C  C2    . GAL N .   ? 0.50340 0.40157 0.62479 -0.00552 0.13589  -0.01753 406 GAL A C2    
4780 C  C3    . GAL N .   ? 0.49988 0.39408 0.61327 -0.01156 0.13471  -0.01479 406 GAL A C3    
4781 C  C4    . GAL N .   ? 0.56136 0.45444 0.67525 -0.01712 0.13309  -0.01171 406 GAL A C4    
4782 C  C5    . GAL N .   ? 0.54042 0.44481 0.65624 -0.01951 0.13684  -0.01313 406 GAL A C5    
4783 C  C6    . GAL N .   ? 0.49590 0.39739 0.61185 -0.02552 0.13415  -0.00993 406 GAL A C6    
4784 O  O2    . GAL N .   ? 0.56969 0.47062 0.68858 -0.00069 0.13822  -0.02137 406 GAL A O2    
4785 O  O3    . GAL N .   ? 0.52914 0.41370 0.63950 -0.01129 0.13092  -0.01278 406 GAL A O3    
4786 O  O4    . GAL N .   ? 0.43166 0.31975 0.55150 -0.01428 0.12965  -0.01059 406 GAL A O4    
4787 O  O5    . GAL N .   ? 0.62557 0.53658 0.74887 -0.01313 0.13920  -0.01684 406 GAL A O5    
4788 O  O6    . GAL N .   ? 0.36805 0.26567 0.47527 -0.03347 0.13272  -0.00635 406 GAL A O6    
4789 MN MN    . MN  O .   ? 0.94004 0.59443 0.74074 -0.03337 0.06180  0.01551  401 MN  B MN    
4790 N  N1    . UDP P .   ? 0.97304 0.66590 0.75153 -0.07502 0.08954  0.04262  402 UDP B N1    
4791 C  C2    . UDP P .   ? 1.04219 0.74641 0.81285 -0.08312 0.09462  0.04828  402 UDP B C2    
4792 N  N3    . UDP P .   ? 1.06153 0.77603 0.83946 -0.09102 0.09775  0.05147  402 UDP B N3    
4793 C  C4    . UDP P .   ? 1.07028 0.78409 0.86187 -0.09087 0.09647  0.04934  402 UDP B C4    
4794 C  C5    . UDP P .   ? 1.03879 0.74121 0.83775 -0.08179 0.09152  0.04351  402 UDP B C5    
4795 C  C6    . UDP P .   ? 1.00548 0.69845 0.79786 -0.07481 0.08824  0.04061  402 UDP B C6    
4796 O  O2    . UDP P .   ? 1.01799 0.72396 0.77611 -0.08368 0.09615  0.05060  402 UDP B O2    
4797 O  O4    . UDP P .   ? 1.22424 0.94768 1.02053 -0.09854 0.09938  0.05269  402 UDP B O4    
4798 C  "C1'" . UDP P .   ? 0.99924 0.68089 0.77066 -0.06688 0.08541  0.03905  402 UDP B "C1'" 
4799 C  "C2'" . UDP P .   ? 1.02669 0.71534 0.80657 -0.05675 0.08572  0.03272  402 UDP B "C2'" 
4800 O  "O2'" . UDP P .   ? 0.93711 0.63978 0.71051 -0.05331 0.09082  0.03240  402 UDP B "O2'" 
4801 C  "C3'" . UDP P .   ? 0.96463 0.63500 0.74064 -0.05133 0.07824  0.02970  402 UDP B "C3'" 
4802 C  "C4'" . UDP P .   ? 0.93914 0.59660 0.71560 -0.05732 0.07401  0.03257  402 UDP B "C4'" 
4803 O  "O4'" . UDP P .   ? 1.01000 0.67227 0.78049 -0.06650 0.07819  0.03835  402 UDP B "O4'" 
4804 O  "O3'" . UDP P .   ? 0.99264 0.65841 0.75388 -0.04881 0.07780  0.03025  402 UDP B "O3'" 
4805 C  "C5'" . UDP P .   ? 0.89560 0.55278 0.68693 -0.05674 0.07150  0.03052  402 UDP B "C5'" 
4806 O  "O5'" . UDP P .   ? 1.16029 0.82251 0.96121 -0.04955 0.07056  0.02548  402 UDP B "O5'" 
4807 P  PA    . UDP P .   ? 0.97804 0.65544 0.79310 -0.04831 0.07489  0.02334  402 UDP B PA    
4808 O  O1A   . UDP P .   ? 1.05263 0.74073 0.86984 -0.05510 0.08078  0.02706  402 UDP B O1A   
4809 O  O2A   . UDP P .   ? 0.97699 0.65904 0.79045 -0.04120 0.07555  0.01933  402 UDP B O2A   
4810 O  O3A   . UDP P .   ? 0.95231 0.62421 0.77943 -0.04711 0.06956  0.02155  402 UDP B O3A   
4811 P  PB    . UDP P .   ? 1.15038 0.81111 0.97888 -0.04314 0.06160  0.01929  402 UDP B PB    
4812 O  O1B   . UDP P .   ? 1.08510 0.73305 0.90059 -0.04441 0.05812  0.02142  402 UDP B O1B   
4813 O  O2B   . UDP P .   ? 0.98054 0.64191 0.80833 -0.03770 0.06005  0.01565  402 UDP B O2B   
4814 O  O3B   . UDP P .   ? 1.19010 0.85432 1.03237 -0.04385 0.05984  0.01902  402 UDP B O3B   
4815 C  C1    . B3P Q .   ? 1.08076 0.46495 0.65099 0.07957  -0.09826 -0.00162 403 B3P B C1    
4816 C  C2    . B3P Q .   ? 0.99234 0.40744 0.59238 0.06961  -0.08544 0.00031  403 B3P B C2    
4817 C  C3    . B3P Q .   ? 1.09357 0.43937 0.63052 0.07659  -0.10554 0.00000  403 B3P B C3    
4818 N  N1    . B3P Q .   ? 1.14616 0.48344 0.68496 0.05632  -0.09729 0.00695  403 B3P B N1    
4819 C  C4    . B3P Q .   ? 1.19750 0.51411 0.71314 0.04879  -0.10112 0.00956  403 B3P B C4    
4820 C  C5    . B3P Q .   ? 1.31824 0.63803 0.84255 0.02782  -0.09111 0.01684  403 B3P B C5    
4821 C  C6    . B3P Q .   ? 1.21138 0.50815 0.70201 0.05371  -0.11309 0.00817  403 B3P B C6    
4822 C  C7    . B3P Q .   ? 1.17250 0.48503 0.68022 0.05471  -0.10263 0.00718  403 B3P B C7    
4823 N  N2    . B3P Q .   ? 1.04917 0.46600 0.64424 0.07437  -0.08720 -0.00204 403 B3P B N2    
4824 C  C8    . B3P Q .   ? 1.02307 0.45393 0.63523 0.06144  -0.07661 0.00113  403 B3P B C8    
4825 C  C9    . B3P Q .   ? 1.10386 0.56958 0.74909 0.05801  -0.06764 0.00145  403 B3P B C9    
4826 C  C10   . B3P Q .   ? 0.99995 0.43588 0.60909 0.06834  -0.07925 -0.00208 403 B3P B C10   
4827 C  C11   . B3P Q .   ? 0.95162 0.35679 0.54892 0.04643  -0.07371 0.00687  403 B3P B C11   
4828 O  O1    . B3P Q .   ? 0.88968 0.37486 0.54271 0.07261  -0.07268 -0.00330 403 B3P B O1    
4829 O  O2    . B3P Q .   ? 0.95034 0.40465 0.57908 0.05864  -0.06985 -0.00008 403 B3P B O2    
4830 O  O3    . B3P Q .   ? 1.18586 0.60690 0.80147 0.03406  -0.06270 0.01015  403 B3P B O3    
4831 O  O4    . B3P Q .   ? 1.21717 0.55597 0.76493 0.02357  -0.08019 0.01785  403 B3P B O4    
4832 O  O5    . B3P Q .   ? 1.26582 0.55469 0.74015 0.07193  -0.12344 0.00185  403 B3P B O5    
4833 O  O6    . B3P Q .   ? 1.28792 0.58089 0.77364 0.04577  -0.10593 0.01046  403 B3P B O6    
4860 O  O     . HOH R .   ? 0.56400 0.31747 0.62061 0.02263  0.04577  -0.00140 501 HOH A O     
4861 O  O     . HOH R .   ? 0.56087 0.44198 0.65246 0.00052  0.13342  -0.02260 502 HOH A O     
4862 O  O     . HOH R .   ? 0.52133 0.48992 0.70570 0.05568  0.10292  0.00197  503 HOH A O     
4863 O  O     . HOH R .   ? 0.29326 0.18652 0.44348 0.01145  0.11663  -0.00431 504 HOH A O     
4864 O  O     . HOH R .   ? 0.59665 0.31638 0.62886 -0.00813 0.03545  0.00450  505 HOH A O     
4865 O  O     . HOH R .   ? 0.46868 0.33281 0.50823 0.00946  0.12944  -0.03051 506 HOH A O     
4866 O  O     . HOH R .   ? 0.36188 0.20768 0.48687 0.04694  0.07976  -0.00655 507 HOH A O     
4867 O  O     . HOH R .   ? 0.46497 0.27237 0.47351 0.01690  0.10773  -0.03357 508 HOH A O     
4868 O  O     . HOH R .   ? 0.45793 0.21505 0.47135 0.01891  0.08620  -0.03041 509 HOH A O     
4869 O  O     . HOH R .   ? 0.25649 0.20648 0.41263 -0.02099 0.14054  -0.02092 510 HOH A O     
4870 O  O     . HOH R .   ? 0.37091 0.33593 0.55891 0.01558  0.10503  0.02220  511 HOH A O     
4871 O  O     . HOH R .   ? 0.44078 0.37832 0.61372 0.01181  0.14117  -0.02962 512 HOH A O     
4872 O  O     . HOH R .   ? 0.56935 0.48482 0.62057 0.00448  0.14550  -0.03059 513 HOH A O     
4873 O  O     . HOH R .   ? 0.55909 0.48305 0.66221 -0.04440 0.14033  -0.00585 514 HOH A O     
4874 O  O     . HOH R .   ? 0.48046 0.31156 0.51447 -0.03032 0.11550  -0.00232 515 HOH A O     
4875 O  O     . HOH R .   ? 0.31998 0.18228 0.44869 0.06941  0.07398  -0.00586 516 HOH A O     
4876 O  O     . HOH R .   ? 0.56299 0.24032 0.49284 0.03864  0.05995  -0.04616 517 HOH A O     
4877 O  O     . HOH R .   ? 0.47992 0.35929 0.55237 -0.07428 0.12243  0.01199  518 HOH A O     
4878 O  O     . HOH R .   ? 0.39729 0.34727 0.55130 0.07647  0.07686  0.00965  519 HOH A O     
4879 O  O     . HOH R .   ? 0.48934 0.34707 0.56959 -0.03529 0.12070  0.00105  520 HOH A O     
4880 O  O     . HOH R .   ? 0.38772 0.33214 0.56206 -0.02843 0.11936  -0.02258 521 HOH A O     
4881 O  O     . HOH R .   ? 0.50575 0.33325 0.57840 -0.05404 0.06033  0.02568  522 HOH A O     
4882 O  O     . HOH R .   ? 0.38124 0.28039 0.54630 0.03268  0.10939  -0.01696 523 HOH A O     
4883 O  O     . HOH R .   ? 0.47717 0.30084 0.55109 -0.05347 0.06188  0.02510  524 HOH A O     
4884 O  O     . HOH R .   ? 0.37623 0.26590 0.42704 -0.06153 0.13423  0.00715  525 HOH A O     
4885 O  O     . HOH R .   ? 0.50554 0.44385 0.67045 0.03462  0.11154  -0.01884 526 HOH A O     
4886 O  O     . HOH R .   ? 0.27412 0.14058 0.40535 0.00945  0.10507  -0.00290 527 HOH A O     
4887 O  O     . HOH R .   ? 0.79529 0.65658 0.88187 0.12775  0.03201  -0.01346 528 HOH A O     
4888 O  O     . HOH R .   ? 0.55969 0.36340 0.61085 -0.06060 0.05063  0.02539  529 HOH A O     
4889 O  O     . HOH R .   ? 0.57918 0.30417 0.57580 -0.11242 0.00486  0.05225  530 HOH A O     
4890 O  O     . HOH R .   ? 0.54553 0.39090 0.48975 0.03541  0.11992  -0.04181 531 HOH A O     
4891 O  O     . HOH R .   ? 0.41399 0.35014 0.59101 0.03549  0.11631  -0.00627 532 HOH A O     
4892 O  O     . HOH R .   ? 0.47695 0.30274 0.60465 -0.01161 0.06825  -0.01493 533 HOH A O     
4893 O  O     . HOH R .   ? 0.44268 0.22050 0.47910 -0.10297 0.06388  0.02584  534 HOH A O     
4894 O  O     . HOH R .   ? 0.44404 0.28599 0.55308 0.07612  0.05645  -0.01317 535 HOH A O     
4895 O  O     . HOH R .   ? 0.35592 0.30623 0.54043 0.02564  0.10804  0.01277  536 HOH A O     
4896 O  O     . HOH R .   ? 0.48354 0.62936 0.64508 -0.00569 0.17613  -0.04636 537 HOH A O     
4897 O  O     . HOH R .   ? 0.49140 0.28573 0.53905 -0.11666 0.06070  0.02629  538 HOH A O     
4898 O  O     . HOH R .   ? 0.41184 0.24802 0.55071 0.01449  0.07850  -0.01857 539 HOH A O     
4899 O  O     . HOH R .   ? 0.40653 0.26037 0.47644 -0.10517 0.09541  0.02163  540 HOH A O     
4900 O  O     . HOH R .   ? 0.28586 0.21956 0.47212 0.03470  0.11850  -0.00056 541 HOH A O     
4901 O  O     . HOH R .   ? 0.35224 0.14931 0.39379 0.02731  0.10381  -0.03528 542 HOH A O     
4902 O  O     . HOH R .   ? 0.74917 0.46967 0.65797 -0.00616 0.06986  -0.01628 543 HOH A O     
4903 O  O     . HOH R .   ? 0.42237 0.19650 0.40018 0.04901  0.09793  -0.05310 544 HOH A O     
4904 O  O     . HOH R .   ? 0.44498 0.44905 0.51723 -0.07420 0.15884  0.00398  545 HOH A O     
4905 O  O     . HOH R .   ? 0.51557 0.15060 0.47502 -0.04944 0.00263  0.01970  546 HOH A O     
4906 O  O     . HOH R .   ? 0.49526 0.40800 0.57553 0.06080  0.04320  0.01633  547 HOH A O     
4907 O  O     . HOH R .   ? 0.34924 0.44834 0.48294 -0.05070 0.17343  -0.01959 548 HOH A O     
4908 O  O     . HOH R .   ? 0.46097 0.24653 0.51733 0.02464  0.09624  -0.02456 549 HOH A O     
4909 O  O     . HOH R .   ? 0.43479 0.38056 0.60864 0.02444  0.12981  -0.03107 550 HOH A O     
4910 O  O     . HOH R .   ? 0.56934 0.29840 0.49215 0.02261  0.07505  -0.03677 551 HOH A O     
4911 O  O     . HOH R .   ? 0.34075 0.26826 0.51628 0.01837  0.11334  0.00695  552 HOH A O     
4912 O  O     . HOH R .   ? 0.51636 0.55951 0.64555 0.01848  0.17326  -0.05027 553 HOH A O     
4913 O  O     . HOH R .   ? 0.54568 0.30651 0.54339 -0.07339 0.08333  0.02621  554 HOH A O     
4914 O  O     . HOH R .   ? 0.44335 0.45610 0.64689 0.07739  0.09801  0.01488  555 HOH A O     
4915 O  O     . HOH R .   ? 0.41175 0.32480 0.48742 -0.11944 0.11659  0.02436  556 HOH A O     
4916 O  O     . HOH R .   ? 0.51914 0.42750 0.66661 0.07585  0.07922  -0.00584 557 HOH A O     
4917 O  O     . HOH R .   ? 0.46873 0.23120 0.38932 0.06174  0.09067  -0.05975 558 HOH A O     
4918 O  O     . HOH R .   ? 0.57811 0.33198 0.57399 0.04757  0.09199  -0.04901 559 HOH A O     
4919 O  O     . HOH R .   ? 0.36545 0.24630 0.50161 0.02634  0.12454  -0.02123 560 HOH A O     
4920 O  O     . HOH R .   ? 0.48624 0.30954 0.51806 -0.16384 0.06712  0.04345  561 HOH A O     
4921 O  O     . HOH R .   ? 0.63568 0.34651 0.57094 0.05555  0.07470  -0.05684 562 HOH A O     
4922 O  O     . HOH R .   ? 0.70216 0.34830 0.59856 -0.00850 0.01682  0.02065  563 HOH A O     
4923 O  O     . HOH R .   ? 0.55317 0.34720 0.58765 0.04856  0.10159  -0.04563 564 HOH A O     
4924 O  O     . HOH R .   ? 0.57605 0.49661 0.75254 0.02633  0.12011  -0.00140 565 HOH A O     
4925 O  O     . HOH R .   ? 0.45651 0.31061 0.57044 0.08157  0.06009  -0.00983 566 HOH A O     
4926 O  O     . HOH R .   ? 0.50014 0.30674 0.53244 0.04983  0.11185  -0.05093 567 HOH A O     
4927 O  O     . HOH R .   ? 0.40077 0.34048 0.57229 0.03613  0.11496  -0.00824 568 HOH A O     
4928 O  O     . HOH R .   ? 0.81210 0.74805 0.91487 0.04557  0.14342  -0.05263 569 HOH A O     
4929 O  O     . HOH S .   ? 0.66721 0.27119 0.48255 -0.02067 0.01248  0.02115  501 HOH B O     
4930 O  O     . HOH S .   ? 0.79520 0.34333 0.51888 -0.01708 0.01024  0.01410  502 HOH B O     
4931 O  O     . HOH S .   ? 0.77637 0.34757 0.52478 0.02337  -0.03014 0.00545  503 HOH B O     
4932 O  O     . HOH S .   ? 0.88426 0.29301 0.45823 0.02095  -0.04136 0.00739  504 HOH B O     
4933 O  O     . HOH S .   ? 1.04262 0.45520 0.57625 0.10245  -0.06449 -0.04790 505 HOH B O     
4934 O  O     . HOH S .   ? 0.75417 0.42437 0.60220 0.01042  -0.01067 0.00946  506 HOH B O     
4935 O  O     . HOH S .   ? 0.80966 0.43721 0.63673 -0.00806 0.00470  0.01478  507 HOH B O     
4936 O  O     . HOH S .   ? 0.86992 0.28323 0.42460 0.02487  -0.02652 0.00479  508 HOH B O     
4937 O  O     . HOH S .   ? 0.93104 0.38295 0.54667 0.03370  -0.04970 -0.01231 509 HOH B O     
4938 O  O     . HOH S .   ? 0.91091 0.32173 0.48651 0.05732  -0.07200 -0.02968 510 HOH B O     
4939 O  O     . HOH S .   ? 0.76729 0.26964 0.45118 -0.02735 0.00344  0.02566  511 HOH B O     
4940 O  O     . HOH S .   ? 0.71704 0.27504 0.46147 -0.00335 -0.02322 -0.00026 512 HOH B O     
4941 O  O     . HOH S .   ? 0.86168 0.30618 0.54720 -0.01048 -0.09255 -0.01951 513 HOH B O     
4942 O  O     . HOH S .   ? 0.70810 0.32056 0.52267 -0.02317 -0.00986 0.00428  514 HOH B O     
4943 O  O     . HOH S .   ? 0.83872 0.44598 0.60862 -0.05032 0.04939  0.02919  515 HOH B O     
4944 O  O     . HOH S .   ? 0.81023 0.41334 0.63596 -0.03748 -0.02547 0.00253  516 HOH B O     
4945 O  O     . HOH S .   ? 1.03680 0.32075 0.44866 0.11819  -0.11784 -0.04248 517 HOH B O     
4946 O  O     . HOH S .   ? 1.02232 0.42083 0.52374 0.12441  -0.15737 -0.05868 518 HOH B O     
# 
