data_9F0M
# 
_entry.id   9F0M 
# 
_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   9F0M         pdb_00009f0m 10.2210/pdb9f0m/pdb 
WWPDB D_1292137968 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9F0M 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rdutoit@spfb.brussels 
_pdbx_contact_author.name_first         Raphael 
_pdbx_contact_author.name_last          Dutoit 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7139-8402 
# 
_audit_author.name               'Dutoit, R.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-7139-8402 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of Ta_Cel5A E133Q Y200F variant in complex with cellopentaose' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Dutoit, R.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0002-7139-8402 
# 
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 cellulase 33843.539 2   3.2.1.4 'E133Q, Y200F' ? 'E133Q and Y200F mutations, no tag' 
2 branched    man 
'beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose' 
828.719   2   ?       ?              ? ?                                   
3 non-polymer syn GLYCEROL 92.094    4   ?       ?              ? ?                                   
4 non-polymer syn 'SULFATE ION' 96.063    2   ?       ?              ? ?                                   
5 water       nat water 18.015    944 ?       ?              ? ?                                   
# 
_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       
;MAKVFQWFGSNESGAEFGSQNLPGVEGKDYIWPDPNTIDTLISKGMNIFRVPFMMERLVPNSMTGSPDPNYLADLIATVN
AITQKGAYAVVDPHNYGRYYNSIISSPSDFQTFWKTVASQFASNPLVIFDTNNQYHDMDQTLVLNLNQAAIDGIRSAGAT
SQYIFVEGNSWTGAWTWTNVNDNMKSLTDPSDKIIYEMHQFLDSDGSGTSATCVSSTIGQERITSATQWLRANGKKGIIG
EFAGGANDVCETAITGMLDYMAQNTDVWTGAIWWAAGPWWGDYIFSMEPDNGIAYQQILPILTPYL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAKVFQWFGSNESGAEFGSQNLPGVEGKDYIWPDPNTIDTLISKGMNIFRVPFMMERLVPNSMTGSPDPNYLADLIATVN
AITQKGAYAVVDPHNYGRYYNSIISSPSDFQTFWKTVASQFASNPLVIFDTNNQYHDMDQTLVLNLNQAAIDGIRSAGAT
SQYIFVEGNSWTGAWTWTNVNDNMKSLTDPSDKIIYEMHQFLDSDGSGTSATCVSSTIGQERITSATQWLRANGKKGIIG
EFAGGANDVCETAITGMLDYMAQNTDVWTGAIWWAAGPWWGDYIFSMEPDNGIAYQQILPILTPYL
;
_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 
3 GLYCEROL      GOL 
4 'SULFATE ION' SO4 
5 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   LYS n 
1 4   VAL n 
1 5   PHE n 
1 6   GLN n 
1 7   TRP n 
1 8   PHE n 
1 9   GLY n 
1 10  SER n 
1 11  ASN n 
1 12  GLU n 
1 13  SER n 
1 14  GLY n 
1 15  ALA n 
1 16  GLU n 
1 17  PHE n 
1 18  GLY n 
1 19  SER n 
1 20  GLN n 
1 21  ASN n 
1 22  LEU n 
1 23  PRO n 
1 24  GLY n 
1 25  VAL n 
1 26  GLU n 
1 27  GLY n 
1 28  LYS n 
1 29  ASP n 
1 30  TYR n 
1 31  ILE n 
1 32  TRP n 
1 33  PRO n 
1 34  ASP n 
1 35  PRO n 
1 36  ASN n 
1 37  THR n 
1 38  ILE n 
1 39  ASP n 
1 40  THR n 
1 41  LEU n 
1 42  ILE n 
1 43  SER n 
1 44  LYS n 
1 45  GLY n 
1 46  MET n 
1 47  ASN n 
1 48  ILE n 
1 49  PHE n 
1 50  ARG n 
1 51  VAL n 
1 52  PRO n 
1 53  PHE n 
1 54  MET n 
1 55  MET n 
1 56  GLU n 
1 57  ARG n 
1 58  LEU n 
1 59  VAL n 
1 60  PRO n 
1 61  ASN n 
1 62  SER n 
1 63  MET n 
1 64  THR n 
1 65  GLY n 
1 66  SER n 
1 67  PRO n 
1 68  ASP n 
1 69  PRO n 
1 70  ASN n 
1 71  TYR n 
1 72  LEU n 
1 73  ALA n 
1 74  ASP n 
1 75  LEU n 
1 76  ILE n 
1 77  ALA n 
1 78  THR n 
1 79  VAL n 
1 80  ASN n 
1 81  ALA n 
1 82  ILE n 
1 83  THR n 
1 84  GLN n 
1 85  LYS n 
1 86  GLY n 
1 87  ALA n 
1 88  TYR n 
1 89  ALA n 
1 90  VAL n 
1 91  VAL n 
1 92  ASP n 
1 93  PRO n 
1 94  HIS n 
1 95  ASN n 
1 96  TYR n 
1 97  GLY n 
1 98  ARG n 
1 99  TYR n 
1 100 TYR n 
1 101 ASN n 
1 102 SER n 
1 103 ILE n 
1 104 ILE n 
1 105 SER n 
1 106 SER n 
1 107 PRO n 
1 108 SER n 
1 109 ASP n 
1 110 PHE n 
1 111 GLN n 
1 112 THR n 
1 113 PHE n 
1 114 TRP n 
1 115 LYS n 
1 116 THR n 
1 117 VAL n 
1 118 ALA n 
1 119 SER n 
1 120 GLN n 
1 121 PHE n 
1 122 ALA n 
1 123 SER n 
1 124 ASN n 
1 125 PRO n 
1 126 LEU n 
1 127 VAL n 
1 128 ILE n 
1 129 PHE n 
1 130 ASP n 
1 131 THR n 
1 132 ASN n 
1 133 ASN n 
1 134 GLN n 
1 135 TYR n 
1 136 HIS n 
1 137 ASP n 
1 138 MET n 
1 139 ASP n 
1 140 GLN n 
1 141 THR n 
1 142 LEU n 
1 143 VAL n 
1 144 LEU n 
1 145 ASN n 
1 146 LEU n 
1 147 ASN n 
1 148 GLN n 
1 149 ALA n 
1 150 ALA n 
1 151 ILE n 
1 152 ASP n 
1 153 GLY n 
1 154 ILE n 
1 155 ARG n 
1 156 SER n 
1 157 ALA n 
1 158 GLY n 
1 159 ALA n 
1 160 THR n 
1 161 SER n 
1 162 GLN n 
1 163 TYR n 
1 164 ILE n 
1 165 PHE n 
1 166 VAL n 
1 167 GLU n 
1 168 GLY n 
1 169 ASN n 
1 170 SER n 
1 171 TRP n 
1 172 THR n 
1 173 GLY n 
1 174 ALA n 
1 175 TRP n 
1 176 THR n 
1 177 TRP n 
1 178 THR n 
1 179 ASN n 
1 180 VAL n 
1 181 ASN n 
1 182 ASP n 
1 183 ASN n 
1 184 MET n 
1 185 LYS n 
1 186 SER n 
1 187 LEU n 
1 188 THR n 
1 189 ASP n 
1 190 PRO n 
1 191 SER n 
1 192 ASP n 
1 193 LYS n 
1 194 ILE n 
1 195 ILE n 
1 196 TYR n 
1 197 GLU n 
1 198 MET n 
1 199 HIS n 
1 200 GLN n 
1 201 PHE n 
1 202 LEU n 
1 203 ASP n 
1 204 SER n 
1 205 ASP n 
1 206 GLY n 
1 207 SER n 
1 208 GLY n 
1 209 THR n 
1 210 SER n 
1 211 ALA n 
1 212 THR n 
1 213 CYS n 
1 214 VAL n 
1 215 SER n 
1 216 SER n 
1 217 THR n 
1 218 ILE n 
1 219 GLY n 
1 220 GLN n 
1 221 GLU n 
1 222 ARG n 
1 223 ILE n 
1 224 THR n 
1 225 SER n 
1 226 ALA n 
1 227 THR n 
1 228 GLN n 
1 229 TRP n 
1 230 LEU n 
1 231 ARG n 
1 232 ALA n 
1 233 ASN n 
1 234 GLY n 
1 235 LYS n 
1 236 LYS n 
1 237 GLY n 
1 238 ILE n 
1 239 ILE n 
1 240 GLY n 
1 241 GLU n 
1 242 PHE n 
1 243 ALA n 
1 244 GLY n 
1 245 GLY n 
1 246 ALA n 
1 247 ASN n 
1 248 ASP n 
1 249 VAL n 
1 250 CYS n 
1 251 GLU n 
1 252 THR n 
1 253 ALA n 
1 254 ILE n 
1 255 THR n 
1 256 GLY n 
1 257 MET n 
1 258 LEU n 
1 259 ASP n 
1 260 TYR n 
1 261 MET n 
1 262 ALA n 
1 263 GLN n 
1 264 ASN n 
1 265 THR n 
1 266 ASP n 
1 267 VAL n 
1 268 TRP n 
1 269 THR n 
1 270 GLY n 
1 271 ALA n 
1 272 ILE n 
1 273 TRP n 
1 274 TRP n 
1 275 ALA n 
1 276 ALA n 
1 277 GLY n 
1 278 PRO n 
1 279 TRP n 
1 280 TRP n 
1 281 GLY n 
1 282 ASP n 
1 283 TYR n 
1 284 ILE n 
1 285 PHE n 
1 286 SER n 
1 287 MET n 
1 288 GLU n 
1 289 PRO n 
1 290 ASP n 
1 291 ASN n 
1 292 GLY n 
1 293 ILE n 
1 294 ALA n 
1 295 TYR n 
1 296 GLN n 
1 297 GLN n 
1 298 ILE n 
1 299 LEU n 
1 300 PRO n 
1 301 ILE n 
1 302 LEU n 
1 303 THR n 
1 304 PRO n 
1 305 TYR n 
1 306 LEU 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                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 eg1 
_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      'Thermoascus aurantiacus ATCC 26904' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1133049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 26904 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET30b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        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 DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-ROH                                              'Glycam Condensed Sequence' GMML 
1.0   
2 2 'WURCS=2.0/1,5,4/[a2122h-1b_1-5]/1-1-1-1-1/a4-b1_b4-c1_c4-d1_d4-e1'                          WURCS                       
PDB2Glycan 1.1.0 
3 2 '[][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{}}}}}' 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 BGC C1 O1 1 BGC O4 HO4 sing ? 
2 2 3 BGC C1 O1 2 BGC O4 HO4 sing ? 
3 2 4 BGC C1 O1 3 BGC O4 HO4 sing ? 
4 2 5 BGC C1 O1 4 BGC O4 HO4 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 
BGC 'D-saccharide, beta linking' . beta-D-glucopyranose 'beta-D-glucose; D-glucose; glucose' 'C6 H12 O6'      180.156 
CYS 'L-peptide linking'          y CYSTEINE             ?                                    'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE            ?                                    'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'      ?                                    'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE              ?                                    'C2 H5 N O2'     75.067  
GOL non-polymer                  . GLYCEROL             'GLYCERIN; PROPANE-1,2,3-TRIOL'      'C3 H8 O3'       92.094  
HIS 'L-peptide linking'          y HISTIDINE            ?                                    'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                  . WATER                ?                                    'H2 O'           18.015  
ILE 'L-peptide linking'          y ISOLEUCINE           ?                                    'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE              ?                                    'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE               ?                                    'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE           ?                                    'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking'          y PHENYLALANINE        ?                                    'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE              ?                                    'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE               ?                                    'C3 H7 N O3'     105.093 
SO4 non-polymer                  . 'SULFATE ION'        ?                                    'O4 S -2'        96.063  
THR 'L-peptide linking'          y THREONINE            ?                                    'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN           ?                                    'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE             ?                                    'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE               ?                                    'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_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               
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   ALA 2   1   ?   ?   ?   A . n 
A 1 3   LYS 3   2   2   LYS LYS A . n 
A 1 4   VAL 4   3   3   VAL VAL A . n 
A 1 5   PHE 5   4   4   PHE PHE A . n 
A 1 6   GLN 6   5   5   GLN GLN A . n 
A 1 7   TRP 7   6   6   TRP TRP A . n 
A 1 8   PHE 8   7   7   PHE PHE A . n 
A 1 9   GLY 9   8   8   GLY GLY A . n 
A 1 10  SER 10  9   9   SER SER A . n 
A 1 11  ASN 11  10  10  ASN ASN A . n 
A 1 12  GLU 12  11  11  GLU GLU A . n 
A 1 13  SER 13  12  12  SER SER A . n 
A 1 14  GLY 14  13  13  GLY GLY A . n 
A 1 15  ALA 15  14  14  ALA ALA A . n 
A 1 16  GLU 16  15  15  GLU GLU A . n 
A 1 17  PHE 17  16  16  PHE PHE A . n 
A 1 18  GLY 18  17  17  GLY GLY A . n 
A 1 19  SER 19  18  18  SER SER A . n 
A 1 20  GLN 20  19  19  GLN GLN A . n 
A 1 21  ASN 21  20  20  ASN ASN A . n 
A 1 22  LEU 22  21  21  LEU LEU A . n 
A 1 23  PRO 23  22  22  PRO PRO A . n 
A 1 24  GLY 24  23  23  GLY GLY A . n 
A 1 25  VAL 25  24  24  VAL VAL A . n 
A 1 26  GLU 26  25  25  GLU GLU A . n 
A 1 27  GLY 27  26  26  GLY GLY A . n 
A 1 28  LYS 28  27  27  LYS LYS A . n 
A 1 29  ASP 29  28  28  ASP ASP A . n 
A 1 30  TYR 30  29  29  TYR TYR A . n 
A 1 31  ILE 31  30  30  ILE ILE A . n 
A 1 32  TRP 32  31  31  TRP TRP A . n 
A 1 33  PRO 33  32  32  PRO PRO A . n 
A 1 34  ASP 34  33  33  ASP ASP A . n 
A 1 35  PRO 35  34  34  PRO PRO A . n 
A 1 36  ASN 36  35  35  ASN ASN A . n 
A 1 37  THR 37  36  36  THR THR A . n 
A 1 38  ILE 38  37  37  ILE ILE A . n 
A 1 39  ASP 39  38  38  ASP ASP A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  LEU 41  40  40  LEU LEU A . n 
A 1 42  ILE 42  41  41  ILE ILE A . n 
A 1 43  SER 43  42  42  SER SER A . n 
A 1 44  LYS 44  43  43  LYS LYS A . n 
A 1 45  GLY 45  44  44  GLY GLY A . n 
A 1 46  MET 46  45  45  MET MET A . n 
A 1 47  ASN 47  46  46  ASN ASN A . n 
A 1 48  ILE 48  47  47  ILE ILE A . n 
A 1 49  PHE 49  48  48  PHE PHE A . n 
A 1 50  ARG 50  49  49  ARG ARG A . n 
A 1 51  VAL 51  50  50  VAL VAL A . n 
A 1 52  PRO 52  51  51  PRO PRO A . n 
A 1 53  PHE 53  52  52  PHE PHE A . n 
A 1 54  MET 54  53  53  MET MET A . n 
A 1 55  MET 55  54  54  MET MET A . n 
A 1 56  GLU 56  55  55  GLU GLU A . n 
A 1 57  ARG 57  56  56  ARG ARG A . n 
A 1 58  LEU 58  57  57  LEU LEU A . n 
A 1 59  VAL 59  58  58  VAL VAL A . n 
A 1 60  PRO 60  59  59  PRO PRO A . n 
A 1 61  ASN 61  60  60  ASN ASN A . n 
A 1 62  SER 62  61  61  SER SER A . n 
A 1 63  MET 63  62  62  MET MET A . n 
A 1 64  THR 64  63  63  THR THR A . n 
A 1 65  GLY 65  64  64  GLY GLY A . n 
A 1 66  SER 66  65  65  SER SER A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  ASP 68  67  67  ASP ASP A . n 
A 1 69  PRO 69  68  68  PRO PRO A . n 
A 1 70  ASN 70  69  69  ASN ASN A . n 
A 1 71  TYR 71  70  70  TYR TYR A . n 
A 1 72  LEU 72  71  71  LEU LEU A . n 
A 1 73  ALA 73  72  72  ALA ALA A . n 
A 1 74  ASP 74  73  73  ASP ASP A . n 
A 1 75  LEU 75  74  74  LEU LEU A . n 
A 1 76  ILE 76  75  75  ILE ILE A . n 
A 1 77  ALA 77  76  76  ALA ALA A . n 
A 1 78  THR 78  77  77  THR THR A . n 
A 1 79  VAL 79  78  78  VAL VAL A . n 
A 1 80  ASN 80  79  79  ASN ASN A . n 
A 1 81  ALA 81  80  80  ALA ALA A . n 
A 1 82  ILE 82  81  81  ILE ILE A . n 
A 1 83  THR 83  82  82  THR THR A . n 
A 1 84  GLN 84  83  83  GLN GLN A . n 
A 1 85  LYS 85  84  84  LYS LYS A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  ALA 87  86  86  ALA ALA A . n 
A 1 88  TYR 88  87  87  TYR TYR A . n 
A 1 89  ALA 89  88  88  ALA ALA A . n 
A 1 90  VAL 90  89  89  VAL VAL A . n 
A 1 91  VAL 91  90  90  VAL VAL A . n 
A 1 92  ASP 92  91  91  ASP ASP A . n 
A 1 93  PRO 93  92  92  PRO PRO A . n 
A 1 94  HIS 94  93  93  HIS HIS A . n 
A 1 95  ASN 95  94  94  ASN ASN A . n 
A 1 96  TYR 96  95  95  TYR TYR A . n 
A 1 97  GLY 97  96  96  GLY GLY A . n 
A 1 98  ARG 98  97  97  ARG ARG A . n 
A 1 99  TYR 99  98  98  TYR TYR A . n 
A 1 100 TYR 100 99  99  TYR TYR A . n 
A 1 101 ASN 101 100 100 ASN ASN A . n 
A 1 102 SER 102 101 101 SER SER A . n 
A 1 103 ILE 103 102 102 ILE ILE A . n 
A 1 104 ILE 104 103 103 ILE ILE A . n 
A 1 105 SER 105 104 104 SER SER A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 PRO 107 106 106 PRO PRO A . n 
A 1 108 SER 108 107 107 SER SER A . n 
A 1 109 ASP 109 108 108 ASP ASP A . n 
A 1 110 PHE 110 109 109 PHE PHE A . n 
A 1 111 GLN 111 110 110 GLN GLN A . n 
A 1 112 THR 112 111 111 THR THR A . n 
A 1 113 PHE 113 112 112 PHE PHE A . n 
A 1 114 TRP 114 113 113 TRP TRP A . n 
A 1 115 LYS 115 114 114 LYS LYS A . n 
A 1 116 THR 116 115 115 THR THR A . n 
A 1 117 VAL 117 116 116 VAL VAL A . n 
A 1 118 ALA 118 117 117 ALA ALA A . n 
A 1 119 SER 119 118 118 SER SER A . n 
A 1 120 GLN 120 119 119 GLN GLN A . n 
A 1 121 PHE 121 120 120 PHE PHE A . n 
A 1 122 ALA 122 121 121 ALA ALA A . n 
A 1 123 SER 123 122 122 SER SER A . n 
A 1 124 ASN 124 123 123 ASN ASN A . n 
A 1 125 PRO 125 124 124 PRO PRO A . n 
A 1 126 LEU 126 125 125 LEU LEU A . n 
A 1 127 VAL 127 126 126 VAL VAL A . n 
A 1 128 ILE 128 127 127 ILE ILE A . n 
A 1 129 PHE 129 128 128 PHE PHE A . n 
A 1 130 ASP 130 129 129 ASP ASP A . n 
A 1 131 THR 131 130 130 THR THR A . n 
A 1 132 ASN 132 131 131 ASN ASN A . n 
A 1 133 ASN 133 132 132 ASN ASN A . n 
A 1 134 GLN 134 133 133 GLN GLN A . n 
A 1 135 TYR 135 134 134 TYR TYR A . n 
A 1 136 HIS 136 135 135 HIS HIS A . n 
A 1 137 ASP 137 136 136 ASP ASP A . n 
A 1 138 MET 138 137 137 MET MET A . n 
A 1 139 ASP 139 138 138 ASP ASP A . n 
A 1 140 GLN 140 139 139 GLN GLN A . n 
A 1 141 THR 141 140 140 THR THR A . n 
A 1 142 LEU 142 141 141 LEU LEU A . n 
A 1 143 VAL 143 142 142 VAL VAL A . n 
A 1 144 LEU 144 143 143 LEU LEU A . n 
A 1 145 ASN 145 144 144 ASN ASN A . n 
A 1 146 LEU 146 145 145 LEU LEU A . n 
A 1 147 ASN 147 146 146 ASN ASN A . n 
A 1 148 GLN 148 147 147 GLN GLN A . n 
A 1 149 ALA 149 148 148 ALA ALA A . n 
A 1 150 ALA 150 149 149 ALA ALA A . n 
A 1 151 ILE 151 150 150 ILE ILE A . n 
A 1 152 ASP 152 151 151 ASP ASP A . n 
A 1 153 GLY 153 152 152 GLY GLY A . n 
A 1 154 ILE 154 153 153 ILE ILE A . n 
A 1 155 ARG 155 154 154 ARG ARG A . n 
A 1 156 SER 156 155 155 SER SER A . n 
A 1 157 ALA 157 156 156 ALA ALA A . n 
A 1 158 GLY 158 157 157 GLY GLY A . n 
A 1 159 ALA 159 158 158 ALA ALA A . n 
A 1 160 THR 160 159 159 THR THR A . n 
A 1 161 SER 161 160 160 SER SER A . n 
A 1 162 GLN 162 161 161 GLN GLN A . n 
A 1 163 TYR 163 162 162 TYR TYR A . n 
A 1 164 ILE 164 163 163 ILE ILE A . n 
A 1 165 PHE 165 164 164 PHE PHE A . n 
A 1 166 VAL 166 165 165 VAL VAL A . n 
A 1 167 GLU 167 166 166 GLU GLU A . n 
A 1 168 GLY 168 167 167 GLY GLY A . n 
A 1 169 ASN 169 168 168 ASN ASN A . n 
A 1 170 SER 170 169 169 SER SER A . n 
A 1 171 TRP 171 170 170 TRP TRP A . n 
A 1 172 THR 172 171 171 THR THR A . n 
A 1 173 GLY 173 172 172 GLY GLY A . n 
A 1 174 ALA 174 173 173 ALA ALA A . n 
A 1 175 TRP 175 174 174 TRP TRP A . n 
A 1 176 THR 176 175 175 THR THR A . n 
A 1 177 TRP 177 176 176 TRP TRP A . n 
A 1 178 THR 178 177 177 THR THR A . n 
A 1 179 ASN 179 178 178 ASN ASN A . n 
A 1 180 VAL 180 179 179 VAL VAL A . n 
A 1 181 ASN 181 180 180 ASN ASN A . n 
A 1 182 ASP 182 181 181 ASP ASP A . n 
A 1 183 ASN 183 182 182 ASN ASN A . n 
A 1 184 MET 184 183 183 MET MET A . n 
A 1 185 LYS 185 184 184 LYS LYS A . n 
A 1 186 SER 186 185 185 SER SER A . n 
A 1 187 LEU 187 186 186 LEU LEU A . n 
A 1 188 THR 188 187 187 THR THR A . n 
A 1 189 ASP 189 188 188 ASP ASP A . n 
A 1 190 PRO 190 189 189 PRO PRO A . n 
A 1 191 SER 191 190 190 SER SER A . n 
A 1 192 ASP 192 191 191 ASP ASP A . n 
A 1 193 LYS 193 192 192 LYS LYS A . n 
A 1 194 ILE 194 193 193 ILE ILE A . n 
A 1 195 ILE 195 194 194 ILE ILE A . n 
A 1 196 TYR 196 195 195 TYR TYR A . n 
A 1 197 GLU 197 196 196 GLU GLU A . n 
A 1 198 MET 198 197 197 MET MET A . n 
A 1 199 HIS 199 198 198 HIS HIS A . n 
A 1 200 GLN 200 199 199 GLN GLN A . n 
A 1 201 PHE 201 200 200 PHE PHE A . n 
A 1 202 LEU 202 201 201 LEU LEU A . n 
A 1 203 ASP 203 202 202 ASP ASP A . n 
A 1 204 SER 204 203 203 SER SER A . n 
A 1 205 ASP 205 204 204 ASP ASP A . n 
A 1 206 GLY 206 205 205 GLY GLY A . n 
A 1 207 SER 207 206 206 SER SER A . n 
A 1 208 GLY 208 207 207 GLY GLY A . n 
A 1 209 THR 209 208 208 THR THR A . n 
A 1 210 SER 210 209 209 SER SER A . n 
A 1 211 ALA 211 210 210 ALA ALA A . n 
A 1 212 THR 212 211 211 THR THR A . n 
A 1 213 CYS 213 212 212 CYS CYS A . n 
A 1 214 VAL 214 213 213 VAL VAL A . n 
A 1 215 SER 215 214 214 SER SER A . n 
A 1 216 SER 216 215 215 SER SER A . n 
A 1 217 THR 217 216 216 THR THR A . n 
A 1 218 ILE 218 217 217 ILE ILE A . n 
A 1 219 GLY 219 218 218 GLY GLY A . n 
A 1 220 GLN 220 219 219 GLN GLN A . n 
A 1 221 GLU 221 220 220 GLU GLU A . n 
A 1 222 ARG 222 221 221 ARG ARG A . n 
A 1 223 ILE 223 222 222 ILE ILE A . n 
A 1 224 THR 224 223 223 THR THR A . n 
A 1 225 SER 225 224 224 SER SER A . n 
A 1 226 ALA 226 225 225 ALA ALA A . n 
A 1 227 THR 227 226 226 THR THR A . n 
A 1 228 GLN 228 227 227 GLN GLN A . n 
A 1 229 TRP 229 228 228 TRP TRP A . n 
A 1 230 LEU 230 229 229 LEU LEU A . n 
A 1 231 ARG 231 230 230 ARG ARG A . n 
A 1 232 ALA 232 231 231 ALA ALA A . n 
A 1 233 ASN 233 232 232 ASN ASN A . n 
A 1 234 GLY 234 233 233 GLY GLY A . n 
A 1 235 LYS 235 234 234 LYS LYS A . n 
A 1 236 LYS 236 235 235 LYS LYS A . n 
A 1 237 GLY 237 236 236 GLY GLY A . n 
A 1 238 ILE 238 237 237 ILE ILE A . n 
A 1 239 ILE 239 238 238 ILE ILE A . n 
A 1 240 GLY 240 239 239 GLY GLY A . n 
A 1 241 GLU 241 240 240 GLU GLU A . n 
A 1 242 PHE 242 241 241 PHE PHE A . n 
A 1 243 ALA 243 242 242 ALA ALA A . n 
A 1 244 GLY 244 243 243 GLY GLY A . n 
A 1 245 GLY 245 244 244 GLY GLY A . n 
A 1 246 ALA 246 245 245 ALA ALA A . n 
A 1 247 ASN 247 246 246 ASN ASN A . n 
A 1 248 ASP 248 247 247 ASP ASP A . n 
A 1 249 VAL 249 248 248 VAL VAL A . n 
A 1 250 CYS 250 249 249 CYS CYS A . n 
A 1 251 GLU 251 250 250 GLU GLU A . n 
A 1 252 THR 252 251 251 THR THR A . n 
A 1 253 ALA 253 252 252 ALA ALA A . n 
A 1 254 ILE 254 253 253 ILE ILE A . n 
A 1 255 THR 255 254 254 THR THR A . n 
A 1 256 GLY 256 255 255 GLY GLY A . n 
A 1 257 MET 257 256 256 MET MET A . n 
A 1 258 LEU 258 257 257 LEU LEU A . n 
A 1 259 ASP 259 258 258 ASP ASP A . n 
A 1 260 TYR 260 259 259 TYR TYR A . n 
A 1 261 MET 261 260 260 MET MET A . n 
A 1 262 ALA 262 261 261 ALA ALA A . n 
A 1 263 GLN 263 262 262 GLN GLN A . n 
A 1 264 ASN 264 263 263 ASN ASN A . n 
A 1 265 THR 265 264 264 THR THR A . n 
A 1 266 ASP 266 265 265 ASP ASP A . n 
A 1 267 VAL 267 266 266 VAL VAL A . n 
A 1 268 TRP 268 267 267 TRP TRP A . n 
A 1 269 THR 269 268 268 THR THR A . n 
A 1 270 GLY 270 269 269 GLY GLY A . n 
A 1 271 ALA 271 270 270 ALA ALA A . n 
A 1 272 ILE 272 271 271 ILE ILE A . n 
A 1 273 TRP 273 272 272 TRP TRP A . n 
A 1 274 TRP 274 273 273 TRP TRP A . n 
A 1 275 ALA 275 274 274 ALA ALA A . n 
A 1 276 ALA 276 275 275 ALA ALA A . n 
A 1 277 GLY 277 276 276 GLY GLY A . n 
A 1 278 PRO 278 277 277 PRO PRO A . n 
A 1 279 TRP 279 278 278 TRP TRP A . n 
A 1 280 TRP 280 279 279 TRP TRP A . n 
A 1 281 GLY 281 280 280 GLY GLY A . n 
A 1 282 ASP 282 281 281 ASP ASP A . n 
A 1 283 TYR 283 282 282 TYR TYR A . n 
A 1 284 ILE 284 283 283 ILE ILE A . n 
A 1 285 PHE 285 284 284 PHE PHE A . n 
A 1 286 SER 286 285 285 SER SER A . n 
A 1 287 MET 287 286 286 MET MET A . n 
A 1 288 GLU 288 287 287 GLU GLU A . n 
A 1 289 PRO 289 288 288 PRO PRO A . n 
A 1 290 ASP 290 289 289 ASP ASP A . n 
A 1 291 ASN 291 290 290 ASN ASN A . n 
A 1 292 GLY 292 291 291 GLY GLY A . n 
A 1 293 ILE 293 292 292 ILE ILE A . n 
A 1 294 ALA 294 293 293 ALA ALA A . n 
A 1 295 TYR 295 294 294 TYR TYR A . n 
A 1 296 GLN 296 295 295 GLN GLN A . n 
A 1 297 GLN 297 296 296 GLN GLN A . n 
A 1 298 ILE 298 297 297 ILE ILE A . n 
A 1 299 LEU 299 298 298 LEU LEU A . n 
A 1 300 PRO 300 299 299 PRO PRO A . n 
A 1 301 ILE 301 300 300 ILE ILE A . n 
A 1 302 LEU 302 301 301 LEU LEU A . n 
A 1 303 THR 303 302 302 THR THR A . n 
A 1 304 PRO 304 303 303 PRO PRO A . n 
A 1 305 TYR 305 304 304 TYR TYR A . n 
A 1 306 LEU 306 305 305 LEU LEU A . n 
B 1 1   MET 1   0   ?   ?   ?   B . n 
B 1 2   ALA 2   1   1   ALA ALA B . n 
B 1 3   LYS 3   2   2   LYS LYS B . n 
B 1 4   VAL 4   3   3   VAL VAL B . n 
B 1 5   PHE 5   4   4   PHE PHE B . n 
B 1 6   GLN 6   5   5   GLN GLN B . n 
B 1 7   TRP 7   6   6   TRP TRP B . n 
B 1 8   PHE 8   7   7   PHE PHE B . n 
B 1 9   GLY 9   8   8   GLY GLY B . n 
B 1 10  SER 10  9   9   SER SER B . n 
B 1 11  ASN 11  10  10  ASN ASN B . n 
B 1 12  GLU 12  11  11  GLU GLU B . n 
B 1 13  SER 13  12  12  SER SER B . n 
B 1 14  GLY 14  13  13  GLY GLY B . n 
B 1 15  ALA 15  14  14  ALA ALA B . n 
B 1 16  GLU 16  15  15  GLU GLU B . n 
B 1 17  PHE 17  16  16  PHE PHE B . n 
B 1 18  GLY 18  17  17  GLY GLY B . n 
B 1 19  SER 19  18  18  SER SER B . n 
B 1 20  GLN 20  19  19  GLN GLN B . n 
B 1 21  ASN 21  20  20  ASN ASN B . n 
B 1 22  LEU 22  21  21  LEU LEU B . n 
B 1 23  PRO 23  22  22  PRO PRO B . n 
B 1 24  GLY 24  23  23  GLY GLY B . n 
B 1 25  VAL 25  24  24  VAL VAL B . n 
B 1 26  GLU 26  25  25  GLU GLU B . n 
B 1 27  GLY 27  26  26  GLY GLY B . n 
B 1 28  LYS 28  27  27  LYS LYS B . n 
B 1 29  ASP 29  28  28  ASP ASP B . n 
B 1 30  TYR 30  29  29  TYR TYR B . n 
B 1 31  ILE 31  30  30  ILE ILE B . n 
B 1 32  TRP 32  31  31  TRP TRP B . n 
B 1 33  PRO 33  32  32  PRO PRO B . n 
B 1 34  ASP 34  33  33  ASP ASP B . n 
B 1 35  PRO 35  34  34  PRO PRO B . n 
B 1 36  ASN 36  35  35  ASN ASN B . n 
B 1 37  THR 37  36  36  THR THR B . n 
B 1 38  ILE 38  37  37  ILE ILE B . n 
B 1 39  ASP 39  38  38  ASP ASP B . n 
B 1 40  THR 40  39  39  THR THR B . n 
B 1 41  LEU 41  40  40  LEU LEU B . n 
B 1 42  ILE 42  41  41  ILE ILE B . n 
B 1 43  SER 43  42  42  SER SER B . n 
B 1 44  LYS 44  43  43  LYS LYS B . n 
B 1 45  GLY 45  44  44  GLY GLY B . n 
B 1 46  MET 46  45  45  MET MET B . n 
B 1 47  ASN 47  46  46  ASN ASN B . n 
B 1 48  ILE 48  47  47  ILE ILE B . n 
B 1 49  PHE 49  48  48  PHE PHE B . n 
B 1 50  ARG 50  49  49  ARG ARG B . n 
B 1 51  VAL 51  50  50  VAL VAL B . n 
B 1 52  PRO 52  51  51  PRO PRO B . n 
B 1 53  PHE 53  52  52  PHE PHE B . n 
B 1 54  MET 54  53  53  MET MET B . n 
B 1 55  MET 55  54  54  MET MET B . n 
B 1 56  GLU 56  55  55  GLU GLU B . n 
B 1 57  ARG 57  56  56  ARG ARG B . n 
B 1 58  LEU 58  57  57  LEU LEU B . n 
B 1 59  VAL 59  58  58  VAL VAL B . n 
B 1 60  PRO 60  59  59  PRO PRO B . n 
B 1 61  ASN 61  60  60  ASN ASN B . n 
B 1 62  SER 62  61  61  SER SER B . n 
B 1 63  MET 63  62  62  MET MET B . n 
B 1 64  THR 64  63  63  THR THR B . n 
B 1 65  GLY 65  64  64  GLY GLY B . n 
B 1 66  SER 66  65  65  SER SER B . n 
B 1 67  PRO 67  66  66  PRO PRO B . n 
B 1 68  ASP 68  67  67  ASP ASP B . n 
B 1 69  PRO 69  68  68  PRO PRO B . n 
B 1 70  ASN 70  69  69  ASN ASN B . n 
B 1 71  TYR 71  70  70  TYR TYR B . n 
B 1 72  LEU 72  71  71  LEU LEU B . n 
B 1 73  ALA 73  72  72  ALA ALA B . n 
B 1 74  ASP 74  73  73  ASP ASP B . n 
B 1 75  LEU 75  74  74  LEU LEU B . n 
B 1 76  ILE 76  75  75  ILE ILE B . n 
B 1 77  ALA 77  76  76  ALA ALA B . n 
B 1 78  THR 78  77  77  THR THR B . n 
B 1 79  VAL 79  78  78  VAL VAL B . n 
B 1 80  ASN 80  79  79  ASN ASN B . n 
B 1 81  ALA 81  80  80  ALA ALA B . n 
B 1 82  ILE 82  81  81  ILE ILE B . n 
B 1 83  THR 83  82  82  THR THR B . n 
B 1 84  GLN 84  83  83  GLN GLN B . n 
B 1 85  LYS 85  84  84  LYS LYS B . n 
B 1 86  GLY 86  85  85  GLY GLY B . n 
B 1 87  ALA 87  86  86  ALA ALA B . n 
B 1 88  TYR 88  87  87  TYR TYR B . n 
B 1 89  ALA 89  88  88  ALA ALA B . n 
B 1 90  VAL 90  89  89  VAL VAL B . n 
B 1 91  VAL 91  90  90  VAL VAL B . n 
B 1 92  ASP 92  91  91  ASP ASP B . n 
B 1 93  PRO 93  92  92  PRO PRO B . n 
B 1 94  HIS 94  93  93  HIS HIS B . n 
B 1 95  ASN 95  94  94  ASN ASN B . n 
B 1 96  TYR 96  95  95  TYR TYR B . n 
B 1 97  GLY 97  96  96  GLY GLY B . n 
B 1 98  ARG 98  97  97  ARG ARG B . n 
B 1 99  TYR 99  98  98  TYR TYR B . n 
B 1 100 TYR 100 99  99  TYR TYR B . n 
B 1 101 ASN 101 100 100 ASN ASN B . n 
B 1 102 SER 102 101 101 SER SER B . n 
B 1 103 ILE 103 102 102 ILE ILE B . n 
B 1 104 ILE 104 103 103 ILE ILE B . n 
B 1 105 SER 105 104 104 SER SER B . n 
B 1 106 SER 106 105 105 SER SER B . n 
B 1 107 PRO 107 106 106 PRO PRO B . n 
B 1 108 SER 108 107 107 SER SER B . n 
B 1 109 ASP 109 108 108 ASP ASP B . n 
B 1 110 PHE 110 109 109 PHE PHE B . n 
B 1 111 GLN 111 110 110 GLN GLN B . n 
B 1 112 THR 112 111 111 THR THR B . n 
B 1 113 PHE 113 112 112 PHE PHE B . n 
B 1 114 TRP 114 113 113 TRP TRP B . n 
B 1 115 LYS 115 114 114 LYS LYS B . n 
B 1 116 THR 116 115 115 THR THR B . n 
B 1 117 VAL 117 116 116 VAL VAL B . n 
B 1 118 ALA 118 117 117 ALA ALA B . n 
B 1 119 SER 119 118 118 SER SER B . n 
B 1 120 GLN 120 119 119 GLN GLN B . n 
B 1 121 PHE 121 120 120 PHE PHE B . n 
B 1 122 ALA 122 121 121 ALA ALA B . n 
B 1 123 SER 123 122 122 SER SER B . n 
B 1 124 ASN 124 123 123 ASN ASN B . n 
B 1 125 PRO 125 124 124 PRO PRO B . n 
B 1 126 LEU 126 125 125 LEU LEU B . n 
B 1 127 VAL 127 126 126 VAL VAL B . n 
B 1 128 ILE 128 127 127 ILE ILE B . n 
B 1 129 PHE 129 128 128 PHE PHE B . n 
B 1 130 ASP 130 129 129 ASP ASP B . n 
B 1 131 THR 131 130 130 THR THR B . n 
B 1 132 ASN 132 131 131 ASN ASN B . n 
B 1 133 ASN 133 132 132 ASN ASN B . n 
B 1 134 GLN 134 133 133 GLN GLN B . n 
B 1 135 TYR 135 134 134 TYR TYR B . n 
B 1 136 HIS 136 135 135 HIS HIS B . n 
B 1 137 ASP 137 136 136 ASP ASP B . n 
B 1 138 MET 138 137 137 MET MET B . n 
B 1 139 ASP 139 138 138 ASP ASP B . n 
B 1 140 GLN 140 139 139 GLN GLN B . n 
B 1 141 THR 141 140 140 THR THR B . n 
B 1 142 LEU 142 141 141 LEU LEU B . n 
B 1 143 VAL 143 142 142 VAL VAL B . n 
B 1 144 LEU 144 143 143 LEU LEU B . n 
B 1 145 ASN 145 144 144 ASN ASN B . n 
B 1 146 LEU 146 145 145 LEU LEU B . n 
B 1 147 ASN 147 146 146 ASN ASN B . n 
B 1 148 GLN 148 147 147 GLN GLN B . n 
B 1 149 ALA 149 148 148 ALA ALA B . n 
B 1 150 ALA 150 149 149 ALA ALA B . n 
B 1 151 ILE 151 150 150 ILE ILE B . n 
B 1 152 ASP 152 151 151 ASP ASP B . n 
B 1 153 GLY 153 152 152 GLY GLY B . n 
B 1 154 ILE 154 153 153 ILE ILE B . n 
B 1 155 ARG 155 154 154 ARG ARG B . n 
B 1 156 SER 156 155 155 SER SER B . n 
B 1 157 ALA 157 156 156 ALA ALA B . n 
B 1 158 GLY 158 157 157 GLY GLY B . n 
B 1 159 ALA 159 158 158 ALA ALA B . n 
B 1 160 THR 160 159 159 THR THR B . n 
B 1 161 SER 161 160 160 SER SER B . n 
B 1 162 GLN 162 161 161 GLN GLN B . n 
B 1 163 TYR 163 162 162 TYR TYR B . n 
B 1 164 ILE 164 163 163 ILE ILE B . n 
B 1 165 PHE 165 164 164 PHE PHE B . n 
B 1 166 VAL 166 165 165 VAL VAL B . n 
B 1 167 GLU 167 166 166 GLU GLU B . n 
B 1 168 GLY 168 167 167 GLY GLY B . n 
B 1 169 ASN 169 168 168 ASN ASN B . n 
B 1 170 SER 170 169 169 SER SER B . n 
B 1 171 TRP 171 170 170 TRP TRP B . n 
B 1 172 THR 172 171 171 THR THR B . n 
B 1 173 GLY 173 172 172 GLY GLY B . n 
B 1 174 ALA 174 173 173 ALA ALA B . n 
B 1 175 TRP 175 174 174 TRP TRP B . n 
B 1 176 THR 176 175 175 THR THR B . n 
B 1 177 TRP 177 176 176 TRP TRP B . n 
B 1 178 THR 178 177 177 THR THR B . n 
B 1 179 ASN 179 178 178 ASN ASN B . n 
B 1 180 VAL 180 179 179 VAL VAL B . n 
B 1 181 ASN 181 180 180 ASN ASN B . n 
B 1 182 ASP 182 181 181 ASP ASP B . n 
B 1 183 ASN 183 182 182 ASN ASN B . n 
B 1 184 MET 184 183 183 MET MET B . n 
B 1 185 LYS 185 184 184 LYS LYS B . n 
B 1 186 SER 186 185 185 SER SER B . n 
B 1 187 LEU 187 186 186 LEU LEU B . n 
B 1 188 THR 188 187 187 THR THR B . n 
B 1 189 ASP 189 188 188 ASP ASP B . n 
B 1 190 PRO 190 189 189 PRO PRO B . n 
B 1 191 SER 191 190 190 SER SER B . n 
B 1 192 ASP 192 191 191 ASP ASP B . n 
B 1 193 LYS 193 192 192 LYS LYS B . n 
B 1 194 ILE 194 193 193 ILE ILE B . n 
B 1 195 ILE 195 194 194 ILE ILE B . n 
B 1 196 TYR 196 195 195 TYR TYR B . n 
B 1 197 GLU 197 196 196 GLU GLU B . n 
B 1 198 MET 198 197 197 MET MET B . n 
B 1 199 HIS 199 198 198 HIS HIS B . n 
B 1 200 GLN 200 199 199 GLN GLN B . n 
B 1 201 PHE 201 200 200 PHE PHE B . n 
B 1 202 LEU 202 201 201 LEU LEU B . n 
B 1 203 ASP 203 202 202 ASP ASP B . n 
B 1 204 SER 204 203 203 SER SER B . n 
B 1 205 ASP 205 204 204 ASP ASP B . n 
B 1 206 GLY 206 205 205 GLY GLY B . n 
B 1 207 SER 207 206 206 SER SER B . n 
B 1 208 GLY 208 207 207 GLY GLY B . n 
B 1 209 THR 209 208 208 THR THR B . n 
B 1 210 SER 210 209 209 SER SER B . n 
B 1 211 ALA 211 210 210 ALA ALA B . n 
B 1 212 THR 212 211 211 THR THR B . n 
B 1 213 CYS 213 212 212 CYS CYS B . n 
B 1 214 VAL 214 213 213 VAL VAL B . n 
B 1 215 SER 215 214 214 SER SER B . n 
B 1 216 SER 216 215 215 SER SER B . n 
B 1 217 THR 217 216 216 THR THR B . n 
B 1 218 ILE 218 217 217 ILE ILE B . n 
B 1 219 GLY 219 218 218 GLY GLY B . n 
B 1 220 GLN 220 219 219 GLN GLN B . n 
B 1 221 GLU 221 220 220 GLU GLU B . n 
B 1 222 ARG 222 221 221 ARG ARG B . n 
B 1 223 ILE 223 222 222 ILE ILE B . n 
B 1 224 THR 224 223 223 THR THR B . n 
B 1 225 SER 225 224 224 SER SER B . n 
B 1 226 ALA 226 225 225 ALA ALA B . n 
B 1 227 THR 227 226 226 THR THR B . n 
B 1 228 GLN 228 227 227 GLN GLN B . n 
B 1 229 TRP 229 228 228 TRP TRP B . n 
B 1 230 LEU 230 229 229 LEU LEU B . n 
B 1 231 ARG 231 230 230 ARG ARG B . n 
B 1 232 ALA 232 231 231 ALA ALA B . n 
B 1 233 ASN 233 232 232 ASN ASN B . n 
B 1 234 GLY 234 233 233 GLY GLY B . n 
B 1 235 LYS 235 234 234 LYS LYS B . n 
B 1 236 LYS 236 235 235 LYS LYS B . n 
B 1 237 GLY 237 236 236 GLY GLY B . n 
B 1 238 ILE 238 237 237 ILE ILE B . n 
B 1 239 ILE 239 238 238 ILE ILE B . n 
B 1 240 GLY 240 239 239 GLY GLY B . n 
B 1 241 GLU 241 240 240 GLU GLU B . n 
B 1 242 PHE 242 241 241 PHE PHE B . n 
B 1 243 ALA 243 242 242 ALA ALA B . n 
B 1 244 GLY 244 243 243 GLY GLY B . n 
B 1 245 GLY 245 244 244 GLY GLY B . n 
B 1 246 ALA 246 245 245 ALA ALA B . n 
B 1 247 ASN 247 246 246 ASN ASN B . n 
B 1 248 ASP 248 247 247 ASP ASP B . n 
B 1 249 VAL 249 248 248 VAL VAL B . n 
B 1 250 CYS 250 249 249 CYS CYS B . n 
B 1 251 GLU 251 250 250 GLU GLU B . n 
B 1 252 THR 252 251 251 THR THR B . n 
B 1 253 ALA 253 252 252 ALA ALA B . n 
B 1 254 ILE 254 253 253 ILE ILE B . n 
B 1 255 THR 255 254 254 THR THR B . n 
B 1 256 GLY 256 255 255 GLY GLY B . n 
B 1 257 MET 257 256 256 MET MET B . n 
B 1 258 LEU 258 257 257 LEU LEU B . n 
B 1 259 ASP 259 258 258 ASP ASP B . n 
B 1 260 TYR 260 259 259 TYR TYR B . n 
B 1 261 MET 261 260 260 MET MET B . n 
B 1 262 ALA 262 261 261 ALA ALA B . n 
B 1 263 GLN 263 262 262 GLN GLN B . n 
B 1 264 ASN 264 263 263 ASN ASN B . n 
B 1 265 THR 265 264 264 THR THR B . n 
B 1 266 ASP 266 265 265 ASP ASP B . n 
B 1 267 VAL 267 266 266 VAL VAL B . n 
B 1 268 TRP 268 267 267 TRP TRP B . n 
B 1 269 THR 269 268 268 THR THR B . n 
B 1 270 GLY 270 269 269 GLY GLY B . n 
B 1 271 ALA 271 270 270 ALA ALA B . n 
B 1 272 ILE 272 271 271 ILE ILE B . n 
B 1 273 TRP 273 272 272 TRP TRP B . n 
B 1 274 TRP 274 273 273 TRP TRP B . n 
B 1 275 ALA 275 274 274 ALA ALA B . n 
B 1 276 ALA 276 275 275 ALA ALA B . n 
B 1 277 GLY 277 276 276 GLY GLY B . n 
B 1 278 PRO 278 277 277 PRO PRO B . n 
B 1 279 TRP 279 278 278 TRP TRP B . n 
B 1 280 TRP 280 279 279 TRP TRP B . n 
B 1 281 GLY 281 280 280 GLY GLY B . n 
B 1 282 ASP 282 281 281 ASP ASP B . n 
B 1 283 TYR 283 282 282 TYR TYR B . n 
B 1 284 ILE 284 283 283 ILE ILE B . n 
B 1 285 PHE 285 284 284 PHE PHE B . n 
B 1 286 SER 286 285 285 SER SER B . n 
B 1 287 MET 287 286 286 MET MET B . n 
B 1 288 GLU 288 287 287 GLU GLU B . n 
B 1 289 PRO 289 288 288 PRO PRO B . n 
B 1 290 ASP 290 289 289 ASP ASP B . n 
B 1 291 ASN 291 290 290 ASN ASN B . n 
B 1 292 GLY 292 291 291 GLY GLY B . n 
B 1 293 ILE 293 292 292 ILE ILE B . n 
B 1 294 ALA 294 293 293 ALA ALA B . n 
B 1 295 TYR 295 294 294 TYR TYR B . n 
B 1 296 GLN 296 295 295 GLN GLN B . n 
B 1 297 GLN 297 296 296 GLN GLN B . n 
B 1 298 ILE 298 297 297 ILE ILE B . n 
B 1 299 LEU 299 298 298 LEU LEU B . n 
B 1 300 PRO 300 299 299 PRO PRO B . n 
B 1 301 ILE 301 300 300 ILE ILE B . n 
B 1 302 LEU 302 301 301 LEU LEU B . n 
B 1 303 THR 303 302 302 THR THR B . n 
B 1 304 PRO 304 303 303 PRO PRO B . n 
B 1 305 TYR 305 304 304 TYR TYR B . n 
B 1 306 LEU 306 305 305 LEU LEU 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 BGC 1 C BGC 1 C BGC 1 n 
C 2 BGC 2 C BGC 2 C BGC 2 n 
C 2 BGC 3 C BGC 3 C BGC 3 n 
C 2 BGC 4 C BGC 4 C BGC 4 n 
C 2 BGC 5 C BGC 5 C BGC 5 n 
D 2 BGC 1 D BGC 1 D BGC 1 n 
D 2 BGC 2 D BGC 2 D BGC 2 n 
D 2 BGC 3 D BGC 3 D BGC 3 n 
D 2 BGC 4 D BGC 4 D BGC 4 n 
D 2 BGC 5 D BGC 5 D BGC 5 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        BGC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   BGC 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 GOL 1   501  501  GOL GOL A . 
F 3 GOL 1   502  502  GOL GOL A . 
G 3 GOL 1   501  501  GOL GOL B . 
H 3 GOL 1   502  502  GOL GOL B . 
I 4 SO4 1   503  1    SO4 SO4 B . 
J 4 SO4 1   504  2    SO4 SO4 B . 
K 5 HOH 1   601  882  HOH HOH A . 
K 5 HOH 2   602  573  HOH HOH A . 
K 5 HOH 3   603  681  HOH HOH A . 
K 5 HOH 4   604  854  HOH HOH A . 
K 5 HOH 5   605  402  HOH HOH A . 
K 5 HOH 6   606  159  HOH HOH A . 
K 5 HOH 7   607  697  HOH HOH A . 
K 5 HOH 8   608  3167 HOH HOH A . 
K 5 HOH 9   609  536  HOH HOH A . 
K 5 HOH 10  610  1229 HOH HOH A . 
K 5 HOH 11  611  522  HOH HOH A . 
K 5 HOH 12  612  276  HOH HOH A . 
K 5 HOH 13  613  540  HOH HOH A . 
K 5 HOH 14  614  156  HOH HOH A . 
K 5 HOH 15  615  716  HOH HOH A . 
K 5 HOH 16  616  840  HOH HOH A . 
K 5 HOH 17  617  715  HOH HOH A . 
K 5 HOH 18  618  174  HOH HOH A . 
K 5 HOH 19  619  859  HOH HOH A . 
K 5 HOH 20  620  730  HOH HOH A . 
K 5 HOH 21  621  2560 HOH HOH A . 
K 5 HOH 22  622  574  HOH HOH A . 
K 5 HOH 23  623  79   HOH HOH A . 
K 5 HOH 24  624  901  HOH HOH A . 
K 5 HOH 25  625  569  HOH HOH A . 
K 5 HOH 26  626  151  HOH HOH A . 
K 5 HOH 27  627  593  HOH HOH A . 
K 5 HOH 28  628  915  HOH HOH A . 
K 5 HOH 29  629  286  HOH HOH A . 
K 5 HOH 30  630  620  HOH HOH A . 
K 5 HOH 31  631  116  HOH HOH A . 
K 5 HOH 32  632  75   HOH HOH A . 
K 5 HOH 33  633  487  HOH HOH A . 
K 5 HOH 34  634  457  HOH HOH A . 
K 5 HOH 35  635  701  HOH HOH A . 
K 5 HOH 36  636  258  HOH HOH A . 
K 5 HOH 37  637  82   HOH HOH A . 
K 5 HOH 38  638  550  HOH HOH A . 
K 5 HOH 39  639  170  HOH HOH A . 
K 5 HOH 40  640  881  HOH HOH A . 
K 5 HOH 41  641  765  HOH HOH A . 
K 5 HOH 42  642  277  HOH HOH A . 
K 5 HOH 43  643  304  HOH HOH A . 
K 5 HOH 44  644  640  HOH HOH A . 
K 5 HOH 45  645  743  HOH HOH A . 
K 5 HOH 46  646  885  HOH HOH A . 
K 5 HOH 47  647  85   HOH HOH A . 
K 5 HOH 48  648  1    HOH HOH A . 
K 5 HOH 49  649  833  HOH HOH A . 
K 5 HOH 50  650  166  HOH HOH A . 
K 5 HOH 51  651  92   HOH HOH A . 
K 5 HOH 52  652  690  HOH HOH A . 
K 5 HOH 53  653  2892 HOH HOH A . 
K 5 HOH 54  654  514  HOH HOH A . 
K 5 HOH 55  655  3177 HOH HOH A . 
K 5 HOH 56  656  748  HOH HOH A . 
K 5 HOH 57  657  125  HOH HOH A . 
K 5 HOH 58  658  559  HOH HOH A . 
K 5 HOH 59  659  250  HOH HOH A . 
K 5 HOH 60  660  3368 HOH HOH A . 
K 5 HOH 61  661  255  HOH HOH A . 
K 5 HOH 62  662  52   HOH HOH A . 
K 5 HOH 63  663  1256 HOH HOH A . 
K 5 HOH 64  664  412  HOH HOH A . 
K 5 HOH 65  665  883  HOH HOH A . 
K 5 HOH 66  666  831  HOH HOH A . 
K 5 HOH 67  667  900  HOH HOH A . 
K 5 HOH 68  668  134  HOH HOH A . 
K 5 HOH 69  669  439  HOH HOH A . 
K 5 HOH 70  670  267  HOH HOH A . 
K 5 HOH 71  671  533  HOH HOH A . 
K 5 HOH 72  672  1988 HOH HOH A . 
K 5 HOH 73  673  200  HOH HOH A . 
K 5 HOH 74  674  463  HOH HOH A . 
K 5 HOH 75  675  299  HOH HOH A . 
K 5 HOH 76  676  120  HOH HOH A . 
K 5 HOH 77  677  671  HOH HOH A . 
K 5 HOH 78  678  535  HOH HOH A . 
K 5 HOH 79  679  584  HOH HOH A . 
K 5 HOH 80  680  60   HOH HOH A . 
K 5 HOH 81  681  153  HOH HOH A . 
K 5 HOH 82  682  105  HOH HOH A . 
K 5 HOH 83  683  117  HOH HOH A . 
K 5 HOH 84  684  504  HOH HOH A . 
K 5 HOH 85  685  318  HOH HOH A . 
K 5 HOH 86  686  2553 HOH HOH A . 
K 5 HOH 87  687  345  HOH HOH A . 
K 5 HOH 88  688  65   HOH HOH A . 
K 5 HOH 89  689  307  HOH HOH A . 
K 5 HOH 90  690  735  HOH HOH A . 
K 5 HOH 91  691  1975 HOH HOH A . 
K 5 HOH 92  692  1269 HOH HOH A . 
K 5 HOH 93  693  611  HOH HOH A . 
K 5 HOH 94  694  219  HOH HOH A . 
K 5 HOH 95  695  692  HOH HOH A . 
K 5 HOH 96  696  509  HOH HOH A . 
K 5 HOH 97  697  731  HOH HOH A . 
K 5 HOH 98  698  178  HOH HOH A . 
K 5 HOH 99  699  2559 HOH HOH A . 
K 5 HOH 100 700  685  HOH HOH A . 
K 5 HOH 101 701  556  HOH HOH A . 
K 5 HOH 102 702  137  HOH HOH A . 
K 5 HOH 103 703  3028 HOH HOH A . 
K 5 HOH 104 704  187  HOH HOH A . 
K 5 HOH 105 705  430  HOH HOH A . 
K 5 HOH 106 706  227  HOH HOH A . 
K 5 HOH 107 707  343  HOH HOH A . 
K 5 HOH 108 708  110  HOH HOH A . 
K 5 HOH 109 709  22   HOH HOH A . 
K 5 HOH 110 710  32   HOH HOH A . 
K 5 HOH 111 711  67   HOH HOH A . 
K 5 HOH 112 712  8    HOH HOH A . 
K 5 HOH 113 713  214  HOH HOH A . 
K 5 HOH 114 714  444  HOH HOH A . 
K 5 HOH 115 715  344  HOH HOH A . 
K 5 HOH 116 716  452  HOH HOH A . 
K 5 HOH 117 717  399  HOH HOH A . 
K 5 HOH 118 718  165  HOH HOH A . 
K 5 HOH 119 719  63   HOH HOH A . 
K 5 HOH 120 720  659  HOH HOH A . 
K 5 HOH 121 721  203  HOH HOH A . 
K 5 HOH 122 722  2636 HOH HOH A . 
K 5 HOH 123 723  3045 HOH HOH A . 
K 5 HOH 124 724  346  HOH HOH A . 
K 5 HOH 125 725  779  HOH HOH A . 
K 5 HOH 126 726  586  HOH HOH A . 
K 5 HOH 127 727  597  HOH HOH A . 
K 5 HOH 128 728  172  HOH HOH A . 
K 5 HOH 129 729  567  HOH HOH A . 
K 5 HOH 130 730  537  HOH HOH A . 
K 5 HOH 131 731  302  HOH HOH A . 
K 5 HOH 132 732  206  HOH HOH A . 
K 5 HOH 133 733  572  HOH HOH A . 
K 5 HOH 134 734  542  HOH HOH A . 
K 5 HOH 135 735  144  HOH HOH A . 
K 5 HOH 136 736  14   HOH HOH A . 
K 5 HOH 137 737  80   HOH HOH A . 
K 5 HOH 138 738  427  HOH HOH A . 
K 5 HOH 139 739  184  HOH HOH A . 
K 5 HOH 140 740  435  HOH HOH A . 
K 5 HOH 141 741  86   HOH HOH A . 
K 5 HOH 142 742  217  HOH HOH A . 
K 5 HOH 143 743  11   HOH HOH A . 
K 5 HOH 144 744  314  HOH HOH A . 
K 5 HOH 145 745  17   HOH HOH A . 
K 5 HOH 146 746  160  HOH HOH A . 
K 5 HOH 147 747  477  HOH HOH A . 
K 5 HOH 148 748  662  HOH HOH A . 
K 5 HOH 149 749  16   HOH HOH A . 
K 5 HOH 150 750  2031 HOH HOH A . 
K 5 HOH 151 751  4    HOH HOH A . 
K 5 HOH 152 752  334  HOH HOH A . 
K 5 HOH 153 753  72   HOH HOH A . 
K 5 HOH 154 754  37   HOH HOH A . 
K 5 HOH 155 755  126  HOH HOH A . 
K 5 HOH 156 756  91   HOH HOH A . 
K 5 HOH 157 757  76   HOH HOH A . 
K 5 HOH 158 758  320  HOH HOH A . 
K 5 HOH 159 759  39   HOH HOH A . 
K 5 HOH 160 760  306  HOH HOH A . 
K 5 HOH 161 761  315  HOH HOH A . 
K 5 HOH 162 762  190  HOH HOH A . 
K 5 HOH 163 763  423  HOH HOH A . 
K 5 HOH 164 764  209  HOH HOH A . 
K 5 HOH 165 765  263  HOH HOH A . 
K 5 HOH 166 766  2945 HOH HOH A . 
K 5 HOH 167 767  711  HOH HOH A . 
K 5 HOH 168 768  213  HOH HOH A . 
K 5 HOH 169 769  106  HOH HOH A . 
K 5 HOH 170 770  47   HOH HOH A . 
K 5 HOH 171 771  222  HOH HOH A . 
K 5 HOH 172 772  62   HOH HOH A . 
K 5 HOH 173 773  389  HOH HOH A . 
K 5 HOH 174 774  273  HOH HOH A . 
K 5 HOH 175 775  88   HOH HOH A . 
K 5 HOH 176 776  46   HOH HOH A . 
K 5 HOH 177 777  152  HOH HOH A . 
K 5 HOH 178 778  467  HOH HOH A . 
K 5 HOH 179 779  57   HOH HOH A . 
K 5 HOH 180 780  469  HOH HOH A . 
K 5 HOH 181 781  38   HOH HOH A . 
K 5 HOH 182 782  90   HOH HOH A . 
K 5 HOH 183 783  830  HOH HOH A . 
K 5 HOH 184 784  283  HOH HOH A . 
K 5 HOH 185 785  127  HOH HOH A . 
K 5 HOH 186 786  388  HOH HOH A . 
K 5 HOH 187 787  354  HOH HOH A . 
K 5 HOH 188 788  512  HOH HOH A . 
K 5 HOH 189 789  396  HOH HOH A . 
K 5 HOH 190 790  136  HOH HOH A . 
K 5 HOH 191 791  236  HOH HOH A . 
K 5 HOH 192 792  53   HOH HOH A . 
K 5 HOH 193 793  56   HOH HOH A . 
K 5 HOH 194 794  673  HOH HOH A . 
K 5 HOH 195 795  245  HOH HOH A . 
K 5 HOH 196 796  323  HOH HOH A . 
K 5 HOH 197 797  544  HOH HOH A . 
K 5 HOH 198 798  175  HOH HOH A . 
K 5 HOH 199 799  541  HOH HOH A . 
K 5 HOH 200 800  10   HOH HOH A . 
K 5 HOH 201 801  35   HOH HOH A . 
K 5 HOH 202 802  3152 HOH HOH A . 
K 5 HOH 203 803  43   HOH HOH A . 
K 5 HOH 204 804  231  HOH HOH A . 
K 5 HOH 205 805  583  HOH HOH A . 
K 5 HOH 206 806  84   HOH HOH A . 
K 5 HOH 207 807  240  HOH HOH A . 
K 5 HOH 208 808  239  HOH HOH A . 
K 5 HOH 209 809  369  HOH HOH A . 
K 5 HOH 210 810  13   HOH HOH A . 
K 5 HOH 211 811  183  HOH HOH A . 
K 5 HOH 212 812  332  HOH HOH A . 
K 5 HOH 213 813  905  HOH HOH A . 
K 5 HOH 214 814  725  HOH HOH A . 
K 5 HOH 215 815  29   HOH HOH A . 
K 5 HOH 216 816  431  HOH HOH A . 
K 5 HOH 217 817  678  HOH HOH A . 
K 5 HOH 218 818  576  HOH HOH A . 
K 5 HOH 219 819  554  HOH HOH A . 
K 5 HOH 220 820  19   HOH HOH A . 
K 5 HOH 221 821  414  HOH HOH A . 
K 5 HOH 222 822  230  HOH HOH A . 
K 5 HOH 223 823  103  HOH HOH A . 
K 5 HOH 224 824  301  HOH HOH A . 
K 5 HOH 225 825  880  HOH HOH A . 
K 5 HOH 226 826  861  HOH HOH A . 
K 5 HOH 227 827  68   HOH HOH A . 
K 5 HOH 228 828  244  HOH HOH A . 
K 5 HOH 229 829  360  HOH HOH A . 
K 5 HOH 230 830  518  HOH HOH A . 
K 5 HOH 231 831  96   HOH HOH A . 
K 5 HOH 232 832  3288 HOH HOH A . 
K 5 HOH 233 833  440  HOH HOH A . 
K 5 HOH 234 834  476  HOH HOH A . 
K 5 HOH 235 835  699  HOH HOH A . 
K 5 HOH 236 836  819  HOH HOH A . 
K 5 HOH 237 837  107  HOH HOH A . 
K 5 HOH 238 838  234  HOH HOH A . 
K 5 HOH 239 839  235  HOH HOH A . 
K 5 HOH 240 840  713  HOH HOH A . 
K 5 HOH 241 841  164  HOH HOH A . 
K 5 HOH 242 842  1430 HOH HOH A . 
K 5 HOH 243 843  121  HOH HOH A . 
K 5 HOH 244 844  1115 HOH HOH A . 
K 5 HOH 245 845  1510 HOH HOH A . 
K 5 HOH 246 846  15   HOH HOH A . 
K 5 HOH 247 847  426  HOH HOH A . 
K 5 HOH 248 848  3394 HOH HOH A . 
K 5 HOH 249 849  453  HOH HOH A . 
K 5 HOH 250 850  357  HOH HOH A . 
K 5 HOH 251 851  313  HOH HOH A . 
K 5 HOH 252 852  689  HOH HOH A . 
K 5 HOH 253 853  525  HOH HOH A . 
K 5 HOH 254 854  634  HOH HOH A . 
K 5 HOH 255 855  192  HOH HOH A . 
K 5 HOH 256 856  563  HOH HOH A . 
K 5 HOH 257 857  128  HOH HOH A . 
K 5 HOH 258 858  377  HOH HOH A . 
K 5 HOH 259 859  734  HOH HOH A . 
K 5 HOH 260 860  395  HOH HOH A . 
K 5 HOH 261 861  316  HOH HOH A . 
K 5 HOH 262 862  154  HOH HOH A . 
K 5 HOH 263 863  272  HOH HOH A . 
K 5 HOH 264 864  275  HOH HOH A . 
K 5 HOH 265 865  417  HOH HOH A . 
K 5 HOH 266 866  523  HOH HOH A . 
K 5 HOH 267 867  94   HOH HOH A . 
K 5 HOH 268 868  866  HOH HOH A . 
K 5 HOH 269 869  66   HOH HOH A . 
K 5 HOH 270 870  521  HOH HOH A . 
K 5 HOH 271 871  639  HOH HOH A . 
K 5 HOH 272 872  201  HOH HOH A . 
K 5 HOH 273 873  499  HOH HOH A . 
K 5 HOH 274 874  367  HOH HOH A . 
K 5 HOH 275 875  752  HOH HOH A . 
K 5 HOH 276 876  350  HOH HOH A . 
K 5 HOH 277 877  687  HOH HOH A . 
K 5 HOH 278 878  1746 HOH HOH A . 
K 5 HOH 279 879  560  HOH HOH A . 
K 5 HOH 280 880  481  HOH HOH A . 
K 5 HOH 281 881  587  HOH HOH A . 
K 5 HOH 282 882  612  HOH HOH A . 
K 5 HOH 283 883  806  HOH HOH A . 
K 5 HOH 284 884  1476 HOH HOH A . 
K 5 HOH 285 885  693  HOH HOH A . 
K 5 HOH 286 886  167  HOH HOH A . 
K 5 HOH 287 887  493  HOH HOH A . 
K 5 HOH 288 888  887  HOH HOH A . 
K 5 HOH 289 889  786  HOH HOH A . 
K 5 HOH 290 890  1005 HOH HOH A . 
K 5 HOH 291 891  843  HOH HOH A . 
K 5 HOH 292 892  721  HOH HOH A . 
K 5 HOH 293 893  385  HOH HOH A . 
K 5 HOH 294 894  964  HOH HOH A . 
K 5 HOH 295 895  361  HOH HOH A . 
K 5 HOH 296 896  932  HOH HOH A . 
K 5 HOH 297 897  2552 HOH HOH A . 
K 5 HOH 298 898  447  HOH HOH A . 
K 5 HOH 299 899  390  HOH HOH A . 
K 5 HOH 300 900  517  HOH HOH A . 
K 5 HOH 301 901  339  HOH HOH A . 
K 5 HOH 302 902  527  HOH HOH A . 
K 5 HOH 303 903  296  HOH HOH A . 
K 5 HOH 304 904  3237 HOH HOH A . 
K 5 HOH 305 905  761  HOH HOH A . 
K 5 HOH 306 906  226  HOH HOH A . 
K 5 HOH 307 907  633  HOH HOH A . 
K 5 HOH 308 908  821  HOH HOH A . 
K 5 HOH 309 909  852  HOH HOH A . 
K 5 HOH 310 910  753  HOH HOH A . 
K 5 HOH 311 911  739  HOH HOH A . 
K 5 HOH 312 912  269  HOH HOH A . 
K 5 HOH 313 913  756  HOH HOH A . 
K 5 HOH 314 914  549  HOH HOH A . 
K 5 HOH 315 915  2985 HOH HOH A . 
K 5 HOH 316 916  3111 HOH HOH A . 
K 5 HOH 317 917  863  HOH HOH A . 
K 5 HOH 318 918  694  HOH HOH A . 
K 5 HOH 319 919  1031 HOH HOH A . 
K 5 HOH 320 920  409  HOH HOH A . 
K 5 HOH 321 921  1073 HOH HOH A . 
K 5 HOH 322 922  646  HOH HOH A . 
K 5 HOH 323 923  3203 HOH HOH A . 
K 5 HOH 324 924  312  HOH HOH A . 
K 5 HOH 325 925  746  HOH HOH A . 
K 5 HOH 326 926  773  HOH HOH A . 
K 5 HOH 327 927  2973 HOH HOH A . 
K 5 HOH 328 928  581  HOH HOH A . 
K 5 HOH 329 929  747  HOH HOH A . 
K 5 HOH 330 930  751  HOH HOH A . 
K 5 HOH 331 931  362  HOH HOH A . 
K 5 HOH 332 932  274  HOH HOH A . 
K 5 HOH 333 933  532  HOH HOH A . 
K 5 HOH 334 934  411  HOH HOH A . 
K 5 HOH 335 935  988  HOH HOH A . 
K 5 HOH 336 936  2879 HOH HOH A . 
K 5 HOH 337 937  1255 HOH HOH A . 
K 5 HOH 338 938  331  HOH HOH A . 
K 5 HOH 339 939  1368 HOH HOH A . 
K 5 HOH 340 940  1601 HOH HOH A . 
K 5 HOH 341 941  433  HOH HOH A . 
K 5 HOH 342 942  700  HOH HOH A . 
K 5 HOH 343 943  363  HOH HOH A . 
K 5 HOH 344 944  894  HOH HOH A . 
K 5 HOH 345 945  1015 HOH HOH A . 
K 5 HOH 346 946  718  HOH HOH A . 
K 5 HOH 347 947  570  HOH HOH A . 
K 5 HOH 348 948  482  HOH HOH A . 
K 5 HOH 349 949  825  HOH HOH A . 
K 5 HOH 350 950  1546 HOH HOH A . 
K 5 HOH 351 951  698  HOH HOH A . 
K 5 HOH 352 952  3012 HOH HOH A . 
K 5 HOH 353 953  2469 HOH HOH A . 
K 5 HOH 354 954  3232 HOH HOH A . 
K 5 HOH 355 955  474  HOH HOH A . 
K 5 HOH 356 956  804  HOH HOH A . 
K 5 HOH 357 957  652  HOH HOH A . 
K 5 HOH 358 958  319  HOH HOH A . 
K 5 HOH 359 959  2946 HOH HOH A . 
K 5 HOH 360 960  710  HOH HOH A . 
K 5 HOH 361 961  618  HOH HOH A . 
K 5 HOH 362 962  2582 HOH HOH A . 
K 5 HOH 363 963  353  HOH HOH A . 
K 5 HOH 364 964  740  HOH HOH A . 
K 5 HOH 365 965  2463 HOH HOH A . 
K 5 HOH 366 966  2769 HOH HOH A . 
K 5 HOH 367 967  672  HOH HOH A . 
K 5 HOH 368 968  808  HOH HOH A . 
K 5 HOH 369 969  519  HOH HOH A . 
K 5 HOH 370 970  3271 HOH HOH A . 
K 5 HOH 371 971  1314 HOH HOH A . 
K 5 HOH 372 972  802  HOH HOH A . 
K 5 HOH 373 973  770  HOH HOH A . 
K 5 HOH 374 974  3051 HOH HOH A . 
K 5 HOH 375 975  287  HOH HOH A . 
K 5 HOH 376 976  205  HOH HOH A . 
K 5 HOH 377 977  607  HOH HOH A . 
K 5 HOH 378 978  783  HOH HOH A . 
K 5 HOH 379 979  606  HOH HOH A . 
K 5 HOH 380 980  613  HOH HOH A . 
K 5 HOH 381 981  585  HOH HOH A . 
K 5 HOH 382 982  789  HOH HOH A . 
K 5 HOH 383 983  364  HOH HOH A . 
K 5 HOH 384 984  555  HOH HOH A . 
K 5 HOH 385 985  359  HOH HOH A . 
K 5 HOH 386 986  1223 HOH HOH A . 
K 5 HOH 387 987  750  HOH HOH A . 
K 5 HOH 388 988  657  HOH HOH A . 
K 5 HOH 389 989  498  HOH HOH A . 
K 5 HOH 390 990  123  HOH HOH A . 
K 5 HOH 391 991  2593 HOH HOH A . 
K 5 HOH 392 992  393  HOH HOH A . 
K 5 HOH 393 993  744  HOH HOH A . 
K 5 HOH 394 994  676  HOH HOH A . 
K 5 HOH 395 995  548  HOH HOH A . 
K 5 HOH 396 996  719  HOH HOH A . 
K 5 HOH 397 997  3022 HOH HOH A . 
K 5 HOH 398 998  268  HOH HOH A . 
K 5 HOH 399 999  202  HOH HOH A . 
K 5 HOH 400 1000 303  HOH HOH A . 
K 5 HOH 401 1001 631  HOH HOH A . 
K 5 HOH 402 1002 44   HOH HOH A . 
K 5 HOH 403 1003 459  HOH HOH A . 
K 5 HOH 404 1004 520  HOH HOH A . 
K 5 HOH 405 1005 380  HOH HOH A . 
K 5 HOH 406 1006 968  HOH HOH A . 
K 5 HOH 407 1007 293  HOH HOH A . 
K 5 HOH 408 1008 329  HOH HOH A . 
K 5 HOH 409 1009 545  HOH HOH A . 
K 5 HOH 410 1010 708  HOH HOH A . 
K 5 HOH 411 1011 717  HOH HOH A . 
K 5 HOH 412 1012 660  HOH HOH A . 
K 5 HOH 413 1013 428  HOH HOH A . 
K 5 HOH 414 1014 422  HOH HOH A . 
K 5 HOH 415 1015 497  HOH HOH A . 
K 5 HOH 416 1016 458  HOH HOH A . 
K 5 HOH 417 1017 232  HOH HOH A . 
K 5 HOH 418 1018 628  HOH HOH A . 
K 5 HOH 419 1019 599  HOH HOH A . 
K 5 HOH 420 1020 615  HOH HOH A . 
K 5 HOH 421 1021 455  HOH HOH A . 
K 5 HOH 422 1022 142  HOH HOH A . 
K 5 HOH 423 1023 456  HOH HOH A . 
K 5 HOH 424 1024 670  HOH HOH A . 
K 5 HOH 425 1025 850  HOH HOH A . 
K 5 HOH 426 1026 1520 HOH HOH A . 
K 5 HOH 427 1027 2570 HOH HOH A . 
K 5 HOH 428 1028 1239 HOH HOH A . 
K 5 HOH 429 1029 410  HOH HOH A . 
K 5 HOH 430 1030 621  HOH HOH A . 
K 5 HOH 431 1031 822  HOH HOH A . 
K 5 HOH 432 1032 407  HOH HOH A . 
K 5 HOH 433 1033 603  HOH HOH A . 
K 5 HOH 434 1034 97   HOH HOH A . 
K 5 HOH 435 1035 460  HOH HOH A . 
K 5 HOH 436 1036 403  HOH HOH A . 
K 5 HOH 437 1037 330  HOH HOH A . 
K 5 HOH 438 1038 479  HOH HOH A . 
K 5 HOH 439 1039 3131 HOH HOH A . 
K 5 HOH 440 1040 552  HOH HOH A . 
K 5 HOH 441 1041 2821 HOH HOH A . 
K 5 HOH 442 1042 505  HOH HOH A . 
K 5 HOH 443 1043 2564 HOH HOH A . 
K 5 HOH 444 1044 365  HOH HOH A . 
K 5 HOH 445 1045 468  HOH HOH A . 
K 5 HOH 446 1046 755  HOH HOH A . 
K 5 HOH 447 1047 337  HOH HOH A . 
K 5 HOH 448 1048 2970 HOH HOH A . 
K 5 HOH 449 1049 714  HOH HOH A . 
K 5 HOH 450 1050 594  HOH HOH A . 
K 5 HOH 451 1051 669  HOH HOH A . 
K 5 HOH 452 1052 841  HOH HOH A . 
K 5 HOH 453 1053 243  HOH HOH A . 
K 5 HOH 454 1054 473  HOH HOH A . 
K 5 HOH 455 1055 1150 HOH HOH A . 
K 5 HOH 456 1056 326  HOH HOH A . 
K 5 HOH 457 1057 760  HOH HOH A . 
K 5 HOH 458 1058 491  HOH HOH A . 
K 5 HOH 459 1059 485  HOH HOH A . 
K 5 HOH 460 1060 349  HOH HOH A . 
K 5 HOH 461 1061 1176 HOH HOH A . 
K 5 HOH 462 1062 1949 HOH HOH A . 
L 5 HOH 1   601  496  HOH HOH B . 
L 5 HOH 2   602  3199 HOH HOH B . 
L 5 HOH 3   603  856  HOH HOH B . 
L 5 HOH 4   604  684  HOH HOH B . 
L 5 HOH 5   605  680  HOH HOH B . 
L 5 HOH 6   606  513  HOH HOH B . 
L 5 HOH 7   607  262  HOH HOH B . 
L 5 HOH 8   608  109  HOH HOH B . 
L 5 HOH 9   609  180  HOH HOH B . 
L 5 HOH 10  610  592  HOH HOH B . 
L 5 HOH 11  611  2753 HOH HOH B . 
L 5 HOH 12  612  723  HOH HOH B . 
L 5 HOH 13  613  372  HOH HOH B . 
L 5 HOH 14  614  7    HOH HOH B . 
L 5 HOH 15  615  327  HOH HOH B . 
L 5 HOH 16  616  824  HOH HOH B . 
L 5 HOH 17  617  271  HOH HOH B . 
L 5 HOH 18  618  289  HOH HOH B . 
L 5 HOH 19  619  193  HOH HOH B . 
L 5 HOH 20  620  847  HOH HOH B . 
L 5 HOH 21  621  1233 HOH HOH B . 
L 5 HOH 22  622  93   HOH HOH B . 
L 5 HOH 23  623  950  HOH HOH B . 
L 5 HOH 24  624  465  HOH HOH B . 
L 5 HOH 25  625  502  HOH HOH B . 
L 5 HOH 26  626  1542 HOH HOH B . 
L 5 HOH 27  627  970  HOH HOH B . 
L 5 HOH 28  628  766  HOH HOH B . 
L 5 HOH 29  629  280  HOH HOH B . 
L 5 HOH 30  630  1088 HOH HOH B . 
L 5 HOH 31  631  451  HOH HOH B . 
L 5 HOH 32  632  736  HOH HOH B . 
L 5 HOH 33  633  1672 HOH HOH B . 
L 5 HOH 34  634  2877 HOH HOH B . 
L 5 HOH 35  635  342  HOH HOH B . 
L 5 HOH 36  636  34   HOH HOH B . 
L 5 HOH 37  637  194  HOH HOH B . 
L 5 HOH 38  638  297  HOH HOH B . 
L 5 HOH 39  639  102  HOH HOH B . 
L 5 HOH 40  640  826  HOH HOH B . 
L 5 HOH 41  641  188  HOH HOH B . 
L 5 HOH 42  642  890  HOH HOH B . 
L 5 HOH 43  643  254  HOH HOH B . 
L 5 HOH 44  644  529  HOH HOH B . 
L 5 HOH 45  645  703  HOH HOH B . 
L 5 HOH 46  646  588  HOH HOH B . 
L 5 HOH 47  647  83   HOH HOH B . 
L 5 HOH 48  648  437  HOH HOH B . 
L 5 HOH 49  649  392  HOH HOH B . 
L 5 HOH 50  650  124  HOH HOH B . 
L 5 HOH 51  651  617  HOH HOH B . 
L 5 HOH 52  652  279  HOH HOH B . 
L 5 HOH 53  653  28   HOH HOH B . 
L 5 HOH 54  654  71   HOH HOH B . 
L 5 HOH 55  655  59   HOH HOH B . 
L 5 HOH 56  656  23   HOH HOH B . 
L 5 HOH 57  657  641  HOH HOH B . 
L 5 HOH 58  658  25   HOH HOH B . 
L 5 HOH 59  659  5    HOH HOH B . 
L 5 HOH 60  660  374  HOH HOH B . 
L 5 HOH 61  661  328  HOH HOH B . 
L 5 HOH 62  662  185  HOH HOH B . 
L 5 HOH 63  663  181  HOH HOH B . 
L 5 HOH 64  664  702  HOH HOH B . 
L 5 HOH 65  665  3369 HOH HOH B . 
L 5 HOH 66  666  553  HOH HOH B . 
L 5 HOH 67  667  674  HOH HOH B . 
L 5 HOH 68  668  143  HOH HOH B . 
L 5 HOH 69  669  31   HOH HOH B . 
L 5 HOH 70  670  472  HOH HOH B . 
L 5 HOH 71  671  204  HOH HOH B . 
L 5 HOH 72  672  629  HOH HOH B . 
L 5 HOH 73  673  475  HOH HOH B . 
L 5 HOH 74  674  727  HOH HOH B . 
L 5 HOH 75  675  720  HOH HOH B . 
L 5 HOH 76  676  30   HOH HOH B . 
L 5 HOH 77  677  292  HOH HOH B . 
L 5 HOH 78  678  139  HOH HOH B . 
L 5 HOH 79  679  777  HOH HOH B . 
L 5 HOH 80  680  73   HOH HOH B . 
L 5 HOH 81  681  54   HOH HOH B . 
L 5 HOH 82  682  149  HOH HOH B . 
L 5 HOH 83  683  199  HOH HOH B . 
L 5 HOH 84  684  225  HOH HOH B . 
L 5 HOH 85  685  416  HOH HOH B . 
L 5 HOH 86  686  78   HOH HOH B . 
L 5 HOH 87  687  163  HOH HOH B . 
L 5 HOH 88  688  294  HOH HOH B . 
L 5 HOH 89  689  601  HOH HOH B . 
L 5 HOH 90  690  111  HOH HOH B . 
L 5 HOH 91  691  282  HOH HOH B . 
L 5 HOH 92  692  198  HOH HOH B . 
L 5 HOH 93  693  290  HOH HOH B . 
L 5 HOH 94  694  483  HOH HOH B . 
L 5 HOH 95  695  356  HOH HOH B . 
L 5 HOH 96  696  41   HOH HOH B . 
L 5 HOH 97  697  904  HOH HOH B . 
L 5 HOH 98  698  260  HOH HOH B . 
L 5 HOH 99  699  118  HOH HOH B . 
L 5 HOH 100 700  605  HOH HOH B . 
L 5 HOH 101 701  543  HOH HOH B . 
L 5 HOH 102 702  879  HOH HOH B . 
L 5 HOH 103 703  9    HOH HOH B . 
L 5 HOH 104 704  251  HOH HOH B . 
L 5 HOH 105 705  406  HOH HOH B . 
L 5 HOH 106 706  95   HOH HOH B . 
L 5 HOH 107 707  135  HOH HOH B . 
L 5 HOH 108 708  534  HOH HOH B . 
L 5 HOH 109 709  488  HOH HOH B . 
L 5 HOH 110 710  147  HOH HOH B . 
L 5 HOH 111 711  873  HOH HOH B . 
L 5 HOH 112 712  132  HOH HOH B . 
L 5 HOH 113 713  445  HOH HOH B . 
L 5 HOH 114 714  148  HOH HOH B . 
L 5 HOH 115 715  20   HOH HOH B . 
L 5 HOH 116 716  352  HOH HOH B . 
L 5 HOH 117 717  101  HOH HOH B . 
L 5 HOH 118 718  40   HOH HOH B . 
L 5 HOH 119 719  466  HOH HOH B . 
L 5 HOH 120 720  104  HOH HOH B . 
L 5 HOH 121 721  281  HOH HOH B . 
L 5 HOH 122 722  305  HOH HOH B . 
L 5 HOH 123 723  324  HOH HOH B . 
L 5 HOH 124 724  347  HOH HOH B . 
L 5 HOH 125 725  247  HOH HOH B . 
L 5 HOH 126 726  249  HOH HOH B . 
L 5 HOH 127 727  220  HOH HOH B . 
L 5 HOH 128 728  322  HOH HOH B . 
L 5 HOH 129 729  565  HOH HOH B . 
L 5 HOH 130 730  511  HOH HOH B . 
L 5 HOH 131 731  33   HOH HOH B . 
L 5 HOH 132 732  484  HOH HOH B . 
L 5 HOH 133 733  382  HOH HOH B . 
L 5 HOH 134 734  24   HOH HOH B . 
L 5 HOH 135 735  626  HOH HOH B . 
L 5 HOH 136 736  791  HOH HOH B . 
L 5 HOH 137 737  683  HOH HOH B . 
L 5 HOH 138 738  89   HOH HOH B . 
L 5 HOH 139 739  265  HOH HOH B . 
L 5 HOH 140 740  241  HOH HOH B . 
L 5 HOH 141 741  288  HOH HOH B . 
L 5 HOH 142 742  130  HOH HOH B . 
L 5 HOH 143 743  391  HOH HOH B . 
L 5 HOH 144 744  98   HOH HOH B . 
L 5 HOH 145 745  638  HOH HOH B . 
L 5 HOH 146 746  448  HOH HOH B . 
L 5 HOH 147 747  338  HOH HOH B . 
L 5 HOH 148 748  196  HOH HOH B . 
L 5 HOH 149 749  216  HOH HOH B . 
L 5 HOH 150 750  516  HOH HOH B . 
L 5 HOH 151 751  171  HOH HOH B . 
L 5 HOH 152 752  26   HOH HOH B . 
L 5 HOH 153 753  650  HOH HOH B . 
L 5 HOH 154 754  218  HOH HOH B . 
L 5 HOH 155 755  113  HOH HOH B . 
L 5 HOH 156 756  228  HOH HOH B . 
L 5 HOH 157 757  425  HOH HOH B . 
L 5 HOH 158 758  441  HOH HOH B . 
L 5 HOH 159 759  489  HOH HOH B . 
L 5 HOH 160 760  737  HOH HOH B . 
L 5 HOH 161 761  420  HOH HOH B . 
L 5 HOH 162 762  157  HOH HOH B . 
L 5 HOH 163 763  115  HOH HOH B . 
L 5 HOH 164 764  270  HOH HOH B . 
L 5 HOH 165 765  812  HOH HOH B . 
L 5 HOH 166 766  528  HOH HOH B . 
L 5 HOH 167 767  589  HOH HOH B . 
L 5 HOH 168 768  432  HOH HOH B . 
L 5 HOH 169 769  27   HOH HOH B . 
L 5 HOH 170 770  51   HOH HOH B . 
L 5 HOH 171 771  155  HOH HOH B . 
L 5 HOH 172 772  295  HOH HOH B . 
L 5 HOH 173 773  839  HOH HOH B . 
L 5 HOH 174 774  179  HOH HOH B . 
L 5 HOH 175 775  169  HOH HOH B . 
L 5 HOH 176 776  74   HOH HOH B . 
L 5 HOH 177 777  224  HOH HOH B . 
L 5 HOH 178 778  131  HOH HOH B . 
L 5 HOH 179 779  138  HOH HOH B . 
L 5 HOH 180 780  539  HOH HOH B . 
L 5 HOH 181 781  49   HOH HOH B . 
L 5 HOH 182 782  252  HOH HOH B . 
L 5 HOH 183 783  733  HOH HOH B . 
L 5 HOH 184 784  816  HOH HOH B . 
L 5 HOH 185 785  266  HOH HOH B . 
L 5 HOH 186 786  3158 HOH HOH B . 
L 5 HOH 187 787  119  HOH HOH B . 
L 5 HOH 188 788  405  HOH HOH B . 
L 5 HOH 189 789  649  HOH HOH B . 
L 5 HOH 190 790  1726 HOH HOH B . 
L 5 HOH 191 791  12   HOH HOH B . 
L 5 HOH 192 792  386  HOH HOH B . 
L 5 HOH 193 793  221  HOH HOH B . 
L 5 HOH 194 794  55   HOH HOH B . 
L 5 HOH 195 795  379  HOH HOH B . 
L 5 HOH 196 796  77   HOH HOH B . 
L 5 HOH 197 797  3    HOH HOH B . 
L 5 HOH 198 798  1038 HOH HOH B . 
L 5 HOH 199 799  298  HOH HOH B . 
L 5 HOH 200 800  2    HOH HOH B . 
L 5 HOH 201 801  291  HOH HOH B . 
L 5 HOH 202 802  186  HOH HOH B . 
L 5 HOH 203 803  983  HOH HOH B . 
L 5 HOH 204 804  168  HOH HOH B . 
L 5 HOH 205 805  788  HOH HOH B . 
L 5 HOH 206 806  368  HOH HOH B . 
L 5 HOH 207 807  557  HOH HOH B . 
L 5 HOH 208 808  176  HOH HOH B . 
L 5 HOH 209 809  158  HOH HOH B . 
L 5 HOH 210 810  173  HOH HOH B . 
L 5 HOH 211 811  141  HOH HOH B . 
L 5 HOH 212 812  21   HOH HOH B . 
L 5 HOH 213 813  162  HOH HOH B . 
L 5 HOH 214 814  308  HOH HOH B . 
L 5 HOH 215 815  807  HOH HOH B . 
L 5 HOH 216 816  45   HOH HOH B . 
L 5 HOH 217 817  207  HOH HOH B . 
L 5 HOH 218 818  2846 HOH HOH B . 
L 5 HOH 219 819  99   HOH HOH B . 
L 5 HOH 220 820  591  HOH HOH B . 
L 5 HOH 221 821  112  HOH HOH B . 
L 5 HOH 222 822  61   HOH HOH B . 
L 5 HOH 223 823  150  HOH HOH B . 
L 5 HOH 224 824  122  HOH HOH B . 
L 5 HOH 225 825  471  HOH HOH B . 
L 5 HOH 226 826  851  HOH HOH B . 
L 5 HOH 227 827  256  HOH HOH B . 
L 5 HOH 228 828  50   HOH HOH B . 
L 5 HOH 229 829  507  HOH HOH B . 
L 5 HOH 230 830  397  HOH HOH B . 
L 5 HOH 231 831  325  HOH HOH B . 
L 5 HOH 232 832  264  HOH HOH B . 
L 5 HOH 233 833  609  HOH HOH B . 
L 5 HOH 234 834  161  HOH HOH B . 
L 5 HOH 235 835  309  HOH HOH B . 
L 5 HOH 236 836  242  HOH HOH B . 
L 5 HOH 237 837  558  HOH HOH B . 
L 5 HOH 238 838  515  HOH HOH B . 
L 5 HOH 239 839  18   HOH HOH B . 
L 5 HOH 240 840  2596 HOH HOH B . 
L 5 HOH 241 841  470  HOH HOH B . 
L 5 HOH 242 842  177  HOH HOH B . 
L 5 HOH 243 843  462  HOH HOH B . 
L 5 HOH 244 844  182  HOH HOH B . 
L 5 HOH 245 845  197  HOH HOH B . 
L 5 HOH 246 846  284  HOH HOH B . 
L 5 HOH 247 847  36   HOH HOH B . 
L 5 HOH 248 848  358  HOH HOH B . 
L 5 HOH 249 849  503  HOH HOH B . 
L 5 HOH 250 850  58   HOH HOH B . 
L 5 HOH 251 851  920  HOH HOH B . 
L 5 HOH 252 852  644  HOH HOH B . 
L 5 HOH 253 853  478  HOH HOH B . 
L 5 HOH 254 854  500  HOH HOH B . 
L 5 HOH 255 855  133  HOH HOH B . 
L 5 HOH 256 856  6    HOH HOH B . 
L 5 HOH 257 857  872  HOH HOH B . 
L 5 HOH 258 858  643  HOH HOH B . 
L 5 HOH 259 859  741  HOH HOH B . 
L 5 HOH 260 860  69   HOH HOH B . 
L 5 HOH 261 861  100  HOH HOH B . 
L 5 HOH 262 862  259  HOH HOH B . 
L 5 HOH 263 863  1505 HOH HOH B . 
L 5 HOH 264 864  229  HOH HOH B . 
L 5 HOH 265 865  108  HOH HOH B . 
L 5 HOH 266 866  378  HOH HOH B . 
L 5 HOH 267 867  384  HOH HOH B . 
L 5 HOH 268 868  64   HOH HOH B . 
L 5 HOH 269 869  598  HOH HOH B . 
L 5 HOH 270 870  793  HOH HOH B . 
L 5 HOH 271 871  772  HOH HOH B . 
L 5 HOH 272 872  745  HOH HOH B . 
L 5 HOH 273 873  413  HOH HOH B . 
L 5 HOH 274 874  732  HOH HOH B . 
L 5 HOH 275 875  749  HOH HOH B . 
L 5 HOH 276 876  888  HOH HOH B . 
L 5 HOH 277 877  742  HOH HOH B . 
L 5 HOH 278 878  3138 HOH HOH B . 
L 5 HOH 279 879  278  HOH HOH B . 
L 5 HOH 280 880  1244 HOH HOH B . 
L 5 HOH 281 881  853  HOH HOH B . 
L 5 HOH 282 882  195  HOH HOH B . 
L 5 HOH 283 883  145  HOH HOH B . 
L 5 HOH 284 884  341  HOH HOH B . 
L 5 HOH 285 885  81   HOH HOH B . 
L 5 HOH 286 886  87   HOH HOH B . 
L 5 HOH 287 887  191  HOH HOH B . 
L 5 HOH 288 888  582  HOH HOH B . 
L 5 HOH 289 889  310  HOH HOH B . 
L 5 HOH 290 890  869  HOH HOH B . 
L 5 HOH 291 891  695  HOH HOH B . 
L 5 HOH 292 892  418  HOH HOH B . 
L 5 HOH 293 893  375  HOH HOH B . 
L 5 HOH 294 894  246  HOH HOH B . 
L 5 HOH 295 895  1025 HOH HOH B . 
L 5 HOH 296 896  424  HOH HOH B . 
L 5 HOH 297 897  48   HOH HOH B . 
L 5 HOH 298 898  738  HOH HOH B . 
L 5 HOH 299 899  248  HOH HOH B . 
L 5 HOH 300 900  623  HOH HOH B . 
L 5 HOH 301 901  42   HOH HOH B . 
L 5 HOH 302 902  600  HOH HOH B . 
L 5 HOH 303 903  884  HOH HOH B . 
L 5 HOH 304 904  855  HOH HOH B . 
L 5 HOH 305 905  114  HOH HOH B . 
L 5 HOH 306 906  616  HOH HOH B . 
L 5 HOH 307 907  2561 HOH HOH B . 
L 5 HOH 308 908  2612 HOH HOH B . 
L 5 HOH 309 909  688  HOH HOH B . 
L 5 HOH 310 910  335  HOH HOH B . 
L 5 HOH 311 911  2094 HOH HOH B . 
L 5 HOH 312 912  897  HOH HOH B . 
L 5 HOH 313 913  614  HOH HOH B . 
L 5 HOH 314 914  705  HOH HOH B . 
L 5 HOH 315 915  381  HOH HOH B . 
L 5 HOH 316 916  208  HOH HOH B . 
L 5 HOH 317 917  774  HOH HOH B . 
L 5 HOH 318 918  846  HOH HOH B . 
L 5 HOH 319 919  868  HOH HOH B . 
L 5 HOH 320 920  682  HOH HOH B . 
L 5 HOH 321 921  2791 HOH HOH B . 
L 5 HOH 322 922  2836 HOH HOH B . 
L 5 HOH 323 923  129  HOH HOH B . 
L 5 HOH 324 924  661  HOH HOH B . 
L 5 HOH 325 925  764  HOH HOH B . 
L 5 HOH 326 926  237  HOH HOH B . 
L 5 HOH 327 927  823  HOH HOH B . 
L 5 HOH 328 928  579  HOH HOH B . 
L 5 HOH 329 929  321  HOH HOH B . 
L 5 HOH 330 930  797  HOH HOH B . 
L 5 HOH 331 931  394  HOH HOH B . 
L 5 HOH 332 932  630  HOH HOH B . 
L 5 HOH 333 933  1084 HOH HOH B . 
L 5 HOH 334 934  210  HOH HOH B . 
L 5 HOH 335 935  757  HOH HOH B . 
L 5 HOH 336 936  862  HOH HOH B . 
L 5 HOH 337 937  707  HOH HOH B . 
L 5 HOH 338 938  1723 HOH HOH B . 
L 5 HOH 339 939  400  HOH HOH B . 
L 5 HOH 340 940  300  HOH HOH B . 
L 5 HOH 341 941  2102 HOH HOH B . 
L 5 HOH 342 942  317  HOH HOH B . 
L 5 HOH 343 943  526  HOH HOH B . 
L 5 HOH 344 944  551  HOH HOH B . 
L 5 HOH 345 945  443  HOH HOH B . 
L 5 HOH 346 946  461  HOH HOH B . 
L 5 HOH 347 947  792  HOH HOH B . 
L 5 HOH 348 948  658  HOH HOH B . 
L 5 HOH 349 949  627  HOH HOH B . 
L 5 HOH 350 950  524  HOH HOH B . 
L 5 HOH 351 951  366  HOH HOH B . 
L 5 HOH 352 952  492  HOH HOH B . 
L 5 HOH 353 953  810  HOH HOH B . 
L 5 HOH 354 954  415  HOH HOH B . 
L 5 HOH 355 955  870  HOH HOH B . 
L 5 HOH 356 956  564  HOH HOH B . 
L 5 HOH 357 957  2009 HOH HOH B . 
L 5 HOH 358 958  340  HOH HOH B . 
L 5 HOH 359 959  215  HOH HOH B . 
L 5 HOH 360 960  844  HOH HOH B . 
L 5 HOH 361 961  2574 HOH HOH B . 
L 5 HOH 362 962  383  HOH HOH B . 
L 5 HOH 363 963  578  HOH HOH B . 
L 5 HOH 364 964  442  HOH HOH B . 
L 5 HOH 365 965  3042 HOH HOH B . 
L 5 HOH 366 966  376  HOH HOH B . 
L 5 HOH 367 967  2426 HOH HOH B . 
L 5 HOH 368 968  336  HOH HOH B . 
L 5 HOH 369 969  590  HOH HOH B . 
L 5 HOH 370 970  140  HOH HOH B . 
L 5 HOH 371 971  706  HOH HOH B . 
L 5 HOH 372 972  450  HOH HOH B . 
L 5 HOH 373 973  913  HOH HOH B . 
L 5 HOH 374 974  801  HOH HOH B . 
L 5 HOH 375 975  547  HOH HOH B . 
L 5 HOH 376 976  679  HOH HOH B . 
L 5 HOH 377 977  762  HOH HOH B . 
L 5 HOH 378 978  876  HOH HOH B . 
L 5 HOH 379 979  974  HOH HOH B . 
L 5 HOH 380 980  937  HOH HOH B . 
L 5 HOH 381 981  404  HOH HOH B . 
L 5 HOH 382 982  561  HOH HOH B . 
L 5 HOH 383 983  1100 HOH HOH B . 
L 5 HOH 384 984  408  HOH HOH B . 
L 5 HOH 385 985  2563 HOH HOH B . 
L 5 HOH 386 986  686  HOH HOH B . 
L 5 HOH 387 987  486  HOH HOH B . 
L 5 HOH 388 988  663  HOH HOH B . 
L 5 HOH 389 989  438  HOH HOH B . 
L 5 HOH 390 990  980  HOH HOH B . 
L 5 HOH 391 991  577  HOH HOH B . 
L 5 HOH 392 992  929  HOH HOH B . 
L 5 HOH 393 993  253  HOH HOH B . 
L 5 HOH 394 994  419  HOH HOH B . 
L 5 HOH 395 995  3181 HOH HOH B . 
L 5 HOH 396 996  1802 HOH HOH B . 
L 5 HOH 397 997  373  HOH HOH B . 
L 5 HOH 398 998  70   HOH HOH B . 
L 5 HOH 399 999  333  HOH HOH B . 
L 5 HOH 400 1000 769  HOH HOH B . 
L 5 HOH 401 1001 508  HOH HOH B . 
L 5 HOH 402 1002 546  HOH HOH B . 
L 5 HOH 403 1003 434  HOH HOH B . 
L 5 HOH 404 1004 906  HOH HOH B . 
L 5 HOH 405 1005 449  HOH HOH B . 
L 5 HOH 406 1006 763  HOH HOH B . 
L 5 HOH 407 1007 632  HOH HOH B . 
L 5 HOH 408 1008 370  HOH HOH B . 
L 5 HOH 409 1009 729  HOH HOH B . 
L 5 HOH 410 1010 580  HOH HOH B . 
L 5 HOH 411 1011 421  HOH HOH B . 
L 5 HOH 412 1012 619  HOH HOH B . 
L 5 HOH 413 1013 811  HOH HOH B . 
L 5 HOH 414 1014 398  HOH HOH B . 
L 5 HOH 415 1015 2854 HOH HOH B . 
L 5 HOH 416 1016 355  HOH HOH B . 
L 5 HOH 417 1017 608  HOH HOH B . 
L 5 HOH 418 1018 726  HOH HOH B . 
L 5 HOH 419 1019 401  HOH HOH B . 
L 5 HOH 420 1020 1537 HOH HOH B . 
L 5 HOH 421 1021 886  HOH HOH B . 
L 5 HOH 422 1022 1637 HOH HOH B . 
L 5 HOH 423 1023 637  HOH HOH B . 
L 5 HOH 424 1024 596  HOH HOH B . 
L 5 HOH 425 1025 538  HOH HOH B . 
L 5 HOH 426 1026 212  HOH HOH B . 
L 5 HOH 427 1027 1983 HOH HOH B . 
L 5 HOH 428 1028 575  HOH HOH B . 
L 5 HOH 429 1029 889  HOH HOH B . 
L 5 HOH 430 1030 604  HOH HOH B . 
L 5 HOH 431 1031 1891 HOH HOH B . 
L 5 HOH 432 1032 648  HOH HOH B . 
L 5 HOH 433 1033 454  HOH HOH B . 
L 5 HOH 434 1034 562  HOH HOH B . 
L 5 HOH 435 1035 790  HOH HOH B . 
L 5 HOH 436 1036 1213 HOH HOH B . 
L 5 HOH 437 1037 189  HOH HOH B . 
L 5 HOH 438 1038 480  HOH HOH B . 
L 5 HOH 439 1039 795  HOH HOH B . 
L 5 HOH 440 1040 571  HOH HOH B . 
L 5 HOH 441 1041 311  HOH HOH B . 
L 5 HOH 442 1042 566  HOH HOH B . 
L 5 HOH 443 1043 595  HOH HOH B . 
L 5 HOH 444 1044 655  HOH HOH B . 
L 5 HOH 445 1045 348  HOH HOH B . 
L 5 HOH 446 1046 238  HOH HOH B . 
L 5 HOH 447 1047 2914 HOH HOH B . 
L 5 HOH 448 1048 506  HOH HOH B . 
L 5 HOH 449 1049 675  HOH HOH B . 
L 5 HOH 450 1050 3382 HOH HOH B . 
L 5 HOH 451 1051 351  HOH HOH B . 
L 5 HOH 452 1052 787  HOH HOH B . 
L 5 HOH 453 1053 1062 HOH HOH B . 
L 5 HOH 454 1054 223  HOH HOH B . 
L 5 HOH 455 1055 691  HOH HOH B . 
L 5 HOH 456 1056 645  HOH HOH B . 
L 5 HOH 457 1057 257  HOH HOH B . 
L 5 HOH 458 1058 1168 HOH HOH B . 
L 5 HOH 459 1059 233  HOH HOH B . 
L 5 HOH 460 1060 636  HOH HOH B . 
L 5 HOH 461 1061 3218 HOH HOH B . 
L 5 HOH 462 1062 464  HOH HOH B . 
L 5 HOH 463 1063 1283 HOH HOH B . 
L 5 HOH 464 1064 3006 HOH HOH B . 
L 5 HOH 465 1065 211  HOH HOH B . 
L 5 HOH 466 1066 146  HOH HOH B . 
L 5 HOH 467 1067 531  HOH HOH B . 
L 5 HOH 468 1068 902  HOH HOH B . 
L 5 HOH 469 1069 387  HOH HOH B . 
L 5 HOH 470 1070 625  HOH HOH B . 
L 5 HOH 471 1071 849  HOH HOH B . 
L 5 HOH 472 1072 261  HOH HOH B . 
L 5 HOH 473 1073 510  HOH HOH B . 
L 5 HOH 474 1074 530  HOH HOH B . 
L 5 HOH 475 1075 285  HOH HOH B . 
L 5 HOH 476 1076 858  HOH HOH B . 
L 5 HOH 477 1077 495  HOH HOH B . 
L 5 HOH 478 1078 666  HOH HOH B . 
L 5 HOH 479 1079 3032 HOH HOH B . 
L 5 HOH 480 1080 768  HOH HOH B . 
L 5 HOH 481 1081 2731 HOH HOH B . 
L 5 HOH 482 1082 490  HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21_5207 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? 20210323  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? 20210323  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? 2.8.3     4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F0M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.390 
_cell.length_a_esd                 ? 
_cell.length_b                     85.420 
_cell.length_b_esd                 ? 
_cell.length_c                     89.310 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9F0M 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9F0M 
_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             2.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.5 
_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              6.0 
_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    
;Reservoir solution: 0.1 M Tris pH 6.0, 1.3 M ammonium sulfate Drop: 2 ul of 465 uM protein mixed with 2 ul of reservoir solution, 0.2 ul cellohexaose 5 mM and 0.2 ul microseeds.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-04-02 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Si 111' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.978565 
_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                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978565 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F0M 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.63 
_reflns.d_resolution_low                               48.01 
_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                                     73367 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.59 
_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                                0.11800000000000001 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9990000000000001 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.113 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_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 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.63 1.67  ? 2.64  ? ? ? ? 5167 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.021                ? ? 1  1 0.8590000000000001 ? ? 95.8 ? 0.981 ? 
? ? ? ? ? ? ? ? 
1.67 1.72  ? 3.47  ? ? ? ? 5225 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.8759999999999999   ? ? 2  1 0.927              ? ? 100  ? 
0.8440000000000001   ? ? ? ? ? ? ? ? ? 
1.72 1.77  ? 4.45  ? ? ? ? 5114 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.7340000000000001   ? ? 3  1 0.95               ? ? 100  ? 0.706 ? 
? ? ? ? ? ? ? ? 
1.77 1.82  ? 5.75  ? ? ? ? 4985 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.594                ? ? 4  1 0.9690000000000001 ? ? 100  ? 
0.5720000000000001   ? ? ? ? ? ? ? ? ? 
1.82 1.88  ? 6.97  ? ? ? ? 4765 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.512                ? ? 5  1 0.977              ? ? 100  ? 
0.49200000000000005  ? ? ? ? ? ? ? ? ? 
1.88 1.95  ? 8.60  ? ? ? ? 4667 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.523                ? ? 6  1 0.9840000000000001 ? ? 100  ? 0.502 ? 
? ? ? ? ? ? ? ? 
1.95 2.02  ? 11.82 ? ? ? ? 4506 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.317                ? ? 7  1 0.99               ? ? 100  ? 0.304 ? 
? ? ? ? ? ? ? ? 
2.02 2.1   ? 14.67 ? ? ? ? 4327 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.27699999999999997  ? ? 8  1 0.9940000000000001 ? ? 100  ? 0.266 ? 
? ? ? ? ? ? ? ? 
2.10 2.2   ? 17.35 ? ? ? ? 4156 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.212                ? ? 9  1 0.995              ? ? 100  ? 0.204 ? 
? ? ? ? ? ? ? ? 
2.20 2.3   ? 19.37 ? ? ? ? 4028 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.20800000000000002  ? ? 10 1 0.995              ? ? 100  ? 0.201 ? 
? ? ? ? ? ? ? ? 
2.30 2.43  ? 22.01 ? ? ? ? 3767 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.155                ? ? 11 1 0.997              ? ? 100  ? 0.15 ? ? 
? ? ? ? ? ? ? 
2.43 2.58  ? 24.2  ? ? ? ? 3602 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.136                ? ? 12 1 0.997              ? ? 100  ? 0.131 ? 
? ? ? ? ? ? ? ? 
2.58 2.75  ? 27.84 ? ? ? ? 3395 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.114                ? ? 13 1 0.997              ? ? 100  ? 0.109 ? 
? ? ? ? ? ? ? ? 
2.75 2.97  ? 32.40 ? ? ? ? 3163 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.091                ? ? 14 1 0.998              ? ? 100  ? 0.087 ? 
? ? ? ? ? ? ? ? 
2.97 3.26  ? 44.47 ? ? ? ? 2927 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.073                ? ? 15 1 0.9990000000000001 ? ? 100  ? 0.071 ? 
? ? ? ? ? ? ? ? 
3.26 3.64  ? 48.73 ? ? ? ? 2668 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.062                ? ? 16 1 0.9990000000000001 ? ? 100  ? 0.06 ? ? 
? ? ? ? ? ? ? 
3.64 4.21  ? 48.73 ? ? ? ? 2359 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.052000000000000005 ? ? 17 1 0.9990000000000001 ? ? 100  ? 0.05 ? ? 
? ? ? ? ? ? ? 
4.21 5.15  ? 49.71 ? ? ? ? 2023 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.048                ? ? 18 1 0.9990000000000001 ? ? 100  ? 0.046 ? 
? ? ? ? ? ? ? ? 
5.15 7.29  ? 46.87 ? ? ? ? 1594 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.05                 ? ? 19 1 0.9990000000000001 ? ? 100  ? 0.048 ? 
? ? ? ? ? ? ? ? 
7.29 48.01 ? 52.51 ? ? ? ? 929  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.042                ? ? 20 1 0.9990000000000001 ? ? 99.5 ? 
0.040999999999999995 ? ? ? ? ? ? ? ? ? 
# 
_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                               19.18 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  
;TLS were used in refinement

TLS DETAILS.
NUMBER OF TLS GROUPS: 15    
ORIGIN: CENTER OF MASS
TLS GROUP : 1     
SELECTION: chain 'A' and (resid 2 through 20 )
ORIGIN FOR THE GROUP (A):  -4.6308  16.5019  -9.7772
T TENSOR                                            
T11:   0.1927 T22:   0.1642                       
T33:   0.2009 T12:  -0.0028                       
T13:  -0.0230 T23:  -0.0098                       
L TENSOR                                            
L11:   0.0558 L22:   0.1118                       
L33:   0.3906 L12:   0.0761                       
L13:   0.1538 L23:   0.2250                       
S TENSOR                                            
S11:   0.0676 S12:  -0.0957 S13:  -0.1023         
S21:   0.0052 S22:  -0.0523 S23:  -0.0398         
S31:   0.1943 S32:   0.0629 S33:   0.0001         
TLS GROUP : 2     
SELECTION: chain 'A' and (resid 21 through 84 )
ORIGIN FOR THE GROUP (A):  -7.1860  16.9285   0.6502
T TENSOR                                            
T11:   0.2073 T22:   0.1618                       
T33:   0.1817 T12:  -0.0039                       
T13:  -0.0150 T23:   0.0314                       
L TENSOR                                            
L11:   0.3000 L22:   0.6249                       
L33:   0.6451 L12:   0.3691                       
L13:  -0.0577 L23:   0.2460                       
S TENSOR                                            
S11:   0.0705 S12:  -0.0710 S13:  -0.0979         
S21:   0.2006 S22:  -0.0545 S23:  -0.0257         
S31:   0.2029 S32:  -0.0568 S33:   0.0002         
TLS GROUP : 3     
SELECTION: chain 'A' and (resid 85 through 185 )
ORIGIN FOR THE GROUP (A):  -9.8970  30.8504  -9.2245
T TENSOR                                            
T11:   0.1288 T22:   0.1286                       
T33:   0.1582 T12:   0.0064                       
T13:  -0.0053 T23:  -0.0041                       
L TENSOR                                            
L11:   0.5347 L22:   0.5469                       
L33:   0.4977 L12:   0.1294                       
L13:  -0.0254 L23:   0.0947                       
S TENSOR                                            
S11:  -0.0074 S12:  -0.0272 S13:   0.0215         
S21:   0.0219 S22:   0.0219 S23:   0.0611         
S31:   0.0155 S32:  -0.0197 S33:  -0.0000         
TLS GROUP : 4     
SELECTION: chain 'A' and (resid 186 through 246 )
ORIGIN FOR THE GROUP (A):  -3.9971  23.6931 -22.8305
T TENSOR                                            
T11:   0.1541 T22:   0.1469                       
T33:   0.1474 T12:  -0.0046                       
T13:  -0.0016 T23:  -0.0111                       
L TENSOR                                            
L11:   0.4427 L22:   0.2773                       
L33:   0.1907 L12:  -0.0903                       
L13:   0.0798 L23:   0.0186                       
S TENSOR                                            
S11:  -0.0181 S12:   0.0763 S13:  -0.0427         
S21:  -0.0485 S22:   0.0337 S23:  -0.0124         
S31:  -0.0370 S32:   0.1025 S33:  -0.0000         
TLS GROUP : 5     
SELECTION: chain 'A' and (resid 247 through 277 )
ORIGIN FOR THE GROUP (A):   1.3258  16.6523 -22.6549
T TENSOR                                            
T11:   0.1576 T22:   0.1645                       
T33:   0.1747 T12:   0.0269                       
T13:  -0.0034 T23:  -0.0317                       
L TENSOR                                            
L11:   0.1060 L22:   0.3129                       
L33:   0.3345 L12:  -0.0810                       
L13:   0.1743 L23:   0.1541                       
S TENSOR                                            
S11:   0.0689 S12:   0.0255 S13:  -0.0700         
S21:   0.0461 S22:  -0.0215 S23:  -0.0349         
S31:   0.0282 S32:   0.2609 S33:  -0.0048         
TLS GROUP : 6     
SELECTION: chain 'A' and (resid 278 through 305 )
ORIGIN FOR THE GROUP (A):  -1.6435   5.5827 -14.6457
T TENSOR                                            
T11:   0.2525 T22:   0.1632                       
T33:   0.2628 T12:   0.0408                       
T13:  -0.0276 T23:  -0.0134                       
L TENSOR                                            
L11:   0.0894 L22:   0.1110                       
L33:   0.5350 L12:  -0.0173                       
L13:  -0.0790 L23:   0.2398                       
S TENSOR                                            
S11:  -0.1228 S12:  -0.0741 S13:  -0.4532         
S21:   0.3292 S22:  -0.0291 S23:  -0.1298         
S31:   0.6060 S32:   0.1017 S33:  -0.0071         
TLS GROUP : 7     
SELECTION: chain 'B' and (resid 1 through 20 )
ORIGIN FOR THE GROUP (A): -39.0059  19.4217 -34.1021
T TENSOR                                            
T11:   0.1581 T22:   0.2108                       
T33:   0.1867 T12:   0.0040                       
T13:   0.0123 T23:   0.0033                       
L TENSOR                                            
L11:   0.1213 L22:   0.0800                       
L33:   0.4310 L12:   0.0097                       
L13:   0.2148 L23:  -0.0853                       
S TENSOR                                            
S11:  -0.0477 S12:  -0.0284 S13:  -0.0893         
S21:   0.0283 S22:   0.0348 S23:   0.0230         
S31:   0.2385 S32:  -0.1119 S33:   0.0001         
TLS GROUP : 8     
SELECTION: chain 'B' and (resid 21 through 52 )
ORIGIN FOR THE GROUP (A): -38.2971  14.5567 -41.5819
T TENSOR                                            
T11:   0.2010 T22:   0.1815                       
T33:   0.1633 T12:  -0.0385                       
T13:   0.0020 T23:  -0.0153                       
L TENSOR                                            
L11:   0.1575 L22:   0.1244                       
L33:   0.4539 L12:   0.0216                       
L13:   0.1372 L23:  -0.2981                       
S TENSOR                                            
S11:   0.0047 S12:   0.0640 S13:  -0.1072         
S21:  -0.1262 S22:   0.0048 S23:   0.0246         
S31:   0.2405 S32:  -0.1639 S33:   0.0021         
TLS GROUP : 9     
SELECTION: chain 'B' and (resid 53 through 84 )
ORIGIN FOR THE GROUP (A): -32.2682  23.2516 -48.3338
T TENSOR                                            
T11:   0.1559 T22:   0.2003                       
T33:   0.1564 T12:  -0.0159                       
T13:  -0.0037 T23:  -0.0140                       
L TENSOR                                            
L11:   0.0286 L22:   0.2819                       
L33:   0.4686 L12:  -0.0237                       
L13:   0.0099 L23:   0.0556                       
S TENSOR                                            
S11:   0.0205 S12:   0.0669 S13:   0.0035         
S21:  -0.1042 S22:   0.0268 S23:  -0.0124         
S31:   0.0817 S32:   0.0170 S33:   0.0000         
TLS GROUP : 10    
SELECTION: chain 'B' and (resid 85 through 138 )
ORIGIN FOR THE GROUP (A): -29.3329  29.6624 -39.7053
T TENSOR                                            
T11:   0.1144 T22:   0.1594                       
T33:   0.1351 T12:  -0.0046                       
T13:  -0.0051 T23:   0.0061                       
L TENSOR                                            
L11:   0.0166 L22:   0.3761                       
L33:   0.5540 L12:   0.0602                       
L13:   0.0178 L23:   0.3342                       
S TENSOR                                            
S11:  -0.0070 S12:   0.0420 S13:   0.0132         
S21:  -0.0208 S22:   0.0348 S23:  -0.0105         
S31:   0.0161 S32:  -0.0149 S33:   0.0000         
TLS GROUP : 11    
SELECTION: chain 'B' and (resid 139 through 216 )
ORIGIN FOR THE GROUP (A): -32.0807  31.2161 -27.9941
T TENSOR                                            
T11:   0.1474 T22:   0.1457                       
T33:   0.1441 T12:   0.0040                       
T13:  -0.0058 T23:   0.0033                       
L TENSOR                                            
L11:   0.1775 L22:   0.3135                       
L33:   0.6299 L12:   0.3057                       
L13:  -0.1453 L23:   0.0916                       
S TENSOR                                            
S11:  -0.0277 S12:  -0.0295 S13:   0.0266         
S21:   0.1021 S22:   0.0183 S23:  -0.0435         
S31:  -0.0580 S32:  -0.0669 S33:  -0.0002         
TLS GROUP : 12    
SELECTION: chain 'B' and (resid 217 through 231 )
ORIGIN FOR THE GROUP (A): -37.0002  30.2209 -15.3864
T TENSOR                                            
T11:   0.2437 T22:   0.2093                       
T33:   0.1521 T12:  -0.0160                       
T13:   0.0262 T23:   0.0097                       
L TENSOR                                            
L11:   0.0280 L22:   0.0301                       
L33:   0.0584 L12:   0.0314                       
L13:   0.0515 L23:   0.0143                       
S TENSOR                                            
S11:   0.0678 S12:  -0.1291 S13:  -0.0430         
S21:   0.4576 S22:  -0.0824 S23:   0.0546         
S31:  -0.0800 S32:  -0.1094 S33:   0.0000         
TLS GROUP : 13    
SELECTION: chain 'B' and (resid 232 through 246 )
ORIGIN FOR THE GROUP (A): -38.4898  24.4467 -23.9162
T TENSOR                                            
T11:   0.2194 T22:   0.1712                       
T33:   0.1654 T12:  -0.0126                       
T13:   0.0155 T23:  -0.0070                       
L TENSOR                                            
L11:   0.0700 L22:   0.0398                       
L33:   0.1241 L12:   0.0597                       
L13:  -0.0675 L23:  -0.0260                       
S TENSOR                                            
S11:   0.0417 S12:  -0.0871 S13:   0.0069         
S21:   0.1881 S22:  -0.1035 S23:   0.1380         
S31:   0.0575 S32:  -0.1808 S33:  -0.0025         
TLS GROUP : 14    
SELECTION: chain 'B' and (resid 247 through 263 )
ORIGIN FOR THE GROUP (A): -43.8889  19.5534 -16.1059
T TENSOR                                            
T11:   0.2575 T22:   0.2404                       
T33:   0.1739 T12:  -0.0431                       
T13:   0.0336 T23:  -0.0024                       
L TENSOR                                            
L11:   0.0283 L22:   0.0270                       
L33:   0.0740 L12:  -0.0218                       
L13:  -0.0114 L23:  -0.0163                       
S TENSOR                                            
S11:  -0.0132 S12:  -0.0626 S13:  -0.0430         
S21:   0.2340 S22:  -0.0338 S23:   0.0866         
S31:   0.1874 S32:  -0.3468 S33:  -0.0001         
TLS GROUP : 15    
SELECTION: chain 'B' and (resid 264 through 305 )
ORIGIN FOR THE GROUP (A): -42.0222  13.2385 -28.5887
T TENSOR                                            
T11:   0.2185 T22:   0.1841                       
T33:   0.1706 T12:  -0.0530                       
T13:  -0.0042 T23:   0.0118                       
L TENSOR                                            
L11:   0.1772 L22:   0.1531                       
L33:   0.5268 L12:   0.0156                       
L13:   0.1172 L23:  -0.2397                       
S TENSOR                                            
S11:   0.0627 S12:   0.0128 S13:  -0.0739         
S21:  -0.1086 S22:  -0.0308 S23:   0.0591         
S31:   0.2241 S32:  -0.2015 S33:   0.0000
;
_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                                 9F0M 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.63 
_refine.ls_d_res_low                             42.71 
_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                     73338 
_refine.ls_number_reflns_R_free                  3665 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.65 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1444 
_refine.ls_R_factor_R_free                       0.1744 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1428 
_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                          1.37 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 16.67 
_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                            0.16 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4749 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         146 
_refine_hist.number_atoms_solvent             944 
_refine_hist.number_atoms_total               5839 
_refine_hist.d_res_high                       1.63 
_refine_hist.d_res_low                        42.71 
# 
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' ? 0.008  ? 5245 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.919  ? 7215 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.856 ? 2068 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.060  ? 810  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 917  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.63 1.65  . . 129 2456 92.00  . . . . 0.2068 . . . . . . . . . . . 0.2604 
'X-RAY DIFFRACTION' 1.65 1.67  . . 139 2645 100.00 . . . . 0.1779 . . . . . . . . . . . 0.2387 
'X-RAY DIFFRACTION' 1.67 1.70  . . 138 2650 100.00 . . . . 0.1678 . . . . . . . . . . . 0.2210 
'X-RAY DIFFRACTION' 1.70 1.72  . . 140 2655 100.00 . . . . 0.1622 . . . . . . . . . . . 0.1783 
'X-RAY DIFFRACTION' 1.72 1.75  . . 141 2668 100.00 . . . . 0.1668 . . . . . . . . . . . 0.2164 
'X-RAY DIFFRACTION' 1.75 1.78  . . 137 2622 100.00 . . . . 0.1707 . . . . . . . . . . . 0.2160 
'X-RAY DIFFRACTION' 1.78 1.81  . . 140 2670 100.00 . . . . 0.1902 . . . . . . . . . . . 0.2431 
'X-RAY DIFFRACTION' 1.81 1.84  . . 140 2661 100.00 . . . . 0.2091 . . . . . . . . . . . 0.2995 
'X-RAY DIFFRACTION' 1.84 1.88  . . 140 2653 100.00 . . . . 0.1896 . . . . . . . . . . . 0.2408 
'X-RAY DIFFRACTION' 1.88 1.92  . . 141 2667 100.00 . . . . 0.1723 . . . . . . . . . . . 0.2004 
'X-RAY DIFFRACTION' 1.92 1.96  . . 141 2679 100.00 . . . . 0.1577 . . . . . . . . . . . 0.1839 
'X-RAY DIFFRACTION' 1.96 2.00  . . 139 2655 100.00 . . . . 0.1451 . . . . . . . . . . . 0.2163 
'X-RAY DIFFRACTION' 2.00 2.05  . . 141 2673 100.00 . . . . 0.1428 . . . . . . . . . . . 0.1777 
'X-RAY DIFFRACTION' 2.05 2.11  . . 140 2664 100.00 . . . . 0.1400 . . . . . . . . . . . 0.1830 
'X-RAY DIFFRACTION' 2.11 2.17  . . 142 2685 100.00 . . . . 0.1460 . . . . . . . . . . . 0.1727 
'X-RAY DIFFRACTION' 2.17 2.24  . . 141 2684 100.00 . . . . 0.1463 . . . . . . . . . . . 0.1883 
'X-RAY DIFFRACTION' 2.24 2.32  . . 141 2674 100.00 . . . . 0.1457 . . . . . . . . . . . 0.1936 
'X-RAY DIFFRACTION' 2.32 2.41  . . 141 2686 100.00 . . . . 0.1414 . . . . . . . . . . . 0.1817 
'X-RAY DIFFRACTION' 2.41 2.52  . . 142 2691 100.00 . . . . 0.1437 . . . . . . . . . . . 0.1677 
'X-RAY DIFFRACTION' 2.52 2.66  . . 142 2700 100.00 . . . . 0.1374 . . . . . . . . . . . 0.1591 
'X-RAY DIFFRACTION' 2.66 2.82  . . 142 2696 100.00 . . . . 0.1392 . . . . . . . . . . . 0.1912 
'X-RAY DIFFRACTION' 2.82 3.04  . . 142 2703 100.00 . . . . 0.1423 . . . . . . . . . . . 0.1755 
'X-RAY DIFFRACTION' 3.04 3.35  . . 144 2741 100.00 . . . . 0.1391 . . . . . . . . . . . 0.1586 
'X-RAY DIFFRACTION' 3.35 3.83  . . 144 2739 100.00 . . . . 0.1275 . . . . . . . . . . . 0.1547 
'X-RAY DIFFRACTION' 3.83 4.82  . . 146 2768 100.00 . . . . 0.1100 . . . . . . . . . . . 0.1315 
'X-RAY DIFFRACTION' 4.83 42.71 . . 152 2888 100.00 . . . . 0.1389 . . . . . . . . . . . 0.1403 
# 
_struct.entry_id                     9F0M 
_struct.title                        'Crystal structure of Ta_Cel5A E133Q Y200F variant in complex with cellopentaose' 
_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        9F0M 
_struct_keywords.text            'cellulase, TIM barrel, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
K N N 5 ? 
L N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q8TG26_THEAU 
_struct_ref.pdbx_db_accession          Q8TG26 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AKVFQWFGSNESGAEFGSQNLPGVEGKDYIWPDPNTIDTLISKGMNIFRVPFMMERLVPNSMTGSPDPNYLADLIATVNA
ITQKGAYAVVDPHNYGRYYNSIISSPSDFQTFWKTVASQFASNPLVIFDTNNEYHDMDQTLVLNLNQAAIDGIRSAGATS
QYIFVEGNSWTGAWTWTNVNDNMKSLTDPSDKIIYEMHQYLDSDGSGTSATCVSSTIGQERITSATQWLRANGKKGIIGE
FAGGANDVCETAITGMLDYMAQNTDVWTGAIWWAAGPWWGDYIFSMEPDNGIAYQQILPILTPYL
;
_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 9F0M A 2 ? 306 ? Q8TG26 31 ? 335 ? 1 305 
2 1 9F0M B 2 ? 306 ? Q8TG26 31 ? 335 ? 1 305 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9F0M MET A 1   ? UNP Q8TG26 ?   ?   'initiating methionine' 0   1 
1 9F0M GLN A 134 ? UNP Q8TG26 GLU 163 'engineered mutation'   133 2 
1 9F0M PHE A 201 ? UNP Q8TG26 TYR 230 'engineered mutation'   200 3 
2 9F0M MET B 1   ? UNP Q8TG26 ?   ?   'initiating methionine' 0   4 
2 9F0M GLN B 134 ? UNP Q8TG26 GLU 163 'engineered mutation'   133 5 
2 9F0M PHE B 201 ? UNP Q8TG26 TYR 230 'engineered mutation'   200 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E,F,K     
2 1 B,D,G,H,I,J,L 
# 
_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                
'Ta_Cel5A eluted as a monomer using a Superdex 75 column conditioned with 50 mM Tris pH 8.0 NaCl 150 mM.' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 34  ? LYS A 44  ? ASP A 33  LYS A 43  1 ? 11 
HELX_P HELX_P2  AA2 MET A 54  ? VAL A 59  ? MET A 53  VAL A 58  1 ? 6  
HELX_P HELX_P3  AA3 ASP A 68  ? GLN A 84  ? ASP A 67  GLN A 83  1 ? 17 
HELX_P HELX_P4  AA4 SER A 106 ? GLN A 120 ? SER A 105 GLN A 119 1 ? 15 
HELX_P HELX_P5  AA5 ASP A 139 ? ALA A 157 ? ASP A 138 ALA A 156 1 ? 19 
HELX_P HELX_P6  AA6 THR A 176 ? ASN A 181 ? THR A 175 ASN A 180 1 ? 6  
HELX_P HELX_P7  AA7 ASP A 182 ? LEU A 187 ? ASP A 181 LEU A 186 5 ? 6  
HELX_P HELX_P8  AA8 THR A 217 ? ILE A 223 ? THR A 216 ILE A 222 1 ? 7  
HELX_P HELX_P9  AA9 ILE A 223 ? ASN A 233 ? ILE A 222 ASN A 232 1 ? 11 
HELX_P HELX_P10 AB1 ASN A 247 ? GLN A 263 ? ASN A 246 GLN A 262 1 ? 17 
HELX_P HELX_P11 AB2 GLY A 292 ? ILE A 298 ? GLY A 291 ILE A 297 1 ? 7  
HELX_P HELX_P12 AB3 ILE A 298 ? THR A 303 ? ILE A 297 THR A 302 1 ? 6  
HELX_P HELX_P13 AB4 PRO A 304 ? LEU A 306 ? PRO A 303 LEU A 305 5 ? 3  
HELX_P HELX_P14 AB5 ASP B 34  ? LYS B 44  ? ASP B 33  LYS B 43  1 ? 11 
HELX_P HELX_P15 AB6 MET B 54  ? VAL B 59  ? MET B 53  VAL B 58  1 ? 6  
HELX_P HELX_P16 AB7 ASP B 68  ? LYS B 85  ? ASP B 67  LYS B 84  1 ? 18 
HELX_P HELX_P17 AB8 SER B 106 ? GLN B 120 ? SER B 105 GLN B 119 1 ? 15 
HELX_P HELX_P18 AB9 ASP B 139 ? ALA B 157 ? ASP B 138 ALA B 156 1 ? 19 
HELX_P HELX_P19 AC1 ASN B 169 ? GLY B 173 ? ASN B 168 GLY B 172 5 ? 5  
HELX_P HELX_P20 AC2 THR B 176 ? ASN B 181 ? THR B 175 ASN B 180 1 ? 6  
HELX_P HELX_P21 AC3 ASP B 182 ? LEU B 187 ? ASP B 181 LEU B 186 5 ? 6  
HELX_P HELX_P22 AC4 THR B 217 ? ASN B 233 ? THR B 216 ASN B 232 1 ? 17 
HELX_P HELX_P23 AC5 ASN B 247 ? GLN B 263 ? ASN B 246 GLN B 262 1 ? 17 
HELX_P HELX_P24 AC6 GLY B 292 ? ILE B 298 ? GLY B 291 ILE B 297 1 ? 7  
HELX_P HELX_P25 AC7 ILE B 298 ? THR B 303 ? ILE B 297 THR B 302 1 ? 6  
HELX_P HELX_P26 AC8 PRO B 304 ? LEU B 306 ? PRO B 303 LEU B 305 5 ? 3  
# 
_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 213 SG ? ? ? 1_555 A CYS 250 SG ? ? A CYS 212 A CYS 249 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
disulf2 disulf ?    ? B CYS 213 SG ? ? ? 1_555 B CYS 250 SG ? ? B CYS 212 B CYS 249 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
covale1 covale both ? C BGC .   O4 ? ? ? 1_555 C BGC .   C1 ? ? C BGC 1   C BGC 2   1_555 ? ? ? ? ? ? ? 1.375 ? ? 
covale2 covale both ? C BGC .   O4 ? ? ? 1_555 C BGC .   C1 ? ? C BGC 2   C BGC 3   1_555 ? ? ? ? ? ? ? 1.435 ? ? 
covale3 covale both ? C BGC .   O4 ? ? ? 1_555 C BGC .   C1 ? ? C BGC 3   C BGC 4   1_555 ? ? ? ? ? ? ? 1.433 ? ? 
covale4 covale both ? C BGC .   O4 ? ? ? 1_555 C BGC .   C1 ? ? C BGC 4   C BGC 5   1_555 ? ? ? ? ? ? ? 1.445 ? ? 
covale5 covale both ? D BGC .   O4 ? ? ? 1_555 D BGC .   C1 ? ? D BGC 1   D BGC 2   1_555 ? ? ? ? ? ? ? 1.431 ? ? 
covale6 covale both ? D BGC .   O4 ? ? ? 1_555 D BGC .   C1 ? ? D BGC 2   D BGC 3   1_555 ? ? ? ? ? ? ? 1.434 ? ? 
covale7 covale both ? D BGC .   O4 ? ? ? 1_555 D BGC .   C1 ? ? D BGC 3   D BGC 4   1_555 ? ? ? ? ? ? ? 1.440 ? ? 
covale8 covale both ? D BGC .   O4 ? ? ? 1_555 D BGC .   C1 ? ? D BGC 4   D BGC 5   1_555 ? ? ? ? ? ? ? 1.443 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 213 ? CYS A 250 ? CYS A 212 ? 1_555 CYS A 249 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 213 ? CYS B 250 ? CYS B 212 ? 1_555 CYS B 249 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 22  A . ? LEU 21  A PRO 23  A ? PRO 22  A 1 2.07  
2 TRP 274 A . ? TRP 273 A ALA 275 A ? ALA 274 A 1 1.07  
3 PRO 289 A . ? PRO 288 A ASP 290 A ? ASP 289 A 1 -0.33 
4 LEU 22  B . ? LEU 21  B PRO 23  B ? PRO 22  B 1 0.83  
5 TRP 274 B . ? TRP 273 B ALA 275 B ? ALA 274 B 1 1.88  
6 PRO 289 B . ? PRO 288 B ASP 290 B ? ASP 289 B 1 0.79  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 2 ? 
AA3 ? 9 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA3 7 8 ? parallel      
AA3 8 9 ? parallel      
AA4 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 TRP A 7   ? GLU A 12  ? TRP A 6   GLU A 11  
AA1 2 ILE A 48  ? PHE A 53  ? ILE A 47  PHE A 52  
AA1 3 TYR A 88  ? PRO A 93  ? TYR A 87  PRO A 92  
AA1 4 VAL A 127 ? ASP A 130 ? VAL A 126 ASP A 129 
AA1 5 ILE A 164 ? GLU A 167 ? ILE A 163 GLU A 166 
AA1 6 ILE A 194 ? PHE A 201 ? ILE A 193 PHE A 200 
AA1 7 GLY A 237 ? ALA A 243 ? GLY A 236 ALA A 242 
AA1 8 TRP A 268 ? ALA A 276 ? TRP A 267 ALA A 275 
AA1 9 TRP A 7   ? GLU A 12  ? TRP A 6   GLU A 11  
AA2 1 ARG A 98  ? TYR A 99  ? ARG A 97  TYR A 98  
AA2 2 SER A 102 ? ILE A 103 ? SER A 101 ILE A 102 
AA3 1 TRP B 7   ? GLU B 12  ? TRP B 6   GLU B 11  
AA3 2 ILE B 48  ? PHE B 53  ? ILE B 47  PHE B 52  
AA3 3 TYR B 88  ? PRO B 93  ? TYR B 87  PRO B 92  
AA3 4 VAL B 127 ? ASP B 130 ? VAL B 126 ASP B 129 
AA3 5 ILE B 164 ? GLU B 167 ? ILE B 163 GLU B 166 
AA3 6 ILE B 194 ? PHE B 201 ? ILE B 193 PHE B 200 
AA3 7 GLY B 237 ? ALA B 243 ? GLY B 236 ALA B 242 
AA3 8 TRP B 268 ? ALA B 276 ? TRP B 267 ALA B 275 
AA3 9 TRP B 7   ? GLU B 12  ? TRP B 6   GLU B 11  
AA4 1 ARG B 98  ? TYR B 99  ? ARG B 97  TYR B 98  
AA4 2 SER B 102 ? ILE B 103 ? SER B 101 ILE B 102 
# 
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 GLU A 12  ? N GLU A 11  O ARG A 50  ? O ARG A 49  
AA1 2 3 N VAL A 51  ? N VAL A 50  O VAL A 90  ? O VAL A 89  
AA1 3 4 N VAL A 91  ? N VAL A 90  O ILE A 128 ? O ILE A 127 
AA1 4 5 N PHE A 129 ? N PHE A 128 O PHE A 165 ? O PHE A 164 
AA1 5 6 N VAL A 166 ? N VAL A 165 O GLU A 197 ? O GLU A 196 
AA1 6 7 N MET A 198 ? N MET A 197 O ILE A 238 ? O ILE A 237 
AA1 7 8 N GLY A 237 ? N GLY A 236 O THR A 269 ? O THR A 268 
AA1 8 9 O TRP A 273 ? O TRP A 272 N ASN A 11  ? N ASN A 10  
AA2 1 2 N TYR A 99  ? N TYR A 98  O SER A 102 ? O SER A 101 
AA3 1 2 N GLU B 12  ? N GLU B 11  O ARG B 50  ? O ARG B 49  
AA3 2 3 N VAL B 51  ? N VAL B 50  O VAL B 90  ? O VAL B 89  
AA3 3 4 N VAL B 91  ? N VAL B 90  O ILE B 128 ? O ILE B 127 
AA3 4 5 N PHE B 129 ? N PHE B 128 O PHE B 165 ? O PHE B 164 
AA3 5 6 N VAL B 166 ? N VAL B 165 O GLU B 197 ? O GLU B 196 
AA3 6 7 N MET B 198 ? N MET B 197 O ILE B 238 ? O ILE B 237 
AA3 7 8 N GLY B 237 ? N GLY B 236 O THR B 269 ? O THR B 268 
AA3 8 9 O TRP B 273 ? O TRP B 272 N ASN B 11  ? N ASN B 10  
AA4 1 2 N TYR B 99  ? N TYR B 98  O SER B 102 ? O SER B 101 
# 
_pdbx_entry_details.entry_id                   9F0M 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 686  ? ? O  A HOH 888  ? ? 1.54 
2  1 O   A HOH 883  ? ? O  A HOH 968  ? ? 1.65 
3  1 O   A HOH 699  ? ? O  A HOH 814  ? ? 1.67 
4  1 O   A HOH 617  ? ? O  A HOH 665  ? ? 1.70 
5  1 O   B HOH 627  ? ? O  B HOH 1018 ? ? 1.72 
6  1 O   A HOH 802  ? ? O  A HOH 892  ? ? 1.72 
7  1 O   A HOH 654  ? ? O  A HOH 967  ? ? 1.74 
8  1 O   A HOH 911  ? ? O  A HOH 964  ? ? 1.78 
9  1 O   A HOH 666  ? ? O  A HOH 965  ? ? 1.80 
10 1 O   A HOH 959  ? ? O  A HOH 1031 ? ? 1.85 
11 1 O   B HOH 664  ? ? O  B HOH 971  ? ? 1.88 
12 1 O6  C BGC 1    ? A O  A HOH 897  ? ? 1.89 
13 1 O   B HOH 904  ? ? O  B HOH 1029 ? ? 1.90 
14 1 O4  D BGC 5    ? ? O  B HOH 875  ? ? 1.91 
15 1 OD1 A ASN 100  ? B O  A HOH 601  ? ? 1.93 
16 1 O   A HOH 628  ? ? O  A HOH 896  ? ? 1.93 
17 1 O   A HOH 859  ? ? O  A HOH 890  ? ? 1.93 
18 1 O   A HOH 873  ? ? O  A HOH 989  ? ? 1.95 
19 1 O   B HOH 789  ? ? O  B HOH 1013 ? ? 1.95 
20 1 O   A HOH 868  ? ? O  A HOH 873  ? ? 1.96 
21 1 O   B HOH 1013 ? ? O  B HOH 1061 ? ? 1.96 
22 1 O1  A GOL 501  ? A O  A HOH 602  ? ? 1.98 
23 1 O   B HOH 783  ? ? O  B HOH 1036 ? ? 1.98 
24 1 C4  C BGC 1    ? A C1 C BGC 2    ? ? 1.98 
25 1 O   A HOH 917  ? ? O  A HOH 972  ? ? 1.99 
26 1 O4  C BGC 5    ? ? O  A HOH 904  ? ? 1.99 
27 1 O   A HOH 655  ? ? O  A HOH 916  ? ? 2.00 
28 1 OD2 B ASP 265  ? ? O  B HOH 601  ? ? 2.00 
29 1 O   B HOH 645  ? ? O  B HOH 799  ? ? 2.01 
30 1 O   B HOH 952  ? ? O  B HOH 974  ? ? 2.05 
31 1 O   A HOH 897  ? ? O  A HOH 1043 ? ? 2.06 
32 1 O4  B SO4 504  ? ? O  B HOH 602  ? ? 2.06 
33 1 C4  C BGC 1    ? B C1 C BGC 2    ? ? 2.07 
34 1 OE1 B GLN 262  ? B O  B HOH 603  ? ? 2.07 
35 1 O   A HOH 918  ? ? O  A HOH 977  ? ? 2.08 
36 1 O   A HOH 690  ? ? O  B HOH 859  ? ? 2.08 
37 1 O3  C BGC 4    ? ? O  A HOH 950  ? ? 2.09 
38 1 O   B HOH 670  ? ? O  B HOH 989  ? ? 2.11 
39 1 O   A HOH 690  ? ? O  A HOH 843  ? ? 2.12 
40 1 O   B HOH 621  ? ? O  B HOH 674  ? ? 2.13 
41 1 O   A HOH 819  ? ? O  A HOH 956  ? ? 2.13 
42 1 O   B HOH 933  ? ? O  B HOH 940  ? ? 2.14 
43 1 O3  B GOL 501  ? ? O  B HOH 604  ? ? 2.15 
44 1 O   A HOH 628  ? ? O  A HOH 645  ? ? 2.16 
45 1 OG1 A THR 302  ? ? O  A HOH 603  ? ? 2.17 
46 1 O   B HOH 807  ? ? O  B HOH 924  ? ? 2.17 
47 1 OE2 A GLU 250  ? ? O  A HOH 604  ? ? 2.17 
48 1 O   B HOH 786  ? ? O  B HOH 988  ? ? 2.17 
49 1 OG  A SER 203  ? ? O  A HOH 605  ? ? 2.18 
50 1 ND2 A ASN 178  ? ? O  A HOH 606  ? ? 2.18 
51 1 O   A HOH 602  ? ? O  A HOH 910  ? ? 2.18 
52 1 O   A HOH 985  ? ? O  B HOH 1024 ? ? 2.18 
53 1 O1  A GOL 501  ? B O  A HOH 607  ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 640 ? ? 1_555 O A HOH 878  ? ? 3_554 1.79 
2 1 O B HOH 938 ? ? 1_555 O B HOH 949  ? ? 3_444 2.02 
3 1 O A HOH 802 ? ? 1_555 O A HOH 877  ? ? 3_554 2.07 
4 1 O A HOH 665 ? ? 1_555 O B HOH 980  ? ? 4_554 2.09 
5 1 O A HOH 624 ? ? 1_555 O A HOH 725  ? ? 4_455 2.12 
6 1 O A HOH 833 ? ? 1_555 O A HOH 1015 ? ? 4_555 2.13 
7 1 O A HOH 799 ? ? 1_555 O B HOH 613  ? ? 4_554 2.16 
# 
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 LYS A 27  ? ? -122.22 -51.50  
2 1 LYS A 27  ? ? -122.08 -51.75  
3 1 ASN A 60  ? ? 72.93   -56.43  
4 1 ASN A 131 ? ? -174.17 145.29  
5 1 ASN B 60  ? ? 75.82   -60.26  
6 1 ASN B 131 ? ? -171.02 147.57  
7 1 ASN B 168 ? ? -69.39  -179.25 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined -4.6308  16.5019 -9.7772  0.1927 ? -0.0028 ? -0.0230 ? 0.1642 ? -0.0098 ? 0.2009 ? 0.0558 ? 
0.0761  ? 0.1538  ? 0.1118 ? 0.2250  ? 0.3906 ? 0.0676  ? -0.0957 ? -0.1023 ? 0.0052  ? -0.0523 ? -0.0398 ? 0.1943  ? 0.0629  ? 
0.0001  ? 
2  'X-RAY DIFFRACTION' ? refined -7.1860  16.9285 0.6502   0.2073 ? -0.0039 ? -0.0150 ? 0.1618 ? 0.0314  ? 0.1817 ? 0.3000 ? 
0.3691  ? -0.0577 ? 0.6249 ? 0.2460  ? 0.6451 ? 0.0705  ? -0.0710 ? -0.0979 ? 0.2006  ? -0.0545 ? -0.0257 ? 0.2029  ? -0.0568 ? 
0.0002  ? 
3  'X-RAY DIFFRACTION' ? refined -9.8970  30.8504 -9.2245  0.1288 ? 0.0064  ? -0.0053 ? 0.1286 ? -0.0041 ? 0.1582 ? 0.5347 ? 
0.1294  ? -0.0254 ? 0.5469 ? 0.0947  ? 0.4977 ? -0.0074 ? -0.0272 ? 0.0215  ? 0.0219  ? 0.0219  ? 0.0611  ? 0.0155  ? -0.0197 ? 
-0.0000 ? 
4  'X-RAY DIFFRACTION' ? refined -3.9971  23.6931 -22.8305 0.1541 ? -0.0046 ? -0.0016 ? 0.1469 ? -0.0111 ? 0.1474 ? 0.4427 ? 
-0.0903 ? 0.0798  ? 0.2773 ? 0.0186  ? 0.1907 ? -0.0181 ? 0.0763  ? -0.0427 ? -0.0485 ? 0.0337  ? -0.0124 ? -0.0370 ? 0.1025  ? 
-0.0000 ? 
5  'X-RAY DIFFRACTION' ? refined 1.3258   16.6523 -22.6549 0.1576 ? 0.0269  ? -0.0034 ? 0.1645 ? -0.0317 ? 0.1747 ? 0.1060 ? 
-0.0810 ? 0.1743  ? 0.3129 ? 0.1541  ? 0.3345 ? 0.0689  ? 0.0255  ? -0.0700 ? 0.0461  ? -0.0215 ? -0.0349 ? 0.0282  ? 0.2609  ? 
-0.0048 ? 
6  'X-RAY DIFFRACTION' ? refined -1.6435  5.5827  -14.6457 0.2525 ? 0.0408  ? -0.0276 ? 0.1632 ? -0.0134 ? 0.2628 ? 0.0894 ? 
-0.0173 ? -0.0790 ? 0.1110 ? 0.2398  ? 0.5350 ? -0.1228 ? -0.0741 ? -0.4532 ? 0.3292  ? -0.0291 ? -0.1298 ? 0.6060  ? 0.1017  ? 
-0.0071 ? 
7  'X-RAY DIFFRACTION' ? refined -39.0059 19.4217 -34.1021 0.1581 ? 0.0040  ? 0.0123  ? 0.2108 ? 0.0033  ? 0.1867 ? 0.1213 ? 
0.0097  ? 0.2148  ? 0.0800 ? -0.0853 ? 0.4310 ? -0.0477 ? -0.0284 ? -0.0893 ? 0.0283  ? 0.0348  ? 0.0230  ? 0.2385  ? -0.1119 ? 
0.0001  ? 
8  'X-RAY DIFFRACTION' ? refined -38.2971 14.5567 -41.5819 0.2010 ? -0.0385 ? 0.0020  ? 0.1815 ? -0.0153 ? 0.1633 ? 0.1575 ? 
0.0216  ? 0.1372  ? 0.1244 ? -0.2981 ? 0.4539 ? 0.0047  ? 0.0640  ? -0.1072 ? -0.1262 ? 0.0048  ? 0.0246  ? 0.2405  ? -0.1639 ? 
0.0021  ? 
9  'X-RAY DIFFRACTION' ? refined -32.2682 23.2516 -48.3338 0.1559 ? -0.0159 ? -0.0037 ? 0.2003 ? -0.0140 ? 0.1564 ? 0.0286 ? 
-0.0237 ? 0.0099  ? 0.2819 ? 0.0556  ? 0.4686 ? 0.0205  ? 0.0669  ? 0.0035  ? -0.1042 ? 0.0268  ? -0.0124 ? 0.0817  ? 0.0170  ? 
0.0000  ? 
10 'X-RAY DIFFRACTION' ? refined -29.3329 29.6624 -39.7053 0.1144 ? -0.0046 ? -0.0051 ? 0.1594 ? 0.0061  ? 0.1351 ? 0.0166 ? 
0.0602  ? 0.0178  ? 0.3761 ? 0.3342  ? 0.5540 ? -0.0070 ? 0.0420  ? 0.0132  ? -0.0208 ? 0.0348  ? -0.0105 ? 0.0161  ? -0.0149 ? 
0.0000  ? 
11 'X-RAY DIFFRACTION' ? refined -32.0807 31.2161 -27.9941 0.1474 ? 0.0040  ? -0.0058 ? 0.1457 ? 0.0033  ? 0.1441 ? 0.1775 ? 
0.3057  ? -0.1453 ? 0.3135 ? 0.0916  ? 0.6299 ? -0.0277 ? -0.0295 ? 0.0266  ? 0.1021  ? 0.0183  ? -0.0435 ? -0.0580 ? -0.0669 ? 
-0.0002 ? 
12 'X-RAY DIFFRACTION' ? refined -37.0002 30.2209 -15.3864 0.2437 ? -0.0160 ? 0.0262  ? 0.2093 ? 0.0097  ? 0.1521 ? 0.0280 ? 
0.0314  ? 0.0515  ? 0.0301 ? 0.0143  ? 0.0584 ? 0.0678  ? -0.1291 ? -0.0430 ? 0.4576  ? -0.0824 ? 0.0546  ? -0.0800 ? -0.1094 ? 
0.0000  ? 
13 'X-RAY DIFFRACTION' ? refined -38.4898 24.4467 -23.9162 0.2194 ? -0.0126 ? 0.0155  ? 0.1712 ? -0.0070 ? 0.1654 ? 0.0700 ? 
0.0597  ? -0.0675 ? 0.0398 ? -0.0260 ? 0.1241 ? 0.0417  ? -0.0871 ? 0.0069  ? 0.1881  ? -0.1035 ? 0.1380  ? 0.0575  ? -0.1808 ? 
-0.0025 ? 
14 'X-RAY DIFFRACTION' ? refined -43.8889 19.5534 -16.1059 0.2575 ? -0.0431 ? 0.0336  ? 0.2404 ? -0.0024 ? 0.1739 ? 0.0283 ? 
-0.0218 ? -0.0114 ? 0.0270 ? -0.0163 ? 0.0740 ? -0.0132 ? -0.0626 ? -0.0430 ? 0.2340  ? -0.0338 ? 0.0866  ? 0.1874  ? -0.3468 ? 
-0.0001 ? 
15 'X-RAY DIFFRACTION' ? refined -42.0222 13.2385 -28.5887 0.2185 ? -0.0530 ? -0.0042 ? 0.1841 ? 0.0118  ? 0.1706 ? 0.1772 ? 
0.0156  ? 0.1172  ? 0.1531 ? -0.2397 ? 0.5268 ? 0.0627  ? 0.0128  ? -0.0739 ? -0.1086 ? -0.0308 ? 0.0591  ? 0.2241  ? -0.2015 ? 
0.0000  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 2 through 20 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 21 through 84 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 85 through 185 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 186 through 246 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 247 through 277 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 278 through 305 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 1 through 20 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 21 through 52 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 53 through 84 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 85 through 138 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 139 through 216 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 217 through 231 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 232 through 246 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 247 through 263 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 264 through 305 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1061 ? 6.05 . 
2 1 O ? A HOH 1062 ? 7.35 . 
3 1 O ? B HOH 1081 ? 6.28 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 0 ? A MET 1 
2 1 Y 1 A ALA 1 ? A ALA 2 
3 1 Y 1 B MET 0 ? B MET 1 
# 
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  
BGC C2   C N R 74  
BGC C3   C N S 75  
BGC C4   C N S 76  
BGC C5   C N R 77  
BGC C6   C N N 78  
BGC C1   C N R 79  
BGC O1   O N N 80  
BGC O2   O N N 81  
BGC O3   O N N 82  
BGC O4   O N N 83  
BGC O5   O N N 84  
BGC O6   O N N 85  
BGC H2   H N N 86  
BGC H3   H N N 87  
BGC H4   H N N 88  
BGC H5   H N N 89  
BGC H61  H N N 90  
BGC H62  H N N 91  
BGC H1   H N N 92  
BGC HO1  H N N 93  
BGC HO2  H N N 94  
BGC HO3  H N N 95  
BGC HO4  H N N 96  
BGC HO6  H N N 97  
CYS N    N N N 98  
CYS CA   C N R 99  
CYS C    C N N 100 
CYS O    O N N 101 
CYS CB   C N N 102 
CYS SG   S N N 103 
CYS OXT  O N N 104 
CYS H    H N N 105 
CYS H2   H N N 106 
CYS HA   H N N 107 
CYS HB2  H N N 108 
CYS HB3  H N N 109 
CYS HG   H N N 110 
CYS HXT  H N N 111 
GLN N    N N N 112 
GLN CA   C N S 113 
GLN C    C N N 114 
GLN O    O N N 115 
GLN CB   C N N 116 
GLN CG   C N N 117 
GLN CD   C N N 118 
GLN OE1  O N N 119 
GLN NE2  N N N 120 
GLN OXT  O N N 121 
GLN H    H N N 122 
GLN H2   H N N 123 
GLN HA   H N N 124 
GLN HB2  H N N 125 
GLN HB3  H N N 126 
GLN HG2  H N N 127 
GLN HG3  H N N 128 
GLN HE21 H N N 129 
GLN HE22 H N N 130 
GLN HXT  H N N 131 
GLU N    N N N 132 
GLU CA   C N S 133 
GLU C    C N N 134 
GLU O    O N N 135 
GLU CB   C N N 136 
GLU CG   C N N 137 
GLU CD   C N N 138 
GLU OE1  O N N 139 
GLU OE2  O N N 140 
GLU OXT  O N N 141 
GLU H    H N N 142 
GLU H2   H N N 143 
GLU HA   H N N 144 
GLU HB2  H N N 145 
GLU HB3  H N N 146 
GLU HG2  H N N 147 
GLU HG3  H N N 148 
GLU HE2  H N N 149 
GLU HXT  H N N 150 
GLY N    N N N 151 
GLY CA   C N N 152 
GLY C    C N N 153 
GLY O    O N N 154 
GLY OXT  O N N 155 
GLY H    H N N 156 
GLY H2   H N N 157 
GLY HA2  H N N 158 
GLY HA3  H N N 159 
GLY HXT  H N N 160 
GOL C1   C N N 161 
GOL O1   O N N 162 
GOL C2   C N N 163 
GOL O2   O N N 164 
GOL C3   C N N 165 
GOL O3   O N N 166 
GOL H11  H N N 167 
GOL H12  H N N 168 
GOL HO1  H N N 169 
GOL H2   H N N 170 
GOL HO2  H N N 171 
GOL H31  H N N 172 
GOL H32  H N N 173 
GOL HO3  H N N 174 
HIS N    N N N 175 
HIS CA   C N S 176 
HIS C    C N N 177 
HIS O    O N N 178 
HIS CB   C N N 179 
HIS CG   C Y N 180 
HIS ND1  N Y N 181 
HIS CD2  C Y N 182 
HIS CE1  C Y N 183 
HIS NE2  N Y N 184 
HIS OXT  O N N 185 
HIS H    H N N 186 
HIS H2   H N N 187 
HIS HA   H N N 188 
HIS HB2  H N N 189 
HIS HB3  H N N 190 
HIS HD1  H N N 191 
HIS HD2  H N N 192 
HIS HE1  H N N 193 
HIS HE2  H N N 194 
HIS HXT  H N N 195 
HOH O    O N N 196 
HOH H1   H N N 197 
HOH H2   H N N 198 
ILE N    N N N 199 
ILE CA   C N S 200 
ILE C    C N N 201 
ILE O    O N N 202 
ILE CB   C N S 203 
ILE CG1  C N N 204 
ILE CG2  C N N 205 
ILE CD1  C N N 206 
ILE OXT  O N N 207 
ILE H    H N N 208 
ILE H2   H N N 209 
ILE HA   H N N 210 
ILE HB   H N N 211 
ILE HG12 H N N 212 
ILE HG13 H N N 213 
ILE HG21 H N N 214 
ILE HG22 H N N 215 
ILE HG23 H N N 216 
ILE HD11 H N N 217 
ILE HD12 H N N 218 
ILE HD13 H N N 219 
ILE HXT  H N N 220 
LEU N    N N N 221 
LEU CA   C N S 222 
LEU C    C N N 223 
LEU O    O N N 224 
LEU CB   C N N 225 
LEU CG   C N N 226 
LEU CD1  C N N 227 
LEU CD2  C N N 228 
LEU OXT  O N N 229 
LEU H    H N N 230 
LEU H2   H N N 231 
LEU HA   H N N 232 
LEU HB2  H N N 233 
LEU HB3  H N N 234 
LEU HG   H N N 235 
LEU HD11 H N N 236 
LEU HD12 H N N 237 
LEU HD13 H N N 238 
LEU HD21 H N N 239 
LEU HD22 H N N 240 
LEU HD23 H N N 241 
LEU HXT  H N N 242 
LYS N    N N N 243 
LYS CA   C N S 244 
LYS C    C N N 245 
LYS O    O N N 246 
LYS CB   C N N 247 
LYS CG   C N N 248 
LYS CD   C N N 249 
LYS CE   C N N 250 
LYS NZ   N N N 251 
LYS OXT  O N N 252 
LYS H    H N N 253 
LYS H2   H N N 254 
LYS HA   H N N 255 
LYS HB2  H N N 256 
LYS HB3  H N N 257 
LYS HG2  H N N 258 
LYS HG3  H N N 259 
LYS HD2  H N N 260 
LYS HD3  H N N 261 
LYS HE2  H N N 262 
LYS HE3  H N N 263 
LYS HZ1  H N N 264 
LYS HZ2  H N N 265 
LYS HZ3  H N N 266 
LYS HXT  H N N 267 
MET N    N N N 268 
MET CA   C N S 269 
MET C    C N N 270 
MET O    O N N 271 
MET CB   C N N 272 
MET CG   C N N 273 
MET SD   S N N 274 
MET CE   C N N 275 
MET OXT  O N N 276 
MET H    H N N 277 
MET H2   H N N 278 
MET HA   H N N 279 
MET HB2  H N N 280 
MET HB3  H N N 281 
MET HG2  H N N 282 
MET HG3  H N N 283 
MET HE1  H N N 284 
MET HE2  H N N 285 
MET HE3  H N N 286 
MET HXT  H N N 287 
PHE N    N N N 288 
PHE CA   C N S 289 
PHE C    C N N 290 
PHE O    O N N 291 
PHE CB   C N N 292 
PHE CG   C Y N 293 
PHE CD1  C Y N 294 
PHE CD2  C Y N 295 
PHE CE1  C Y N 296 
PHE CE2  C Y N 297 
PHE CZ   C Y N 298 
PHE OXT  O N N 299 
PHE H    H N N 300 
PHE H2   H N N 301 
PHE HA   H N N 302 
PHE HB2  H N N 303 
PHE HB3  H N N 304 
PHE HD1  H N N 305 
PHE HD2  H N N 306 
PHE HE1  H N N 307 
PHE HE2  H N N 308 
PHE HZ   H N N 309 
PHE HXT  H N N 310 
PRO N    N N N 311 
PRO CA   C N S 312 
PRO C    C N N 313 
PRO O    O N N 314 
PRO CB   C N N 315 
PRO CG   C N N 316 
PRO CD   C N N 317 
PRO OXT  O N N 318 
PRO H    H N N 319 
PRO HA   H N N 320 
PRO HB2  H N N 321 
PRO HB3  H N N 322 
PRO HG2  H N N 323 
PRO HG3  H N N 324 
PRO HD2  H N N 325 
PRO HD3  H N N 326 
PRO HXT  H N N 327 
SER N    N N N 328 
SER CA   C N S 329 
SER C    C N N 330 
SER O    O N N 331 
SER CB   C N N 332 
SER OG   O N N 333 
SER OXT  O N N 334 
SER H    H N N 335 
SER H2   H N N 336 
SER HA   H N N 337 
SER HB2  H N N 338 
SER HB3  H N N 339 
SER HG   H N N 340 
SER HXT  H N N 341 
SO4 S    S N N 342 
SO4 O1   O N N 343 
SO4 O2   O N N 344 
SO4 O3   O N N 345 
SO4 O4   O N N 346 
THR N    N N N 347 
THR CA   C N S 348 
THR C    C N N 349 
THR O    O N N 350 
THR CB   C N R 351 
THR OG1  O N N 352 
THR CG2  C N N 353 
THR OXT  O N N 354 
THR H    H N N 355 
THR H2   H N N 356 
THR HA   H N N 357 
THR HB   H N N 358 
THR HG1  H N N 359 
THR HG21 H N N 360 
THR HG22 H N N 361 
THR HG23 H N N 362 
THR HXT  H N N 363 
TRP N    N N N 364 
TRP CA   C N S 365 
TRP C    C N N 366 
TRP O    O N N 367 
TRP CB   C N N 368 
TRP CG   C Y N 369 
TRP CD1  C Y N 370 
TRP CD2  C Y N 371 
TRP NE1  N Y N 372 
TRP CE2  C Y N 373 
TRP CE3  C Y N 374 
TRP CZ2  C Y N 375 
TRP CZ3  C Y N 376 
TRP CH2  C Y N 377 
TRP OXT  O N N 378 
TRP H    H N N 379 
TRP H2   H N N 380 
TRP HA   H N N 381 
TRP HB2  H N N 382 
TRP HB3  H N N 383 
TRP HD1  H N N 384 
TRP HE1  H N N 385 
TRP HE3  H N N 386 
TRP HZ2  H N N 387 
TRP HZ3  H N N 388 
TRP HH2  H N N 389 
TRP HXT  H N N 390 
TYR N    N N N 391 
TYR CA   C N S 392 
TYR C    C N N 393 
TYR O    O N N 394 
TYR CB   C N N 395 
TYR CG   C Y N 396 
TYR CD1  C Y N 397 
TYR CD2  C Y N 398 
TYR CE1  C Y N 399 
TYR CE2  C Y N 400 
TYR CZ   C Y N 401 
TYR OH   O N N 402 
TYR OXT  O N N 403 
TYR H    H N N 404 
TYR H2   H N N 405 
TYR HA   H N N 406 
TYR HB2  H N N 407 
TYR HB3  H N N 408 
TYR HD1  H N N 409 
TYR HD2  H N N 410 
TYR HE1  H N N 411 
TYR HE2  H N N 412 
TYR HH   H N N 413 
TYR HXT  H N N 414 
VAL N    N N N 415 
VAL CA   C N S 416 
VAL C    C N N 417 
VAL O    O N N 418 
VAL CB   C N N 419 
VAL CG1  C N N 420 
VAL CG2  C N N 421 
VAL OXT  O N N 422 
VAL H    H N N 423 
VAL H2   H N N 424 
VAL HA   H N N 425 
VAL HB   H N N 426 
VAL HG11 H N N 427 
VAL HG12 H N N 428 
VAL HG13 H N N 429 
VAL HG21 H N N 430 
VAL HG22 H N N 431 
VAL HG23 H N N 432 
VAL HXT  H N N 433 
# 
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  
BGC C2  C3   sing N N 70  
BGC C2  C1   sing N N 71  
BGC C2  O2   sing N N 72  
BGC C2  H2   sing N N 73  
BGC C3  C4   sing N N 74  
BGC C3  O3   sing N N 75  
BGC C3  H3   sing N N 76  
BGC C4  C5   sing N N 77  
BGC C4  O4   sing N N 78  
BGC C4  H4   sing N N 79  
BGC C5  C6   sing N N 80  
BGC C5  O5   sing N N 81  
BGC C5  H5   sing N N 82  
BGC C6  O6   sing N N 83  
BGC C6  H61  sing N N 84  
BGC C6  H62  sing N N 85  
BGC C1  O1   sing N N 86  
BGC C1  O5   sing N N 87  
BGC C1  H1   sing N N 88  
BGC O1  HO1  sing N N 89  
BGC O2  HO2  sing N N 90  
BGC O3  HO3  sing N N 91  
BGC O4  HO4  sing N N 92  
BGC O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
GOL C1  O1   sing N N 153 
GOL C1  C2   sing N N 154 
GOL C1  H11  sing N N 155 
GOL C1  H12  sing N N 156 
GOL O1  HO1  sing N N 157 
GOL C2  O2   sing N N 158 
GOL C2  C3   sing N N 159 
GOL C2  H2   sing N N 160 
GOL O2  HO2  sing N N 161 
GOL C3  O3   sing N N 162 
GOL C3  H31  sing N N 163 
GOL C3  H32  sing N N 164 
GOL O3  HO3  sing N N 165 
HIS N   CA   sing N N 166 
HIS N   H    sing N N 167 
HIS N   H2   sing N N 168 
HIS CA  C    sing N N 169 
HIS CA  CB   sing N N 170 
HIS CA  HA   sing N N 171 
HIS C   O    doub N N 172 
HIS C   OXT  sing N N 173 
HIS CB  CG   sing N N 174 
HIS CB  HB2  sing N N 175 
HIS CB  HB3  sing N N 176 
HIS CG  ND1  sing Y N 177 
HIS CG  CD2  doub Y N 178 
HIS ND1 CE1  doub Y N 179 
HIS ND1 HD1  sing N N 180 
HIS CD2 NE2  sing Y N 181 
HIS CD2 HD2  sing N N 182 
HIS CE1 NE2  sing Y N 183 
HIS CE1 HE1  sing N N 184 
HIS NE2 HE2  sing N N 185 
HIS OXT HXT  sing N N 186 
HOH O   H1   sing N N 187 
HOH O   H2   sing N N 188 
ILE N   CA   sing N N 189 
ILE N   H    sing N N 190 
ILE N   H2   sing N N 191 
ILE CA  C    sing N N 192 
ILE CA  CB   sing N N 193 
ILE CA  HA   sing N N 194 
ILE C   O    doub N N 195 
ILE C   OXT  sing N N 196 
ILE CB  CG1  sing N N 197 
ILE CB  CG2  sing N N 198 
ILE CB  HB   sing N N 199 
ILE CG1 CD1  sing N N 200 
ILE CG1 HG12 sing N N 201 
ILE CG1 HG13 sing N N 202 
ILE CG2 HG21 sing N N 203 
ILE CG2 HG22 sing N N 204 
ILE CG2 HG23 sing N N 205 
ILE CD1 HD11 sing N N 206 
ILE CD1 HD12 sing N N 207 
ILE CD1 HD13 sing N N 208 
ILE OXT HXT  sing N N 209 
LEU N   CA   sing N N 210 
LEU N   H    sing N N 211 
LEU N   H2   sing N N 212 
LEU CA  C    sing N N 213 
LEU CA  CB   sing N N 214 
LEU CA  HA   sing N N 215 
LEU C   O    doub N N 216 
LEU C   OXT  sing N N 217 
LEU CB  CG   sing N N 218 
LEU CB  HB2  sing N N 219 
LEU CB  HB3  sing N N 220 
LEU CG  CD1  sing N N 221 
LEU CG  CD2  sing N N 222 
LEU CG  HG   sing N N 223 
LEU CD1 HD11 sing N N 224 
LEU CD1 HD12 sing N N 225 
LEU CD1 HD13 sing N N 226 
LEU CD2 HD21 sing N N 227 
LEU CD2 HD22 sing N N 228 
LEU CD2 HD23 sing N N 229 
LEU OXT HXT  sing N N 230 
LYS N   CA   sing N N 231 
LYS N   H    sing N N 232 
LYS N   H2   sing N N 233 
LYS CA  C    sing N N 234 
LYS CA  CB   sing N N 235 
LYS CA  HA   sing N N 236 
LYS C   O    doub N N 237 
LYS C   OXT  sing N N 238 
LYS CB  CG   sing N N 239 
LYS CB  HB2  sing N N 240 
LYS CB  HB3  sing N N 241 
LYS CG  CD   sing N N 242 
LYS CG  HG2  sing N N 243 
LYS CG  HG3  sing N N 244 
LYS CD  CE   sing N N 245 
LYS CD  HD2  sing N N 246 
LYS CD  HD3  sing N N 247 
LYS CE  NZ   sing N N 248 
LYS CE  HE2  sing N N 249 
LYS CE  HE3  sing N N 250 
LYS NZ  HZ1  sing N N 251 
LYS NZ  HZ2  sing N N 252 
LYS NZ  HZ3  sing N N 253 
LYS OXT HXT  sing N N 254 
MET N   CA   sing N N 255 
MET N   H    sing N N 256 
MET N   H2   sing N N 257 
MET CA  C    sing N N 258 
MET CA  CB   sing N N 259 
MET CA  HA   sing N N 260 
MET C   O    doub N N 261 
MET C   OXT  sing N N 262 
MET CB  CG   sing N N 263 
MET CB  HB2  sing N N 264 
MET CB  HB3  sing N N 265 
MET CG  SD   sing N N 266 
MET CG  HG2  sing N N 267 
MET CG  HG3  sing N N 268 
MET SD  CE   sing N N 269 
MET CE  HE1  sing N N 270 
MET CE  HE2  sing N N 271 
MET CE  HE3  sing N N 272 
MET OXT HXT  sing N N 273 
PHE N   CA   sing N N 274 
PHE N   H    sing N N 275 
PHE N   H2   sing N N 276 
PHE CA  C    sing N N 277 
PHE CA  CB   sing N N 278 
PHE CA  HA   sing N N 279 
PHE C   O    doub N N 280 
PHE C   OXT  sing N N 281 
PHE CB  CG   sing N N 282 
PHE CB  HB2  sing N N 283 
PHE CB  HB3  sing N N 284 
PHE CG  CD1  doub Y N 285 
PHE CG  CD2  sing Y N 286 
PHE CD1 CE1  sing Y N 287 
PHE CD1 HD1  sing N N 288 
PHE CD2 CE2  doub Y N 289 
PHE CD2 HD2  sing N N 290 
PHE CE1 CZ   doub Y N 291 
PHE CE1 HE1  sing N N 292 
PHE CE2 CZ   sing Y N 293 
PHE CE2 HE2  sing N N 294 
PHE CZ  HZ   sing N N 295 
PHE OXT HXT  sing N N 296 
PRO N   CA   sing N N 297 
PRO N   CD   sing N N 298 
PRO N   H    sing N N 299 
PRO CA  C    sing N N 300 
PRO CA  CB   sing N N 301 
PRO CA  HA   sing N N 302 
PRO C   O    doub N N 303 
PRO C   OXT  sing N N 304 
PRO CB  CG   sing N N 305 
PRO CB  HB2  sing N N 306 
PRO CB  HB3  sing N N 307 
PRO CG  CD   sing N N 308 
PRO CG  HG2  sing N N 309 
PRO CG  HG3  sing N N 310 
PRO CD  HD2  sing N N 311 
PRO CD  HD3  sing N N 312 
PRO OXT HXT  sing N N 313 
SER N   CA   sing N N 314 
SER N   H    sing N N 315 
SER N   H2   sing N N 316 
SER CA  C    sing N N 317 
SER CA  CB   sing N N 318 
SER CA  HA   sing N N 319 
SER C   O    doub N N 320 
SER C   OXT  sing N N 321 
SER CB  OG   sing N N 322 
SER CB  HB2  sing N N 323 
SER CB  HB3  sing N N 324 
SER OG  HG   sing N N 325 
SER OXT HXT  sing N N 326 
SO4 S   O1   doub N N 327 
SO4 S   O2   doub N N 328 
SO4 S   O3   sing N N 329 
SO4 S   O4   sing N N 330 
THR N   CA   sing N N 331 
THR N   H    sing N N 332 
THR N   H2   sing N N 333 
THR CA  C    sing N N 334 
THR CA  CB   sing N N 335 
THR CA  HA   sing N N 336 
THR C   O    doub N N 337 
THR C   OXT  sing N N 338 
THR CB  OG1  sing N N 339 
THR CB  CG2  sing N N 340 
THR CB  HB   sing N N 341 
THR OG1 HG1  sing N N 342 
THR CG2 HG21 sing N N 343 
THR CG2 HG22 sing N N 344 
THR CG2 HG23 sing N N 345 
THR OXT HXT  sing N N 346 
TRP N   CA   sing N N 347 
TRP N   H    sing N N 348 
TRP N   H2   sing N N 349 
TRP CA  C    sing N N 350 
TRP CA  CB   sing N N 351 
TRP CA  HA   sing N N 352 
TRP C   O    doub N N 353 
TRP C   OXT  sing N N 354 
TRP CB  CG   sing N N 355 
TRP CB  HB2  sing N N 356 
TRP CB  HB3  sing N N 357 
TRP CG  CD1  doub Y N 358 
TRP CG  CD2  sing Y N 359 
TRP CD1 NE1  sing Y N 360 
TRP CD1 HD1  sing N N 361 
TRP CD2 CE2  doub Y N 362 
TRP CD2 CE3  sing Y N 363 
TRP NE1 CE2  sing Y N 364 
TRP NE1 HE1  sing N N 365 
TRP CE2 CZ2  sing Y N 366 
TRP CE3 CZ3  doub Y N 367 
TRP CE3 HE3  sing N N 368 
TRP CZ2 CH2  doub Y N 369 
TRP CZ2 HZ2  sing N N 370 
TRP CZ3 CH2  sing Y N 371 
TRP CZ3 HZ3  sing N N 372 
TRP CH2 HH2  sing N N 373 
TRP OXT HXT  sing N N 374 
TYR N   CA   sing N N 375 
TYR N   H    sing N N 376 
TYR N   H2   sing N N 377 
TYR CA  C    sing N N 378 
TYR CA  CB   sing N N 379 
TYR CA  HA   sing N N 380 
TYR C   O    doub N N 381 
TYR C   OXT  sing N N 382 
TYR CB  CG   sing N N 383 
TYR CB  HB2  sing N N 384 
TYR CB  HB3  sing N N 385 
TYR CG  CD1  doub Y N 386 
TYR CG  CD2  sing Y N 387 
TYR CD1 CE1  sing Y N 388 
TYR CD1 HD1  sing N N 389 
TYR CD2 CE2  doub Y N 390 
TYR CD2 HD2  sing N N 391 
TYR CE1 CZ   doub Y N 392 
TYR CE1 HE1  sing N N 393 
TYR CE2 CZ   sing Y N 394 
TYR CE2 HE2  sing N N 395 
TYR CZ  OH   sing N N 396 
TYR OH  HH   sing N N 397 
TYR OXT HXT  sing N N 398 
VAL N   CA   sing N N 399 
VAL N   H    sing N N 400 
VAL N   H2   sing N N 401 
VAL CA  C    sing N N 402 
VAL CA  CB   sing N N 403 
VAL CA  HA   sing N N 404 
VAL C   O    doub N N 405 
VAL C   OXT  sing N N 406 
VAL CB  CG1  sing N N 407 
VAL CB  CG2  sing N N 408 
VAL CB  HB   sing N N 409 
VAL CG1 HG11 sing N N 410 
VAL CG1 HG12 sing N N 411 
VAL CG1 HG13 sing N N 412 
VAL CG2 HG21 sing N N 413 
VAL CG2 HG22 sing N N 414 
VAL CG2 HG23 sing N N 415 
VAL OXT HXT  sing N N 416 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                Belgium 
_pdbx_audit_support.grant_number           'BAG 20210875' 
_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 BGC 1 n 
2 BGC 2 n 
2 BGC 3 n 
2 BGC 4 n 
2 BGC 5 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      PDB 
_pdbx_initial_refinement_model.accession_code   1gzj 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9F0M 
_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]   0.013091 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011707 
_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]   0.011197 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LYS A 1 3   ? 14.888  18.247 -15.712 1.00 46.22 ? 2    LYS A N   1 
ATOM   2    C CA  . LYS A 1 3   ? 13.530  17.976 -16.168 1.00 36.85 ? 2    LYS A CA  1 
ATOM   3    C C   . LYS A 1 3   ? 13.194  18.846 -17.373 1.00 33.30 ? 2    LYS A C   1 
ATOM   4    O O   . LYS A 1 3   ? 13.747  19.934 -17.538 1.00 33.81 ? 2    LYS A O   1 
ATOM   5    C CB  . LYS A 1 3   ? 12.527  18.219 -15.032 1.00 31.69 ? 2    LYS A CB  1 
ATOM   6    C CG  . LYS A 1 3   ? 12.812  19.473 -14.228 1.00 45.72 ? 2    LYS A CG  1 
ATOM   7    C CD  . LYS A 1 3   ? 11.778  19.679 -13.136 1.00 45.19 ? 2    LYS A CD  1 
ATOM   8    C CE  . LYS A 1 3   ? 11.958  21.028 -12.507 1.00 47.29 ? 2    LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 3   ? 12.228  22.043 -13.567 1.00 38.44 ? 2    LYS A NZ  1 
ATOM   10   N N   . VAL A 1 4   ? 12.263  18.374 -18.203 1.00 21.18 ? 3    VAL A N   1 
ATOM   11   C CA  . VAL A 1 4   ? 11.869  19.136 -19.383 1.00 22.25 ? 3    VAL A CA  1 
ATOM   12   C C   . VAL A 1 4   ? 11.060  20.371 -18.998 1.00 21.66 ? 3    VAL A C   1 
ATOM   13   O O   . VAL A 1 4   ? 11.250  21.454 -19.564 1.00 23.66 ? 3    VAL A O   1 
ATOM   14   C CB  . VAL A 1 4   ? 11.084  18.234 -20.345 1.00 20.98 ? 3    VAL A CB  1 
ATOM   15   C CG1 . VAL A 1 4   ? 10.499  19.079 -21.459 1.00 20.70 ? 3    VAL A CG1 1 
ATOM   16   C CG2 . VAL A 1 4   ? 11.999  17.154 -20.900 1.00 23.55 ? 3    VAL A CG2 1 
ATOM   17   N N   . PHE A 1 5   ? 10.134  20.225 -18.058 1.00 16.69 ? 4    PHE A N   1 
ATOM   18   C CA  . PHE A 1 5   ? 9.205   21.277 -17.691 1.00 15.21 ? 4    PHE A CA  1 
ATOM   19   C C   . PHE A 1 5   ? 9.476   21.751 -16.271 1.00 16.07 ? 4    PHE A C   1 
ATOM   20   O O   . PHE A 1 5   ? 10.055  21.029 -15.457 1.00 20.20 ? 4    PHE A O   1 
ATOM   21   C CB  . PHE A 1 5   ? 7.760   20.770 -17.772 1.00 16.70 ? 4    PHE A CB  1 
ATOM   22   C CG  . PHE A 1 5   ? 7.335   20.367 -19.161 1.00 14.99 ? 4    PHE A CG  1 
ATOM   23   C CD1 . PHE A 1 5   ? 7.145   21.330 -20.128 1.00 16.38 ? 4    PHE A CD1 1 
ATOM   24   C CD2 . PHE A 1 5   ? 7.101   19.036 -19.485 1.00 15.24 ? 4    PHE A CD2 1 
ATOM   25   C CE1 . PHE A 1 5   ? 6.775   20.974 -21.418 1.00 16.77 ? 4    PHE A CE1 1 
ATOM   26   C CE2 . PHE A 1 5   ? 6.695   18.673 -20.783 1.00 17.90 ? 4    PHE A CE2 1 
ATOM   27   C CZ  . PHE A 1 5   ? 6.528   19.657 -21.732 1.00 17.34 ? 4    PHE A CZ  1 
ATOM   28   N N   . GLN A 1 6   ? 8.995   22.958 -15.970 1.00 15.16 ? 5    GLN A N   1 
ATOM   29   C CA  . GLN A 1 6   ? 9.003   23.416 -14.583 1.00 17.27 ? 5    GLN A CA  1 
ATOM   30   C C   . GLN A 1 6   ? 8.210   22.460 -13.695 1.00 17.66 ? 5    GLN A C   1 
ATOM   31   O O   . GLN A 1 6   ? 8.646   22.119 -12.587 1.00 18.75 ? 5    GLN A O   1 
ATOM   32   C CB  . GLN A 1 6   ? 8.444   24.836 -14.509 1.00 18.81 ? 5    GLN A CB  1 
ATOM   33   C CG  . GLN A 1 6   ? 8.396   25.446 -13.096 1.00 16.74 ? 5    GLN A CG  1 
ATOM   34   C CD  . GLN A 1 6   ? 8.005   26.920 -13.133 1.00 17.68 ? 5    GLN A CD  1 
ATOM   35   O OE1 . GLN A 1 6   ? 7.691   27.466 -14.197 1.00 19.39 ? 5    GLN A OE1 1 
ATOM   36   N NE2 . GLN A 1 6   ? 8.026   27.574 -11.968 1.00 16.16 ? 5    GLN A NE2 1 
ATOM   37   N N   . TRP A 1 7   ? 7.049   22.003 -14.175 1.00 17.31 ? 6    TRP A N   1 
ATOM   38   C CA  . TRP A 1 7   ? 6.133   21.170 -13.409 1.00 16.01 ? 6    TRP A CA  1 
ATOM   39   C C   . TRP A 1 7   ? 5.648   20.008 -14.258 1.00 16.06 ? 6    TRP A C   1 
ATOM   40   O O   . TRP A 1 7   ? 5.245   20.205 -15.410 1.00 16.97 ? 6    TRP A O   1 
ATOM   41   C CB  . TRP A 1 7   ? 4.919   21.975 -12.950 1.00 17.17 ? 6    TRP A CB  1 
ATOM   42   C CG  . TRP A 1 7   ? 5.191   22.996 -11.905 1.00 15.00 ? 6    TRP A CG  1 
ATOM   43   C CD1 . TRP A 1 7   ? 5.759   22.790 -10.669 1.00 14.81 ? 6    TRP A CD1 1 
ATOM   44   C CD2 . TRP A 1 7   ? 4.878   24.392 -11.976 1.00 13.84 ? 6    TRP A CD2 1 
ATOM   45   N NE1 . TRP A 1 7   ? 5.803   23.976 -9.978  1.00 17.41 ? 6    TRP A NE1 1 
ATOM   46   C CE2 . TRP A 1 7   ? 5.270   24.973 -10.751 1.00 15.15 ? 6    TRP A CE2 1 
ATOM   47   C CE3 . TRP A 1 7   ? 4.276   25.207 -12.949 1.00 14.14 ? 6    TRP A CE3 1 
ATOM   48   C CZ2 . TRP A 1 7   ? 5.101   26.337 -10.480 1.00 15.42 ? 6    TRP A CZ2 1 
ATOM   49   C CZ3 . TRP A 1 7   ? 4.126   26.552 -12.691 1.00 16.16 ? 6    TRP A CZ3 1 
ATOM   50   C CH2 . TRP A 1 7   ? 4.528   27.110 -11.460 1.00 15.67 ? 6    TRP A CH2 1 
ATOM   51   N N   . PHE A 1 8   ? 5.656   18.804 -13.691 1.00 15.89 ? 7    PHE A N   1 
ATOM   52   C CA  . PHE A 1 8   ? 5.021   17.676 -14.373 1.00 15.37 ? 7    PHE A CA  1 
ATOM   53   C C   . PHE A 1 8   ? 4.512   16.718 -13.312 1.00 17.15 ? 7    PHE A C   1 
ATOM   54   O O   . PHE A 1 8   ? 5.279   16.290 -12.443 1.00 18.89 ? 7    PHE A O   1 
ATOM   55   C CB  . PHE A 1 8   ? 5.999   16.986 -15.331 1.00 17.81 ? 7    PHE A CB  1 
ATOM   56   C CG  . PHE A 1 8   ? 5.327   16.071 -16.308 1.00 19.13 ? 7    PHE A CG  1 
ATOM   57   C CD1 . PHE A 1 8   ? 5.108   14.744 -16.000 1.00 26.13 ? 7    PHE A CD1 1 
ATOM   58   C CD2 . PHE A 1 8   ? 4.883   16.549 -17.527 1.00 20.58 ? 7    PHE A CD2 1 
ATOM   59   C CE1 . PHE A 1 8   ? 4.471   13.905 -16.903 1.00 28.38 ? 7    PHE A CE1 1 
ATOM   60   C CE2 . PHE A 1 8   ? 4.238   15.716 -18.423 1.00 22.18 ? 7    PHE A CE2 1 
ATOM   61   C CZ  . PHE A 1 8   ? 4.033   14.401 -18.116 1.00 20.51 ? 7    PHE A CZ  1 
ATOM   62   N N   . GLY A 1 9   ? 3.223   16.400 -13.349 1.00 17.39 ? 8    GLY A N   1 
ATOM   63   C CA  . GLY A 1 9   ? 2.676   15.626 -12.251 1.00 15.93 ? 8    GLY A CA  1 
ATOM   64   C C   . GLY A 1 9   ? 1.277   15.102 -12.481 1.00 18.76 ? 8    GLY A C   1 
ATOM   65   O O   . GLY A 1 9   ? 0.905   14.803 -13.621 1.00 17.13 ? 8    GLY A O   1 
ATOM   66   N N   . SER A 1 10  ? 0.494   14.979 -11.407 1.00 19.11 ? 9    SER A N   1 
ATOM   67   C CA  . SER A 1 10  ? -0.798  14.317 -11.505 1.00 16.77 ? 9    SER A CA  1 
ATOM   68   C C   . SER A 1 10  ? -1.810  14.968 -10.568 1.00 15.34 ? 9    SER A C   1 
ATOM   69   O O   . SER A 1 10  ? -1.468  15.443 -9.476  1.00 16.46 ? 9    SER A O   1 
ATOM   70   C CB  . SER A 1 10  ? -0.659  12.817 -11.187 1.00 17.34 ? 9    SER A CB  1 
ATOM   71   O OG  . SER A 1 10  ? -1.887  12.117 -11.361 1.00 19.78 ? 9    SER A OG  1 
ATOM   72   N N   . ASN A 1 11  ? -3.062  14.984 -11.017 1.00 15.73 ? 10   ASN A N   1 
ATOM   73   C CA  . ASN A 1 11  ? -4.165  15.209 -10.104 1.00 16.13 ? 10   ASN A CA  1 
ATOM   74   C C   . ASN A 1 11  ? -4.286  14.055 -9.109  1.00 19.99 ? 10   ASN A C   1 
ATOM   75   O O   . ASN A 1 11  ? -3.954  12.902 -9.406  1.00 18.74 ? 10   ASN A O   1 
ATOM   76   C CB  . ASN A 1 11  ? -5.466  15.384 -10.880 1.00 17.72 ? 10   ASN A CB  1 
ATOM   77   C CG  . ASN A 1 11  ? -5.555  16.743 -11.558 1.00 15.68 ? 10   ASN A CG  1 
ATOM   78   O OD1 . ASN A 1 11  ? -6.053  17.709 -10.976 1.00 15.10 ? 10   ASN A OD1 1 
ATOM   79   N ND2 . ASN A 1 11  ? -5.066  16.826 -12.790 1.00 14.88 ? 10   ASN A ND2 1 
ATOM   80   N N   . GLU A 1 12  ? -4.747  14.387 -7.903  1.00 16.75 ? 11   GLU A N   1 
ATOM   81   C CA  . GLU A 1 12  ? -4.937  13.428 -6.808  1.00 15.84 ? 11   GLU A CA  1 
ATOM   82   C C   . GLU A 1 12  ? -6.381  13.602 -6.359  1.00 16.75 ? 11   GLU A C   1 
ATOM   83   O O   . GLU A 1 12  ? -6.668  14.374 -5.442  1.00 19.08 ? 11   GLU A O   1 
ATOM   84   C CB  . GLU A 1 12  ? -3.945  13.665 -5.683  1.00 16.14 ? 11   GLU A CB  1 
ATOM   85   C CG  . GLU A 1 12  ? -2.548  13.197 -6.038  1.00 18.80 ? 11   GLU A CG  1 
ATOM   86   C CD  . GLU A 1 12  ? -2.401  11.685 -5.940  1.00 23.22 ? 11   GLU A CD  1 
ATOM   87   O OE1 . GLU A 1 12  ? -3.310  11.029 -5.381  1.00 18.71 ? 11   GLU A OE1 1 
ATOM   88   O OE2 . GLU A 1 12  ? -1.368  11.155 -6.416  1.00 20.57 ? 11   GLU A OE2 1 
ATOM   89   N N   . SER A 1 13  ? -7.270  12.876 -7.027  1.00 17.99 ? 12   SER A N   1 
ATOM   90   C CA  A SER A 1 13  ? -8.707  13.066 -6.930  0.53 19.67 ? 12   SER A CA  1 
ATOM   91   C CA  B SER A 1 13  ? -8.706  13.076 -6.912  0.47 19.66 ? 12   SER A CA  1 
ATOM   92   C C   . SER A 1 13  ? -9.314  12.150 -5.874  1.00 24.97 ? 12   SER A C   1 
ATOM   93   O O   . SER A 1 13  ? -8.794  11.070 -5.591  1.00 22.23 ? 12   SER A O   1 
ATOM   94   C CB  A SER A 1 13  ? -9.338  12.797 -8.299  0.53 17.25 ? 12   SER A CB  1 
ATOM   95   C CB  B SER A 1 13  ? -9.387  12.833 -8.256  0.47 17.29 ? 12   SER A CB  1 
ATOM   96   O OG  A SER A 1 13  ? -10.744 12.910 -8.271  0.53 19.82 ? 12   SER A OG  1 
ATOM   97   O OG  B SER A 1 13  ? -8.869  13.700 -9.235  0.47 18.42 ? 12   SER A OG  1 
ATOM   98   N N   . GLY A 1 14  ? -10.437 12.591 -5.308  1.00 17.74 ? 13   GLY A N   1 
ATOM   99   C CA  . GLY A 1 14  ? -11.149 11.803 -4.325  1.00 21.48 ? 13   GLY A CA  1 
ATOM   100  C C   . GLY A 1 14  ? -11.916 12.648 -3.327  1.00 20.65 ? 13   GLY A C   1 
ATOM   101  O O   . GLY A 1 14  ? -13.033 12.282 -2.938  1.00 19.23 ? 13   GLY A O   1 
ATOM   102  N N   . ALA A 1 15  ? -11.339 13.772 -2.897  1.00 18.91 ? 14   ALA A N   1 
ATOM   103  C CA  . ALA A 1 15  ? -11.999 14.573 -1.868  1.00 16.10 ? 14   ALA A CA  1 
ATOM   104  C C   . ALA A 1 15  ? -13.232 15.282 -2.405  1.00 19.67 ? 14   ALA A C   1 
ATOM   105  O O   . ALA A 1 15  ? -14.076 15.726 -1.619  1.00 20.11 ? 14   ALA A O   1 
ATOM   106  C CB  . ALA A 1 15  ? -11.012 15.578 -1.273  1.00 17.13 ? 14   ALA A CB  1 
ATOM   107  N N   . GLU A 1 16  ? -13.369 15.365 -3.728  1.00 19.65 ? 15   GLU A N   1 
ATOM   108  C CA  . GLU A 1 16  ? -14.508 15.984 -4.382  1.00 23.03 ? 15   GLU A CA  1 
ATOM   109  C C   . GLU A 1 16  ? -15.519 14.952 -4.869  1.00 21.71 ? 15   GLU A C   1 
ATOM   110  O O   . GLU A 1 16  ? -16.491 15.318 -5.530  1.00 24.17 ? 15   GLU A O   1 
ATOM   111  C CB  . GLU A 1 16  ? -14.016 16.863 -5.547  1.00 16.56 ? 15   GLU A CB  1 
ATOM   112  C CG  . GLU A 1 16  ? -13.806 16.160 -6.912  1.00 21.27 ? 15   GLU A CG  1 
ATOM   113  C CD  . GLU A 1 16  ? -12.595 15.227 -6.984  1.00 22.45 ? 15   GLU A CD  1 
ATOM   114  O OE1 . GLU A 1 16  ? -11.982 14.903 -5.928  1.00 18.06 ? 15   GLU A OE1 1 
ATOM   115  O OE2 . GLU A 1 16  ? -12.258 14.803 -8.122  1.00 20.28 ? 15   GLU A OE2 1 
ATOM   116  N N   . PHE A 1 17  ? -15.317 13.678 -4.541  1.00 19.49 ? 16   PHE A N   1 
ATOM   117  C CA  . PHE A 1 17  ? -16.198 12.618 -5.026  1.00 25.19 ? 16   PHE A CA  1 
ATOM   118  C C   . PHE A 1 17  ? -17.569 12.698 -4.362  1.00 26.65 ? 16   PHE A C   1 
ATOM   119  O O   . PHE A 1 17  ? -17.741 13.291 -3.291  1.00 23.99 ? 16   PHE A O   1 
ATOM   120  C CB  . PHE A 1 17  ? -15.601 11.237 -4.747  1.00 22.48 ? 16   PHE A CB  1 
ATOM   121  C CG  . PHE A 1 17  ? -14.611 10.769 -5.775  1.00 23.88 ? 16   PHE A CG  1 
ATOM   122  C CD1 . PHE A 1 17  ? -14.020 11.661 -6.657  1.00 26.91 ? 16   PHE A CD1 1 
ATOM   123  C CD2 . PHE A 1 17  ? -14.269 9.429  -5.856  1.00 25.73 ? 16   PHE A CD2 1 
ATOM   124  C CE1 . PHE A 1 17  ? -13.106 11.210 -7.599  1.00 22.73 ? 16   PHE A CE1 1 
ATOM   125  C CE2 . PHE A 1 17  ? -13.358 8.971  -6.800  1.00 30.74 ? 16   PHE A CE2 1 
ATOM   126  C CZ  . PHE A 1 17  ? -12.775 9.867  -7.678  1.00 22.85 ? 16   PHE A CZ  1 
ATOM   127  N N   . GLY A 1 18  ? -18.546 12.047 -4.993  1.00 30.22 ? 17   GLY A N   1 
ATOM   128  C CA  . GLY A 1 18  ? -19.897 11.998 -4.459  1.00 35.12 ? 17   GLY A CA  1 
ATOM   129  C C   . GLY A 1 18  ? -20.463 13.367 -4.140  1.00 27.48 ? 17   GLY A C   1 
ATOM   130  O O   . GLY A 1 18  ? -21.004 13.587 -3.049  1.00 30.63 ? 17   GLY A O   1 
ATOM   131  N N   . SER A 1 19  ? -20.341 14.299 -5.088  1.00 29.13 ? 18   SER A N   1 
ATOM   132  C CA  . SER A 1 19  ? -20.634 15.707 -4.834  1.00 31.09 ? 18   SER A CA  1 
ATOM   133  C C   . SER A 1 19  ? -22.105 15.984 -4.555  1.00 39.38 ? 18   SER A C   1 
ATOM   134  O O   . SER A 1 19  ? -22.428 17.078 -4.079  1.00 37.59 ? 18   SER A O   1 
ATOM   135  C CB  . SER A 1 19  ? -20.178 16.563 -6.016  1.00 27.78 ? 18   SER A CB  1 
ATOM   136  O OG  . SER A 1 19  ? -20.768 16.117 -7.228  1.00 40.54 ? 18   SER A OG  1 
ATOM   137  N N   . GLN A 1 20  ? -23.002 15.044 -4.852  1.00 38.67 ? 19   GLN A N   1 
ATOM   138  C CA  . GLN A 1 20  ? -24.412 15.249 -4.561  1.00 33.63 ? 19   GLN A CA  1 
ATOM   139  C C   . GLN A 1 20  ? -24.729 15.058 -3.087  1.00 41.64 ? 19   GLN A C   1 
ATOM   140  O O   . GLN A 1 20  ? -25.840 15.384 -2.655  1.00 45.01 ? 19   GLN A O   1 
ATOM   141  C CB  . GLN A 1 20  ? -25.266 14.314 -5.433  1.00 49.60 ? 19   GLN A CB  1 
ATOM   142  C CG  . GLN A 1 20  ? -25.303 12.836 -5.022  1.00 54.81 ? 19   GLN A CG  1 
ATOM   143  C CD  . GLN A 1 20  ? -23.976 12.091 -5.202  1.00 48.94 ? 19   GLN A CD  1 
ATOM   144  O OE1 . GLN A 1 20  ? -23.099 12.515 -5.959  1.00 46.94 ? 19   GLN A OE1 1 
ATOM   145  N NE2 . GLN A 1 20  ? -23.833 10.968 -4.500  1.00 49.11 ? 19   GLN A NE2 1 
ATOM   146  N N   . ASN A 1 21  ? -23.771 14.575 -2.305  1.00 32.13 ? 20   ASN A N   1 
ATOM   147  C CA  . ASN A 1 21  ? -23.931 14.344 -0.876  1.00 32.37 ? 20   ASN A CA  1 
ATOM   148  C C   . ASN A 1 21  ? -23.106 15.417 -0.166  1.00 34.97 ? 20   ASN A C   1 
ATOM   149  O O   . ASN A 1 21  ? -21.880 15.307 -0.083  1.00 30.76 ? 20   ASN A O   1 
ATOM   150  C CB  . ASN A 1 21  ? -23.484 12.928 -0.506  1.00 36.07 ? 20   ASN A CB  1 
ATOM   151  C CG  . ASN A 1 21  ? -24.473 11.844 -0.973  1.00 47.41 ? 20   ASN A CG  1 
ATOM   152  O OD1 . ASN A 1 21  ? -24.541 10.757 -0.400  1.00 50.76 ? 20   ASN A OD1 1 
ATOM   153  N ND2 . ASN A 1 21  ? -25.242 12.148 -2.002  1.00 51.58 ? 20   ASN A ND2 1 
ATOM   154  N N   . LEU A 1 22  ? -23.781 16.467 0.313   1.00 33.98 ? 21   LEU A N   1 
ATOM   155  C CA  . LEU A 1 22  ? -23.184 17.571 1.055   1.00 27.66 ? 21   LEU A CA  1 
ATOM   156  C C   . LEU A 1 22  ? -23.817 17.652 2.436   1.00 37.34 ? 21   LEU A C   1 
ATOM   157  O O   . LEU A 1 22  ? -25.048 17.761 2.536   1.00 35.32 ? 21   LEU A O   1 
ATOM   158  C CB  . LEU A 1 22  ? -23.374 18.919 0.320   1.00 32.00 ? 21   LEU A CB  1 
ATOM   159  C CG  . LEU A 1 22  ? -22.492 19.195 -0.899  1.00 37.07 ? 21   LEU A CG  1 
ATOM   160  C CD1 . LEU A 1 22  ? -22.808 20.548 -1.539  1.00 29.89 ? 21   LEU A CD1 1 
ATOM   161  C CD2 . LEU A 1 22  ? -21.030 19.132 -0.481  1.00 34.29 ? 21   LEU A CD2 1 
ATOM   162  N N   . PRO A 1 23  ? -23.028 17.628 3.523   1.00 31.95 ? 22   PRO A N   1 
ATOM   163  C CA  . PRO A 1 23  ? -21.555 17.571 3.571   1.00 25.17 ? 22   PRO A CA  1 
ATOM   164  C C   . PRO A 1 23  ? -20.958 16.257 3.084   1.00 27.36 ? 22   PRO A C   1 
ATOM   165  O O   . PRO A 1 23  ? -19.789 16.217 2.695   1.00 24.07 ? 22   PRO A O   1 
ATOM   166  C CB  . PRO A 1 23  ? -21.241 17.794 5.064   1.00 27.31 ? 22   PRO A CB  1 
ATOM   167  C CG  . PRO A 1 23  ? -22.518 17.477 5.807   1.00 35.78 ? 22   PRO A CG  1 
ATOM   168  C CD  . PRO A 1 23  ? -23.622 17.849 4.859   1.00 29.38 ? 22   PRO A CD  1 
ATOM   169  N N   . GLY A 1 24  ? -21.714 15.163 3.089   1.00 28.49 ? 23   GLY A N   1 
ATOM   170  C CA  . GLY A 1 24  ? -21.156 13.862 2.792   1.00 31.97 ? 23   GLY A CA  1 
ATOM   171  C C   . GLY A 1 24  ? -20.308 13.366 3.945   1.00 29.09 ? 23   GLY A C   1 
ATOM   172  O O   . GLY A 1 24  ? -20.045 14.071 4.926   1.00 29.65 ? 23   GLY A O   1 
ATOM   173  N N   . VAL A 1 25  ? -19.865 12.115 3.827   1.00 23.68 ? 24   VAL A N   1 
ATOM   174  C CA  . VAL A 1 25  ? -19.175 11.432 4.914   1.00 26.62 ? 24   VAL A CA  1 
ATOM   175  C C   . VAL A 1 25  ? -17.843 10.905 4.401   1.00 30.54 ? 24   VAL A C   1 
ATOM   176  O O   . VAL A 1 25  ? -17.806 10.150 3.422   1.00 26.86 ? 24   VAL A O   1 
ATOM   177  C CB  . VAL A 1 25  ? -20.029 10.289 5.488   1.00 35.66 ? 24   VAL A CB  1 
ATOM   178  C CG1 . VAL A 1 25  ? -19.268 9.567  6.577   1.00 39.06 ? 24   VAL A CG1 1 
ATOM   179  C CG2 . VAL A 1 25  ? -21.348 10.838 6.023   1.00 37.14 ? 24   VAL A CG2 1 
ATOM   180  N N   . GLU A 1 26  ? -16.757 11.301 5.059   1.00 25.63 ? 25   GLU A N   1 
ATOM   181  C CA  . GLU A 1 26  ? -15.438 10.819 4.676   1.00 28.11 ? 25   GLU A CA  1 
ATOM   182  C C   . GLU A 1 26  ? -15.378 9.303  4.815   1.00 31.62 ? 25   GLU A C   1 
ATOM   183  O O   . GLU A 1 26  ? -15.816 8.735  5.818   1.00 30.40 ? 25   GLU A O   1 
ATOM   184  C CB  . GLU A 1 26  ? -14.367 11.479 5.543   1.00 27.19 ? 25   GLU A CB  1 
ATOM   185  C CG  . GLU A 1 26  ? -12.910 11.173 5.150   1.00 26.91 ? 25   GLU A CG  1 
ATOM   186  C CD  . GLU A 1 26  ? -12.444 9.799  5.604   1.00 37.71 ? 25   GLU A CD  1 
ATOM   187  O OE1 . GLU A 1 26  ? -12.829 9.373  6.711   1.00 35.37 ? 25   GLU A OE1 1 
ATOM   188  O OE2 . GLU A 1 26  ? -11.709 9.130  4.845   1.00 31.61 ? 25   GLU A OE2 1 
ATOM   189  N N   . GLY A 1 27  ? -14.814 8.646  3.806   1.00 26.72 ? 26   GLY A N   1 
ATOM   190  C CA  . GLY A 1 27  ? -14.744 7.204  3.793   1.00 30.76 ? 26   GLY A CA  1 
ATOM   191  C C   . GLY A 1 27  ? -15.962 6.530  3.208   1.00 33.57 ? 26   GLY A C   1 
ATOM   192  O O   . GLY A 1 27  ? -15.948 5.309  3.027   1.00 31.38 ? 26   GLY A O   1 
ATOM   193  N N   . LYS A 1 28  ? -17.018 7.288  2.928   1.00 28.29 ? 27   LYS A N   1 
ATOM   194  C CA  A LYS A 1 28  ? -18.220 6.769  2.290   0.72 33.78 ? 27   LYS A CA  1 
ATOM   195  C CA  B LYS A 1 28  ? -18.222 6.771  2.292   0.28 33.80 ? 27   LYS A CA  1 
ATOM   196  C C   . LYS A 1 28  ? -18.537 7.498  0.995   1.00 32.12 ? 27   LYS A C   1 
ATOM   197  O O   . LYS A 1 28  ? -18.727 6.855  -0.044  1.00 32.04 ? 27   LYS A O   1 
ATOM   198  C CB  A LYS A 1 28  ? -19.414 6.859  3.259   0.72 36.41 ? 27   LYS A CB  1 
ATOM   199  C CB  B LYS A 1 28  ? -19.412 6.873  3.261   0.28 36.43 ? 27   LYS A CB  1 
ATOM   200  C CG  A LYS A 1 28  ? -20.745 6.435  2.652   0.72 41.91 ? 27   LYS A CG  1 
ATOM   201  C CG  B LYS A 1 28  ? -20.738 6.410  2.678   0.28 41.84 ? 27   LYS A CG  1 
ATOM   202  C CD  A LYS A 1 28  ? -21.898 6.677  3.619   0.72 47.54 ? 27   LYS A CD  1 
ATOM   203  C CD  B LYS A 1 28  ? -21.874 6.618  3.669   0.28 47.33 ? 27   LYS A CD  1 
ATOM   204  C CE  A LYS A 1 28  ? -23.232 6.255  3.015   0.72 48.22 ? 27   LYS A CE  1 
ATOM   205  C CE  B LYS A 1 28  ? -23.198 6.119  3.110   0.28 48.04 ? 27   LYS A CE  1 
ATOM   206  N NZ  A LYS A 1 28  ? -23.275 4.796  2.713   0.72 53.90 ? 27   LYS A NZ  1 
ATOM   207  N NZ  B LYS A 1 28  ? -23.578 6.829  1.858   0.28 49.31 ? 27   LYS A NZ  1 
ATOM   208  N N   . ASP A 1 29  ? -18.588 8.828  1.021   1.00 26.89 ? 28   ASP A N   1 
ATOM   209  C CA  . ASP A 1 29  ? -18.854 9.610  -0.179  1.00 25.01 ? 28   ASP A CA  1 
ATOM   210  C C   . ASP A 1 29  ? -17.593 10.128 -0.846  1.00 25.11 ? 28   ASP A C   1 
ATOM   211  O O   . ASP A 1 29  ? -17.591 10.337 -2.062  1.00 25.09 ? 28   ASP A O   1 
ATOM   212  C CB  . ASP A 1 29  ? -19.763 10.795 0.153   1.00 32.13 ? 28   ASP A CB  1 
ATOM   213  C CG  . ASP A 1 29  ? -21.091 10.357 0.727   1.00 31.74 ? 28   ASP A CG  1 
ATOM   214  O OD1 . ASP A 1 29  ? -21.835 9.659  0.005   1.00 37.31 ? 28   ASP A OD1 1 
ATOM   215  O OD2 . ASP A 1 29  ? -21.375 10.695 1.897   1.00 31.42 ? 28   ASP A OD2 1 
ATOM   216  N N   . TYR A 1 30  ? -16.527 10.337 -0.083  1.00 25.11 ? 29   TYR A N   1 
ATOM   217  C CA  . TYR A 1 30  ? -15.296 10.895 -0.619  1.00 24.87 ? 29   TYR A CA  1 
ATOM   218  C C   . TYR A 1 30  ? -14.133 10.374 0.211   1.00 20.36 ? 29   TYR A C   1 
ATOM   219  O O   . TYR A 1 30  ? -14.316 9.819  1.299   1.00 24.78 ? 29   TYR A O   1 
ATOM   220  C CB  . TYR A 1 30  ? -15.329 12.433 -0.616  1.00 22.62 ? 29   TYR A CB  1 
ATOM   221  C CG  . TYR A 1 30  ? -15.475 13.049 0.766   1.00 22.97 ? 29   TYR A CG  1 
ATOM   222  C CD1 . TYR A 1 30  ? -14.364 13.241 1.590   1.00 19.98 ? 29   TYR A CD1 1 
ATOM   223  C CD2 . TYR A 1 30  ? -16.724 13.442 1.243   1.00 21.73 ? 29   TYR A CD2 1 
ATOM   224  C CE1 . TYR A 1 30  ? -14.495 13.802 2.867   1.00 22.43 ? 29   TYR A CE1 1 
ATOM   225  C CE2 . TYR A 1 30  ? -16.867 14.007 2.507   1.00 25.98 ? 29   TYR A CE2 1 
ATOM   226  C CZ  . TYR A 1 30  ? -15.745 14.191 3.312   1.00 23.58 ? 29   TYR A CZ  1 
ATOM   227  O OH  . TYR A 1 30  ? -15.869 14.751 4.571   1.00 24.58 ? 29   TYR A OH  1 
ATOM   228  N N   . ILE A 1 31  ? -12.918 10.586 -0.299  1.00 20.92 ? 30   ILE A N   1 
ATOM   229  C CA  . ILE A 1 31  ? -11.712 10.140 0.393   1.00 22.54 ? 30   ILE A CA  1 
ATOM   230  C C   . ILE A 1 31  ? -10.556 11.043 -0.023  1.00 22.14 ? 30   ILE A C   1 
ATOM   231  O O   . ILE A 1 31  ? -10.566 11.628 -1.104  1.00 20.96 ? 30   ILE A O   1 
ATOM   232  C CB  . ILE A 1 31  ? -11.422 8.652  0.078   1.00 26.14 ? 30   ILE A CB  1 
ATOM   233  C CG1 . ILE A 1 31  ? -10.375 8.082  1.032   1.00 27.50 ? 30   ILE A CG1 1 
ATOM   234  C CG2 . ILE A 1 31  ? -10.981 8.507  -1.370  1.00 25.41 ? 30   ILE A CG2 1 
ATOM   235  C CD1 . ILE A 1 31  ? -10.241 6.583  0.972   1.00 37.02 ? 30   ILE A CD1 1 
ATOM   236  N N   . TRP A 1 32  ? -9.555  11.159 0.840   1.00 21.62 ? 31   TRP A N   1 
ATOM   237  C CA  . TRP A 1 32  ? -8.396  11.985 0.530   1.00 23.01 ? 31   TRP A CA  1 
ATOM   238  C C   . TRP A 1 32  ? -7.267  11.144 -0.063  1.00 20.97 ? 31   TRP A C   1 
ATOM   239  O O   . TRP A 1 32  ? -7.256  9.914  0.081   1.00 21.97 ? 31   TRP A O   1 
ATOM   240  C CB  . TRP A 1 32  ? -7.928  12.715 1.798   1.00 19.42 ? 31   TRP A CB  1 
ATOM   241  C CG  . TRP A 1 32  ? -8.883  13.805 2.183   1.00 18.18 ? 31   TRP A CG  1 
ATOM   242  C CD1 . TRP A 1 32  ? -9.975  13.682 3.005   1.00 22.05 ? 31   TRP A CD1 1 
ATOM   243  C CD2 . TRP A 1 32  ? -8.876  15.169 1.727   1.00 19.12 ? 31   TRP A CD2 1 
ATOM   244  N NE1 . TRP A 1 32  ? -10.632 14.886 3.101   1.00 19.05 ? 31   TRP A NE1 1 
ATOM   245  C CE2 . TRP A 1 32  ? -9.980  15.815 2.330   1.00 19.33 ? 31   TRP A CE2 1 
ATOM   246  C CE3 . TRP A 1 32  ? -8.039  15.911 0.881   1.00 17.37 ? 31   TRP A CE3 1 
ATOM   247  C CZ2 . TRP A 1 32  ? -10.267 17.164 2.117   1.00 18.31 ? 31   TRP A CZ2 1 
ATOM   248  C CZ3 . TRP A 1 32  ? -8.339  17.253 0.648   1.00 18.41 ? 31   TRP A CZ3 1 
ATOM   249  C CH2 . TRP A 1 32  ? -9.447  17.865 1.262   1.00 16.91 ? 31   TRP A CH2 1 
ATOM   250  N N   . PRO A 1 33  ? -6.310  11.779 -0.755  1.00 19.74 ? 32   PRO A N   1 
ATOM   251  C CA  . PRO A 1 33  ? -5.236  11.021 -1.412  1.00 21.40 ? 32   PRO A CA  1 
ATOM   252  C C   . PRO A 1 33  ? -4.387  10.256 -0.412  1.00 23.77 ? 32   PRO A C   1 
ATOM   253  O O   . PRO A 1 33  ? -4.295  10.607 0.762   1.00 22.93 ? 32   PRO A O   1 
ATOM   254  C CB  . PRO A 1 33  ? -4.411  12.107 -2.120  1.00 17.49 ? 32   PRO A CB  1 
ATOM   255  C CG  . PRO A 1 33  ? -5.405  13.208 -2.401  1.00 18.63 ? 32   PRO A CG  1 
ATOM   256  C CD  . PRO A 1 33  ? -6.316  13.192 -1.182  1.00 16.11 ? 32   PRO A CD  1 
ATOM   257  N N   . ASP A 1 34  ? -3.748  9.202  -0.911  1.00 19.34 ? 33   ASP A N   1 
ATOM   258  C CA  . ASP A 1 34  ? -2.893  8.351  -0.093  1.00 21.27 ? 33   ASP A CA  1 
ATOM   259  C C   . ASP A 1 34  ? -1.463  8.868  -0.159  1.00 25.35 ? 33   ASP A C   1 
ATOM   260  O O   . ASP A 1 34  ? -0.838  8.798  -1.230  1.00 23.01 ? 33   ASP A O   1 
ATOM   261  C CB  . ASP A 1 34  ? -2.966  6.908  -0.582  1.00 24.13 ? 33   ASP A CB  1 
ATOM   262  C CG  . ASP A 1 34  ? -2.145  5.945  0.271   1.00 32.68 ? 33   ASP A CG  1 
ATOM   263  O OD1 . ASP A 1 34  ? -1.351  6.396  1.126   1.00 30.87 ? 33   ASP A OD1 1 
ATOM   264  O OD2 . ASP A 1 34  ? -2.315  4.722  0.083   1.00 36.75 ? 33   ASP A OD2 1 
ATOM   265  N N   . PRO A 1 35  ? -0.891  9.346  0.943   1.00 23.49 ? 34   PRO A N   1 
ATOM   266  C CA  . PRO A 1 35  ? 0.486   9.853  0.884   1.00 25.36 ? 34   PRO A CA  1 
ATOM   267  C C   . PRO A 1 35  ? 1.491   8.814  0.435   1.00 25.96 ? 34   PRO A C   1 
ATOM   268  O O   . PRO A 1 35  ? 2.517   9.186  -0.142  1.00 27.30 ? 34   PRO A O   1 
ATOM   269  C CB  . PRO A 1 35  ? 0.757   10.303 2.327   1.00 29.15 ? 34   PRO A CB  1 
ATOM   270  C CG  . PRO A 1 35  ? -0.603  10.532 2.915   1.00 38.09 ? 34   PRO A CG  1 
ATOM   271  C CD  . PRO A 1 35  ? -1.482  9.493  2.283   1.00 27.91 ? 34   PRO A CD  1 
ATOM   272  N N   . ASN A 1 36  ? 1.246   7.524  0.678   1.00 25.26 ? 35   ASN A N   1 
ATOM   273  C CA  A ASN A 1 36  ? 2.213   6.513  0.267   0.62 27.43 ? 35   ASN A CA  1 
ATOM   274  C CA  B ASN A 1 36  ? 2.221   6.522  0.263   0.38 27.48 ? 35   ASN A CA  1 
ATOM   275  C C   . ASN A 1 36  ? 2.274   6.392  -1.252  1.00 29.50 ? 35   ASN A C   1 
ATOM   276  O O   . ASN A 1 36  ? 3.355   6.208  -1.822  1.00 29.57 ? 35   ASN A O   1 
ATOM   277  C CB  A ASN A 1 36  ? 1.871   5.168  0.907   0.62 33.35 ? 35   ASN A CB  1 
ATOM   278  C CB  B ASN A 1 36  ? 1.920   5.165  0.888   0.38 33.30 ? 35   ASN A CB  1 
ATOM   279  C CG  A ASN A 1 36  ? 1.930   5.212  2.423   0.62 37.13 ? 35   ASN A CG  1 
ATOM   280  C CG  B ASN A 1 36  ? 2.812   4.073  0.328   0.38 31.43 ? 35   ASN A CG  1 
ATOM   281  O OD1 A ASN A 1 36  ? 2.817   5.839  3.007   0.62 35.48 ? 35   ASN A OD1 1 
ATOM   282  O OD1 B ASN A 1 36  ? 4.019   4.065  0.568   0.38 34.53 ? 35   ASN A OD1 1 
ATOM   283  N ND2 A ASN A 1 36  ? 0.979   4.549  3.069   0.62 39.40 ? 35   ASN A ND2 1 
ATOM   284  N ND2 B ASN A 1 36  ? 2.229   3.163  -0.445  0.38 33.28 ? 35   ASN A ND2 1 
ATOM   285  N N   . THR A 1 37  ? 1.124   6.486  -1.935  1.00 25.96 ? 36   THR A N   1 
ATOM   286  C CA  . THR A 1 37  ? 1.208   6.381  -3.390  1.00 22.29 ? 36   THR A CA  1 
ATOM   287  C C   . THR A 1 37  ? 1.660   7.689  -4.015  1.00 23.63 ? 36   THR A C   1 
ATOM   288  O O   . THR A 1 37  ? 2.275   7.669  -5.086  1.00 25.04 ? 36   THR A O   1 
ATOM   289  C CB  . THR A 1 37  ? -0.119  5.935  -4.016  1.00 24.26 ? 36   THR A CB  1 
ATOM   290  O OG1 . THR A 1 37  ? -1.136  6.902  -3.744  1.00 25.05 ? 36   THR A OG1 1 
ATOM   291  C CG2 . THR A 1 37  ? -0.534  4.548  -3.496  1.00 30.18 ? 36   THR A CG2 1 
ATOM   292  N N   . ILE A 1 38  ? 1.391   8.824  -3.357  1.00 23.95 ? 37   ILE A N   1 
ATOM   293  C CA  . ILE A 1 38  ? 2.006   10.084 -3.773  1.00 22.65 ? 37   ILE A CA  1 
ATOM   294  C C   . ILE A 1 38  ? 3.524   9.960  -3.740  1.00 25.91 ? 37   ILE A C   1 
ATOM   295  O O   . ILE A 1 38  ? 4.210   10.364 -4.685  1.00 24.31 ? 37   ILE A O   1 
ATOM   296  C CB  . ILE A 1 38  ? 1.511   11.251 -2.898  1.00 24.99 ? 37   ILE A CB  1 
ATOM   297  C CG1 . ILE A 1 38  ? 0.045   11.553 -3.218  1.00 24.35 ? 37   ILE A CG1 1 
ATOM   298  C CG2 . ILE A 1 38  ? 2.348   12.499 -3.149  1.00 19.86 ? 37   ILE A CG2 1 
ATOM   299  C CD1 . ILE A 1 38  ? -0.585  12.611 -2.323  1.00 22.86 ? 37   ILE A CD1 1 
ATOM   300  N N   . ASP A 1 39  ? 4.065   9.379  -2.657  1.00 25.71 ? 38   ASP A N   1 
ATOM   301  C CA  . ASP A 1 39  ? 5.507   9.131  -2.566  1.00 21.12 ? 38   ASP A CA  1 
ATOM   302  C C   . ASP A 1 39  ? 6.015   8.345  -3.768  1.00 21.82 ? 38   ASP A C   1 
ATOM   303  O O   . ASP A 1 39  ? 7.096   8.633  -4.300  1.00 26.27 ? 38   ASP A O   1 
ATOM   304  C CB  . ASP A 1 39  ? 5.847   8.360  -1.286  1.00 25.13 ? 38   ASP A CB  1 
ATOM   305  C CG  . ASP A 1 39  ? 5.771   9.215  -0.034  1.00 34.53 ? 38   ASP A CG  1 
ATOM   306  O OD1 . ASP A 1 39  ? 5.595   10.443 -0.149  1.00 34.52 ? 38   ASP A OD1 1 
ATOM   307  O OD2 . ASP A 1 39  ? 5.879   8.646  1.077   1.00 39.14 ? 38   ASP A OD2 1 
ATOM   308  N N   . THR A 1 40  ? 5.267   7.323  -4.186  1.00 23.75 ? 39   THR A N   1 
ATOM   309  C CA  . THR A 1 40  ? 5.684   6.518  -5.333  1.00 24.76 ? 39   THR A CA  1 
ATOM   310  C C   . THR A 1 40  ? 5.754   7.366  -6.599  1.00 26.44 ? 39   THR A C   1 
ATOM   311  O O   . THR A 1 40  ? 6.716   7.275  -7.370  1.00 22.56 ? 39   THR A O   1 
ATOM   312  C CB  . THR A 1 40  ? 4.728   5.339  -5.527  1.00 28.13 ? 39   THR A CB  1 
ATOM   313  O OG1 . THR A 1 40  ? 4.889   4.413  -4.443  1.00 27.63 ? 39   THR A OG1 1 
ATOM   314  C CG2 . THR A 1 40  ? 4.997   4.625  -6.850  1.00 25.24 ? 39   THR A CG2 1 
ATOM   315  N N   . LEU A 1 41  ? 4.733   8.192  -6.835  1.00 26.22 ? 40   LEU A N   1 
ATOM   316  C CA  . LEU A 1 41  ? 4.762   9.060  -8.004  1.00 20.00 ? 40   LEU A CA  1 
ATOM   317  C C   . LEU A 1 41  ? 5.893   10.074 -7.905  1.00 19.74 ? 40   LEU A C   1 
ATOM   318  O O   . LEU A 1 41  ? 6.521   10.412 -8.914  1.00 26.73 ? 40   LEU A O   1 
ATOM   319  C CB  . LEU A 1 41  ? 3.410   9.754  -8.177  1.00 21.51 ? 40   LEU A CB  1 
ATOM   320  C CG  . LEU A 1 41  ? 2.227   8.865  -8.570  1.00 23.49 ? 40   LEU A CG  1 
ATOM   321  C CD1 . LEU A 1 41  ? 0.995   9.733  -8.785  1.00 20.41 ? 40   LEU A CD1 1 
ATOM   322  C CD2 . LEU A 1 41  ? 2.513   8.061  -9.824  1.00 20.45 ? 40   LEU A CD2 1 
ATOM   323  N N   . ILE A 1 42  ? 6.176   10.565 -6.694  1.00 23.46 ? 41   ILE A N   1 
ATOM   324  C CA  . ILE A 1 42  ? 7.324   11.448 -6.507  1.00 23.90 ? 41   ILE A CA  1 
ATOM   325  C C   . ILE A 1 42  ? 8.619   10.736 -6.884  1.00 26.13 ? 41   ILE A C   1 
ATOM   326  O O   . ILE A 1 42  ? 9.499   11.316 -7.535  1.00 26.49 ? 41   ILE A O   1 
ATOM   327  C CB  . ILE A 1 42  ? 7.364   11.972 -5.060  1.00 24.80 ? 41   ILE A CB  1 
ATOM   328  C CG1 . ILE A 1 42  ? 6.269   13.016 -4.854  1.00 22.27 ? 41   ILE A CG1 1 
ATOM   329  C CG2 . ILE A 1 42  ? 8.714   12.577 -4.773  1.00 23.74 ? 41   ILE A CG2 1 
ATOM   330  C CD1 . ILE A 1 42  ? 6.170   13.503 -3.417  1.00 24.63 ? 41   ILE A CD1 1 
ATOM   331  N N   . SER A 1 43  ? 8.749   9.461  -6.509  1.00 26.95 ? 42   SER A N   1 
ATOM   332  C CA  . SER A 1 43  ? 9.961   8.723  -6.850  1.00 24.96 ? 42   SER A CA  1 
ATOM   333  C C   . SER A 1 43  ? 10.091  8.485  -8.347  1.00 30.28 ? 42   SER A C   1 
ATOM   334  O O   . SER A 1 43  ? 11.210  8.310  -8.835  1.00 31.37 ? 42   SER A O   1 
ATOM   335  C CB  . SER A 1 43  ? 10.000  7.389  -6.100  1.00 29.09 ? 42   SER A CB  1 
ATOM   336  O OG  . SER A 1 43  ? 9.114   6.448  -6.686  1.00 37.86 ? 42   SER A OG  1 
ATOM   337  N N   . LYS A 1 44  ? 8.979   8.479  -9.087  1.00 28.40 ? 43   LYS A N   1 
ATOM   338  C CA  . LYS A 1 44  ? 9.031   8.377  -10.541 1.00 22.70 ? 43   LYS A CA  1 
ATOM   339  C C   . LYS A 1 44  ? 9.437   9.684  -11.206 1.00 31.58 ? 43   LYS A C   1 
ATOM   340  O O   . LYS A 1 44  ? 9.704   9.685  -12.413 1.00 29.57 ? 43   LYS A O   1 
ATOM   341  C CB  . LYS A 1 44  ? 7.674   7.942  -11.109 1.00 29.61 ? 43   LYS A CB  1 
ATOM   342  C CG  . LYS A 1 44  ? 7.216   6.540  -10.708 1.00 30.19 ? 43   LYS A CG  1 
ATOM   343  C CD  . LYS A 1 44  ? 7.958   5.446  -11.464 1.00 35.33 ? 43   LYS A CD  1 
ATOM   344  C CE  . LYS A 1 44  ? 7.537   4.051  -10.985 1.00 38.07 ? 43   LYS A CE  1 
ATOM   345  N NZ  . LYS A 1 44  ? 7.983   2.975  -11.911 1.00 46.22 ? 43   LYS A NZ  1 
ATOM   346  N N   . GLY A 1 45  ? 9.477   10.789 -10.463 1.00 24.36 ? 44   GLY A N   1 
ATOM   347  C CA  . GLY A 1 45  ? 9.911   12.064 -10.999 1.00 26.36 ? 44   GLY A CA  1 
ATOM   348  C C   . GLY A 1 45  ? 8.853   13.149 -11.064 1.00 24.98 ? 44   GLY A C   1 
ATOM   349  O O   . GLY A 1 45  ? 9.174   14.261 -11.494 1.00 23.49 ? 44   GLY A O   1 
ATOM   350  N N   . MET A 1 46  ? 7.615   12.884 -10.650 1.00 18.81 ? 45   MET A N   1 
ATOM   351  C CA  . MET A 1 46  ? 6.595   13.933 -10.645 1.00 19.17 ? 45   MET A CA  1 
ATOM   352  C C   . MET A 1 46  ? 6.842   14.920 -9.507  1.00 21.80 ? 45   MET A C   1 
ATOM   353  O O   . MET A 1 46  ? 7.291   14.539 -8.420  1.00 23.32 ? 45   MET A O   1 
ATOM   354  C CB  . MET A 1 46  ? 5.213   13.314 -10.499 1.00 16.44 ? 45   MET A CB  1 
ATOM   355  C CG  . MET A 1 46  ? 4.843   12.432 -11.673 1.00 20.56 ? 45   MET A CG  1 
ATOM   356  S SD  . MET A 1 46  ? 3.123   11.899 -11.589 1.00 22.01 ? 45   MET A SD  1 
ATOM   357  C CE  . MET A 1 46  ? 2.993   11.076 -13.176 1.00 25.57 ? 45   MET A CE  1 
ATOM   358  N N   . ASN A 1 47  ? 6.538   16.202 -9.756  1.00 18.25 ? 46   ASN A N   1 
ATOM   359  C CA  . ASN A 1 47  ? 6.853   17.234 -8.768  1.00 18.05 ? 46   ASN A CA  1 
ATOM   360  C C   . ASN A 1 47  ? 5.697   18.183 -8.499  1.00 17.98 ? 46   ASN A C   1 
ATOM   361  O O   . ASN A 1 47  ? 5.909   19.231 -7.882  1.00 16.80 ? 46   ASN A O   1 
ATOM   362  C CB  . ASN A 1 47  ? 8.091   18.038 -9.185  1.00 17.98 ? 46   ASN A CB  1 
ATOM   363  C CG  . ASN A 1 47  ? 7.844   18.931 -10.391 1.00 20.22 ? 46   ASN A CG  1 
ATOM   364  O OD1 . ASN A 1 47  ? 6.859   18.771 -11.103 1.00 22.44 ? 46   ASN A OD1 1 
ATOM   365  N ND2 . ASN A 1 47  ? 8.751   19.879 -10.623 1.00 23.72 ? 46   ASN A ND2 1 
ATOM   366  N N   . ILE A 1 48  ? 4.492   17.855 -8.953  1.00 18.06 ? 47   ILE A N   1 
ATOM   367  C CA  . ILE A 1 48  ? 3.322   18.687 -8.704  1.00 15.87 ? 47   ILE A CA  1 
ATOM   368  C C   . ILE A 1 48  ? 2.133   17.757 -8.574  1.00 15.11 ? 47   ILE A C   1 
ATOM   369  O O   . ILE A 1 48  ? 1.995   16.800 -9.339  1.00 17.13 ? 47   ILE A O   1 
ATOM   370  C CB  . ILE A 1 48  ? 3.116   19.754 -9.807  1.00 15.37 ? 47   ILE A CB  1 
ATOM   371  C CG1 . ILE A 1 48  ? 1.951   20.691 -9.454  1.00 15.79 ? 47   ILE A CG1 1 
ATOM   372  C CG2 . ILE A 1 48  ? 2.886   19.108 -11.200 1.00 14.86 ? 47   ILE A CG2 1 
ATOM   373  C CD1 . ILE A 1 48  ? 1.953   21.981 -10.284 1.00 17.58 ? 47   ILE A CD1 1 
ATOM   374  N N   . PHE A 1 49  ? 1.288   18.030 -7.581  1.00 14.57 ? 48   PHE A N   1 
ATOM   375  C CA  . PHE A 1 49  ? 0.097   17.227 -7.335  1.00 13.31 ? 48   PHE A CA  1 
ATOM   376  C C   . PHE A 1 49  ? -1.063  18.174 -7.072  1.00 15.35 ? 48   PHE A C   1 
ATOM   377  O O   . PHE A 1 49  ? -0.979  19.036 -6.188  1.00 16.14 ? 48   PHE A O   1 
ATOM   378  C CB  . PHE A 1 49  ? 0.334   16.268 -6.162  1.00 18.47 ? 48   PHE A CB  1 
ATOM   379  C CG  . PHE A 1 49  ? 1.420   15.287 -6.446  1.00 15.93 ? 48   PHE A CG  1 
ATOM   380  C CD1 . PHE A 1 49  ? 2.755   15.619 -6.200  1.00 17.69 ? 48   PHE A CD1 1 
ATOM   381  C CD2 . PHE A 1 49  ? 1.126   14.064 -7.032  1.00 19.15 ? 48   PHE A CD2 1 
ATOM   382  C CE1 . PHE A 1 49  ? 3.768   14.722 -6.503  1.00 20.03 ? 48   PHE A CE1 1 
ATOM   383  C CE2 . PHE A 1 49  ? 2.134   13.168 -7.340  1.00 17.77 ? 48   PHE A CE2 1 
ATOM   384  C CZ  . PHE A 1 49  ? 3.459   13.502 -7.078  1.00 19.37 ? 48   PHE A CZ  1 
ATOM   385  N N   . ARG A 1 50  ? -2.120  18.047 -7.866  1.00 15.40 ? 49   ARG A N   1 
ATOM   386  C CA  . ARG A 1 50  ? -3.283  18.920 -7.764  1.00 15.54 ? 49   ARG A CA  1 
ATOM   387  C C   . ARG A 1 50  ? -4.371  18.195 -6.989  1.00 18.27 ? 49   ARG A C   1 
ATOM   388  O O   . ARG A 1 50  ? -4.691  17.044 -7.302  1.00 17.85 ? 49   ARG A O   1 
ATOM   389  C CB  . ARG A 1 50  ? -3.775  19.315 -9.158  1.00 15.68 ? 49   ARG A CB  1 
ATOM   390  C CG  . ARG A 1 50  ? -4.995  20.235 -9.162  1.00 14.65 ? 49   ARG A CG  1 
ATOM   391  C CD  . ARG A 1 50  ? -5.154  20.829 -10.560 1.00 12.42 ? 49   ARG A CD  1 
ATOM   392  N NE  . ARG A 1 50  ? -6.308  21.714 -10.728 1.00 14.31 ? 49   ARG A NE  1 
ATOM   393  C CZ  . ARG A 1 50  ? -7.423  21.347 -11.358 1.00 15.35 ? 49   ARG A CZ  1 
ATOM   394  N NH1 . ARG A 1 50  ? -7.643  20.082 -11.683 1.00 14.62 ? 49   ARG A NH1 1 
ATOM   395  N NH2 . ARG A 1 50  ? -8.339  22.273 -11.679 1.00 13.80 ? 49   ARG A NH2 1 
ATOM   396  N N   . VAL A 1 51  ? -4.918  18.848 -5.968  1.00 14.84 ? 50   VAL A N   1 
ATOM   397  C CA  . VAL A 1 51  ? -5.815  18.208 -5.014  1.00 15.34 ? 50   VAL A CA  1 
ATOM   398  C C   . VAL A 1 51  ? -7.195  18.855 -5.112  1.00 16.71 ? 50   VAL A C   1 
ATOM   399  O O   . VAL A 1 51  ? -7.445  19.909 -4.516  1.00 16.85 ? 50   VAL A O   1 
ATOM   400  C CB  . VAL A 1 51  ? -5.258  18.312 -3.583  1.00 14.25 ? 50   VAL A CB  1 
ATOM   401  C CG1 . VAL A 1 51  ? -6.172  17.590 -2.587  1.00 14.94 ? 50   VAL A CG1 1 
ATOM   402  C CG2 . VAL A 1 51  ? -3.838  17.734 -3.533  1.00 15.69 ? 50   VAL A CG2 1 
ATOM   403  N N   . PRO A 1 52  ? -8.128  18.239 -5.848  1.00 16.52 ? 51   PRO A N   1 
ATOM   404  C CA  . PRO A 1 52  ? -9.506  18.746 -5.864  1.00 14.60 ? 51   PRO A CA  1 
ATOM   405  C C   . PRO A 1 52  ? -10.173 18.580 -4.507  1.00 16.82 ? 51   PRO A C   1 
ATOM   406  O O   . PRO A 1 52  ? -9.988  17.572 -3.829  1.00 17.14 ? 51   PRO A O   1 
ATOM   407  C CB  . PRO A 1 52  ? -10.199 17.863 -6.913  1.00 16.79 ? 51   PRO A CB  1 
ATOM   408  C CG  . PRO A 1 52  ? -9.046  17.359 -7.816  1.00 16.42 ? 51   PRO A CG  1 
ATOM   409  C CD  . PRO A 1 52  ? -7.930  17.127 -6.801  1.00 17.81 ? 51   PRO A CD  1 
ATOM   410  N N   . PHE A 1 53  ? -10.974 19.570 -4.129  1.00 16.19 ? 52   PHE A N   1 
ATOM   411  C CA  . PHE A 1 53  ? -11.847 19.469 -2.963  1.00 16.92 ? 52   PHE A CA  1 
ATOM   412  C C   . PHE A 1 53  ? -13.086 20.313 -3.240  1.00 15.65 ? 52   PHE A C   1 
ATOM   413  O O   . PHE A 1 53  ? -13.108 21.126 -4.168  1.00 17.89 ? 52   PHE A O   1 
ATOM   414  C CB  . PHE A 1 53  ? -11.140 19.937 -1.684  1.00 17.50 ? 52   PHE A CB  1 
ATOM   415  C CG  . PHE A 1 53  ? -10.891 21.422 -1.654  1.00 14.62 ? 52   PHE A CG  1 
ATOM   416  C CD1 . PHE A 1 53  ? -11.841 22.295 -1.126  1.00 15.60 ? 52   PHE A CD1 1 
ATOM   417  C CD2 . PHE A 1 53  ? -9.728  21.949 -2.188  1.00 16.03 ? 52   PHE A CD2 1 
ATOM   418  C CE1 . PHE A 1 53  ? -11.630 23.672 -1.131  1.00 16.25 ? 52   PHE A CE1 1 
ATOM   419  C CE2 . PHE A 1 53  ? -9.499  23.333 -2.183  1.00 14.97 ? 52   PHE A CE2 1 
ATOM   420  C CZ  . PHE A 1 53  ? -10.449 24.195 -1.669  1.00 15.39 ? 52   PHE A CZ  1 
ATOM   421  N N   . MET A 1 54  ? -14.124 20.141 -2.417  1.00 15.26 ? 53   MET A N   1 
ATOM   422  C CA  A MET A 1 54  ? -15.366 20.885 -2.588  0.76 14.73 ? 53   MET A CA  1 
ATOM   423  C CA  B MET A 1 54  ? -15.379 20.869 -2.570  0.24 14.88 ? 53   MET A CA  1 
ATOM   424  C C   . MET A 1 54  ? -15.401 22.094 -1.665  1.00 16.82 ? 53   MET A C   1 
ATOM   425  O O   . MET A 1 54  ? -15.175 21.966 -0.451  1.00 16.86 ? 53   MET A O   1 
ATOM   426  C CB  A MET A 1 54  ? -16.581 20.000 -2.313  0.76 19.16 ? 53   MET A CB  1 
ATOM   427  C CB  B MET A 1 54  ? -16.557 19.959 -2.227  0.24 19.15 ? 53   MET A CB  1 
ATOM   428  C CG  A MET A 1 54  ? -16.801 18.898 -3.330  0.76 20.05 ? 53   MET A CG  1 
ATOM   429  C CG  B MET A 1 54  ? -16.622 18.716 -3.076  0.24 19.67 ? 53   MET A CG  1 
ATOM   430  S SD  A MET A 1 54  ? -18.420 18.131 -3.134  0.76 23.33 ? 53   MET A SD  1 
ATOM   431  S SD  B MET A 1 54  ? -17.123 19.166 -4.736  0.24 24.70 ? 53   MET A SD  1 
ATOM   432  C CE  A MET A 1 54  ? -19.512 19.388 -3.795  0.76 23.94 ? 53   MET A CE  1 
ATOM   433  C CE  B MET A 1 54  ? -18.803 19.704 -4.404  0.24 28.71 ? 53   MET A CE  1 
ATOM   434  N N   . MET A 1 55  ? -15.708 23.270 -2.239  1.00 16.71 ? 54   MET A N   1 
ATOM   435  C CA  . MET A 1 55  ? -15.831 24.479 -1.416  1.00 15.84 ? 54   MET A CA  1 
ATOM   436  C C   . MET A 1 55  ? -16.822 24.275 -0.281  1.00 19.28 ? 54   MET A C   1 
ATOM   437  O O   . MET A 1 55  ? -16.591 24.733 0.841   1.00 18.18 ? 54   MET A O   1 
ATOM   438  C CB  . MET A 1 55  ? -16.286 25.682 -2.249  1.00 16.09 ? 54   MET A CB  1 
ATOM   439  C CG  . MET A 1 55  ? -15.248 26.231 -3.204  1.00 13.92 ? 54   MET A CG  1 
ATOM   440  S SD  . MET A 1 55  ? -15.952 27.535 -4.242  1.00 17.14 ? 54   MET A SD  1 
ATOM   441  C CE  . MET A 1 55  ? -16.100 28.892 -3.050  1.00 16.79 ? 54   MET A CE  1 
ATOM   442  N N   . GLU A 1 56  ? -17.953 23.614 -0.569  1.00 18.82 ? 55   GLU A N   1 
ATOM   443  C CA  . GLU A 1 56  ? -19.019 23.462 0.420   1.00 16.24 ? 55   GLU A CA  1 
ATOM   444  C C   . GLU A 1 56  ? -18.610 22.549 1.564   1.00 18.43 ? 55   GLU A C   1 
ATOM   445  O O   . GLU A 1 56  ? -19.178 22.638 2.661   1.00 19.42 ? 55   GLU A O   1 
ATOM   446  C CB  . GLU A 1 56  ? -20.270 22.912 -0.261  1.00 23.25 ? 55   GLU A CB  1 
ATOM   447  C CG  . GLU A 1 56  ? -20.843 23.820 -1.358  1.00 22.22 ? 55   GLU A CG  1 
ATOM   448  C CD  . GLU A 1 56  ? -20.236 23.574 -2.748  1.00 19.79 ? 55   GLU A CD  1 
ATOM   449  O OE1 . GLU A 1 56  ? -19.193 22.888 -2.876  1.00 18.64 ? 55   GLU A OE1 1 
ATOM   450  O OE2 . GLU A 1 56  ? -20.830 24.072 -3.733  1.00 20.12 ? 55   GLU A OE2 1 
ATOM   451  N N   . ARG A 1 57  ? -17.670 21.640 1.315   1.00 19.06 ? 56   ARG A N   1 
ATOM   452  C CA  . ARG A 1 57  ? -17.163 20.759 2.365   1.00 19.20 ? 56   ARG A CA  1 
ATOM   453  C C   . ARG A 1 57  ? -16.080 21.436 3.199   1.00 16.38 ? 56   ARG A C   1 
ATOM   454  O O   . ARG A 1 57  ? -15.969 21.173 4.412   1.00 18.11 ? 56   ARG A O   1 
ATOM   455  C CB  . ARG A 1 57  ? -16.624 19.473 1.738   1.00 20.18 ? 56   ARG A CB  1 
ATOM   456  C CG  . ARG A 1 57  ? -17.709 18.559 1.180   1.00 20.54 ? 56   ARG A CG  1 
ATOM   457  C CD  . ARG A 1 57  ? -17.146 17.252 0.640   1.00 19.23 ? 56   ARG A CD  1 
ATOM   458  N NE  . ARG A 1 57  ? -18.228 16.357 0.239   1.00 21.72 ? 56   ARG A NE  1 
ATOM   459  C CZ  . ARG A 1 57  ? -18.171 15.534 -0.801  1.00 21.96 ? 56   ARG A CZ  1 
ATOM   460  N NH1 . ARG A 1 57  ? -17.084 15.446 -1.561  1.00 23.14 ? 56   ARG A NH1 1 
ATOM   461  N NH2 . ARG A 1 57  ? -19.231 14.784 -1.092  1.00 24.16 ? 56   ARG A NH2 1 
ATOM   462  N N   . LEU A 1 58  ? -15.280 22.311 2.579   1.00 18.26 ? 57   LEU A N   1 
ATOM   463  C CA  . LEU A 1 58  ? -14.256 23.035 3.325   1.00 15.91 ? 57   LEU A CA  1 
ATOM   464  C C   . LEU A 1 58  ? -14.843 24.197 4.118   1.00 20.41 ? 57   LEU A C   1 
ATOM   465  O O   . LEU A 1 58  ? -14.422 24.452 5.252   1.00 20.27 ? 57   LEU A O   1 
ATOM   466  C CB  . LEU A 1 58  ? -13.161 23.548 2.374   1.00 16.98 ? 57   LEU A CB  1 
ATOM   467  C CG  . LEU A 1 58  ? -11.951 24.175 3.099   1.00 17.32 ? 57   LEU A CG  1 
ATOM   468  C CD1 . LEU A 1 58  ? -11.143 23.083 3.798   1.00 18.11 ? 57   LEU A CD1 1 
ATOM   469  C CD2 . LEU A 1 58  ? -11.065 24.948 2.138   1.00 18.54 ? 57   LEU A CD2 1 
ATOM   470  N N   . VAL A 1 59  ? -15.791 24.929 3.538   1.00 17.61 ? 58   VAL A N   1 
ATOM   471  C CA  . VAL A 1 59  ? -16.401 26.092 4.189   1.00 17.33 ? 58   VAL A CA  1 
ATOM   472  C C   . VAL A 1 59  ? -17.906 26.003 3.962   1.00 21.42 ? 58   VAL A C   1 
ATOM   473  O O   . VAL A 1 59  ? -18.414 26.526 2.956   1.00 20.36 ? 58   VAL A O   1 
ATOM   474  C CB  . VAL A 1 59  ? -15.840 27.416 3.640   1.00 21.70 ? 58   VAL A CB  1 
ATOM   475  C CG1 . VAL A 1 59  ? -16.438 28.609 4.400   1.00 21.15 ? 58   VAL A CG1 1 
ATOM   476  C CG2 . VAL A 1 59  ? -14.312 27.440 3.716   1.00 21.19 ? 58   VAL A CG2 1 
ATOM   477  N N   . PRO A 1 60  ? -18.641 25.353 4.854   1.00 21.37 ? 59   PRO A N   1 
ATOM   478  C CA  . PRO A 1 60  ? -20.053 25.050 4.595   1.00 20.55 ? 59   PRO A CA  1 
ATOM   479  C C   . PRO A 1 60  ? -20.958 26.266 4.743   1.00 21.03 ? 59   PRO A C   1 
ATOM   480  O O   . PRO A 1 60  ? -20.629 27.249 5.412   1.00 22.68 ? 59   PRO A O   1 
ATOM   481  C CB  . PRO A 1 60  ? -20.388 24.000 5.667   1.00 24.56 ? 59   PRO A CB  1 
ATOM   482  C CG  . PRO A 1 60  ? -19.036 23.534 6.208   1.00 25.69 ? 59   PRO A CG  1 
ATOM   483  C CD  . PRO A 1 60  ? -18.158 24.737 6.102   1.00 19.03 ? 59   PRO A CD  1 
ATOM   484  N N   . ASN A 1 61  ? -22.131 26.161 4.095   1.00 20.77 ? 60   ASN A N   1 
ATOM   485  C CA  . ASN A 1 61  ? -23.275 27.062 4.260   1.00 24.21 ? 60   ASN A CA  1 
ATOM   486  C C   . ASN A 1 61  ? -23.057 28.428 3.622   1.00 25.74 ? 60   ASN A C   1 
ATOM   487  O O   . ASN A 1 61  ? -23.856 28.856 2.778   1.00 25.15 ? 60   ASN A O   1 
ATOM   488  C CB  . ASN A 1 61  ? -23.626 27.231 5.746   1.00 25.10 ? 60   ASN A CB  1 
ATOM   489  C CG  . ASN A 1 61  ? -23.864 25.903 6.443   1.00 28.22 ? 60   ASN A CG  1 
ATOM   490  O OD1 . ASN A 1 61  ? -24.446 24.981 5.867   1.00 32.32 ? 60   ASN A OD1 1 
ATOM   491  N ND2 . ASN A 1 61  ? -23.411 25.800 7.690   1.00 36.10 ? 60   ASN A ND2 1 
ATOM   492  N N   . SER A 1 62  ? -21.989 29.123 4.014   1.00 18.99 ? 61   SER A N   1 
ATOM   493  C CA  A SER A 1 62  ? -21.629 30.402 3.419   0.63 19.18 ? 61   SER A CA  1 
ATOM   494  C CA  B SER A 1 62  ? -21.628 30.402 3.414   0.37 19.23 ? 61   SER A CA  1 
ATOM   495  C C   . SER A 1 62  ? -20.123 30.438 3.216   1.00 20.42 ? 61   SER A C   1 
ATOM   496  O O   . SER A 1 62  ? -19.371 30.096 4.131   1.00 23.49 ? 61   SER A O   1 
ATOM   497  C CB  A SER A 1 62  ? -22.084 31.565 4.312   0.63 24.45 ? 61   SER A CB  1 
ATOM   498  C CB  B SER A 1 62  ? -22.075 31.584 4.286   0.37 24.39 ? 61   SER A CB  1 
ATOM   499  O OG  A SER A 1 62  ? -21.580 32.792 3.835   0.63 21.94 ? 61   SER A OG  1 
ATOM   500  O OG  B SER A 1 62  ? -23.481 31.742 4.249   0.37 23.83 ? 61   SER A OG  1 
ATOM   501  N N   . MET A 1 63  ? -19.682 30.851 2.020   1.00 19.15 ? 62   MET A N   1 
ATOM   502  C CA  . MET A 1 63  ? -18.250 30.820 1.739   1.00 18.37 ? 62   MET A CA  1 
ATOM   503  C C   . MET A 1 63  ? -17.482 31.876 2.516   1.00 21.52 ? 62   MET A C   1 
ATOM   504  O O   . MET A 1 63  ? -16.250 31.834 2.517   1.00 19.72 ? 62   MET A O   1 
ATOM   505  C CB  . MET A 1 63  ? -17.977 30.969 0.235   1.00 19.73 ? 62   MET A CB  1 
ATOM   506  C CG  . MET A 1 63  ? -18.165 32.380 -0.304  1.00 21.27 ? 62   MET A CG  1 
ATOM   507  S SD  . MET A 1 63  ? -17.786 32.499 -2.068  1.00 21.85 ? 62   MET A SD  1 
ATOM   508  C CE  . MET A 1 63  ? -19.169 31.656 -2.824  1.00 23.62 ? 62   MET A CE  1 
ATOM   509  N N   . THR A 1 64  ? -18.172 32.797 3.188   1.00 21.59 ? 63   THR A N   1 
ATOM   510  C CA  . THR A 1 64  ? -17.534 33.761 4.070   1.00 21.60 ? 63   THR A CA  1 
ATOM   511  C C   . THR A 1 64  ? -17.377 33.247 5.496   1.00 21.36 ? 63   THR A C   1 
ATOM   512  O O   . THR A 1 64  ? -16.845 33.977 6.341   1.00 26.95 ? 63   THR A O   1 
ATOM   513  C CB  . THR A 1 64  ? -18.337 35.066 4.095   1.00 20.68 ? 63   THR A CB  1 
ATOM   514  O OG1 . THR A 1 64  ? -19.657 34.798 4.589   1.00 25.70 ? 63   THR A OG1 1 
ATOM   515  C CG2 . THR A 1 64  ? -18.431 35.666 2.684   1.00 23.31 ? 63   THR A CG2 1 
ATOM   516  N N   . GLY A 1 65  ? -17.822 32.022 5.788   1.00 20.26 ? 64   GLY A N   1 
ATOM   517  C CA  . GLY A 1 65  ? -17.828 31.498 7.141   1.00 22.25 ? 64   GLY A CA  1 
ATOM   518  C C   . GLY A 1 65  ? -16.541 30.789 7.532   1.00 21.45 ? 64   GLY A C   1 
ATOM   519  O O   . GLY A 1 65  ? -15.516 30.856 6.852   1.00 21.35 ? 64   GLY A O   1 
ATOM   520  N N   . SER A 1 66  ? -16.606 30.089 8.680   1.00 25.79 ? 65   SER A N   1 
ATOM   521  C CA  A SER A 1 66  ? -15.411 29.400 9.138   0.48 23.69 ? 65   SER A CA  1 
ATOM   522  C CA  B SER A 1 66  ? -15.434 29.378 9.177   0.52 23.74 ? 65   SER A CA  1 
ATOM   523  C C   . SER A 1 66  ? -15.299 28.020 8.493   1.00 21.42 ? 65   SER A C   1 
ATOM   524  O O   . SER A 1 66  ? -16.302 27.418 8.095   1.00 22.22 ? 65   SER A O   1 
ATOM   525  C CB  A SER A 1 66  ? -15.426 29.261 10.663  0.48 26.76 ? 65   SER A CB  1 
ATOM   526  C CB  B SER A 1 66  ? -15.533 29.170 10.687  0.52 26.63 ? 65   SER A CB  1 
ATOM   527  O OG  A SER A 1 66  ? -16.598 28.606 11.112  0.48 30.49 ? 65   SER A OG  1 
ATOM   528  O OG  B SER A 1 66  ? -15.836 30.376 11.352  0.52 30.68 ? 65   SER A OG  1 
ATOM   529  N N   . PRO A 1 67  ? -14.078 27.504 8.370   1.00 22.85 ? 66   PRO A N   1 
ATOM   530  C CA  . PRO A 1 67  ? -13.897 26.171 7.782   1.00 23.00 ? 66   PRO A CA  1 
ATOM   531  C C   . PRO A 1 67  ? -14.519 25.063 8.619   1.00 24.82 ? 66   PRO A C   1 
ATOM   532  O O   . PRO A 1 67  ? -14.726 25.185 9.832   1.00 25.11 ? 66   PRO A O   1 
ATOM   533  C CB  . PRO A 1 67  ? -12.374 26.011 7.735   1.00 21.62 ? 66   PRO A CB  1 
ATOM   534  C CG  . PRO A 1 67  ? -11.843 27.412 7.727   1.00 22.99 ? 66   PRO A CG  1 
ATOM   535  C CD  . PRO A 1 67  ? -12.797 28.208 8.559   1.00 24.56 ? 66   PRO A CD  1 
ATOM   536  N N   . ASP A 1 68  ? -14.787 23.949 7.951   1.00 19.80 ? 67   ASP A N   1 
ATOM   537  C CA  . ASP A 1 68  ? -15.133 22.721 8.653   1.00 19.98 ? 67   ASP A CA  1 
ATOM   538  C C   . ASP A 1 68  ? -13.866 22.102 9.228   1.00 22.25 ? 67   ASP A C   1 
ATOM   539  O O   . ASP A 1 68  ? -12.954 21.765 8.465   1.00 22.17 ? 67   ASP A O   1 
ATOM   540  C CB  . ASP A 1 68  ? -15.803 21.727 7.721   1.00 21.83 ? 67   ASP A CB  1 
ATOM   541  C CG  . ASP A 1 68  ? -16.091 20.410 8.404   1.00 23.86 ? 67   ASP A CG  1 
ATOM   542  O OD1 . ASP A 1 68  ? -16.971 20.381 9.296   1.00 27.71 ? 67   ASP A OD1 1 
ATOM   543  O OD2 . ASP A 1 68  ? -15.426 19.403 8.071   1.00 22.83 ? 67   ASP A OD2 1 
ATOM   544  N N   . PRO A 1 69  ? -13.758 21.944 10.545  1.00 19.64 ? 68   PRO A N   1 
ATOM   545  C CA  . PRO A 1 69  ? -12.501 21.430 11.113  1.00 23.12 ? 68   PRO A CA  1 
ATOM   546  C C   . PRO A 1 69  ? -11.980 20.125 10.511  1.00 23.68 ? 68   PRO A C   1 
ATOM   547  O O   . PRO A 1 69  ? -10.786 20.043 10.196  1.00 20.20 ? 68   PRO A O   1 
ATOM   548  C CB  . PRO A 1 69  ? -12.856 21.272 12.595  1.00 21.44 ? 68   PRO A CB  1 
ATOM   549  C CG  . PRO A 1 69  ? -13.872 22.305 12.843  1.00 24.15 ? 68   PRO A CG  1 
ATOM   550  C CD  . PRO A 1 69  ? -14.720 22.346 11.591  1.00 19.63 ? 68   PRO A CD  1 
ATOM   551  N N   . ASN A 1 70  ? -12.823 19.100 10.347  1.00 21.63 ? 69   ASN A N   1 
ATOM   552  C CA  A ASN A 1 70  ? -12.324 17.793 9.917   0.52 21.07 ? 69   ASN A CA  1 
ATOM   553  C CA  B ASN A 1 70  ? -12.317 17.799 9.921   0.48 21.07 ? 69   ASN A CA  1 
ATOM   554  C C   . ASN A 1 70  ? -11.886 17.822 8.456   1.00 23.64 ? 69   ASN A C   1 
ATOM   555  O O   . ASN A 1 70  ? -10.814 17.306 8.104   1.00 22.14 ? 69   ASN A O   1 
ATOM   556  C CB  A ASN A 1 70  ? -13.395 16.719 10.126  0.52 23.80 ? 69   ASN A CB  1 
ATOM   557  C CB  B ASN A 1 70  ? -13.377 16.728 10.171  0.48 23.83 ? 69   ASN A CB  1 
ATOM   558  C CG  A ASN A 1 70  ? -12.843 15.302 9.993   0.52 36.03 ? 69   ASN A CG  1 
ATOM   559  C CG  B ASN A 1 70  ? -13.767 16.641 11.636  0.48 30.17 ? 69   ASN A CG  1 
ATOM   560  O OD1 A ASN A 1 70  ? -11.719 15.093 9.534   0.52 40.61 ? 69   ASN A OD1 1 
ATOM   561  O OD1 B ASN A 1 70  ? -14.931 16.445 11.979  0.48 36.29 ? 69   ASN A OD1 1 
ATOM   562  N ND2 A ASN A 1 70  ? -13.642 14.318 10.398  0.52 40.95 ? 69   ASN A ND2 1 
ATOM   563  N ND2 B ASN A 1 70  ? -12.791 16.828 12.507  0.48 26.85 ? 69   ASN A ND2 1 
ATOM   564  N N   . TYR A 1 71  ? -12.705 18.413 7.585   1.00 19.30 ? 70   TYR A N   1 
ATOM   565  C CA  . TYR A 1 71  ? -12.325 18.471 6.169   1.00 17.79 ? 70   TYR A CA  1 
ATOM   566  C C   . TYR A 1 71  ? -11.085 19.332 5.971   1.00 19.13 ? 70   TYR A C   1 
ATOM   567  O O   . TYR A 1 71  ? -10.184 18.960 5.209   1.00 17.62 ? 70   TYR A O   1 
ATOM   568  C CB  . TYR A 1 71  ? -13.486 19.001 5.340   1.00 20.01 ? 70   TYR A CB  1 
ATOM   569  C CG  . TYR A 1 71  ? -13.458 18.728 3.839   1.00 18.25 ? 70   TYR A CG  1 
ATOM   570  C CD1 . TYR A 1 71  ? -13.850 17.483 3.326   1.00 18.37 ? 70   TYR A CD1 1 
ATOM   571  C CD2 . TYR A 1 71  ? -13.107 19.737 2.935   1.00 16.01 ? 70   TYR A CD2 1 
ATOM   572  C CE1 . TYR A 1 71  ? -13.886 17.250 1.945   1.00 17.42 ? 70   TYR A CE1 1 
ATOM   573  C CE2 . TYR A 1 71  ? -13.130 19.504 1.549   1.00 16.28 ? 70   TYR A CE2 1 
ATOM   574  C CZ  . TYR A 1 71  ? -13.519 18.253 1.077   1.00 18.71 ? 70   TYR A CZ  1 
ATOM   575  O OH  . TYR A 1 71  ? -13.564 18.015 -0.282  1.00 18.59 ? 70   TYR A OH  1 
ATOM   576  N N   . LEU A 1 72  ? -10.999 20.472 6.669   1.00 18.95 ? 71   LEU A N   1 
ATOM   577  C CA  . LEU A 1 72  ? -9.786  21.291 6.587   1.00 18.00 ? 71   LEU A CA  1 
ATOM   578  C C   . LEU A 1 72  ? -8.561  20.540 7.100   1.00 19.69 ? 71   LEU A C   1 
ATOM   579  O O   . LEU A 1 72  ? -7.481  20.624 6.502   1.00 18.78 ? 71   LEU A O   1 
ATOM   580  C CB  . LEU A 1 72  ? -9.966  22.601 7.368   1.00 16.69 ? 71   LEU A CB  1 
ATOM   581  C CG  . LEU A 1 72  ? -8.691  23.439 7.536   1.00 17.01 ? 71   LEU A CG  1 
ATOM   582  C CD1 . LEU A 1 72  ? -8.117  23.876 6.188   1.00 19.19 ? 71   LEU A CD1 1 
ATOM   583  C CD2 . LEU A 1 72  ? -8.958  24.671 8.388   1.00 20.48 ? 71   LEU A CD2 1 
ATOM   584  N N   . ALA A 1 73  ? -8.694  19.820 8.220   1.00 20.90 ? 72   ALA A N   1 
ATOM   585  C CA  . ALA A 1 73  ? -7.543  19.103 8.760   1.00 20.33 ? 72   ALA A CA  1 
ATOM   586  C C   . ALA A 1 73  ? -6.989  18.102 7.749   1.00 23.15 ? 72   ALA A C   1 
ATOM   587  O O   . ALA A 1 73  ? -5.770  17.922 7.646   1.00 21.48 ? 72   ALA A O   1 
ATOM   588  C CB  . ALA A 1 73  ? -7.927  18.405 10.068  1.00 20.56 ? 72   ALA A CB  1 
ATOM   589  N N   . ASP A 1 74  ? -7.866  17.463 6.971   1.00 18.96 ? 73   ASP A N   1 
ATOM   590  C CA  . ASP A 1 74  ? -7.407  16.492 5.982   1.00 21.85 ? 73   ASP A CA  1 
ATOM   591  C C   . ASP A 1 74  ? -6.834  17.159 4.736   1.00 19.18 ? 73   ASP A C   1 
ATOM   592  O O   . ASP A 1 74  ? -5.903  16.614 4.132   1.00 19.87 ? 73   ASP A O   1 
ATOM   593  C CB  . ASP A 1 74  ? -8.544  15.545 5.594   1.00 21.48 ? 73   ASP A CB  1 
ATOM   594  C CG  . ASP A 1 74  ? -8.855  14.534 6.680   1.00 27.98 ? 73   ASP A CG  1 
ATOM   595  O OD1 . ASP A 1 74  ? -8.079  14.430 7.654   1.00 30.37 ? 73   ASP A OD1 1 
ATOM   596  O OD2 . ASP A 1 74  ? -9.897  13.857 6.581   1.00 29.09 ? 73   ASP A OD2 1 
ATOM   597  N N   . LEU A 1 75  ? -7.350  18.332 4.349   1.00 18.65 ? 74   LEU A N   1 
ATOM   598  C CA  . LEU A 1 75  ? -6.694  19.115 3.302   1.00 18.98 ? 74   LEU A CA  1 
ATOM   599  C C   . LEU A 1 75  ? -5.282  19.503 3.734   1.00 18.19 ? 74   LEU A C   1 
ATOM   600  O O   . LEU A 1 75  ? -4.320  19.361 2.972   1.00 19.06 ? 74   LEU A O   1 
ATOM   601  C CB  . LEU A 1 75  ? -7.520  20.364 2.968   1.00 15.97 ? 74   LEU A CB  1 
ATOM   602  C CG  . LEU A 1 75  ? -6.864  21.308 1.946   1.00 17.34 ? 74   LEU A CG  1 
ATOM   603  C CD1 . LEU A 1 75  ? -6.716  20.629 0.568   1.00 18.89 ? 74   LEU A CD1 1 
ATOM   604  C CD2 . LEU A 1 75  ? -7.660  22.614 1.812   1.00 16.12 ? 74   LEU A CD2 1 
ATOM   605  N N   . ILE A 1 76  ? -5.150  19.994 4.964   1.00 17.89 ? 75   ILE A N   1 
ATOM   606  C CA  . ILE A 1 76  ? -3.844  20.360 5.506   1.00 16.39 ? 75   ILE A CA  1 
ATOM   607  C C   . ILE A 1 76  ? -2.899  19.165 5.482   1.00 18.73 ? 75   ILE A C   1 
ATOM   608  O O   . ILE A 1 76  ? -1.735  19.275 5.078   1.00 18.24 ? 75   ILE A O   1 
ATOM   609  C CB  . ILE A 1 76  ? -4.014  20.916 6.934   1.00 15.28 ? 75   ILE A CB  1 
ATOM   610  C CG1 . ILE A 1 76  ? -4.694  22.285 6.880   1.00 18.98 ? 75   ILE A CG1 1 
ATOM   611  C CG2 . ILE A 1 76  ? -2.658  21.016 7.662   1.00 18.54 ? 75   ILE A CG2 1 
ATOM   612  C CD1 . ILE A 1 76  ? -5.111  22.810 8.267   1.00 17.56 ? 75   ILE A CD1 1 
ATOM   613  N N   . ALA A 1 77  ? -3.368  18.016 5.962   1.00 18.41 ? 76   ALA A N   1 
ATOM   614  C CA  . ALA A 1 77  ? -2.512  16.833 5.997   1.00 18.93 ? 76   ALA A CA  1 
ATOM   615  C C   . ALA A 1 77  ? -2.055  16.444 4.596   1.00 18.02 ? 76   ALA A C   1 
ATOM   616  O O   . ALA A 1 77  ? -0.898  16.054 4.395   1.00 21.40 ? 76   ALA A O   1 
ATOM   617  C CB  . ALA A 1 77  ? -3.245  15.669 6.658   1.00 20.93 ? 76   ALA A CB  1 
ATOM   618  N N   . THR A 1 78  ? -2.958  16.531 3.616   1.00 17.30 ? 77   THR A N   1 
ATOM   619  C CA  . THR A 1 78  ? -2.601  16.163 2.251   1.00 15.25 ? 77   THR A CA  1 
ATOM   620  C C   . THR A 1 78  ? -1.571  17.120 1.671   1.00 18.94 ? 77   THR A C   1 
ATOM   621  O O   . THR A 1 78  ? -0.585  16.690 1.057   1.00 17.59 ? 77   THR A O   1 
ATOM   622  C CB  . THR A 1 78  ? -3.853  16.148 1.372   1.00 15.84 ? 77   THR A CB  1 
ATOM   623  O OG1 . THR A 1 78  ? -4.798  15.217 1.907   1.00 21.05 ? 77   THR A OG1 1 
ATOM   624  C CG2 . THR A 1 78  ? -3.515  15.743 -0.060  1.00 18.11 ? 77   THR A CG2 1 
ATOM   625  N N   . VAL A 1 79  ? -1.808  18.422 1.825   1.00 16.05 ? 78   VAL A N   1 
ATOM   626  C CA  . VAL A 1 79  ? -0.874  19.426 1.334   1.00 15.92 ? 78   VAL A CA  1 
ATOM   627  C C   . VAL A 1 79  ? 0.496   19.223 1.956   1.00 19.94 ? 78   VAL A C   1 
ATOM   628  O O   . VAL A 1 79  ? 1.517   19.244 1.261   1.00 20.28 ? 78   VAL A O   1 
ATOM   629  C CB  . VAL A 1 79  ? -1.413  20.840 1.608   1.00 20.08 ? 78   VAL A CB  1 
ATOM   630  C CG1 . VAL A 1 79  ? -0.298  21.866 1.430   1.00 21.23 ? 78   VAL A CG1 1 
ATOM   631  C CG2 . VAL A 1 79  ? -2.587  21.133 0.678   1.00 19.76 ? 78   VAL A CG2 1 
ATOM   632  N N   . ASN A 1 80  ? 0.547   19.021 3.280   1.00 18.55 ? 79   ASN A N   1 
ATOM   633  C CA  A ASN A 1 80  ? 1.849   18.872 3.913   0.69 22.09 ? 79   ASN A CA  1 
ATOM   634  C CA  B ASN A 1 80  ? 1.833   18.847 3.950   0.31 22.16 ? 79   ASN A CA  1 
ATOM   635  C C   . ASN A 1 80  ? 2.537   17.586 3.473   1.00 23.70 ? 79   ASN A C   1 
ATOM   636  O O   . ASN A 1 80  ? 3.762   17.570 3.310   1.00 25.60 ? 79   ASN A O   1 
ATOM   637  C CB  A ASN A 1 80  ? 1.705   18.948 5.437   0.69 23.75 ? 79   ASN A CB  1 
ATOM   638  C CB  B ASN A 1 80  ? 1.647   18.805 5.469   0.31 23.81 ? 79   ASN A CB  1 
ATOM   639  C CG  A ASN A 1 80  ? 1.226   20.319 5.908   0.69 26.73 ? 79   ASN A CG  1 
ATOM   640  C CG  B ASN A 1 80  ? 2.930   18.454 6.201   0.31 25.33 ? 79   ASN A CG  1 
ATOM   641  O OD1 A ASN A 1 80  ? 1.427   21.334 5.234   0.69 30.69 ? 79   ASN A OD1 1 
ATOM   642  O OD1 B ASN A 1 80  ? 3.920   19.178 6.117   0.31 30.53 ? 79   ASN A OD1 1 
ATOM   643  N ND2 A ASN A 1 80  ? 0.586   20.352 7.067   0.69 31.08 ? 79   ASN A ND2 1 
ATOM   644  N ND2 B ASN A 1 80  ? 2.915   17.342 6.927   0.31 32.87 ? 79   ASN A ND2 1 
ATOM   645  N N   . ALA A 1 81  ? 1.778   16.515 3.238   1.00 20.06 ? 80   ALA A N   1 
ATOM   646  C CA  . ALA A 1 81  ? 2.388   15.274 2.771   1.00 23.89 ? 80   ALA A CA  1 
ATOM   647  C C   . ALA A 1 81  ? 3.099   15.481 1.439   1.00 25.05 ? 80   ALA A C   1 
ATOM   648  O O   . ALA A 1 81  ? 4.151   14.883 1.185   1.00 28.48 ? 80   ALA A O   1 
ATOM   649  C CB  . ALA A 1 81  ? 1.330   14.174 2.655   1.00 29.04 ? 80   ALA A CB  1 
ATOM   650  N N   . ILE A 1 82  ? 2.550   16.343 0.587   1.00 19.17 ? 81   ILE A N   1 
ATOM   651  C CA  . ILE A 1 82  ? 3.170   16.628 -0.704  1.00 18.22 ? 81   ILE A CA  1 
ATOM   652  C C   . ILE A 1 82  ? 4.358   17.567 -0.536  1.00 21.94 ? 81   ILE A C   1 
ATOM   653  O O   . ILE A 1 82  ? 5.457   17.294 -1.035  1.00 22.92 ? 81   ILE A O   1 
ATOM   654  C CB  . ILE A 1 82  ? 2.124   17.222 -1.664  1.00 18.32 ? 81   ILE A CB  1 
ATOM   655  C CG1 . ILE A 1 82  ? 1.043   16.195 -2.017  1.00 18.92 ? 81   ILE A CG1 1 
ATOM   656  C CG2 . ILE A 1 82  ? 2.786   17.760 -2.926  1.00 17.97 ? 81   ILE A CG2 1 
ATOM   657  C CD1 . ILE A 1 82  ? -0.274  16.846 -2.433  1.00 18.27 ? 81   ILE A CD1 1 
ATOM   658  N N   . THR A 1 83  ? 4.162   18.683 0.176   1.00 17.52 ? 82   THR A N   1 
ATOM   659  C CA  . THR A 1 83  ? 5.191   19.714 0.189   1.00 18.15 ? 82   THR A CA  1 
ATOM   660  C C   . THR A 1 83  ? 6.370   19.350 1.087   1.00 22.34 ? 82   THR A C   1 
ATOM   661  O O   . THR A 1 83  ? 7.483   19.828 0.841   1.00 22.08 ? 82   THR A O   1 
ATOM   662  C CB  . THR A 1 83  ? 4.618   21.073 0.611   1.00 18.91 ? 82   THR A CB  1 
ATOM   663  O OG1 . THR A 1 83  ? 4.103   21.000 1.947   1.00 19.48 ? 82   THR A OG1 1 
ATOM   664  C CG2 . THR A 1 83  ? 3.532   21.564 -0.372  1.00 21.09 ? 82   THR A CG2 1 
ATOM   665  N N   . GLN A 1 84  ? 6.154   18.531 2.130   1.00 22.41 ? 83   GLN A N   1 
ATOM   666  C CA  A GLN A 1 84  ? 7.271   18.150 2.990   0.61 22.94 ? 83   GLN A CA  1 
ATOM   667  C CA  B GLN A 1 84  ? 7.248   18.095 2.998   0.39 23.09 ? 83   GLN A CA  1 
ATOM   668  C C   . GLN A 1 84  ? 8.354   17.414 2.205   1.00 23.75 ? 83   GLN A C   1 
ATOM   669  O O   . GLN A 1 84  ? 9.526   17.443 2.602   1.00 23.31 ? 83   GLN A O   1 
ATOM   670  C CB  A GLN A 1 84  ? 6.767   17.303 4.179   0.61 26.31 ? 83   GLN A CB  1 
ATOM   671  C CB  B GLN A 1 84  ? 6.702   17.147 4.073   0.39 26.27 ? 83   GLN A CB  1 
ATOM   672  C CG  A GLN A 1 84  ? 6.111   18.141 5.313   0.61 24.72 ? 83   GLN A CG  1 
ATOM   673  C CG  B GLN A 1 84  ? 7.726   16.234 4.709   0.39 31.26 ? 83   GLN A CG  1 
ATOM   674  C CD  A GLN A 1 84  ? 5.307   17.320 6.324   0.61 31.09 ? 83   GLN A CD  1 
ATOM   675  C CD  B GLN A 1 84  ? 7.102   15.145 5.560   0.39 34.31 ? 83   GLN A CD  1 
ATOM   676  O OE1 A GLN A 1 84  ? 5.165   16.102 6.193   0.61 33.15 ? 83   GLN A OE1 1 
ATOM   677  O OE1 B GLN A 1 84  ? 6.011   14.661 5.266   0.39 40.81 ? 83   GLN A OE1 1 
ATOM   678  N NE2 A GLN A 1 84  ? 4.766   18.000 7.337   0.61 32.49 ? 83   GLN A NE2 1 
ATOM   679  N NE2 B GLN A 1 84  ? 7.791   14.757 6.621   0.39 32.23 ? 83   GLN A NE2 1 
ATOM   680  N N   . LYS A 1 85  ? 8.005   16.792 1.085   1.00 26.76 ? 84   LYS A N   1 
ATOM   681  C CA  A LYS A 1 85  ? 8.962   16.091 0.243   0.55 28.62 ? 84   LYS A CA  1 
ATOM   682  C CA  B LYS A 1 85  ? 8.997   16.103 0.272   0.36 28.57 ? 84   LYS A CA  1 
ATOM   683  C CA  C LYS A 1 85  ? 8.983   16.097 0.258   0.09 28.59 ? 84   LYS A CA  1 
ATOM   684  C C   . LYS A 1 85  ? 9.648   16.997 -0.773  1.00 31.85 ? 84   LYS A C   1 
ATOM   685  O O   . LYS A 1 85  ? 10.586  16.551 -1.440  1.00 32.48 ? 84   LYS A O   1 
ATOM   686  C CB  A LYS A 1 85  ? 8.254   14.948 -0.494  0.55 30.12 ? 84   LYS A CB  1 
ATOM   687  C CB  B LYS A 1 85  ? 8.369   14.893 -0.427  0.36 30.17 ? 84   LYS A CB  1 
ATOM   688  C CB  C LYS A 1 85  ? 8.332   14.911 -0.466  0.09 30.13 ? 84   LYS A CB  1 
ATOM   689  C CG  A LYS A 1 85  ? 7.448   14.038 0.427   0.55 29.95 ? 84   LYS A CG  1 
ATOM   690  C CG  B LYS A 1 85  ? 8.045   13.740 0.505   0.36 31.59 ? 84   LYS A CG  1 
ATOM   691  C CG  C LYS A 1 85  ? 8.492   13.586 0.261   0.09 31.89 ? 84   LYS A CG  1 
ATOM   692  C CD  A LYS A 1 85  ? 8.270   13.598 1.642   0.55 32.49 ? 84   LYS A CD  1 
ATOM   693  C CD  B LYS A 1 85  ? 7.813   12.466 -0.283  0.36 32.98 ? 84   LYS A CD  1 
ATOM   694  C CD  C LYS A 1 85  ? 7.643   13.535 1.519   0.09 32.31 ? 84   LYS A CD  1 
ATOM   695  C CE  A LYS A 1 85  ? 7.662   12.391 2.344   0.55 34.41 ? 84   LYS A CE  1 
ATOM   696  C CE  B LYS A 1 85  ? 9.098   11.937 -0.906  0.36 33.72 ? 84   LYS A CE  1 
ATOM   697  C CE  C LYS A 1 85  ? 8.117   12.437 2.455   0.09 34.21 ? 84   LYS A CE  1 
ATOM   698  N NZ  A LYS A 1 85  ? 8.015   12.386 3.792   0.55 38.01 ? 84   LYS A NZ  1 
ATOM   699  N NZ  B LYS A 1 85  ? 10.048  11.433 0.124   0.36 41.22 ? 84   LYS A NZ  1 
ATOM   700  N NZ  C LYS A 1 85  ? 8.286   11.136 1.748   0.09 34.60 ? 84   LYS A NZ  1 
ATOM   701  N N   . GLY A 1 86  ? 9.190   18.240 -0.925  1.00 26.78 ? 85   GLY A N   1 
ATOM   702  C CA  . GLY A 1 86  ? 9.730   19.145 -1.922  1.00 23.06 ? 85   GLY A CA  1 
ATOM   703  C C   . GLY A 1 86  ? 8.882   19.340 -3.166  1.00 23.26 ? 85   GLY A C   1 
ATOM   704  O O   . GLY A 1 86  ? 9.247   20.159 -4.016  1.00 26.29 ? 85   GLY A O   1 
ATOM   705  N N   . ALA A 1 87  ? 7.764   18.631 -3.300  1.00 20.97 ? 86   ALA A N   1 
ATOM   706  C CA  . ALA A 1 87  ? 6.875   18.795 -4.447  1.00 19.68 ? 86   ALA A CA  1 
ATOM   707  C C   . ALA A 1 87  ? 5.872   19.917 -4.198  1.00 19.96 ? 86   ALA A C   1 
ATOM   708  O O   . ALA A 1 87  ? 5.666   20.362 -3.065  1.00 19.15 ? 86   ALA A O   1 
ATOM   709  C CB  . ALA A 1 87  ? 6.128   17.493 -4.737  1.00 20.68 ? 86   ALA A CB  1 
ATOM   710  N N   . TYR A 1 88  ? 5.228   20.360 -5.279  1.00 16.84 ? 87   TYR A N   1 
ATOM   711  C CA  . TYR A 1 88  ? 4.198   21.394 -5.204  1.00 14.94 ? 87   TYR A CA  1 
ATOM   712  C C   . TYR A 1 88  ? 2.815   20.770 -5.051  1.00 17.56 ? 87   TYR A C   1 
ATOM   713  O O   . TYR A 1 88  ? 2.508   19.759 -5.684  1.00 17.27 ? 87   TYR A O   1 
ATOM   714  C CB  . TYR A 1 88  ? 4.211   22.265 -6.465  1.00 14.78 ? 87   TYR A CB  1 
ATOM   715  C CG  . TYR A 1 88  ? 5.392   23.204 -6.571  1.00 15.82 ? 87   TYR A CG  1 
ATOM   716  C CD1 . TYR A 1 88  ? 6.631   22.752 -7.026  1.00 16.27 ? 87   TYR A CD1 1 
ATOM   717  C CD2 . TYR A 1 88  ? 5.257   24.559 -6.266  1.00 14.64 ? 87   TYR A CD2 1 
ATOM   718  C CE1 . TYR A 1 88  ? 7.714   23.619 -7.131  1.00 13.84 ? 87   TYR A CE1 1 
ATOM   719  C CE2 . TYR A 1 88  ? 6.350   25.431 -6.356  1.00 13.72 ? 87   TYR A CE2 1 
ATOM   720  C CZ  . TYR A 1 88  ? 7.560   24.950 -6.813  1.00 17.22 ? 87   TYR A CZ  1 
ATOM   721  O OH  . TYR A 1 88  ? 8.634   25.806 -6.914  1.00 18.01 ? 87   TYR A OH  1 
ATOM   722  N N   . ALA A 1 89  ? 1.978   21.387 -4.214  1.00 15.52 ? 88   ALA A N   1 
ATOM   723  C CA  . ALA A 1 89  ? 0.603   20.948 -3.993  1.00 14.86 ? 88   ALA A CA  1 
ATOM   724  C C   . ALA A 1 89  ? -0.322  22.044 -4.490  1.00 15.35 ? 88   ALA A C   1 
ATOM   725  O O   . ALA A 1 89  ? -0.268  23.166 -3.979  1.00 16.73 ? 88   ALA A O   1 
ATOM   726  C CB  . ALA A 1 89  ? 0.347   20.680 -2.504  1.00 15.36 ? 88   ALA A CB  1 
ATOM   727  N N   . VAL A 1 90  ? -1.180  21.723 -5.462  1.00 14.84 ? 89   VAL A N   1 
ATOM   728  C CA  . VAL A 1 90  ? -2.163  22.681 -5.963  1.00 14.57 ? 89   VAL A CA  1 
ATOM   729  C C   . VAL A 1 90  ? -3.465  22.509 -5.194  1.00 16.93 ? 89   VAL A C   1 
ATOM   730  O O   . VAL A 1 90  ? -4.071  21.435 -5.226  1.00 15.13 ? 89   VAL A O   1 
ATOM   731  C CB  . VAL A 1 90  ? -2.415  22.500 -7.464  1.00 15.16 ? 89   VAL A CB  1 
ATOM   732  C CG1 . VAL A 1 90  ? -3.360  23.598 -7.945  1.00 16.35 ? 89   VAL A CG1 1 
ATOM   733  C CG2 . VAL A 1 90  ? -1.105  22.503 -8.256  1.00 15.70 ? 89   VAL A CG2 1 
ATOM   734  N N   . VAL A 1 91  ? -3.893  23.566 -4.511  1.00 15.24 ? 90   VAL A N   1 
ATOM   735  C CA  A VAL A 1 91  ? -5.138  23.590 -3.749  0.77 14.43 ? 90   VAL A CA  1 
ATOM   736  C CA  B VAL A 1 91  ? -5.149  23.536 -3.767  0.23 14.52 ? 90   VAL A CA  1 
ATOM   737  C C   . VAL A 1 91  ? -6.265  23.982 -4.710  1.00 13.97 ? 90   VAL A C   1 
ATOM   738  O O   . VAL A 1 91  ? -6.346  25.143 -5.117  1.00 16.33 ? 90   VAL A O   1 
ATOM   739  C CB  A VAL A 1 91  ? -5.002  24.575 -2.584  0.77 15.23 ? 90   VAL A CB  1 
ATOM   740  C CB  B VAL A 1 91  ? -5.088  24.389 -2.494  0.23 15.41 ? 90   VAL A CB  1 
ATOM   741  C CG1 A VAL A 1 91  ? -6.307  24.776 -1.830  0.77 15.38 ? 90   VAL A CG1 1 
ATOM   742  C CG1 B VAL A 1 91  ? -4.229  23.691 -1.449  0.23 16.24 ? 90   VAL A CG1 1 
ATOM   743  C CG2 A VAL A 1 91  ? -3.896  24.091 -1.658  0.77 15.81 ? 90   VAL A CG2 1 
ATOM   744  C CG2 B VAL A 1 91  ? -4.547  25.765 -2.782  0.23 15.15 ? 90   VAL A CG2 1 
ATOM   745  N N   . ASP A 1 92  ? -7.130  23.027 -5.074  1.00 13.35 ? 91   ASP A N   1 
ATOM   746  C CA  . ASP A 1 92  ? -8.114  23.198 -6.149  1.00 15.43 ? 91   ASP A CA  1 
ATOM   747  C C   . ASP A 1 92  ? -9.547  23.114 -5.639  1.00 14.26 ? 91   ASP A C   1 
ATOM   748  O O   . ASP A 1 92  ? -10.077 21.998 -5.482  1.00 16.14 ? 91   ASP A O   1 
ATOM   749  C CB  . ASP A 1 92  ? -7.865  22.121 -7.211  1.00 15.46 ? 91   ASP A CB  1 
ATOM   750  C CG  . ASP A 1 92  ? -9.053  21.869 -8.120  1.00 16.61 ? 91   ASP A CG  1 
ATOM   751  O OD1 . ASP A 1 92  ? -9.833  22.816 -8.384  1.00 16.42 ? 91   ASP A OD1 1 
ATOM   752  O OD2 . ASP A 1 92  ? -9.176  20.700 -8.583  1.00 16.19 ? 91   ASP A OD2 1 
ATOM   753  N N   . PRO A 1 93  ? -10.228 24.256 -5.389  1.00 13.56 ? 92   PRO A N   1 
ATOM   754  C CA  . PRO A 1 93  ? -11.670 24.200 -5.133  1.00 14.09 ? 92   PRO A CA  1 
ATOM   755  C C   . PRO A 1 93  ? -12.347 23.819 -6.429  1.00 12.64 ? 92   PRO A C   1 
ATOM   756  O O   . PRO A 1 93  ? -12.458 24.623 -7.366  1.00 16.66 ? 92   PRO A O   1 
ATOM   757  C CB  . PRO A 1 93  ? -12.039 25.621 -4.673  1.00 15.12 ? 92   PRO A CB  1 
ATOM   758  C CG  . PRO A 1 93  ? -10.776 26.441 -4.773  1.00 16.51 ? 92   PRO A CG  1 
ATOM   759  C CD  . PRO A 1 93  ? -9.762  25.641 -5.542  1.00 20.46 ? 92   PRO A CD  1 
ATOM   760  N N   . HIS A 1 94  ? -12.767 22.567 -6.480  1.00 15.00 ? 93   HIS A N   1 
ATOM   761  C CA  . HIS A 1 94  ? -13.180 21.924 -7.717  1.00 12.96 ? 93   HIS A CA  1 
ATOM   762  C C   . HIS A 1 94  ? -14.659 22.215 -7.985  1.00 15.11 ? 93   HIS A C   1 
ATOM   763  O O   . HIS A 1 94  ? -15.501 21.313 -8.035  1.00 17.13 ? 93   HIS A O   1 
ATOM   764  C CB  . HIS A 1 94  ? -12.889 20.430 -7.618  1.00 14.44 ? 93   HIS A CB  1 
ATOM   765  C CG  . HIS A 1 94  ? -12.673 19.746 -8.931  1.00 15.46 ? 93   HIS A CG  1 
ATOM   766  N ND1 . HIS A 1 94  ? -11.489 19.829 -9.639  1.00 16.87 ? 93   HIS A ND1 1 
ATOM   767  C CD2 . HIS A 1 94  ? -13.490 18.942 -9.651  1.00 16.24 ? 93   HIS A CD2 1 
ATOM   768  C CE1 . HIS A 1 94  ? -11.593 19.108 -10.745 1.00 18.29 ? 93   HIS A CE1 1 
ATOM   769  N NE2 . HIS A 1 94  ? -12.799 18.561 -10.780 1.00 18.53 ? 93   HIS A NE2 1 
ATOM   770  N N   . ASN A 1 95  ? -14.963 23.508 -8.179  1.00 15.80 ? 94   ASN A N   1 
ATOM   771  C CA  . ASN A 1 95  ? -16.339 23.972 -8.016  1.00 13.65 ? 94   ASN A CA  1 
ATOM   772  C C   . ASN A 1 95  ? -16.994 24.621 -9.227  1.00 15.62 ? 94   ASN A C   1 
ATOM   773  O O   . ASN A 1 95  ? -18.150 25.033 -9.113  1.00 16.02 ? 94   ASN A O   1 
ATOM   774  C CB  . ASN A 1 95  ? -16.446 24.930 -6.823  1.00 16.08 ? 94   ASN A CB  1 
ATOM   775  C CG  . ASN A 1 95  ? -16.791 24.187 -5.560  1.00 14.82 ? 94   ASN A CG  1 
ATOM   776  O OD1 . ASN A 1 95  ? -15.964 23.448 -5.033  1.00 17.71 ? 94   ASN A OD1 1 
ATOM   777  N ND2 . ASN A 1 95  ? -18.040 24.296 -5.125  1.00 17.00 ? 94   ASN A ND2 1 
ATOM   778  N N   . TYR A 1 96  ? -16.334 24.699 -10.382 1.00 17.21 ? 95   TYR A N   1 
ATOM   779  C CA  . TYR A 1 96  ? -17.015 25.107 -11.616 1.00 15.36 ? 95   TYR A CA  1 
ATOM   780  C C   . TYR A 1 96  ? -17.599 26.517 -11.522 1.00 14.70 ? 95   TYR A C   1 
ATOM   781  O O   . TYR A 1 96  ? -18.576 26.836 -12.200 1.00 17.55 ? 95   TYR A O   1 
ATOM   782  C CB  . TYR A 1 96  ? -18.102 24.083 -11.990 1.00 15.39 ? 95   TYR A CB  1 
ATOM   783  C CG  . TYR A 1 96  ? -17.551 22.663 -12.073 1.00 16.22 ? 95   TYR A CG  1 
ATOM   784  C CD1 . TYR A 1 96  ? -16.864 22.224 -13.207 1.00 18.68 ? 95   TYR A CD1 1 
ATOM   785  C CD2 . TYR A 1 96  ? -17.697 21.772 -11.014 1.00 18.89 ? 95   TYR A CD2 1 
ATOM   786  C CE1 . TYR A 1 96  ? -16.349 20.950 -13.288 1.00 19.66 ? 95   TYR A CE1 1 
ATOM   787  C CE2 . TYR A 1 96  ? -17.182 20.481 -11.095 1.00 19.80 ? 95   TYR A CE2 1 
ATOM   788  C CZ  . TYR A 1 96  ? -16.510 20.080 -12.231 1.00 19.70 ? 95   TYR A CZ  1 
ATOM   789  O OH  . TYR A 1 96  ? -15.988 18.807 -12.329 1.00 24.04 ? 95   TYR A OH  1 
ATOM   790  N N   . GLY A 1 97  ? -17.013 27.383 -10.695 1.00 15.75 ? 96   GLY A N   1 
ATOM   791  C CA  . GLY A 1 97  ? -17.541 28.726 -10.506 1.00 17.16 ? 96   GLY A CA  1 
ATOM   792  C C   . GLY A 1 97  ? -18.858 28.787 -9.757  1.00 17.43 ? 96   GLY A C   1 
ATOM   793  O O   . GLY A 1 97  ? -19.569 29.800 -9.847  1.00 16.70 ? 96   GLY A O   1 
ATOM   794  N N   . ARG A 1 98  ? -19.207 27.722 -9.034  1.00 15.36 ? 97   ARG A N   1 
ATOM   795  C CA  . ARG A 1 98  ? -20.516 27.580 -8.402  1.00 15.65 ? 97   ARG A CA  1 
ATOM   796  C C   . ARG A 1 98  ? -20.370 27.144 -6.951  1.00 18.27 ? 97   ARG A C   1 
ATOM   797  O O   . ARG A 1 98  ? -19.430 26.444 -6.581  1.00 18.32 ? 97   ARG A O   1 
ATOM   798  C CB  . ARG A 1 98  ? -21.388 26.560 -9.165  1.00 16.87 ? 97   ARG A CB  1 
ATOM   799  C CG  . ARG A 1 98  ? -21.847 27.074 -10.535 1.00 16.75 ? 97   ARG A CG  1 
ATOM   800  C CD  . ARG A 1 98  ? -22.088 25.949 -11.548 1.00 17.44 ? 97   ARG A CD  1 
ATOM   801  N NE  . ARG A 1 98  ? -22.795 26.439 -12.730 1.00 17.86 ? 97   ARG A NE  1 
ATOM   802  C CZ  . ARG A 1 98  ? -22.221 27.049 -13.761 1.00 17.48 ? 97   ARG A CZ  1 
ATOM   803  N NH1 . ARG A 1 98  ? -20.902 27.215 -13.831 1.00 18.50 ? 97   ARG A NH1 1 
ATOM   804  N NH2 . ARG A 1 98  ? -22.989 27.513 -14.747 1.00 17.51 ? 97   ARG A NH2 1 
ATOM   805  N N   . TYR A 1 99  ? -21.336 27.550 -6.134  1.00 18.55 ? 98   TYR A N   1 
ATOM   806  C CA  . TYR A 1 99  ? -21.337 27.253 -4.710  1.00 18.99 ? 98   TYR A CA  1 
ATOM   807  C C   . TYR A 1 99  ? -22.774 26.914 -4.344  1.00 17.98 ? 98   TYR A C   1 
ATOM   808  O O   . TYR A 1 99  ? -23.678 27.717 -4.597  1.00 18.04 ? 98   TYR A O   1 
ATOM   809  C CB  . TYR A 1 99  ? -20.794 28.456 -3.914  1.00 16.64 ? 98   TYR A CB  1 
ATOM   810  C CG  . TYR A 1 99  ? -20.669 28.247 -2.420  1.00 17.96 ? 98   TYR A CG  1 
ATOM   811  C CD1 . TYR A 1 99  ? -19.625 27.496 -1.881  1.00 18.52 ? 98   TYR A CD1 1 
ATOM   812  C CD2 . TYR A 1 99  ? -21.582 28.818 -1.553  1.00 17.74 ? 98   TYR A CD2 1 
ATOM   813  C CE1 . TYR A 1 99  ? -19.509 27.314 -0.495  1.00 16.87 ? 98   TYR A CE1 1 
ATOM   814  C CE2 . TYR A 1 99  ? -21.476 28.650 -0.171  1.00 19.98 ? 98   TYR A CE2 1 
ATOM   815  C CZ  . TYR A 1 99  ? -20.448 27.891 0.344   1.00 21.52 ? 98   TYR A CZ  1 
ATOM   816  O OH  . TYR A 1 99  ? -20.352 27.731 1.707   1.00 19.62 ? 98   TYR A OH  1 
ATOM   817  N N   . TYR A 1 100 ? -22.982 25.712 -3.803  1.00 17.52 ? 99   TYR A N   1 
ATOM   818  C CA  . TYR A 1 100 ? -24.328 25.126 -3.645  1.00 17.89 ? 99   TYR A CA  1 
ATOM   819  C C   . TYR A 1 100 ? -25.109 25.198 -4.958  1.00 19.80 ? 99   TYR A C   1 
ATOM   820  O O   . TYR A 1 100 ? -26.305 25.501 -4.989  1.00 20.91 ? 99   TYR A O   1 
ATOM   821  C CB  . TYR A 1 100 ? -25.093 25.769 -2.487  1.00 20.76 ? 99   TYR A CB  1 
ATOM   822  C CG  . TYR A 1 100 ? -24.548 25.319 -1.152  1.00 19.34 ? 99   TYR A CG  1 
ATOM   823  C CD1 . TYR A 1 100 ? -24.843 24.050 -0.644  1.00 20.65 ? 99   TYR A CD1 1 
ATOM   824  C CD2 . TYR A 1 100 ? -23.713 26.137 -0.422  1.00 21.63 ? 99   TYR A CD2 1 
ATOM   825  C CE1 . TYR A 1 100 ? -24.327 23.623 0.585   1.00 21.91 ? 99   TYR A CE1 1 
ATOM   826  C CE2 . TYR A 1 100 ? -23.191 25.721 0.792   1.00 25.96 ? 99   TYR A CE2 1 
ATOM   827  C CZ  . TYR A 1 100 ? -23.498 24.466 1.290   1.00 24.23 ? 99   TYR A CZ  1 
ATOM   828  O OH  . TYR A 1 100 ? -22.970 24.065 2.510   1.00 22.96 ? 99   TYR A OH  1 
ATOM   829  N N   . ASN A 1 101 ? -24.386 24.959 -6.058  1.00 18.65 ? 100  ASN A N   1 
ATOM   830  C CA  A ASN A 1 101 ? -24.934 24.809 -7.402  0.59 20.38 ? 100  ASN A CA  1 
ATOM   831  C CA  B ASN A 1 101 ? -24.952 24.806 -7.396  0.41 20.42 ? 100  ASN A CA  1 
ATOM   832  C C   . ASN A 1 101 ? -25.511 26.106 -7.965  1.00 20.51 ? 100  ASN A C   1 
ATOM   833  O O   . ASN A 1 101 ? -26.269 26.078 -8.945  1.00 24.14 ? 100  ASN A O   1 
ATOM   834  C CB  A ASN A 1 101 ? -25.977 23.687 -7.429  0.59 21.72 ? 100  ASN A CB  1 
ATOM   835  C CB  B ASN A 1 101 ? -26.037 23.724 -7.420  0.41 21.73 ? 100  ASN A CB  1 
ATOM   836  C CG  A ASN A 1 101 ? -25.431 22.390 -6.848  0.59 24.66 ? 100  ASN A CG  1 
ATOM   837  C CG  B ASN A 1 101 ? -26.338 23.246 -8.815  0.41 26.40 ? 100  ASN A CG  1 
ATOM   838  O OD1 A ASN A 1 101 ? -24.616 21.718 -7.480  0.59 23.67 ? 100  ASN A OD1 1 
ATOM   839  O OD1 B ASN A 1 101 ? -25.476 23.300 -9.690  0.41 28.65 ? 100  ASN A OD1 1 
ATOM   840  N ND2 A ASN A 1 101 ? -25.836 22.058 -5.621  0.59 22.50 ? 100  ASN A ND2 1 
ATOM   841  N ND2 B ASN A 1 101 ? -27.568 22.801 -9.044  0.41 33.20 ? 100  ASN A ND2 1 
ATOM   842  N N   . SER A 1 102 ? -25.168 27.245 -7.376  1.00 19.60 ? 101  SER A N   1 
ATOM   843  C CA  . SER A 1 102 ? -25.491 28.561 -7.913  1.00 16.92 ? 101  SER A CA  1 
ATOM   844  C C   . SER A 1 102 ? -24.191 29.247 -8.312  1.00 17.39 ? 101  SER A C   1 
ATOM   845  O O   . SER A 1 102 ? -23.194 29.157 -7.594  1.00 19.74 ? 101  SER A O   1 
ATOM   846  C CB  . SER A 1 102 ? -26.226 29.439 -6.890  1.00 23.73 ? 101  SER A CB  1 
ATOM   847  O OG  . SER A 1 102 ? -27.441 28.833 -6.469  1.00 28.81 ? 101  SER A OG  1 
ATOM   848  N N   . ILE A 1 103 ? -24.209 29.951 -9.447  1.00 18.17 ? 102  ILE A N   1 
ATOM   849  C CA  . ILE A 1 103 ? -23.044 30.720 -9.872  1.00 17.29 ? 102  ILE A CA  1 
ATOM   850  C C   . ILE A 1 103 ? -22.607 31.672 -8.768  1.00 21.63 ? 102  ILE A C   1 
ATOM   851  O O   . ILE A 1 103 ? -23.431 32.368 -8.159  1.00 21.32 ? 102  ILE A O   1 
ATOM   852  C CB  . ILE A 1 103 ? -23.368 31.479 -11.172 1.00 19.74 ? 102  ILE A CB  1 
ATOM   853  C CG1 . ILE A 1 103 ? -23.431 30.496 -12.342 1.00 20.21 ? 102  ILE A CG1 1 
ATOM   854  C CG2 . ILE A 1 103 ? -22.313 32.552 -11.447 1.00 20.93 ? 102  ILE A CG2 1 
ATOM   855  C CD1 . ILE A 1 103 ? -24.008 31.085 -13.617 1.00 25.11 ? 102  ILE A CD1 1 
ATOM   856  N N   . ILE A 1 104 ? -21.301 31.699 -8.501  1.00 18.10 ? 103  ILE A N   1 
ATOM   857  C CA  . ILE A 1 104 ? -20.719 32.629 -7.537  1.00 18.11 ? 103  ILE A CA  1 
ATOM   858  C C   . ILE A 1 104 ? -20.750 34.027 -8.141  1.00 22.26 ? 103  ILE A C   1 
ATOM   859  O O   . ILE A 1 104 ? -19.932 34.352 -9.007  1.00 20.80 ? 103  ILE A O   1 
ATOM   860  C CB  . ILE A 1 104 ? -19.283 32.215 -7.183  1.00 17.76 ? 103  ILE A CB  1 
ATOM   861  C CG1 . ILE A 1 104 ? -19.268 30.782 -6.646  1.00 18.39 ? 103  ILE A CG1 1 
ATOM   862  C CG2 . ILE A 1 104 ? -18.685 33.199 -6.174  1.00 23.20 ? 103  ILE A CG2 1 
ATOM   863  C CD1 . ILE A 1 104 ? -17.879 30.224 -6.473  1.00 20.22 ? 103  ILE A CD1 1 
ATOM   864  N N   . SER A 1 105 ? -21.698 34.860 -7.726  1.00 20.65 ? 104  SER A N   1 
ATOM   865  C CA  . SER A 1 105 ? -21.827 36.179 -8.342  1.00 22.01 ? 104  SER A CA  1 
ATOM   866  C C   . SER A 1 105 ? -21.295 37.302 -7.463  1.00 22.66 ? 104  SER A C   1 
ATOM   867  O O   . SER A 1 105 ? -21.398 38.476 -7.845  1.00 23.55 ? 104  SER A O   1 
ATOM   868  C CB  . SER A 1 105 ? -23.294 36.447 -8.707  1.00 29.01 ? 104  SER A CB  1 
ATOM   869  O OG  . SER A 1 105 ? -24.098 36.364 -7.551  1.00 33.72 ? 104  SER A OG  1 
ATOM   870  N N   . SER A 1 106 ? -20.725 36.975 -6.302  1.00 20.91 ? 105  SER A N   1 
ATOM   871  C CA  . SER A 1 106 ? -20.165 37.971 -5.390  1.00 21.66 ? 105  SER A CA  1 
ATOM   872  C C   . SER A 1 106 ? -18.642 37.877 -5.369  1.00 17.74 ? 105  SER A C   1 
ATOM   873  O O   . SER A 1 106 ? -18.088 37.018 -4.670  1.00 19.05 ? 105  SER A O   1 
ATOM   874  C CB  . SER A 1 106 ? -20.724 37.775 -3.977  1.00 23.58 ? 105  SER A CB  1 
ATOM   875  O OG  . SER A 1 106 ? -20.087 38.647 -3.044  1.00 20.55 ? 105  SER A OG  1 
ATOM   876  N N   . PRO A 1 107 ? -17.926 38.740 -6.095  1.00 19.08 ? 106  PRO A N   1 
ATOM   877  C CA  . PRO A 1 107 ? -16.458 38.760 -5.954  1.00 16.95 ? 106  PRO A CA  1 
ATOM   878  C C   . PRO A 1 107 ? -16.013 39.001 -4.520  1.00 20.57 ? 106  PRO A C   1 
ATOM   879  O O   . PRO A 1 107 ? -15.015 38.420 -4.070  1.00 18.08 ? 106  PRO A O   1 
ATOM   880  C CB  . PRO A 1 107 ? -16.042 39.904 -6.884  1.00 20.07 ? 106  PRO A CB  1 
ATOM   881  C CG  . PRO A 1 107 ? -17.121 39.921 -7.945  1.00 28.29 ? 106  PRO A CG  1 
ATOM   882  C CD  . PRO A 1 107 ? -18.392 39.609 -7.193  1.00 21.34 ? 106  PRO A CD  1 
ATOM   883  N N   . SER A 1 108 ? -16.727 39.847 -3.777  1.00 20.78 ? 107  SER A N   1 
ATOM   884  C CA  A SER A 1 108 ? -16.336 40.100 -2.395  0.45 22.63 ? 107  SER A CA  1 
ATOM   885  C CA  B SER A 1 108 ? -16.322 40.097 -2.399  0.38 22.63 ? 107  SER A CA  1 
ATOM   886  C CA  C SER A 1 108 ? -16.352 40.104 -2.389  0.17 22.64 ? 107  SER A CA  1 
ATOM   887  C C   . SER A 1 108 ? -16.444 38.834 -1.554  1.00 17.97 ? 107  SER A C   1 
ATOM   888  O O   . SER A 1 108 ? -15.552 38.534 -0.752  1.00 20.00 ? 107  SER A O   1 
ATOM   889  C CB  A SER A 1 108 ? -17.188 41.223 -1.806  0.45 23.65 ? 107  SER A CB  1 
ATOM   890  C CB  B SER A 1 108 ? -17.135 41.247 -1.800  0.38 23.65 ? 107  SER A CB  1 
ATOM   891  C CB  C SER A 1 108 ? -17.244 41.195 -1.797  0.17 23.68 ? 107  SER A CB  1 
ATOM   892  O OG  A SER A 1 108 ? -16.757 41.562 -0.505  0.45 18.98 ? 107  SER A OG  1 
ATOM   893  O OG  B SER A 1 108 ? -18.516 40.949 -1.750  0.38 21.90 ? 107  SER A OG  1 
ATOM   894  O OG  C SER A 1 108 ? -17.338 42.312 -2.662  0.17 23.89 ? 107  SER A OG  1 
ATOM   895  N N   . ASP A 1 109 ? -17.531 38.070 -1.720  1.00 20.29 ? 108  ASP A N   1 
ATOM   896  C CA  . ASP A 1 109 ? -17.654 36.824 -0.965  1.00 16.47 ? 108  ASP A CA  1 
ATOM   897  C C   . ASP A 1 109 ? -16.546 35.848 -1.337  1.00 18.65 ? 108  ASP A C   1 
ATOM   898  O O   . ASP A 1 109 ? -15.999 35.158 -0.467  1.00 18.54 ? 108  ASP A O   1 
ATOM   899  C CB  . ASP A 1 109 ? -19.013 36.168 -1.211  1.00 21.99 ? 108  ASP A CB  1 
ATOM   900  C CG  . ASP A 1 109 ? -20.154 36.866 -0.497  1.00 27.88 ? 108  ASP A CG  1 
ATOM   901  O OD1 . ASP A 1 109 ? -19.923 37.825 0.272   1.00 25.08 ? 108  ASP A OD1 1 
ATOM   902  O OD2 . ASP A 1 109 ? -21.302 36.444 -0.726  1.00 28.72 ? 108  ASP A OD2 1 
ATOM   903  N N   . PHE A 1 110 ? -16.208 35.779 -2.630  1.00 16.74 ? 109  PHE A N   1 
ATOM   904  C CA  . PHE A 1 110 ? -15.162 34.880 -3.111  1.00 14.99 ? 109  PHE A CA  1 
ATOM   905  C C   . PHE A 1 110 ? -13.794 35.291 -2.581  1.00 15.73 ? 109  PHE A C   1 
ATOM   906  O O   . PHE A 1 110 ? -12.958 34.437 -2.246  1.00 16.36 ? 109  PHE A O   1 
ATOM   907  C CB  . PHE A 1 110 ? -15.198 34.892 -4.640  1.00 14.99 ? 109  PHE A CB  1 
ATOM   908  C CG  . PHE A 1 110 ? -14.498 33.731 -5.297  1.00 16.80 ? 109  PHE A CG  1 
ATOM   909  C CD1 . PHE A 1 110 ? -14.834 32.410 -4.991  1.00 15.45 ? 109  PHE A CD1 1 
ATOM   910  C CD2 . PHE A 1 110 ? -13.540 33.960 -6.267  1.00 15.53 ? 109  PHE A CD2 1 
ATOM   911  C CE1 . PHE A 1 110 ? -14.205 31.345 -5.662  1.00 15.38 ? 109  PHE A CE1 1 
ATOM   912  C CE2 . PHE A 1 110 ? -12.913 32.906 -6.917  1.00 15.26 ? 109  PHE A CE2 1 
ATOM   913  C CZ  . PHE A 1 110 ? -13.234 31.603 -6.621  1.00 16.12 ? 109  PHE A CZ  1 
ATOM   914  N N   . GLN A 1 111 ? -13.561 36.600 -2.481  1.00 17.83 ? 110  GLN A N   1 
ATOM   915  C CA  . GLN A 1 111 ? -12.303 37.089 -1.930  1.00 15.55 ? 110  GLN A CA  1 
ATOM   916  C C   . GLN A 1 111 ? -12.165 36.707 -0.458  1.00 15.36 ? 110  GLN A C   1 
ATOM   917  O O   . GLN A 1 111 ? -11.088 36.311 -0.019  1.00 18.47 ? 110  GLN A O   1 
ATOM   918  C CB  . GLN A 1 111 ? -12.208 38.604 -2.127  1.00 15.49 ? 110  GLN A CB  1 
ATOM   919  C CG  . GLN A 1 111 ? -10.897 39.171 -1.576  1.00 15.58 ? 110  GLN A CG  1 
ATOM   920  C CD  . GLN A 1 111 ? -10.624 40.596 -1.981  1.00 21.11 ? 110  GLN A CD  1 
ATOM   921  O OE1 . GLN A 1 111 ? -11.286 41.161 -2.850  1.00 23.14 ? 110  GLN A OE1 1 
ATOM   922  N NE2 . GLN A 1 111 ? -9.618  41.192 -1.350  1.00 19.81 ? 110  GLN A NE2 1 
ATOM   923  N N   . THR A 1 112 ? -13.258 36.767 0.306   1.00 17.83 ? 111  THR A N   1 
ATOM   924  C CA  . THR A 1 112 ? -13.200 36.344 1.704   1.00 17.97 ? 111  THR A CA  1 
ATOM   925  C C   . THR A 1 112 ? -12.908 34.851 1.827   1.00 21.98 ? 111  THR A C   1 
ATOM   926  O O   . THR A 1 112 ? -12.074 34.443 2.646   1.00 17.06 ? 111  THR A O   1 
ATOM   927  C CB  . THR A 1 112 ? -14.509 36.706 2.399   1.00 18.94 ? 111  THR A CB  1 
ATOM   928  O OG1 . THR A 1 112 ? -14.632 38.134 2.447   1.00 20.26 ? 111  THR A OG1 1 
ATOM   929  C CG2 . THR A 1 112 ? -14.540 36.139 3.801   1.00 20.86 ? 111  THR A CG2 1 
ATOM   930  N N   . PHE A 1 113 ? -13.575 34.018 1.017   1.00 17.35 ? 112  PHE A N   1 
ATOM   931  C CA  . PHE A 1 113 ? -13.230 32.600 0.955   1.00 13.54 ? 112  PHE A CA  1 
ATOM   932  C C   . PHE A 1 113 ? -11.738 32.407 0.720   1.00 17.69 ? 112  PHE A C   1 
ATOM   933  O O   . PHE A 1 113 ? -11.083 31.615 1.402   1.00 15.65 ? 112  PHE A O   1 
ATOM   934  C CB  . PHE A 1 113 ? -14.045 31.917 -0.160  1.00 16.94 ? 112  PHE A CB  1 
ATOM   935  C CG  . PHE A 1 113 ? -13.635 30.499 -0.437  1.00 17.33 ? 112  PHE A CG  1 
ATOM   936  C CD1 . PHE A 1 113 ? -14.129 29.445 0.323   1.00 17.98 ? 112  PHE A CD1 1 
ATOM   937  C CD2 . PHE A 1 113 ? -12.771 30.221 -1.496  1.00 15.36 ? 112  PHE A CD2 1 
ATOM   938  C CE1 . PHE A 1 113 ? -13.734 28.134 0.050   1.00 17.70 ? 112  PHE A CE1 1 
ATOM   939  C CE2 . PHE A 1 113 ? -12.358 28.935 -1.771  1.00 16.86 ? 112  PHE A CE2 1 
ATOM   940  C CZ  . PHE A 1 113 ? -12.844 27.880 -1.013  1.00 16.43 ? 112  PHE A CZ  1 
ATOM   941  N N   . TRP A 1 114 ? -11.177 33.146 -0.232  1.00 15.60 ? 113  TRP A N   1 
ATOM   942  C CA  . TRP A 1 114 ? -9.785  32.909 -0.584  1.00 14.07 ? 113  TRP A CA  1 
ATOM   943  C C   . TRP A 1 114 ? -8.822  33.456 0.460   1.00 15.23 ? 113  TRP A C   1 
ATOM   944  O O   . TRP A 1 114 ? -7.757  32.869 0.648   1.00 15.37 ? 113  TRP A O   1 
ATOM   945  C CB  . TRP A 1 114 ? -9.497  33.471 -1.981  1.00 15.59 ? 113  TRP A CB  1 
ATOM   946  C CG  . TRP A 1 114 ? -9.632  32.391 -2.981  1.00 13.49 ? 113  TRP A CG  1 
ATOM   947  C CD1 . TRP A 1 114 ? -10.567 32.277 -3.988  1.00 15.07 ? 113  TRP A CD1 1 
ATOM   948  C CD2 . TRP A 1 114 ? -8.818  31.230 -3.055  1.00 13.88 ? 113  TRP A CD2 1 
ATOM   949  N NE1 . TRP A 1 114 ? -10.350 31.113 -4.693  1.00 15.77 ? 113  TRP A NE1 1 
ATOM   950  C CE2 . TRP A 1 114 ? -9.280  30.456 -4.147  1.00 16.59 ? 113  TRP A CE2 1 
ATOM   951  C CE3 . TRP A 1 114 ? -7.720  30.770 -2.312  1.00 19.29 ? 113  TRP A CE3 1 
ATOM   952  C CZ2 . TRP A 1 114 ? -8.712  29.232 -4.481  1.00 14.53 ? 113  TRP A CZ2 1 
ATOM   953  C CZ3 . TRP A 1 114 ? -7.136  29.562 -2.661  1.00 18.12 ? 113  TRP A CZ3 1 
ATOM   954  C CH2 . TRP A 1 114 ? -7.629  28.809 -3.732  1.00 14.81 ? 113  TRP A CH2 1 
ATOM   955  N N   . LYS A 1 115 ? -9.177  34.535 1.164   1.00 16.83 ? 114  LYS A N   1 
ATOM   956  C CA  . LYS A 1 115 ? -8.342  34.937 2.291   1.00 16.66 ? 114  LYS A CA  1 
ATOM   957  C C   . LYS A 1 115 ? -8.356  33.859 3.366   1.00 15.41 ? 114  LYS A C   1 
ATOM   958  O O   . LYS A 1 115 ? -7.315  33.528 3.955   1.00 16.86 ? 114  LYS A O   1 
ATOM   959  C CB  . LYS A 1 115 ? -8.799  36.281 2.876   1.00 15.46 ? 114  LYS A CB  1 
ATOM   960  C CG  . LYS A 1 115 ? -7.806  36.813 3.923   1.00 16.75 ? 114  LYS A CG  1 
ATOM   961  C CD  . LYS A 1 115 ? -8.373  37.970 4.736   1.00 17.29 ? 114  LYS A CD  1 
ATOM   962  C CE  . LYS A 1 115 ? -7.294  38.504 5.692   1.00 25.89 ? 114  LYS A CE  1 
ATOM   963  N NZ  . LYS A 1 115 ? -7.907  39.308 6.782   1.00 29.90 ? 114  LYS A NZ  1 
ATOM   964  N N   . THR A 1 116 ? -9.527  33.279 3.618   1.00 17.06 ? 115  THR A N   1 
ATOM   965  C CA  . THR A 1 116 ? -9.632  32.208 4.606   1.00 16.12 ? 115  THR A CA  1 
ATOM   966  C C   . THR A 1 116 ? -8.740  31.025 4.241   1.00 16.62 ? 115  THR A C   1 
ATOM   967  O O   . THR A 1 116 ? -7.999  30.509 5.087   1.00 17.39 ? 115  THR A O   1 
ATOM   968  C CB  . THR A 1 116 ? -11.091 31.769 4.715   1.00 17.38 ? 115  THR A CB  1 
ATOM   969  O OG1 . THR A 1 116 ? -11.870 32.838 5.268   1.00 19.84 ? 115  THR A OG1 1 
ATOM   970  C CG2 . THR A 1 116 ? -11.220 30.528 5.590   1.00 19.93 ? 115  THR A CG2 1 
ATOM   971  N N   . VAL A 1 117 ? -8.782  30.599 2.971   1.00 16.85 ? 116  VAL A N   1 
ATOM   972  C CA  . VAL A 1 117 ? -7.994  29.444 2.532   1.00 17.20 ? 116  VAL A CA  1 
ATOM   973  C C   . VAL A 1 117 ? -6.509  29.782 2.507   1.00 18.26 ? 116  VAL A C   1 
ATOM   974  O O   . VAL A 1 117 ? -5.677  29.004 2.994   1.00 15.84 ? 116  VAL A O   1 
ATOM   975  C CB  . VAL A 1 117 ? -8.482  28.948 1.154   1.00 14.48 ? 116  VAL A CB  1 
ATOM   976  C CG1 . VAL A 1 117 ? -7.548  27.848 0.628   1.00 16.65 ? 116  VAL A CG1 1 
ATOM   977  C CG2 . VAL A 1 117 ? -9.910  28.421 1.283   1.00 18.11 ? 116  VAL A CG2 1 
ATOM   978  N N   . ALA A 1 118 ? -6.149  30.926 1.910   1.00 15.56 ? 117  ALA A N   1 
ATOM   979  C CA  . ALA A 1 118 ? -4.736  31.295 1.810   1.00 14.57 ? 117  ALA A CA  1 
ATOM   980  C C   . ALA A 1 118 ? -4.086  31.443 3.174   1.00 16.49 ? 117  ALA A C   1 
ATOM   981  O O   . ALA A 1 118 ? -2.895  31.137 3.323   1.00 18.02 ? 117  ALA A O   1 
ATOM   982  C CB  . ALA A 1 118 ? -4.564  32.593 1.014   1.00 17.77 ? 117  ALA A CB  1 
ATOM   983  N N   . SER A 1 119 ? -4.848  31.904 4.174   1.00 16.80 ? 118  SER A N   1 
ATOM   984  C CA  . SER A 1 119 ? -4.309  32.068 5.525   1.00 15.92 ? 118  SER A CA  1 
ATOM   985  C C   . SER A 1 119 ? -3.793  30.761 6.097   1.00 18.91 ? 118  SER A C   1 
ATOM   986  O O   . SER A 1 119 ? -2.852  30.774 6.902   1.00 19.13 ? 118  SER A O   1 
ATOM   987  C CB  . SER A 1 119 ? -5.375  32.655 6.451   1.00 20.07 ? 118  SER A CB  1 
ATOM   988  O OG  . SER A 1 119 ? -5.659  33.992 6.103   1.00 21.21 ? 118  SER A OG  1 
ATOM   989  N N   . GLN A 1 120 ? -4.376  29.626 5.693   1.00 17.06 ? 119  GLN A N   1 
ATOM   990  C CA  . GLN A 1 120 ? -3.933  28.331 6.215   1.00 15.90 ? 119  GLN A CA  1 
ATOM   991  C C   . GLN A 1 120 ? -2.600  27.892 5.627   1.00 21.06 ? 119  GLN A C   1 
ATOM   992  O O   . GLN A 1 120 ? -1.953  26.997 6.178   1.00 23.90 ? 119  GLN A O   1 
ATOM   993  C CB  . GLN A 1 120 ? -4.988  27.264 5.927   1.00 18.33 ? 119  GLN A CB  1 
ATOM   994  C CG  . GLN A 1 120 ? -6.322  27.514 6.597   1.00 18.67 ? 119  GLN A CG  1 
ATOM   995  C CD  . GLN A 1 120 ? -6.288  27.113 8.053   1.00 21.75 ? 119  GLN A CD  1 
ATOM   996  O OE1 . GLN A 1 120 ? -5.498  26.243 8.446   1.00 18.14 ? 119  GLN A OE1 1 
ATOM   997  N NE2 . GLN A 1 120 ? -7.129  27.753 8.868   1.00 19.18 ? 119  GLN A NE2 1 
ATOM   998  N N   . PHE A 1 121 ? -2.176  28.492 4.511   1.00 17.60 ? 120  PHE A N   1 
ATOM   999  C CA  . PHE A 1 121 ? -1.005  28.028 3.782   1.00 14.90 ? 120  PHE A CA  1 
ATOM   1000 C C   . PHE A 1 121 ? -0.028  29.155 3.464   1.00 16.66 ? 120  PHE A C   1 
ATOM   1001 O O   . PHE A 1 121 ? 0.892   28.949 2.665   1.00 17.39 ? 120  PHE A O   1 
ATOM   1002 C CB  . PHE A 1 121 ? -1.457  27.331 2.483   1.00 17.40 ? 120  PHE A CB  1 
ATOM   1003 C CG  . PHE A 1 121 ? -2.370  26.158 2.727   1.00 16.53 ? 120  PHE A CG  1 
ATOM   1004 C CD1 . PHE A 1 121 ? -1.860  24.982 3.274   1.00 22.79 ? 120  PHE A CD1 1 
ATOM   1005 C CD2 . PHE A 1 121 ? -3.732  26.237 2.437   1.00 16.66 ? 120  PHE A CD2 1 
ATOM   1006 C CE1 . PHE A 1 121 ? -2.682  23.880 3.517   1.00 19.45 ? 120  PHE A CE1 1 
ATOM   1007 C CE2 . PHE A 1 121 ? -4.576  25.136 2.678   1.00 16.60 ? 120  PHE A CE2 1 
ATOM   1008 C CZ  . PHE A 1 121 ? -4.043  23.956 3.226   1.00 15.38 ? 120  PHE A CZ  1 
ATOM   1009 N N   . ALA A 1 122 ? -0.180  30.324 4.096   1.00 17.74 ? 121  ALA A N   1 
ATOM   1010 C CA  . ALA A 1 122 ? 0.507   31.526 3.630   1.00 17.28 ? 121  ALA A CA  1 
ATOM   1011 C C   . ALA A 1 122 ? 2.027   31.417 3.710   1.00 19.69 ? 121  ALA A C   1 
ATOM   1012 O O   . ALA A 1 122 ? 2.724   32.066 2.923   1.00 19.06 ? 121  ALA A O   1 
ATOM   1013 C CB  . ALA A 1 122 ? 0.015   32.747 4.410   1.00 16.25 ? 121  ALA A CB  1 
ATOM   1014 N N   . SER A 1 123 ? 2.561   30.622 4.636   1.00 18.53 ? 122  SER A N   1 
ATOM   1015 C CA  . SER A 1 123 ? 4.003   30.462 4.781   1.00 19.20 ? 122  SER A CA  1 
ATOM   1016 C C   . SER A 1 123 ? 4.590   29.359 3.904   1.00 20.13 ? 122  SER A C   1 
ATOM   1017 O O   . SER A 1 123 ? 5.812   29.162 3.925   1.00 24.72 ? 122  SER A O   1 
ATOM   1018 C CB  . SER A 1 123 ? 4.359   30.169 6.240   1.00 25.95 ? 122  SER A CB  1 
ATOM   1019 O OG  . SER A 1 123 ? 4.166   28.789 6.509   1.00 37.53 ? 122  SER A OG  1 
ATOM   1020 N N   . ASN A 1 124 ? 3.774   28.638 3.141   1.00 17.19 ? 123  ASN A N   1 
ATOM   1021 C CA  . ASN A 1 124 ? 4.266   27.471 2.418   1.00 17.29 ? 123  ASN A CA  1 
ATOM   1022 C C   . ASN A 1 124 ? 4.497   27.836 0.962   1.00 18.76 ? 123  ASN A C   1 
ATOM   1023 O O   . ASN A 1 124 ? 3.523   27.936 0.194   1.00 16.57 ? 123  ASN A O   1 
ATOM   1024 C CB  . ASN A 1 124 ? 3.276   26.309 2.529   1.00 19.10 ? 123  ASN A CB  1 
ATOM   1025 C CG  . ASN A 1 124 ? 3.853   24.987 2.042   1.00 21.47 ? 123  ASN A CG  1 
ATOM   1026 O OD1 . ASN A 1 124 ? 4.791   24.952 1.237   1.00 18.94 ? 123  ASN A OD1 1 
ATOM   1027 N ND2 . ASN A 1 124 ? 3.280   23.886 2.518   1.00 19.32 ? 123  ASN A ND2 1 
ATOM   1028 N N   . PRO A 1 125 ? 5.750   28.003 0.524   1.00 17.44 ? 124  PRO A N   1 
ATOM   1029 C CA  . PRO A 1 125 ? 6.001   28.438 -0.857  1.00 17.87 ? 124  PRO A CA  1 
ATOM   1030 C C   . PRO A 1 125 ? 5.765   27.356 -1.894  1.00 18.66 ? 124  PRO A C   1 
ATOM   1031 O O   . PRO A 1 125 ? 5.784   27.666 -3.085  1.00 18.65 ? 124  PRO A O   1 
ATOM   1032 C CB  . PRO A 1 125 ? 7.471   28.869 -0.823  1.00 20.82 ? 124  PRO A CB  1 
ATOM   1033 C CG  . PRO A 1 125 ? 8.065   28.025 0.255   1.00 23.34 ? 124  PRO A CG  1 
ATOM   1034 C CD  . PRO A 1 125 ? 6.994   27.855 1.302   1.00 21.05 ? 124  PRO A CD  1 
ATOM   1035 N N   . LEU A 1 126 ? 5.538   26.110 -1.491  1.00 16.02 ? 125  LEU A N   1 
ATOM   1036 C CA  . LEU A 1 126 ? 5.264   25.041 -2.438  1.00 17.22 ? 125  LEU A CA  1 
ATOM   1037 C C   . LEU A 1 126 ? 3.772   24.790 -2.619  1.00 17.01 ? 125  LEU A C   1 
ATOM   1038 O O   . LEU A 1 126 ? 3.394   23.910 -3.396  1.00 17.84 ? 125  LEU A O   1 
ATOM   1039 C CB  . LEU A 1 126 ? 5.977   23.758 -1.996  1.00 17.53 ? 125  LEU A CB  1 
ATOM   1040 C CG  . LEU A 1 126 ? 7.500   23.849 -1.939  1.00 18.38 ? 125  LEU A CG  1 
ATOM   1041 C CD1 . LEU A 1 126 ? 8.061   22.563 -1.370  1.00 18.72 ? 125  LEU A CD1 1 
ATOM   1042 C CD2 . LEU A 1 126 ? 8.028   24.045 -3.365  1.00 21.99 ? 125  LEU A CD2 1 
ATOM   1043 N N   . VAL A 1 127 ? 2.908   25.551 -1.934  1.00 12.92 ? 126  VAL A N   1 
ATOM   1044 C CA  . VAL A 1 127 ? 1.481   25.526 -2.237  1.00 12.52 ? 126  VAL A CA  1 
ATOM   1045 C C   . VAL A 1 127 ? 1.212   26.403 -3.450  1.00 14.05 ? 126  VAL A C   1 
ATOM   1046 O O   . VAL A 1 127 ? 1.776   27.494 -3.579  1.00 15.20 ? 126  VAL A O   1 
ATOM   1047 C CB  . VAL A 1 127 ? 0.677   26.002 -1.015  1.00 14.02 ? 126  VAL A CB  1 
ATOM   1048 C CG1 . VAL A 1 127 ? -0.783  26.269 -1.393  1.00 17.07 ? 126  VAL A CG1 1 
ATOM   1049 C CG2 . VAL A 1 127 ? 0.754   24.957 0.055   1.00 16.92 ? 126  VAL A CG2 1 
ATOM   1050 N N   . ILE A 1 128 ? 0.339   25.929 -4.330  1.00 14.20 ? 127  ILE A N   1 
ATOM   1051 C CA  . ILE A 1 128 ? -0.153  26.683 -5.479  1.00 12.78 ? 127  ILE A CA  1 
ATOM   1052 C C   . ILE A 1 128 ? -1.653  26.825 -5.307  1.00 13.19 ? 127  ILE A C   1 
ATOM   1053 O O   . ILE A 1 128 ? -2.338  25.834 -5.044  1.00 17.22 ? 127  ILE A O   1 
ATOM   1054 C CB  . ILE A 1 128 ? 0.174   25.975 -6.801  1.00 14.84 ? 127  ILE A CB  1 
ATOM   1055 C CG1 . ILE A 1 128 ? 1.683   25.920 -7.007  1.00 15.02 ? 127  ILE A CG1 1 
ATOM   1056 C CG2 . ILE A 1 128 ? -0.441  26.727 -7.971  1.00 13.15 ? 127  ILE A CG2 1 
ATOM   1057 C CD1 . ILE A 1 128 ? 2.108   25.008 -8.185  1.00 14.02 ? 127  ILE A CD1 1 
ATOM   1058 N N   . PHE A 1 129 ? -2.162  28.043 -5.430  1.00 11.74 ? 128  PHE A N   1 
ATOM   1059 C CA  . PHE A 1 129 ? -3.585  28.279 -5.251  1.00 12.68 ? 128  PHE A CA  1 
ATOM   1060 C C   . PHE A 1 129 ? -4.249  28.301 -6.620  1.00 15.02 ? 128  PHE A C   1 
ATOM   1061 O O   . PHE A 1 129 ? -3.808  29.033 -7.501  1.00 16.95 ? 128  PHE A O   1 
ATOM   1062 C CB  . PHE A 1 129 ? -3.839  29.606 -4.528  1.00 13.00 ? 128  PHE A CB  1 
ATOM   1063 C CG  . PHE A 1 129 ? -3.174  29.708 -3.174  1.00 14.55 ? 128  PHE A CG  1 
ATOM   1064 C CD1 . PHE A 1 129 ? -3.644  28.964 -2.106  1.00 16.57 ? 128  PHE A CD1 1 
ATOM   1065 C CD2 . PHE A 1 129 ? -2.090  30.546 -2.973  1.00 16.40 ? 128  PHE A CD2 1 
ATOM   1066 C CE1 . PHE A 1 129 ? -3.041  29.060 -0.855  1.00 16.10 ? 128  PHE A CE1 1 
ATOM   1067 C CE2 . PHE A 1 129 ? -1.487  30.641 -1.738  1.00 16.90 ? 128  PHE A CE2 1 
ATOM   1068 C CZ  . PHE A 1 129 ? -1.971  29.898 -0.678  1.00 16.63 ? 128  PHE A CZ  1 
ATOM   1069 N N   . ASP A 1 130 ? -5.330  27.539 -6.778  1.00 12.40 ? 129  ASP A N   1 
ATOM   1070 C CA  . ASP A 1 130 ? -6.045  27.403 -8.046  1.00 11.33 ? 129  ASP A CA  1 
ATOM   1071 C C   . ASP A 1 130 ? -7.419  28.028 -7.833  1.00 12.95 ? 129  ASP A C   1 
ATOM   1072 O O   . ASP A 1 130 ? -8.175  27.546 -6.990  1.00 13.96 ? 129  ASP A O   1 
ATOM   1073 C CB  . ASP A 1 130 ? -6.139  25.917 -8.393  1.00 13.41 ? 129  ASP A CB  1 
ATOM   1074 C CG  . ASP A 1 130 ? -6.674  25.634 -9.776  1.00 14.14 ? 129  ASP A CG  1 
ATOM   1075 O OD1 . ASP A 1 130 ? -7.445  26.462 -10.331 1.00 14.67 ? 129  ASP A OD1 1 
ATOM   1076 O OD2 . ASP A 1 130 ? -6.335  24.530 -10.274 1.00 14.58 ? 129  ASP A OD2 1 
ATOM   1077 N N   . THR A 1 131 ? -7.741  29.105 -8.564  1.00 14.59 ? 130  THR A N   1 
ATOM   1078 C CA  . THR A 1 131 ? -8.874  29.931 -8.118  1.00 11.42 ? 130  THR A CA  1 
ATOM   1079 C C   . THR A 1 131 ? -10.191 29.148 -8.125  1.00 14.93 ? 130  THR A C   1 
ATOM   1080 O O   . THR A 1 131 ? -11.011 29.300 -7.207  1.00 14.40 ? 130  THR A O   1 
ATOM   1081 C CB  . THR A 1 131 ? -9.025  31.210 -8.958  1.00 12.32 ? 130  THR A CB  1 
ATOM   1082 O OG1 . THR A 1 131 ? -9.424  30.878 -10.290 1.00 13.90 ? 130  THR A OG1 1 
ATOM   1083 C CG2 . THR A 1 131 ? -7.727  32.019 -9.022  1.00 13.55 ? 130  THR A CG2 1 
ATOM   1084 N N   . ASN A 1 132 ? -10.421 28.322 -9.147  1.00 14.23 ? 131  ASN A N   1 
ATOM   1085 C CA  . ASN A 1 132 ? -11.582 27.442 -9.215  1.00 12.09 ? 131  ASN A CA  1 
ATOM   1086 C C   . ASN A 1 132 ? -11.430 26.558 -10.437 1.00 14.11 ? 131  ASN A C   1 
ATOM   1087 O O   . ASN A 1 132 ? -10.913 27.010 -11.461 1.00 15.44 ? 131  ASN A O   1 
ATOM   1088 C CB  . ASN A 1 132 ? -12.904 28.230 -9.313  1.00 14.34 ? 131  ASN A CB  1 
ATOM   1089 C CG  . ASN A 1 132 ? -13.944 27.768 -8.289  1.00 16.71 ? 131  ASN A CG  1 
ATOM   1090 O OD1 . ASN A 1 132 ? -14.989 27.179 -8.640  1.00 14.94 ? 131  ASN A OD1 1 
ATOM   1091 N ND2 . ASN A 1 132 ? -13.659 28.015 -7.016  1.00 13.79 ? 131  ASN A ND2 1 
ATOM   1092 N N   . ASN A 1 133 ? -11.893 25.317 -10.335 1.00 13.54 ? 132  ASN A N   1 
ATOM   1093 C CA  . ASN A 1 133 ? -11.838 24.369 -11.452 1.00 13.84 ? 132  ASN A CA  1 
ATOM   1094 C C   . ASN A 1 133 ? -12.931 24.648 -12.483 1.00 14.19 ? 132  ASN A C   1 
ATOM   1095 O O   . ASN A 1 133 ? -14.121 24.604 -12.158 1.00 15.38 ? 132  ASN A O   1 
ATOM   1096 C CB  . ASN A 1 133 ? -11.999 22.943 -10.935 1.00 14.46 ? 132  ASN A CB  1 
ATOM   1097 C CG  . ASN A 1 133 ? -12.006 21.942 -12.058 1.00 16.07 ? 132  ASN A CG  1 
ATOM   1098 O OD1 . ASN A 1 133 ? -10.969 21.690 -12.659 1.00 14.88 ? 132  ASN A OD1 1 
ATOM   1099 N ND2 . ASN A 1 133 ? -13.170 21.350 -12.340 1.00 17.72 ? 132  ASN A ND2 1 
ATOM   1100 N N   . GLN A 1 134 ? -12.522 24.880 -13.725 1.00 12.80 ? 133  GLN A N   1 
ATOM   1101 C CA  . GLN A 1 134 ? -13.398 24.820 -14.912 1.00 14.28 ? 133  GLN A CA  1 
ATOM   1102 C C   . GLN A 1 134 ? -14.658 25.682 -14.774 1.00 16.77 ? 133  GLN A C   1 
ATOM   1103 O O   . GLN A 1 134 ? -15.790 25.182 -14.797 1.00 15.27 ? 133  GLN A O   1 
ATOM   1104 C CB  . GLN A 1 134 ? -13.776 23.367 -15.227 1.00 14.72 ? 133  GLN A CB  1 
ATOM   1105 C CG  . GLN A 1 134 ? -12.599 22.502 -15.674 1.00 15.23 ? 133  GLN A CG  1 
ATOM   1106 C CD  . GLN A 1 134 ? -13.030 21.116 -16.145 1.00 22.14 ? 133  GLN A CD  1 
ATOM   1107 O OE1 . GLN A 1 134 ? -14.159 20.694 -15.918 1.00 25.42 ? 133  GLN A OE1 1 
ATOM   1108 N NE2 . GLN A 1 134 ? -12.139 20.416 -16.835 1.00 23.53 ? 133  GLN A NE2 1 
ATOM   1109 N N   . TYR A 1 135 ? -14.455 27.001 -14.674 1.00 14.43 ? 134  TYR A N   1 
ATOM   1110 C CA  . TYR A 1 135 ? -15.560 27.933 -14.913 1.00 12.96 ? 134  TYR A CA  1 
ATOM   1111 C C   . TYR A 1 135 ? -16.232 27.592 -16.237 1.00 15.05 ? 134  TYR A C   1 
ATOM   1112 O O   . TYR A 1 135 ? -15.558 27.238 -17.210 1.00 15.67 ? 134  TYR A O   1 
ATOM   1113 C CB  . TYR A 1 135 ? -15.063 29.382 -14.967 1.00 12.13 ? 134  TYR A CB  1 
ATOM   1114 C CG  . TYR A 1 135 ? -14.315 29.873 -13.743 1.00 14.08 ? 134  TYR A CG  1 
ATOM   1115 C CD1 . TYR A 1 135 ? -12.925 29.779 -13.667 1.00 14.11 ? 134  TYR A CD1 1 
ATOM   1116 C CD2 . TYR A 1 135 ? -14.996 30.478 -12.685 1.00 13.15 ? 134  TYR A CD2 1 
ATOM   1117 C CE1 . TYR A 1 135 ? -12.238 30.247 -12.551 1.00 15.63 ? 134  TYR A CE1 1 
ATOM   1118 C CE2 . TYR A 1 135 ? -14.308 30.943 -11.573 1.00 15.19 ? 134  TYR A CE2 1 
ATOM   1119 C CZ  . TYR A 1 135 ? -12.945 30.836 -11.521 1.00 15.47 ? 134  TYR A CZ  1 
ATOM   1120 O OH  . TYR A 1 135 ? -12.271 31.283 -10.399 1.00 14.70 ? 134  TYR A OH  1 
ATOM   1121 N N   . HIS A 1 136 ? -17.560 27.702 -16.280 1.00 14.43 ? 135  HIS A N   1 
ATOM   1122 C CA  . HIS A 1 136 ? -18.272 27.388 -17.518 1.00 14.34 ? 135  HIS A CA  1 
ATOM   1123 C C   . HIS A 1 136 ? -19.676 27.968 -17.459 1.00 17.44 ? 135  HIS A C   1 
ATOM   1124 O O   . HIS A 1 136 ? -20.238 28.164 -16.379 1.00 17.43 ? 135  HIS A O   1 
ATOM   1125 C CB  . HIS A 1 136 ? -18.348 25.872 -17.755 1.00 16.68 ? 135  HIS A CB  1 
ATOM   1126 C CG  . HIS A 1 136 ? -19.220 25.162 -16.770 1.00 15.07 ? 135  HIS A CG  1 
ATOM   1127 N ND1 . HIS A 1 136 ? -20.571 24.963 -16.974 1.00 16.86 ? 135  HIS A ND1 1 
ATOM   1128 C CD2 . HIS A 1 136 ? -18.943 24.652 -15.544 1.00 13.90 ? 135  HIS A CD2 1 
ATOM   1129 C CE1 . HIS A 1 136 ? -21.083 24.337 -15.927 1.00 17.72 ? 135  HIS A CE1 1 
ATOM   1130 N NE2 . HIS A 1 136 ? -20.118 24.142 -15.041 1.00 15.94 ? 135  HIS A NE2 1 
ATOM   1131 N N   . ASP A 1 137 ? -20.249 28.204 -18.646 1.00 14.91 ? 136  ASP A N   1 
ATOM   1132 C CA  . ASP A 1 137 ? -21.636 28.656 -18.787 1.00 13.64 ? 136  ASP A CA  1 
ATOM   1133 C C   . ASP A 1 137 ? -21.978 29.751 -17.778 1.00 15.94 ? 136  ASP A C   1 
ATOM   1134 O O   . ASP A 1 137 ? -22.932 29.651 -17.000 1.00 16.35 ? 136  ASP A O   1 
ATOM   1135 C CB  . ASP A 1 137 ? -22.592 27.475 -18.673 1.00 16.16 ? 136  ASP A CB  1 
ATOM   1136 C CG  . ASP A 1 137 ? -22.280 26.400 -19.683 1.00 20.76 ? 136  ASP A CG  1 
ATOM   1137 O OD1 . ASP A 1 137 ? -22.344 26.687 -20.906 1.00 18.57 ? 136  ASP A OD1 1 
ATOM   1138 O OD2 . ASP A 1 137 ? -21.936 25.280 -19.268 1.00 18.50 ? 136  ASP A OD2 1 
ATOM   1139 N N   . MET A 1 138 ? -21.156 30.799 -17.778 1.00 15.71 ? 137  MET A N   1 
ATOM   1140 C CA  . MET A 1 138 ? -21.380 31.945 -16.912 1.00 17.30 ? 137  MET A CA  1 
ATOM   1141 C C   . MET A 1 138 ? -20.785 33.187 -17.575 1.00 16.83 ? 137  MET A C   1 
ATOM   1142 O O   . MET A 1 138 ? -20.097 33.104 -18.595 1.00 17.20 ? 137  MET A O   1 
ATOM   1143 C CB  . MET A 1 138 ? -20.786 31.673 -15.521 1.00 15.46 ? 137  MET A CB  1 
ATOM   1144 C CG  . MET A 1 138 ? -19.312 31.320 -15.572 1.00 17.82 ? 137  MET A CG  1 
ATOM   1145 S SD  . MET A 1 138 ? -18.726 30.588 -14.011 1.00 17.09 ? 137  MET A SD  1 
ATOM   1146 C CE  . MET A 1 138 ? -18.840 32.004 -12.884 1.00 16.57 ? 137  MET A CE  1 
ATOM   1147 N N   . ASP A 1 139 ? -21.070 34.351 -16.987 1.00 19.12 ? 138  ASP A N   1 
ATOM   1148 C CA  . ASP A 1 139 ? -20.696 35.629 -17.589 1.00 18.34 ? 138  ASP A CA  1 
ATOM   1149 C C   . ASP A 1 139 ? -19.177 35.779 -17.682 1.00 17.12 ? 138  ASP A C   1 
ATOM   1150 O O   . ASP A 1 139 ? -18.449 35.502 -16.718 1.00 17.47 ? 138  ASP A O   1 
ATOM   1151 C CB  . ASP A 1 139 ? -21.297 36.762 -16.760 1.00 17.38 ? 138  ASP A CB  1 
ATOM   1152 C CG  . ASP A 1 139 ? -21.011 38.116 -17.333 1.00 23.94 ? 138  ASP A CG  1 
ATOM   1153 O OD1 . ASP A 1 139 ? -21.784 38.566 -18.209 1.00 24.12 ? 138  ASP A OD1 1 
ATOM   1154 O OD2 . ASP A 1 139 ? -20.025 38.750 -16.899 1.00 20.98 ? 138  ASP A OD2 1 
ATOM   1155 N N   . GLN A 1 140 ? -18.696 36.228 -18.848 1.00 17.23 ? 139  GLN A N   1 
ATOM   1156 C CA  . GLN A 1 140 ? -17.252 36.272 -19.088 1.00 16.60 ? 139  GLN A CA  1 
ATOM   1157 C C   . GLN A 1 140 ? -16.563 37.329 -18.225 1.00 16.26 ? 139  GLN A C   1 
ATOM   1158 O O   . GLN A 1 140 ? -15.432 37.121 -17.775 1.00 17.02 ? 139  GLN A O   1 
ATOM   1159 C CB  . GLN A 1 140 ? -16.985 36.530 -20.572 1.00 16.06 ? 139  GLN A CB  1 
ATOM   1160 C CG  . GLN A 1 140 ? -15.516 36.392 -20.963 1.00 15.18 ? 139  GLN A CG  1 
ATOM   1161 C CD  . GLN A 1 140 ? -14.941 35.014 -20.630 1.00 15.89 ? 139  GLN A CD  1 
ATOM   1162 O OE1 . GLN A 1 140 ? -15.616 33.991 -20.807 1.00 18.03 ? 139  GLN A OE1 1 
ATOM   1163 N NE2 . GLN A 1 140 ? -13.690 34.981 -20.148 1.00 14.59 ? 139  GLN A NE2 1 
ATOM   1164 N N   . THR A 1 141 ? -17.218 38.469 -17.990 1.00 16.91 ? 140  THR A N   1 
ATOM   1165 C CA  . THR A 1 141 ? -16.641 39.478 -17.106 1.00 17.46 ? 140  THR A CA  1 
ATOM   1166 C C   . THR A 1 141 ? -16.616 38.981 -15.673 1.00 18.40 ? 140  THR A C   1 
ATOM   1167 O O   . THR A 1 141 ? -15.645 39.224 -14.941 1.00 15.76 ? 140  THR A O   1 
ATOM   1168 C CB  . THR A 1 141 ? -17.429 40.782 -17.221 1.00 17.59 ? 140  THR A CB  1 
ATOM   1169 O OG1 . THR A 1 141 ? -17.267 41.290 -18.551 1.00 19.66 ? 140  THR A OG1 1 
ATOM   1170 C CG2 . THR A 1 141 ? -16.934 41.831 -16.220 1.00 20.45 ? 140  THR A CG2 1 
ATOM   1171 N N   . LEU A 1 142 ? -17.663 38.250 -15.263 1.00 17.02 ? 141  LEU A N   1 
ATOM   1172 C CA  . LEU A 1 142 ? -17.675 37.682 -13.918 1.00 16.76 ? 141  LEU A CA  1 
ATOM   1173 C C   . LEU A 1 142 ? -16.499 36.728 -13.714 1.00 16.58 ? 141  LEU A C   1 
ATOM   1174 O O   . LEU A 1 142 ? -15.842 36.768 -12.666 1.00 18.44 ? 141  LEU A O   1 
ATOM   1175 C CB  . LEU A 1 142 ? -19.007 36.971 -13.650 1.00 16.57 ? 141  LEU A CB  1 
ATOM   1176 C CG  . LEU A 1 142 ? -19.132 36.210 -12.321 1.00 18.22 ? 141  LEU A CG  1 
ATOM   1177 C CD1 . LEU A 1 142 ? -18.987 37.155 -11.133 1.00 18.88 ? 141  LEU A CD1 1 
ATOM   1178 C CD2 . LEU A 1 142 ? -20.479 35.475 -12.231 1.00 18.31 ? 141  LEU A CD2 1 
ATOM   1179 N N   . VAL A 1 143 ? -16.182 35.897 -14.719 1.00 15.37 ? 142  VAL A N   1 
ATOM   1180 C CA  . VAL A 1 143 ? -15.048 34.971 -14.577 1.00 15.51 ? 142  VAL A CA  1 
ATOM   1181 C C   . VAL A 1 143 ? -13.748 35.743 -14.347 1.00 14.97 ? 142  VAL A C   1 
ATOM   1182 O O   . VAL A 1 143 ? -12.941 35.396 -13.464 1.00 15.47 ? 142  VAL A O   1 
ATOM   1183 C CB  . VAL A 1 143 ? -14.952 34.036 -15.801 1.00 15.39 ? 142  VAL A CB  1 
ATOM   1184 C CG1 . VAL A 1 143 ? -13.636 33.235 -15.763 1.00 14.24 ? 142  VAL A CG1 1 
ATOM   1185 C CG2 . VAL A 1 143 ? -16.124 33.084 -15.829 1.00 15.84 ? 142  VAL A CG2 1 
ATOM   1186 N N   . LEU A 1 144 ? -13.530 36.810 -15.121 1.00 15.37 ? 143  LEU A N   1 
ATOM   1187 C CA  . LEU A 1 144 ? -12.376 37.672 -14.888 1.00 16.31 ? 143  LEU A CA  1 
ATOM   1188 C C   . LEU A 1 144 ? -12.374 38.204 -13.462 1.00 15.26 ? 143  LEU A C   1 
ATOM   1189 O O   . LEU A 1 144 ? -11.359 38.135 -12.754 1.00 14.85 ? 143  LEU A O   1 
ATOM   1190 C CB  . LEU A 1 144 ? -12.389 38.829 -15.892 1.00 16.00 ? 143  LEU A CB  1 
ATOM   1191 C CG  . LEU A 1 144 ? -11.351 39.916 -15.654 1.00 14.94 ? 143  LEU A CG  1 
ATOM   1192 C CD1 . LEU A 1 144 ? -9.935  39.340 -15.867 1.00 15.04 ? 143  LEU A CD1 1 
ATOM   1193 C CD2 . LEU A 1 144 ? -11.603 41.085 -16.613 1.00 18.00 ? 143  LEU A CD2 1 
ATOM   1194 N N   . ASN A 1 145 ? -13.507 38.760 -13.031 1.00 14.95 ? 144  ASN A N   1 
ATOM   1195 C CA  . ASN A 1 145 ? -13.548 39.411 -11.723 1.00 13.27 ? 144  ASN A CA  1 
ATOM   1196 C C   . ASN A 1 145 ? -13.400 38.414 -10.582 1.00 17.10 ? 144  ASN A C   1 
ATOM   1197 O O   . ASN A 1 145 ? -12.870 38.776 -9.523  1.00 16.31 ? 144  ASN A O   1 
ATOM   1198 C CB  . ASN A 1 145 ? -14.858 40.197 -11.563 1.00 17.12 ? 144  ASN A CB  1 
ATOM   1199 C CG  . ASN A 1 145 ? -14.945 41.381 -12.504 1.00 19.26 ? 144  ASN A CG  1 
ATOM   1200 O OD1 . ASN A 1 145 ? -13.927 41.883 -12.991 1.00 21.41 ? 144  ASN A OD1 1 
ATOM   1201 N ND2 . ASN A 1 145 ? -16.162 41.850 -12.745 1.00 19.17 ? 144  ASN A ND2 1 
ATOM   1202 N N   . LEU A 1 146 ? -13.900 37.180 -10.753 1.00 14.06 ? 145  LEU A N   1 
ATOM   1203 C CA  . LEU A 1 146 ? -13.703 36.159 -9.718  1.00 13.62 ? 145  LEU A CA  1 
ATOM   1204 C C   . LEU A 1 146 ? -12.238 35.775 -9.592  1.00 16.29 ? 145  LEU A C   1 
ATOM   1205 O O   . LEU A 1 146 ? -11.717 35.647 -8.475  1.00 15.59 ? 145  LEU A O   1 
ATOM   1206 C CB  . LEU A 1 146 ? -14.530 34.914 -10.015 1.00 13.65 ? 145  LEU A CB  1 
ATOM   1207 C CG  . LEU A 1 146 ? -16.047 35.016 -9.862  1.00 15.88 ? 145  LEU A CG  1 
ATOM   1208 C CD1 . LEU A 1 146 ? -16.697 33.655 -10.165 1.00 15.62 ? 145  LEU A CD1 1 
ATOM   1209 C CD2 . LEU A 1 146 ? -16.392 35.485 -8.458  1.00 15.61 ? 145  LEU A CD2 1 
ATOM   1210 N N   . ASN A 1 147 ? -11.554 35.594 -10.725 1.00 16.53 ? 146  ASN A N   1 
ATOM   1211 C CA  . ASN A 1 147 ? -10.124 35.315 -10.663 1.00 13.53 ? 146  ASN A CA  1 
ATOM   1212 C C   . ASN A 1 147 ? -9.381  36.454 -9.977  1.00 14.87 ? 146  ASN A C   1 
ATOM   1213 O O   . ASN A 1 147 ? -8.479  36.212 -9.168  1.00 13.74 ? 146  ASN A O   1 
ATOM   1214 C CB  . ASN A 1 147 ? -9.579  35.065 -12.079 1.00 13.60 ? 146  ASN A CB  1 
ATOM   1215 C CG  . ASN A 1 147 ? -9.811  33.627 -12.549 1.00 13.09 ? 146  ASN A CG  1 
ATOM   1216 O OD1 . ASN A 1 147 ? -9.060  32.710 -12.198 1.00 13.46 ? 146  ASN A OD1 1 
ATOM   1217 N ND2 . ASN A 1 147 ? -10.865 33.420 -13.346 1.00 13.75 ? 146  ASN A ND2 1 
ATOM   1218 N N   . GLN A 1 148 ? -9.730  37.702 -10.297 1.00 13.27 ? 147  GLN A N   1 
ATOM   1219 C CA  . GLN A 1 148 ? -9.032  38.825 -9.673  1.00 12.21 ? 147  GLN A CA  1 
ATOM   1220 C C   . GLN A 1 148 ? -9.324  38.886 -8.177  1.00 14.98 ? 147  GLN A C   1 
ATOM   1221 O O   . GLN A 1 148 ? -8.424  39.171 -7.375  1.00 14.46 ? 147  GLN A O   1 
ATOM   1222 C CB  . GLN A 1 148 ? -9.395  40.150 -10.341 1.00 16.53 ? 147  GLN A CB  1 
ATOM   1223 C CG  . GLN A 1 148 ? -8.521  41.302 -9.807  1.00 14.67 ? 147  GLN A CG  1 
ATOM   1224 C CD  . GLN A 1 148 ? -7.085  41.138 -10.220 1.00 18.60 ? 147  GLN A CD  1 
ATOM   1225 O OE1 . GLN A 1 148 ? -6.799  41.045 -11.409 1.00 16.20 ? 147  GLN A OE1 1 
ATOM   1226 N NE2 . GLN A 1 148 ? -6.171  41.088 -9.253  1.00 15.54 ? 147  GLN A NE2 1 
ATOM   1227 N N   . ALA A 1 149 ? -10.570 38.612 -7.783  1.00 15.39 ? 148  ALA A N   1 
ATOM   1228 C CA  . ALA A 1 149 ? -10.916 38.642 -6.363  1.00 15.13 ? 148  ALA A CA  1 
ATOM   1229 C C   . ALA A 1 149 ? -10.158 37.572 -5.588  1.00 15.84 ? 148  ALA A C   1 
ATOM   1230 O O   . ALA A 1 149 ? -9.736  37.800 -4.440  1.00 16.59 ? 148  ALA A O   1 
ATOM   1231 C CB  . ALA A 1 149 ? -12.429 38.461 -6.206  1.00 16.46 ? 148  ALA A CB  1 
ATOM   1232 N N   . ALA A 1 150 ? -9.975  36.398 -6.201  1.00 14.48 ? 149  ALA A N   1 
ATOM   1233 C CA  . ALA A 1 150 ? -9.192  35.339 -5.578  1.00 13.67 ? 149  ALA A CA  1 
ATOM   1234 C C   . ALA A 1 150 ? -7.756  35.792 -5.355  1.00 16.35 ? 149  ALA A C   1 
ATOM   1235 O O   . ALA A 1 150 ? -7.197  35.616 -4.262  1.00 15.29 ? 149  ALA A O   1 
ATOM   1236 C CB  . ALA A 1 150 ? -9.231  34.085 -6.453  1.00 13.86 ? 149  ALA A CB  1 
ATOM   1237 N N   . ILE A 1 151 ? -7.138  36.366 -6.394  1.00 14.58 ? 150  ILE A N   1 
ATOM   1238 C CA  . ILE A 1 151 ? -5.772  36.873 -6.271  1.00 13.35 ? 150  ILE A CA  1 
ATOM   1239 C C   . ILE A 1 151 ? -5.683  37.888 -5.138  1.00 17.86 ? 150  ILE A C   1 
ATOM   1240 O O   . ILE A 1 151 ? -4.769  37.837 -4.300  1.00 14.96 ? 150  ILE A O   1 
ATOM   1241 C CB  . ILE A 1 151 ? -5.307  37.488 -7.602  1.00 14.46 ? 150  ILE A CB  1 
ATOM   1242 C CG1 . ILE A 1 151 ? -5.141  36.412 -8.658  1.00 11.96 ? 150  ILE A CG1 1 
ATOM   1243 C CG2 . ILE A 1 151 ? -3.967  38.232 -7.419  1.00 16.91 ? 150  ILE A CG2 1 
ATOM   1244 C CD1 . ILE A 1 151 ? -5.014  37.012 -10.080 1.00 16.56 ? 150  ILE A CD1 1 
ATOM   1245 N N   . ASP A 1 152 ? -6.628  38.834 -5.108  1.00 16.04 ? 151  ASP A N   1 
ATOM   1246 C CA  . ASP A 1 152 ? -6.603  39.868 -4.079  1.00 14.96 ? 151  ASP A CA  1 
ATOM   1247 C C   . ASP A 1 152 ? -6.725  39.252 -2.694  1.00 13.60 ? 151  ASP A C   1 
ATOM   1248 O O   . ASP A 1 152 ? -6.013  39.654 -1.765  1.00 14.30 ? 151  ASP A O   1 
ATOM   1249 C CB  . ASP A 1 152 ? -7.725  40.873 -4.312  1.00 14.95 ? 151  ASP A CB  1 
ATOM   1250 C CG  . ASP A 1 152 ? -7.528  41.720 -5.578  1.00 17.80 ? 151  ASP A CG  1 
ATOM   1251 O OD1 . ASP A 1 152 ? -6.475  41.608 -6.256  1.00 19.25 ? 151  ASP A OD1 1 
ATOM   1252 O OD2 . ASP A 1 152 ? -8.457  42.507 -5.869  1.00 17.96 ? 151  ASP A OD2 1 
ATOM   1253 N N   . GLY A 1 153 ? -7.613  38.269 -2.537  1.00 14.61 ? 152  GLY A N   1 
ATOM   1254 C CA  . GLY A 1 153 ? -7.777  37.647 -1.225  1.00 15.63 ? 152  GLY A CA  1 
ATOM   1255 C C   . GLY A 1 153 ? -6.546  36.876 -0.787  1.00 16.30 ? 152  GLY A C   1 
ATOM   1256 O O   . GLY A 1 153 ? -6.108  36.981 0.365   1.00 15.74 ? 152  GLY A O   1 
ATOM   1257 N N   . ILE A 1 154 ? -5.951  36.119 -1.713  1.00 15.53 ? 153  ILE A N   1 
ATOM   1258 C CA  . ILE A 1 154 ? -4.738  35.347 -1.430  1.00 14.73 ? 153  ILE A CA  1 
ATOM   1259 C C   . ILE A 1 154 ? -3.593  36.263 -0.998  1.00 16.80 ? 153  ILE A C   1 
ATOM   1260 O O   . ILE A 1 154 ? -2.953  36.049 0.043   1.00 14.92 ? 153  ILE A O   1 
ATOM   1261 C CB  . ILE A 1 154 ? -4.356  34.514 -2.672  1.00 13.48 ? 153  ILE A CB  1 
ATOM   1262 C CG1 . ILE A 1 154 ? -5.384  33.404 -2.900  1.00 12.86 ? 153  ILE A CG1 1 
ATOM   1263 C CG2 . ILE A 1 154 ? -2.943  33.952 -2.517  1.00 15.37 ? 153  ILE A CG2 1 
ATOM   1264 C CD1 . ILE A 1 154 ? -5.403  32.881 -4.362  1.00 11.95 ? 153  ILE A CD1 1 
ATOM   1265 N N   . ARG A 1 155 ? -3.315  37.304 -1.783  1.00 14.52 ? 154  ARG A N   1 
ATOM   1266 C CA  . ARG A 1 155 ? -2.205  38.182 -1.432  1.00 14.09 ? 154  ARG A CA  1 
ATOM   1267 C C   . ARG A 1 155 ? -2.500  38.973 -0.160  1.00 15.49 ? 154  ARG A C   1 
ATOM   1268 O O   . ARG A 1 155 ? -1.579  39.285 0.599   1.00 17.23 ? 154  ARG A O   1 
ATOM   1269 C CB  . ARG A 1 155 ? -1.898  39.127 -2.600  1.00 14.29 ? 154  ARG A CB  1 
ATOM   1270 C CG  . ARG A 1 155 ? -1.566  38.400 -3.929  1.00 15.00 ? 154  ARG A CG  1 
ATOM   1271 C CD  . ARG A 1 155 ? -0.448  37.370 -3.741  1.00 12.87 ? 154  ARG A CD  1 
ATOM   1272 N NE  . ARG A 1 155 ? -0.015  36.821 -5.026  1.00 13.70 ? 154  ARG A NE  1 
ATOM   1273 C CZ  . ARG A 1 155 ? 0.554   35.632 -5.194  1.00 14.44 ? 154  ARG A CZ  1 
ATOM   1274 N NH1 . ARG A 1 155 ? 0.740   34.794 -4.178  1.00 14.72 ? 154  ARG A NH1 1 
ATOM   1275 N NH2 . ARG A 1 155 ? 0.923   35.255 -6.420  1.00 14.17 ? 154  ARG A NH2 1 
ATOM   1276 N N   . SER A 1 156 ? -3.773  39.284 0.104   1.00 16.22 ? 155  SER A N   1 
ATOM   1277 C CA  . SER A 1 156 ? -4.111  40.014 1.330   1.00 19.07 ? 155  SER A CA  1 
ATOM   1278 C C   . SER A 1 156 ? -3.803  39.202 2.580   1.00 20.16 ? 155  SER A C   1 
ATOM   1279 O O   . SER A 1 156 ? -3.600  39.782 3.665   1.00 17.22 ? 155  SER A O   1 
ATOM   1280 C CB  . SER A 1 156 ? -5.592  40.403 1.336   1.00 19.10 ? 155  SER A CB  1 
ATOM   1281 O OG  . SER A 1 156 ? -6.387  39.322 1.800   1.00 16.78 ? 155  SER A OG  1 
ATOM   1282 N N   . ALA A 1 157 ? -3.808  37.872 2.468   1.00 16.63 ? 156  ALA A N   1 
ATOM   1283 C CA  . ALA A 1 157 ? -3.483  36.997 3.597   1.00 21.00 ? 156  ALA A CA  1 
ATOM   1284 C C   . ALA A 1 157 ? -1.990  36.912 3.879   1.00 21.67 ? 156  ALA A C   1 
ATOM   1285 O O   . ALA A 1 157 ? -1.596  36.213 4.822   1.00 22.73 ? 156  ALA A O   1 
ATOM   1286 C CB  . ALA A 1 157 ? -4.019  35.587 3.352   1.00 22.00 ? 156  ALA A CB  1 
ATOM   1287 N N   . GLY A 1 158 ? -1.159  37.590 3.091   1.00 16.52 ? 157  GLY A N   1 
ATOM   1288 C CA  . GLY A 1 158 ? 0.275   37.458 3.185   1.00 18.95 ? 157  GLY A CA  1 
ATOM   1289 C C   . GLY A 1 158 ? 0.837   36.258 2.464   1.00 21.53 ? 157  GLY A C   1 
ATOM   1290 O O   . GLY A 1 158 ? 2.020   35.939 2.633   1.00 19.07 ? 157  GLY A O   1 
ATOM   1291 N N   . ALA A 1 159 ? 0.026   35.577 1.663   1.00 17.83 ? 158  ALA A N   1 
ATOM   1292 C CA  . ALA A 1 159 ? 0.500   34.449 0.866   1.00 14.65 ? 158  ALA A CA  1 
ATOM   1293 C C   . ALA A 1 159 ? 1.024   35.041 -0.435  1.00 15.53 ? 158  ALA A C   1 
ATOM   1294 O O   . ALA A 1 159 ? 0.296   35.170 -1.418  1.00 16.51 ? 158  ALA A O   1 
ATOM   1295 C CB  . ALA A 1 159 ? -0.624  33.444 0.648   1.00 13.32 ? 158  ALA A CB  1 
ATOM   1296 N N   . THR A 1 160 ? 2.295   35.457 -0.422  1.00 16.20 ? 159  THR A N   1 
ATOM   1297 C CA  . THR A 1 160 ? 2.873   36.226 -1.525  1.00 15.40 ? 159  THR A CA  1 
ATOM   1298 C C   . THR A 1 160 ? 3.919   35.460 -2.322  1.00 18.63 ? 159  THR A C   1 
ATOM   1299 O O   . THR A 1 160 ? 4.303   35.918 -3.406  1.00 19.12 ? 159  THR A O   1 
ATOM   1300 C CB  . THR A 1 160 ? 3.523   37.520 -1.004  1.00 20.55 ? 159  THR A CB  1 
ATOM   1301 O OG1 . THR A 1 160 ? 4.467   37.196 0.028   1.00 20.32 ? 159  THR A OG1 1 
ATOM   1302 C CG2 . THR A 1 160 ? 2.477   38.452 -0.401  1.00 23.61 ? 159  THR A CG2 1 
ATOM   1303 N N   . SER A 1 161 ? 4.418   34.341 -1.801  1.00 15.99 ? 160  SER A N   1 
ATOM   1304 C CA  . SER A 1 161 ? 5.447   33.563 -2.483  1.00 16.73 ? 160  SER A CA  1 
ATOM   1305 C C   . SER A 1 161 ? 4.873   32.573 -3.487  1.00 15.12 ? 160  SER A C   1 
ATOM   1306 O O   . SER A 1 161 ? 5.617   32.059 -4.327  1.00 17.20 ? 160  SER A O   1 
ATOM   1307 C CB  . SER A 1 161 ? 6.280   32.783 -1.466  1.00 19.93 ? 160  SER A CB  1 
ATOM   1308 O OG  . SER A 1 161 ? 5.461   31.841 -0.799  1.00 20.75 ? 160  SER A OG  1 
ATOM   1309 N N   . GLN A 1 162 ? 3.578   32.285 -3.404  1.00 15.46 ? 161  GLN A N   1 
ATOM   1310 C CA  . GLN A 1 162 ? 2.975   31.170 -4.111  1.00 14.94 ? 161  GLN A CA  1 
ATOM   1311 C C   . GLN A 1 162 ? 2.525   31.558 -5.512  1.00 13.43 ? 161  GLN A C   1 
ATOM   1312 O O   . GLN A 1 162 ? 1.991   32.650 -5.724  1.00 14.22 ? 161  GLN A O   1 
ATOM   1313 C CB  . GLN A 1 162 ? 1.753   30.667 -3.348  1.00 13.96 ? 161  GLN A CB  1 
ATOM   1314 C CG  . GLN A 1 162 ? 2.072   30.059 -1.982  1.00 14.04 ? 161  GLN A CG  1 
ATOM   1315 C CD  . GLN A 1 162 ? 2.125   31.079 -0.863  1.00 16.54 ? 161  GLN A CD  1 
ATOM   1316 O OE1 . GLN A 1 162 ? 2.004   32.275 -1.090  1.00 14.46 ? 161  GLN A OE1 1 
ATOM   1317 N NE2 . GLN A 1 162 ? 2.325   30.601 0.356   1.00 17.21 ? 161  GLN A NE2 1 
ATOM   1318 N N   . TYR A 1 163 ? 2.657   30.619 -6.442  1.00 12.91 ? 162  TYR A N   1 
ATOM   1319 C CA  . TYR A 1 163 ? 1.991   30.775 -7.729  1.00 12.56 ? 162  TYR A CA  1 
ATOM   1320 C C   . TYR A 1 163 ? 0.477   30.691 -7.561  1.00 16.46 ? 162  TYR A C   1 
ATOM   1321 O O   . TYR A 1 163 ? -0.041  29.996 -6.679  1.00 15.46 ? 162  TYR A O   1 
ATOM   1322 C CB  . TYR A 1 163 ? 2.458   29.703 -8.720  1.00 11.36 ? 162  TYR A CB  1 
ATOM   1323 C CG  . TYR A 1 163 ? 3.877   29.901 -9.157  1.00 14.56 ? 162  TYR A CG  1 
ATOM   1324 C CD1 . TYR A 1 163 ? 4.182   30.754 -10.211 1.00 16.18 ? 162  TYR A CD1 1 
ATOM   1325 C CD2 . TYR A 1 163 ? 4.917   29.253 -8.501  1.00 14.34 ? 162  TYR A CD2 1 
ATOM   1326 C CE1 . TYR A 1 163 ? 5.492   30.934 -10.627 1.00 18.32 ? 162  TYR A CE1 1 
ATOM   1327 C CE2 . TYR A 1 163 ? 6.248   29.440 -8.910  1.00 19.25 ? 162  TYR A CE2 1 
ATOM   1328 C CZ  . TYR A 1 163 ? 6.509   30.285 -9.973  1.00 19.83 ? 162  TYR A CZ  1 
ATOM   1329 O OH  . TYR A 1 163 ? 7.802   30.487 -10.395 1.00 22.03 ? 162  TYR A OH  1 
ATOM   1330 N N   . ILE A 1 164 ? -0.235  31.403 -8.427  1.00 13.20 ? 163  ILE A N   1 
ATOM   1331 C CA  . ILE A 1 164 ? -1.689  31.321 -8.496  1.00 13.31 ? 163  ILE A CA  1 
ATOM   1332 C C   . ILE A 1 164 ? -2.058  30.817 -9.881  1.00 15.00 ? 163  ILE A C   1 
ATOM   1333 O O   . ILE A 1 164 ? -1.703  31.447 -10.889 1.00 14.92 ? 163  ILE A O   1 
ATOM   1334 C CB  . ILE A 1 164 ? -2.356  32.671 -8.199  1.00 12.81 ? 163  ILE A CB  1 
ATOM   1335 C CG1 . ILE A 1 164 ? -2.008  33.130 -6.773  1.00 13.69 ? 163  ILE A CG1 1 
ATOM   1336 C CG2 . ILE A 1 164 ? -3.887  32.562 -8.362  1.00 14.57 ? 163  ILE A CG2 1 
ATOM   1337 C CD1 . ILE A 1 164 ? -2.483  34.562 -6.483  1.00 15.46 ? 163  ILE A CD1 1 
ATOM   1338 N N   . PHE A 1 165 ? -2.757  29.685 -9.930  1.00 12.62 ? 164  PHE A N   1 
ATOM   1339 C CA  . PHE A 1 165 ? -3.318  29.161 -11.178 1.00 13.03 ? 164  PHE A CA  1 
ATOM   1340 C C   . PHE A 1 165 ? -4.691  29.800 -11.387 1.00 14.62 ? 164  PHE A C   1 
ATOM   1341 O O   . PHE A 1 165 ? -5.601  29.612 -10.568 1.00 15.86 ? 164  PHE A O   1 
ATOM   1342 C CB  . PHE A 1 165 ? -3.443  27.633 -11.131 1.00 11.81 ? 164  PHE A CB  1 
ATOM   1343 C CG  . PHE A 1 165 ? -2.130  26.887 -11.226 1.00 11.75 ? 164  PHE A CG  1 
ATOM   1344 C CD1 . PHE A 1 165 ? -0.924  27.568 -11.365 1.00 12.32 ? 164  PHE A CD1 1 
ATOM   1345 C CD2 . PHE A 1 165 ? -2.114  25.492 -11.187 1.00 13.76 ? 164  PHE A CD2 1 
ATOM   1346 C CE1 . PHE A 1 165 ? 0.282   26.868 -11.461 1.00 16.87 ? 164  PHE A CE1 1 
ATOM   1347 C CE2 . PHE A 1 165 ? -0.917  24.796 -11.294 1.00 14.47 ? 164  PHE A CE2 1 
ATOM   1348 C CZ  . PHE A 1 165 ? 0.279   25.485 -11.423 1.00 14.41 ? 164  PHE A CZ  1 
ATOM   1349 N N   . VAL A 1 166 ? -4.836  30.589 -12.455 1.00 10.88 ? 165  VAL A N   1 
ATOM   1350 C CA  . VAL A 1 166 ? -6.127  31.160 -12.816 1.00 11.34 ? 165  VAL A CA  1 
ATOM   1351 C C   . VAL A 1 166 ? -6.737  30.260 -13.878 1.00 13.26 ? 165  VAL A C   1 
ATOM   1352 O O   . VAL A 1 166 ? -6.018  29.611 -14.659 1.00 14.36 ? 165  VAL A O   1 
ATOM   1353 C CB  . VAL A 1 166 ? -5.989  32.623 -13.305 1.00 13.52 ? 165  VAL A CB  1 
ATOM   1354 C CG1 . VAL A 1 166 ? -5.378  33.500 -12.217 1.00 14.80 ? 165  VAL A CG1 1 
ATOM   1355 C CG2 . VAL A 1 166 ? -5.139  32.707 -14.621 1.00 13.09 ? 165  VAL A CG2 1 
ATOM   1356 N N   . GLU A 1 167 ? -8.078  30.203 -13.913 1.00 12.28 ? 166  GLU A N   1 
ATOM   1357 C CA  . GLU A 1 167 ? -8.773  29.367 -14.894 1.00 13.70 ? 166  GLU A CA  1 
ATOM   1358 C C   . GLU A 1 167 ? -9.813  30.191 -15.630 1.00 15.56 ? 166  GLU A C   1 
ATOM   1359 O O   . GLU A 1 167 ? -10.381 31.137 -15.090 1.00 14.37 ? 166  GLU A O   1 
ATOM   1360 C CB  . GLU A 1 167 ? -9.447  28.143 -14.247 1.00 14.17 ? 166  GLU A CB  1 
ATOM   1361 C CG  . GLU A 1 167 ? -8.445  27.228 -13.544 1.00 14.17 ? 166  GLU A CG  1 
ATOM   1362 C CD  . GLU A 1 167 ? -8.969  25.820 -13.274 1.00 15.25 ? 166  GLU A CD  1 
ATOM   1363 O OE1 . GLU A 1 167 ? -9.736  25.288 -14.089 1.00 13.13 ? 166  GLU A OE1 1 
ATOM   1364 O OE2 . GLU A 1 167 ? -8.593  25.208 -12.240 1.00 14.53 ? 166  GLU A OE2 1 
ATOM   1365 N N   . GLY A 1 168 ? -10.060 29.817 -16.884 1.00 14.53 ? 167  GLY A N   1 
ATOM   1366 C CA  . GLY A 1 168 ? -10.964 30.547 -17.737 1.00 15.13 ? 167  GLY A CA  1 
ATOM   1367 C C   . GLY A 1 168 ? -12.290 29.828 -17.908 1.00 14.75 ? 167  GLY A C   1 
ATOM   1368 O O   . GLY A 1 168 ? -12.523 28.749 -17.372 1.00 14.45 ? 167  GLY A O   1 
ATOM   1369 N N   . ASN A 1 169 ? -13.143 30.456 -18.717 1.00 14.59 ? 168  ASN A N   1 
ATOM   1370 C CA  . ASN A 1 169 ? -14.459 29.964 -19.093 1.00 16.32 ? 168  ASN A CA  1 
ATOM   1371 C C   . ASN A 1 169 ? -14.321 28.826 -20.113 1.00 15.38 ? 168  ASN A C   1 
ATOM   1372 O O   . ASN A 1 169 ? -13.217 28.420 -20.475 1.00 14.41 ? 168  ASN A O   1 
ATOM   1373 C CB  . ASN A 1 169 ? -15.271 31.128 -19.654 1.00 14.59 ? 168  ASN A CB  1 
ATOM   1374 C CG  . ASN A 1 169 ? -16.724 31.118 -19.198 1.00 16.54 ? 168  ASN A CG  1 
ATOM   1375 O OD1 . ASN A 1 169 ? -17.292 30.064 -18.926 1.00 17.46 ? 168  ASN A OD1 1 
ATOM   1376 N ND2 . ASN A 1 169 ? -17.333 32.295 -19.160 1.00 16.17 ? 168  ASN A ND2 1 
ATOM   1377 N N   . SER A 1 170 ? -15.455 28.274 -20.556 1.00 15.35 ? 169  SER A N   1 
ATOM   1378 C CA  . SER A 1 170 ? -15.459 27.097 -21.441 1.00 15.29 ? 169  SER A CA  1 
ATOM   1379 C C   . SER A 1 170 ? -14.654 25.946 -20.827 1.00 17.03 ? 169  SER A C   1 
ATOM   1380 O O   . SER A 1 170 ? -13.870 25.260 -21.492 1.00 16.94 ? 169  SER A O   1 
ATOM   1381 C CB  . SER A 1 170 ? -14.967 27.461 -22.853 1.00 17.07 ? 169  SER A CB  1 
ATOM   1382 O OG  . SER A 1 170 ? -15.989 28.155 -23.577 1.00 19.41 ? 169  SER A OG  1 
ATOM   1383 N N   . TRP A 1 171 ? -14.874 25.716 -19.529 1.00 14.53 ? 170  TRP A N   1 
ATOM   1384 C CA  . TRP A 1 171 ? -14.247 24.602 -18.820 1.00 15.68 ? 170  TRP A CA  1 
ATOM   1385 C C   . TRP A 1 171 ? -12.724 24.695 -18.919 1.00 14.96 ? 170  TRP A C   1 
ATOM   1386 O O   . TRP A 1 171 ? -12.027 23.677 -18.960 1.00 14.54 ? 170  TRP A O   1 
ATOM   1387 C CB  . TRP A 1 171 ? -14.744 23.244 -19.339 1.00 19.97 ? 170  TRP A CB  1 
ATOM   1388 C CG  . TRP A 1 171 ? -16.258 23.123 -19.490 1.00 17.70 ? 170  TRP A CG  1 
ATOM   1389 C CD1 . TRP A 1 171 ? -17.010 23.525 -20.566 1.00 20.44 ? 170  TRP A CD1 1 
ATOM   1390 C CD2 . TRP A 1 171 ? -17.178 22.560 -18.544 1.00 18.70 ? 170  TRP A CD2 1 
ATOM   1391 N NE1 . TRP A 1 171 ? -18.341 23.237 -20.340 1.00 19.15 ? 170  TRP A NE1 1 
ATOM   1392 C CE2 . TRP A 1 171 ? -18.469 22.648 -19.110 1.00 19.58 ? 170  TRP A CE2 1 
ATOM   1393 C CE3 . TRP A 1 171 ? -17.033 21.978 -17.278 1.00 19.96 ? 170  TRP A CE3 1 
ATOM   1394 C CZ2 . TRP A 1 171 ? -19.611 22.186 -18.451 1.00 19.70 ? 170  TRP A CZ2 1 
ATOM   1395 C CZ3 . TRP A 1 171 ? -18.176 21.521 -16.621 1.00 20.41 ? 170  TRP A CZ3 1 
ATOM   1396 C CH2 . TRP A 1 171 ? -19.443 21.635 -17.209 1.00 22.53 ? 170  TRP A CH2 1 
ATOM   1397 N N   . THR A 1 172 ? -12.221 25.940 -18.913 1.00 13.78 ? 171  THR A N   1 
ATOM   1398 C CA  . THR A 1 172 ? -10.819 26.338 -19.097 1.00 11.48 ? 171  THR A CA  1 
ATOM   1399 C C   . THR A 1 172 ? -10.109 25.554 -20.212 1.00 15.97 ? 171  THR A C   1 
ATOM   1400 O O   . THR A 1 172 ? -8.886  25.372 -20.190 1.00 16.08 ? 171  THR A O   1 
ATOM   1401 C CB  . THR A 1 172 ? -10.078 26.307 -17.726 1.00 13.40 ? 171  THR A CB  1 
ATOM   1402 O OG1 . THR A 1 172 ? -9.037  27.289 -17.738 1.00 14.29 ? 171  THR A OG1 1 
ATOM   1403 C CG2 . THR A 1 172 ? -9.495  24.938 -17.321 1.00 12.72 ? 171  THR A CG2 1 
ATOM   1404 N N   . GLY A 1 173 ? -10.852 25.170 -21.246 1.00 16.14 ? 172  GLY A N   1 
ATOM   1405 C CA  . GLY A 1 173 ? -10.257 24.379 -22.322 1.00 13.73 ? 172  GLY A CA  1 
ATOM   1406 C C   . GLY A 1 173 ? -9.217  25.171 -23.093 1.00 14.99 ? 172  GLY A C   1 
ATOM   1407 O O   . GLY A 1 173 ? -9.387  26.361 -23.372 1.00 16.64 ? 172  GLY A O   1 
ATOM   1408 N N   . ALA A 1 174 ? -8.106  24.503 -23.425 1.00 14.24 ? 173  ALA A N   1 
ATOM   1409 C CA  . ALA A 1 174 ? -7.108  25.175 -24.250 1.00 14.98 ? 173  ALA A CA  1 
ATOM   1410 C C   . ALA A 1 174 ? -7.650  25.429 -25.640 1.00 17.34 ? 173  ALA A C   1 
ATOM   1411 O O   . ALA A 1 174 ? -7.469  26.521 -26.192 1.00 15.56 ? 173  ALA A O   1 
ATOM   1412 C CB  . ALA A 1 174 ? -5.817  24.351 -24.342 1.00 16.09 ? 173  ALA A CB  1 
ATOM   1413 N N   . TRP A 1 175 ? -8.324  24.431 -26.215 1.00 16.61 ? 174  TRP A N   1 
ATOM   1414 C CA  . TRP A 1 175 ? -8.758  24.535 -27.600 1.00 14.73 ? 174  TRP A CA  1 
ATOM   1415 C C   . TRP A 1 175 ? -9.796  25.624 -27.812 1.00 18.24 ? 174  TRP A C   1 
ATOM   1416 O O   . TRP A 1 175 ? -9.953  26.102 -28.942 1.00 18.19 ? 174  TRP A O   1 
ATOM   1417 C CB  . TRP A 1 175 ? -9.297  23.183 -28.084 1.00 16.24 ? 174  TRP A CB  1 
ATOM   1418 C CG  . TRP A 1 175 ? -10.505 22.613 -27.343 1.00 15.97 ? 174  TRP A CG  1 
ATOM   1419 C CD1 . TRP A 1 175 ? -10.822 22.751 -26.013 1.00 16.82 ? 174  TRP A CD1 1 
ATOM   1420 C CD2 . TRP A 1 175 ? -11.516 21.779 -27.911 1.00 19.98 ? 174  TRP A CD2 1 
ATOM   1421 N NE1 . TRP A 1 175 ? -11.981 22.062 -25.732 1.00 19.56 ? 174  TRP A NE1 1 
ATOM   1422 C CE2 . TRP A 1 175 ? -12.426 21.457 -26.881 1.00 20.06 ? 174  TRP A CE2 1 
ATOM   1423 C CE3 . TRP A 1 175 ? -11.744 21.278 -29.198 1.00 19.91 ? 174  TRP A CE3 1 
ATOM   1424 C CZ2 . TRP A 1 175 ? -13.550 20.656 -27.099 1.00 17.74 ? 174  TRP A CZ2 1 
ATOM   1425 C CZ3 . TRP A 1 175 ? -12.859 20.480 -29.417 1.00 19.34 ? 174  TRP A CZ3 1 
ATOM   1426 C CH2 . TRP A 1 175 ? -13.751 20.178 -28.367 1.00 17.29 ? 174  TRP A CH2 1 
ATOM   1427 N N   . THR A 1 176 ? -10.509 26.023 -26.764 1.00 15.39 ? 175  THR A N   1 
ATOM   1428 C CA  . THR A 1 176 ? -11.519 27.074 -26.864 1.00 14.61 ? 175  THR A CA  1 
ATOM   1429 C C   . THR A 1 176 ? -11.025 28.408 -26.318 1.00 18.32 ? 175  THR A C   1 
ATOM   1430 O O   . THR A 1 176 ? -11.779 29.388 -26.324 1.00 17.42 ? 175  THR A O   1 
ATOM   1431 C CB  . THR A 1 176 ? -12.780 26.648 -26.101 1.00 13.52 ? 175  THR A CB  1 
ATOM   1432 O OG1 . THR A 1 176 ? -12.398 26.197 -24.795 1.00 17.43 ? 175  THR A OG1 1 
ATOM   1433 C CG2 . THR A 1 176 ? -13.482 25.485 -26.823 1.00 17.21 ? 175  THR A CG2 1 
ATOM   1434 N N   . TRP A 1 177 ? -9.774  28.471 -25.850 1.00 16.34 ? 176  TRP A N   1 
ATOM   1435 C CA  . TRP A 1 177 ? -9.348  29.615 -25.049 1.00 16.01 ? 176  TRP A CA  1 
ATOM   1436 C C   . TRP A 1 177 ? -9.475  30.929 -25.814 1.00 17.90 ? 176  TRP A C   1 
ATOM   1437 O O   . TRP A 1 177 ? -10.079 31.884 -25.318 1.00 17.10 ? 176  TRP A O   1 
ATOM   1438 C CB  . TRP A 1 177 ? -7.906  29.431 -24.578 1.00 14.44 ? 176  TRP A CB  1 
ATOM   1439 C CG  . TRP A 1 177 ? -7.511  30.522 -23.635 1.00 14.96 ? 176  TRP A CG  1 
ATOM   1440 C CD1 . TRP A 1 177 ? -7.033  31.747 -23.949 1.00 14.83 ? 176  TRP A CD1 1 
ATOM   1441 C CD2 . TRP A 1 177 ? -7.629  30.485 -22.201 1.00 13.71 ? 176  TRP A CD2 1 
ATOM   1442 N NE1 . TRP A 1 177 ? -6.801  32.481 -22.791 1.00 16.43 ? 176  TRP A NE1 1 
ATOM   1443 C CE2 . TRP A 1 177 ? -7.163  31.721 -21.709 1.00 13.48 ? 176  TRP A CE2 1 
ATOM   1444 C CE3 . TRP A 1 177 ? -8.054  29.508 -21.291 1.00 13.85 ? 176  TRP A CE3 1 
ATOM   1445 C CZ2 . TRP A 1 177 ? -7.111  32.020 -20.334 1.00 14.99 ? 176  TRP A CZ2 1 
ATOM   1446 C CZ3 . TRP A 1 177 ? -8.012  29.806 -19.920 1.00 15.64 ? 176  TRP A CZ3 1 
ATOM   1447 C CH2 . TRP A 1 177 ? -7.557  31.059 -19.463 1.00 15.45 ? 176  TRP A CH2 1 
ATOM   1448 N N   . THR A 1 178 ? -8.868  31.019 -27.006 1.00 17.47 ? 177  THR A N   1 
ATOM   1449 C CA  . THR A 1 178 ? -8.898  32.304 -27.699 1.00 16.59 ? 177  THR A CA  1 
ATOM   1450 C C   . THR A 1 178 ? -10.304 32.704 -28.126 1.00 20.12 ? 177  THR A C   1 
ATOM   1451 O O   . THR A 1 178 ? -10.569 33.898 -28.295 1.00 23.54 ? 177  THR A O   1 
ATOM   1452 C CB  . THR A 1 178 ? -7.972  32.289 -28.915 1.00 19.60 ? 177  THR A CB  1 
ATOM   1453 O OG1 . THR A 1 178 ? -8.397  31.265 -29.824 1.00 21.45 ? 177  THR A OG1 1 
ATOM   1454 C CG2 . THR A 1 178 ? -6.545  32.002 -28.464 1.00 18.79 ? 177  THR A CG2 1 
ATOM   1455 N N   . ASN A 1 179 ? -11.217 31.748 -28.267 1.00 21.02 ? 178  ASN A N   1 
ATOM   1456 C CA  . ASN A 1 179 ? -12.564 32.098 -28.691 1.00 21.61 ? 178  ASN A CA  1 
ATOM   1457 C C   . ASN A 1 179 ? -13.344 32.842 -27.609 1.00 17.80 ? 178  ASN A C   1 
ATOM   1458 O O   . ASN A 1 179 ? -14.237 33.631 -27.939 1.00 19.70 ? 178  ASN A O   1 
ATOM   1459 C CB  . ASN A 1 179 ? -13.296 30.831 -29.130 1.00 20.77 ? 178  ASN A CB  1 
ATOM   1460 C CG  . ASN A 1 179 ? -12.659 30.199 -30.360 1.00 29.59 ? 178  ASN A CG  1 
ATOM   1461 O OD1 . ASN A 1 179 ? -12.143 30.895 -31.234 1.00 37.37 ? 178  ASN A OD1 1 
ATOM   1462 N ND2 . ASN A 1 179 ? -12.700 28.879 -30.432 1.00 35.78 ? 178  ASN A ND2 1 
ATOM   1463 N N   . VAL A 1 180 ? -13.043 32.620 -26.326 1.00 17.34 ? 179  VAL A N   1 
ATOM   1464 C CA  . VAL A 1 180 ? -13.870 33.215 -25.276 1.00 15.29 ? 179  VAL A CA  1 
ATOM   1465 C C   . VAL A 1 180 ? -13.086 33.935 -24.184 1.00 16.70 ? 179  VAL A C   1 
ATOM   1466 O O   . VAL A 1 180 ? -13.665 34.821 -23.531 1.00 17.46 ? 179  VAL A O   1 
ATOM   1467 C CB  . VAL A 1 180 ? -14.810 32.166 -24.629 1.00 20.40 ? 179  VAL A CB  1 
ATOM   1468 C CG1 . VAL A 1 180 ? -15.674 31.474 -25.681 1.00 22.91 ? 179  VAL A CG1 1 
ATOM   1469 C CG2 . VAL A 1 180 ? -14.030 31.155 -23.804 1.00 19.28 ? 179  VAL A CG2 1 
ATOM   1470 N N   . ASN A 1 181 ? -11.802 33.647 -23.945 1.00 15.26 ? 180  ASN A N   1 
ATOM   1471 C CA  . ASN A 1 181 ? -11.127 34.042 -22.705 1.00 13.80 ? 180  ASN A CA  1 
ATOM   1472 C C   . ASN A 1 181 ? -10.121 35.180 -22.872 1.00 15.99 ? 180  ASN A C   1 
ATOM   1473 O O   . ASN A 1 181 ? -9.268  35.368 -21.999 1.00 14.25 ? 180  ASN A O   1 
ATOM   1474 C CB  . ASN A 1 181 ? -10.421 32.832 -22.076 1.00 14.32 ? 180  ASN A CB  1 
ATOM   1475 C CG  . ASN A 1 181 ? -11.369 31.958 -21.269 1.00 15.15 ? 180  ASN A CG  1 
ATOM   1476 O OD1 . ASN A 1 181 ? -12.155 32.467 -20.488 1.00 15.74 ? 180  ASN A OD1 1 
ATOM   1477 N ND2 . ASN A 1 181 ? -11.308 30.646 -21.470 1.00 13.87 ? 180  ASN A ND2 1 
ATOM   1478 N N   . ASP A 1 182 ? -10.190 35.947 -23.963 1.00 15.25 ? 181  ASP A N   1 
ATOM   1479 C CA  . ASP A 1 182 ? -9.183  36.982 -24.166 1.00 15.06 ? 181  ASP A CA  1 
ATOM   1480 C C   . ASP A 1 182 ? -9.151  37.981 -23.016 1.00 18.09 ? 181  ASP A C   1 
ATOM   1481 O O   . ASP A 1 182 ? -8.077  38.479 -22.674 1.00 19.17 ? 181  ASP A O   1 
ATOM   1482 C CB  . ASP A 1 182 ? -9.418  37.714 -25.489 1.00 16.71 ? 181  ASP A CB  1 
ATOM   1483 C CG  . ASP A 1 182 ? -8.291  38.686 -25.811 1.00 19.78 ? 181  ASP A CG  1 
ATOM   1484 O OD1 . ASP A 1 182 ? -7.136  38.233 -25.997 1.00 18.23 ? 181  ASP A OD1 1 
ATOM   1485 O OD2 . ASP A 1 182 ? -8.558  39.905 -25.851 1.00 19.12 ? 181  ASP A OD2 1 
ATOM   1486 N N   . ASN A 1 183 ? -10.299 38.274 -22.390 1.00 17.36 ? 182  ASN A N   1 
ATOM   1487 C CA  . ASN A 1 183 ? -10.315 39.291 -21.337 1.00 16.56 ? 182  ASN A CA  1 
ATOM   1488 C C   . ASN A 1 183 ? -9.482  38.883 -20.121 1.00 20.44 ? 182  ASN A C   1 
ATOM   1489 O O   . ASN A 1 183 ? -9.112  39.744 -19.313 1.00 18.87 ? 182  ASN A O   1 
ATOM   1490 C CB  . ASN A 1 183 ? -11.774 39.638 -20.944 1.00 16.87 ? 182  ASN A CB  1 
ATOM   1491 C CG  . ASN A 1 183 ? -12.454 38.563 -20.114 1.00 17.22 ? 182  ASN A CG  1 
ATOM   1492 O OD1 . ASN A 1 183 ? -12.077 37.389 -20.148 1.00 17.10 ? 182  ASN A OD1 1 
ATOM   1493 N ND2 . ASN A 1 183 ? -13.460 38.981 -19.324 1.00 16.11 ? 182  ASN A ND2 1 
ATOM   1494 N N   . MET A 1 184 ? -9.125  37.603 -20.001 1.00 15.10 ? 183  MET A N   1 
ATOM   1495 C CA  . MET A 1 184 ? -8.308  37.129 -18.886 1.00 12.39 ? 183  MET A CA  1 
ATOM   1496 C C   . MET A 1 184 ? -6.898  37.711 -18.904 1.00 16.77 ? 183  MET A C   1 
ATOM   1497 O O   . MET A 1 184 ? -6.185  37.636 -17.894 1.00 16.09 ? 183  MET A O   1 
ATOM   1498 C CB  . MET A 1 184 ? -8.263  35.597 -18.919 1.00 13.42 ? 183  MET A CB  1 
ATOM   1499 C CG  . MET A 1 184 ? -9.642  34.953 -18.627 1.00 14.41 ? 183  MET A CG  1 
ATOM   1500 S SD  . MET A 1 184 ? -9.982  34.831 -16.862 1.00 17.87 ? 183  MET A SD  1 
ATOM   1501 C CE  . MET A 1 184 ? -8.729  33.646 -16.379 1.00 17.01 ? 183  MET A CE  1 
ATOM   1502 N N   . LYS A 1 185 ? -6.482  38.313 -20.017 1.00 15.38 ? 184  LYS A N   1 
ATOM   1503 C CA  . LYS A 1 185 ? -5.158  38.913 -20.085 1.00 14.21 ? 184  LYS A CA  1 
ATOM   1504 C C   . LYS A 1 185 ? -4.964  40.053 -19.096 1.00 18.54 ? 184  LYS A C   1 
ATOM   1505 O O   . LYS A 1 185 ? -3.816  40.402 -18.810 1.00 18.40 ? 184  LYS A O   1 
ATOM   1506 C CB  . LYS A 1 185 ? -4.887  39.435 -21.505 1.00 15.19 ? 184  LYS A CB  1 
ATOM   1507 C CG  . LYS A 1 185 ? -5.763  40.614 -21.943 1.00 13.91 ? 184  LYS A CG  1 
ATOM   1508 C CD  . LYS A 1 185 ? -5.777  40.701 -23.483 1.00 16.89 ? 184  LYS A CD  1 
ATOM   1509 C CE  . LYS A 1 185 ? -6.611  41.869 -23.983 1.00 20.25 ? 184  LYS A CE  1 
ATOM   1510 N NZ  . LYS A 1 185 ? -6.701  41.875 -25.486 1.00 19.91 ? 184  LYS A NZ  1 
ATOM   1511 N N   . SER A 1 186 ? -6.043  40.652 -18.575 1.00 16.47 ? 185  SER A N   1 
ATOM   1512 C CA  A SER A 1 186 ? -5.902  41.857 -17.762 0.68 15.90 ? 185  SER A CA  1 
ATOM   1513 C CA  B SER A 1 186 ? -5.953  41.855 -17.758 0.32 16.00 ? 185  SER A CA  1 
ATOM   1514 C C   . SER A 1 186 ? -5.705  41.567 -16.286 1.00 16.38 ? 185  SER A C   1 
ATOM   1515 O O   . SER A 1 186 ? -5.530  42.511 -15.518 1.00 19.10 ? 185  SER A O   1 
ATOM   1516 C CB  A SER A 1 186 ? -7.114  42.778 -17.925 0.68 19.16 ? 185  SER A CB  1 
ATOM   1517 C CB  B SER A 1 186 ? -7.236  42.682 -17.891 0.32 19.12 ? 185  SER A CB  1 
ATOM   1518 O OG  A SER A 1 186 ? -8.297  42.170 -17.455 0.68 20.89 ? 185  SER A OG  1 
ATOM   1519 O OG  B SER A 1 186 ? -7.532  42.950 -19.251 0.32 17.70 ? 185  SER A OG  1 
ATOM   1520 N N   . LEU A 1 187 ? -5.709  40.304 -15.883 1.00 15.31 ? 186  LEU A N   1 
ATOM   1521 C CA  . LEU A 1 187 ? -5.479  39.978 -14.481 1.00 14.36 ? 186  LEU A CA  1 
ATOM   1522 C C   . LEU A 1 187 ? -4.148  40.543 -13.996 1.00 16.62 ? 186  LEU A C   1 
ATOM   1523 O O   . LEU A 1 187 ? -3.143  40.525 -14.713 1.00 17.75 ? 186  LEU A O   1 
ATOM   1524 C CB  . LEU A 1 187 ? -5.510  38.464 -14.280 1.00 14.08 ? 186  LEU A CB  1 
ATOM   1525 C CG  . LEU A 1 187 ? -6.879  37.803 -14.459 1.00 15.19 ? 186  LEU A CG  1 
ATOM   1526 C CD1 . LEU A 1 187 ? -6.781  36.288 -14.517 1.00 16.22 ? 186  LEU A CD1 1 
ATOM   1527 C CD2 . LEU A 1 187 ? -7.770  38.225 -13.287 1.00 16.69 ? 186  LEU A CD2 1 
ATOM   1528 N N   . THR A 1 188 ? -4.141  41.017 -12.750 1.00 14.73 ? 187  THR A N   1 
ATOM   1529 C CA  . THR A 1 188 ? -2.953  41.600 -12.131 1.00 14.96 ? 187  THR A CA  1 
ATOM   1530 C C   . THR A 1 188 ? -2.636  40.895 -10.819 1.00 16.44 ? 187  THR A C   1 
ATOM   1531 O O   . THR A 1 188 ? -3.533  40.457 -10.098 1.00 18.02 ? 187  THR A O   1 
ATOM   1532 C CB  . THR A 1 188 ? -3.133  43.109 -11.871 1.00 21.06 ? 187  THR A CB  1 
ATOM   1533 O OG1 . THR A 1 188 ? -4.202  43.332 -10.933 1.00 23.86 ? 187  THR A OG1 1 
ATOM   1534 C CG2 . THR A 1 188 ? -3.427  43.828 -13.156 1.00 23.51 ? 187  THR A CG2 1 
ATOM   1535 N N   . ASP A 1 189 ? -1.336  40.799 -10.505 1.00 16.21 ? 188  ASP A N   1 
ATOM   1536 C CA  . ASP A 1 189 ? -0.860  40.140 -9.286  1.00 12.92 ? 188  ASP A CA  1 
ATOM   1537 C C   . ASP A 1 189 ? 0.383   40.882 -8.819  1.00 13.56 ? 188  ASP A C   1 
ATOM   1538 O O   . ASP A 1 189 ? 1.361   40.981 -9.569  1.00 15.79 ? 188  ASP A O   1 
ATOM   1539 C CB  . ASP A 1 189 ? -0.533  38.675 -9.578  1.00 14.14 ? 188  ASP A CB  1 
ATOM   1540 C CG  . ASP A 1 189 ? 0.142   37.969 -8.429  1.00 16.55 ? 188  ASP A CG  1 
ATOM   1541 O OD1 . ASP A 1 189 ? 0.070   38.465 -7.268  1.00 15.34 ? 188  ASP A OD1 1 
ATOM   1542 O OD2 . ASP A 1 189 ? 0.727   36.886 -8.694  1.00 15.83 ? 188  ASP A OD2 1 
ATOM   1543 N N   . PRO A 1 190 ? 0.381   41.454 -7.620  1.00 15.54 ? 189  PRO A N   1 
ATOM   1544 C CA  . PRO A 1 190 ? 1.590   42.146 -7.144  1.00 18.96 ? 189  PRO A CA  1 
ATOM   1545 C C   . PRO A 1 190 ? 2.809   41.244 -7.043  1.00 19.26 ? 189  PRO A C   1 
ATOM   1546 O O   . PRO A 1 190 ? 3.940   41.748 -7.121  1.00 23.41 ? 189  PRO A O   1 
ATOM   1547 C CB  . PRO A 1 190 ? 1.173   42.684 -5.769  1.00 22.25 ? 189  PRO A CB  1 
ATOM   1548 C CG  . PRO A 1 190 ? -0.031  41.867 -5.378  1.00 20.57 ? 189  PRO A CG  1 
ATOM   1549 C CD  . PRO A 1 190 ? -0.728  41.493 -6.650  1.00 15.98 ? 189  PRO A CD  1 
ATOM   1550 N N   . SER A 1 191 ? 2.622   39.931 -6.888  1.00 16.98 ? 190  SER A N   1 
ATOM   1551 C CA  . SER A 1 191 ? 3.737   38.990 -6.884  1.00 16.33 ? 190  SER A CA  1 
ATOM   1552 C C   . SER A 1 191 ? 4.182   38.560 -8.280  1.00 17.10 ? 190  SER A C   1 
ATOM   1553 O O   . SER A 1 191 ? 5.214   37.884 -8.395  1.00 18.39 ? 190  SER A O   1 
ATOM   1554 C CB  . SER A 1 191 ? 3.383   37.742 -6.073  1.00 18.75 ? 190  SER A CB  1 
ATOM   1555 O OG  . SER A 1 191 ? 3.196   38.096 -4.703  1.00 19.51 ? 190  SER A OG  1 
ATOM   1556 N N   . ASP A 1 192 ? 3.450   38.938 -9.327  1.00 16.79 ? 191  ASP A N   1 
ATOM   1557 C CA  . ASP A 1 192 ? 3.754   38.532 -10.706 1.00 17.28 ? 191  ASP A CA  1 
ATOM   1558 C C   . ASP A 1 192 ? 3.936   37.014 -10.826 1.00 16.09 ? 191  ASP A C   1 
ATOM   1559 O O   . ASP A 1 192 ? 4.877   36.521 -11.463 1.00 18.88 ? 191  ASP A O   1 
ATOM   1560 C CB  . ASP A 1 192 ? 4.992   39.280 -11.230 1.00 19.24 ? 191  ASP A CB  1 
ATOM   1561 C CG  . ASP A 1 192 ? 5.150   39.168 -12.744 1.00 22.51 ? 191  ASP A CG  1 
ATOM   1562 O OD1 . ASP A 1 192 ? 4.141   38.981 -13.458 1.00 24.97 ? 191  ASP A OD1 1 
ATOM   1563 O OD2 . ASP A 1 192 ? 6.297   39.240 -13.217 1.00 28.89 ? 191  ASP A OD2 1 
ATOM   1564 N N   . LYS A 1 193 ? 2.998   36.251 -10.252 1.00 14.84 ? 192  LYS A N   1 
ATOM   1565 C CA  . LYS A 1 193 ? 3.095   34.791 -10.317 1.00 13.17 ? 192  LYS A CA  1 
ATOM   1566 C C   . LYS A 1 193 ? 1.789   34.151 -10.769 1.00 14.96 ? 192  LYS A C   1 
ATOM   1567 O O   . LYS A 1 193 ? 1.421   33.065 -10.308 1.00 14.81 ? 192  LYS A O   1 
ATOM   1568 C CB  . LYS A 1 193 ? 3.530   34.206 -8.973  1.00 15.53 ? 192  LYS A CB  1 
ATOM   1569 C CG  . LYS A 1 193 ? 5.025   34.356 -8.697  1.00 17.64 ? 192  LYS A CG  1 
ATOM   1570 C CD  . LYS A 1 193 ? 5.410   33.563 -7.449  1.00 21.30 ? 192  LYS A CD  1 
ATOM   1571 C CE  . LYS A 1 193 ? 6.909   33.325 -7.386  1.00 27.77 ? 192  LYS A CE  1 
ATOM   1572 N NZ  . LYS A 1 193 ? 7.618   34.607 -7.219  1.00 34.09 ? 192  LYS A NZ  1 
ATOM   1573 N N   . ILE A 1 194 ? 1.096   34.789 -11.716 1.00 14.43 ? 193  ILE A N   1 
ATOM   1574 C CA  . ILE A 1 194 ? -0.084  34.197 -12.336 1.00 14.06 ? 193  ILE A CA  1 
ATOM   1575 C C   . ILE A 1 194 ? 0.369   33.188 -13.376 1.00 14.44 ? 193  ILE A C   1 
ATOM   1576 O O   . ILE A 1 194 ? 1.246   33.492 -14.195 1.00 15.22 ? 193  ILE A O   1 
ATOM   1577 C CB  . ILE A 1 194 ? -0.953  35.269 -12.995 1.00 12.19 ? 193  ILE A CB  1 
ATOM   1578 C CG1 . ILE A 1 194 ? -1.517  36.238 -11.946 1.00 12.61 ? 193  ILE A CG1 1 
ATOM   1579 C CG2 . ILE A 1 194 ? -2.068  34.610 -13.812 1.00 13.54 ? 193  ILE A CG2 1 
ATOM   1580 C CD1 . ILE A 1 194 ? -2.082  37.509 -12.560 1.00 13.82 ? 193  ILE A CD1 1 
ATOM   1581 N N   . ILE A 1 195 ? -0.218  31.997 -13.336 1.00 13.50 ? 194  ILE A N   1 
ATOM   1582 C CA  . ILE A 1 195 ? -0.096  31.000 -14.395 1.00 16.00 ? 194  ILE A CA  1 
ATOM   1583 C C   . ILE A 1 195 ? -1.493  30.719 -14.924 1.00 15.81 ? 194  ILE A C   1 
ATOM   1584 O O   . ILE A 1 195 ? -2.409  30.472 -14.136 1.00 14.89 ? 194  ILE A O   1 
ATOM   1585 C CB  . ILE A 1 195 ? 0.539   29.695 -13.878 1.00 14.04 ? 194  ILE A CB  1 
ATOM   1586 C CG1 . ILE A 1 195 ? 1.844   29.972 -13.115 1.00 18.24 ? 194  ILE A CG1 1 
ATOM   1587 C CG2 . ILE A 1 195 ? 0.759   28.720 -15.041 1.00 14.64 ? 194  ILE A CG2 1 
ATOM   1588 C CD1 . ILE A 1 195 ? 2.946   30.587 -13.940 1.00 15.25 ? 194  ILE A CD1 1 
ATOM   1589 N N   . TYR A 1 196 ? -1.654  30.729 -16.247 1.00 11.77 ? 195  TYR A N   1 
ATOM   1590 C CA  . TYR A 1 196 ? -2.949  30.461 -16.871 1.00 13.92 ? 195  TYR A CA  1 
ATOM   1591 C C   . TYR A 1 196 ? -3.115  28.952 -17.014 1.00 13.40 ? 195  TYR A C   1 
ATOM   1592 O O   . TYR A 1 196 ? -2.446  28.309 -17.831 1.00 14.66 ? 195  TYR A O   1 
ATOM   1593 C CB  . TYR A 1 196 ? -3.039  31.188 -18.217 1.00 14.73 ? 195  TYR A CB  1 
ATOM   1594 C CG  . TYR A 1 196 ? -3.211  32.686 -18.026 1.00 15.56 ? 195  TYR A CG  1 
ATOM   1595 C CD1 . TYR A 1 196 ? -2.119  33.504 -17.749 1.00 14.96 ? 195  TYR A CD1 1 
ATOM   1596 C CD2 . TYR A 1 196 ? -4.473  33.278 -18.103 1.00 16.13 ? 195  TYR A CD2 1 
ATOM   1597 C CE1 . TYR A 1 196 ? -2.274  34.867 -17.545 1.00 15.95 ? 195  TYR A CE1 1 
ATOM   1598 C CE2 . TYR A 1 196 ? -4.638  34.644 -17.897 1.00 14.51 ? 195  TYR A CE2 1 
ATOM   1599 C CZ  . TYR A 1 196 ? -3.533  35.436 -17.624 1.00 15.67 ? 195  TYR A CZ  1 
ATOM   1600 O OH  . TYR A 1 196 ? -3.687  36.799 -17.416 1.00 15.13 ? 195  TYR A OH  1 
ATOM   1601 N N   . GLU A 1 197 ? -4.018  28.379 -16.235 1.00 13.80 ? 196  GLU A N   1 
ATOM   1602 C CA  . GLU A 1 197 ? -4.211  26.940 -16.241 1.00 11.58 ? 196  GLU A CA  1 
ATOM   1603 C C   . GLU A 1 197 ? -5.300  26.591 -17.240 1.00 14.05 ? 196  GLU A C   1 
ATOM   1604 O O   . GLU A 1 197 ? -6.445  27.030 -17.096 1.00 15.35 ? 196  GLU A O   1 
ATOM   1605 C CB  . GLU A 1 197 ? -4.596  26.431 -14.852 1.00 12.32 ? 196  GLU A CB  1 
ATOM   1606 C CG  . GLU A 1 197 ? -4.975  24.943 -14.904 1.00 14.94 ? 196  GLU A CG  1 
ATOM   1607 C CD  . GLU A 1 197 ? -5.416  24.413 -13.564 1.00 14.73 ? 196  GLU A CD  1 
ATOM   1608 O OE1 . GLU A 1 197 ? -5.392  25.187 -12.574 1.00 16.13 ? 196  GLU A OE1 1 
ATOM   1609 O OE2 . GLU A 1 197 ? -5.808  23.233 -13.503 1.00 17.00 ? 196  GLU A OE2 1 
ATOM   1610 N N   . MET A 1 198 ? -4.945  25.795 -18.235 1.00 13.72 ? 197  MET A N   1 
ATOM   1611 C CA  . MET A 1 198 ? -5.882  25.307 -19.230 1.00 11.80 ? 197  MET A CA  1 
ATOM   1612 C C   . MET A 1 198 ? -5.955  23.784 -19.159 1.00 15.27 ? 197  MET A C   1 
ATOM   1613 O O   . MET A 1 198 ? -5.021  23.120 -18.716 1.00 15.02 ? 197  MET A O   1 
ATOM   1614 C CB  . MET A 1 198 ? -5.443  25.753 -20.630 1.00 13.50 ? 197  MET A CB  1 
ATOM   1615 C CG  . MET A 1 198 ? -5.195  27.241 -20.680 1.00 12.87 ? 197  MET A CG  1 
ATOM   1616 S SD  . MET A 1 198 ? -4.861  27.743 -22.387 1.00 16.22 ? 197  MET A SD  1 
ATOM   1617 C CE  . MET A 1 198 ? -4.297  29.408 -22.081 1.00 16.54 ? 197  MET A CE  1 
ATOM   1618 N N   . HIS A 1 199 ? -7.067  23.214 -19.618 1.00 12.89 ? 198  HIS A N   1 
ATOM   1619 C CA  . HIS A 1 199 ? -7.231  21.770 -19.651 1.00 13.14 ? 198  HIS A CA  1 
ATOM   1620 C C   . HIS A 1 199 ? -7.385  21.313 -21.087 1.00 12.68 ? 198  HIS A C   1 
ATOM   1621 O O   . HIS A 1 199 ? -7.920  22.046 -21.917 1.00 15.47 ? 198  HIS A O   1 
ATOM   1622 C CB  . HIS A 1 199 ? -8.454  21.330 -18.875 1.00 14.51 ? 198  HIS A CB  1 
ATOM   1623 C CG  . HIS A 1 199 ? -8.387  21.649 -17.413 1.00 14.10 ? 198  HIS A CG  1 
ATOM   1624 N ND1 . HIS A 1 199 ? -9.436  21.409 -16.555 1.00 15.19 ? 198  HIS A ND1 1 
ATOM   1625 C CD2 . HIS A 1 199 ? -7.398  22.191 -16.664 1.00 12.33 ? 198  HIS A CD2 1 
ATOM   1626 C CE1 . HIS A 1 199 ? -9.086  21.763 -15.330 1.00 14.16 ? 198  HIS A CE1 1 
ATOM   1627 N NE2 . HIS A 1 199 ? -7.863  22.260 -15.373 1.00 15.30 ? 198  HIS A NE2 1 
ATOM   1628 N N   . GLN A 1 200 ? -6.923  20.101 -21.386 1.00 14.26 ? 199  GLN A N   1 
ATOM   1629 C CA  . GLN A 1 200 ? -7.110  19.607 -22.750 1.00 12.22 ? 199  GLN A CA  1 
ATOM   1630 C C   . GLN A 1 200 ? -7.280  18.100 -22.751 1.00 14.07 ? 199  GLN A C   1 
ATOM   1631 O O   . GLN A 1 200 ? -6.345  17.349 -22.446 1.00 15.65 ? 199  GLN A O   1 
ATOM   1632 C CB  . GLN A 1 200 ? -5.948  20.004 -23.666 1.00 14.47 ? 199  GLN A CB  1 
ATOM   1633 C CG  . GLN A 1 200 ? -6.333  19.804 -25.122 1.00 13.99 ? 199  GLN A CG  1 
ATOM   1634 C CD  . GLN A 1 200 ? -7.573  20.632 -25.477 1.00 14.84 ? 199  GLN A CD  1 
ATOM   1635 O OE1 . GLN A 1 200 ? -7.502  21.864 -25.512 1.00 17.20 ? 199  GLN A OE1 1 
ATOM   1636 N NE2 . GLN A 1 200 ? -8.715  19.961 -25.721 1.00 15.91 ? 199  GLN A NE2 1 
ATOM   1637 N N   . PHE A 1 201 ? -8.463  17.664 -23.152 1.00 16.68 ? 200  PHE A N   1 
ATOM   1638 C CA  . PHE A 1 201 ? -8.699  16.259 -23.394 1.00 19.95 ? 200  PHE A CA  1 
ATOM   1639 C C   . PHE A 1 201 ? -8.766  16.026 -24.894 1.00 19.20 ? 200  PHE A C   1 
ATOM   1640 O O   . PHE A 1 201 ? -8.818  16.968 -25.696 1.00 17.21 ? 200  PHE A O   1 
ATOM   1641 C CB  . PHE A 1 201 ? -9.957  15.797 -22.652 1.00 16.51 ? 200  PHE A CB  1 
ATOM   1642 C CG  . PHE A 1 201 ? -9.782  15.802 -21.165 1.00 18.16 ? 200  PHE A CG  1 
ATOM   1643 C CD1 . PHE A 1 201 ? -9.167  14.731 -20.529 1.00 17.29 ? 200  PHE A CD1 1 
ATOM   1644 C CD2 . PHE A 1 201 ? -10.193 16.885 -20.411 1.00 18.86 ? 200  PHE A CD2 1 
ATOM   1645 C CE1 . PHE A 1 201 ? -8.968  14.732 -19.138 1.00 19.23 ? 200  PHE A CE1 1 
ATOM   1646 C CE2 . PHE A 1 201 ? -10.005 16.900 -19.022 1.00 19.28 ? 200  PHE A CE2 1 
ATOM   1647 C CZ  . PHE A 1 201 ? -9.403  15.822 -18.390 1.00 18.53 ? 200  PHE A CZ  1 
ATOM   1648 N N   . LEU A 1 202 ? -8.748  14.746 -25.251 1.00 15.33 ? 201  LEU A N   1 
ATOM   1649 C CA  . LEU A 1 202 ? -8.376  14.296 -26.585 1.00 13.44 ? 201  LEU A CA  1 
ATOM   1650 C C   . LEU A 1 202 ? -9.483  13.519 -27.273 1.00 17.41 ? 201  LEU A C   1 
ATOM   1651 O O   . LEU A 1 202 ? -9.304  13.112 -28.426 1.00 18.86 ? 201  LEU A O   1 
ATOM   1652 C CB  . LEU A 1 202 ? -7.106  13.430 -26.492 1.00 15.21 ? 201  LEU A CB  1 
ATOM   1653 C CG  . LEU A 1 202 ? -5.935  14.085 -25.744 1.00 19.66 ? 201  LEU A CG  1 
ATOM   1654 C CD1 . LEU A 1 202 ? -4.732  13.136 -25.631 1.00 20.73 ? 201  LEU A CD1 1 
ATOM   1655 C CD2 . LEU A 1 202 ? -5.510  15.401 -26.411 1.00 18.84 ? 201  LEU A CD2 1 
ATOM   1656 N N   . ASP A 1 203 ? -10.627 13.321 -26.613 1.00 19.09 ? 202  ASP A N   1 
ATOM   1657 C CA  . ASP A 1 203 ? -11.756 12.694 -27.287 1.00 17.13 ? 202  ASP A CA  1 
ATOM   1658 C C   . ASP A 1 203 ? -12.528 13.741 -28.085 1.00 15.39 ? 202  ASP A C   1 
ATOM   1659 O O   . ASP A 1 203 ? -12.269 14.945 -27.996 1.00 20.10 ? 202  ASP A O   1 
ATOM   1660 C CB  . ASP A 1 203 ? -12.665 11.949 -26.290 1.00 18.84 ? 202  ASP A CB  1 
ATOM   1661 C CG  . ASP A 1 203 ? -13.041 12.757 -25.054 1.00 19.47 ? 202  ASP A CG  1 
ATOM   1662 O OD1 . ASP A 1 203 ? -12.552 13.889 -24.828 1.00 19.18 ? 202  ASP A OD1 1 
ATOM   1663 O OD2 . ASP A 1 203 ? -13.871 12.218 -24.289 1.00 21.52 ? 202  ASP A OD2 1 
ATOM   1664 N N   . SER A 1 204 ? -13.491 13.266 -28.886 1.00 21.12 ? 203  SER A N   1 
ATOM   1665 C CA  . SER A 1 204 ? -14.064 14.112 -29.927 1.00 21.67 ? 203  SER A CA  1 
ATOM   1666 C C   . SER A 1 204 ? -14.634 15.411 -29.365 1.00 19.94 ? 203  SER A C   1 
ATOM   1667 O O   . SER A 1 204 ? -14.376 16.487 -29.912 1.00 23.01 ? 203  SER A O   1 
ATOM   1668 C CB  . SER A 1 204 ? -15.123 13.337 -30.715 1.00 32.53 ? 203  SER A CB  1 
ATOM   1669 O OG  . SER A 1 204 ? -15.953 12.588 -29.849 1.00 44.24 ? 203  SER A OG  1 
ATOM   1670 N N   . ASP A 1 205 ? -15.386 15.350 -28.259 1.00 21.76 ? 204  ASP A N   1 
ATOM   1671 C CA  . ASP A 1 205 ? -15.970 16.579 -27.723 1.00 20.12 ? 204  ASP A CA  1 
ATOM   1672 C C   . ASP A 1 205 ? -15.131 17.227 -26.624 1.00 20.67 ? 204  ASP A C   1 
ATOM   1673 O O   . ASP A 1 205 ? -15.572 18.213 -26.022 1.00 19.48 ? 204  ASP A O   1 
ATOM   1674 C CB  . ASP A 1 205 ? -17.399 16.323 -27.218 1.00 22.78 ? 204  ASP A CB  1 
ATOM   1675 C CG  . ASP A 1 205 ? -17.453 15.374 -26.035 1.00 26.01 ? 204  ASP A CG  1 
ATOM   1676 O OD1 . ASP A 1 205 ? -16.392 14.974 -25.504 1.00 23.98 ? 204  ASP A OD1 1 
ATOM   1677 O OD2 . ASP A 1 205 ? -18.579 15.008 -25.636 1.00 28.38 ? 204  ASP A OD2 1 
ATOM   1678 N N   . GLY A 1 206 ? -13.921 16.725 -26.372 1.00 19.17 ? 205  GLY A N   1 
ATOM   1679 C CA  . GLY A 1 206 ? -13.041 17.316 -25.380 1.00 18.21 ? 205  GLY A CA  1 
ATOM   1680 C C   . GLY A 1 206 ? -13.497 17.172 -23.945 1.00 18.12 ? 205  GLY A C   1 
ATOM   1681 O O   . GLY A 1 206 ? -12.949 17.841 -23.061 1.00 17.67 ? 205  GLY A O   1 
ATOM   1682 N N   . SER A 1 207 ? -14.497 16.327 -23.689 1.00 19.11 ? 206  SER A N   1 
ATOM   1683 C CA  . SER A 1 207 ? -15.026 16.132 -22.345 1.00 20.60 ? 206  SER A CA  1 
ATOM   1684 C C   . SER A 1 207 ? -14.157 15.223 -21.492 1.00 21.58 ? 206  SER A C   1 
ATOM   1685 O O   . SER A 1 207 ? -14.333 15.193 -20.267 1.00 22.06 ? 206  SER A O   1 
ATOM   1686 C CB  . SER A 1 207 ? -16.434 15.544 -22.420 1.00 21.41 ? 206  SER A CB  1 
ATOM   1687 O OG  . SER A 1 207 ? -16.398 14.239 -22.975 1.00 25.16 ? 206  SER A OG  1 
ATOM   1688 N N   . GLY A 1 208 ? -13.236 14.480 -22.093 1.00 18.77 ? 207  GLY A N   1 
ATOM   1689 C CA  . GLY A 1 208 ? -12.421 13.583 -21.287 1.00 19.62 ? 207  GLY A CA  1 
ATOM   1690 C C   . GLY A 1 208 ? -13.207 12.450 -20.662 1.00 23.82 ? 207  GLY A C   1 
ATOM   1691 O O   . GLY A 1 208 ? -12.945 12.076 -19.505 1.00 25.95 ? 207  GLY A O   1 
ATOM   1692 N N   . THR A 1 209 ? -14.187 11.906 -21.382 1.00 19.84 ? 208  THR A N   1 
ATOM   1693 C CA  . THR A 1 209 ? -14.962 10.791 -20.862 1.00 20.86 ? 208  THR A CA  1 
ATOM   1694 C C   . THR A 1 209 ? -14.766 9.508  -21.657 1.00 23.31 ? 208  THR A C   1 
ATOM   1695 O O   . THR A 1 209 ? -15.137 8.437  -21.163 1.00 28.85 ? 208  THR A O   1 
ATOM   1696 C CB  . THR A 1 209 ? -16.461 11.148 -20.809 1.00 23.38 ? 208  THR A CB  1 
ATOM   1697 O OG1 . THR A 1 209 ? -16.905 11.578 -22.102 1.00 27.32 ? 208  THR A OG1 1 
ATOM   1698 C CG2 . THR A 1 209 ? -16.709 12.258 -19.790 1.00 27.47 ? 208  THR A CG2 1 
ATOM   1699 N N   . SER A 1 210 ? -14.170 9.583  -22.845 1.00 20.51 ? 209  SER A N   1 
ATOM   1700 C CA  . SER A 1 210 ? -13.909 8.433  -23.705 1.00 19.75 ? 209  SER A CA  1 
ATOM   1701 C C   . SER A 1 210 ? -12.418 8.126  -23.768 1.00 20.61 ? 209  SER A C   1 
ATOM   1702 O O   . SER A 1 210 ? -11.583 9.039  -23.818 1.00 22.51 ? 209  SER A O   1 
ATOM   1703 C CB  . SER A 1 210 ? -14.438 8.689  -25.123 1.00 22.35 ? 209  SER A CB  1 
ATOM   1704 O OG  . SER A 1 210 ? -14.049 7.654  -25.998 1.00 24.60 ? 209  SER A OG  1 
ATOM   1705 N N   . ALA A 1 211 ? -12.087 6.836  -23.775 1.00 21.01 ? 210  ALA A N   1 
ATOM   1706 C CA  . ALA A 1 211 ? -10.700 6.432  -23.942 1.00 21.84 ? 210  ALA A CA  1 
ATOM   1707 C C   . ALA A 1 211 ? -10.211 6.590  -25.375 1.00 19.80 ? 210  ALA A C   1 
ATOM   1708 O O   . ALA A 1 211 ? -9.016  6.410  -25.624 1.00 24.29 ? 210  ALA A O   1 
ATOM   1709 C CB  . ALA A 1 211 ? -10.506 4.979  -23.504 1.00 22.99 ? 210  ALA A CB  1 
ATOM   1710 N N   . THR A 1 212 ? -11.089 6.910  -26.314 1.00 20.88 ? 211  THR A N   1 
ATOM   1711 C CA  . THR A 1 212 ? -10.703 7.042  -27.712 1.00 21.30 ? 211  THR A CA  1 
ATOM   1712 C C   . THR A 1 212 ? -10.234 8.464  -27.995 1.00 23.98 ? 211  THR A C   1 
ATOM   1713 O O   . THR A 1 212 ? -10.901 9.425  -27.614 1.00 25.52 ? 211  THR A O   1 
ATOM   1714 C CB  . THR A 1 212 ? -11.880 6.698  -28.622 1.00 24.79 ? 211  THR A CB  1 
ATOM   1715 O OG1 . THR A 1 212 ? -12.271 5.340  -28.397 1.00 28.47 ? 211  THR A OG1 1 
ATOM   1716 C CG2 . THR A 1 212 ? -11.491 6.873  -30.082 1.00 29.57 ? 211  THR A CG2 1 
ATOM   1717 N N   . CYS A 1 213 ? -9.102  8.598  -28.679 1.00 22.62 ? 212  CYS A N   1 
ATOM   1718 C CA  . CYS A 1 213 ? -8.634  9.906  -29.105 1.00 18.14 ? 212  CYS A CA  1 
ATOM   1719 C C   . CYS A 1 213 ? -8.993  10.128 -30.573 1.00 20.65 ? 212  CYS A C   1 
ATOM   1720 O O   . CYS A 1 213 ? -9.081  9.177  -31.355 1.00 22.39 ? 212  CYS A O   1 
ATOM   1721 C CB  . CYS A 1 213 ? -7.126  10.043 -28.888 1.00 20.66 ? 212  CYS A CB  1 
ATOM   1722 S SG  . CYS A 1 213 ? -6.663  9.938  -27.118 1.00 21.85 ? 212  CYS A SG  1 
ATOM   1723 N N   . VAL A 1 214 ? -9.236  11.397 -30.928 1.00 19.53 ? 213  VAL A N   1 
ATOM   1724 C CA  . VAL A 1 214 ? -9.667  11.730 -32.289 1.00 18.00 ? 213  VAL A CA  1 
ATOM   1725 C C   . VAL A 1 214 ? -8.636  11.262 -33.311 1.00 22.22 ? 213  VAL A C   1 
ATOM   1726 O O   . VAL A 1 214 ? -8.982  10.673 -34.341 1.00 20.90 ? 213  VAL A O   1 
ATOM   1727 C CB  . VAL A 1 214 ? -9.920  13.241 -32.430 1.00 19.62 ? 213  VAL A CB  1 
ATOM   1728 C CG1 . VAL A 1 214 ? -10.271 13.578 -33.893 1.00 23.30 ? 213  VAL A CG1 1 
ATOM   1729 C CG2 . VAL A 1 214 ? -11.014 13.703 -31.501 1.00 20.41 ? 213  VAL A CG2 1 
ATOM   1730 N N   . SER A 1 215 ? -7.362  11.550 -33.056 1.00 18.27 ? 214  SER A N   1 
ATOM   1731 C CA  . SER A 1 215 ? -6.297  11.232 -33.998 1.00 19.89 ? 214  SER A CA  1 
ATOM   1732 C C   . SER A 1 215 ? -4.975  11.269 -33.249 1.00 18.60 ? 214  SER A C   1 
ATOM   1733 O O   . SER A 1 215 ? -4.900  11.706 -32.096 1.00 19.27 ? 214  SER A O   1 
ATOM   1734 C CB  . SER A 1 215 ? -6.261  12.227 -35.160 1.00 21.70 ? 214  SER A CB  1 
ATOM   1735 O OG  . SER A 1 215 ? -5.739  13.468 -34.691 1.00 19.62 ? 214  SER A OG  1 
ATOM   1736 N N   . SER A 1 216 ? -3.918  10.831 -33.935 1.00 21.01 ? 215  SER A N   1 
ATOM   1737 C CA  . SER A 1 216 ? -2.614  10.827 -33.290 1.00 20.10 ? 215  SER A CA  1 
ATOM   1738 C C   . SER A 1 216 ? -2.042  12.232 -33.107 1.00 20.33 ? 215  SER A C   1 
ATOM   1739 O O   . SER A 1 216 ? -1.008  12.380 -32.444 1.00 19.51 ? 215  SER A O   1 
ATOM   1740 C CB  . SER A 1 216 ? -1.641  9.975  -34.104 1.00 22.12 ? 215  SER A CB  1 
ATOM   1741 O OG  . SER A 1 216 ? -1.403  10.592 -35.352 1.00 24.33 ? 215  SER A OG  1 
ATOM   1742 N N   . THR A 1 217 ? -2.670  13.264 -33.679 1.00 18.33 ? 216  THR A N   1 
ATOM   1743 C CA  . THR A 1 217 ? -2.162  14.630 -33.561 1.00 18.51 ? 216  THR A CA  1 
ATOM   1744 C C   . THR A 1 217 ? -3.112  15.572 -32.831 1.00 17.69 ? 216  THR A C   1 
ATOM   1745 O O   . THR A 1 217 ? -2.851  16.782 -32.782 1.00 16.34 ? 216  THR A O   1 
ATOM   1746 C CB  . THR A 1 217 ? -1.835  15.223 -34.940 1.00 16.87 ? 216  THR A CB  1 
ATOM   1747 O OG1 . THR A 1 217 ? -3.013  15.266 -35.768 1.00 18.12 ? 216  THR A OG1 1 
ATOM   1748 C CG2 . THR A 1 217 ? -0.739  14.399 -35.643 1.00 20.57 ? 216  THR A CG2 1 
ATOM   1749 N N   . ILE A 1 218 ? -4.200  15.064 -32.246 1.00 15.91 ? 217  ILE A N   1 
ATOM   1750 C CA  . ILE A 1 218 ? -5.274  15.972 -31.831 1.00 16.90 ? 217  ILE A CA  1 
ATOM   1751 C C   . ILE A 1 218 ? -4.862  16.846 -30.651 1.00 17.95 ? 217  ILE A C   1 
ATOM   1752 O O   . ILE A 1 218 ? -5.345  17.979 -30.520 1.00 16.17 ? 217  ILE A O   1 
ATOM   1753 C CB  . ILE A 1 218 ? -6.550  15.169 -31.531 1.00 16.23 ? 217  ILE A CB  1 
ATOM   1754 C CG1 . ILE A 1 218 ? -7.749  16.106 -31.383 1.00 16.84 ? 217  ILE A CG1 1 
ATOM   1755 C CG2 . ILE A 1 218 ? -6.387  14.305 -30.274 1.00 18.46 ? 217  ILE A CG2 1 
ATOM   1756 C CD1 . ILE A 1 218 ? -8.091  16.863 -32.665 1.00 21.61 ? 217  ILE A CD1 1 
ATOM   1757 N N   . GLY A 1 219 ? -3.958  16.365 -29.798 1.00 15.96 ? 218  GLY A N   1 
ATOM   1758 C CA  . GLY A 1 219 ? -3.545  17.166 -28.650 1.00 16.08 ? 218  GLY A CA  1 
ATOM   1759 C C   . GLY A 1 219 ? -2.693  18.347 -29.065 1.00 15.70 ? 218  GLY A C   1 
ATOM   1760 O O   . GLY A 1 219 ? -2.929  19.489 -28.648 1.00 16.45 ? 218  GLY A O   1 
ATOM   1761 N N   . GLN A 1 220 ? -1.677  18.087 -29.886 1.00 17.74 ? 219  GLN A N   1 
ATOM   1762 C CA  . GLN A 1 220 ? -0.829  19.177 -30.339 1.00 19.94 ? 219  GLN A CA  1 
ATOM   1763 C C   . GLN A 1 220 ? -1.631  20.173 -31.168 1.00 18.31 ? 219  GLN A C   1 
ATOM   1764 O O   . GLN A 1 220 ? -1.440  21.386 -31.041 1.00 20.60 ? 219  GLN A O   1 
ATOM   1765 C CB  . GLN A 1 220 ? 0.384   18.622 -31.106 1.00 18.64 ? 219  GLN A CB  1 
ATOM   1766 C CG  . GLN A 1 220 ? 0.070   17.840 -32.384 1.00 21.44 ? 219  GLN A CG  1 
ATOM   1767 C CD  . GLN A 1 220 ? 1.034   16.665 -32.640 1.00 20.84 ? 219  GLN A CD  1 
ATOM   1768 O OE1 . GLN A 1 220 ? 0.818   15.542 -32.146 1.00 20.12 ? 219  GLN A OE1 1 
ATOM   1769 N NE2 . GLN A 1 220 ? 2.088   16.909 -33.445 1.00 19.02 ? 219  GLN A NE2 1 
ATOM   1770 N N   . GLU A 1 221 ? -2.591  19.688 -31.962 1.00 18.07 ? 220  GLU A N   1 
ATOM   1771 C CA  . GLU A 1 221 ? -3.472  20.603 -32.684 1.00 17.61 ? 220  GLU A CA  1 
ATOM   1772 C C   . GLU A 1 221 ? -4.276  21.483 -31.734 1.00 19.32 ? 220  GLU A C   1 
ATOM   1773 O O   . GLU A 1 221 ? -4.464  22.680 -31.993 1.00 18.25 ? 220  GLU A O   1 
ATOM   1774 C CB  . GLU A 1 221 ? -4.432  19.822 -33.577 1.00 18.04 ? 220  GLU A CB  1 
ATOM   1775 C CG  . GLU A 1 221 ? -3.777  19.146 -34.768 1.00 18.05 ? 220  GLU A CG  1 
ATOM   1776 C CD  . GLU A 1 221 ? -4.808  18.430 -35.629 1.00 19.94 ? 220  GLU A CD  1 
ATOM   1777 O OE1 . GLU A 1 221 ? -5.619  19.146 -36.264 1.00 24.31 ? 220  GLU A OE1 1 
ATOM   1778 O OE2 . GLU A 1 221 ? -4.839  17.172 -35.633 1.00 18.70 ? 220  GLU A OE2 1 
ATOM   1779 N N   . ARG A 1 222 ? -4.780  20.907 -30.643 1.00 15.74 ? 221  ARG A N   1 
ATOM   1780 C CA  . ARG A 1 222 ? -5.740  21.626 -29.809 1.00 16.64 ? 221  ARG A CA  1 
ATOM   1781 C C   . ARG A 1 222 ? -5.094  22.661 -28.899 1.00 17.98 ? 221  ARG A C   1 
ATOM   1782 O O   . ARG A 1 222 ? -5.810  23.450 -28.276 1.00 17.57 ? 221  ARG A O   1 
ATOM   1783 C CB  . ARG A 1 222 ? -6.568  20.642 -28.972 1.00 14.32 ? 221  ARG A CB  1 
ATOM   1784 C CG  . ARG A 1 222 ? -7.751  20.049 -29.788 1.00 13.92 ? 221  ARG A CG  1 
ATOM   1785 C CD  . ARG A 1 222 ? -8.530  18.989 -29.022 1.00 15.69 ? 221  ARG A CD  1 
ATOM   1786 N NE  . ARG A 1 222 ? -9.685  18.554 -29.805 1.00 14.38 ? 221  ARG A NE  1 
ATOM   1787 C CZ  . ARG A 1 222 ? -10.532 17.610 -29.415 1.00 19.08 ? 221  ARG A CZ  1 
ATOM   1788 N NH1 . ARG A 1 222 ? -10.381 16.982 -28.257 1.00 17.49 ? 221  ARG A NH1 1 
ATOM   1789 N NH2 . ARG A 1 222 ? -11.553 17.280 -30.208 1.00 19.68 ? 221  ARG A NH2 1 
ATOM   1790 N N   . ILE A 1 223 ? -3.769  22.721 -28.823 1.00 15.64 ? 222  ILE A N   1 
ATOM   1791 C CA  . ILE A 1 223 ? -3.125  23.716 -27.977 1.00 14.62 ? 222  ILE A CA  1 
ATOM   1792 C C   . ILE A 1 223 ? -2.339  24.753 -28.766 1.00 16.43 ? 222  ILE A C   1 
ATOM   1793 O O   . ILE A 1 223 ? -1.709  25.619 -28.142 1.00 17.97 ? 222  ILE A O   1 
ATOM   1794 C CB  . ILE A 1 223 ? -2.220  23.059 -26.913 1.00 14.62 ? 222  ILE A CB  1 
ATOM   1795 C CG1 . ILE A 1 223 ? -1.045  22.314 -27.555 1.00 15.23 ? 222  ILE A CG1 1 
ATOM   1796 C CG2 . ILE A 1 223 ? -3.030  22.144 -26.003 1.00 16.35 ? 222  ILE A CG2 1 
ATOM   1797 C CD1 . ILE A 1 223 ? -0.011  21.848 -26.511 1.00 20.42 ? 222  ILE A CD1 1 
ATOM   1798 N N   . THR A 1 224 ? -2.371  24.745 -30.105 1.00 15.67 ? 223  THR A N   1 
ATOM   1799 C CA  A THR A 1 224 ? -1.521  25.694 -30.816 0.85 17.00 ? 223  THR A CA  1 
ATOM   1800 C CA  B THR A 1 224 ? -1.535  25.691 -30.839 0.15 17.13 ? 223  THR A CA  1 
ATOM   1801 C C   . THR A 1 224 ? -2.023  27.128 -30.660 1.00 15.93 ? 223  THR A C   1 
ATOM   1802 O O   . THR A 1 224 ? -1.227  28.031 -30.396 1.00 17.48 ? 223  THR A O   1 
ATOM   1803 C CB  A THR A 1 224 ? -1.376  25.327 -32.302 0.85 22.38 ? 223  THR A CB  1 
ATOM   1804 C CB  B THR A 1 224 ? -1.460  25.311 -32.323 0.15 22.21 ? 223  THR A CB  1 
ATOM   1805 O OG1 A THR A 1 224 ? -2.635  25.448 -32.966 0.85 24.09 ? 223  THR A OG1 1 
ATOM   1806 O OG1 B THR A 1 224 ? -0.741  26.319 -33.043 0.15 19.02 ? 223  THR A OG1 1 
ATOM   1807 C CG2 A THR A 1 224 ? -0.865  23.916 -32.452 0.85 16.93 ? 223  THR A CG2 1 
ATOM   1808 C CG2 B THR A 1 224 ? -2.832  25.176 -32.919 0.15 22.90 ? 223  THR A CG2 1 
ATOM   1809 N N   . SER A 1 225 ? -3.334  27.375 -30.794 1.00 16.62 ? 224  SER A N   1 
ATOM   1810 C CA  . SER A 1 225 ? -3.757  28.772 -30.691 1.00 17.51 ? 224  SER A CA  1 
ATOM   1811 C C   . SER A 1 225 ? -3.634  29.297 -29.263 1.00 18.42 ? 224  SER A C   1 
ATOM   1812 O O   . SER A 1 225 ? -3.371  30.492 -29.068 1.00 17.95 ? 224  SER A O   1 
ATOM   1813 C CB  . SER A 1 225 ? -5.176  28.974 -31.230 1.00 23.44 ? 224  SER A CB  1 
ATOM   1814 O OG  . SER A 1 225 ? -6.137  28.239 -30.524 1.00 23.13 ? 224  SER A OG  1 
ATOM   1815 N N   . ALA A 1 226 ? -3.808  28.431 -28.262 1.00 17.91 ? 225  ALA A N   1 
ATOM   1816 C CA  . ALA A 1 226 ? -3.578  28.861 -26.883 1.00 15.30 ? 225  ALA A CA  1 
ATOM   1817 C C   . ALA A 1 226 ? -2.112  29.212 -26.659 1.00 16.15 ? 225  ALA A C   1 
ATOM   1818 O O   . ALA A 1 226 ? -1.798  30.171 -25.941 1.00 16.21 ? 225  ALA A O   1 
ATOM   1819 C CB  . ALA A 1 226 ? -4.032  27.774 -25.901 1.00 17.72 ? 225  ALA A CB  1 
ATOM   1820 N N   . THR A 1 227 ? -1.200  28.444 -27.263 1.00 15.91 ? 226  THR A N   1 
ATOM   1821 C CA  . THR A 1 227 ? 0.222   28.761 -27.155 1.00 15.87 ? 226  THR A CA  1 
ATOM   1822 C C   . THR A 1 227 ? 0.519   30.150 -27.710 1.00 16.40 ? 226  THR A C   1 
ATOM   1823 O O   . THR A 1 227 ? 1.247   30.936 -27.093 1.00 16.83 ? 226  THR A O   1 
ATOM   1824 C CB  . THR A 1 227 ? 1.047   27.700 -27.901 1.00 15.49 ? 226  THR A CB  1 
ATOM   1825 O OG1 . THR A 1 227 ? 0.769   26.398 -27.358 1.00 16.29 ? 226  THR A OG1 1 
ATOM   1826 C CG2 . THR A 1 227 ? 2.540   28.005 -27.783 1.00 16.52 ? 226  THR A CG2 1 
ATOM   1827 N N   . GLN A 1 228 ? -0.024  30.467 -28.895 1.00 17.36 ? 227  GLN A N   1 
ATOM   1828 C CA  A GLN A 1 228 ? 0.191   31.781 -29.504 0.42 19.68 ? 227  GLN A CA  1 
ATOM   1829 C CA  B GLN A 1 228 ? 0.269   31.781 -29.454 0.58 19.64 ? 227  GLN A CA  1 
ATOM   1830 C C   . GLN A 1 228 ? -0.395  32.888 -28.640 1.00 18.01 ? 227  GLN A C   1 
ATOM   1831 O O   . GLN A 1 228 ? 0.167   33.985 -28.546 1.00 19.32 ? 227  GLN A O   1 
ATOM   1832 C CB  A GLN A 1 228 ? -0.447  31.835 -30.896 0.42 20.74 ? 227  GLN A CB  1 
ATOM   1833 C CB  B GLN A 1 228 ? -0.141  31.848 -30.929 0.58 22.86 ? 227  GLN A CB  1 
ATOM   1834 C CG  A GLN A 1 228 ? -0.305  30.586 -31.724 0.42 25.09 ? 227  GLN A CG  1 
ATOM   1835 C CG  B GLN A 1 228 ? 0.440   33.063 -31.704 0.58 27.60 ? 227  GLN A CG  1 
ATOM   1836 C CD  A GLN A 1 228 ? 1.129   30.155 -31.903 0.42 29.70 ? 227  GLN A CD  1 
ATOM   1837 C CD  B GLN A 1 228 ? 1.855   33.504 -31.262 0.58 34.70 ? 227  GLN A CD  1 
ATOM   1838 O OE1 A GLN A 1 228 ? 2.009   30.968 -32.194 0.42 29.92 ? 227  GLN A OE1 1 
ATOM   1839 O OE1 B GLN A 1 228 ? 2.033   34.607 -30.726 0.58 20.31 ? 227  GLN A OE1 1 
ATOM   1840 N NE2 A GLN A 1 228 ? 1.377   28.861 -31.730 0.42 29.22 ? 227  GLN A NE2 1 
ATOM   1841 N NE2 B GLN A 1 228 ? 2.862   32.661 -31.518 0.58 31.44 ? 227  GLN A NE2 1 
ATOM   1842 N N   . TRP A 1 229 ? -1.546  32.614 -28.021 1.00 16.44 ? 228  TRP A N   1 
ATOM   1843 C CA  . TRP A 1 229 ? -2.204  33.598 -27.164 1.00 17.40 ? 228  TRP A CA  1 
ATOM   1844 C C   . TRP A 1 229 ? -1.340  33.922 -25.958 1.00 15.56 ? 228  TRP A C   1 
ATOM   1845 O O   . TRP A 1 229 ? -1.112  35.096 -25.634 1.00 16.68 ? 228  TRP A O   1 
ATOM   1846 C CB  . TRP A 1 229 ? -3.567  33.080 -26.693 1.00 15.99 ? 228  TRP A CB  1 
ATOM   1847 C CG  . TRP A 1 229 ? -4.353  34.125 -25.914 1.00 16.12 ? 228  TRP A CG  1 
ATOM   1848 C CD1 . TRP A 1 229 ? -5.193  35.067 -26.440 1.00 18.93 ? 228  TRP A CD1 1 
ATOM   1849 C CD2 . TRP A 1 229 ? -4.359  34.339 -24.483 1.00 15.11 ? 228  TRP A CD2 1 
ATOM   1850 N NE1 . TRP A 1 229 ? -5.725  35.847 -25.433 1.00 17.78 ? 228  TRP A NE1 1 
ATOM   1851 C CE2 . TRP A 1 229 ? -5.229  35.421 -24.226 1.00 17.06 ? 228  TRP A CE2 1 
ATOM   1852 C CE3 . TRP A 1 229 ? -3.712  33.720 -23.401 1.00 16.00 ? 228  TRP A CE3 1 
ATOM   1853 C CZ2 . TRP A 1 229 ? -5.475  35.897 -22.934 1.00 14.81 ? 228  TRP A CZ2 1 
ATOM   1854 C CZ3 . TRP A 1 229 ? -3.965  34.191 -22.111 1.00 20.42 ? 228  TRP A CZ3 1 
ATOM   1855 C CH2 . TRP A 1 229 ? -4.833  35.272 -21.893 1.00 17.81 ? 228  TRP A CH2 1 
ATOM   1856 N N   . LEU A 1 230 ? -0.844  32.885 -25.282 1.00 14.40 ? 229  LEU A N   1 
ATOM   1857 C CA  . LEU A 1 230 ? 0.070   33.119 -24.163 1.00 15.60 ? 229  LEU A CA  1 
ATOM   1858 C C   . LEU A 1 230 ? 1.276   33.942 -24.600 1.00 16.42 ? 229  LEU A C   1 
ATOM   1859 O O   . LEU A 1 230 ? 1.664   34.898 -23.915 1.00 16.31 ? 229  LEU A O   1 
ATOM   1860 C CB  . LEU A 1 230 ? 0.535   31.791 -23.568 1.00 16.81 ? 229  LEU A CB  1 
ATOM   1861 C CG  . LEU A 1 230 ? -0.539  30.940 -22.909 1.00 16.08 ? 229  LEU A CG  1 
ATOM   1862 C CD1 . LEU A 1 230 ? -0.010  29.537 -22.667 1.00 15.04 ? 229  LEU A CD1 1 
ATOM   1863 C CD2 . LEU A 1 230 ? -0.957  31.587 -21.572 1.00 15.48 ? 229  LEU A CD2 1 
ATOM   1864 N N   . ARG A 1 231 ? 1.881   33.601 -25.749 1.00 16.94 ? 230  ARG A N   1 
ATOM   1865 C CA  . ARG A 1 231 ? 3.086   34.311 -26.173 1.00 15.90 ? 230  ARG A CA  1 
ATOM   1866 C C   . ARG A 1 231 ? 2.774   35.755 -26.561 1.00 17.01 ? 230  ARG A C   1 
ATOM   1867 O O   . ARG A 1 231 ? 3.511   36.679 -26.194 1.00 19.16 ? 230  ARG A O   1 
ATOM   1868 C CB  . ARG A 1 231 ? 3.755   33.567 -27.340 1.00 15.97 ? 230  ARG A CB  1 
ATOM   1869 C CG  . ARG A 1 231 ? 5.064   34.204 -27.792 1.00 18.78 ? 230  ARG A CG  1 
ATOM   1870 C CD  . ARG A 1 231 ? 5.764   33.336 -28.833 1.00 22.24 ? 230  ARG A CD  1 
ATOM   1871 N NE  . ARG A 1 231 ? 6.123   32.037 -28.276 1.00 20.78 ? 230  ARG A NE  1 
ATOM   1872 C CZ  . ARG A 1 231 ? 5.680   30.869 -28.725 1.00 20.99 ? 230  ARG A CZ  1 
ATOM   1873 N NH1 . ARG A 1 231 ? 4.867   30.785 -29.777 1.00 22.02 ? 230  ARG A NH1 1 
ATOM   1874 N NH2 . ARG A 1 231 ? 6.079   29.751 -28.121 1.00 21.08 ? 230  ARG A NH2 1 
ATOM   1875 N N   . ALA A 1 232 ? 1.684   35.971 -27.301 1.00 19.52 ? 231  ALA A N   1 
ATOM   1876 C CA  . ALA A 1 232 ? 1.352   37.323 -27.742 1.00 22.11 ? 231  ALA A CA  1 
ATOM   1877 C C   . ALA A 1 232 ? 1.071   38.248 -26.568 1.00 20.64 ? 231  ALA A C   1 
ATOM   1878 O O   . ALA A 1 232 ? 1.315   39.457 -26.659 1.00 19.42 ? 231  ALA A O   1 
ATOM   1879 C CB  . ALA A 1 232 ? 0.147   37.290 -28.682 1.00 18.47 ? 231  ALA A CB  1 
ATOM   1880 N N   . ASN A 1 233 ? 0.579   37.701 -25.456 1.00 16.52 ? 232  ASN A N   1 
ATOM   1881 C CA  . ASN A 1 233 ? 0.189   38.501 -24.312 1.00 14.42 ? 232  ASN A CA  1 
ATOM   1882 C C   . ASN A 1 233 ? 1.202   38.447 -23.175 1.00 17.13 ? 232  ASN A C   1 
ATOM   1883 O O   . ASN A 1 233 ? 0.941   39.002 -22.102 1.00 17.48 ? 232  ASN A O   1 
ATOM   1884 C CB  . ASN A 1 233 ? -1.196  38.066 -23.841 1.00 17.99 ? 232  ASN A CB  1 
ATOM   1885 C CG  . ASN A 1 233 ? -2.272  38.485 -24.818 1.00 20.50 ? 232  ASN A CG  1 
ATOM   1886 O OD1 . ASN A 1 233 ? -2.629  39.663 -24.869 1.00 21.21 ? 232  ASN A OD1 1 
ATOM   1887 N ND2 . ASN A 1 233 ? -2.780  37.534 -25.616 1.00 19.74 ? 232  ASN A ND2 1 
ATOM   1888 N N   . GLY A 1 234 ? 2.365   37.840 -23.404 1.00 16.79 ? 233  GLY A N   1 
ATOM   1889 C CA  . GLY A 1 234 ? 3.407   37.800 -22.387 1.00 16.29 ? 233  GLY A CA  1 
ATOM   1890 C C   . GLY A 1 234 ? 3.058   36.992 -21.151 1.00 16.84 ? 233  GLY A C   1 
ATOM   1891 O O   . GLY A 1 234 ? 3.532   37.324 -20.051 1.00 19.70 ? 233  GLY A O   1 
ATOM   1892 N N   . LYS A 1 235 ? 2.261   35.931 -21.303 1.00 15.78 ? 234  LYS A N   1 
ATOM   1893 C CA  . LYS A 1 235 ? 1.756   35.149 -20.177 1.00 15.63 ? 234  LYS A CA  1 
ATOM   1894 C C   . LYS A 1 235 ? 2.406   33.773 -20.136 1.00 18.66 ? 234  LYS A C   1 
ATOM   1895 O O   . LYS A 1 235 ? 3.008   33.317 -21.115 1.00 16.38 ? 234  LYS A O   1 
ATOM   1896 C CB  . LYS A 1 235 ? 0.232   34.977 -20.266 1.00 16.32 ? 234  LYS A CB  1 
ATOM   1897 C CG  . LYS A 1 235 ? -0.543  36.260 -20.472 1.00 13.72 ? 234  LYS A CG  1 
ATOM   1898 C CD  . LYS A 1 235 ? -0.270  37.332 -19.399 1.00 15.80 ? 234  LYS A CD  1 
ATOM   1899 C CE  . LYS A 1 235 ? -1.169  38.573 -19.629 1.00 17.86 ? 234  LYS A CE  1 
ATOM   1900 N NZ  . LYS A 1 235 ? -0.877  39.749 -18.725 1.00 18.24 ? 234  LYS A NZ  1 
ATOM   1901 N N   . LYS A 1 236 ? 2.264   33.105 -18.986 1.00 15.27 ? 235  LYS A N   1 
ATOM   1902 C CA  A LYS A 1 236 ? 2.696   31.725 -18.821 0.54 13.55 ? 235  LYS A CA  1 
ATOM   1903 C CA  B LYS A 1 236 ? 2.699   31.728 -18.796 0.46 13.60 ? 235  LYS A CA  1 
ATOM   1904 C C   . LYS A 1 236 ? 1.477   30.843 -18.587 1.00 16.29 ? 235  LYS A C   1 
ATOM   1905 O O   . LYS A 1 236 ? 0.487   31.278 -17.998 1.00 16.35 ? 235  LYS A O   1 
ATOM   1906 C CB  A LYS A 1 236 ? 3.676   31.583 -17.645 0.54 17.21 ? 235  LYS A CB  1 
ATOM   1907 C CB  B LYS A 1 236 ? 3.628   31.600 -17.578 0.46 17.13 ? 235  LYS A CB  1 
ATOM   1908 C CG  A LYS A 1 236 ? 4.992   32.321 -17.842 0.54 24.16 ? 235  LYS A CG  1 
ATOM   1909 C CG  B LYS A 1 236 ? 4.805   32.557 -17.570 0.46 24.59 ? 235  LYS A CG  1 
ATOM   1910 C CD  A LYS A 1 236 ? 6.155   31.351 -18.007 0.54 29.28 ? 235  LYS A CD  1 
ATOM   1911 C CD  B LYS A 1 236 ? 5.844   32.154 -18.596 0.46 27.44 ? 235  LYS A CD  1 
ATOM   1912 C CE  A LYS A 1 236 ? 7.465   32.093 -18.250 0.54 34.79 ? 235  LYS A CE  1 
ATOM   1913 C CE  B LYS A 1 236 ? 7.225   32.684 -18.209 0.46 34.51 ? 235  LYS A CE  1 
ATOM   1914 N NZ  A LYS A 1 236 ? 8.444   31.283 -19.030 0.54 30.66 ? 235  LYS A NZ  1 
ATOM   1915 N NZ  B LYS A 1 236 ? 7.654   32.198 -16.861 0.46 33.90 ? 235  LYS A NZ  1 
ATOM   1916 N N   . GLY A 1 237 ? 1.558   29.583 -19.043 1.00 15.55 ? 236  GLY A N   1 
ATOM   1917 C CA  . GLY A 1 237 ? 0.455   28.656 -18.885 1.00 15.98 ? 236  GLY A CA  1 
ATOM   1918 C C   . GLY A 1 237 ? 0.886   27.311 -18.322 1.00 14.45 ? 236  GLY A C   1 
ATOM   1919 O O   . GLY A 1 237 ? 2.073   26.991 -18.254 1.00 15.10 ? 236  GLY A O   1 
ATOM   1920 N N   . ILE A 1 238 ? -0.115  26.523 -17.913 1.00 12.66 ? 237  ILE A N   1 
ATOM   1921 C CA  . ILE A 1 238 ? 0.096   25.124 -17.560 1.00 13.77 ? 237  ILE A CA  1 
ATOM   1922 C C   . ILE A 1 238 ? -1.117  24.345 -18.034 1.00 13.98 ? 237  ILE A C   1 
ATOM   1923 O O   . ILE A 1 238 ? -2.228  24.880 -18.095 1.00 15.51 ? 237  ILE A O   1 
ATOM   1924 C CB  . ILE A 1 238 ? 0.327   24.930 -16.033 1.00 14.00 ? 237  ILE A CB  1 
ATOM   1925 C CG1 . ILE A 1 238 ? 0.769   23.492 -15.715 1.00 13.02 ? 237  ILE A CG1 1 
ATOM   1926 C CG2 . ILE A 1 238 ? -0.920  25.299 -15.222 1.00 14.45 ? 237  ILE A CG2 1 
ATOM   1927 C CD1 . ILE A 1 238 ? 1.209   23.328 -14.238 1.00 15.68 ? 237  ILE A CD1 1 
ATOM   1928 N N   . ILE A 1 239 ? -0.900  23.086 -18.418 1.00 14.80 ? 238  ILE A N   1 
ATOM   1929 C CA  . ILE A 1 239 ? -2.015  22.184 -18.685 1.00 14.88 ? 238  ILE A CA  1 
ATOM   1930 C C   . ILE A 1 239 ? -2.338  21.501 -17.363 1.00 15.36 ? 238  ILE A C   1 
ATOM   1931 O O   . ILE A 1 239 ? -1.577  20.647 -16.896 1.00 17.41 ? 238  ILE A O   1 
ATOM   1932 C CB  . ILE A 1 239 ? -1.682  21.175 -19.790 1.00 13.94 ? 238  ILE A CB  1 
ATOM   1933 C CG1 . ILE A 1 239 ? -1.451  21.916 -21.119 1.00 13.92 ? 238  ILE A CG1 1 
ATOM   1934 C CG2 . ILE A 1 239 ? -2.818  20.130 -19.917 1.00 15.68 ? 238  ILE A CG2 1 
ATOM   1935 C CD1 . ILE A 1 239 ? -2.735  22.473 -21.733 1.00 17.03 ? 238  ILE A CD1 1 
ATOM   1936 N N   . GLY A 1 240 ? -3.450  21.910 -16.724 1.00 13.71 ? 239  GLY A N   1 
ATOM   1937 C CA  . GLY A 1 240 ? -3.761  21.391 -15.391 1.00 16.48 ? 239  GLY A CA  1 
ATOM   1938 C C   . GLY A 1 240 ? -4.488  20.061 -15.371 1.00 16.56 ? 239  GLY A C   1 
ATOM   1939 O O   . GLY A 1 240 ? -4.563  19.417 -14.320 1.00 13.97 ? 239  GLY A O   1 
ATOM   1940 N N   . GLU A 1 241 ? -5.041  19.650 -16.508 1.00 15.48 ? 240  GLU A N   1 
ATOM   1941 C CA  . GLU A 1 241 ? -5.692  18.355 -16.672 1.00 12.82 ? 240  GLU A CA  1 
ATOM   1942 C C   . GLU A 1 241 ? -5.498  17.925 -18.114 1.00 12.75 ? 240  GLU A C   1 
ATOM   1943 O O   . GLU A 1 241 ? -5.778  18.718 -19.021 1.00 14.56 ? 240  GLU A O   1 
ATOM   1944 C CB  . GLU A 1 241 ? -7.194  18.429 -16.388 1.00 15.17 ? 240  GLU A CB  1 
ATOM   1945 C CG  . GLU A 1 241 ? -7.554  18.735 -14.940 1.00 14.75 ? 240  GLU A CG  1 
ATOM   1946 C CD  . GLU A 1 241 ? -9.012  18.443 -14.654 1.00 17.32 ? 240  GLU A CD  1 
ATOM   1947 O OE1 . GLU A 1 241 ? -9.664  17.751 -15.480 1.00 17.89 ? 240  GLU A OE1 1 
ATOM   1948 O OE2 . GLU A 1 241 ? -9.531  18.892 -13.617 1.00 16.23 ? 240  GLU A OE2 1 
ATOM   1949 N N   . PHE A 1 242 ? -5.038  16.689 -18.316 1.00 15.78 ? 241  PHE A N   1 
ATOM   1950 C CA  . PHE A 1 242 ? -5.034  16.054 -19.636 1.00 14.71 ? 241  PHE A CA  1 
ATOM   1951 C C   . PHE A 1 242 ? -5.025  14.548 -19.434 1.00 15.53 ? 241  PHE A C   1 
ATOM   1952 O O   . PHE A 1 242 ? -4.592  14.050 -18.391 1.00 15.23 ? 241  PHE A O   1 
ATOM   1953 C CB  . PHE A 1 242 ? -3.847  16.495 -20.524 1.00 16.11 ? 241  PHE A CB  1 
ATOM   1954 C CG  . PHE A 1 242 ? -2.523  15.862 -20.175 1.00 14.92 ? 241  PHE A CG  1 
ATOM   1955 C CD1 . PHE A 1 242 ? -1.825  16.251 -19.038 1.00 15.94 ? 241  PHE A CD1 1 
ATOM   1956 C CD2 . PHE A 1 242 ? -1.950  14.901 -21.005 1.00 17.58 ? 241  PHE A CD2 1 
ATOM   1957 C CE1 . PHE A 1 242 ? -0.584  15.670 -18.720 1.00 15.58 ? 241  PHE A CE1 1 
ATOM   1958 C CE2 . PHE A 1 242 ? -0.703  14.326 -20.703 1.00 19.36 ? 241  PHE A CE2 1 
ATOM   1959 C CZ  . PHE A 1 242 ? -0.024  14.707 -19.550 1.00 17.17 ? 241  PHE A CZ  1 
ATOM   1960 N N   . ALA A 1 243 ? -5.543  13.827 -20.428 1.00 16.54 ? 242  ALA A N   1 
ATOM   1961 C CA  . ALA A 1 243 ? -5.545  12.371 -20.371 1.00 15.96 ? 242  ALA A CA  1 
ATOM   1962 C C   . ALA A 1 243 ? -5.826  11.844 -21.763 1.00 18.68 ? 242  ALA A C   1 
ATOM   1963 O O   . ALA A 1 243 ? -6.283  12.578 -22.643 1.00 19.21 ? 242  ALA A O   1 
ATOM   1964 C CB  . ALA A 1 243 ? -6.595  11.824 -19.397 1.00 19.51 ? 242  ALA A CB  1 
ATOM   1965 N N   . GLY A 1 244 ? -5.558  10.545 -21.932 1.00 20.60 ? 243  GLY A N   1 
ATOM   1966 C CA  . GLY A 1 244 ? -5.967  9.784  -23.102 1.00 18.32 ? 243  GLY A CA  1 
ATOM   1967 C C   . GLY A 1 244 ? -5.979  8.323  -22.720 1.00 19.47 ? 243  GLY A C   1 
ATOM   1968 O O   . GLY A 1 244 ? -5.350  7.921  -21.736 1.00 19.42 ? 243  GLY A O   1 
ATOM   1969 N N   . GLY A 1 245 ? -6.717  7.527  -23.493 1.00 21.41 ? 244  GLY A N   1 
ATOM   1970 C CA  . GLY A 1 245 ? -6.824  6.111  -23.189 1.00 21.88 ? 244  GLY A CA  1 
ATOM   1971 C C   . GLY A 1 245 ? -5.533  5.349  -23.438 1.00 24.36 ? 244  GLY A C   1 
ATOM   1972 O O   . GLY A 1 245 ? -4.626  5.801  -24.131 1.00 21.93 ? 244  GLY A O   1 
ATOM   1973 N N   . ALA A 1 246 ? -5.462  4.146  -22.859 1.00 21.64 ? 245  ALA A N   1 
ATOM   1974 C CA  . ALA A 1 246 ? -4.302  3.265  -22.996 1.00 24.27 ? 245  ALA A CA  1 
ATOM   1975 C C   . ALA A 1 246 ? -4.391  2.527  -24.332 1.00 28.89 ? 245  ALA A C   1 
ATOM   1976 O O   . ALA A 1 246 ? -4.708  1.336  -24.413 1.00 24.32 ? 245  ALA A O   1 
ATOM   1977 C CB  . ALA A 1 246 ? -4.228  2.300  -21.818 1.00 27.59 ? 245  ALA A CB  1 
ATOM   1978 N N   . ASN A 1 247 ? -4.098  3.259  -25.405 1.00 22.65 ? 246  ASN A N   1 
ATOM   1979 C CA  . ASN A 1 247 ? -4.124  2.698  -26.751 1.00 20.92 ? 246  ASN A CA  1 
ATOM   1980 C C   . ASN A 1 247 ? -3.151  3.474  -27.627 1.00 22.22 ? 246  ASN A C   1 
ATOM   1981 O O   . ASN A 1 247 ? -2.700  4.565  -27.270 1.00 24.67 ? 246  ASN A O   1 
ATOM   1982 C CB  . ASN A 1 247 ? -5.539  2.710  -27.358 1.00 22.34 ? 246  ASN A CB  1 
ATOM   1983 C CG  . ASN A 1 247 ? -6.161  4.096  -27.385 1.00 24.01 ? 246  ASN A CG  1 
ATOM   1984 O OD1 . ASN A 1 247 ? -5.666  4.990  -28.059 1.00 23.93 ? 246  ASN A OD1 1 
ATOM   1985 N ND2 . ASN A 1 247 ? -7.247  4.278  -26.639 1.00 20.12 ? 246  ASN A ND2 1 
ATOM   1986 N N   . ASP A 1 248 ? -2.837  2.891  -28.790 1.00 24.16 ? 247  ASP A N   1 
ATOM   1987 C CA  . ASP A 1 248 ? -1.748  3.402  -29.620 1.00 26.02 ? 247  ASP A CA  1 
ATOM   1988 C C   . ASP A 1 248 ? -2.007  4.828  -30.086 1.00 22.64 ? 247  ASP A C   1 
ATOM   1989 O O   . ASP A 1 248 ? -1.106  5.673  -30.043 1.00 22.94 ? 247  ASP A O   1 
ATOM   1990 C CB  . ASP A 1 248 ? -1.530  2.495  -30.834 1.00 26.55 ? 247  ASP A CB  1 
ATOM   1991 C CG  . ASP A 1 248 ? -0.622  1.307  -30.536 1.00 37.21 ? 247  ASP A CG  1 
ATOM   1992 O OD1 . ASP A 1 248 ? -0.344  1.035  -29.349 1.00 34.76 ? 247  ASP A OD1 1 
ATOM   1993 O OD2 . ASP A 1 248 ? -0.199  0.637  -31.505 1.00 43.21 ? 247  ASP A OD2 1 
ATOM   1994 N N   . VAL A 1 249 ? -3.217  5.108  -30.584 1.00 23.86 ? 248  VAL A N   1 
ATOM   1995 C CA  . VAL A 1 249 ? -3.509  6.447  -31.101 1.00 19.76 ? 248  VAL A CA  1 
ATOM   1996 C C   . VAL A 1 249 ? -3.378  7.496  -29.998 1.00 21.33 ? 248  VAL A C   1 
ATOM   1997 O O   . VAL A 1 249 ? -2.811  8.574  -30.217 1.00 21.72 ? 248  VAL A O   1 
ATOM   1998 C CB  . VAL A 1 249 ? -4.902  6.493  -31.762 1.00 22.17 ? 248  VAL A CB  1 
ATOM   1999 C CG1 . VAL A 1 249 ? -5.254  7.941  -32.162 1.00 20.72 ? 248  VAL A CG1 1 
ATOM   2000 C CG2 . VAL A 1 249 ? -4.952  5.584  -32.982 1.00 24.55 ? 248  VAL A CG2 1 
ATOM   2001 N N   . CYS A 1 250 ? -3.905  7.204  -28.803 1.00 23.12 ? 249  CYS A N   1 
ATOM   2002 C CA  . CYS A 1 250 ? -3.802  8.152  -27.692 1.00 22.40 ? 249  CYS A CA  1 
ATOM   2003 C C   . CYS A 1 250 ? -2.365  8.307  -27.217 1.00 22.92 ? 249  CYS A C   1 
ATOM   2004 O O   . CYS A 1 250 ? -1.940  9.417  -26.869 1.00 21.23 ? 249  CYS A O   1 
ATOM   2005 C CB  . CYS A 1 250 ? -4.683  7.711  -26.528 1.00 21.21 ? 249  CYS A CB  1 
ATOM   2006 S SG  . CYS A 1 250 ? -6.434  7.932  -26.789 1.00 21.55 ? 249  CYS A SG  1 
ATOM   2007 N N   . GLU A 1 251 ? -1.607  7.207  -27.178 1.00 22.85 ? 250  GLU A N   1 
ATOM   2008 C CA  . GLU A 1 251 ? -0.200  7.302  -26.796 1.00 28.32 ? 250  GLU A CA  1 
ATOM   2009 C C   . GLU A 1 251 ? 0.522   8.308  -27.676 1.00 24.07 ? 250  GLU A C   1 
ATOM   2010 O O   . GLU A 1 251 ? 1.226   9.198  -27.180 1.00 23.56 ? 250  GLU A O   1 
ATOM   2011 C CB  . GLU A 1 251 ? 0.489   5.939  -26.896 1.00 28.01 ? 250  GLU A CB  1 
ATOM   2012 C CG  . GLU A 1 251 ? 0.119   4.934  -25.828 1.00 30.73 ? 250  GLU A CG  1 
ATOM   2013 C CD  . GLU A 1 251 ? 0.922   3.641  -25.960 1.00 30.17 ? 250  GLU A CD  1 
ATOM   2014 O OE1 . GLU A 1 251 ? 2.124   3.712  -26.301 1.00 40.21 ? 250  GLU A OE1 1 
ATOM   2015 O OE2 . GLU A 1 251 ? 0.356   2.554  -25.740 1.00 40.40 ? 250  GLU A OE2 1 
ATOM   2016 N N   . THR A 1 252 ? 0.338   8.186  -28.994 1.00 20.59 ? 251  THR A N   1 
ATOM   2017 C CA  . THR A 1 252 ? 0.982   9.102  -29.923 1.00 20.24 ? 251  THR A CA  1 
ATOM   2018 C C   . THR A 1 252 ? 0.454   10.524 -29.765 1.00 23.30 ? 251  THR A C   1 
ATOM   2019 O O   . THR A 1 252 ? 1.221   11.487 -29.882 1.00 22.56 ? 251  THR A O   1 
ATOM   2020 C CB  . THR A 1 252 ? 0.791   8.606  -31.354 1.00 22.32 ? 251  THR A CB  1 
ATOM   2021 O OG1 . THR A 1 252 ? 1.301   7.271  -31.454 1.00 26.88 ? 251  THR A OG1 1 
ATOM   2022 C CG2 . THR A 1 252 ? 1.539   9.502  -32.322 1.00 24.49 ? 251  THR A CG2 1 
ATOM   2023 N N   . ALA A 1 253 ? -0.846  10.685 -29.487 1.00 18.34 ? 252  ALA A N   1 
ATOM   2024 C CA  . ALA A 1 253 ? -1.377  12.032 -29.302 1.00 18.78 ? 252  ALA A CA  1 
ATOM   2025 C C   . ALA A 1 253 ? -0.802  12.681 -28.046 1.00 18.03 ? 252  ALA A C   1 
ATOM   2026 O O   . ALA A 1 253 ? -0.498  13.883 -28.041 1.00 20.83 ? 252  ALA A O   1 
ATOM   2027 C CB  . ALA A 1 253 ? -2.910  12.001 -29.233 1.00 18.77 ? 252  ALA A CB  1 
ATOM   2028 N N   . ILE A 1 254 ? -0.645  11.898 -26.977 1.00 16.80 ? 253  ILE A N   1 
ATOM   2029 C CA  . ILE A 1 254 ? -0.072  12.424 -25.742 1.00 14.84 ? 253  ILE A CA  1 
ATOM   2030 C C   . ILE A 1 254 ? 1.368   12.877 -25.967 1.00 20.09 ? 253  ILE A C   1 
ATOM   2031 O O   . ILE A 1 254 ? 1.745   14.006 -25.614 1.00 18.53 ? 253  ILE A O   1 
ATOM   2032 C CB  . ILE A 1 254 ? -0.169  11.377 -24.619 1.00 19.70 ? 253  ILE A CB  1 
ATOM   2033 C CG1 . ILE A 1 254 ? -1.625  11.218 -24.182 1.00 19.75 ? 253  ILE A CG1 1 
ATOM   2034 C CG2 . ILE A 1 254 ? 0.662   11.830 -23.430 1.00 16.76 ? 253  ILE A CG2 1 
ATOM   2035 C CD1 . ILE A 1 254 ? -1.899  9.968  -23.367 1.00 23.46 ? 253  ILE A CD1 1 
ATOM   2036 N N   . THR A 1 255 ? 2.202   12.011 -26.552 1.00 18.86 ? 254  THR A N   1 
ATOM   2037 C CA  A THR A 1 255 ? 3.590   12.419 -26.719 0.68 19.74 ? 254  THR A CA  1 
ATOM   2038 C CA  B THR A 1 255 ? 3.602   12.357 -26.789 0.32 19.77 ? 254  THR A CA  1 
ATOM   2039 C C   . THR A 1 255 ? 3.727   13.552 -27.728 1.00 17.67 ? 254  THR A C   1 
ATOM   2040 O O   . THR A 1 255 ? 4.572   14.433 -27.536 1.00 20.85 ? 254  THR A O   1 
ATOM   2041 C CB  A THR A 1 255 ? 4.484   11.236 -27.100 0.68 23.96 ? 254  THR A CB  1 
ATOM   2042 C CB  B THR A 1 255 ? 4.342   11.148 -27.367 0.32 23.85 ? 254  THR A CB  1 
ATOM   2043 O OG1 A THR A 1 255 ? 3.995   10.599 -28.284 0.68 19.98 ? 254  THR A OG1 1 
ATOM   2044 O OG1 B THR A 1 255 ? 4.302   10.059 -26.435 0.32 26.51 ? 254  THR A OG1 1 
ATOM   2045 C CG2 A THR A 1 255 ? 4.539   10.229 -25.955 0.68 25.85 ? 254  THR A CG2 1 
ATOM   2046 C CG2 B THR A 1 255 ? 5.785   11.497 -27.672 0.32 24.75 ? 254  THR A CG2 1 
ATOM   2047 N N   . GLY A 1 256 ? 2.899   13.592 -28.769 1.00 17.59 ? 255  GLY A N   1 
ATOM   2048 C CA  . GLY A 1 256 ? 2.990   14.708 -29.698 1.00 18.31 ? 255  GLY A CA  1 
ATOM   2049 C C   . GLY A 1 256 ? 2.642   16.033 -29.046 1.00 17.80 ? 255  GLY A C   1 
ATOM   2050 O O   . GLY A 1 256 ? 3.264   17.062 -29.328 1.00 17.71 ? 255  GLY A O   1 
ATOM   2051 N N   . MET A 1 257 ? 1.647   16.024 -28.164 1.00 15.48 ? 256  MET A N   1 
ATOM   2052 C CA  . MET A 1 257 ? 1.279   17.243 -27.457 1.00 18.01 ? 256  MET A CA  1 
ATOM   2053 C C   . MET A 1 257 ? 2.399   17.679 -26.520 1.00 16.30 ? 256  MET A C   1 
ATOM   2054 O O   . MET A 1 257 ? 2.790   18.851 -26.505 1.00 18.06 ? 256  MET A O   1 
ATOM   2055 C CB  . MET A 1 257 ? -0.029  17.034 -26.688 1.00 16.89 ? 256  MET A CB  1 
ATOM   2056 C CG  . MET A 1 257 ? -0.550  18.309 -26.064 1.00 16.30 ? 256  MET A CG  1 
ATOM   2057 S SD  . MET A 1 257 ? -2.104  18.097 -25.137 1.00 20.00 ? 256  MET A SD  1 
ATOM   2058 C CE  . MET A 1 257 ? -1.464  17.445 -23.601 1.00 20.84 ? 256  MET A CE  1 
ATOM   2059 N N   . LEU A 1 258 ? 2.943   16.742 -25.740 1.00 15.62 ? 257  LEU A N   1 
ATOM   2060 C CA  . LEU A 1 258 ? 3.993   17.125 -24.801 1.00 15.75 ? 257  LEU A CA  1 
ATOM   2061 C C   . LEU A 1 258 ? 5.273   17.517 -25.524 1.00 15.87 ? 257  LEU A C   1 
ATOM   2062 O O   . LEU A 1 258 ? 5.993   18.413 -25.058 1.00 17.35 ? 257  LEU A O   1 
ATOM   2063 C CB  . LEU A 1 258 ? 4.255   15.990 -23.804 1.00 16.62 ? 257  LEU A CB  1 
ATOM   2064 C CG  . LEU A 1 258 ? 3.042   15.686 -22.915 1.00 15.60 ? 257  LEU A CG  1 
ATOM   2065 C CD1 . LEU A 1 258 ? 3.310   14.422 -22.127 1.00 18.07 ? 257  LEU A CD1 1 
ATOM   2066 C CD2 . LEU A 1 258 ? 2.748   16.851 -21.963 1.00 16.96 ? 257  LEU A CD2 1 
ATOM   2067 N N   . ASP A 1 259 ? 5.574   16.868 -26.654 1.00 17.23 ? 258  ASP A N   1 
ATOM   2068 C CA  . ASP A 1 259 ? 6.735   17.273 -27.449 1.00 17.34 ? 258  ASP A CA  1 
ATOM   2069 C C   . ASP A 1 259 ? 6.585   18.704 -27.961 1.00 17.33 ? 258  ASP A C   1 
ATOM   2070 O O   . ASP A 1 259 ? 7.559   19.465 -28.011 1.00 16.86 ? 258  ASP A O   1 
ATOM   2071 C CB  . ASP A 1 259 ? 6.933   16.310 -28.627 1.00 18.76 ? 258  ASP A CB  1 
ATOM   2072 C CG  . ASP A 1 259 ? 7.521   14.960 -28.209 1.00 21.67 ? 258  ASP A CG  1 
ATOM   2073 O OD1 . ASP A 1 259 ? 8.013   14.840 -27.060 1.00 22.17 ? 258  ASP A OD1 1 
ATOM   2074 O OD2 . ASP A 1 259 ? 7.500   14.020 -29.050 1.00 23.81 ? 258  ASP A OD2 1 
ATOM   2075 N N   . TYR A 1 260 ? 5.376   19.079 -28.378 1.00 16.24 ? 259  TYR A N   1 
ATOM   2076 C CA  . TYR A 1 260 ? 5.139   20.455 -28.796 1.00 15.59 ? 259  TYR A CA  1 
ATOM   2077 C C   . TYR A 1 260 ? 5.301   21.420 -27.627 1.00 14.48 ? 259  TYR A C   1 
ATOM   2078 O O   . TYR A 1 260 ? 5.955   22.462 -27.751 1.00 17.35 ? 259  TYR A O   1 
ATOM   2079 C CB  . TYR A 1 260 ? 3.743   20.557 -29.411 1.00 18.71 ? 259  TYR A CB  1 
ATOM   2080 C CG  . TYR A 1 260 ? 3.345   21.955 -29.820 1.00 17.64 ? 259  TYR A CG  1 
ATOM   2081 C CD1 . TYR A 1 260 ? 3.716   22.473 -31.065 1.00 16.10 ? 259  TYR A CD1 1 
ATOM   2082 C CD2 . TYR A 1 260 ? 2.594   22.760 -28.964 1.00 19.36 ? 259  TYR A CD2 1 
ATOM   2083 C CE1 . TYR A 1 260 ? 3.333   23.759 -31.441 1.00 16.88 ? 259  TYR A CE1 1 
ATOM   2084 C CE2 . TYR A 1 260 ? 2.209   24.040 -29.335 1.00 20.93 ? 259  TYR A CE2 1 
ATOM   2085 C CZ  . TYR A 1 260 ? 2.587   24.537 -30.567 1.00 17.94 ? 259  TYR A CZ  1 
ATOM   2086 O OH  . TYR A 1 260 ? 2.184   25.814 -30.903 1.00 21.36 ? 259  TYR A OH  1 
ATOM   2087 N N   . MET A 1 261 ? 4.695   21.103 -26.483 1.00 15.95 ? 260  MET A N   1 
ATOM   2088 C CA  . MET A 1 261 ? 4.894   21.966 -25.321 1.00 13.79 ? 260  MET A CA  1 
ATOM   2089 C C   . MET A 1 261 ? 6.369   22.104 -24.990 1.00 15.27 ? 260  MET A C   1 
ATOM   2090 O O   . MET A 1 261 ? 6.826   23.188 -24.600 1.00 16.85 ? 260  MET A O   1 
ATOM   2091 C CB  . MET A 1 261 ? 4.133   21.430 -24.106 1.00 15.32 ? 260  MET A CB  1 
ATOM   2092 C CG  . MET A 1 261 ? 2.640   21.483 -24.309 1.00 15.22 ? 260  MET A CG  1 
ATOM   2093 S SD  . MET A 1 261 ? 1.690   20.616 -23.064 1.00 16.92 ? 260  MET A SD  1 
ATOM   2094 C CE  . MET A 1 261 ? 2.081   21.596 -21.603 1.00 16.99 ? 260  MET A CE  1 
ATOM   2095 N N   . ALA A 1 262 ? 7.133   21.019 -25.138 1.00 15.17 ? 261  ALA A N   1 
ATOM   2096 C CA  . ALA A 1 262 ? 8.554   21.068 -24.793 1.00 16.76 ? 261  ALA A CA  1 
ATOM   2097 C C   . ALA A 1 262 ? 9.349   21.999 -25.707 1.00 17.75 ? 261  ALA A C   1 
ATOM   2098 O O   . ALA A 1 262 ? 10.412  22.484 -25.304 1.00 20.26 ? 261  ALA A O   1 
ATOM   2099 C CB  . ALA A 1 262 ? 9.136   19.654 -24.808 1.00 15.91 ? 261  ALA A CB  1 
ATOM   2100 N N   . GLN A 1 263 ? 8.867   22.272 -26.921 1.00 17.18 ? 262  GLN A N   1 
ATOM   2101 C CA  . GLN A 1 263 ? 9.518   23.269 -27.760 1.00 17.82 ? 262  GLN A CA  1 
ATOM   2102 C C   . GLN A 1 263 ? 8.903   24.640 -27.598 1.00 22.81 ? 262  GLN A C   1 
ATOM   2103 O O   . GLN A 1 263 ? 9.192   25.541 -28.390 1.00 22.01 ? 262  GLN A O   1 
ATOM   2104 C CB  . GLN A 1 263 ? 9.476   22.853 -29.235 1.00 16.19 ? 262  GLN A CB  1 
ATOM   2105 C CG  . GLN A 1 263 ? 10.209  21.552 -29.493 1.00 29.07 ? 262  GLN A CG  1 
ATOM   2106 C CD  . GLN A 1 263 ? 11.624  21.543 -28.918 1.00 31.71 ? 262  GLN A CD  1 
ATOM   2107 O OE1 . GLN A 1 263 ? 12.366  22.529 -29.016 1.00 32.15 ? 262  GLN A OE1 1 
ATOM   2108 N NE2 . GLN A 1 263 ? 11.997  20.430 -28.298 1.00 31.94 ? 262  GLN A NE2 1 
ATOM   2109 N N   . ASN A 1 264 ? 8.057   24.823 -26.590 1.00 18.91 ? 263  ASN A N   1 
ATOM   2110 C CA  . ASN A 1 264 ? 7.408   26.102 -26.376 1.00 17.60 ? 263  ASN A CA  1 
ATOM   2111 C C   . ASN A 1 264 ? 7.387   26.419 -24.889 1.00 17.41 ? 263  ASN A C   1 
ATOM   2112 O O   . ASN A 1 264 ? 6.373   26.869 -24.337 1.00 19.10 ? 263  ASN A O   1 
ATOM   2113 C CB  . ASN A 1 264 ? 6.007   26.100 -26.982 1.00 15.24 ? 263  ASN A CB  1 
ATOM   2114 C CG  . ASN A 1 264 ? 6.047   26.079 -28.496 1.00 18.23 ? 263  ASN A CG  1 
ATOM   2115 O OD1 . ASN A 1 264 ? 6.275   27.108 -29.124 1.00 20.71 ? 263  ASN A OD1 1 
ATOM   2116 N ND2 . ASN A 1 264 ? 5.836   24.903 -29.087 1.00 15.98 ? 263  ASN A ND2 1 
ATOM   2117 N N   . THR A 1 265 ? 8.507   26.163 -24.214 1.00 17.66 ? 264  THR A N   1 
ATOM   2118 C CA  . THR A 1 265 ? 8.561   26.390 -22.769 1.00 16.05 ? 264  THR A CA  1 
ATOM   2119 C C   . THR A 1 265 ? 8.721   27.861 -22.405 1.00 18.79 ? 264  THR A C   1 
ATOM   2120 O O   . THR A 1 265 ? 8.697   28.190 -21.213 1.00 21.24 ? 264  THR A O   1 
ATOM   2121 C CB  . THR A 1 265 ? 9.690   25.574 -22.118 1.00 18.98 ? 264  THR A CB  1 
ATOM   2122 O OG1 . THR A 1 265 ? 10.956  25.869 -22.732 1.00 20.96 ? 264  THR A OG1 1 
ATOM   2123 C CG2 . THR A 1 265 ? 9.403   24.074 -22.208 1.00 17.01 ? 264  THR A CG2 1 
ATOM   2124 N N   . ASP A 1 266 ? 8.880   28.755 -23.379 1.00 20.23 ? 265  ASP A N   1 
ATOM   2125 C CA  . ASP A 1 266 ? 8.777   30.170 -23.061 1.00 21.86 ? 265  ASP A CA  1 
ATOM   2126 C C   . ASP A 1 266 ? 7.398   30.504 -22.513 1.00 23.33 ? 265  ASP A C   1 
ATOM   2127 O O   . ASP A 1 266 ? 7.259   31.467 -21.748 1.00 21.91 ? 265  ASP A O   1 
ATOM   2128 C CB  . ASP A 1 266 ? 9.115   31.048 -24.276 1.00 20.39 ? 265  ASP A CB  1 
ATOM   2129 C CG  . ASP A 1 266 ? 8.145   30.872 -25.453 1.00 21.36 ? 265  ASP A CG  1 
ATOM   2130 O OD1 . ASP A 1 266 ? 7.623   29.763 -25.662 1.00 22.24 ? 265  ASP A OD1 1 
ATOM   2131 O OD2 . ASP A 1 266 ? 7.924   31.855 -26.180 1.00 25.34 ? 265  ASP A OD2 1 
ATOM   2132 N N   . VAL A 1 267 ? 6.379   29.708 -22.854 1.00 18.85 ? 266  VAL A N   1 
ATOM   2133 C CA  . VAL A 1 267 ? 5.047   29.935 -22.296 1.00 15.32 ? 266  VAL A CA  1 
ATOM   2134 C C   . VAL A 1 267 ? 4.516   28.742 -21.504 1.00 17.51 ? 266  VAL A C   1 
ATOM   2135 O O   . VAL A 1 267 ? 3.734   28.941 -20.572 1.00 18.11 ? 266  VAL A O   1 
ATOM   2136 C CB  . VAL A 1 267 ? 4.028   30.353 -23.381 1.00 20.21 ? 266  VAL A CB  1 
ATOM   2137 C CG1 . VAL A 1 267 ? 4.485   31.625 -24.085 1.00 20.26 ? 266  VAL A CG1 1 
ATOM   2138 C CG2 . VAL A 1 267 ? 3.764   29.241 -24.387 1.00 19.56 ? 266  VAL A CG2 1 
ATOM   2139 N N   . TRP A 1 268 ? 4.915   27.506 -21.829 1.00 16.36 ? 267  TRP A N   1 
ATOM   2140 C CA  . TRP A 1 268 ? 4.368   26.341 -21.114 1.00 15.64 ? 267  TRP A CA  1 
ATOM   2141 C C   . TRP A 1 268 ? 5.259   25.930 -19.947 1.00 17.85 ? 267  TRP A C   1 
ATOM   2142 O O   . TRP A 1 268 ? 6.420   25.547 -20.142 1.00 18.04 ? 267  TRP A O   1 
ATOM   2143 C CB  . TRP A 1 268 ? 4.165   25.147 -22.047 1.00 15.18 ? 267  TRP A CB  1 
ATOM   2144 C CG  . TRP A 1 268 ? 2.992   25.346 -22.974 1.00 16.16 ? 267  TRP A CG  1 
ATOM   2145 C CD1 . TRP A 1 268 ? 3.055   25.485 -24.322 1.00 16.74 ? 267  TRP A CD1 1 
ATOM   2146 C CD2 . TRP A 1 268 ? 1.604   25.490 -22.616 1.00 15.32 ? 267  TRP A CD2 1 
ATOM   2147 N NE1 . TRP A 1 268 ? 1.793   25.668 -24.841 1.00 15.36 ? 267  TRP A NE1 1 
ATOM   2148 C CE2 . TRP A 1 268 ? 0.887   25.684 -23.814 1.00 14.78 ? 267  TRP A CE2 1 
ATOM   2149 C CE3 . TRP A 1 268 ? 0.898   25.456 -21.407 1.00 14.94 ? 267  TRP A CE3 1 
ATOM   2150 C CZ2 . TRP A 1 268 ? -0.495  25.853 -23.853 1.00 15.49 ? 267  TRP A CZ2 1 
ATOM   2151 C CZ3 . TRP A 1 268 ? -0.502  25.623 -21.442 1.00 16.14 ? 267  TRP A CZ3 1 
ATOM   2152 C CH2 . TRP A 1 268 ? -1.174  25.819 -22.667 1.00 18.08 ? 267  TRP A CH2 1 
ATOM   2153 N N   . THR A 1 269 ? 4.696   25.979 -18.740 1.00 15.98 ? 268  THR A N   1 
ATOM   2154 C CA  . THR A 1 269 ? 5.386   25.564 -17.531 1.00 14.62 ? 268  THR A CA  1 
ATOM   2155 C C   . THR A 1 269 ? 5.245   24.078 -17.242 1.00 17.61 ? 268  THR A C   1 
ATOM   2156 O O   . THR A 1 269 ? 5.934   23.588 -16.348 1.00 17.10 ? 268  THR A O   1 
ATOM   2157 C CB  . THR A 1 269 ? 4.878   26.363 -16.313 1.00 14.91 ? 268  THR A CB  1 
ATOM   2158 O OG1 . THR A 1 269 ? 3.503   26.015 -16.038 1.00 16.59 ? 268  THR A OG1 1 
ATOM   2159 C CG2 . THR A 1 269 ? 4.995   27.876 -16.578 1.00 18.34 ? 268  THR A CG2 1 
ATOM   2160 N N   . GLY A 1 270 ? 4.380   23.341 -17.958 1.00 15.15 ? 269  GLY A N   1 
ATOM   2161 C CA  . GLY A 1 270 ? 4.271   21.909 -17.747 1.00 13.89 ? 269  GLY A CA  1 
ATOM   2162 C C   . GLY A 1 270 ? 2.834   21.428 -17.814 1.00 18.06 ? 269  GLY A C   1 
ATOM   2163 O O   . GLY A 1 270 ? 1.975   22.067 -18.427 1.00 16.19 ? 269  GLY A O   1 
ATOM   2164 N N   . ALA A 1 271 ? 2.591   20.268 -17.193 1.00 13.29 ? 270  ALA A N   1 
ATOM   2165 C CA  . ALA A 1 271 ? 1.366   19.521 -17.427 1.00 15.64 ? 270  ALA A CA  1 
ATOM   2166 C C   . ALA A 1 271 ? 1.060   18.602 -16.256 1.00 18.06 ? 270  ALA A C   1 
ATOM   2167 O O   . ALA A 1 271 ? 1.967   18.123 -15.560 1.00 17.55 ? 270  ALA A O   1 
ATOM   2168 C CB  . ALA A 1 271 ? 1.473   18.714 -18.728 1.00 15.45 ? 270  ALA A CB  1 
ATOM   2169 N N   . ILE A 1 272 ? -0.235  18.369 -16.038 1.00 15.09 ? 271  ILE A N   1 
ATOM   2170 C CA  . ILE A 1 272 ? -0.726  17.596 -14.901 1.00 16.45 ? 271  ILE A CA  1 
ATOM   2171 C C   . ILE A 1 272 ? -1.754  16.592 -15.412 1.00 15.26 ? 271  ILE A C   1 
ATOM   2172 O O   . ILE A 1 272 ? -2.788  16.988 -15.967 1.00 15.60 ? 271  ILE A O   1 
ATOM   2173 C CB  . ILE A 1 272 ? -1.351  18.494 -13.821 1.00 13.62 ? 271  ILE A CB  1 
ATOM   2174 C CG1 . ILE A 1 272 ? -0.431  19.671 -13.448 1.00 14.27 ? 271  ILE A CG1 1 
ATOM   2175 C CG2 . ILE A 1 272 ? -1.663  17.656 -12.560 1.00 14.33 ? 271  ILE A CG2 1 
ATOM   2176 C CD1 . ILE A 1 272 ? -0.979  20.568 -12.295 1.00 14.28 ? 271  ILE A CD1 1 
ATOM   2177 N N   . TRP A 1 273 ? -1.476  15.303 -15.212 1.00 14.41 ? 272  TRP A N   1 
ATOM   2178 C CA  . TRP A 1 273 ? -2.346  14.228 -15.695 1.00 16.21 ? 272  TRP A CA  1 
ATOM   2179 C C   . TRP A 1 273 ? -3.639  14.170 -14.885 1.00 16.92 ? 272  TRP A C   1 
ATOM   2180 O O   . TRP A 1 273 ? -3.640  14.414 -13.680 1.00 16.56 ? 272  TRP A O   1 
ATOM   2181 C CB  . TRP A 1 273 ? -1.609  12.871 -15.591 1.00 15.50 ? 272  TRP A CB  1 
ATOM   2182 C CG  . TRP A 1 273 ? -2.410  11.678 -16.071 1.00 14.45 ? 272  TRP A CG  1 
ATOM   2183 C CD1 . TRP A 1 273 ? -3.209  10.865 -15.318 1.00 16.02 ? 272  TRP A CD1 1 
ATOM   2184 C CD2 . TRP A 1 273 ? -2.490  11.184 -17.416 1.00 17.57 ? 272  TRP A CD2 1 
ATOM   2185 N NE1 . TRP A 1 273 ? -3.794  9.899  -16.116 1.00 20.16 ? 272  TRP A NE1 1 
ATOM   2186 C CE2 . TRP A 1 273 ? -3.356  10.070 -17.407 1.00 17.79 ? 272  TRP A CE2 1 
ATOM   2187 C CE3 . TRP A 1 273 ? -1.906  11.573 -18.624 1.00 18.59 ? 272  TRP A CE3 1 
ATOM   2188 C CZ2 . TRP A 1 273 ? -3.659  9.342  -18.569 1.00 19.91 ? 272  TRP A CZ2 1 
ATOM   2189 C CZ3 . TRP A 1 273 ? -2.207  10.845 -19.781 1.00 19.19 ? 272  TRP A CZ3 1 
ATOM   2190 C CH2 . TRP A 1 273 ? -3.069  9.743  -19.738 1.00 18.59 ? 272  TRP A CH2 1 
ATOM   2191 N N   . TRP A 1 274 ? -4.751  13.827 -15.543 1.00 16.17 ? 273  TRP A N   1 
ATOM   2192 C CA  . TRP A 1 274 ? -6.002  13.506 -14.848 1.00 17.71 ? 273  TRP A CA  1 
ATOM   2193 C C   . TRP A 1 274 ? -6.258  12.013 -15.032 1.00 19.82 ? 273  TRP A C   1 
ATOM   2194 O O   . TRP A 1 274 ? -6.511  11.579 -16.157 1.00 19.06 ? 273  TRP A O   1 
ATOM   2195 C CB  . TRP A 1 274 ? -7.176  14.319 -15.410 1.00 16.44 ? 273  TRP A CB  1 
ATOM   2196 C CG  . TRP A 1 274 ? -8.466  13.975 -14.718 1.00 15.25 ? 273  TRP A CG  1 
ATOM   2197 C CD1 . TRP A 1 274 ? -9.333  12.974 -15.051 1.00 17.94 ? 273  TRP A CD1 1 
ATOM   2198 C CD2 . TRP A 1 274 ? -8.979  14.569 -13.518 1.00 18.69 ? 273  TRP A CD2 1 
ATOM   2199 N NE1 . TRP A 1 274 ? -10.379 12.934 -14.152 1.00 19.05 ? 273  TRP A NE1 1 
ATOM   2200 C CE2 . TRP A 1 274 ? -10.180 13.895 -13.198 1.00 18.34 ? 273  TRP A CE2 1 
ATOM   2201 C CE3 . TRP A 1 274 ? -8.557  15.619 -12.699 1.00 15.96 ? 273  TRP A CE3 1 
ATOM   2202 C CZ2 . TRP A 1 274 ? -10.949 14.233 -12.087 1.00 20.46 ? 273  TRP A CZ2 1 
ATOM   2203 C CZ3 . TRP A 1 274 ? -9.325  15.954 -11.599 1.00 16.64 ? 273  TRP A CZ3 1 
ATOM   2204 C CH2 . TRP A 1 274 ? -10.508 15.261 -11.307 1.00 17.20 ? 273  TRP A CH2 1 
ATOM   2205 N N   . ALA A 1 275 ? -6.207  11.205 -13.958 1.00 17.59 ? 274  ALA A N   1 
ATOM   2206 C CA  . ALA A 1 275 ? -5.947  11.583 -12.566 1.00 15.62 ? 274  ALA A CA  1 
ATOM   2207 C C   . ALA A 1 275 ? -5.473  10.354 -11.785 1.00 19.81 ? 274  ALA A C   1 
ATOM   2208 O O   . ALA A 1 275 ? -5.736  9.222  -12.180 1.00 19.96 ? 274  ALA A O   1 
ATOM   2209 C CB  . ALA A 1 275 ? -7.200  12.139 -11.904 1.00 18.56 ? 274  ALA A CB  1 
ATOM   2210 N N   . ALA A 1 276 ? -4.802  10.580 -10.664 1.00 17.73 ? 275  ALA A N   1 
ATOM   2211 C CA  . ALA A 1 276 ? -4.590  9.545  -9.664  1.00 20.48 ? 275  ALA A CA  1 
ATOM   2212 C C   . ALA A 1 276 ? -5.579  9.746  -8.507  1.00 18.70 ? 275  ALA A C   1 
ATOM   2213 O O   . ALA A 1 276 ? -6.465  10.608 -8.557  1.00 20.41 ? 275  ALA A O   1 
ATOM   2214 C CB  . ALA A 1 276 ? -3.141  9.571  -9.178  1.00 18.94 ? 275  ALA A CB  1 
ATOM   2215 N N   . GLY A 1 277 ? -5.413  8.965  -7.443  1.00 19.12 ? 276  GLY A N   1 
ATOM   2216 C CA  . GLY A 1 277 ? -6.335  8.977  -6.327  1.00 19.54 ? 276  GLY A CA  1 
ATOM   2217 C C   . GLY A 1 277 ? -6.728  7.555  -5.974  1.00 19.32 ? 276  GLY A C   1 
ATOM   2218 O O   . GLY A 1 277 ? -6.632  6.648  -6.808  1.00 23.11 ? 276  GLY A O   1 
ATOM   2219 N N   . PRO A 1 278 ? -7.181  7.328  -4.735  1.00 21.35 ? 277  PRO A N   1 
ATOM   2220 C CA  . PRO A 1 278 ? -7.325  5.951  -4.240  1.00 22.11 ? 277  PRO A CA  1 
ATOM   2221 C C   . PRO A 1 278 ? -8.644  5.257  -4.558  1.00 24.50 ? 277  PRO A C   1 
ATOM   2222 O O   . PRO A 1 278 ? -8.746  4.047  -4.305  1.00 26.30 ? 277  PRO A O   1 
ATOM   2223 C CB  . PRO A 1 278 ? -7.158  6.120  -2.719  1.00 25.75 ? 277  PRO A CB  1 
ATOM   2224 C CG  . PRO A 1 278 ? -7.667  7.453  -2.443  1.00 22.21 ? 277  PRO A CG  1 
ATOM   2225 C CD  . PRO A 1 278 ? -7.406  8.320  -3.670  1.00 23.02 ? 277  PRO A CD  1 
ATOM   2226 N N   . TRP A 1 279 ? -9.634  5.946  -5.131  1.00 24.10 ? 278  TRP A N   1 
ATOM   2227 C CA  . TRP A 1 279 ? -10.947 5.351  -5.368  1.00 27.37 ? 278  TRP A CA  1 
ATOM   2228 C C   . TRP A 1 279 ? -11.304 5.277  -6.853  1.00 30.17 ? 278  TRP A C   1 
ATOM   2229 O O   . TRP A 1 279 ? -12.483 5.264  -7.218  1.00 26.53 ? 278  TRP A O   1 
ATOM   2230 C CB  . TRP A 1 279 ? -12.023 6.123  -4.608  1.00 22.78 ? 278  TRP A CB  1 
ATOM   2231 C CG  . TRP A 1 279 ? -12.223 5.677  -3.174  1.00 32.14 ? 278  TRP A CG  1 
ATOM   2232 C CD1 . TRP A 1 279 ? -11.466 4.774  -2.466  1.00 26.90 ? 278  TRP A CD1 1 
ATOM   2233 C CD2 . TRP A 1 279 ? -13.262 6.110  -2.286  1.00 25.40 ? 278  TRP A CD2 1 
ATOM   2234 N NE1 . TRP A 1 279 ? -11.973 4.631  -1.192  1.00 27.19 ? 278  TRP A NE1 1 
ATOM   2235 C CE2 . TRP A 1 279 ? -13.080 5.429  -1.063  1.00 26.74 ? 278  TRP A CE2 1 
ATOM   2236 C CE3 . TRP A 1 279 ? -14.341 6.996  -2.415  1.00 27.86 ? 278  TRP A CE3 1 
ATOM   2237 C CZ2 . TRP A 1 279 ? -13.928 5.625  0.036   1.00 33.08 ? 278  TRP A CZ2 1 
ATOM   2238 C CZ3 . TRP A 1 279 ? -15.185 7.187  -1.327  1.00 27.71 ? 278  TRP A CZ3 1 
ATOM   2239 C CH2 . TRP A 1 279 ? -14.971 6.503  -0.117  1.00 29.95 ? 278  TRP A CH2 1 
ATOM   2240 N N   . TRP A 1 280 ? -10.305 5.213  -7.729  1.00 25.34 ? 279  TRP A N   1 
ATOM   2241 C CA  . TRP A 1 280 ? -10.576 5.162  -9.158  1.00 21.64 ? 279  TRP A CA  1 
ATOM   2242 C C   . TRP A 1 280 ? -10.799 3.748  -9.696  1.00 28.03 ? 279  TRP A C   1 
ATOM   2243 O O   . TRP A 1 280 ? -11.435 3.597  -10.744 1.00 27.19 ? 279  TRP A O   1 
ATOM   2244 C CB  . TRP A 1 280 ? -9.426  5.810  -9.930  1.00 20.60 ? 279  TRP A CB  1 
ATOM   2245 C CG  . TRP A 1 280 ? -9.427  7.322  -9.979  1.00 19.62 ? 279  TRP A CG  1 
ATOM   2246 C CD1 . TRP A 1 280 ? -8.436  8.152  -9.536  1.00 21.41 ? 279  TRP A CD1 1 
ATOM   2247 C CD2 . TRP A 1 280 ? -10.445 8.174  -10.525 1.00 20.37 ? 279  TRP A CD2 1 
ATOM   2248 N NE1 . TRP A 1 280 ? -8.771  9.465  -9.774  1.00 19.22 ? 279  TRP A NE1 1 
ATOM   2249 C CE2 . TRP A 1 280 ? -9.999  9.503  -10.382 1.00 20.10 ? 279  TRP A CE2 1 
ATOM   2250 C CE3 . TRP A 1 280 ? -11.689 7.939  -11.123 1.00 23.01 ? 279  TRP A CE3 1 
ATOM   2251 C CZ2 . TRP A 1 280 ? -10.750 10.596 -10.812 1.00 22.40 ? 279  TRP A CZ2 1 
ATOM   2252 C CZ3 . TRP A 1 280 ? -12.432 9.018  -11.551 1.00 21.07 ? 279  TRP A CZ3 1 
ATOM   2253 C CH2 . TRP A 1 280 ? -11.957 10.335 -11.401 1.00 20.29 ? 279  TRP A CH2 1 
ATOM   2254 N N   . GLY A 1 281 ? -10.284 2.720  -9.030  1.00 27.30 ? 280  GLY A N   1 
ATOM   2255 C CA  . GLY A 1 281 ? -10.486 1.363  -9.514  1.00 27.75 ? 280  GLY A CA  1 
ATOM   2256 C C   . GLY A 1 281 ? -10.028 1.224  -10.950 1.00 31.35 ? 280  GLY A C   1 
ATOM   2257 O O   . GLY A 1 281 ? -8.912  1.619  -11.308 1.00 25.49 ? 280  GLY A O   1 
ATOM   2258 N N   . ASP A 1 282 ? -10.914 0.705  -11.802 1.00 28.38 ? 281  ASP A N   1 
ATOM   2259 C CA  . ASP A 1 282 ? -10.591 0.413  -13.192 1.00 28.48 ? 281  ASP A CA  1 
ATOM   2260 C C   . ASP A 1 282 ? -10.799 1.610  -14.128 1.00 29.77 ? 281  ASP A C   1 
ATOM   2261 O O   . ASP A 1 282 ? -10.910 1.413  -15.344 1.00 26.97 ? 281  ASP A O   1 
ATOM   2262 C CB  . ASP A 1 282 ? -11.411 -0.791 -13.678 1.00 29.80 ? 281  ASP A CB  1 
ATOM   2263 C CG  . ASP A 1 282 ? -12.911 -0.498 -13.786 1.00 38.03 ? 281  ASP A CG  1 
ATOM   2264 O OD1 . ASP A 1 282 ? -13.367 0.605  -13.403 1.00 36.89 ? 281  ASP A OD1 1 
ATOM   2265 O OD2 . ASP A 1 282 ? -13.643 -1.390 -14.271 1.00 47.80 ? 281  ASP A OD2 1 
ATOM   2266 N N   . TYR A 1 283 ? -10.856 2.832  -13.586 1.00 26.36 ? 282  TYR A N   1 
ATOM   2267 C CA  . TYR A 1 283 ? -11.000 4.044  -14.388 1.00 20.64 ? 282  TYR A CA  1 
ATOM   2268 C C   . TYR A 1 283 ? -10.004 4.068  -15.537 1.00 25.53 ? 282  TYR A C   1 
ATOM   2269 O O   . TYR A 1 283 ? -8.821  3.781  -15.350 1.00 23.91 ? 282  TYR A O   1 
ATOM   2270 C CB  . TYR A 1 283 ? -10.773 5.259  -13.491 1.00 24.24 ? 282  TYR A CB  1 
ATOM   2271 C CG  . TYR A 1 283 ? -10.962 6.630  -14.100 1.00 22.58 ? 282  TYR A CG  1 
ATOM   2272 C CD1 . TYR A 1 283 ? -12.108 6.957  -14.808 1.00 24.00 ? 282  TYR A CD1 1 
ATOM   2273 C CD2 . TYR A 1 283 ? -10.025 7.629  -13.879 1.00 18.61 ? 282  TYR A CD2 1 
ATOM   2274 C CE1 . TYR A 1 283 ? -12.295 8.240  -15.315 1.00 21.91 ? 282  TYR A CE1 1 
ATOM   2275 C CE2 . TYR A 1 283 ? -10.202 8.908  -14.373 1.00 19.65 ? 282  TYR A CE2 1 
ATOM   2276 C CZ  . TYR A 1 283 ? -11.345 9.209  -15.096 1.00 24.76 ? 282  TYR A CZ  1 
ATOM   2277 O OH  . TYR A 1 283 ? -11.516 10.491 -15.579 1.00 20.92 ? 282  TYR A OH  1 
ATOM   2278 N N   . ILE A 1 284 ? -10.488 4.451  -16.724 1.00 23.40 ? 283  ILE A N   1 
ATOM   2279 C CA  . ILE A 1 284 ? -9.673  4.419  -17.935 1.00 22.96 ? 283  ILE A CA  1 
ATOM   2280 C C   . ILE A 1 284 ? -8.437  5.318  -17.851 1.00 20.73 ? 283  ILE A C   1 
ATOM   2281 O O   . ILE A 1 284 ? -7.478  5.106  -18.605 1.00 23.46 ? 283  ILE A O   1 
ATOM   2282 C CB  . ILE A 1 284 ? -10.528 4.806  -19.171 1.00 22.88 ? 283  ILE A CB  1 
ATOM   2283 C CG1 . ILE A 1 284 ? -11.314 6.094  -18.904 1.00 20.66 ? 283  ILE A CG1 1 
ATOM   2284 C CG2 . ILE A 1 284 ? -11.460 3.665  -19.570 1.00 24.25 ? 283  ILE A CG2 1 
ATOM   2285 C CD1 . ILE A 1 284 ? -11.998 6.662  -20.148 1.00 25.11 ? 283  ILE A CD1 1 
ATOM   2286 N N   . PHE A 1 285 ? -8.434  6.333  -16.976 1.00 21.05 ? 284  PHE A N   1 
ATOM   2287 C CA  . PHE A 1 285 ? -7.303  7.254  -16.875 1.00 20.23 ? 284  PHE A CA  1 
ATOM   2288 C C   . PHE A 1 285 ? -6.543  7.144  -15.549 1.00 17.69 ? 284  PHE A C   1 
ATOM   2289 O O   . PHE A 1 285 ? -5.752  8.044  -15.229 1.00 18.81 ? 284  PHE A O   1 
ATOM   2290 C CB  . PHE A 1 285 ? -7.752  8.710  -17.059 1.00 19.81 ? 284  PHE A CB  1 
ATOM   2291 C CG  . PHE A 1 285 ? -8.463  8.989  -18.364 1.00 20.96 ? 284  PHE A CG  1 
ATOM   2292 C CD1 . PHE A 1 285 ? -8.067  8.391  -19.541 1.00 22.51 ? 284  PHE A CD1 1 
ATOM   2293 C CD2 . PHE A 1 285 ? -9.527  9.887  -18.398 1.00 20.94 ? 284  PHE A CD2 1 
ATOM   2294 C CE1 . PHE A 1 285 ? -8.729  8.671  -20.731 1.00 21.48 ? 284  PHE A CE1 1 
ATOM   2295 C CE2 . PHE A 1 285 ? -10.196 10.165 -19.577 1.00 20.26 ? 284  PHE A CE2 1 
ATOM   2296 C CZ  . PHE A 1 285 ? -9.805  9.569  -20.736 1.00 22.35 ? 284  PHE A CZ  1 
ATOM   2297 N N   . SER A 1 286 ? -6.745  6.077  -14.766 1.00 19.18 ? 285  SER A N   1 
ATOM   2298 C CA  . SER A 1 286 ? -6.207  6.070  -13.406 1.00 20.59 ? 285  SER A CA  1 
ATOM   2299 C C   . SER A 1 286 ? -4.688  5.983  -13.403 1.00 21.20 ? 285  SER A C   1 
ATOM   2300 O O   . SER A 1 286 ? -4.107  4.989  -13.862 1.00 23.45 ? 285  SER A O   1 
ATOM   2301 C CB  . SER A 1 286 ? -6.770  4.924  -12.574 1.00 18.71 ? 285  SER A CB  1 
ATOM   2302 O OG  . SER A 1 286 ? -6.119  4.951  -11.312 1.00 22.43 ? 285  SER A OG  1 
ATOM   2303 N N   . MET A 1 287 ? -4.060  7.008  -12.829 1.00 18.62 ? 286  MET A N   1 
ATOM   2304 C CA  . MET A 1 287 ? -2.622  7.070  -12.624 1.00 20.85 ? 286  MET A CA  1 
ATOM   2305 C C   . MET A 1 287 ? -2.221  6.577  -11.229 1.00 24.05 ? 286  MET A C   1 
ATOM   2306 O O   . MET A 1 287 ? -1.072  6.759  -10.818 1.00 22.16 ? 286  MET A O   1 
ATOM   2307 C CB  . MET A 1 287 ? -2.161  8.514  -12.880 1.00 22.66 ? 286  MET A CB  1 
ATOM   2308 C CG  . MET A 1 287 ? -0.665  8.807  -12.880 1.00 20.62 ? 286  MET A CG  1 
ATOM   2309 S SD  . MET A 1 287 ? 0.302   7.857  -14.072 1.00 23.40 ? 286  MET A SD  1 
ATOM   2310 C CE  . MET A 1 287 ? -0.180  8.643  -15.618 1.00 22.77 ? 286  MET A CE  1 
ATOM   2311 N N   . GLU A 1 288 ? -3.132  5.933  -10.498 1.00 20.43 ? 287  GLU A N   1 
ATOM   2312 C CA  . GLU A 1 288 ? -2.832  5.528  -9.124  1.00 21.82 ? 287  GLU A CA  1 
ATOM   2313 C C   . GLU A 1 288 ? -1.928  4.300  -9.092  1.00 23.64 ? 287  GLU A C   1 
ATOM   2314 O O   . GLU A 1 288 ? -2.305  3.249  -9.622  1.00 25.00 ? 287  GLU A O   1 
ATOM   2315 C CB  . GLU A 1 288 ? -4.114  5.239  -8.349  1.00 22.41 ? 287  GLU A CB  1 
ATOM   2316 C CG  . GLU A 1 288 ? -3.887  4.949  -6.858  1.00 22.91 ? 287  GLU A CG  1 
ATOM   2317 C CD  . GLU A 1 288 ? -3.601  6.207  -6.052  1.00 20.11 ? 287  GLU A CD  1 
ATOM   2318 O OE1 . GLU A 1 288 ? -3.388  7.282  -6.658  1.00 22.74 ? 287  GLU A OE1 1 
ATOM   2319 O OE2 . GLU A 1 288 ? -3.597  6.118  -4.797  1.00 22.34 ? 287  GLU A OE2 1 
ATOM   2320 N N   . PRO A 1 289 ? -0.767  4.372  -8.453  1.00 23.34 ? 288  PRO A N   1 
ATOM   2321 C CA  . PRO A 1 289 ? 0.022   3.154  -8.218  1.00 24.78 ? 288  PRO A CA  1 
ATOM   2322 C C   . PRO A 1 289 ? -0.760  2.184  -7.341  1.00 31.23 ? 288  PRO A C   1 
ATOM   2323 O O   . PRO A 1 289 ? -1.546  2.599  -6.485  1.00 29.78 ? 288  PRO A O   1 
ATOM   2324 C CB  . PRO A 1 289 ? 1.273   3.672  -7.495  1.00 26.12 ? 288  PRO A CB  1 
ATOM   2325 C CG  . PRO A 1 289 ? 1.269   5.158  -7.666  1.00 25.38 ? 288  PRO A CG  1 
ATOM   2326 C CD  . PRO A 1 289 ? -0.161  5.569  -7.854  1.00 24.92 ? 288  PRO A CD  1 
ATOM   2327 N N   . ASP A 1 290 ? -0.537  0.881  -7.538  1.00 33.23 ? 289  ASP A N   1 
ATOM   2328 C CA  . ASP A 1 290 ? 0.390   0.337  -8.531  1.00 31.14 ? 289  ASP A CA  1 
ATOM   2329 C C   . ASP A 1 290 ? -0.319  -0.227 -9.749  1.00 37.14 ? 289  ASP A C   1 
ATOM   2330 O O   . ASP A 1 290 ? 0.341   -0.693 -10.680 1.00 38.47 ? 289  ASP A O   1 
ATOM   2331 C CB  . ASP A 1 290 ? 1.236   -0.785 -7.913  1.00 37.69 ? 289  ASP A CB  1 
ATOM   2332 C CG  . ASP A 1 290 ? 2.023   -0.329 -6.706  1.00 42.63 ? 289  ASP A CG  1 
ATOM   2333 O OD1 . ASP A 1 290 ? 2.607   0.774  -6.759  1.00 39.95 ? 289  ASP A OD1 1 
ATOM   2334 O OD2 . ASP A 1 290 ? 2.054   -1.076 -5.702  1.00 60.82 ? 289  ASP A OD2 1 
ATOM   2335 N N   . ASN A 1 291 ? -1.655  -0.209 -9.740  1.00 31.99 ? 290  ASN A N   1 
ATOM   2336 C CA  . ASN A 1 291 ? -2.435  -0.968 -10.712 1.00 33.97 ? 290  ASN A CA  1 
ATOM   2337 C C   . ASN A 1 291 ? -3.397  -0.130 -11.548 1.00 27.13 ? 290  ASN A C   1 
ATOM   2338 O O   . ASN A 1 291 ? -4.183  -0.704 -12.307 1.00 28.79 ? 290  ASN A O   1 
ATOM   2339 C CB  . ASN A 1 291 ? -3.219  -2.073 -10.004 1.00 36.92 ? 290  ASN A CB  1 
ATOM   2340 C CG  . ASN A 1 291 ? -2.316  -3.089 -9.348  1.00 44.73 ? 290  ASN A CG  1 
ATOM   2341 O OD1 . ASN A 1 291 ? -1.549  -3.777 -10.022 1.00 47.26 ? 290  ASN A OD1 1 
ATOM   2342 N ND2 . ASN A 1 291 ? -2.404  -3.197 -8.025  1.00 43.47 ? 290  ASN A ND2 1 
ATOM   2343 N N   . GLY A 1 292 ? -3.379  1.196  -11.431 1.00 24.41 ? 291  GLY A N   1 
ATOM   2344 C CA  . GLY A 1 292 ? -4.168  2.008  -12.341 1.00 26.39 ? 291  GLY A CA  1 
ATOM   2345 C C   . GLY A 1 292 ? -3.728  1.820  -13.781 1.00 23.15 ? 291  GLY A C   1 
ATOM   2346 O O   . GLY A 1 292 ? -2.543  1.634  -14.071 1.00 24.46 ? 291  GLY A O   1 
ATOM   2347 N N   . ILE A 1 293 ? -4.698  1.875  -14.696 1.00 24.33 ? 292  ILE A N   1 
ATOM   2348 C CA  . ILE A 1 293 ? -4.416  1.562  -16.099 1.00 22.89 ? 292  ILE A CA  1 
ATOM   2349 C C   . ILE A 1 293 ? -3.416  2.551  -16.690 1.00 22.27 ? 292  ILE A C   1 
ATOM   2350 O O   . ILE A 1 293 ? -2.529  2.172  -17.471 1.00 24.04 ? 292  ILE A O   1 
ATOM   2351 C CB  . ILE A 1 293 ? -5.721  1.536  -16.918 1.00 26.57 ? 292  ILE A CB  1 
ATOM   2352 C CG1 . ILE A 1 293 ? -6.577  0.326  -16.523 1.00 30.48 ? 292  ILE A CG1 1 
ATOM   2353 C CG2 . ILE A 1 293 ? -5.418  1.470  -18.406 1.00 41.75 ? 292  ILE A CG2 1 
ATOM   2354 C CD1 . ILE A 1 293 ? -8.004  0.373  -17.076 1.00 44.52 ? 292  ILE A CD1 1 
ATOM   2355 N N   . ALA A 1 294 ? -3.554  3.835  -16.360 1.00 19.15 ? 293  ALA A N   1 
ATOM   2356 C CA  . ALA A 1 294 ? -2.596  4.806  -16.872 1.00 17.60 ? 293  ALA A CA  1 
ATOM   2357 C C   . ALA A 1 294 ? -1.256  4.683  -16.163 1.00 20.95 ? 293  ALA A C   1 
ATOM   2358 O O   . ALA A 1 294 ? -0.204  4.889  -16.782 1.00 22.95 ? 293  ALA A O   1 
ATOM   2359 C CB  . ALA A 1 294 ? -3.150  6.228  -16.745 1.00 18.76 ? 293  ALA A CB  1 
ATOM   2360 N N   . TYR A 1 295 ? -1.268  4.333  -14.874 1.00 20.73 ? 294  TYR A N   1 
ATOM   2361 C CA  . TYR A 1 295 ? -0.008  4.085  -14.177 1.00 20.90 ? 294  TYR A CA  1 
ATOM   2362 C C   . TYR A 1 295 ? 0.786   2.968  -14.848 1.00 23.48 ? 294  TYR A C   1 
ATOM   2363 O O   . TYR A 1 295 ? 2.009   3.077  -15.024 1.00 24.73 ? 294  TYR A O   1 
ATOM   2364 C CB  . TYR A 1 295 ? -0.273  3.751  -12.704 1.00 23.70 ? 294  TYR A CB  1 
ATOM   2365 C CG  . TYR A 1 295 ? 1.006   3.505  -11.938 1.00 24.90 ? 294  TYR A CG  1 
ATOM   2366 C CD1 . TYR A 1 295 ? 1.783   4.566  -11.500 1.00 24.78 ? 294  TYR A CD1 1 
ATOM   2367 C CD2 . TYR A 1 295 ? 1.449   2.219  -11.686 1.00 25.61 ? 294  TYR A CD2 1 
ATOM   2368 C CE1 . TYR A 1 295 ? 2.960   4.354  -10.815 1.00 28.62 ? 294  TYR A CE1 1 
ATOM   2369 C CE2 . TYR A 1 295 ? 2.630   1.996  -11.004 1.00 27.28 ? 294  TYR A CE2 1 
ATOM   2370 C CZ  . TYR A 1 295 ? 3.381   3.070  -10.575 1.00 27.97 ? 294  TYR A CZ  1 
ATOM   2371 O OH  . TYR A 1 295 ? 4.557   2.862  -9.895  1.00 31.69 ? 294  TYR A OH  1 
ATOM   2372 N N   . GLN A 1 296 ? 0.105   1.894  -15.249 1.00 21.67 ? 295  GLN A N   1 
ATOM   2373 C CA  . GLN A 1 296 ? 0.774   0.756  -15.868 1.00 24.92 ? 295  GLN A CA  1 
ATOM   2374 C C   . GLN A 1 296 ? 1.145   1.020  -17.320 1.00 21.99 ? 295  GLN A C   1 
ATOM   2375 O O   . GLN A 1 296 ? 2.252   0.667  -17.747 1.00 24.27 ? 295  GLN A O   1 
ATOM   2376 C CB  . GLN A 1 296 ? -0.118  -0.483 -15.784 1.00 27.00 ? 295  GLN A CB  1 
ATOM   2377 C CG  . GLN A 1 296 ? -0.065  -1.158 -14.451 1.00 34.70 ? 295  GLN A CG  1 
ATOM   2378 C CD  . GLN A 1 296 ? 1.296   -1.747 -14.176 1.00 47.40 ? 295  GLN A CD  1 
ATOM   2379 O OE1 . GLN A 1 296 ? 1.962   -2.244 -15.088 1.00 37.47 ? 295  GLN A OE1 1 
ATOM   2380 N NE2 . GLN A 1 296 ? 1.734   -1.676 -12.919 1.00 43.82 ? 295  GLN A NE2 1 
ATOM   2381 N N   . GLN A 1 297 ? 0.229   1.617  -18.097 1.00 22.15 ? 296  GLN A N   1 
ATOM   2382 C CA  . GLN A 1 297 ? 0.366   1.645  -19.547 1.00 23.41 ? 296  GLN A CA  1 
ATOM   2383 C C   . GLN A 1 297 ? 0.732   3.004  -20.123 1.00 27.67 ? 296  GLN A C   1 
ATOM   2384 O O   . GLN A 1 297 ? 1.330   3.046  -21.200 1.00 26.04 ? 296  GLN A O   1 
ATOM   2385 C CB  . GLN A 1 297 ? -0.925  1.145  -20.215 1.00 24.13 ? 296  GLN A CB  1 
ATOM   2386 C CG  . GLN A 1 297 ? -1.153  -0.352 -20.007 1.00 29.73 ? 296  GLN A CG  1 
ATOM   2387 C CD  . GLN A 1 297 ? -2.413  -0.877 -20.687 1.00 24.77 ? 296  GLN A CD  1 
ATOM   2388 O OE1 . GLN A 1 297 ? -2.581  -0.750 -21.895 1.00 33.19 ? 296  GLN A OE1 1 
ATOM   2389 N NE2 . GLN A 1 297 ? -3.303  -1.456 -19.901 1.00 37.75 ? 296  GLN A NE2 1 
ATOM   2390 N N   . ILE A 1 298 ? 0.432   4.105  -19.438 1.00 20.98 ? 297  ILE A N   1 
ATOM   2391 C CA  . ILE A 1 298 ? 0.772   5.432  -19.945 1.00 20.69 ? 297  ILE A CA  1 
ATOM   2392 C C   . ILE A 1 298 ? 2.057   5.965  -19.323 1.00 22.17 ? 297  ILE A C   1 
ATOM   2393 O O   . ILE A 1 298 ? 2.882   6.564  -20.014 1.00 24.88 ? 297  ILE A O   1 
ATOM   2394 C CB  . ILE A 1 298 ? -0.395  6.417  -19.725 1.00 19.75 ? 297  ILE A CB  1 
ATOM   2395 C CG1 . ILE A 1 298 ? -1.606  6.015  -20.566 1.00 23.41 ? 297  ILE A CG1 1 
ATOM   2396 C CG2 . ILE A 1 298 ? 0.027   7.858  -20.069 1.00 19.11 ? 297  ILE A CG2 1 
ATOM   2397 C CD1 . ILE A 1 298 ? -1.309  6.006  -22.062 1.00 25.77 ? 297  ILE A CD1 1 
ATOM   2398 N N   . LEU A 1 299 ? 2.253   5.762  -18.025 1.00 21.74 ? 298  LEU A N   1 
ATOM   2399 C CA  . LEU A 1 299 ? 3.435   6.326  -17.378 1.00 18.45 ? 298  LEU A CA  1 
ATOM   2400 C C   . LEU A 1 299 ? 4.745   5.958  -18.072 1.00 22.24 ? 298  LEU A C   1 
ATOM   2401 O O   . LEU A 1 299 ? 5.636   6.820  -18.120 1.00 25.83 ? 298  LEU A O   1 
ATOM   2402 C CB  . LEU A 1 299 ? 3.468   5.911  -15.897 1.00 22.87 ? 298  LEU A CB  1 
ATOM   2403 C CG  . LEU A 1 299 ? 4.603   6.521  -15.070 1.00 25.54 ? 298  LEU A CG  1 
ATOM   2404 C CD1 . LEU A 1 299 ? 4.557   8.044  -15.091 1.00 28.51 ? 298  LEU A CD1 1 
ATOM   2405 C CD2 . LEU A 1 299 ? 4.548   5.998  -13.646 1.00 28.88 ? 298  LEU A CD2 1 
ATOM   2406 N N   . PRO A 1 300 ? 4.930   4.755  -18.639 1.00 20.61 ? 299  PRO A N   1 
ATOM   2407 C CA  . PRO A 1 300 ? 6.176   4.491  -19.379 1.00 30.17 ? 299  PRO A CA  1 
ATOM   2408 C C   . PRO A 1 300 ? 6.444   5.457  -20.532 1.00 25.85 ? 299  PRO A C   1 
ATOM   2409 O O   . PRO A 1 300 ? 7.615   5.697  -20.858 1.00 33.66 ? 299  PRO A O   1 
ATOM   2410 C CB  . PRO A 1 300 ? 5.979   3.054  -19.889 1.00 29.23 ? 299  PRO A CB  1 
ATOM   2411 C CG  . PRO A 1 300 ? 5.071   2.418  -18.890 1.00 26.75 ? 299  PRO A CG  1 
ATOM   2412 C CD  . PRO A 1 300 ? 4.112   3.530  -18.511 1.00 28.37 ? 299  PRO A CD  1 
ATOM   2413 N N   . ILE A 1 301 ? 5.412   6.010  -21.174 1.00 23.32 ? 300  ILE A N   1 
ATOM   2414 C CA  . ILE A 1 301 ? 5.669   6.948  -22.265 1.00 28.68 ? 300  ILE A CA  1 
ATOM   2415 C C   . ILE A 1 301 ? 5.881   8.369  -21.765 1.00 30.93 ? 300  ILE A C   1 
ATOM   2416 O O   . ILE A 1 301 ? 6.302   9.232  -22.550 1.00 31.25 ? 300  ILE A O   1 
ATOM   2417 C CB  . ILE A 1 301 ? 4.557   6.925  -23.338 1.00 30.23 ? 300  ILE A CB  1 
ATOM   2418 C CG1 . ILE A 1 301 ? 3.320   7.694  -22.878 1.00 27.39 ? 300  ILE A CG1 1 
ATOM   2419 C CG2 . ILE A 1 301 ? 4.189   5.487  -23.690 1.00 32.30 ? 300  ILE A CG2 1 
ATOM   2420 C CD1 . ILE A 1 301 ? 2.273   7.856  -23.962 1.00 29.03 ? 300  ILE A CD1 1 
ATOM   2421 N N   . LEU A 1 302 ? 5.635   8.637  -20.481 1.00 25.60 ? 301  LEU A N   1 
ATOM   2422 C CA  . LEU A 1 302 ? 5.892   9.951  -19.901 1.00 27.24 ? 301  LEU A CA  1 
ATOM   2423 C C   . LEU A 1 302 ? 7.306   10.083 -19.353 1.00 33.57 ? 301  LEU A C   1 
ATOM   2424 O O   . LEU A 1 302 ? 7.721   11.194 -18.994 1.00 26.67 ? 301  LEU A O   1 
ATOM   2425 C CB  . LEU A 1 302 ? 4.879   10.237 -18.795 1.00 27.66 ? 301  LEU A CB  1 
ATOM   2426 C CG  . LEU A 1 302 ? 3.431   10.133 -19.284 1.00 29.23 ? 301  LEU A CG  1 
ATOM   2427 C CD1 . LEU A 1 302 ? 2.476   10.471 -18.165 1.00 25.85 ? 301  LEU A CD1 1 
ATOM   2428 C CD2 . LEU A 1 302 ? 3.193   11.052 -20.485 1.00 27.16 ? 301  LEU A CD2 1 
ATOM   2429 N N   . THR A 1 303 ? 8.046   8.973  -19.297 1.00 36.49 ? 302  THR A N   1 
ATOM   2430 C CA  . THR A 1 303 ? 9.436   8.944  -18.834 1.00 42.71 ? 302  THR A CA  1 
ATOM   2431 C C   . THR A 1 303 ? 10.303  10.093 -19.339 1.00 38.56 ? 302  THR A C   1 
ATOM   2432 O O   . THR A 1 303 ? 10.986  10.713 -18.512 1.00 33.49 ? 302  THR A O   1 
ATOM   2433 C CB  . THR A 1 303 ? 10.032  7.581  -19.220 1.00 37.00 ? 302  THR A CB  1 
ATOM   2434 O OG1 . THR A 1 303 ? 9.511   6.576  -18.341 1.00 42.28 ? 302  THR A OG1 1 
ATOM   2435 C CG2 . THR A 1 303 ? 11.558  7.605  -19.146 1.00 48.68 ? 302  THR A CG2 1 
ATOM   2436 N N   . PRO A 1 304 ? 10.331  10.434 -20.636 1.00 30.44 ? 303  PRO A N   1 
ATOM   2437 C CA  . PRO A 1 304 ? 11.228  11.513 -21.082 1.00 38.25 ? 303  PRO A CA  1 
ATOM   2438 C C   . PRO A 1 304 ? 10.902  12.874 -20.501 1.00 36.78 ? 303  PRO A C   1 
ATOM   2439 O O   . PRO A 1 304 ? 11.735  13.782 -20.604 1.00 37.48 ? 303  PRO A O   1 
ATOM   2440 C CB  . PRO A 1 304 ? 11.066  11.508 -22.611 1.00 43.99 ? 303  PRO A CB  1 
ATOM   2441 C CG  . PRO A 1 304 ? 9.855   10.716 -22.889 1.00 37.79 ? 303  PRO A CG  1 
ATOM   2442 C CD  . PRO A 1 304 ? 9.733   9.730  -21.788 1.00 36.05 ? 303  PRO A CD  1 
ATOM   2443 N N   . TYR A 1 305 ? 9.736   13.053 -19.888 1.00 25.65 ? 304  TYR A N   1 
ATOM   2444 C CA  . TYR A 1 305 ? 9.373   14.335 -19.309 1.00 29.08 ? 304  TYR A CA  1 
ATOM   2445 C C   . TYR A 1 305 ? 9.517   14.338 -17.795 1.00 29.60 ? 304  TYR A C   1 
ATOM   2446 O O   . TYR A 1 305 ? 9.046   15.275 -17.143 1.00 35.32 ? 304  TYR A O   1 
ATOM   2447 C CB  . TYR A 1 305 ? 7.944   14.713 -19.707 1.00 27.50 ? 304  TYR A CB  1 
ATOM   2448 C CG  . TYR A 1 305 ? 7.634   14.368 -21.142 1.00 25.10 ? 304  TYR A CG  1 
ATOM   2449 C CD1 . TYR A 1 305 ? 8.120   15.149 -22.185 1.00 27.01 ? 304  TYR A CD1 1 
ATOM   2450 C CD2 . TYR A 1 305 ? 6.870   13.247 -21.458 1.00 21.84 ? 304  TYR A CD2 1 
ATOM   2451 C CE1 . TYR A 1 305 ? 7.846   14.825 -23.519 1.00 21.41 ? 304  TYR A CE1 1 
ATOM   2452 C CE2 . TYR A 1 305 ? 6.603   12.906 -22.781 1.00 25.00 ? 304  TYR A CE2 1 
ATOM   2453 C CZ  . TYR A 1 305 ? 7.092   13.699 -23.803 1.00 25.51 ? 304  TYR A CZ  1 
ATOM   2454 O OH  . TYR A 1 305 ? 6.810   13.359 -25.106 1.00 24.37 ? 304  TYR A OH  1 
ATOM   2455 N N   . LEU A 1 306 ? 10.128  13.307 -17.222 1.00 25.25 ? 305  LEU A N   1 
ATOM   2456 C CA  . LEU A 1 306 ? 10.222  13.210 -15.766 1.00 33.49 ? 305  LEU A CA  1 
ATOM   2457 C C   . LEU A 1 306 ? 11.651  13.431 -15.287 1.00 43.30 ? 305  LEU A C   1 
ATOM   2458 O O   . LEU A 1 306 ? 12.584  13.531 -16.087 1.00 39.13 ? 305  LEU A O   1 
ATOM   2459 C CB  . LEU A 1 306 ? 9.714   11.853 -15.285 1.00 31.67 ? 305  LEU A CB  1 
ATOM   2460 C CG  . LEU A 1 306 ? 8.244   11.550 -15.582 1.00 37.72 ? 305  LEU A CG  1 
ATOM   2461 C CD1 . LEU A 1 306 ? 7.964   10.049 -15.472 1.00 38.73 ? 305  LEU A CD1 1 
ATOM   2462 C CD2 . LEU A 1 306 ? 7.364   12.333 -14.642 1.00 38.40 ? 305  LEU A CD2 1 
ATOM   2463 O OXT . LEU A 1 306 ? 11.904  13.507 -14.082 1.00 45.83 ? 305  LEU A OXT 1 
ATOM   2464 N N   . ALA B 1 2   ? -58.675 25.072 -26.852 1.00 44.01 ? 1    ALA B N   1 
ATOM   2465 C CA  . ALA B 1 2   ? -58.465 23.675 -26.488 1.00 51.61 ? 1    ALA B CA  1 
ATOM   2466 C C   . ALA B 1 2   ? -56.991 23.406 -26.197 1.00 39.97 ? 1    ALA B C   1 
ATOM   2467 O O   . ALA B 1 2   ? -56.653 22.838 -25.155 1.00 42.44 ? 1    ALA B O   1 
ATOM   2468 C CB  . ALA B 1 2   ? -58.965 22.758 -27.589 1.00 49.62 ? 1    ALA B CB  1 
ATOM   2469 N N   . LYS B 1 3   ? -56.115 23.794 -27.121 1.00 43.15 ? 2    LYS B N   1 
ATOM   2470 C CA  A LYS B 1 3   ? -54.684 23.651 -26.893 0.54 31.79 ? 2    LYS B CA  1 
ATOM   2471 C CA  B LYS B 1 3   ? -54.689 23.639 -26.882 0.46 31.79 ? 2    LYS B CA  1 
ATOM   2472 C C   . LYS B 1 3   ? -54.234 24.588 -25.779 1.00 24.31 ? 2    LYS B C   1 
ATOM   2473 O O   . LYS B 1 3   ? -54.760 25.692 -25.617 1.00 31.55 ? 2    LYS B O   1 
ATOM   2474 C CB  A LYS B 1 3   ? -53.899 23.948 -28.173 0.54 30.28 ? 2    LYS B CB  1 
ATOM   2475 C CB  B LYS B 1 3   ? -53.896 23.892 -28.165 0.46 30.34 ? 2    LYS B CB  1 
ATOM   2476 C CG  A LYS B 1 3   ? -54.318 23.106 -29.370 0.54 34.25 ? 2    LYS B CG  1 
ATOM   2477 C CG  B LYS B 1 3   ? -53.928 25.319 -28.670 0.46 26.70 ? 2    LYS B CG  1 
ATOM   2478 C CD  A LYS B 1 3   ? -53.144 22.402 -30.053 0.54 31.72 ? 2    LYS B CD  1 
ATOM   2479 C CD  B LYS B 1 3   ? -53.232 25.428 -30.022 0.46 35.19 ? 2    LYS B CD  1 
ATOM   2480 C CE  A LYS B 1 3   ? -53.636 21.732 -31.322 0.54 35.75 ? 2    LYS B CE  1 
ATOM   2481 C CE  B LYS B 1 3   ? -53.330 26.833 -30.568 0.46 36.51 ? 2    LYS B CE  1 
ATOM   2482 N NZ  A LYS B 1 3   ? -54.305 22.723 -32.206 0.54 23.80 ? 2    LYS B NZ  1 
ATOM   2483 N NZ  B LYS B 1 3   ? -52.965 27.825 -29.528 0.46 22.03 ? 2    LYS B NZ  1 
ATOM   2484 N N   . VAL B 1 4   ? -53.239 24.140 -25.011 1.00 23.64 ? 3    VAL B N   1 
ATOM   2485 C CA  . VAL B 1 4   ? -52.735 24.947 -23.906 1.00 23.94 ? 3    VAL B CA  1 
ATOM   2486 C C   . VAL B 1 4   ? -51.759 26.010 -24.390 1.00 27.64 ? 3    VAL B C   1 
ATOM   2487 O O   . VAL B 1 4   ? -51.775 27.146 -23.906 1.00 23.66 ? 3    VAL B O   1 
ATOM   2488 C CB  . VAL B 1 4   ? -52.093 24.032 -22.854 1.00 22.47 ? 3    VAL B CB  1 
ATOM   2489 C CG1 . VAL B 1 4   ? -51.333 24.856 -21.820 1.00 23.88 ? 3    VAL B CG1 1 
ATOM   2490 C CG2 . VAL B 1 4   ? -53.177 23.198 -22.183 1.00 25.53 ? 3    VAL B CG2 1 
ATOM   2491 N N   . PHE B 1 5   ? -50.893 25.668 -25.342 1.00 22.73 ? 4    PHE B N   1 
ATOM   2492 C CA  . PHE B 1 5   ? -49.838 26.559 -25.789 1.00 18.01 ? 4    PHE B CA  1 
ATOM   2493 C C   . PHE B 1 5   ? -50.084 27.004 -27.225 1.00 24.00 ? 4    PHE B C   1 
ATOM   2494 O O   . PHE B 1 5   ? -50.834 26.377 -27.969 1.00 23.36 ? 4    PHE B O   1 
ATOM   2495 C CB  . PHE B 1 5   ? -48.477 25.864 -25.711 1.00 19.00 ? 4    PHE B CB  1 
ATOM   2496 C CG  . PHE B 1 5   ? -48.089 25.431 -24.331 1.00 19.10 ? 4    PHE B CG  1 
ATOM   2497 C CD1 . PHE B 1 5   ? -47.555 26.340 -23.438 1.00 19.64 ? 4    PHE B CD1 1 
ATOM   2498 C CD2 . PHE B 1 5   ? -48.213 24.104 -23.951 1.00 19.57 ? 4    PHE B CD2 1 
ATOM   2499 C CE1 . PHE B 1 5   ? -47.171 25.934 -22.161 1.00 21.68 ? 4    PHE B CE1 1 
ATOM   2500 C CE2 . PHE B 1 5   ? -47.849 23.691 -22.666 1.00 23.50 ? 4    PHE B CE2 1 
ATOM   2501 C CZ  . PHE B 1 5   ? -47.319 24.609 -21.781 1.00 23.46 ? 4    PHE B CZ  1 
ATOM   2502 N N   . GLN B 1 6   ? -49.399 28.080 -27.616 1.00 20.13 ? 5    GLN B N   1 
ATOM   2503 C CA  . GLN B 1 6   ? -49.432 28.514 -29.009 1.00 20.37 ? 5    GLN B CA  1 
ATOM   2504 C C   . GLN B 1 6   ? -48.898 27.427 -29.930 1.00 25.50 ? 5    GLN B C   1 
ATOM   2505 O O   . GLN B 1 6   ? -49.469 27.162 -30.996 1.00 21.02 ? 5    GLN B O   1 
ATOM   2506 C CB  . GLN B 1 6   ? -48.617 29.801 -29.159 1.00 19.62 ? 5    GLN B CB  1 
ATOM   2507 C CG  . GLN B 1 6   ? -48.561 30.350 -30.585 1.00 20.75 ? 5    GLN B CG  1 
ATOM   2508 C CD  . GLN B 1 6   ? -47.880 31.708 -30.644 1.00 22.03 ? 5    GLN B CD  1 
ATOM   2509 O OE1 . GLN B 1 6   ? -47.411 32.226 -29.629 1.00 23.01 ? 5    GLN B OE1 1 
ATOM   2510 N NE2 . GLN B 1 6   ? -47.825 32.294 -31.835 1.00 22.82 ? 5    GLN B NE2 1 
ATOM   2511 N N   . TRP B 1 7   ? -47.810 26.774 -29.522 1.00 17.36 ? 6    TRP B N   1 
ATOM   2512 C CA  . TRP B 1 7   ? -47.111 25.792 -30.341 1.00 16.27 ? 6    TRP B CA  1 
ATOM   2513 C C   . TRP B 1 7   ? -46.791 24.574 -29.495 1.00 19.55 ? 6    TRP B C   1 
ATOM   2514 O O   . TRP B 1 7   ? -46.337 24.708 -28.357 1.00 21.33 ? 6    TRP B O   1 
ATOM   2515 C CB  . TRP B 1 7   ? -45.786 26.336 -30.889 1.00 18.26 ? 6    TRP B CB  1 
ATOM   2516 C CG  . TRP B 1 7   ? -45.927 27.370 -31.947 1.00 15.11 ? 6    TRP B CG  1 
ATOM   2517 C CD1 . TRP B 1 7   ? -46.635 27.263 -33.110 1.00 19.08 ? 6    TRP B CD1 1 
ATOM   2518 C CD2 . TRP B 1 7   ? -45.349 28.680 -31.942 1.00 17.13 ? 6    TRP B CD2 1 
ATOM   2519 N NE1 . TRP B 1 7   ? -46.510 28.424 -33.848 1.00 19.48 ? 6    TRP B NE1 1 
ATOM   2520 C CE2 . TRP B 1 7   ? -45.734 29.313 -33.149 1.00 17.56 ? 6    TRP B CE2 1 
ATOM   2521 C CE3 . TRP B 1 7   ? -44.537 29.379 -31.034 1.00 18.08 ? 6    TRP B CE3 1 
ATOM   2522 C CZ2 . TRP B 1 7   ? -45.343 30.610 -33.473 1.00 17.37 ? 6    TRP B CZ2 1 
ATOM   2523 C CZ3 . TRP B 1 7   ? -44.140 30.670 -31.357 1.00 18.30 ? 6    TRP B CZ3 1 
ATOM   2524 C CH2 . TRP B 1 7   ? -44.544 31.272 -32.570 1.00 16.77 ? 6    TRP B CH2 1 
ATOM   2525 N N   . PHE B 1 8   ? -46.972 23.391 -30.067 1.00 16.95 ? 7    PHE B N   1 
ATOM   2526 C CA  . PHE B 1 8   ? -46.535 22.171 -29.393 1.00 15.55 ? 7    PHE B CA  1 
ATOM   2527 C C   . PHE B 1 8   ? -46.287 21.123 -30.457 1.00 19.45 ? 7    PHE B C   1 
ATOM   2528 O O   . PHE B 1 8   ? -47.177 20.841 -31.265 1.00 17.94 ? 7    PHE B O   1 
ATOM   2529 C CB  . PHE B 1 8   ? -47.565 21.671 -28.380 1.00 16.72 ? 7    PHE B CB  1 
ATOM   2530 C CG  . PHE B 1 8   ? -46.949 20.836 -27.289 1.00 21.78 ? 7    PHE B CG  1 
ATOM   2531 C CD1 . PHE B 1 8   ? -46.496 19.558 -27.557 1.00 20.63 ? 7    PHE B CD1 1 
ATOM   2532 C CD2 . PHE B 1 8   ? -46.769 21.358 -26.021 1.00 26.04 ? 7    PHE B CD2 1 
ATOM   2533 C CE1 . PHE B 1 8   ? -45.899 18.790 -26.564 1.00 26.52 ? 7    PHE B CE1 1 
ATOM   2534 C CE2 . PHE B 1 8   ? -46.184 20.595 -25.013 1.00 30.23 ? 7    PHE B CE2 1 
ATOM   2535 C CZ  . PHE B 1 8   ? -45.742 19.314 -25.291 1.00 23.54 ? 7    PHE B CZ  1 
ATOM   2536 N N   . GLY B 1 9   ? -45.086 20.559 -30.474 1.00 16.01 ? 8    GLY B N   1 
ATOM   2537 C CA  . GLY B 1 9   ? -44.799 19.659 -31.578 1.00 16.25 ? 8    GLY B CA  1 
ATOM   2538 C C   . GLY B 1 9   ? -43.525 18.868 -31.397 1.00 17.58 ? 8    GLY B C   1 
ATOM   2539 O O   . GLY B 1 9   ? -43.143 18.499 -30.277 1.00 16.98 ? 8    GLY B O   1 
ATOM   2540 N N   . SER B 1 10  ? -42.849 18.600 -32.505 1.00 15.52 ? 9    SER B N   1 
ATOM   2541 C CA  . SER B 1 10  ? -41.723 17.687 -32.456 1.00 15.63 ? 9    SER B CA  1 
ATOM   2542 C C   . SER B 1 10  ? -40.669 18.099 -33.462 1.00 16.05 ? 9    SER B C   1 
ATOM   2543 O O   . SER B 1 10  ? -40.974 18.614 -34.544 1.00 18.21 ? 9    SER B O   1 
ATOM   2544 C CB  . SER B 1 10  ? -42.165 16.246 -32.727 1.00 19.40 ? 9    SER B CB  1 
ATOM   2545 O OG  . SER B 1 10  ? -41.059 15.350 -32.625 1.00 16.69 ? 9    SER B OG  1 
ATOM   2546 N N   . ASN B 1 11  ? -39.418 17.856 -33.098 1.00 15.21 ? 10   ASN B N   1 
ATOM   2547 C CA  . ASN B 1 11  ? -38.366 17.897 -34.094 1.00 16.03 ? 10   ASN B CA  1 
ATOM   2548 C C   . ASN B 1 11  ? -38.531 16.727 -35.058 1.00 17.86 ? 10   ASN B C   1 
ATOM   2549 O O   . ASN B 1 11  ? -39.050 15.664 -34.705 1.00 17.28 ? 10   ASN B O   1 
ATOM   2550 C CB  . ASN B 1 11  ? -36.994 17.856 -33.423 1.00 15.18 ? 10   ASN B CB  1 
ATOM   2551 C CG  . ASN B 1 11  ? -36.613 19.193 -32.801 1.00 16.08 ? 10   ASN B CG  1 
ATOM   2552 O OD1 . ASN B 1 11  ? -35.961 20.030 -33.439 1.00 14.91 ? 10   ASN B OD1 1 
ATOM   2553 N ND2 . ASN B 1 11  ? -37.045 19.418 -31.562 1.00 16.00 ? 10   ASN B ND2 1 
ATOM   2554 N N   . GLU B 1 12  ? -38.111 16.944 -36.299 1.00 15.20 ? 11   GLU B N   1 
ATOM   2555 C CA  . GLU B 1 12  ? -38.208 15.939 -37.360 1.00 15.50 ? 11   GLU B CA  1 
ATOM   2556 C C   . GLU B 1 12  ? -36.807 15.821 -37.941 1.00 16.22 ? 11   GLU B C   1 
ATOM   2557 O O   . GLU B 1 12  ? -36.471 16.503 -38.914 1.00 17.17 ? 11   GLU B O   1 
ATOM   2558 C CB  . GLU B 1 12  ? -39.222 16.339 -38.410 1.00 16.08 ? 11   GLU B CB  1 
ATOM   2559 C CG  . GLU B 1 12  ? -40.674 16.136 -37.971 1.00 17.88 ? 11   GLU B CG  1 
ATOM   2560 C CD  . GLU B 1 12  ? -41.099 14.675 -37.977 1.00 17.94 ? 11   GLU B CD  1 
ATOM   2561 O OE1 . GLU B 1 12  ? -40.379 13.845 -38.562 1.00 17.54 ? 11   GLU B OE1 1 
ATOM   2562 O OE2 . GLU B 1 12  ? -42.155 14.355 -37.382 1.00 17.85 ? 11   GLU B OE2 1 
ATOM   2563 N N   . SER B 1 13  ? -36.013 14.937 -37.343 1.00 15.63 ? 12   SER B N   1 
ATOM   2564 C CA  . SER B 1 13  ? -34.572 14.865 -37.504 1.00 16.05 ? 12   SER B CA  1 
ATOM   2565 C C   . SER B 1 13  ? -34.189 13.834 -38.561 1.00 20.95 ? 12   SER B C   1 
ATOM   2566 O O   . SER B 1 13  ? -34.858 12.804 -38.725 1.00 19.14 ? 12   SER B O   1 
ATOM   2567 C CB  . SER B 1 13  ? -33.934 14.527 -36.150 1.00 17.40 ? 12   SER B CB  1 
ATOM   2568 O OG  . SER B 1 13  ? -32.544 14.313 -36.260 1.00 23.89 ? 12   SER B OG  1 
ATOM   2569 N N   . GLY B 1 14  ? -33.117 14.130 -39.293 1.00 17.43 ? 13   GLY B N   1 
ATOM   2570 C CA  . GLY B 1 14  ? -32.635 13.200 -40.294 1.00 16.79 ? 13   GLY B CA  1 
ATOM   2571 C C   . GLY B 1 14  ? -31.823 13.843 -41.405 1.00 16.31 ? 13   GLY B C   1 
ATOM   2572 O O   . GLY B 1 14  ? -30.846 13.250 -41.879 1.00 18.23 ? 13   GLY B O   1 
ATOM   2573 N N   . ALA B 1 15  ? -32.227 15.041 -41.844 1.00 15.77 ? 14   ALA B N   1 
ATOM   2574 C CA  . ALA B 1 15  ? -31.508 15.664 -42.956 1.00 15.06 ? 14   ALA B CA  1 
ATOM   2575 C C   . ALA B 1 15  ? -30.126 16.120 -42.535 1.00 18.98 ? 14   ALA B C   1 
ATOM   2576 O O   . ALA B 1 15  ? -29.289 16.412 -43.393 1.00 16.82 ? 14   ALA B O   1 
ATOM   2577 C CB  . ALA B 1 15  ? -32.317 16.841 -43.522 1.00 15.16 ? 14   ALA B CB  1 
ATOM   2578 N N   . GLU B 1 16  ? -29.871 16.173 -41.229 1.00 15.55 ? 15   GLU B N   1 
ATOM   2579 C CA  . GLU B 1 16  ? -28.571 16.537 -40.688 1.00 16.71 ? 15   GLU B CA  1 
ATOM   2580 C C   . GLU B 1 16  ? -27.758 15.327 -40.248 1.00 20.06 ? 15   GLU B C   1 
ATOM   2581 O O   . GLU B 1 16  ? -26.663 15.501 -39.705 1.00 22.13 ? 15   GLU B O   1 
ATOM   2582 C CB  . GLU B 1 16  ? -28.762 17.519 -39.508 1.00 18.58 ? 15   GLU B CB  1 
ATOM   2583 C CG  . GLU B 1 16  ? -28.961 16.916 -38.104 1.00 16.02 ? 15   GLU B CG  1 
ATOM   2584 C CD  . GLU B 1 16  ? -30.324 16.265 -37.855 1.00 17.09 ? 15   GLU B CD  1 
ATOM   2585 O OE1 . GLU B 1 16  ? -31.075 15.976 -38.821 1.00 17.94 ? 15   GLU B OE1 1 
ATOM   2586 O OE2 . GLU B 1 16  ? -30.645 16.042 -36.652 1.00 19.33 ? 15   GLU B OE2 1 
ATOM   2587 N N   . PHE B 1 17  ? -28.263 14.112 -40.465 1.00 19.82 ? 16   PHE B N   1 
ATOM   2588 C CA  . PHE B 1 17  ? -27.562 12.902 -40.048 1.00 21.08 ? 16   PHE B CA  1 
ATOM   2589 C C   . PHE B 1 17  ? -26.259 12.718 -40.825 1.00 25.58 ? 16   PHE B C   1 
ATOM   2590 O O   . PHE B 1 17  ? -26.067 13.269 -41.913 1.00 22.30 ? 16   PHE B O   1 
ATOM   2591 C CB  . PHE B 1 17  ? -28.446 11.671 -40.257 1.00 20.42 ? 16   PHE B CB  1 
ATOM   2592 C CG  . PHE B 1 17  ? -29.401 11.407 -39.133 1.00 20.98 ? 16   PHE B CG  1 
ATOM   2593 C CD1 . PHE B 1 17  ? -29.711 12.401 -38.226 1.00 21.09 ? 16   PHE B CD1 1 
ATOM   2594 C CD2 . PHE B 1 17  ? -29.949 10.146 -38.960 1.00 18.99 ? 16   PHE B CD2 1 
ATOM   2595 C CE1 . PHE B 1 17  ? -30.573 12.156 -37.175 1.00 21.37 ? 16   PHE B CE1 1 
ATOM   2596 C CE2 . PHE B 1 17  ? -30.808 9.875  -37.904 1.00 24.47 ? 16   PHE B CE2 1 
ATOM   2597 C CZ  . PHE B 1 17  ? -31.129 10.884 -37.008 1.00 19.01 ? 16   PHE B CZ  1 
ATOM   2598 N N   . GLY B 1 18  ? -25.369 11.910 -40.255 1.00 23.51 ? 17   GLY B N   1 
ATOM   2599 C CA  . GLY B 1 18  ? -24.128 11.580 -40.953 1.00 25.25 ? 17   GLY B CA  1 
ATOM   2600 C C   . GLY B 1 18  ? -23.345 12.794 -41.386 1.00 25.82 ? 17   GLY B C   1 
ATOM   2601 O O   . GLY B 1 18  ? -22.822 12.835 -42.507 1.00 27.73 ? 17   GLY B O   1 
ATOM   2602 N N   . SER B 1 19  ? -23.257 13.799 -40.512 1.00 27.91 ? 18   SER B N   1 
ATOM   2603 C CA  . SER B 1 19  ? -22.693 15.101 -40.846 1.00 28.24 ? 18   SER B CA  1 
ATOM   2604 C C   . SER B 1 19  ? -21.186 15.074 -41.056 1.00 29.81 ? 18   SER B C   1 
ATOM   2605 O O   . SER B 1 19  ? -20.620 16.092 -41.466 1.00 32.40 ? 18   SER B O   1 
ATOM   2606 C CB  . SER B 1 19  ? -23.035 16.115 -39.751 1.00 28.57 ? 18   SER B CB  1 
ATOM   2607 O OG  . SER B 1 19  ? -22.669 15.656 -38.473 1.00 42.92 ? 18   SER B OG  1 
ATOM   2608 N N   . GLN B 1 20  ? -20.518 13.958 -40.768 1.00 30.55 ? 19   GLN B N   1 
ATOM   2609 C CA  . GLN B 1 20  ? -19.105 13.867 -41.104 1.00 31.95 ? 19   GLN B CA  1 
ATOM   2610 C C   . GLN B 1 20  ? -18.886 13.700 -42.600 1.00 35.59 ? 19   GLN B C   1 
ATOM   2611 O O   . GLN B 1 20  ? -17.751 13.840 -43.066 1.00 31.10 ? 19   GLN B O   1 
ATOM   2612 C CB  . GLN B 1 20  ? -18.453 12.711 -40.335 1.00 34.27 ? 19   GLN B CB  1 
ATOM   2613 C CG  . GLN B 1 20  ? -18.702 11.334 -40.933 1.00 46.71 ? 19   GLN B CG  1 
ATOM   2614 C CD  . GLN B 1 20  ? -20.055 10.751 -40.566 1.00 43.18 ? 19   GLN B CD  1 
ATOM   2615 O OE1 . GLN B 1 20  ? -20.869 11.393 -39.902 1.00 41.21 ? 19   GLN B OE1 1 
ATOM   2616 N NE2 . GLN B 1 20  ? -20.298 9.518  -40.997 1.00 49.14 ? 19   GLN B NE2 1 
ATOM   2617 N N   . ASN B 1 21  ? -19.940 13.425 -43.361 1.00 27.07 ? 20   ASN B N   1 
ATOM   2618 C CA  . ASN B 1 21  ? -19.857 13.289 -44.811 1.00 25.92 ? 20   ASN B CA  1 
ATOM   2619 C C   . ASN B 1 21  ? -20.564 14.479 -45.441 1.00 28.80 ? 20   ASN B C   1 
ATOM   2620 O O   . ASN B 1 21  ? -21.795 14.553 -45.444 1.00 24.16 ? 20   ASN B O   1 
ATOM   2621 C CB  . ASN B 1 21  ? -20.455 11.964 -45.262 1.00 31.84 ? 20   ASN B CB  1 
ATOM   2622 C CG  . ASN B 1 21  ? -19.543 10.792 -44.949 1.00 41.32 ? 20   ASN B CG  1 
ATOM   2623 O OD1 . ASN B 1 21  ? -19.995 9.662  -44.779 1.00 43.35 ? 20   ASN B OD1 1 
ATOM   2624 N ND2 . ASN B 1 21  ? -18.247 11.067 -44.852 1.00 44.59 ? 20   ASN B ND2 1 
ATOM   2625 N N   . LEU B 1 22  ? -19.781 15.419 -45.953 1.00 24.71 ? 21   LEU B N   1 
ATOM   2626 C CA  . LEU B 1 22  ? -20.314 16.559 -46.671 1.00 25.56 ? 21   LEU B CA  1 
ATOM   2627 C C   . LEU B 1 22  ? -19.787 16.524 -48.096 1.00 36.54 ? 21   LEU B C   1 
ATOM   2628 O O   . LEU B 1 22  ? -18.573 16.367 -48.292 1.00 34.30 ? 21   LEU B O   1 
ATOM   2629 C CB  . LEU B 1 22  ? -19.920 17.877 -46.003 1.00 25.24 ? 21   LEU B CB  1 
ATOM   2630 C CG  . LEU B 1 22  ? -20.472 18.084 -44.593 1.00 21.06 ? 21   LEU B CG  1 
ATOM   2631 C CD1 . LEU B 1 22  ? -19.942 19.371 -43.954 1.00 24.49 ? 21   LEU B CD1 1 
ATOM   2632 C CD2 . LEU B 1 22  ? -22.006 18.107 -44.665 1.00 25.33 ? 21   LEU B CD2 1 
ATOM   2633 N N   . PRO B 1 23  ? -20.654 16.660 -49.118 1.00 25.01 ? 22   PRO B N   1 
ATOM   2634 C CA  . PRO B 1 23  ? -22.106 16.863 -49.032 1.00 24.81 ? 22   PRO B CA  1 
ATOM   2635 C C   . PRO B 1 23  ? -22.845 15.631 -48.534 1.00 20.59 ? 22   PRO B C   1 
ATOM   2636 O O   . PRO B 1 23  ? -23.952 15.753 -48.020 1.00 19.83 ? 22   PRO B O   1 
ATOM   2637 C CB  . PRO B 1 23  ? -22.494 17.200 -50.483 1.00 24.99 ? 22   PRO B CB  1 
ATOM   2638 C CG  . PRO B 1 23  ? -21.450 16.537 -51.311 1.00 27.98 ? 22   PRO B CG  1 
ATOM   2639 C CD  . PRO B 1 23  ? -20.186 16.671 -50.520 1.00 25.77 ? 22   PRO B CD  1 
ATOM   2640 N N   . GLY B 1 24  ? -22.270 14.440 -48.684 1.00 21.60 ? 23   GLY B N   1 
ATOM   2641 C CA  . GLY B 1 24  ? -22.977 13.216 -48.361 1.00 23.97 ? 23   GLY B CA  1 
ATOM   2642 C C   . GLY B 1 24  ? -24.050 12.920 -49.394 1.00 23.55 ? 23   GLY B C   1 
ATOM   2643 O O   . GLY B 1 24  ? -24.277 13.675 -50.341 1.00 25.56 ? 23   GLY B O   1 
ATOM   2644 N N   . VAL B 1 25  ? -24.725 11.790 -49.197 1.00 22.93 ? 24   VAL B N   1 
ATOM   2645 C CA  . VAL B 1 25  ? -25.651 11.265 -50.190 1.00 24.11 ? 24   VAL B CA  1 
ATOM   2646 C C   . VAL B 1 25  ? -26.997 10.990 -49.530 1.00 25.05 ? 24   VAL B C   1 
ATOM   2647 O O   . VAL B 1 25  ? -27.069 10.261 -48.530 1.00 24.67 ? 24   VAL B O   1 
ATOM   2648 C CB  . VAL B 1 25  ? -25.090 9.999  -50.860 1.00 27.96 ? 24   VAL B CB  1 
ATOM   2649 C CG1 . VAL B 1 25  ? -26.084 9.432  -51.858 1.00 30.57 ? 24   VAL B CG1 1 
ATOM   2650 C CG2 . VAL B 1 25  ? -23.774 10.331 -51.540 1.00 32.94 ? 24   VAL B CG2 1 
ATOM   2651 N N   . GLU B 1 26  ? -28.058 11.587 -50.077 1.00 24.17 ? 25   GLU B N   1 
ATOM   2652 C CA  . GLU B 1 26  ? -29.401 11.299 -49.591 1.00 25.49 ? 25   GLU B CA  1 
ATOM   2653 C C   . GLU B 1 26  ? -29.701 9.808  -49.713 1.00 24.03 ? 25   GLU B C   1 
ATOM   2654 O O   . GLU B 1 26  ? -29.343 9.157  -50.702 1.00 26.64 ? 25   GLU B O   1 
ATOM   2655 C CB  . GLU B 1 26  ? -30.440 12.119 -50.360 1.00 23.08 ? 25   GLU B CB  1 
ATOM   2656 C CG  . GLU B 1 26  ? -31.852 12.062 -49.773 1.00 23.26 ? 25   GLU B CG  1 
ATOM   2657 C CD  . GLU B 1 26  ? -32.607 10.799 -50.184 1.00 25.13 ? 25   GLU B CD  1 
ATOM   2658 O OE1 . GLU B 1 26  ? -32.394 10.319 -51.321 1.00 29.90 ? 25   GLU B OE1 1 
ATOM   2659 O OE2 . GLU B 1 26  ? -33.386 10.275 -49.357 1.00 29.94 ? 25   GLU B OE2 1 
ATOM   2660 N N   . GLY B 1 27  ? -30.363 9.268  -48.690 1.00 24.20 ? 26   GLY B N   1 
ATOM   2661 C CA  . GLY B 1 27  ? -30.664 7.854  -48.625 1.00 23.25 ? 26   GLY B CA  1 
ATOM   2662 C C   . GLY B 1 27  ? -29.532 6.996  -48.112 1.00 26.31 ? 26   GLY B C   1 
ATOM   2663 O O   . GLY B 1 27  ? -29.746 5.798  -47.860 1.00 30.66 ? 26   GLY B O   1 
ATOM   2664 N N   . LYS B 1 28  ? -28.329 7.557  -47.988 1.00 24.41 ? 27   LYS B N   1 
ATOM   2665 C CA  A LYS B 1 28  ? -27.180 6.846  -47.436 0.48 29.00 ? 27   LYS B CA  1 
ATOM   2666 C CA  B LYS B 1 28  ? -27.184 6.843  -47.431 0.32 29.01 ? 27   LYS B CA  1 
ATOM   2667 C CA  C LYS B 1 28  ? -27.185 6.845  -47.431 0.20 29.02 ? 27   LYS B CA  1 
ATOM   2668 C C   . LYS B 1 28  ? -26.695 7.502  -46.149 1.00 26.31 ? 27   LYS B C   1 
ATOM   2669 O O   . LYS B 1 28  ? -26.706 6.864  -45.091 1.00 29.01 ? 27   LYS B O   1 
ATOM   2670 C CB  A LYS B 1 28  ? -26.061 6.783  -48.491 0.48 32.86 ? 27   LYS B CB  1 
ATOM   2671 C CB  B LYS B 1 28  ? -26.052 6.755  -48.468 0.32 32.84 ? 27   LYS B CB  1 
ATOM   2672 C CB  C LYS B 1 28  ? -26.058 6.764  -48.470 0.20 32.81 ? 27   LYS B CB  1 
ATOM   2673 C CG  A LYS B 1 28  ? -24.716 6.239  -48.007 0.48 34.21 ? 27   LYS B CG  1 
ATOM   2674 C CG  B LYS B 1 28  ? -24.794 6.043  -47.968 0.32 34.37 ? 27   LYS B CG  1 
ATOM   2675 C CG  C LYS B 1 28  ? -24.855 5.957  -48.016 0.20 34.36 ? 27   LYS B CG  1 
ATOM   2676 C CD  A LYS B 1 28  ? -24.644 4.711  -48.056 0.48 39.14 ? 27   LYS B CD  1 
ATOM   2677 C CD  B LYS B 1 28  ? -23.811 5.741  -49.103 0.32 33.18 ? 27   LYS B CD  1 
ATOM   2678 C CD  C LYS B 1 28  ? -23.791 5.892  -49.099 0.20 33.23 ? 27   LYS B CD  1 
ATOM   2679 C CE  A LYS B 1 28  ? -24.786 4.143  -49.467 0.48 28.36 ? 27   LYS B CE  1 
ATOM   2680 C CE  B LYS B 1 28  ? -23.153 7.009  -49.635 0.32 32.33 ? 27   LYS B CE  1 
ATOM   2681 C CE  C LYS B 1 28  ? -22.680 4.933  -48.712 0.20 32.26 ? 27   LYS B CE  1 
ATOM   2682 N NZ  A LYS B 1 28  ? -24.749 2.641  -49.465 0.48 37.97 ? 27   LYS B NZ  1 
ATOM   2683 N NZ  B LYS B 1 28  ? -22.243 6.751  -50.788 0.32 30.33 ? 27   LYS B NZ  1 
ATOM   2684 N NZ  C LYS B 1 28  ? -22.102 5.270  -47.383 0.20 33.65 ? 27   LYS B NZ  1 
ATOM   2685 N N   . ASP B 1 29  ? -26.289 8.772  -46.204 1.00 23.26 ? 28   ASP B N   1 
ATOM   2686 C CA  . ASP B 1 29  ? -25.846 9.485  -45.015 1.00 20.33 ? 28   ASP B CA  1 
ATOM   2687 C C   . ASP B 1 29  ? -26.980 10.188 -44.282 1.00 22.15 ? 28   ASP B C   1 
ATOM   2688 O O   . ASP B 1 29  ? -26.890 10.383 -43.064 1.00 24.66 ? 28   ASP B O   1 
ATOM   2689 C CB  . ASP B 1 29  ? -24.790 10.522 -45.396 1.00 24.89 ? 28   ASP B CB  1 
ATOM   2690 C CG  . ASP B 1 29  ? -23.594 9.900  -46.086 1.00 30.71 ? 28   ASP B CG  1 
ATOM   2691 O OD1 . ASP B 1 29  ? -22.869 9.132  -45.414 1.00 33.59 ? 28   ASP B OD1 1 
ATOM   2692 O OD2 . ASP B 1 29  ? -23.401 10.158 -47.298 1.00 27.54 ? 28   ASP B OD2 1 
ATOM   2693 N N   . TYR B 1 30  ? -28.027 10.603 -44.990 1.00 20.04 ? 29   TYR B N   1 
ATOM   2694 C CA  . TYR B 1 30  ? -29.091 11.384 -44.375 1.00 19.77 ? 29   TYR B CA  1 
ATOM   2695 C C   . TYR B 1 30  ? -30.400 11.074 -45.085 1.00 21.58 ? 29   TYR B C   1 
ATOM   2696 O O   . TYR B 1 30  ? -30.424 10.466 -46.157 1.00 22.55 ? 29   TYR B O   1 
ATOM   2697 C CB  . TYR B 1 30  ? -28.763 12.889 -44.410 1.00 17.77 ? 29   TYR B CB  1 
ATOM   2698 C CG  . TYR B 1 30  ? -28.617 13.470 -45.807 1.00 20.02 ? 29   TYR B CG  1 
ATOM   2699 C CD1 . TYR B 1 30  ? -29.731 13.924 -46.514 1.00 19.33 ? 29   TYR B CD1 1 
ATOM   2700 C CD2 . TYR B 1 30  ? -27.370 13.564 -46.420 1.00 18.17 ? 29   TYR B CD2 1 
ATOM   2701 C CE1 . TYR B 1 30  ? -29.610 14.463 -47.809 1.00 17.41 ? 29   TYR B CE1 1 
ATOM   2702 C CE2 . TYR B 1 30  ? -27.240 14.117 -47.719 1.00 18.93 ? 29   TYR B CE2 1 
ATOM   2703 C CZ  . TYR B 1 30  ? -28.366 14.559 -48.388 1.00 16.98 ? 29   TYR B CZ  1 
ATOM   2704 O OH  . TYR B 1 30  ? -28.235 15.088 -49.659 1.00 18.84 ? 29   TYR B OH  1 
ATOM   2705 N N   . ILE B 1 31  ? -31.501 11.499 -44.467 1.00 18.75 ? 30   ILE B N   1 
ATOM   2706 C CA  . ILE B 1 31  ? -32.835 11.267 -45.011 1.00 16.60 ? 30   ILE B CA  1 
ATOM   2707 C C   . ILE B 1 31  ? -33.749 12.382 -44.518 1.00 17.18 ? 30   ILE B C   1 
ATOM   2708 O O   . ILE B 1 31  ? -33.552 12.931 -43.431 1.00 19.07 ? 30   ILE B O   1 
ATOM   2709 C CB  . ILE B 1 31  ? -33.378 9.877  -44.601 1.00 21.61 ? 30   ILE B CB  1 
ATOM   2710 C CG1 . ILE B 1 31  ? -34.588 9.504  -45.478 1.00 24.89 ? 30   ILE B CG1 1 
ATOM   2711 C CG2 . ILE B 1 31  ? -33.700 9.857  -43.097 1.00 23.81 ? 30   ILE B CG2 1 
ATOM   2712 C CD1 . ILE B 1 31  ? -35.071 8.081  -45.273 1.00 35.73 ? 30   ILE B CD1 1 
ATOM   2713 N N   . TRP B 1 32  ? -34.757 12.722 -45.331 1.00 20.01 ? 31   TRP B N   1 
ATOM   2714 C CA  . TRP B 1 32  ? -35.682 13.777 -44.940 1.00 17.42 ? 31   TRP B CA  1 
ATOM   2715 C C   . TRP B 1 32  ? -36.884 13.176 -44.223 1.00 19.90 ? 31   TRP B C   1 
ATOM   2716 O O   . TRP B 1 32  ? -37.142 11.972 -44.326 1.00 19.34 ? 31   TRP B O   1 
ATOM   2717 C CB  . TRP B 1 32  ? -36.108 14.579 -46.181 1.00 19.29 ? 31   TRP B CB  1 
ATOM   2718 C CG  . TRP B 1 32  ? -34.988 15.458 -46.669 1.00 14.80 ? 31   TRP B CG  1 
ATOM   2719 C CD1 . TRP B 1 32  ? -34.008 15.122 -47.577 1.00 18.32 ? 31   TRP B CD1 1 
ATOM   2720 C CD2 . TRP B 1 32  ? -34.695 16.792 -46.235 1.00 19.14 ? 31   TRP B CD2 1 
ATOM   2721 N NE1 . TRP B 1 32  ? -33.135 16.169 -47.732 1.00 18.44 ? 31   TRP B NE1 1 
ATOM   2722 C CE2 . TRP B 1 32  ? -33.536 17.210 -46.926 1.00 16.81 ? 31   TRP B CE2 1 
ATOM   2723 C CE3 . TRP B 1 32  ? -35.300 17.676 -45.322 1.00 16.45 ? 31   TRP B CE3 1 
ATOM   2724 C CZ2 . TRP B 1 32  ? -32.977 18.476 -46.746 1.00 16.16 ? 31   TRP B CZ2 1 
ATOM   2725 C CZ3 . TRP B 1 32  ? -34.731 18.939 -45.135 1.00 15.62 ? 31   TRP B CZ3 1 
ATOM   2726 C CH2 . TRP B 1 32  ? -33.594 19.327 -45.858 1.00 13.24 ? 31   TRP B CH2 1 
ATOM   2727 N N   . PRO B 1 33  ? -37.621 13.984 -43.456 1.00 17.62 ? 32   PRO B N   1 
ATOM   2728 C CA  . PRO B 1 33  ? -38.755 13.450 -42.683 1.00 18.13 ? 32   PRO B CA  1 
ATOM   2729 C C   . PRO B 1 33  ? -39.822 12.824 -43.572 1.00 18.26 ? 32   PRO B C   1 
ATOM   2730 O O   . PRO B 1 33  ? -39.957 13.148 -44.755 1.00 21.24 ? 32   PRO B O   1 
ATOM   2731 C CB  . PRO B 1 33  ? -39.306 14.686 -41.967 1.00 18.59 ? 32   PRO B CB  1 
ATOM   2732 C CG  . PRO B 1 33  ? -38.090 15.578 -41.790 1.00 15.05 ? 32   PRO B CG  1 
ATOM   2733 C CD  . PRO B 1 33  ? -37.322 15.387 -43.103 1.00 16.98 ? 32   PRO B CD  1 
ATOM   2734 N N   . ASP B 1 34  ? -40.609 11.933 -42.965 1.00 18.88 ? 33   ASP B N   1 
ATOM   2735 C CA  . ASP B 1 34  ? -41.688 11.231 -43.661 1.00 19.34 ? 33   ASP B CA  1 
ATOM   2736 C C   . ASP B 1 34  ? -42.970 12.043 -43.525 1.00 26.25 ? 33   ASP B C   1 
ATOM   2737 O O   . ASP B 1 34  ? -43.494 12.163 -42.411 1.00 19.33 ? 33   ASP B O   1 
ATOM   2738 C CB  . ASP B 1 34  ? -41.867 9.843  -43.051 1.00 22.12 ? 33   ASP B CB  1 
ATOM   2739 C CG  . ASP B 1 34  ? -42.894 8.995  -43.777 1.00 21.68 ? 33   ASP B CG  1 
ATOM   2740 O OD1 . ASP B 1 34  ? -43.711 9.541  -44.548 1.00 26.06 ? 33   ASP B OD1 1 
ATOM   2741 O OD2 . ASP B 1 34  ? -42.884 7.764  -43.551 1.00 23.57 ? 33   ASP B OD2 1 
ATOM   2742 N N   . PRO B 1 35  ? -43.528 12.589 -44.603 1.00 21.76 ? 34   PRO B N   1 
ATOM   2743 C CA  . PRO B 1 35  ? -44.747 13.398 -44.442 1.00 21.62 ? 34   PRO B CA  1 
ATOM   2744 C C   . PRO B 1 35  ? -45.912 12.607 -43.875 1.00 22.48 ? 34   PRO B C   1 
ATOM   2745 O O   . PRO B 1 35  ? -46.808 13.197 -43.257 1.00 22.33 ? 34   PRO B O   1 
ATOM   2746 C CB  . PRO B 1 35  ? -45.032 13.892 -45.870 1.00 23.49 ? 34   PRO B CB  1 
ATOM   2747 C CG  . PRO B 1 35  ? -44.351 12.899 -46.751 1.00 24.60 ? 34   PRO B CG  1 
ATOM   2748 C CD  . PRO B 1 35  ? -43.110 12.483 -46.010 1.00 20.03 ? 34   PRO B CD  1 
ATOM   2749 N N   . ASN B 1 36  ? -45.927 11.288 -44.069 1.00 22.53 ? 35   ASN B N   1 
ATOM   2750 C CA  . ASN B 1 36  ? -47.064 10.494 -43.613 1.00 23.01 ? 35   ASN B CA  1 
ATOM   2751 C C   . ASN B 1 36  ? -47.060 10.347 -42.101 1.00 26.37 ? 35   ASN B C   1 
ATOM   2752 O O   . ASN B 1 36  ? -48.126 10.375 -41.470 1.00 23.79 ? 35   ASN B O   1 
ATOM   2753 C CB  . ASN B 1 36  ? -47.060 9.124  -44.289 1.00 30.87 ? 35   ASN B CB  1 
ATOM   2754 C CG  . ASN B 1 36  ? -47.280 9.221  -45.787 1.00 37.16 ? 35   ASN B CG  1 
ATOM   2755 O OD1 . ASN B 1 36  ? -48.051 10.062 -46.257 1.00 43.59 ? 35   ASN B OD1 1 
ATOM   2756 N ND2 . ASN B 1 36  ? -46.596 8.373  -46.546 1.00 52.70 ? 35   ASN B ND2 1 
ATOM   2757 N N   . THR B 1 37  ? -45.874 10.189 -41.496 1.00 21.52 ? 36   THR B N   1 
ATOM   2758 C CA  . THR B 1 37  ? -45.822 10.122 -40.037 1.00 19.85 ? 36   THR B CA  1 
ATOM   2759 C C   . THR B 1 37  ? -45.973 11.497 -39.403 1.00 23.98 ? 36   THR B C   1 
ATOM   2760 O O   . THR B 1 37  ? -46.508 11.604 -38.292 1.00 20.69 ? 36   THR B O   1 
ATOM   2761 C CB  . THR B 1 37  ? -44.528 9.453  -39.550 1.00 21.38 ? 36   THR B CB  1 
ATOM   2762 O OG1 . THR B 1 37  ? -43.385 10.240 -39.920 1.00 20.45 ? 36   THR B OG1 1 
ATOM   2763 C CG2 . THR B 1 37  ? -44.385 8.044  -40.140 1.00 22.98 ? 36   THR B CG2 1 
ATOM   2764 N N   . ILE B 1 38  ? -45.531 12.559 -40.083 1.00 21.96 ? 37   ILE B N   1 
ATOM   2765 C CA  . ILE B 1 38  ? -45.881 13.896 -39.622 1.00 19.30 ? 37   ILE B CA  1 
ATOM   2766 C C   . ILE B 1 38  ? -47.397 14.064 -39.603 1.00 23.98 ? 37   ILE B C   1 
ATOM   2767 O O   . ILE B 1 38  ? -47.953 14.634 -38.659 1.00 22.75 ? 37   ILE B O   1 
ATOM   2768 C CB  . ILE B 1 38  ? -45.204 14.969 -40.493 1.00 20.20 ? 37   ILE B CB  1 
ATOM   2769 C CG1 . ILE B 1 38  ? -43.705 15.027 -40.195 1.00 21.63 ? 37   ILE B CG1 1 
ATOM   2770 C CG2 . ILE B 1 38  ? -45.837 16.354 -40.239 1.00 20.37 ? 37   ILE B CG2 1 
ATOM   2771 C CD1 . ILE B 1 38  ? -42.930 15.920 -41.183 1.00 22.18 ? 37   ILE B CD1 1 
ATOM   2772 N N   . ASP B 1 39  ? -48.088 13.575 -40.645 1.00 21.63 ? 38   ASP B N   1 
ATOM   2773 C CA  . ASP B 1 39  ? -49.553 13.628 -40.663 1.00 19.68 ? 38   ASP B CA  1 
ATOM   2774 C C   . ASP B 1 39  ? -50.149 12.979 -39.420 1.00 25.10 ? 38   ASP B C   1 
ATOM   2775 O O   . ASP B 1 39  ? -51.118 13.487 -38.840 1.00 23.77 ? 38   ASP B O   1 
ATOM   2776 C CB  . ASP B 1 39  ? -50.096 12.938 -41.914 1.00 23.50 ? 38   ASP B CB  1 
ATOM   2777 C CG  . ASP B 1 39  ? -49.973 13.789 -43.161 1.00 38.78 ? 38   ASP B CG  1 
ATOM   2778 O OD1 . ASP B 1 39  ? -49.573 14.974 -43.068 1.00 40.70 ? 38   ASP B OD1 1 
ATOM   2779 O OD2 . ASP B 1 39  ? -50.279 13.258 -44.246 1.00 40.85 ? 38   ASP B OD2 1 
ATOM   2780 N N   . THR B 1 40  ? -49.583 11.848 -39.000 1.00 20.88 ? 39   THR B N   1 
ATOM   2781 C CA  . THR B 1 40  ? -50.062 11.182 -37.797 1.00 19.43 ? 39   THR B CA  1 
ATOM   2782 C C   . THR B 1 40  ? -49.876 12.061 -36.563 1.00 25.75 ? 39   THR B C   1 
ATOM   2783 O O   . THR B 1 40  ? -50.796 12.195 -35.745 1.00 21.88 ? 39   THR B O   1 
ATOM   2784 C CB  . THR B 1 40  ? -49.342 9.844  -37.641 1.00 20.36 ? 39   THR B CB  1 
ATOM   2785 O OG1 . THR B 1 40  ? -49.707 8.981  -38.726 1.00 23.64 ? 39   THR B OG1 1 
ATOM   2786 C CG2 . THR B 1 40  ? -49.725 9.170  -36.333 1.00 25.29 ? 39   THR B CG2 1 
ATOM   2787 N N   . LEU B 1 41  ? -48.710 12.704 -36.429 1.00 20.43 ? 40   LEU B N   1 
ATOM   2788 C CA  . LEU B 1 41  ? -48.503 13.591 -35.284 1.00 17.45 ? 40   LEU B CA  1 
ATOM   2789 C C   . LEU B 1 41  ? -49.442 14.794 -35.325 1.00 21.94 ? 40   LEU B C   1 
ATOM   2790 O O   . LEU B 1 41  ? -49.854 15.301 -34.273 1.00 20.77 ? 40   LEU B O   1 
ATOM   2791 C CB  . LEU B 1 41  ? -47.037 14.047 -35.234 1.00 19.63 ? 40   LEU B CB  1 
ATOM   2792 C CG  . LEU B 1 41  ? -46.044 12.929 -34.909 1.00 17.32 ? 40   LEU B CG  1 
ATOM   2793 C CD1 . LEU B 1 41  ? -44.594 13.445 -34.894 1.00 18.78 ? 40   LEU B CD1 1 
ATOM   2794 C CD2 . LEU B 1 41  ? -46.389 12.301 -33.552 1.00 17.39 ? 40   LEU B CD2 1 
ATOM   2795 N N   . ILE B 1 42  ? -49.802 15.260 -36.523 1.00 19.75 ? 41   ILE B N   1 
ATOM   2796 C CA  . ILE B 1 42  ? -50.762 16.358 -36.614 1.00 19.84 ? 41   ILE B CA  1 
ATOM   2797 C C   . ILE B 1 42  ? -52.140 15.897 -36.160 1.00 21.01 ? 41   ILE B C   1 
ATOM   2798 O O   . ILE B 1 42  ? -52.872 16.643 -35.498 1.00 23.42 ? 41   ILE B O   1 
ATOM   2799 C CB  . ILE B 1 42  ? -50.780 16.929 -38.045 1.00 19.76 ? 41   ILE B CB  1 
ATOM   2800 C CG1 . ILE B 1 42  ? -49.463 17.660 -38.309 1.00 18.15 ? 41   ILE B CG1 1 
ATOM   2801 C CG2 . ILE B 1 42  ? -51.973 17.866 -38.227 1.00 20.07 ? 41   ILE B CG2 1 
ATOM   2802 C CD1 . ILE B 1 42  ? -49.266 18.016 -39.784 1.00 23.35 ? 41   ILE B CD1 1 
ATOM   2803 N N   . SER B 1 43  ? -52.518 14.663 -36.497 1.00 23.18 ? 42   SER B N   1 
ATOM   2804 C CA  A SER B 1 43  ? -53.805 14.151 -36.046 0.73 21.22 ? 42   SER B CA  1 
ATOM   2805 C CA  B SER B 1 43  ? -53.800 14.135 -36.047 0.27 21.28 ? 42   SER B CA  1 
ATOM   2806 C C   . SER B 1 43  ? -53.855 14.010 -34.531 1.00 24.74 ? 42   SER B C   1 
ATOM   2807 O O   . SER B 1 43  ? -54.946 14.040 -33.952 1.00 25.95 ? 42   SER B O   1 
ATOM   2808 C CB  A SER B 1 43  ? -54.105 12.811 -36.721 0.73 22.15 ? 42   SER B CB  1 
ATOM   2809 C CB  B SER B 1 43  ? -54.065 12.780 -36.696 0.27 22.23 ? 42   SER B CB  1 
ATOM   2810 O OG  A SER B 1 43  ? -53.491 11.718 -36.048 0.73 23.79 ? 42   SER B OG  1 
ATOM   2811 O OG  B SER B 1 43  ? -54.146 12.906 -38.100 0.27 22.54 ? 42   SER B OG  1 
ATOM   2812 N N   . LYS B 1 44  ? -52.699 13.868 -33.880 1.00 22.53 ? 43   LYS B N   1 
ATOM   2813 C CA  . LYS B 1 44  ? -52.645 13.838 -32.420 1.00 24.10 ? 43   LYS B CA  1 
ATOM   2814 C C   . LYS B 1 44  ? -52.712 15.224 -31.795 1.00 32.23 ? 43   LYS B C   1 
ATOM   2815 O O   . LYS B 1 44  ? -52.832 15.329 -30.567 1.00 26.32 ? 43   LYS B O   1 
ATOM   2816 C CB  . LYS B 1 44  ? -51.374 13.133 -31.948 1.00 23.67 ? 43   LYS B CB  1 
ATOM   2817 C CG  . LYS B 1 44  ? -51.294 11.685 -32.385 1.00 28.09 ? 43   LYS B CG  1 
ATOM   2818 C CD  . LYS B 1 44  ? -52.500 10.910 -31.856 1.00 37.51 ? 43   LYS B CD  1 
ATOM   2819 C CE  . LYS B 1 44  ? -52.207 9.428  -31.786 1.00 44.86 ? 43   LYS B CE  1 
ATOM   2820 N NZ  . LYS B 1 44  ? -53.059 8.740  -30.764 1.00 46.87 ? 43   LYS B NZ  1 
ATOM   2821 N N   . GLY B 1 45  ? -52.653 16.282 -32.600 1.00 22.68 ? 44   GLY B N   1 
ATOM   2822 C CA  . GLY B 1 45  ? -52.756 17.639 -32.106 1.00 23.30 ? 44   GLY B CA  1 
ATOM   2823 C C   . GLY B 1 45  ? -51.469 18.445 -32.150 1.00 26.58 ? 44   GLY B C   1 
ATOM   2824 O O   . GLY B 1 45  ? -51.472 19.590 -31.692 1.00 24.07 ? 44   GLY B O   1 
ATOM   2825 N N   . MET B 1 46  ? -50.375 17.913 -32.690 1.00 19.55 ? 45   MET B N   1 
ATOM   2826 C CA  . MET B 1 46  ? -49.154 18.704 -32.759 1.00 19.22 ? 45   MET B CA  1 
ATOM   2827 C C   . MET B 1 46  ? -49.262 19.680 -33.921 1.00 22.12 ? 45   MET B C   1 
ATOM   2828 O O   . MET B 1 46  ? -49.836 19.351 -34.958 1.00 21.23 ? 45   MET B O   1 
ATOM   2829 C CB  . MET B 1 46  ? -47.929 17.804 -32.922 1.00 16.21 ? 45   MET B CB  1 
ATOM   2830 C CG  . MET B 1 46  ? -47.631 17.005 -31.651 1.00 18.22 ? 45   MET B CG  1 
ATOM   2831 S SD  . MET B 1 46  ? -46.110 16.078 -31.892 1.00 20.71 ? 45   MET B SD  1 
ATOM   2832 C CE  . MET B 1 46  ? -45.767 15.526 -30.220 1.00 25.60 ? 45   MET B CE  1 
ATOM   2833 N N   . ASN B 1 47  ? -48.730 20.896 -33.738 1.00 18.65 ? 46   ASN B N   1 
ATOM   2834 C CA  . ASN B 1 47  ? -48.909 21.937 -34.747 1.00 18.44 ? 46   ASN B CA  1 
ATOM   2835 C C   . ASN B 1 47  ? -47.610 22.637 -35.116 1.00 17.27 ? 46   ASN B C   1 
ATOM   2836 O O   . ASN B 1 47  ? -47.652 23.712 -35.726 1.00 18.57 ? 46   ASN B O   1 
ATOM   2837 C CB  . ASN B 1 47  ? -49.946 22.974 -34.283 1.00 22.65 ? 46   ASN B CB  1 
ATOM   2838 C CG  . ASN B 1 47  ? -49.444 23.826 -33.140 1.00 23.69 ? 46   ASN B CG  1 
ATOM   2839 O OD1 . ASN B 1 47  ? -48.474 23.474 -32.480 1.00 24.12 ? 46   ASN B OD1 1 
ATOM   2840 N ND2 . ASN B 1 47  ? -50.075 24.975 -32.929 1.00 26.08 ? 46   ASN B ND2 1 
ATOM   2841 N N   . ILE B 1 48  ? -46.460 22.085 -34.747 1.00 15.52 ? 47   ILE B N   1 
ATOM   2842 C CA  . ILE B 1 48  ? -45.183 22.682 -35.142 1.00 17.14 ? 47   ILE B CA  1 
ATOM   2843 C C   . ILE B 1 48  ? -44.167 21.560 -35.309 1.00 15.42 ? 47   ILE B C   1 
ATOM   2844 O O   . ILE B 1 48  ? -44.150 20.604 -34.537 1.00 17.09 ? 47   ILE B O   1 
ATOM   2845 C CB  . ILE B 1 48  ? -44.708 23.741 -34.116 1.00 16.33 ? 47   ILE B CB  1 
ATOM   2846 C CG1 . ILE B 1 48  ? -43.469 24.500 -34.626 1.00 17.18 ? 47   ILE B CG1 1 
ATOM   2847 C CG2 . ILE B 1 48  ? -44.466 23.113 -32.727 1.00 17.00 ? 47   ILE B CG2 1 
ATOM   2848 C CD1 . ILE B 1 48  ? -43.104 25.700 -33.736 1.00 15.79 ? 47   ILE B CD1 1 
ATOM   2849 N N   . PHE B 1 49  ? -43.343 21.658 -36.352 1.00 16.14 ? 48   PHE B N   1 
ATOM   2850 C CA  . PHE B 1 49  ? -42.351 20.633 -36.648 1.00 15.25 ? 48   PHE B CA  1 
ATOM   2851 C C   . PHE B 1 49  ? -41.056 21.340 -36.991 1.00 16.86 ? 48   PHE B C   1 
ATOM   2852 O O   . PHE B 1 49  ? -41.031 22.190 -37.884 1.00 16.46 ? 48   PHE B O   1 
ATOM   2853 C CB  . PHE B 1 49  ? -42.841 19.701 -37.774 1.00 15.12 ? 48   PHE B CB  1 
ATOM   2854 C CG  . PHE B 1 49  ? -44.094 18.984 -37.377 1.00 15.05 ? 48   PHE B CG  1 
ATOM   2855 C CD1 . PHE B 1 49  ? -44.017 17.800 -36.662 1.00 16.12 ? 48   PHE B CD1 1 
ATOM   2856 C CD2 . PHE B 1 49  ? -45.336 19.564 -37.589 1.00 19.09 ? 48   PHE B CD2 1 
ATOM   2857 C CE1 . PHE B 1 49  ? -45.163 17.164 -36.199 1.00 16.78 ? 48   PHE B CE1 1 
ATOM   2858 C CE2 . PHE B 1 49  ? -46.497 18.937 -37.135 1.00 19.55 ? 48   PHE B CE2 1 
ATOM   2859 C CZ  . PHE B 1 49  ? -46.405 17.723 -36.446 1.00 16.83 ? 48   PHE B CZ  1 
ATOM   2860 N N   . ARG B 1 50  ? -40.005 21.036 -36.238 1.00 15.19 ? 49   ARG B N   1 
ATOM   2861 C CA  . ARG B 1 50  ? -38.702 21.658 -36.442 1.00 13.52 ? 49   ARG B CA  1 
ATOM   2862 C C   . ARG B 1 50  ? -37.850 20.716 -37.279 1.00 13.52 ? 49   ARG B C   1 
ATOM   2863 O O   . ARG B 1 50  ? -37.715 19.536 -36.931 1.00 14.24 ? 49   ARG B O   1 
ATOM   2864 C CB  . ARG B 1 50  ? -38.029 21.945 -35.097 1.00 13.91 ? 49   ARG B CB  1 
ATOM   2865 C CG  . ARG B 1 50  ? -36.662 22.625 -35.208 1.00 11.93 ? 49   ARG B CG  1 
ATOM   2866 C CD  . ARG B 1 50  ? -36.334 23.349 -33.904 1.00 12.97 ? 49   ARG B CD  1 
ATOM   2867 N NE  . ARG B 1 50  ? -34.981 23.908 -33.862 1.00 12.63 ? 49   ARG B NE  1 
ATOM   2868 C CZ  . ARG B 1 50  ? -33.955 23.331 -33.243 1.00 16.19 ? 49   ARG B CZ  1 
ATOM   2869 N NH1 . ARG B 1 50  ? -33.993 22.059 -32.858 1.00 13.27 ? 49   ARG B NH1 1 
ATOM   2870 N NH2 . ARG B 1 50  ? -32.859 24.041 -33.014 1.00 14.01 ? 49   ARG B NH2 1 
ATOM   2871 N N   . VAL B 1 51  ? -37.263 21.236 -38.359 1.00 13.77 ? 50   VAL B N   1 
ATOM   2872 C CA  . VAL B 1 51  ? -36.587 20.437 -39.374 1.00 15.30 ? 50   VAL B CA  1 
ATOM   2873 C C   . VAL B 1 51  ? -35.104 20.799 -39.396 1.00 13.90 ? 50   VAL B C   1 
ATOM   2874 O O   . VAL B 1 51  ? -34.702 21.772 -40.032 1.00 14.80 ? 50   VAL B O   1 
ATOM   2875 C CB  . VAL B 1 51  ? -37.213 20.656 -40.759 1.00 15.19 ? 50   VAL B CB  1 
ATOM   2876 C CG1 . VAL B 1 51  ? -36.520 19.783 -41.805 1.00 16.03 ? 50   VAL B CG1 1 
ATOM   2877 C CG2 . VAL B 1 51  ? -38.716 20.356 -40.680 1.00 17.03 ? 50   VAL B CG2 1 
ATOM   2878 N N   . PRO B 1 52  ? -34.255 20.030 -38.704 1.00 13.16 ? 51   PRO B N   1 
ATOM   2879 C CA  . PRO B 1 52  ? -32.804 20.244 -38.803 1.00 14.52 ? 51   PRO B CA  1 
ATOM   2880 C C   . PRO B 1 52  ? -32.279 19.941 -40.197 1.00 17.33 ? 51   PRO B C   1 
ATOM   2881 O O   . PRO B 1 52  ? -32.755 19.029 -40.882 1.00 16.40 ? 51   PRO B O   1 
ATOM   2882 C CB  . PRO B 1 52  ? -32.215 19.250 -37.788 1.00 15.32 ? 51   PRO B CB  1 
ATOM   2883 C CG  . PRO B 1 52  ? -33.342 18.889 -36.872 1.00 18.50 ? 51   PRO B CG  1 
ATOM   2884 C CD  . PRO B 1 52  ? -34.600 18.975 -37.739 1.00 11.88 ? 51   PRO B CD  1 
ATOM   2885 N N   . PHE B 1 53  ? -31.269 20.713 -40.605 1.00 13.32 ? 52   PHE B N   1 
ATOM   2886 C CA  . PHE B 1 53  ? -30.533 20.455 -41.834 1.00 11.61 ? 52   PHE B CA  1 
ATOM   2887 C C   . PHE B 1 53  ? -29.136 21.040 -41.649 1.00 14.46 ? 52   PHE B C   1 
ATOM   2888 O O   . PHE B 1 53  ? -28.909 21.831 -40.739 1.00 13.47 ? 52   PHE B O   1 
ATOM   2889 C CB  . PHE B 1 53  ? -31.256 21.078 -43.038 1.00 14.04 ? 52   PHE B CB  1 
ATOM   2890 C CG  . PHE B 1 53  ? -31.199 22.573 -43.055 1.00 14.97 ? 52   PHE B CG  1 
ATOM   2891 C CD1 . PHE B 1 53  ? -32.166 23.338 -42.409 1.00 13.99 ? 52   PHE B CD1 1 
ATOM   2892 C CD2 . PHE B 1 53  ? -30.153 23.231 -43.702 1.00 13.77 ? 52   PHE B CD2 1 
ATOM   2893 C CE1 . PHE B 1 53  ? -32.093 24.736 -42.397 1.00 14.19 ? 52   PHE B CE1 1 
ATOM   2894 C CE2 . PHE B 1 53  ? -30.085 24.624 -43.698 1.00 14.27 ? 52   PHE B CE2 1 
ATOM   2895 C CZ  . PHE B 1 53  ? -31.062 25.377 -43.051 1.00 13.28 ? 52   PHE B CZ  1 
ATOM   2896 N N   . MET B 1 54  ? -28.198 20.702 -42.536 1.00 14.86 ? 53   MET B N   1 
ATOM   2897 C CA  A MET B 1 54  ? -26.838 21.239 -42.467 0.61 16.70 ? 53   MET B CA  1 
ATOM   2898 C CA  B MET B 1 54  ? -26.851 21.254 -42.453 0.39 16.68 ? 53   MET B CA  1 
ATOM   2899 C C   . MET B 1 54  ? -26.695 22.434 -43.401 1.00 14.71 ? 53   MET B C   1 
ATOM   2900 O O   . MET B 1 54  ? -27.041 22.335 -44.581 1.00 16.77 ? 53   MET B O   1 
ATOM   2901 C CB  A MET B 1 54  ? -25.791 20.189 -42.851 0.61 17.60 ? 53   MET B CB  1 
ATOM   2902 C CB  B MET B 1 54  ? -25.803 20.195 -42.776 0.39 17.59 ? 53   MET B CB  1 
ATOM   2903 C CG  A MET B 1 54  ? -25.700 18.989 -41.935 0.61 18.83 ? 53   MET B CG  1 
ATOM   2904 C CG  B MET B 1 54  ? -25.900 18.981 -41.902 0.39 19.26 ? 53   MET B CG  1 
ATOM   2905 S SD  A MET B 1 54  ? -25.381 19.437 -40.226 0.61 18.41 ? 53   MET B SD  1 
ATOM   2906 S SD  B MET B 1 54  ? -24.470 17.946 -42.142 0.39 15.73 ? 53   MET B SD  1 
ATOM   2907 C CE  A MET B 1 54  ? -23.713 20.087 -40.362 0.61 17.12 ? 53   MET B CE  1 
ATOM   2908 C CE  B MET B 1 54  ? -23.175 19.068 -41.591 0.39 18.84 ? 53   MET B CE  1 
ATOM   2909 N N   . MET B 1 55  ? -26.156 23.547 -42.875 1.00 13.66 ? 54   MET B N   1 
ATOM   2910 C CA  . MET B 1 55  ? -25.844 24.700 -43.720 1.00 14.61 ? 54   MET B CA  1 
ATOM   2911 C C   . MET B 1 55  ? -25.005 24.290 -44.926 1.00 14.62 ? 54   MET B C   1 
ATOM   2912 O O   . MET B 1 55  ? -25.197 24.813 -46.026 1.00 15.21 ? 54   MET B O   1 
ATOM   2913 C CB  . MET B 1 55  ? -25.081 25.781 -42.946 1.00 13.62 ? 54   MET B CB  1 
ATOM   2914 C CG  . MET B 1 55  ? -25.881 26.486 -41.883 1.00 13.81 ? 54   MET B CG  1 
ATOM   2915 S SD  . MET B 1 55  ? -24.865 27.684 -40.995 1.00 15.82 ? 54   MET B SD  1 
ATOM   2916 C CE  . MET B 1 55  ? -24.591 28.937 -42.276 1.00 14.74 ? 54   MET B CE  1 
ATOM   2917 N N   . GLU B 1 56  ? -24.043 23.381 -44.724 1.00 15.04 ? 55   GLU B N   1 
ATOM   2918 C CA  . GLU B 1 56  ? -23.088 23.058 -45.778 1.00 15.36 ? 55   GLU B CA  1 
ATOM   2919 C C   . GLU B 1 56  ? -23.730 22.240 -46.885 1.00 16.08 ? 55   GLU B C   1 
ATOM   2920 O O   . GLU B 1 56  ? -23.244 22.250 -48.029 1.00 15.65 ? 55   GLU B O   1 
ATOM   2921 C CB  . GLU B 1 56  ? -21.895 22.288 -45.208 1.00 17.55 ? 55   GLU B CB  1 
ATOM   2922 C CG  . GLU B 1 56  ? -21.100 23.024 -44.112 1.00 16.58 ? 55   GLU B CG  1 
ATOM   2923 C CD  . GLU B 1 56  ? -21.669 22.843 -42.706 1.00 18.59 ? 55   GLU B CD  1 
ATOM   2924 O OE1 . GLU B 1 56  ? -22.853 22.446 -42.549 1.00 16.74 ? 55   GLU B OE1 1 
ATOM   2925 O OE2 . GLU B 1 56  ? -20.900 23.104 -41.760 1.00 18.98 ? 55   GLU B OE2 1 
ATOM   2926 N N   . ARG B 1 57  ? -24.796 21.504 -46.568 1.00 14.24 ? 56   ARG B N   1 
ATOM   2927 C CA  . ARG B 1 57  ? -25.532 20.786 -47.607 1.00 15.30 ? 56   ARG B CA  1 
ATOM   2928 C C   . ARG B 1 57  ? -26.492 21.696 -48.364 1.00 16.38 ? 56   ARG B C   1 
ATOM   2929 O O   . ARG B 1 57  ? -26.707 21.502 -49.570 1.00 16.95 ? 56   ARG B O   1 
ATOM   2930 C CB  . ARG B 1 57  ? -26.282 19.598 -46.985 1.00 17.23 ? 56   ARG B CB  1 
ATOM   2931 C CG  . ARG B 1 57  ? -25.342 18.501 -46.434 1.00 16.89 ? 56   ARG B CG  1 
ATOM   2932 C CD  . ARG B 1 57  ? -26.099 17.304 -45.828 1.00 18.20 ? 56   ARG B CD  1 
ATOM   2933 N NE  . ARG B 1 57  ? -25.187 16.221 -45.461 1.00 18.31 ? 56   ARG B NE  1 
ATOM   2934 C CZ  . ARG B 1 57  ? -25.356 15.391 -44.438 1.00 19.87 ? 56   ARG B CZ  1 
ATOM   2935 N NH1 . ARG B 1 57  ? -26.406 15.484 -43.633 1.00 17.88 ? 56   ARG B NH1 1 
ATOM   2936 N NH2 . ARG B 1 57  ? -24.445 14.446 -44.211 1.00 20.29 ? 56   ARG B NH2 1 
ATOM   2937 N N   . LEU B 1 58  ? -27.078 22.689 -47.690 1.00 14.08 ? 57   LEU B N   1 
ATOM   2938 C CA  . LEU B 1 58  ? -28.010 23.579 -48.375 1.00 13.70 ? 57   LEU B CA  1 
ATOM   2939 C C   . LEU B 1 58  ? -27.278 24.627 -49.209 1.00 15.41 ? 57   LEU B C   1 
ATOM   2940 O O   . LEU B 1 58  ? -27.739 24.982 -50.301 1.00 15.07 ? 57   LEU B O   1 
ATOM   2941 C CB  . LEU B 1 58  ? -28.940 24.256 -47.364 1.00 14.43 ? 57   LEU B CB  1 
ATOM   2942 C CG  . LEU B 1 58  ? -30.050 25.128 -47.970 1.00 13.48 ? 57   LEU B CG  1 
ATOM   2943 C CD1 . LEU B 1 58  ? -31.077 24.243 -48.648 1.00 13.51 ? 57   LEU B CD1 1 
ATOM   2944 C CD2 . LEU B 1 58  ? -30.742 25.985 -46.927 1.00 15.04 ? 57   LEU B CD2 1 
ATOM   2945 N N   . VAL B 1 59  ? -26.167 25.158 -48.703 1.00 16.06 ? 58   VAL B N   1 
ATOM   2946 C CA  . VAL B 1 59  ? -25.396 26.190 -49.408 1.00 15.35 ? 58   VAL B CA  1 
ATOM   2947 C C   . VAL B 1 59  ? -23.928 25.803 -49.292 1.00 16.94 ? 58   VAL B C   1 
ATOM   2948 O O   . VAL B 1 59  ? -23.246 26.217 -48.342 1.00 17.03 ? 58   VAL B O   1 
ATOM   2949 C CB  . VAL B 1 59  ? -25.646 27.595 -48.827 1.00 13.88 ? 58   VAL B CB  1 
ATOM   2950 C CG1 . VAL B 1 59  ? -24.873 28.654 -49.649 1.00 17.27 ? 58   VAL B CG1 1 
ATOM   2951 C CG2 . VAL B 1 59  ? -27.158 27.917 -48.766 1.00 15.74 ? 58   VAL B CG2 1 
ATOM   2952 N N   . PRO B 1 60  ? -23.410 24.999 -50.215 1.00 17.28 ? 59   PRO B N   1 
ATOM   2953 C CA  . PRO B 1 60  ? -22.077 24.410 -50.024 1.00 17.58 ? 59   PRO B CA  1 
ATOM   2954 C C   . PRO B 1 60  ? -20.947 25.411 -50.193 1.00 21.38 ? 59   PRO B C   1 
ATOM   2955 O O   . PRO B 1 60  ? -21.059 26.389 -50.936 1.00 17.11 ? 59   PRO B O   1 
ATOM   2956 C CB  . PRO B 1 60  ? -21.994 23.337 -51.114 1.00 16.14 ? 59   PRO B CB  1 
ATOM   2957 C CG  . PRO B 1 60  ? -23.408 23.077 -51.543 1.00 25.10 ? 59   PRO B CG  1 
ATOM   2958 C CD  . PRO B 1 60  ? -24.186 24.341 -51.277 1.00 19.26 ? 59   PRO B CD  1 
ATOM   2959 N N   . ASN B 1 61  ? -19.848 25.131 -49.475 1.00 18.68 ? 60   ASN B N   1 
ATOM   2960 C CA  . ASN B 1 61  ? -18.527 25.740 -49.636 1.00 16.76 ? 60   ASN B CA  1 
ATOM   2961 C C   . ASN B 1 61  ? -18.444 27.148 -49.066 1.00 20.92 ? 60   ASN B C   1 
ATOM   2962 O O   . ASN B 1 61  ? -17.623 27.407 -48.178 1.00 21.68 ? 60   ASN B O   1 
ATOM   2963 C CB  . ASN B 1 61  ? -18.105 25.754 -51.102 1.00 20.49 ? 60   ASN B CB  1 
ATOM   2964 C CG  . ASN B 1 61  ? -17.933 24.362 -51.658 1.00 27.00 ? 60   ASN B CG  1 
ATOM   2965 O OD1 . ASN B 1 61  ? -17.438 23.465 -50.978 1.00 27.46 ? 60   ASN B OD1 1 
ATOM   2966 N ND2 . ASN B 1 61  ? -18.364 24.167 -52.889 1.00 28.97 ? 60   ASN B ND2 1 
ATOM   2967 N N   . SER B 1 62  ? -19.261 28.064 -49.581 1.00 19.79 ? 61   SER B N   1 
ATOM   2968 C CA  . SER B 1 62  ? -19.348 29.430 -49.087 1.00 18.38 ? 61   SER B CA  1 
ATOM   2969 C C   . SER B 1 62  ? -20.799 29.727 -48.732 1.00 15.61 ? 61   SER B C   1 
ATOM   2970 O O   . SER B 1 62  ? -21.691 29.529 -49.564 1.00 19.16 ? 61   SER B O   1 
ATOM   2971 C CB  . SER B 1 62  ? -18.870 30.424 -50.143 1.00 22.15 ? 61   SER B CB  1 
ATOM   2972 O OG  . SER B 1 62  ? -19.326 31.729 -49.839 1.00 28.19 ? 61   SER B OG  1 
ATOM   2973 N N   . MET B 1 63  ? -21.035 30.225 -47.513 1.00 15.79 ? 62   MET B N   1 
ATOM   2974 C CA  . MET B 1 63  ? -22.420 30.454 -47.121 1.00 16.05 ? 62   MET B CA  1 
ATOM   2975 C C   . MET B 1 63  ? -23.057 31.615 -47.877 1.00 23.38 ? 62   MET B C   1 
ATOM   2976 O O   . MET B 1 63  ? -24.277 31.800 -47.772 1.00 17.46 ? 62   MET B O   1 
ATOM   2977 C CB  . MET B 1 63  ? -22.525 30.693 -45.604 1.00 17.27 ? 62   MET B CB  1 
ATOM   2978 C CG  . MET B 1 63  ? -22.021 32.031 -45.131 1.00 16.51 ? 62   MET B CG  1 
ATOM   2979 S SD  . MET B 1 63  ? -22.195 32.123 -43.309 1.00 20.24 ? 62   MET B SD  1 
ATOM   2980 C CE  . MET B 1 63  ? -20.907 30.997 -42.766 1.00 23.62 ? 62   MET B CE  1 
ATOM   2981 N N   . THR B 1 64  ? -22.273 32.384 -48.639 1.00 20.30 ? 63   THR B N   1 
ATOM   2982 C CA  . THR B 1 64  ? -22.796 33.472 -49.452 1.00 19.46 ? 63   THR B CA  1 
ATOM   2983 C C   . THR B 1 64  ? -23.107 33.022 -50.865 1.00 20.71 ? 63   THR B C   1 
ATOM   2984 O O   . THR B 1 64  ? -23.501 33.853 -51.696 1.00 21.55 ? 63   THR B O   1 
ATOM   2985 C CB  . THR B 1 64  ? -21.801 34.632 -49.513 1.00 21.36 ? 63   THR B CB  1 
ATOM   2986 O OG1 . THR B 1 64  ? -20.603 34.198 -50.166 1.00 22.15 ? 63   THR B OG1 1 
ATOM   2987 C CG2 . THR B 1 64  ? -21.459 35.131 -48.099 1.00 22.20 ? 63   THR B CG2 1 
ATOM   2988 N N   . GLY B 1 65  ? -22.929 31.736 -51.152 1.00 19.22 ? 64   GLY B N   1 
ATOM   2989 C CA  . GLY B 1 65  ? -23.122 31.207 -52.488 1.00 18.62 ? 64   GLY B CA  1 
ATOM   2990 C C   . GLY B 1 65  ? -24.561 30.804 -52.774 1.00 15.62 ? 64   GLY B C   1 
ATOM   2991 O O   . GLY B 1 65  ? -25.490 31.061 -52.005 1.00 18.61 ? 64   GLY B O   1 
ATOM   2992 N N   . SER B 1 66  ? -24.732 30.136 -53.924 1.00 20.59 ? 65   SER B N   1 
ATOM   2993 C CA  A SER B 1 66  ? -26.049 29.669 -54.345 0.69 21.48 ? 65   SER B CA  1 
ATOM   2994 C CA  B SER B 1 66  ? -26.066 29.700 -54.300 0.31 21.41 ? 65   SER B CA  1 
ATOM   2995 C C   . SER B 1 66  ? -26.415 28.370 -53.628 1.00 18.18 ? 65   SER B C   1 
ATOM   2996 O O   . SER B 1 66  ? -25.533 27.571 -53.296 1.00 20.19 ? 65   SER B O   1 
ATOM   2997 C CB  A SER B 1 66  ? -26.066 29.429 -55.846 0.69 21.37 ? 65   SER B CB  1 
ATOM   2998 C CB  B SER B 1 66  ? -26.174 29.570 -55.816 0.31 21.43 ? 65   SER B CB  1 
ATOM   2999 O OG  A SER B 1 66  ? -25.676 30.592 -56.540 0.69 23.34 ? 65   SER B OG  1 
ATOM   3000 O OG  B SER B 1 66  ? -25.006 28.995 -56.365 0.31 21.88 ? 65   SER B OG  1 
ATOM   3001 N N   . PRO B 1 67  ? -27.698 28.122 -53.395 1.00 19.10 ? 66   PRO B N   1 
ATOM   3002 C CA  . PRO B 1 67  ? -28.088 26.870 -52.736 1.00 17.78 ? 66   PRO B CA  1 
ATOM   3003 C C   . PRO B 1 67  ? -27.885 25.667 -53.645 1.00 19.29 ? 66   PRO B C   1 
ATOM   3004 O O   . PRO B 1 67  ? -27.804 25.774 -54.878 1.00 20.16 ? 66   PRO B O   1 
ATOM   3005 C CB  . PRO B 1 67  ? -29.574 27.077 -52.406 1.00 18.38 ? 66   PRO B CB  1 
ATOM   3006 C CG  . PRO B 1 67  ? -30.032 28.158 -53.345 1.00 21.50 ? 66   PRO B CG  1 
ATOM   3007 C CD  . PRO B 1 67  ? -28.839 29.032 -53.610 1.00 18.59 ? 66   PRO B CD  1 
ATOM   3008 N N   . ASP B 1 68  ? -27.772 24.502 -53.013 1.00 15.97 ? 67   ASP B N   1 
ATOM   3009 C CA  . ASP B 1 68  ? -27.736 23.242 -53.753 1.00 17.37 ? 67   ASP B CA  1 
ATOM   3010 C C   . ASP B 1 68  ? -29.154 22.883 -54.185 1.00 14.67 ? 67   ASP B C   1 
ATOM   3011 O O   . ASP B 1 68  ? -30.003 22.664 -53.324 1.00 15.35 ? 67   ASP B O   1 
ATOM   3012 C CB  . ASP B 1 68  ? -27.170 22.133 -52.869 1.00 17.35 ? 67   ASP B CB  1 
ATOM   3013 C CG  . ASP B 1 68  ? -27.100 20.800 -53.586 1.00 18.91 ? 67   ASP B CG  1 
ATOM   3014 O OD1 . ASP B 1 68  ? -26.211 20.641 -54.460 1.00 21.36 ? 67   ASP B OD1 1 
ATOM   3015 O OD2 . ASP B 1 68  ? -27.938 19.911 -53.302 1.00 18.04 ? 67   ASP B OD2 1 
ATOM   3016 N N   . PRO B 1 69  ? -29.464 22.826 -55.484 1.00 16.14 ? 68   PRO B N   1 
ATOM   3017 C CA  . PRO B 1 69  ? -30.872 22.635 -55.864 1.00 15.70 ? 68   PRO B CA  1 
ATOM   3018 C C   . PRO B 1 69  ? -31.496 21.353 -55.332 1.00 16.92 ? 68   PRO B C   1 
ATOM   3019 O O   . PRO B 1 69  ? -32.671 21.376 -54.949 1.00 17.31 ? 68   PRO B O   1 
ATOM   3020 C CB  . PRO B 1 69  ? -30.824 22.655 -57.404 1.00 16.14 ? 68   PRO B CB  1 
ATOM   3021 C CG  . PRO B 1 69  ? -29.668 23.545 -57.702 1.00 18.94 ? 68   PRO B CG  1 
ATOM   3022 C CD  . PRO B 1 69  ? -28.628 23.196 -56.642 1.00 18.21 ? 68   PRO B CD  1 
ATOM   3023 N N   . ASN B 1 70  ? -30.759 20.234 -55.288 1.00 15.30 ? 69   ASN B N   1 
ATOM   3024 C CA  . ASN B 1 70  ? -31.394 18.975 -54.893 1.00 15.01 ? 69   ASN B CA  1 
ATOM   3025 C C   . ASN B 1 70  ? -31.665 18.907 -53.394 1.00 14.74 ? 69   ASN B C   1 
ATOM   3026 O O   . ASN B 1 70  ? -32.717 18.403 -52.979 1.00 16.16 ? 69   ASN B O   1 
ATOM   3027 C CB  . ASN B 1 70  ? -30.552 17.794 -55.352 1.00 16.56 ? 69   ASN B CB  1 
ATOM   3028 C CG  . ASN B 1 70  ? -30.698 17.568 -56.835 1.00 21.64 ? 69   ASN B CG  1 
ATOM   3029 O OD1 . ASN B 1 70  ? -31.733 17.900 -57.398 1.00 20.92 ? 69   ASN B OD1 1 
ATOM   3030 N ND2 . ASN B 1 70  ? -29.673 17.030 -57.464 1.00 22.06 ? 69   ASN B ND2 1 
ATOM   3031 N N   . TYR B 1 71  ? -30.727 19.358 -52.559 1.00 15.30 ? 70   TYR B N   1 
ATOM   3032 C CA  . TYR B 1 71  ? -31.011 19.380 -51.127 1.00 14.32 ? 70   TYR B CA  1 
ATOM   3033 C C   . TYR B 1 71  ? -32.058 20.433 -50.800 1.00 14.13 ? 70   TYR B C   1 
ATOM   3034 O O   . TYR B 1 71  ? -32.969 20.190 -49.993 1.00 16.52 ? 70   TYR B O   1 
ATOM   3035 C CB  . TYR B 1 71  ? -29.713 19.639 -50.366 1.00 14.23 ? 70   TYR B CB  1 
ATOM   3036 C CG  . TYR B 1 71  ? -29.703 19.391 -48.870 1.00 14.02 ? 70   TYR B CG  1 
ATOM   3037 C CD1 . TYR B 1 71  ? -29.557 18.100 -48.350 1.00 14.08 ? 70   TYR B CD1 1 
ATOM   3038 C CD2 . TYR B 1 71  ? -29.751 20.457 -47.982 1.00 13.77 ? 70   TYR B CD2 1 
ATOM   3039 C CE1 . TYR B 1 71  ? -29.473 17.888 -46.970 1.00 15.10 ? 70   TYR B CE1 1 
ATOM   3040 C CE2 . TYR B 1 71  ? -29.661 20.251 -46.611 1.00 15.02 ? 70   TYR B CE2 1 
ATOM   3041 C CZ  . TYR B 1 71  ? -29.543 18.967 -46.118 1.00 14.73 ? 70   TYR B CZ  1 
ATOM   3042 O OH  . TYR B 1 71  ? -29.431 18.787 -44.746 1.00 14.34 ? 70   TYR B OH  1 
ATOM   3043 N N   . LEU B 1 72  ? -31.943 21.616 -51.406 1.00 14.68 ? 71   LEU B N   1 
ATOM   3044 C CA  . LEU B 1 72  ? -32.992 22.625 -51.255 1.00 15.57 ? 71   LEU B CA  1 
ATOM   3045 C C   . LEU B 1 72  ? -34.359 22.085 -51.654 1.00 17.27 ? 71   LEU B C   1 
ATOM   3046 O O   . LEU B 1 72  ? -35.353 22.376 -50.989 1.00 16.36 ? 71   LEU B O   1 
ATOM   3047 C CB  . LEU B 1 72  ? -32.656 23.860 -52.091 1.00 17.17 ? 71   LEU B CB  1 
ATOM   3048 C CG  . LEU B 1 72  ? -33.753 24.927 -52.197 1.00 18.18 ? 71   LEU B CG  1 
ATOM   3049 C CD1 . LEU B 1 72  ? -34.113 25.529 -50.835 1.00 16.51 ? 71   LEU B CD1 1 
ATOM   3050 C CD2 . LEU B 1 72  ? -33.332 26.019 -53.199 1.00 19.13 ? 71   LEU B CD2 1 
ATOM   3051 N N   . ALA B 1 73  ? -34.431 21.309 -52.744 1.00 15.56 ? 72   ALA B N   1 
ATOM   3052 C CA  . ALA B 1 73  ? -35.718 20.786 -53.193 1.00 14.48 ? 72   ALA B CA  1 
ATOM   3053 C C   . ALA B 1 73  ? -36.385 19.964 -52.099 1.00 17.72 ? 72   ALA B C   1 
ATOM   3054 O O   . ALA B 1 73  ? -37.603 20.054 -51.891 1.00 17.28 ? 72   ALA B O   1 
ATOM   3055 C CB  . ALA B 1 73  ? -35.527 19.941 -54.462 1.00 15.61 ? 72   ALA B CB  1 
ATOM   3056 N N   . ASP B 1 74  ? -35.600 19.160 -51.390 1.00 15.73 ? 73   ASP B N   1 
ATOM   3057 C CA  . ASP B 1 74  ? -36.170 18.341 -50.334 1.00 18.58 ? 73   ASP B CA  1 
ATOM   3058 C C   . ASP B 1 74  ? -36.504 19.165 -49.093 1.00 16.95 ? 73   ASP B C   1 
ATOM   3059 O O   . ASP B 1 74  ? -37.474 18.854 -48.397 1.00 16.67 ? 73   ASP B O   1 
ATOM   3060 C CB  . ASP B 1 74  ? -35.216 17.203 -49.985 1.00 17.82 ? 73   ASP B CB  1 
ATOM   3061 C CG  . ASP B 1 74  ? -35.311 16.038 -50.943 1.00 24.12 ? 73   ASP B CG  1 
ATOM   3062 O OD1 . ASP B 1 74  ? -36.406 15.789 -51.490 1.00 31.61 ? 73   ASP B OD1 1 
ATOM   3063 O OD2 . ASP B 1 74  ? -34.288 15.361 -51.144 1.00 23.08 ? 73   ASP B OD2 1 
ATOM   3064 N N   . LEU B 1 75  ? -35.728 20.211 -48.791 1.00 14.79 ? 74   LEU B N   1 
ATOM   3065 C CA  . LEU B 1 75  ? -36.122 21.116 -47.712 1.00 14.88 ? 74   LEU B CA  1 
ATOM   3066 C C   . LEU B 1 75  ? -37.467 21.771 -48.022 1.00 17.08 ? 74   LEU B C   1 
ATOM   3067 O O   . LEU B 1 75  ? -38.363 21.819 -47.167 1.00 16.09 ? 74   LEU B O   1 
ATOM   3068 C CB  . LEU B 1 75  ? -35.041 22.178 -47.480 1.00 15.34 ? 74   LEU B CB  1 
ATOM   3069 C CG  . LEU B 1 75  ? -35.367 23.211 -46.399 1.00 15.54 ? 74   LEU B CG  1 
ATOM   3070 C CD1 . LEU B 1 75  ? -35.469 22.537 -45.001 1.00 14.88 ? 74   LEU B CD1 1 
ATOM   3071 C CD2 . LEU B 1 75  ? -34.339 24.332 -46.402 1.00 15.97 ? 74   LEU B CD2 1 
ATOM   3072 N N   . ILE B 1 76  ? -37.615 22.288 -49.243 1.00 15.49 ? 75   ILE B N   1 
ATOM   3073 C CA  . ILE B 1 76  ? -38.874 22.911 -49.658 1.00 15.86 ? 75   ILE B CA  1 
ATOM   3074 C C   . ILE B 1 76  ? -40.009 21.910 -49.594 1.00 17.87 ? 75   ILE B C   1 
ATOM   3075 O O   . ILE B 1 76  ? -41.097 22.218 -49.089 1.00 19.42 ? 75   ILE B O   1 
ATOM   3076 C CB  . ILE B 1 76  ? -38.741 23.515 -51.064 1.00 16.18 ? 75   ILE B CB  1 
ATOM   3077 C CG1 . ILE B 1 76  ? -37.722 24.654 -51.077 1.00 16.74 ? 75   ILE B CG1 1 
ATOM   3078 C CG2 . ILE B 1 76  ? -40.106 24.012 -51.546 1.00 19.05 ? 75   ILE B CG2 1 
ATOM   3079 C CD1 . ILE B 1 76  ? -37.375 25.105 -52.524 1.00 17.85 ? 75   ILE B CD1 1 
ATOM   3080 N N   . ALA B 1 77  ? -39.783 20.694 -50.091 1.00 17.19 ? 76   ALA B N   1 
ATOM   3081 C CA  . ALA B 1 77  ? -40.865 19.711 -50.093 1.00 17.72 ? 76   ALA B CA  1 
ATOM   3082 C C   . ALA B 1 77  ? -41.314 19.414 -48.669 1.00 16.52 ? 76   ALA B C   1 
ATOM   3083 O O   . ALA B 1 77  ? -42.521 19.389 -48.384 1.00 18.50 ? 76   ALA B O   1 
ATOM   3084 C CB  . ALA B 1 77  ? -40.424 18.428 -50.797 1.00 20.94 ? 76   ALA B CB  1 
ATOM   3085 N N   . THR B 1 78  ? -40.351 19.235 -47.753 1.00 16.62 ? 77   THR B N   1 
ATOM   3086 C CA  . THR B 1 78  ? -40.685 18.908 -46.367 1.00 18.70 ? 77   THR B CA  1 
ATOM   3087 C C   . THR B 1 78  ? -41.419 20.056 -45.697 1.00 17.04 ? 77   THR B C   1 
ATOM   3088 O O   . THR B 1 78  ? -42.455 19.852 -45.053 1.00 15.90 ? 77   THR B O   1 
ATOM   3089 C CB  . THR B 1 78  ? -39.413 18.573 -45.582 1.00 18.74 ? 77   THR B CB  1 
ATOM   3090 O OG1 . THR B 1 78  ? -38.825 17.385 -46.129 1.00 18.99 ? 77   THR B OG1 1 
ATOM   3091 C CG2 . THR B 1 78  ? -39.743 18.350 -44.089 1.00 17.98 ? 77   THR B CG2 1 
ATOM   3092 N N   . VAL B 1 79  ? -40.887 21.268 -45.846 1.00 17.94 ? 78   VAL B N   1 
ATOM   3093 C CA  . VAL B 1 79  ? -41.488 22.452 -45.235 1.00 14.31 ? 78   VAL B CA  1 
ATOM   3094 C C   . VAL B 1 79  ? -42.902 22.671 -45.750 1.00 18.41 ? 78   VAL B C   1 
ATOM   3095 O O   . VAL B 1 79  ? -43.843 22.824 -44.968 1.00 17.95 ? 78   VAL B O   1 
ATOM   3096 C CB  . VAL B 1 79  ? -40.600 23.684 -45.486 1.00 16.12 ? 78   VAL B CB  1 
ATOM   3097 C CG1 . VAL B 1 79  ? -41.380 24.963 -45.229 1.00 21.86 ? 78   VAL B CG1 1 
ATOM   3098 C CG2 . VAL B 1 79  ? -39.368 23.632 -44.600 1.00 17.62 ? 78   VAL B CG2 1 
ATOM   3099 N N   . ASN B 1 80  ? -43.083 22.667 -47.070 1.00 17.28 ? 79   ASN B N   1 
ATOM   3100 C CA  . ASN B 1 80  ? -44.385 23.046 -47.594 1.00 17.41 ? 79   ASN B CA  1 
ATOM   3101 C C   . ASN B 1 80  ? -45.424 21.960 -47.333 1.00 20.28 ? 79   ASN B C   1 
ATOM   3102 O O   . ASN B 1 80  ? -46.615 22.270 -47.212 1.00 21.61 ? 79   ASN B O   1 
ATOM   3103 C CB  . ASN B 1 80  ? -44.266 23.397 -49.090 1.00 15.30 ? 79   ASN B CB  1 
ATOM   3104 C CG  . ASN B 1 80  ? -43.565 24.743 -49.316 1.00 19.54 ? 79   ASN B CG  1 
ATOM   3105 O OD1 . ASN B 1 80  ? -43.223 25.453 -48.362 1.00 23.87 ? 79   ASN B OD1 1 
ATOM   3106 N ND2 . ASN B 1 80  ? -43.319 25.086 -50.582 1.00 23.28 ? 79   ASN B ND2 1 
ATOM   3107 N N   . ALA B 1 81  ? -45.001 20.691 -47.210 1.00 18.04 ? 80   ALA B N   1 
ATOM   3108 C CA  . ALA B 1 81  ? -45.952 19.645 -46.838 1.00 19.15 ? 80   ALA B CA  1 
ATOM   3109 C C   . ALA B 1 81  ? -46.465 19.855 -45.423 1.00 22.12 ? 80   ALA B C   1 
ATOM   3110 O O   . ALA B 1 81  ? -47.642 19.591 -45.139 1.00 23.09 ? 80   ALA B O   1 
ATOM   3111 C CB  . ALA B 1 81  ? -45.322 18.259 -46.958 1.00 21.47 ? 80   ALA B CB  1 
ATOM   3112 N N   . ILE B 1 82  ? -45.587 20.304 -44.520 1.00 16.58 ? 81   ILE B N   1 
ATOM   3113 C CA  . ILE B 1 82  ? -46.017 20.665 -43.171 1.00 14.59 ? 81   ILE B CA  1 
ATOM   3114 C C   . ILE B 1 82  ? -47.005 21.825 -43.218 1.00 16.87 ? 81   ILE B C   1 
ATOM   3115 O O   . ILE B 1 82  ? -48.093 21.769 -42.618 1.00 20.13 ? 81   ILE B O   1 
ATOM   3116 C CB  . ILE B 1 82  ? -44.790 21.002 -42.296 1.00 18.80 ? 81   ILE B CB  1 
ATOM   3117 C CG1 . ILE B 1 82  ? -43.938 19.758 -42.014 1.00 18.87 ? 81   ILE B CG1 1 
ATOM   3118 C CG2 . ILE B 1 82  ? -45.205 21.699 -40.987 1.00 18.44 ? 81   ILE B CG2 1 
ATOM   3119 C CD1 . ILE B 1 82  ? -42.479 20.085 -41.652 1.00 17.08 ? 81   ILE B CD1 1 
ATOM   3120 N N   . THR B 1 83  ? -46.651 22.900 -43.936 1.00 16.38 ? 82   THR B N   1 
ATOM   3121 C CA  . THR B 1 83  ? -47.487 24.098 -43.887 1.00 17.01 ? 82   THR B CA  1 
ATOM   3122 C C   . THR B 1 83  ? -48.787 23.923 -44.669 1.00 17.82 ? 82   THR B C   1 
ATOM   3123 O O   . THR B 1 83  ? -49.788 24.564 -44.336 1.00 20.14 ? 82   THR B O   1 
ATOM   3124 C CB  . THR B 1 83  ? -46.706 25.330 -44.366 1.00 15.43 ? 82   THR B CB  1 
ATOM   3125 O OG1 . THR B 1 83  ? -46.367 25.210 -45.762 1.00 17.30 ? 82   THR B OG1 1 
ATOM   3126 C CG2 . THR B 1 83  ? -45.417 25.503 -43.531 1.00 16.18 ? 82   THR B CG2 1 
ATOM   3127 N N   . GLN B 1 84  ? -48.800 23.072 -45.703 1.00 15.53 ? 83   GLN B N   1 
ATOM   3128 C CA  . GLN B 1 84  ? -50.056 22.785 -46.397 1.00 18.04 ? 83   GLN B CA  1 
ATOM   3129 C C   . GLN B 1 84  ? -51.077 22.136 -45.465 1.00 22.91 ? 83   GLN B C   1 
ATOM   3130 O O   . GLN B 1 84  ? -52.293 22.241 -45.694 1.00 22.69 ? 83   GLN B O   1 
ATOM   3131 C CB  . GLN B 1 84  ? -49.790 21.886 -47.606 1.00 23.62 ? 83   GLN B CB  1 
ATOM   3132 C CG  . GLN B 1 84  ? -51.017 21.658 -48.446 1.00 32.27 ? 83   GLN B CG  1 
ATOM   3133 C CD  . GLN B 1 84  ? -51.339 22.838 -49.343 1.00 38.28 ? 83   GLN B CD  1 
ATOM   3134 O OE1 . GLN B 1 84  ? -50.482 23.311 -50.095 1.00 43.43 ? 83   GLN B OE1 1 
ATOM   3135 N NE2 . GLN B 1 84  ? -52.589 23.311 -49.282 1.00 38.22 ? 83   GLN B NE2 1 
ATOM   3136 N N   . LYS B 1 85  ? -50.609 21.454 -44.422 1.00 17.97 ? 84   LYS B N   1 
ATOM   3137 C CA  . LYS B 1 85  ? -51.503 20.873 -43.420 1.00 21.34 ? 84   LYS B CA  1 
ATOM   3138 C C   . LYS B 1 85  ? -51.912 21.867 -42.333 1.00 22.86 ? 84   LYS B C   1 
ATOM   3139 O O   . LYS B 1 85  ? -52.698 21.508 -41.445 1.00 25.76 ? 84   LYS B O   1 
ATOM   3140 C CB  . LYS B 1 85  ? -50.842 19.647 -42.782 1.00 20.62 ? 84   LYS B CB  1 
ATOM   3141 C CG  . LYS B 1 85  ? -50.714 18.452 -43.714 1.00 26.14 ? 84   LYS B CG  1 
ATOM   3142 C CD  . LYS B 1 85  ? -51.987 17.615 -43.692 1.00 28.51 ? 84   LYS B CD  1 
ATOM   3143 C CE  . LYS B 1 85  ? -52.141 16.891 -42.354 1.00 37.16 ? 84   LYS B CE  1 
ATOM   3144 N NZ  . LYS B 1 85  ? -53.533 16.390 -42.171 1.00 29.20 ? 84   LYS B NZ  1 
ATOM   3145 N N   . GLY B 1 86  ? -51.389 23.094 -42.370 1.00 20.90 ? 85   GLY B N   1 
ATOM   3146 C CA  . GLY B 1 86  ? -51.733 24.133 -41.424 1.00 18.87 ? 85   GLY B CA  1 
ATOM   3147 C C   . GLY B 1 86  ? -50.823 24.233 -40.229 1.00 17.65 ? 85   GLY B C   1 
ATOM   3148 O O   . GLY B 1 86  ? -51.065 25.082 -39.356 1.00 21.83 ? 85   GLY B O   1 
ATOM   3149 N N   . ALA B 1 87  ? -49.800 23.388 -40.157 1.00 19.11 ? 86   ALA B N   1 
ATOM   3150 C CA  . ALA B 1 87  ? -48.819 23.406 -39.086 1.00 19.21 ? 86   ALA B CA  1 
ATOM   3151 C C   . ALA B 1 87  ? -47.657 24.312 -39.451 1.00 17.60 ? 86   ALA B C   1 
ATOM   3152 O O   . ALA B 1 87  ? -47.425 24.632 -40.625 1.00 17.03 ? 86   ALA B O   1 
ATOM   3153 C CB  . ALA B 1 87  ? -48.303 21.996 -38.791 1.00 18.73 ? 86   ALA B CB  1 
ATOM   3154 N N   . TYR B 1 88  ? -46.923 24.726 -38.422 1.00 16.25 ? 87   TYR B N   1 
ATOM   3155 C CA  . TYR B 1 88  ? -45.729 25.538 -38.587 1.00 13.27 ? 87   TYR B CA  1 
ATOM   3156 C C   . TYR B 1 88  ? -44.514 24.653 -38.813 1.00 16.11 ? 87   TYR B C   1 
ATOM   3157 O O   . TYR B 1 88  ? -44.394 23.579 -38.220 1.00 15.38 ? 87   TYR B O   1 
ATOM   3158 C CB  . TYR B 1 88  ? -45.498 26.412 -37.349 1.00 14.40 ? 87   TYR B CB  1 
ATOM   3159 C CG  . TYR B 1 88  ? -46.469 27.570 -37.200 1.00 14.94 ? 87   TYR B CG  1 
ATOM   3160 C CD1 . TYR B 1 88  ? -47.748 27.366 -36.673 1.00 18.60 ? 87   TYR B CD1 1 
ATOM   3161 C CD2 . TYR B 1 88  ? -46.091 28.874 -37.544 1.00 14.58 ? 87   TYR B CD2 1 
ATOM   3162 C CE1 . TYR B 1 88  ? -48.629 28.413 -36.523 1.00 15.90 ? 87   TYR B CE1 1 
ATOM   3163 C CE2 . TYR B 1 88  ? -46.971 29.940 -37.401 1.00 18.18 ? 87   TYR B CE2 1 
ATOM   3164 C CZ  . TYR B 1 88  ? -48.239 29.701 -36.868 1.00 19.41 ? 87   TYR B CZ  1 
ATOM   3165 O OH  . TYR B 1 88  ? -49.136 30.736 -36.707 1.00 20.78 ? 87   TYR B OH  1 
ATOM   3166 N N   . ALA B 1 89  ? -43.609 25.123 -39.674 1.00 13.37 ? 88   ALA B N   1 
ATOM   3167 C CA  . ALA B 1 89  ? -42.385 24.416 -40.021 1.00 13.08 ? 88   ALA B CA  1 
ATOM   3168 C C   . ALA B 1 89  ? -41.210 25.297 -39.642 1.00 13.27 ? 88   ALA B C   1 
ATOM   3169 O O   . ALA B 1 89  ? -41.089 26.410 -40.163 1.00 14.72 ? 88   ALA B O   1 
ATOM   3170 C CB  . ALA B 1 89  ? -42.341 24.091 -41.527 1.00 13.46 ? 88   ALA B CB  1 
ATOM   3171 N N   . VAL B 1 90  ? -40.345 24.800 -38.751 1.00 13.80 ? 89   VAL B N   1 
ATOM   3172 C CA  . VAL B 1 90  ? -39.162 25.536 -38.312 1.00 13.43 ? 89   VAL B CA  1 
ATOM   3173 C C   . VAL B 1 90  ? -37.973 25.083 -39.136 1.00 13.80 ? 89   VAL B C   1 
ATOM   3174 O O   . VAL B 1 90  ? -37.617 23.896 -39.138 1.00 15.63 ? 89   VAL B O   1 
ATOM   3175 C CB  . VAL B 1 90  ? -38.876 25.335 -36.816 1.00 14.25 ? 89   VAL B CB  1 
ATOM   3176 C CG1 . VAL B 1 90  ? -37.716 26.241 -36.398 1.00 15.35 ? 89   VAL B CG1 1 
ATOM   3177 C CG2 . VAL B 1 90  ? -40.121 25.597 -35.963 1.00 13.90 ? 89   VAL B CG2 1 
ATOM   3178 N N   . VAL B 1 91  ? -37.352 26.039 -39.819 1.00 14.30 ? 90   VAL B N   1 
ATOM   3179 C CA  . VAL B 1 91  ? -36.206 25.792 -40.684 1.00 13.66 ? 90   VAL B CA  1 
ATOM   3180 C C   . VAL B 1 91  ? -34.970 25.969 -39.810 1.00 16.39 ? 90   VAL B C   1 
ATOM   3181 O O   . VAL B 1 91  ? -34.642 27.095 -39.428 1.00 16.72 ? 90   VAL B O   1 
ATOM   3182 C CB  . VAL B 1 91  ? -36.213 26.764 -41.870 1.00 13.70 ? 90   VAL B CB  1 
ATOM   3183 C CG1 . VAL B 1 91  ? -34.952 26.646 -42.673 1.00 20.96 ? 90   VAL B CG1 1 
ATOM   3184 C CG2 . VAL B 1 91  ? -37.416 26.465 -42.784 1.00 17.28 ? 90   VAL B CG2 1 
ATOM   3185 N N   . ASP B 1 92  ? -34.308 24.861 -39.465 1.00 12.06 ? 91   ASP B N   1 
ATOM   3186 C CA  . ASP B 1 92  ? -33.244 24.847 -38.450 1.00 13.25 ? 91   ASP B CA  1 
ATOM   3187 C C   . ASP B 1 92  ? -31.896 24.478 -39.053 1.00 14.32 ? 91   ASP B C   1 
ATOM   3188 O O   . ASP B 1 92  ? -31.618 23.285 -39.257 1.00 14.98 ? 91   ASP B O   1 
ATOM   3189 C CB  . ASP B 1 92  ? -33.620 23.850 -37.352 1.00 14.93 ? 91   ASP B CB  1 
ATOM   3190 C CG  . ASP B 1 92  ? -32.432 23.405 -36.495 1.00 17.50 ? 91   ASP B CG  1 
ATOM   3191 O OD1 . ASP B 1 92  ? -31.480 24.194 -36.290 1.00 15.62 ? 91   ASP B OD1 1 
ATOM   3192 O OD2 . ASP B 1 92  ? -32.463 22.240 -36.020 1.00 16.51 ? 91   ASP B OD2 1 
ATOM   3193 N N   . PRO B 1 93  ? -31.008 25.452 -39.347 1.00 14.17 ? 92   PRO B N   1 
ATOM   3194 C CA  . PRO B 1 93  ? -29.627 25.094 -39.690 1.00 14.50 ? 92   PRO B CA  1 
ATOM   3195 C C   . PRO B 1 93  ? -28.939 24.594 -38.429 1.00 14.34 ? 92   PRO B C   1 
ATOM   3196 O O   . PRO B 1 93  ? -28.643 25.362 -37.500 1.00 15.55 ? 92   PRO B O   1 
ATOM   3197 C CB  . PRO B 1 93  ? -29.020 26.409 -40.208 1.00 14.75 ? 92   PRO B CB  1 
ATOM   3198 C CG  . PRO B 1 93  ? -30.106 27.492 -39.987 1.00 14.16 ? 92   PRO B CG  1 
ATOM   3199 C CD  . PRO B 1 93  ? -31.121 26.880 -39.051 1.00 17.97 ? 92   PRO B CD  1 
ATOM   3200 N N   . HIS B 1 94  ? -28.739 23.280 -38.372 1.00 13.72 ? 93   HIS B N   1 
ATOM   3201 C CA  . HIS B 1 94  ? -28.391 22.580 -37.136 1.00 14.92 ? 93   HIS B CA  1 
ATOM   3202 C C   . HIS B 1 94  ? -26.869 22.582 -36.954 1.00 16.03 ? 93   HIS B C   1 
ATOM   3203 O O   . HIS B 1 94  ? -26.200 21.547 -36.958 1.00 16.99 ? 93   HIS B O   1 
ATOM   3204 C CB  . HIS B 1 94  ? -28.965 21.166 -37.176 1.00 17.13 ? 93   HIS B CB  1 
ATOM   3205 C CG  . HIS B 1 94  ? -29.232 20.580 -35.829 1.00 15.32 ? 93   HIS B CG  1 
ATOM   3206 N ND1 . HIS B 1 94  ? -30.336 20.917 -35.075 1.00 14.91 ? 93   HIS B ND1 1 
ATOM   3207 C CD2 . HIS B 1 94  ? -28.543 19.667 -35.103 1.00 18.77 ? 93   HIS B CD2 1 
ATOM   3208 C CE1 . HIS B 1 94  ? -30.310 20.243 -33.936 1.00 15.28 ? 93   HIS B CE1 1 
ATOM   3209 N NE2 . HIS B 1 94  ? -29.239 19.470 -33.931 1.00 15.88 ? 93   HIS B NE2 1 
ATOM   3210 N N   . ASN B 1 95  ? -26.321 23.790 -36.807 1.00 13.84 ? 94   ASN B N   1 
ATOM   3211 C CA  . ASN B 1 95  ? -24.904 23.999 -37.094 1.00 14.81 ? 94   ASN B CA  1 
ATOM   3212 C C   . ASN B 1 95  ? -24.053 24.524 -35.945 1.00 17.42 ? 94   ASN B C   1 
ATOM   3213 O O   . ASN B 1 95  ? -22.843 24.673 -36.126 1.00 15.29 ? 94   ASN B O   1 
ATOM   3214 C CB  . ASN B 1 95  ? -24.749 24.945 -38.282 1.00 13.80 ? 94   ASN B CB  1 
ATOM   3215 C CG  . ASN B 1 95  ? -24.682 24.196 -39.582 1.00 16.79 ? 94   ASN B CG  1 
ATOM   3216 O OD1 . ASN B 1 95  ? -25.700 23.721 -40.095 1.00 15.21 ? 94   ASN B OD1 1 
ATOM   3217 N ND2 . ASN B 1 95  ? -23.479 24.053 -40.108 1.00 16.63 ? 94   ASN B ND2 1 
ATOM   3218 N N   . TYR B 1 96  ? -24.620 24.796 -34.776 1.00 14.39 ? 95   TYR B N   1 
ATOM   3219 C CA  . TYR B 1 96  ? -23.807 25.088 -33.592 1.00 14.83 ? 95   TYR B CA  1 
ATOM   3220 C C   . TYR B 1 96  ? -22.968 26.354 -33.765 1.00 14.74 ? 95   TYR B C   1 
ATOM   3221 O O   . TYR B 1 96  ? -21.892 26.497 -33.160 1.00 16.44 ? 95   TYR B O   1 
ATOM   3222 C CB  . TYR B 1 96  ? -22.931 23.878 -33.232 1.00 16.17 ? 95   TYR B CB  1 
ATOM   3223 C CG  . TYR B 1 96  ? -23.755 22.633 -33.003 1.00 19.53 ? 95   TYR B CG  1 
ATOM   3224 C CD1 . TYR B 1 96  ? -24.418 22.427 -31.794 1.00 17.68 ? 95   TYR B CD1 1 
ATOM   3225 C CD2 . TYR B 1 96  ? -23.894 21.670 -34.002 1.00 20.34 ? 95   TYR B CD2 1 
ATOM   3226 C CE1 . TYR B 1 96  ? -25.191 21.287 -31.579 1.00 17.89 ? 95   TYR B CE1 1 
ATOM   3227 C CE2 . TYR B 1 96  ? -24.660 20.535 -33.798 1.00 21.78 ? 95   TYR B CE2 1 
ATOM   3228 C CZ  . TYR B 1 96  ? -25.307 20.346 -32.588 1.00 19.92 ? 95   TYR B CZ  1 
ATOM   3229 O OH  . TYR B 1 96  ? -26.055 19.203 -32.375 1.00 22.34 ? 95   TYR B OH  1 
ATOM   3230 N N   . GLY B 1 97  ? -23.458 27.286 -34.586 1.00 15.23 ? 96   GLY B N   1 
ATOM   3231 C CA  . GLY B 1 97  ? -22.740 28.514 -34.858 1.00 15.75 ? 96   GLY B CA  1 
ATOM   3232 C C   . GLY B 1 97  ? -21.478 28.309 -35.656 1.00 14.04 ? 96   GLY B C   1 
ATOM   3233 O O   . GLY B 1 97  ? -20.586 29.159 -35.615 1.00 15.88 ? 96   GLY B O   1 
ATOM   3234 N N   . ARG B 1 98  ? -21.382 27.190 -36.365 1.00 14.30 ? 97   ARG B N   1 
ATOM   3235 C CA  . ARG B 1 98  ? -20.160 26.795 -37.051 1.00 15.94 ? 97   ARG B CA  1 
ATOM   3236 C C   . ARG B 1 98  ? -20.484 26.343 -38.467 1.00 15.20 ? 97   ARG B C   1 
ATOM   3237 O O   . ARG B 1 98  ? -21.585 25.866 -38.754 1.00 16.54 ? 97   ARG B O   1 
ATOM   3238 C CB  . ARG B 1 98  ? -19.434 25.679 -36.278 1.00 14.03 ? 97   ARG B CB  1 
ATOM   3239 C CG  . ARG B 1 98  ? -18.789 26.183 -34.973 1.00 15.71 ? 97   ARG B CG  1 
ATOM   3240 C CD  . ARG B 1 98  ? -18.619 25.094 -33.937 1.00 20.54 ? 97   ARG B CD  1 
ATOM   3241 N NE  . ARG B 1 98  ? -17.769 25.568 -32.844 1.00 15.04 ? 97   ARG B NE  1 
ATOM   3242 C CZ  . ARG B 1 98  ? -18.189 26.317 -31.833 1.00 16.63 ? 97   ARG B CZ  1 
ATOM   3243 N NH1 . ARG B 1 98  ? -19.444 26.738 -31.751 1.00 17.25 ? 97   ARG B NH1 1 
ATOM   3244 N NH2 . ARG B 1 98  ? -17.323 26.661 -30.877 1.00 16.51 ? 97   ARG B NH2 1 
ATOM   3245 N N   . TYR B 1 99  ? -19.499 26.497 -39.345 1.00 16.37 ? 98   TYR B N   1 
ATOM   3246 C CA  . TYR B 1 99  ? -19.648 26.214 -40.767 1.00 16.34 ? 98   TYR B CA  1 
ATOM   3247 C C   . TYR B 1 99  ? -18.357 25.527 -41.179 1.00 17.84 ? 98   TYR B C   1 
ATOM   3248 O O   . TYR B 1 99  ? -17.275 26.097 -40.990 1.00 16.97 ? 98   TYR B O   1 
ATOM   3249 C CB  . TYR B 1 99  ? -19.892 27.513 -41.545 1.00 13.85 ? 98   TYR B CB  1 
ATOM   3250 C CG  . TYR B 1 99  ? -20.194 27.372 -43.031 1.00 13.88 ? 98   TYR B CG  1 
ATOM   3251 C CD1 . TYR B 1 99  ? -21.416 26.876 -43.475 1.00 14.62 ? 98   TYR B CD1 1 
ATOM   3252 C CD2 . TYR B 1 99  ? -19.263 27.766 -43.980 1.00 16.99 ? 98   TYR B CD2 1 
ATOM   3253 C CE1 . TYR B 1 99  ? -21.689 26.759 -44.839 1.00 16.72 ? 98   TYR B CE1 1 
ATOM   3254 C CE2 . TYR B 1 99  ? -19.529 27.670 -45.345 1.00 17.09 ? 98   TYR B CE2 1 
ATOM   3255 C CZ  . TYR B 1 99  ? -20.742 27.168 -45.767 1.00 16.85 ? 98   TYR B CZ  1 
ATOM   3256 O OH  . TYR B 1 99  ? -21.006 27.067 -47.129 1.00 16.88 ? 98   TYR B OH  1 
ATOM   3257 N N   . TYR B 1 100 ? -18.469 24.279 -41.648 1.00 16.73 ? 99   TYR B N   1 
ATOM   3258 C CA  . TYR B 1 100 ? -17.308 23.394 -41.829 1.00 15.99 ? 99   TYR B CA  1 
ATOM   3259 C C   . TYR B 1 100 ? -16.482 23.337 -40.546 1.00 19.90 ? 99   TYR B C   1 
ATOM   3260 O O   . TYR B 1 100 ? -15.249 23.359 -40.560 1.00 19.84 ? 99   TYR B O   1 
ATOM   3261 C CB  . TYR B 1 100 ? -16.478 23.816 -43.046 1.00 18.26 ? 99   TYR B CB  1 
ATOM   3262 C CG  . TYR B 1 100 ? -17.232 23.570 -44.353 1.00 19.20 ? 99   TYR B CG  1 
ATOM   3263 C CD1 . TYR B 1 100 ? -17.265 22.300 -44.929 1.00 18.69 ? 99   TYR B CD1 1 
ATOM   3264 C CD2 . TYR B 1 100 ? -17.938 24.599 -44.988 1.00 17.70 ? 99   TYR B CD2 1 
ATOM   3265 C CE1 . TYR B 1 100 ? -17.957 22.062 -46.106 1.00 20.58 ? 99   TYR B CE1 1 
ATOM   3266 C CE2 . TYR B 1 100 ? -18.646 24.367 -46.174 1.00 16.32 ? 99   TYR B CE2 1 
ATOM   3267 C CZ  . TYR B 1 100 ? -18.643 23.095 -46.719 1.00 20.22 ? 99   TYR B CZ  1 
ATOM   3268 O OH  . TYR B 1 100 ? -19.321 22.833 -47.886 1.00 17.56 ? 99   TYR B OH  1 
ATOM   3269 N N   . ASN B 1 101 ? -17.212 23.264 -39.428 1.00 17.12 ? 100  ASN B N   1 
ATOM   3270 C CA  A ASN B 1 101 ? -16.709 23.162 -38.050 0.58 20.92 ? 100  ASN B CA  1 
ATOM   3271 C CA  B ASN B 1 101 ? -16.662 23.129 -38.081 0.42 20.90 ? 100  ASN B CA  1 
ATOM   3272 C C   . ASN B 1 101 ? -15.803 24.322 -37.655 1.00 24.44 ? 100  ASN B C   1 
ATOM   3273 O O   . ASN B 1 101 ? -15.013 24.204 -36.720 1.00 22.30 ? 100  ASN B O   1 
ATOM   3274 C CB  A ASN B 1 101 ? -15.998 21.828 -37.776 0.58 21.72 ? 100  ASN B CB  1 
ATOM   3275 C CB  B ASN B 1 101 ? -15.877 21.817 -37.941 0.42 21.37 ? 100  ASN B CB  1 
ATOM   3276 C CG  A ASN B 1 101 ? -16.018 21.452 -36.278 0.58 23.95 ? 100  ASN B CG  1 
ATOM   3277 C CG  B ASN B 1 101 ? -16.785 20.594 -37.930 0.42 23.82 ? 100  ASN B CG  1 
ATOM   3278 O OD1 A ASN B 1 101 ? -17.017 21.676 -35.577 0.58 22.79 ? 100  ASN B OD1 1 
ATOM   3279 O OD1 B ASN B 1 101 ? -16.655 19.702 -38.766 0.42 34.88 ? 100  ASN B OD1 1 
ATOM   3280 N ND2 A ASN B 1 101 ? -14.909 20.909 -35.785 0.58 25.53 ? 100  ASN B ND2 1 
ATOM   3281 N ND2 B ASN B 1 101 ? -17.708 20.548 -36.975 0.42 27.18 ? 100  ASN B ND2 1 
ATOM   3282 N N   . SER B 1 102 ? -15.929 25.472 -38.315 1.00 18.72 ? 101  SER B N   1 
ATOM   3283 C CA  . SER B 1 102 ? -15.281 26.707 -37.882 1.00 18.38 ? 101  SER B CA  1 
ATOM   3284 C C   . SER B 1 102 ? -16.332 27.716 -37.424 1.00 18.03 ? 101  SER B C   1 
ATOM   3285 O O   . SER B 1 102 ? -17.376 27.867 -38.062 1.00 17.26 ? 101  SER B O   1 
ATOM   3286 C CB  . SER B 1 102 ? -14.447 27.325 -39.004 1.00 21.19 ? 101  SER B CB  1 
ATOM   3287 O OG  . SER B 1 102 ? -13.299 26.534 -39.261 1.00 25.81 ? 101  SER B OG  1 
ATOM   3288 N N   . ILE B 1 103 ? -16.043 28.435 -36.336 1.00 18.16 ? 102  ILE B N   1 
ATOM   3289 C CA  . ILE B 1 103 ? -16.977 29.448 -35.855 1.00 15.21 ? 102  ILE B CA  1 
ATOM   3290 C C   . ILE B 1 103 ? -17.320 30.427 -36.970 1.00 17.84 ? 102  ILE B C   1 
ATOM   3291 O O   . ILE B 1 103 ? -16.441 30.904 -37.700 1.00 18.56 ? 102  ILE B O   1 
ATOM   3292 C CB  . ILE B 1 103 ? -16.376 30.168 -34.635 1.00 17.88 ? 102  ILE B CB  1 
ATOM   3293 C CG1 . ILE B 1 103 ? -16.362 29.209 -33.446 1.00 18.03 ? 102  ILE B CG1 1 
ATOM   3294 C CG2 . ILE B 1 103 ? -17.144 31.457 -34.323 1.00 21.38 ? 102  ILE B CG2 1 
ATOM   3295 C CD1 . ILE B 1 103 ? -15.480 29.697 -32.282 1.00 22.38 ? 102  ILE B CD1 1 
ATOM   3296 N N   . ILE B 1 104 ? -18.612 30.712 -37.121 1.00 17.35 ? 103  ILE B N   1 
ATOM   3297 C CA  . ILE B 1 104 ? -19.064 31.721 -38.069 1.00 16.31 ? 103  ILE B CA  1 
ATOM   3298 C C   . ILE B 1 104 ? -18.722 33.093 -37.509 1.00 17.03 ? 103  ILE B C   1 
ATOM   3299 O O   . ILE B 1 104 ? -19.372 33.578 -36.574 1.00 19.63 ? 103  ILE B O   1 
ATOM   3300 C CB  . ILE B 1 104 ? -20.567 31.583 -38.341 1.00 15.45 ? 103  ILE B CB  1 
ATOM   3301 C CG1 . ILE B 1 104 ? -20.872 30.202 -38.916 1.00 17.12 ? 103  ILE B CG1 1 
ATOM   3302 C CG2 . ILE B 1 104 ? -21.055 32.701 -39.286 1.00 19.57 ? 103  ILE B CG2 1 
ATOM   3303 C CD1 . ILE B 1 104 ? -22.344 29.860 -38.915 1.00 17.45 ? 103  ILE B CD1 1 
ATOM   3304 N N   . SER B 1 105 ? -17.690 33.722 -38.059 1.00 19.44 ? 104  SER B N   1 
ATOM   3305 C CA  . SER B 1 105 ? -17.195 34.971 -37.506 1.00 19.90 ? 104  SER B CA  1 
ATOM   3306 C C   . SER B 1 105 ? -17.576 36.195 -38.325 1.00 21.44 ? 104  SER B C   1 
ATOM   3307 O O   . SER B 1 105 ? -17.234 37.316 -37.924 1.00 20.89 ? 104  SER B O   1 
ATOM   3308 C CB  . SER B 1 105 ? -15.674 34.898 -37.359 1.00 22.58 ? 104  SER B CB  1 
ATOM   3309 O OG  . SER B 1 105 ? -15.103 34.650 -38.620 1.00 24.71 ? 104  SER B OG  1 
ATOM   3310 N N   . SER B 1 106 ? -18.303 36.017 -39.439 1.00 18.63 ? 105  SER B N   1 
ATOM   3311 C CA  . SER B 1 106 ? -18.695 37.109 -40.326 1.00 18.70 ? 105  SER B CA  1 
ATOM   3312 C C   . SER B 1 106 ? -20.196 37.322 -40.270 1.00 17.41 ? 105  SER B C   1 
ATOM   3313 O O   . SER B 1 106 ? -20.944 36.594 -40.943 1.00 16.65 ? 105  SER B O   1 
ATOM   3314 C CB  . SER B 1 106 ? -18.279 36.809 -41.767 1.00 17.58 ? 105  SER B CB  1 
ATOM   3315 O OG  . SER B 1 106 ? -18.848 37.753 -42.654 1.00 20.59 ? 105  SER B OG  1 
ATOM   3316 N N   . PRO B 1 107 ? -20.686 38.295 -39.504 1.00 17.08 ? 106  PRO B N   1 
ATOM   3317 C CA  . PRO B 1 107 ? -22.128 38.580 -39.542 1.00 16.08 ? 106  PRO B CA  1 
ATOM   3318 C C   . PRO B 1 107 ? -22.619 38.908 -40.948 1.00 17.04 ? 106  PRO B C   1 
ATOM   3319 O O   . PRO B 1 107 ? -23.742 38.524 -41.313 1.00 19.58 ? 106  PRO B O   1 
ATOM   3320 C CB  . PRO B 1 107 ? -22.267 39.766 -38.576 1.00 20.06 ? 106  PRO B CB  1 
ATOM   3321 C CG  . PRO B 1 107 ? -21.125 39.574 -37.603 1.00 21.84 ? 106  PRO B CG  1 
ATOM   3322 C CD  . PRO B 1 107 ? -19.992 39.074 -38.462 1.00 19.70 ? 106  PRO B CD  1 
ATOM   3323 N N   . SER B 1 108 ? -21.802 39.586 -41.760 1.00 17.57 ? 107  SER B N   1 
ATOM   3324 C CA  A SER B 1 108 ? -22.256 39.930 -43.104 0.47 19.21 ? 107  SER B CA  1 
ATOM   3325 C CA  B SER B 1 108 ? -22.247 39.930 -43.106 0.53 19.20 ? 107  SER B CA  1 
ATOM   3326 C C   . SER B 1 108 ? -22.455 38.679 -43.960 1.00 19.07 ? 107  SER B C   1 
ATOM   3327 O O   . SER B 1 108 ? -23.443 38.584 -44.703 1.00 18.59 ? 107  SER B O   1 
ATOM   3328 C CB  A SER B 1 108 ? -21.283 40.913 -43.767 0.47 22.16 ? 107  SER B CB  1 
ATOM   3329 C CB  B SER B 1 108 ? -21.249 40.882 -43.761 0.53 22.19 ? 107  SER B CB  1 
ATOM   3330 O OG  A SER B 1 108 ? -20.053 40.304 -44.122 0.47 25.73 ? 107  SER B OG  1 
ATOM   3331 O OG  B SER B 1 108 ? -21.707 41.278 -45.037 0.53 22.31 ? 107  SER B OG  1 
ATOM   3332 N N   . ASP B 1 109 ? -21.538 37.701 -43.873 1.00 17.06 ? 108  ASP B N   1 
ATOM   3333 C CA  . ASP B 1 109 ? -21.719 36.463 -44.636 1.00 17.00 ? 108  ASP B CA  1 
ATOM   3334 C C   . ASP B 1 109 ? -22.960 35.721 -44.156 1.00 18.13 ? 108  ASP B C   1 
ATOM   3335 O O   . ASP B 1 109 ? -23.708 35.145 -44.955 1.00 17.90 ? 108  ASP B O   1 
ATOM   3336 C CB  . ASP B 1 109 ? -20.507 35.531 -44.501 1.00 17.15 ? 108  ASP B CB  1 
ATOM   3337 C CG  . ASP B 1 109 ? -19.273 36.027 -45.221 1.00 23.42 ? 108  ASP B CG  1 
ATOM   3338 O OD1 . ASP B 1 109 ? -19.322 37.045 -45.942 1.00 23.67 ? 108  ASP B OD1 1 
ATOM   3339 O OD2 . ASP B 1 109 ? -18.233 35.360 -45.044 1.00 24.90 ? 108  ASP B OD2 1 
ATOM   3340 N N   . PHE B 1 110 ? -23.177 35.717 -42.840 1.00 16.25 ? 109  PHE B N   1 
ATOM   3341 C CA  . PHE B 1 110 ? -24.328 35.032 -42.263 1.00 15.22 ? 109  PHE B CA  1 
ATOM   3342 C C   . PHE B 1 110 ? -25.615 35.704 -42.683 1.00 16.46 ? 109  PHE B C   1 
ATOM   3343 O O   . PHE B 1 110 ? -26.612 35.028 -42.946 1.00 15.24 ? 109  PHE B O   1 
ATOM   3344 C CB  . PHE B 1 110 ? -24.191 35.033 -40.740 1.00 13.50 ? 109  PHE B CB  1 
ATOM   3345 C CG  . PHE B 1 110 ? -25.062 34.033 -40.015 1.00 12.75 ? 109  PHE B CG  1 
ATOM   3346 C CD1 . PHE B 1 110 ? -25.047 32.687 -40.347 1.00 13.50 ? 109  PHE B CD1 1 
ATOM   3347 C CD2 . PHE B 1 110 ? -25.811 34.434 -38.900 1.00 15.10 ? 109  PHE B CD2 1 
ATOM   3348 C CE1 . PHE B 1 110 ? -25.816 31.756 -39.622 1.00 15.51 ? 109  PHE B CE1 1 
ATOM   3349 C CE2 . PHE B 1 110 ? -26.564 33.503 -38.161 1.00 14.23 ? 109  PHE B CE2 1 
ATOM   3350 C CZ  . PHE B 1 110 ? -26.558 32.166 -38.522 1.00 15.38 ? 109  PHE B CZ  1 
ATOM   3351 N N   . GLN B 1 111 ? -25.602 37.036 -42.767 1.00 17.29 ? 110  GLN B N   1 
ATOM   3352 C CA  . GLN B 1 111 ? -26.774 37.757 -43.247 1.00 16.64 ? 110  GLN B CA  1 
ATOM   3353 C C   . GLN B 1 111 ? -27.100 37.370 -44.684 1.00 17.43 ? 110  GLN B C   1 
ATOM   3354 O O   . GLN B 1 111 ? -28.270 37.176 -45.023 1.00 17.97 ? 110  GLN B O   1 
ATOM   3355 C CB  . GLN B 1 111 ? -26.549 39.268 -43.127 1.00 17.76 ? 110  GLN B CB  1 
ATOM   3356 C CG  . GLN B 1 111 ? -27.732 40.071 -43.641 1.00 15.72 ? 110  GLN B CG  1 
ATOM   3357 C CD  . GLN B 1 111 ? -27.725 41.542 -43.239 1.00 20.87 ? 110  GLN B CD  1 
ATOM   3358 O OE1 . GLN B 1 111 ? -26.948 41.977 -42.378 1.00 22.55 ? 110  GLN B OE1 1 
ATOM   3359 N NE2 . GLN B 1 111 ? -28.622 42.315 -43.853 1.00 18.79 ? 110  GLN B NE2 1 
ATOM   3360 N N   . THR B 1 112 ? -26.079 37.260 -45.549 1.00 16.79 ? 111  THR B N   1 
ATOM   3361 C CA  . THR B 1 112 ? -26.345 36.831 -46.924 1.00 16.33 ? 111  THR B CA  1 
ATOM   3362 C C   . THR B 1 112 ? -26.921 35.420 -46.965 1.00 16.23 ? 111  THR B C   1 
ATOM   3363 O O   . THR B 1 112 ? -27.875 35.153 -47.711 1.00 15.58 ? 111  THR B O   1 
ATOM   3364 C CB  . THR B 1 112 ? -25.067 36.921 -47.754 1.00 18.77 ? 111  THR B CB  1 
ATOM   3365 O OG1 . THR B 1 112 ? -24.661 38.292 -47.808 1.00 22.95 ? 111  THR B OG1 1 
ATOM   3366 C CG2 . THR B 1 112 ? -25.309 36.410 -49.191 1.00 19.16 ? 111  THR B CG2 1 
ATOM   3367 N N   . PHE B 1 113 ? -26.345 34.498 -46.186 1.00 15.41 ? 112  PHE B N   1 
ATOM   3368 C CA  . PHE B 1 113 ? -26.924 33.160 -46.077 1.00 15.40 ? 112  PHE B CA  1 
ATOM   3369 C C   . PHE B 1 113 ? -28.412 33.242 -45.742 1.00 16.00 ? 112  PHE B C   1 
ATOM   3370 O O   . PHE B 1 113 ? -29.248 32.575 -46.360 1.00 15.76 ? 112  PHE B O   1 
ATOM   3371 C CB  . PHE B 1 113 ? -26.163 32.345 -45.017 1.00 15.64 ? 112  PHE B CB  1 
ATOM   3372 C CG  . PHE B 1 113 ? -26.816 31.022 -44.665 1.00 13.86 ? 112  PHE B CG  1 
ATOM   3373 C CD1 . PHE B 1 113 ? -26.563 29.880 -45.414 1.00 14.88 ? 112  PHE B CD1 1 
ATOM   3374 C CD2 . PHE B 1 113 ? -27.686 30.924 -43.570 1.00 12.99 ? 112  PHE B CD2 1 
ATOM   3375 C CE1 . PHE B 1 113 ? -27.176 28.650 -45.073 1.00 14.26 ? 112  PHE B CE1 1 
ATOM   3376 C CE2 . PHE B 1 113 ? -28.324 29.713 -43.250 1.00 14.36 ? 112  PHE B CE2 1 
ATOM   3377 C CZ  . PHE B 1 113 ? -28.051 28.572 -43.992 1.00 16.66 ? 112  PHE B CZ  1 
ATOM   3378 N N   . TRP B 1 114 ? -28.764 34.078 -44.767 1.00 15.17 ? 113  TRP B N   1 
ATOM   3379 C CA  . TRP B 1 114 ? -30.151 34.127 -44.338 1.00 13.67 ? 113  TRP B CA  1 
ATOM   3380 C C   . TRP B 1 114 ? -31.058 34.840 -45.338 1.00 13.28 ? 113  TRP B C   1 
ATOM   3381 O O   . TRP B 1 114 ? -32.233 34.478 -45.447 1.00 13.35 ? 113  TRP B O   1 
ATOM   3382 C CB  . TRP B 1 114 ? -30.218 34.747 -42.934 1.00 12.12 ? 113  TRP B CB  1 
ATOM   3383 C CG  . TRP B 1 114 ? -30.203 33.627 -41.913 1.00 14.22 ? 113  TRP B CG  1 
ATOM   3384 C CD1 . TRP B 1 114 ? -29.221 33.314 -41.011 1.00 13.44 ? 113  TRP B CD1 1 
ATOM   3385 C CD2 . TRP B 1 114 ? -31.210 32.626 -41.784 1.00 14.45 ? 113  TRP B CD2 1 
ATOM   3386 N NE1 . TRP B 1 114 ? -29.584 32.183 -40.300 1.00 13.78 ? 113  TRP B NE1 1 
ATOM   3387 C CE2 . TRP B 1 114 ? -30.800 31.738 -40.770 1.00 13.19 ? 113  TRP B CE2 1 
ATOM   3388 C CE3 . TRP B 1 114 ? -32.429 32.393 -42.440 1.00 15.46 ? 113  TRP B CE3 1 
ATOM   3389 C CZ2 . TRP B 1 114 ? -31.584 30.648 -40.375 1.00 15.02 ? 113  TRP B CZ2 1 
ATOM   3390 C CZ3 . TRP B 1 114 ? -33.202 31.314 -42.050 1.00 14.68 ? 113  TRP B CZ3 1 
ATOM   3391 C CH2 . TRP B 1 114 ? -32.779 30.455 -41.030 1.00 15.26 ? 113  TRP B CH2 1 
ATOM   3392 N N   . LYS B 1 115 ? -30.564 35.841 -46.076 1.00 14.18 ? 114  LYS B N   1 
ATOM   3393 C CA  . LYS B 1 115 ? -31.385 36.371 -47.162 1.00 14.17 ? 114  LYS B CA  1 
ATOM   3394 C C   . LYS B 1 115 ? -31.659 35.282 -48.192 1.00 13.72 ? 114  LYS B C   1 
ATOM   3395 O O   . LYS B 1 115 ? -32.788 35.142 -48.672 1.00 15.45 ? 114  LYS B O   1 
ATOM   3396 C CB  . LYS B 1 115 ? -30.712 37.587 -47.824 1.00 14.60 ? 114  LYS B CB  1 
ATOM   3397 C CG  . LYS B 1 115 ? -31.659 38.276 -48.818 1.00 16.86 ? 114  LYS B CG  1 
ATOM   3398 C CD  . LYS B 1 115 ? -31.022 39.425 -49.619 1.00 19.07 ? 114  LYS B CD  1 
ATOM   3399 C CE  . LYS B 1 115 ? -32.040 39.952 -50.627 1.00 26.57 ? 114  LYS B CE  1 
ATOM   3400 N NZ  . LYS B 1 115 ? -31.418 40.826 -51.674 1.00 29.79 ? 114  LYS B NZ  1 
ATOM   3401 N N   . THR B 1 116 ? -30.634 34.487 -48.527 1.00 15.43 ? 115  THR B N   1 
ATOM   3402 C CA  . THR B 1 116 ? -30.812 33.374 -49.459 1.00 14.92 ? 115  THR B CA  1 
ATOM   3403 C C   . THR B 1 116 ? -31.885 32.401 -48.985 1.00 16.37 ? 115  THR B C   1 
ATOM   3404 O O   . THR B 1 116 ? -32.791 32.038 -49.751 1.00 17.42 ? 115  THR B O   1 
ATOM   3405 C CB  . THR B 1 116 ? -29.476 32.656 -49.643 1.00 15.01 ? 115  THR B CB  1 
ATOM   3406 O OG1 . THR B 1 116 ? -28.594 33.539 -50.328 1.00 17.12 ? 115  THR B OG1 1 
ATOM   3407 C CG2 . THR B 1 116 ? -29.656 31.374 -50.450 1.00 17.43 ? 115  THR B CG2 1 
ATOM   3408 N N   . VAL B 1 117 ? -31.800 31.963 -47.727 1.00 14.29 ? 116  VAL B N   1 
ATOM   3409 C CA  . VAL B 1 117 ? -32.748 30.968 -47.222 1.00 16.69 ? 116  VAL B CA  1 
ATOM   3410 C C   . VAL B 1 117 ? -34.155 31.554 -47.144 1.00 14.65 ? 116  VAL B C   1 
ATOM   3411 O O   . VAL B 1 117 ? -35.133 30.926 -47.575 1.00 14.00 ? 116  VAL B O   1 
ATOM   3412 C CB  . VAL B 1 117 ? -32.284 30.421 -45.860 1.00 15.31 ? 116  VAL B CB  1 
ATOM   3413 C CG1 . VAL B 1 117 ? -33.378 29.541 -45.238 1.00 17.11 ? 116  VAL B CG1 1 
ATOM   3414 C CG2 . VAL B 1 117 ? -30.967 29.660 -46.012 1.00 18.38 ? 116  VAL B CG2 1 
ATOM   3415 N N   . ALA B 1 118 ? -34.285 32.759 -46.572 1.00 15.12 ? 117  ALA B N   1 
ATOM   3416 C CA  . ALA B 1 118 ? -35.606 33.357 -46.391 1.00 13.02 ? 117  ALA B CA  1 
ATOM   3417 C C   . ALA B 1 118 ? -36.288 33.627 -47.717 1.00 16.29 ? 117  ALA B C   1 
ATOM   3418 O O   . ALA B 1 118 ? -37.524 33.583 -47.804 1.00 17.56 ? 117  ALA B O   1 
ATOM   3419 C CB  . ALA B 1 118 ? -35.495 34.662 -45.594 1.00 19.29 ? 117  ALA B CB  1 
ATOM   3420 N N   . SER B 1 119 ? -35.508 33.936 -48.757 1.00 15.73 ? 118  SER B N   1 
ATOM   3421 C CA  A SER B 1 119 ? -36.082 34.184 -50.074 0.49 14.50 ? 118  SER B CA  1 
ATOM   3422 C CA  B SER B 1 119 ? -36.132 34.202 -50.044 0.51 14.48 ? 118  SER B CA  1 
ATOM   3423 C C   . SER B 1 119 ? -36.807 32.966 -50.620 1.00 17.99 ? 118  SER B C   1 
ATOM   3424 O O   . SER B 1 119 ? -37.676 33.107 -51.485 1.00 21.99 ? 118  SER B O   1 
ATOM   3425 C CB  A SER B 1 119 ? -34.990 34.608 -51.058 0.49 18.26 ? 118  SER B CB  1 
ATOM   3426 C CB  B SER B 1 119 ? -35.107 34.754 -51.035 0.51 18.43 ? 118  SER B CB  1 
ATOM   3427 O OG  A SER B 1 119 ? -34.501 35.904 -50.763 0.49 18.76 ? 118  SER B OG  1 
ATOM   3428 O OG  B SER B 1 119 ? -34.196 33.754 -51.433 0.51 15.39 ? 118  SER B OG  1 
ATOM   3429 N N   . GLN B 1 120 ? -36.456 31.765 -50.148 1.00 16.18 ? 119  GLN B N   1 
ATOM   3430 C CA  . GLN B 1 120 ? -37.128 30.565 -50.635 1.00 17.50 ? 119  GLN B CA  1 
ATOM   3431 C C   . GLN B 1 120 ? -38.489 30.363 -49.991 1.00 16.32 ? 119  GLN B C   1 
ATOM   3432 O O   . GLN B 1 120 ? -39.266 29.532 -50.467 1.00 16.79 ? 119  GLN B O   1 
ATOM   3433 C CB  . GLN B 1 120 ? -36.282 29.313 -50.377 1.00 17.59 ? 119  GLN B CB  1 
ATOM   3434 C CG  . GLN B 1 120 ? -34.796 29.477 -50.610 1.00 19.96 ? 119  GLN B CG  1 
ATOM   3435 C CD  . GLN B 1 120 ? -34.496 29.751 -52.057 1.00 20.96 ? 119  GLN B CD  1 
ATOM   3436 O OE1 . GLN B 1 120 ? -35.208 29.278 -52.950 1.00 19.81 ? 119  GLN B OE1 1 
ATOM   3437 N NE2 . GLN B 1 120 ? -33.453 30.541 -52.307 1.00 23.55 ? 119  GLN B NE2 1 
ATOM   3438 N N   . PHE B 1 121 ? -38.787 31.089 -48.912 1.00 14.86 ? 120  PHE B N   1 
ATOM   3439 C CA  . PHE B 1 121 ? -40.015 30.876 -48.162 1.00 13.43 ? 120  PHE B CA  1 
ATOM   3440 C C   . PHE B 1 121 ? -40.736 32.185 -47.862 1.00 16.13 ? 120  PHE B C   1 
ATOM   3441 O O   . PHE B 1 121 ? -41.582 32.221 -46.970 1.00 15.44 ? 120  PHE B O   1 
ATOM   3442 C CB  . PHE B 1 121 ? -39.690 30.144 -46.858 1.00 16.71 ? 120  PHE B CB  1 
ATOM   3443 C CG  . PHE B 1 121 ? -39.081 28.788 -47.065 1.00 17.01 ? 120  PHE B CG  1 
ATOM   3444 C CD1 . PHE B 1 121 ? -39.874 27.726 -47.491 1.00 18.24 ? 120  PHE B CD1 1 
ATOM   3445 C CD2 . PHE B 1 121 ? -37.724 28.574 -46.865 1.00 16.64 ? 120  PHE B CD2 1 
ATOM   3446 C CE1 . PHE B 1 121 ? -39.333 26.472 -47.685 1.00 17.96 ? 120  PHE B CE1 1 
ATOM   3447 C CE2 . PHE B 1 121 ? -37.169 27.314 -47.054 1.00 18.16 ? 120  PHE B CE2 1 
ATOM   3448 C CZ  . PHE B 1 121 ? -37.972 26.260 -47.469 1.00 18.79 ? 120  PHE B CZ  1 
ATOM   3449 N N   . ALA B 1 122 ? -40.459 33.251 -48.621 1.00 15.52 ? 121  ALA B N   1 
ATOM   3450 C CA  . ALA B 1 122 ? -40.741 34.599 -48.126 1.00 17.59 ? 121  ALA B CA  1 
ATOM   3451 C C   . ALA B 1 122 ? -42.228 34.886 -47.997 1.00 18.00 ? 121  ALA B C   1 
ATOM   3452 O O   . ALA B 1 122 ? -42.614 35.733 -47.183 1.00 20.94 ? 121  ALA B O   1 
ATOM   3453 C CB  . ALA B 1 122 ? -40.094 35.644 -49.037 1.00 18.84 ? 121  ALA B CB  1 
ATOM   3454 N N   . SER B 1 123 ? -43.074 34.215 -48.777 1.00 16.14 ? 122  SER B N   1 
ATOM   3455 C CA  A SER B 1 123 ? -44.516 34.428 -48.786 0.58 20.41 ? 122  SER B CA  1 
ATOM   3456 C CA  B SER B 1 123 ? -44.502 34.501 -48.674 0.42 20.44 ? 122  SER B CA  1 
ATOM   3457 C C   . SER B 1 123 ? -45.277 33.399 -47.953 1.00 22.39 ? 122  SER B C   1 
ATOM   3458 O O   . SER B 1 123 ? -46.514 33.372 -47.998 1.00 24.48 ? 122  SER B O   1 
ATOM   3459 C CB  A SER B 1 123 ? -45.036 34.411 -50.228 0.58 24.09 ? 122  SER B CB  1 
ATOM   3460 C CB  B SER B 1 123 ? -45.079 34.782 -50.059 0.42 23.69 ? 122  SER B CB  1 
ATOM   3461 O OG  A SER B 1 123 ? -44.857 33.140 -50.842 0.58 22.00 ? 122  SER B OG  1 
ATOM   3462 O OG  B SER B 1 123 ? -44.558 36.018 -50.526 0.42 20.26 ? 122  SER B OG  1 
ATOM   3463 N N   . ASN B 1 124 ? -44.579 32.528 -47.231 1.00 19.23 ? 123  ASN B N   1 
ATOM   3464 C CA  . ASN B 1 124 ? -45.248 31.474 -46.481 1.00 15.94 ? 123  ASN B CA  1 
ATOM   3465 C C   . ASN B 1 124 ? -45.281 31.852 -45.003 1.00 18.14 ? 123  ASN B C   1 
ATOM   3466 O O   . ASN B 1 124 ? -44.248 31.755 -44.325 1.00 17.11 ? 123  ASN B O   1 
ATOM   3467 C CB  . ASN B 1 124 ? -44.517 30.149 -46.689 1.00 17.66 ? 123  ASN B CB  1 
ATOM   3468 C CG  . ASN B 1 124 ? -45.261 28.972 -46.098 1.00 18.41 ? 123  ASN B CG  1 
ATOM   3469 O OD1 . ASN B 1 124 ? -46.063 29.129 -45.167 1.00 18.08 ? 123  ASN B OD1 1 
ATOM   3470 N ND2 . ASN B 1 124 ? -45.004 27.775 -46.636 1.00 17.40 ? 123  ASN B ND2 1 
ATOM   3471 N N   . PRO B 1 125 ? -46.435 32.257 -44.456 1.00 18.65 ? 124  PRO B N   1 
ATOM   3472 C CA  . PRO B 1 125 ? -46.473 32.746 -43.075 1.00 17.86 ? 124  PRO B CA  1 
ATOM   3473 C C   . PRO B 1 125 ? -46.331 31.658 -42.032 1.00 18.09 ? 124  PRO B C   1 
ATOM   3474 O O   . PRO B 1 125 ? -46.179 31.990 -40.855 1.00 18.68 ? 124  PRO B O   1 
ATOM   3475 C CB  . PRO B 1 125 ? -47.848 33.421 -42.974 1.00 21.02 ? 124  PRO B CB  1 
ATOM   3476 C CG  . PRO B 1 125 ? -48.675 32.727 -44.009 1.00 24.40 ? 124  PRO B CG  1 
ATOM   3477 C CD  . PRO B 1 125 ? -47.742 32.373 -45.128 1.00 18.63 ? 124  PRO B CD  1 
ATOM   3478 N N   . LEU B 1 126 ? -46.403 30.384 -42.410 1.00 17.73 ? 125  LEU B N   1 
ATOM   3479 C CA  . LEU B 1 126 ? -46.294 29.292 -41.457 1.00 17.40 ? 125  LEU B CA  1 
ATOM   3480 C C   . LEU B 1 126 ? -44.879 28.745 -41.348 1.00 16.03 ? 125  LEU B C   1 
ATOM   3481 O O   . LEU B 1 126 ? -44.640 27.824 -40.565 1.00 16.46 ? 125  LEU B O   1 
ATOM   3482 C CB  . LEU B 1 126 ? -47.271 28.169 -41.822 1.00 18.14 ? 125  LEU B CB  1 
ATOM   3483 C CG  . LEU B 1 126 ? -48.750 28.522 -41.628 1.00 17.80 ? 125  LEU B CG  1 
ATOM   3484 C CD1 . LEU B 1 126 ? -49.633 27.393 -42.124 1.00 17.29 ? 125  LEU B CD1 1 
ATOM   3485 C CD2 . LEU B 1 126 ? -49.063 28.848 -40.151 1.00 19.81 ? 125  LEU B CD2 1 
ATOM   3486 N N   . VAL B 1 127 ? -43.929 29.297 -42.104 1.00 14.19 ? 126  VAL B N   1 
ATOM   3487 C CA  . VAL B 1 127 ? -42.526 28.963 -41.917 1.00 12.24 ? 126  VAL B CA  1 
ATOM   3488 C C   . VAL B 1 127 ? -41.980 29.797 -40.773 1.00 14.34 ? 126  VAL B C   1 
ATOM   3489 O O   . VAL B 1 127 ? -42.313 30.983 -40.645 1.00 16.99 ? 126  VAL B O   1 
ATOM   3490 C CB  . VAL B 1 127 ? -41.749 29.227 -43.217 1.00 12.18 ? 126  VAL B CB  1 
ATOM   3491 C CG1 . VAL B 1 127 ? -40.228 29.067 -43.021 1.00 16.14 ? 126  VAL B CG1 1 
ATOM   3492 C CG2 . VAL B 1 127 ? -42.241 28.279 -44.281 1.00 16.88 ? 126  VAL B CG2 1 
ATOM   3493 N N   . ILE B 1 128 ? -41.136 29.178 -39.942 1.00 12.93 ? 127  ILE B N   1 
ATOM   3494 C CA  . ILE B 1 128 ? -40.423 29.849 -38.859 1.00 12.84 ? 127  ILE B CA  1 
ATOM   3495 C C   . ILE B 1 128 ? -38.932 29.691 -39.121 1.00 12.87 ? 127  ILE B C   1 
ATOM   3496 O O   . ILE B 1 128 ? -38.466 28.584 -39.423 1.00 15.10 ? 127  ILE B O   1 
ATOM   3497 C CB  . ILE B 1 128 ? -40.796 29.262 -37.486 1.00 13.51 ? 127  ILE B CB  1 
ATOM   3498 C CG1 . ILE B 1 128 ? -42.258 29.535 -37.181 1.00 12.90 ? 127  ILE B CG1 1 
ATOM   3499 C CG2 . ILE B 1 128 ? -39.908 29.846 -36.396 1.00 13.70 ? 127  ILE B CG2 1 
ATOM   3500 C CD1 . ILE B 1 128 ? -42.756 28.755 -35.937 1.00 13.14 ? 127  ILE B CD1 1 
ATOM   3501 N N   . PHE B 1 129 ? -38.189 30.790 -39.036 1.00 13.04 ? 128  PHE B N   1 
ATOM   3502 C CA  . PHE B 1 129 ? -36.754 30.754 -39.304 1.00 14.35 ? 128  PHE B CA  1 
ATOM   3503 C C   . PHE B 1 129 ? -35.996 30.676 -37.989 1.00 13.12 ? 128  PHE B C   1 
ATOM   3504 O O   . PHE B 1 129 ? -36.244 31.481 -37.091 1.00 16.14 ? 128  PHE B O   1 
ATOM   3505 C CB  . PHE B 1 129 ? -36.300 31.986 -40.084 1.00 14.78 ? 128  PHE B CB  1 
ATOM   3506 C CG  . PHE B 1 129 ? -37.032 32.175 -41.365 1.00 14.70 ? 128  PHE B CG  1 
ATOM   3507 C CD1 . PHE B 1 129 ? -36.840 31.285 -42.406 1.00 13.97 ? 128  PHE B CD1 1 
ATOM   3508 C CD2 . PHE B 1 129 ? -37.933 33.223 -41.526 1.00 14.54 ? 128  PHE B CD2 1 
ATOM   3509 C CE1 . PHE B 1 129 ? -37.525 31.444 -43.620 1.00 12.78 ? 128  PHE B CE1 1 
ATOM   3510 C CE2 . PHE B 1 129 ? -38.617 33.391 -42.731 1.00 14.37 ? 128  PHE B CE2 1 
ATOM   3511 C CZ  . PHE B 1 129 ? -38.400 32.491 -43.771 1.00 14.16 ? 128  PHE B CZ  1 
ATOM   3512 N N   . ASP B 1 130 ? -35.075 29.717 -37.875 1.00 10.94 ? 129  ASP B N   1 
ATOM   3513 C CA  . ASP B 1 130 ? -34.345 29.462 -36.631 1.00 12.01 ? 129  ASP B CA  1 
ATOM   3514 C C   . ASP B 1 130 ? -32.882 29.797 -36.913 1.00 13.28 ? 129  ASP B C   1 
ATOM   3515 O O   . ASP B 1 130 ? -32.258 29.140 -37.744 1.00 14.41 ? 129  ASP B O   1 
ATOM   3516 C CB  . ASP B 1 130 ? -34.553 27.997 -36.243 1.00 12.28 ? 129  ASP B CB  1 
ATOM   3517 C CG  . ASP B 1 130 ? -33.995 27.650 -34.891 1.00 13.47 ? 129  ASP B CG  1 
ATOM   3518 O OD1 . ASP B 1 130 ? -33.041 28.322 -34.440 1.00 15.37 ? 129  ASP B OD1 1 
ATOM   3519 O OD2 . ASP B 1 130 ? -34.499 26.663 -34.317 1.00 14.81 ? 129  ASP B OD2 1 
ATOM   3520 N N   . THR B 1 131 ? -32.329 30.834 -36.258 1.00 12.64 ? 130  THR B N   1 
ATOM   3521 C CA  . THR B 1 131 ? -31.079 31.413 -36.775 1.00 11.68 ? 130  THR B CA  1 
ATOM   3522 C C   . THR B 1 131 ? -29.940 30.390 -36.830 1.00 14.10 ? 130  THR B C   1 
ATOM   3523 O O   . THR B 1 131 ? -29.202 30.344 -37.823 1.00 14.07 ? 130  THR B O   1 
ATOM   3524 C CB  . THR B 1 131 ? -30.639 32.656 -35.984 1.00 12.72 ? 130  THR B CB  1 
ATOM   3525 O OG1 . THR B 1 131 ? -30.216 32.283 -34.665 1.00 13.80 ? 130  THR B OG1 1 
ATOM   3526 C CG2 . THR B 1 131 ? -31.780 33.707 -35.864 1.00 11.38 ? 130  THR B CG2 1 
ATOM   3527 N N   . ASN B 1 132 ? -29.768 29.574 -35.784 1.00 13.92 ? 131  ASN B N   1 
ATOM   3528 C CA  . ASN B 1 132 ? -28.826 28.464 -35.788 1.00 12.30 ? 131  ASN B CA  1 
ATOM   3529 C C   . ASN B 1 132 ? -29.078 27.651 -34.531 1.00 13.68 ? 131  ASN B C   1 
ATOM   3530 O O   . ASN B 1 132 ? -29.409 28.214 -33.482 1.00 14.68 ? 131  ASN B O   1 
ATOM   3531 C CB  . ASN B 1 132 ? -27.370 28.970 -35.782 1.00 12.00 ? 131  ASN B CB  1 
ATOM   3532 C CG  . ASN B 1 132 ? -26.520 28.334 -36.833 1.00 16.20 ? 131  ASN B CG  1 
ATOM   3533 O OD1 . ASN B 1 132 ? -25.594 27.592 -36.508 1.00 14.66 ? 131  ASN B OD1 1 
ATOM   3534 N ND2 . ASN B 1 132 ? -26.779 28.656 -38.108 1.00 12.64 ? 131  ASN B ND2 1 
ATOM   3535 N N   . ASN B 1 133 ? -28.866 26.344 -34.622 1.00 13.82 ? 132  ASN B N   1 
ATOM   3536 C CA  . ASN B 1 133 ? -28.998 25.474 -33.453 1.00 14.11 ? 132  ASN B CA  1 
ATOM   3537 C C   . ASN B 1 133 ? -27.794 25.567 -32.516 1.00 15.08 ? 132  ASN B C   1 
ATOM   3538 O O   . ASN B 1 133 ? -26.674 25.252 -32.916 1.00 14.88 ? 132  ASN B O   1 
ATOM   3539 C CB  . ASN B 1 133 ? -29.150 24.032 -33.923 1.00 14.27 ? 132  ASN B CB  1 
ATOM   3540 C CG  . ASN B 1 133 ? -29.271 23.072 -32.776 1.00 14.00 ? 132  ASN B CG  1 
ATOM   3541 O OD1 . ASN B 1 133 ? -30.297 23.029 -32.118 1.00 14.89 ? 132  ASN B OD1 1 
ATOM   3542 N ND2 . ASN B 1 133 ? -28.209 22.306 -32.520 1.00 14.95 ? 132  ASN B ND2 1 
ATOM   3543 N N   . GLN B 1 134 ? -28.025 25.996 -31.273 1.00 12.61 ? 133  GLN B N   1 
ATOM   3544 C CA  A GLN B 1 134 ? -27.107 25.784 -30.145 0.55 12.44 ? 133  GLN B CA  1 
ATOM   3545 C CA  B GLN B 1 134 ? -27.095 25.761 -30.163 0.45 12.47 ? 133  GLN B CA  1 
ATOM   3546 C C   . GLN B 1 134 ? -25.698 26.347 -30.403 1.00 15.94 ? 133  GLN B C   1 
ATOM   3547 O O   . GLN B 1 134 ? -24.697 25.627 -30.443 1.00 16.61 ? 133  GLN B O   1 
ATOM   3548 C CB  A GLN B 1 134 ? -27.069 24.287 -29.792 0.55 14.95 ? 133  GLN B CB  1 
ATOM   3549 C CB  B GLN B 1 134 ? -26.992 24.260 -29.871 0.45 14.97 ? 133  GLN B CB  1 
ATOM   3550 C CG  A GLN B 1 134 ? -28.429 23.739 -29.307 0.55 13.59 ? 133  GLN B CG  1 
ATOM   3551 C CG  B GLN B 1 134 ? -28.174 23.657 -29.144 0.45 14.10 ? 133  GLN B CG  1 
ATOM   3552 C CD  A GLN B 1 134 ? -28.445 22.226 -29.049 0.55 16.14 ? 133  GLN B CD  1 
ATOM   3553 C CD  B GLN B 1 134 ? -27.788 22.383 -28.412 0.45 17.38 ? 133  GLN B CD  1 
ATOM   3554 O OE1 A GLN B 1 134 ? -27.891 21.448 -29.813 0.55 18.35 ? 133  GLN B OE1 1 
ATOM   3555 O OE1 B GLN B 1 134 ? -26.896 21.647 -28.844 0.45 16.03 ? 133  GLN B OE1 1 
ATOM   3556 N NE2 A GLN B 1 134 ? -29.099 21.813 -27.967 0.55 17.60 ? 133  GLN B NE2 1 
ATOM   3557 N NE2 B GLN B 1 134 ? -28.444 22.127 -27.288 0.45 19.00 ? 133  GLN B NE2 1 
ATOM   3558 N N   . TYR B 1 135 ? -25.624 27.678 -30.510 1.00 14.96 ? 134  TYR B N   1 
ATOM   3559 C CA  . TYR B 1 135 ? -24.333 28.362 -30.403 1.00 12.33 ? 134  TYR B CA  1 
ATOM   3560 C C   . TYR B 1 135 ? -23.644 27.948 -29.104 1.00 14.06 ? 134  TYR B C   1 
ATOM   3561 O O   . TYR B 1 135 ? -24.308 27.727 -28.089 1.00 15.07 ? 134  TYR B O   1 
ATOM   3562 C CB  . TYR B 1 135 ? -24.527 29.882 -30.386 1.00 12.14 ? 134  TYR B CB  1 
ATOM   3563 C CG  . TYR B 1 135 ? -25.281 30.457 -31.560 1.00 13.45 ? 134  TYR B CG  1 
ATOM   3564 C CD1 . TYR B 1 135 ? -26.662 30.635 -31.504 1.00 13.44 ? 134  TYR B CD1 1 
ATOM   3565 C CD2 . TYR B 1 135 ? -24.603 30.868 -32.700 1.00 14.46 ? 134  TYR B CD2 1 
ATOM   3566 C CE1 . TYR B 1 135 ? -27.347 31.183 -32.568 1.00 14.19 ? 134  TYR B CE1 1 
ATOM   3567 C CE2 . TYR B 1 135 ? -25.283 31.404 -33.771 1.00 14.99 ? 134  TYR B CE2 1 
ATOM   3568 C CZ  . TYR B 1 135 ? -26.652 31.565 -33.692 1.00 12.70 ? 134  TYR B CZ  1 
ATOM   3569 O OH  . TYR B 1 135 ? -27.337 32.104 -34.758 1.00 13.33 ? 134  TYR B OH  1 
ATOM   3570 N N   . HIS B 1 136 ? -22.310 27.837 -29.128 1.00 13.07 ? 135  HIS B N   1 
ATOM   3571 C CA  . HIS B 1 136 ? -21.584 27.485 -27.908 1.00 12.73 ? 135  HIS B CA  1 
ATOM   3572 C C   . HIS B 1 136 ? -20.111 27.834 -28.078 1.00 13.87 ? 135  HIS B C   1 
ATOM   3573 O O   . HIS B 1 136 ? -19.589 27.870 -29.197 1.00 17.08 ? 135  HIS B O   1 
ATOM   3574 C CB  . HIS B 1 136 ? -21.722 25.991 -27.590 1.00 15.46 ? 135  HIS B CB  1 
ATOM   3575 C CG  . HIS B 1 136 ? -21.069 25.099 -28.610 1.00 15.18 ? 135  HIS B CG  1 
ATOM   3576 N ND1 . HIS B 1 136 ? -19.779 24.633 -28.476 1.00 15.96 ? 135  HIS B ND1 1 
ATOM   3577 C CD2 . HIS B 1 136 ? -21.522 24.614 -29.794 1.00 15.36 ? 135  HIS B CD2 1 
ATOM   3578 C CE1 . HIS B 1 136 ? -19.475 23.869 -29.514 1.00 16.40 ? 135  HIS B CE1 1 
ATOM   3579 N NE2 . HIS B 1 136 ? -20.511 23.852 -30.337 1.00 17.04 ? 135  HIS B NE2 1 
ATOM   3580 N N   . ASP B 1 137 ? -19.434 28.008 -26.937 1.00 13.26 ? 136  ASP B N   1 
ATOM   3581 C CA  . ASP B 1 137 ? -17.978 28.225 -26.857 1.00 14.27 ? 136  ASP B CA  1 
ATOM   3582 C C   . ASP B 1 137 ? -17.508 29.237 -27.899 1.00 14.58 ? 136  ASP B C   1 
ATOM   3583 O O   . ASP B 1 137 ? -16.622 28.972 -28.723 1.00 17.21 ? 136  ASP B O   1 
ATOM   3584 C CB  . ASP B 1 137 ? -17.211 26.904 -26.988 1.00 15.30 ? 136  ASP B CB  1 
ATOM   3585 C CG  . ASP B 1 137 ? -17.606 25.897 -25.929 1.00 17.94 ? 136  ASP B CG  1 
ATOM   3586 O OD1 . ASP B 1 137 ? -17.343 26.143 -24.736 1.00 20.73 ? 136  ASP B OD1 1 
ATOM   3587 O OD2 . ASP B 1 137 ? -18.213 24.869 -26.277 1.00 19.49 ? 136  ASP B OD2 1 
ATOM   3588 N N   . MET B 1 138 ? -18.131 30.411 -27.865 1.00 15.78 ? 137  MET B N   1 
ATOM   3589 C CA  . MET B 1 138 ? -17.802 31.475 -28.799 1.00 15.58 ? 137  MET B CA  1 
ATOM   3590 C C   . MET B 1 138 ? -18.159 32.812 -28.161 1.00 15.12 ? 137  MET B C   1 
ATOM   3591 O O   . MET B 1 138 ? -18.838 32.876 -27.130 1.00 16.63 ? 137  MET B O   1 
ATOM   3592 C CB  . MET B 1 138 ? -18.508 31.271 -30.147 1.00 15.94 ? 137  MET B CB  1 
ATOM   3593 C CG  . MET B 1 138 ? -20.005 31.190 -30.008 1.00 17.64 ? 137  MET B CG  1 
ATOM   3594 S SD  . MET B 1 138 ? -20.772 30.443 -31.482 1.00 17.45 ? 137  MET B SD  1 
ATOM   3595 C CE  . MET B 1 138 ? -20.613 31.771 -32.701 1.00 18.30 ? 137  MET B CE  1 
ATOM   3596 N N   . ASP B 1 139 ? -17.663 33.885 -28.778 1.00 15.54 ? 138  ASP B N   1 
ATOM   3597 C CA  . ASP B 1 139 ? -17.796 35.219 -28.203 1.00 13.82 ? 138  ASP B CA  1 
ATOM   3598 C C   . ASP B 1 139 ? -19.269 35.604 -28.067 1.00 16.23 ? 138  ASP B C   1 
ATOM   3599 O O   . ASP B 1 139 ? -20.066 35.376 -28.982 1.00 16.07 ? 138  ASP B O   1 
ATOM   3600 C CB  . ASP B 1 139 ? -17.046 36.218 -29.085 1.00 17.99 ? 138  ASP B CB  1 
ATOM   3601 C CG  . ASP B 1 139 ? -17.120 37.632 -28.554 1.00 20.90 ? 138  ASP B CG  1 
ATOM   3602 O OD1 . ASP B 1 139 ? -16.261 38.005 -27.721 1.00 22.05 ? 138  ASP B OD1 1 
ATOM   3603 O OD2 . ASP B 1 139 ? -18.035 38.372 -28.964 1.00 19.27 ? 138  ASP B OD2 1 
ATOM   3604 N N   . GLN B 1 140 ? -19.627 36.163 -26.899 1.00 15.59 ? 139  GLN B N   1 
ATOM   3605 C CA  . GLN B 1 140 ? -21.030 36.433 -26.582 1.00 13.75 ? 139  GLN B CA  1 
ATOM   3606 C C   . GLN B 1 140 ? -21.596 37.582 -27.398 1.00 18.29 ? 139  GLN B C   1 
ATOM   3607 O O   . GLN B 1 140 ? -22.793 37.571 -27.735 1.00 16.14 ? 139  GLN B O   1 
ATOM   3608 C CB  . GLN B 1 140 ? -21.173 36.741 -25.090 1.00 17.77 ? 139  GLN B CB  1 
ATOM   3609 C CG  . GLN B 1 140 ? -22.617 36.886 -24.637 1.00 16.63 ? 139  GLN B CG  1 
ATOM   3610 C CD  . GLN B 1 140 ? -23.438 35.620 -24.851 1.00 18.92 ? 139  GLN B CD  1 
ATOM   3611 O OE1 . GLN B 1 140 ? -22.932 34.510 -24.707 1.00 18.00 ? 139  GLN B OE1 1 
ATOM   3612 N NE2 . GLN B 1 140 ? -24.709 35.785 -25.211 1.00 16.09 ? 139  GLN B NE2 1 
ATOM   3613 N N   . THR B 1 141 ? -20.774 38.598 -27.692 1.00 16.06 ? 140  THR B N   1 
ATOM   3614 C CA  . THR B 1 141 ? -21.226 39.662 -28.587 1.00 16.01 ? 140  THR B CA  1 
ATOM   3615 C C   . THR B 1 141 ? -21.391 39.136 -30.009 1.00 17.60 ? 140  THR B C   1 
ATOM   3616 O O   . THR B 1 141 ? -22.327 39.524 -30.720 1.00 16.97 ? 140  THR B O   1 
ATOM   3617 C CB  . THR B 1 141 ? -20.251 40.838 -28.540 1.00 18.27 ? 140  THR B CB  1 
ATOM   3618 O OG1 . THR B 1 141 ? -20.230 41.372 -27.211 1.00 19.25 ? 140  THR B OG1 1 
ATOM   3619 C CG2 . THR B 1 141 ? -20.685 41.945 -29.506 1.00 18.49 ? 140  THR B CG2 1 
ATOM   3620 N N   . LEU B 1 142 ? -20.499 38.240 -30.441 1.00 16.12 ? 141  LEU B N   1 
ATOM   3621 C CA  . LEU B 1 142 ? -20.671 37.612 -31.749 1.00 18.04 ? 141  LEU B CA  1 
ATOM   3622 C C   . LEU B 1 142 ? -22.006 36.877 -31.848 1.00 16.03 ? 141  LEU B C   1 
ATOM   3623 O O   . LEU B 1 142 ? -22.697 36.979 -32.871 1.00 15.50 ? 141  LEU B O   1 
ATOM   3624 C CB  . LEU B 1 142 ? -19.511 36.658 -32.030 1.00 17.92 ? 141  LEU B CB  1 
ATOM   3625 C CG  . LEU B 1 142 ? -19.599 35.851 -33.327 1.00 15.32 ? 141  LEU B CG  1 
ATOM   3626 C CD1 . LEU B 1 142 ? -19.595 36.771 -34.560 1.00 15.54 ? 141  LEU B CD1 1 
ATOM   3627 C CD2 . LEU B 1 142 ? -18.438 34.877 -33.400 1.00 19.94 ? 141  LEU B CD2 1 
ATOM   3628 N N   . VAL B 1 143 ? -22.394 36.123 -30.805 1.00 15.80 ? 142  VAL B N   1 
ATOM   3629 C CA  . VAL B 1 143 ? -23.679 35.416 -30.863 1.00 13.95 ? 142  VAL B CA  1 
ATOM   3630 C C   . VAL B 1 143 ? -24.822 36.408 -31.048 1.00 15.72 ? 142  VAL B C   1 
ATOM   3631 O O   . VAL B 1 143 ? -25.728 36.193 -31.869 1.00 15.33 ? 142  VAL B O   1 
ATOM   3632 C CB  . VAL B 1 143 ? -23.894 34.550 -29.609 1.00 13.66 ? 142  VAL B CB  1 
ATOM   3633 C CG1 . VAL B 1 143 ? -25.336 33.986 -29.592 1.00 14.76 ? 142  VAL B CG1 1 
ATOM   3634 C CG2 . VAL B 1 143 ? -22.884 33.410 -29.580 1.00 16.04 ? 142  VAL B CG2 1 
ATOM   3635 N N   . LEU B 1 144 ? -24.822 37.488 -30.263 1.00 15.72 ? 143  LEU B N   1 
ATOM   3636 C CA  . LEU B 1 144 ? -25.805 38.552 -30.461 1.00 15.60 ? 143  LEU B CA  1 
ATOM   3637 C C   . LEU B 1 144 ? -25.793 39.043 -31.904 1.00 16.07 ? 143  LEU B C   1 
ATOM   3638 O O   . LEU B 1 144 ? -26.837 39.107 -32.556 1.00 15.87 ? 143  LEU B O   1 
ATOM   3639 C CB  . LEU B 1 144 ? -25.535 39.714 -29.500 1.00 16.79 ? 143  LEU B CB  1 
ATOM   3640 C CG  . LEU B 1 144 ? -26.381 40.971 -29.748 1.00 14.72 ? 143  LEU B CG  1 
ATOM   3641 C CD1 . LEU B 1 144 ? -27.865 40.716 -29.419 1.00 20.81 ? 143  LEU B CD1 1 
ATOM   3642 C CD2 . LEU B 1 144 ? -25.875 42.121 -28.892 1.00 18.19 ? 143  LEU B CD2 1 
ATOM   3643 N N   . ASN B 1 145 ? -24.606 39.349 -32.430 1.00 15.80 ? 144  ASN B N   1 
ATOM   3644 C CA  . ASN B 1 145 ? -24.506 39.935 -33.764 1.00 16.08 ? 144  ASN B CA  1 
ATOM   3645 C C   . ASN B 1 145 ? -24.902 38.959 -34.861 1.00 15.92 ? 144  ASN B C   1 
ATOM   3646 O O   . ASN B 1 145 ? -25.422 39.382 -35.903 1.00 17.18 ? 144  ASN B O   1 
ATOM   3647 C CB  . ASN B 1 145 ? -23.077 40.416 -34.028 1.00 17.46 ? 144  ASN B CB  1 
ATOM   3648 C CG  . ASN B 1 145 ? -22.687 41.609 -33.180 1.00 19.70 ? 144  ASN B CG  1 
ATOM   3649 O OD1 . ASN B 1 145 ? -23.539 42.328 -32.645 1.00 22.90 ? 144  ASN B OD1 1 
ATOM   3650 N ND2 . ASN B 1 145 ? -21.378 41.831 -33.061 1.00 18.83 ? 144  ASN B ND2 1 
ATOM   3651 N N   . LEU B 1 146 ? -24.634 37.665 -34.679 1.00 14.59 ? 145  LEU B N   1 
ATOM   3652 C CA  . LEU B 1 146 ? -25.087 36.681 -35.667 1.00 13.92 ? 145  LEU B CA  1 
ATOM   3653 C C   . LEU B 1 146 ? -26.604 36.584 -35.692 1.00 15.37 ? 145  LEU B C   1 
ATOM   3654 O O   . LEU B 1 146 ? -27.209 36.532 -36.770 1.00 14.31 ? 145  LEU B O   1 
ATOM   3655 C CB  . LEU B 1 146 ? -24.471 35.312 -35.377 1.00 14.19 ? 145  LEU B CB  1 
ATOM   3656 C CG  . LEU B 1 146 ? -22.954 35.228 -35.630 1.00 15.12 ? 145  LEU B CG  1 
ATOM   3657 C CD1 . LEU B 1 146 ? -22.456 33.846 -35.259 1.00 17.12 ? 145  LEU B CD1 1 
ATOM   3658 C CD2 . LEU B 1 146 ? -22.610 35.528 -37.099 1.00 17.71 ? 145  LEU B CD2 1 
ATOM   3659 N N   . ASN B 1 147 ? -27.233 36.545 -34.514 1.00 14.67 ? 146  ASN B N   1 
ATOM   3660 C CA  . ASN B 1 147 ? -28.690 36.540 -34.458 1.00 13.59 ? 146  ASN B CA  1 
ATOM   3661 C C   . ASN B 1 147 ? -29.261 37.781 -35.119 1.00 14.75 ? 146  ASN B C   1 
ATOM   3662 O O   . ASN B 1 147 ? -30.240 37.693 -35.866 1.00 14.19 ? 146  ASN B O   1 
ATOM   3663 C CB  . ASN B 1 147 ? -29.168 36.422 -33.001 1.00 13.50 ? 146  ASN B CB  1 
ATOM   3664 C CG  . ASN B 1 147 ? -29.191 34.974 -32.519 1.00 14.31 ? 146  ASN B CG  1 
ATOM   3665 O OD1 . ASN B 1 147 ? -30.123 34.204 -32.822 1.00 15.03 ? 146  ASN B OD1 1 
ATOM   3666 N ND2 . ASN B 1 147 ? -28.155 34.583 -31.784 1.00 16.24 ? 146  ASN B ND2 1 
ATOM   3667 N N   . GLN B 1 148 ? -28.647 38.944 -34.887 1.00 13.62 ? 147  GLN B N   1 
ATOM   3668 C CA  . GLN B 1 148 ? -29.179 40.151 -35.521 1.00 13.11 ? 147  GLN B CA  1 
ATOM   3669 C C   . GLN B 1 148 ? -28.980 40.112 -37.021 1.00 14.91 ? 147  GLN B C   1 
ATOM   3670 O O   . GLN B 1 148 ? -29.865 40.536 -37.774 1.00 14.76 ? 147  GLN B O   1 
ATOM   3671 C CB  . GLN B 1 148 ? -28.527 41.411 -34.958 1.00 16.37 ? 147  GLN B CB  1 
ATOM   3672 C CG  . GLN B 1 148 ? -29.250 42.691 -35.421 1.00 13.13 ? 147  GLN B CG  1 
ATOM   3673 C CD  . GLN B 1 148 ? -30.678 42.760 -34.887 1.00 18.36 ? 147  GLN B CD  1 
ATOM   3674 O OE1 . GLN B 1 148 ? -30.894 42.759 -33.668 1.00 17.26 ? 147  GLN B OE1 1 
ATOM   3675 N NE2 . GLN B 1 148 ? -31.656 42.829 -35.787 1.00 15.48 ? 147  GLN B NE2 1 
ATOM   3676 N N   . ALA B 1 149 ? -27.804 39.651 -37.472 1.00 12.94 ? 148  ALA B N   1 
ATOM   3677 C CA  . ALA B 1 149 ? -27.573 39.536 -38.908 1.00 15.44 ? 148  ALA B CA  1 
ATOM   3678 C C   . ALA B 1 149 ? -28.611 38.633 -39.569 1.00 16.28 ? 148  ALA B C   1 
ATOM   3679 O O   . ALA B 1 149 ? -29.058 38.905 -40.692 1.00 15.71 ? 148  ALA B O   1 
ATOM   3680 C CB  . ALA B 1 149 ? -26.156 39.004 -39.159 1.00 16.57 ? 148  ALA B CB  1 
ATOM   3681 N N   . ALA B 1 150 ? -28.982 37.537 -38.910 1.00 13.83 ? 149  ALA B N   1 
ATOM   3682 C CA  . ALA B 1 150 ? -29.991 36.638 -39.475 1.00 14.30 ? 149  ALA B CA  1 
ATOM   3683 C C   . ALA B 1 150 ? -31.333 37.347 -39.615 1.00 14.58 ? 149  ALA B C   1 
ATOM   3684 O O   . ALA B 1 150 ? -31.985 37.276 -40.670 1.00 13.96 ? 149  ALA B O   1 
ATOM   3685 C CB  . ALA B 1 150 ? -30.144 35.394 -38.587 1.00 15.03 ? 149  ALA B CB  1 
ATOM   3686 N N   . ILE B 1 151 ? -31.768 38.026 -38.548 1.00 13.30 ? 150  ILE B N   1 
ATOM   3687 C CA  . ILE B 1 151 ? -33.005 38.799 -38.592 1.00 11.83 ? 150  ILE B CA  1 
ATOM   3688 C C   . ILE B 1 151 ? -32.963 39.780 -39.754 1.00 13.75 ? 150  ILE B C   1 
ATOM   3689 O O   . ILE B 1 151 ? -33.898 39.863 -40.560 1.00 15.19 ? 150  ILE B O   1 
ATOM   3690 C CB  . ILE B 1 151 ? -33.237 39.523 -37.250 1.00 14.08 ? 150  ILE B CB  1 
ATOM   3691 C CG1 . ILE B 1 151 ? -33.492 38.485 -36.160 1.00 14.06 ? 150  ILE B CG1 1 
ATOM   3692 C CG2 . ILE B 1 151 ? -34.406 40.516 -37.374 1.00 15.99 ? 150  ILE B CG2 1 
ATOM   3693 C CD1 . ILE B 1 151 ? -33.376 39.067 -34.745 1.00 14.66 ? 150  ILE B CD1 1 
ATOM   3694 N N   . ASP B 1 152 ? -31.870 40.542 -39.855 1.00 13.61 ? 151  ASP B N   1 
ATOM   3695 C CA  . ASP B 1 152 ? -31.775 41.557 -40.900 1.00 13.38 ? 151  ASP B CA  1 
ATOM   3696 C C   . ASP B 1 152 ? -31.847 40.924 -42.284 1.00 16.98 ? 151  ASP B C   1 
ATOM   3697 O O   . ASP B 1 152 ? -32.483 41.467 -43.193 1.00 16.58 ? 151  ASP B O   1 
ATOM   3698 C CB  . ASP B 1 152 ? -30.472 42.354 -40.757 1.00 13.29 ? 151  ASP B CB  1 
ATOM   3699 C CG  . ASP B 1 152 ? -30.425 43.211 -39.497 1.00 19.30 ? 151  ASP B CG  1 
ATOM   3700 O OD1 . ASP B 1 152 ? -31.454 43.293 -38.782 1.00 16.67 ? 151  ASP B OD1 1 
ATOM   3701 O OD2 . ASP B 1 152 ? -29.344 43.785 -39.227 1.00 18.27 ? 151  ASP B OD2 1 
ATOM   3702 N N   . GLY B 1 153 ? -31.176 39.790 -42.473 1.00 14.32 ? 152  GLY B N   1 
ATOM   3703 C CA  . GLY B 1 153 ? -31.220 39.147 -43.783 1.00 14.46 ? 152  GLY B CA  1 
ATOM   3704 C C   . GLY B 1 153 ? -32.608 38.639 -44.114 1.00 13.77 ? 152  GLY B C   1 
ATOM   3705 O O   . GLY B 1 153 ? -33.104 38.801 -45.233 1.00 15.48 ? 152  GLY B O   1 
ATOM   3706 N N   . ILE B 1 154 ? -33.243 37.987 -43.144 1.00 13.26 ? 153  ILE B N   1 
ATOM   3707 C CA  . ILE B 1 154 ? -34.601 37.479 -43.340 1.00 13.55 ? 153  ILE B CA  1 
ATOM   3708 C C   . ILE B 1 154 ? -35.547 38.606 -43.732 1.00 15.19 ? 153  ILE B C   1 
ATOM   3709 O O   . ILE B 1 154 ? -36.309 38.490 -44.696 1.00 13.85 ? 153  ILE B O   1 
ATOM   3710 C CB  . ILE B 1 154 ? -35.080 36.777 -42.060 1.00 12.92 ? 153  ILE B CB  1 
ATOM   3711 C CG1 . ILE B 1 154 ? -34.302 35.481 -41.851 1.00 12.24 ? 153  ILE B CG1 1 
ATOM   3712 C CG2 . ILE B 1 154 ? -36.578 36.485 -42.137 1.00 14.21 ? 153  ILE B CG2 1 
ATOM   3713 C CD1 . ILE B 1 154 ? -34.289 35.025 -40.375 1.00 13.55 ? 153  ILE B CD1 1 
ATOM   3714 N N   . ARG B 1 155 ? -35.554 39.695 -42.956 1.00 13.93 ? 154  ARG B N   1 
ATOM   3715 C CA  . ARG B 1 155 ? -36.507 40.763 -43.252 1.00 14.39 ? 154  ARG B CA  1 
ATOM   3716 C C   . ARG B 1 155 ? -36.170 41.466 -44.565 1.00 14.88 ? 154  ARG B C   1 
ATOM   3717 O O   . ARG B 1 155 ? -37.080 41.907 -45.287 1.00 16.54 ? 154  ARG B O   1 
ATOM   3718 C CB  . ARG B 1 155 ? -36.572 41.760 -42.088 1.00 14.82 ? 154  ARG B CB  1 
ATOM   3719 C CG  . ARG B 1 155 ? -37.002 41.146 -40.729 1.00 12.88 ? 154  ARG B CG  1 
ATOM   3720 C CD  . ARG B 1 155 ? -38.277 40.307 -40.817 1.00 13.49 ? 154  ARG B CD  1 
ATOM   3721 N NE  . ARG B 1 155 ? -38.685 39.858 -39.483 1.00 15.10 ? 154  ARG B NE  1 
ATOM   3722 C CZ  . ARG B 1 155 ? -39.467 38.813 -39.260 1.00 14.69 ? 154  ARG B CZ  1 
ATOM   3723 N NH1 . ARG B 1 155 ? -39.897 38.056 -40.252 1.00 15.25 ? 154  ARG B NH1 1 
ATOM   3724 N NH2 . ARG B 1 155 ? -39.811 38.508 -38.006 1.00 14.60 ? 154  ARG B NH2 1 
ATOM   3725 N N   . SER B 1 156 ? -34.882 41.521 -44.935 1.00 14.86 ? 155  SER B N   1 
ATOM   3726 C CA  . SER B 1 156 ? -34.510 42.159 -46.197 1.00 15.59 ? 155  SER B CA  1 
ATOM   3727 C C   . SER B 1 156 ? -35.026 41.390 -47.398 1.00 16.42 ? 155  SER B C   1 
ATOM   3728 O O   . SER B 1 156 ? -35.167 41.984 -48.477 1.00 16.50 ? 155  SER B O   1 
ATOM   3729 C CB  . SER B 1 156 ? -32.995 42.304 -46.304 1.00 16.84 ? 155  SER B CB  1 
ATOM   3730 O OG  . SER B 1 156 ? -32.391 41.080 -46.679 1.00 15.78 ? 155  SER B OG  1 
ATOM   3731 N N   . ALA B 1 157 ? -35.322 40.093 -47.233 1.00 16.88 ? 156  ALA B N   1 
ATOM   3732 C CA  . ALA B 1 157 ? -35.909 39.291 -48.305 1.00 16.03 ? 156  ALA B CA  1 
ATOM   3733 C C   . ALA B 1 157 ? -37.402 39.535 -48.482 1.00 18.06 ? 156  ALA B C   1 
ATOM   3734 O O   . ALA B 1 157 ? -38.012 38.947 -49.386 1.00 20.51 ? 156  ALA B O   1 
ATOM   3735 C CB  . ALA B 1 157 ? -35.675 37.803 -48.045 1.00 17.26 ? 156  ALA B CB  1 
ATOM   3736 N N   . GLY B 1 158 ? -38.003 40.391 -47.661 1.00 18.41 ? 157  GLY B N   1 
ATOM   3737 C CA  . GLY B 1 158 ? -39.444 40.524 -47.683 1.00 17.42 ? 157  GLY B CA  1 
ATOM   3738 C C   . GLY B 1 158 ? -40.171 39.459 -46.902 1.00 18.74 ? 157  GLY B C   1 
ATOM   3739 O O   . GLY B 1 158 ? -41.403 39.373 -46.993 1.00 18.39 ? 157  GLY B O   1 
ATOM   3740 N N   . ALA B 1 159 ? -39.444 38.636 -46.136 1.00 15.32 ? 158  ALA B N   1 
ATOM   3741 C CA  . ALA B 1 159 ? -40.056 37.605 -45.307 1.00 14.44 ? 158  ALA B CA  1 
ATOM   3742 C C   . ALA B 1 159 ? -40.378 38.268 -43.978 1.00 15.09 ? 158  ALA B C   1 
ATOM   3743 O O   . ALA B 1 159 ? -39.609 38.192 -43.021 1.00 14.42 ? 158  ALA B O   1 
ATOM   3744 C CB  . ALA B 1 159 ? -39.112 36.420 -45.118 1.00 13.99 ? 158  ALA B CB  1 
ATOM   3745 N N   . THR B 1 160 ? -41.516 38.968 -43.949 1.00 16.49 ? 159  THR B N   1 
ATOM   3746 C CA  . THR B 1 160 ? -41.884 39.810 -42.816 1.00 14.67 ? 159  THR B CA  1 
ATOM   3747 C C   . THR B 1 160 ? -42.985 39.220 -41.949 1.00 17.72 ? 159  THR B C   1 
ATOM   3748 O O   . THR B 1 160 ? -43.201 39.709 -40.831 1.00 18.21 ? 159  THR B O   1 
ATOM   3749 C CB  . THR B 1 160 ? -42.347 41.193 -43.300 1.00 16.88 ? 159  THR B CB  1 
ATOM   3750 O OG1 . THR B 1 160 ? -43.415 41.042 -44.258 1.00 19.96 ? 159  THR B OG1 1 
ATOM   3751 C CG2 . THR B 1 160 ? -41.186 41.961 -43.951 1.00 20.28 ? 159  THR B CG2 1 
ATOM   3752 N N   . SER B 1 161 ? -43.710 38.223 -42.449 1.00 16.73 ? 160  SER B N   1 
ATOM   3753 C CA  . SER B 1 161 ? -44.830 37.649 -41.714 1.00 15.42 ? 160  SER B CA  1 
ATOM   3754 C C   . SER B 1 161 ? -44.402 36.597 -40.694 1.00 17.58 ? 160  SER B C   1 
ATOM   3755 O O   . SER B 1 161 ? -45.195 36.269 -39.806 1.00 18.45 ? 160  SER B O   1 
ATOM   3756 C CB  . SER B 1 161 ? -45.808 37.011 -42.700 1.00 21.88 ? 160  SER B CB  1 
ATOM   3757 O OG  . SER B 1 161 ? -45.215 35.858 -43.278 1.00 19.86 ? 160  SER B OG  1 
ATOM   3758 N N   . GLN B 1 162 ? -43.191 36.052 -40.823 1.00 16.82 ? 161  GLN B N   1 
ATOM   3759 C CA  . GLN B 1 162 ? -42.762 34.849 -40.116 1.00 15.96 ? 161  GLN B CA  1 
ATOM   3760 C C   . GLN B 1 162 ? -42.151 35.158 -38.763 1.00 14.99 ? 161  GLN B C   1 
ATOM   3761 O O   . GLN B 1 162 ? -41.439 36.150 -38.591 1.00 15.45 ? 161  GLN B O   1 
ATOM   3762 C CB  . GLN B 1 162 ? -41.708 34.079 -40.924 1.00 13.65 ? 161  GLN B CB  1 
ATOM   3763 C CG  . GLN B 1 162 ? -42.204 33.555 -42.279 1.00 14.14 ? 161  GLN B CG  1 
ATOM   3764 C CD  . GLN B 1 162 ? -42.108 34.576 -43.418 1.00 19.41 ? 161  GLN B CD  1 
ATOM   3765 O OE1 . GLN B 1 162 ? -41.797 35.757 -43.225 1.00 14.87 ? 161  GLN B OE1 1 
ATOM   3766 N NE2 . GLN B 1 162 ? -42.383 34.108 -44.622 1.00 18.73 ? 161  GLN B NE2 1 
ATOM   3767 N N   . TYR B 1 163 ? -42.393 34.264 -37.809 1.00 13.35 ? 162  TYR B N   1 
ATOM   3768 C CA  . TYR B 1 163 ? -41.633 34.315 -36.567 1.00 12.33 ? 162  TYR B CA  1 
ATOM   3769 C C   . TYR B 1 163 ? -40.184 33.936 -36.822 1.00 14.73 ? 162  TYR B C   1 
ATOM   3770 O O   . TYR B 1 163 ? -39.878 33.146 -37.717 1.00 15.41 ? 162  TYR B O   1 
ATOM   3771 C CB  . TYR B 1 163 ? -42.242 33.373 -35.522 1.00 14.83 ? 162  TYR B CB  1 
ATOM   3772 C CG  . TYR B 1 163 ? -43.571 33.870 -35.013 1.00 15.26 ? 162  TYR B CG  1 
ATOM   3773 C CD1 . TYR B 1 163 ? -43.643 34.757 -33.950 1.00 17.66 ? 162  TYR B CD1 1 
ATOM   3774 C CD2 . TYR B 1 163 ? -44.764 33.460 -35.613 1.00 18.19 ? 162  TYR B CD2 1 
ATOM   3775 C CE1 . TYR B 1 163 ? -44.872 35.216 -33.491 1.00 18.55 ? 162  TYR B CE1 1 
ATOM   3776 C CE2 . TYR B 1 163 ? -45.995 33.919 -35.163 1.00 18.31 ? 162  TYR B CE2 1 
ATOM   3777 C CZ  . TYR B 1 163 ? -46.034 34.794 -34.107 1.00 22.92 ? 162  TYR B CZ  1 
ATOM   3778 O OH  . TYR B 1 163 ? -47.253 35.248 -33.654 1.00 26.32 ? 162  TYR B OH  1 
ATOM   3779 N N   . ILE B 1 164 ? -39.294 34.481 -35.990 1.00 12.40 ? 163  ILE B N   1 
ATOM   3780 C CA  . ILE B 1 164 ? -37.868 34.146 -36.001 1.00 12.12 ? 163  ILE B CA  1 
ATOM   3781 C C   . ILE B 1 164 ? -37.516 33.580 -34.632 1.00 13.96 ? 163  ILE B C   1 
ATOM   3782 O O   . ILE B 1 164 ? -37.697 34.258 -33.615 1.00 15.61 ? 163  ILE B O   1 
ATOM   3783 C CB  . ILE B 1 164 ? -37.004 35.362 -36.328 1.00 13.99 ? 163  ILE B CB  1 
ATOM   3784 C CG1 . ILE B 1 164 ? -37.359 35.850 -37.740 1.00 14.03 ? 163  ILE B CG1 1 
ATOM   3785 C CG2 . ILE B 1 164 ? -35.531 34.972 -36.288 1.00 15.27 ? 163  ILE B CG2 1 
ATOM   3786 C CD1 . ILE B 1 164 ? -36.641 37.133 -38.170 1.00 15.25 ? 163  ILE B CD1 1 
ATOM   3787 N N   . PHE B 1 165 ? -37.012 32.345 -34.606 1.00 13.26 ? 164  PHE B N   1 
ATOM   3788 C CA  . PHE B 1 165 ? -36.508 31.760 -33.366 1.00 15.31 ? 164  PHE B CA  1 
ATOM   3789 C C   . PHE B 1 165 ? -35.032 32.136 -33.251 1.00 15.00 ? 164  PHE B C   1 
ATOM   3790 O O   . PHE B 1 165 ? -34.229 31.771 -34.117 1.00 14.22 ? 164  PHE B O   1 
ATOM   3791 C CB  . PHE B 1 165 ? -36.665 30.236 -33.358 1.00 13.25 ? 164  PHE B CB  1 
ATOM   3792 C CG  . PHE B 1 165 ? -38.082 29.738 -33.163 1.00 12.94 ? 164  PHE B CG  1 
ATOM   3793 C CD1 . PHE B 1 165 ? -39.150 30.622 -33.030 1.00 14.47 ? 164  PHE B CD1 1 
ATOM   3794 C CD2 . PHE B 1 165 ? -38.330 28.366 -33.109 1.00 13.22 ? 164  PHE B CD2 1 
ATOM   3795 C CE1 . PHE B 1 165 ? -40.459 30.153 -32.872 1.00 13.53 ? 164  PHE B CE1 1 
ATOM   3796 C CE2 . PHE B 1 165 ? -39.631 27.876 -32.910 1.00 15.99 ? 164  PHE B CE2 1 
ATOM   3797 C CZ  . PHE B 1 165 ? -40.701 28.777 -32.800 1.00 15.53 ? 164  PHE B CZ  1 
ATOM   3798 N N   . VAL B 1 166 ? -34.675 32.874 -32.195 1.00 13.14 ? 165  VAL B N   1 
ATOM   3799 C CA  . VAL B 1 166 ? -33.281 33.210 -31.942 1.00 14.85 ? 165  VAL B CA  1 
ATOM   3800 C C   . VAL B 1 166 ? -32.762 32.234 -30.900 1.00 13.67 ? 165  VAL B C   1 
ATOM   3801 O O   . VAL B 1 166 ? -33.520 31.738 -30.051 1.00 14.94 ? 165  VAL B O   1 
ATOM   3802 C CB  . VAL B 1 166 ? -33.106 34.683 -31.498 1.00 13.71 ? 165  VAL B CB  1 
ATOM   3803 C CG1 . VAL B 1 166 ? -33.639 35.658 -32.566 1.00 14.58 ? 165  VAL B CG1 1 
ATOM   3804 C CG2 . VAL B 1 166 ? -33.776 34.948 -30.137 1.00 13.05 ? 165  VAL B CG2 1 
ATOM   3805 N N   . GLU B 1 167 ? -31.474 31.910 -30.982 1.00 12.58 ? 166  GLU B N   1 
ATOM   3806 C CA  . GLU B 1 167 ? -30.865 30.991 -30.034 1.00 11.56 ? 166  GLU B CA  1 
ATOM   3807 C C   . GLU B 1 167 ? -29.660 31.655 -29.397 1.00 14.37 ? 166  GLU B C   1 
ATOM   3808 O O   . GLU B 1 167 ? -28.967 32.461 -30.023 1.00 13.81 ? 166  GLU B O   1 
ATOM   3809 C CB  . GLU B 1 167 ? -30.458 29.647 -30.702 1.00 13.85 ? 166  GLU B CB  1 
ATOM   3810 C CG  . GLU B 1 167 ? -31.668 28.898 -31.304 1.00 15.27 ? 166  GLU B CG  1 
ATOM   3811 C CD  . GLU B 1 167 ? -31.422 27.416 -31.573 1.00 15.83 ? 166  GLU B CD  1 
ATOM   3812 O OE1 . GLU B 1 167 ? -30.676 26.775 -30.813 1.00 15.93 ? 166  GLU B OE1 1 
ATOM   3813 O OE2 . GLU B 1 167 ? -31.982 26.873 -32.558 1.00 13.01 ? 166  GLU B OE2 1 
ATOM   3814 N N   . GLY B 1 168 ? -29.416 31.306 -28.137 1.00 14.86 ? 167  GLY B N   1 
ATOM   3815 C CA  . GLY B 1 168 ? -28.308 31.867 -27.401 1.00 15.09 ? 167  GLY B CA  1 
ATOM   3816 C C   . GLY B 1 168 ? -27.102 30.946 -27.315 1.00 16.36 ? 167  GLY B C   1 
ATOM   3817 O O   . GLY B 1 168 ? -27.079 29.822 -27.828 1.00 14.15 ? 167  GLY B O   1 
ATOM   3818 N N   . ASN B 1 169 ? -26.079 31.472 -26.646 1.00 14.17 ? 168  ASN B N   1 
ATOM   3819 C CA  . ASN B 1 169 ? -24.853 30.749 -26.327 1.00 14.55 ? 168  ASN B CA  1 
ATOM   3820 C C   . ASN B 1 169 ? -25.142 29.661 -25.282 1.00 14.93 ? 168  ASN B C   1 
ATOM   3821 O O   . ASN B 1 169 ? -26.277 29.482 -24.822 1.00 17.51 ? 168  ASN B O   1 
ATOM   3822 C CB  . ASN B 1 169 ? -23.813 31.755 -25.825 1.00 14.96 ? 168  ASN B CB  1 
ATOM   3823 C CG  . ASN B 1 169 ? -22.389 31.416 -26.250 1.00 17.05 ? 168  ASN B CG  1 
ATOM   3824 O OD1 . ASN B 1 169 ? -22.059 30.266 -26.532 1.00 19.25 ? 168  ASN B OD1 1 
ATOM   3825 N ND2 . ASN B 1 169 ? -21.533 32.430 -26.272 1.00 16.43 ? 168  ASN B ND2 1 
ATOM   3826 N N   . SER B 1 170 ? -24.098 28.923 -24.880 1.00 15.96 ? 169  SER B N   1 
ATOM   3827 C CA  . SER B 1 170 ? -24.242 27.827 -23.901 1.00 14.88 ? 169  SER B CA  1 
ATOM   3828 C C   . SER B 1 170 ? -25.275 26.800 -24.373 1.00 15.70 ? 169  SER B C   1 
ATOM   3829 O O   . SER B 1 170 ? -26.114 26.319 -23.600 1.00 17.64 ? 169  SER B O   1 
ATOM   3830 C CB  . SER B 1 170 ? -24.575 28.353 -22.491 1.00 18.91 ? 169  SER B CB  1 
ATOM   3831 O OG  . SER B 1 170 ? -23.406 28.906 -21.859 1.00 18.11 ? 169  SER B OG  1 
ATOM   3832 N N   . TRP B 1 171 ? -25.203 26.454 -25.665 1.00 14.59 ? 170  TRP B N   1 
ATOM   3833 C CA  . TRP B 1 171 ? -26.089 25.461 -26.279 1.00 14.88 ? 170  TRP B CA  1 
ATOM   3834 C C   . TRP B 1 171 ? -27.559 25.835 -26.105 1.00 14.05 ? 170  TRP B C   1 
ATOM   3835 O O   . TRP B 1 171 ? -28.434 24.962 -25.995 1.00 16.62 ? 170  TRP B O   1 
ATOM   3836 C CB  . TRP B 1 171 ? -25.790 24.061 -25.718 1.00 17.00 ? 170  TRP B CB  1 
ATOM   3837 C CG  . TRP B 1 171 ? -24.294 23.707 -25.642 1.00 18.92 ? 170  TRP B CG  1 
ATOM   3838 C CD1 . TRP B 1 171 ? -23.421 24.002 -24.618 1.00 20.93 ? 170  TRP B CD1 1 
ATOM   3839 C CD2 . TRP B 1 171 ? -23.534 22.960 -26.604 1.00 19.83 ? 170  TRP B CD2 1 
ATOM   3840 N NE1 . TRP B 1 171 ? -22.170 23.504 -24.905 1.00 19.51 ? 170  TRP B NE1 1 
ATOM   3841 C CE2 . TRP B 1 171 ? -22.212 22.849 -26.106 1.00 18.34 ? 170  TRP B CE2 1 
ATOM   3842 C CE3 . TRP B 1 171 ? -23.844 22.368 -27.834 1.00 20.18 ? 170  TRP B CE3 1 
ATOM   3843 C CZ2 . TRP B 1 171 ? -21.198 22.182 -26.801 1.00 18.05 ? 170  TRP B CZ2 1 
ATOM   3844 C CZ3 . TRP B 1 171 ? -22.833 21.692 -28.522 1.00 22.32 ? 170  TRP B CZ3 1 
ATOM   3845 C CH2 . TRP B 1 171 ? -21.530 21.602 -28.000 1.00 18.06 ? 170  TRP B CH2 1 
ATOM   3846 N N   . THR B 1 172 ? -27.819 27.149 -26.092 1.00 13.45 ? 171  THR B N   1 
ATOM   3847 C CA  . THR B 1 172 ? -29.109 27.789 -25.817 1.00 12.09 ? 171  THR B CA  1 
ATOM   3848 C C   . THR B 1 172 ? -29.886 27.110 -24.675 1.00 15.38 ? 171  THR B C   1 
ATOM   3849 O O   . THR B 1 172 ? -31.117 27.104 -24.649 1.00 14.77 ? 171  THR B O   1 
ATOM   3850 C CB  . THR B 1 172 ? -29.907 27.903 -27.146 1.00 15.21 ? 171  THR B CB  1 
ATOM   3851 O OG1 . THR B 1 172 ? -30.797 29.024 -27.075 1.00 15.70 ? 171  THR B OG1 1 
ATOM   3852 C CG2 . THR B 1 172 ? -30.708 26.640 -27.522 1.00 14.64 ? 171  THR B CG2 1 
ATOM   3853 N N   . GLY B 1 173 ? -29.172 26.630 -23.660 1.00 15.69 ? 172  GLY B N   1 
ATOM   3854 C CA  . GLY B 1 173 ? -29.848 25.961 -22.550 1.00 16.35 ? 172  GLY B CA  1 
ATOM   3855 C C   . GLY B 1 173 ? -30.673 26.938 -21.726 1.00 16.57 ? 172  GLY B C   1 
ATOM   3856 O O   . GLY B 1 173 ? -30.245 28.056 -21.432 1.00 15.73 ? 172  GLY B O   1 
ATOM   3857 N N   . ALA B 1 174 ? -31.870 26.498 -21.323 1.00 16.22 ? 173  ALA B N   1 
ATOM   3858 C CA  . ALA B 1 174 ? -32.673 27.341 -20.443 1.00 14.12 ? 173  ALA B CA  1 
ATOM   3859 C C   . ALA B 1 174 ? -31.995 27.490 -19.088 1.00 14.97 ? 173  ALA B C   1 
ATOM   3860 O O   . ALA B 1 174 ? -31.938 28.592 -18.530 1.00 15.84 ? 173  ALA B O   1 
ATOM   3861 C CB  . ALA B 1 174 ? -34.077 26.751 -20.273 1.00 18.50 ? 173  ALA B CB  1 
ATOM   3862 N N   . TRP B 1 175 ? -31.411 26.404 -18.586 1.00 13.81 ? 174  TRP B N   1 
ATOM   3863 C CA  . TRP B 1 175 ? -30.869 26.451 -17.229 1.00 13.79 ? 174  TRP B CA  1 
ATOM   3864 C C   . TRP B 1 175 ? -29.658 27.366 -17.120 1.00 17.59 ? 174  TRP B C   1 
ATOM   3865 O O   . TRP B 1 175 ? -29.329 27.810 -16.011 1.00 21.69 ? 174  TRP B O   1 
ATOM   3866 C CB  . TRP B 1 175 ? -30.533 25.032 -16.737 1.00 14.71 ? 174  TRP B CB  1 
ATOM   3867 C CG  . TRP B 1 175 ? -29.527 24.228 -17.529 1.00 15.67 ? 174  TRP B CG  1 
ATOM   3868 C CD1 . TRP B 1 175 ? -29.267 24.286 -18.868 1.00 19.30 ? 174  TRP B CD1 1 
ATOM   3869 C CD2 . TRP B 1 175 ? -28.631 23.238 -16.989 1.00 18.97 ? 174  TRP B CD2 1 
ATOM   3870 N NE1 . TRP B 1 175 ? -28.263 23.380 -19.195 1.00 19.37 ? 174  TRP B NE1 1 
ATOM   3871 C CE2 . TRP B 1 175 ? -27.868 22.727 -18.056 1.00 19.25 ? 174  TRP B CE2 1 
ATOM   3872 C CE3 . TRP B 1 175 ? -28.412 22.734 -15.701 1.00 22.59 ? 174  TRP B CE3 1 
ATOM   3873 C CZ2 . TRP B 1 175 ? -26.895 21.737 -17.877 1.00 21.38 ? 174  TRP B CZ2 1 
ATOM   3874 C CZ3 . TRP B 1 175 ? -27.460 21.747 -15.523 1.00 19.51 ? 174  TRP B CZ3 1 
ATOM   3875 C CH2 . TRP B 1 175 ? -26.704 21.262 -16.604 1.00 20.96 ? 174  TRP B CH2 1 
ATOM   3876 N N   . THR B 1 176 ? -29.000 27.670 -18.238 1.00 15.60 ? 175  THR B N   1 
ATOM   3877 C CA  . THR B 1 176 ? -27.836 28.543 -18.248 1.00 17.80 ? 175  THR B CA  1 
ATOM   3878 C C   . THR B 1 176 ? -28.133 29.930 -18.810 1.00 18.14 ? 175  THR B C   1 
ATOM   3879 O O   . THR B 1 176 ? -27.210 30.747 -18.945 1.00 17.57 ? 175  THR B O   1 
ATOM   3880 C CB  . THR B 1 176 ? -26.717 27.877 -19.060 1.00 17.09 ? 175  THR B CB  1 
ATOM   3881 O OG1 . THR B 1 176 ? -27.248 27.415 -20.309 1.00 19.50 ? 175  THR B OG1 1 
ATOM   3882 C CG2 . THR B 1 176 ? -26.149 26.679 -18.291 1.00 22.54 ? 175  THR B CG2 1 
ATOM   3883 N N   . TRP B 1 177 ? -29.393 30.227 -19.115 1.00 15.23 ? 176  TRP B N   1 
ATOM   3884 C CA  . TRP B 1 177 ? -29.698 31.386 -19.940 1.00 15.31 ? 176  TRP B CA  1 
ATOM   3885 C C   . TRP B 1 177 ? -29.373 32.699 -19.237 1.00 17.72 ? 176  TRP B C   1 
ATOM   3886 O O   . TRP B 1 177 ? -28.730 33.578 -19.821 1.00 18.92 ? 176  TRP B O   1 
ATOM   3887 C CB  . TRP B 1 177 ? -31.173 31.370 -20.352 1.00 15.16 ? 176  TRP B CB  1 
ATOM   3888 C CG  . TRP B 1 177 ? -31.485 32.506 -21.266 1.00 17.15 ? 176  TRP B CG  1 
ATOM   3889 C CD1 . TRP B 1 177 ? -31.816 33.795 -20.922 1.00 18.28 ? 176  TRP B CD1 1 
ATOM   3890 C CD2 . TRP B 1 177 ? -31.453 32.468 -22.689 1.00 14.03 ? 176  TRP B CD2 1 
ATOM   3891 N NE1 . TRP B 1 177 ? -31.975 34.563 -22.057 1.00 16.59 ? 176  TRP B NE1 1 
ATOM   3892 C CE2 . TRP B 1 177 ? -31.771 33.759 -23.152 1.00 17.01 ? 176  TRP B CE2 1 
ATOM   3893 C CE3 . TRP B 1 177 ? -31.181 31.459 -23.624 1.00 16.52 ? 176  TRP B CE3 1 
ATOM   3894 C CZ2 . TRP B 1 177 ? -31.821 34.073 -24.511 1.00 16.47 ? 176  TRP B CZ2 1 
ATOM   3895 C CZ3 . TRP B 1 177 ? -31.259 31.767 -24.977 1.00 16.08 ? 176  TRP B CZ3 1 
ATOM   3896 C CH2 . TRP B 1 177 ? -31.580 33.063 -25.403 1.00 15.54 ? 176  TRP B CH2 1 
ATOM   3897 N N   . THR B 1 178 ? -29.828 32.868 -17.991 1.00 15.91 ? 177  THR B N   1 
ATOM   3898 C CA  A THR B 1 178 ? -29.831 34.196 -17.389 0.53 17.70 ? 177  THR B CA  1 
ATOM   3899 C CA  B THR B 1 178 ? -29.831 34.207 -17.406 0.47 17.70 ? 177  THR B CA  1 
ATOM   3900 C C   . THR B 1 178 ? -28.422 34.766 -17.234 1.00 20.39 ? 177  THR B C   1 
ATOM   3901 O O   . THR B 1 178 ? -28.190 35.948 -17.507 1.00 23.67 ? 177  THR B O   1 
ATOM   3902 C CB  A THR B 1 178 ? -30.545 34.135 -16.046 0.53 20.35 ? 177  THR B CB  1 
ATOM   3903 C CB  B THR B 1 178 ? -30.576 34.226 -16.070 0.47 20.38 ? 177  THR B CB  1 
ATOM   3904 O OG1 A THR B 1 178 ? -31.886 33.680 -16.267 0.53 22.40 ? 177  THR B OG1 1 
ATOM   3905 O OG1 B THR B 1 178 ? -30.179 33.114 -15.262 0.47 22.79 ? 177  THR B OG1 1 
ATOM   3906 C CG2 A THR B 1 178 ? -30.579 35.500 -15.411 0.53 20.07 ? 177  THR B CG2 1 
ATOM   3907 C CG2 B THR B 1 178 ? -32.072 34.172 -16.311 0.47 21.73 ? 177  THR B CG2 1 
ATOM   3908 N N   . ASN B 1 179 ? -27.463 33.949 -16.811 1.00 20.30 ? 178  ASN B N   1 
ATOM   3909 C CA  . ASN B 1 179 ? -26.140 34.534 -16.586 1.00 23.91 ? 178  ASN B CA  1 
ATOM   3910 C C   . ASN B 1 179 ? -25.247 34.494 -17.813 1.00 22.91 ? 178  ASN B C   1 
ATOM   3911 O O   . ASN B 1 179 ? -24.157 35.077 -17.772 1.00 29.03 ? 178  ASN B O   1 
ATOM   3912 C CB  . ASN B 1 179 ? -25.412 33.858 -15.417 1.00 25.72 ? 178  ASN B CB  1 
ATOM   3913 C CG  . ASN B 1 179 ? -24.160 34.665 -14.921 1.00 31.84 ? 178  ASN B CG  1 
ATOM   3914 O OD1 . ASN B 1 179 ? -23.031 34.173 -14.978 1.00 25.11 ? 178  ASN B OD1 1 
ATOM   3915 N ND2 . ASN B 1 179 ? -24.378 35.892 -14.429 1.00 30.43 ? 178  ASN B ND2 1 
ATOM   3916 N N   . VAL B 1 180 ? -25.669 33.862 -18.905 1.00 15.81 ? 179  VAL B N   1 
ATOM   3917 C CA  . VAL B 1 180 ? -24.872 33.845 -20.128 1.00 17.37 ? 179  VAL B CA  1 
ATOM   3918 C C   . VAL B 1 180 ? -25.434 34.783 -21.190 1.00 19.45 ? 179  VAL B C   1 
ATOM   3919 O O   . VAL B 1 180 ? -24.677 35.526 -21.815 1.00 15.36 ? 179  VAL B O   1 
ATOM   3920 C CB  . VAL B 1 180 ? -24.756 32.405 -20.679 1.00 17.76 ? 179  VAL B CB  1 
ATOM   3921 C CG1 . VAL B 1 180 ? -24.220 32.397 -22.107 1.00 18.47 ? 179  VAL B CG1 1 
ATOM   3922 C CG2 . VAL B 1 180 ? -23.810 31.601 -19.788 1.00 17.45 ? 179  VAL B CG2 1 
ATOM   3923 N N   . ASN B 1 181 ? -26.755 34.764 -21.398 1.00 18.25 ? 180  ASN B N   1 
ATOM   3924 C CA  . ASN B 1 181 ? -27.369 35.313 -22.607 1.00 16.27 ? 180  ASN B CA  1 
ATOM   3925 C C   . ASN B 1 181 ? -28.171 36.586 -22.348 1.00 15.76 ? 180  ASN B C   1 
ATOM   3926 O O   . ASN B 1 181 ? -29.062 36.930 -23.135 1.00 15.90 ? 180  ASN B O   1 
ATOM   3927 C CB  . ASN B 1 181 ? -28.266 34.260 -23.264 1.00 16.06 ? 180  ASN B CB  1 
ATOM   3928 C CG  . ASN B 1 181 ? -27.465 33.195 -23.994 1.00 15.55 ? 180  ASN B CG  1 
ATOM   3929 O OD1 . ASN B 1 181 ? -26.628 33.513 -24.834 1.00 17.07 ? 180  ASN B OD1 1 
ATOM   3930 N ND2 . ASN B 1 181 ? -27.699 31.941 -23.657 1.00 15.12 ? 180  ASN B ND2 1 
ATOM   3931 N N   . ASP B 1 182 ? -27.858 37.321 -21.281 1.00 16.59 ? 181  ASP B N   1 
ATOM   3932 C CA  . ASP B 1 182 ? -28.626 38.529 -20.993 1.00 16.81 ? 181  ASP B CA  1 
ATOM   3933 C C   . ASP B 1 182 ? -28.591 39.515 -22.160 1.00 18.15 ? 181  ASP B C   1 
ATOM   3934 O O   . ASP B 1 182 ? -29.601 40.170 -22.453 1.00 18.95 ? 181  ASP B O   1 
ATOM   3935 C CB  . ASP B 1 182 ? -28.110 39.174 -19.705 1.00 14.70 ? 181  ASP B CB  1 
ATOM   3936 C CG  . ASP B 1 182 ? -28.928 40.383 -19.297 1.00 23.65 ? 181  ASP B CG  1 
ATOM   3937 O OD1 . ASP B 1 182 ? -30.149 40.221 -19.055 1.00 19.40 ? 181  ASP B OD1 1 
ATOM   3938 O OD2 . ASP B 1 182 ? -28.349 41.498 -19.241 1.00 25.02 ? 181  ASP B OD2 1 
ATOM   3939 N N   . ASN B 1 183 ? -27.455 39.599 -22.874 1.00 16.63 ? 182  ASN B N   1 
ATOM   3940 C CA  . ASN B 1 183 ? -27.329 40.596 -23.934 1.00 18.12 ? 182  ASN B CA  1 
ATOM   3941 C C   . ASN B 1 183 ? -28.292 40.348 -25.086 1.00 16.87 ? 182  ASN B C   1 
ATOM   3942 O O   . ASN B 1 183 ? -28.537 41.264 -25.877 1.00 17.60 ? 182  ASN B O   1 
ATOM   3943 C CB  . ASN B 1 183 ? -25.883 40.670 -24.456 1.00 17.37 ? 182  ASN B CB  1 
ATOM   3944 C CG  . ASN B 1 183 ? -25.463 39.464 -25.289 1.00 15.57 ? 182  ASN B CG  1 
ATOM   3945 O OD1 . ASN B 1 183 ? -26.018 38.367 -25.178 1.00 18.79 ? 182  ASN B OD1 1 
ATOM   3946 N ND2 . ASN B 1 183 ? -24.424 39.661 -26.097 1.00 18.37 ? 182  ASN B ND2 1 
ATOM   3947 N N   . MET B 1 184 ? -28.849 39.142 -25.183 1.00 15.06 ? 183  MET B N   1 
ATOM   3948 C CA  . MET B 1 184 ? -29.778 38.817 -26.258 1.00 13.31 ? 183  MET B CA  1 
ATOM   3949 C C   . MET B 1 184 ? -31.068 39.601 -26.157 1.00 13.79 ? 183  MET B C   1 
ATOM   3950 O O   . MET B 1 184 ? -31.827 39.634 -27.128 1.00 13.45 ? 183  MET B O   1 
ATOM   3951 C CB  . MET B 1 184 ? -30.088 37.317 -26.264 1.00 16.27 ? 183  MET B CB  1 
ATOM   3952 C CG  . MET B 1 184 ? -28.855 36.439 -26.490 1.00 14.46 ? 183  MET B CG  1 
ATOM   3953 S SD  . MET B 1 184 ? -28.656 36.203 -28.281 1.00 17.38 ? 183  MET B SD  1 
ATOM   3954 C CE  . MET B 1 184 ? -30.086 35.185 -28.673 1.00 18.51 ? 183  MET B CE  1 
ATOM   3955 N N   . LYS B 1 185 ? -31.347 40.228 -25.017 1.00 14.43 ? 184  LYS B N   1 
ATOM   3956 C CA  . LYS B 1 185 ? -32.543 41.058 -24.940 1.00 15.64 ? 184  LYS B CA  1 
ATOM   3957 C C   . LYS B 1 185 ? -32.513 42.232 -25.917 1.00 16.51 ? 184  LYS B C   1 
ATOM   3958 O O   . LYS B 1 185 ? -33.573 42.796 -26.221 1.00 17.73 ? 184  LYS B O   1 
ATOM   3959 C CB  . LYS B 1 185 ? -32.717 41.576 -23.510 1.00 18.14 ? 184  LYS B CB  1 
ATOM   3960 C CG  . LYS B 1 185 ? -31.594 42.488 -23.093 1.00 17.49 ? 184  LYS B CG  1 
ATOM   3961 C CD  . LYS B 1 185 ? -31.551 42.588 -21.563 1.00 21.61 ? 184  LYS B CD  1 
ATOM   3962 C CE  . LYS B 1 185 ? -30.353 43.407 -21.131 1.00 25.24 ? 184  LYS B CE  1 
ATOM   3963 N NZ  . LYS B 1 185 ? -30.270 43.451 -19.632 1.00 25.06 ? 184  LYS B NZ  1 
ATOM   3964 N N   . SER B 1 186 ? -31.340 42.619 -26.423 1.00 14.45 ? 185  SER B N   1 
ATOM   3965 C CA  A SER B 1 186 ? -31.275 43.802 -27.276 0.53 16.62 ? 185  SER B CA  1 
ATOM   3966 C CA  B SER B 1 186 ? -31.207 43.788 -27.285 0.47 16.63 ? 185  SER B CA  1 
ATOM   3967 C C   . SER B 1 186 ? -31.514 43.492 -28.744 1.00 18.23 ? 185  SER B C   1 
ATOM   3968 O O   . SER B 1 186 ? -31.482 44.416 -29.558 1.00 19.82 ? 185  SER B O   1 
ATOM   3969 C CB  A SER B 1 186 ? -29.931 44.509 -27.125 0.53 18.09 ? 185  SER B CB  1 
ATOM   3970 C CB  B SER B 1 186 ? -29.794 44.363 -27.180 0.47 17.89 ? 185  SER B CB  1 
ATOM   3971 O OG  A SER B 1 186 ? -28.876 43.653 -27.486 0.53 18.97 ? 185  SER B OG  1 
ATOM   3972 O OG  B SER B 1 186 ? -29.492 44.726 -25.842 0.47 18.65 ? 185  SER B OG  1 
ATOM   3973 N N   . LEU B 1 187 ? -31.763 42.234 -29.097 1.00 16.26 ? 186  LEU B N   1 
ATOM   3974 C CA  . LEU B 1 187 ? -32.139 41.926 -30.477 1.00 14.08 ? 186  LEU B CA  1 
ATOM   3975 C C   . LEU B 1 187 ? -33.366 42.734 -30.891 1.00 17.90 ? 186  LEU B C   1 
ATOM   3976 O O   . LEU B 1 187 ? -34.293 42.944 -30.101 1.00 17.40 ? 186  LEU B O   1 
ATOM   3977 C CB  . LEU B 1 187 ? -32.418 40.431 -30.624 1.00 13.58 ? 186  LEU B CB  1 
ATOM   3978 C CG  . LEU B 1 187 ? -31.143 39.579 -30.578 1.00 14.41 ? 186  LEU B CG  1 
ATOM   3979 C CD1 . LEU B 1 187 ? -31.503 38.106 -30.404 1.00 14.46 ? 186  LEU B CD1 1 
ATOM   3980 C CD2 . LEU B 1 187 ? -30.320 39.747 -31.862 1.00 16.87 ? 186  LEU B CD2 1 
ATOM   3981 N N   . THR B 1 188 ? -33.367 43.186 -32.143 1.00 16.45 ? 187  THR B N   1 
ATOM   3982 C CA  . THR B 1 188 ? -34.427 44.028 -32.691 1.00 14.83 ? 187  THR B CA  1 
ATOM   3983 C C   . THR B 1 188 ? -35.017 43.362 -33.934 1.00 17.39 ? 187  THR B C   1 
ATOM   3984 O O   . THR B 1 188 ? -34.314 42.666 -34.662 1.00 17.05 ? 187  THR B O   1 
ATOM   3985 C CB  . THR B 1 188 ? -33.881 45.429 -33.068 1.00 17.62 ? 187  THR B CB  1 
ATOM   3986 O OG1 . THR B 1 188 ? -32.976 45.314 -34.183 1.00 21.94 ? 187  THR B OG1 1 
ATOM   3987 C CG2 . THR B 1 188 ? -33.138 46.047 -31.917 1.00 25.52 ? 187  THR B CG2 1 
ATOM   3988 N N   . ASP B 1 189 ? -36.313 43.583 -34.176 1.00 15.62 ? 188  ASP B N   1 
ATOM   3989 C CA  . ASP B 1 189 ? -37.011 43.022 -35.345 1.00 17.44 ? 188  ASP B CA  1 
ATOM   3990 C C   . ASP B 1 189 ? -38.145 43.964 -35.735 1.00 17.61 ? 188  ASP B C   1 
ATOM   3991 O O   . ASP B 1 189 ? -39.053 44.191 -34.931 1.00 17.95 ? 188  ASP B O   1 
ATOM   3992 C CB  . ASP B 1 189 ? -37.554 41.624 -35.016 1.00 14.41 ? 188  ASP B CB  1 
ATOM   3993 C CG  . ASP B 1 189 ? -38.425 41.039 -36.110 1.00 15.07 ? 188  ASP B CG  1 
ATOM   3994 O OD1 . ASP B 1 189 ? -38.376 41.518 -37.276 1.00 15.73 ? 188  ASP B OD1 1 
ATOM   3995 O OD2 . ASP B 1 189 ? -39.175 40.078 -35.800 1.00 15.77 ? 188  ASP B OD2 1 
ATOM   3996 N N   . PRO B 1 190 ? -38.129 44.541 -36.937 1.00 15.91 ? 189  PRO B N   1 
ATOM   3997 C CA  . PRO B 1 190 ? -39.234 45.433 -37.329 1.00 18.50 ? 189  PRO B CA  1 
ATOM   3998 C C   . PRO B 1 190 ? -40.593 44.747 -37.369 1.00 18.03 ? 189  PRO B C   1 
ATOM   3999 O O   . PRO B 1 190 ? -41.616 45.437 -37.220 1.00 21.26 ? 189  PRO B O   1 
ATOM   4000 C CB  . PRO B 1 190 ? -38.807 45.938 -38.717 1.00 20.37 ? 189  PRO B CB  1 
ATOM   4001 C CG  . PRO B 1 190 ? -37.840 44.943 -39.213 1.00 20.04 ? 189  PRO B CG  1 
ATOM   4002 C CD  . PRO B 1 190 ? -37.104 44.429 -37.986 1.00 17.80 ? 189  PRO B CD  1 
ATOM   4003 N N   . SER B 1 191 ? -40.639 43.418 -37.522 1.00 17.44 ? 190  SER B N   1 
ATOM   4004 C CA  . SER B 1 191 ? -41.895 42.680 -37.478 1.00 16.88 ? 190  SER B CA  1 
ATOM   4005 C C   . SER B 1 191 ? -42.348 42.346 -36.065 1.00 14.70 ? 190  SER B C   1 
ATOM   4006 O O   . SER B 1 191 ? -43.478 41.872 -35.903 1.00 18.61 ? 190  SER B O   1 
ATOM   4007 C CB  . SER B 1 191 ? -41.778 41.383 -38.274 1.00 20.27 ? 190  SER B CB  1 
ATOM   4008 O OG  . SER B 1 191 ? -41.573 41.679 -39.646 1.00 20.98 ? 190  SER B OG  1 
ATOM   4009 N N   . ASP B 1 192 ? -41.494 42.555 -35.056 1.00 15.87 ? 191  ASP B N   1 
ATOM   4010 C CA  . ASP B 1 192 ? -41.828 42.264 -33.656 1.00 16.15 ? 191  ASP B CA  1 
ATOM   4011 C C   . ASP B 1 192 ? -42.267 40.806 -33.482 1.00 18.21 ? 191  ASP B C   1 
ATOM   4012 O O   . ASP B 1 192 ? -43.257 40.499 -32.804 1.00 19.53 ? 191  ASP B O   1 
ATOM   4013 C CB  . ASP B 1 192 ? -42.890 43.243 -33.151 1.00 18.78 ? 191  ASP B CB  1 
ATOM   4014 C CG  . ASP B 1 192 ? -43.107 43.146 -31.661 1.00 31.20 ? 191  ASP B CG  1 
ATOM   4015 O OD1 . ASP B 1 192 ? -42.170 42.723 -30.946 1.00 27.08 ? 191  ASP B OD1 1 
ATOM   4016 O OD2 . ASP B 1 192 ? -44.226 43.482 -31.212 1.00 31.37 ? 191  ASP B OD2 1 
ATOM   4017 N N   . LYS B 1 193 ? -41.498 39.891 -34.076 1.00 15.88 ? 192  LYS B N   1 
ATOM   4018 C CA  . LYS B 1 193 ? -41.829 38.474 -34.001 1.00 15.69 ? 192  LYS B CA  1 
ATOM   4019 C C   . LYS B 1 193 ? -40.626 37.635 -33.595 1.00 15.23 ? 192  LYS B C   1 
ATOM   4020 O O   . LYS B 1 193 ? -40.452 36.509 -34.065 1.00 16.68 ? 192  LYS B O   1 
ATOM   4021 C CB  . LYS B 1 193 ? -42.424 37.987 -35.323 1.00 16.46 ? 192  LYS B CB  1 
ATOM   4022 C CG  . LYS B 1 193 ? -43.869 38.418 -35.502 1.00 16.05 ? 192  LYS B CG  1 
ATOM   4023 C CD  . LYS B 1 193 ? -44.502 37.708 -36.698 1.00 20.32 ? 192  LYS B CD  1 
ATOM   4024 C CE  . LYS B 1 193 ? -46.006 37.917 -36.721 1.00 21.84 ? 192  LYS B CE  1 
ATOM   4025 N NZ  . LYS B 1 193 ? -46.372 39.359 -36.820 1.00 26.05 ? 192  LYS B NZ  1 
ATOM   4026 N N   . ILE B 1 194 ? -39.816 38.138 -32.661 1.00 14.56 ? 193  ILE B N   1 
ATOM   4027 C CA  . ILE B 1 194 ? -38.703 37.357 -32.123 1.00 15.74 ? 193  ILE B CA  1 
ATOM   4028 C C   . ILE B 1 194 ? -39.236 36.421 -31.046 1.00 16.85 ? 193  ILE B C   1 
ATOM   4029 O O   . ILE B 1 194 ? -39.967 36.854 -30.153 1.00 16.83 ? 193  ILE B O   1 
ATOM   4030 C CB  . ILE B 1 194 ? -37.622 38.278 -31.532 1.00 12.90 ? 193  ILE B CB  1 
ATOM   4031 C CG1 . ILE B 1 194 ? -36.908 39.085 -32.621 1.00 14.39 ? 193  ILE B CG1 1 
ATOM   4032 C CG2 . ILE B 1 194 ? -36.591 37.458 -30.694 1.00 13.14 ? 193  ILE B CG2 1 
ATOM   4033 C CD1 . ILE B 1 194 ? -36.073 40.218 -32.068 1.00 17.69 ? 193  ILE B CD1 1 
ATOM   4034 N N   . ILE B 1 195 ? -38.875 35.139 -31.123 1.00 14.46 ? 194  ILE B N   1 
ATOM   4035 C CA  . ILE B 1 195 ? -39.123 34.195 -30.034 1.00 15.80 ? 194  ILE B CA  1 
ATOM   4036 C C   . ILE B 1 195 ? -37.780 33.672 -29.563 1.00 14.21 ? 194  ILE B C   1 
ATOM   4037 O O   . ILE B 1 195 ? -36.980 33.200 -30.382 1.00 13.80 ? 194  ILE B O   1 
ATOM   4038 C CB  . ILE B 1 195 ? -40.019 33.018 -30.476 1.00 14.18 ? 194  ILE B CB  1 
ATOM   4039 C CG1 . ILE B 1 195 ? -41.261 33.523 -31.215 1.00 15.71 ? 194  ILE B CG1 1 
ATOM   4040 C CG2 . ILE B 1 195 ? -40.378 32.145 -29.261 1.00 14.26 ? 194  ILE B CG2 1 
ATOM   4041 C CD1 . ILE B 1 195 ? -42.251 34.306 -30.338 1.00 16.23 ? 194  ILE B CD1 1 
ATOM   4042 N N   . TYR B 1 196 ? -37.540 33.724 -28.244 1.00 14.51 ? 195  TYR B N   1 
ATOM   4043 C CA  . TYR B 1 196 ? -36.296 33.211 -27.681 1.00 15.49 ? 195  TYR B CA  1 
ATOM   4044 C C   . TYR B 1 196 ? -36.401 31.698 -27.505 1.00 16.94 ? 195  TYR B C   1 
ATOM   4045 O O   . TYR B 1 196 ? -37.116 31.205 -26.624 1.00 16.60 ? 195  TYR B O   1 
ATOM   4046 C CB  . TYR B 1 196 ? -35.980 33.932 -26.366 1.00 14.95 ? 195  TYR B CB  1 
ATOM   4047 C CG  . TYR B 1 196 ? -35.590 35.365 -26.614 1.00 14.43 ? 195  TYR B CG  1 
ATOM   4048 C CD1 . TYR B 1 196 ? -36.556 36.346 -26.803 1.00 15.02 ? 195  TYR B CD1 1 
ATOM   4049 C CD2 . TYR B 1 196 ? -34.260 35.735 -26.704 1.00 14.99 ? 195  TYR B CD2 1 
ATOM   4050 C CE1 . TYR B 1 196 ? -36.192 37.659 -27.064 1.00 17.27 ? 195  TYR B CE1 1 
ATOM   4051 C CE2 . TYR B 1 196 ? -33.894 37.044 -26.975 1.00 16.98 ? 195  TYR B CE2 1 
ATOM   4052 C CZ  . TYR B 1 196 ? -34.863 38.003 -27.133 1.00 16.03 ? 195  TYR B CZ  1 
ATOM   4053 O OH  . TYR B 1 196 ? -34.492 39.308 -27.405 1.00 18.04 ? 195  TYR B OH  1 
ATOM   4054 N N   . GLU B 1 197 ? -35.675 30.954 -28.334 1.00 12.87 ? 196  GLU B N   1 
ATOM   4055 C CA  . GLU B 1 197 ? -35.721 29.499 -28.303 1.00 14.16 ? 196  GLU B CA  1 
ATOM   4056 C C   . GLU B 1 197 ? -34.637 28.965 -27.379 1.00 15.09 ? 196  GLU B C   1 
ATOM   4057 O O   . GLU B 1 197 ? -33.447 29.214 -27.598 1.00 15.35 ? 196  GLU B O   1 
ATOM   4058 C CB  . GLU B 1 197 ? -35.535 28.923 -29.703 1.00 13.73 ? 196  GLU B CB  1 
ATOM   4059 C CG  . GLU B 1 197 ? -35.445 27.403 -29.669 1.00 14.89 ? 196  GLU B CG  1 
ATOM   4060 C CD  . GLU B 1 197 ? -35.172 26.828 -31.031 1.00 17.48 ? 196  GLU B CD  1 
ATOM   4061 O OE1 . GLU B 1 197 ? -35.036 27.615 -31.990 1.00 16.81 ? 196  GLU B OE1 1 
ATOM   4062 O OE2 . GLU B 1 197 ? -35.046 25.595 -31.133 1.00 20.73 ? 196  GLU B OE2 1 
ATOM   4063 N N   . MET B 1 198 ? -35.055 28.254 -26.334 1.00 14.01 ? 197  MET B N   1 
ATOM   4064 C CA  . MET B 1 198 ? -34.146 27.608 -25.404 1.00 11.69 ? 197  MET B CA  1 
ATOM   4065 C C   . MET B 1 198 ? -34.392 26.108 -25.433 1.00 14.98 ? 197  MET B C   1 
ATOM   4066 O O   . MET B 1 198 ? -35.488 25.659 -25.760 1.00 14.65 ? 197  MET B O   1 
ATOM   4067 C CB  . MET B 1 198 ? -34.367 28.142 -23.981 1.00 15.62 ? 197  MET B CB  1 
ATOM   4068 C CG  . MET B 1 198 ? -34.412 29.664 -23.954 1.00 12.78 ? 197  MET B CG  1 
ATOM   4069 S SD  . MET B 1 198 ? -34.534 30.257 -22.238 1.00 15.48 ? 197  MET B SD  1 
ATOM   4070 C CE  . MET B 1 198 ? -34.965 31.978 -22.505 1.00 18.72 ? 197  MET B CE  1 
ATOM   4071 N N   . HIS B 1 199 ? -33.366 25.336 -25.099 1.00 14.32 ? 198  HIS B N   1 
ATOM   4072 C CA  . HIS B 1 199 ? -33.466 23.886 -25.011 1.00 16.02 ? 198  HIS B CA  1 
ATOM   4073 C C   . HIS B 1 199 ? -33.294 23.451 -23.567 1.00 18.82 ? 198  HIS B C   1 
ATOM   4074 O O   . HIS B 1 199 ? -32.565 24.087 -22.804 1.00 17.63 ? 198  HIS B O   1 
ATOM   4075 C CB  . HIS B 1 199 ? -32.396 23.215 -25.864 1.00 13.78 ? 198  HIS B CB  1 
ATOM   4076 C CG  . HIS B 1 199 ? -32.507 23.553 -27.315 1.00 14.50 ? 198  HIS B CG  1 
ATOM   4077 N ND1 . HIS B 1 199 ? -31.541 23.212 -28.232 1.00 18.88 ? 198  HIS B ND1 1 
ATOM   4078 C CD2 . HIS B 1 199 ? -33.482 24.189 -28.004 1.00 14.68 ? 198  HIS B CD2 1 
ATOM   4079 C CE1 . HIS B 1 199 ? -31.914 23.622 -29.436 1.00 14.68 ? 198  HIS B CE1 1 
ATOM   4080 N NE2 . HIS B 1 199 ? -33.083 24.229 -29.322 1.00 13.98 ? 198  HIS B NE2 1 
ATOM   4081 N N   . GLN B 1 200 ? -33.961 22.359 -23.188 1.00 15.22 ? 199  GLN B N   1 
ATOM   4082 C CA  . GLN B 1 200 ? -33.745 21.831 -21.842 1.00 15.56 ? 199  GLN B CA  1 
ATOM   4083 C C   . GLN B 1 200 ? -33.836 20.314 -21.857 1.00 17.48 ? 199  GLN B C   1 
ATOM   4084 O O   . GLN B 1 200 ? -34.921 19.745 -22.048 1.00 18.44 ? 199  GLN B O   1 
ATOM   4085 C CB  . GLN B 1 200 ? -34.736 22.402 -20.847 1.00 17.19 ? 199  GLN B CB  1 
ATOM   4086 C CG  . GLN B 1 200 ? -34.251 22.113 -19.417 1.00 14.94 ? 199  GLN B CG  1 
ATOM   4087 C CD  . GLN B 1 200 ? -32.889 22.740 -19.197 1.00 14.70 ? 199  GLN B CD  1 
ATOM   4088 O OE1 . GLN B 1 200 ? -32.763 23.969 -19.187 1.00 17.51 ? 199  GLN B OE1 1 
ATOM   4089 N NE2 . GLN B 1 200 ? -31.851 21.902 -19.062 1.00 16.01 ? 199  GLN B NE2 1 
ATOM   4090 N N   . PHE B 1 201 ? -32.715 19.667 -21.590 1.00 16.19 ? 200  PHE B N   1 
ATOM   4091 C CA  . PHE B 1 201 ? -32.697 18.240 -21.321 1.00 16.70 ? 200  PHE B CA  1 
ATOM   4092 C C   . PHE B 1 201 ? -32.586 18.019 -19.821 1.00 16.79 ? 200  PHE B C   1 
ATOM   4093 O O   . PHE B 1 201 ? -32.315 18.947 -19.052 1.00 17.55 ? 200  PHE B O   1 
ATOM   4094 C CB  . PHE B 1 201 ? -31.570 17.563 -22.104 1.00 15.91 ? 200  PHE B CB  1 
ATOM   4095 C CG  . PHE B 1 201 ? -31.831 17.575 -23.580 1.00 17.01 ? 200  PHE B CG  1 
ATOM   4096 C CD1 . PHE B 1 201 ? -32.681 16.638 -24.145 1.00 18.17 ? 200  PHE B CD1 1 
ATOM   4097 C CD2 . PHE B 1 201 ? -31.293 18.567 -24.382 1.00 18.16 ? 200  PHE B CD2 1 
ATOM   4098 C CE1 . PHE B 1 201 ? -32.986 16.667 -25.501 1.00 17.24 ? 200  PHE B CE1 1 
ATOM   4099 C CE2 . PHE B 1 201 ? -31.579 18.606 -25.751 1.00 20.91 ? 200  PHE B CE2 1 
ATOM   4100 C CZ  . PHE B 1 201 ? -32.429 17.654 -26.308 1.00 20.72 ? 200  PHE B CZ  1 
ATOM   4101 N N   . LEU B 1 202 ? -32.858 16.780 -19.410 1.00 15.31 ? 201  LEU B N   1 
ATOM   4102 C CA  . LEU B 1 202 ? -33.187 16.484 -18.020 1.00 17.19 ? 201  LEU B CA  1 
ATOM   4103 C C   . LEU B 1 202 ? -32.227 15.507 -17.361 1.00 19.56 ? 201  LEU B C   1 
ATOM   4104 O O   . LEU B 1 202 ? -32.446 15.138 -16.193 1.00 19.55 ? 201  LEU B O   1 
ATOM   4105 C CB  . LEU B 1 202 ? -34.625 15.935 -17.932 1.00 17.62 ? 201  LEU B CB  1 
ATOM   4106 C CG  . LEU B 1 202 ? -35.672 16.777 -18.663 1.00 20.31 ? 201  LEU B CG  1 
ATOM   4107 C CD1 . LEU B 1 202 ? -37.032 16.102 -18.597 1.00 20.79 ? 201  LEU B CD1 1 
ATOM   4108 C CD2 . LEU B 1 202 ? -35.735 18.183 -18.085 1.00 19.36 ? 201  LEU B CD2 1 
ATOM   4109 N N   . ASP B 1 203 ? -31.174 15.091 -18.056 1.00 17.59 ? 202  ASP B N   1 
ATOM   4110 C CA  . ASP B 1 203 ? -30.168 14.229 -17.467 1.00 21.68 ? 202  ASP B CA  1 
ATOM   4111 C C   . ASP B 1 203 ? -29.117 15.056 -16.730 1.00 18.73 ? 202  ASP B C   1 
ATOM   4112 O O   . ASP B 1 203 ? -29.140 16.291 -16.734 1.00 18.36 ? 202  ASP B O   1 
ATOM   4113 C CB  . ASP B 1 203 ? -29.527 13.314 -18.528 1.00 19.96 ? 202  ASP B CB  1 
ATOM   4114 C CG  . ASP B 1 203 ? -29.008 14.048 -19.766 1.00 22.52 ? 202  ASP B CG  1 
ATOM   4115 O OD1 . ASP B 1 203 ? -29.277 15.245 -19.967 1.00 19.79 ? 202  ASP B OD1 1 
ATOM   4116 O OD2 . ASP B 1 203 ? -28.310 13.374 -20.558 1.00 20.79 ? 202  ASP B OD2 1 
ATOM   4117 N N   . SER B 1 204 ? -28.220 14.331 -16.048 1.00 25.63 ? 203  SER B N   1 
ATOM   4118 C CA  . SER B 1 204 ? -27.143 14.849 -15.209 1.00 32.52 ? 203  SER B CA  1 
ATOM   4119 C C   . SER B 1 204 ? -26.598 16.192 -15.676 1.00 26.34 ? 203  SER B C   1 
ATOM   4120 O O   . SER B 1 204 ? -26.737 17.205 -14.980 1.00 28.68 ? 203  SER B O   1 
ATOM   4121 C CB  . SER B 1 204 ? -26.003 13.822 -15.163 1.00 35.54 ? 203  SER B CB  1 
ATOM   4122 O OG  . SER B 1 204 ? -25.616 13.435 -16.493 1.00 34.77 ? 203  SER B OG  1 
ATOM   4123 N N   . ASP B 1 205 ? -25.980 16.201 -16.852 1.00 22.33 ? 204  ASP B N   1 
ATOM   4124 C CA  . ASP B 1 205 ? -25.269 17.359 -17.374 1.00 24.34 ? 204  ASP B CA  1 
ATOM   4125 C C   . ASP B 1 205 ? -26.067 18.147 -18.409 1.00 21.98 ? 204  ASP B C   1 
ATOM   4126 O O   . ASP B 1 205 ? -25.494 18.999 -19.095 1.00 22.89 ? 204  ASP B O   1 
ATOM   4127 C CB  . ASP B 1 205 ? -23.933 16.912 -17.978 1.00 26.84 ? 204  ASP B CB  1 
ATOM   4128 C CG  . ASP B 1 205 ? -24.106 15.894 -19.090 1.00 26.27 ? 204  ASP B CG  1 
ATOM   4129 O OD1 . ASP B 1 205 ? -25.258 15.587 -19.465 1.00 23.95 ? 204  ASP B OD1 1 
ATOM   4130 O OD2 . ASP B 1 205 ? -23.085 15.386 -19.597 1.00 30.25 ? 204  ASP B OD2 1 
ATOM   4131 N N   . GLY B 1 206 ? -27.367 17.875 -18.551 1.00 19.91 ? 205  GLY B N   1 
ATOM   4132 C CA  . GLY B 1 206 ? -28.183 18.568 -19.536 1.00 20.08 ? 205  GLY B CA  1 
ATOM   4133 C C   . GLY B 1 206 ? -27.847 18.291 -20.987 1.00 19.22 ? 205  GLY B C   1 
ATOM   4134 O O   . GLY B 1 206 ? -28.315 19.025 -21.866 1.00 19.39 ? 205  GLY B O   1 
ATOM   4135 N N   . SER B 1 207 ? -27.042 17.262 -21.262 1.00 17.56 ? 206  SER B N   1 
ATOM   4136 C CA  . SER B 1 207 ? -26.615 16.968 -22.626 1.00 16.65 ? 206  SER B CA  1 
ATOM   4137 C C   . SER B 1 207 ? -27.685 16.270 -23.460 1.00 19.15 ? 206  SER B C   1 
ATOM   4138 O O   . SER B 1 207 ? -27.570 16.253 -24.697 1.00 22.02 ? 206  SER B O   1 
ATOM   4139 C CB  . SER B 1 207 ? -25.352 16.096 -22.592 1.00 20.23 ? 206  SER B CB  1 
ATOM   4140 O OG  . SER B 1 207 ? -25.611 14.854 -21.952 1.00 22.76 ? 206  SER B OG  1 
ATOM   4141 N N   . GLY B 1 208 ? -28.708 15.681 -22.836 1.00 20.04 ? 207  GLY B N   1 
ATOM   4142 C CA  . GLY B 1 208 ? -29.674 14.917 -23.618 1.00 17.79 ? 207  GLY B CA  1 
ATOM   4143 C C   . GLY B 1 208 ? -29.116 13.638 -24.196 1.00 21.43 ? 207  GLY B C   1 
ATOM   4144 O O   . GLY B 1 208 ? -29.476 13.257 -25.324 1.00 22.49 ? 207  GLY B O   1 
ATOM   4145 N N   . THR B 1 209 ? -28.208 12.978 -23.479 1.00 17.30 ? 208  THR B N   1 
ATOM   4146 C CA  . THR B 1 209 ? -27.638 11.732 -23.968 1.00 19.48 ? 208  THR B CA  1 
ATOM   4147 C C   . THR B 1 209 ? -28.009 10.512 -23.136 1.00 22.08 ? 208  THR B C   1 
ATOM   4148 O O   . THR B 1 209 ? -27.818 9.390  -23.613 1.00 27.20 ? 208  THR B O   1 
ATOM   4149 C CB  . THR B 1 209 ? -26.111 11.832 -24.054 1.00 25.24 ? 208  THR B CB  1 
ATOM   4150 O OG1 . THR B 1 209 ? -25.584 12.151 -22.767 1.00 25.20 ? 208  THR B OG1 1 
ATOM   4151 C CG2 . THR B 1 209 ? -25.693 12.909 -25.039 1.00 22.33 ? 208  THR B CG2 1 
ATOM   4152 N N   . SER B 1 210 ? -28.535 10.691 -21.920 1.00 19.75 ? 209  SER B N   1 
ATOM   4153 C CA  . SER B 1 210 ? -28.994 9.594  -21.082 1.00 23.15 ? 209  SER B CA  1 
ATOM   4154 C C   . SER B 1 210 ? -30.510 9.624  -20.933 1.00 22.89 ? 209  SER B C   1 
ATOM   4155 O O   . SER B 1 210 ? -31.122 10.697 -20.887 1.00 20.48 ? 209  SER B O   1 
ATOM   4156 C CB  . SER B 1 210 ? -28.347 9.668  -19.696 1.00 22.57 ? 209  SER B CB  1 
ATOM   4157 O OG  . SER B 1 210 ? -28.917 8.718  -18.800 1.00 25.90 ? 209  SER B OG  1 
ATOM   4158 N N   . ALA B 1 211 ? -31.110 8.428  -20.851 1.00 20.21 ? 210  ALA B N   1 
ATOM   4159 C CA  . ALA B 1 211 ? -32.542 8.300  -20.589 1.00 22.13 ? 210  ALA B CA  1 
ATOM   4160 C C   . ALA B 1 211 ? -32.900 8.549  -19.135 1.00 20.21 ? 210  ALA B C   1 
ATOM   4161 O O   . ALA B 1 211 ? -34.092 8.654  -18.817 1.00 22.92 ? 210  ALA B O   1 
ATOM   4162 C CB  . ALA B 1 211 ? -33.045 6.907  -20.984 1.00 21.47 ? 210  ALA B CB  1 
ATOM   4163 N N   . THR B 1 212 ? -31.909 8.648  -18.253 1.00 19.82 ? 211  THR B N   1 
ATOM   4164 C CA  . THR B 1 212 ? -32.145 8.889  -16.837 1.00 21.30 ? 211  THR B CA  1 
ATOM   4165 C C   . THR B 1 212 ? -32.252 10.384 -16.568 1.00 21.66 ? 211  THR B C   1 
ATOM   4166 O O   . THR B 1 212 ? -31.410 11.161 -17.024 1.00 24.40 ? 211  THR B O   1 
ATOM   4167 C CB  . THR B 1 212 ? -31.016 8.293  -16.003 1.00 22.18 ? 211  THR B CB  1 
ATOM   4168 O OG1 . THR B 1 212 ? -30.946 6.886  -16.251 1.00 25.35 ? 211  THR B OG1 1 
ATOM   4169 C CG2 . THR B 1 212 ? -31.268 8.532  -14.502 1.00 26.66 ? 211  THR B CG2 1 
ATOM   4170 N N   . CYS B 1 213 ? -33.275 10.776 -15.812 1.00 21.99 ? 212  CYS B N   1 
ATOM   4171 C CA  . CYS B 1 213 ? -33.447 12.155 -15.376 1.00 20.44 ? 212  CYS B CA  1 
ATOM   4172 C C   . CYS B 1 213 ? -32.954 12.325 -13.944 1.00 21.53 ? 212  CYS B C   1 
ATOM   4173 O O   . CYS B 1 213 ? -33.009 11.389 -13.140 1.00 22.05 ? 212  CYS B O   1 
ATOM   4174 C CB  . CYS B 1 213 ? -34.914 12.583 -15.490 1.00 21.74 ? 212  CYS B CB  1 
ATOM   4175 S SG  . CYS B 1 213 ? -35.489 12.561 -17.235 1.00 21.61 ? 212  CYS B SG  1 
ATOM   4176 N N   . VAL B 1 214 ? -32.461 13.536 -13.641 1.00 19.46 ? 213  VAL B N   1 
ATOM   4177 C CA  . VAL B 1 214 ? -31.893 13.828 -12.320 1.00 20.65 ? 213  VAL B CA  1 
ATOM   4178 C C   . VAL B 1 214 ? -32.924 13.603 -11.220 1.00 19.28 ? 213  VAL B C   1 
ATOM   4179 O O   . VAL B 1 214 ? -32.614 13.040 -10.153 1.00 19.92 ? 213  VAL B O   1 
ATOM   4180 C CB  . VAL B 1 214 ? -31.362 15.276 -12.280 1.00 21.25 ? 213  VAL B CB  1 
ATOM   4181 C CG1 . VAL B 1 214 ? -30.842 15.621 -10.890 1.00 21.63 ? 213  VAL B CG1 1 
ATOM   4182 C CG2 . VAL B 1 214 ? -30.283 15.485 -13.315 1.00 22.80 ? 213  VAL B CG2 1 
ATOM   4183 N N   . SER B 1 215 ? -34.155 14.062 -11.448 1.00 17.16 ? 214  SER B N   1 
ATOM   4184 C CA  . SER B 1 215 ? -35.177 14.059 -10.410 1.00 22.41 ? 214  SER B CA  1 
ATOM   4185 C C   . SER B 1 215 ? -36.526 14.306 -11.063 1.00 20.09 ? 214  SER B C   1 
ATOM   4186 O O   . SER B 1 215 ? -36.618 14.695 -12.236 1.00 21.04 ? 214  SER B O   1 
ATOM   4187 C CB  . SER B 1 215 ? -34.902 15.126 -9.353  1.00 20.93 ? 214  SER B CB  1 
ATOM   4188 O OG  . SER B 1 215 ? -35.320 16.384 -9.849  1.00 20.50 ? 214  SER B OG  1 
ATOM   4189 N N   . SER B 1 216 ? -37.572 14.099 -10.275 1.00 19.05 ? 215  SER B N   1 
ATOM   4190 C CA  A SER B 1 216 ? -38.943 14.302 -10.723 0.42 20.66 ? 215  SER B CA  1 
ATOM   4191 C CA  B SER B 1 216 ? -38.930 14.298 -10.761 0.58 20.60 ? 215  SER B CA  1 
ATOM   4192 C C   . SER B 1 216 ? -39.311 15.767 -10.894 1.00 18.32 ? 215  SER B C   1 
ATOM   4193 O O   . SER B 1 216 ? -40.410 16.056 -11.383 1.00 19.98 ? 215  SER B O   1 
ATOM   4194 C CB  A SER B 1 216 ? -39.918 13.666 -9.728  0.42 20.00 ? 215  SER B CB  1 
ATOM   4195 C CB  B SER B 1 216 ? -39.905 13.597 -9.819  0.58 20.13 ? 215  SER B CB  1 
ATOM   4196 O OG  A SER B 1 216 ? -39.869 12.258 -9.802  0.42 23.37 ? 215  SER B OG  1 
ATOM   4197 O OG  B SER B 1 216 ? -39.608 13.960 -8.490  0.58 21.14 ? 215  SER B OG  1 
ATOM   4198 N N   . THR B 1 217 ? -38.457 16.699 -10.475 1.00 17.68 ? 216  THR B N   1 
ATOM   4199 C CA  . THR B 1 217 ? -38.779 18.114 -10.586 1.00 15.57 ? 216  THR B CA  1 
ATOM   4200 C C   . THR B 1 217 ? -37.751 18.887 -11.392 1.00 19.11 ? 216  THR B C   1 
ATOM   4201 O O   . THR B 1 217 ? -37.804 20.125 -11.406 1.00 18.97 ? 216  THR B O   1 
ATOM   4202 C CB  . THR B 1 217 ? -38.918 18.746 -9.203  1.00 17.78 ? 216  THR B CB  1 
ATOM   4203 O OG1 . THR B 1 217 ? -37.690 18.590 -8.479  1.00 18.50 ? 216  THR B OG1 1 
ATOM   4204 C CG2 . THR B 1 217 ? -40.049 18.075 -8.418  1.00 20.67 ? 216  THR B CG2 1 
ATOM   4205 N N   . ILE B 1 218 ? -36.836 18.194 -12.073 1.00 18.68 ? 217  ILE B N   1 
ATOM   4206 C CA  . ILE B 1 218 ? -35.649 18.870 -12.599 1.00 19.18 ? 217  ILE B CA  1 
ATOM   4207 C C   . ILE B 1 218 ? -35.998 19.777 -13.771 1.00 16.42 ? 217  ILE B C   1 
ATOM   4208 O O   . ILE B 1 218 ? -35.311 20.779 -14.014 1.00 17.81 ? 217  ILE B O   1 
ATOM   4209 C CB  . ILE B 1 218 ? -34.568 17.836 -12.975 1.00 19.40 ? 217  ILE B CB  1 
ATOM   4210 C CG1 . ILE B 1 218 ? -33.229 18.523 -13.259 1.00 20.17 ? 217  ILE B CG1 1 
ATOM   4211 C CG2 . ILE B 1 218 ? -35.008 16.980 -14.196 1.00 18.86 ? 217  ILE B CG2 1 
ATOM   4212 C CD1 . ILE B 1 218 ? -32.485 19.029 -12.020 1.00 26.45 ? 217  ILE B CD1 1 
ATOM   4213 N N   . GLY B 1 219 ? -37.055 19.458 -14.518 1.00 17.83 ? 218  GLY B N   1 
ATOM   4214 C CA  . GLY B 1 219 ? -37.407 20.303 -15.653 1.00 17.80 ? 218  GLY B CA  1 
ATOM   4215 C C   . GLY B 1 219 ? -37.887 21.676 -15.219 1.00 16.93 ? 218  GLY B C   1 
ATOM   4216 O O   . GLY B 1 219 ? -37.364 22.701 -15.665 1.00 17.74 ? 218  GLY B O   1 
ATOM   4217 N N   . GLN B 1 220 ? -38.894 21.704 -14.345 1.00 16.99 ? 219  GLN B N   1 
ATOM   4218 C CA  . GLN B 1 220 ? -39.345 22.944 -13.721 1.00 17.73 ? 219  GLN B CA  1 
ATOM   4219 C C   . GLN B 1 220 ? -38.184 23.724 -13.119 1.00 20.31 ? 219  GLN B C   1 
ATOM   4220 O O   . GLN B 1 220 ? -38.046 24.931 -13.359 1.00 20.91 ? 219  GLN B O   1 
ATOM   4221 C CB  . GLN B 1 220 ? -40.378 22.630 -12.632 1.00 19.38 ? 219  GLN B CB  1 
ATOM   4222 C CG  . GLN B 1 220 ? -40.761 23.858 -11.823 1.00 18.25 ? 219  GLN B CG  1 
ATOM   4223 C CD  . GLN B 1 220 ? -41.818 23.566 -10.769 1.00 18.98 ? 219  GLN B CD  1 
ATOM   4224 O OE1 . GLN B 1 220 ? -42.409 22.478 -10.733 1.00 19.92 ? 219  GLN B OE1 1 
ATOM   4225 N NE2 . GLN B 1 220 ? -42.064 24.542 -9.905  1.00 19.90 ? 219  GLN B NE2 1 
ATOM   4226 N N   . GLU B 1 221 ? -37.344 23.051 -12.315 1.00 21.52 ? 220  GLU B N   1 
ATOM   4227 C CA  . GLU B 1 221 ? -36.223 23.741 -11.671 1.00 18.91 ? 220  GLU B CA  1 
ATOM   4228 C C   . GLU B 1 221 ? -35.346 24.436 -12.698 1.00 19.30 ? 220  GLU B C   1 
ATOM   4229 O O   . GLU B 1 221 ? -34.929 25.584 -12.494 1.00 19.41 ? 220  GLU B O   1 
ATOM   4230 C CB  . GLU B 1 221 ? -35.352 22.769 -10.867 1.00 19.38 ? 220  GLU B CB  1 
ATOM   4231 C CG  . GLU B 1 221 ? -36.005 22.035 -9.712  1.00 28.38 ? 220  GLU B CG  1 
ATOM   4232 C CD  . GLU B 1 221 ? -35.062 21.000 -9.108  1.00 26.18 ? 220  GLU B CD  1 
ATOM   4233 O OE1 . GLU B 1 221 ? -33.891 21.356 -8.851  1.00 45.41 ? 220  GLU B OE1 1 
ATOM   4234 O OE2 . GLU B 1 221 ? -35.472 19.833 -8.899  1.00 35.35 ? 220  GLU B OE2 1 
ATOM   4235 N N   . ARG B 1 222 ? -35.047 23.746 -13.803 1.00 18.41 ? 221  ARG B N   1 
ATOM   4236 C CA  . ARG B 1 222 ? -34.084 24.240 -14.777 1.00 18.10 ? 221  ARG B CA  1 
ATOM   4237 C C   . ARG B 1 222 ? -34.626 25.336 -15.680 1.00 19.89 ? 221  ARG B C   1 
ATOM   4238 O O   . ARG B 1 222 ? -33.831 26.027 -16.319 1.00 21.63 ? 221  ARG B O   1 
ATOM   4239 C CB  . ARG B 1 222 ? -33.563 23.078 -15.630 1.00 17.10 ? 221  ARG B CB  1 
ATOM   4240 C CG  . ARG B 1 222 ? -32.520 22.251 -14.890 1.00 19.07 ? 221  ARG B CG  1 
ATOM   4241 C CD  . ARG B 1 222 ? -31.973 21.088 -15.707 1.00 16.97 ? 221  ARG B CD  1 
ATOM   4242 N NE  . ARG B 1 222 ? -30.931 20.372 -14.967 1.00 16.91 ? 221  ARG B NE  1 
ATOM   4243 C CZ  . ARG B 1 222 ? -30.320 19.278 -15.411 1.00 19.67 ? 221  ARG B CZ  1 
ATOM   4244 N NH1 . ARG B 1 222 ? -30.599 18.766 -16.597 1.00 22.36 ? 221  ARG B NH1 1 
ATOM   4245 N NH2 . ARG B 1 222 ? -29.394 18.693 -14.653 1.00 22.45 ? 221  ARG B NH2 1 
ATOM   4246 N N   . ILE B 1 223 ? -35.938 25.533 -15.760 1.00 16.33 ? 222  ILE B N   1 
ATOM   4247 C CA  . ILE B 1 223 ? -36.452 26.621 -16.580 1.00 15.36 ? 222  ILE B CA  1 
ATOM   4248 C C   . ILE B 1 223 ? -37.001 27.776 -15.764 1.00 16.65 ? 222  ILE B C   1 
ATOM   4249 O O   . ILE B 1 223 ? -37.457 28.767 -16.358 1.00 16.83 ? 222  ILE B O   1 
ATOM   4250 C CB  . ILE B 1 223 ? -37.511 26.121 -17.580 1.00 16.32 ? 222  ILE B CB  1 
ATOM   4251 C CG1 . ILE B 1 223 ? -38.756 25.656 -16.844 1.00 15.62 ? 222  ILE B CG1 1 
ATOM   4252 C CG2 . ILE B 1 223 ? -36.943 24.993 -18.431 1.00 19.46 ? 222  ILE B CG2 1 
ATOM   4253 C CD1 . ILE B 1 223 ? -39.944 25.488 -17.765 1.00 21.70 ? 222  ILE B CD1 1 
ATOM   4254 N N   . THR B 1 224 ? -36.931 27.716 -14.422 1.00 16.36 ? 223  THR B N   1 
ATOM   4255 C CA  . THR B 1 224 ? -37.533 28.757 -13.590 1.00 16.99 ? 223  THR B CA  1 
ATOM   4256 C C   . THR B 1 224 ? -36.838 30.105 -13.776 1.00 18.05 ? 223  THR B C   1 
ATOM   4257 O O   . THR B 1 224 ? -37.498 31.126 -13.986 1.00 18.69 ? 223  THR B O   1 
ATOM   4258 C CB  . THR B 1 224 ? -37.508 28.308 -12.122 1.00 18.29 ? 223  THR B CB  1 
ATOM   4259 O OG1 . THR B 1 224 ? -38.469 27.260 -11.933 1.00 21.46 ? 223  THR B OG1 1 
ATOM   4260 C CG2 . THR B 1 224 ? -37.850 29.463 -11.169 1.00 20.58 ? 223  THR B CG2 1 
ATOM   4261 N N   . SER B 1 225 ? -35.505 30.136 -13.732 1.00 17.81 ? 224  SER B N   1 
ATOM   4262 C CA  A SER B 1 225 ? -34.787 31.400 -13.892 0.38 19.31 ? 224  SER B CA  1 
ATOM   4263 C CA  B SER B 1 225 ? -34.837 31.424 -13.870 0.47 19.31 ? 224  SER B CA  1 
ATOM   4264 C CA  C SER B 1 225 ? -34.799 31.405 -13.887 0.15 19.32 ? 224  SER B CA  1 
ATOM   4265 C C   . SER B 1 225 ? -35.022 32.000 -15.273 1.00 17.23 ? 224  SER B C   1 
ATOM   4266 O O   . SER B 1 225 ? -35.176 33.217 -15.418 1.00 17.49 ? 224  SER B O   1 
ATOM   4267 C CB  A SER B 1 225 ? -33.291 31.187 -13.655 0.38 19.98 ? 224  SER B CB  1 
ATOM   4268 C CB  B SER B 1 225 ? -33.357 31.308 -13.496 0.47 20.27 ? 224  SER B CB  1 
ATOM   4269 C CB  C SER B 1 225 ? -33.308 31.209 -13.617 0.15 20.09 ? 224  SER B CB  1 
ATOM   4270 O OG  A SER B 1 225 ? -32.578 32.405 -13.795 0.38 24.38 ? 224  SER B OG  1 
ATOM   4271 O OG  B SER B 1 225 ? -32.608 30.621 -14.466 0.47 20.77 ? 224  SER B OG  1 
ATOM   4272 O OG  C SER B 1 225 ? -33.086 30.878 -12.257 0.15 19.89 ? 224  SER B OG  1 
ATOM   4273 N N   . ALA B 1 226 ? -35.040 31.153 -16.305 1.00 16.88 ? 225  ALA B N   1 
ATOM   4274 C CA  . ALA B 1 226 ? -35.295 31.645 -17.661 1.00 17.44 ? 225  ALA B CA  1 
ATOM   4275 C C   . ALA B 1 226 ? -36.691 32.248 -17.780 1.00 17.66 ? 225  ALA B C   1 
ATOM   4276 O O   . ALA B 1 226 ? -36.885 33.260 -18.470 1.00 17.87 ? 225  ALA B O   1 
ATOM   4277 C CB  . ALA B 1 226 ? -35.114 30.512 -18.672 1.00 17.69 ? 225  ALA B CB  1 
ATOM   4278 N N   . THR B 1 227 ? -37.676 31.637 -17.117 1.00 16.49 ? 226  THR B N   1 
ATOM   4279 C CA  . THR B 1 227 ? -39.035 32.177 -17.122 1.00 18.19 ? 226  THR B CA  1 
ATOM   4280 C C   . THR B 1 227 ? -39.067 33.596 -16.558 1.00 20.01 ? 226  THR B C   1 
ATOM   4281 O O   . THR B 1 227 ? -39.677 34.497 -17.149 1.00 18.26 ? 226  THR B O   1 
ATOM   4282 C CB  . THR B 1 227 ? -39.956 31.254 -16.325 1.00 16.26 ? 226  THR B CB  1 
ATOM   4283 O OG1 . THR B 1 227 ? -39.897 29.941 -16.885 1.00 18.80 ? 226  THR B OG1 1 
ATOM   4284 C CG2 . THR B 1 227 ? -41.419 31.773 -16.345 1.00 20.21 ? 226  THR B CG2 1 
ATOM   4285 N N   . GLN B 1 228 ? -38.390 33.818 -15.425 1.00 17.50 ? 227  GLN B N   1 
ATOM   4286 C CA  A GLN B 1 228 ? -38.356 35.152 -14.840 0.54 20.85 ? 227  GLN B CA  1 
ATOM   4287 C CA  B GLN B 1 228 ? -38.342 35.154 -14.832 0.46 20.87 ? 227  GLN B CA  1 
ATOM   4288 C C   . GLN B 1 228 ? -37.644 36.141 -15.756 1.00 20.75 ? 227  GLN B C   1 
ATOM   4289 O O   . GLN B 1 228 ? -38.027 37.319 -15.823 1.00 21.49 ? 227  GLN B O   1 
ATOM   4290 C CB  A GLN B 1 228 ? -37.676 35.097 -13.474 0.54 20.93 ? 227  GLN B CB  1 
ATOM   4291 C CB  B GLN B 1 228 ? -37.620 35.117 -13.479 0.46 20.89 ? 227  GLN B CB  1 
ATOM   4292 C CG  A GLN B 1 228 ? -38.121 33.908 -12.638 0.54 20.27 ? 227  GLN B CG  1 
ATOM   4293 C CG  B GLN B 1 228 ? -38.036 36.220 -12.483 0.46 25.98 ? 227  GLN B CG  1 
ATOM   4294 C CD  A GLN B 1 228 ? -39.610 33.897 -12.351 0.54 34.91 ? 227  GLN B CD  1 
ATOM   4295 C CD  B GLN B 1 228 ? -37.689 37.632 -12.935 0.46 38.56 ? 227  GLN B CD  1 
ATOM   4296 O OE1 A GLN B 1 228 ? -40.140 34.807 -11.707 0.54 39.28 ? 227  GLN B OE1 1 
ATOM   4297 O OE1 B GLN B 1 228 ? -38.575 38.471 -13.126 0.46 38.19 ? 227  GLN B OE1 1 
ATOM   4298 N NE2 A GLN B 1 228 ? -40.296 32.856 -12.821 0.54 30.62 ? 227  GLN B NE2 1 
ATOM   4299 N NE2 B GLN B 1 228 ? -36.399 37.901 -13.109 0.46 35.56 ? 227  GLN B NE2 1 
ATOM   4300 N N   . TRP B 1 229 ? -36.602 35.682 -16.467 1.00 18.75 ? 228  TRP B N   1 
ATOM   4301 C CA  . TRP B 1 229 ? -35.885 36.569 -17.378 1.00 16.99 ? 228  TRP B CA  1 
ATOM   4302 C C   . TRP B 1 229 ? -36.783 37.012 -18.521 1.00 17.96 ? 228  TRP B C   1 
ATOM   4303 O O   . TRP B 1 229 ? -36.807 38.197 -18.885 1.00 17.67 ? 228  TRP B O   1 
ATOM   4304 C CB  . TRP B 1 229 ? -34.647 35.867 -17.940 1.00 18.03 ? 228  TRP B CB  1 
ATOM   4305 C CG  . TRP B 1 229 ? -33.770 36.736 -18.803 1.00 20.03 ? 228  TRP B CG  1 
ATOM   4306 C CD1 . TRP B 1 229 ? -32.723 37.491 -18.383 1.00 16.59 ? 228  TRP B CD1 1 
ATOM   4307 C CD2 . TRP B 1 229 ? -33.839 36.907 -20.237 1.00 15.88 ? 228  TRP B CD2 1 
ATOM   4308 N NE1 . TRP B 1 229 ? -32.137 38.141 -19.456 1.00 17.64 ? 228  TRP B NE1 1 
ATOM   4309 C CE2 . TRP B 1 229 ? -32.809 37.802 -20.600 1.00 17.74 ? 228  TRP B CE2 1 
ATOM   4310 C CE3 . TRP B 1 229 ? -34.686 36.409 -21.243 1.00 16.35 ? 228  TRP B CE3 1 
ATOM   4311 C CZ2 . TRP B 1 229 ? -32.583 38.201 -21.930 1.00 15.07 ? 228  TRP B CZ2 1 
ATOM   4312 C CZ3 . TRP B 1 229 ? -34.466 36.812 -22.581 1.00 18.92 ? 228  TRP B CZ3 1 
ATOM   4313 C CH2 . TRP B 1 229 ? -33.418 37.700 -22.905 1.00 17.47 ? 228  TRP B CH2 1 
ATOM   4314 N N   . LEU B 1 230 ? -37.521 36.068 -19.107 1.00 16.47 ? 229  LEU B N   1 
ATOM   4315 C CA  . LEU B 1 230 ? -38.459 36.428 -20.166 1.00 18.71 ? 229  LEU B CA  1 
ATOM   4316 C C   . LEU B 1 230 ? -39.473 37.439 -19.668 1.00 22.98 ? 229  LEU B C   1 
ATOM   4317 O O   . LEU B 1 230 ? -39.734 38.441 -20.338 1.00 17.59 ? 229  LEU B O   1 
ATOM   4318 C CB  . LEU B 1 230 ? -39.171 35.186 -20.687 1.00 17.55 ? 229  LEU B CB  1 
ATOM   4319 C CG  . LEU B 1 230 ? -38.302 34.162 -21.403 1.00 16.80 ? 229  LEU B CG  1 
ATOM   4320 C CD1 . LEU B 1 230 ? -39.077 32.866 -21.574 1.00 17.85 ? 229  LEU B CD1 1 
ATOM   4321 C CD2 . LEU B 1 230 ? -37.831 34.681 -22.781 1.00 15.95 ? 229  LEU B CD2 1 
ATOM   4322 N N   . ARG B 1 231 ? -40.024 37.220 -18.469 1.00 17.72 ? 230  ARG B N   1 
ATOM   4323 C CA  . ARG B 1 231 ? -41.066 38.120 -17.986 1.00 18.29 ? 230  ARG B CA  1 
ATOM   4324 C C   . ARG B 1 231 ? -40.490 39.495 -17.679 1.00 22.56 ? 230  ARG B C   1 
ATOM   4325 O O   . ARG B 1 231 ? -41.060 40.523 -18.068 1.00 21.36 ? 230  ARG B O   1 
ATOM   4326 C CB  . ARG B 1 231 ? -41.747 37.534 -16.746 1.00 20.84 ? 230  ARG B CB  1 
ATOM   4327 C CG  . ARG B 1 231 ? -42.840 38.442 -16.204 1.00 26.82 ? 230  ARG B CG  1 
ATOM   4328 C CD  . ARG B 1 231 ? -43.688 37.738 -15.161 1.00 29.34 ? 230  ARG B CD  1 
ATOM   4329 N NE  . ARG B 1 231 ? -44.287 36.517 -15.691 1.00 29.97 ? 230  ARG B NE  1 
ATOM   4330 C CZ  . ARG B 1 231 ? -44.019 35.298 -15.246 1.00 30.25 ? 230  ARG B CZ  1 
ATOM   4331 N NH1 . ARG B 1 231 ? -43.164 35.096 -14.257 1.00 31.97 ? 230  ARG B NH1 1 
ATOM   4332 N NH2 . ARG B 1 231 ? -44.629 34.254 -15.805 1.00 28.57 ? 230  ARG B NH2 1 
ATOM   4333 N N   . ALA B 1 232 ? -39.347 39.532 -16.988 1.00 22.20 ? 231  ALA B N   1 
ATOM   4334 C CA  . ALA B 1 232 ? -38.751 40.812 -16.619 1.00 22.47 ? 231  ALA B CA  1 
ATOM   4335 C C   . ALA B 1 232 ? -38.419 41.649 -17.840 1.00 26.35 ? 231  ALA B C   1 
ATOM   4336 O O   . ALA B 1 232 ? -38.464 42.884 -17.777 1.00 22.80 ? 231  ALA B O   1 
ATOM   4337 C CB  . ALA B 1 232 ? -37.492 40.583 -15.783 1.00 25.16 ? 231  ALA B CB  1 
ATOM   4338 N N   . ASN B 1 233 ? -38.100 41.000 -18.957 1.00 18.57 ? 232  ASN B N   1 
ATOM   4339 C CA  . ASN B 1 233 ? -37.668 41.701 -20.157 1.00 19.97 ? 232  ASN B CA  1 
ATOM   4340 C C   . ASN B 1 233 ? -38.746 41.788 -21.221 1.00 21.94 ? 232  ASN B C   1 
ATOM   4341 O O   . ASN B 1 233 ? -38.465 42.254 -22.330 1.00 21.37 ? 232  ASN B O   1 
ATOM   4342 C CB  . ASN B 1 233 ? -36.409 41.040 -20.702 1.00 19.04 ? 232  ASN B CB  1 
ATOM   4343 C CG  . ASN B 1 233 ? -35.197 41.345 -19.834 1.00 23.12 ? 232  ASN B CG  1 
ATOM   4344 O OD1 . ASN B 1 233 ? -34.742 42.495 -19.787 1.00 22.71 ? 232  ASN B OD1 1 
ATOM   4345 N ND2 . ASN B 1 233 ? -34.696 40.343 -19.111 1.00 20.72 ? 232  ASN B ND2 1 
ATOM   4346 N N   . GLY B 1 234 ? -39.972 41.386 -20.901 1.00 19.68 ? 233  GLY B N   1 
ATOM   4347 C CA  . GLY B 1 234 ? -41.066 41.486 -21.857 1.00 18.27 ? 233  GLY B CA  1 
ATOM   4348 C C   . GLY B 1 234 ? -40.875 40.673 -23.120 1.00 21.01 ? 233  GLY B C   1 
ATOM   4349 O O   . GLY B 1 234 ? -41.290 41.109 -24.202 1.00 20.11 ? 233  GLY B O   1 
ATOM   4350 N N   . LYS B 1 235 ? -40.285 39.484 -23.002 1.00 19.12 ? 234  LYS B N   1 
ATOM   4351 C CA  . LYS B 1 235 ? -39.964 38.626 -24.134 1.00 14.69 ? 234  LYS B CA  1 
ATOM   4352 C C   . LYS B 1 235 ? -40.865 37.402 -24.156 1.00 18.36 ? 234  LYS B C   1 
ATOM   4353 O O   . LYS B 1 235 ? -41.526 37.065 -23.170 1.00 19.53 ? 234  LYS B O   1 
ATOM   4354 C CB  . LYS B 1 235 ? -38.503 38.155 -24.080 1.00 16.14 ? 234  LYS B CB  1 
ATOM   4355 C CG  . LYS B 1 235 ? -37.462 39.262 -23.992 1.00 20.93 ? 234  LYS B CG  1 
ATOM   4356 C CD  . LYS B 1 235 ? -37.650 40.357 -25.036 1.00 17.49 ? 234  LYS B CD  1 
ATOM   4357 C CE  . LYS B 1 235 ? -36.444 41.308 -25.019 1.00 20.40 ? 234  LYS B CE  1 
ATOM   4358 N NZ  . LYS B 1 235 ? -36.642 42.499 -25.922 1.00 20.36 ? 234  LYS B NZ  1 
ATOM   4359 N N   . LYS B 1 236 ? -40.893 36.740 -25.307 1.00 18.21 ? 235  LYS B N   1 
ATOM   4360 C CA  . LYS B 1 236 ? -41.528 35.440 -25.464 1.00 18.91 ? 235  LYS B CA  1 
ATOM   4361 C C   . LYS B 1 236 ? -40.466 34.379 -25.707 1.00 17.14 ? 235  LYS B C   1 
ATOM   4362 O O   . LYS B 1 236 ? -39.483 34.626 -26.416 1.00 17.88 ? 235  LYS B O   1 
ATOM   4363 C CB  . LYS B 1 236 ? -42.493 35.426 -26.650 1.00 18.75 ? 235  LYS B CB  1 
ATOM   4364 C CG  . LYS B 1 236 ? -43.649 36.404 -26.553 1.00 25.74 ? 235  LYS B CG  1 
ATOM   4365 C CD  . LYS B 1 236 ? -44.656 35.977 -25.518 1.00 32.77 ? 235  LYS B CD  1 
ATOM   4366 C CE  . LYS B 1 236 ? -46.040 36.520 -25.872 1.00 40.00 ? 235  LYS B CE  1 
ATOM   4367 N NZ  . LYS B 1 236 ? -47.094 36.080 -24.905 1.00 38.57 ? 235  LYS B NZ  1 
ATOM   4368 N N   . GLY B 1 237 ? -40.688 33.176 -25.171 1.00 17.01 ? 236  GLY B N   1 
ATOM   4369 C CA  . GLY B 1 237 ? -39.789 32.067 -25.409 1.00 14.82 ? 236  GLY B CA  1 
ATOM   4370 C C   . GLY B 1 237 ? -40.512 30.827 -25.906 1.00 15.05 ? 236  GLY B C   1 
ATOM   4371 O O   . GLY B 1 237 ? -41.750 30.736 -25.885 1.00 16.52 ? 236  GLY B O   1 
ATOM   4372 N N   . ILE B 1 238 ? -39.711 29.865 -26.346 1.00 16.25 ? 237  ILE B N   1 
ATOM   4373 C CA  . ILE B 1 238 ? -40.192 28.533 -26.683 1.00 15.73 ? 237  ILE B CA  1 
ATOM   4374 C C   . ILE B 1 238 ? -39.107 27.551 -26.279 1.00 17.56 ? 237  ILE B C   1 
ATOM   4375 O O   . ILE B 1 238 ? -37.919 27.874 -26.315 1.00 16.71 ? 237  ILE B O   1 
ATOM   4376 C CB  . ILE B 1 238 ? -40.548 28.402 -28.186 1.00 14.03 ? 237  ILE B CB  1 
ATOM   4377 C CG1 . ILE B 1 238 ? -41.292 27.088 -28.447 1.00 16.28 ? 237  ILE B CG1 1 
ATOM   4378 C CG2 . ILE B 1 238 ? -39.296 28.526 -29.073 1.00 17.57 ? 237  ILE B CG2 1 
ATOM   4379 C CD1 . ILE B 1 238 ? -41.784 26.927 -29.931 1.00 16.35 ? 237  ILE B CD1 1 
ATOM   4380 N N   . ILE B 1 239 ? -39.519 26.362 -25.848 1.00 14.74 ? 238  ILE B N   1 
ATOM   4381 C CA  . ILE B 1 239 ? -38.581 25.268 -25.623 1.00 14.79 ? 238  ILE B CA  1 
ATOM   4382 C C   . ILE B 1 239 ? -38.471 24.519 -26.947 1.00 16.94 ? 238  ILE B C   1 
ATOM   4383 O O   . ILE B 1 239 ? -39.395 23.809 -27.359 1.00 17.70 ? 238  ILE B O   1 
ATOM   4384 C CB  . ILE B 1 239 ? -39.028 24.355 -24.471 1.00 17.40 ? 238  ILE B CB  1 
ATOM   4385 C CG1 . ILE B 1 239 ? -39.011 25.113 -23.134 1.00 17.61 ? 238  ILE B CG1 1 
ATOM   4386 C CG2 . ILE B 1 239 ? -38.142 23.106 -24.398 1.00 16.93 ? 238  ILE B CG2 1 
ATOM   4387 C CD1 . ILE B 1 239 ? -37.601 25.439 -22.615 1.00 17.46 ? 238  ILE B CD1 1 
ATOM   4388 N N   . GLY B 1 240 ? -37.347 24.710 -27.645 1.00 13.90 ? 239  GLY B N   1 
ATOM   4389 C CA  . GLY B 1 240 ? -37.219 24.139 -28.984 1.00 15.02 ? 239  GLY B CA  1 
ATOM   4390 C C   . GLY B 1 240 ? -36.741 22.699 -29.027 1.00 15.86 ? 239  GLY B C   1 
ATOM   4391 O O   . GLY B 1 240 ? -36.848 22.055 -30.077 1.00 15.91 ? 239  GLY B O   1 
ATOM   4392 N N   . GLU B 1 241 ? -36.184 22.195 -27.925 1.00 13.86 ? 240  GLU B N   1 
ATOM   4393 C CA  . GLU B 1 241 ? -35.820 20.792 -27.754 1.00 13.10 ? 240  GLU B CA  1 
ATOM   4394 C C   . GLU B 1 241 ? -35.960 20.457 -26.283 1.00 14.95 ? 240  GLU B C   1 
ATOM   4395 O O   . GLU B 1 241 ? -35.434 21.187 -25.439 1.00 15.86 ? 240  GLU B O   1 
ATOM   4396 C CB  . GLU B 1 241 ? -34.372 20.481 -28.173 1.00 13.57 ? 240  GLU B CB  1 
ATOM   4397 C CG  . GLU B 1 241 ? -34.039 20.715 -29.652 1.00 14.15 ? 240  GLU B CG  1 
ATOM   4398 C CD  . GLU B 1 241 ? -32.623 20.260 -29.996 1.00 21.00 ? 240  GLU B CD  1 
ATOM   4399 O OE1 . GLU B 1 241 ? -31.987 19.524 -29.199 1.00 18.35 ? 240  GLU B OE1 1 
ATOM   4400 O OE2 . GLU B 1 241 ? -32.131 20.643 -31.064 1.00 17.15 ? 240  GLU B OE2 1 
ATOM   4401 N N   . PHE B 1 242 ? -36.656 19.364 -25.985 1.00 15.03 ? 241  PHE B N   1 
ATOM   4402 C CA  . PHE B 1 242 ? -36.620 18.756 -24.658 1.00 14.37 ? 241  PHE B CA  1 
ATOM   4403 C C   . PHE B 1 242 ? -36.899 17.271 -24.823 1.00 18.93 ? 241  PHE B C   1 
ATOM   4404 O O   . PHE B 1 242 ? -37.505 16.838 -25.805 1.00 15.99 ? 241  PHE B O   1 
ATOM   4405 C CB  . PHE B 1 242 ? -37.618 19.401 -23.685 1.00 17.94 ? 241  PHE B CB  1 
ATOM   4406 C CG  . PHE B 1 242 ? -39.063 19.030 -23.934 1.00 17.80 ? 241  PHE B CG  1 
ATOM   4407 C CD1 . PHE B 1 242 ? -39.723 19.487 -25.055 1.00 17.38 ? 241  PHE B CD1 1 
ATOM   4408 C CD2 . PHE B 1 242 ? -39.768 18.252 -23.018 1.00 18.56 ? 241  PHE B CD2 1 
ATOM   4409 C CE1 . PHE B 1 242 ? -41.070 19.169 -25.287 1.00 17.19 ? 241  PHE B CE1 1 
ATOM   4410 C CE2 . PHE B 1 242 ? -41.116 17.924 -23.227 1.00 17.75 ? 241  PHE B CE2 1 
ATOM   4411 C CZ  . PHE B 1 242 ? -41.771 18.379 -24.384 1.00 18.36 ? 241  PHE B CZ  1 
ATOM   4412 N N   . ALA B 1 243 ? -36.456 16.488 -23.847 1.00 16.92 ? 242  ALA B N   1 
ATOM   4413 C CA  . ALA B 1 243 ? -36.692 15.053 -23.895 1.00 16.86 ? 242  ALA B CA  1 
ATOM   4414 C C   . ALA B 1 243 ? -36.393 14.485 -22.524 1.00 17.44 ? 242  ALA B C   1 
ATOM   4415 O O   . ALA B 1 243 ? -35.717 15.121 -21.713 1.00 17.08 ? 242  ALA B O   1 
ATOM   4416 C CB  . ALA B 1 243 ? -35.823 14.356 -24.955 1.00 19.79 ? 242  ALA B CB  1 
ATOM   4417 N N   . GLY B 1 244 ? -36.935 13.295 -22.284 1.00 16.37 ? 243  GLY B N   1 
ATOM   4418 C CA  . GLY B 1 244 ? -36.563 12.458 -21.155 1.00 16.23 ? 243  GLY B CA  1 
ATOM   4419 C C   . GLY B 1 244 ? -36.868 11.018 -21.516 1.00 17.34 ? 243  GLY B C   1 
ATOM   4420 O O   . GLY B 1 244 ? -37.644 10.735 -22.439 1.00 18.34 ? 243  GLY B O   1 
ATOM   4421 N N   . GLY B 1 245 ? -36.250 10.103 -20.776 1.00 18.87 ? 244  GLY B N   1 
ATOM   4422 C CA  . GLY B 1 245 ? -36.467 8.695  -21.029 1.00 22.03 ? 244  GLY B CA  1 
ATOM   4423 C C   . GLY B 1 245 ? -37.877 8.264  -20.681 1.00 22.95 ? 244  GLY B C   1 
ATOM   4424 O O   . GLY B 1 245 ? -38.600 8.942  -19.960 1.00 20.53 ? 244  GLY B O   1 
ATOM   4425 N N   . ALA B 1 246 ? -38.277 7.109  -21.220 1.00 20.68 ? 245  ALA B N   1 
ATOM   4426 C CA  . ALA B 1 246 ? -39.584 6.525  -20.923 1.00 23.16 ? 245  ALA B CA  1 
ATOM   4427 C C   . ALA B 1 246 ? -39.491 5.780  -19.593 1.00 22.78 ? 245  ALA B C   1 
ATOM   4428 O O   . ALA B 1 246 ? -39.378 4.553  -19.525 1.00 24.11 ? 245  ALA B O   1 
ATOM   4429 C CB  . ALA B 1 246 ? -40.037 5.604  -22.053 1.00 24.01 ? 245  ALA B CB  1 
ATOM   4430 N N   . ASN B 1 247 ? -39.562 6.544  -18.508 1.00 20.58 ? 246  ASN B N   1 
ATOM   4431 C CA  . ASN B 1 247 ? -39.488 5.976  -17.168 1.00 21.53 ? 246  ASN B CA  1 
ATOM   4432 C C   . ASN B 1 247 ? -40.188 6.925  -16.207 1.00 22.81 ? 246  ASN B C   1 
ATOM   4433 O O   . ASN B 1 247 ? -40.533 8.057  -16.556 1.00 23.49 ? 246  ASN B O   1 
ATOM   4434 C CB  . ASN B 1 247 ? -38.040 5.738  -16.738 1.00 23.28 ? 246  ASN B CB  1 
ATOM   4435 C CG  . ASN B 1 247 ? -37.202 6.992  -16.833 1.00 22.29 ? 246  ASN B CG  1 
ATOM   4436 O OD1 . ASN B 1 247 ? -37.443 7.970  -16.122 1.00 25.99 ? 246  ASN B OD1 1 
ATOM   4437 N ND2 . ASN B 1 247 ? -36.215 6.980  -17.722 1.00 21.56 ? 246  ASN B ND2 1 
ATOM   4438 N N   . ASP B 1 248 ? -40.369 6.454  -14.975 1.00 20.53 ? 247  ASP B N   1 
ATOM   4439 C CA  . ASP B 1 248 ? -41.256 7.151  -14.052 1.00 25.88 ? 247  ASP B CA  1 
ATOM   4440 C C   . ASP B 1 248 ? -40.732 8.540  -13.702 1.00 26.24 ? 247  ASP B C   1 
ATOM   4441 O O   . ASP B 1 248 ? -41.482 9.523  -13.743 1.00 21.98 ? 247  ASP B O   1 
ATOM   4442 C CB  . ASP B 1 248 ? -41.444 6.331  -12.783 1.00 23.30 ? 247  ASP B CB  1 
ATOM   4443 C CG  . ASP B 1 248 ? -42.462 6.952  -11.857 1.00 29.79 ? 247  ASP B CG  1 
ATOM   4444 O OD1 . ASP B 1 248 ? -43.614 7.155  -12.294 1.00 35.45 ? 247  ASP B OD1 1 
ATOM   4445 O OD2 . ASP B 1 248 ? -42.105 7.236  -10.702 1.00 35.74 ? 247  ASP B OD2 1 
ATOM   4446 N N   . VAL B 1 249 ? -39.454 8.639  -13.322 1.00 20.49 ? 248  VAL B N   1 
ATOM   4447 C CA  . VAL B 1 249 ? -38.918 9.924  -12.878 1.00 21.82 ? 248  VAL B CA  1 
ATOM   4448 C C   . VAL B 1 249 ? -38.958 10.944 -14.010 1.00 22.04 ? 248  VAL B C   1 
ATOM   4449 O O   . VAL B 1 249 ? -39.316 12.111 -13.801 1.00 22.24 ? 248  VAL B O   1 
ATOM   4450 C CB  . VAL B 1 249 ? -37.498 9.751  -12.308 1.00 24.35 ? 248  VAL B CB  1 
ATOM   4451 C CG1 . VAL B 1 249 ? -36.871 11.106 -12.033 1.00 18.98 ? 248  VAL B CG1 1 
ATOM   4452 C CG2 . VAL B 1 249 ? -37.559 8.943  -11.009 1.00 22.55 ? 248  VAL B CG2 1 
ATOM   4453 N N   . CYS B 1 250 ? -38.611 10.523 -15.235 1.00 20.47 ? 249  CYS B N   1 
ATOM   4454 C CA  . CYS B 1 250 ? -38.593 11.468 -16.347 1.00 20.15 ? 249  CYS B CA  1 
ATOM   4455 C C   . CYS B 1 250 ? -39.997 11.909 -16.717 1.00 21.64 ? 249  CYS B C   1 
ATOM   4456 O O   . CYS B 1 250 ? -40.219 13.082 -17.046 1.00 23.55 ? 249  CYS B O   1 
ATOM   4457 C CB  . CYS B 1 250 ? -37.934 10.846 -17.572 1.00 23.62 ? 249  CYS B CB  1 
ATOM   4458 S SG  . CYS B 1 250 ? -36.149 10.647 -17.473 1.00 21.95 ? 249  CYS B SG  1 
ATOM   4459 N N   . GLU B 1 251 ? -40.940 10.963 -16.732 1.00 21.57 ? 250  GLU B N   1 
ATOM   4460 C CA  . GLU B 1 251 ? -42.322 11.305 -17.034 1.00 21.83 ? 250  GLU B CA  1 
ATOM   4461 C C   . GLU B 1 251 ? -42.866 12.312 -16.028 1.00 23.21 ? 250  GLU B C   1 
ATOM   4462 O O   . GLU B 1 251 ? -43.518 13.289 -16.408 1.00 21.47 ? 250  GLU B O   1 
ATOM   4463 C CB  . GLU B 1 251 ? -43.167 10.027 -17.089 1.00 21.06 ? 250  GLU B CB  1 
ATOM   4464 C CG  . GLU B 1 251 ? -42.956 9.324  -18.433 1.00 24.78 ? 250  GLU B CG  1 
ATOM   4465 C CD  . GLU B 1 251 ? -43.432 7.890  -18.480 1.00 30.09 ? 250  GLU B CD  1 
ATOM   4466 O OE1 . GLU B 1 251 ? -44.194 7.481  -17.588 1.00 30.87 ? 250  GLU B OE1 1 
ATOM   4467 O OE2 . GLU B 1 251 ? -43.033 7.172  -19.430 1.00 26.43 ? 250  GLU B OE2 1 
ATOM   4468 N N   . THR B 1 252 ? -42.562 12.125 -14.745 1.00 20.02 ? 251  THR B N   1 
ATOM   4469 C CA  . THR B 1 252 ? -43.001 13.099 -13.756 1.00 20.79 ? 251  THR B CA  1 
ATOM   4470 C C   . THR B 1 252 ? -42.339 14.452 -13.983 1.00 25.05 ? 251  THR B C   1 
ATOM   4471 O O   . THR B 1 252 ? -42.987 15.499 -13.860 1.00 20.28 ? 251  THR B O   1 
ATOM   4472 C CB  . THR B 1 252 ? -42.705 12.576 -12.353 1.00 19.75 ? 251  THR B CB  1 
ATOM   4473 O OG1 . THR B 1 252 ? -43.280 11.273 -12.218 1.00 22.78 ? 251  THR B OG1 1 
ATOM   4474 C CG2 . THR B 1 252 ? -43.315 13.509 -11.307 1.00 23.55 ? 251  THR B CG2 1 
ATOM   4475 N N   . ALA B 1 253 ? -41.042 14.448 -14.311 1.00 20.54 ? 252  ALA B N   1 
ATOM   4476 C CA  . ALA B 1 253 ? -40.337 15.694 -14.581 1.00 19.25 ? 252  ALA B CA  1 
ATOM   4477 C C   . ALA B 1 253 ? -40.890 16.392 -15.815 1.00 18.78 ? 252  ALA B C   1 
ATOM   4478 O O   . ALA B 1 253 ? -40.982 17.626 -15.848 1.00 19.06 ? 252  ALA B O   1 
ATOM   4479 C CB  . ALA B 1 253 ? -38.849 15.415 -14.754 1.00 16.95 ? 252  ALA B CB  1 
ATOM   4480 N N   . ILE B 1 254 ? -41.247 15.623 -16.843 1.00 20.05 ? 253  ILE B N   1 
ATOM   4481 C CA  . ILE B 1 254 ? -41.789 16.221 -18.059 1.00 17.60 ? 253  ILE B CA  1 
ATOM   4482 C C   . ILE B 1 254 ? -43.136 16.866 -17.770 1.00 20.31 ? 253  ILE B C   1 
ATOM   4483 O O   . ILE B 1 254 ? -43.378 18.021 -18.142 1.00 19.43 ? 253  ILE B O   1 
ATOM   4484 C CB  . ILE B 1 254 ? -41.898 15.164 -19.170 1.00 17.02 ? 253  ILE B CB  1 
ATOM   4485 C CG1 . ILE B 1 254 ? -40.501 14.819 -19.683 1.00 19.05 ? 253  ILE B CG1 1 
ATOM   4486 C CG2 . ILE B 1 254 ? -42.780 15.690 -20.296 1.00 19.62 ? 253  ILE B CG2 1 
ATOM   4487 C CD1 . ILE B 1 254 ? -40.464 13.596 -20.578 1.00 19.97 ? 253  ILE B CD1 1 
ATOM   4488 N N   . THR B 1 255 ? -44.026 16.121 -17.104 1.00 19.18 ? 254  THR B N   1 
ATOM   4489 C CA  . THR B 1 255 ? -45.326 16.652 -16.711 1.00 20.76 ? 254  THR B CA  1 
ATOM   4490 C C   . THR B 1 255 ? -45.166 17.880 -15.824 1.00 20.36 ? 254  THR B C   1 
ATOM   4491 O O   . THR B 1 255 ? -45.859 18.884 -16.010 1.00 20.61 ? 254  THR B O   1 
ATOM   4492 C CB  . THR B 1 255 ? -46.139 15.557 -16.002 1.00 23.88 ? 254  THR B CB  1 
ATOM   4493 O OG1 . THR B 1 255 ? -46.519 14.559 -16.960 1.00 24.28 ? 254  THR B OG1 1 
ATOM   4494 C CG2 . THR B 1 255 ? -47.387 16.124 -15.352 1.00 30.52 ? 254  THR B CG2 1 
ATOM   4495 N N   . GLY B 1 256 ? -44.219 17.839 -14.888 1.00 19.70 ? 255  GLY B N   1 
ATOM   4496 C CA  . GLY B 1 256 ? -44.022 18.978 -14.012 1.00 19.26 ? 255  GLY B CA  1 
ATOM   4497 C C   . GLY B 1 256 ? -43.528 20.209 -14.747 1.00 20.62 ? 255  GLY B C   1 
ATOM   4498 O O   . GLY B 1 256 ? -43.958 21.332 -14.460 1.00 20.10 ? 255  GLY B O   1 
ATOM   4499 N N   . MET B 1 257 ? -42.619 20.019 -15.702 1.00 19.50 ? 256  MET B N   1 
ATOM   4500 C CA  . MET B 1 257 ? -42.090 21.156 -16.449 1.00 18.87 ? 256  MET B CA  1 
ATOM   4501 C C   . MET B 1 257 ? -43.163 21.781 -17.330 1.00 18.20 ? 256  MET B C   1 
ATOM   4502 O O   . MET B 1 257 ? -43.279 23.014 -17.394 1.00 17.61 ? 256  MET B O   1 
ATOM   4503 C CB  . MET B 1 257 ? -40.890 20.720 -17.287 1.00 18.75 ? 256  MET B CB  1 
ATOM   4504 C CG  . MET B 1 257 ? -40.226 21.870 -18.006 1.00 17.51 ? 256  MET B CG  1 
ATOM   4505 S SD  . MET B 1 257 ? -38.879 21.336 -19.075 1.00 21.27 ? 256  MET B SD  1 
ATOM   4506 C CE  . MET B 1 257 ? -39.803 20.826 -20.531 1.00 25.38 ? 256  MET B CE  1 
ATOM   4507 N N   . LEU B 1 258 ? -43.974 20.948 -17.998 1.00 18.62 ? 257  LEU B N   1 
ATOM   4508 C CA  . LEU B 1 258 ? -45.004 21.488 -18.882 1.00 19.91 ? 257  LEU B CA  1 
ATOM   4509 C C   . LEU B 1 258 ? -46.153 22.088 -18.082 1.00 19.37 ? 257  LEU B C   1 
ATOM   4510 O O   . LEU B 1 258 ? -46.717 23.117 -18.480 1.00 21.18 ? 257  LEU B O   1 
ATOM   4511 C CB  . LEU B 1 258 ? -45.506 20.403 -19.839 1.00 21.26 ? 257  LEU B CB  1 
ATOM   4512 C CG  . LEU B 1 258 ? -44.443 19.816 -20.770 1.00 18.66 ? 257  LEU B CG  1 
ATOM   4513 C CD1 . LEU B 1 258 ? -44.977 18.594 -21.491 1.00 19.70 ? 257  LEU B CD1 1 
ATOM   4514 C CD2 . LEU B 1 258 ? -43.932 20.863 -21.764 1.00 17.58 ? 257  LEU B CD2 1 
ATOM   4515 N N   . ASP B 1 259 ? -46.511 21.470 -16.946 1.00 20.04 ? 258  ASP B N   1 
ATOM   4516 C CA  . ASP B 1 259 ? -47.495 22.094 -16.070 1.00 19.47 ? 258  ASP B CA  1 
ATOM   4517 C C   . ASP B 1 259 ? -47.011 23.463 -15.605 1.00 24.15 ? 258  ASP B C   1 
ATOM   4518 O O   . ASP B 1 259 ? -47.784 24.427 -15.579 1.00 23.35 ? 258  ASP B O   1 
ATOM   4519 C CB  . ASP B 1 259 ? -47.790 21.188 -14.865 1.00 21.10 ? 258  ASP B CB  1 
ATOM   4520 C CG  . ASP B 1 259 ? -48.736 20.045 -15.207 1.00 22.23 ? 258  ASP B CG  1 
ATOM   4521 O OD1 . ASP B 1 259 ? -49.333 20.074 -16.299 1.00 24.35 ? 258  ASP B OD1 1 
ATOM   4522 O OD2 . ASP B 1 259 ? -48.878 19.108 -14.387 1.00 24.62 ? 258  ASP B OD2 1 
ATOM   4523 N N   . TYR B 1 260 ? -45.725 23.574 -15.252 1.00 21.36 ? 259  TYR B N   1 
ATOM   4524 C CA  . TYR B 1 260 ? -45.167 24.871 -14.874 1.00 19.77 ? 259  TYR B CA  1 
ATOM   4525 C C   . TYR B 1 260 ? -45.254 25.867 -16.027 1.00 21.27 ? 259  TYR B C   1 
ATOM   4526 O O   . TYR B 1 260 ? -45.655 27.022 -15.833 1.00 23.19 ? 259  TYR B O   1 
ATOM   4527 C CB  . TYR B 1 260 ? -43.720 24.699 -14.404 1.00 22.23 ? 259  TYR B CB  1 
ATOM   4528 C CG  . TYR B 1 260 ? -43.025 26.005 -14.081 1.00 17.14 ? 259  TYR B CG  1 
ATOM   4529 C CD1 . TYR B 1 260 ? -43.164 26.616 -12.838 1.00 18.96 ? 259  TYR B CD1 1 
ATOM   4530 C CD2 . TYR B 1 260 ? -42.230 26.634 -15.036 1.00 21.57 ? 259  TYR B CD2 1 
ATOM   4531 C CE1 . TYR B 1 260 ? -42.518 27.819 -12.560 1.00 21.25 ? 259  TYR B CE1 1 
ATOM   4532 C CE2 . TYR B 1 260 ? -41.592 27.820 -14.767 1.00 24.58 ? 259  TYR B CE2 1 
ATOM   4533 C CZ  . TYR B 1 260 ? -41.730 28.412 -13.542 1.00 27.10 ? 259  TYR B CZ  1 
ATOM   4534 O OH  . TYR B 1 260 ? -41.081 29.606 -13.311 1.00 29.89 ? 259  TYR B OH  1 
ATOM   4535 N N   . MET B 1 261 ? -44.872 25.437 -17.239 1.00 20.34 ? 260  MET B N   1 
ATOM   4536 C CA  . MET B 1 261 ? -44.965 26.314 -18.407 1.00 17.93 ? 260  MET B CA  1 
ATOM   4537 C C   . MET B 1 261 ? -46.401 26.759 -18.651 1.00 23.19 ? 260  MET B C   1 
ATOM   4538 O O   . MET B 1 261 ? -46.639 27.896 -19.075 1.00 19.82 ? 260  MET B O   1 
ATOM   4539 C CB  . MET B 1 261 ? -44.404 25.617 -19.649 1.00 19.20 ? 260  MET B CB  1 
ATOM   4540 C CG  . MET B 1 261 ? -42.900 25.420 -19.581 1.00 16.17 ? 260  MET B CG  1 
ATOM   4541 S SD  . MET B 1 261 ? -42.236 24.431 -20.919 1.00 18.21 ? 260  MET B SD  1 
ATOM   4542 C CE  . MET B 1 261 ? -42.519 25.551 -22.304 1.00 16.58 ? 260  MET B CE  1 
ATOM   4543 N N   . ALA B 1 262 ? -47.370 25.879 -18.384 1.00 20.25 ? 261  ALA B N   1 
ATOM   4544 C CA  . ALA B 1 262 ? -48.770 26.222 -18.603 1.00 22.45 ? 261  ALA B CA  1 
ATOM   4545 C C   . ALA B 1 262 ? -49.264 27.279 -17.624 1.00 20.00 ? 261  ALA B C   1 
ATOM   4546 O O   . ALA B 1 262 ? -50.247 27.970 -17.918 1.00 22.85 ? 261  ALA B O   1 
ATOM   4547 C CB  . ALA B 1 262 ? -49.646 24.969 -18.516 1.00 23.38 ? 261  ALA B CB  1 
ATOM   4548 N N   . GLN B 1 263 ? -48.612 27.422 -16.476 1.00 21.58 ? 262  GLN B N   1 
ATOM   4549 C CA  A GLN B 1 263 ? -48.924 28.503 -15.555 0.59 24.30 ? 262  GLN B CA  1 
ATOM   4550 C CA  B GLN B 1 263 ? -48.922 28.508 -15.557 0.41 24.29 ? 262  GLN B CA  1 
ATOM   4551 C C   . GLN B 1 263 ? -48.210 29.793 -15.926 1.00 21.66 ? 262  GLN B C   1 
ATOM   4552 O O   . GLN B 1 263 ? -48.388 30.807 -15.236 1.00 23.21 ? 262  GLN B O   1 
ATOM   4553 C CB  A GLN B 1 263 ? -48.557 28.096 -14.119 0.59 24.20 ? 262  GLN B CB  1 
ATOM   4554 C CB  B GLN B 1 263 ? -48.541 28.119 -14.131 0.41 24.24 ? 262  GLN B CB  1 
ATOM   4555 C CG  A GLN B 1 263 ? -48.781 26.613 -13.787 0.59 28.61 ? 262  GLN B CG  1 
ATOM   4556 C CG  B GLN B 1 263 ? -49.180 26.844 -13.660 0.41 27.22 ? 262  GLN B CG  1 
ATOM   4557 C CD  A GLN B 1 263 ? -50.198 26.124 -14.087 0.59 25.68 ? 262  GLN B CD  1 
ATOM   4558 C CD  B GLN B 1 263 ? -48.434 26.249 -12.503 0.41 30.78 ? 262  GLN B CD  1 
ATOM   4559 O OE1 A GLN B 1 263 ? -51.173 26.794 -13.741 0.59 28.85 ? 262  GLN B OE1 1 
ATOM   4560 O OE1 B GLN B 1 263 ? -48.229 26.905 -11.485 0.41 37.88 ? 262  GLN B OE1 1 
ATOM   4561 N NE2 A GLN B 1 263 ? -50.317 24.953 -14.746 0.59 21.24 ? 262  GLN B NE2 1 
ATOM   4562 N NE2 B GLN B 1 263 ? -47.999 25.003 -12.656 0.41 34.88 ? 262  GLN B NE2 1 
ATOM   4563 N N   . ASN B 1 264 ? -47.419 29.774 -16.992 1.00 21.32 ? 263  ASN B N   1 
ATOM   4564 C CA  . ASN B 1 264 ? -46.565 30.880 -17.368 1.00 20.44 ? 263  ASN B CA  1 
ATOM   4565 C C   . ASN B 1 264 ? -46.636 31.125 -18.862 1.00 22.58 ? 263  ASN B C   1 
ATOM   4566 O O   . ASN B 1 264 ? -45.612 31.381 -19.513 1.00 24.03 ? 263  ASN B O   1 
ATOM   4567 C CB  . ASN B 1 264 ? -45.130 30.608 -16.931 1.00 20.37 ? 263  ASN B CB  1 
ATOM   4568 C CG  . ASN B 1 264 ? -44.988 30.620 -15.432 1.00 21.17 ? 263  ASN B CG  1 
ATOM   4569 O OD1 . ASN B 1 264 ? -44.898 31.681 -14.836 1.00 24.47 ? 263  ASN B OD1 1 
ATOM   4570 N ND2 . ASN B 1 264 ? -45.006 29.442 -14.813 1.00 23.71 ? 263  ASN B ND2 1 
ATOM   4571 N N   . THR B 1 265 ? -47.848 31.052 -19.430 1.00 21.98 ? 264  THR B N   1 
ATOM   4572 C CA  . THR B 1 265 ? -47.997 31.228 -20.873 1.00 21.74 ? 264  THR B CA  1 
ATOM   4573 C C   . THR B 1 265 ? -47.917 32.682 -21.315 1.00 21.88 ? 264  THR B C   1 
ATOM   4574 O O   . THR B 1 265 ? -47.915 32.941 -22.528 1.00 23.01 ? 264  THR B O   1 
ATOM   4575 C CB  . THR B 1 265 ? -49.307 30.614 -21.380 1.00 21.99 ? 264  THR B CB  1 
ATOM   4576 O OG1 . THR B 1 265 ? -50.442 31.200 -20.714 1.00 22.62 ? 264  THR B OG1 1 
ATOM   4577 C CG2 . THR B 1 265 ? -49.297 29.107 -21.173 1.00 20.62 ? 264  THR B CG2 1 
ATOM   4578 N N   . ASP B 1 266 ? -47.839 33.634 -20.377 1.00 24.46 ? 265  ASP B N   1 
ATOM   4579 C CA  . ASP B 1 266 ? -47.520 35.002 -20.771 1.00 20.73 ? 265  ASP B CA  1 
ATOM   4580 C C   . ASP B 1 266 ? -46.117 35.107 -21.355 1.00 22.36 ? 265  ASP B C   1 
ATOM   4581 O O   . ASP B 1 266 ? -45.843 36.051 -22.111 1.00 23.76 ? 265  ASP B O   1 
ATOM   4582 C CB  . ASP B 1 266 ? -47.680 35.967 -19.586 1.00 27.91 ? 265  ASP B CB  1 
ATOM   4583 C CG  . ASP B 1 266 ? -46.730 35.664 -18.428 1.00 28.25 ? 265  ASP B CG  1 
ATOM   4584 O OD1 . ASP B 1 266 ? -46.346 34.497 -18.221 1.00 27.07 ? 265  ASP B OD1 1 
ATOM   4585 O OD2 . ASP B 1 266 ? -46.368 36.611 -17.706 1.00 37.03 ? 265  ASP B OD2 1 
ATOM   4586 N N   . VAL B 1 267 ? -45.229 34.155 -21.047 1.00 21.06 ? 266  VAL B N   1 
ATOM   4587 C CA  . VAL B 1 267 ? -43.913 34.167 -21.677 1.00 18.36 ? 266  VAL B CA  1 
ATOM   4588 C C   . VAL B 1 267 ? -43.643 32.907 -22.499 1.00 20.89 ? 266  VAL B C   1 
ATOM   4589 O O   . VAL B 1 267 ? -42.872 32.968 -23.454 1.00 19.92 ? 266  VAL B O   1 
ATOM   4590 C CB  . VAL B 1 267 ? -42.773 34.380 -20.664 1.00 21.61 ? 266  VAL B CB  1 
ATOM   4591 C CG1 . VAL B 1 267 ? -42.915 35.743 -19.960 1.00 21.28 ? 266  VAL B CG1 1 
ATOM   4592 C CG2 . VAL B 1 267 ? -42.702 33.239 -19.663 1.00 20.02 ? 266  VAL B CG2 1 
ATOM   4593 N N   . TRP B 1 268 ? -44.214 31.757 -22.146 1.00 17.95 ? 267  TRP B N   1 
ATOM   4594 C CA  . TRP B 1 268 ? -43.896 30.526 -22.882 1.00 16.62 ? 267  TRP B CA  1 
ATOM   4595 C C   . TRP B 1 268 ? -44.923 30.271 -23.978 1.00 16.31 ? 267  TRP B C   1 
ATOM   4596 O O   . TRP B 1 268 ? -46.117 30.080 -23.691 1.00 20.22 ? 267  TRP B O   1 
ATOM   4597 C CB  . TRP B 1 268 ? -43.828 29.303 -21.961 1.00 18.33 ? 267  TRP B CB  1 
ATOM   4598 C CG  . TRP B 1 268 ? -42.628 29.301 -21.091 1.00 19.39 ? 267  TRP B CG  1 
ATOM   4599 C CD1 . TRP B 1 268 ? -42.603 29.422 -19.726 1.00 18.07 ? 267  TRP B CD1 1 
ATOM   4600 C CD2 . TRP B 1 268 ? -41.260 29.204 -21.512 1.00 16.40 ? 267  TRP B CD2 1 
ATOM   4601 N NE1 . TRP B 1 268 ? -41.305 29.394 -19.287 1.00 14.77 ? 267  TRP B NE1 1 
ATOM   4602 C CE2 . TRP B 1 268 ? -40.462 29.270 -20.360 1.00 16.38 ? 267  TRP B CE2 1 
ATOM   4603 C CE3 . TRP B 1 268 ? -40.629 29.068 -22.761 1.00 15.88 ? 267  TRP B CE3 1 
ATOM   4604 C CZ2 . TRP B 1 268 ? -39.069 29.205 -20.406 1.00 18.25 ? 267  TRP B CZ2 1 
ATOM   4605 C CZ3 . TRP B 1 268 ? -39.258 29.016 -22.809 1.00 17.95 ? 267  TRP B CZ3 1 
ATOM   4606 C CH2 . TRP B 1 268 ? -38.482 29.082 -21.638 1.00 16.19 ? 267  TRP B CH2 1 
ATOM   4607 N N   . THR B 1 269 ? -44.449 30.245 -25.228 1.00 15.48 ? 268  THR B N   1 
ATOM   4608 C CA  . THR B 1 269 ? -45.274 29.947 -26.389 1.00 17.01 ? 268  THR B CA  1 
ATOM   4609 C C   . THR B 1 269 ? -45.433 28.453 -26.647 1.00 20.89 ? 268  THR B C   1 
ATOM   4610 O O   . THR B 1 269 ? -46.279 28.072 -27.462 1.00 18.81 ? 268  THR B O   1 
ATOM   4611 C CB  . THR B 1 269 ? -44.693 30.610 -27.643 1.00 17.73 ? 268  THR B CB  1 
ATOM   4612 O OG1 . THR B 1 269 ? -43.421 30.018 -27.976 1.00 17.90 ? 268  THR B OG1 1 
ATOM   4613 C CG2 . THR B 1 269 ? -44.488 32.116 -27.430 1.00 18.06 ? 268  THR B CG2 1 
ATOM   4614 N N   . GLY B 1 270 ? -44.667 27.601 -25.975 1.00 15.82 ? 269  GLY B N   1 
ATOM   4615 C CA  . GLY B 1 270 ? -44.845 26.171 -26.136 1.00 18.39 ? 269  GLY B CA  1 
ATOM   4616 C C   . GLY B 1 270 ? -43.553 25.384 -26.105 1.00 13.60 ? 269  GLY B C   1 
ATOM   4617 O O   . GLY B 1 270 ? -42.552 25.855 -25.557 1.00 15.34 ? 269  GLY B O   1 
ATOM   4618 N N   . ALA B 1 271 ? -43.559 24.198 -26.725 1.00 15.96 ? 270  ALA B N   1 
ATOM   4619 C CA  . ALA B 1 271 ? -42.486 23.226 -26.521 1.00 14.39 ? 270  ALA B CA  1 
ATOM   4620 C C   . ALA B 1 271 ? -42.431 22.277 -27.704 1.00 21.80 ? 270  ALA B C   1 
ATOM   4621 O O   . ALA B 1 271 ? -43.461 21.968 -28.315 1.00 17.04 ? 270  ALA B O   1 
ATOM   4622 C CB  . ALA B 1 271 ? -42.702 22.429 -25.230 1.00 16.74 ? 270  ALA B CB  1 
ATOM   4623 N N   . ILE B 1 272 ? -41.223 21.789 -27.995 1.00 16.16 ? 271  ILE B N   1 
ATOM   4624 C CA  . ILE B 1 272 ? -40.953 20.956 -29.167 1.00 14.69 ? 271  ILE B CA  1 
ATOM   4625 C C   . ILE B 1 272 ? -40.078 19.783 -28.731 1.00 16.31 ? 271  ILE B C   1 
ATOM   4626 O O   . ILE B 1 272 ? -38.942 19.981 -28.289 1.00 16.33 ? 271  ILE B O   1 
ATOM   4627 C CB  . ILE B 1 272 ? -40.260 21.745 -30.290 1.00 15.40 ? 271  ILE B CB  1 
ATOM   4628 C CG1 . ILE B 1 272 ? -41.029 23.031 -30.637 1.00 15.24 ? 271  ILE B CG1 1 
ATOM   4629 C CG2 . ILE B 1 272 ? -40.077 20.849 -31.536 1.00 16.51 ? 271  ILE B CG2 1 
ATOM   4630 C CD1 . ILE B 1 272 ? -40.420 23.790 -31.837 1.00 14.49 ? 271  ILE B CD1 1 
ATOM   4631 N N   . TRP B 1 273 ? -40.607 18.570 -28.836 1.00 15.68 ? 272  TRP B N   1 
ATOM   4632 C CA  . TRP B 1 273 ? -39.897 17.369 -28.410 1.00 13.55 ? 272  TRP B CA  1 
ATOM   4633 C C   . TRP B 1 273 ? -38.704 17.055 -29.309 1.00 16.39 ? 272  TRP B C   1 
ATOM   4634 O O   . TRP B 1 273 ? -38.745 17.259 -30.523 1.00 16.66 ? 272  TRP B O   1 
ATOM   4635 C CB  . TRP B 1 273 ? -40.869 16.180 -28.423 1.00 16.77 ? 272  TRP B CB  1 
ATOM   4636 C CG  . TRP B 1 273 ? -40.281 14.902 -27.945 1.00 15.83 ? 272  TRP B CG  1 
ATOM   4637 C CD1 . TRP B 1 273 ? -39.722 13.906 -28.699 1.00 15.82 ? 272  TRP B CD1 1 
ATOM   4638 C CD2 . TRP B 1 273 ? -40.209 14.467 -26.579 1.00 17.10 ? 272  TRP B CD2 1 
ATOM   4639 N NE1 . TRP B 1 273 ? -39.297 12.876 -27.872 1.00 16.10 ? 272  TRP B NE1 1 
ATOM   4640 C CE2 . TRP B 1 273 ? -39.591 13.199 -26.573 1.00 16.23 ? 272  TRP B CE2 1 
ATOM   4641 C CE3 . TRP B 1 273 ? -40.602 15.037 -25.361 1.00 19.72 ? 272  TRP B CE3 1 
ATOM   4642 C CZ2 . TRP B 1 273 ? -39.347 12.487 -25.392 1.00 17.72 ? 272  TRP B CZ2 1 
ATOM   4643 C CZ3 . TRP B 1 273 ? -40.369 14.325 -24.191 1.00 18.31 ? 272  TRP B CZ3 1 
ATOM   4644 C CH2 . TRP B 1 273 ? -39.748 13.062 -24.220 1.00 16.39 ? 272  TRP B CH2 1 
ATOM   4645 N N   . TRP B 1 274 ? -37.633 16.528 -28.707 1.00 14.94 ? 273  TRP B N   1 
ATOM   4646 C CA  . TRP B 1 274 ? -36.509 15.948 -29.451 1.00 15.93 ? 273  TRP B CA  1 
ATOM   4647 C C   . TRP B 1 274 ? -36.547 14.434 -29.231 1.00 17.13 ? 273  TRP B C   1 
ATOM   4648 O O   . TRP B 1 274 ? -36.313 13.979 -28.111 1.00 17.44 ? 273  TRP B O   1 
ATOM   4649 C CB  . TRP B 1 274 ? -35.166 16.525 -28.970 1.00 15.61 ? 273  TRP B CB  1 
ATOM   4650 C CG  . TRP B 1 274 ? -34.019 15.911 -29.730 1.00 15.20 ? 273  TRP B CG  1 
ATOM   4651 C CD1 . TRP B 1 274 ? -33.336 14.772 -29.415 1.00 16.46 ? 273  TRP B CD1 1 
ATOM   4652 C CD2 . TRP B 1 274 ? -33.487 16.364 -30.985 1.00 15.93 ? 273  TRP B CD2 1 
ATOM   4653 N NE1 . TRP B 1 274 ? -32.398 14.500 -30.383 1.00 18.04 ? 273  TRP B NE1 1 
ATOM   4654 C CE2 . TRP B 1 274 ? -32.472 15.461 -31.357 1.00 15.61 ? 273  TRP B CE2 1 
ATOM   4655 C CE3 . TRP B 1 274 ? -33.765 17.453 -31.816 1.00 14.73 ? 273  TRP B CE3 1 
ATOM   4656 C CZ2 . TRP B 1 274 ? -31.738 15.603 -32.542 1.00 18.95 ? 273  TRP B CZ2 1 
ATOM   4657 C CZ3 . TRP B 1 274 ? -33.018 17.603 -32.999 1.00 16.09 ? 273  TRP B CZ3 1 
ATOM   4658 C CH2 . TRP B 1 274 ? -32.024 16.675 -33.339 1.00 17.43 ? 273  TRP B CH2 1 
ATOM   4659 N N   . ALA B 1 275 ? -36.831 13.631 -30.268 1.00 15.29 ? 274  ALA B N   1 
ATOM   4660 C CA  . ALA B 1 275 ? -37.085 14.025 -31.650 1.00 14.49 ? 274  ALA B CA  1 
ATOM   4661 C C   . ALA B 1 275 ? -37.848 12.891 -32.357 1.00 14.78 ? 274  ALA B C   1 
ATOM   4662 O O   . ALA B 1 275 ? -37.768 11.725 -31.951 1.00 17.21 ? 274  ALA B O   1 
ATOM   4663 C CB  . ALA B 1 275 ? -35.775 14.291 -32.388 1.00 17.31 ? 274  ALA B CB  1 
ATOM   4664 N N   . ALA B 1 276 ? -38.578 13.236 -33.416 1.00 15.67 ? 275  ALA B N   1 
ATOM   4665 C CA  . ALA B 1 276 ? -39.103 12.253 -34.351 1.00 18.57 ? 275  ALA B CA  1 
ATOM   4666 C C   . ALA B 1 276 ? -38.182 12.221 -35.571 1.00 18.23 ? 275  ALA B C   1 
ATOM   4667 O O   . ALA B 1 276 ? -37.160 12.910 -35.605 1.00 16.19 ? 275  ALA B O   1 
ATOM   4668 C CB  . ALA B 1 276 ? -40.546 12.585 -34.745 1.00 18.66 ? 275  ALA B CB  1 
ATOM   4669 N N   . GLY B 1 277 ? -38.564 11.447 -36.596 1.00 16.00 ? 276  GLY B N   1 
ATOM   4670 C CA  . GLY B 1 277 ? -37.735 11.264 -37.779 1.00 16.42 ? 276  GLY B CA  1 
ATOM   4671 C C   . GLY B 1 277 ? -37.646 9.785  -38.131 1.00 18.74 ? 276  GLY B C   1 
ATOM   4672 O O   . GLY B 1 277 ? -37.887 8.913  -37.289 1.00 21.21 ? 276  GLY B O   1 
ATOM   4673 N N   . PRO B 1 278 ? -37.292 9.462  -39.378 1.00 18.15 ? 277  PRO B N   1 
ATOM   4674 C CA  . PRO B 1 278 ? -37.435 8.074  -39.838 1.00 20.56 ? 277  PRO B CA  1 
ATOM   4675 C C   . PRO B 1 278 ? -36.260 7.148  -39.565 1.00 20.75 ? 277  PRO B C   1 
ATOM   4676 O O   . PRO B 1 278 ? -36.415 5.933  -39.755 1.00 23.82 ? 277  PRO B O   1 
ATOM   4677 C CB  . PRO B 1 278 ? -37.631 8.236  -41.360 1.00 23.22 ? 277  PRO B CB  1 
ATOM   4678 C CG  . PRO B 1 278 ? -36.984 9.505  -41.696 1.00 22.45 ? 277  PRO B CG  1 
ATOM   4679 C CD  . PRO B 1 278 ? -36.962 10.389 -40.476 1.00 16.79 ? 277  PRO B CD  1 
ATOM   4680 N N   . TRP B 1 279 ? -35.098 7.665  -39.160 1.00 20.63 ? 278  TRP B N   1 
ATOM   4681 C CA  . TRP B 1 279 ? -33.909 6.835  -38.988 1.00 21.02 ? 278  TRP B CA  1 
ATOM   4682 C C   . TRP B 1 279 ? -33.472 6.740  -37.533 1.00 28.27 ? 278  TRP B C   1 
ATOM   4683 O O   . TRP B 1 279 ? -32.280 6.612  -37.250 1.00 23.97 ? 278  TRP B O   1 
ATOM   4684 C CB  . TRP B 1 279 ? -32.749 7.347  -39.847 1.00 19.05 ? 278  TRP B CB  1 
ATOM   4685 C CG  . TRP B 1 279 ? -32.799 6.864  -41.280 1.00 22.87 ? 278  TRP B CG  1 
ATOM   4686 C CD1 . TRP B 1 279 ? -33.788 6.123  -41.863 1.00 23.95 ? 278  TRP B CD1 1 
ATOM   4687 C CD2 . TRP B 1 279 ? -31.817 7.099  -42.305 1.00 21.56 ? 278  TRP B CD2 1 
ATOM   4688 N NE1 . TRP B 1 279 ? -33.479 5.883  -43.190 1.00 26.09 ? 278  TRP B NE1 1 
ATOM   4689 C CE2 . TRP B 1 279 ? -32.275 6.470  -43.477 1.00 21.92 ? 278  TRP B CE2 1 
ATOM   4690 C CE3 . TRP B 1 279 ? -30.595 7.781  -42.338 1.00 26.87 ? 278  TRP B CE3 1 
ATOM   4691 C CZ2 . TRP B 1 279 ? -31.554 6.503  -44.675 1.00 27.86 ? 278  TRP B CZ2 1 
ATOM   4692 C CZ3 . TRP B 1 279 ? -29.883 7.813  -43.521 1.00 26.99 ? 278  TRP B CZ3 1 
ATOM   4693 C CH2 . TRP B 1 279 ? -30.360 7.179  -44.672 1.00 24.70 ? 278  TRP B CH2 1 
ATOM   4694 N N   . TRP B 1 280 ? -34.421 6.788  -36.599 1.00 22.70 ? 279  TRP B N   1 
ATOM   4695 C CA  . TRP B 1 280 ? -34.073 6.708  -35.188 1.00 22.17 ? 279  TRP B CA  1 
ATOM   4696 C C   . TRP B 1 280 ? -34.069 5.285  -34.632 1.00 24.00 ? 279  TRP B C   1 
ATOM   4697 O O   . TRP B 1 280 ? -33.423 5.047  -33.604 1.00 24.21 ? 279  TRP B O   1 
ATOM   4698 C CB  . TRP B 1 280 ? -35.036 7.569  -34.354 1.00 20.38 ? 279  TRP B CB  1 
ATOM   4699 C CG  . TRP B 1 280 ? -34.762 9.049  -34.390 1.00 19.02 ? 279  TRP B CG  1 
ATOM   4700 C CD1 . TRP B 1 280 ? -35.613 10.032 -34.822 1.00 18.71 ? 279  TRP B CD1 1 
ATOM   4701 C CD2 . TRP B 1 280 ? -33.572 9.714  -33.955 1.00 18.39 ? 279  TRP B CD2 1 
ATOM   4702 N NE1 . TRP B 1 280 ? -35.018 11.265 -34.694 1.00 21.22 ? 279  TRP B NE1 1 
ATOM   4703 C CE2 . TRP B 1 280 ? -33.769 11.097 -34.147 1.00 18.97 ? 279  TRP B CE2 1 
ATOM   4704 C CE3 . TRP B 1 280 ? -32.356 9.274  -33.419 1.00 20.00 ? 279  TRP B CE3 1 
ATOM   4705 C CZ2 . TRP B 1 280 ? -32.795 12.047 -33.822 1.00 19.65 ? 279  TRP B CZ2 1 
ATOM   4706 C CZ3 . TRP B 1 280 ? -31.390 10.227 -33.095 1.00 18.73 ? 279  TRP B CZ3 1 
ATOM   4707 C CH2 . TRP B 1 280 ? -31.620 11.592 -33.297 1.00 17.35 ? 279  TRP B CH2 1 
ATOM   4708 N N   . GLY B 1 281 ? -34.778 4.342  -35.255 1.00 24.82 ? 280  GLY B N   1 
ATOM   4709 C CA  . GLY B 1 281 ? -34.848 2.997  -34.694 1.00 27.92 ? 280  GLY B CA  1 
ATOM   4710 C C   . GLY B 1 281 ? -35.304 2.996  -33.237 1.00 26.71 ? 280  GLY B C   1 
ATOM   4711 O O   . GLY B 1 281 ? -36.318 3.608  -32.875 1.00 28.71 ? 280  GLY B O   1 
ATOM   4712 N N   . ASP B 1 282 ? -34.550 2.317  -32.370 1.00 25.30 ? 281  ASP B N   1 
ATOM   4713 C CA  . ASP B 1 282 ? -34.925 2.207  -30.963 1.00 24.69 ? 281  ASP B CA  1 
ATOM   4714 C C   . ASP B 1 282 ? -34.383 3.345  -30.102 1.00 25.53 ? 281  ASP B C   1 
ATOM   4715 O O   . ASP B 1 282 ? -34.257 3.170  -28.885 1.00 25.42 ? 281  ASP B O   1 
ATOM   4716 C CB  . ASP B 1 282 ? -34.469 0.862  -30.384 1.00 28.03 ? 281  ASP B CB  1 
ATOM   4717 C CG  . ASP B 1 282 ? -35.358 -0.300 -30.822 1.00 37.26 ? 281  ASP B CG  1 
ATOM   4718 O OD1 . ASP B 1 282 ? -36.544 -0.064 -31.167 1.00 30.94 ? 281  ASP B OD1 1 
ATOM   4719 O OD2 . ASP B 1 282 ? -34.869 -1.456 -30.830 1.00 39.26 ? 281  ASP B OD2 1 
ATOM   4720 N N   . TYR B 1 283 ? -34.072 4.497  -30.700 1.00 22.43 ? 282  TYR B N   1 
ATOM   4721 C CA  . TYR B 1 283 ? -33.610 5.679  -29.969 1.00 21.02 ? 282  TYR B CA  1 
ATOM   4722 C C   . TYR B 1 283 ? -34.434 5.928  -28.720 1.00 19.57 ? 282  TYR B C   1 
ATOM   4723 O O   . TYR B 1 283 ? -35.666 5.845  -28.743 1.00 22.13 ? 282  TYR B O   1 
ATOM   4724 C CB  . TYR B 1 283 ? -33.708 6.902  -30.871 1.00 18.35 ? 282  TYR B CB  1 
ATOM   4725 C CG  . TYR B 1 283 ? -33.161 8.212  -30.352 1.00 21.24 ? 282  TYR B CG  1 
ATOM   4726 C CD1 . TYR B 1 283 ? -31.901 8.294  -29.763 1.00 21.92 ? 282  TYR B CD1 1 
ATOM   4727 C CD2 . TYR B 1 283 ? -33.883 9.398  -30.532 1.00 17.84 ? 282  TYR B CD2 1 
ATOM   4728 C CE1 . TYR B 1 283 ? -31.387 9.532  -29.343 1.00 21.54 ? 282  TYR B CE1 1 
ATOM   4729 C CE2 . TYR B 1 283 ? -33.377 10.628 -30.129 1.00 17.14 ? 282  TYR B CE2 1 
ATOM   4730 C CZ  . TYR B 1 283 ? -32.135 10.690 -29.529 1.00 17.63 ? 282  TYR B CZ  1 
ATOM   4731 O OH  . TYR B 1 283 ? -31.635 11.916 -29.138 1.00 19.37 ? 282  TYR B OH  1 
ATOM   4732 N N   . ILE B 1 284 ? -33.741 6.279  -27.634 1.00 19.75 ? 283  ILE B N   1 
ATOM   4733 C CA  . ILE B 1 284 ? -34.401 6.448  -26.348 1.00 18.88 ? 283  ILE B CA  1 
ATOM   4734 C C   . ILE B 1 284 ? -35.438 7.564  -26.351 1.00 21.03 ? 283  ILE B C   1 
ATOM   4735 O O   . ILE B 1 284 ? -36.332 7.565  -25.494 1.00 19.98 ? 283  ILE B O   1 
ATOM   4736 C CB  . ILE B 1 284 ? -33.364 6.698  -25.233 1.00 20.75 ? 283  ILE B CB  1 
ATOM   4737 C CG1 . ILE B 1 284 ? -32.406 7.840  -25.604 1.00 19.76 ? 283  ILE B CG1 1 
ATOM   4738 C CG2 . ILE B 1 284 ? -32.612 5.402  -24.902 1.00 23.50 ? 283  ILE B CG2 1 
ATOM   4739 C CD1 . ILE B 1 284 ? -31.514 8.283  -24.426 1.00 24.98 ? 283  ILE B CD1 1 
ATOM   4740 N N   . PHE B 1 285 ? -35.353 8.516  -27.285 1.00 18.82 ? 284  PHE B N   1 
ATOM   4741 C CA  . PHE B 1 285 ? -36.298 9.629  -27.313 1.00 18.31 ? 284  PHE B CA  1 
ATOM   4742 C C   . PHE B 1 285 ? -37.201 9.623  -28.551 1.00 17.31 ? 284  PHE B C   1 
ATOM   4743 O O   . PHE B 1 285 ? -37.799 10.659 -28.867 1.00 18.46 ? 284  PHE B O   1 
ATOM   4744 C CB  . PHE B 1 285 ? -35.560 10.974 -27.229 1.00 16.60 ? 284  PHE B CB  1 
ATOM   4745 C CG  . PHE B 1 285 ? -34.673 11.140 -26.014 1.00 17.87 ? 284  PHE B CG  1 
ATOM   4746 C CD1 . PHE B 1 285 ? -35.062 10.687 -24.764 1.00 20.22 ? 284  PHE B CD1 1 
ATOM   4747 C CD2 . PHE B 1 285 ? -33.447 11.792 -26.145 1.00 17.95 ? 284  PHE B CD2 1 
ATOM   4748 C CE1 . PHE B 1 285 ? -34.235 10.869 -23.665 1.00 22.62 ? 284  PHE B CE1 1 
ATOM   4749 C CE2 . PHE B 1 285 ? -32.612 11.988 -25.065 1.00 19.08 ? 284  PHE B CE2 1 
ATOM   4750 C CZ  . PHE B 1 285 ? -33.008 11.522 -23.808 1.00 18.67 ? 284  PHE B CZ  1 
ATOM   4751 N N   . SER B 1 286 ? -37.323 8.503  -29.273 1.00 16.91 ? 285  SER B N   1 
ATOM   4752 C CA  . SER B 1 286 ? -37.956 8.579  -30.597 1.00 15.89 ? 285  SER B CA  1 
ATOM   4753 C C   . SER B 1 286 ? -39.456 8.844  -30.499 1.00 18.81 ? 285  SER B C   1 
ATOM   4754 O O   . SER B 1 286 ? -40.214 8.032  -29.953 1.00 19.70 ? 285  SER B O   1 
ATOM   4755 C CB  . SER B 1 286 ? -37.721 7.318  -31.411 1.00 20.86 ? 285  SER B CB  1 
ATOM   4756 O OG  . SER B 1 286 ? -38.475 7.449  -32.611 1.00 20.46 ? 285  SER B OG  1 
ATOM   4757 N N   . MET B 1 287 ? -39.883 9.964  -31.069 1.00 17.98 ? 286  MET B N   1 
ATOM   4758 C CA  . MET B 1 287 ? -41.291 10.310 -31.193 1.00 20.48 ? 286  MET B CA  1 
ATOM   4759 C C   . MET B 1 287 ? -41.873 9.840  -32.533 1.00 19.24 ? 286  MET B C   1 
ATOM   4760 O O   . MET B 1 287 ? -42.991 10.233 -32.892 1.00 20.00 ? 286  MET B O   1 
ATOM   4761 C CB  . MET B 1 287 ? -41.442 11.833 -31.005 1.00 19.71 ? 286  MET B CB  1 
ATOM   4762 C CG  . MET B 1 287 ? -42.862 12.417 -30.958 1.00 20.99 ? 286  MET B CG  1 
ATOM   4763 S SD  . MET B 1 287 ? -43.885 11.717 -29.659 1.00 21.29 ? 286  MET B SD  1 
ATOM   4764 C CE  . MET B 1 287 ? -43.010 12.342 -28.213 1.00 24.08 ? 286  MET B CE  1 
ATOM   4765 N N   . GLU B 1 288 ? -41.157 8.991  -33.270 1.00 18.80 ? 287  GLU B N   1 
ATOM   4766 C CA  . GLU B 1 288 ? -41.619 8.618  -34.613 1.00 19.00 ? 287  GLU B CA  1 
ATOM   4767 C C   . GLU B 1 288 ? -42.761 7.604  -34.550 1.00 19.96 ? 287  GLU B C   1 
ATOM   4768 O O   . GLU B 1 288 ? -42.564 6.498  -34.035 1.00 23.30 ? 287  GLU B O   1 
ATOM   4769 C CB  . GLU B 1 288 ? -40.474 8.044  -35.445 1.00 19.67 ? 287  GLU B CB  1 
ATOM   4770 C CG  . GLU B 1 288 ? -40.846 7.742  -36.917 1.00 20.71 ? 287  GLU B CG  1 
ATOM   4771 C CD  . GLU B 1 288 ? -40.969 9.014  -37.766 1.00 21.00 ? 287  GLU B CD  1 
ATOM   4772 O OE1 . GLU B 1 288 ? -40.996 10.130 -37.178 1.00 20.60 ? 287  GLU B OE1 1 
ATOM   4773 O OE2 . GLU B 1 288 ? -41.049 8.894  -39.015 1.00 20.04 ? 287  GLU B OE2 1 
ATOM   4774 N N   . PRO B 1 289 ? -43.946 7.925  -35.071 1.00 19.00 ? 288  PRO B N   1 
ATOM   4775 C CA  . PRO B 1 289 ? -45.009 6.916  -35.180 1.00 18.77 ? 288  PRO B CA  1 
ATOM   4776 C C   . PRO B 1 289 ? -44.552 5.798  -36.102 1.00 26.58 ? 288  PRO B C   1 
ATOM   4777 O O   . PRO B 1 289 ? -43.781 6.032  -37.033 1.00 23.97 ? 288  PRO B O   1 
ATOM   4778 C CB  . PRO B 1 289 ? -46.184 7.697  -35.799 1.00 25.12 ? 288  PRO B CB  1 
ATOM   4779 C CG  . PRO B 1 289 ? -45.848 9.161  -35.619 1.00 25.66 ? 288  PRO B CG  1 
ATOM   4780 C CD  . PRO B 1 289 ? -44.336 9.225  -35.644 1.00 19.42 ? 288  PRO B CD  1 
ATOM   4781 N N   . ASP B 1 290 ? -45.048 4.574  -35.874 1.00 24.74 ? 289  ASP B N   1 
ATOM   4782 C CA  . ASP B 1 290 ? -46.003 4.206  -34.831 1.00 22.80 ? 289  ASP B CA  1 
ATOM   4783 C C   . ASP B 1 290 ? -45.302 3.529  -33.654 1.00 31.70 ? 289  ASP B C   1 
ATOM   4784 O O   . ASP B 1 290 ? -45.945 3.182  -32.647 1.00 28.26 ? 289  ASP B O   1 
ATOM   4785 C CB  . ASP B 1 290 ? -47.059 3.244  -35.391 1.00 22.65 ? 289  ASP B CB  1 
ATOM   4786 C CG  . ASP B 1 290 ? -47.937 3.875  -36.445 1.00 34.18 ? 289  ASP B CG  1 
ATOM   4787 O OD1 . ASP B 1 290 ? -48.185 5.089  -36.358 1.00 28.01 ? 289  ASP B OD1 1 
ATOM   4788 O OD2 . ASP B 1 290 ? -48.395 3.152  -37.356 1.00 39.27 ? 289  ASP B OD2 1 
ATOM   4789 N N   . ASN B 1 291 ? -43.986 3.342  -33.751 1.00 24.97 ? 290  ASN B N   1 
ATOM   4790 C CA  . ASN B 1 291 ? -43.294 2.479  -32.795 1.00 24.21 ? 290  ASN B CA  1 
ATOM   4791 C C   . ASN B 1 291 ? -42.176 3.145  -31.997 1.00 30.06 ? 290  ASN B C   1 
ATOM   4792 O O   . ASN B 1 291 ? -41.517 2.459  -31.199 1.00 25.79 ? 290  ASN B O   1 
ATOM   4793 C CB  . ASN B 1 291 ? -42.748 1.249  -33.532 1.00 30.66 ? 290  ASN B CB  1 
ATOM   4794 C CG  . ASN B 1 291 ? -43.860 0.446  -34.205 1.00 33.15 ? 290  ASN B CG  1 
ATOM   4795 O OD1 . ASN B 1 291 ? -44.896 0.178  -33.595 1.00 34.73 ? 290  ASN B OD1 1 
ATOM   4796 N ND2 . ASN B 1 291 ? -43.660 0.086  -35.463 1.00 34.73 ? 290  ASN B ND2 1 
ATOM   4797 N N   . GLY B 1 292 ? -41.944 4.444  -32.163 1.00 21.16 ? 291  GLY B N   1 
ATOM   4798 C CA  . GLY B 1 292 ? -40.981 5.114  -31.302 1.00 20.61 ? 291  GLY B CA  1 
ATOM   4799 C C   . GLY B 1 292 ? -41.400 5.011  -29.847 1.00 22.18 ? 291  GLY B C   1 
ATOM   4800 O O   . GLY B 1 292 ? -42.587 5.064  -29.520 1.00 22.42 ? 291  GLY B O   1 
ATOM   4801 N N   . ILE B 1 293 ? -40.409 4.842  -28.966 1.00 18.61 ? 292  ILE B N   1 
ATOM   4802 C CA  . ILE B 1 293 ? -40.735 4.605  -27.560 1.00 22.19 ? 292  ILE B CA  1 
ATOM   4803 C C   . ILE B 1 293 ? -41.364 5.845  -26.935 1.00 22.22 ? 292  ILE B C   1 
ATOM   4804 O O   . ILE B 1 293 ? -42.254 5.729  -26.080 1.00 23.10 ? 292  ILE B O   1 
ATOM   4805 C CB  . ILE B 1 293 ? -39.493 4.127  -26.775 1.00 21.65 ? 292  ILE B CB  1 
ATOM   4806 C CG1 . ILE B 1 293 ? -39.920 3.568  -25.417 1.00 23.59 ? 292  ILE B CG1 1 
ATOM   4807 C CG2 . ILE B 1 293 ? -38.468 5.250  -26.569 1.00 21.24 ? 292  ILE B CG2 1 
ATOM   4808 C CD1 . ILE B 1 293 ? -38.760 3.062  -24.572 1.00 20.65 ? 292  ILE B CD1 1 
ATOM   4809 N N   . ALA B 1 294 ? -40.945 7.046  -27.356 1.00 20.41 ? 293  ALA B N   1 
ATOM   4810 C CA  . ALA B 1 294 ? -41.594 8.246  -26.845 1.00 18.82 ? 293  ALA B CA  1 
ATOM   4811 C C   . ALA B 1 294 ? -42.966 8.425  -27.478 1.00 21.22 ? 293  ALA B C   1 
ATOM   4812 O O   . ALA B 1 294 ? -43.880 8.945  -26.828 1.00 20.44 ? 293  ALA B O   1 
ATOM   4813 C CB  . ALA B 1 294 ? -40.722 9.489  -27.076 1.00 19.26 ? 293  ALA B CB  1 
ATOM   4814 N N   . TYR B 1 295 ? -43.132 7.982  -28.734 1.00 19.59 ? 294  TYR B N   1 
ATOM   4815 C CA  . TYR B 1 295 ? -44.449 8.031  -29.361 1.00 21.09 ? 294  TYR B CA  1 
ATOM   4816 C C   . TYR B 1 295 ? -45.443 7.184  -28.577 1.00 21.34 ? 294  TYR B C   1 
ATOM   4817 O O   . TYR B 1 295 ? -46.614 7.554  -28.427 1.00 23.85 ? 294  TYR B O   1 
ATOM   4818 C CB  . TYR B 1 295 ? -44.379 7.561  -30.825 1.00 19.89 ? 294  TYR B CB  1 
ATOM   4819 C CG  . TYR B 1 295 ? -45.739 7.602  -31.501 1.00 21.45 ? 294  TYR B CG  1 
ATOM   4820 C CD1 . TYR B 1 295 ? -46.316 8.819  -31.855 1.00 20.71 ? 294  TYR B CD1 1 
ATOM   4821 C CD2 . TYR B 1 295 ? -46.463 6.437  -31.743 1.00 23.32 ? 294  TYR B CD2 1 
ATOM   4822 C CE1 . TYR B 1 295 ? -47.567 8.873  -32.442 1.00 22.46 ? 294  TYR B CE1 1 
ATOM   4823 C CE2 . TYR B 1 295 ? -47.714 6.482  -32.331 1.00 24.15 ? 294  TYR B CE2 1 
ATOM   4824 C CZ  . TYR B 1 295 ? -48.264 7.705  -32.668 1.00 22.75 ? 294  TYR B CZ  1 
ATOM   4825 O OH  . TYR B 1 295 ? -49.512 7.754  -33.235 1.00 29.32 ? 294  TYR B OH  1 
ATOM   4826 N N   . GLN B 1 296 ? -44.990 6.053  -28.053 1.00 21.16 ? 295  GLN B N   1 
ATOM   4827 C CA  . GLN B 1 296 ? -45.914 5.151  -27.381 1.00 22.14 ? 295  GLN B CA  1 
ATOM   4828 C C   . GLN B 1 296 ? -46.101 5.487  -25.910 1.00 24.93 ? 295  GLN B C   1 
ATOM   4829 O O   . GLN B 1 296 ? -47.225 5.397  -25.402 1.00 29.51 ? 295  GLN B O   1 
ATOM   4830 C CB  . GLN B 1 296 ? -45.438 3.707  -27.528 1.00 24.18 ? 295  GLN B CB  1 
ATOM   4831 C CG  . GLN B 1 296 ? -45.308 3.299  -28.979 1.00 28.77 ? 295  GLN B CG  1 
ATOM   4832 C CD  . GLN B 1 296 ? -45.622 1.838  -29.220 1.00 38.17 ? 295  GLN B CD  1 
ATOM   4833 O OE1 . GLN B 1 296 ? -45.760 1.390  -30.374 1.00 35.22 ? 295  GLN B OE1 1 
ATOM   4834 N NE2 . GLN B 1 296 ? -45.750 1.079  -28.135 1.00 33.57 ? 295  GLN B NE2 1 
ATOM   4835 N N   . GLN B 1 297 ? -45.026 5.883  -25.211 1.00 23.75 ? 296  GLN B N   1 
ATOM   4836 C CA  . GLN B 1 297 ? -45.094 6.077  -23.771 1.00 23.51 ? 296  GLN B CA  1 
ATOM   4837 C C   . GLN B 1 297 ? -45.075 7.528  -23.311 1.00 22.43 ? 296  GLN B C   1 
ATOM   4838 O O   . GLN B 1 297 ? -45.548 7.803  -22.204 1.00 26.04 ? 296  GLN B O   1 
ATOM   4839 C CB  . GLN B 1 297 ? -43.941 5.327  -23.085 1.00 21.16 ? 296  GLN B CB  1 
ATOM   4840 C CG  . GLN B 1 297 ? -44.097 3.817  -23.162 1.00 24.82 ? 296  GLN B CG  1 
ATOM   4841 C CD  . GLN B 1 297 ? -42.979 3.093  -22.426 1.00 22.77 ? 296  GLN B CD  1 
ATOM   4842 O OE1 . GLN B 1 297 ? -42.230 2.304  -23.013 1.00 29.20 ? 296  GLN B OE1 1 
ATOM   4843 N NE2 . GLN B 1 297 ? -42.861 3.366  -21.142 1.00 21.13 ? 296  GLN B NE2 1 
ATOM   4844 N N   . ILE B 1 298 ? -44.534 8.453  -24.099 1.00 20.81 ? 297  ILE B N   1 
ATOM   4845 C CA  . ILE B 1 298 ? -44.490 9.861  -23.716 1.00 16.85 ? 297  ILE B CA  1 
ATOM   4846 C C   . ILE B 1 298 ? -45.654 10.638 -24.317 1.00 24.04 ? 297  ILE B C   1 
ATOM   4847 O O   . ILE B 1 298 ? -46.226 11.506 -23.662 1.00 24.26 ? 297  ILE B O   1 
ATOM   4848 C CB  . ILE B 1 298 ? -43.136 10.502 -24.110 1.00 19.75 ? 297  ILE B CB  1 
ATOM   4849 C CG1 . ILE B 1 298 ? -41.967 9.799  -23.414 1.00 19.26 ? 297  ILE B CG1 1 
ATOM   4850 C CG2 . ILE B 1 298 ? -43.126 12.001 -23.752 1.00 22.43 ? 297  ILE B CG2 1 
ATOM   4851 C CD1 . ILE B 1 298 ? -41.984 9.931  -21.866 1.00 22.63 ? 297  ILE B CD1 1 
ATOM   4852 N N   . LEU B 1 299 ? -46.018 10.359 -25.570 1.00 21.54 ? 298  LEU B N   1 
ATOM   4853 C CA  . LEU B 1 299 ? -47.146 11.078 -26.150 1.00 22.58 ? 298  LEU B CA  1 
ATOM   4854 C C   . LEU B 1 299 ? -48.378 11.059 -25.248 1.00 23.29 ? 298  LEU B C   1 
ATOM   4855 O O   . LEU B 1 299 ? -49.023 12.114 -25.119 1.00 26.43 ? 298  LEU B O   1 
ATOM   4856 C CB  . LEU B 1 299 ? -47.460 10.521 -27.551 1.00 22.35 ? 298  LEU B CB  1 
ATOM   4857 C CG  . LEU B 1 299 ? -48.522 11.319 -28.312 1.00 27.63 ? 298  LEU B CG  1 
ATOM   4858 C CD1 . LEU B 1 299 ? -48.074 12.760 -28.490 1.00 24.97 ? 298  LEU B CD1 1 
ATOM   4859 C CD2 . LEU B 1 299 ? -48.818 10.673 -29.658 1.00 31.49 ? 298  LEU B CD2 1 
ATOM   4860 N N   . PRO B 1 300 ? -48.721 9.963  -24.559 1.00 26.08 ? 299  PRO B N   1 
ATOM   4861 C CA  . PRO B 1 300 ? -49.889 10.017 -23.663 1.00 32.59 ? 299  PRO B CA  1 
ATOM   4862 C C   . PRO B 1 300 ? -49.794 11.073 -22.574 1.00 30.89 ? 299  PRO B C   1 
ATOM   4863 O O   . PRO B 1 300 ? -50.837 11.574 -22.130 1.00 30.66 ? 299  PRO B O   1 
ATOM   4864 C CB  . PRO B 1 300 ? -49.937 8.601  -23.073 1.00 33.60 ? 299  PRO B CB  1 
ATOM   4865 C CG  . PRO B 1 300 ? -49.337 7.741  -24.138 1.00 31.08 ? 299  PRO B CG  1 
ATOM   4866 C CD  . PRO B 1 300 ? -48.205 8.585  -24.685 1.00 27.15 ? 299  PRO B CD  1 
ATOM   4867 N N   . ILE B 1 301 ? -48.591 11.449 -22.126 1.00 27.25 ? 300  ILE B N   1 
ATOM   4868 C CA  . ILE B 1 301 ? -48.497 12.515 -21.134 1.00 28.96 ? 300  ILE B CA  1 
ATOM   4869 C C   . ILE B 1 301 ? -48.337 13.891 -21.768 1.00 31.21 ? 300  ILE B C   1 
ATOM   4870 O O   . ILE B 1 301 ? -48.358 14.895 -21.048 1.00 28.33 ? 300  ILE B O   1 
ATOM   4871 C CB  . ILE B 1 301 ? -47.380 12.255 -20.096 1.00 30.14 ? 300  ILE B CB  1 
ATOM   4872 C CG1 . ILE B 1 301 ? -45.980 12.519 -20.652 1.00 28.32 ? 300  ILE B CG1 1 
ATOM   4873 C CG2 . ILE B 1 301 ? -47.466 10.828 -19.557 1.00 31.46 ? 300  ILE B CG2 1 
ATOM   4874 C CD1 . ILE B 1 301 ? -44.881 12.485 -19.541 1.00 26.68 ? 300  ILE B CD1 1 
ATOM   4875 N N   . LEU B 1 302 ? -48.203 13.976 -23.095 1.00 23.59 ? 301  LEU B N   1 
ATOM   4876 C CA  . LEU B 1 302 ? -48.219 15.264 -23.778 1.00 22.85 ? 301  LEU B CA  1 
ATOM   4877 C C   . LEU B 1 302 ? -49.619 15.633 -24.250 1.00 25.08 ? 301  LEU B C   1 
ATOM   4878 O O   . LEU B 1 302 ? -49.951 16.821 -24.345 1.00 25.47 ? 301  LEU B O   1 
ATOM   4879 C CB  . LEU B 1 302 ? -47.262 15.242 -24.977 1.00 24.45 ? 301  LEU B CB  1 
ATOM   4880 C CG  . LEU B 1 302 ? -45.825 14.780 -24.705 1.00 23.49 ? 301  LEU B CG  1 
ATOM   4881 C CD1 . LEU B 1 302 ? -44.987 14.838 -25.988 1.00 24.96 ? 301  LEU B CD1 1 
ATOM   4882 C CD2 . LEU B 1 302 ? -45.167 15.605 -23.594 1.00 27.31 ? 301  LEU B CD2 1 
ATOM   4883 N N   . THR B 1 303 ? -50.432 14.624 -24.533 1.00 29.76 ? 302  THR B N   1 
ATOM   4884 C CA  . THR B 1 303 ? -51.821 14.816 -24.940 1.00 32.15 ? 302  THR B CA  1 
ATOM   4885 C C   . THR B 1 303 ? -52.611 15.825 -24.107 1.00 29.60 ? 302  THR B C   1 
ATOM   4886 O O   . THR B 1 303 ? -53.411 16.570 -24.702 1.00 31.90 ? 302  THR B O   1 
ATOM   4887 C CB  . THR B 1 303 ? -52.482 13.431 -24.942 1.00 31.66 ? 302  THR B CB  1 
ATOM   4888 O OG1 . THR B 1 303 ? -52.085 12.743 -26.137 1.00 34.99 ? 302  THR B OG1 1 
ATOM   4889 C CG2 . THR B 1 303 ? -53.994 13.530 -24.854 1.00 47.61 ? 302  THR B CG2 1 
ATOM   4890 N N   . PRO B 1 304 ? -52.439 15.932 -22.782 1.00 30.23 ? 303  PRO B N   1 
ATOM   4891 C CA  . PRO B 1 304 ? -53.211 16.939 -22.029 1.00 27.38 ? 303  PRO B CA  1 
ATOM   4892 C C   . PRO B 1 304 ? -52.991 18.374 -22.477 1.00 34.67 ? 303  PRO B C   1 
ATOM   4893 O O   . PRO B 1 304 ? -53.824 19.232 -22.164 1.00 36.56 ? 303  PRO B O   1 
ATOM   4894 C CB  . PRO B 1 304 ? -52.739 16.732 -20.583 1.00 32.61 ? 303  PRO B CB  1 
ATOM   4895 C CG  . PRO B 1 304 ? -52.358 15.311 -20.529 1.00 28.88 ? 303  PRO B CG  1 
ATOM   4896 C CD  . PRO B 1 304 ? -51.735 15.013 -21.869 1.00 31.97 ? 303  PRO B CD  1 
ATOM   4897 N N   . TYR B 1 305 ? -51.914 18.673 -23.204 1.00 26.07 ? 304  TYR B N   1 
ATOM   4898 C CA  . TYR B 1 305 ? -51.630 20.046 -23.594 1.00 28.40 ? 304  TYR B CA  1 
ATOM   4899 C C   . TYR B 1 305 ? -52.083 20.356 -25.010 1.00 30.71 ? 304  TYR B C   1 
ATOM   4900 O O   . TYR B 1 305 ? -52.061 21.529 -25.407 1.00 29.19 ? 304  TYR B O   1 
ATOM   4901 C CB  . TYR B 1 305 ? -50.129 20.333 -23.444 1.00 22.74 ? 304  TYR B CB  1 
ATOM   4902 C CG  . TYR B 1 305 ? -49.628 19.896 -22.093 1.00 23.18 ? 304  TYR B CG  1 
ATOM   4903 C CD1 . TYR B 1 305 ? -49.919 20.630 -20.957 1.00 25.69 ? 304  TYR B CD1 1 
ATOM   4904 C CD2 . TYR B 1 305 ? -48.931 18.707 -21.943 1.00 23.13 ? 304  TYR B CD2 1 
ATOM   4905 C CE1 . TYR B 1 305 ? -49.489 20.208 -19.709 1.00 22.71 ? 304  TYR B CE1 1 
ATOM   4906 C CE2 . TYR B 1 305 ? -48.507 18.272 -20.697 1.00 28.50 ? 304  TYR B CE2 1 
ATOM   4907 C CZ  . TYR B 1 305 ? -48.789 19.025 -19.588 1.00 25.95 ? 304  TYR B CZ  1 
ATOM   4908 O OH  . TYR B 1 305 ? -48.367 18.573 -18.351 1.00 25.60 ? 304  TYR B OH  1 
ATOM   4909 N N   . LEU B 1 306 ? -52.521 19.341 -25.755 1.00 29.06 ? 305  LEU B N   1 
ATOM   4910 C CA  . LEU B 1 306 ? -52.800 19.464 -27.181 1.00 31.29 ? 305  LEU B CA  1 
ATOM   4911 C C   . LEU B 1 306 ? -54.272 19.740 -27.450 1.00 32.06 ? 305  LEU B C   1 
ATOM   4912 O O   . LEU B 1 306 ? -54.650 20.064 -28.572 1.00 33.83 ? 305  LEU B O   1 
ATOM   4913 C CB  . LEU B 1 306 ? -52.350 18.192 -27.910 1.00 26.56 ? 305  LEU B CB  1 
ATOM   4914 C CG  . LEU B 1 306 ? -50.856 17.863 -27.752 1.00 29.07 ? 305  LEU B CG  1 
ATOM   4915 C CD1 . LEU B 1 306 ? -50.497 16.549 -28.428 1.00 30.22 ? 305  LEU B CD1 1 
ATOM   4916 C CD2 . LEU B 1 306 ? -49.952 18.991 -28.280 1.00 28.24 ? 305  LEU B CD2 1 
ATOM   4917 O OXT . LEU B 1 306 ? -55.120 19.651 -26.558 1.00 35.60 ? 305  LEU B OXT 1 
HETATM 4918 C C2  A BGC C 2 .   ? -13.146 16.978 -15.034 0.37 41.50 ? 1    BGC C C2  1 
HETATM 4919 C C2  B BGC C 2 .   ? -13.233 17.065 -15.066 0.48 41.68 ? 1    BGC C C2  1 
HETATM 4920 C C3  A BGC C 2 .   ? -13.410 15.823 -14.095 0.37 39.18 ? 1    BGC C C3  1 
HETATM 4921 C C3  B BGC C 2 .   ? -13.462 15.907 -14.115 0.48 39.24 ? 1    BGC C C3  1 
HETATM 4922 C C4  A BGC C 2 .   ? -14.577 14.975 -14.596 0.37 41.36 ? 1    BGC C C4  1 
HETATM 4923 C C4  B BGC C 2 .   ? -14.537 15.001 -14.715 0.48 41.45 ? 1    BGC C C4  1 
HETATM 4924 C C5  A BGC C 2 .   ? -14.679 14.821 -16.126 0.37 44.20 ? 1    BGC C C5  1 
HETATM 4925 C C5  B BGC C 2 .   ? -14.222 14.616 -16.170 0.48 44.83 ? 1    BGC C C5  1 
HETATM 4926 C C6  A BGC C 2 .   ? -16.038 15.279 -16.628 0.37 40.62 ? 1    BGC C C6  1 
HETATM 4927 C C6  B BGC C 2 .   ? -15.352 14.954 -17.131 0.48 42.80 ? 1    BGC C C6  1 
HETATM 4928 C C1  A BGC C 2 .   ? -12.791 16.415 -16.406 0.37 42.56 ? 1    BGC C C1  1 
HETATM 4929 C C1  B BGC C 2 .   ? -12.660 16.526 -16.380 0.48 42.61 ? 1    BGC C C1  1 
HETATM 4930 O O1  A BGC C 2 .   ? -12.751 17.473 -17.294 0.37 45.18 ? 1    BGC C O1  1 
HETATM 4931 O O1  B BGC C 2 .   ? -13.067 17.344 -17.424 0.48 45.13 ? 1    BGC C O1  1 
HETATM 4932 O O2  A BGC C 2 .   ? -12.068 17.687 -14.481 0.37 37.41 ? 1    BGC C O2  1 
HETATM 4933 O O2  B BGC C 2 .   ? -12.345 17.953 -14.428 0.48 38.54 ? 1    BGC C O2  1 
HETATM 4934 O O3  A BGC C 2 .   ? -13.710 16.252 -12.774 0.37 29.58 ? 1    BGC C O3  1 
HETATM 4935 O O3  B BGC C 2 .   ? -13.866 16.321 -12.817 0.48 29.62 ? 1    BGC C O3  1 
HETATM 4936 O O4  . BGC C 2 .   ? -13.943 13.730 -14.698 1.00 36.10 ? 1    BGC C O4  1 
HETATM 4937 O O5  A BGC C 2 .   ? -13.756 15.532 -16.933 0.37 45.20 ? 1    BGC C O5  1 
HETATM 4938 O O5  B BGC C 2 .   ? -13.036 15.195 -16.696 0.48 46.13 ? 1    BGC C O5  1 
HETATM 4939 O O6  A BGC C 2 .   ? -15.913 15.687 -17.973 0.37 47.87 ? 1    BGC C O6  1 
HETATM 4940 O O6  B BGC C 2 .   ? -16.521 14.254 -16.773 0.48 43.61 ? 1    BGC C O6  1 
HETATM 4941 C C2  . BGC C 2 .   ? -14.992 11.700 -14.037 1.00 28.63 ? 2    BGC C C2  1 
HETATM 4942 C C3  . BGC C 2 .   ? -16.000 11.209 -13.017 1.00 37.57 ? 2    BGC C C3  1 
HETATM 4943 C C4  . BGC C 2 .   ? -15.570 11.560 -11.596 1.00 29.78 ? 2    BGC C C4  1 
HETATM 4944 C C5  . BGC C 2 .   ? -15.138 13.026 -11.464 1.00 34.32 ? 2    BGC C C5  1 
HETATM 4945 C C6  . BGC C 2 .   ? -14.436 13.334 -10.153 1.00 30.21 ? 2    BGC C C6  1 
HETATM 4946 C C1  . BGC C 2 .   ? -14.794 13.185 -13.766 1.00 31.88 ? 2    BGC C C1  1 
HETATM 4947 O O2  . BGC C 2 .   ? -15.551 11.457 -15.303 1.00 34.50 ? 2    BGC C O2  1 
HETATM 4948 O O3  . BGC C 2 .   ? -16.155 9.809  -13.086 1.00 37.10 ? 2    BGC C O3  1 
HETATM 4949 O O4  . BGC C 2 .   ? -16.644 11.429 -10.709 1.00 29.06 ? 2    BGC C O4  1 
HETATM 4950 O O5  . BGC C 2 .   ? -14.231 13.343 -12.484 1.00 29.94 ? 2    BGC C O5  1 
HETATM 4951 O O6  . BGC C 2 .   ? -14.083 14.707 -10.118 1.00 26.60 ? 2    BGC C O6  1 
HETATM 4952 C C2  . BGC C 2 .   ? -17.475 10.383 -8.732  0.91 32.23 ? 3    BGC C C2  1 
HETATM 4953 C C3  . BGC C 2 .   ? -17.195 9.282  -7.723  0.91 37.58 ? 3    BGC C C3  1 
HETATM 4954 C C4  . BGC C 2 .   ? -17.064 7.908  -8.390  0.91 25.44 ? 3    BGC C C4  1 
HETATM 4955 C C5  . BGC C 2 .   ? -16.185 7.993  -9.637  0.91 26.32 ? 3    BGC C C5  1 
HETATM 4956 C C6  . BGC C 2 .   ? -16.319 6.721  -10.442 0.91 32.36 ? 3    BGC C C6  1 
HETATM 4957 C C1  . BGC C 2 .   ? -16.399 10.334 -9.815  0.91 31.18 ? 3    BGC C C1  1 
HETATM 4958 O O2  . BGC C 2 .   ? -17.490 11.612 -8.042  0.91 31.78 ? 3    BGC C O2  1 
HETATM 4959 O O3  . BGC C 2 .   ? -18.212 9.252  -6.747  0.91 31.18 ? 3    BGC C O3  1 
HETATM 4960 O O4  . BGC C 2 .   ? -16.348 6.989  -7.597  0.91 32.42 ? 3    BGC C O4  1 
HETATM 4961 O O5  . BGC C 2 .   ? -16.495 9.090  -10.472 0.91 28.90 ? 3    BGC C O5  1 
HETATM 4962 O O6  . BGC C 2 .   ? -15.208 6.674  -11.303 0.91 47.98 ? 3    BGC C O6  1 
HETATM 4963 C C2  . BGC C 2 .   ? -16.500 4.945  -6.373  0.85 37.71 ? 4    BGC C C2  1 
HETATM 4964 C C3  . BGC C 2 .   ? -17.289 4.197  -5.300  0.85 43.34 ? 4    BGC C C3  1 
HETATM 4965 C C4  . BGC C 2 .   ? -17.632 5.050  -4.077  0.85 30.81 ? 4    BGC C C4  1 
HETATM 4966 C C5  . BGC C 2 .   ? -18.184 6.406  -4.532  0.85 38.57 ? 4    BGC C C5  1 
HETATM 4967 C C6  . BGC C 2 .   ? -18.372 7.425  -3.420  0.85 34.79 ? 4    BGC C C6  1 
HETATM 4968 C C1  . BGC C 2 .   ? -17.168 6.283  -6.657  0.85 35.50 ? 4    BGC C C1  1 
HETATM 4969 O O2  . BGC C 2 .   ? -16.483 4.141  -7.531  0.85 39.85 ? 4    BGC C O2  1 
HETATM 4970 O O3  . BGC C 2 .   ? -16.586 3.072  -4.821  0.85 41.70 ? 4    BGC C O3  1 
HETATM 4971 O O4  . BGC C 2 .   ? -18.629 4.400  -3.323  0.85 42.35 ? 4    BGC C O4  1 
HETATM 4972 O O5  . BGC C 2 .   ? -17.270 6.968  -5.438  0.85 34.75 ? 4    BGC C O5  1 
HETATM 4973 O O6  . BGC C 2 .   ? -18.888 8.632  -3.957  0.85 25.87 ? 4    BGC C O6  1 
HETATM 4974 C C2  . BGC C 2 .   ? -19.453 3.678  -1.193  0.89 45.63 ? 5    BGC C C2  1 
HETATM 4975 C C3  . BGC C 2 .   ? -19.093 3.420  0.260   0.89 46.06 ? 5    BGC C C3  1 
HETATM 4976 C C4  . BGC C 2 .   ? -17.921 2.451  0.337   0.89 43.86 ? 5    BGC C C4  1 
HETATM 4977 C C5  . BGC C 2 .   ? -16.759 2.945  -0.532  0.89 32.28 ? 5    BGC C C5  1 
HETATM 4978 C C6  . BGC C 2 .   ? -15.672 1.893  -0.602  0.89 43.24 ? 5    BGC C C6  1 
HETATM 4979 C C1  . BGC C 2 .   ? -18.221 4.186  -1.953  0.89 39.14 ? 5    BGC C C1  1 
HETATM 4980 O O2  . BGC C 2 .   ? -20.506 4.611  -1.197  0.89 54.43 ? 5    BGC C O2  1 
HETATM 4981 O O3  . BGC C 2 .   ? -20.169 2.849  0.969   0.89 49.60 ? 5    BGC C O3  1 
HETATM 4982 O O4  . BGC C 2 .   ? -17.453 2.327  1.655   0.89 47.72 ? 5    BGC C O4  1 
HETATM 4983 O O5  . BGC C 2 .   ? -17.181 3.235  -1.853  0.89 38.13 ? 5    BGC C O5  1 
HETATM 4984 O O6  . BGC C 2 .   ? -15.255 1.598  0.713   0.89 51.24 ? 5    BGC C O6  1 
HETATM 4985 C C2  . BGC D 2 .   ? -28.761 18.292 -29.823 0.95 28.05 ? 1    BGC D C2  1 
HETATM 4986 C C3  . BGC D 2 .   ? -29.074 16.984 -30.548 0.95 19.43 ? 1    BGC D C3  1 
HETATM 4987 C C4  . BGC D 2 .   ? -28.323 15.782 -29.924 0.95 28.65 ? 1    BGC D C4  1 
HETATM 4988 C C5  . BGC D 2 .   ? -28.372 15.823 -28.391 0.95 30.39 ? 1    BGC D C5  1 
HETATM 4989 C C6  . BGC D 2 .   ? -27.427 14.847 -27.700 0.95 27.12 ? 1    BGC D C6  1 
HETATM 4990 C C1  . BGC D 2 .   ? -28.936 18.081 -28.323 0.95 32.32 ? 1    BGC D C1  1 
HETATM 4991 O O1  . BGC D 2 .   ? -28.570 19.203 -27.620 0.95 36.40 ? 1    BGC D O1  1 
HETATM 4992 O O2  . BGC D 2 .   ? -29.609 19.289 -30.325 0.95 29.17 ? 1    BGC D O2  1 
HETATM 4993 O O3  . BGC D 2 .   ? -28.741 17.090 -31.922 0.95 21.15 ? 1    BGC D O3  1 
HETATM 4994 O O4  . BGC D 2 .   ? -28.872 14.529 -30.266 0.95 21.23 ? 1    BGC D O4  1 
HETATM 4995 O O5  . BGC D 2 .   ? -28.005 17.102 -27.953 0.95 34.78 ? 1    BGC D O5  1 
HETATM 4996 O O6  . BGC D 2 .   ? -26.081 15.090 -28.096 0.95 25.03 ? 1    BGC D O6  1 
HETATM 4997 C C2  . BGC D 2 .   ? -28.238 12.394 -31.155 1.00 21.38 ? 2    BGC D C2  1 
HETATM 4998 C C3  . BGC D 2 .   ? -27.410 11.736 -32.243 1.00 22.24 ? 2    BGC D C3  1 
HETATM 4999 C C4  . BGC D 2 .   ? -27.882 12.190 -33.615 1.00 22.73 ? 2    BGC D C4  1 
HETATM 5000 C C5  . BGC D 2 .   ? -27.932 13.724 -33.669 1.00 26.79 ? 2    BGC D C5  1 
HETATM 5001 C C6  . BGC D 2 .   ? -28.656 14.245 -34.895 1.00 21.20 ? 2    BGC D C6  1 
HETATM 5002 C C1  . BGC D 2 .   ? -28.126 13.904 -31.315 1.00 27.80 ? 2    BGC D C1  1 
HETATM 5003 O O2  . BGC D 2 .   ? -27.733 11.916 -29.926 1.00 24.93 ? 2    BGC D O2  1 
HETATM 5004 O O3  . BGC D 2 .   ? -27.529 10.327 -32.152 1.00 28.85 ? 2    BGC D O3  1 
HETATM 5005 O O4  . BGC D 2 .   ? -26.957 11.839 -34.609 1.00 23.18 ? 2    BGC D O4  1 
HETATM 5006 O O5  . BGC D 2 .   ? -28.655 14.239 -32.579 1.00 23.74 ? 2    BGC D O5  1 
HETATM 5007 O O6  . BGC D 2 .   ? -28.600 15.663 -34.883 1.00 19.23 ? 2    BGC D O6  1 
HETATM 5008 C C2  . BGC D 2 .   ? -26.448 10.542 -36.528 0.95 22.96 ? 3    BGC D C2  1 
HETATM 5009 C C3  . BGC D 2 .   ? -26.941 9.419  -37.444 0.95 23.48 ? 3    BGC D C3  1 
HETATM 5010 C C4  . BGC D 2 .   ? -27.319 8.140  -36.681 0.95 23.83 ? 3    BGC D C4  1 
HETATM 5011 C C5  . BGC D 2 .   ? -28.079 8.490  -35.382 0.95 25.17 ? 3    BGC D C5  1 
HETATM 5012 C C6  . BGC D 2 .   ? -28.246 7.299  -34.462 0.95 24.63 ? 3    BGC D C6  1 
HETATM 5013 C C1  . BGC D 2 .   ? -27.427 10.722 -35.375 0.95 23.56 ? 3    BGC D C1  1 
HETATM 5014 O O2  . BGC D 2 .   ? -26.358 11.747 -37.261 0.95 24.38 ? 3    BGC D O2  1 
HETATM 5015 O O3  . BGC D 2 .   ? -25.968 9.103  -38.425 0.95 25.58 ? 3    BGC D O3  1 
HETATM 5016 O O4  . BGC D 2 .   ? -28.218 7.312  -37.403 0.95 27.51 ? 3    BGC D O4  1 
HETATM 5017 O O5  . BGC D 2 .   ? -27.445 9.516  -34.641 0.95 25.44 ? 3    BGC D O5  1 
HETATM 5018 O O6  . BGC D 2 .   ? -26.977 6.973  -33.960 0.95 30.05 ? 3    BGC D O6  1 
HETATM 5019 C C2  . BGC D 2 .   ? -28.529 5.270  -38.606 0.95 29.89 ? 4    BGC D C2  1 
HETATM 5020 C C3  . BGC D 2 .   ? -27.996 4.390  -39.732 0.95 27.98 ? 4    BGC D C3  1 
HETATM 5021 C C4  . BGC D 2 .   ? -27.692 5.156  -41.015 0.95 31.39 ? 4    BGC D C4  1 
HETATM 5022 C C5  . BGC D 2 .   ? -26.846 6.389  -40.657 0.95 30.51 ? 4    BGC D C5  1 
HETATM 5023 C C6  . BGC D 2 .   ? -26.624 7.351  -41.814 0.95 28.02 ? 4    BGC D C6  1 
HETATM 5024 C C1  . BGC D 2 .   ? -27.611 6.468  -38.399 0.95 26.43 ? 4    BGC D C1  1 
HETATM 5025 O O2  . BGC D 2 .   ? -28.582 4.477  -37.440 0.95 30.26 ? 4    BGC D O2  1 
HETATM 5026 O O3  . BGC D 2 .   ? -28.872 3.342  -40.081 0.95 34.10 ? 4    BGC D O3  1 
HETATM 5027 O O4  . BGC D 2 .   ? -26.918 4.276  -41.802 0.95 33.07 ? 4    BGC D O4  1 
HETATM 5028 O O5  . BGC D 2 .   ? -27.472 7.137  -39.628 0.95 23.98 ? 4    BGC D O5  1 
HETATM 5029 O O6  . BGC D 2 .   ? -25.802 8.434  -41.405 0.95 27.87 ? 4    BGC D O6  1 
HETATM 5030 C C2  . BGC D 2 .   ? -26.103 3.473  -43.872 0.95 37.36 ? 5    BGC D C2  1 
HETATM 5031 C C3  . BGC D 2 .   ? -26.353 3.343  -45.362 0.95 48.37 ? 5    BGC D C3  1 
HETATM 5032 C C4  . BGC D 2 .   ? -27.699 2.677  -45.622 0.95 35.18 ? 5    BGC D C4  1 
HETATM 5033 C C5  . BGC D 2 .   ? -28.789 3.413  -44.819 0.95 35.42 ? 5    BGC D C5  1 
HETATM 5034 C C6  . BGC D 2 .   ? -30.178 2.803  -44.895 0.95 41.27 ? 5    BGC D C6  1 
HETATM 5035 C C1  . BGC D 2 .   ? -27.268 4.194  -43.200 0.95 37.50 ? 5    BGC D C1  1 
HETATM 5036 O O2  . BGC D 2 .   ? -24.875 4.140  -43.692 0.95 44.90 ? 5    BGC D O2  1 
HETATM 5037 O O3  . BGC D 2 .   ? -25.337 2.577  -45.975 0.95 40.21 ? 5    BGC D O3  1 
HETATM 5038 O O4  . BGC D 2 .   ? -28.024 2.703  -46.988 0.95 43.04 ? 5    BGC D O4  1 
HETATM 5039 O O5  . BGC D 2 .   ? -28.434 3.456  -43.448 0.95 39.83 ? 5    BGC D O5  1 
HETATM 5040 O O6  . BGC D 2 .   ? -30.157 1.574  -45.577 0.95 52.21 ? 5    BGC D O6  1 
HETATM 5041 C C1  A GOL E 3 .   ? -19.600 41.418 -4.265  0.58 30.64 ? 501  GOL A C1  1 
HETATM 5042 C C1  B GOL E 3 .   ? -19.838 41.763 -4.635  0.42 31.25 ? 501  GOL A C1  1 
HETATM 5043 O O1  A GOL E 3 .   ? -18.514 41.985 -4.950  0.58 30.06 ? 501  GOL A O1  1 
HETATM 5044 O O1  B GOL E 3 .   ? -19.298 42.790 -3.835  0.42 37.07 ? 501  GOL A O1  1 
HETATM 5045 C C2  A GOL E 3 .   ? -20.897 42.114 -4.611  0.58 28.35 ? 501  GOL A C2  1 
HETATM 5046 C C2  B GOL E 3 .   ? -21.350 41.804 -4.571  0.42 31.53 ? 501  GOL A C2  1 
HETATM 5047 O O2  A GOL E 3 .   ? -21.115 41.973 -5.997  0.58 32.95 ? 501  GOL A O2  1 
HETATM 5048 O O2  B GOL E 3 .   ? -21.874 40.855 -5.474  0.42 33.45 ? 501  GOL A O2  1 
HETATM 5049 C C3  A GOL E 3 .   ? -22.025 41.449 -3.838  0.58 37.00 ? 501  GOL A C3  1 
HETATM 5050 C C3  B GOL E 3 .   ? -21.844 41.528 -3.161  0.42 36.75 ? 501  GOL A C3  1 
HETATM 5051 O O3  A GOL E 3 .   ? -21.473 40.826 -2.696  0.58 35.16 ? 501  GOL A O3  1 
HETATM 5052 O O3  B GOL E 3 .   ? -23.243 41.351 -3.241  0.42 38.62 ? 501  GOL A O3  1 
HETATM 5053 C C1  . GOL F 3 .   ? -12.061 18.591 -32.912 0.85 23.19 ? 502  GOL A C1  1 
HETATM 5054 O O1  . GOL F 3 .   ? -11.673 17.492 -33.708 0.85 50.36 ? 502  GOL A O1  1 
HETATM 5055 C C2  . GOL F 3 .   ? -11.308 19.860 -33.274 0.85 27.66 ? 502  GOL A C2  1 
HETATM 5056 O O2  . GOL F 3 .   ? -12.167 20.970 -33.089 0.85 44.02 ? 502  GOL A O2  1 
HETATM 5057 C C3  . GOL F 3 .   ? -10.070 20.015 -32.414 0.85 15.12 ? 502  GOL A C3  1 
HETATM 5058 O O3  . GOL F 3 .   ? -10.102 21.280 -31.798 0.85 46.79 ? 502  GOL A O3  1 
HETATM 5059 C C1  . GOL G 3 .   ? -16.006 39.780 -41.902 1.00 48.23 ? 501  GOL B C1  1 
HETATM 5060 O O1  . GOL G 3 .   ? -16.628 39.604 -43.152 1.00 45.92 ? 501  GOL B O1  1 
HETATM 5061 C C2  . GOL G 3 .   ? -17.073 40.207 -40.920 1.00 42.31 ? 501  GOL B C2  1 
HETATM 5062 O O2  . GOL G 3 .   ? -16.522 40.515 -39.656 1.00 47.59 ? 501  GOL B O2  1 
HETATM 5063 C C3  . GOL G 3 .   ? -17.883 41.343 -41.508 1.00 36.41 ? 501  GOL B C3  1 
HETATM 5064 O O3  . GOL G 3 .   ? -19.245 41.072 -41.232 1.00 30.39 ? 501  GOL B O3  1 
HETATM 5065 C C1  . GOL H 3 .   ? -29.013 22.427 -12.188 0.78 39.57 ? 502  GOL B C1  1 
HETATM 5066 O O1  . GOL H 3 .   ? -30.220 21.764 -12.429 0.78 21.50 ? 502  GOL B O1  1 
HETATM 5067 C C2  . GOL H 3 .   ? -28.000 21.325 -12.196 0.78 33.51 ? 502  GOL B C2  1 
HETATM 5068 O O2  . GOL H 3 .   ? -26.972 21.628 -11.285 0.78 53.91 ? 502  GOL B O2  1 
HETATM 5069 C C3  . GOL H 3 .   ? -28.748 20.058 -11.849 0.78 22.93 ? 502  GOL B C3  1 
HETATM 5070 O O3  . GOL H 3 .   ? -28.012 18.966 -12.335 0.78 40.50 ? 502  GOL B O3  1 
HETATM 5071 S S   . SO4 I 4 .   ? -41.108 1.641  -37.927 0.73 29.72 ? 503  SO4 B S   1 
HETATM 5072 O O1  . SO4 I 4 .   ? -39.955 1.231  -38.793 0.73 30.04 ? 503  SO4 B O1  1 
HETATM 5073 O O2  . SO4 I 4 .   ? -42.392 1.371  -38.643 0.73 43.64 ? 503  SO4 B O2  1 
HETATM 5074 O O3  . SO4 I 4 .   ? -41.052 0.867  -36.644 0.73 33.53 ? 503  SO4 B O3  1 
HETATM 5075 O O4  . SO4 I 4 .   ? -41.020 3.110  -37.633 0.73 30.51 ? 503  SO4 B O4  1 
HETATM 5076 S S   . SO4 J 4 .   ? -12.658 27.842 -34.882 0.65 39.17 ? 504  SO4 B S   1 
HETATM 5077 O O1  . SO4 J 4 .   ? -11.777 26.949 -35.705 0.65 50.49 ? 504  SO4 B O1  1 
HETATM 5078 O O2  . SO4 J 4 .   ? -13.992 27.225 -34.705 0.65 28.62 ? 504  SO4 B O2  1 
HETATM 5079 O O3  . SO4 J 4 .   ? -12.040 28.035 -33.516 0.65 34.34 ? 504  SO4 B O3  1 
HETATM 5080 O O4  . SO4 J 4 .   ? -12.807 29.171 -35.534 0.65 32.26 ? 504  SO4 B O4  1 
HETATM 5081 O O   . HOH K 5 .   ? -23.738 22.498 -9.901  1.00 36.13 ? 601  HOH A O   1 
HETATM 5082 O O   . HOH K 5 .   ? -17.395 43.494 -5.571  1.00 43.74 ? 602  HOH A O   1 
HETATM 5083 O O   . HOH K 5 .   ? 8.209   6.602  -16.611 1.00 49.84 ? 603  HOH A O   1 
HETATM 5084 O O   . HOH K 5 .   ? -0.871  3.066  -24.024 1.00 36.91 ? 604  HOH A O   1 
HETATM 5085 O O   . HOH K 5 .   ? -16.519 12.683 -27.748 1.00 34.45 ? 605  HOH A O   1 
HETATM 5086 O O   . HOH K 5 .   ? -14.169 27.848 -29.198 1.00 24.99 ? 606  HOH A O   1 
HETATM 5087 O O   . HOH K 5 .   ? -19.630 43.873 -1.968  1.00 40.27 ? 607  HOH A O   1 
HETATM 5088 O O   . HOH K 5 .   ? -16.700 15.695 10.813  1.00 43.61 ? 608  HOH A O   1 
HETATM 5089 O O   . HOH K 5 .   ? -8.387  22.679 -32.292 1.00 30.84 ? 609  HOH A O   1 
HETATM 5090 O O   . HOH K 5 .   ? -10.178 39.771 6.984   1.00 43.91 ? 610  HOH A O   1 
HETATM 5091 O O   . HOH K 5 .   ? 12.232  23.789 -12.007 1.00 36.10 ? 611  HOH A O   1 
HETATM 5092 O O   . HOH K 5 .   ? 6.103   13.340 -30.901 1.00 28.65 ? 612  HOH A O   1 
HETATM 5093 O O   . HOH K 5 .   ? 2.387   2.939  -28.579 1.00 43.40 ? 613  HOH A O   1 
HETATM 5094 O O   . HOH K 5 .   ? -9.819  42.551 -19.967 1.00 25.32 ? 614  HOH A O   1 
HETATM 5095 O O   . HOH K 5 .   ? -25.311 23.376 -12.113 1.00 48.28 ? 615  HOH A O   1 
HETATM 5096 O O   . HOH K 5 .   ? 17.344  18.203 -15.682 1.00 52.73 ? 616  HOH A O   1 
HETATM 5097 O O   . HOH K 5 .   ? 3.724   28.470 -31.036 1.00 38.00 ? 617  HOH A O   1 
HETATM 5098 O O   . HOH K 5 .   ? -18.657 39.888 0.954   1.00 29.22 ? 618  HOH A O   1 
HETATM 5099 O O   . HOH K 5 .   ? -14.442 19.919 -32.862 1.00 37.42 ? 619  HOH A O   1 
HETATM 5100 O O   . HOH K 5 .   ? -15.585 18.803 11.361  1.00 29.12 ? 620  HOH A O   1 
HETATM 5101 O O   . HOH K 5 .   ? 5.017   0.791  -8.522  1.00 40.25 ? 621  HOH A O   1 
HETATM 5102 O O   . HOH K 5 .   ? -11.343 6.634  5.031   1.00 38.00 ? 622  HOH A O   1 
HETATM 5103 O O   . HOH K 5 .   ? -1.141  8.671  -5.926  1.00 23.39 ? 623  HOH A O   1 
HETATM 5104 O O   . HOH K 5 .   ? -26.189 19.977 2.030   1.00 45.86 ? 624  HOH A O   1 
HETATM 5105 O O   . HOH K 5 .   ? -20.794 40.347 -15.075 1.00 36.55 ? 625  HOH A O   1 
HETATM 5106 O O   . HOH K 5 .   ? -27.750 27.983 -4.091  1.00 28.10 ? 626  HOH A O   1 
HETATM 5107 O O   . HOH K 5 .   ? -29.580 23.120 -7.491  1.00 40.83 ? 627  HOH A O   1 
HETATM 5108 O O   . HOH K 5 .   ? -24.194 38.092 -18.951 1.00 47.20 ? 628  HOH A O   1 
HETATM 5109 O O   . HOH K 5 .   ? -15.611 18.274 -31.285 1.00 35.48 ? 629  HOH A O   1 
HETATM 5110 O O   . HOH K 5 .   ? -23.543 37.610 -1.214  1.00 37.41 ? 630  HOH A O   1 
HETATM 5111 O O   . HOH K 5 .   ? -6.689  15.461 -36.173 1.00 24.18 ? 631  HOH A O   1 
HETATM 5112 O O   . HOH K 5 .   ? -21.805 23.615 -6.080  1.00 21.88 ? 632  HOH A O   1 
HETATM 5113 O O   . HOH K 5 .   ? 5.912   6.084  1.403   1.00 35.05 ? 633  HOH A O   1 
HETATM 5114 O O   . HOH K 5 .   ? -0.588  2.798  0.086   1.00 41.72 ? 634  HOH A O   1 
HETATM 5115 O O   . HOH K 5 .   ? -23.880 19.127 -4.699  1.00 41.84 ? 635  HOH A O   1 
HETATM 5116 O O   . HOH K 5 .   ? 7.570   28.684 -18.935 1.00 29.40 ? 636  HOH A O   1 
HETATM 5117 O O   . HOH K 5 .   ? 6.877   29.554 -4.510  1.00 24.29 ? 637  HOH A O   1 
HETATM 5118 O O   . HOH K 5 .   ? -6.212  14.837 9.431   1.00 40.35 ? 638  HOH A O   1 
HETATM 5119 O O   . HOH K 5 .   ? -13.533 10.763 -17.327 1.00 24.05 ? 639  HOH A O   1 
HETATM 5120 O O   . HOH K 5 .   ? -4.989  38.742 -27.408 1.00 31.13 ? 640  HOH A O   1 
HETATM 5121 O O   . HOH K 5 .   ? 2.868   42.708 -10.842 1.00 34.00 ? 641  HOH A O   1 
HETATM 5122 O O   . HOH K 5 .   ? -16.984 39.243 2.787   1.00 30.96 ? 642  HOH A O   1 
HETATM 5123 O O   . HOH K 5 .   ? -8.841  10.234 -36.927 1.00 34.37 ? 643  HOH A O   1 
HETATM 5124 O O   . HOH K 5 .   ? -8.230  18.864 -36.324 1.00 38.17 ? 644  HOH A O   1 
HETATM 5125 O O   . HOH K 5 .   ? -22.727 37.015 -20.115 1.00 35.47 ? 645  HOH A O   1 
HETATM 5126 O O   . HOH K 5 .   ? 9.513   16.747 6.685   1.00 40.92 ? 646  HOH A O   1 
HETATM 5127 O O   . HOH K 5 .   ? 11.220  25.435 -25.317 1.00 24.18 ? 647  HOH A O   1 
HETATM 5128 O O   . HOH K 5 .   ? -11.425 27.949 -22.851 1.00 17.43 ? 648  HOH A O   1 
HETATM 5129 O O   . HOH K 5 .   ? -14.264 4.101  -8.781  1.00 44.75 ? 649  HOH A O   1 
HETATM 5130 O O   . HOH K 5 .   ? -1.261  32.525 8.078   1.00 27.18 ? 650  HOH A O   1 
HETATM 5131 O O   . HOH K 5 .   ? -17.760 16.602 4.453   1.00 23.76 ? 651  HOH A O   1 
HETATM 5132 O O   . HOH K 5 .   ? -13.381 41.375 -4.457  1.00 43.30 ? 652  HOH A O   1 
HETATM 5133 O O   . HOH K 5 .   ? 14.804  14.248 -14.824 1.00 53.57 ? 653  HOH A O   1 
HETATM 5134 O O   . HOH K 5 .   ? -10.287 43.439 -4.189  1.00 33.32 ? 654  HOH A O   1 
HETATM 5135 O O   . HOH K 5 .   ? 12.394  15.248 -12.140 1.00 51.83 ? 655  HOH A O   1 
HETATM 5136 O O   . HOH K 5 .   ? -4.951  -1.232 -22.990 1.00 40.00 ? 656  HOH A O   1 
HETATM 5137 O O   . HOH K 5 .   ? -4.237  3.831  -3.609  1.00 27.45 ? 657  HOH A O   1 
HETATM 5138 O O   . HOH K 5 .   ? -13.567 26.283 11.956  1.00 35.64 ? 658  HOH A O   1 
HETATM 5139 O O   . HOH K 5 .   ? -24.294 32.392 -5.646  1.00 28.92 ? 659  HOH A O   1 
HETATM 5140 O O   . HOH K 5 .   ? -16.051 13.552 11.220  1.00 50.29 ? 660  HOH A O   1 
HETATM 5141 O O   . HOH K 5 .   ? -5.051  45.105 -15.866 1.00 29.23 ? 661  HOH A O   1 
HETATM 5142 O O   . HOH K 5 .   ? -14.405 32.312 4.635   1.00 20.76 ? 662  HOH A O   1 
HETATM 5143 O O   . HOH K 5 .   ? -23.739 10.174 3.016   1.00 38.46 ? 663  HOH A O   1 
HETATM 5144 O O   . HOH K 5 .   ? 7.565   30.128 -14.309 1.00 40.21 ? 664  HOH A O   1 
HETATM 5145 O O   . HOH K 5 .   ? 5.228   27.812 -31.475 1.00 36.51 ? 665  HOH A O   1 
HETATM 5146 O O   . HOH K 5 .   ? -9.042  43.654 -15.358 1.00 40.72 ? 666  HOH A O   1 
HETATM 5147 O O   . HOH K 5 .   ? 13.031  14.328 -22.880 1.00 39.98 ? 667  HOH A O   1 
HETATM 5148 O O   . HOH K 5 .   ? -9.192  9.943  -24.608 1.00 20.09 ? 668  HOH A O   1 
HETATM 5149 O O   . HOH K 5 .   ? 5.808   4.599  -1.350  1.00 39.18 ? 669  HOH A O   1 
HETATM 5150 O O   . HOH K 5 .   ? -23.698 21.671 3.461   1.00 26.96 ? 670  HOH A O   1 
HETATM 5151 O O   . HOH K 5 .   ? 9.292   9.380  -2.962  1.00 42.39 ? 671  HOH A O   1 
HETATM 5152 O O   . HOH K 5 .   ? -13.299 3.980  -26.330 1.00 54.22 ? 672  HOH A O   1 
HETATM 5153 O O   . HOH K 5 .   ? -3.815  41.803 -5.988  1.00 24.56 ? 673  HOH A O   1 
HETATM 5154 O O   . HOH K 5 .   ? -1.451  41.815 -20.334 1.00 33.58 ? 674  HOH A O   1 
HETATM 5155 O O   . HOH K 5 .   ? 2.755   2.788  -4.471  1.00 38.61 ? 675  HOH A O   1 
HETATM 5156 O O   . HOH K 5 .   ? -7.018  2.872  -9.869  1.00 25.28 ? 676  HOH A O   1 
HETATM 5157 O O   . HOH K 5 .   ? -7.638  44.345 -21.544 1.00 38.86 ? 677  HOH A O   1 
HETATM 5158 O O   . HOH K 5 .   ? -8.565  42.126 -13.121 1.00 30.66 ? 678  HOH A O   1 
HETATM 5159 O O   . HOH K 5 .   ? 3.266   40.317 -15.619 1.00 47.49 ? 679  HOH A O   1 
HETATM 5160 O O   . HOH K 5 .   ? -7.525  4.176  -7.372  1.00 24.14 ? 680  HOH A O   1 
HETATM 5161 O O   . HOH K 5 .   ? -10.759 41.067 -24.832 1.00 26.97 ? 681  HOH A O   1 
HETATM 5162 O O   . HOH K 5 .   ? -17.470 32.656 -22.229 1.00 21.35 ? 682  HOH A O   1 
HETATM 5163 O O   . HOH K 5 .   ? -16.289 16.858 8.268   1.00 24.53 ? 683  HOH A O   1 
HETATM 5164 O O   . HOH K 5 .   ? -17.511 19.754 -7.146  1.00 31.69 ? 684  HOH A O   1 
HETATM 5165 O O   . HOH K 5 .   ? -6.505  7.651  1.338   1.00 27.69 ? 685  HOH A O   1 
HETATM 5166 O O   . HOH K 5 .   ? -13.565 23.690 -23.662 1.00 35.57 ? 686  HOH A O   1 
HETATM 5167 O O   . HOH K 5 .   ? -3.464  12.690 2.263   1.00 35.38 ? 687  HOH A O   1 
HETATM 5168 O O   . HOH K 5 .   ? -12.200 14.758 5.497   1.00 20.39 ? 688  HOH A O   1 
HETATM 5169 O O   . HOH K 5 .   ? -2.806  1.736  -4.258  1.00 31.22 ? 689  HOH A O   1 
HETATM 5170 O O   . HOH K 5 .   ? -20.089 32.947 -21.291 1.00 38.68 ? 690  HOH A O   1 
HETATM 5171 O O   . HOH K 5 .   ? -6.746  -1.218 -12.997 1.00 52.00 ? 691  HOH A O   1 
HETATM 5172 O O   . HOH K 5 .   ? 11.297  13.327 -7.717  1.00 44.23 ? 692  HOH A O   1 
HETATM 5173 O O   . HOH K 5 .   ? 8.699   11.679 -28.412 1.00 40.83 ? 693  HOH A O   1 
HETATM 5174 O O   . HOH K 5 .   ? 8.550   28.428 -6.248  1.00 29.77 ? 694  HOH A O   1 
HETATM 5175 O O   . HOH K 5 .   ? 11.362  16.813 -4.022  1.00 37.84 ? 695  HOH A O   1 
HETATM 5176 O O   . HOH K 5 .   ? 9.364   17.938 -16.760 1.00 26.16 ? 696  HOH A O   1 
HETATM 5177 O O   . HOH K 5 .   ? 11.968  24.275 -31.051 1.00 37.75 ? 697  HOH A O   1 
HETATM 5178 O O   . HOH K 5 .   ? -8.903  36.018 -28.577 1.00 28.24 ? 698  HOH A O   1 
HETATM 5179 O O   . HOH K 5 .   ? -0.204  18.332 8.694   1.00 31.04 ? 699  HOH A O   1 
HETATM 5180 O O   . HOH K 5 .   ? 6.401   39.595 -15.904 1.00 44.83 ? 700  HOH A O   1 
HETATM 5181 O O   . HOH K 5 .   ? 10.257  16.206 -26.366 1.00 32.11 ? 701  HOH A O   1 
HETATM 5182 O O   . HOH K 5 .   ? -17.557 19.172 5.342   1.00 23.96 ? 702  HOH A O   1 
HETATM 5183 O O   . HOH K 5 .   ? -11.620 -0.092 -17.495 1.00 48.36 ? 703  HOH A O   1 
HETATM 5184 O O   . HOH K 5 .   ? 9.880   23.430 -10.548 1.00 25.03 ? 704  HOH A O   1 
HETATM 5185 O O   . HOH K 5 .   ? 9.562   20.091 -6.719  1.00 39.25 ? 705  HOH A O   1 
HETATM 5186 O O   . HOH K 5 .   ? -27.679 22.932 -3.818  1.00 25.59 ? 706  HOH A O   1 
HETATM 5187 O O   . HOH K 5 .   ? -4.731  3.845  -0.821  1.00 30.67 ? 707  HOH A O   1 
HETATM 5188 O O   . HOH K 5 .   ? -4.029  41.327 -26.513 1.00 23.07 ? 708  HOH A O   1 
HETATM 5189 O O   . HOH K 5 .   ? -17.807 29.979 -22.667 1.00 19.70 ? 709  HOH A O   1 
HETATM 5190 O O   . HOH K 5 .   ? 1.903   37.423 -13.286 1.00 19.92 ? 710  HOH A O   1 
HETATM 5191 O O   . HOH K 5 .   ? -2.112  41.564 -22.971 1.00 24.23 ? 711  HOH A O   1 
HETATM 5192 O O   . HOH K 5 .   ? -1.199  15.340 -30.248 1.00 17.28 ? 712  HOH A O   1 
HETATM 5193 O O   . HOH K 5 .   ? 0.720   15.056 6.368   1.00 26.08 ? 713  HOH A O   1 
HETATM 5194 O O   . HOH K 5 .   ? 5.368   39.350 -19.871 1.00 36.58 ? 714  HOH A O   1 
HETATM 5195 O O   . HOH K 5 .   ? -18.613 22.382 10.195  1.00 33.68 ? 715  HOH A O   1 
HETATM 5196 O O   . HOH K 5 .   ? 8.409   16.622 -12.662 1.00 37.48 ? 716  HOH A O   1 
HETATM 5197 O O   . HOH K 5 .   ? -18.517 40.686 -11.950 1.00 38.13 ? 717  HOH A O   1 
HETATM 5198 O O   . HOH K 5 .   ? -25.546 30.422 -16.665 1.00 26.92 ? 718  HOH A O   1 
HETATM 5199 O O   . HOH K 5 .   ? -8.917  12.543 -23.421 1.00 20.33 ? 719  HOH A O   1 
HETATM 5200 O O   . HOH K 5 .   ? 13.167  11.248 -13.158 1.00 47.52 ? 720  HOH A O   1 
HETATM 5201 O O   . HOH K 5 .   ? 3.816   34.418 -13.848 1.00 27.42 ? 721  HOH A O   1 
HETATM 5202 O O   . HOH K 5 .   ? -16.061 33.033 10.661  1.00 48.21 ? 722  HOH A O   1 
HETATM 5203 O O   . HOH K 5 .   ? -21.583 12.391 -8.256  1.00 54.74 ? 723  HOH A O   1 
HETATM 5204 O O   . HOH K 5 .   ? -21.051 20.916 3.720   1.00 31.62 ? 724  HOH A O   1 
HETATM 5205 O O   . HOH K 5 .   ? 11.361  21.926 -3.883  1.00 44.18 ? 725  HOH A O   1 
HETATM 5206 O O   . HOH K 5 .   ? -22.455 34.805 1.170   1.00 36.18 ? 726  HOH A O   1 
HETATM 5207 O O   . HOH K 5 .   ? -5.254  35.873 8.080   1.00 39.53 ? 727  HOH A O   1 
HETATM 5208 O O   . HOH K 5 .   ? -16.357 11.531 -25.273 1.00 25.92 ? 728  HOH A O   1 
HETATM 5209 O O   . HOH K 5 .   ? -19.237 40.143 -20.108 1.00 36.64 ? 729  HOH A O   1 
HETATM 5210 O O   . HOH K 5 .   ? 12.652  15.644 -18.058 1.00 36.45 ? 730  HOH A O   1 
HETATM 5211 O O   . HOH K 5 .   ? -14.589 15.295 6.957   1.00 26.83 ? 731  HOH A O   1 
HETATM 5212 O O   . HOH K 5 .   ? 13.214  22.025 -21.420 1.00 23.32 ? 732  HOH A O   1 
HETATM 5213 O O   . HOH K 5 .   ? 4.273   7.849  -28.258 1.00 32.86 ? 733  HOH A O   1 
HETATM 5214 O O   . HOH K 5 .   ? -26.119 28.497 1.229   1.00 37.32 ? 734  HOH A O   1 
HETATM 5215 O O   . HOH K 5 .   ? -5.390  21.899 -36.431 1.00 23.83 ? 735  HOH A O   1 
HETATM 5216 O O   . HOH K 5 .   ? -7.424  28.665 -28.111 1.00 19.20 ? 736  HOH A O   1 
HETATM 5217 O O   . HOH K 5 .   ? 10.134  18.385 -28.174 1.00 22.09 ? 737  HOH A O   1 
HETATM 5218 O O   . HOH K 5 .   ? 4.531   1.954  -14.807 1.00 35.07 ? 738  HOH A O   1 
HETATM 5219 O O   . HOH K 5 .   ? 1.375   24.044 4.666   1.00 24.24 ? 739  HOH A O   1 
HETATM 5220 O O   . HOH K 5 .   ? -21.377 40.919 -19.612 1.00 38.36 ? 740  HOH A O   1 
HETATM 5221 O O   . HOH K 5 .   ? -12.812 41.471 -8.885  1.00 25.02 ? 741  HOH A O   1 
HETATM 5222 O O   . HOH K 5 .   ? -9.838  8.569  -6.178  1.00 24.80 ? 742  HOH A O   1 
HETATM 5223 O O   . HOH K 5 .   ? 1.150   34.658 -16.711 1.00 17.33 ? 743  HOH A O   1 
HETATM 5224 O O   . HOH K 5 .   ? 4.559   44.376 -6.469  1.00 35.84 ? 744  HOH A O   1 
HETATM 5225 O O   . HOH K 5 .   ? -13.055 37.525 -23.352 1.00 17.82 ? 745  HOH A O   1 
HETATM 5226 O O   . HOH K 5 .   ? -18.999 27.876 7.601   1.00 23.62 ? 746  HOH A O   1 
HETATM 5227 O O   . HOH K 5 .   ? 11.100  24.901 -6.004  1.00 39.99 ? 747  HOH A O   1 
HETATM 5228 O O   . HOH K 5 .   ? -16.227 9.397  8.487   1.00 40.98 ? 748  HOH A O   1 
HETATM 5229 O O   . HOH K 5 .   ? -5.422  26.183 -28.610 1.00 19.22 ? 749  HOH A O   1 
HETATM 5230 O O   . HOH K 5 .   ? 8.777   28.215 -29.635 1.00 46.38 ? 750  HOH A O   1 
HETATM 5231 O O   . HOH K 5 .   ? 3.845   28.096 -5.341  1.00 18.24 ? 751  HOH A O   1 
HETATM 5232 O O   . HOH K 5 .   ? -8.787  6.954  -33.006 1.00 29.39 ? 752  HOH A O   1 
HETATM 5233 O O   . HOH K 5 .   ? -9.980  28.984 -29.538 1.00 26.57 ? 753  HOH A O   1 
HETATM 5234 O O   . HOH K 5 .   ? -8.302  30.342 7.858   1.00 21.09 ? 754  HOH A O   1 
HETATM 5235 O O   . HOH K 5 .   ? 6.650   36.201 -4.893  1.00 27.80 ? 755  HOH A O   1 
HETATM 5236 O O   . HOH K 5 .   ? 5.761   36.118 -24.637 1.00 29.15 ? 756  HOH A O   1 
HETATM 5237 O O   . HOH K 5 .   ? -21.050 22.456 -13.017 1.00 20.49 ? 757  HOH A O   1 
HETATM 5238 O O   . HOH K 5 .   ? 5.332   34.609 -21.976 1.00 29.25 ? 758  HOH A O   1 
HETATM 5239 O O   . HOH K 5 .   ? -1.844  38.540 -16.238 1.00 17.50 ? 759  HOH A O   1 
HETATM 5240 O O   . HOH K 5 .   ? 0.552   41.008 1.153   1.00 35.05 ? 760  HOH A O   1 
HETATM 5241 O O   . HOH K 5 .   ? -3.881  32.549 -30.894 1.00 27.35 ? 761  HOH A O   1 
HETATM 5242 O O   . HOH K 5 .   ? 2.114   26.365 -33.645 1.00 26.28 ? 762  HOH A O   1 
HETATM 5243 O O   . HOH K 5 .   ? -25.881 33.444 -8.977  1.00 30.74 ? 763  HOH A O   1 
HETATM 5244 O O   . HOH K 5 .   ? -9.426  10.155 3.590   1.00 26.75 ? 764  HOH A O   1 
HETATM 5245 O O   . HOH K 5 .   ? -8.332  43.872 -26.577 1.00 35.32 ? 765  HOH A O   1 
HETATM 5246 O O   . HOH K 5 .   ? -25.024 2.673  3.262   1.00 52.67 ? 766  HOH A O   1 
HETATM 5247 O O   . HOH K 5 .   ? -2.075  -1.044 -6.197  1.00 44.80 ? 767  HOH A O   1 
HETATM 5248 O O   . HOH K 5 .   ? -23.856 23.302 -18.741 1.00 27.40 ? 768  HOH A O   1 
HETATM 5249 O O   . HOH K 5 .   ? -7.769  6.261  -29.491 1.00 23.64 ? 769  HOH A O   1 
HETATM 5250 O O   . HOH K 5 .   ? -10.694 19.525 -23.121 1.00 22.37 ? 770  HOH A O   1 
HETATM 5251 O O   . HOH K 5 .   ? -25.524 26.189 -11.660 1.00 28.94 ? 771  HOH A O   1 
HETATM 5252 O O   . HOH K 5 .   ? -8.884  22.007 10.880  1.00 20.29 ? 772  HOH A O   1 
HETATM 5253 O O   . HOH K 5 .   ? -2.322  42.481 -16.574 1.00 28.29 ? 773  HOH A O   1 
HETATM 5254 O O   . HOH K 5 .   ? -24.072 30.422 -3.876  1.00 28.73 ? 774  HOH A O   1 
HETATM 5255 O O   . HOH K 5 .   ? 1.790   12.779 -32.541 1.00 26.24 ? 775  HOH A O   1 
HETATM 5256 O O   . HOH K 5 .   ? -7.542  1.784  -13.809 1.00 27.99 ? 776  HOH A O   1 
HETATM 5257 O O   . HOH K 5 .   ? -4.990  6.116  -19.504 1.00 24.15 ? 777  HOH A O   1 
HETATM 5258 O O   . HOH K 5 .   ? 2.474   0.672  -25.700 1.00 37.66 ? 778  HOH A O   1 
HETATM 5259 O O   . HOH K 5 .   ? -7.693  3.623  -21.010 1.00 23.04 ? 779  HOH A O   1 
HETATM 5260 O O   . HOH K 5 .   ? -21.068 15.378 -26.943 1.00 39.31 ? 780  HOH A O   1 
HETATM 5261 O O   . HOH K 5 .   ? -4.017  8.750  -3.829  1.00 22.57 ? 781  HOH A O   1 
HETATM 5262 O O   . HOH K 5 .   ? 4.822   17.774 -31.588 1.00 19.82 ? 782  HOH A O   1 
HETATM 5263 O O   . HOH K 5 .   ? -15.650 19.755 -23.642 1.00 37.90 ? 783  HOH A O   1 
HETATM 5264 O O   . HOH K 5 .   ? 3.290   40.630 -28.324 1.00 29.29 ? 784  HOH A O   1 
HETATM 5265 O O   . HOH K 5 .   ? -10.964 35.466 5.840   1.00 24.96 ? 785  HOH A O   1 
HETATM 5266 O O   . HOH K 5 .   ? -20.520 34.124 7.208   1.00 36.32 ? 786  HOH A O   1 
HETATM 5267 O O   . HOH K 5 .   ? -17.120 17.182 -7.577  1.00 29.70 ? 787  HOH A O   1 
HETATM 5268 O O   . HOH K 5 .   ? -13.441 19.036 -20.533 1.00 30.32 ? 788  HOH A O   1 
HETATM 5269 O O   . HOH K 5 .   ? -8.283  25.405 -31.131 1.00 29.52 ? 789  HOH A O   1 
HETATM 5270 O O   . HOH K 5 .   ? 7.275   23.915 2.144   1.00 25.53 ? 790  HOH A O   1 
HETATM 5271 O O   . HOH K 5 .   ? 1.306   11.411 -35.105 1.00 26.53 ? 791  HOH A O   1 
HETATM 5272 O O   . HOH K 5 .   ? -9.045  40.201 1.314   1.00 18.15 ? 792  HOH A O   1 
HETATM 5273 O O   . HOH K 5 .   ? -11.905 21.555 -20.846 1.00 21.36 ? 793  HOH A O   1 
HETATM 5274 O O   . HOH K 5 .   ? 0.205   36.184 -32.226 1.00 43.72 ? 794  HOH A O   1 
HETATM 5275 O O   . HOH K 5 .   ? -14.945 33.726 8.443   1.00 30.95 ? 795  HOH A O   1 
HETATM 5276 O O   . HOH K 5 .   ? -0.679  34.957 7.212   1.00 32.43 ? 796  HOH A O   1 
HETATM 5277 O O   . HOH K 5 .   ? -22.079 39.572 -10.388 1.00 35.30 ? 797  HOH A O   1 
HETATM 5278 O O   . HOH K 5 .   ? -20.410 36.472 -21.116 1.00 24.44 ? 798  HOH A O   1 
HETATM 5279 O O   . HOH K 5 .   ? -3.159  11.688 -37.318 1.00 34.46 ? 799  HOH A O   1 
HETATM 5280 O O   . HOH K 5 .   ? 8.570   24.827 -18.406 1.00 17.48 ? 800  HOH A O   1 
HETATM 5281 O O   . HOH K 5 .   ? -20.092 23.176 -8.146  1.00 18.56 ? 801  HOH A O   1 
HETATM 5282 O O   . HOH K 5 .   ? -0.325  40.969 -14.846 1.00 52.53 ? 802  HOH A O   1 
HETATM 5283 O O   . HOH K 5 .   ? -8.781  14.981 -3.616  1.00 19.21 ? 803  HOH A O   1 
HETATM 5284 O O   . HOH K 5 .   ? -9.527  2.120  -6.269  1.00 28.80 ? 804  HOH A O   1 
HETATM 5285 O O   . HOH K 5 .   ? -17.125 36.716 7.117   1.00 40.18 ? 805  HOH A O   1 
HETATM 5286 O O   . HOH K 5 .   ? 9.179   25.927 -9.720  1.00 21.40 ? 806  HOH A O   1 
HETATM 5287 O O   . HOH K 5 .   ? 1.332   28.397 6.411   1.00 29.14 ? 807  HOH A O   1 
HETATM 5288 O O   . HOH K 5 .   ? -18.778 12.479 -24.307 1.00 32.69 ? 808  HOH A O   1 
HETATM 5289 O O   . HOH K 5 .   ? 7.939   34.593 -25.333 1.00 37.55 ? 809  HOH A O   1 
HETATM 5290 O O   . HOH K 5 .   ? -18.668 27.838 -21.015 1.00 16.63 ? 810  HOH A O   1 
HETATM 5291 O O   . HOH K 5 .   ? -17.554 20.053 -26.991 1.00 26.71 ? 811  HOH A O   1 
HETATM 5292 O O   . HOH K 5 .   ? -17.175 12.777 7.490   1.00 32.98 ? 812  HOH A O   1 
HETATM 5293 O O   . HOH K 5 .   ? -15.774 18.583 -17.014 1.00 42.08 ? 813  HOH A O   1 
HETATM 5294 O O   . HOH K 5 .   ? 0.510   16.845 8.426   1.00 29.44 ? 814  HOH A O   1 
HETATM 5295 O O   . HOH K 5 .   ? 4.345   33.746 1.241   1.00 22.29 ? 815  HOH A O   1 
HETATM 5296 O O   . HOH K 5 .   ? -3.635  1.118  -8.126  1.00 37.84 ? 816  HOH A O   1 
HETATM 5297 O O   . HOH K 5 .   ? -11.891 25.279 -30.906 1.00 41.00 ? 817  HOH A O   1 
HETATM 5298 O O   . HOH K 5 .   ? -11.135 3.298  1.220   1.00 37.72 ? 818  HOH A O   1 
HETATM 5299 O O   . HOH K 5 .   ? -15.852 9.982  -28.623 1.00 41.62 ? 819  HOH A O   1 
HETATM 5300 O O   . HOH K 5 .   ? -14.527 41.741 -19.325 1.00 21.68 ? 820  HOH A O   1 
HETATM 5301 O O   . HOH K 5 .   ? -3.883  0.275  -29.403 1.00 35.50 ? 821  HOH A O   1 
HETATM 5302 O O   . HOH K 5 .   ? 3.474   1.247  -21.905 1.00 30.76 ? 822  HOH A O   1 
HETATM 5303 O O   . HOH K 5 .   ? 8.676   27.351 -16.908 1.00 25.51 ? 823  HOH A O   1 
HETATM 5304 O O   . HOH K 5 .   ? -1.516  0.591  -26.729 1.00 29.23 ? 824  HOH A O   1 
HETATM 5305 O O   . HOH K 5 .   ? -11.250 42.429 -12.056 1.00 31.04 ? 825  HOH A O   1 
HETATM 5306 O O   . HOH K 5 .   ? -24.064 38.973 -5.429  1.00 48.19 ? 826  HOH A O   1 
HETATM 5307 O O   . HOH K 5 .   ? -5.559  25.300 -31.458 1.00 21.50 ? 827  HOH A O   1 
HETATM 5308 O O   . HOH K 5 .   ? -14.136 4.840  -23.349 1.00 28.92 ? 828  HOH A O   1 
HETATM 5309 O O   . HOH K 5 .   ? 12.677  21.192 -24.053 1.00 26.94 ? 829  HOH A O   1 
HETATM 5310 O O   . HOH K 5 .   ? 9.750   29.994 -8.314  1.00 34.02 ? 830  HOH A O   1 
HETATM 5311 O O   . HOH K 5 .   ? -21.727 32.075 0.380   1.00 22.73 ? 831  HOH A O   1 
HETATM 5312 O O   . HOH K 5 .   ? 12.060  28.295 -21.584 1.00 48.83 ? 832  HOH A O   1 
HETATM 5313 O O   . HOH K 5 .   ? 10.071  21.019 1.398   1.00 32.99 ? 833  HOH A O   1 
HETATM 5314 O O   . HOH K 5 .   ? 7.636   8.133  -24.884 1.00 34.11 ? 834  HOH A O   1 
HETATM 5315 O O   . HOH K 5 .   ? 10.014  32.327 -28.143 1.00 40.98 ? 835  HOH A O   1 
HETATM 5316 O O   . HOH K 5 .   ? 7.092   36.666 -1.101  1.00 29.64 ? 836  HOH A O   1 
HETATM 5317 O O   . HOH K 5 .   ? 11.100  24.264 -18.837 1.00 24.15 ? 837  HOH A O   1 
HETATM 5318 O O   . HOH K 5 .   ? -3.792  43.622 -8.070  1.00 27.95 ? 838  HOH A O   1 
HETATM 5319 O O   . HOH K 5 .   ? -13.932 43.981 -15.004 1.00 30.26 ? 839  HOH A O   1 
HETATM 5320 O O   . HOH K 5 .   ? 10.067  15.180 -7.830  1.00 39.56 ? 840  HOH A O   1 
HETATM 5321 O O   . HOH K 5 .   ? -21.022 23.717 -21.550 1.00 25.76 ? 841  HOH A O   1 
HETATM 5322 O O   . HOH K 5 .   ? 6.731   41.344 -7.853  1.00 47.46 ? 842  HOH A O   1 
HETATM 5323 O O   . HOH K 5 .   ? -20.006 30.960 -20.567 1.00 27.27 ? 843  HOH A O   1 
HETATM 5324 O O   . HOH K 5 .   ? -5.310  10.180 3.462   1.00 43.20 ? 844  HOH A O   1 
HETATM 5325 O O   . HOH K 5 .   ? -16.856 6.087  6.472   1.00 39.58 ? 845  HOH A O   1 
HETATM 5326 O O   . HOH K 5 .   ? -11.926 35.760 -26.308 1.00 17.49 ? 846  HOH A O   1 
HETATM 5327 O O   . HOH K 5 .   ? -25.878 27.986 -14.785 1.00 28.42 ? 847  HOH A O   1 
HETATM 5328 O O   . HOH K 5 .   ? 11.068  29.297 -19.891 1.00 50.51 ? 848  HOH A O   1 
HETATM 5329 O O   . HOH K 5 .   ? -21.435 34.382 -2.806  1.00 44.58 ? 849  HOH A O   1 
HETATM 5330 O O   . HOH K 5 .   ? -14.966 43.365 -4.030  1.00 34.39 ? 850  HOH A O   1 
HETATM 5331 O O   . HOH K 5 .   ? -1.104  0.501  -24.104 1.00 34.74 ? 851  HOH A O   1 
HETATM 5332 O O   . HOH K 5 .   ? 4.520   37.968 2.869   1.00 42.58 ? 852  HOH A O   1 
HETATM 5333 O O   . HOH K 5 .   ? 11.537  26.683 -29.763 1.00 31.50 ? 853  HOH A O   1 
HETATM 5334 O O   . HOH K 5 .   ? 8.164   32.905 -12.044 1.00 46.25 ? 854  HOH A O   1 
HETATM 5335 O O   . HOH K 5 .   ? 1.934   40.192 -19.593 1.00 26.49 ? 855  HOH A O   1 
HETATM 5336 O O   . HOH K 5 .   ? -19.168 19.222 7.702   1.00 36.26 ? 856  HOH A O   1 
HETATM 5337 O O   . HOH K 5 .   ? -13.350 10.332 -29.200 1.00 27.05 ? 857  HOH A O   1 
HETATM 5338 O O   . HOH K 5 .   ? -22.602 34.602 -4.925  1.00 31.47 ? 858  HOH A O   1 
HETATM 5339 O O   . HOH K 5 .   ? -19.129 30.149 10.220  1.00 35.22 ? 859  HOH A O   1 
HETATM 5340 O O   . HOH K 5 .   ? -8.903  2.045  -25.596 1.00 34.43 ? 860  HOH A O   1 
HETATM 5341 O O   . HOH K 5 .   ? 1.533   4.398  -30.733 1.00 38.09 ? 861  HOH A O   1 
HETATM 5342 O O   . HOH K 5 .   ? 6.387   21.630 3.742   1.00 27.87 ? 862  HOH A O   1 
HETATM 5343 O O   . HOH K 5 .   ? -22.152 20.564 -6.268  1.00 32.33 ? 863  HOH A O   1 
HETATM 5344 O O   . HOH K 5 .   ? -12.455 32.522 8.173   1.00 33.88 ? 864  HOH A O   1 
HETATM 5345 O O   . HOH K 5 .   ? -8.627  28.592 -32.124 1.00 41.92 ? 865  HOH A O   1 
HETATM 5346 O O   . HOH K 5 .   ? -24.444 14.601 4.161   1.00 33.31 ? 866  HOH A O   1 
HETATM 5347 O O   . HOH K 5 .   ? -13.612 40.402 0.786   1.00 27.81 ? 867  HOH A O   1 
HETATM 5348 O O   . HOH K 5 .   ? -14.693 39.634 5.050   1.00 43.33 ? 868  HOH A O   1 
HETATM 5349 O O   . HOH K 5 .   ? -4.680  8.864  -36.076 1.00 27.07 ? 869  HOH A O   1 
HETATM 5350 O O   . HOH K 5 .   ? 8.870   18.644 -14.060 1.00 28.46 ? 870  HOH A O   1 
HETATM 5351 O O   . HOH K 5 .   ? -21.100 14.471 7.715   1.00 40.56 ? 871  HOH A O   1 
HETATM 5352 O O   . HOH K 5 .   ? 0.511   20.943 -33.290 1.00 26.94 ? 872  HOH A O   1 
HETATM 5353 O O   . HOH K 5 .   ? -12.830 39.473 4.463   1.00 38.83 ? 873  HOH A O   1 
HETATM 5354 O O   . HOH K 5 .   ? 8.544   11.035 -25.947 1.00 37.06 ? 874  HOH A O   1 
HETATM 5355 O O   . HOH K 5 .   ? -14.542 3.203  -14.408 1.00 44.34 ? 875  HOH A O   1 
HETATM 5356 O O   . HOH K 5 .   ? -16.203 16.659 -10.207 1.00 34.44 ? 876  HOH A O   1 
HETATM 5357 O O   . HOH K 5 .   ? -0.408  -2.386 -31.639 1.00 26.32 ? 877  HOH A O   1 
HETATM 5358 O O   . HOH K 5 .   ? 3.686   -4.511 -16.142 1.00 48.89 ? 878  HOH A O   1 
HETATM 5359 O O   . HOH K 5 .   ? 4.633   22.115 5.773   1.00 33.98 ? 879  HOH A O   1 
HETATM 5360 O O   . HOH K 5 .   ? 2.774   38.484 -17.342 1.00 32.69 ? 880  HOH A O   1 
HETATM 5361 O O   . HOH K 5 .   ? -11.284 42.344 -6.992  1.00 38.08 ? 881  HOH A O   1 
HETATM 5362 O O   . HOH K 5 .   ? -7.063  -0.195 -23.232 1.00 41.87 ? 882  HOH A O   1 
HETATM 5363 O O   . HOH K 5 .   ? -26.909 30.057 -10.860 1.00 28.34 ? 883  HOH A O   1 
HETATM 5364 O O   . HOH K 5 .   ? 2.983   41.745 -12.881 1.00 42.77 ? 884  HOH A O   1 
HETATM 5365 O O   . HOH K 5 .   ? -24.922 21.982 5.550   1.00 46.47 ? 885  HOH A O   1 
HETATM 5366 O O   . HOH K 5 .   ? -5.260  2.946  -31.275 1.00 27.65 ? 886  HOH A O   1 
HETATM 5367 O O   . HOH K 5 .   ? -8.384  2.033  -2.023  1.00 42.78 ? 887  HOH A O   1 
HETATM 5368 O O   . HOH K 5 .   ? -13.365 22.323 -22.992 1.00 32.37 ? 888  HOH A O   1 
HETATM 5369 O O   . HOH K 5 .   ? -4.068  25.682 -35.685 1.00 37.44 ? 889  HOH A O   1 
HETATM 5370 O O   . HOH K 5 .   ? -18.553 31.810 11.022  1.00 44.32 ? 890  HOH A O   1 
HETATM 5371 O O   . HOH K 5 .   ? 3.877   34.648 4.745   1.00 43.28 ? 891  HOH A O   1 
HETATM 5372 O O   . HOH K 5 .   ? 0.690   40.548 -16.173 1.00 36.01 ? 892  HOH A O   1 
HETATM 5373 O O   . HOH K 5 .   ? -15.196 8.649  -18.060 1.00 34.78 ? 893  HOH A O   1 
HETATM 5374 O O   . HOH K 5 .   ? -8.315  11.386 5.509   1.00 39.51 ? 894  HOH A O   1 
HETATM 5375 O O   . HOH K 5 .   ? 3.983   11.745 -31.340 1.00 32.79 ? 895  HOH A O   1 
HETATM 5376 O O   . HOH K 5 .   ? -24.774 39.114 -17.425 1.00 39.51 ? 896  HOH A O   1 
HETATM 5377 O O   . HOH K 5 .   ? -17.105 16.316 -19.298 1.00 48.73 ? 897  HOH A O   1 
HETATM 5378 O O   . HOH K 5 .   ? -0.776  6.261  -33.591 1.00 35.49 ? 898  HOH A O   1 
HETATM 5379 O O   . HOH K 5 .   ? -18.165 15.441 7.056   1.00 35.90 ? 899  HOH A O   1 
HETATM 5380 O O   . HOH K 5 .   ? -13.358 36.099 -29.696 1.00 31.04 ? 900  HOH A O   1 
HETATM 5381 O O   . HOH K 5 .   ? -4.991  44.354 -20.521 1.00 32.10 ? 901  HOH A O   1 
HETATM 5382 O O   . HOH K 5 .   ? 11.391  12.834 2.670   1.00 35.00 ? 902  HOH A O   1 
HETATM 5383 O O   . HOH K 5 .   ? 10.460  28.057 -26.079 1.00 28.70 ? 903  HOH A O   1 
HETATM 5384 O O   . HOH K 5 .   ? -16.464 2.157  3.375   1.00 52.55 ? 904  HOH A O   1 
HETATM 5385 O O   . HOH K 5 .   ? -16.564 44.821 -13.909 1.00 35.99 ? 905  HOH A O   1 
HETATM 5386 O O   . HOH K 5 .   ? -3.411  23.104 -35.049 1.00 26.09 ? 906  HOH A O   1 
HETATM 5387 O O   . HOH K 5 .   ? -15.785 5.035  -25.215 1.00 53.36 ? 907  HOH A O   1 
HETATM 5388 O O   . HOH K 5 .   ? 6.384   32.691 -13.921 1.00 33.96 ? 908  HOH A O   1 
HETATM 5389 O O   . HOH K 5 .   ? 11.745  19.042 -9.630  1.00 43.41 ? 909  HOH A O   1 
HETATM 5390 O O   . HOH K 5 .   ? -17.434 43.339 -7.745  1.00 44.00 ? 910  HOH A O   1 
HETATM 5391 O O   . HOH K 5 .   ? -17.961 25.446 10.435  1.00 44.57 ? 911  HOH A O   1 
HETATM 5392 O O   . HOH K 5 .   ? -13.787 4.329  -16.838 1.00 28.73 ? 912  HOH A O   1 
HETATM 5393 O O   . HOH K 5 .   ? -13.793 14.944 -33.653 1.00 44.44 ? 913  HOH A O   1 
HETATM 5394 O O   . HOH K 5 .   ? -19.880 13.057 -22.027 1.00 40.52 ? 914  HOH A O   1 
HETATM 5395 O O   . HOH K 5 .   ? -0.021  1.830  -34.621 1.00 63.75 ? 915  HOH A O   1 
HETATM 5396 O O   . HOH K 5 .   ? 11.677  16.296 -10.595 1.00 53.00 ? 916  HOH A O   1 
HETATM 5397 O O   . HOH K 5 .   ? 13.235  19.777 -31.349 1.00 39.39 ? 917  HOH A O   1 
HETATM 5398 O O   . HOH K 5 .   ? -27.514 17.338 0.281   1.00 48.95 ? 918  HOH A O   1 
HETATM 5399 O O   . HOH K 5 .   ? -18.111 28.816 14.127  1.00 50.71 ? 919  HOH A O   1 
HETATM 5400 O O   . HOH K 5 .   ? -8.701  35.057 7.166   1.00 34.38 ? 920  HOH A O   1 
HETATM 5401 O O   . HOH K 5 .   ? -19.765 28.682 12.341  1.00 49.67 ? 921  HOH A O   1 
HETATM 5402 O O   . HOH K 5 .   ? 5.987   35.616 -18.421 1.00 40.29 ? 922  HOH A O   1 
HETATM 5403 O O   . HOH K 5 .   ? -14.235 4.744  -12.344 1.00 52.17 ? 923  HOH A O   1 
HETATM 5404 O O   . HOH K 5 .   ? -6.118  2.361  -5.720  1.00 34.65 ? 924  HOH A O   1 
HETATM 5405 O O   . HOH K 5 .   ? -26.940 15.425 4.269   1.00 44.27 ? 925  HOH A O   1 
HETATM 5406 O O   . HOH K 5 .   ? -9.863  29.674 9.920   1.00 40.17 ? 926  HOH A O   1 
HETATM 5407 O O   . HOH K 5 .   ? 12.105  25.489 -14.306 1.00 52.21 ? 927  HOH A O   1 
HETATM 5408 O O   . HOH K 5 .   ? -11.864 34.639 -31.509 1.00 32.94 ? 928  HOH A O   1 
HETATM 5409 O O   . HOH K 5 .   ? -21.097 29.679 7.955   1.00 44.33 ? 929  HOH A O   1 
HETATM 5410 O O   . HOH K 5 .   ? -3.283  37.918 7.441   1.00 38.89 ? 930  HOH A O   1 
HETATM 5411 O O   . HOH K 5 .   ? -17.998 18.104 -15.177 1.00 37.79 ? 931  HOH A O   1 
HETATM 5412 O O   . HOH K 5 .   ? 10.869  21.811 -8.511  1.00 35.50 ? 932  HOH A O   1 
HETATM 5413 O O   . HOH K 5 .   ? 4.023   35.914 -16.796 1.00 30.85 ? 933  HOH A O   1 
HETATM 5414 O O   . HOH K 5 .   ? -4.158  7.463  3.090   1.00 40.93 ? 934  HOH A O   1 
HETATM 5415 O O   . HOH K 5 .   ? -27.198 12.780 0.942   1.00 55.76 ? 935  HOH A O   1 
HETATM 5416 O O   . HOH K 5 .   ? 14.843  14.965 -12.600 1.00 47.82 ? 936  HOH A O   1 
HETATM 5417 O O   . HOH K 5 .   ? 5.875   42.710 -10.039 1.00 46.27 ? 937  HOH A O   1 
HETATM 5418 O O   . HOH K 5 .   ? -6.042  0.493  -9.062  1.00 37.93 ? 938  HOH A O   1 
HETATM 5419 O O   . HOH K 5 .   ? 1.642   4.138  -33.264 1.00 48.18 ? 939  HOH A O   1 
HETATM 5420 O O   . HOH K 5 .   ? 7.196   42.468 -11.776 1.00 53.71 ? 940  HOH A O   1 
HETATM 5421 O O   . HOH K 5 .   ? -6.078  26.244 -33.913 1.00 33.60 ? 941  HOH A O   1 
HETATM 5422 O O   . HOH K 5 .   ? 4.256   25.146 6.121   1.00 38.59 ? 942  HOH A O   1 
HETATM 5423 O O   . HOH K 5 .   ? -29.467 21.678 -5.290  1.00 34.09 ? 943  HOH A O   1 
HETATM 5424 O O   . HOH K 5 .   ? -26.133 25.624 -14.999 1.00 42.83 ? 944  HOH A O   1 
HETATM 5425 O O   . HOH K 5 .   ? 2.556   6.734  -34.891 1.00 37.52 ? 945  HOH A O   1 
HETATM 5426 O O   . HOH K 5 .   ? 11.234  27.406 -10.129 1.00 33.98 ? 946  HOH A O   1 
HETATM 5427 O O   . HOH K 5 .   ? -9.249  16.429 -36.304 1.00 45.22 ? 947  HOH A O   1 
HETATM 5428 O O   . HOH K 5 .   ? -11.040 44.330 -18.704 1.00 40.66 ? 948  HOH A O   1 
HETATM 5429 O O   . HOH K 5 .   ? 6.691   3.401  -15.654 1.00 36.82 ? 949  HOH A O   1 
HETATM 5430 O O   . HOH K 5 .   ? -14.500 3.201  -4.858  1.00 53.52 ? 950  HOH A O   1 
HETATM 5431 O O   . HOH K 5 .   ? 9.366   6.444  -24.064 1.00 51.69 ? 951  HOH A O   1 
HETATM 5432 O O   . HOH K 5 .   ? -10.801 2.385  -26.645 1.00 53.30 ? 952  HOH A O   1 
HETATM 5433 O O   . HOH K 5 .   ? 11.460  28.968 -12.455 1.00 52.03 ? 953  HOH A O   1 
HETATM 5434 O O   . HOH K 5 .   ? -12.707 29.979 13.361  1.00 51.16 ? 954  HOH A O   1 
HETATM 5435 O O   . HOH K 5 .   ? 9.963   17.357 -6.403  1.00 36.89 ? 955  HOH A O   1 
HETATM 5436 O O   . HOH K 5 .   ? -17.204 8.535  -27.832 1.00 51.28 ? 956  HOH A O   1 
HETATM 5437 O O   . HOH K 5 .   ? -23.550 21.589 7.261   1.00 46.36 ? 957  HOH A O   1 
HETATM 5438 O O   . HOH K 5 .   ? -7.099  23.097 -34.666 1.00 34.18 ? 958  HOH A O   1 
HETATM 5439 O O   . HOH K 5 .   ? 8.935   33.942 -3.740  1.00 52.86 ? 959  HOH A O   1 
HETATM 5440 O O   . HOH K 5 .   ? -4.663  -1.189 -5.691  1.00 47.50 ? 960  HOH A O   1 
HETATM 5441 O O   . HOH K 5 .   ? 8.012   12.508 -32.552 1.00 36.41 ? 961  HOH A O   1 
HETATM 5442 O O   . HOH K 5 .   ? -16.276 19.425 14.011  1.00 41.27 ? 962  HOH A O   1 
HETATM 5443 O O   . HOH K 5 .   ? -3.594  35.200 -30.024 1.00 34.30 ? 963  HOH A O   1 
HETATM 5444 O O   . HOH K 5 .   ? -19.485 25.835 9.606   1.00 43.78 ? 964  HOH A O   1 
HETATM 5445 O O   . HOH K 5 .   ? -10.207 45.003 -15.622 1.00 54.78 ? 965  HOH A O   1 
HETATM 5446 O O   . HOH K 5 .   ? 14.595  24.113 -11.285 1.00 53.54 ? 966  HOH A O   1 
HETATM 5447 O O   . HOH K 5 .   ? -10.332 44.913 -3.264  1.00 34.74 ? 967  HOH A O   1 
HETATM 5448 O O   . HOH K 5 .   ? -26.956 28.842 -11.980 1.00 38.11 ? 968  HOH A O   1 
HETATM 5449 O O   . HOH K 5 .   ? -11.157 26.145 11.133  1.00 28.78 ? 969  HOH A O   1 
HETATM 5450 O O   . HOH K 5 .   ? 6.687   34.795 2.189   1.00 45.56 ? 970  HOH A O   1 
HETATM 5451 O O   . HOH K 5 .   ? -17.762 6.786  -25.074 1.00 50.43 ? 971  HOH A O   1 
HETATM 5452 O O   . HOH K 5 .   ? 12.869  17.837 -31.118 1.00 47.29 ? 972  HOH A O   1 
HETATM 5453 O O   . HOH K 5 .   ? 5.049   40.581 1.939   1.00 47.47 ? 973  HOH A O   1 
HETATM 5454 O O   . HOH K 5 .   ? 7.179   25.498 4.546   1.00 42.61 ? 974  HOH A O   1 
HETATM 5455 O O   . HOH K 5 .   ? -15.098 39.510 -22.898 1.00 30.49 ? 975  HOH A O   1 
HETATM 5456 O O   . HOH K 5 .   ? 10.530  16.285 -30.280 1.00 27.31 ? 976  HOH A O   1 
HETATM 5457 O O   . HOH K 5 .   ? -28.566 17.996 -1.387  1.00 42.39 ? 977  HOH A O   1 
HETATM 5458 O O   . HOH K 5 .   ? -18.213 13.674 -9.065  1.00 46.91 ? 978  HOH A O   1 
HETATM 5459 O O   . HOH K 5 .   ? -2.908  7.031  -36.336 1.00 39.10 ? 979  HOH A O   1 
HETATM 5460 O O   . HOH K 5 .   ? 6.567   6.824  -27.047 1.00 41.67 ? 980  HOH A O   1 
HETATM 5461 O O   . HOH K 5 .   ? 14.404  22.657 -25.471 1.00 46.00 ? 981  HOH A O   1 
HETATM 5462 O O   . HOH K 5 .   ? -9.245  44.621 -24.067 1.00 48.00 ? 982  HOH A O   1 
HETATM 5463 O O   . HOH K 5 .   ? -12.956 10.006 -31.977 1.00 32.11 ? 983  HOH A O   1 
HETATM 5464 O O   . HOH K 5 .   ? -7.771  8.098  3.629   1.00 37.47 ? 984  HOH A O   1 
HETATM 5465 O O   . HOH K 5 .   ? -10.151 38.249 -29.150 1.00 38.52 ? 985  HOH A O   1 
HETATM 5466 O O   . HOH K 5 .   ? -1.712  45.231 -8.382  1.00 46.16 ? 986  HOH A O   1 
HETATM 5467 O O   . HOH K 5 .   ? 15.492  20.819 -21.080 1.00 45.12 ? 987  HOH A O   1 
HETATM 5468 O O   . HOH K 5 .   ? 12.945  9.054  1.657   1.00 47.84 ? 988  HOH A O   1 
HETATM 5469 O O   . HOH K 5 .   ? -11.680 38.086 5.221   1.00 39.96 ? 989  HOH A O   1 
HETATM 5470 O O   . HOH K 5 .   ? -24.589 24.022 -16.047 1.00 25.97 ? 990  HOH A O   1 
HETATM 5471 O O   . HOH K 5 .   ? -19.005 15.188 -20.002 1.00 40.33 ? 991  HOH A O   1 
HETATM 5472 O O   . HOH K 5 .   ? -20.968 23.013 9.369   1.00 35.58 ? 992  HOH A O   1 
HETATM 5473 O O   . HOH K 5 .   ? -12.115 4.085  3.698   1.00 43.29 ? 993  HOH A O   1 
HETATM 5474 O O   . HOH K 5 .   ? 1.940   -5.841 -13.158 1.00 49.40 ? 994  HOH A O   1 
HETATM 5475 O O   . HOH K 5 .   ? -15.786 22.062 -24.251 1.00 40.04 ? 995  HOH A O   1 
HETATM 5476 O O   . HOH K 5 .   ? -16.262 19.763 -20.883 1.00 37.80 ? 996  HOH A O   1 
HETATM 5477 O O   . HOH K 5 .   ? 11.185  27.867 -16.277 1.00 54.86 ? 997  HOH A O   1 
HETATM 5478 O O   . HOH K 5 .   ? -23.612 22.240 -14.104 1.00 26.78 ? 998  HOH A O   1 
HETATM 5479 O O   . HOH K 5 .   ? -21.493 22.576 -10.289 1.00 27.74 ? 999  HOH A O   1 
HETATM 5480 O O   . HOH K 5 .   ? -8.506  28.879 12.558  1.00 30.46 ? 1000 HOH A O   1 
HETATM 5481 O O   . HOH K 5 .   ? -17.769 9.318  -18.104 1.00 42.16 ? 1001 HOH A O   1 
HETATM 5482 O O   . HOH K 5 .   ? 0.693   37.288 -15.788 1.00 17.33 ? 1002 HOH A O   1 
HETATM 5483 O O   . HOH K 5 .   ? -0.993  12.694 6.891   1.00 46.32 ? 1003 HOH A O   1 
HETATM 5484 O O   . HOH K 5 .   ? -23.686 13.919 7.045   1.00 41.26 ? 1004 HOH A O   1 
HETATM 5485 O O   . HOH K 5 .   ? -14.623 42.004 -22.026 1.00 35.50 ? 1005 HOH A O   1 
HETATM 5486 O O   . HOH K 5 .   ? -6.517  46.882 -18.074 1.00 39.67 ? 1006 HOH A O   1 
HETATM 5487 O O   . HOH K 5 .   ? 6.099   15.772 -32.699 1.00 27.44 ? 1007 HOH A O   1 
HETATM 5488 O O   . HOH K 5 .   ? -10.867 42.480 -22.691 1.00 29.89 ? 1008 HOH A O   1 
HETATM 5489 O O   . HOH K 5 .   ? -14.882 43.070 -8.872  1.00 35.08 ? 1009 HOH A O   1 
HETATM 5490 O O   . HOH K 5 .   ? -11.163 15.246 -37.294 1.00 42.45 ? 1010 HOH A O   1 
HETATM 5491 O O   . HOH K 5 .   ? 6.341   33.313 4.802   1.00 53.29 ? 1011 HOH A O   1 
HETATM 5492 O O   . HOH K 5 .   ? -17.803 38.669 5.267   1.00 41.27 ? 1012 HOH A O   1 
HETATM 5493 O O   . HOH K 5 .   ? 13.132  18.706 -24.541 1.00 33.73 ? 1013 HOH A O   1 
HETATM 5494 O O   . HOH K 5 .   ? -19.719 19.324 -25.651 1.00 31.67 ? 1014 HOH A O   1 
HETATM 5495 O O   . HOH K 5 .   ? -26.732 20.355 -0.486  1.00 35.78 ? 1015 HOH A O   1 
HETATM 5496 O O   . HOH K 5 .   ? -3.884  2.523  -34.010 1.00 35.04 ? 1016 HOH A O   1 
HETATM 5497 O O   . HOH K 5 .   ? -20.055 19.794 -13.503 1.00 30.25 ? 1017 HOH A O   1 
HETATM 5498 O O   . HOH K 5 .   ? -21.697 32.122 8.214   1.00 45.36 ? 1018 HOH A O   1 
HETATM 5499 O O   . HOH K 5 .   ? 12.548  24.042 -7.713  1.00 45.03 ? 1019 HOH A O   1 
HETATM 5500 O O   . HOH K 5 .   ? -26.725 32.897 -4.988  1.00 49.49 ? 1020 HOH A O   1 
HETATM 5501 O O   . HOH K 5 .   ? -21.305 17.834 -27.612 1.00 38.32 ? 1021 HOH A O   1 
HETATM 5502 O O   . HOH K 5 .   ? -19.663 38.771 -22.301 1.00 29.17 ? 1022 HOH A O   1 
HETATM 5503 O O   . HOH K 5 .   ? -14.582 34.143 -32.917 1.00 35.68 ? 1023 HOH A O   1 
HETATM 5504 O O   . HOH K 5 .   ? 9.565   30.428 -3.226  1.00 40.48 ? 1024 HOH A O   1 
HETATM 5505 O O   . HOH K 5 .   ? -12.162 0.222  -0.716  1.00 46.97 ? 1025 HOH A O   1 
HETATM 5506 O O   . HOH K 5 .   ? -13.898 45.220 -10.059 1.00 43.63 ? 1026 HOH A O   1 
HETATM 5507 O O   . HOH K 5 .   ? -19.948 20.330 -8.391  1.00 38.53 ? 1027 HOH A O   1 
HETATM 5508 O O   . HOH K 5 .   ? -7.955  -0.121 -6.516  1.00 49.34 ? 1028 HOH A O   1 
HETATM 5509 O O   . HOH K 5 .   ? -1.053  0.744  -2.237  1.00 40.63 ? 1029 HOH A O   1 
HETATM 5510 O O   . HOH K 5 .   ? -3.092  12.183 4.752   1.00 37.25 ? 1030 HOH A O   1 
HETATM 5511 O O   . HOH K 5 .   ? 8.664   35.401 -2.642  1.00 51.15 ? 1031 HOH A O   1 
HETATM 5512 O O   . HOH K 5 .   ? -17.647 19.544 -29.745 1.00 33.23 ? 1032 HOH A O   1 
HETATM 5513 O O   . HOH K 5 .   ? -14.660 37.681 7.575   1.00 38.76 ? 1033 HOH A O   1 
HETATM 5514 O O   . HOH K 5 .   ? -13.631 43.796 -17.680 1.00 28.08 ? 1034 HOH A O   1 
HETATM 5515 O O   . HOH K 5 .   ? -11.597 31.267 10.109  1.00 42.53 ? 1035 HOH A O   1 
HETATM 5516 O O   . HOH K 5 .   ? 1.908   34.846 7.388   1.00 37.02 ? 1036 HOH A O   1 
HETATM 5517 O O   . HOH K 5 .   ? 8.660   36.167 -27.469 1.00 43.16 ? 1037 HOH A O   1 
HETATM 5518 O O   . HOH K 5 .   ? -6.843  5.028  0.599   1.00 34.04 ? 1038 HOH A O   1 
HETATM 5519 O O   . HOH K 5 .   ? -18.950 12.367 9.024   1.00 50.03 ? 1039 HOH A O   1 
HETATM 5520 O O   . HOH K 5 .   ? 11.308  16.506 -24.251 1.00 37.90 ? 1040 HOH A O   1 
HETATM 5521 O O   . HOH K 5 .   ? -10.228 -0.530 -19.443 1.00 35.36 ? 1041 HOH A O   1 
HETATM 5522 O O   . HOH K 5 .   ? -20.967 20.896 7.090   1.00 43.77 ? 1042 HOH A O   1 
HETATM 5523 O O   . HOH K 5 .   ? -17.397 18.284 -18.760 1.00 48.39 ? 1043 HOH A O   1 
HETATM 5524 O O   . HOH K 5 .   ? -9.131  1.534  -21.805 1.00 36.36 ? 1044 HOH A O   1 
HETATM 5525 O O   . HOH K 5 .   ? -8.304  4.562  -31.838 1.00 42.63 ? 1045 HOH A O   1 
HETATM 5526 O O   . HOH K 5 .   ? -13.972 12.402 -34.082 1.00 41.73 ? 1046 HOH A O   1 
HETATM 5527 O O   . HOH K 5 .   ? -6.707  35.700 -30.224 1.00 37.60 ? 1047 HOH A O   1 
HETATM 5528 O O   . HOH K 5 .   ? -5.972  46.898 -13.894 1.00 47.04 ? 1048 HOH A O   1 
HETATM 5529 O O   . HOH K 5 .   ? -2.270  32.680 -33.358 1.00 40.58 ? 1049 HOH A O   1 
HETATM 5530 O O   . HOH K 5 .   ? -20.312 17.021 8.843   1.00 32.56 ? 1050 HOH A O   1 
HETATM 5531 O O   . HOH K 5 .   ? -18.360 8.384  9.834   1.00 50.50 ? 1051 HOH A O   1 
HETATM 5532 O O   . HOH K 5 .   ? 13.129  26.533 -8.391  1.00 48.20 ? 1052 HOH A O   1 
HETATM 5533 O O   . HOH K 5 .   ? -23.124 32.191 -1.987  1.00 36.24 ? 1053 HOH A O   1 
HETATM 5534 O O   . HOH K 5 .   ? -13.140 2.237  -22.656 1.00 45.18 ? 1054 HOH A O   1 
HETATM 5535 O O   . HOH K 5 .   ? -11.831 13.017 -37.493 1.00 47.46 ? 1055 HOH A O   1 
HETATM 5536 O O   . HOH K 5 .   ? -15.395 6.545  -16.662 1.00 35.88 ? 1056 HOH A O   1 
HETATM 5537 O O   . HOH K 5 .   ? -11.912 0.499  1.512   1.00 44.52 ? 1057 HOH A O   1 
HETATM 5538 O O   . HOH K 5 .   ? -15.833 7.655  -13.999 1.00 38.90 ? 1058 HOH A O   1 
HETATM 5539 O O   . HOH K 5 .   ? -19.968 18.203 -29.993 1.00 44.70 ? 1059 HOH A O   1 
HETATM 5540 O O   . HOH K 5 .   ? -11.115 1.257  -23.211 1.00 39.90 ? 1060 HOH A O   1 
HETATM 5541 O O   . HOH K 5 .   ? -23.384 17.161 9.541   1.00 49.56 ? 1061 HOH A O   1 
HETATM 5542 O O   . HOH K 5 .   ? 9.467   40.928 3.916   1.00 58.42 ? 1062 HOH A O   1 
HETATM 5543 O O   . HOH L 5 .   ? -46.173 38.542 -18.198 1.00 44.92 ? 601  HOH B O   1 
HETATM 5544 O O   . HOH L 5 .   ? -11.928 28.535 -37.291 1.00 58.08 ? 602  HOH B O   1 
HETATM 5545 O O   . HOH L 5 .   ? -46.460 27.949 -11.264 1.00 45.92 ? 603  HOH B O   1 
HETATM 5546 O O   . HOH L 5 .   ? -20.309 42.769 -40.454 1.00 38.71 ? 604  HOH B O   1 
HETATM 5547 O O   . HOH L 5 .   ? -11.883 30.481 -34.029 1.00 37.03 ? 605  HOH B O   1 
HETATM 5548 O O   . HOH L 5 .   ? -45.660 31.103 -50.467 1.00 35.36 ? 606  HOH B O   1 
HETATM 5549 O O   . HOH L 5 .   ? -31.923 22.137 -9.711  1.00 44.22 ? 607  HOH B O   1 
HETATM 5550 O O   . HOH L 5 .   ? -31.494 30.881 -16.493 1.00 23.47 ? 608  HOH B O   1 
HETATM 5551 O O   . HOH L 5 .   ? -33.891 18.162 -8.459  1.00 29.92 ? 609  HOH B O   1 
HETATM 5552 O O   . HOH L 5 .   ? -29.047 37.867 -16.406 1.00 39.75 ? 610  HOH B O   1 
HETATM 5553 O O   . HOH L 5 .   ? -29.155 45.724 -23.701 1.00 40.14 ? 611  HOH B O   1 
HETATM 5554 O O   . HOH L 5 .   ? -47.305 6.761  -20.819 1.00 40.26 ? 612  HOH B O   1 
HETATM 5555 O O   . HOH L 5 .   ? -42.774 31.824 -50.578 1.00 27.13 ? 613  HOH B O   1 
HETATM 5556 O O   . HOH L 5 .   ? -42.887 12.003 -37.687 1.00 17.97 ? 614  HOH B O   1 
HETATM 5557 O O   . HOH L 5 .   ? -14.585 36.529 -26.594 1.00 33.48 ? 615  HOH B O   1 
HETATM 5558 O O   . HOH L 5 .   ? -53.779 14.862 -44.143 1.00 36.21 ? 616  HOH B O   1 
HETATM 5559 O O   . HOH L 5 .   ? -27.186 43.875 -25.303 1.00 36.25 ? 617  HOH B O   1 
HETATM 5560 O O   . HOH L 5 .   ? -22.281 38.750 -48.522 1.00 30.29 ? 618  HOH B O   1 
HETATM 5561 O O   . HOH L 5 .   ? -41.808 4.048  -35.415 1.00 28.19 ? 619  HOH B O   1 
HETATM 5562 O O   . HOH L 5 .   ? -55.433 28.011 -26.386 1.00 48.80 ? 620  HOH B O   1 
HETATM 5563 O O   . HOH L 5 .   ? -41.228 10.125 -10.078 1.00 37.84 ? 621  HOH B O   1 
HETATM 5564 O O   . HOH L 5 .   ? -43.965 4.811  -19.242 1.00 25.81 ? 622  HOH B O   1 
HETATM 5565 O O   . HOH L 5 .   ? -32.370 -1.941 -30.818 1.00 44.86 ? 623  HOH B O   1 
HETATM 5566 O O   . HOH L 5 .   ? -51.776 26.006 -45.039 1.00 33.11 ? 624  HOH B O   1 
HETATM 5567 O O   . HOH L 5 .   ? -53.436 14.660 -39.818 1.00 30.11 ? 625  HOH B O   1 
HETATM 5568 O O   . HOH L 5 .   ? -51.136 7.048  -30.848 1.00 48.25 ? 626  HOH B O   1 
HETATM 5569 O O   . HOH L 5 .   ? -41.172 43.959 -40.750 1.00 38.88 ? 627  HOH B O   1 
HETATM 5570 O O   . HOH L 5 .   ? -54.290 22.544 -47.518 1.00 38.39 ? 628  HOH B O   1 
HETATM 5571 O O   . HOH L 5 .   ? -42.000 43.362 -28.464 1.00 31.24 ? 629  HOH B O   1 
HETATM 5572 O O   . HOH L 5 .   ? -12.993 33.182 -38.699 1.00 40.50 ? 630  HOH B O   1 
HETATM 5573 O O   . HOH L 5 .   ? -41.521 36.833 -12.489 1.00 37.52 ? 631  HOH B O   1 
HETATM 5574 O O   . HOH L 5 .   ? -40.008 15.032 -46.525 1.00 37.51 ? 632  HOH B O   1 
HETATM 5575 O O   . HOH L 5 .   ? -52.702 31.217 -21.976 1.00 44.60 ? 633  HOH B O   1 
HETATM 5576 O O   . HOH L 5 .   ? -23.045 36.219 -52.652 1.00 41.23 ? 634  HOH B O   1 
HETATM 5577 O O   . HOH L 5 .   ? -15.813 36.046 -44.412 1.00 42.46 ? 635  HOH B O   1 
HETATM 5578 O O   . HOH L 5 .   ? -20.064 22.438 -39.396 1.00 20.02 ? 636  HOH B O   1 
HETATM 5579 O O   . HOH L 5 .   ? -33.972 43.949 -38.922 1.00 25.63 ? 637  HOH B O   1 
HETATM 5580 O O   . HOH L 5 .   ? -46.755 33.496 -24.882 1.00 29.82 ? 638  HOH B O   1 
HETATM 5581 O O   . HOH L 5 .   ? -33.117 44.186 -18.647 1.00 22.06 ? 639  HOH B O   1 
HETATM 5582 O O   . HOH L 5 .   ? -48.655 12.721 -46.219 1.00 41.47 ? 640  HOH B O   1 
HETATM 5583 O O   . HOH L 5 .   ? -40.756 6.424  -42.828 1.00 25.54 ? 641  HOH B O   1 
HETATM 5584 O O   . HOH L 5 .   ? -53.602 22.038 -39.045 1.00 31.55 ? 642  HOH B O   1 
HETATM 5585 O O   . HOH L 5 .   ? -19.110 20.500 -49.057 1.00 26.20 ? 643  HOH B O   1 
HETATM 5586 O O   . HOH L 5 .   ? -26.159 25.142 -21.021 1.00 37.23 ? 644  HOH B O   1 
HETATM 5587 O O   . HOH L 5 .   ? -23.813 41.963 -46.436 1.00 39.64 ? 645  HOH B O   1 
HETATM 5588 O O   . HOH L 5 .   ? -42.362 37.223 -51.300 1.00 37.98 ? 646  HOH B O   1 
HETATM 5589 O O   . HOH L 5 .   ? -29.375 11.802 -27.507 1.00 22.41 ? 647  HOH B O   1 
HETATM 5590 O O   . HOH L 5 .   ? -50.249 5.495  -34.356 1.00 31.71 ? 648  HOH B O   1 
HETATM 5591 O O   . HOH L 5 .   ? -50.778 17.302 -14.627 1.00 34.56 ? 649  HOH B O   1 
HETATM 5592 O O   . HOH L 5 .   ? -37.642 16.888 -6.470  1.00 28.20 ? 650  HOH B O   1 
HETATM 5593 O O   . HOH L 5 .   ? -45.128 37.400 -52.697 1.00 40.18 ? 651  HOH B O   1 
HETATM 5594 O O   . HOH L 5 .   ? -46.784 34.193 -39.442 1.00 29.68 ? 652  HOH B O   1 
HETATM 5595 O O   . HOH L 5 .   ? -37.511 6.381  -36.637 1.00 19.02 ? 653  HOH B O   1 
HETATM 5596 O O   . HOH L 5 .   ? -27.586 17.287 -53.317 1.00 22.22 ? 654  HOH B O   1 
HETATM 5597 O O   . HOH L 5 .   ? -50.414 23.207 -26.626 1.00 23.54 ? 655  HOH B O   1 
HETATM 5598 O O   . HOH L 5 .   ? -40.107 26.849 -9.891  1.00 19.25 ? 656  HOH B O   1 
HETATM 5599 O O   . HOH L 5 .   ? -30.423 12.436 -8.788  1.00 39.62 ? 657  HOH B O   1 
HETATM 5600 O O   . HOH L 5 .   ? -21.412 30.284 -22.949 1.00 17.85 ? 658  HOH B O   1 
HETATM 5601 O O   . HOH L 5 .   ? -28.034 29.333 -22.177 1.00 15.88 ? 659  HOH B O   1 
HETATM 5602 O O   . HOH L 5 .   ? -30.772 4.879  -35.904 1.00 33.39 ? 660  HOH B O   1 
HETATM 5603 O O   . HOH L 5 .   ? -13.848 31.431 -37.399 1.00 29.69 ? 661  HOH B O   1 
HETATM 5604 O O   . HOH L 5 .   ? -41.125 27.666 -50.874 1.00 24.19 ? 662  HOH B O   1 
HETATM 5605 O O   . HOH L 5 .   ? -48.627 33.154 -37.706 1.00 28.84 ? 663  HOH B O   1 
HETATM 5606 O O   . HOH L 5 .   ? -27.377 44.288 -40.954 1.00 32.29 ? 664  HOH B O   1 
HETATM 5607 O O   . HOH L 5 .   ? -25.919 1.539  -51.592 1.00 58.54 ? 665  HOH B O   1 
HETATM 5608 O O   . HOH L 5 .   ? -45.822 8.292  -15.635 1.00 36.70 ? 666  HOH B O   1 
HETATM 5609 O O   . HOH L 5 .   ? -55.816 20.595 -23.975 1.00 44.93 ? 667  HOH B O   1 
HETATM 5610 O O   . HOH L 5 .   ? -44.651 2.474  -37.746 1.00 26.05 ? 668  HOH B O   1 
HETATM 5611 O O   . HOH L 5 .   ? -33.642 28.678 -16.058 1.00 21.56 ? 669  HOH B O   1 
HETATM 5612 O O   . HOH L 5 .   ? -24.676 41.781 -40.982 1.00 34.70 ? 670  HOH B O   1 
HETATM 5613 O O   . HOH L 5 .   ? -48.437 25.752 -47.366 1.00 29.43 ? 671  HOH B O   1 
HETATM 5614 O O   . HOH L 5 .   ? -32.165 11.715 -53.591 1.00 45.29 ? 672  HOH B O   1 
HETATM 5615 O O   . HOH L 5 .   ? -33.392 9.462  -11.323 1.00 34.71 ? 673  HOH B O   1 
HETATM 5616 O O   . HOH L 5 .   ? -43.315 9.713  -10.043 1.00 36.43 ? 674  HOH B O   1 
HETATM 5617 O O   . HOH L 5 .   ? -30.739 27.825 -13.734 1.00 34.83 ? 675  HOH B O   1 
HETATM 5618 O O   . HOH L 5 .   ? -26.145 32.586 -49.801 1.00 18.37 ? 676  HOH B O   1 
HETATM 5619 O O   . HOH L 5 .   ? -46.924 12.525 -15.261 1.00 34.22 ? 677  HOH B O   1 
HETATM 5620 O O   . HOH L 5 .   ? -37.073 37.752 -51.595 1.00 23.62 ? 678  HOH B O   1 
HETATM 5621 O O   . HOH L 5 .   ? -52.348 10.076 -26.285 1.00 41.24 ? 679  HOH B O   1 
HETATM 5622 O O   . HOH L 5 .   ? -40.635 6.459  -40.070 1.00 24.19 ? 680  HOH B O   1 
HETATM 5623 O O   . HOH L 5 .   ? -33.290 11.977 -19.951 1.00 19.94 ? 681  HOH B O   1 
HETATM 5624 O O   . HOH L 5 .   ? -37.930 5.261  -34.248 1.00 23.35 ? 682  HOH B O   1 
HETATM 5625 O O   . HOH L 5 .   ? -50.566 28.493 -33.056 1.00 28.49 ? 683  HOH B O   1 
HETATM 5626 O O   . HOH L 5 .   ? -37.432 3.100  -20.679 1.00 27.95 ? 684  HOH B O   1 
HETATM 5627 O O   . HOH L 5 .   ? -34.579 7.865  -49.348 1.00 40.61 ? 685  HOH B O   1 
HETATM 5628 O O   . HOH L 5 .   ? -26.004 16.590 -49.694 1.00 22.63 ? 686  HOH B O   1 
HETATM 5629 O O   . HOH L 5 .   ? -25.315 16.769 -37.752 1.00 29.38 ? 687  HOH B O   1 
HETATM 5630 O O   . HOH L 5 .   ? -20.438 39.359 -46.744 1.00 29.53 ? 688  HOH B O   1 
HETATM 5631 O O   . HOH L 5 .   ? -18.497 35.873 -50.017 1.00 40.69 ? 689  HOH B O   1 
HETATM 5632 O O   . HOH L 5 .   ? -51.215 29.660 -24.705 1.00 26.70 ? 690  HOH B O   1 
HETATM 5633 O O   . HOH L 5 .   ? -24.547 22.576 -55.338 1.00 25.52 ? 691  HOH B O   1 
HETATM 5634 O O   . HOH L 5 .   ? -26.029 12.288 -19.608 1.00 26.81 ? 692  HOH B O   1 
HETATM 5635 O O   . HOH L 5 .   ? -26.121 42.359 -20.499 1.00 33.84 ? 693  HOH B O   1 
HETATM 5636 O O   . HOH L 5 .   ? -28.243 45.230 -19.492 1.00 34.37 ? 694  HOH B O   1 
HETATM 5637 O O   . HOH L 5 .   ? -18.385 17.576 -41.143 1.00 39.80 ? 695  HOH B O   1 
HETATM 5638 O O   . HOH L 5 .   ? -34.312 10.204 -38.231 1.00 21.50 ? 696  HOH B O   1 
HETATM 5639 O O   . HOH L 5 .   ? -34.982 33.310 -53.982 1.00 33.09 ? 697  HOH B O   1 
HETATM 5640 O O   . HOH L 5 .   ? -39.723 2.434  -41.204 1.00 38.92 ? 698  HOH B O   1 
HETATM 5641 O O   . HOH L 5 .   ? -35.245 11.740 -48.047 1.00 24.22 ? 699  HOH B O   1 
HETATM 5642 O O   . HOH L 5 .   ? -21.172 9.306  -48.577 1.00 40.76 ? 700  HOH B O   1 
HETATM 5643 O O   . HOH L 5 .   ? -43.521 41.550 -18.540 1.00 38.18 ? 701  HOH B O   1 
HETATM 5644 O O   . HOH L 5 .   ? -26.148 36.884 -19.023 1.00 25.44 ? 702  HOH B O   1 
HETATM 5645 O O   . HOH L 5 .   ? -44.019 32.010 -38.803 1.00 17.58 ? 703  HOH B O   1 
HETATM 5646 O O   . HOH L 5 .   ? -23.293 12.870 -20.592 1.00 34.53 ? 704  HOH B O   1 
HETATM 5647 O O   . HOH L 5 .   ? -43.231 28.067 -49.094 1.00 27.31 ? 705  HOH B O   1 
HETATM 5648 O O   . HOH L 5 .   ? -44.808 21.964 -11.895 1.00 23.15 ? 706  HOH B O   1 
HETATM 5649 O O   . HOH L 5 .   ? -41.038 2.440  -19.129 1.00 25.97 ? 707  HOH B O   1 
HETATM 5650 O O   . HOH L 5 .   ? -16.114 38.254 -35.631 1.00 32.65 ? 708  HOH B O   1 
HETATM 5651 O O   . HOH L 5 .   ? -18.193 20.913 -51.541 1.00 41.43 ? 709  HOH B O   1 
HETATM 5652 O O   . HOH L 5 .   ? -51.547 21.657 -16.364 1.00 31.99 ? 710  HOH B O   1 
HETATM 5653 O O   . HOH L 5 .   ? -45.442 10.480 -13.673 1.00 44.49 ? 711  HOH B O   1 
HETATM 5654 O O   . HOH L 5 .   ? -13.373 25.219 -41.646 1.00 22.62 ? 712  HOH B O   1 
HETATM 5655 O O   . HOH L 5 .   ? -37.633 44.330 -15.621 1.00 38.92 ? 713  HOH B O   1 
HETATM 5656 O O   . HOH L 5 .   ? -48.860 15.325 -18.403 1.00 28.06 ? 714  HOH B O   1 
HETATM 5657 O O   . HOH L 5 .   ? -31.756 15.842 -50.245 1.00 19.12 ? 715  HOH B O   1 
HETATM 5658 O O   . HOH L 5 .   ? -17.920 32.915 -43.870 1.00 37.16 ? 716  HOH B O   1 
HETATM 5659 O O   . HOH L 5 .   ? -34.474 28.368 -55.419 1.00 20.69 ? 717  HOH B O   1 
HETATM 5660 O O   . HOH L 5 .   ? -29.691 41.391 -46.400 1.00 17.70 ? 718  HOH B O   1 
HETATM 5661 O O   . HOH L 5 .   ? -48.572 16.084 -45.356 1.00 37.95 ? 719  HOH B O   1 
HETATM 5662 O O   . HOH L 5 .   ? -44.251 19.589 -50.495 1.00 23.14 ? 720  HOH B O   1 
HETATM 5663 O O   . HOH L 5 .   ? -48.634 28.528 -45.896 1.00 25.06 ? 721  HOH B O   1 
HETATM 5664 O O   . HOH L 5 .   ? -16.015 30.695 -40.399 1.00 30.27 ? 722  HOH B O   1 
HETATM 5665 O O   . HOH L 5 .   ? -52.754 27.219 -39.659 1.00 32.10 ? 723  HOH B O   1 
HETATM 5666 O O   . HOH L 5 .   ? -47.987 6.846  -38.687 1.00 36.30 ? 724  HOH B O   1 
HETATM 5667 O O   . HOH L 5 .   ? -36.288 43.819 -22.909 1.00 24.44 ? 725  HOH B O   1 
HETATM 5668 O O   . HOH L 5 .   ? -52.646 27.499 -19.165 1.00 27.62 ? 726  HOH B O   1 
HETATM 5669 O O   . HOH L 5 .   ? -52.552 19.635 -35.252 1.00 26.58 ? 727  HOH B O   1 
HETATM 5670 O O   . HOH L 5 .   ? -53.859 20.475 -19.712 1.00 34.56 ? 728  HOH B O   1 
HETATM 5671 O O   . HOH L 5 .   ? -53.501 10.924 -22.350 1.00 41.35 ? 729  HOH B O   1 
HETATM 5672 O O   . HOH L 5 .   ? -29.136 27.182 -56.832 1.00 24.14 ? 730  HOH B O   1 
HETATM 5673 O O   . HOH L 5 .   ? -36.476 6.085  -23.032 1.00 20.68 ? 731  HOH B O   1 
HETATM 5674 O O   . HOH L 5 .   ? -45.151 6.221  -43.283 1.00 38.33 ? 732  HOH B O   1 
HETATM 5675 O O   . HOH L 5 .   ? -49.521 4.990  -26.871 1.00 35.83 ? 733  HOH B O   1 
HETATM 5676 O O   . HOH L 5 .   ? -21.473 22.513 -37.154 1.00 18.09 ? 734  HOH B O   1 
HETATM 5677 O O   . HOH L 5 .   ? -34.702 38.311 -52.093 1.00 37.86 ? 735  HOH B O   1 
HETATM 5678 O O   . HOH L 5 .   ? -27.009 36.588 -13.962 1.00 36.63 ? 736  HOH B O   1 
HETATM 5679 O O   . HOH L 5 .   ? -16.693 16.702 -50.288 1.00 38.98 ? 737  HOH B O   1 
HETATM 5680 O O   . HOH L 5 .   ? -30.093 21.130 -21.668 1.00 22.18 ? 738  HOH B O   1 
HETATM 5681 O O   . HOH L 5 .   ? -38.597 9.826  -45.281 1.00 28.80 ? 739  HOH B O   1 
HETATM 5682 O O   . HOH L 5 .   ? -25.619 33.904 -53.473 1.00 30.03 ? 740  HOH B O   1 
HETATM 5683 O O   . HOH L 5 .   ? -41.714 31.008 -11.012 1.00 36.65 ? 741  HOH B O   1 
HETATM 5684 O O   . HOH L 5 .   ? -39.224 20.888 -53.973 1.00 23.59 ? 742  HOH B O   1 
HETATM 5685 O O   . HOH L 5 .   ? -37.457 1.781  -37.732 1.00 35.62 ? 743  HOH B O   1 
HETATM 5686 O O   . HOH L 5 .   ? -16.330 28.477 -42.045 1.00 23.67 ? 744  HOH B O   1 
HETATM 5687 O O   . HOH L 5 .   ? -23.614 13.816 -53.027 1.00 38.39 ? 745  HOH B O   1 
HETATM 5688 O O   . HOH L 5 .   ? -43.722 38.441 -22.190 1.00 30.08 ? 746  HOH B O   1 
HETATM 5689 O O   . HOH L 5 .   ? -33.705 45.707 -36.828 1.00 28.02 ? 747  HOH B O   1 
HETATM 5690 O O   . HOH L 5 .   ? -33.845 16.174 -54.180 1.00 27.94 ? 748  HOH B O   1 
HETATM 5691 O O   . HOH L 5 .   ? -38.947 4.774  -38.419 1.00 26.49 ? 749  HOH B O   1 
HETATM 5692 O O   . HOH L 5 .   ? -50.566 30.797 -17.974 1.00 32.15 ? 750  HOH B O   1 
HETATM 5693 O O   . HOH L 5 .   ? -45.360 40.459 -39.262 1.00 28.02 ? 751  HOH B O   1 
HETATM 5694 O O   . HOH L 5 .   ? -33.045 14.617 -21.172 1.00 18.77 ? 752  HOH B O   1 
HETATM 5695 O O   . HOH L 5 .   ? -37.829 16.688 -53.695 1.00 34.96 ? 753  HOH B O   1 
HETATM 5696 O O   . HOH L 5 .   ? -34.709 45.007 -28.293 1.00 25.43 ? 754  HOH B O   1 
HETATM 5697 O O   . HOH L 5 .   ? -33.724 27.978 -13.213 1.00 22.88 ? 755  HOH B O   1 
HETATM 5698 O O   . HOH L 5 .   ? -43.285 32.709 -12.822 1.00 35.52 ? 756  HOH B O   1 
HETATM 5699 O O   . HOH L 5 .   ? -53.426 25.112 -33.318 1.00 34.30 ? 757  HOH B O   1 
HETATM 5700 O O   . HOH L 5 .   ? -49.101 18.122 -46.992 1.00 31.07 ? 758  HOH B O   1 
HETATM 5701 O O   . HOH L 5 .   ? -28.075 6.626  -23.750 1.00 38.48 ? 759  HOH B O   1 
HETATM 5702 O O   . HOH L 5 .   ? -12.123 24.329 -36.577 1.00 43.42 ? 760  HOH B O   1 
HETATM 5703 O O   . HOH L 5 .   ? -51.776 30.199 -37.406 1.00 41.00 ? 761  HOH B O   1 
HETATM 5704 O O   . HOH L 5 .   ? -25.036 42.007 -36.746 1.00 28.22 ? 762  HOH B O   1 
HETATM 5705 O O   . HOH L 5 .   ? -53.369 28.136 -21.848 1.00 25.15 ? 763  HOH B O   1 
HETATM 5706 O O   . HOH L 5 .   ? -42.810 4.670  -39.265 1.00 28.34 ? 764  HOH B O   1 
HETATM 5707 O O   . HOH L 5 .   ? -28.768 40.669 -52.532 1.00 43.48 ? 765  HOH B O   1 
HETATM 5708 O O   . HOH L 5 .   ? -49.326 6.919  -28.661 1.00 32.37 ? 766  HOH B O   1 
HETATM 5709 O O   . HOH L 5 .   ? -17.611 32.867 -47.945 1.00 39.14 ? 767  HOH B O   1 
HETATM 5710 O O   . HOH L 5 .   ? -28.823 6.529  -51.507 1.00 38.57 ? 768  HOH B O   1 
HETATM 5711 O O   . HOH L 5 .   ? -39.652 38.081 -27.656 1.00 18.90 ? 769  HOH B O   1 
HETATM 5712 O O   . HOH L 5 .   ? -22.748 27.664 -52.771 1.00 22.48 ? 770  HOH B O   1 
HETATM 5713 O O   . HOH L 5 .   ? -39.863 3.756  -14.415 1.00 25.69 ? 771  HOH B O   1 
HETATM 5714 O O   . HOH L 5 .   ? -16.452 22.774 -26.879 1.00 32.74 ? 772  HOH B O   1 
HETATM 5715 O O   . HOH L 5 .   ? -43.470 41.252 -47.216 1.00 44.59 ? 773  HOH B O   1 
HETATM 5716 O O   . HOH L 5 .   ? -47.399 18.356 -12.127 1.00 22.73 ? 774  HOH B O   1 
HETATM 5717 O O   . HOH L 5 .   ? -33.961 35.218 -13.872 1.00 27.77 ? 775  HOH B O   1 
HETATM 5718 O O   . HOH L 5 .   ? -25.729 19.105 -50.658 1.00 19.33 ? 776  HOH B O   1 
HETATM 5719 O O   . HOH L 5 .   ? -19.140 40.243 -33.661 1.00 34.68 ? 777  HOH B O   1 
HETATM 5720 O O   . HOH L 5 .   ? -29.617 6.099  -21.340 1.00 26.25 ? 778  HOH B O   1 
HETATM 5721 O O   . HOH L 5 .   ? -38.449 35.526 -52.687 1.00 25.09 ? 779  HOH B O   1 
HETATM 5722 O O   . HOH L 5 .   ? -23.167 13.017 -37.645 1.00 38.88 ? 780  HOH B O   1 
HETATM 5723 O O   . HOH L 5 .   ? -40.137 40.782 -31.062 1.00 19.54 ? 781  HOH B O   1 
HETATM 5724 O O   . HOH L 5 .   ? -43.131 43.228 -24.399 1.00 27.64 ? 782  HOH B O   1 
HETATM 5725 O O   . HOH L 5 .   ? -38.931 43.946 -45.874 1.00 32.05 ? 783  HOH B O   1 
HETATM 5726 O O   . HOH L 5 .   ? -38.970 1.351  -31.661 1.00 41.80 ? 784  HOH B O   1 
HETATM 5727 O O   . HOH L 5 .   ? -37.452 4.051  -41.575 1.00 28.59 ? 785  HOH B O   1 
HETATM 5728 O O   . HOH L 5 .   ? -20.454 24.603 -54.729 1.00 55.01 ? 786  HOH B O   1 
HETATM 5729 O O   . HOH L 5 .   ? -28.795 43.673 -32.024 1.00 24.47 ? 787  HOH B O   1 
HETATM 5730 O O   . HOH L 5 .   ? -19.139 23.545 -23.967 1.00 34.26 ? 788  HOH B O   1 
HETATM 5731 O O   . HOH L 5 .   ? -47.893 37.080 -39.703 1.00 41.55 ? 789  HOH B O   1 
HETATM 5732 O O   . HOH L 5 .   ? -50.786 9.242  -41.320 1.00 39.79 ? 790  HOH B O   1 
HETATM 5733 O O   . HOH L 5 .   ? -42.901 17.346 -11.074 1.00 18.54 ? 791  HOH B O   1 
HETATM 5734 O O   . HOH L 5 .   ? -48.617 3.060  -31.740 1.00 35.47 ? 792  HOH B O   1 
HETATM 5735 O O   . HOH L 5 .   ? -47.687 23.399 -50.494 1.00 31.67 ? 793  HOH B O   1 
HETATM 5736 O O   . HOH L 5 .   ? -43.962 37.450 -45.390 1.00 19.34 ? 794  HOH B O   1 
HETATM 5737 O O   . HOH L 5 .   ? -25.036 20.089 -21.661 1.00 38.99 ? 795  HOH B O   1 
HETATM 5738 O O   . HOH L 5 .   ? -36.051 41.400 -28.494 1.00 21.57 ? 796  HOH B O   1 
HETATM 5739 O O   . HOH L 5 .   ? -34.392 16.725 -40.959 1.00 16.62 ? 797  HOH B O   1 
HETATM 5740 O O   . HOH L 5 .   ? -30.718 4.977  -32.783 1.00 43.61 ? 798  HOH B O   1 
HETATM 5741 O O   . HOH L 5 .   ? -25.179 40.519 -46.144 1.00 27.30 ? 799  HOH B O   1 
HETATM 5742 O O   . HOH L 5 .   ? -39.927 19.126 -13.695 1.00 17.62 ? 800  HOH B O   1 
HETATM 5743 O O   . HOH L 5 .   ? -23.304 44.392 -30.724 1.00 31.82 ? 801  HOH B O   1 
HETATM 5744 O O   . HOH L 5 .   ? -37.364 45.480 -32.353 1.00 27.46 ? 802  HOH B O   1 
HETATM 5745 O O   . HOH L 5 .   ? -43.427 38.122 -49.000 1.00 43.96 ? 803  HOH B O   1 
HETATM 5746 O O   . HOH L 5 .   ? -18.469 33.789 -24.472 1.00 26.84 ? 804  HOH B O   1 
HETATM 5747 O O   . HOH L 5 .   ? -45.938 42.410 -37.206 1.00 40.66 ? 805  HOH B O   1 
HETATM 5748 O O   . HOH L 5 .   ? -17.299 39.924 -31.221 1.00 32.85 ? 806  HOH B O   1 
HETATM 5749 O O   . HOH L 5 .   ? -52.679 30.041 -31.276 1.00 38.26 ? 807  HOH B O   1 
HETATM 5750 O O   . HOH L 5 .   ? -29.602 16.019 -51.964 1.00 23.67 ? 808  HOH B O   1 
HETATM 5751 O O   . HOH L 5 .   ? -28.873 36.316 -50.837 1.00 27.07 ? 809  HOH B O   1 
HETATM 5752 O O   . HOH L 5 .   ? -29.029 11.563 -15.534 1.00 26.15 ? 810  HOH B O   1 
HETATM 5753 O O   . HOH L 5 .   ? -21.991 20.100 -49.396 1.00 27.22 ? 811  HOH B O   1 
HETATM 5754 O O   . HOH L 5 .   ? -38.578 8.966  -24.465 1.00 19.32 ? 812  HOH B O   1 
HETATM 5755 O O   . HOH L 5 .   ? -23.258 20.523 -18.231 1.00 27.37 ? 813  HOH B O   1 
HETATM 5756 O O   . HOH L 5 .   ? -35.324 26.655 -9.891  1.00 28.99 ? 814  HOH B O   1 
HETATM 5757 O O   . HOH L 5 .   ? -29.812 47.526 -25.468 1.00 36.84 ? 815  HOH B O   1 
HETATM 5758 O O   . HOH L 5 .   ? -15.599 33.431 -30.681 1.00 20.37 ? 816  HOH B O   1 
HETATM 5759 O O   . HOH L 5 .   ? -48.239 32.321 -26.907 1.00 27.77 ? 817  HOH B O   1 
HETATM 5760 O O   . HOH L 5 .   ? -30.221 46.940 -29.960 1.00 40.60 ? 818  HOH B O   1 
HETATM 5761 O O   . HOH L 5 .   ? -20.309 21.872 -32.377 1.00 23.28 ? 819  HOH B O   1 
HETATM 5762 O O   . HOH L 5 .   ? -41.658 48.141 -38.121 1.00 41.83 ? 820  HOH B O   1 
HETATM 5763 O O   . HOH L 5 .   ? -48.490 29.859 -25.262 1.00 19.16 ? 821  HOH B O   1 
HETATM 5764 O O   . HOH L 5 .   ? -40.252 11.461 -40.127 1.00 18.97 ? 822  HOH B O   1 
HETATM 5765 O O   . HOH L 5 .   ? -35.882 3.825  -37.905 1.00 23.60 ? 823  HOH B O   1 
HETATM 5766 O O   . HOH L 5 .   ? -49.526 31.195 -33.915 1.00 22.12 ? 824  HOH B O   1 
HETATM 5767 O O   . HOH L 5 .   ? -34.033 37.980 -14.712 1.00 32.83 ? 825  HOH B O   1 
HETATM 5768 O O   . HOH L 5 .   ? -42.576 37.979 -30.475 1.00 26.54 ? 826  HOH B O   1 
HETATM 5769 O O   . HOH L 5 .   ? -35.010 8.724  -14.821 1.00 23.38 ? 827  HOH B O   1 
HETATM 5770 O O   . HOH L 5 .   ? -37.679 4.132  -29.836 1.00 21.67 ? 828  HOH B O   1 
HETATM 5771 O O   . HOH L 5 .   ? -53.957 18.977 -40.949 1.00 23.55 ? 829  HOH B O   1 
HETATM 5772 O O   . HOH L 5 .   ? -18.246 39.587 -26.152 1.00 32.08 ? 830  HOH B O   1 
HETATM 5773 O O   . HOH L 5 .   ? -24.317 19.002 -53.054 1.00 30.84 ? 831  HOH B O   1 
HETATM 5774 O O   . HOH L 5 .   ? -51.091 25.610 -36.532 1.00 27.08 ? 832  HOH B O   1 
HETATM 5775 O O   . HOH L 5 .   ? -46.538 34.956 -29.414 1.00 42.66 ? 833  HOH B O   1 
HETATM 5776 O O   . HOH L 5 .   ? -26.279 17.302 -34.523 1.00 29.50 ? 834  HOH B O   1 
HETATM 5777 O O   . HOH L 5 .   ? -28.206 33.230 -53.165 1.00 30.98 ? 835  HOH B O   1 
HETATM 5778 O O   . HOH L 5 .   ? -39.178 43.475 -24.967 1.00 29.67 ? 836  HOH B O   1 
HETATM 5779 O O   . HOH L 5 .   ? -19.841 13.208 -49.624 1.00 40.75 ? 837  HOH B O   1 
HETATM 5780 O O   . HOH L 5 .   ? -25.189 18.865 -36.650 1.00 29.67 ? 838  HOH B O   1 
HETATM 5781 O O   . HOH L 5 .   ? -24.903 38.390 -22.077 1.00 20.62 ? 839  HOH B O   1 
HETATM 5782 O O   . HOH L 5 .   ? -42.483 34.481 -10.054 1.00 48.28 ? 840  HOH B O   1 
HETATM 5783 O O   . HOH L 5 .   ? -14.390 36.872 -40.321 1.00 43.32 ? 841  HOH B O   1 
HETATM 5784 O O   . HOH L 5 .   ? -26.216 43.312 -33.112 1.00 29.78 ? 842  HOH B O   1 
HETATM 5785 O O   . HOH L 5 .   ? -25.115 16.660 -26.167 1.00 31.89 ? 843  HOH B O   1 
HETATM 5786 O O   . HOH L 5 .   ? -19.838 21.872 -34.977 1.00 25.77 ? 844  HOH B O   1 
HETATM 5787 O O   . HOH L 5 .   ? -31.855 31.112 -54.649 1.00 27.23 ? 845  HOH B O   1 
HETATM 5788 O O   . HOH L 5 .   ? -45.961 41.067 -42.884 1.00 34.10 ? 846  HOH B O   1 
HETATM 5789 O O   . HOH L 5 .   ? -34.768 23.182 -55.811 1.00 19.27 ? 847  HOH B O   1 
HETATM 5790 O O   . HOH L 5 .   ? -27.689 13.032 -52.563 1.00 29.57 ? 848  HOH B O   1 
HETATM 5791 O O   . HOH L 5 .   ? -19.959 44.251 -32.323 1.00 41.05 ? 849  HOH B O   1 
HETATM 5792 O O   . HOH L 5 .   ? -14.728 25.430 -30.453 1.00 23.72 ? 850  HOH B O   1 
HETATM 5793 O O   . HOH L 5 .   ? -54.725 20.539 -34.076 1.00 42.69 ? 851  HOH B O   1 
HETATM 5794 O O   . HOH L 5 .   ? -46.004 40.961 -34.420 1.00 35.42 ? 852  HOH B O   1 
HETATM 5795 O O   . HOH L 5 .   ? -41.725 1.173  -28.598 1.00 37.71 ? 853  HOH B O   1 
HETATM 5796 O O   . HOH L 5 .   ? -29.549 9.764  -53.541 1.00 42.06 ? 854  HOH B O   1 
HETATM 5797 O O   . HOH L 5 .   ? -27.449 16.115 -55.824 1.00 25.28 ? 855  HOH B O   1 
HETATM 5798 O O   . HOH L 5 .   ? -20.983 27.842 -24.474 1.00 15.43 ? 856  HOH B O   1 
HETATM 5799 O O   . HOH L 5 .   ? -19.071 26.590 -54.347 1.00 40.69 ? 857  HOH B O   1 
HETATM 5800 O O   . HOH L 5 .   ? -16.932 14.849 -45.712 1.00 39.82 ? 858  HOH B O   1 
HETATM 5801 O O   . HOH L 5 .   ? -20.666 34.107 -22.917 1.00 28.67 ? 859  HOH B O   1 
HETATM 5802 O O   . HOH L 5 .   ? -28.809 22.834 -24.031 1.00 21.59 ? 860  HOH B O   1 
HETATM 5803 O O   . HOH L 5 .   ? -27.594 31.439 -15.310 1.00 29.36 ? 861  HOH B O   1 
HETATM 5804 O O   . HOH L 5 .   ? -22.269 29.734 -55.615 1.00 28.14 ? 862  HOH B O   1 
HETATM 5805 O O   . HOH L 5 .   ? -51.428 8.645  -28.326 1.00 43.30 ? 863  HOH B O   1 
HETATM 5806 O O   . HOH L 5 .   ? -19.539 19.737 -39.312 1.00 31.28 ? 864  HOH B O   1 
HETATM 5807 O O   . HOH L 5 .   ? -22.893 42.185 -26.279 1.00 23.99 ? 865  HOH B O   1 
HETATM 5808 O O   . HOH L 5 .   ? -34.922 4.590  -45.403 1.00 41.19 ? 866  HOH B O   1 
HETATM 5809 O O   . HOH L 5 .   ? -17.031 18.844 -47.916 1.00 30.76 ? 867  HOH B O   1 
HETATM 5810 O O   . HOH L 5 .   ? -18.667 31.111 -46.003 1.00 21.48 ? 868  HOH B O   1 
HETATM 5811 O O   . HOH L 5 .   ? -33.859 29.201 -9.958  1.00 43.20 ? 869  HOH B O   1 
HETATM 5812 O O   . HOH L 5 .   ? -39.217 13.278 -47.612 1.00 46.51 ? 870  HOH B O   1 
HETATM 5813 O O   . HOH L 5 .   ? -15.162 24.474 -33.701 1.00 26.93 ? 871  HOH B O   1 
HETATM 5814 O O   . HOH L 5 .   ? -47.740 36.857 -15.099 1.00 45.43 ? 872  HOH B O   1 
HETATM 5815 O O   . HOH L 5 .   ? -27.257 23.475 -21.976 1.00 34.46 ? 873  HOH B O   1 
HETATM 5816 O O   . HOH L 5 .   ? -27.970 19.923 -56.731 1.00 30.27 ? 874  HOH B O   1 
HETATM 5817 O O   . HOH L 5 .   ? -28.919 3.063  -48.638 1.00 48.73 ? 875  HOH B O   1 
HETATM 5818 O O   . HOH L 5 .   ? -28.213 45.178 -29.945 1.00 34.35 ? 876  HOH B O   1 
HETATM 5819 O O   . HOH L 5 .   ? -17.615 36.277 -24.718 1.00 28.78 ? 877  HOH B O   1 
HETATM 5820 O O   . HOH L 5 .   ? -53.812 9.590  -38.098 1.00 53.85 ? 878  HOH B O   1 
HETATM 5821 O O   . HOH L 5 .   ? -20.934 18.054 -38.127 1.00 39.77 ? 879  HOH B O   1 
HETATM 5822 O O   . HOH L 5 .   ? -32.139 1.097  -33.632 1.00 44.15 ? 880  HOH B O   1 
HETATM 5823 O O   . HOH L 5 .   ? -12.711 23.125 -39.006 1.00 33.54 ? 881  HOH B O   1 
HETATM 5824 O O   . HOH L 5 .   ? -24.718 25.451 -55.238 1.00 30.77 ? 882  HOH B O   1 
HETATM 5825 O O   . HOH L 5 .   ? -37.675 6.254  -13.034 1.00 24.30 ? 883  HOH B O   1 
HETATM 5826 O O   . HOH L 5 .   ? -50.293 23.778 -29.346 1.00 28.65 ? 884  HOH B O   1 
HETATM 5827 O O   . HOH L 5 .   ? -43.289 17.026 -44.539 1.00 21.74 ? 885  HOH B O   1 
HETATM 5828 O O   . HOH L 5 .   ? -41.768 19.683 -11.601 1.00 18.63 ? 886  HOH B O   1 
HETATM 5829 O O   . HOH L 5 .   ? -40.502 41.985 -26.971 1.00 29.61 ? 887  HOH B O   1 
HETATM 5830 O O   . HOH L 5 .   ? -40.543 39.132 -51.014 1.00 39.01 ? 888  HOH B O   1 
HETATM 5831 O O   . HOH L 5 .   ? -49.345 34.941 -35.804 1.00 34.76 ? 889  HOH B O   1 
HETATM 5832 O O   . HOH L 5 .   ? -25.030 19.371 -13.760 1.00 42.10 ? 890  HOH B O   1 
HETATM 5833 O O   . HOH L 5 .   ? -27.002 16.265 -11.440 1.00 44.99 ? 891  HOH B O   1 
HETATM 5834 O O   . HOH L 5 .   ? -45.396 29.893 -11.852 1.00 27.69 ? 892  HOH B O   1 
HETATM 5835 O O   . HOH L 5 .   ? -25.555 19.169 -27.737 1.00 33.27 ? 893  HOH B O   1 
HETATM 5836 O O   . HOH L 5 .   ? -37.148 12.109 -8.024  1.00 22.04 ? 894  HOH B O   1 
HETATM 5837 O O   . HOH L 5 .   ? -18.214 21.371 -54.068 1.00 47.82 ? 895  HOH B O   1 
HETATM 5838 O O   . HOH L 5 .   ? -38.574 15.787 -48.705 1.00 32.06 ? 896  HOH B O   1 
HETATM 5839 O O   . HOH L 5 .   ? -19.160 30.705 -25.017 1.00 20.04 ? 897  HOH B O   1 
HETATM 5840 O O   . HOH L 5 .   ? -42.759 46.675 -34.678 1.00 43.57 ? 898  HOH B O   1 
HETATM 5841 O O   . HOH L 5 .   ? -34.999 4.382  -18.763 1.00 25.69 ? 899  HOH B O   1 
HETATM 5842 O O   . HOH L 5 .   ? -44.520 45.544 -36.278 1.00 49.52 ? 900  HOH B O   1 
HETATM 5843 O O   . HOH L 5 .   ? -30.835 5.367  -27.921 1.00 22.67 ? 901  HOH B O   1 
HETATM 5844 O O   . HOH L 5 .   ? -52.817 29.557 -27.002 1.00 39.86 ? 902  HOH B O   1 
HETATM 5845 O O   . HOH L 5 .   ? -27.918 19.883 -24.789 1.00 36.64 ? 903  HOH B O   1 
HETATM 5846 O O   . HOH L 5 .   ? -26.570 39.691 -49.768 1.00 32.84 ? 904  HOH B O   1 
HETATM 5847 O O   . HOH L 5 .   ? -17.302 33.176 -41.059 1.00 25.66 ? 905  HOH B O   1 
HETATM 5848 O O   . HOH L 5 .   ? -35.146 31.873 -10.200 1.00 38.04 ? 906  HOH B O   1 
HETATM 5849 O O   . HOH L 5 .   ? -27.797 5.937  -19.499 1.00 50.41 ? 907  HOH B O   1 
HETATM 5850 O O   . HOH L 5 .   ? -21.040 34.719 -53.348 1.00 43.23 ? 908  HOH B O   1 
HETATM 5851 O O   . HOH L 5 .   ? -19.551 32.920 -52.776 1.00 37.63 ? 909  HOH B O   1 
HETATM 5852 O O   . HOH L 5 .   ? -25.876 15.418 -52.345 1.00 30.61 ? 910  HOH B O   1 
HETATM 5853 O O   . HOH L 5 .   ? -53.507 10.649 -40.128 1.00 46.22 ? 911  HOH B O   1 
HETATM 5854 O O   . HOH L 5 .   ? -40.825 45.214 -32.214 1.00 39.45 ? 912  HOH B O   1 
HETATM 5855 O O   . HOH L 5 .   ? -18.360 18.938 -34.400 1.00 43.55 ? 913  HOH B O   1 
HETATM 5856 O O   . HOH L 5 .   ? -22.888 38.332 -13.192 1.00 40.67 ? 914  HOH B O   1 
HETATM 5857 O O   . HOH L 5 .   ? -31.552 2.667  -27.419 1.00 43.54 ? 915  HOH B O   1 
HETATM 5858 O O   . HOH L 5 .   ? -19.763 26.049 -22.752 1.00 24.33 ? 916  HOH B O   1 
HETATM 5859 O O   . HOH L 5 .   ? -17.399 35.487 -48.084 1.00 47.19 ? 917  HOH B O   1 
HETATM 5860 O O   . HOH L 5 .   ? -16.128 29.727 -46.644 1.00 45.26 ? 918  HOH B O   1 
HETATM 5861 O O   . HOH L 5 .   ? -56.554 25.664 -23.011 1.00 42.47 ? 919  HOH B O   1 
HETATM 5862 O O   . HOH L 5 .   ? -52.024 14.877 -46.343 1.00 41.12 ? 920  HOH B O   1 
HETATM 5863 O O   . HOH L 5 .   ? -15.373 17.727 -35.866 1.00 52.89 ? 921  HOH B O   1 
HETATM 5864 O O   . HOH L 5 .   ? -29.985 46.446 -33.827 1.00 41.91 ? 922  HOH B O   1 
HETATM 5865 O O   . HOH L 5 .   ? -45.449 16.267 -11.906 1.00 20.52 ? 923  HOH B O   1 
HETATM 5866 O O   . HOH L 5 .   ? -52.086 30.948 -29.398 1.00 44.34 ? 924  HOH B O   1 
HETATM 5867 O O   . HOH L 5 .   ? -20.090 28.823 -52.891 1.00 41.60 ? 925  HOH B O   1 
HETATM 5868 O O   . HOH L 5 .   ? -43.023 4.582  -16.613 1.00 33.75 ? 926  HOH B O   1 
HETATM 5869 O O   . HOH L 5 .   ? -54.453 24.116 -44.092 1.00 33.75 ? 927  HOH B O   1 
HETATM 5870 O O   . HOH L 5 .   ? -49.350 33.209 -17.437 1.00 35.92 ? 928  HOH B O   1 
HETATM 5871 O O   . HOH L 5 .   ? -28.239 9.308  -26.913 1.00 32.37 ? 929  HOH B O   1 
HETATM 5872 O O   . HOH L 5 .   ? -31.153 24.946 -12.724 1.00 36.53 ? 930  HOH B O   1 
HETATM 5873 O O   . HOH L 5 .   ? -22.409 13.126 -23.054 1.00 40.95 ? 931  HOH B O   1 
HETATM 5874 O O   . HOH L 5 .   ? -50.951 16.668 -17.419 1.00 38.93 ? 932  HOH B O   1 
HETATM 5875 O O   . HOH L 5 .   ? -38.243 1.445  -34.911 1.00 50.72 ? 933  HOH B O   1 
HETATM 5876 O O   . HOH L 5 .   ? -42.169 39.941 -27.227 1.00 29.59 ? 934  HOH B O   1 
HETATM 5877 O O   . HOH L 5 .   ? -23.285 7.994  -41.549 1.00 47.71 ? 935  HOH B O   1 
HETATM 5878 O O   . HOH L 5 .   ? -27.496 0.881  -48.456 1.00 51.75 ? 936  HOH B O   1 
HETATM 5879 O O   . HOH L 5 .   ? -48.463 34.231 -15.151 1.00 48.74 ? 937  HOH B O   1 
HETATM 5880 O O   . HOH L 5 .   ? -33.516 1.605  -25.906 1.00 50.82 ? 938  HOH B O   1 
HETATM 5881 O O   . HOH L 5 .   ? -13.030 32.569 -34.970 1.00 34.64 ? 939  HOH B O   1 
HETATM 5882 O O   . HOH L 5 .   ? -39.489 2.994  -34.120 1.00 32.85 ? 940  HOH B O   1 
HETATM 5883 O O   . HOH L 5 .   ? -18.045 41.757 -36.780 1.00 48.15 ? 941  HOH B O   1 
HETATM 5884 O O   . HOH L 5 .   ? -14.964 34.830 -42.097 1.00 35.32 ? 942  HOH B O   1 
HETATM 5885 O O   . HOH L 5 .   ? -38.477 47.460 -33.845 1.00 39.52 ? 943  HOH B O   1 
HETATM 5886 O O   . HOH L 5 .   ? -38.130 44.440 -28.419 1.00 38.82 ? 944  HOH B O   1 
HETATM 5887 O O   . HOH L 5 .   ? -38.757 43.447 -31.370 1.00 33.41 ? 945  HOH B O   1 
HETATM 5888 O O   . HOH L 5 .   ? -17.019 16.204 -38.973 1.00 41.87 ? 946  HOH B O   1 
HETATM 5889 O O   . HOH L 5 .   ? -44.720 44.965 -38.847 1.00 52.45 ? 947  HOH B O   1 
HETATM 5890 O O   . HOH L 5 .   ? -23.627 18.458 -29.894 1.00 39.77 ? 948  HOH B O   1 
HETATM 5891 O O   . HOH L 5 .   ? -41.301 44.558 -19.996 1.00 41.64 ? 949  HOH B O   1 
HETATM 5892 O O   . HOH L 5 .   ? -45.433 35.114 -53.853 1.00 28.82 ? 950  HOH B O   1 
HETATM 5893 O O   . HOH L 5 .   ? -46.001 16.735 -43.792 1.00 26.40 ? 951  HOH B O   1 
HETATM 5894 O O   . HOH L 5 .   ? -44.343 39.861 -25.595 1.00 40.53 ? 952  HOH B O   1 
HETATM 5895 O O   . HOH L 5 .   ? -36.267 41.399 -12.356 1.00 38.23 ? 953  HOH B O   1 
HETATM 5896 O O   . HOH L 5 .   ? -25.860 45.473 -26.812 1.00 38.97 ? 954  HOH B O   1 
HETATM 5897 O O   . HOH L 5 .   ? -46.692 37.077 -13.087 1.00 42.91 ? 955  HOH B O   1 
HETATM 5898 O O   . HOH L 5 .   ? -46.924 20.413 -50.276 1.00 34.35 ? 956  HOH B O   1 
HETATM 5899 O O   . HOH L 5 .   ? -37.858 32.820 -9.741  1.00 45.31 ? 957  HOH B O   1 
HETATM 5900 O O   . HOH L 5 .   ? -51.894 27.226 -35.087 1.00 30.69 ? 958  HOH B O   1 
HETATM 5901 O O   . HOH L 5 .   ? -24.960 13.907 -36.265 1.00 30.16 ? 959  HOH B O   1 
HETATM 5902 O O   . HOH L 5 .   ? -43.865 44.392 -45.618 1.00 49.50 ? 960  HOH B O   1 
HETATM 5903 O O   . HOH L 5 .   ? -48.388 30.275 -48.501 1.00 37.84 ? 961  HOH B O   1 
HETATM 5904 O O   . HOH L 5 .   ? -45.320 10.423 -9.302  1.00 38.29 ? 962  HOH B O   1 
HETATM 5905 O O   . HOH L 5 .   ? -27.438 32.552 -12.792 1.00 36.52 ? 963  HOH B O   1 
HETATM 5906 O O   . HOH L 5 .   ? -42.338 15.738 -47.629 1.00 40.72 ? 964  HOH B O   1 
HETATM 5907 O O   . HOH L 5 .   ? -21.576 12.780 -52.762 1.00 53.34 ? 965  HOH B O   1 
HETATM 5908 O O   . HOH L 5 .   ? -45.531 28.106 -50.445 1.00 29.87 ? 966  HOH B O   1 
HETATM 5909 O O   . HOH L 5 .   ? -19.082 15.900 -37.421 1.00 51.55 ? 967  HOH B O   1 
HETATM 5910 O O   . HOH L 5 .   ? -21.814 21.345 -21.864 1.00 40.05 ? 968  HOH B O   1 
HETATM 5911 O O   . HOH L 5 .   ? -30.310 9.612  -11.213 1.00 44.20 ? 969  HOH B O   1 
HETATM 5912 O O   . HOH L 5 .   ? -22.743 43.246 -41.438 1.00 30.19 ? 970  HOH B O   1 
HETATM 5913 O O   . HOH L 5 .   ? -27.048 45.764 -42.069 1.00 35.32 ? 971  HOH B O   1 
HETATM 5914 O O   . HOH L 5 .   ? -51.978 21.874 -36.880 1.00 35.44 ? 972  HOH B O   1 
HETATM 5915 O O   . HOH L 5 .   ? -18.167 23.867 -56.729 1.00 38.99 ? 973  HOH B O   1 
HETATM 5916 O O   . HOH L 5 .   ? -45.489 39.454 -23.940 1.00 49.16 ? 974  HOH B O   1 
HETATM 5917 O O   . HOH L 5 .   ? -15.292 14.485 -47.464 1.00 45.82 ? 975  HOH B O   1 
HETATM 5918 O O   . HOH L 5 .   ? -28.629 47.858 -27.953 1.00 38.51 ? 976  HOH B O   1 
HETATM 5919 O O   . HOH L 5 .   ? -45.942 38.901 -46.283 1.00 35.88 ? 977  HOH B O   1 
HETATM 5920 O O   . HOH L 5 .   ? -51.009 33.957 -30.344 1.00 50.17 ? 978  HOH B O   1 
HETATM 5921 O O   . HOH L 5 .   ? -51.178 34.688 -18.671 1.00 45.26 ? 979  HOH B O   1 
HETATM 5922 O O   . HOH L 5 .   ? -32.290 14.330 -55.938 1.00 42.92 ? 980  HOH B O   1 
HETATM 5923 O O   . HOH L 5 .   ? -37.208 5.238  -44.133 1.00 39.55 ? 981  HOH B O   1 
HETATM 5924 O O   . HOH L 5 .   ? -47.037 26.189 -49.592 1.00 34.69 ? 982  HOH B O   1 
HETATM 5925 O O   . HOH L 5 .   ? -44.670 43.721 -40.944 1.00 61.42 ? 983  HOH B O   1 
HETATM 5926 O O   . HOH L 5 .   ? -22.716 40.052 -22.576 1.00 35.33 ? 984  HOH B O   1 
HETATM 5927 O O   . HOH L 5 .   ? -24.758 22.707 -20.858 1.00 43.37 ? 985  HOH B O   1 
HETATM 5928 O O   . HOH L 5 .   ? -57.776 11.565 -35.181 1.00 35.30 ? 986  HOH B O   1 
HETATM 5929 O O   . HOH L 5 .   ? -37.480 10.048 -47.777 1.00 41.34 ? 987  HOH B O   1 
HETATM 5930 O O   . HOH L 5 .   ? -22.075 26.052 -54.764 1.00 41.95 ? 988  HOH B O   1 
HETATM 5931 O O   . HOH L 5 .   ? -24.593 43.190 -39.410 1.00 39.84 ? 989  HOH B O   1 
HETATM 5932 O O   . HOH L 5 .   ? -17.270 21.754 -31.321 1.00 49.56 ? 990  HOH B O   1 
HETATM 5933 O O   . HOH L 5 .   ? -51.550 32.509 -33.262 1.00 39.45 ? 991  HOH B O   1 
HETATM 5934 O O   . HOH L 5 .   ? -20.058 43.214 -37.952 1.00 45.34 ? 992  HOH B O   1 
HETATM 5935 O O   . HOH L 5 .   ? -13.009 39.212 -25.676 1.00 27.46 ? 993  HOH B O   1 
HETATM 5936 O O   . HOH L 5 .   ? -44.270 17.272 -51.331 1.00 34.03 ? 994  HOH B O   1 
HETATM 5937 O O   . HOH L 5 .   ? -48.490 8.820  -50.077 1.00 54.13 ? 995  HOH B O   1 
HETATM 5938 O O   . HOH L 5 .   ? -53.426 10.737 -44.396 1.00 48.86 ? 996  HOH B O   1 
HETATM 5939 O O   . HOH L 5 .   ? -21.531 19.404 -19.777 1.00 35.31 ? 997  HOH B O   1 
HETATM 5940 O O   . HOH L 5 .   ? -38.835 40.515 -28.681 1.00 21.69 ? 998  HOH B O   1 
HETATM 5941 O O   . HOH L 5 .   ? -19.486 20.798 -23.515 1.00 38.33 ? 999  HOH B O   1 
HETATM 5942 O O   . HOH L 5 .   ? -49.637 36.032 -30.462 1.00 53.96 ? 1000 HOH B O   1 
HETATM 5943 O O   . HOH L 5 .   ? -41.302 29.256 -9.266  1.00 26.80 ? 1001 HOH B O   1 
HETATM 5944 O O   . HOH L 5 .   ? -49.361 11.975 -15.568 1.00 38.10 ? 1002 HOH B O   1 
HETATM 5945 O O   . HOH L 5 .   ? -22.942 42.543 -23.608 1.00 36.81 ? 1003 HOH B O   1 
HETATM 5946 O O   . HOH L 5 .   ? -35.846 4.570  -14.423 1.00 35.50 ? 1004 HOH B O   1 
HETATM 5947 O O   . HOH L 5 .   ? -53.005 23.786 -35.972 1.00 38.79 ? 1005 HOH B O   1 
HETATM 5948 O O   . HOH L 5 .   ? -24.861 20.402 -24.676 1.00 42.89 ? 1006 HOH B O   1 
HETATM 5949 O O   . HOH L 5 .   ? -14.838 38.159 -31.597 1.00 35.56 ? 1007 HOH B O   1 
HETATM 5950 O O   . HOH L 5 .   ? -22.550 42.994 -36.852 1.00 36.93 ? 1008 HOH B O   1 
HETATM 5951 O O   . HOH L 5 .   ? -49.047 33.818 -51.237 1.00 42.00 ? 1009 HOH B O   1 
HETATM 5952 O O   . HOH L 5 .   ? -22.782 15.173 -24.961 1.00 34.66 ? 1010 HOH B O   1 
HETATM 5953 O O   . HOH L 5 .   ? -26.088 44.309 -35.265 1.00 36.53 ? 1011 HOH B O   1 
HETATM 5954 O O   . HOH L 5 .   ? -26.477 36.453 -52.998 1.00 45.18 ? 1012 HOH B O   1 
HETATM 5955 O O   . HOH L 5 .   ? -49.281 36.042 -40.607 1.00 41.48 ? 1013 HOH B O   1 
HETATM 5956 O O   . HOH L 5 .   ? -17.554 38.604 -23.789 1.00 33.17 ? 1014 HOH B O   1 
HETATM 5957 O O   . HOH L 5 .   ? -54.228 29.252 -17.879 1.00 39.44 ? 1015 HOH B O   1 
HETATM 5958 O O   . HOH L 5 .   ? -28.830 11.457 -12.980 1.00 32.22 ? 1016 HOH B O   1 
HETATM 5959 O O   . HOH L 5 .   ? -45.142 42.114 -22.880 1.00 45.02 ? 1017 HOH B O   1 
HETATM 5960 O O   . HOH L 5 .   ? -40.452 45.069 -41.849 1.00 38.22 ? 1018 HOH B O   1 
HETATM 5961 O O   . HOH L 5 .   ? -22.371 19.812 -36.908 1.00 31.53 ? 1019 HOH B O   1 
HETATM 5962 O O   . HOH L 5 .   ? -31.441 2.187  -36.661 1.00 47.50 ? 1020 HOH B O   1 
HETATM 5963 O O   . HOH L 5 .   ? -35.063 10.127 -8.332  1.00 36.05 ? 1021 HOH B O   1 
HETATM 5964 O O   . HOH L 5 .   ? -35.137 2.249  -41.815 1.00 43.46 ? 1022 HOH B O   1 
HETATM 5965 O O   . HOH L 5 .   ? -31.151 18.159 -8.402  1.00 42.04 ? 1023 HOH B O   1 
HETATM 5966 O O   . HOH L 5 .   ? -12.090 38.609 -28.214 1.00 38.91 ? 1024 HOH B O   1 
HETATM 5967 O O   . HOH L 5 .   ? -25.688 9.824  -27.266 1.00 43.98 ? 1025 HOH B O   1 
HETATM 5968 O O   . HOH L 5 .   ? -38.812 7.249  -44.659 1.00 25.55 ? 1026 HOH B O   1 
HETATM 5969 O O   . HOH L 5 .   ? -24.723 40.621 -51.382 1.00 57.13 ? 1027 HOH B O   1 
HETATM 5970 O O   . HOH L 5 .   ? -23.282 45.611 -35.369 1.00 35.83 ? 1028 HOH B O   1 
HETATM 5971 O O   . HOH L 5 .   ? -27.847 38.655 -50.722 1.00 41.78 ? 1029 HOH B O   1 
HETATM 5972 O O   . HOH L 5 .   ? -33.577 2.754  -39.061 1.00 42.45 ? 1030 HOH B O   1 
HETATM 5973 O O   . HOH L 5 .   ? -21.782 15.916 -34.267 1.00 53.04 ? 1031 HOH B O   1 
HETATM 5974 O O   . HOH L 5 .   ? -41.542 3.741  -42.797 1.00 44.29 ? 1032 HOH B O   1 
HETATM 5975 O O   . HOH L 5 .   ? -28.781 6.519  -26.688 1.00 37.53 ? 1033 HOH B O   1 
HETATM 5976 O O   . HOH L 5 .   ? -44.483 4.374  -41.399 1.00 39.61 ? 1034 HOH B O   1 
HETATM 5977 O O   . HOH L 5 .   ? -29.793 5.138  -30.618 1.00 42.31 ? 1035 HOH B O   1 
HETATM 5978 O O   . HOH L 5 .   ? -40.621 43.801 -46.901 1.00 40.83 ? 1036 HOH B O   1 
HETATM 5979 O O   . HOH L 5 .   ? -21.810 19.519 -31.562 1.00 25.26 ? 1037 HOH B O   1 
HETATM 5980 O O   . HOH L 5 .   ? -55.680 27.174 -21.644 1.00 40.05 ? 1038 HOH B O   1 
HETATM 5981 O O   . HOH L 5 .   ? -23.119 19.862 -15.548 1.00 38.51 ? 1039 HOH B O   1 
HETATM 5982 O O   . HOH L 5 .   ? -30.031 14.039 -53.489 1.00 37.48 ? 1040 HOH B O   1 
HETATM 5983 O O   . HOH L 5 .   ? -44.122 15.466 -49.418 1.00 39.81 ? 1041 HOH B O   1 
HETATM 5984 O O   . HOH L 5 .   ? -50.550 13.052 -17.758 1.00 40.84 ? 1042 HOH B O   1 
HETATM 5985 O O   . HOH L 5 .   ? -25.423 45.750 -30.650 1.00 40.51 ? 1043 HOH B O   1 
HETATM 5986 O O   . HOH L 5 .   ? -34.413 7.328  -12.189 1.00 44.62 ? 1044 HOH B O   1 
HETATM 5987 O O   . HOH L 5 .   ? -40.185 45.350 -28.022 1.00 36.22 ? 1045 HOH B O   1 
HETATM 5988 O O   . HOH L 5 .   ? -23.419 44.373 -27.775 1.00 32.92 ? 1046 HOH B O   1 
HETATM 5989 O O   . HOH L 5 .   ? -47.536 10.099 -11.836 1.00 52.44 ? 1047 HOH B O   1 
HETATM 5990 O O   . HOH L 5 .   ? -45.249 37.019 -30.116 1.00 29.11 ? 1048 HOH B O   1 
HETATM 5991 O O   . HOH L 5 .   ? -43.920 49.179 -36.615 1.00 48.43 ? 1049 HOH B O   1 
HETATM 5992 O O   . HOH L 5 .   ? -47.746 39.963 -41.024 1.00 56.40 ? 1050 HOH B O   1 
HETATM 5993 O O   . HOH L 5 .   ? -25.774 43.751 -22.809 1.00 32.55 ? 1051 HOH B O   1 
HETATM 5994 O O   . HOH L 5 .   ? -41.073 11.664 -48.840 1.00 43.52 ? 1052 HOH B O   1 
HETATM 5995 O O   . HOH L 5 .   ? -24.382 12.628 -54.722 1.00 49.73 ? 1053 HOH B O   1 
HETATM 5996 O O   . HOH L 5 .   ? -21.970 22.205 -54.761 1.00 31.34 ? 1054 HOH B O   1 
HETATM 5997 O O   . HOH L 5 .   ? -31.067 -1.513 -28.380 1.00 43.07 ? 1055 HOH B O   1 
HETATM 5998 O O   . HOH L 5 .   ? -44.314 43.708 -26.695 1.00 40.57 ? 1056 HOH B O   1 
HETATM 5999 O O   . HOH L 5 .   ? -40.741 46.155 -21.920 1.00 26.40 ? 1057 HOH B O   1 
HETATM 6000 O O   . HOH L 5 .   ? -31.689 9.691  -7.225  1.00 47.27 ? 1058 HOH B O   1 
HETATM 6001 O O   . HOH L 5 .   ? -53.612 24.970 -18.534 1.00 33.47 ? 1059 HOH B O   1 
HETATM 6002 O O   . HOH L 5 .   ? -32.215 5.643  -12.045 1.00 46.61 ? 1060 HOH B O   1 
HETATM 6003 O O   . HOH L 5 .   ? -49.445 37.199 -42.185 1.00 52.90 ? 1061 HOH B O   1 
HETATM 6004 O O   . HOH L 5 .   ? -43.557 39.412 -53.429 1.00 37.77 ? 1062 HOH B O   1 
HETATM 6005 O O   . HOH L 5 .   ? -44.722 40.315 -20.813 1.00 57.05 ? 1063 HOH B O   1 
HETATM 6006 O O   . HOH L 5 .   ? -29.833 6.627  -11.783 1.00 52.16 ? 1064 HOH B O   1 
HETATM 6007 O O   . HOH L 5 .   ? -14.896 23.126 -29.177 1.00 29.76 ? 1065 HOH B O   1 
HETATM 6008 O O   . HOH L 5 .   ? -52.205 22.633 -18.956 1.00 27.25 ? 1066 HOH B O   1 
HETATM 6009 O O   . HOH L 5 .   ? -23.848 16.626 -54.050 1.00 37.56 ? 1067 HOH B O   1 
HETATM 6010 O O   . HOH L 5 .   ? -14.860 36.599 -33.878 1.00 39.32 ? 1068 HOH B O   1 
HETATM 6011 O O   . HOH L 5 .   ? -50.832 29.244 -44.892 1.00 34.56 ? 1069 HOH B O   1 
HETATM 6012 O O   . HOH L 5 .   ? -8.811  27.710 -40.499 1.00 40.35 ? 1070 HOH B O   1 
HETATM 6013 O O   . HOH L 5 .   ? -49.666 7.772  -19.218 1.00 46.39 ? 1071 HOH B O   1 
HETATM 6014 O O   . HOH L 5 .   ? -21.783 20.160 -52.345 1.00 31.76 ? 1072 HOH B O   1 
HETATM 6015 O O   . HOH L 5 .   ? -31.037 3.594  -21.626 1.00 35.39 ? 1073 HOH B O   1 
HETATM 6016 O O   . HOH L 5 .   ? -42.829 45.787 -23.591 1.00 39.52 ? 1074 HOH B O   1 
HETATM 6017 O O   . HOH L 5 .   ? -21.385 18.597 -34.265 1.00 35.06 ? 1075 HOH B O   1 
HETATM 6018 O O   . HOH L 5 .   ? -13.669 11.828 -46.993 1.00 36.10 ? 1076 HOH B O   1 
HETATM 6019 O O   . HOH L 5 .   ? -21.180 44.075 -22.718 1.00 49.29 ? 1077 HOH B O   1 
HETATM 6020 O O   . HOH L 5 .   ? -27.602 8.542  -30.125 1.00 39.74 ? 1078 HOH B O   1 
HETATM 6021 O O   . HOH L 5 .   ? -23.739 12.932 -33.765 1.00 48.79 ? 1079 HOH B O   1 
HETATM 6022 O O   . HOH L 5 .   ? -24.920 12.592 -28.741 1.00 44.49 ? 1080 HOH B O   1 
HETATM 6023 O O   . HOH L 5 .   ? -21.785 46.343 -23.701 1.00 53.13 ? 1081 HOH B O   1 
HETATM 6024 O O   . HOH L 5 .   ? -24.801 8.285  -33.499 1.00 39.09 ? 1082 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   . LYS A 3   ? 0.5482 0.6094 0.5986 0.0606  -0.0122 -0.0377 2   LYS A N   
2    C CA  . LYS A 3   ? 0.4349 0.4839 0.4813 0.0580  -0.0126 -0.0358 2   LYS A CA  
3    C C   . LYS A 3   ? 0.3902 0.4392 0.4360 0.0545  -0.0091 -0.0384 2   LYS A C   
4    O O   . LYS A 3   ? 0.3929 0.4510 0.4407 0.0520  -0.0063 -0.0406 2   LYS A O   
5    C CB  . LYS A 3   ? 0.3712 0.4168 0.4159 0.0537  -0.0137 -0.0317 2   LYS A CB  
6    C CG  . LYS A 3   ? 0.5446 0.6007 0.5919 0.0498  -0.0117 -0.0315 2   LYS A CG  
7    C CD  . LYS A 3   ? 0.5396 0.5924 0.5852 0.0456  -0.0128 -0.0276 2   LYS A CD  
8    C CE  . LYS A 3   ? 0.5620 0.6247 0.6101 0.0414  -0.0106 -0.0277 2   LYS A CE  
9    N NZ  . LYS A 3   ? 0.4482 0.5153 0.4971 0.0394  -0.0072 -0.0312 2   LYS A NZ  
10   N N   . VAL A 4   ? 0.2413 0.2795 0.2838 0.0541  -0.0095 -0.0382 3   VAL A N   
11   C CA  . VAL A 4   ? 0.2559 0.2925 0.2972 0.0510  -0.0065 -0.0406 3   VAL A CA  
12   C C   . VAL A 4   ? 0.2483 0.2860 0.2886 0.0446  -0.0048 -0.0394 3   VAL A C   
13   O O   . VAL A 4   ? 0.2720 0.3144 0.3124 0.0416  -0.0021 -0.0417 3   VAL A O   
14   C CB  . VAL A 4   ? 0.2448 0.2693 0.2828 0.0526  -0.0076 -0.0406 3   VAL A CB  
15   C CG1 . VAL A 4   ? 0.2428 0.2647 0.2790 0.0488  -0.0048 -0.0426 3   VAL A CG1 
16   C CG2 . VAL A 4   ? 0.2771 0.3015 0.3162 0.0589  -0.0090 -0.0426 3   VAL A CG2 
17   N N   . PHE A 5   ? 0.1872 0.2206 0.2263 0.0425  -0.0066 -0.0360 4   PHE A N   
18   C CA  . PHE A 5   ? 0.1689 0.2022 0.2069 0.0368  -0.0055 -0.0349 4   PHE A CA  
19   C C   . PHE A 5   ? 0.1764 0.2175 0.2166 0.0352  -0.0060 -0.0328 4   PHE A C   
20   O O   . PHE A 5   ? 0.2275 0.2710 0.2692 0.0383  -0.0080 -0.0312 4   PHE A O   
21   C CB  . PHE A 5   ? 0.1927 0.2147 0.2273 0.0351  -0.0070 -0.0330 4   PHE A CB  
22   C CG  . PHE A 5   ? 0.1745 0.1882 0.2067 0.0362  -0.0065 -0.0349 4   PHE A CG  
23   C CD1 . PHE A 5   ? 0.1924 0.2063 0.2235 0.0335  -0.0041 -0.0376 4   PHE A CD1 
24   C CD2 . PHE A 5   ? 0.1811 0.1862 0.2116 0.0398  -0.0086 -0.0341 4   PHE A CD2 
25   C CE1 . PHE A 5   ? 0.2007 0.2069 0.2295 0.0345  -0.0036 -0.0394 4   PHE A CE1 
26   C CE2 . PHE A 5   ? 0.2182 0.2155 0.2464 0.0408  -0.0081 -0.0359 4   PHE A CE2 
27   C CZ  . PHE A 5   ? 0.2111 0.2092 0.2386 0.0381  -0.0055 -0.0386 4   PHE A CZ  
28   N N   . GLN A 6   ? 0.1637 0.2083 0.2039 0.0302  -0.0046 -0.0327 5   GLN A N   
29   C CA  . GLN A 6   ? 0.1878 0.2385 0.2297 0.0281  -0.0052 -0.0304 5   GLN A CA  
30   C C   . GLN A 6   ? 0.1954 0.2397 0.2360 0.0284  -0.0081 -0.0270 5   GLN A C   
31   O O   . GLN A 6   ? 0.2073 0.2556 0.2494 0.0295  -0.0096 -0.0248 5   GLN A O   
32   C CB  . GLN A 6   ? 0.2064 0.2603 0.2480 0.0227  -0.0034 -0.0311 5   GLN A CB  
33   C CG  . GLN A 6   ? 0.1773 0.2381 0.2207 0.0200  -0.0039 -0.0289 5   GLN A CG  
34   C CD  . GLN A 6   ? 0.1881 0.2525 0.2311 0.0151  -0.0022 -0.0302 5   GLN A CD  
35   O OE1 . GLN A 6   ? 0.2118 0.2726 0.2524 0.0136  -0.0008 -0.0326 5   GLN A OE1 
36   N NE2 . GLN A 6   ? 0.1660 0.2372 0.2108 0.0127  -0.0024 -0.0287 5   GLN A NE2 
37   N N   . TRP A 7   ? 0.1953 0.2296 0.2328 0.0272  -0.0089 -0.0264 6   TRP A N   
38   C CA  . TRP A 7   ? 0.1818 0.2094 0.2172 0.0264  -0.0113 -0.0234 6   TRP A CA  
39   C C   . TRP A 7   ? 0.1871 0.2037 0.2195 0.0289  -0.0126 -0.0234 6   TRP A C   
40   O O   . TRP A 7   ? 0.2005 0.2128 0.2316 0.0285  -0.0113 -0.0256 6   TRP A O   
41   C CB  . TRP A 7   ? 0.1969 0.2240 0.2314 0.0208  -0.0109 -0.0227 6   TRP A CB  
42   C CG  . TRP A 7   ? 0.1653 0.2021 0.2024 0.0180  -0.0102 -0.0220 6   TRP A CG  
43   C CD1 . TRP A 7   ? 0.1605 0.2029 0.1994 0.0187  -0.0114 -0.0197 6   TRP A CD1 
44   C CD2 . TRP A 7   ? 0.1487 0.1905 0.1866 0.0141  -0.0084 -0.0237 6   TRP A CD2 
45   N NE1 . TRP A 7   ? 0.1899 0.2406 0.2308 0.0153  -0.0102 -0.0198 6   TRP A NE1 
46   C CE2 . TRP A 7   ? 0.1616 0.2121 0.2019 0.0124  -0.0084 -0.0222 6   TRP A CE2 
47   C CE3 . TRP A 7   ? 0.1539 0.1930 0.1902 0.0118  -0.0069 -0.0263 6   TRP A CE3 
48   C CZ2 . TRP A 7   ? 0.1626 0.2193 0.2040 0.0086  -0.0071 -0.0233 6   TRP A CZ2 
49   C CZ3 . TRP A 7   ? 0.1773 0.2223 0.2144 0.0081  -0.0057 -0.0274 6   TRP A CZ3 
50   C CH2 . TRP A 7   ? 0.1673 0.2211 0.2069 0.0066  -0.0058 -0.0259 6   TRP A CH2 
51   N N   . PHE A 8   ? 0.1871 0.1987 0.2179 0.0314  -0.0153 -0.0209 7   PHE A N   
52   C CA  . PHE A 8   ? 0.1855 0.1856 0.2128 0.0331  -0.0169 -0.0205 7   PHE A CA  
53   C C   . PHE A 8   ? 0.2109 0.2054 0.2354 0.0326  -0.0198 -0.0170 7   PHE A C   
54   O O   . PHE A 8   ? 0.2318 0.2293 0.2568 0.0349  -0.0216 -0.0153 7   PHE A O   
55   C CB  . PHE A 8   ? 0.2168 0.2154 0.2445 0.0388  -0.0171 -0.0225 7   PHE A CB  
56   C CG  . PHE A 8   ? 0.2384 0.2257 0.2627 0.0403  -0.0180 -0.0229 7   PHE A CG  
57   C CD1 . PHE A 8   ? 0.3310 0.3097 0.3521 0.0426  -0.0211 -0.0206 7   PHE A CD1 
58   C CD2 . PHE A 8   ? 0.2578 0.2426 0.2817 0.0391  -0.0159 -0.0255 7   PHE A CD2 
59   C CE1 . PHE A 8   ? 0.3642 0.3323 0.3820 0.0438  -0.0219 -0.0209 7   PHE A CE1 
60   C CE2 . PHE A 8   ? 0.2825 0.2569 0.3033 0.0403  -0.0167 -0.0258 7   PHE A CE2 
61   C CZ  . PHE A 8   ? 0.2650 0.2313 0.2830 0.0427  -0.0196 -0.0236 7   PHE A CZ  
62   N N   . GLY A 9   ? 0.2177 0.2043 0.2389 0.0293  -0.0205 -0.0159 8   GLY A N   
63   C CA  . GLY A 9   ? 0.2017 0.1837 0.2198 0.0276  -0.0230 -0.0125 8   GLY A CA  
64   C C   . GLY A 9   ? 0.2422 0.2145 0.2563 0.0243  -0.0237 -0.0117 8   GLY A C   
65   O O   . GLY A 9   ? 0.2241 0.1900 0.2368 0.0255  -0.0232 -0.0134 8   GLY A O   
66   N N   . SER A 10  ? 0.2476 0.2188 0.2596 0.0200  -0.0248 -0.0093 9   SER A N   
67   C CA  . SER A 10  ? 0.2225 0.1844 0.2302 0.0168  -0.0258 -0.0084 9   SER A CA  
68   C C   . SER A 10  ? 0.2031 0.1689 0.2108 0.0105  -0.0252 -0.0077 9   SER A C   
69   O O   . SER A 10  ? 0.2142 0.1874 0.2237 0.0089  -0.0253 -0.0063 9   SER A O   
70   C CB  . SER A 10  ? 0.2346 0.1869 0.2373 0.0192  -0.0290 -0.0056 9   SER A CB  
71   O OG  . SER A 10  ? 0.2703 0.2130 0.2682 0.0160  -0.0299 -0.0049 9   SER A OG  
72   N N   . ASN A 11  ? 0.2102 0.1713 0.2161 0.0069  -0.0246 -0.0088 10  ASN A N   
73   C CA  . ASN A 11  ? 0.2152 0.1778 0.2199 0.0009  -0.0248 -0.0080 10  ASN A CA  
74   C C   . ASN A 11  ? 0.2677 0.2245 0.2676 -0.0004 -0.0274 -0.0043 10  ASN A C   
75   O O   . ASN A 11  ? 0.2560 0.2040 0.2521 0.0029  -0.0293 -0.0028 10  ASN A O   
76   C CB  . ASN A 11  ? 0.2370 0.1956 0.2406 -0.0022 -0.0238 -0.0105 10  ASN A CB  
77   C CG  . ASN A 11  ? 0.2075 0.1728 0.2154 -0.0025 -0.0214 -0.0140 10  ASN A CG  
78   O OD1 . ASN A 11  ? 0.1971 0.1696 0.2072 -0.0063 -0.0206 -0.0151 10  ASN A OD1 
79   N ND2 . ASN A 11  ? 0.1980 0.1608 0.2067 0.0015  -0.0205 -0.0160 10  ASN A ND2 
80   N N   . GLU A 12  ? 0.2250 0.1867 0.2248 -0.0052 -0.0276 -0.0030 11  GLU A N   
81   C CA  . GLU A 12  ? 0.2168 0.1737 0.2116 -0.0075 -0.0300 0.0006  11  GLU A CA  
82   C C   . GLU A 12  ? 0.2288 0.1859 0.2218 -0.0145 -0.0295 0.0000  11  GLU A C   
83   O O   . GLU A 12  ? 0.2548 0.2202 0.2501 -0.0185 -0.0287 0.0000  11  GLU A O   
84   C CB  . GLU A 12  ? 0.2177 0.1813 0.2141 -0.0065 -0.0309 0.0028  11  GLU A CB  
85   C CG  . GLU A 12  ? 0.2518 0.2138 0.2488 0.0005  -0.0321 0.0035  11  GLU A CG  
86   C CD  . GLU A 12  ? 0.3140 0.2641 0.3044 0.0026  -0.0354 0.0062  11  GLU A CD  
87   O OE1 . GLU A 12  ? 0.2607 0.2043 0.2457 -0.0019 -0.0367 0.0081  11  GLU A OE1 
88   O OE2 . GLU A 12  ? 0.2813 0.2285 0.2717 0.0088  -0.0367 0.0062  11  GLU A OE2 
89   N N   . SER A 13  ? 0.2487 0.1969 0.2379 -0.0158 -0.0298 -0.0006 12  SER A N   
90   C CA  A SER A 13  ? 0.2703 0.2187 0.2584 -0.0220 -0.0290 -0.0022 12  SER A CA  
91   C CA  B SER A 13  ? 0.2701 0.2186 0.2582 -0.0220 -0.0290 -0.0022 12  SER A CA  
92   C C   . SER A 13  ? 0.3410 0.2845 0.3231 -0.0269 -0.0308 0.0007  12  SER A C   
93   O O   . SER A 13  ? 0.3107 0.2462 0.2877 -0.0251 -0.0331 0.0039  12  SER A O   
94   C CB  A SER A 13  ? 0.2422 0.1838 0.2294 -0.0207 -0.0283 -0.0048 12  SER A CB  
95   C CB  B SER A 13  ? 0.2426 0.1845 0.2298 -0.0210 -0.0282 -0.0049 12  SER A CB  
96   O OG  A SER A 13  ? 0.2753 0.2167 0.2613 -0.0263 -0.0276 -0.0067 12  SER A OG  
97   O OG  B SER A 13  ? 0.2539 0.1999 0.2461 -0.0169 -0.0265 -0.0076 12  SER A OG  
98   N N   . GLY A 14  ? 0.2479 0.1961 0.2301 -0.0334 -0.0299 -0.0006 13  GLY A N   
99   C CA  . GLY A 14  ? 0.2985 0.2427 0.2748 -0.0392 -0.0313 0.0017  13  GLY A CA  
100  C C   . GLY A 14  ? 0.2838 0.2383 0.2625 -0.0455 -0.0301 0.0004  13  GLY A C   
101  O O   . GLY A 14  ? 0.2676 0.2205 0.2427 -0.0516 -0.0302 0.0000  13  GLY A O   
102  N N   . ALA A 15  ? 0.2562 0.2215 0.2408 -0.0443 -0.0291 -0.0003 14  ALA A N   
103  C CA  . ALA A 15  ? 0.2164 0.1919 0.2034 -0.0501 -0.0282 -0.0014 14  ALA A CA  
104  C C   . ALA A 15  ? 0.2591 0.2391 0.2489 -0.0534 -0.0265 -0.0061 14  ALA A C   
105  O O   . ALA A 15  ? 0.2622 0.2492 0.2528 -0.0591 -0.0260 -0.0075 14  ALA A O   
106  C CB  . ALA A 15  ? 0.2243 0.2099 0.2167 -0.0477 -0.0276 -0.0009 14  ALA A CB  
107  N N   . GLU A 16  ? 0.2598 0.2358 0.2509 -0.0499 -0.0258 -0.0087 15  GLU A N   
108  C CA  . GLU A 16  ? 0.3008 0.2798 0.2943 -0.0521 -0.0245 -0.0134 15  GLU A CA  
109  C C   . GLU A 16  ? 0.2888 0.2587 0.2772 -0.0549 -0.0250 -0.0140 15  GLU A C   
110  O O   . GLU A 16  ? 0.3192 0.2903 0.3090 -0.0564 -0.0241 -0.0180 15  GLU A O   
111  C CB  . GLU A 16  ? 0.2167 0.1975 0.2150 -0.0466 -0.0234 -0.0161 15  GLU A CB  
112  C CG  . GLU A 16  ? 0.2806 0.2508 0.2767 -0.0420 -0.0236 -0.0163 15  GLU A CG  
113  C CD  . GLU A 16  ? 0.2989 0.2618 0.2922 -0.0374 -0.0247 -0.0122 15  GLU A CD  
114  O OE1 . GLU A 16  ? 0.2433 0.2076 0.2352 -0.0380 -0.0258 -0.0087 15  GLU A OE1 
115  O OE2 . GLU A 16  ? 0.2742 0.2299 0.2666 -0.0329 -0.0248 -0.0126 15  GLU A OE2 
116  N N   . PHE A 17  ? 0.2660 0.2267 0.2480 -0.0557 -0.0265 -0.0101 16  PHE A N   
117  C CA  . PHE A 17  ? 0.3432 0.2943 0.3196 -0.0583 -0.0270 -0.0104 16  PHE A CA  
118  C C   . PHE A 17  ? 0.3605 0.3163 0.3356 -0.0662 -0.0265 -0.0126 16  PHE A C   
119  O O   . PHE A 17  ? 0.3232 0.2882 0.3002 -0.0701 -0.0261 -0.0128 16  PHE A O   
120  C CB  . PHE A 17  ? 0.3151 0.2548 0.2844 -0.0573 -0.0292 -0.0055 16  PHE A CB  
121  C CG  . PHE A 17  ? 0.3357 0.2672 0.3046 -0.0498 -0.0299 -0.0042 16  PHE A CG  
122  C CD1 . PHE A 17  ? 0.3704 0.3065 0.3456 -0.0443 -0.0286 -0.0066 16  PHE A CD1 
123  C CD2 . PHE A 17  ? 0.3655 0.2847 0.3274 -0.0483 -0.0321 -0.0008 16  PHE A CD2 
124  C CE1 . PHE A 17  ? 0.3200 0.2491 0.2948 -0.0376 -0.0293 -0.0056 16  PHE A CE1 
125  C CE2 . PHE A 17  ? 0.4314 0.3435 0.3931 -0.0413 -0.0329 0.0001  16  PHE A CE2 
126  C CZ  . PHE A 17  ? 0.3275 0.2449 0.2959 -0.0359 -0.0314 -0.0024 16  PHE A CZ  
127  N N   . GLY A 18  ? 0.4091 0.3585 0.3808 -0.0686 -0.0264 -0.0144 17  GLY A N   
128  C CA  . GLY A 18  ? 0.4704 0.4237 0.4404 -0.0763 -0.0258 -0.0169 17  GLY A CA  
129  C C   . GLY A 18  ? 0.3667 0.3339 0.3435 -0.0785 -0.0244 -0.0214 17  GLY A C   
130  O O   . GLY A 18  ? 0.4041 0.3788 0.3808 -0.0845 -0.0242 -0.0219 17  GLY A O   
131  N N   . SER A 19  ? 0.3845 0.3553 0.3671 -0.0737 -0.0236 -0.0248 18  SER A N   
132  C CA  . SER A 19  ? 0.4029 0.3863 0.3922 -0.0743 -0.0227 -0.0287 18  SER A CA  
133  C C   . SER A 19  ? 0.5054 0.4955 0.4954 -0.0806 -0.0221 -0.0335 18  SER A C   
134  O O   . SER A 19  ? 0.4773 0.4787 0.4722 -0.0821 -0.0217 -0.0367 18  SER A O   
135  C CB  . SER A 19  ? 0.3593 0.3430 0.3533 -0.0677 -0.0222 -0.0312 18  SER A CB  
136  O OG  . SER A 19  ? 0.5240 0.5000 0.5163 -0.0662 -0.0221 -0.0336 18  SER A OG  
137  N N   . GLN A 20  ? 0.5001 0.4839 0.4855 -0.0841 -0.0222 -0.0343 19  GLN A N   
138  C CA  . GLN A 20  ? 0.4338 0.4244 0.4197 -0.0904 -0.0216 -0.0392 19  GLN A CA  
139  C C   . GLN A 20  ? 0.5338 0.5308 0.5176 -0.0976 -0.0216 -0.0377 19  GLN A C   
140  O O   . GLN A 20  ? 0.5733 0.5786 0.5584 -0.1032 -0.0211 -0.0420 19  GLN A O   
141  C CB  . GLN A 20  ? 0.6403 0.6222 0.6220 -0.0919 -0.0216 -0.0408 19  GLN A CB  
142  C CG  . GLN A 20  ? 0.7124 0.6843 0.6858 -0.0960 -0.0222 -0.0363 19  GLN A CG  
143  C CD  . GLN A 20  ? 0.6430 0.6038 0.6126 -0.0908 -0.0233 -0.0302 19  GLN A CD  
144  O OE1 . GLN A 20  ? 0.6171 0.5760 0.5902 -0.0837 -0.0234 -0.0296 19  GLN A OE1 
145  N NE2 . GLN A 20  ? 0.6500 0.6037 0.6124 -0.0945 -0.0243 -0.0257 19  GLN A NE2 
146  N N   . ASN A 21  ? 0.4156 0.4091 0.3961 -0.0974 -0.0223 -0.0321 20  ASN A N   
147  C CA  . ASN A 21  ? 0.4179 0.4163 0.3957 -0.1040 -0.0225 -0.0301 20  ASN A CA  
148  C C   . ASN A 21  ? 0.4458 0.4537 0.4291 -0.1016 -0.0224 -0.0292 20  ASN A C   
149  O O   . ASN A 21  ? 0.3940 0.3978 0.3769 -0.0970 -0.0231 -0.0248 20  ASN A O   
150  C CB  . ASN A 21  ? 0.4717 0.4580 0.4408 -0.1058 -0.0237 -0.0242 20  ASN A CB  
151  C CG  . ASN A 21  ? 0.6203 0.5981 0.5831 -0.1101 -0.0237 -0.0252 20  ASN A CG  
152  O OD1 . ASN A 21  ? 0.6679 0.6381 0.6228 -0.1147 -0.0246 -0.0216 20  ASN A OD1 
153  N ND2 . ASN A 21  ? 0.6718 0.6506 0.6376 -0.1089 -0.0229 -0.0301 20  ASN A ND2 
154  N N   . LEU A 22  ? 0.4134 0.4534 0.4243 -0.0635 0.0421  0.0001  21  LEU A N   
155  C CA  . LEU A 22  ? 0.3338 0.3728 0.3444 -0.0593 0.0423  0.0008  21  LEU A CA  
156  C C   . LEU A 22  ? 0.4589 0.4965 0.4634 -0.0662 0.0484  -0.0016 21  LEU A C   
157  O O   . LEU A 22  ? 0.4272 0.4758 0.4390 -0.0705 0.0534  -0.0060 21  LEU A O   
158  C CB  . LEU A 22  ? 0.3789 0.4319 0.4050 -0.0518 0.0414  -0.0009 21  LEU A CB  
159  C CG  . LEU A 22  ? 0.4415 0.4946 0.4723 -0.0441 0.0353  0.0017  21  LEU A CG  
160  C CD1 . LEU A 22  ? 0.3417 0.4076 0.3864 -0.0376 0.0347  0.0000  21  LEU A CD1 
161  C CD2 . LEU A 22  ? 0.4144 0.4538 0.4346 -0.0412 0.0318  0.0056  21  LEU A CD2 
162  N N   . PRO A 23  ? 0.3992 0.4242 0.3908 -0.0678 0.0483  0.0009  22  PRO A N   
163  C CA  . PRO A 23  ? 0.3201 0.3329 0.3035 -0.0628 0.0425  0.0058  22  PRO A CA  
164  C C   . PRO A 23  ? 0.3544 0.3557 0.3296 -0.0636 0.0380  0.0092  22  PRO A C   
165  O O   . PRO A 23  ? 0.3154 0.3102 0.2888 -0.0578 0.0325  0.0125  22  PRO A O   
166  C CB  . PRO A 23  ? 0.3543 0.3579 0.3255 -0.0669 0.0449  0.0065  22  PRO A CB  
167  C CG  . PRO A 23  ? 0.4614 0.4680 0.4299 -0.0762 0.0519  0.0026  22  PRO A CG  
168  C CD  . PRO A 23  ? 0.3690 0.3929 0.3545 -0.0746 0.0545  -0.0017 22  PRO A CD  
169  N N   . GLY A 24  ? 0.3714 0.3696 0.3415 -0.0707 0.0403  0.0082  23  GLY A N   
170  C CA  . GLY A 24  ? 0.4232 0.4080 0.3835 -0.0721 0.0366  0.0114  23  GLY A CA  
171  C C   . GLY A 24  ? 0.3981 0.3655 0.3417 -0.0745 0.0347  0.0151  23  GLY A C   
172  O O   . GLY A 24  ? 0.4070 0.3728 0.3466 -0.0748 0.0358  0.0155  23  GLY A O   
173  N N   . VAL A 25  ? 0.3375 0.2911 0.2710 -0.0764 0.0316  0.0181  24  VAL A N   
174  C CA  . VAL A 25  ? 0.3867 0.3219 0.3027 -0.0795 0.0293  0.0219  24  VAL A CA  
175  C C   . VAL A 25  ? 0.4405 0.3655 0.3543 -0.0726 0.0220  0.0261  24  VAL A C   
176  O O   . VAL A 25  ? 0.3934 0.3169 0.3102 -0.0711 0.0204  0.0261  24  VAL A O   
177  C CB  . VAL A 25  ? 0.5088 0.4343 0.4118 -0.0900 0.0331  0.0214  24  VAL A CB  
178  C CG1 . VAL A 25  ? 0.5650 0.4700 0.4490 -0.0929 0.0299  0.0260  24  VAL A CG1 
179  C CG2 . VAL A 25  ? 0.5226 0.4595 0.4289 -0.0971 0.0409  0.0165  24  VAL A CG2 
180  N N   . GLU A 26  ? 0.3821 0.3005 0.2911 -0.0685 0.0179  0.0292  25  GLU A N   
181  C CA  . GLU A 26  ? 0.4172 0.3262 0.3246 -0.0617 0.0108  0.0329  25  GLU A CA  
182  C C   . GLU A 26  ? 0.4717 0.3637 0.3662 -0.0658 0.0089  0.0354  25  GLU A C   
183  O O   . GLU A 26  ? 0.4646 0.3457 0.3448 -0.0733 0.0107  0.0366  25  GLU A O   
184  C CB  . GLU A 26  ? 0.4084 0.3131 0.3115 -0.0579 0.0068  0.0357  25  GLU A CB  
185  C CG  . GLU A 26  ? 0.4067 0.3046 0.3110 -0.0499 -0.0006 0.0389  25  GLU A CG  
186  C CD  . GLU A 26  ? 0.5545 0.4334 0.4450 -0.0518 -0.0049 0.0428  25  GLU A CD  
187  O OE1 . GLU A 26  ? 0.5333 0.4014 0.4092 -0.0589 -0.0038 0.0446  25  GLU A OE1 
188  O OE2 . GLU A 26  ? 0.4777 0.3517 0.3714 -0.0465 -0.0092 0.0439  25  GLU A OE2 
189  N N   . GLY A 27  ? 0.4091 0.2980 0.3081 -0.0609 0.0054  0.0362  26  GLY A N   
190  C CA  . GLY A 27  ? 0.4693 0.3420 0.3573 -0.0639 0.0036  0.0383  26  GLY A CA  
191  C C   . GLY A 27  ? 0.5041 0.3793 0.3922 -0.0707 0.0089  0.0353  26  GLY A C   
192  O O   . GLY A 27  ? 0.4836 0.3455 0.3632 -0.0733 0.0079  0.0366  26  GLY A O   
193  N N   . LYS A 28  ? 0.4287 0.3202 0.3260 -0.0737 0.0144  0.0312  27  LYS A N   
194  C CA  A LYS A 28  ? 0.4954 0.3927 0.3953 -0.0800 0.0193  0.0278  27  LYS A CA  
195  C CA  B LYS A 28  ? 0.4957 0.3930 0.3957 -0.0800 0.0193  0.0278  27  LYS A CA  
196  C C   . LYS A 28  ? 0.4622 0.3781 0.3801 -0.0755 0.0203  0.0244  27  LYS A C   
197  O O   . LYS A 28  ? 0.4597 0.3764 0.3812 -0.0756 0.0203  0.0232  27  LYS A O   
198  C CB  A LYS A 28  ? 0.5303 0.4297 0.4235 -0.0898 0.0256  0.0256  27  LYS A CB  
199  C CB  B LYS A 28  ? 0.5304 0.4300 0.4237 -0.0897 0.0256  0.0256  27  LYS A CB  
200  C CG  A LYS A 28  ? 0.5957 0.5038 0.4930 -0.0967 0.0311  0.0213  27  LYS A CG  
201  C CG  B LYS A 28  ? 0.5951 0.5026 0.4919 -0.0969 0.0311  0.0214  27  LYS A CG  
202  C CD  A LYS A 28  ? 0.6669 0.5795 0.5598 -0.1060 0.0377  0.0183  27  LYS A CD  
203  C CD  B LYS A 28  ? 0.6651 0.5764 0.5569 -0.1063 0.0377  0.0185  27  LYS A CD  
204  C CE  A LYS A 28  ? 0.6704 0.5930 0.5685 -0.1131 0.0432  0.0136  27  LYS A CE  
205  C CE  B LYS A 28  ? 0.6699 0.5899 0.5656 -0.1138 0.0432  0.0140  27  LYS A CE  
206  N NZ  A LYS A 28  ? 0.7513 0.6591 0.6378 -0.1183 0.0428  0.0149  27  LYS A NZ  
207  N NZ  B LYS A 28  ? 0.6727 0.6128 0.5880 -0.1085 0.0432  0.0108  27  LYS A NZ  
208  N N   . ASP A 29  ? 0.3877 0.3179 0.3163 -0.0715 0.0211  0.0229  28  ASP A N   
209  C CA  . ASP A 29  ? 0.3529 0.2999 0.2977 -0.0669 0.0213  0.0201  28  ASP A CA  
210  C C   . ASP A 29  ? 0.3515 0.2994 0.3032 -0.0574 0.0161  0.0218  28  ASP A C   
211  O O   . ASP A 29  ? 0.3450 0.3014 0.3068 -0.0539 0.0152  0.0202  28  ASP A O   
212  C CB  . ASP A 29  ? 0.4349 0.3976 0.3883 -0.0682 0.0256  0.0169  28  ASP A CB  
213  C CG  . ASP A 29  ? 0.4308 0.3954 0.3798 -0.0778 0.0315  0.0142  28  ASP A CG  
214  O OD1 . ASP A 29  ? 0.4996 0.4674 0.4507 -0.0819 0.0332  0.0122  28  ASP A OD1 
215  O OD2 . ASP A 29  ? 0.4293 0.3922 0.3724 -0.0818 0.0345  0.0138  28  ASP A OD2 
216  N N   . TYR A 30  ? 0.3564 0.2956 0.3022 -0.0536 0.0127  0.0248  29  TYR A N   
217  C CA  . TYR A 30  ? 0.3505 0.2913 0.3030 -0.0450 0.0080  0.0260  29  TYR A CA  
218  C C   . TYR A 30  ? 0.3020 0.2274 0.2441 -0.0428 0.0035  0.0298  29  TYR A C   
219  O O   . TYR A 30  ? 0.3657 0.2803 0.2954 -0.0479 0.0040  0.0318  29  TYR A O   
220  C CB  . TYR A 30  ? 0.3141 0.2688 0.2764 -0.0411 0.0091  0.0244  29  TYR A CB  
221  C CG  . TYR A 30  ? 0.3211 0.2745 0.2773 -0.0437 0.0109  0.0251  29  TYR A CG  
222  C CD1 . TYR A 30  ? 0.2882 0.2332 0.2378 -0.0408 0.0072  0.0280  29  TYR A CD1 
223  C CD2 . TYR A 30  ? 0.3025 0.2635 0.2596 -0.0494 0.0164  0.0225  29  TYR A CD2 
224  C CE1 . TYR A 30  ? 0.3220 0.2653 0.2649 -0.0438 0.0090  0.0286  29  TYR A CE1 
225  C CE2 . TYR A 30  ? 0.3588 0.3184 0.3100 -0.0523 0.0187  0.0227  29  TYR A CE2 
226  C CZ  . TYR A 30  ? 0.3340 0.2844 0.2776 -0.0497 0.0150  0.0258  29  TYR A CZ  
227  O OH  . TYR A 30  ? 0.3496 0.2981 0.2862 -0.0532 0.0174  0.0260  29  TYR A OH  
228  N N   . ILE A 31  ? 0.3076 0.2325 0.2549 -0.0353 -0.0010 0.0308  30  ILE A N   
229  C CA  . ILE A 31  ? 0.3350 0.2468 0.2747 -0.0321 -0.0062 0.0343  30  ILE A CA  
230  C C   . ILE A 31  ? 0.3245 0.2432 0.2736 -0.0240 -0.0097 0.0340  30  ILE A C   
231  O O   . ILE A 31  ? 0.3021 0.2318 0.2624 -0.0209 -0.0086 0.0314  30  ILE A O   
232  C CB  . ILE A 31  ? 0.3874 0.2852 0.3207 -0.0327 -0.0085 0.0357  30  ILE A CB  
233  C CG1 . ILE A 31  ? 0.4130 0.2955 0.3363 -0.0304 -0.0140 0.0398  30  ILE A CG1 
234  C CG2 . ILE A 31  ? 0.3728 0.2757 0.3170 -0.0277 -0.0094 0.0335  30  ILE A CG2 
235  C CD1 . ILE A 31  ? 0.5420 0.4081 0.4564 -0.0319 -0.0160 0.0417  30  ILE A CD1 
236  N N   . TRP A 32  ? 0.3218 0.2337 0.2659 -0.0211 -0.0139 0.0367  31  TRP A N   
237  C CA  . TRP A 32  ? 0.3346 0.2527 0.2872 -0.0140 -0.0173 0.0363  31  TRP A CA  
238  C C   . TRP A 32  ? 0.3102 0.2212 0.2653 -0.0086 -0.0221 0.0370  31  TRP A C   
239  O O   . TRP A 32  ? 0.3294 0.2279 0.2774 -0.0101 -0.0238 0.0387  31  TRP A O   
240  C CB  . TRP A 32  ? 0.2915 0.2082 0.2383 -0.0139 -0.0191 0.0384  31  TRP A CB  
241  C CG  . TRP A 32  ? 0.2721 0.1986 0.2201 -0.0178 -0.0140 0.0366  31  TRP A CG  
242  C CD1 . TRP A 32  ? 0.3247 0.2486 0.2644 -0.0249 -0.0100 0.0368  31  TRP A CD1 
243  C CD2 . TRP A 32  ? 0.2761 0.2162 0.2341 -0.0148 -0.0118 0.0340  31  TRP A CD2 
244  N NE1 . TRP A 32  ? 0.2810 0.2167 0.2260 -0.0261 -0.0055 0.0343  31  TRP A NE1 
245  C CE2 . TRP A 32  ? 0.2778 0.2230 0.2338 -0.0198 -0.0067 0.0328  31  TRP A CE2 
246  C CE3 . TRP A 32  ? 0.2480 0.1958 0.2161 -0.0086 -0.0136 0.0325  31  TRP A CE3 
247  C CZ2 . TRP A 32  ? 0.2582 0.2154 0.2220 -0.0182 -0.0037 0.0304  31  TRP A CZ2 
248  C CZ3 . TRP A 32  ? 0.2551 0.2145 0.2300 -0.0076 -0.0105 0.0302  31  TRP A CZ3 
249  C CH2 . TRP A 32  ? 0.2353 0.1990 0.2082 -0.0120 -0.0058 0.0293  31  TRP A CH2 
250  N N   . PRO A 33  ? 0.2887 0.2072 0.2540 -0.0024 -0.0241 0.0352  32  PRO A N   
251  C CA  . PRO A 33  ? 0.3100 0.2233 0.2797 0.0029  -0.0280 0.0349  32  PRO A CA  
252  C C   . PRO A 33  ? 0.3470 0.2472 0.3089 0.0049  -0.0337 0.0385  32  PRO A C   
253  O O   . PRO A 33  ? 0.3399 0.2371 0.2943 0.0035  -0.0355 0.0412  32  PRO A O   
254  C CB  . PRO A 33  ? 0.2527 0.1780 0.2339 0.0082  -0.0284 0.0321  32  PRO A CB  
255  C CG  . PRO A 33  ? 0.2622 0.1991 0.2465 0.0050  -0.0234 0.0303  32  PRO A CG  
256  C CD  . PRO A 33  ? 0.2351 0.1678 0.2093 -0.0005 -0.0218 0.0327  32  PRO A CD  
257  N N   . ASP A 34  ? 0.2931 0.1852 0.2566 0.0084  -0.0366 0.0385  33  ASP A N   
258  C CA  . ASP A 34  ? 0.3242 0.2028 0.2811 0.0112  -0.0428 0.0420  33  ASP A CA  
259  C C   . ASP A 34  ? 0.3709 0.2551 0.3372 0.0187  -0.0476 0.0411  33  ASP A C   
260  O O   . ASP A 34  ? 0.3358 0.2251 0.3133 0.0232  -0.0474 0.0377  33  ASP A O   
261  C CB  . ASP A 34  ? 0.3655 0.2316 0.3196 0.0113  -0.0434 0.0423  33  ASP A CB  
262  C CG  . ASP A 34  ? 0.4816 0.3319 0.4282 0.0145  -0.0503 0.0463  33  ASP A CG  
263  O OD1 . ASP A 34  ? 0.4589 0.3094 0.4045 0.0176  -0.0553 0.0485  33  ASP A OD1 
264  O OD2 . ASP A 34  ? 0.5393 0.3766 0.4805 0.0138  -0.0508 0.0472  33  ASP A OD2 
265  N N   . PRO A 35  ? 0.3490 0.2323 0.3112 0.0198  -0.0518 0.0439  34  PRO A N   
266  C CA  . PRO A 35  ? 0.3674 0.2571 0.3390 0.0266  -0.0564 0.0427  34  PRO A CA  
267  C C   . PRO A 35  ? 0.3753 0.2582 0.3528 0.0329  -0.0611 0.0422  34  PRO A C   
268  O O   . PRO A 35  ? 0.3854 0.2768 0.3751 0.0385  -0.0628 0.0391  34  PRO A O   
269  C CB  . PRO A 35  ? 0.4194 0.3060 0.3820 0.0252  -0.0605 0.0466  34  PRO A CB  
270  C CG  . PRO A 35  ? 0.5373 0.4215 0.4886 0.0172  -0.0556 0.0482  34  PRO A CG  
271  C CD  . PRO A 35  ? 0.4116 0.2886 0.3601 0.0143  -0.0523 0.0478  34  PRO A CD  
272  N N   . ASN A 36  ? 0.3743 0.2419 0.3437 0.0322  -0.0632 0.0449  35  ASN A N   
273  C CA  A ASN A 36  ? 0.4021 0.2625 0.3776 0.0388  -0.0678 0.0443  35  ASN A CA  
274  C CA  B ASN A 36  ? 0.4026 0.2632 0.3782 0.0388  -0.0678 0.0443  35  ASN A CA  
275  C C   . ASN A 36  ? 0.4219 0.2895 0.4096 0.0408  -0.0630 0.0388  35  ASN A C   
276  O O   . ASN A 36  ? 0.4179 0.2886 0.4172 0.0473  -0.0655 0.0359  35  ASN A O   
277  C CB  A ASN A 36  ? 0.4881 0.3288 0.4503 0.0371  -0.0709 0.0488  35  ASN A CB  
278  C CB  B ASN A 36  ? 0.4872 0.3281 0.4500 0.0374  -0.0711 0.0487  35  ASN A CB  
279  C CG  A ASN A 36  ? 0.5432 0.3752 0.4922 0.0351  -0.0764 0.0545  35  ASN A CG  
280  C CG  B ASN A 36  ? 0.4638 0.2967 0.4336 0.0444  -0.0749 0.0476  35  ASN A CG  
281  O OD1 A ASN A 36  ? 0.5194 0.3568 0.4718 0.0388  -0.0814 0.0554  35  ASN A OD1 
282  O OD1 B ASN A 36  ? 0.5004 0.3343 0.4774 0.0514  -0.0812 0.0477  35  ASN A OD1 
283  N ND2 A ASN A 36  ? 0.5818 0.4002 0.5150 0.0287  -0.0754 0.0581  35  ASN A ND2 
284  N ND2 B ASN A 36  ? 0.4902 0.3156 0.4585 0.0425  -0.0710 0.0461  35  ASN A ND2 
285  N N   . THR A 37  ? 0.3767 0.2473 0.3624 0.0350  -0.0562 0.0370  36  THR A N   
286  C CA  . THR A 37  ? 0.3245 0.2015 0.3210 0.0365  -0.0519 0.0318  36  THR A CA  
287  C C   . THR A 37  ? 0.3319 0.2261 0.3398 0.0382  -0.0498 0.0279  36  THR A C   
288  O O   . THR A 37  ? 0.3444 0.2441 0.3630 0.0415  -0.0483 0.0234  36  THR A O   
289  C CB  . THR A 37  ? 0.3522 0.2264 0.3432 0.0299  -0.0459 0.0311  36  THR A CB  
290  O OG1 . THR A 37  ? 0.3607 0.2434 0.3476 0.0242  -0.0421 0.0317  36  THR A OG1 
291  C CG2 . THR A 37  ? 0.4370 0.2931 0.4164 0.0277  -0.0476 0.0345  36  THR A CG2 
292  N N   . ILE A 38  ? 0.3344 0.2363 0.3394 0.0359  -0.0493 0.0293  37  ILE A N   
293  C CA  . ILE A 38  ? 0.3098 0.2262 0.3245 0.0381  -0.0483 0.0260  37  ILE A CA  
294  C C   . ILE A 38  ? 0.3477 0.2656 0.3714 0.0451  -0.0534 0.0244  37  ILE A C   
295  O O   . ILE A 38  ? 0.3206 0.2475 0.3554 0.0479  -0.0518 0.0197  37  ILE A O   
296  C CB  . ILE A 38  ? 0.3394 0.2618 0.3484 0.0346  -0.0474 0.0282  37  ILE A CB  
297  C CG1 . ILE A 38  ? 0.3321 0.2570 0.3363 0.0283  -0.0415 0.0281  37  ILE A CG1 
298  C CG2 . ILE A 38  ? 0.2671 0.2024 0.2850 0.0374  -0.0474 0.0252  37  ILE A CG2 
299  C CD1 . ILE A 38  ? 0.3136 0.2432 0.3119 0.0246  -0.0399 0.0300  37  ILE A CD1 
300  N N   . ASP A 39  ? 0.3498 0.2585 0.3687 0.0479  -0.0598 0.0283  38  ASP A N   
301  C CA  . ASP A 39  ? 0.2882 0.1980 0.3164 0.0551  -0.0655 0.0269  38  ASP A CA  
302  C C   . ASP A 39  ? 0.2938 0.2028 0.3325 0.0590  -0.0640 0.0223  38  ASP A C   
303  O O   . ASP A 39  ? 0.3430 0.2607 0.3943 0.0638  -0.0649 0.0180  38  ASP A O   
304  C CB  . ASP A 39  ? 0.3460 0.2430 0.3659 0.0573  -0.0731 0.0324  38  ASP A CB  
305  C CG  . ASP A 39  ? 0.4671 0.3662 0.4786 0.0547  -0.0759 0.0362  38  ASP A CG  
306  O OD1 . ASP A 39  ? 0.4622 0.3733 0.4760 0.0520  -0.0721 0.0343  38  ASP A OD1 
307  O OD2 . ASP A 39  ? 0.5325 0.4202 0.5344 0.0549  -0.0818 0.0413  38  ASP A OD2 
308  N N   . THR A 40  ? 0.3234 0.2221 0.3570 0.0568  -0.0616 0.0229  39  THR A N   
309  C CA  . THR A 40  ? 0.3338 0.2305 0.3763 0.0598  -0.0596 0.0184  39  THR A CA  
310  C C   . THR A 40  ? 0.3472 0.2580 0.3994 0.0584  -0.0535 0.0124  39  THR A C   
311  O O   . THR A 40  ? 0.2924 0.2083 0.3566 0.0627  -0.0532 0.0073  39  THR A O   
312  C CB  . THR A 40  ? 0.3843 0.2670 0.4177 0.0563  -0.0574 0.0202  39  THR A CB  
313  O OG1 . THR A 40  ? 0.3857 0.2535 0.4107 0.0586  -0.0636 0.0254  39  THR A OG1 
314  C CG2 . THR A 40  ? 0.3452 0.2268 0.3872 0.0581  -0.0537 0.0149  39  THR A CG2 
315  N N   . LEU A 41  ? 0.3441 0.2611 0.3912 0.0523  -0.0487 0.0127  40  LEU A N   
316  C CA  . LEU A 41  ? 0.2586 0.1880 0.3133 0.0506  -0.0435 0.0075  40  LEU A CA  
317  C C   . LEU A 41  ? 0.2486 0.1894 0.3122 0.0543  -0.0453 0.0049  40  LEU A C   
318  O O   . LEU A 41  ? 0.3312 0.2800 0.4044 0.0554  -0.0425 -0.0006 40  LEU A O   
319  C CB  . LEU A 41  ? 0.2790 0.2122 0.3262 0.0438  -0.0389 0.0090  40  LEU A CB  
320  C CG  . LEU A 41  ? 0.3092 0.2341 0.3492 0.0391  -0.0357 0.0102  40  LEU A CG  
321  C CD1 . LEU A 41  ? 0.2696 0.2013 0.3048 0.0331  -0.0315 0.0109  40  LEU A CD1 
322  C CD2 . LEU A 41  ? 0.2695 0.1920 0.3155 0.0398  -0.0329 0.0056  40  LEU A CD2 
323  N N   . ILE A 42  ? 0.2966 0.2382 0.3567 0.0556  -0.0498 0.0086  41  ILE A N   
324  C CA  . ILE A 42  ? 0.2959 0.2479 0.3644 0.0591  -0.0521 0.0061  41  ILE A CA  
325  C C   . ILE A 42  ? 0.3200 0.2722 0.4005 0.0655  -0.0551 0.0022  41  ILE A C   
326  O O   . ILE A 42  ? 0.3175 0.2803 0.4086 0.0673  -0.0535 -0.0031 41  ILE A O   
327  C CB  . ILE A 42  ? 0.3099 0.2612 0.3712 0.0590  -0.0569 0.0111  41  ILE A CB  
328  C CG1 . ILE A 42  ? 0.2793 0.2346 0.3322 0.0529  -0.0527 0.0130  41  ILE A CG1 
329  C CG2 . ILE A 42  ? 0.2904 0.2508 0.3608 0.0633  -0.0606 0.0087  41  ILE A CG2 
330  C CD1 . ILE A 42  ? 0.3127 0.2662 0.3570 0.0517  -0.0564 0.0178  41  ILE A CD1 
331  N N   . SER A 43  ? 0.3349 0.2752 0.4139 0.0689  -0.0591 0.0045  42  SER A N   
332  C CA  . SER A 43  ? 0.3057 0.2457 0.3970 0.0757  -0.0620 0.0007  42  SER A CA  
333  C C   . SER A 43  ? 0.3688 0.3126 0.4690 0.0751  -0.0558 -0.0061 42  SER A C   
334  O O   . SER A 43  ? 0.3766 0.3257 0.4898 0.0799  -0.0564 -0.0114 42  SER A O   
335  C CB  . SER A 43  ? 0.3646 0.2893 0.4513 0.0795  -0.0679 0.0051  42  SER A CB  
336  O OG  . SER A 43  ? 0.4813 0.3951 0.5621 0.0766  -0.0641 0.0055  42  SER A OG  
337  N N   . LYS A 44  ? 0.3481 0.2896 0.4415 0.0691  -0.0498 -0.0063 43  LYS A N   
338  C CA  . LYS A 44  ? 0.2723 0.2177 0.3724 0.0673  -0.0435 -0.0126 43  LYS A CA  
339  C C   . LYS A 44  ? 0.3779 0.3379 0.4840 0.0652  -0.0398 -0.0173 43  LYS A C   
340  O O   . LYS A 44  ? 0.3490 0.3132 0.4616 0.0639  -0.0348 -0.0232 43  LYS A O   
341  C CB  . LYS A 44  ? 0.3655 0.3037 0.4558 0.0612  -0.0388 -0.0110 43  LYS A CB  
342  C CG  . LYS A 44  ? 0.3803 0.3029 0.4641 0.0621  -0.0409 -0.0075 43  LYS A CG  
343  C CD  . LYS A 44  ? 0.4442 0.3613 0.5369 0.0663  -0.0401 -0.0123 43  LYS A CD  
344  C CE  . LYS A 44  ? 0.4872 0.3871 0.5723 0.0674  -0.0426 -0.0085 43  LYS A CE  
345  N NZ  . LYS A 44  ? 0.5902 0.4836 0.6823 0.0699  -0.0400 -0.0135 43  LYS A NZ  
346  N N   . GLY A 45  ? 0.2851 0.2521 0.3885 0.0644  -0.0417 -0.0148 44  GLY A N   
347  C CA  . GLY A 45  ? 0.3046 0.2844 0.4127 0.0624  -0.0385 -0.0190 44  GLY A CA  
348  C C   . GLY A 45  ? 0.2891 0.2723 0.3878 0.0563  -0.0352 -0.0165 44  GLY A C   
349  O O   . GLY A 45  ? 0.2662 0.2588 0.3674 0.0544  -0.0326 -0.0196 44  GLY A O   
350  N N   . MET A 46  ? 0.2169 0.1928 0.3050 0.0532  -0.0351 -0.0112 45  MET A N   
351  C CA  . MET A 46  ? 0.2229 0.2025 0.3031 0.0481  -0.0322 -0.0090 45  MET A CA  
352  C C   . MET A 46  ? 0.2555 0.2397 0.3331 0.0488  -0.0352 -0.0061 45  MET A C   
353  O O   . MET A 46  ? 0.2763 0.2568 0.3531 0.0521  -0.0403 -0.0032 45  MET A O   
354  C CB  . MET A 46  ? 0.1941 0.1655 0.2649 0.0445  -0.0312 -0.0047 45  MET A CB  
355  C CG  . MET A 46  ? 0.2473 0.2145 0.3194 0.0426  -0.0276 -0.0076 45  MET A CG  
356  S SD  . MET A 46  ? 0.2718 0.2316 0.3327 0.0371  -0.0257 -0.0032 45  MET A SD  
357  C CE  . MET A 46  ? 0.3166 0.2740 0.3809 0.0348  -0.0213 -0.0080 45  MET A CE  
358  N N   . ASN A 47  ? 0.2088 0.2004 0.2844 0.0456  -0.0322 -0.0069 46  ASN A N   
359  C CA  . ASN A 47  ? 0.2054 0.2017 0.2787 0.0460  -0.0343 -0.0050 46  ASN A CA  
360  C C   . ASN A 47  ? 0.2070 0.2044 0.2718 0.0417  -0.0317 -0.0020 46  ASN A C   
361  O O   . ASN A 47  ? 0.1912 0.1933 0.2541 0.0412  -0.0322 -0.0013 46  ASN A O   
362  C CB  . ASN A 47  ? 0.1986 0.2044 0.2802 0.0475  -0.0338 -0.0101 46  ASN A CB  
363  C CG  . ASN A 47  ? 0.2250 0.2363 0.3069 0.0437  -0.0282 -0.0139 46  ASN A CG  
364  O OD1 . ASN A 47  ? 0.2554 0.2637 0.3333 0.0407  -0.0252 -0.0133 46  ASN A OD1 
365  N ND2 . ASN A 47  ? 0.2653 0.2845 0.3515 0.0436  -0.0272 -0.0178 46  ASN A ND2 
366  N N   . ILE A 48  ? 0.2108 0.2044 0.2709 0.0386  -0.0290 -0.0005 47  ILE A N   
367  C CA  . ILE A 48  ? 0.1849 0.1800 0.2382 0.0349  -0.0267 0.0022  47  ILE A CA  
368  C C   . ILE A 48  ? 0.1794 0.1675 0.2273 0.0327  -0.0262 0.0053  47  ILE A C   
369  O O   . ILE A 48  ? 0.2056 0.1899 0.2553 0.0324  -0.0254 0.0040  47  ILE A O   
370  C CB  . ILE A 48  ? 0.1758 0.1775 0.2306 0.0326  -0.0226 -0.0009 47  ILE A CB  
371  C CG1 . ILE A 48  ? 0.1826 0.1860 0.2313 0.0297  -0.0207 0.0019  47  ILE A CG1 
372  C CG2 . ILE A 48  ? 0.1688 0.1695 0.2265 0.0312  -0.0201 -0.0038 47  ILE A CG2 
373  C CD1 . ILE A 48  ? 0.2030 0.2125 0.2526 0.0283  -0.0178 -0.0006 47  ILE A CD1 
374  N N   . PHE A 49  ? 0.1755 0.1617 0.2165 0.0306  -0.0264 0.0092  48  PHE A N   
375  C CA  . PHE A 49  ? 0.1635 0.1436 0.1986 0.0277  -0.0255 0.0120  48  PHE A CA  
376  C C   . PHE A 49  ? 0.1893 0.1735 0.2203 0.0243  -0.0226 0.0134  48  PHE A C   
377  O O   . PHE A 49  ? 0.1995 0.1860 0.2280 0.0243  -0.0230 0.0148  48  PHE A O   
378  C CB  . PHE A 49  ? 0.2335 0.2046 0.2636 0.0288  -0.0294 0.0154  48  PHE A CB  
379  C CG  . PHE A 49  ? 0.2013 0.1679 0.2363 0.0328  -0.0325 0.0139  48  PHE A CG  
380  C CD1 . PHE A 49  ? 0.2206 0.1905 0.2611 0.0370  -0.0357 0.0124  48  PHE A CD1 
381  C CD2 . PHE A 49  ? 0.2443 0.2040 0.2792 0.0323  -0.0320 0.0135  48  PHE A CD2 
382  C CE1 . PHE A 49  ? 0.2492 0.2160 0.2959 0.0412  -0.0385 0.0105  48  PHE A CE1 
383  C CE2 . PHE A 49  ? 0.2265 0.1820 0.2668 0.0364  -0.0346 0.0117  48  PHE A CE2 
384  C CZ  . PHE A 49  ? 0.2433 0.2026 0.2900 0.0411  -0.0379 0.0101  48  PHE A CZ  
385  N N   . ARG A 50  ? 0.1896 0.1752 0.2205 0.0214  -0.0197 0.0129  49  ARG A N   
386  C CA  . ARG A 50  ? 0.1903 0.1808 0.2192 0.0186  -0.0169 0.0138  49  ARG A CA  
387  C C   . ARG A 50  ? 0.2284 0.2142 0.2515 0.0153  -0.0162 0.0165  49  ARG A C   
388  O O   . ARG A 50  ? 0.2254 0.2059 0.2471 0.0138  -0.0163 0.0168  49  ARG A O   
389  C CB  . ARG A 50  ? 0.1889 0.1850 0.2218 0.0174  -0.0145 0.0114  49  ARG A CB  
390  C CG  . ARG A 50  ? 0.1742 0.1759 0.2064 0.0153  -0.0121 0.0121  49  ARG A CG  
391  C CD  . ARG A 50  ? 0.1430 0.1499 0.1790 0.0150  -0.0109 0.0098  49  ARG A CD  
392  N NE  . ARG A 50  ? 0.1649 0.1775 0.2014 0.0136  -0.0093 0.0104  49  ARG A NE  
393  C CZ  . ARG A 50  ? 0.1771 0.1918 0.2144 0.0110  -0.0084 0.0105  49  ARG A CZ  
394  N NH1 . ARG A 50  ? 0.1694 0.1804 0.2059 0.0088  -0.0085 0.0104  49  ARG A NH1 
395  N NH2 . ARG A 50  ? 0.1548 0.1755 0.1939 0.0106  -0.0075 0.0106  49  ARG A NH2 
396  N N   . VAL A 51  ? 0.1858 0.1729 0.2050 0.0138  -0.0153 0.0183  50  VAL A N   
397  C CA  . VAL A 51  ? 0.1961 0.1781 0.2087 0.0102  -0.0145 0.0207  50  VAL A CA  
398  C C   . VAL A 51  ? 0.2109 0.1995 0.2244 0.0070  -0.0107 0.0202  50  VAL A C   
399  O O   . VAL A 51  ? 0.2114 0.2043 0.2246 0.0069  -0.0092 0.0203  50  VAL A O   
400  C CB  . VAL A 51  ? 0.1859 0.1630 0.1924 0.0105  -0.0167 0.0231  50  VAL A CB  
401  C CG1 . VAL A 51  ? 0.1997 0.1702 0.1978 0.0059  -0.0157 0.0255  50  VAL A CG1 
402  C CG2 . VAL A 51  ? 0.2056 0.1775 0.2129 0.0144  -0.0212 0.0234  50  VAL A CG2 
403  N N   . PRO A 52  ? 0.2077 0.1974 0.2225 0.0043  -0.0090 0.0195  51  PRO A N   
404  C CA  . PRO A 52  ? 0.1806 0.1771 0.1970 0.0013  -0.0057 0.0190  51  PRO A CA  
405  C C   . PRO A 52  ? 0.2119 0.2052 0.2220 -0.0023 -0.0040 0.0205  51  PRO A C   
406  O O   . PRO A 52  ? 0.2212 0.2056 0.2245 -0.0043 -0.0051 0.0222  51  PRO A O   
407  C CB  . PRO A 52  ? 0.2075 0.2045 0.2259 -0.0012 -0.0050 0.0179  51  PRO A CB  
408  C CG  . PRO A 52  ? 0.2035 0.1966 0.2238 0.0018  -0.0075 0.0171  51  PRO A CG  
409  C CD  . PRO A 52  ? 0.2249 0.2106 0.2409 0.0042  -0.0100 0.0187  51  PRO A CD  
410  N N   . PHE A 53  ? 0.2008 0.2011 0.2130 -0.0033 -0.0011 0.0197  52  PHE A N   
411  C CA  . PHE A 53  ? 0.2122 0.2113 0.2193 -0.0077 0.0017  0.0203  52  PHE A CA  
412  C C   . PHE A 53  ? 0.1904 0.2001 0.2042 -0.0088 0.0053  0.0182  52  PHE A C   
413  O O   . PHE A 53  ? 0.2138 0.2308 0.2351 -0.0054 0.0049  0.0169  52  PHE A O   
414  C CB  . PHE A 53  ? 0.2233 0.2175 0.2241 -0.0073 0.0011  0.0218  52  PHE A CB  
415  C CG  . PHE A 53  ? 0.1830 0.1841 0.1884 -0.0040 0.0021  0.0206  52  PHE A CG  
416  C CD1 . PHE A 53  ? 0.1929 0.1999 0.2000 -0.0058 0.0062  0.0192  52  PHE A CD1 
417  C CD2 . PHE A 53  ? 0.1998 0.2014 0.2080 0.0007  -0.0008 0.0205  52  PHE A CD2 
418  C CE1 . PHE A 53  ? 0.1981 0.2104 0.2090 -0.0027 0.0072  0.0181  52  PHE A CE1 
419  C CE2 . PHE A 53  ? 0.1835 0.1905 0.1949 0.0033  0.0003  0.0194  52  PHE A CE2 
420  C CZ  . PHE A 53  ? 0.1868 0.1986 0.1994 0.0017  0.0042  0.0183  52  PHE A CZ  
421  N N   . MET A 54  ? 0.1859 0.1966 0.1972 -0.0135 0.0088  0.0176  53  MET A N   
422  C CA  A MET A 54  ? 0.1731 0.1946 0.1918 -0.0145 0.0124  0.0152  53  MET A CA  
423  C CA  B MET A 54  ? 0.1752 0.1966 0.1938 -0.0146 0.0125  0.0152  53  MET A CA  
424  C C   . MET A 54  ? 0.1986 0.2229 0.2176 -0.0134 0.0149  0.0145  53  MET A C   
425  O O   . MET A 54  ? 0.2039 0.2218 0.2148 -0.0163 0.0162  0.0154  53  MET A O   
426  C CB  A MET A 54  ? 0.2294 0.2520 0.2467 -0.0207 0.0155  0.0141  53  MET A CB  
427  C CB  B MET A 54  ? 0.2297 0.2516 0.2462 -0.0210 0.0156  0.0142  53  MET A CB  
428  C CG  A MET A 54  ? 0.2407 0.2623 0.2589 -0.0224 0.0139  0.0142  53  MET A CG  
429  C CG  B MET A 54  ? 0.2379 0.2564 0.2532 -0.0229 0.0137  0.0147  53  MET A CG  
430  S SD  A MET A 54  ? 0.2804 0.3067 0.2991 -0.0299 0.0182  0.0119  53  MET A SD  
431  S SD  B MET A 54  ? 0.2936 0.3237 0.3210 -0.0198 0.0124  0.0129  53  MET A SD  
432  C CE  A MET A 54  ? 0.2776 0.3211 0.3108 -0.0274 0.0200  0.0088  53  MET A CE  
433  C CE  B MET A 54  ? 0.3378 0.3803 0.3726 -0.0231 0.0171  0.0099  53  MET A CE  
434  N N   . MET A 55  ? 0.1914 0.2245 0.2191 -0.0096 0.0156  0.0129  54  MET A N   
435  C CA  . MET A 55  ? 0.1791 0.2149 0.2077 -0.0086 0.0185  0.0117  54  MET A CA  
436  C C   . MET A 55  ? 0.2233 0.2600 0.2492 -0.0141 0.0234  0.0102  54  MET A C   
437  O O   . MET A 55  ? 0.2124 0.2455 0.2328 -0.0156 0.0257  0.0101  54  MET A O   
438  C CB  . MET A 55  ? 0.1758 0.2210 0.2146 -0.0040 0.0188  0.0100  54  MET A CB  
439  C CG  . MET A 55  ? 0.1482 0.1921 0.1884 0.0012  0.0149  0.0111  54  MET A CG  
440  S SD  . MET A 55  ? 0.1822 0.2358 0.2333 0.0060  0.0149  0.0095  54  MET A SD  
441  C CE  . MET A 55  ? 0.1776 0.2319 0.2286 0.0071  0.0192  0.0080  54  MET A CE  
442  N N   . GLU A 56  ? 0.2144 0.2563 0.2443 -0.0176 0.0253  0.0086  55  GLU A N   
443  C CA  . GLU A 56  ? 0.1813 0.2256 0.2100 -0.0234 0.0306  0.0063  55  GLU A CA  
444  C C   . GLU A 56  ? 0.2175 0.2501 0.2325 -0.0291 0.0314  0.0081  55  GLU A C   
445  O O   . GLU A 56  ? 0.2317 0.2637 0.2425 -0.0341 0.0360  0.0064  55  GLU A O   
446  C CB  . GLU A 56  ? 0.2647 0.3178 0.3011 -0.0260 0.0321  0.0041  55  GLU A CB  
447  C CG  . GLU A 56  ? 0.2429 0.3082 0.2932 -0.0207 0.0311  0.0023  55  GLU A CG  
448  C CD  . GLU A 56  ? 0.2115 0.2762 0.2641 -0.0166 0.0255  0.0044  55  GLU A CD  
449  O OE1 . GLU A 56  ? 0.2030 0.2579 0.2475 -0.0166 0.0224  0.0071  55  GLU A OE1 
450  O OE2 . GLU A 56  ? 0.2093 0.2833 0.2720 -0.0135 0.0242  0.0033  55  GLU A OE2 
451  N N   . ARG A 57  ? 0.2312 0.2543 0.2389 -0.0287 0.0269  0.0113  56  ARG A N   
452  C CA  . ARG A 57  ? 0.2416 0.2521 0.2356 -0.0334 0.0263  0.0136  56  ARG A CA  
453  C C   . ARG A 57  ? 0.2102 0.2146 0.1977 -0.0312 0.0247  0.0154  56  ARG A C   
454  O O   . ARG A 57  ? 0.2383 0.2348 0.2150 -0.0360 0.0261  0.0164  56  ARG A O   
455  C CB  . ARG A 57  ? 0.2582 0.2607 0.2477 -0.0334 0.0220  0.0161  56  ARG A CB  
456  C CG  . ARG A 57  ? 0.2609 0.2666 0.2529 -0.0378 0.0240  0.0145  56  ARG A CG  
457  C CD  . ARG A 57  ? 0.2494 0.2455 0.2358 -0.0382 0.0201  0.0170  56  ARG A CD  
458  N NE  . ARG A 57  ? 0.2799 0.2782 0.2670 -0.0436 0.0226  0.0153  56  ARG A NE  
459  C CZ  . ARG A 57  ? 0.2828 0.2798 0.2716 -0.0431 0.0204  0.0156  56  ARG A CZ  
460  N NH1 . ARG A 57  ? 0.2985 0.2918 0.2888 -0.0374 0.0157  0.0174  56  ARG A NH1 
461  N NH2 . ARG A 57  ? 0.3096 0.3094 0.2989 -0.0488 0.0231  0.0137  56  ARG A NH2 
462  N N   . LEU A 58  ? 0.2308 0.2386 0.2243 -0.0246 0.0220  0.0158  57  LEU A N   
463  C CA  . LEU A 58  ? 0.2043 0.2076 0.1925 -0.0227 0.0206  0.0171  57  LEU A CA  
464  C C   . LEU A 58  ? 0.2593 0.2676 0.2488 -0.0242 0.0258  0.0145  57  LEU A C   
465  O O   . LEU A 58  ? 0.2624 0.2648 0.2431 -0.0269 0.0267  0.0153  57  LEU A O   
466  C CB  . LEU A 58  ? 0.2156 0.2206 0.2091 -0.0158 0.0162  0.0180  57  LEU A CB  
467  C CG  . LEU A 58  ? 0.2235 0.2235 0.2111 -0.0140 0.0140  0.0194  57  LEU A CG  
468  C CD1 . LEU A 58  ? 0.2408 0.2296 0.2177 -0.0163 0.0101  0.0226  57  LEU A CD1 
469  C CD2 . LEU A 58  ? 0.2353 0.2393 0.2297 -0.0077 0.0112  0.0191  57  LEU A CD2 
470  N N   . VAL A 59  ? 0.2165 0.2354 0.2170 -0.0224 0.0292  0.0114  58  VAL A N   
471  C CA  . VAL A 59  ? 0.2101 0.2344 0.2138 -0.0230 0.0345  0.0084  58  VAL A CA  
472  C C   . VAL A 59  ? 0.2559 0.2895 0.2683 -0.0254 0.0390  0.0050  58  VAL A C   
473  O O   . VAL A 59  ? 0.2355 0.2783 0.2597 -0.0209 0.0387  0.0035  58  VAL A O   
474  C CB  . VAL A 59  ? 0.2619 0.2904 0.2722 -0.0163 0.0333  0.0080  58  VAL A CB  
475  C CG1 . VAL A 59  ? 0.2527 0.2853 0.2655 -0.0170 0.0391  0.0047  58  VAL A CG1 
476  C CG2 . VAL A 59  ? 0.2605 0.2811 0.2635 -0.0139 0.0285  0.0110  58  VAL A CG2 
477  N N   . PRO A 60  ? 0.2578 0.2894 0.2646 -0.0325 0.0431  0.0037  59  PRO A N   
478  C CA  . PRO A 60  ? 0.2417 0.2825 0.2566 -0.0356 0.0471  0.0003  59  PRO A CA  
479  C C   . PRO A 60  ? 0.2404 0.2921 0.2664 -0.0338 0.0524  -0.0042 59  PRO A C   
480  O O   . PRO A 60  ? 0.2624 0.3126 0.2867 -0.0326 0.0547  -0.0050 59  PRO A O   
481  C CB  . PRO A 60  ? 0.2991 0.3321 0.3019 -0.0446 0.0501  0.0003  59  PRO A CB  
482  C CG  . PRO A 60  ? 0.3230 0.3418 0.3114 -0.0451 0.0455  0.0049  59  PRO A CG  
483  C CD  . PRO A 60  ? 0.2372 0.2571 0.2287 -0.0386 0.0436  0.0056  59  PRO A CD  
484  N N   . ASN A 61  ? 0.2295 0.2924 0.2673 -0.0338 0.0542  -0.0072 60  ASN A N   
485  C CA  . ASN A 61  ? 0.2650 0.3397 0.3150 -0.0331 0.0597  -0.0122 60  ASN A CA  
486  C C   . ASN A 61  ? 0.2793 0.3594 0.3393 -0.0244 0.0580  -0.0125 60  ASN A C   
487  O O   . ASN A 61  ? 0.2635 0.3547 0.3373 -0.0203 0.0576  -0.0145 60  ASN A O   
488  C CB  . ASN A 61  ? 0.2796 0.3513 0.3227 -0.0399 0.0668  -0.0152 60  ASN A CB  
489  C CG  . ASN A 61  ? 0.3254 0.3902 0.3567 -0.0492 0.0687  -0.0148 60  ASN A CG  
490  O OD1 . ASN A 61  ? 0.3752 0.4436 0.4094 -0.0516 0.0678  -0.0151 60  ASN A OD1 
491  N ND2 . ASN A 61  ? 0.4334 0.4878 0.4506 -0.0549 0.0714  -0.0142 60  ASN A ND2 
492  N N   . SER A 62  ? 0.1988 0.2709 0.2517 -0.0218 0.0569  -0.0105 61  SER A N   
493  C CA  A SER A 62  ? 0.1980 0.2728 0.2580 -0.0140 0.0551  -0.0103 61  SER A CA  
494  C CA  B SER A 62  ? 0.1986 0.2734 0.2586 -0.0140 0.0550  -0.0103 61  SER A CA  
495  C C   . SER A 62  ? 0.2204 0.2850 0.2706 -0.0114 0.0498  -0.0060 61  SER A C   
496  O O   . SER A 62  ? 0.2663 0.3218 0.3044 -0.0154 0.0502  -0.0044 61  SER A O   
497  C CB  A SER A 62  ? 0.2627 0.3402 0.3260 -0.0138 0.0614  -0.0143 61  SER A CB  
498  C CB  B SER A 62  ? 0.2620 0.3395 0.3254 -0.0136 0.0613  -0.0142 61  SER A CB  
499  O OG  A SER A 62  ? 0.2297 0.3069 0.2970 -0.0067 0.0596  -0.0137 61  SER A OG  
500  O OG  B SER A 62  ? 0.2468 0.3359 0.3229 -0.0141 0.0657  -0.0188 61  SER A OG  
501  N N   . MET A 63  ? 0.2019 0.2682 0.2575 -0.0050 0.0449  -0.0042 62  MET A N   
502  C CA  . MET A 63  ? 0.1976 0.2553 0.2449 -0.0028 0.0401  -0.0006 62  MET A CA  
503  C C   . MET A 63  ? 0.2412 0.2936 0.2829 -0.0017 0.0419  -0.0008 62  MET A C   
504  O O   . MET A 63  ? 0.2233 0.2686 0.2573 -0.0009 0.0385  0.0019  62  MET A O   
505  C CB  . MET A 63  ? 0.2118 0.2724 0.2655 0.0029  0.0347  0.0011  62  MET A CB  
506  C CG  . MET A 63  ? 0.2273 0.2922 0.2888 0.0089  0.0350  -0.0002 62  MET A CG  
507  S SD  . MET A 63  ? 0.2325 0.2990 0.2988 0.0144  0.0285  0.0020  62  MET A SD  
508  C CE  . MET A 63  ? 0.2482 0.3247 0.3244 0.0132  0.0276  0.0009  62  MET A CE  
509  N N   . THR A 64  ? 0.2397 0.2955 0.2851 -0.0019 0.0474  -0.0041 63  THR A N   
510  C CA  . THR A 64  ? 0.2437 0.2941 0.2828 -0.0021 0.0502  -0.0047 63  THR A CA  
511  C C   . THR A 64  ? 0.2465 0.2908 0.2742 -0.0094 0.0536  -0.0050 63  THR A C   
512  O O   . THR A 64  ? 0.3212 0.3605 0.3422 -0.0107 0.0561  -0.0056 63  THR A O   
513  C CB  . THR A 64  ? 0.2271 0.2832 0.2755 0.0015  0.0548  -0.0084 63  THR A CB  
514  O OG1 . THR A 64  ? 0.2861 0.3492 0.3410 -0.0018 0.0600  -0.0120 63  THR A OG1 
515  C CG2 . THR A 64  ? 0.2556 0.3163 0.3138 0.0090  0.0507  -0.0077 63  THR A CG2 
516  N N   . GLY A 65  ? 0.2338 0.2776 0.2583 -0.0147 0.0538  -0.0045 64  GLY A N   
517  C CA  . GLY A 65  ? 0.2649 0.3024 0.2780 -0.0224 0.0572  -0.0048 64  GLY A CA  
518  C C   . GLY A 65  ? 0.2629 0.2898 0.2624 -0.0246 0.0522  -0.0005 64  GLY A C   
519  O O   . GLY A 65  ? 0.2625 0.2870 0.2616 -0.0200 0.0466  0.0023  64  GLY A O   
520  N N   . SER A 66  ? 0.3238 0.3441 0.3119 -0.0321 0.0542  -0.0001 65  SER A N   
521  C CA  A SER A 66  ? 0.3051 0.3149 0.2802 -0.0342 0.0490  0.0042  65  SER A CA  
522  C CA  B SER A 66  ? 0.3059 0.3156 0.2807 -0.0345 0.0492  0.0042  65  SER A CA  
523  C C   . SER A 66  ? 0.2776 0.2847 0.2516 -0.0343 0.0439  0.0072  65  SER A C   
524  O O   . SER A 66  ? 0.2844 0.2961 0.2638 -0.0359 0.0458  0.0057  65  SER A O   
525  C CB  A SER A 66  ? 0.3512 0.3532 0.3125 -0.0424 0.0526  0.0039  65  SER A CB  
526  C CB  B SER A 66  ? 0.3495 0.3516 0.3107 -0.0429 0.0529  0.0038  65  SER A CB  
527  O OG  A SER A 66  ? 0.3984 0.4016 0.3586 -0.0487 0.0575  0.0016  65  SER A OG  
528  O OG  B SER A 66  ? 0.3996 0.4043 0.3618 -0.0440 0.0590  0.0001  65  SER A OG  
529  N N   . PRO A 67  ? 0.3002 0.3002 0.2677 -0.0325 0.0374  0.0112  66  PRO A N   
530  C CA  . PRO A 67  ? 0.3039 0.3002 0.2700 -0.0323 0.0326  0.0140  66  PRO A CA  
531  C C   . PRO A 67  ? 0.3324 0.3219 0.2886 -0.0401 0.0345  0.0146  66  PRO A C   
532  O O   . PRO A 67  ? 0.3409 0.3257 0.2875 -0.0462 0.0379  0.0140  66  PRO A O   
533  C CB  . PRO A 67  ? 0.2905 0.2800 0.2511 -0.0290 0.0258  0.0176  66  PRO A CB  
534  C CG  . PRO A 67  ? 0.3052 0.2988 0.2694 -0.0252 0.0268  0.0162  66  PRO A CG  
535  C CD  . PRO A 67  ? 0.3243 0.3209 0.2880 -0.0293 0.0341  0.0128  66  PRO A CD  
536  N N   . ASP A 68  ? 0.2688 0.2572 0.2264 -0.0403 0.0321  0.0158  67  ASP A N   
537  C CA  . ASP A 68  ? 0.2779 0.2572 0.2240 -0.0475 0.0324  0.0173  67  ASP A CA  
538  C C   . ASP A 68  ? 0.3151 0.2816 0.2485 -0.0477 0.0261  0.0220  67  ASP A C   
539  O O   . ASP A 68  ? 0.3136 0.2785 0.2501 -0.0420 0.0201  0.0244  67  ASP A O   
540  C CB  . ASP A 68  ? 0.2989 0.2805 0.2502 -0.0477 0.0319  0.0170  67  ASP A CB  
541  C CG  . ASP A 68  ? 0.3326 0.3032 0.2709 -0.0552 0.0320  0.0188  67  ASP A CG  
542  O OD1 . ASP A 68  ? 0.3835 0.3534 0.3161 -0.0626 0.0377  0.0165  67  ASP A OD1 
543  O OD2 . ASP A 68  ? 0.3241 0.2862 0.2573 -0.0539 0.0265  0.0222  67  ASP A OD2 
544  N N   . PRO A 69  ? 0.2898 0.2471 0.2092 -0.0541 0.0270  0.0232  68  PRO A N   
545  C CA  . PRO A 69  ? 0.3417 0.2872 0.2495 -0.0537 0.0201  0.0279  68  PRO A CA  
546  C C   . PRO A 69  ? 0.3520 0.2900 0.2577 -0.0512 0.0137  0.0315  68  PRO A C   
547  O O   . PRO A 69  ? 0.3084 0.2438 0.2152 -0.0455 0.0072  0.0341  68  PRO A O   
548  C CB  . PRO A 69  ? 0.3288 0.2652 0.2207 -0.0629 0.0232  0.0283  68  PRO A CB  
549  C CG  . PRO A 69  ? 0.3580 0.3040 0.2558 -0.0658 0.0317  0.0233  68  PRO A CG  
550  C CD  . PRO A 69  ? 0.2914 0.2492 0.2053 -0.0617 0.0344  0.0201  68  PRO A CD  
551  N N   . ASN A 70  ? 0.3281 0.2625 0.2311 -0.0555 0.0156  0.0313  69  ASN A N   
552  C CA  A ASN A 70  ? 0.3255 0.2505 0.2244 -0.0539 0.0098  0.0348  69  ASN A CA  
553  C CA  B ASN A 70  ? 0.3256 0.2506 0.2245 -0.0539 0.0097  0.0348  69  ASN A CA  
554  C C   . ASN A 70  ? 0.3507 0.2835 0.2640 -0.0456 0.0067  0.0342  69  ASN A C   
555  O O   . ASN A 70  ? 0.3337 0.2609 0.2467 -0.0407 0.0003  0.0370  69  ASN A O   
556  C CB  A ASN A 70  ? 0.3647 0.2834 0.2560 -0.0615 0.0132  0.0344  69  ASN A CB  
557  C CB  B ASN A 70  ? 0.3653 0.2838 0.2563 -0.0616 0.0132  0.0345  69  ASN A CB  
558  C CG  A ASN A 70  ? 0.5271 0.4321 0.4099 -0.0612 0.0072  0.0385  69  ASN A CG  
559  C CG  B ASN A 70  ? 0.4540 0.3633 0.3289 -0.0707 0.0162  0.0350  69  ASN A CG  
560  O OD1 A ASN A 70  ? 0.5851 0.4872 0.4708 -0.0544 0.0006  0.0411  69  ASN A OD1 
561  O OD1 B ASN A 70  ? 0.5323 0.4426 0.4040 -0.0782 0.0226  0.0323  69  ASN A OD1 
562  N ND2 A ASN A 70  ? 0.5957 0.4919 0.4681 -0.0689 0.0098  0.0388  69  ASN A ND2 
563  N ND2 B ASN A 70  ? 0.4181 0.3191 0.2830 -0.0706 0.0117  0.0383  69  ASN A ND2 
564  N N   . TYR A 71  ? 0.2871 0.2327 0.2133 -0.0439 0.0113  0.0304  70  TYR A N   
565  C CA  . TYR A 71  ? 0.2615 0.2141 0.2003 -0.0367 0.0086  0.0297  70  TYR A CA  
566  C C   . TYR A 71  ? 0.2761 0.2315 0.2195 -0.0301 0.0047  0.0305  70  TYR A C   
567  O O   . TYR A 71  ? 0.2561 0.2101 0.2034 -0.0248 -0.0002 0.0318  70  TYR A O   
568  C CB  . TYR A 71  ? 0.2812 0.2469 0.2321 -0.0367 0.0139  0.0257  70  TYR A CB  
569  C CG  . TYR A 71  ? 0.2534 0.2249 0.2150 -0.0318 0.0119  0.0249  70  TYR A CG  
570  C CD1 . TYR A 71  ? 0.2570 0.2241 0.2169 -0.0342 0.0112  0.0254  70  TYR A CD1 
571  C CD2 . TYR A 71  ? 0.2181 0.1992 0.1910 -0.0255 0.0111  0.0234  70  TYR A CD2 
572  C CE1 . TYR A 71  ? 0.2400 0.2126 0.2093 -0.0305 0.0099  0.0244  70  TYR A CE1 
573  C CE2 . TYR A 71  ? 0.2168 0.2030 0.1987 -0.0219 0.0095  0.0226  70  TYR A CE2 
574  C CZ  . TYR A 71  ? 0.2497 0.2317 0.2297 -0.0245 0.0089  0.0231  70  TYR A CZ  
575  O OH  . TYR A 71  ? 0.2438 0.2306 0.2319 -0.0216 0.0076  0.0221  70  TYR A OH  
576  N N   . LEU A 72  ? 0.2728 0.2319 0.2154 -0.0305 0.0069  0.0294  71  LEU A N   
577  C CA  . LEU A 72  ? 0.2591 0.2202 0.2046 -0.0251 0.0033  0.0300  71  LEU A CA  
578  C C   . LEU A 72  ? 0.2869 0.2374 0.2238 -0.0240 -0.0035 0.0339  71  LEU A C   
579  O O   . LEU A 72  ? 0.2731 0.2250 0.2154 -0.0182 -0.0081 0.0345  71  LEU A O   
580  C CB  . LEU A 72  ? 0.2414 0.2070 0.1858 -0.0268 0.0075  0.0281  71  LEU A CB  
581  C CG  . LEU A 72  ? 0.2451 0.2114 0.1897 -0.0228 0.0040  0.0289  71  LEU A CG  
582  C CD1 . LEU A 72  ? 0.2662 0.2399 0.2229 -0.0156 0.0019  0.0276  71  LEU A CD1 
583  C CD2 . LEU A 72  ? 0.2890 0.2582 0.2310 -0.0255 0.0088  0.0269  71  LEU A CD2 
584  N N   . ALA A 73  ? 0.3103 0.2501 0.2339 -0.0297 -0.0043 0.0364  72  ALA A N   
585  C CA  . ALA A 73  ? 0.3094 0.2385 0.2245 -0.0285 -0.0116 0.0404  72  ALA A CA  
586  C C   . ALA A 73  ? 0.3442 0.2706 0.2649 -0.0233 -0.0164 0.0416  72  ALA A C   
587  O O   . ALA A 73  ? 0.3234 0.2472 0.2454 -0.0183 -0.0226 0.0434  72  ALA A O   
588  C CB  . ALA A 73  ? 0.3220 0.2386 0.2205 -0.0361 -0.0116 0.0431  72  ALA A CB  
589  N N   . ASP A 74  ? 0.2894 0.2169 0.2140 -0.0244 -0.0135 0.0403  73  ASP A N   
590  C CA  . ASP A 74  ? 0.3254 0.2499 0.2549 -0.0200 -0.0173 0.0410  73  ASP A CA  
591  C C   . ASP A 74  ? 0.2831 0.2186 0.2271 -0.0131 -0.0179 0.0384  73  ASP A C   
592  O O   . ASP A 74  ? 0.2913 0.2244 0.2392 -0.0082 -0.0226 0.0391  73  ASP A O   
593  C CB  . ASP A 74  ? 0.3223 0.2437 0.2499 -0.0244 -0.0139 0.0404  73  ASP A CB  
594  C CG  . ASP A 74  ? 0.4148 0.3217 0.3266 -0.0307 -0.0148 0.0435  73  ASP A CG  
595  O OD1 . ASP A 74  ? 0.4512 0.3493 0.3536 -0.0309 -0.0193 0.0467  73  ASP A OD1 
596  O OD2 . ASP A 74  ? 0.4309 0.3351 0.3393 -0.0360 -0.0110 0.0427  73  ASP A OD2 
597  N N   . LEU A 75  ? 0.2700 0.2171 0.2215 -0.0128 -0.0133 0.0354  74  LEU A N   
598  C CA  . LEU A 75  ? 0.2673 0.2236 0.2304 -0.0068 -0.0141 0.0332  74  LEU A CA  
599  C C   . LEU A 75  ? 0.2580 0.2129 0.2203 -0.0031 -0.0189 0.0344  74  LEU A C   
600  O O   . LEU A 75  ? 0.2662 0.2228 0.2351 0.0020  -0.0224 0.0338  74  LEU A O   
601  C CB  . LEU A 75  ? 0.2233 0.1907 0.1930 -0.0073 -0.0085 0.0301  74  LEU A CB  
602  C CG  . LEU A 75  ? 0.2343 0.2103 0.2142 -0.0018 -0.0091 0.0280  74  LEU A CG  
603  C CD1 . LEU A 75  ? 0.2511 0.2285 0.2382 0.0013  -0.0107 0.0270  74  LEU A CD1 
604  C CD2 . LEU A 75  ? 0.2143 0.1993 0.1989 -0.0023 -0.0041 0.0254  74  LEU A CD2 
605  N N   . ILE A 76  ? 0.2578 0.2099 0.2119 -0.0060 -0.0190 0.0358  75  ILE A N   
606  C CA  . ILE A 76  ? 0.2398 0.1907 0.1922 -0.0032 -0.0239 0.0370  75  ILE A CA  
607  C C   . ILE A 76  ? 0.2728 0.2155 0.2235 -0.0002 -0.0308 0.0396  75  ILE A C   
608  O O   . ILE A 76  ? 0.2635 0.2091 0.2205 0.0050  -0.0349 0.0391  75  ILE A O   
609  C CB  . ILE A 76  ? 0.2306 0.1780 0.1721 -0.0083 -0.0227 0.0384  75  ILE A CB  
610  C CG1 . ILE A 76  ? 0.2730 0.2296 0.2185 -0.0098 -0.0162 0.0351  75  ILE A CG1 
611  C CG2 . ILE A 76  ? 0.2744 0.2184 0.2117 -0.0064 -0.0290 0.0405  75  ILE A CG2 
612  C CD1 . ILE A 76  ? 0.2598 0.2129 0.1944 -0.0159 -0.0133 0.0357  75  ILE A CD1 
613  N N   . ALA A 77  ? 0.2752 0.2073 0.2171 -0.0035 -0.0320 0.0423  76  ALA A N   
614  C CA  . ALA A 77  ? 0.2856 0.2083 0.2252 -0.0003 -0.0388 0.0451  76  ALA A CA  
615  C C   . ALA A 77  ? 0.2685 0.1956 0.2204 0.0055  -0.0397 0.0428  76  ALA A C   
616  O O   . ALA A 77  ? 0.3104 0.2359 0.2666 0.0107  -0.0453 0.0432  76  ALA A O   
617  C CB  . ALA A 77  ? 0.3196 0.2291 0.2468 -0.0055 -0.0391 0.0482  76  ALA A CB  
618  N N   . THR A 78  ? 0.2555 0.1883 0.2134 0.0045  -0.0344 0.0401  77  THR A N   
619  C CA  . THR A 78  ? 0.2247 0.1613 0.1933 0.0091  -0.0347 0.0376  77  THR A CA  
620  C C   . THR A 78  ? 0.2649 0.2114 0.2435 0.0140  -0.0358 0.0350  77  THR A C   
621  O O   . THR A 78  ? 0.2455 0.1920 0.2307 0.0188  -0.0393 0.0340  77  THR A O   
622  C CB  . THR A 78  ? 0.2296 0.1708 0.2016 0.0062  -0.0289 0.0354  77  THR A CB  
623  O OG1 . THR A 78  ? 0.3017 0.2339 0.2643 0.0010  -0.0276 0.0375  77  THR A OG1 
624  C CG2 . THR A 78  ? 0.2539 0.1984 0.2357 0.0101  -0.0291 0.0329  77  THR A CG2 
625  N N   . VAL A 79  ? 0.2250 0.1798 0.2050 0.0128  -0.0325 0.0335  78  VAL A N   
626  C CA  . VAL A 79  ? 0.2178 0.1814 0.2058 0.0166  -0.0330 0.0308  78  VAL A CA  
627  C C   . VAL A 79  ? 0.2697 0.2306 0.2572 0.0198  -0.0392 0.0321  78  VAL A C   
628  O O   . VAL A 79  ? 0.2698 0.2350 0.2658 0.0243  -0.0415 0.0299  78  VAL A O   
629  C CB  . VAL A 79  ? 0.2684 0.2391 0.2557 0.0141  -0.0284 0.0295  78  VAL A CB  
630  C CG1 . VAL A 79  ? 0.2788 0.2564 0.2714 0.0173  -0.0297 0.0274  78  VAL A CG1 
631  C CG2 . VAL A 79  ? 0.2612 0.2369 0.2528 0.0127  -0.0230 0.0275  78  VAL A CG2 
632  N N   . ASN A 80  ? 0.2578 0.2117 0.2353 0.0173  -0.0421 0.0356  79  ASN A N   
633  C CA  A ASN A 80  ? 0.3036 0.2554 0.2805 0.0204  -0.0487 0.0370  79  ASN A CA  
634  C CA  B ASN A 80  ? 0.3046 0.2561 0.2811 0.0202  -0.0488 0.0371  79  ASN A CA  
635  C C   . ASN A 80  ? 0.3245 0.2706 0.3056 0.0249  -0.0539 0.0377  79  ASN A C   
636  O O   . ASN A 80  ? 0.3451 0.2945 0.3332 0.0297  -0.0584 0.0366  79  ASN A O   
637  C CB  A ASN A 80  ? 0.3311 0.2761 0.2951 0.0161  -0.0509 0.0408  79  ASN A CB  
638  C CB  B ASN A 80  ? 0.3326 0.2763 0.2958 0.0159  -0.0511 0.0411  79  ASN A CB  
639  C CG  A ASN A 80  ? 0.3679 0.3191 0.3287 0.0121  -0.0458 0.0394  79  ASN A CG  
640  C CG  B ASN A 80  ? 0.3536 0.2937 0.3151 0.0189  -0.0592 0.0435  79  ASN A CG  
641  O OD1 A ASN A 80  ? 0.4120 0.3731 0.3808 0.0138  -0.0427 0.0360  79  ASN A OD1 
642  O OD1 B ASN A 80  ? 0.4147 0.3627 0.3826 0.0218  -0.0612 0.0415  79  ASN A OD1 
643  N ND2 A ASN A 80  ? 0.4291 0.3740 0.3779 0.0065  -0.0448 0.0420  79  ASN A ND2 
644  N ND2 B ASN A 80  ? 0.4562 0.3840 0.4086 0.0180  -0.0641 0.0476  79  ASN A ND2 
645  N N   . ALA A 81  ? 0.2823 0.2202 0.2598 0.0235  -0.0530 0.0392  80  ALA A N   
646  C CA  . ALA A 81  ? 0.3316 0.2630 0.3130 0.0279  -0.0574 0.0396  80  ALA A CA  
647  C C   . ALA A 81  ? 0.3384 0.2791 0.3342 0.0328  -0.0563 0.0349  80  ALA A C   
648  O O   . ALA A 81  ? 0.3800 0.3196 0.3824 0.0381  -0.0610 0.0341  80  ALA A O   
649  C CB  . ALA A 81  ? 0.4025 0.3237 0.3772 0.0247  -0.0554 0.0414  80  ALA A CB  
650  N N   . ILE A 82  ? 0.2592 0.2091 0.2600 0.0312  -0.0503 0.0315  81  ILE A N   
651  C CA  . ILE A 82  ? 0.2402 0.1987 0.2532 0.0348  -0.0487 0.0269  81  ILE A CA  
652  C C   . ILE A 82  ? 0.2826 0.2496 0.3014 0.0376  -0.0509 0.0248  81  ILE A C   
653  O O   . ILE A 82  ? 0.2911 0.2610 0.3187 0.0421  -0.0537 0.0222  81  ILE A O   
654  C CB  . ILE A 82  ? 0.2390 0.2033 0.2539 0.0317  -0.0419 0.0245  81  ILE A CB  
655  C CG1 . ILE A 82  ? 0.2502 0.2073 0.2612 0.0290  -0.0398 0.0257  81  ILE A CG1 
656  C CG2 . ILE A 82  ? 0.2280 0.2013 0.2536 0.0344  -0.0400 0.0197  81  ILE A CG2 
657  C CD1 . ILE A 82  ? 0.2410 0.2029 0.2504 0.0247  -0.0339 0.0249  81  ILE A CD1 
658  N N   . THR A 83  ? 0.2269 0.1979 0.2409 0.0347  -0.0494 0.0256  82  THR A N   
659  C CA  . THR A 83  ? 0.2300 0.2100 0.2494 0.0365  -0.0503 0.0229  82  THR A CA  
660  C C   . THR A 83  ? 0.2837 0.2619 0.3032 0.0395  -0.0575 0.0245  82  THR A C   
661  O O   . THR A 83  ? 0.2751 0.2611 0.3026 0.0423  -0.0592 0.0214  82  THR A O   
662  C CB  . THR A 83  ? 0.2399 0.2246 0.2541 0.0324  -0.0460 0.0229  82  THR A CB  
663  O OG1 . THR A 83  ? 0.2530 0.2311 0.2561 0.0291  -0.0475 0.0270  82  THR A OG1 
664  C CG2 . THR A 83  ? 0.2659 0.2539 0.2817 0.0303  -0.0394 0.0209  82  THR A CG2 
665  N N   . GLN A 84  ? 0.2909 0.2590 0.3016 0.0387  -0.0618 0.0293  83  GLN A N   
666  C CA  A GLN A 84  ? 0.2984 0.2642 0.3090 0.0418  -0.0696 0.0312  83  GLN A CA  
667  C CA  B GLN A 84  ? 0.3006 0.2659 0.3109 0.0418  -0.0697 0.0314  83  GLN A CA  
668  C C   . GLN A 84  ? 0.3036 0.2719 0.3268 0.0483  -0.0733 0.0284  83  GLN A C   
669  O O   . GLN A 84  ? 0.2952 0.2672 0.3235 0.0518  -0.0791 0.0279  83  GLN A O   
670  C CB  A GLN A 84  ? 0.3500 0.3025 0.3473 0.0394  -0.0737 0.0371  83  GLN A CB  
671  C CB  B GLN A 84  ? 0.3497 0.3013 0.3473 0.0397  -0.0736 0.0371  83  GLN A CB  
672  C CG  A GLN A 84  ? 0.3345 0.2855 0.3193 0.0331  -0.0718 0.0398  83  GLN A CG  
673  C CG  B GLN A 84  ? 0.4148 0.3602 0.4127 0.0441  -0.0827 0.0399  83  GLN A CG  
674  C CD  A GLN A 84  ? 0.4246 0.3617 0.3948 0.0290  -0.0736 0.0450  83  GLN A CD  
675  C CD  B GLN A 84  ? 0.4631 0.3928 0.4479 0.0419  -0.0861 0.0455  83  GLN A CD  
676  O OE1 A GLN A 84  ? 0.4545 0.3822 0.4229 0.0307  -0.0763 0.0471  83  GLN A OE1 
677  O OE1 B GLN A 84  ? 0.5493 0.4725 0.5287 0.0387  -0.0817 0.0463  83  GLN A OE1 
678  N NE2 A GLN A 84  ? 0.4466 0.3821 0.4056 0.0232  -0.0717 0.0470  83  GLN A NE2 
679  N NE2 B GLN A 84  ? 0.4407 0.3640 0.4197 0.0433  -0.0943 0.0494  83  GLN A NE2 
680  N N   . LYS A 85  ? 0.3403 0.3073 0.3692 0.0497  -0.0700 0.0261  84  LYS A N   
681  C CA  A LYS A 85  ? 0.3590 0.3283 0.4003 0.0555  -0.0724 0.0226  84  LYS A CA  
682  C CA  B LYS A 85  ? 0.3582 0.3277 0.3996 0.0556  -0.0726 0.0226  84  LYS A CA  
683  C CA  C LYS A 85  ? 0.3585 0.3279 0.3999 0.0555  -0.0725 0.0226  84  LYS A CA  
684  C C   . LYS A 85  ? 0.3914 0.3742 0.4445 0.0566  -0.0686 0.0163  84  LYS A C   
685  O O   . LYS A 85  ? 0.3944 0.3809 0.4589 0.0612  -0.0702 0.0125  84  LYS A O   
686  C CB  A LYS A 85  ? 0.3809 0.3417 0.4219 0.0558  -0.0702 0.0228  84  LYS A CB  
687  C CB  B LYS A 85  ? 0.3815 0.3421 0.4229 0.0563  -0.0709 0.0229  84  LYS A CB  
688  C CB  C LYS A 85  ? 0.3809 0.3416 0.4223 0.0562  -0.0706 0.0228  84  LYS A CB  
689  C CG  A LYS A 85  ? 0.3878 0.3343 0.4158 0.0536  -0.0729 0.0288  84  LYS A CG  
690  C CG  B LYS A 85  ? 0.4076 0.3536 0.4391 0.0566  -0.0761 0.0286  84  LYS A CG  
691  C CG  C LYS A 85  ? 0.4092 0.3568 0.4458 0.0590  -0.0772 0.0272  84  LYS A CG  
692  C CD  A LYS A 85  ? 0.4232 0.3638 0.4476 0.0566  -0.0816 0.0327  84  LYS A CD  
693  C CD  B LYS A 85  ? 0.4270 0.3648 0.4614 0.0588  -0.0754 0.0278  84  LYS A CD  
694  C CD  C LYS A 85  ? 0.4230 0.3611 0.4436 0.0542  -0.0788 0.0332  84  LYS A CD  
695  C CE  A LYS A 85  ? 0.4570 0.3810 0.4695 0.0554  -0.0850 0.0381  84  LYS A CE  
696  C CE  B LYS A 85  ? 0.4305 0.3717 0.4790 0.0659  -0.0788 0.0239  84  LYS A CE  
697  C CE  C LYS A 85  ? 0.4530 0.3787 0.4682 0.0573  -0.0872 0.0379  84  LYS A CE  
698  N NZ  A LYS A 85  ? 0.5078 0.4258 0.5106 0.0549  -0.0920 0.0432  84  LYS A NZ  
699  N NZ  B LYS A 85  ? 0.5271 0.4635 0.5756 0.0707  -0.0879 0.0271  84  LYS A NZ  
700  N NZ  C LYS A 85  ? 0.4588 0.3767 0.4793 0.0616  -0.0885 0.0370  84  LYS A NZ  
701  N N   . GLY A 86  ? 0.3262 0.3348 0.3563 0.0506  -0.0415 0.0013  85  GLY A N   
702  C CA  . GLY A 86  ? 0.2745 0.2904 0.3113 0.0489  -0.0393 -0.0035 85  GLY A CA  
703  C C   . GLY A 86  ? 0.2780 0.2907 0.3150 0.0457  -0.0343 -0.0054 85  GLY A C   
704  O O   . GLY A 86  ? 0.3130 0.3312 0.3546 0.0438  -0.0322 -0.0091 85  GLY A O   
705  N N   . ALA A 87  ? 0.2535 0.2576 0.2856 0.0449  -0.0326 -0.0031 86  ALA A N   
706  C CA  . ALA A 87  ? 0.2383 0.2393 0.2700 0.0417  -0.0284 -0.0048 86  ALA A CA  
707  C C   . ALA A 87  ? 0.2434 0.2449 0.2702 0.0373  -0.0267 -0.0045 86  ALA A C   
708  O O   . ALA A 87  ? 0.2344 0.2366 0.2568 0.0366  -0.0283 -0.0027 86  ALA A O   
709  C CB  . ALA A 87  ? 0.2548 0.2466 0.2842 0.0426  -0.0274 -0.0027 86  ALA A CB  
710  N N   . TYR A 88  ? 0.2038 0.2047 0.2312 0.0344  -0.0235 -0.0064 87  TYR A N   
711  C CA  . TYR A 88  ? 0.1810 0.1819 0.2048 0.0305  -0.0216 -0.0063 87  TYR A CA  
712  C C   . TYR A 88  ? 0.2181 0.2119 0.2371 0.0291  -0.0203 -0.0036 87  TYR A C   
713  O O   . TYR A 88  ? 0.2159 0.2048 0.2353 0.0297  -0.0195 -0.0032 87  TYR A O   
714  C CB  . TYR A 88  ? 0.1768 0.1809 0.2038 0.0280  -0.0191 -0.0094 87  TYR A CB  
715  C CG  . TYR A 88  ? 0.1860 0.1976 0.2174 0.0280  -0.0197 -0.0121 87  TYR A CG  
716  C CD1 . TYR A 88  ? 0.1886 0.2040 0.2256 0.0305  -0.0204 -0.0140 87  TYR A CD1 
717  C CD2 . TYR A 88  ? 0.1704 0.1852 0.2008 0.0254  -0.0193 -0.0129 87  TYR A CD2 
718  C CE1 . TYR A 88  ? 0.1538 0.1767 0.1954 0.0300  -0.0207 -0.0166 87  TYR A CE1 
719  C CE2 . TYR A 88  ? 0.1551 0.1767 0.1897 0.0249  -0.0198 -0.0154 87  TYR A CE2 
720  C CZ  . TYR A 88  ? 0.1961 0.2219 0.2363 0.0270  -0.0204 -0.0173 87  TYR A CZ  
721  O OH  . TYR A 88  ? 0.2022 0.2351 0.2471 0.0261  -0.0206 -0.0199 87  TYR A OH  
722  N N   . ALA A 89  ? 0.1939 0.1872 0.2084 0.0270  -0.0200 -0.0021 88  ALA A N   
723  C CA  . ALA A 89  ? 0.1889 0.1766 0.1993 0.0252  -0.0184 0.0002  88  ALA A CA  
724  C C   . ALA A 89  ? 0.1944 0.1840 0.2050 0.0219  -0.0160 -0.0011 88  ALA A C   
725  O O   . ALA A 89  ? 0.2107 0.2041 0.2207 0.0209  -0.0160 -0.0020 88  ALA A O   
726  C CB  . ALA A 89  ? 0.1978 0.1834 0.2025 0.0256  -0.0197 0.0034  88  ALA A CB  
727  N N   . VAL A 90  ? 0.1884 0.1753 0.2001 0.0202  -0.0142 -0.0014 89  VAL A N   
728  C CA  . VAL A 90  ? 0.1843 0.1727 0.1966 0.0174  -0.0123 -0.0022 89  VAL A CA  
729  C C   . VAL A 90  ? 0.2162 0.2019 0.2253 0.0158  -0.0111 0.0000  89  VAL A C   
730  O O   . VAL A 90  ? 0.1953 0.1765 0.2032 0.0154  -0.0107 0.0017  89  VAL A O   
731  C CB  . VAL A 90  ? 0.1911 0.1788 0.2061 0.0163  -0.0113 -0.0037 89  VAL A CB  
732  C CG1 . VAL A 90  ? 0.2052 0.1949 0.2210 0.0137  -0.0100 -0.0043 89  VAL A CG1 
733  C CG2 . VAL A 90  ? 0.1961 0.1862 0.2140 0.0178  -0.0120 -0.0061 89  VAL A CG2 
734  N N   . VAL A 91  ? 0.1942 0.1826 0.2022 0.0147  -0.0104 -0.0002 90  VAL A N   
735  C CA  A VAL A 91  ? 0.1852 0.1722 0.1907 0.0131  -0.0086 0.0014  90  VAL A CA  
736  C CA  B VAL A 91  ? 0.1865 0.1733 0.1920 0.0131  -0.0086 0.0015  90  VAL A CA  
737  C C   . VAL A 91  ? 0.1781 0.1657 0.1870 0.0110  -0.0070 0.0007  90  VAL A C   
738  O O   . VAL A 91  ? 0.2062 0.1969 0.2174 0.0105  -0.0066 -0.0010 90  VAL A O   
739  C CB  A VAL A 91  ? 0.1954 0.1852 0.1983 0.0131  -0.0085 0.0009  90  VAL A CB  
740  C CB  B VAL A 91  ? 0.1980 0.1872 0.2004 0.0131  -0.0084 0.0014  90  VAL A CB  
741  C CG1 A VAL A 91  ? 0.1981 0.1874 0.1989 0.0113  -0.0060 0.0019  90  VAL A CG1 
742  C CG1 B VAL A 91  ? 0.2105 0.1982 0.2085 0.0149  -0.0103 0.0030  90  VAL A CG1 
743  C CG2 A VAL A 91  ? 0.2040 0.1934 0.2033 0.0151  -0.0107 0.0019  90  VAL A CG2 
744  C CG2 B VAL A 91  ? 0.1925 0.1859 0.1974 0.0131  -0.0087 -0.0014 90  VAL A CG2 
745  N N   . ASP A 92  ? 0.1712 0.1557 0.1804 0.0097  -0.0062 0.0020  91  ASP A N   
746  C CA  . ASP A 92  ? 0.1961 0.1813 0.2088 0.0078  -0.0054 0.0013  91  ASP A CA  
747  C C   . ASP A 92  ? 0.1811 0.1664 0.1943 0.0058  -0.0035 0.0026  91  ASP A C   
748  O O   . ASP A 92  ? 0.2065 0.1884 0.2185 0.0046  -0.0028 0.0042  91  ASP A O   
749  C CB  . ASP A 92  ? 0.1972 0.1793 0.2108 0.0077  -0.0063 0.0011  91  ASP A CB  
750  C CG  . ASP A 92  ? 0.2110 0.1929 0.2271 0.0053  -0.0057 0.0009  91  ASP A CG  
751  O OD1 . ASP A 92  ? 0.2067 0.1921 0.2253 0.0042  -0.0052 0.0005  91  ASP A OD1 
752  O OD2 . ASP A 92  ? 0.2071 0.1851 0.2228 0.0046  -0.0059 0.0012  91  ASP A OD2 
753  N N   . PRO A 93  ? 0.1704 0.1594 0.1855 0.0052  -0.0023 0.0019  92  PRO A N   
754  C CA  . PRO A 93  ? 0.1760 0.1661 0.1932 0.0032  -0.0002 0.0026  92  PRO A CA  
755  C C   . PRO A 93  ? 0.1563 0.1465 0.1775 0.0017  -0.0010 0.0024  92  PRO A C   
756  O O   . PRO A 93  ? 0.2053 0.1981 0.2297 0.0019  -0.0020 0.0012  92  PRO A O   
757  C CB  . PRO A 93  ? 0.1871 0.1813 0.2062 0.0037  0.0010  0.0013  92  PRO A CB  
758  C CG  . PRO A 93  ? 0.2049 0.1996 0.2227 0.0056  -0.0006 -0.0001 92  PRO A CG  
759  C CD  . PRO A 93  ? 0.2562 0.2485 0.2728 0.0062  -0.0027 0.0001  92  PRO A CD  
760  N N   . HIS A 94  ? 0.1875 0.1746 0.2080 0.0002  -0.0006 0.0036  93  HIS A N   
761  C CA  . HIS A 94  ? 0.1610 0.1472 0.1840 -0.0014 -0.0018 0.0031  93  HIS A CA  
762  C C   . HIS A 94  ? 0.1854 0.1754 0.2134 -0.0036 -0.0009 0.0031  93  HIS A C   
763  O O   . HIS A 94  ? 0.2108 0.1997 0.2402 -0.0061 -0.0001 0.0038  93  HIS A O   
764  C CB  . HIS A 94  ? 0.1827 0.1631 0.2028 -0.0020 -0.0018 0.0042  93  HIS A CB  
765  C CG  . HIS A 94  ? 0.1962 0.1742 0.2171 -0.0027 -0.0034 0.0029  93  HIS A CG  
766  N ND1 . HIS A 94  ? 0.2148 0.1919 0.2344 -0.0007 -0.0049 0.0014  93  HIS A ND1 
767  C CD2 . HIS A 94  ? 0.2059 0.1824 0.2286 -0.0054 -0.0035 0.0025  93  HIS A CD2 
768  C CE1 . HIS A 94  ? 0.2333 0.2082 0.2535 -0.0021 -0.0058 0.0001  93  HIS A CE1 
769  N NE2 . HIS A 94  ? 0.2360 0.2103 0.2579 -0.0050 -0.0051 0.0007  93  HIS A NE2 
770  N N   . ASN A 95  ? 0.1915 0.1861 0.2228 -0.0028 -0.0011 0.0022  94  ASN A N   
771  C CA  . ASN A 95  ? 0.1609 0.1601 0.1975 -0.0041 0.0002  0.0023  94  ASN A CA  
772  C C   . ASN A 95  ? 0.1828 0.1858 0.2247 -0.0044 -0.0018 0.0016  94  ASN A C   
773  O O   . ASN A 95  ? 0.1847 0.1921 0.2320 -0.0051 -0.0009 0.0016  94  ASN A O   
774  C CB  . ASN A 95  ? 0.1910 0.1925 0.2276 -0.0027 0.0025  0.0022  94  ASN A CB  
775  C CG  . ASN A 95  ? 0.1764 0.1765 0.2103 -0.0040 0.0054  0.0033  94  ASN A CG  
776  O OD1 . ASN A 95  ? 0.2163 0.2120 0.2444 -0.0037 0.0053  0.0044  94  ASN A OD1 
777  N ND2 . ASN A 95  ? 0.2013 0.2053 0.2395 -0.0055 0.0078  0.0034  94  ASN A ND2 
778  N N   . TYR A 96  ? 0.2039 0.2056 0.2444 -0.0040 -0.0043 0.0010  95  TYR A N   
779  C CA  . TYR A 96  ? 0.1780 0.1829 0.2225 -0.0048 -0.0067 0.0007  95  TYR A CA  
780  C C   . TYR A 96  ? 0.1666 0.1759 0.2159 -0.0032 -0.0068 0.0008  95  TYR A C   
781  O O   . TYR A 96  ? 0.1999 0.2129 0.2541 -0.0039 -0.0083 0.0011  95  TYR A O   
782  C CB  . TYR A 96  ? 0.1771 0.1830 0.2246 -0.0078 -0.0070 0.0009  95  TYR A CB  
783  C CG  . TYR A 96  ? 0.1910 0.1914 0.2340 -0.0093 -0.0068 0.0006  95  TYR A CG  
784  C CD1 . TYR A 96  ? 0.2242 0.2218 0.2639 -0.0097 -0.0089 -0.0004 95  TYR A CD1 
785  C CD2 . TYR A 96  ? 0.2261 0.2239 0.2677 -0.0104 -0.0043 0.0015  95  TYR A CD2 
786  C CE1 . TYR A 96  ? 0.2396 0.2318 0.2757 -0.0108 -0.0085 -0.0010 95  TYR A CE1 
787  C CE2 . TYR A 96  ? 0.2409 0.2328 0.2786 -0.0115 -0.0043 0.0014  95  TYR A CE2 
788  C CZ  . TYR A 96  ? 0.2414 0.2305 0.2767 -0.0115 -0.0064 0.0001  95  TYR A CZ  
789  O OH  . TYR A 96  ? 0.2996 0.2825 0.3315 -0.0123 -0.0062 -0.0003 95  TYR A OH  
790  N N   . GLY A 97  ? 0.1806 0.1895 0.2285 -0.0011 -0.0053 0.0006  96  GLY A N   
791  C CA  . GLY A 97  ? 0.1958 0.2079 0.2482 0.0006  -0.0050 0.0004  96  GLY A CA  
792  C C   . GLY A 97  ? 0.1958 0.2122 0.2541 0.0003  -0.0029 0.0003  96  GLY A C   
793  O O   . GLY A 97  ? 0.1835 0.2034 0.2475 0.0017  -0.0030 0.0001  96  GLY A O   
794  N N   . ARG A 98  ? 0.1700 0.1861 0.2273 -0.0016 -0.0007 0.0005  97  ARG A N   
795  C CA  . ARG A 98  ? 0.1703 0.1909 0.2334 -0.0027 0.0017  0.0005  97  ARG A CA  
796  C C   . ARG A 98  ? 0.2052 0.2243 0.2645 -0.0033 0.0056  0.0004  97  ARG A C   
797  O O   . ARG A 98  ? 0.2099 0.2241 0.2622 -0.0037 0.0058  0.0010  97  ARG A O   
798  C CB  . ARG A 98  ? 0.1839 0.2064 0.2506 -0.0057 0.0003  0.0011  97  ARG A CB  
799  C CG  . ARG A 98  ? 0.1798 0.2055 0.2512 -0.0053 -0.0036 0.0011  97  ARG A CG  
800  C CD  . ARG A 98  ? 0.1888 0.2139 0.2598 -0.0084 -0.0061 0.0014  97  ARG A CD  
801  N NE  . ARG A 98  ? 0.1910 0.2204 0.2673 -0.0084 -0.0098 0.0015  97  ARG A NE  
802  C CZ  . ARG A 98  ? 0.1875 0.2154 0.2611 -0.0070 -0.0130 0.0019  97  ARG A CZ  
803  N NH1 . ARG A 98  ? 0.2047 0.2273 0.2711 -0.0058 -0.0130 0.0018  97  ARG A NH1 
804  N NH2 . ARG A 98  ? 0.1848 0.2171 0.2634 -0.0070 -0.0165 0.0024  97  ARG A NH2 
805  N N   . TYR A 99  ? 0.2058 0.2292 0.2698 -0.0033 0.0087  -0.0002 98  TYR A N   
806  C CA  . TYR A 99  ? 0.2130 0.2356 0.2731 -0.0041 0.0127  -0.0003 98  TYR A CA  
807  C C   . TYR A 99  ? 0.1961 0.2241 0.2630 -0.0063 0.0157  -0.0004 98  TYR A C   
808  O O   . TYR A 99  ? 0.1922 0.2260 0.2674 -0.0052 0.0159  -0.0015 98  TYR A O   
809  C CB  . TYR A 99  ? 0.1840 0.2063 0.2419 -0.0013 0.0142  -0.0018 98  TYR A CB  
810  C CG  . TYR A 99  ? 0.2029 0.2242 0.2553 -0.0020 0.0182  -0.0021 98  TYR A CG  
811  C CD1 . TYR A 99  ? 0.2149 0.2308 0.2580 -0.0026 0.0178  -0.0008 98  TYR A CD1 
812  C CD2 . TYR A 99  ? 0.1974 0.2231 0.2535 -0.0020 0.0222  -0.0037 98  TYR A CD2 
813  C CE1 . TYR A 99  ? 0.1964 0.2112 0.2335 -0.0033 0.0211  -0.0008 98  TYR A CE1 
814  C CE2 . TYR A 99  ? 0.2281 0.2528 0.2781 -0.0029 0.0260  -0.0040 98  TYR A CE2 
815  C CZ  . TYR A 99  ? 0.2528 0.2720 0.2929 -0.0037 0.0253  -0.0024 98  TYR A CZ  
816  O OH  . TYR A 99  ? 0.2313 0.2495 0.2646 -0.0046 0.0287  -0.0024 98  TYR A OH  
817  N N   . TYR A 100 ? 0.1920 0.2181 0.2556 -0.0094 0.0178  0.0009  99  TYR A N   
818  C CA  . TYR A 100 ? 0.1928 0.2238 0.2629 -0.0125 0.0203  0.0011  99  TYR A CA  
819  C C   . TYR A 100 ? 0.2125 0.2482 0.2915 -0.0130 0.0170  0.0007  99  TYR A C   
820  O O   . TYR A 100 ? 0.2211 0.2640 0.3094 -0.0136 0.0183  -0.0002 99  TYR A O   
821  C CB  . TYR A 100 ? 0.2264 0.2625 0.2997 -0.0122 0.0252  -0.0003 99  TYR A CB  
822  C CG  . TYR A 100 ? 0.2133 0.2448 0.2769 -0.0133 0.0288  0.0006  99  TYR A CG  
823  C CD1 . TYR A 100 ? 0.2318 0.2609 0.2919 -0.0172 0.0311  0.0026  99  TYR A CD1 
824  C CD2 . TYR A 100 ? 0.2450 0.2743 0.3027 -0.0106 0.0295  -0.0004 99  TYR A CD2 
825  C CE1 . TYR A 100 ? 0.2525 0.2771 0.3029 -0.0182 0.0340  0.0040  99  TYR A CE1 
826  C CE2 . TYR A 100 ? 0.3042 0.3296 0.3524 -0.0116 0.0322  0.0005  99  TYR A CE2 
827  C CZ  . TYR A 100 ? 0.2845 0.3075 0.3288 -0.0153 0.0344  0.0029  99  TYR A CZ  
828  O OH  . TYR A 100 ? 0.2732 0.2919 0.3073 -0.0162 0.0368  0.0044  99  TYR A OH  
829  N N   . ASN A 101 ? 0.2002 0.2320 0.2764 -0.0125 0.0126  0.0012  100 ASN A N   
830  C CA  A ASN A 101 ? 0.2191 0.2539 0.3012 -0.0135 0.0087  0.0011  100 ASN A CA  
831  C CA  B ASN A 101 ? 0.2195 0.2545 0.3017 -0.0135 0.0088  0.0011  100 ASN A CA  
832  C C   . ASN A 101 ? 0.2161 0.2571 0.3062 -0.0107 0.0068  0.0002  100 ASN A C   
833  O O   . ASN A 101 ? 0.2584 0.3039 0.3550 -0.0115 0.0038  0.0002  100 ASN A O   
834  C CB  A ASN A 101 ? 0.2338 0.2713 0.3203 -0.0179 0.0099  0.0015  100 ASN A CB  
835  C CB  B ASN A 101 ? 0.2336 0.2715 0.3206 -0.0178 0.0100  0.0014  100 ASN A CB  
836  C CG  A ASN A 101 ? 0.2761 0.3064 0.3545 -0.0206 0.0119  0.0027  100 ASN A CG  
837  C CG  B ASN A 101 ? 0.2913 0.3303 0.3814 -0.0196 0.0056  0.0013  100 ASN A CG  
838  O OD1 A ASN A 101 ? 0.2675 0.2916 0.3403 -0.0210 0.0093  0.0032  100 ASN A OD1 
839  O OD1 B ASN A 101 ? 0.3229 0.3576 0.4081 -0.0183 0.0020  0.0014  100 ASN A OD1 
840  N ND2 A ASN A 101 ? 0.2489 0.2795 0.3264 -0.0223 0.0166  0.0033  100 ASN A ND2 
841  N ND2 B ASN A 101 ? 0.3728 0.4178 0.4709 -0.0227 0.0058  0.0009  100 ASN A ND2 
842  N N   . SER A 102 ? 0.2046 0.2458 0.2942 -0.0073 0.0082  -0.0005 101 SER A N   
843  C CA  . SER A 102 ? 0.1672 0.2123 0.2633 -0.0040 0.0062  -0.0012 101 SER A CA  
844  C C   . SER A 102 ? 0.1775 0.2166 0.2667 -0.0015 0.0038  -0.0009 101 SER A C   
845  O O   . SER A 102 ? 0.2115 0.2456 0.2930 -0.0011 0.0055  -0.0011 101 SER A O   
846  C CB  . SER A 102 ? 0.2498 0.2998 0.3520 -0.0021 0.0102  -0.0028 101 SER A CB  
847  O OG  . SER A 102 ? 0.3097 0.3659 0.4188 -0.0047 0.0130  -0.0032 101 SER A OG  
848  N N   . ILE A 103 ? 0.1861 0.2261 0.2782 0.0002  -0.0003 -0.0004 102 ILE A N   
849  C CA  . ILE A 103 ? 0.1786 0.2135 0.2650 0.0024  -0.0023 -0.0001 102 ILE A CA  
850  C C   . ILE A 103 ? 0.2345 0.2678 0.3195 0.0048  0.0009  -0.0014 102 ILE A C   
851  O O   . ILE A 103 ? 0.2271 0.2645 0.3186 0.0064  0.0031  -0.0026 102 ILE A O   
852  C CB  . ILE A 103 ? 0.2075 0.2442 0.2982 0.0038  -0.0068 0.0010  102 ILE A CB  
853  C CG1 . ILE A 103 ? 0.2141 0.2508 0.3029 0.0011  -0.0103 0.0020  102 ILE A CG1 
854  C CG2 . ILE A 103 ? 0.2257 0.2577 0.3119 0.0063  -0.0080 0.0012  102 ILE A CG2 
855  C CD1 . ILE A 103 ? 0.2737 0.3135 0.3671 0.0019  -0.0150 0.0033  102 ILE A CD1 
856  N N   . ILE A 104 ? 0.1944 0.2221 0.2712 0.0051  0.0011  -0.0016 103 ILE A N   
857  C CA  . ILE A 104 ? 0.1960 0.2217 0.2703 0.0072  0.0035  -0.0031 103 ILE A CA  
858  C C   . ILE A 104 ? 0.2473 0.2727 0.3256 0.0099  0.0016  -0.0033 103 ILE A C   
859  O O   . ILE A 104 ? 0.2312 0.2532 0.3061 0.0102  -0.0013 -0.0023 103 ILE A O   
860  C CB  . ILE A 104 ? 0.1966 0.2168 0.2614 0.0065  0.0036  -0.0032 103 ILE A CB  
861  C CG1 . ILE A 104 ? 0.2061 0.2256 0.2669 0.0041  0.0051  -0.0025 103 ILE A CG1 
862  C CG2 . ILE A 104 ? 0.2669 0.2853 0.3292 0.0083  0.0058  -0.0050 103 ILE A CG2 
863  C CD1 . ILE A 104 ? 0.2338 0.2483 0.2862 0.0037  0.0044  -0.0022 103 ILE A CD1 
864  N N   . SER A 105 ? 0.2232 0.2523 0.3090 0.0118  0.0033  -0.0044 104 SER A N   
865  C CA  . SER A 105 ? 0.2392 0.2676 0.3295 0.0147  0.0012  -0.0042 104 SER A CA  
866  C C   . SER A 105 ? 0.2490 0.2742 0.3378 0.0168  0.0038  -0.0064 104 SER A C   
867  O O   . SER A 105 ? 0.2595 0.2831 0.3521 0.0193  0.0025  -0.0064 104 SER A O   
868  C CB  . SER A 105 ? 0.3221 0.3567 0.4233 0.0161  0.0004  -0.0038 104 SER A CB  
869  O OG  . SER A 105 ? 0.3788 0.4177 0.4846 0.0163  0.0049  -0.0060 104 SER A OG  
870  N N   . SER A 106 ? 0.2293 0.2530 0.3123 0.0157  0.0071  -0.0082 105 SER A N   
871  C CA  . SER A 106 ? 0.2406 0.2612 0.3212 0.0171  0.0095  -0.0108 105 SER A CA  
872  C C   . SER A 106 ? 0.1958 0.2112 0.2672 0.0159  0.0083  -0.0108 105 SER A C   
873  O O   . SER A 106 ? 0.2146 0.2296 0.2798 0.0141  0.0096  -0.0111 105 SER A O   
874  C CB  . SER A 106 ? 0.2638 0.2874 0.3448 0.0169  0.0144  -0.0134 105 SER A CB  
875  O OG  . SER A 106 ? 0.2278 0.2481 0.3049 0.0178  0.0168  -0.0163 105 SER A OG  
876  N N   . PRO A 107 ? 0.2143 0.2258 0.2849 0.0168  0.0059  -0.0103 106 PRO A N   
877  C CA  . PRO A 107 ? 0.1913 0.1986 0.2542 0.0156  0.0053  -0.0108 106 PRO A CA  
878  C C   . PRO A 107 ? 0.2388 0.2453 0.2976 0.0155  0.0085  -0.0139 106 PRO A C   
879  O O   . PRO A 107 ? 0.2098 0.2152 0.2619 0.0140  0.0084  -0.0142 106 PRO A O   
880  C CB  . PRO A 107 ? 0.2315 0.2351 0.2958 0.0166  0.0030  -0.0100 106 PRO A CB  
881  C CG  . PRO A 107 ? 0.3328 0.3386 0.4036 0.0177  0.0007  -0.0075 106 PRO A CG  
882  C CD  . PRO A 107 ? 0.2412 0.2519 0.3176 0.0186  0.0033  -0.0087 106 PRO A CD  
883  N N   . SER A 108 ? 0.2398 0.2470 0.3026 0.0171  0.0112  -0.0164 107 SER A N   
884  C CA  A SER A 108 ? 0.2650 0.2716 0.3233 0.0167  0.0144  -0.0197 107 SER A CA  
885  C CA  B SER A 108 ? 0.2651 0.2716 0.3233 0.0167  0.0144  -0.0197 107 SER A CA  
886  C CA  C SER A 108 ? 0.2651 0.2717 0.3235 0.0167  0.0144  -0.0197 107 SER A CA  
887  C C   . SER A 108 ? 0.2066 0.2159 0.2601 0.0149  0.0162  -0.0194 107 SER A C   
888  O O   . SER A 108 ? 0.2353 0.2433 0.2815 0.0137  0.0166  -0.0204 107 SER A O   
889  C CB  A SER A 108 ? 0.2759 0.2828 0.3399 0.0189  0.0174  -0.0228 107 SER A CB  
890  C CB  B SER A 108 ? 0.2760 0.2827 0.3398 0.0189  0.0174  -0.0228 107 SER A CB  
891  C CB  C SER A 108 ? 0.2761 0.2832 0.3403 0.0189  0.0175  -0.0227 107 SER A CB  
892  O OG  A SER A 108 ? 0.2188 0.2246 0.2777 0.0183  0.0204  -0.0264 107 SER A OG  
893  O OG  B SER A 108 ? 0.2500 0.2615 0.3206 0.0199  0.0192  -0.0225 107 SER A OG  
894  O OG  C SER A 108 ? 0.2779 0.2821 0.3476 0.0209  0.0156  -0.0224 107 SER A OG  
895  N N   . ASP A 109 ? 0.2333 0.2465 0.2910 0.0147  0.0170  -0.0178 108 ASP A N   
896  C CA  . ASP A 109 ? 0.1859 0.2011 0.2389 0.0126  0.0188  -0.0170 108 ASP A CA  
897  C C   . ASP A 109 ? 0.2166 0.2292 0.2628 0.0111  0.0158  -0.0147 108 ASP A C   
898  O O   . ASP A 109 ? 0.2178 0.2296 0.2570 0.0098  0.0167  -0.0146 108 ASP A O   
899  C CB  . ASP A 109 ? 0.2522 0.2719 0.3115 0.0122  0.0201  -0.0157 108 ASP A CB  
900  C CG  . ASP A 109 ? 0.3234 0.3469 0.3889 0.0135  0.0242  -0.0183 108 ASP A CG  
901  O OD1 . ASP A 109 ? 0.2889 0.3110 0.3531 0.0147  0.0264  -0.0215 108 ASP A OD1 
902  O OD2 . ASP A 109 ? 0.3303 0.3585 0.4026 0.0132  0.0253  -0.0175 108 ASP A OD2 
903  N N   . PHE A 110 ? 0.1922 0.2036 0.2404 0.0113  0.0123  -0.0127 109 PHE A N   
904  C CA  . PHE A 110 ? 0.1725 0.1817 0.2153 0.0101  0.0096  -0.0108 109 PHE A CA  
905  C C   . PHE A 110 ? 0.1848 0.1913 0.2217 0.0101  0.0090  -0.0123 109 PHE A C   
906  O O   . PHE A 110 ? 0.1950 0.2005 0.2262 0.0093  0.0081  -0.0115 109 PHE A O   
907  C CB  . PHE A 110 ? 0.1714 0.1803 0.2180 0.0102  0.0064  -0.0090 109 PHE A CB  
908  C CG  . PHE A 110 ? 0.1961 0.2036 0.2388 0.0089  0.0042  -0.0071 109 PHE A CG  
909  C CD1 . PHE A 110 ? 0.1794 0.1875 0.2202 0.0075  0.0049  -0.0058 109 PHE A CD1 
910  C CD2 . PHE A 110 ? 0.1811 0.1865 0.2224 0.0089  0.0016  -0.0066 109 PHE A CD2 
911  C CE1 . PHE A 110 ? 0.1802 0.1864 0.2179 0.0066  0.0028  -0.0043 109 PHE A CE1 
912  C CE2 . PHE A 110 ? 0.1791 0.1834 0.2173 0.0079  -0.0002 -0.0053 109 PHE A CE2 
913  C CZ  . PHE A 110 ? 0.1905 0.1950 0.2271 0.0069  0.0003  -0.0042 109 PHE A CZ  
914  N N   . GLN A 111 ? 0.2113 0.2166 0.2497 0.0112  0.0093  -0.0145 110 GLN A N   
915  C CA  . GLN A 111 ? 0.1847 0.1880 0.2181 0.0109  0.0088  -0.0164 110 GLN A CA  
916  C C   . GLN A 111 ? 0.1839 0.1880 0.2115 0.0103  0.0109  -0.0179 110 GLN A C   
917  O O   . GLN A 111 ? 0.2255 0.2289 0.2474 0.0096  0.0095  -0.0180 110 GLN A O   
918  C CB  . GLN A 111 ? 0.1835 0.1847 0.2202 0.0119  0.0090  -0.0186 110 GLN A CB  
919  C CG  . GLN A 111 ? 0.1868 0.1862 0.2188 0.0111  0.0084  -0.0209 110 GLN A CG  
920  C CD  . GLN A 111 ? 0.2569 0.2532 0.2919 0.0115  0.0081  -0.0226 110 GLN A CD  
921  O OE1 . GLN A 111 ? 0.2811 0.2763 0.3216 0.0126  0.0078  -0.0215 110 GLN A OE1 
922  N NE2 . GLN A 111 ? 0.2421 0.2370 0.2736 0.0106  0.0080  -0.0253 110 GLN A NE2 
923  N N   . THR A 112 ? 0.2143 0.2201 0.2432 0.0104  0.0142  -0.0189 111 THR A N   
924  C CA  . THR A 112 ? 0.2179 0.2245 0.2403 0.0095  0.0164  -0.0200 111 THR A CA  
925  C C   . THR A 112 ? 0.2703 0.2769 0.2877 0.0083  0.0152  -0.0169 111 THR A C   
926  O O   . THR A 112 ? 0.2108 0.2164 0.2209 0.0076  0.0145  -0.0169 111 THR A O   
927  C CB  . THR A 112 ? 0.2285 0.2373 0.2539 0.0098  0.0207  -0.0219 111 THR A CB  
928  O OG1 . THR A 112 ? 0.2442 0.2522 0.2735 0.0112  0.0219  -0.0253 111 THR A OG1 
929  C CG2 . THR A 112 ? 0.2551 0.2647 0.2728 0.0083  0.0234  -0.0225 111 THR A CG2 
930  N N   . PHE A 113 ? 0.2102 0.2175 0.2314 0.0080  0.0147  -0.0141 112 PHE A N   
931  C CA  . PHE A 113 ? 0.1638 0.1700 0.1809 0.0069  0.0133  -0.0111 112 PHE A CA  
932  C C   . PHE A 113 ? 0.2183 0.2224 0.2313 0.0074  0.0098  -0.0107 112 PHE A C   
933  O O   . PHE A 113 ? 0.1949 0.1979 0.2017 0.0070  0.0090  -0.0095 112 PHE A O   
934  C CB  . PHE A 113 ? 0.2046 0.2115 0.2274 0.0065  0.0126  -0.0089 112 PHE A CB  
935  C CG  . PHE A 113 ? 0.2114 0.2163 0.2308 0.0056  0.0109  -0.0060 112 PHE A CG  
936  C CD1 . PHE A 113 ? 0.2209 0.2253 0.2369 0.0041  0.0128  -0.0043 112 PHE A CD1 
937  C CD2 . PHE A 113 ? 0.1868 0.1900 0.2067 0.0061  0.0076  -0.0052 112 PHE A CD2 
938  C CE1 . PHE A 113 ? 0.2194 0.2209 0.2324 0.0033  0.0111  -0.0016 112 PHE A CE1 
939  C CE2 . PHE A 113 ? 0.2076 0.2084 0.2247 0.0055  0.0060  -0.0030 112 PHE A CE2 
940  C CZ  . PHE A 113 ? 0.2036 0.2032 0.2174 0.0042  0.0076  -0.0012 112 PHE A CZ  
941  N N   . TRP A 114 ? 0.1908 0.1945 0.2073 0.0082  0.0078  -0.0116 113 TRP A N   
942  C CA  . TRP A 114 ? 0.1727 0.1752 0.1866 0.0084  0.0047  -0.0112 113 TRP A CA  
943  C C   . TRP A 114 ? 0.1891 0.1917 0.1980 0.0085  0.0044  -0.0134 113 TRP A C   
944  O O   . TRP A 114 ? 0.1921 0.1945 0.1974 0.0086  0.0021  -0.0127 113 TRP A O   
945  C CB  . TRP A 114 ? 0.1904 0.1926 0.2092 0.0088  0.0030  -0.0113 113 TRP A CB  
946  C CG  . TRP A 114 ? 0.1636 0.1653 0.1838 0.0085  0.0016  -0.0088 113 TRP A CG  
947  C CD1 . TRP A 114 ? 0.1820 0.1839 0.2067 0.0083  0.0016  -0.0076 113 TRP A CD1 
948  C CD2 . TRP A 114 ? 0.1699 0.1705 0.1868 0.0086  -0.0001 -0.0074 113 TRP A CD2 
949  N NE1 . TRP A 114 ? 0.1914 0.1924 0.2154 0.0078  0.0002  -0.0059 113 TRP A NE1 
950  C CE2 . TRP A 114 ? 0.2037 0.2036 0.2231 0.0081  -0.0007 -0.0057 113 TRP A CE2 
951  C CE3 . TRP A 114 ? 0.2402 0.2404 0.2524 0.0090  -0.0013 -0.0075 113 TRP A CE3 
952  C CZ2 . TRP A 114 ? 0.1788 0.1771 0.1962 0.0082  -0.0021 -0.0044 113 TRP A CZ2 
953  C CZ3 . TRP A 114 ? 0.2262 0.2251 0.2370 0.0095  -0.0029 -0.0058 113 TRP A CZ3 
954  C CH2 . TRP A 114 ? 0.1838 0.1815 0.1972 0.0090  -0.0032 -0.0044 113 TRP A CH2 
955  N N   . LYS A 115 ? 0.2091 0.2122 0.2181 0.0084  0.0064  -0.0161 114 LYS A N   
956  C CA  . LYS A 115 ? 0.2088 0.2121 0.2121 0.0080  0.0061  -0.0184 114 LYS A CA  
957  C C   . LYS A 115 ? 0.1952 0.1987 0.1915 0.0076  0.0064  -0.0167 114 LYS A C   
958  O O   . LYS A 115 ? 0.2153 0.2190 0.2063 0.0075  0.0041  -0.0166 114 LYS A O   
959  C CB  . LYS A 115 ? 0.1933 0.1966 0.1976 0.0079  0.0087  -0.0221 114 LYS A CB  
960  C CG  . LYS A 115 ? 0.2115 0.2150 0.2100 0.0072  0.0078  -0.0251 114 LYS A CG  
961  C CD  . LYS A 115 ? 0.2186 0.2217 0.2166 0.0069  0.0110  -0.0291 114 LYS A CD  
962  C CE  . LYS A 115 ? 0.3295 0.3328 0.3215 0.0058  0.0096  -0.0324 114 LYS A CE  
963  N NZ  . LYS A 115 ? 0.3813 0.3844 0.3705 0.0052  0.0132  -0.0364 114 LYS A NZ  
964  N N   . THR A 116 ? 0.2162 0.2197 0.2125 0.0071  0.0091  -0.0152 115 THR A N   
965  C CA  . THR A 116 ? 0.2067 0.2098 0.1960 0.0063  0.0097  -0.0130 115 THR A CA  
966  C C   . THR A 116 ? 0.2144 0.2158 0.2014 0.0069  0.0062  -0.0097 115 THR A C   
967  O O   . THR A 116 ? 0.2266 0.2274 0.2068 0.0069  0.0045  -0.0087 115 THR A O   
968  C CB  . THR A 116 ? 0.2219 0.2254 0.2131 0.0054  0.0134  -0.0117 115 THR A CB  
969  O OG1 . THR A 116 ? 0.2519 0.2572 0.2447 0.0052  0.0170  -0.0151 115 THR A OG1 
970  C CG2 . THR A 116 ? 0.2571 0.2592 0.2411 0.0042  0.0141  -0.0087 115 THR A CG2 
971  N N   . VAL A 117 ? 0.2156 0.2164 0.2083 0.0074  0.0049  -0.0082 116 VAL A N   
972  C CA  . VAL A 117 ? 0.2210 0.2200 0.2124 0.0081  0.0019  -0.0055 116 VAL A CA  
973  C C   . VAL A 117 ? 0.2345 0.2344 0.2249 0.0093  -0.0014 -0.0068 116 VAL A C   
974  O O   . VAL A 117 ? 0.2055 0.2047 0.1916 0.0101  -0.0038 -0.0052 116 VAL A O   
975  C CB  . VAL A 117 ? 0.1849 0.1830 0.1824 0.0081  0.0017  -0.0042 116 VAL A CB  
976  C CG1 . VAL A 117 ? 0.2132 0.2093 0.2099 0.0091  -0.0012 -0.0022 116 VAL A CG1 
977  C CG2 . VAL A 117 ? 0.2307 0.2283 0.2292 0.0067  0.0047  -0.0027 116 VAL A CG2 
978  N N   . ALA A 118 ? 0.1982 0.1999 0.1930 0.0094  -0.0017 -0.0096 117 ALA A N   
979  C CA  . ALA A 118 ? 0.1852 0.1884 0.1800 0.0100  -0.0046 -0.0110 117 ALA A CA  
980  C C   . ALA A 118 ? 0.2113 0.2157 0.1998 0.0099  -0.0058 -0.0120 117 ALA A C   
981  O O   . ALA A 118 ? 0.2305 0.2363 0.2178 0.0108  -0.0090 -0.0119 117 ALA A O   
982  C CB  . ALA A 118 ? 0.2236 0.2278 0.2236 0.0095  -0.0043 -0.0138 117 ALA A CB  
983  N N   . SER A 119 ? 0.2165 0.2207 0.2010 0.0089  -0.0033 -0.0132 118 SER A N   
984  C CA  . SER A 119 ? 0.2074 0.2127 0.1847 0.0085  -0.0043 -0.0143 118 SER A CA  
985  C C   . SER A 119 ? 0.2475 0.2520 0.2191 0.0094  -0.0069 -0.0108 118 SER A C   
986  O O   . SER A 119 ? 0.2513 0.2574 0.2182 0.0096  -0.0098 -0.0113 118 SER A O   
987  C CB  . SER A 119 ? 0.2614 0.2663 0.2350 0.0071  -0.0005 -0.0161 118 SER A CB  
988  O OG  . SER A 119 ? 0.2740 0.2795 0.2524 0.0066  0.0014  -0.0199 118 SER A OG  
989  N N   . GLN A 120 ? 0.2248 0.2266 0.1969 0.0098  -0.0062 -0.0072 119 GLN A N   
990  C CA  . GLN A 120 ? 0.2125 0.2123 0.1793 0.0108  -0.0087 -0.0034 119 GLN A CA  
991  C C   . GLN A 120 ? 0.2763 0.2773 0.2464 0.0130  -0.0129 -0.0028 119 GLN A C   
992  O O   . GLN A 120 ? 0.3141 0.3140 0.2799 0.0143  -0.0158 -0.0001 119 GLN A O   
993  C CB  . GLN A 120 ? 0.2444 0.2405 0.2113 0.0104  -0.0064 0.0001  119 GLN A CB  
994  C CG  . GLN A 120 ? 0.2500 0.2455 0.2138 0.0083  -0.0019 -0.0001 119 GLN A CG  
995  C CD  . GLN A 120 ? 0.2927 0.2872 0.2464 0.0075  -0.0019 0.0017  119 GLN A CD  
996  O OE1 . GLN A 120 ? 0.2493 0.2419 0.1982 0.0086  -0.0052 0.0046  119 GLN A OE1 
997  N NE2 . GLN A 120 ? 0.2611 0.2566 0.2111 0.0056  0.0019  -0.0002 119 GLN A NE2 
998  N N   . PHE A 121 ? 0.2295 0.2324 0.2070 0.0133  -0.0133 -0.0051 120 PHE A N   
999  C CA  . PHE A 121 ? 0.1933 0.1977 0.1751 0.0152  -0.0165 -0.0048 120 PHE A CA  
1000 C C   . PHE A 121 ? 0.2127 0.2215 0.1987 0.0149  -0.0179 -0.0085 120 PHE A C   
1001 O O   . PHE A 121 ? 0.2197 0.2304 0.2107 0.0161  -0.0198 -0.0089 120 PHE A O   
1002 C CB  . PHE A 121 ? 0.2242 0.2259 0.2112 0.0157  -0.0153 -0.0034 120 PHE A CB  
1003 C CG  . PHE A 121 ? 0.2157 0.2128 0.1993 0.0157  -0.0140 0.0002  120 PHE A CG  
1004 C CD1 . PHE A 121 ? 0.2972 0.2919 0.2769 0.0174  -0.0165 0.0033  120 PHE A CD1 
1005 C CD2 . PHE A 121 ? 0.2178 0.2130 0.2023 0.0139  -0.0105 0.0006  120 PHE A CD2 
1006 C CE1 . PHE A 121 ? 0.2577 0.2473 0.2340 0.0170  -0.0152 0.0069  120 PHE A CE1 
1007 C CE2 . PHE A 121 ? 0.2194 0.2104 0.2009 0.0133  -0.0092 0.0038  120 PHE A CE2 
1008 C CZ  . PHE A 121 ? 0.2064 0.1943 0.1836 0.0147  -0.0114 0.0070  120 PHE A CZ  
1009 N N   . ALA A 122 ? 0.2265 0.2369 0.2105 0.0132  -0.0168 -0.0114 121 ALA A N   
1010 C CA  . ALA A 122 ? 0.2180 0.2317 0.2067 0.0122  -0.0172 -0.0151 121 ALA A CA  
1011 C C   . ALA A 122 ? 0.2465 0.2644 0.2370 0.0132  -0.0212 -0.0160 121 ALA A C   
1012 O O   . ALA A 122 ? 0.2358 0.2564 0.2322 0.0126  -0.0215 -0.0183 121 ALA A O   
1013 C CB  . ALA A 122 ? 0.2059 0.2197 0.1917 0.0102  -0.0152 -0.0182 121 ALA A CB  
1014 N N   . SER A 123 ? 0.2331 0.2520 0.2189 0.0146  -0.0243 -0.0142 122 SER A N   
1015 C CA  . SER A 123 ? 0.2392 0.2630 0.2274 0.0159  -0.0285 -0.0149 122 SER A CA  
1016 C C   . SER A 123 ? 0.2491 0.2732 0.2425 0.0186  -0.0301 -0.0127 122 SER A C   
1017 O O   . SER A 123 ? 0.3046 0.3333 0.3014 0.0201  -0.0335 -0.0133 122 SER A O   
1018 C CB  . SER A 123 ? 0.3268 0.3518 0.3072 0.0164  -0.0317 -0.0140 122 SER A CB  
1019 O OG  . SER A 123 ? 0.4757 0.4976 0.4526 0.0188  -0.0331 -0.0094 122 SER A OG  
1020 N N   . ASN A 124 ? 0.2131 0.2326 0.2075 0.0193  -0.0277 -0.0104 123 ASN A N   
1021 C CA  . ASN A 124 ? 0.2133 0.2320 0.2117 0.0220  -0.0290 -0.0083 123 ASN A CA  
1022 C C   . ASN A 124 ? 0.2289 0.2491 0.2349 0.0214  -0.0271 -0.0104 123 ASN A C   
1023 O O   . ASN A 124 ? 0.2020 0.2187 0.2086 0.0201  -0.0239 -0.0102 123 ASN A O   
1024 C CB  . ASN A 124 ? 0.2397 0.2520 0.2339 0.0229  -0.0278 -0.0044 123 ASN A CB  
1025 C CG  . ASN A 124 ? 0.2693 0.2800 0.2665 0.0260  -0.0297 -0.0022 123 ASN A CG  
1026 O OD1 . ASN A 124 ? 0.2339 0.2481 0.2377 0.0274  -0.0307 -0.0039 123 ASN A OD1 
1027 N ND2 . ASN A 124 ? 0.2455 0.2507 0.2379 0.0271  -0.0299 0.0016  123 ASN A ND2 
1028 N N   . PRO A 125 ? 0.2084 0.2340 0.2203 0.0222  -0.0289 -0.0125 124 PRO A N   
1029 C CA  . PRO A 125 ? 0.2112 0.2383 0.2295 0.0212  -0.0268 -0.0146 124 PRO A CA  
1030 C C   . PRO A 125 ? 0.2214 0.2453 0.2422 0.0228  -0.0255 -0.0130 124 PRO A C   
1031 O O   . PRO A 125 ? 0.2198 0.2442 0.2446 0.0217  -0.0233 -0.0145 124 PRO A O   
1032 C CB  . PRO A 125 ? 0.2444 0.2788 0.2680 0.0215  -0.0291 -0.0173 124 PRO A CB  
1033 C CG  . PRO A 125 ? 0.2764 0.3125 0.2979 0.0244  -0.0332 -0.0155 124 PRO A CG  
1034 C CD  . PRO A 125 ? 0.2521 0.2830 0.2649 0.0240  -0.0331 -0.0130 124 PRO A CD  
1035 N N   . LEU A 126 ? 0.1901 0.2103 0.2082 0.0253  -0.0268 -0.0101 125 LEU A N   
1036 C CA  . LEU A 126 ? 0.2059 0.2222 0.2260 0.0268  -0.0255 -0.0089 125 LEU A CA  
1037 C C   . LEU A 126 ? 0.2069 0.2168 0.2227 0.0251  -0.0229 -0.0070 125 LEU A C   
1038 O O   . LEU A 126 ? 0.2183 0.2244 0.2352 0.0258  -0.0218 -0.0061 125 LEU A O   
1039 C CB  . LEU A 126 ? 0.2100 0.2255 0.2306 0.0306  -0.0285 -0.0070 125 LEU A CB  
1040 C CG  . LEU A 126 ? 0.2164 0.2390 0.2429 0.0328  -0.0313 -0.0090 125 LEU A CG  
1041 C CD1 . LEU A 126 ? 0.2212 0.2423 0.2478 0.0371  -0.0346 -0.0065 125 LEU A CD1 
1042 C CD2 . LEU A 126 ? 0.2587 0.2845 0.2923 0.0324  -0.0290 -0.0121 125 LEU A CD2 
1043 N N   . VAL A 127 ? 0.1568 0.1658 0.1683 0.0229  -0.0219 -0.0066 126 VAL A N   
1044 C CA  . VAL A 127 ? 0.1539 0.1585 0.1633 0.0210  -0.0191 -0.0054 126 VAL A CA  
1045 C C   . VAL A 127 ? 0.1716 0.1775 0.1848 0.0190  -0.0169 -0.0076 126 VAL A C   
1046 O O   . VAL A 127 ? 0.1842 0.1939 0.1996 0.0180  -0.0169 -0.0099 126 VAL A O   
1047 C CB  . VAL A 127 ? 0.1751 0.1787 0.1789 0.0197  -0.0185 -0.0045 126 VAL A CB  
1048 C CG1 . VAL A 127 ? 0.2149 0.2156 0.2181 0.0175  -0.0153 -0.0040 126 VAL A CG1 
1049 C CG2 . VAL A 127 ? 0.2144 0.2153 0.2131 0.0214  -0.0203 -0.0015 126 VAL A CG2 
1050 N N   . ILE A 128 ? 0.1745 0.1769 0.1883 0.0183  -0.0151 -0.0068 127 ILE A N   
1051 C CA  . ILE A 128 ? 0.1554 0.1583 0.1718 0.0163  -0.0133 -0.0081 127 ILE A CA  
1052 C C   . ILE A 128 ? 0.1622 0.1622 0.1765 0.0147  -0.0116 -0.0067 127 ILE A C   
1053 O O   . ILE A 128 ? 0.2151 0.2118 0.2274 0.0150  -0.0113 -0.0047 127 ILE A O   
1054 C CB  . ILE A 128 ? 0.1808 0.1829 0.2000 0.0167  -0.0129 -0.0087 127 ILE A CB  
1055 C CG1 . ILE A 128 ? 0.1808 0.1867 0.2031 0.0182  -0.0141 -0.0105 127 ILE A CG1 
1056 C CG2 . ILE A 128 ? 0.1590 0.1611 0.1796 0.0144  -0.0112 -0.0095 127 ILE A CG2 
1057 C CD1 . ILE A 128 ? 0.1676 0.1727 0.1925 0.0191  -0.0136 -0.0114 127 ILE A CD1 
1058 N N   . PHE A 129 ? 0.1433 0.1445 0.1584 0.0131  -0.0104 -0.0077 128 PHE A N   
1059 C CA  . PHE A 129 ? 0.1560 0.1555 0.1704 0.0119  -0.0088 -0.0067 128 PHE A CA  
1060 C C   . PHE A 129 ? 0.1849 0.1836 0.2020 0.0107  -0.0081 -0.0066 128 PHE A C   
1061 O O   . PHE A 129 ? 0.2083 0.2083 0.2275 0.0102  -0.0082 -0.0078 128 PHE A O   
1062 C CB  . PHE A 129 ? 0.1596 0.1607 0.1736 0.0111  -0.0079 -0.0080 128 PHE A CB  
1063 C CG  . PHE A 129 ? 0.1800 0.1824 0.1906 0.0118  -0.0088 -0.0086 128 PHE A CG  
1064 C CD1 . PHE A 129 ? 0.2075 0.2083 0.2140 0.0122  -0.0086 -0.0069 128 PHE A CD1 
1065 C CD2 . PHE A 129 ? 0.2023 0.2074 0.2136 0.0118  -0.0099 -0.0107 128 PHE A CD2 
1066 C CE1 . PHE A 129 ? 0.2024 0.2044 0.2048 0.0128  -0.0097 -0.0073 128 PHE A CE1 
1067 C CE2 . PHE A 129 ? 0.2091 0.2158 0.2171 0.0123  -0.0111 -0.0114 128 PHE A CE2 
1068 C CZ  . PHE A 129 ? 0.2079 0.2130 0.2111 0.0128  -0.0111 -0.0096 128 PHE A CZ  
1069 N N   . ASP A 130 ? 0.1526 0.1490 0.1694 0.0102  -0.0074 -0.0050 129 ASP A N   
1070 C CA  . ASP A 130 ? 0.1386 0.1344 0.1577 0.0089  -0.0071 -0.0048 129 ASP A CA  
1071 C C   . ASP A 130 ? 0.1584 0.1547 0.1789 0.0079  -0.0060 -0.0042 129 ASP A C   
1072 O O   . ASP A 130 ? 0.1717 0.1673 0.1913 0.0077  -0.0050 -0.0031 129 ASP A O   
1073 C CB  . ASP A 130 ? 0.1662 0.1591 0.1843 0.0090  -0.0075 -0.0039 129 ASP A CB  
1074 C CG  . ASP A 130 ? 0.1751 0.1673 0.1948 0.0076  -0.0076 -0.0041 129 ASP A CG  
1075 O OD1 . ASP A 130 ? 0.1808 0.1745 0.2023 0.0064  -0.0075 -0.0041 129 ASP A OD1 
1076 O OD2 . ASP A 130 ? 0.1817 0.1716 0.2007 0.0078  -0.0080 -0.0044 129 ASP A OD2 
1077 N N   . THR A 131 ? 0.1779 0.1756 0.2010 0.0073  -0.0060 -0.0047 130 THR A N   
1078 C CA  . THR A 131 ? 0.1366 0.1354 0.1618 0.0070  -0.0048 -0.0045 130 THR A CA  
1079 C C   . THR A 131 ? 0.1806 0.1793 0.2073 0.0061  -0.0042 -0.0032 130 THR A C   
1080 O O   . THR A 131 ? 0.1733 0.1730 0.2009 0.0061  -0.0026 -0.0030 130 THR A O   
1081 C CB  . THR A 131 ? 0.1469 0.1464 0.1749 0.0068  -0.0053 -0.0049 130 THR A CB  
1082 O OG1 . THR A 131 ? 0.1666 0.1659 0.1957 0.0059  -0.0065 -0.0040 130 THR A OG1 
1083 C CG2 . THR A 131 ? 0.1628 0.1623 0.1896 0.0071  -0.0057 -0.0063 130 THR A CG2 
1084 N N   . ASN A 132 ? 0.1719 0.1697 0.1991 0.0052  -0.0052 -0.0026 131 ASN A N   
1085 C CA  . ASN A 132 ? 0.1443 0.1420 0.1731 0.0039  -0.0048 -0.0015 131 ASN A CA  
1086 C C   . ASN A 132 ? 0.1705 0.1667 0.1988 0.0028  -0.0063 -0.0015 131 ASN A C   
1087 O O   . ASN A 132 ? 0.1874 0.1838 0.2154 0.0028  -0.0076 -0.0021 131 ASN A O   
1088 C CB  . ASN A 132 ? 0.1702 0.1710 0.2037 0.0034  -0.0043 -0.0012 131 ASN A CB  
1089 C CG  . ASN A 132 ? 0.1994 0.2013 0.2343 0.0027  -0.0022 -0.0006 131 ASN A CG  
1090 O OD1 . ASN A 132 ? 0.1756 0.1787 0.2135 0.0011  -0.0021 0.0000  131 ASN A OD1 
1091 N ND2 . ASN A 132 ? 0.1632 0.1648 0.1958 0.0035  -0.0003 -0.0010 131 ASN A ND2 
1092 N N   . ASN A 133 ? 0.1641 0.1584 0.1918 0.0016  -0.0059 -0.0009 132 ASN A N   
1093 C CA  . ASN A 133 ? 0.1688 0.1611 0.1958 0.0004  -0.0072 -0.0013 132 ASN A CA  
1094 C C   . ASN A 133 ? 0.1714 0.1661 0.2017 -0.0014 -0.0084 -0.0013 132 ASN A C   
1095 O O   . ASN A 133 ? 0.1847 0.1815 0.2183 -0.0025 -0.0078 -0.0005 132 ASN A O   
1096 C CB  . ASN A 133 ? 0.1785 0.1671 0.2039 -0.0004 -0.0064 -0.0007 132 ASN A CB  
1097 C CG  . ASN A 133 ? 0.1999 0.1860 0.2248 -0.0019 -0.0074 -0.0016 132 ASN A CG  
1098 O OD1 . ASN A 133 ? 0.1861 0.1703 0.2089 -0.0009 -0.0081 -0.0028 132 ASN A OD1 
1099 N ND2 . ASN A 133 ? 0.2201 0.2061 0.2471 -0.0044 -0.0075 -0.0013 132 ASN A ND2 
1100 N N   . GLN A 134 ? 0.1540 0.1488 0.1833 -0.0017 -0.0100 -0.0021 133 GLN A N   
1101 C CA  . GLN A 134 ? 0.1718 0.1682 0.2027 -0.0037 -0.0118 -0.0022 133 GLN A CA  
1102 C C   . GLN A 134 ? 0.2003 0.2009 0.2362 -0.0039 -0.0124 -0.0010 133 GLN A C   
1103 O O   . GLN A 134 ? 0.1796 0.1819 0.2187 -0.0056 -0.0127 -0.0007 133 GLN A O   
1104 C CB  . GLN A 134 ? 0.1785 0.1724 0.2086 -0.0058 -0.0120 -0.0029 133 GLN A CB  
1105 C CG  . GLN A 134 ? 0.1877 0.1774 0.2135 -0.0055 -0.0117 -0.0044 133 GLN A CG  
1106 C CD  . GLN A 134 ? 0.2766 0.2631 0.3017 -0.0078 -0.0120 -0.0055 133 GLN A CD  
1107 O OE1 . GLN A 134 ? 0.3170 0.3042 0.3448 -0.0097 -0.0121 -0.0048 133 GLN A OE1 
1108 N NE2 . GLN A 134 ? 0.2964 0.2795 0.3181 -0.0077 -0.0120 -0.0074 133 GLN A NE2 
1109 N N   . TYR A 135 ? 0.1697 0.1719 0.2066 -0.0023 -0.0125 -0.0005 134 TYR A N   
1110 C CA  . TYR A 135 ? 0.1482 0.1542 0.1901 -0.0021 -0.0137 0.0005  134 TYR A CA  
1111 C C   . TYR A 135 ? 0.1740 0.1813 0.2164 -0.0040 -0.0166 0.0008  134 TYR A C   
1112 O O   . TYR A 135 ? 0.1841 0.1893 0.2220 -0.0050 -0.0178 0.0002  134 TYR A O   
1113 C CB  . TYR A 135 ? 0.1377 0.1437 0.1795 -0.0001 -0.0140 0.0010  134 TYR A CB  
1114 C CG  . TYR A 135 ? 0.1632 0.1679 0.2040 0.0016  -0.0115 0.0004  134 TYR A CG  
1115 C CD1 . TYR A 135 ? 0.1660 0.1680 0.2022 0.0020  -0.0109 -0.0005 134 TYR A CD1 
1116 C CD2 . TYR A 135 ? 0.1494 0.1561 0.1942 0.0028  -0.0099 0.0004  134 TYR A CD2 
1117 C CE1 . TYR A 135 ? 0.1857 0.1871 0.2210 0.0034  -0.0092 -0.0012 134 TYR A CE1 
1118 C CE2 . TYR A 135 ? 0.1762 0.1816 0.2193 0.0041  -0.0078 -0.0006 134 TYR A CE2 
1119 C CZ  . TYR A 135 ? 0.1821 0.1851 0.2205 0.0043  -0.0077 -0.0013 134 TYR A CZ  
1120 O OH  . TYR A 135 ? 0.1732 0.1754 0.2099 0.0055  -0.0061 -0.0023 134 TYR A OH  
1121 N N   . HIS A 136 ? 0.1629 0.1742 0.2110 -0.0046 -0.0176 0.0016  135 HIS A N   
1122 C CA  . HIS A 136 ? 0.1608 0.1742 0.2097 -0.0067 -0.0209 0.0018  135 HIS A CA  
1123 C C   . HIS A 136 ? 0.1956 0.2146 0.2524 -0.0063 -0.0223 0.0029  135 HIS A C   
1124 O O   . HIS A 136 ? 0.1931 0.2144 0.2549 -0.0053 -0.0200 0.0029  135 HIS A O   
1125 C CB  . HIS A 136 ? 0.1917 0.2034 0.2385 -0.0095 -0.0207 0.0004  135 HIS A CB  
1126 C CG  . HIS A 136 ? 0.1693 0.1826 0.2207 -0.0106 -0.0187 0.0002  135 HIS A CG  
1127 N ND1 . HIS A 136 ? 0.1883 0.2065 0.2459 -0.0124 -0.0201 0.0004  135 HIS A ND1 
1128 C CD2 . HIS A 136 ? 0.1554 0.1665 0.2063 -0.0102 -0.0154 0.0001  135 HIS A CD2 
1129 C CE1 . HIS A 136 ? 0.1980 0.2168 0.2587 -0.0133 -0.0173 0.0003  135 HIS A CE1 
1130 N NE2 . HIS A 136 ? 0.1784 0.1926 0.2346 -0.0120 -0.0144 0.0002  135 HIS A NE2 
1131 N N   . ASP A 137 ? 0.1624 0.1840 0.2202 -0.0072 -0.0261 0.0038  136 ASP A N   
1132 C CA  . ASP A 137 ? 0.1416 0.1692 0.2075 -0.0069 -0.0284 0.0048  136 ASP A CA  
1133 C C   . ASP A 137 ? 0.1680 0.1977 0.2400 -0.0036 -0.0264 0.0055  136 ASP A C   
1134 O O   . ASP A 137 ? 0.1693 0.2033 0.2485 -0.0035 -0.0248 0.0051  136 ASP A O   
1135 C CB  . ASP A 137 ? 0.1710 0.2020 0.2410 -0.0099 -0.0283 0.0037  136 ASP A CB  
1136 C CG  . ASP A 137 ? 0.2322 0.2606 0.2962 -0.0132 -0.0302 0.0025  136 ASP A CG  
1137 O OD1 . ASP A 137 ? 0.2049 0.2342 0.2664 -0.0138 -0.0342 0.0031  136 ASP A OD1 
1138 O OD2 . ASP A 137 ? 0.2055 0.2307 0.2668 -0.0150 -0.0278 0.0009  136 ASP A OD2 
1139 N N   . MET A 138 ? 0.1673 0.1936 0.2362 -0.0013 -0.0261 0.0064  137 MET A N   
1140 C CA  . MET A 138 ? 0.1853 0.2126 0.2592 0.0019  -0.0243 0.0067  137 MET A CA  
1141 C C   . MET A 138 ? 0.1813 0.2055 0.2525 0.0038  -0.0263 0.0084  137 MET A C   
1142 O O   . MET A 138 ? 0.1892 0.2105 0.2539 0.0025  -0.0285 0.0092  137 MET A O   
1143 C CB  . MET A 138 ? 0.1634 0.1884 0.2355 0.0023  -0.0196 0.0050  137 MET A CB  
1144 C CG  . MET A 138 ? 0.1982 0.2175 0.2614 0.0016  -0.0186 0.0044  137 MET A CG  
1145 S SD  . MET A 138 ? 0.1905 0.2078 0.2512 0.0014  -0.0140 0.0026  137 MET A SD  
1146 C CE  . MET A 138 ? 0.1823 0.2003 0.2468 0.0045  -0.0115 0.0022  137 MET A CE  
1147 N N   . ASP A 139 ? 0.2086 0.2331 0.2848 0.0068  -0.0254 0.0088  138 ASP A N   
1148 C CA  . ASP A 139 ? 0.2002 0.2215 0.2751 0.0088  -0.0274 0.0107  138 ASP A CA  
1149 C C   . ASP A 139 ? 0.1897 0.2049 0.2557 0.0079  -0.0260 0.0104  138 ASP A C   
1150 O O   . ASP A 139 ? 0.1956 0.2089 0.2592 0.0078  -0.0225 0.0084  138 ASP A O   
1151 C CB  . ASP A 139 ? 0.1852 0.2076 0.2677 0.0123  -0.0260 0.0106  138 ASP A CB  
1152 C CG  . ASP A 139 ? 0.2698 0.2881 0.3517 0.0144  -0.0280 0.0128  138 ASP A CG  
1153 O OD1 . ASP A 139 ? 0.2702 0.2905 0.3559 0.0155  -0.0321 0.0153  138 ASP A OD1 
1154 O OD2 . ASP A 139 ? 0.2353 0.2485 0.3132 0.0149  -0.0258 0.0121  138 ASP A OD2 
1155 N N   . GLN A 140 ? 0.1937 0.2060 0.2548 0.0073  -0.0288 0.0125  139 GLN A N   
1156 C CA  . GLN A 140 ? 0.1901 0.1975 0.2430 0.0059  -0.0274 0.0120  139 GLN A CA  
1157 C C   . GLN A 140 ? 0.1869 0.1907 0.2402 0.0077  -0.0247 0.0114  139 GLN A C   
1158 O O   . GLN A 140 ? 0.1987 0.2002 0.2476 0.0068  -0.0222 0.0096  139 GLN A O   
1159 C CB  . GLN A 140 ? 0.1858 0.1912 0.2331 0.0044  -0.0308 0.0145  139 GLN A CB  
1160 C CG  . GLN A 140 ? 0.1788 0.1801 0.2177 0.0024  -0.0292 0.0138  139 GLN A CG  
1161 C CD  . GLN A 140 ? 0.1885 0.1908 0.2245 0.0007  -0.0269 0.0109  139 GLN A CD  
1162 O OE1 . GLN A 140 ? 0.2143 0.2195 0.2514 -0.0004 -0.0280 0.0101  139 GLN A OE1 
1163 N NE2 . GLN A 140 ? 0.1739 0.1737 0.2065 0.0004  -0.0240 0.0092  139 GLN A NE2 
1164 N N   . THR A 141 ? 0.1934 0.1969 0.2523 0.0103  -0.0254 0.0125  140 THR A N   
1165 C CA  . THR A 141 ? 0.2012 0.2012 0.2610 0.0119  -0.0227 0.0114  140 THR A CA  
1166 C C   . THR A 141 ? 0.2118 0.2137 0.2736 0.0123  -0.0189 0.0081  140 THR A C   
1167 O O   . THR A 141 ? 0.1802 0.1794 0.2390 0.0121  -0.0163 0.0063  140 THR A O   
1168 C CB  . THR A 141 ? 0.2014 0.2000 0.2671 0.0148  -0.0243 0.0132  140 THR A CB  
1169 O OG1 . THR A 141 ? 0.2298 0.2254 0.2918 0.0142  -0.0278 0.0167  140 THR A OG1 
1170 C CG2 . THR A 141 ? 0.2384 0.2330 0.3055 0.0165  -0.0212 0.0114  140 THR A CG2 
1171 N N   . LEU A 142 ? 0.1910 0.1979 0.2577 0.0127  -0.0186 0.0074  141 LEU A N   
1172 C CA  . LEU A 142 ? 0.1868 0.1954 0.2545 0.0127  -0.0150 0.0047  141 LEU A CA  
1173 C C   . LEU A 142 ? 0.1876 0.1945 0.2480 0.0105  -0.0136 0.0035  141 LEU A C   
1174 O O   . LEU A 142 ? 0.2122 0.2178 0.2705 0.0106  -0.0109 0.0016  141 LEU A O   
1175 C CB  . LEU A 142 ? 0.1804 0.1949 0.2544 0.0128  -0.0149 0.0045  141 LEU A CB  
1176 C CG  . LEU A 142 ? 0.2005 0.2170 0.2748 0.0122  -0.0110 0.0022  141 LEU A CG  
1177 C CD1 . LEU A 142 ? 0.2088 0.2240 0.2847 0.0142  -0.0078 0.0001  141 LEU A CD1 
1178 C CD2 . LEU A 142 ? 0.1975 0.2199 0.2783 0.0116  -0.0110 0.0022  141 LEU A CD2 
1179 N N   . VAL A 143 ? 0.1736 0.1804 0.2299 0.0084  -0.0157 0.0046  142 VAL A N   
1180 C CA  . VAL A 143 ? 0.1780 0.1831 0.2281 0.0067  -0.0145 0.0033  142 VAL A CA  
1181 C C   . VAL A 143 ? 0.1737 0.1752 0.2200 0.0070  -0.0133 0.0025  142 VAL A C   
1182 O O   . VAL A 143 ? 0.1810 0.1819 0.2249 0.0068  -0.0112 0.0008  142 VAL A O   
1183 C CB  . VAL A 143 ? 0.1776 0.1829 0.2242 0.0046  -0.0167 0.0042  142 VAL A CB  
1184 C CG1 . VAL A 143 ? 0.1658 0.1688 0.2064 0.0033  -0.0154 0.0028  142 VAL A CG1 
1185 C CG2 . VAL A 143 ? 0.1810 0.1898 0.2312 0.0038  -0.0175 0.0043  142 VAL A CG2 
1186 N N   . LEU A 144 ? 0.1796 0.1788 0.2255 0.0072  -0.0147 0.0040  143 LEU A N   
1187 C CA  . LEU A 144 ? 0.1935 0.1894 0.2367 0.0071  -0.0135 0.0032  143 LEU A CA  
1188 C C   . LEU A 144 ? 0.1795 0.1752 0.2252 0.0087  -0.0110 0.0011  143 LEU A C   
1189 O O   . LEU A 144 ? 0.1754 0.1703 0.2183 0.0081  -0.0094 -0.0009 143 LEU A O   
1190 C CB  . LEU A 144 ? 0.1907 0.1836 0.2337 0.0072  -0.0154 0.0055  143 LEU A CB  
1191 C CG  . LEU A 144 ? 0.1791 0.1681 0.2203 0.0069  -0.0141 0.0049  143 LEU A CG  
1192 C CD1 . LEU A 144 ? 0.1823 0.1711 0.2181 0.0046  -0.0130 0.0036  143 LEU A CD1 
1193 C CD2 . LEU A 144 ? 0.2190 0.2043 0.2605 0.0071  -0.0160 0.0078  143 LEU A CD2 
1194 N N   . ASN A 145 ? 0.1733 0.1701 0.2246 0.0105  -0.0108 0.0012  144 ASN A N   
1195 C CA  . ASN A 145 ? 0.1515 0.1477 0.2049 0.0120  -0.0082 -0.0012 144 ASN A CA  
1196 C C   . ASN A 145 ? 0.1998 0.1985 0.2514 0.0115  -0.0060 -0.0032 144 ASN A C   
1197 O O   . ASN A 145 ? 0.1906 0.1883 0.2407 0.0117  -0.0039 -0.0055 144 ASN A O   
1198 C CB  . ASN A 145 ? 0.1975 0.1947 0.2580 0.0144  -0.0082 -0.0008 144 ASN A CB  
1199 C CG  . ASN A 145 ? 0.2253 0.2189 0.2875 0.0153  -0.0103 0.0013  144 ASN A CG  
1200 O OD1 . ASN A 145 ? 0.2553 0.2450 0.3133 0.0141  -0.0109 0.0019  144 ASN A OD1 
1201 N ND2 . ASN A 145 ? 0.2215 0.2165 0.2902 0.0175  -0.0115 0.0026  144 ASN A ND2 
1202 N N   . LEU A 146 ? 0.1604 0.1620 0.2119 0.0107  -0.0064 -0.0024 145 LEU A N   
1203 C CA  . LEU A 146 ? 0.1552 0.1581 0.2041 0.0100  -0.0045 -0.0038 145 LEU A CA  
1204 C C   . LEU A 146 ? 0.1916 0.1926 0.2346 0.0090  -0.0045 -0.0045 145 LEU A C   
1205 O O   . LEU A 146 ? 0.1836 0.1845 0.2242 0.0091  -0.0029 -0.0061 145 LEU A O   
1206 C CB  . LEU A 146 ? 0.1543 0.1599 0.2044 0.0091  -0.0050 -0.0026 145 LEU A CB  
1207 C CG  . LEU A 146 ? 0.1792 0.1884 0.2359 0.0098  -0.0044 -0.0022 145 LEU A CG  
1208 C CD1 . LEU A 146 ? 0.1749 0.1864 0.2322 0.0081  -0.0050 -0.0012 145 LEU A CD1 
1209 C CD2 . LEU A 146 ? 0.1749 0.1850 0.2333 0.0110  -0.0011 -0.0042 145 LEU A CD2 
1210 N N   . ASN A 147 ? 0.1958 0.1957 0.2366 0.0080  -0.0064 -0.0035 146 ASN A N   
1211 C CA  . ASN A 147 ? 0.1597 0.1584 0.1961 0.0072  -0.0064 -0.0044 146 ASN A CA  
1212 C C   . ASN A 147 ? 0.1772 0.1745 0.2132 0.0076  -0.0054 -0.0061 146 ASN A C   
1213 O O   . ASN A 147 ? 0.1637 0.1613 0.1970 0.0075  -0.0047 -0.0077 146 ASN A O   
1214 C CB  . ASN A 147 ? 0.1614 0.1593 0.1959 0.0060  -0.0081 -0.0033 146 ASN A CB  
1215 C CG  . ASN A 147 ? 0.1552 0.1540 0.1882 0.0052  -0.0088 -0.0027 146 ASN A CG  
1216 O OD1 . ASN A 147 ? 0.1607 0.1595 0.1912 0.0051  -0.0083 -0.0036 146 ASN A OD1 
1217 N ND2 . ASN A 147 ? 0.1626 0.1622 0.1976 0.0048  -0.0101 -0.0013 146 ASN A ND2 
1218 N N   . GLN A 148 ? 0.1566 0.1523 0.1952 0.0080  -0.0055 -0.0058 147 GLN A N   
1219 C CA  . GLN A 148 ? 0.1440 0.1377 0.1823 0.0081  -0.0045 -0.0077 147 GLN A CA  
1220 C C   . GLN A 148 ? 0.1787 0.1734 0.2172 0.0090  -0.0025 -0.0100 147 GLN A C   
1221 O O   . GLN A 148 ? 0.1729 0.1673 0.2091 0.0085  -0.0018 -0.0122 147 GLN A O   
1222 C CB  . GLN A 148 ? 0.1989 0.1894 0.2399 0.0084  -0.0050 -0.0068 147 GLN A CB  
1223 C CG  . GLN A 148 ? 0.1764 0.1642 0.2169 0.0079  -0.0040 -0.0089 147 GLN A CG  
1224 C CD  . GLN A 148 ? 0.2273 0.2151 0.2643 0.0057  -0.0044 -0.0093 147 GLN A CD  
1225 O OE1 . GLN A 148 ? 0.1976 0.1846 0.2335 0.0046  -0.0056 -0.0072 147 GLN A OE1 
1226 N NE2 . GLN A 148 ? 0.1887 0.1777 0.2239 0.0051  -0.0036 -0.0119 147 GLN A NE2 
1227 N N   . ALA A 149 ? 0.1824 0.1787 0.2237 0.0102  -0.0016 -0.0097 148 ALA A N   
1228 C CA  . ALA A 149 ? 0.1788 0.1762 0.2197 0.0109  0.0007  -0.0119 148 ALA A CA  
1229 C C   . ALA A 149 ? 0.1891 0.1879 0.2249 0.0100  0.0010  -0.0125 148 ALA A C   
1230 O O   . ALA A 149 ? 0.1996 0.1984 0.2325 0.0099  0.0022  -0.0147 148 ALA A O   
1231 C CB  . ALA A 149 ? 0.1935 0.1930 0.2389 0.0120  0.0019  -0.0113 148 ALA A CB  
1232 N N   . ALA A 150 ? 0.1721 0.1717 0.2064 0.0094  -0.0004 -0.0105 149 ALA A N   
1233 C CA  . ALA A 150 ? 0.1632 0.1635 0.1929 0.0089  -0.0006 -0.0106 149 ALA A CA  
1234 C C   . ALA A 150 ? 0.1982 0.1980 0.2253 0.0085  -0.0015 -0.0122 149 ALA A C   
1235 O O   . ALA A 150 ? 0.1855 0.1860 0.2093 0.0086  -0.0012 -0.0135 149 ALA A O   
1236 C CB  . ALA A 150 ? 0.1656 0.1662 0.1949 0.0084  -0.0020 -0.0085 149 ALA A CB  
1237 N N   . ILE A 151 ? 0.1756 0.1745 0.2040 0.0079  -0.0026 -0.0121 150 ILE A N   
1238 C CA  . ILE A 151 ? 0.1604 0.1594 0.1874 0.0072  -0.0033 -0.0137 150 ILE A CA  
1239 C C   . ILE A 151 ? 0.2178 0.2163 0.2443 0.0071  -0.0022 -0.0164 150 ILE A C   
1240 O O   . ILE A 151 ? 0.1816 0.1814 0.2054 0.0067  -0.0026 -0.0181 150 ILE A O   
1241 C CB  . ILE A 151 ? 0.1744 0.1721 0.2031 0.0061  -0.0041 -0.0130 150 ILE A CB  
1242 C CG1 . ILE A 151 ? 0.1425 0.1411 0.1707 0.0059  -0.0051 -0.0112 150 ILE A CG1 
1243 C CG2 . ILE A 151 ? 0.2055 0.2035 0.2336 0.0049  -0.0043 -0.0151 150 ILE A CG2 
1244 C CD1 . ILE A 151 ? 0.2010 0.1981 0.2303 0.0047  -0.0057 -0.0100 150 ILE A CD1 
1245 N N   . ASP A 152 ? 0.1946 0.1912 0.2238 0.0076  -0.0009 -0.0168 151 ASP A N   
1246 C CA  . ASP A 152 ? 0.1814 0.1769 0.2102 0.0076  0.0006  -0.0198 151 ASP A CA  
1247 C C   . ASP A 152 ? 0.1647 0.1622 0.1897 0.0079  0.0015  -0.0211 151 ASP A C   
1248 O O   . ASP A 152 ? 0.1745 0.1723 0.1965 0.0072  0.0016  -0.0238 151 ASP A O   
1249 C CB  . ASP A 152 ? 0.1807 0.1737 0.2137 0.0086  0.0019  -0.0199 151 ASP A CB  
1250 C CG  . ASP A 152 ? 0.2168 0.2068 0.2528 0.0081  0.0008  -0.0186 151 ASP A CG  
1251 O OD1 . ASP A 152 ? 0.2357 0.2257 0.2702 0.0066  -0.0006 -0.0179 151 ASP A OD1 
1252 O OD2 . ASP A 152 ? 0.2183 0.2060 0.2581 0.0093  0.0015  -0.0181 151 ASP A OD2 
1253 N N   . GLY A 153 ? 0.1772 0.1760 0.2018 0.0087  0.0022  -0.0193 152 GLY A N   
1254 C CA  . GLY A 153 ? 0.1912 0.1915 0.2114 0.0087  0.0034  -0.0201 152 GLY A CA  
1255 C C   . GLY A 153 ? 0.2008 0.2024 0.2162 0.0082  0.0013  -0.0199 152 GLY A C   
1256 O O   . GLY A 153 ? 0.1949 0.1972 0.2059 0.0078  0.0015  -0.0217 152 GLY A O   
1257 N N   . ILE A 154 ? 0.1906 0.1925 0.2068 0.0083  -0.0007 -0.0178 153 ILE A N   
1258 C CA  . ILE A 154 ? 0.1811 0.1845 0.1941 0.0083  -0.0029 -0.0175 153 ILE A CA  
1259 C C   . ILE A 154 ? 0.2071 0.2117 0.2194 0.0074  -0.0039 -0.0203 153 ILE A C   
1260 O O   . ILE A 154 ? 0.1841 0.1903 0.1923 0.0074  -0.0050 -0.0214 153 ILE A O   
1261 C CB  . ILE A 154 ? 0.1645 0.1680 0.1797 0.0086  -0.0044 -0.0153 153 ILE A CB  
1262 C CG1 . ILE A 154 ? 0.1570 0.1595 0.1720 0.0091  -0.0037 -0.0127 153 ILE A CG1 
1263 C CG2 . ILE A 154 ? 0.1883 0.1939 0.2020 0.0089  -0.0067 -0.0156 153 ILE A CG2 
1264 C CD1 . ILE A 154 ? 0.1447 0.1467 0.1628 0.0090  -0.0045 -0.0111 153 ILE A CD1 
1265 N N   . ARG A 155 ? 0.1774 0.1810 0.1933 0.0066  -0.0038 -0.0216 154 ARG A N   
1266 C CA  . ARG A 155 ? 0.1716 0.1763 0.1874 0.0053  -0.0047 -0.0244 154 ARG A CA  
1267 C C   . ARG A 155 ? 0.1906 0.1946 0.2034 0.0048  -0.0035 -0.0274 154 ARG A C   
1268 O O   . ARG A 155 ? 0.2128 0.2186 0.2234 0.0038  -0.0047 -0.0298 154 ARG A O   
1269 C CB  . ARG A 155 ? 0.1732 0.1763 0.1933 0.0041  -0.0045 -0.0247 154 ARG A CB  
1270 C CG  . ARG A 155 ? 0.1812 0.1851 0.2035 0.0042  -0.0054 -0.0222 154 ARG A CG  
1271 C CD  . ARG A 155 ? 0.1534 0.1611 0.1745 0.0047  -0.0074 -0.0220 154 ARG A CD  
1272 N NE  . ARG A 155 ? 0.1629 0.1713 0.1863 0.0046  -0.0078 -0.0205 154 ARG A NE  
1273 C CZ  . ARG A 155 ? 0.1716 0.1823 0.1947 0.0057  -0.0090 -0.0195 154 ARG A CZ  
1274 N NH1 . ARG A 155 ? 0.1755 0.1876 0.1960 0.0072  -0.0103 -0.0193 154 ARG A NH1 
1275 N NH2 . ARG A 155 ? 0.1673 0.1785 0.1925 0.0055  -0.0089 -0.0186 154 ARG A NH2 
1276 N N   . SER A 156 ? 0.2005 0.2023 0.2136 0.0055  -0.0010 -0.0275 155 SER A N   
1277 C CA  . SER A 156 ? 0.2377 0.2388 0.2479 0.0051  0.0007  -0.0308 155 SER A CA  
1278 C C   . SER A 156 ? 0.2530 0.2566 0.2566 0.0050  -0.0001 -0.0310 155 SER A C   
1279 O O   . SER A 156 ? 0.2169 0.2208 0.2166 0.0041  0.0004  -0.0343 155 SER A O   
1280 C CB  . SER A 156 ? 0.2380 0.2370 0.2506 0.0061  0.0038  -0.0308 155 SER A CB  
1281 O OG  . SER A 156 ? 0.2090 0.2095 0.2191 0.0070  0.0048  -0.0287 155 SER A OG  
1282 N N   . ALA A 157 ? 0.2083 0.2133 0.2101 0.0059  -0.0013 -0.0276 156 ALA A N   
1283 C CA  . ALA A 157 ? 0.2653 0.2721 0.2605 0.0061  -0.0025 -0.0269 156 ALA A CA  
1284 C C   . ALA A 157 ? 0.2735 0.2830 0.2669 0.0056  -0.0060 -0.0279 156 ALA A C   
1285 O O   . ALA A 157 ? 0.2883 0.2993 0.2759 0.0059  -0.0078 -0.0271 156 ALA A O   
1286 C CB  . ALA A 157 ? 0.2784 0.2848 0.2727 0.0072  -0.0025 -0.0228 156 ALA A CB  
1287 N N   . GLY A 158 ? 0.2064 0.2167 0.2046 0.0049  -0.0073 -0.0294 157 GLY A N   
1288 C CA  . GLY A 158 ? 0.2360 0.2498 0.2343 0.0045  -0.0106 -0.0302 157 GLY A CA  
1289 C C   . GLY A 158 ? 0.2674 0.2830 0.2678 0.0060  -0.0128 -0.0269 157 GLY A C   
1290 O O   . GLY A 158 ? 0.2349 0.2542 0.2356 0.0063  -0.0158 -0.0273 157 GLY A O   
1291 N N   . ALA A 159 ? 0.2206 0.2339 0.2228 0.0072  -0.0113 -0.0240 158 ALA A N   
1292 C CA  . ALA A 159 ? 0.1793 0.1935 0.1838 0.0086  -0.0129 -0.0213 158 ALA A CA  
1293 C C   . ALA A 159 ? 0.1882 0.2031 0.1988 0.0078  -0.0126 -0.0223 158 ALA A C   
1294 O O   . ALA A 159 ? 0.2006 0.2130 0.2137 0.0076  -0.0108 -0.0212 158 ALA A O   
1295 C CB  . ALA A 159 ? 0.1639 0.1751 0.1671 0.0098  -0.0115 -0.0181 158 ALA A CB  
1296 N N   . THR A 160 ? 0.1949 0.2134 0.2075 0.0070  -0.0145 -0.0244 159 THR A N   
1297 C CA  . THR A 160 ? 0.1827 0.2020 0.2005 0.0054  -0.0138 -0.0257 159 THR A CA  
1298 C C   . THR A 160 ? 0.2211 0.2440 0.2427 0.0062  -0.0153 -0.0250 159 THR A C   
1299 O O   . THR A 160 ? 0.2259 0.2492 0.2514 0.0048  -0.0142 -0.0256 159 THR A O   
1300 C CB  . THR A 160 ? 0.2472 0.2680 0.2656 0.0030  -0.0141 -0.0293 159 THR A CB  
1301 O OG1 . THR A 160 ? 0.2434 0.2687 0.2601 0.0034  -0.0170 -0.0306 159 THR A OG1 
1302 C CG2 . THR A 160 ? 0.2882 0.3049 0.3040 0.0021  -0.0121 -0.0306 159 THR A CG2 
1303 N N   . SER A 161 ? 0.1873 0.2126 0.2076 0.0084  -0.0176 -0.0239 160 SER A N   
1304 C CA  . SER A 161 ? 0.1940 0.2230 0.2185 0.0096  -0.0189 -0.0236 160 SER A CA  
1305 C C   . SER A 161 ? 0.1744 0.2004 0.1996 0.0111  -0.0176 -0.0212 160 SER A C   
1306 O O   . SER A 161 ? 0.1987 0.2271 0.2278 0.0118  -0.0177 -0.0214 160 SER A O   
1307 C CB  . SER A 161 ? 0.2336 0.2664 0.2571 0.0118  -0.0223 -0.0234 160 SER A CB  
1308 O OG  . SER A 161 ? 0.2470 0.2762 0.2653 0.0137  -0.0228 -0.0206 160 SER A OG  
1309 N N   . GLN A 162 ? 0.1815 0.2027 0.2032 0.0114  -0.0162 -0.0191 161 GLN A N   
1310 C CA  . GLN A 162 ? 0.1760 0.1942 0.1975 0.0128  -0.0155 -0.0168 161 GLN A CA  
1311 C C   . GLN A 162 ? 0.1566 0.1730 0.1805 0.0113  -0.0133 -0.0168 161 GLN A C   
1312 O O   . GLN A 162 ? 0.1671 0.1822 0.1911 0.0094  -0.0119 -0.0174 161 GLN A O   
1313 C CB  . GLN A 162 ? 0.1665 0.1807 0.1833 0.0134  -0.0150 -0.0146 161 GLN A CB  
1314 C CG  . GLN A 162 ? 0.1685 0.1834 0.1814 0.0149  -0.0172 -0.0137 161 GLN A CG  
1315 C CD  . GLN A 162 ? 0.2007 0.2172 0.2107 0.0137  -0.0175 -0.0155 161 GLN A CD  
1316 O OE1 . GLN A 162 ? 0.1737 0.1906 0.1853 0.0118  -0.0161 -0.0176 161 GLN A OE1 
1317 N NE2 . GLN A 162 ? 0.2105 0.2274 0.2159 0.0147  -0.0195 -0.0146 161 GLN A NE2 
1318 N N   . TYR A 163 ? 0.1498 0.1656 0.1751 0.0123  -0.0131 -0.0160 162 TYR A N   
1319 C CA  . TYR A 163 ? 0.1459 0.1594 0.1720 0.0109  -0.0112 -0.0155 162 TYR A CA  
1320 C C   . TYR A 163 ? 0.1976 0.2070 0.2210 0.0106  -0.0104 -0.0136 162 TYR A C   
1321 O O   . TYR A 163 ? 0.1861 0.1940 0.2071 0.0118  -0.0109 -0.0123 162 TYR A O   
1322 C CB  . TYR A 163 ? 0.1301 0.1438 0.1578 0.0119  -0.0111 -0.0155 162 TYR A CB  
1323 C CG  . TYR A 163 ? 0.1678 0.1863 0.1992 0.0118  -0.0111 -0.0177 162 TYR A CG  
1324 C CD1 . TYR A 163 ? 0.1873 0.2070 0.2203 0.0094  -0.0095 -0.0189 162 TYR A CD1 
1325 C CD2 . TYR A 163 ? 0.1631 0.1850 0.1966 0.0141  -0.0129 -0.0185 162 TYR A CD2 
1326 C CE1 . TYR A 163 ? 0.2116 0.2361 0.2484 0.0090  -0.0090 -0.0210 162 TYR A CE1 
1327 C CE2 . TYR A 163 ? 0.2220 0.2492 0.2601 0.0140  -0.0128 -0.0208 162 TYR A CE2 
1328 C CZ  . TYR A 163 ? 0.2283 0.2569 0.2681 0.0113  -0.0106 -0.0222 162 TYR A CZ  
1329 O OH  . TYR A 163 ? 0.2527 0.2871 0.2973 0.0108  -0.0101 -0.0246 162 TYR A OH  
1330 N N   . ILE A 164 ? 0.1566 0.1644 0.1806 0.0090  -0.0092 -0.0133 163 ILE A N   
1331 C CA  . ILE A 164 ? 0.1593 0.1641 0.1821 0.0087  -0.0085 -0.0116 163 ILE A CA  
1332 C C   . ILE A 164 ? 0.1810 0.1844 0.2043 0.0080  -0.0081 -0.0108 163 ILE A C   
1333 O O   . ILE A 164 ? 0.1796 0.1836 0.2039 0.0067  -0.0077 -0.0113 163 ILE A O   
1334 C CB  . ILE A 164 ? 0.1531 0.1572 0.1763 0.0076  -0.0076 -0.0118 163 ILE A CB  
1335 C CG1 . ILE A 164 ? 0.1643 0.1696 0.1863 0.0081  -0.0078 -0.0132 163 ILE A CG1 
1336 C CG2 . ILE A 164 ? 0.1761 0.1780 0.1995 0.0076  -0.0069 -0.0102 163 ILE A CG2 
1337 C CD1 . ILE A 164 ? 0.1867 0.1910 0.2095 0.0071  -0.0068 -0.0142 163 ILE A CD1 
1338 N N   . PHE A 165 ? 0.1519 0.1535 0.1743 0.0086  -0.0083 -0.0095 164 PHE A N   
1339 C CA  . PHE A 165 ? 0.1576 0.1576 0.1800 0.0077  -0.0081 -0.0089 164 PHE A CA  
1340 C C   . PHE A 165 ? 0.1778 0.1769 0.2008 0.0066  -0.0079 -0.0076 164 PHE A C   
1341 O O   . PHE A 165 ? 0.1937 0.1922 0.2167 0.0070  -0.0076 -0.0067 164 PHE A O   
1342 C CB  . PHE A 165 ? 0.1431 0.1412 0.1645 0.0086  -0.0084 -0.0084 164 PHE A CB  
1343 C CG  . PHE A 165 ? 0.1419 0.1408 0.1636 0.0101  -0.0087 -0.0098 164 PHE A CG  
1344 C CD1 . PHE A 165 ? 0.1477 0.1498 0.1709 0.0103  -0.0087 -0.0114 164 PHE A CD1 
1345 C CD2 . PHE A 165 ? 0.1685 0.1648 0.1896 0.0113  -0.0090 -0.0095 164 PHE A CD2 
1346 C CE1 . PHE A 165 ? 0.2042 0.2079 0.2288 0.0118  -0.0090 -0.0128 164 PHE A CE1 
1347 C CE2 . PHE A 165 ? 0.1768 0.1739 0.1990 0.0131  -0.0094 -0.0108 164 PHE A CE2 
1348 C CZ  . PHE A 165 ? 0.1741 0.1752 0.1983 0.0135  -0.0093 -0.0125 164 PHE A CZ  
1349 N N   . VAL A 166 ? 0.1302 0.1294 0.1537 0.0053  -0.0080 -0.0075 165 VAL A N   
1350 C CA  . VAL A 166 ? 0.1360 0.1345 0.1606 0.0046  -0.0083 -0.0060 165 VAL A CA  
1351 C C   . VAL A 166 ? 0.1607 0.1584 0.1845 0.0036  -0.0090 -0.0054 165 VAL A C   
1352 O O   . VAL A 166 ? 0.1753 0.1728 0.1974 0.0031  -0.0091 -0.0062 165 VAL A O   
1353 C CB  . VAL A 166 ? 0.1633 0.1618 0.1887 0.0038  -0.0083 -0.0058 165 VAL A CB  
1354 C CG1 . VAL A 166 ? 0.1791 0.1779 0.2052 0.0045  -0.0075 -0.0070 165 VAL A CG1 
1355 C CG2 . VAL A 166 ? 0.1585 0.1569 0.1821 0.0024  -0.0085 -0.0060 165 VAL A CG2 
1356 N N   . GLU A 167 ? 0.1478 0.1455 0.1732 0.0033  -0.0095 -0.0041 166 GLU A N   
1357 C CA  . GLU A 167 ? 0.1661 0.1634 0.1910 0.0020  -0.0106 -0.0036 166 GLU A CA  
1358 C C   . GLU A 167 ? 0.1888 0.1870 0.2155 0.0012  -0.0120 -0.0021 166 GLU A C   
1359 O O   . GLU A 167 ? 0.1725 0.1715 0.2021 0.0021  -0.0119 -0.0013 166 GLU A O   
1360 C CB  . GLU A 167 ? 0.1720 0.1687 0.1977 0.0020  -0.0102 -0.0035 166 GLU A CB  
1361 C CG  . GLU A 167 ? 0.1733 0.1684 0.1970 0.0031  -0.0093 -0.0045 166 GLU A CG  
1362 C CD  . GLU A 167 ? 0.1877 0.1807 0.2110 0.0026  -0.0091 -0.0042 166 GLU A CD  
1363 O OE1 . GLU A 167 ? 0.1609 0.1535 0.1846 0.0010  -0.0098 -0.0041 166 GLU A OE1 
1364 O OE2 . GLU A 167 ? 0.1794 0.1710 0.2018 0.0038  -0.0083 -0.0040 166 GLU A OE2 
1365 N N   . GLY A 168 ? 0.1763 0.1744 0.2014 -0.0003 -0.0134 -0.0019 167 GLY A N   
1366 C CA  . GLY A 168 ? 0.1833 0.1822 0.2093 -0.0010 -0.0154 -0.0002 167 GLY A CA  
1367 C C   . GLY A 168 ? 0.1771 0.1777 0.2057 -0.0019 -0.0168 0.0004  167 GLY A C   
1368 O O   . GLY A 168 ? 0.1731 0.1735 0.2023 -0.0022 -0.0159 -0.0005 167 GLY A O   
1369 N N   . ASN A 169 ? 0.1741 0.1761 0.2041 -0.0024 -0.0192 0.0020  168 ASN A N   
1370 C CA  . ASN A 169 ? 0.1942 0.1987 0.2272 -0.0034 -0.0212 0.0027  168 ASN A CA  
1371 C C   . ASN A 169 ? 0.1840 0.1876 0.2127 -0.0059 -0.0223 0.0014  168 ASN A C   
1372 O O   . ASN A 169 ? 0.1742 0.1754 0.1980 -0.0065 -0.0212 0.0000  168 ASN A O   
1373 C CB  . ASN A 169 ? 0.1707 0.1770 0.2066 -0.0027 -0.0238 0.0050  168 ASN A CB  
1374 C CG  . ASN A 169 ? 0.1916 0.2020 0.2348 -0.0021 -0.0248 0.0057  168 ASN A CG  
1375 O OD1 . ASN A 169 ? 0.2021 0.2141 0.2472 -0.0034 -0.0244 0.0046  168 ASN A OD1 
1376 N ND2 . ASN A 169 ? 0.1849 0.1968 0.2325 -0.0002 -0.0260 0.0074  168 ASN A ND2 
1377 N N   . SER A 170 ? 0.1821 0.1880 0.2131 -0.0075 -0.0244 0.0016  169 SER A N   
1378 C CA  . SER A 170 ? 0.1828 0.1878 0.2101 -0.0101 -0.0254 0.0000  169 SER A CA  
1379 C C   . SER A 170 ? 0.2067 0.2084 0.2319 -0.0102 -0.0225 -0.0023 169 SER A C   
1380 O O   . SER A 170 ? 0.2081 0.2071 0.2283 -0.0113 -0.0221 -0.0042 169 SER A O   
1381 C CB  . SER A 170 ? 0.2077 0.2119 0.2289 -0.0114 -0.0274 0.0002  169 SER A CB  
1382 O OG  . SER A 170 ? 0.2359 0.2431 0.2587 -0.0119 -0.0311 0.0024  169 SER A OG  
1383 N N   . TRP A 171 ? 0.1738 0.1755 0.2029 -0.0090 -0.0205 -0.0021 170 TRP A N   
1384 C CA  . TRP A 171 ? 0.1900 0.1883 0.2176 -0.0089 -0.0181 -0.0036 170 TRP A CA  
1385 C C   . TRP A 171 ? 0.1832 0.1788 0.2063 -0.0075 -0.0167 -0.0047 170 TRP A C   
1386 O O   . TRP A 171 ? 0.1798 0.1723 0.2004 -0.0076 -0.0156 -0.0065 170 TRP A O   
1387 C CB  . TRP A 171 ? 0.2450 0.2418 0.2718 -0.0115 -0.0188 -0.0052 170 TRP A CB  
1388 C CG  . TRP A 171 ? 0.2136 0.2140 0.2451 -0.0136 -0.0206 -0.0044 170 TRP A CG  
1389 C CD1 . TRP A 171 ? 0.2470 0.2507 0.2791 -0.0152 -0.0238 -0.0041 170 TRP A CD1 
1390 C CD2 . TRP A 171 ? 0.2243 0.2257 0.2606 -0.0144 -0.0194 -0.0039 170 TRP A CD2 
1391 N NE1 . TRP A 171 ? 0.2275 0.2348 0.2654 -0.0168 -0.0248 -0.0036 170 TRP A NE1 
1392 C CE2 . TRP A 171 ? 0.2325 0.2385 0.2731 -0.0165 -0.0219 -0.0036 170 TRP A CE2 
1393 C CE3 . TRP A 171 ? 0.2408 0.2398 0.2779 -0.0138 -0.0166 -0.0037 170 TRP A CE3 
1394 C CZ2 . TRP A 171 ? 0.2311 0.2398 0.2775 -0.0181 -0.0212 -0.0032 170 TRP A CZ2 
1395 C CZ3 . TRP A 171 ? 0.2442 0.2452 0.2862 -0.0155 -0.0157 -0.0030 170 TRP A CZ3 
1396 C CH2 . TRP A 171 ? 0.2677 0.2737 0.3146 -0.0177 -0.0179 -0.0029 170 TRP A CH2 
1397 N N   . THR A 172 ? 0.1679 0.1647 0.1908 -0.0061 -0.0167 -0.0037 171 THR A N   
1398 C CA  . THR A 172 ? 0.1404 0.1360 0.1600 -0.0050 -0.0155 -0.0046 171 THR A CA  
1399 C C   . THR A 172 ? 0.1993 0.1930 0.2143 -0.0064 -0.0154 -0.0067 171 THR A C   
1400 O O   . THR A 172 ? 0.2018 0.1943 0.2147 -0.0055 -0.0138 -0.0082 171 THR A O   
1401 C CB  . THR A 172 ? 0.1645 0.1593 0.1854 -0.0028 -0.0134 -0.0049 171 THR A CB  
1402 O OG1 . THR A 172 ? 0.1760 0.1713 0.1958 -0.0018 -0.0127 -0.0050 171 THR A OG1 
1403 C CG2 . THR A 172 ? 0.1572 0.1492 0.1768 -0.0024 -0.0122 -0.0064 171 THR A CG2 
1404 N N   . GLY A 173 ? 0.2020 0.1960 0.2153 -0.0087 -0.0173 -0.0070 172 GLY A N   
1405 C CA  . GLY A 173 ? 0.1736 0.1657 0.1822 -0.0103 -0.0170 -0.0095 172 GLY A CA  
1406 C C   . GLY A 173 ? 0.1908 0.1833 0.1953 -0.0104 -0.0162 -0.0098 172 GLY A C   
1407 O O   . GLY A 173 ? 0.2113 0.2055 0.2155 -0.0105 -0.0173 -0.0076 172 GLY A O   
1408 N N   . ALA A 174 ? 0.1828 0.1738 0.1846 -0.0102 -0.0141 -0.0126 173 ALA A N   
1409 C CA  . ALA A 174 ? 0.1932 0.1850 0.1911 -0.0109 -0.0129 -0.0132 173 ALA A CA  
1410 C C   . ALA A 174 ? 0.2246 0.2168 0.2172 -0.0138 -0.0148 -0.0128 173 ALA A C   
1411 O O   . ALA A 174 ? 0.2027 0.1959 0.1926 -0.0146 -0.0152 -0.0109 173 ALA A O   
1412 C CB  . ALA A 174 ? 0.2080 0.1986 0.2048 -0.0100 -0.0101 -0.0166 173 ALA A CB  
1413 N N   . TRP A 175 ? 0.2165 0.2075 0.2072 -0.0156 -0.0160 -0.0145 174 TRP A N   
1414 C CA  . TRP A 175 ? 0.1945 0.1860 0.1791 -0.0186 -0.0179 -0.0146 174 TRP A CA  
1415 C C   . TRP A 175 ? 0.2382 0.2318 0.2233 -0.0192 -0.0215 -0.0106 174 TRP A C   
1416 O O   . TRP A 175 ? 0.2391 0.2333 0.2185 -0.0214 -0.0232 -0.0096 174 TRP A O   
1417 C CB  . TRP A 175 ? 0.2148 0.2045 0.1976 -0.0205 -0.0187 -0.0177 174 TRP A CB  
1418 C CG  . TRP A 175 ? 0.2096 0.1993 0.1979 -0.0204 -0.0207 -0.0169 174 TRP A CG  
1419 C CD1 . TRP A 175 ? 0.2179 0.2081 0.2129 -0.0181 -0.0203 -0.0150 174 TRP A CD1 
1420 C CD2 . TRP A 175 ? 0.2608 0.2502 0.2481 -0.0232 -0.0230 -0.0183 174 TRP A CD2 
1421 N NE1 . TRP A 175 ? 0.2515 0.2418 0.2499 -0.0193 -0.0221 -0.0149 174 TRP A NE1 
1422 C CE2 . TRP A 175 ? 0.2594 0.2493 0.2535 -0.0225 -0.0238 -0.0170 174 TRP A CE2 
1423 C CE3 . TRP A 175 ? 0.2621 0.2511 0.2432 -0.0264 -0.0245 -0.0208 174 TRP A CE3 
1424 C CZ2 . TRP A 175 ? 0.2295 0.2195 0.2250 -0.0250 -0.0260 -0.0180 174 TRP A CZ2 
1425 C CZ3 . TRP A 175 ? 0.2545 0.2435 0.2367 -0.0289 -0.0270 -0.0220 174 TRP A CZ3 
1426 C CH2 . TRP A 175 ? 0.2258 0.2155 0.2156 -0.0283 -0.0277 -0.0205 174 TRP A CH2 
1427 N N   . THR A 176 ? 0.1995 0.1943 0.1911 -0.0173 -0.0225 -0.0082 175 THR A N   
1428 C CA  . THR A 176 ? 0.1881 0.1851 0.1818 -0.0173 -0.0258 -0.0045 175 THR A CA  
1429 C C   . THR A 176 ? 0.2345 0.2315 0.2301 -0.0152 -0.0248 -0.0019 175 THR A C   
1430 O O   . THR A 176 ? 0.2220 0.2202 0.2198 -0.0146 -0.0273 0.0013  175 THR A O   
1431 C CB  . THR A 176 ? 0.1715 0.1703 0.1719 -0.0167 -0.0275 -0.0039 175 THR A CB  
1432 O OG1 . THR A 176 ? 0.2200 0.2176 0.2248 -0.0146 -0.0246 -0.0050 175 THR A OG1 
1433 C CG2 . THR A 176 ? 0.2189 0.2178 0.2173 -0.0195 -0.0294 -0.0061 175 THR A CG2 
1434 N N   . TRP A 177 ? 0.2100 0.2058 0.2052 -0.0141 -0.0214 -0.0033 176 TRP A N   
1435 C CA  . TRP A 177 ? 0.2047 0.2004 0.2031 -0.0122 -0.0203 -0.0014 176 TRP A CA  
1436 C C   . TRP A 177 ? 0.2298 0.2251 0.2253 -0.0130 -0.0220 0.0018  176 TRP A C   
1437 O O   . TRP A 177 ? 0.2183 0.2138 0.2177 -0.0115 -0.0234 0.0044  176 TRP A O   
1438 C CB  . TRP A 177 ? 0.1852 0.1802 0.1832 -0.0113 -0.0167 -0.0038 176 TRP A CB  
1439 C CG  . TRP A 177 ? 0.1905 0.1856 0.1921 -0.0096 -0.0157 -0.0023 176 TRP A CG  
1440 C CD1 . TRP A 177 ? 0.1896 0.1841 0.1896 -0.0101 -0.0154 -0.0006 176 TRP A CD1 
1441 C CD2 . TRP A 177 ? 0.1727 0.1683 0.1799 -0.0072 -0.0150 -0.0025 176 TRP A CD2 
1442 N NE1 . TRP A 177 ? 0.2084 0.2029 0.2131 -0.0082 -0.0144 -0.0001 176 TRP A NE1 
1443 C CE2 . TRP A 177 ? 0.1693 0.1647 0.1781 -0.0064 -0.0142 -0.0014 176 TRP A CE2 
1444 C CE3 . TRP A 177 ? 0.1733 0.1692 0.1838 -0.0059 -0.0147 -0.0037 176 TRP A CE3 
1445 C CZ2 . TRP A 177 ? 0.1869 0.1826 0.2001 -0.0043 -0.0133 -0.0016 176 TRP A CZ2 
1446 C CZ3 . TRP A 177 ? 0.1945 0.1907 0.2091 -0.0038 -0.0138 -0.0035 176 TRP A CZ3 
1447 C CH2 . TRP A 177 ? 0.1916 0.1879 0.2074 -0.0030 -0.0132 -0.0026 176 TRP A CH2 
1448 N N   . THR A 178 ? 0.2270 0.2214 0.2154 -0.0154 -0.0217 0.0016  177 THR A N   
1449 C CA  . THR A 178 ? 0.2174 0.2106 0.2024 -0.0163 -0.0231 0.0051  177 THR A CA  
1450 C C   . THR A 178 ? 0.2616 0.2555 0.2474 -0.0162 -0.0277 0.0084  177 THR A C   
1451 O O   . THR A 178 ? 0.3053 0.2979 0.2912 -0.0157 -0.0294 0.0120  177 THR A O   
1452 C CB  . THR A 178 ? 0.2586 0.2508 0.2351 -0.0193 -0.0216 0.0044  177 THR A CB  
1453 O OG1 . THR A 178 ? 0.2834 0.2764 0.2551 -0.0213 -0.0230 0.0026  177 THR A OG1 
1454 C CG2 . THR A 178 ? 0.2482 0.2406 0.2253 -0.0190 -0.0170 0.0012  177 THR A CG2 
1455 N N   . ASN A 179 ? 0.2719 0.2678 0.2589 -0.0167 -0.0299 0.0072  178 ASN A N   
1456 C CA  . ASN A 179 ? 0.2783 0.2758 0.2669 -0.0166 -0.0346 0.0101  178 ASN A CA  
1457 C C   . ASN A 179 ? 0.2267 0.2254 0.2243 -0.0134 -0.0355 0.0122  178 ASN A C   
1458 O O   . ASN A 179 ? 0.2499 0.2493 0.2493 -0.0126 -0.0391 0.0156  178 ASN A O   
1459 C CB  . ASN A 179 ? 0.2672 0.2670 0.2551 -0.0184 -0.0365 0.0078  178 ASN A CB  
1460 C CG  . ASN A 179 ? 0.3825 0.3811 0.3607 -0.0217 -0.0360 0.0057  178 ASN A CG  
1461 O OD1 . ASN A 179 ? 0.4838 0.4808 0.4551 -0.0231 -0.0362 0.0075  178 ASN A OD1 
1462 N ND2 . ASN A 179 ? 0.4609 0.4599 0.4385 -0.0231 -0.0351 0.0018  178 ASN A ND2 
1463 N N   . VAL A 180 ? 0.2189 0.2177 0.2221 -0.0115 -0.0324 0.0103  179 VAL A N   
1464 C CA  . VAL A 180 ? 0.1897 0.1899 0.2013 -0.0087 -0.0329 0.0117  179 VAL A CA  
1465 C C   . VAL A 180 ? 0.2074 0.2056 0.2217 -0.0067 -0.0296 0.0113  179 VAL A C   
1466 O O   . VAL A 180 ? 0.2150 0.2134 0.2349 -0.0044 -0.0301 0.0129  179 VAL A O   
1467 C CB  . VAL A 180 ? 0.2514 0.2550 0.2687 -0.0084 -0.0333 0.0098  179 VAL A CB  
1468 C CG1 . VAL A 180 ? 0.2831 0.2890 0.2984 -0.0107 -0.0369 0.0099  179 VAL A CG1 
1469 C CG2 . VAL A 180 ? 0.2376 0.2401 0.2547 -0.0085 -0.0295 0.0065  179 VAL A CG2 
1470 N N   . ASN A 181 ? 0.1907 0.1873 0.2018 -0.0073 -0.0263 0.0091  180 ASN A N   
1471 C CA  . ASN A 181 ? 0.1715 0.1671 0.1859 -0.0055 -0.0233 0.0079  180 ASN A CA  
1472 C C   . ASN A 181 ? 0.2009 0.1938 0.2127 -0.0058 -0.0219 0.0089  180 ASN A C   
1473 O O   . ASN A 181 ? 0.1786 0.1709 0.1919 -0.0051 -0.0193 0.0072  180 ASN A O   
1474 C CB  . ASN A 181 ? 0.1779 0.1742 0.1920 -0.0056 -0.0207 0.0045  180 ASN A CB  
1475 C CG  . ASN A 181 ? 0.1862 0.1845 0.2050 -0.0047 -0.0209 0.0037  180 ASN A CG  
1476 O OD1 . ASN A 181 ? 0.1916 0.1910 0.2156 -0.0030 -0.0213 0.0047  180 ASN A OD1 
1477 N ND2 . ASN A 181 ? 0.1705 0.1690 0.1876 -0.0058 -0.0206 0.0017  180 ASN A ND2 
1478 N N   . ASP A 182 ? 0.1936 0.1846 0.2014 -0.0071 -0.0238 0.0116  181 ASP A N   
1479 C CA  . ASP A 182 ? 0.1931 0.1810 0.1980 -0.0080 -0.0222 0.0126  181 ASP A CA  
1480 C C   . ASP A 182 ? 0.2301 0.2165 0.2406 -0.0059 -0.0210 0.0128  181 ASP A C   
1481 O O   . ASP A 182 ? 0.2446 0.2295 0.2544 -0.0065 -0.0185 0.0117  181 ASP A O   
1482 C CB  . ASP A 182 ? 0.2166 0.2021 0.2161 -0.0097 -0.0246 0.0163  181 ASP A CB  
1483 C CG  . ASP A 182 ? 0.2580 0.2400 0.2536 -0.0115 -0.0225 0.0174  181 ASP A CG  
1484 O OD1 . ASP A 182 ? 0.2392 0.2220 0.2314 -0.0135 -0.0195 0.0149  181 ASP A OD1 
1485 O OD2 . ASP A 182 ? 0.2505 0.2290 0.2471 -0.0109 -0.0237 0.0205  181 ASP A OD2 
1486 N N   . ASN A 183 ? 0.2187 0.2058 0.2350 -0.0034 -0.0227 0.0137  182 ASN A N   
1487 C CA  . ASN A 183 ? 0.2075 0.1928 0.2288 -0.0013 -0.0214 0.0136  182 ASN A CA  
1488 C C   . ASN A 183 ? 0.2558 0.2423 0.2787 -0.0010 -0.0182 0.0100  182 ASN A C   
1489 O O   . ASN A 183 ? 0.2357 0.2203 0.2610 -0.0001 -0.0167 0.0092  182 ASN A O   
1490 C CB  . ASN A 183 ? 0.2090 0.1953 0.2367 0.0014  -0.0236 0.0150  182 ASN A CB  
1491 C CG  . ASN A 183 ? 0.2106 0.2014 0.2425 0.0025  -0.0230 0.0127  182 ASN A CG  
1492 O OD1 . ASN A 183 ? 0.2092 0.2020 0.2385 0.0011  -0.0222 0.0108  182 ASN A OD1 
1493 N ND2 . ASN A 183 ? 0.1938 0.1859 0.2325 0.0051  -0.0232 0.0128  182 ASN A ND2 
1494 N N   . MET A 184 ? 0.1876 0.1770 0.2091 -0.0017 -0.0172 0.0077  183 MET A N   
1495 C CA  . MET A 184 ? 0.1525 0.1431 0.1751 -0.0011 -0.0147 0.0047  183 MET A CA  
1496 C C   . MET A 184 ? 0.2093 0.1985 0.2296 -0.0025 -0.0127 0.0037  183 MET A C   
1497 O O   . MET A 184 ? 0.1997 0.1900 0.2216 -0.0020 -0.0110 0.0013  183 MET A O   
1498 C CB  . MET A 184 ? 0.1652 0.1584 0.1865 -0.0015 -0.0144 0.0030  183 MET A CB  
1499 C CG  . MET A 184 ? 0.1760 0.1709 0.2005 -0.0004 -0.0159 0.0035  183 MET A CG  
1500 S SD  . MET A 184 ? 0.2178 0.2140 0.2472 0.0018  -0.0141 0.0019  183 MET A SD  
1501 C CE  . MET A 184 ? 0.2078 0.2045 0.2342 0.0014  -0.0123 -0.0006 183 MET A CE  
1502 N N   . LYS A 185 ? 0.1935 0.1807 0.2101 -0.0046 -0.0131 0.0054  184 LYS A N   
1503 C CA  . LYS A 185 ? 0.1797 0.1658 0.1945 -0.0064 -0.0110 0.0045  184 LYS A CA  
1504 C C   . LYS A 185 ? 0.2341 0.2181 0.2524 -0.0056 -0.0101 0.0040  184 LYS A C   
1505 O O   . LYS A 185 ? 0.2323 0.2165 0.2504 -0.0070 -0.0082 0.0022  184 LYS A O   
1506 C CB  . LYS A 185 ? 0.1946 0.1783 0.2042 -0.0090 -0.0113 0.0070  184 LYS A CB  
1507 C CG  . LYS A 185 ? 0.1799 0.1593 0.1895 -0.0087 -0.0135 0.0108  184 LYS A CG  
1508 C CD  . LYS A 185 ? 0.2204 0.1981 0.2234 -0.0112 -0.0147 0.0137  184 LYS A CD  
1509 C CE  . LYS A 185 ? 0.2645 0.2376 0.2672 -0.0107 -0.0173 0.0181  184 LYS A CE  
1510 N NZ  . LYS A 185 ? 0.2633 0.2348 0.2585 -0.0132 -0.0189 0.0213  184 LYS A NZ  
1511 N N   . SER A 186 ? 0.2073 0.1895 0.2290 -0.0035 -0.0113 0.0051  185 SER A N   
1512 C CA  A SER A 186 ? 0.2001 0.1793 0.2247 -0.0029 -0.0104 0.0045  185 SER A CA  
1513 C CA  B SER A 186 ? 0.2013 0.1805 0.2260 -0.0028 -0.0104 0.0046  185 SER A CA  
1514 C C   . SER A 186 ? 0.2043 0.1859 0.2320 -0.0015 -0.0090 0.0011  185 SER A C   
1515 O O   . SER A 186 ? 0.2388 0.2182 0.2687 -0.0012 -0.0080 -0.0001 185 SER A O   
1516 C CB  A SER A 186 ? 0.2416 0.2173 0.2689 -0.0011 -0.0122 0.0072  185 SER A CB  
1517 C CB  B SER A 186 ? 0.2409 0.2170 0.2685 -0.0009 -0.0123 0.0072  185 SER A CB  
1518 O OG  A SER A 186 ? 0.2615 0.2399 0.2922 0.0014  -0.0132 0.0071  185 SER A OG  
1519 O OG  B SER A 186 ? 0.2248 0.1985 0.2490 -0.0020 -0.0143 0.0109  185 SER A OG  
1520 N N   . LEU A 187 ? 0.2199 0.1669 0.1951 -0.0212 -0.0143 0.0018  186 LEU A N   
1521 C CA  . LEU A 187 ? 0.2068 0.1556 0.1832 -0.0186 -0.0146 -0.0005 186 LEU A CA  
1522 C C   . LEU A 187 ? 0.2341 0.1853 0.2121 -0.0207 -0.0152 -0.0020 186 LEU A C   
1523 O O   . LEU A 187 ? 0.2469 0.2014 0.2261 -0.0235 -0.0145 -0.0016 186 LEU A O   
1524 C CB  . LEU A 187 ? 0.2016 0.1549 0.1786 -0.0160 -0.0132 -0.0010 186 LEU A CB  
1525 C CG  . LEU A 187 ? 0.2166 0.1677 0.1927 -0.0134 -0.0127 0.0001  186 LEU A CG  
1526 C CD1 . LEU A 187 ? 0.2278 0.1834 0.2051 -0.0114 -0.0112 -0.0001 186 LEU A CD1 
1527 C CD2 . LEU A 187 ? 0.2369 0.1847 0.2126 -0.0106 -0.0137 -0.0005 186 LEU A CD2 
1528 N N   . THR A 188 ? 0.2105 0.1604 0.1889 -0.0192 -0.0166 -0.0039 187 THR A N   
1529 C CA  . THR A 188 ? 0.2120 0.1640 0.1923 -0.0208 -0.0177 -0.0058 187 THR A CA  
1530 C C   . THR A 188 ? 0.2295 0.1850 0.2101 -0.0176 -0.0179 -0.0081 187 THR A C   
1531 O O   . THR A 188 ? 0.2503 0.2048 0.2295 -0.0141 -0.0178 -0.0084 187 THR A O   
1532 C CB  . THR A 188 ? 0.2911 0.2375 0.2715 -0.0224 -0.0198 -0.0063 187 THR A CB  
1533 O OG1 . THR A 188 ? 0.3283 0.2710 0.3071 -0.0190 -0.0208 -0.0074 187 THR A OG1 
1534 C CG2 . THR A 188 ? 0.3235 0.2662 0.3035 -0.0255 -0.0197 -0.0037 187 THR A CG2 
1535 N N   . ASP A 189 ? 0.2243 0.1845 0.2072 -0.0189 -0.0182 -0.0097 188 ASP A N   
1536 C CA  . ASP A 189 ? 0.1811 0.1453 0.1644 -0.0161 -0.0186 -0.0118 188 ASP A CA  
1537 C C   . ASP A 189 ? 0.1877 0.1541 0.1734 -0.0182 -0.0202 -0.0139 188 ASP A C   
1538 O O   . ASP A 189 ? 0.2142 0.1833 0.2024 -0.0215 -0.0197 -0.0136 188 ASP A O   
1539 C CB  . ASP A 189 ? 0.1945 0.1641 0.1786 -0.0147 -0.0167 -0.0111 188 ASP A CB  
1540 C CG  . ASP A 189 ? 0.2232 0.1975 0.2081 -0.0121 -0.0171 -0.0129 188 ASP A CG  
1541 O OD1 . ASP A 189 ? 0.2085 0.1818 0.1925 -0.0104 -0.0188 -0.0147 188 ASP A OD1 
1542 O OD2 . ASP A 189 ? 0.2120 0.1911 0.1985 -0.0116 -0.0158 -0.0126 188 ASP A OD2 
1543 N N   . PRO A 190 ? 0.2134 0.1785 0.1986 -0.0166 -0.0222 -0.0163 189 PRO A N   
1544 C CA  . PRO A 190 ? 0.2550 0.2223 0.2429 -0.0187 -0.0241 -0.0187 189 PRO A CA  
1545 C C   . PRO A 190 ? 0.2556 0.2301 0.2459 -0.0188 -0.0235 -0.0195 189 PRO A C   
1546 O O   . PRO A 190 ? 0.3063 0.2833 0.3000 -0.0217 -0.0245 -0.0207 189 PRO A O   
1547 C CB  . PRO A 190 ? 0.2982 0.2631 0.2842 -0.0158 -0.0263 -0.0214 189 PRO A CB  
1548 C CG  . PRO A 190 ? 0.2784 0.2423 0.2609 -0.0115 -0.0250 -0.0203 189 PRO A CG  
1549 C CD  . PRO A 190 ? 0.2210 0.1830 0.2032 -0.0128 -0.0228 -0.0171 189 PRO A CD  
1550 N N   . SER A 191 ? 0.2259 0.2039 0.2152 -0.0158 -0.0220 -0.0187 190 SER A N   
1551 C CA  . SER A 191 ? 0.2146 0.1994 0.2065 -0.0157 -0.0213 -0.0192 190 SER A CA  
1552 C C   . SER A 191 ? 0.2229 0.2101 0.2169 -0.0186 -0.0191 -0.0173 190 SER A C   
1553 O O   . SER A 191 ? 0.2363 0.2293 0.2330 -0.0190 -0.0185 -0.0179 190 SER A O   
1554 C CB  . SER A 191 ? 0.2450 0.2323 0.2351 -0.0112 -0.0207 -0.0192 190 SER A CB  
1555 O OG  . SER A 191 ? 0.2556 0.2421 0.2438 -0.0085 -0.0227 -0.0211 190 SER A OG  
1556 N N   . ASP A 192 ? 0.2208 0.2038 0.2134 -0.0204 -0.0180 -0.0152 191 ASP A N   
1557 C CA  . ASP A 192 ? 0.2259 0.2111 0.2197 -0.0229 -0.0159 -0.0133 191 ASP A CA  
1558 C C   . ASP A 192 ? 0.2089 0.1991 0.2033 -0.0204 -0.0142 -0.0132 191 ASP A C   
1559 O O   . ASP A 192 ? 0.2417 0.2369 0.2386 -0.0219 -0.0130 -0.0133 191 ASP A O   
1560 C CB  . ASP A 192 ? 0.2486 0.2366 0.2459 -0.0272 -0.0160 -0.0137 191 ASP A CB  
1561 C CG  . ASP A 192 ? 0.2895 0.2787 0.2872 -0.0301 -0.0138 -0.0114 191 ASP A CG  
1562 O OD1 . ASP A 192 ? 0.3228 0.3085 0.3175 -0.0296 -0.0127 -0.0095 191 ASP A OD1 
1563 O OD2 . ASP A 192 ? 0.3675 0.3615 0.3685 -0.0329 -0.0131 -0.0117 191 ASP A OD2 
1564 N N   . LYS A 193 ? 0.1943 0.1830 0.1865 -0.0166 -0.0140 -0.0129 192 LYS A N   
1565 C CA  . LYS A 193 ? 0.1716 0.1643 0.1647 -0.0141 -0.0126 -0.0126 192 LYS A CA  
1566 C C   . LYS A 193 ? 0.1961 0.1854 0.1870 -0.0121 -0.0114 -0.0108 192 LYS A C   
1567 O O   . LYS A 193 ? 0.1938 0.1843 0.1847 -0.0089 -0.0109 -0.0106 192 LYS A O   
1568 C CB  . LYS A 193 ? 0.2001 0.1960 0.1939 -0.0109 -0.0137 -0.0141 192 LYS A CB  
1569 C CG  . LYS A 193 ? 0.2239 0.2253 0.2211 -0.0124 -0.0146 -0.0161 192 LYS A CG  
1570 C CD  . LYS A 193 ? 0.2689 0.2738 0.2666 -0.0087 -0.0156 -0.0173 192 LYS A CD  
1571 C CE  . LYS A 193 ? 0.3473 0.3587 0.3491 -0.0098 -0.0161 -0.0189 192 LYS A CE  
1572 N NZ  . LYS A 193 ? 0.4269 0.4384 0.4301 -0.0129 -0.0178 -0.0206 192 LYS A NZ  
1573 N N   . ILE A 194 ? 0.1913 0.1765 0.1804 -0.0142 -0.0110 -0.0094 193 ILE A N   
1574 C CA  . ILE A 194 ? 0.1881 0.1705 0.1756 -0.0128 -0.0099 -0.0077 193 ILE A CA  
1575 C C   . ILE A 194 ? 0.1911 0.1775 0.1802 -0.0133 -0.0082 -0.0075 193 ILE A C   
1576 O O   . ILE A 194 ? 0.1996 0.1888 0.1897 -0.0163 -0.0076 -0.0077 193 ILE A O   
1577 C CB  . ILE A 194 ? 0.1670 0.1438 0.1522 -0.0148 -0.0103 -0.0063 193 ILE A CB  
1578 C CG1 . ILE A 194 ? 0.1743 0.1467 0.1580 -0.0138 -0.0121 -0.0068 193 ILE A CG1 
1579 C CG2 . ILE A 194 ? 0.1853 0.1599 0.1692 -0.0137 -0.0093 -0.0047 193 ILE A CG2 
1580 C CD1 . ILE A 194 ? 0.1920 0.1590 0.1742 -0.0163 -0.0128 -0.0057 193 ILE A CD1 
1581 N N   . ILE A 195 ? 0.1789 0.1659 0.1683 -0.0105 -0.0075 -0.0071 194 ILE A N   
1582 C CA  . ILE A 195 ? 0.2092 0.1989 0.1998 -0.0105 -0.0060 -0.0070 194 ILE A CA  
1583 C C   . ILE A 195 ? 0.2088 0.1942 0.1976 -0.0094 -0.0058 -0.0056 194 ILE A C   
1584 O O   . ILE A 195 ? 0.1982 0.1808 0.1866 -0.0069 -0.0062 -0.0050 194 ILE A O   
1585 C CB  . ILE A 195 ? 0.1818 0.1762 0.1754 -0.0080 -0.0055 -0.0081 194 ILE A CB  
1586 C CG1 . ILE A 195 ? 0.2331 0.2317 0.2285 -0.0085 -0.0062 -0.0096 194 ILE A CG1 
1587 C CG2 . ILE A 195 ? 0.1879 0.1853 0.1829 -0.0081 -0.0041 -0.0085 194 ILE A CG2 
1588 C CD1 . ILE A 195 ? 0.1937 0.1955 0.1902 -0.0121 -0.0057 -0.0103 194 ILE A CD1 
1589 N N   . TYR A 196 ? 0.1580 0.1432 0.1459 -0.0113 -0.0050 -0.0051 195 TYR A N   
1590 C CA  . TYR A 196 ? 0.1870 0.1685 0.1735 -0.0104 -0.0050 -0.0040 195 TYR A CA  
1591 C C   . TYR A 196 ? 0.1789 0.1627 0.1677 -0.0079 -0.0042 -0.0047 195 TYR A C   
1592 O O   . TYR A 196 ? 0.1931 0.1807 0.1831 -0.0084 -0.0033 -0.0057 195 TYR A O   
1593 C CB  . TYR A 196 ? 0.1985 0.1786 0.1825 -0.0134 -0.0047 -0.0031 195 TYR A CB  
1594 C CG  . TYR A 196 ? 0.2110 0.1873 0.1930 -0.0155 -0.0058 -0.0020 195 TYR A CG  
1595 C CD1 . TYR A 196 ? 0.2027 0.1807 0.1852 -0.0178 -0.0059 -0.0024 195 TYR A CD1 
1596 C CD2 . TYR A 196 ? 0.2208 0.1915 0.2007 -0.0152 -0.0067 -0.0005 195 TYR A CD2 
1597 C CE1 . TYR A 196 ? 0.2170 0.1910 0.1981 -0.0198 -0.0071 -0.0015 195 TYR A CE1 
1598 C CE2 . TYR A 196 ? 0.2020 0.1687 0.1804 -0.0169 -0.0078 0.0004  195 TYR A CE2 
1599 C CZ  . TYR A 196 ? 0.2161 0.1843 0.1950 -0.0192 -0.0080 -0.0001 195 TYR A CZ  
1600 O OH  . TYR A 196 ? 0.2110 0.1751 0.1889 -0.0210 -0.0093 0.0006  195 TYR A OH  
1601 N N   . GLU A 197 ? 0.1843 0.1660 0.1741 -0.0050 -0.0046 -0.0041 196 GLU A N   
1602 C CA  . GLU A 197 ? 0.1547 0.1381 0.1473 -0.0025 -0.0040 -0.0045 196 GLU A CA  
1603 C C   . GLU A 197 ? 0.1870 0.1678 0.1793 -0.0024 -0.0041 -0.0040 196 GLU A C   
1604 O O   . GLU A 197 ? 0.2052 0.1817 0.1962 -0.0020 -0.0047 -0.0027 196 GLU A O   
1605 C CB  . GLU A 197 ? 0.1637 0.1464 0.1580 0.0005  -0.0043 -0.0038 196 GLU A CB  
1606 C CG  . GLU A 197 ? 0.1955 0.1791 0.1932 0.0030  -0.0038 -0.0038 196 GLU A CG  
1607 C CD  . GLU A 197 ? 0.1924 0.1754 0.1917 0.0060  -0.0039 -0.0026 196 GLU A CD  
1608 O OE1 . GLU A 197 ? 0.2111 0.1932 0.2085 0.0062  -0.0043 -0.0020 196 GLU A OE1 
1609 O OE2 . GLU A 197 ? 0.2201 0.2033 0.2226 0.0080  -0.0035 -0.0021 196 GLU A OE2 
1610 N N   . MET A 198 ? 0.1815 0.1650 0.1749 -0.0027 -0.0035 -0.0053 197 MET A N   
1611 C CA  . MET A 198 ? 0.1578 0.1394 0.1512 -0.0023 -0.0037 -0.0053 197 MET A CA  
1612 C C   . MET A 198 ? 0.1997 0.1831 0.1973 0.0002  -0.0034 -0.0064 197 MET A C   
1613 O O   . MET A 198 ? 0.1945 0.1815 0.1946 0.0012  -0.0029 -0.0075 197 MET A O   
1614 C CB  . MET A 198 ? 0.1797 0.1630 0.1704 -0.0049 -0.0033 -0.0061 197 MET A CB  
1615 C CG  . MET A 198 ? 0.1734 0.1551 0.1605 -0.0077 -0.0035 -0.0048 197 MET A CG  
1616 S SD  . MET A 198 ? 0.2164 0.1997 0.2000 -0.0106 -0.0030 -0.0049 197 MET A SD  
1617 C CE  . MET A 198 ? 0.2219 0.2038 0.2028 -0.0137 -0.0031 -0.0033 197 MET A CE  
1618 N N   . HIS A 199 ? 0.1700 0.1509 0.1688 0.0013  -0.0039 -0.0062 198 HIS A N   
1619 C CA  . HIS A 199 ? 0.1714 0.1534 0.1746 0.0035  -0.0039 -0.0073 198 HIS A CA  
1620 C C   . HIS A 199 ? 0.1653 0.1482 0.1683 0.0029  -0.0042 -0.0092 198 HIS A C   
1621 O O   . HIS A 199 ? 0.2025 0.1835 0.2020 0.0013  -0.0047 -0.0088 198 HIS A O   
1622 C CB  . HIS A 199 ? 0.1889 0.1674 0.1948 0.0056  -0.0044 -0.0056 198 HIS A CB  
1623 C CG  . HIS A 199 ? 0.1840 0.1619 0.1900 0.0067  -0.0041 -0.0037 198 HIS A CG  
1624 N ND1 . HIS A 199 ? 0.1979 0.1731 0.2059 0.0085  -0.0042 -0.0018 198 HIS A ND1 
1625 C CD2 . HIS A 199 ? 0.1614 0.1414 0.1659 0.0063  -0.0037 -0.0037 198 HIS A CD2 
1626 C CE1 . HIS A 199 ? 0.1850 0.1607 0.1922 0.0094  -0.0038 -0.0006 198 HIS A CE1 
1627 N NE2 . HIS A 199 ? 0.1992 0.1777 0.2043 0.0080  -0.0037 -0.0018 198 HIS A NE2 
1628 N N   . GLN A 200 ? 0.1832 0.1688 0.1897 0.0043  -0.0039 -0.0112 199 GLN A N   
1629 C CA  . GLN A 200 ? 0.1571 0.1437 0.1634 0.0041  -0.0043 -0.0135 199 GLN A CA  
1630 C C   . GLN A 200 ? 0.1785 0.1656 0.1904 0.0065  -0.0047 -0.0152 199 GLN A C   
1631 O O   . GLN A 200 ? 0.1964 0.1867 0.2113 0.0077  -0.0041 -0.0165 199 GLN A O   
1632 C CB  . GLN A 200 ? 0.1852 0.1761 0.1883 0.0022  -0.0034 -0.0152 199 GLN A CB  
1633 C CG  . GLN A 200 ? 0.1798 0.1711 0.1807 0.0017  -0.0039 -0.0171 199 GLN A CG  
1634 C CD  . GLN A 200 ? 0.1931 0.1799 0.1908 0.0006  -0.0051 -0.0152 199 GLN A CD  
1635 O OE1 . GLN A 200 ? 0.2248 0.2106 0.2182 -0.0015 -0.0048 -0.0133 199 GLN A OE1 
1636 N NE2 . GLN A 200 ? 0.2068 0.1907 0.2068 0.0021  -0.0064 -0.0157 199 GLN A NE2 
1637 N N   . PHE A 201 ? 0.2120 0.1960 0.2256 0.0073  -0.0059 -0.0153 200 PHE A N   
1638 C CA  . PHE A 201 ? 0.2515 0.2357 0.2706 0.0093  -0.0066 -0.0173 200 PHE A CA  
1639 C C   . PHE A 201 ? 0.2422 0.2277 0.2595 0.0088  -0.0073 -0.0204 200 PHE A C   
1640 O O   . PHE A 201 ? 0.2188 0.2046 0.2306 0.0069  -0.0073 -0.0203 200 PHE A O   
1641 C CB  . PHE A 201 ? 0.2080 0.1880 0.2313 0.0108  -0.0074 -0.0152 200 PHE A CB  
1642 C CG  . PHE A 201 ? 0.2284 0.2079 0.2537 0.0118  -0.0065 -0.0124 200 PHE A CG  
1643 C CD1 . PHE A 201 ? 0.2153 0.1965 0.2454 0.0138  -0.0061 -0.0128 200 PHE A CD1 
1644 C CD2 . PHE A 201 ? 0.2390 0.2165 0.2610 0.0110  -0.0062 -0.0096 200 PHE A CD2 
1645 C CE1 . PHE A 201 ? 0.2394 0.2204 0.2709 0.0149  -0.0054 -0.0101 200 PHE A CE1 
1646 C CE2 . PHE A 201 ? 0.2439 0.2213 0.2672 0.0122  -0.0054 -0.0072 200 PHE A CE2 
1647 C CZ  . PHE A 201 ? 0.2323 0.2116 0.2602 0.0141  -0.0050 -0.0074 200 PHE A CZ  
1648 N N   . LEU A 202 ? 0.1913 0.1777 0.2134 0.0106  -0.0079 -0.0230 201 LEU A N   
1649 C CA  . LEU A 202 ? 0.1668 0.1560 0.1878 0.0106  -0.0083 -0.0269 201 LEU A CA  
1650 C C   . LEU A 202 ? 0.2169 0.2037 0.2410 0.0117  -0.0103 -0.0288 201 LEU A C   
1651 O O   . LEU A 202 ? 0.2348 0.2237 0.2579 0.0119  -0.0109 -0.0324 201 LEU A O   
1652 C CB  . LEU A 202 ? 0.1867 0.1802 0.2109 0.0120  -0.0073 -0.0295 201 LEU A CB  
1653 C CG  . LEU A 202 ? 0.2428 0.2393 0.2651 0.0111  -0.0055 -0.0279 201 LEU A CG  
1654 C CD1 . LEU A 202 ? 0.2536 0.2544 0.2799 0.0128  -0.0048 -0.0305 201 LEU A CD1 
1655 C CD2 . LEU A 202 ? 0.2342 0.2326 0.2492 0.0084  -0.0046 -0.0274 201 LEU A CD2 
1656 N N   . ASP A 203 ? 0.2384 0.2208 0.2662 0.0123  -0.0113 -0.0266 202 ASP A N   
1657 C CA  . ASP A 203 ? 0.2133 0.1933 0.2442 0.0131  -0.0134 -0.0282 202 ASP A CA  
1658 C C   . ASP A 203 ? 0.1937 0.1723 0.2188 0.0113  -0.0143 -0.0275 202 ASP A C   
1659 O O   . ASP A 203 ? 0.2552 0.2341 0.2743 0.0096  -0.0133 -0.0254 202 ASP A O   
1660 C CB  . ASP A 203 ? 0.2338 0.2101 0.2721 0.0145  -0.0140 -0.0261 202 ASP A CB  
1661 C CG  . ASP A 203 ? 0.2428 0.2169 0.2802 0.0139  -0.0130 -0.0214 202 ASP A CG  
1662 O OD1 . ASP A 203 ? 0.2407 0.2158 0.2722 0.0125  -0.0118 -0.0198 202 ASP A OD1 
1663 O OD2 . ASP A 203 ? 0.2677 0.2391 0.3107 0.0150  -0.0133 -0.0194 202 ASP A OD2 
1664 N N   . SER A 204 ? 0.2661 0.2431 0.2931 0.0118  -0.0165 -0.0295 203 SER A N   
1665 C CA  . SER A 204 ? 0.2753 0.2518 0.2962 0.0105  -0.0177 -0.0298 203 SER A CA  
1666 C C   . SER A 204 ? 0.2555 0.2293 0.2729 0.0090  -0.0173 -0.0255 203 SER A C   
1667 O O   . SER A 204 ? 0.2964 0.2711 0.3068 0.0073  -0.0169 -0.0247 203 SER A O   
1668 C CB  . SER A 204 ? 0.4122 0.3870 0.4368 0.0115  -0.0204 -0.0325 203 SER A CB  
1669 O OG  . SER A 204 ? 0.5589 0.5305 0.5915 0.0127  -0.0211 -0.0312 203 SER A OG  
1670 N N   . ASP A 205 ? 0.2780 0.2487 0.3000 0.0095  -0.0173 -0.0227 204 ASP A N   
1671 C CA  . ASP A 205 ? 0.2593 0.2274 0.2779 0.0083  -0.0170 -0.0189 204 ASP A CA  
1672 C C   . ASP A 205 ? 0.2666 0.2354 0.2834 0.0078  -0.0147 -0.0164 204 ASP A C   
1673 O O   . ASP A 205 ? 0.2531 0.2196 0.2676 0.0070  -0.0144 -0.0134 204 ASP A O   
1674 C CB  . ASP A 205 ? 0.2923 0.2567 0.3164 0.0092  -0.0182 -0.0172 204 ASP A CB  
1675 C CG  . ASP A 205 ? 0.3311 0.2948 0.3624 0.0108  -0.0173 -0.0161 204 ASP A CG  
1676 O OD1 . ASP A 205 ? 0.3044 0.2703 0.3365 0.0113  -0.0158 -0.0163 204 ASP A OD1 
1677 O OD2 . ASP A 205 ? 0.3602 0.3214 0.3969 0.0115  -0.0181 -0.0147 204 ASP A OD2 
1678 N N   . GLY A 206 ? 0.2463 0.2182 0.2638 0.0082  -0.0133 -0.0176 205 GLY A N   
1679 C CA  . GLY A 206 ? 0.2344 0.2074 0.2500 0.0077  -0.0114 -0.0156 205 GLY A CA  
1680 C C   . GLY A 206 ? 0.2327 0.2034 0.2524 0.0089  -0.0108 -0.0127 205 GLY A C   
1681 O O   . GLY A 206 ? 0.2275 0.1987 0.2451 0.0085  -0.0096 -0.0108 205 GLY A O   
1682 N N   . SER A 207 ? 0.2440 0.2126 0.2695 0.0103  -0.0117 -0.0123 206 SER A N   
1683 C CA  . SER A 207 ? 0.2621 0.2288 0.2917 0.0116  -0.0110 -0.0093 206 SER A CA  
1684 C C   . SER A 207 ? 0.2727 0.2413 0.3061 0.0130  -0.0099 -0.0092 206 SER A C   
1685 O O   . SER A 207 ? 0.2783 0.2461 0.3137 0.0140  -0.0089 -0.0064 206 SER A O   
1686 C CB  . SER A 207 ? 0.2716 0.2354 0.3065 0.0124  -0.0123 -0.0087 206 SER A CB  
1687 O OG  . SER A 207 ? 0.3170 0.2815 0.3573 0.0134  -0.0133 -0.0114 206 SER A OG  
1688 N N   . GLY A 208 ? 0.2358 0.2071 0.2702 0.0134  -0.0099 -0.0122 207 GLY A N   
1689 C CA  . GLY A 208 ? 0.2447 0.2177 0.2832 0.0150  -0.0090 -0.0120 207 GLY A CA  
1690 C C   . GLY A 208 ? 0.2960 0.2668 0.3421 0.0169  -0.0094 -0.0106 207 GLY A C   
1691 O O   . GLY A 208 ? 0.3221 0.2931 0.3709 0.0182  -0.0084 -0.0083 207 GLY A O   
1692 N N   . THR A 209 ? 0.2451 0.2139 0.2948 0.0170  -0.0109 -0.0119 208 THR A N   
1693 C CA  . THR A 209 ? 0.2560 0.2226 0.3139 0.0185  -0.0114 -0.0106 208 THR A CA  
1694 C C   . THR A 209 ? 0.2851 0.2521 0.3485 0.0195  -0.0128 -0.0142 208 THR A C   
1695 O O   . THR A 209 ? 0.3533 0.3188 0.4242 0.0209  -0.0131 -0.0132 208 THR A O   
1696 C CB  . THR A 209 ? 0.2884 0.2520 0.3478 0.0180  -0.0121 -0.0085 208 THR A CB  
1697 O OG1 . THR A 209 ? 0.3395 0.3026 0.3959 0.0168  -0.0137 -0.0113 208 THR A OG1 
1698 C CG2 . THR A 209 ? 0.3419 0.3048 0.3971 0.0176  -0.0106 -0.0047 208 THR A CG2 
1699 N N   . SER A 210 ? 0.2500 0.2191 0.3100 0.0189  -0.0136 -0.0183 209 SER A N   
1700 C CA  . SER A 210 ? 0.2386 0.2085 0.3032 0.0199  -0.0150 -0.0224 209 SER A CA  
1701 C C   . SER A 210 ? 0.2488 0.2224 0.3120 0.0207  -0.0140 -0.0247 209 SER A C   
1702 O O   . SER A 210 ? 0.2742 0.2505 0.3308 0.0196  -0.0127 -0.0246 209 SER A O   
1703 C CB  . SER A 210 ? 0.2726 0.2424 0.3342 0.0189  -0.0168 -0.0259 209 SER A CB  
1704 O OG  . SER A 210 ? 0.2995 0.2706 0.3645 0.0201  -0.0181 -0.0305 209 SER A OG  
1705 N N   . ALA A 211 ? 0.2516 0.2253 0.3216 0.0225  -0.0147 -0.0267 210 ALA A N   
1706 C CA  . ALA A 211 ? 0.2609 0.2383 0.3305 0.0235  -0.0140 -0.0294 210 ALA A CA  
1707 C C   . ALA A 211 ? 0.2355 0.2159 0.3008 0.0229  -0.0145 -0.0344 210 ALA A C   
1708 O O   . ALA A 211 ? 0.2915 0.2758 0.3557 0.0235  -0.0137 -0.0368 210 ALA A O   
1709 C CB  . ALA A 211 ? 0.2728 0.2492 0.3514 0.0258  -0.0146 -0.0300 210 ALA A CB  
1710 N N   . THR A 212 ? 0.2503 0.2295 0.3134 0.0219  -0.0159 -0.0359 211 THR A N   
1711 C CA  . THR A 212 ? 0.2562 0.2384 0.3148 0.0215  -0.0165 -0.0405 211 THR A CA  
1712 C C   . THR A 212 ? 0.2925 0.2772 0.3416 0.0193  -0.0150 -0.0393 211 THR A C   
1713 O O   . THR A 212 ? 0.3138 0.2963 0.3596 0.0178  -0.0148 -0.0357 211 THR A O   
1714 C CB  . THR A 212 ? 0.3006 0.2802 0.3610 0.0215  -0.0190 -0.0429 211 THR A CB  
1715 O OG1 . THR A 212 ? 0.3448 0.3221 0.4147 0.0233  -0.0206 -0.0443 211 THR A OG1 
1716 C CG2 . THR A 212 ? 0.3618 0.3449 0.4167 0.0212  -0.0197 -0.0476 211 THR A CG2 
1717 N N   . CYS A 213 ? 0.2750 0.2644 0.3202 0.0192  -0.0140 -0.0422 212 CYS A N   
1718 C CA  . CYS A 213 ? 0.2202 0.2121 0.2568 0.0170  -0.0126 -0.0412 212 CYS A CA  
1719 C C   . CYS A 213 ? 0.2533 0.2464 0.2851 0.0164  -0.0138 -0.0443 212 CYS A C   
1720 O O   . CYS A 213 ? 0.2740 0.2679 0.3087 0.0179  -0.0151 -0.0486 212 CYS A O   
1721 C CB  . CYS A 213 ? 0.2511 0.2479 0.2861 0.0170  -0.0105 -0.0418 212 CYS A CB  
1722 S SG  . CYS A 213 ? 0.2650 0.2607 0.3044 0.0178  -0.0093 -0.0377 212 CYS A SG  
1723 N N   . VAL A 214 ? 0.2415 0.2346 0.2661 0.0142  -0.0133 -0.0422 213 VAL A N   
1724 C CA  . VAL A 214 ? 0.2236 0.2176 0.2429 0.0135  -0.0145 -0.0445 213 VAL A CA  
1725 C C   . VAL A 214 ? 0.2758 0.2753 0.2930 0.0143  -0.0138 -0.0491 213 VAL A C   
1726 O O   . VAL A 214 ? 0.2590 0.2592 0.2760 0.0154  -0.0154 -0.0531 213 VAL A O   
1727 C CB  . VAL A 214 ? 0.2468 0.2400 0.2585 0.0110  -0.0139 -0.0408 213 VAL A CB  
1728 C CG1 . VAL A 214 ? 0.2951 0.2897 0.3006 0.0104  -0.0151 -0.0431 213 VAL A CG1 
1729 C CG2 . VAL A 214 ? 0.2579 0.2459 0.2716 0.0104  -0.0147 -0.0367 213 VAL A CG2 
1730 N N   . SER A 215 ? 0.2251 0.2286 0.2404 0.0138  -0.0113 -0.0487 214 SER A N   
1731 C CA  . SER A 215 ? 0.2444 0.2539 0.2575 0.0144  -0.0101 -0.0528 214 SER A CA  
1732 C C   . SER A 215 ? 0.2263 0.2394 0.2410 0.0143  -0.0077 -0.0520 214 SER A C   
1733 O O   . SER A 215 ? 0.2350 0.2460 0.2512 0.0136  -0.0070 -0.0481 214 SER A O   
1734 C CB  . SER A 215 ? 0.2695 0.2816 0.2735 0.0125  -0.0096 -0.0528 214 SER A CB  
1735 O OG  . SER A 215 ? 0.2443 0.2572 0.2440 0.0100  -0.0075 -0.0485 214 SER A OG  
1736 N N   . SER A 216 ? 0.2551 0.2739 0.2693 0.0153  -0.0064 -0.0558 215 SER A N   
1737 C CA  . SER A 216 ? 0.2416 0.2644 0.2577 0.0153  -0.0042 -0.0554 215 SER A CA  
1738 C C   . SER A 216 ? 0.2458 0.2706 0.2560 0.0123  -0.0020 -0.0516 215 SER A C   
1739 O O   . SER A 216 ? 0.2338 0.2617 0.2457 0.0120  -0.0003 -0.0506 215 SER A O   
1740 C CB  . SER A 216 ? 0.2647 0.2935 0.2822 0.0172  -0.0033 -0.0607 215 SER A CB  
1741 O OG  . SER A 216 ? 0.2937 0.3267 0.3039 0.0159  -0.0022 -0.0622 215 SER A OG  
1742 N N   . THR A 217 ? 0.2232 0.2465 0.2267 0.0101  -0.0022 -0.0494 216 THR A N   
1743 C CA  . THR A 217 ? 0.2268 0.2516 0.2249 0.0071  -0.0004 -0.0457 216 THR A CA  
1744 C C   . THR A 217 ? 0.2189 0.2377 0.2154 0.0054  -0.0014 -0.0410 216 THR A C   
1745 O O   . THR A 217 ? 0.2033 0.2225 0.1952 0.0028  -0.0003 -0.0379 216 THR A O   
1746 C CB  . THR A 217 ? 0.2069 0.2361 0.1979 0.0057  0.0008  -0.0468 216 THR A CB  
1747 O OG1 . THR A 217 ? 0.2250 0.2511 0.2124 0.0058  -0.0012 -0.0474 216 THR A OG1 
1748 C CG2 . THR A 217 ? 0.2510 0.2872 0.2432 0.0073  0.0024  -0.0515 216 THR A CG2 
1749 N N   . ILE A 218 ? 0.1968 0.2102 0.1973 0.0068  -0.0035 -0.0404 217 ILE A N   
1750 C CA  . ILE A 218 ? 0.2120 0.2200 0.2102 0.0053  -0.0046 -0.0364 217 ILE A CA  
1751 C C   . ILE A 218 ? 0.2257 0.2326 0.2239 0.0038  -0.0034 -0.0326 217 ILE A C   
1752 O O   . ILE A 218 ? 0.2053 0.2094 0.1995 0.0019  -0.0036 -0.0293 217 ILE A O   
1753 C CB  . ILE A 218 ? 0.2036 0.2065 0.2065 0.0072  -0.0070 -0.0368 217 ILE A CB  
1754 C CG1 . ILE A 218 ? 0.2139 0.2118 0.2139 0.0058  -0.0083 -0.0334 217 ILE A CG1 
1755 C CG2 . ILE A 218 ? 0.2299 0.2315 0.2402 0.0090  -0.0070 -0.0365 217 ILE A CG2 
1756 C CD1 . ILE A 218 ? 0.2765 0.2750 0.2695 0.0043  -0.0088 -0.0336 217 ILE A CD1 
1757 N N   . GLY A 219 ? 0.1983 0.2074 0.2007 0.0048  -0.0024 -0.0330 218 GLY A N   
1758 C CA  . GLY A 219 ? 0.2000 0.2084 0.2025 0.0036  -0.0015 -0.0296 218 GLY A CA  
1759 C C   . GLY A 219 ? 0.1959 0.2076 0.1931 0.0007  0.0002  -0.0284 218 GLY A C   
1760 O O   . GLY A 219 ? 0.2073 0.2164 0.2015 -0.0013 0.0002  -0.0252 218 GLY A O   
1761 N N   . GLN A 220 ? 0.2200 0.2375 0.2164 0.0006  0.0016  -0.0310 219 GLN A N   
1762 C CA  . GLN A 220 ? 0.2482 0.2693 0.2400 -0.0023 0.0034  -0.0297 219 GLN A CA  
1763 C C   . GLN A 220 ? 0.2306 0.2490 0.2160 -0.0044 0.0029  -0.0277 219 GLN A C   
1764 O O   . GLN A 220 ? 0.2610 0.2787 0.2431 -0.0070 0.0036  -0.0246 219 GLN A O   
1765 C CB  . GLN A 220 ? 0.2291 0.2575 0.2214 -0.0018 0.0053  -0.0331 219 GLN A CB  
1766 C CG  . GLN A 220 ? 0.2645 0.2948 0.2553 -0.0003 0.0050  -0.0366 219 GLN A CG  
1767 C CD  . GLN A 220 ? 0.2536 0.2897 0.2486 0.0020  0.0060  -0.0410 219 GLN A CD  
1768 O OE1 . GLN A 220 ? 0.2430 0.2776 0.2437 0.0047  0.0048  -0.0431 219 GLN A OE1 
1769 N NE2 . GLN A 220 ? 0.2291 0.2719 0.2216 0.0009  0.0083  -0.0424 219 GLN A NE2 
1770 N N   . GLU A 221 ? 0.2287 0.2451 0.2128 -0.0031 0.0014  -0.0292 220 GLU A N   
1771 C CA  . GLU A 221 ? 0.2258 0.2391 0.2041 -0.0048 0.0005  -0.0270 220 GLU A CA  
1772 C C   . GLU A 221 ? 0.2496 0.2568 0.2278 -0.0059 -0.0006 -0.0231 220 GLU A C   
1773 O O   . GLU A 221 ? 0.2381 0.2436 0.2116 -0.0082 -0.0006 -0.0202 220 GLU A O   
1774 C CB  . GLU A 221 ? 0.2319 0.2438 0.2095 -0.0030 -0.0013 -0.0296 220 GLU A CB  
1775 C CG  . GLU A 221 ? 0.2307 0.2485 0.2066 -0.0021 -0.0004 -0.0335 220 GLU A CG  
1776 C CD  . GLU A 221 ? 0.2554 0.2715 0.2306 -0.0003 -0.0026 -0.0362 220 GLU A CD  
1777 O OE1 . GLU A 221 ? 0.3133 0.3269 0.2834 -0.0014 -0.0038 -0.0344 220 GLU A OE1 
1778 O OE2 . GLU A 221 ? 0.2378 0.2548 0.2180 0.0023  -0.0034 -0.0400 220 GLU A OE2 
1779 N N   . ARG A 222 ? 0.2037 0.2075 0.1870 -0.0040 -0.0017 -0.0230 221 ARG A N   
1780 C CA  . ARG A 222 ? 0.2170 0.2150 0.2003 -0.0045 -0.0029 -0.0197 221 ARG A CA  
1781 C C   . ARG A 222 ? 0.2342 0.2320 0.2168 -0.0064 -0.0019 -0.0170 221 ARG A C   
1782 O O   . ARG A 222 ? 0.2309 0.2241 0.2126 -0.0070 -0.0028 -0.0144 221 ARG A O   
1783 C CB  . ARG A 222 ? 0.1868 0.1816 0.1758 -0.0019 -0.0043 -0.0203 221 ARG A CB  
1784 C CG  . ARG A 222 ? 0.1824 0.1748 0.1716 -0.0006 -0.0062 -0.0218 221 ARG A CG  
1785 C CD  . ARG A 222 ? 0.2036 0.1931 0.1992 0.0018  -0.0074 -0.0224 221 ARG A CD  
1786 N NE  . ARG A 222 ? 0.1877 0.1749 0.1837 0.0027  -0.0094 -0.0236 221 ARG A NE  
1787 C CZ  . ARG A 222 ? 0.2462 0.2308 0.2478 0.0047  -0.0108 -0.0243 221 ARG A CZ  
1788 N NH1 . ARG A 222 ? 0.2245 0.2084 0.2316 0.0060  -0.0103 -0.0236 221 ARG A NH1 
1789 N NH2 . ARG A 222 ? 0.2543 0.2371 0.2562 0.0052  -0.0128 -0.0257 221 ARG A NH2 
1790 N N   . ILE A 223 ? 0.2029 0.2055 0.1859 -0.0073 -0.0001 -0.0178 222 ILE A N   
1791 C CA  . ILE A 223 ? 0.1901 0.1926 0.1728 -0.0091 0.0007  -0.0155 222 ILE A CA  
1792 C C   . ILE A 223 ? 0.2135 0.2190 0.1919 -0.0123 0.0021  -0.0144 222 ILE A C   
1793 O O   . ILE A 223 ? 0.2328 0.2386 0.2112 -0.0141 0.0027  -0.0127 222 ILE A O   
1794 C CB  . ILE A 223 ? 0.1874 0.1928 0.1752 -0.0077 0.0014  -0.0167 222 ILE A CB  
1795 C CG1 . ILE A 223 ? 0.1924 0.2045 0.1817 -0.0074 0.0030  -0.0196 222 ILE A CG1 
1796 C CG2 . ILE A 223 ? 0.2091 0.2111 0.2011 -0.0048 0.0001  -0.0170 222 ILE A CG2 
1797 C CD1 . ILE A 223 ? 0.2555 0.2708 0.2495 -0.0063 0.0036  -0.0205 222 ILE A CD1 
1798 N N   . THR A 224 ? 0.2044 0.2121 0.1790 -0.0130 0.0025  -0.0151 223 THR A N   
1799 C CA  A THR A 224 ? 0.2214 0.2324 0.1922 -0.0160 0.0042  -0.0137 223 THR A CA  
1800 C CA  B THR A 224 ? 0.2230 0.2341 0.1938 -0.0160 0.0042  -0.0137 223 THR A CA  
1801 C C   . THR A 224 ? 0.2105 0.2167 0.1780 -0.0185 0.0035  -0.0098 223 THR A C   
1802 O O   . THR A 224 ? 0.2298 0.2373 0.1970 -0.0210 0.0045  -0.0081 223 THR A O   
1803 C CB  A THR A 224 ? 0.2894 0.3046 0.2565 -0.0161 0.0051  -0.0154 223 THR A CB  
1804 C CB  B THR A 224 ? 0.2873 0.3021 0.2543 -0.0160 0.0050  -0.0154 223 THR A CB  
1805 O OG1 A THR A 224 ? 0.3137 0.3246 0.2772 -0.0156 0.0033  -0.0146 223 THR A OG1 
1806 O OG1 B THR A 224 ? 0.2473 0.2652 0.2102 -0.0191 0.0067  -0.0133 223 THR A OG1 
1807 C CG2 A THR A 224 ? 0.2176 0.2374 0.1883 -0.0134 0.0058  -0.0196 223 THR A CG2 
1808 C CG2 B THR A 224 ? 0.2984 0.3089 0.2626 -0.0148 0.0029  -0.0152 223 THR A CG2 
1809 N N   . SER A 225 ? 0.2218 0.2224 0.1872 -0.0179 0.0015  -0.0085 224 SER A N   
1810 C CA  . SER A 225 ? 0.2356 0.2317 0.1979 -0.0203 0.0008  -0.0049 224 SER A CA  
1811 C C   . SER A 225 ? 0.2471 0.2402 0.2127 -0.0205 0.0003  -0.0037 224 SER A C   
1812 O O   . SER A 225 ? 0.2421 0.2335 0.2063 -0.0230 0.0004  -0.0013 224 SER A O   
1813 C CB  . SER A 225 ? 0.3134 0.3044 0.2727 -0.0196 -0.0013 -0.0037 224 SER A CB  
1814 O OG  . SER A 225 ? 0.3095 0.2972 0.2722 -0.0169 -0.0029 -0.0049 224 SER A OG  
1815 N N   . ALA A 226 ? 0.2393 0.2319 0.2092 -0.0180 -0.0002 -0.0055 225 ALA A N   
1816 C CA  . ALA A 226 ? 0.2060 0.1967 0.1788 -0.0180 -0.0005 -0.0047 225 ALA A CA  
1817 C C   . ALA A 226 ? 0.2147 0.2102 0.1887 -0.0199 0.0011  -0.0049 225 ALA A C   
1818 O O   . ALA A 226 ? 0.2159 0.2097 0.1902 -0.0215 0.0009  -0.0034 225 ALA A O   
1819 C CB  . ALA A 226 ? 0.2355 0.2253 0.2126 -0.0147 -0.0012 -0.0062 225 ALA A CB  
1820 N N   . THR A 227 ? 0.2093 0.2109 0.1843 -0.0197 0.0027  -0.0070 226 THR A N   
1821 C CA  . THR A 227 ? 0.2066 0.2133 0.1831 -0.0216 0.0044  -0.0073 226 THR A CA  
1822 C C   . THR A 227 ? 0.2147 0.2208 0.1878 -0.0254 0.0049  -0.0046 226 THR A C   
1823 O O   . THR A 227 ? 0.2194 0.2260 0.1941 -0.0274 0.0052  -0.0036 226 THR A O   
1824 C CB  . THR A 227 ? 0.1990 0.2125 0.1768 -0.0207 0.0061  -0.0101 226 THR A CB  
1825 O OG1 . THR A 227 ? 0.2079 0.2215 0.1894 -0.0172 0.0054  -0.0125 226 THR A OG1 
1826 C CG2 . THR A 227 ? 0.2094 0.2289 0.1894 -0.0227 0.0079  -0.0104 226 THR A CG2 
1827 N N   . GLN A 228 ? 0.2286 0.2336 0.1972 -0.0264 0.0050  -0.0032 227 GLN A N   
1828 C CA  A GLN A 228 ? 0.2594 0.2635 0.2247 -0.0300 0.0055  -0.0001 227 GLN A CA  
1829 C CA  B GLN A 228 ? 0.2588 0.2632 0.2244 -0.0301 0.0056  -0.0002 227 GLN A CA  
1830 C C   . GLN A 228 ? 0.2405 0.2380 0.2059 -0.0310 0.0037  0.0023  227 GLN A C   
1831 O O   . GLN A 228 ? 0.2573 0.2543 0.2226 -0.0340 0.0040  0.0043  227 GLN A O   
1832 C CB  A GLN A 228 ? 0.2748 0.2785 0.2348 -0.0304 0.0056  0.0010  227 GLN A CB  
1833 C CB  B GLN A 228 ? 0.3011 0.3062 0.2615 -0.0308 0.0061  0.0009  227 GLN A CB  
1834 C CG  A GLN A 228 ? 0.3284 0.3372 0.2879 -0.0283 0.0066  -0.0020 227 GLN A CG  
1835 C CG  B GLN A 228 ? 0.3617 0.3680 0.3190 -0.0347 0.0074  0.0042  227 GLN A CG  
1836 C CD  A GLN A 228 ? 0.3834 0.3999 0.3452 -0.0290 0.0092  -0.0038 227 GLN A CD  
1837 C CD  B GLN A 228 ? 0.4490 0.4598 0.4097 -0.0372 0.0092  0.0044  227 GLN A CD  
1838 O OE1 A GLN A 228 ? 0.3854 0.4049 0.3466 -0.0320 0.0108  -0.0019 227 GLN A OE1 
1839 O OE1 B GLN A 228 ? 0.2674 0.2751 0.2292 -0.0396 0.0086  0.0067  227 GLN A OE1 
1840 N NE2 A GLN A 228 ? 0.3750 0.3951 0.3400 -0.0262 0.0095  -0.0074 227 GLN A NE2 
1841 N NE2 B GLN A 228 ? 0.4045 0.4227 0.3674 -0.0366 0.0113  0.0019  227 GLN A NE2 
1842 N N   . TRP A 229 ? 0.2221 0.2145 0.1879 -0.0285 0.0018  0.0019  228 TRP A N   
1843 C CA  . TRP A 229 ? 0.2363 0.2224 0.2022 -0.0290 0.0000  0.0038  228 TRP A CA  
1844 C C   . TRP A 229 ? 0.2115 0.1985 0.1811 -0.0296 0.0001  0.0031  228 TRP A C   
1845 O O   . TRP A 229 ? 0.2265 0.2111 0.1961 -0.0319 -0.0004 0.0048  228 TRP A O   
1846 C CB  . TRP A 229 ? 0.2201 0.2014 0.1862 -0.0259 -0.0018 0.0032  228 TRP A CB  
1847 C CG  . TRP A 229 ? 0.2239 0.1988 0.1898 -0.0261 -0.0035 0.0050  228 TRP A CG  
1848 C CD1 . TRP A 229 ? 0.2622 0.2322 0.2250 -0.0272 -0.0047 0.0075  228 TRP A CD1 
1849 C CD2 . TRP A 229 ? 0.2109 0.1836 0.1797 -0.0250 -0.0043 0.0044  228 TRP A CD2 
1850 N NE1 . TRP A 229 ? 0.2489 0.2138 0.2128 -0.0269 -0.0062 0.0083  228 TRP A NE1 
1851 C CE2 . TRP A 229 ? 0.2381 0.2047 0.2054 -0.0255 -0.0059 0.0064  228 TRP A CE2 
1852 C CE3 . TRP A 229 ? 0.2200 0.1956 0.1924 -0.0235 -0.0039 0.0025  228 TRP A CE3 
1853 C CZ2 . TRP A 229 ? 0.2100 0.1734 0.1792 -0.0245 -0.0070 0.0061  228 TRP A CZ2 
1854 C CZ3 . TRP A 229 ? 0.2766 0.2490 0.2504 -0.0225 -0.0050 0.0024  228 TRP A CZ3 
1855 C CH2 . TRP A 229 ? 0.2460 0.2125 0.2182 -0.0231 -0.0065 0.0041  228 TRP A CH2 
1856 N N   . LEU A 230 ? 0.1944 0.1852 0.1675 -0.0274 0.0006  0.0005  229 LEU A N   
1857 C CA  . LEU A 230 ? 0.2078 0.2004 0.1844 -0.0278 0.0006  -0.0003 229 LEU A CA  
1858 C C   . LEU A 230 ? 0.2169 0.2130 0.1939 -0.0315 0.0019  0.0006  229 LEU A C   
1859 O O   . LEU A 230 ? 0.2156 0.2101 0.1939 -0.0332 0.0011  0.0013  229 LEU A O   
1860 C CB  . LEU A 230 ? 0.2205 0.2174 0.2007 -0.0249 0.0011  -0.0031 229 LEU A CB  
1861 C CG  . LEU A 230 ? 0.2121 0.2057 0.1930 -0.0213 0.0000  -0.0038 229 LEU A CG  
1862 C CD1 . LEU A 230 ? 0.1963 0.1947 0.1806 -0.0188 0.0007  -0.0063 229 LEU A CD1 
1863 C CD2 . LEU A 230 ? 0.2057 0.1950 0.1874 -0.0206 -0.0016 -0.0032 229 LEU A CD2 
1864 N N   . ARG A 231 ? 0.2222 0.2234 0.1982 -0.0327 0.0038  0.0005  230 ARG A N   
1865 C CA  . ARG A 231 ? 0.2072 0.2127 0.1841 -0.0362 0.0054  0.0015  230 ARG A CA  
1866 C C   . ARG A 231 ? 0.2238 0.2246 0.1980 -0.0395 0.0047  0.0049  230 ARG A C   
1867 O O   . ARG A 231 ? 0.2502 0.2512 0.2265 -0.0423 0.0047  0.0059  230 ARG A O   
1868 C CB  . ARG A 231 ? 0.2061 0.2184 0.1822 -0.0365 0.0078  0.0005  230 ARG A CB  
1869 C CG  . ARG A 231 ? 0.2395 0.2572 0.2170 -0.0401 0.0098  0.0015  230 ARG A CG  
1870 C CD  . ARG A 231 ? 0.2808 0.3061 0.2580 -0.0398 0.0124  0.0001  230 ARG A CD  
1871 N NE  . ARG A 231 ? 0.2598 0.2890 0.2406 -0.0365 0.0125  -0.0036 230 ARG A NE  
1872 C CZ  . ARG A 231 ? 0.2624 0.2928 0.2422 -0.0334 0.0127  -0.0058 230 ARG A CZ  
1873 N NH1 . ARG A 231 ? 0.2776 0.3063 0.2526 -0.0331 0.0128  -0.0050 230 ARG A NH1 
1874 N NH2 . ARG A 231 ? 0.2611 0.2948 0.2450 -0.0306 0.0127  -0.0089 230 ARG A NH2 
1875 N N   . ALA A 232 ? 0.2584 0.2549 0.2283 -0.0392 0.0041  0.0067  231 ALA A N   
1876 C CA  . ALA A 232 ? 0.2937 0.2855 0.2610 -0.0422 0.0034  0.0102  231 ALA A CA  
1877 C C   . ALA A 232 ? 0.2763 0.2624 0.2457 -0.0426 0.0013  0.0107  231 ALA A C   
1878 O O   . ALA A 232 ? 0.2616 0.2451 0.2311 -0.0457 0.0009  0.0131  231 ALA A O   
1879 C CB  . ALA A 232 ? 0.2505 0.2386 0.2128 -0.0413 0.0027  0.0118  231 ALA A CB  
1880 N N   . ASN A 233 ? 0.2241 0.2082 0.1953 -0.0395 -0.0001 0.0084  232 ASN A N   
1881 C CA  . ASN A 233 ? 0.1989 0.1775 0.1716 -0.0392 -0.0022 0.0085  232 ASN A CA  
1882 C C   . ASN A 233 ? 0.2307 0.2125 0.2078 -0.0392 -0.0023 0.0063  232 ASN A C   
1883 O O   . ASN A 233 ? 0.2359 0.2138 0.2143 -0.0386 -0.0041 0.0057  232 ASN A O   
1884 C CB  . ASN A 233 ? 0.2461 0.2199 0.2174 -0.0357 -0.0038 0.0079  232 ASN A CB  
1885 C CG  . ASN A 233 ? 0.2807 0.2501 0.2480 -0.0361 -0.0044 0.0103  232 ASN A CG  
1886 O OD1 . ASN A 233 ? 0.2917 0.2561 0.2579 -0.0378 -0.0056 0.0125  232 ASN A OD1 
1887 N ND2 . ASN A 233 ? 0.2713 0.2424 0.2365 -0.0344 -0.0038 0.0099  232 ASN A ND2 
1888 N N   . GLY A 234 ? 0.2233 0.2121 0.2026 -0.0399 -0.0005 0.0050  233 GLY A N   
1889 C CA  . GLY A 234 ? 0.2143 0.2066 0.1981 -0.0401 -0.0007 0.0030  233 GLY A CA  
1890 C C   . GLY A 234 ? 0.2210 0.2128 0.2062 -0.0362 -0.0019 0.0005  233 GLY A C   
1891 O O   . GLY A 234 ? 0.2563 0.2482 0.2442 -0.0360 -0.0031 -0.0008 233 GLY A O   
1892 N N   . LYS A 235 ? 0.2082 0.1997 0.1918 -0.0330 -0.0017 -0.0002 234 LYS A N   
1893 C CA  . LYS A 235 ? 0.2063 0.1966 0.1910 -0.0292 -0.0027 -0.0019 234 LYS A CA  
1894 C C   . LYS A 235 ? 0.2418 0.2382 0.2289 -0.0271 -0.0015 -0.0040 234 LYS A C   
1895 O O   . LYS A 235 ? 0.2113 0.2124 0.1987 -0.0281 0.0002  -0.0042 234 LYS A O   
1896 C CB  . LYS A 235 ? 0.2179 0.2027 0.1997 -0.0270 -0.0036 -0.0009 234 LYS A CB  
1897 C CG  . LYS A 235 ? 0.1878 0.1663 0.1671 -0.0287 -0.0048 0.0012  234 LYS A CG  
1898 C CD  . LYS A 235 ? 0.2147 0.1905 0.1953 -0.0297 -0.0064 0.0009  234 LYS A CD  
1899 C CE  . LYS A 235 ? 0.2438 0.2127 0.2220 -0.0311 -0.0077 0.0030  234 LYS A CE  
1900 N NZ  . LYS A 235 ? 0.2492 0.2151 0.2288 -0.0324 -0.0094 0.0026  234 LYS A NZ  
1901 N N   . LYS A 236 ? 0.1983 0.1948 0.1872 -0.0240 -0.0024 -0.0054 235 LYS A N   
1902 C CA  A LYS A 236 ? 0.1741 0.1754 0.1654 -0.0214 -0.0015 -0.0072 235 LYS A CA  
1903 C CA  B LYS A 236 ? 0.1747 0.1759 0.1660 -0.0213 -0.0016 -0.0072 235 LYS A CA  
1904 C C   . LYS A 236 ? 0.2102 0.2082 0.2006 -0.0180 -0.0020 -0.0071 235 LYS A C   
1905 O O   . LYS A 236 ? 0.2133 0.2061 0.2020 -0.0170 -0.0032 -0.0061 235 LYS A O   
1906 C CB  A LYS A 236 ? 0.2182 0.2230 0.2129 -0.0205 -0.0022 -0.0088 235 LYS A CB  
1907 C CB  B LYS A 236 ? 0.2173 0.2218 0.2120 -0.0204 -0.0023 -0.0088 235 LYS A CB  
1908 C CG  A LYS A 236 ? 0.3040 0.3130 0.3008 -0.0238 -0.0018 -0.0092 235 LYS A CG  
1909 C CG  B LYS A 236 ? 0.3101 0.3175 0.3065 -0.0237 -0.0023 -0.0090 235 LYS A CG  
1910 C CD  A LYS A 236 ? 0.3653 0.3817 0.3657 -0.0232 -0.0005 -0.0110 235 LYS A CD  
1911 C CD  B LYS A 236 ? 0.3435 0.3573 0.3419 -0.0255 -0.0003 -0.0096 235 LYS A CD  
1912 C CE  A LYS A 236 ? 0.4325 0.4536 0.4357 -0.0266 0.0001  -0.0114 235 LYS A CE  
1913 C CE  B LYS A 236 ? 0.4302 0.4487 0.4322 -0.0277 -0.0004 -0.0106 235 LYS A CE  
1914 N NZ  A LYS A 236 ? 0.3770 0.4053 0.3828 -0.0269 0.0022  -0.0126 235 LYS A NZ  
1915 N NZ  B LYS A 236 ? 0.4210 0.4414 0.4258 -0.0250 -0.0018 -0.0125 235 LYS A NZ  
1916 N N   . GLY A 237 ? 0.1993 0.2005 0.1911 -0.0161 -0.0010 -0.0082 236 GLY A N   
1917 C CA  . GLY A 237 ? 0.2057 0.2041 0.1975 -0.0130 -0.0014 -0.0081 236 GLY A CA  
1918 C C   . GLY A 237 ? 0.1838 0.1859 0.1792 -0.0101 -0.0011 -0.0096 236 GLY A C   
1919 O O   . GLY A 237 ? 0.1895 0.1968 0.1875 -0.0103 -0.0005 -0.0110 236 GLY A O   
1920 N N   . ILE A 238 ? 0.1620 0.1611 0.1580 -0.0072 -0.0016 -0.0092 237 ILE A N   
1921 C CA  . ILE A 238 ? 0.1739 0.1757 0.1735 -0.0043 -0.0013 -0.0103 237 ILE A CA  
1922 C C   . ILE A 238 ? 0.1776 0.1763 0.1774 -0.0026 -0.0014 -0.0099 237 ILE A C   
1923 O O   . ILE A 238 ? 0.1994 0.1933 0.1968 -0.0029 -0.0020 -0.0084 237 ILE A O   
1924 C CB  . ILE A 238 ? 0.1762 0.1783 0.1776 -0.0021 -0.0021 -0.0100 237 ILE A CB  
1925 C CG1 . ILE A 238 ? 0.1612 0.1667 0.1668 0.0008  -0.0019 -0.0110 237 ILE A CG1 
1926 C CG2 . ILE A 238 ? 0.1843 0.1810 0.1839 -0.0008 -0.0030 -0.0081 237 ILE A CG2 
1927 C CD1 . ILE A 238 ? 0.1940 0.2007 0.2010 0.0028  -0.0027 -0.0107 237 ILE A CD1 
1928 N N   . ILE A 239 ? 0.1861 0.1873 0.1889 -0.0008 -0.0010 -0.0114 238 ILE A N   
1929 C CA  . ILE A 239 ? 0.1876 0.1860 0.1918 0.0011  -0.0013 -0.0112 238 ILE A CA  
1930 C C   . ILE A 239 ? 0.1932 0.1903 0.2003 0.0040  -0.0018 -0.0101 238 ILE A C   
1931 O O   . ILE A 239 ? 0.2169 0.2173 0.2274 0.0057  -0.0016 -0.0110 238 ILE A O   
1932 C CB  . ILE A 239 ? 0.1741 0.1755 0.1803 0.0016  -0.0007 -0.0135 238 ILE A CB  
1933 C CG1 . ILE A 239 ? 0.1746 0.1773 0.1771 -0.0012 -0.0001 -0.0142 238 ILE A CG1 
1934 C CG2 . ILE A 239 ? 0.1963 0.1946 0.2050 0.0039  -0.0014 -0.0135 238 ILE A CG2 
1935 C CD1 . ILE A 239 ? 0.2166 0.2145 0.2158 -0.0021 -0.0008 -0.0129 238 ILE A CD1 
1936 N N   . GLY A 240 ? 0.1742 0.1668 0.1799 0.0046  -0.0024 -0.0080 239 GLY A N   
1937 C CA  . GLY A 240 ? 0.2089 0.2005 0.2167 0.0073  -0.0027 -0.0066 239 GLY A CA  
1938 C C   . GLY A 240 ? 0.2090 0.1995 0.2209 0.0097  -0.0027 -0.0061 239 GLY A C   
1939 O O   . GLY A 240 ? 0.1754 0.1659 0.1897 0.0121  -0.0027 -0.0049 239 GLY A O   
1940 N N   . GLU A 241 ? 0.1954 0.1847 0.2081 0.0093  -0.0027 -0.0071 240 GLU A N   
1941 C CA  . GLU A 241 ? 0.1606 0.1488 0.1777 0.0113  -0.0029 -0.0072 240 GLU A CA  
1942 C C   . GLU A 241 ? 0.1590 0.1487 0.1767 0.0104  -0.0030 -0.0099 240 GLU A C   
1943 O O   . GLU A 241 ? 0.1835 0.1723 0.1975 0.0083  -0.0031 -0.0104 240 GLU A O   
1944 C CB  . GLU A 241 ? 0.1917 0.1754 0.2092 0.0120  -0.0033 -0.0051 240 GLU A CB  
1945 C CG  . GLU A 241 ? 0.1870 0.1692 0.2041 0.0133  -0.0031 -0.0023 240 GLU A CG  
1946 C CD  . GLU A 241 ? 0.2202 0.1986 0.2393 0.0145  -0.0032 -0.0003 240 GLU A CD  
1947 O OE1 . GLU A 241 ? 0.2269 0.2041 0.2489 0.0146  -0.0036 -0.0010 240 GLU A OE1 
1948 O OE2 . GLU A 241 ? 0.2072 0.1842 0.2252 0.0154  -0.0029 0.0020  240 GLU A OE2 
1949 N N   . PHE A 242 ? 0.1951 0.1870 0.2173 0.0121  -0.0030 -0.0116 241 PHE A N   
1950 C CA  . PHE A 242 ? 0.1809 0.1738 0.2042 0.0119  -0.0032 -0.0144 241 PHE A CA  
1951 C C   . PHE A 242 ? 0.1890 0.1822 0.2187 0.0145  -0.0036 -0.0153 241 PHE A C   
1952 O O   . PHE A 242 ? 0.1840 0.1781 0.2166 0.0162  -0.0034 -0.0141 241 PHE A O   
1953 C CB  . PHE A 242 ? 0.1980 0.1955 0.2185 0.0101  -0.0024 -0.0169 241 PHE A CB  
1954 C CG  . PHE A 242 ? 0.1804 0.1825 0.2040 0.0113  -0.0019 -0.0184 241 PHE A CG  
1955 C CD1 . PHE A 242 ? 0.1929 0.1965 0.2164 0.0115  -0.0016 -0.0169 241 PHE A CD1 
1956 C CD2 . PHE A 242 ? 0.2120 0.2173 0.2385 0.0123  -0.0017 -0.0216 241 PHE A CD2 
1957 C CE1 . PHE A 242 ? 0.1857 0.1939 0.2123 0.0126  -0.0012 -0.0183 241 PHE A CE1 
1958 C CE2 . PHE A 242 ? 0.2320 0.2418 0.2617 0.0135  -0.0012 -0.0231 241 PHE A CE2 
1959 C CZ  . PHE A 242 ? 0.2037 0.2150 0.2336 0.0136  -0.0010 -0.0214 241 PHE A CZ  
1960 N N   . ALA A 243 ? 0.2014 0.1939 0.2333 0.0149  -0.0043 -0.0175 242 ALA A N   
1961 C CA  . ALA A 243 ? 0.1919 0.1843 0.2303 0.0174  -0.0048 -0.0187 242 ALA A CA  
1962 C C   . ALA A 243 ? 0.2260 0.2186 0.2652 0.0172  -0.0056 -0.0222 242 ALA A C   
1963 O O   . ALA A 243 ? 0.2344 0.2264 0.2692 0.0154  -0.0058 -0.0229 242 ALA A O   
1964 C CB  . ALA A 243 ? 0.2368 0.2251 0.2794 0.0189  -0.0053 -0.0156 242 ALA A CB  
1965 N N   . GLY A 244 ? 0.2480 0.2415 0.2931 0.0193  -0.0061 -0.0245 243 GLY A N   
1966 C CA  . GLY A 244 ? 0.2186 0.2116 0.2660 0.0198  -0.0072 -0.0280 243 GLY A CA  
1967 C C   . GLY A 244 ? 0.2308 0.2228 0.2863 0.0225  -0.0081 -0.0288 243 GLY A C   
1968 O O   . GLY A 244 ? 0.2288 0.2217 0.2873 0.0239  -0.0076 -0.0272 243 GLY A O   
1969 N N   . GLY A 245 ? 0.2548 0.2448 0.3140 0.0232  -0.0095 -0.0312 244 GLY A N   
1970 C CA  . GLY A 245 ? 0.2584 0.2468 0.3260 0.0257  -0.0106 -0.0321 244 GLY A CA  
1971 C C   . GLY A 245 ? 0.2877 0.2800 0.3579 0.0273  -0.0103 -0.0355 244 GLY A C   
1972 O O   . GLY A 245 ? 0.2569 0.2536 0.3228 0.0266  -0.0094 -0.0382 244 GLY A O   
1973 N N   . ALA A 246 ? 0.2512 0.2420 0.3292 0.0297  -0.0111 -0.0353 245 ALA A N   
1974 C CA  . ALA A 246 ? 0.2820 0.2761 0.3641 0.0317  -0.0111 -0.0385 245 ALA A CA  
1975 C C   . ALA A 246 ? 0.3395 0.3342 0.4240 0.0325  -0.0124 -0.0442 245 ALA A C   
1976 O O   . ALA A 246 ? 0.2800 0.2722 0.3720 0.0345  -0.0140 -0.0459 245 ALA A O   
1977 C CB  . ALA A 246 ? 0.3224 0.3142 0.4118 0.0340  -0.0115 -0.0356 245 ALA A CB  
1978 N N   . ASN A 247 ? 0.2615 0.2596 0.3394 0.0311  -0.0118 -0.0472 246 ASN A N   
1979 C CA  . ASN A 247 ? 0.2389 0.2383 0.3175 0.0318  -0.0129 -0.0529 246 ASN A CA  
1980 C C   . ASN A 247 ? 0.2558 0.2612 0.3272 0.0307  -0.0113 -0.0557 246 ASN A C   
1981 O O   . ASN A 247 ? 0.2880 0.2956 0.3537 0.0288  -0.0095 -0.0529 246 ASN A O   
1982 C CB  . ASN A 247 ? 0.2585 0.2536 0.3369 0.0309  -0.0147 -0.0533 246 ASN A CB  
1983 C CG  . ASN A 247 ? 0.2825 0.2768 0.3531 0.0281  -0.0139 -0.0500 246 ASN A CG  
1984 O OD1 . ASN A 247 ? 0.2827 0.2807 0.3460 0.0266  -0.0128 -0.0511 246 ASN A OD1 
1985 N ND2 . ASN A 247 ? 0.2341 0.2238 0.3065 0.0274  -0.0145 -0.0458 246 ASN A ND2 
1986 N N   . ASP A 248 ? 0.3078 0.2699 0.3403 0.0846  -0.0310 -0.0384 247 ASP A N   
1987 C CA  . ASP A 248 ? 0.3271 0.3005 0.3610 0.0877  -0.0311 -0.0410 247 ASP A CA  
1988 C C   . ASP A 248 ? 0.2835 0.2586 0.3183 0.0851  -0.0274 -0.0420 247 ASP A C   
1989 O O   . ASP A 248 ? 0.2838 0.2677 0.3200 0.0868  -0.0268 -0.0442 247 ASP A O   
1990 C CB  . ASP A 248 ? 0.3328 0.3095 0.3665 0.0899  -0.0326 -0.0414 247 ASP A CB  
1991 C CG  . ASP A 248 ? 0.4669 0.4472 0.4998 0.0941  -0.0368 -0.0420 247 ASP A CG  
1992 O OD1 . ASP A 248 ? 0.4367 0.4151 0.4687 0.0949  -0.0388 -0.0415 247 ASP A OD1 
1993 O OD2 . ASP A 248 ? 0.5416 0.5261 0.5742 0.0965  -0.0382 -0.0429 247 ASP A OD2 
1994 N N   . VAL A 249 ? 0.3014 0.2692 0.3359 0.0811  -0.0248 -0.0405 248 VAL A N   
1995 C CA  . VAL A 249 ? 0.2492 0.2177 0.2839 0.0785  -0.0214 -0.0416 248 VAL A CA  
1996 C C   . VAL A 249 ? 0.2693 0.2370 0.3041 0.0769  -0.0201 -0.0425 248 VAL A C   
1997 O O   . VAL A 249 ? 0.2720 0.2461 0.3071 0.0763  -0.0182 -0.0444 248 VAL A O   
1998 C CB  . VAL A 249 ? 0.2827 0.2432 0.3166 0.0744  -0.0191 -0.0396 248 VAL A CB  
1999 C CG1 . VAL A 249 ? 0.2648 0.2246 0.2981 0.0714  -0.0157 -0.0407 248 VAL A CG1 
2000 C CG2 . VAL A 249 ? 0.3122 0.2744 0.3460 0.0762  -0.0202 -0.0392 248 VAL A CG2 
2001 N N   . CYS A 250 ? 0.2948 0.2549 0.3289 0.0750  -0.0206 -0.0408 249 CYS A N   
2002 C CA  . CYS A 250 ? 0.2863 0.2458 0.3189 0.0707  -0.0187 -0.0402 249 CYS A CA  
2003 C C   . CYS A 250 ? 0.2892 0.2605 0.3209 0.0705  -0.0194 -0.0400 249 CYS A C   
2004 O O   . CYS A 250 ? 0.2665 0.2432 0.2967 0.0652  -0.0166 -0.0391 249 CYS A O   
2005 C CB  . CYS A 250 ? 0.2753 0.2238 0.3068 0.0686  -0.0191 -0.0382 249 CYS A CB  
2006 S SG  . CYS A 250 ? 0.2833 0.2207 0.3147 0.0639  -0.0160 -0.0367 249 CYS A SG  
2007 N N   . GLU A 251 ? 0.2867 0.2621 0.3194 0.0762  -0.0232 -0.0407 250 GLU A N   
2008 C CA  . GLU A 251 ? 0.3521 0.3395 0.3845 0.0766  -0.0241 -0.0410 250 GLU A CA  
2009 C C   . GLU A 251 ? 0.2940 0.2929 0.3275 0.0748  -0.0214 -0.0423 250 GLU A C   
2010 O O   . GLU A 251 ? 0.2855 0.2917 0.3181 0.0702  -0.0195 -0.0415 250 GLU A O   
2011 C CB  . GLU A 251 ? 0.3467 0.3372 0.3803 0.0841  -0.0290 -0.0424 250 GLU A CB  
2012 C CG  . GLU A 251 ? 0.3850 0.3659 0.4166 0.0857  -0.0322 -0.0408 250 GLU A CG  
2013 C CD  . GLU A 251 ? 0.3765 0.3611 0.4089 0.0933  -0.0374 -0.0425 250 GLU A CD  
2014 O OE1 . GLU A 251 ? 0.4988 0.4963 0.5327 0.0957  -0.0383 -0.0443 250 GLU A OE1 
2015 O OE2 . GLU A 251 ? 0.5096 0.4851 0.5403 0.0946  -0.0398 -0.0412 250 GLU A OE2 
2016 N N   . THR A 252 ? 0.2491 0.2492 0.2843 0.0783  -0.0212 -0.0442 251 THR A N   
2017 C CA  . THR A 252 ? 0.2410 0.2512 0.2766 0.0767  -0.0185 -0.0455 251 THR A CA  
2018 C C   . THR A 252 ? 0.2816 0.2888 0.3150 0.0689  -0.0142 -0.0440 251 THR A C   
2019 O O   . THR A 252 ? 0.2693 0.2856 0.3021 0.0650  -0.0117 -0.0440 251 THR A O   
2020 C CB  . THR A 252 ? 0.2667 0.2774 0.3040 0.0824  -0.0194 -0.0478 251 THR A CB  
2021 O OG1 . THR A 252 ? 0.3230 0.3363 0.3622 0.0898  -0.0238 -0.0493 251 THR A OG1 
2022 C CG2 . THR A 252 ? 0.2905 0.3122 0.3279 0.0809  -0.0165 -0.0490 251 THR A CG2 
2023 N N   . ALA A 253 ? 0.2234 0.2179 0.2555 0.0665  -0.0133 -0.0429 252 ALA A N   
2024 C CA  . ALA A 253 ? 0.2309 0.2220 0.2606 0.0594  -0.0095 -0.0418 252 ALA A CA  
2025 C C   . ALA A 253 ? 0.2207 0.2156 0.2487 0.0540  -0.0085 -0.0398 252 ALA A C   
2026 O O   . ALA A 253 ? 0.2553 0.2545 0.2816 0.0486  -0.0057 -0.0393 252 ALA A O   
2027 C CB  . ALA A 253 ? 0.2356 0.2126 0.2649 0.0584  -0.0090 -0.0413 252 ALA A CB  
2028 N N   . ILE A 254 ? 0.2057 0.1988 0.2338 0.0554  -0.0109 -0.0387 253 ILE A N   
2029 C CA  . ILE A 254 ? 0.1805 0.1768 0.2066 0.0509  -0.0103 -0.0370 253 ILE A CA  
2030 C C   . ILE A 254 ? 0.2418 0.2527 0.2690 0.0503  -0.0101 -0.0378 253 ILE A C   
2031 O O   . ILE A 254 ? 0.2211 0.2362 0.2467 0.0445  -0.0078 -0.0370 253 ILE A O   
2032 C CB  . ILE A 254 ? 0.2441 0.2349 0.2695 0.0533  -0.0133 -0.0358 253 ILE A CB  
2033 C CG1 . ILE A 254 ? 0.2500 0.2265 0.2740 0.0517  -0.0125 -0.0346 253 ILE A CG1 
2034 C CG2 . ILE A 254 ? 0.2058 0.2018 0.2293 0.0497  -0.0134 -0.0345 253 ILE A CG2 
2035 C CD1 . ILE A 254 ? 0.2996 0.2690 0.3230 0.0551  -0.0156 -0.0336 253 ILE A CD1 
2036 N N   . THR A 255 ? 0.2226 0.2417 0.2525 0.0562  -0.0126 -0.0397 254 THR A N   
2037 C CA  A THR A 255 ? 0.2282 0.2620 0.2596 0.0556  -0.0123 -0.0406 254 THR A CA  
2038 C CA  B THR A 255 ? 0.2286 0.2626 0.2602 0.0560  -0.0124 -0.0408 254 THR A CA  
2039 C C   . THR A 255 ? 0.2003 0.2395 0.2316 0.0519  -0.0086 -0.0412 254 THR A C   
2040 O O   . THR A 255 ? 0.2376 0.2859 0.2688 0.0475  -0.0069 -0.0409 254 THR A O   
2041 C CB  A THR A 255 ? 0.2780 0.3200 0.3125 0.0630  -0.0158 -0.0428 254 THR A CB  
2042 C CB  B THR A 255 ? 0.2768 0.3179 0.3114 0.0639  -0.0158 -0.0430 254 THR A CB  
2043 O OG1 A THR A 255 ? 0.2280 0.2672 0.2638 0.0682  -0.0165 -0.0444 254 THR A OG1 
2044 O OG1 B THR A 255 ? 0.3123 0.3484 0.3466 0.0675  -0.0196 -0.0426 254 THR A OG1 
2045 C CG2 A THR A 255 ? 0.3036 0.3410 0.3374 0.0660  -0.0196 -0.0420 254 THR A CG2 
2046 C CG2 B THR A 255 ? 0.2820 0.3395 0.3190 0.0638  -0.0154 -0.0446 254 THR A CG2 
2047 N N   . GLY A 256 ? 0.2014 0.2346 0.2322 0.0532  -0.0074 -0.0420 255 GLY A N   
2048 C CA  . GLY A 256 ? 0.2096 0.2467 0.2393 0.0494  -0.0039 -0.0424 255 GLY A CA  
2049 C C   . GLY A 256 ? 0.2056 0.2387 0.2321 0.0414  -0.0011 -0.0404 255 GLY A C   
2050 O O   . GLY A 256 ? 0.2024 0.2427 0.2279 0.0368  0.0013  -0.0402 255 GLY A O   
2051 N N   . MET A 257 ? 0.1807 0.2022 0.2054 0.0395  -0.0015 -0.0389 256 MET A N   
2052 C CA  . MET A 257 ? 0.2152 0.2325 0.2366 0.0322  0.0008  -0.0372 256 MET A CA  
2053 C C   . MET A 257 ? 0.1904 0.2169 0.2118 0.0287  0.0007  -0.0362 256 MET A C   
2054 O O   . MET A 257 ? 0.2120 0.2426 0.2317 0.0230  0.0029  -0.0356 256 MET A O   
2055 C CB  . MET A 257 ? 0.2061 0.2096 0.2260 0.0315  0.0004  -0.0360 256 MET A CB  
2056 C CG  . MET A 257 ? 0.2016 0.1998 0.2179 0.0244  0.0028  -0.0346 256 MET A CG  
2057 S SD  . MET A 257 ? 0.2543 0.2369 0.2689 0.0234  0.0028  -0.0334 256 MET A SD  
2058 C CE  . MET A 257 ? 0.2641 0.2491 0.2786 0.0238  0.0007  -0.0317 256 MET A CE  
2059 N N   . LEU A 258 ? 0.1802 0.2098 0.2034 0.0321  -0.0021 -0.0361 257 LEU A N   
2060 C CA  . LEU A 258 ? 0.1790 0.2170 0.2023 0.0291  -0.0026 -0.0354 257 LEU A CA  
2061 C C   . LEU A 258 ? 0.1748 0.2276 0.2006 0.0286  -0.0018 -0.0368 257 LEU A C   
2062 O O   . LEU A 258 ? 0.1914 0.2509 0.2168 0.0235  -0.0007 -0.0361 257 LEU A O   
2063 C CB  . LEU A 258 ? 0.1901 0.2271 0.2143 0.0333  -0.0062 -0.0351 257 LEU A CB  
2064 C CG  . LEU A 258 ? 0.1831 0.2056 0.2042 0.0327  -0.0066 -0.0334 257 LEU A CG  
2065 C CD1 . LEU A 258 ? 0.2146 0.2357 0.2362 0.0377  -0.0103 -0.0333 257 LEU A CD1 
2066 C CD2 . LEU A 258 ? 0.2028 0.2212 0.2204 0.0257  -0.0046 -0.0315 257 LEU A CD2 
2067 N N   . ASP A 259 ? 0.1892 0.2476 0.2178 0.0338  -0.0022 -0.0387 258 ASP A N   
2068 C CA  . ASP A 259 ? 0.1851 0.2578 0.2161 0.0332  -0.0008 -0.0402 258 ASP A CA  
2069 C C   . ASP A 259 ? 0.1859 0.2586 0.2141 0.0262  0.0030  -0.0393 258 ASP A C   
2070 O O   . ASP A 259 ? 0.1761 0.2594 0.2052 0.0222  0.0046  -0.0394 258 ASP A O   
2071 C CB  . ASP A 259 ? 0.2006 0.2778 0.2343 0.0403  -0.0019 -0.0425 258 ASP A CB  
2072 C CG  . ASP A 259 ? 0.2349 0.3167 0.2719 0.0472  -0.0060 -0.0438 258 ASP A CG  
2073 O OD1 . ASP A 259 ? 0.2404 0.3243 0.2777 0.0462  -0.0079 -0.0432 258 ASP A OD1 
2074 O OD2 . ASP A 259 ? 0.2610 0.3439 0.2998 0.0537  -0.0076 -0.0457 258 ASP A OD2 
2075 N N   . TYR A 260 ? 0.1772 0.2378 0.2021 0.0249  0.0045  -0.0386 259 TYR A N   
2076 C CA  . TYR A 260 ? 0.1707 0.2294 0.1921 0.0183  0.0078  -0.0378 259 TYR A CA  
2077 C C   . TYR A 260 ? 0.1577 0.2155 0.1769 0.0115  0.0083  -0.0359 259 TYR A C   
2078 O O   . TYR A 260 ? 0.1922 0.2566 0.2104 0.0060  0.0103  -0.0354 259 TYR A O   
2079 C CB  . TYR A 260 ? 0.2158 0.2609 0.2342 0.0190  0.0086  -0.0378 259 TYR A CB  
2080 C CG  . TYR A 260 ? 0.2052 0.2459 0.2190 0.0126  0.0115  -0.0370 259 TYR A CG  
2081 C CD1 . TYR A 260 ? 0.1845 0.2301 0.1970 0.0117  0.0136  -0.0379 259 TYR A CD1 
2082 C CD2 . TYR A 260 ? 0.2313 0.2626 0.2417 0.0075  0.0120  -0.0355 259 TYR A CD2 
2083 C CE1 . TYR A 260 ? 0.1977 0.2383 0.2054 0.0057  0.0160  -0.0371 259 TYR A CE1 
2084 C CE2 . TYR A 260 ? 0.2542 0.2808 0.2601 0.0018  0.0142  -0.0349 259 TYR A CE2 
2085 C CZ  . TYR A 260 ? 0.2154 0.2464 0.2197 0.0009  0.0161  -0.0357 259 TYR A CZ  
2086 O OH  . TYR A 260 ? 0.2625 0.2877 0.2615 -0.0048 0.0180  -0.0351 259 TYR A OH  
2087 N N   . MET A 261 ? 0.1794 0.2289 0.1977 0.0117  0.0066  -0.0348 260 MET A N   
2088 C CA  . MET A 261 ? 0.1529 0.2019 0.1691 0.0057  0.0068  -0.0331 260 MET A CA  
2089 C C   . MET A 261 ? 0.1660 0.2293 0.1850 0.0044  0.0062  -0.0334 260 MET A C   
2090 O O   . MET A 261 ? 0.1853 0.2520 0.2028 -0.0018 0.0074  -0.0325 260 MET A O   
2091 C CB  . MET A 261 ? 0.1761 0.2151 0.1910 0.0070  0.0049  -0.0319 260 MET A CB  
2092 C CG  . MET A 261 ? 0.1804 0.2053 0.1925 0.0071  0.0059  -0.0316 260 MET A CG  
2093 S SD  . MET A 261 ? 0.2061 0.2195 0.2173 0.0095  0.0039  -0.0304 260 MET A SD  
2094 C CE  . MET A 261 ? 0.2078 0.2217 0.2158 0.0031  0.0041  -0.0285 260 MET A CE  
2095 N N   . ALA A 262 ? 0.1604 0.2324 0.1838 0.0101  0.0042  -0.0349 261 ALA A N   
2096 C CA  . ALA A 262 ? 0.1745 0.2608 0.2013 0.0094  0.0033  -0.0357 261 ALA A CA  
2097 C C   . ALA A 262 ? 0.1832 0.2802 0.2111 0.0052  0.0061  -0.0363 261 ALA A C   
2098 O O   . ALA A 262 ? 0.2107 0.3183 0.2406 0.0018  0.0061  -0.0364 261 ALA A O   
2099 C CB  . ALA A 262 ? 0.1603 0.2529 0.1913 0.0171  0.0002  -0.0375 261 ALA A CB  
2100 N N   . GLN A 263 ? 0.1773 0.2717 0.2036 0.0051  0.0086  -0.0366 262 GLN A N   
2101 C CA  . GLN A 263 ? 0.1828 0.2856 0.2088 0.0002  0.0116  -0.0368 262 GLN A CA  
2102 C C   . GLN A 263 ? 0.2506 0.3448 0.2712 -0.0073 0.0138  -0.0349 262 GLN A C   
2103 O O   . GLN A 263 ? 0.2399 0.3377 0.2588 -0.0118 0.0165  -0.0347 262 GLN A O   
2104 C CB  . GLN A 263 ? 0.1609 0.2666 0.1876 0.0043  0.0131  -0.0384 262 GLN A CB  
2105 C CG  . GLN A 263 ? 0.3189 0.4346 0.3511 0.0119  0.0110  -0.0407 262 GLN A CG  
2106 C CD  . GLN A 263 ? 0.3457 0.4767 0.3826 0.0108  0.0101  -0.0415 262 GLN A CD  
2107 O OE1 . GLN A 263 ? 0.3483 0.4877 0.3855 0.0047  0.0124  -0.0411 262 GLN A OE1 
2108 N NE2 . GLN A 263 ? 0.3462 0.4807 0.3867 0.0166  0.0066  -0.0427 262 GLN A NE2 
2109 N N   . ASN A 264 ? 0.2060 0.2888 0.2236 -0.0089 0.0126  -0.0334 263 ASN A N   
2110 C CA  . ASN A 264 ? 0.1942 0.2680 0.2064 -0.0157 0.0142  -0.0317 263 ASN A CA  
2111 C C   . ASN A 264 ? 0.1934 0.2638 0.2044 -0.0187 0.0125  -0.0303 263 ASN A C   
2112 O O   . ASN A 264 ? 0.2202 0.2784 0.2271 -0.0210 0.0125  -0.0291 263 ASN A O   
2113 C CB  . ASN A 264 ? 0.1702 0.2301 0.1786 -0.0141 0.0150  -0.0317 263 ASN A CB  
2114 C CG  . ASN A 264 ? 0.2072 0.2698 0.2154 -0.0124 0.0169  -0.0330 263 ASN A CG  
2115 O OD1 . ASN A 264 ? 0.2391 0.3033 0.2443 -0.0174 0.0192  -0.0326 263 ASN A OD1 
2116 N ND2 . ASN A 264 ? 0.1778 0.2406 0.1888 -0.0052 0.0159  -0.0344 263 ASN A ND2 
2117 N N   . THR A 265 ? 0.1917 0.2729 0.2065 -0.0186 0.0110  -0.0306 264 THR A N   
2118 C CA  . THR A 265 ? 0.1727 0.2510 0.1863 -0.0210 0.0090  -0.0294 264 THR A CA  
2119 C C   . THR A 265 ? 0.2087 0.2862 0.2189 -0.0291 0.0103  -0.0280 264 THR A C   
2120 O O   . THR A 265 ? 0.2415 0.3156 0.2499 -0.0315 0.0088  -0.0269 264 THR A O   
2121 C CB  . THR A 265 ? 0.2044 0.2939 0.2230 -0.0176 0.0064  -0.0304 264 THR A CB  
2122 O OG1 . THR A 265 ? 0.2229 0.3276 0.2457 -0.0193 0.0074  -0.0316 264 THR A OG1 
2123 C CG2 . THR A 265 ? 0.1792 0.2668 0.2002 -0.0094 0.0044  -0.0315 264 THR A CG2 
2124 N N   . ASP A 266 ? 0.2267 0.3067 0.2353 -0.0334 0.0128  -0.0280 265 ASP A N   
2125 C CA  . ASP A 266 ? 0.2502 0.3262 0.2543 -0.0410 0.0138  -0.0265 265 ASP A CA  
2126 C C   . ASP A 266 ? 0.2760 0.3358 0.2746 -0.0418 0.0134  -0.0254 265 ASP A C   
2127 O O   . ASP A 266 ? 0.2609 0.3160 0.2557 -0.0470 0.0130  -0.0242 265 ASP A O   
2128 C CB  . ASP A 266 ? 0.2306 0.3107 0.2332 -0.0454 0.0166  -0.0266 265 ASP A CB  
2129 C CG  . ASP A 266 ? 0.2467 0.3186 0.2465 -0.0427 0.0184  -0.0271 265 ASP A CG  
2130 O OD1 . ASP A 266 ? 0.2581 0.3271 0.2599 -0.0361 0.0176  -0.0281 265 ASP A OD1 
2131 O OD2 . ASP A 266 ? 0.2997 0.3680 0.2951 -0.0473 0.0203  -0.0266 265 ASP A OD2 
2132 N N   . VAL A 267 ? 0.2223 0.2737 0.2204 -0.0366 0.0134  -0.0260 266 VAL A N   
2133 C CA  . VAL A 267 ? 0.1840 0.2207 0.1775 -0.0370 0.0131  -0.0252 266 VAL A CA  
2134 C C   . VAL A 267 ? 0.2127 0.2447 0.2081 -0.0314 0.0113  -0.0253 266 VAL A C   
2135 O O   . VAL A 267 ? 0.2244 0.2470 0.2167 -0.0325 0.0106  -0.0244 266 VAL A O   
2136 C CB  . VAL A 267 ? 0.2501 0.2778 0.2401 -0.0374 0.0149  -0.0257 266 VAL A CB  
2137 C CG1 . VAL A 267 ? 0.2508 0.2813 0.2376 -0.0436 0.0166  -0.0253 266 VAL A CG1 
2138 C CG2 . VAL A 267 ? 0.2406 0.2691 0.2337 -0.0309 0.0153  -0.0271 266 VAL A CG2 
2139 N N   . TRP A 268 ? 0.1945 0.2325 0.1946 -0.0254 0.0104  -0.0263 267 TRP A N   
2140 C CA  . TRP A 268 ? 0.1869 0.2194 0.1881 -0.0201 0.0085  -0.0263 267 TRP A CA  
2141 C C   . TRP A 268 ? 0.2122 0.2509 0.2152 -0.0194 0.0062  -0.0259 267 TRP A C   
2142 O O   . TRP A 268 ? 0.2092 0.2599 0.2162 -0.0177 0.0052  -0.0268 267 TRP A O   
2143 C CB  . TRP A 268 ? 0.1796 0.2130 0.1842 -0.0134 0.0082  -0.0277 267 TRP A CB  
2144 C CG  . TRP A 268 ? 0.1959 0.2197 0.1983 -0.0130 0.0099  -0.0282 267 TRP A CG  
2145 C CD1 . TRP A 268 ? 0.2021 0.2287 0.2051 -0.0122 0.0114  -0.0293 267 TRP A CD1 
2146 C CD2 . TRP A 268 ? 0.1909 0.2010 0.1901 -0.0135 0.0103  -0.0277 267 TRP A CD2 
2147 N NE1 . TRP A 268 ? 0.1894 0.2046 0.1897 -0.0119 0.0124  -0.0297 267 TRP A NE1 
2148 C CE2 . TRP A 268 ? 0.1860 0.1913 0.1843 -0.0127 0.0117  -0.0288 267 TRP A CE2 
2149 C CE3 . TRP A 268 ? 0.1896 0.1913 0.1866 -0.0144 0.0096  -0.0266 267 TRP A CE3 
2150 C CZ2 . TRP A 268 ? 0.2001 0.1928 0.1959 -0.0127 0.0123  -0.0290 267 TRP A CZ2 
2151 C CZ3 . TRP A 268 ? 0.2097 0.1991 0.2043 -0.0146 0.0105  -0.0267 267 TRP A CZ3 
2152 C CH2 . TRP A 268 ? 0.2358 0.2211 0.2301 -0.0137 0.0117  -0.0280 267 TRP A CH2 
2153 N N   . THR A 269 ? 0.1924 0.2227 0.1922 -0.0203 0.0052  -0.0246 268 THR A N   
2154 C CA  . THR A 269 ? 0.1738 0.2077 0.1742 -0.0194 0.0027  -0.0241 268 THR A CA  
2155 C C   . THR A 269 ? 0.2116 0.2436 0.2140 -0.0126 0.0007  -0.0245 268 THR A C   
2156 O O   . THR A 269 ? 0.2037 0.2394 0.2067 -0.0109 -0.0017 -0.0244 268 THR A O   
2157 C CB  . THR A 269 ? 0.1819 0.2074 0.1772 -0.0238 0.0026  -0.0225 268 THR A CB  
2158 O OG1 . THR A 269 ? 0.2085 0.2210 0.2009 -0.0221 0.0033  -0.0219 268 THR A OG1 
2159 C CG2 . THR A 269 ? 0.2258 0.2523 0.2187 -0.0306 0.0042  -0.0221 268 THR A CG2 
2160 N N   . GLY A 270 ? 0.1822 0.2082 0.1854 -0.0086 0.0013  -0.0251 269 GLY A N   
2161 C CA  . GLY A 270 ? 0.1662 0.1903 0.1711 -0.0023 -0.0008 -0.0254 269 GLY A CA  
2162 C C   . GLY A 270 ? 0.2241 0.2351 0.2272 -0.0003 0.0000  -0.0250 269 GLY A C   
2163 O O   . GLY A 270 ? 0.2026 0.2080 0.2044 -0.0027 0.0023  -0.0250 269 GLY A O   
2164 N N   . ALA A 271 ? 0.1651 0.1715 0.1682 0.0041  -0.0020 -0.0246 270 ALA A N   
2165 C CA  . ALA A 271 ? 0.1985 0.1943 0.2013 0.0071  -0.0016 -0.0245 270 ALA A CA  
2166 C C   . ALA A 271 ? 0.2322 0.2210 0.2328 0.0095  -0.0035 -0.0233 270 ALA A C   
2167 O O   . ALA A 271 ? 0.2243 0.2179 0.2247 0.0112  -0.0060 -0.0231 270 ALA A O   
2168 C CB  . ALA A 271 ? 0.1934 0.1931 0.2004 0.0122  -0.0021 -0.0263 270 ALA A CB  
2169 N N   . ILE A 272 ? 0.1990 0.1762 0.1979 0.0094  -0.0022 -0.0225 271 ILE A N   
2170 C CA  . ILE A 272 ? 0.2201 0.1888 0.2161 0.0107  -0.0033 -0.0210 271 ILE A CA  
2171 C C   . ILE A 272 ? 0.2072 0.1679 0.2049 0.0144  -0.0033 -0.0213 271 ILE A C   
2172 O O   . ILE A 272 ? 0.2130 0.1681 0.2114 0.0129  -0.0009 -0.0218 271 ILE A O   
2173 C CB  . ILE A 272 ? 0.1882 0.1500 0.1795 0.0054  -0.0014 -0.0194 271 ILE A CB  
2174 C CG1 . ILE A 272 ? 0.1945 0.1637 0.1841 0.0011  -0.0013 -0.0192 271 ILE A CG1 
2175 C CG2 . ILE A 272 ? 0.2010 0.1550 0.1887 0.0069  -0.0026 -0.0177 271 ILE A CG2 
2176 C CD1 . ILE A 272 ? 0.1985 0.1609 0.1830 -0.0038 0.0002  -0.0177 271 ILE A CD1 
2177 N N   . TRP A 273 ? 0.1965 0.1563 0.1948 0.0194  -0.0061 -0.0212 272 TRP A N   
2178 C CA  . TRP A 273 ? 0.2211 0.1737 0.2212 0.0234  -0.0066 -0.0216 272 TRP A CA  
2179 C C   . TRP A 273 ? 0.2352 0.1754 0.2324 0.0209  -0.0047 -0.0200 272 TRP A C   
2180 O O   . TRP A 273 ? 0.2332 0.1701 0.2261 0.0182  -0.0044 -0.0183 272 TRP A O   
2181 C CB  . TRP A 273 ? 0.2111 0.1659 0.2119 0.0292  -0.0106 -0.0218 272 TRP A CB  
2182 C CG  . TRP A 273 ? 0.1997 0.1470 0.2023 0.0336  -0.0118 -0.0222 272 TRP A CG  
2183 C CD1 . TRP A 273 ? 0.2241 0.1605 0.2241 0.0343  -0.0123 -0.0206 272 TRP A CD1 
2184 C CD2 . TRP A 273 ? 0.2369 0.1868 0.2440 0.0378  -0.0126 -0.0241 272 TRP A CD2 
2185 N NE1 . TRP A 273 ? 0.2770 0.2090 0.2800 0.0384  -0.0135 -0.0215 272 TRP A NE1 
2186 C CE2 . TRP A 273 ? 0.2429 0.1830 0.2502 0.0408  -0.0138 -0.0238 272 TRP A CE2 
2187 C CE3 . TRP A 273 ? 0.2454 0.2047 0.2561 0.0391  -0.0124 -0.0262 272 TRP A CE3 
2188 C CZ2 . TRP A 273 ? 0.2686 0.2081 0.2798 0.0455  -0.0151 -0.0255 272 TRP A CZ2 
2189 C CZ3 . TRP A 273 ? 0.2521 0.2108 0.2663 0.0438  -0.0135 -0.0279 272 TRP A CZ3 
2190 C CH2 . TRP A 273 ? 0.2476 0.1965 0.2621 0.0471  -0.0150 -0.0275 272 TRP A CH2 
2191 N N   . TRP A 274 ? 0.2271 0.1606 0.2266 0.0220  -0.0035 -0.0206 273 TRP A N   
2192 C CA  . TRP A 274 ? 0.2511 0.1730 0.2487 0.0205  -0.0020 -0.0193 273 TRP A CA  
2193 C C   . TRP A 274 ? 0.2789 0.1960 0.2782 0.0255  -0.0044 -0.0193 273 TRP A C   
2194 O O   . TRP A 274 ? 0.2677 0.1853 0.2711 0.0288  -0.0051 -0.0209 273 TRP A O   
2195 C CB  . TRP A 274 ? 0.2358 0.1534 0.2353 0.0174  0.0013  -0.0203 273 TRP A CB  
2196 C CG  . TRP A 274 ? 0.2248 0.1315 0.2231 0.0159  0.0030  -0.0193 273 TRP A CG  
2197 C CD1 . TRP A 274 ? 0.2603 0.1600 0.2612 0.0186  0.0026  -0.0196 273 TRP A CD1 
2198 C CD2 . TRP A 274 ? 0.2716 0.1731 0.2656 0.0114  0.0054  -0.0177 273 TRP A CD2 
2199 N NE1 . TRP A 274 ? 0.2779 0.1689 0.2769 0.0157  0.0049  -0.0183 273 TRP A NE1 
2200 C CE2 . TRP A 274 ? 0.2701 0.1621 0.2648 0.0114  0.0066  -0.0172 273 TRP A CE2 
2201 C CE3 . TRP A 274 ? 0.2375 0.1416 0.2274 0.0073  0.0065  -0.0168 273 TRP A CE3 
2202 C CZ2 . TRP A 274 ? 0.3002 0.1857 0.2913 0.0075  0.0092  -0.0158 273 TRP A CZ2 
2203 C CZ3 . TRP A 274 ? 0.2497 0.1469 0.2358 0.0037  0.0088  -0.0154 273 TRP A CZ3 
2204 C CH2 . TRP A 274 ? 0.2595 0.1477 0.2463 0.0039  0.0103  -0.0150 273 TRP A CH2 
2205 N N   . ALA A 275 ? 0.2536 0.1653 0.2492 0.0264  -0.0059 -0.0174 274 ALA A N   
2206 C CA  . ALA A 275 ? 0.2312 0.1411 0.2212 0.0231  -0.0053 -0.0154 274 ALA A CA  
2207 C C   . ALA A 275 ? 0.2866 0.1929 0.2732 0.0265  -0.0087 -0.0140 274 ALA A C   
2208 O O   . ALA A 275 ? 0.2893 0.1915 0.2775 0.0305  -0.0106 -0.0142 274 ALA A O   
2209 C CB  . ALA A 275 ? 0.2720 0.1732 0.2599 0.0184  -0.0016 -0.0142 274 ALA A CB  
2210 N N   . ALA A 276 ? 0.2617 0.1688 0.2432 0.0251  -0.0095 -0.0126 275 ALA A N   
2211 C CA  . ALA A 276 ? 0.3003 0.2011 0.2768 0.0272  -0.0120 -0.0108 275 ALA A CA  
2212 C C   . ALA A 276 ? 0.2828 0.1733 0.2542 0.0229  -0.0090 -0.0085 275 ALA A C   
2213 O O   . ALA A 276 ? 0.3048 0.1932 0.2773 0.0188  -0.0051 -0.0085 275 ALA A O   
2214 C CB  . ALA A 276 ? 0.2790 0.1875 0.2531 0.0291  -0.0154 -0.0110 275 ALA A CB  
2215 N N   . GLY A 277 ? 0.2924 0.1763 0.2578 0.0240  -0.0109 -0.0065 276 GLY A N   
2216 C CA  . GLY A 277 ? 0.3030 0.1765 0.2630 0.0204  -0.0081 -0.0042 276 GLY A CA  
2217 C C   . GLY A 277 ? 0.3045 0.1681 0.2615 0.0231  -0.0099 -0.0026 276 GLY A C   
2218 O O   . GLY A 277 ? 0.3511 0.2151 0.3119 0.0273  -0.0126 -0.0037 276 GLY A O   
2219 N N   . PRO A 278 ? 0.3357 0.1900 0.2857 0.0207  -0.0086 -0.0001 277 PRO A N   
2220 C CA  . PRO A 278 ? 0.3500 0.1946 0.2955 0.0233  -0.0110 0.0017  277 PRO A CA  
2221 C C   . PRO A 278 ? 0.3824 0.2181 0.3304 0.0224  -0.0088 0.0023  277 PRO A C   
2222 O O   . PRO A 278 ? 0.4088 0.2366 0.3537 0.0248  -0.0112 0.0037  277 PRO A O   
2223 C CB  . PRO A 278 ? 0.4012 0.2399 0.3372 0.0208  -0.0105 0.0041  277 PRO A CB  
2224 C CG  . PRO A 278 ? 0.3554 0.1966 0.2920 0.0157  -0.0058 0.0041  277 PRO A CG  
2225 C CD  . PRO A 278 ? 0.3591 0.2116 0.3040 0.0159  -0.0054 0.0012  277 PRO A CD  
2226 N N   . TRP A 279 ? 0.4125 0.2244 0.2787 -0.0335 -0.0027 0.0318  278 TRP A N   
2227 C CA  . TRP A 279 ? 0.4603 0.2595 0.3203 -0.0482 0.0090  0.0250  278 TRP A CA  
2228 C C   . TRP A 279 ? 0.4863 0.2976 0.3624 -0.0537 0.0145  0.0117  278 TRP A C   
2229 O O   . TRP A 279 ? 0.4395 0.2533 0.3154 -0.0672 0.0224  0.0033  278 TRP A O   
2230 C CB  . TRP A 279 ? 0.4018 0.2103 0.2535 -0.0598 0.0098  0.0251  278 TRP A CB  
2231 C CG  . TRP A 279 ? 0.5354 0.3200 0.3659 -0.0605 0.0108  0.0362  278 TRP A CG  
2232 C CD1 . TRP A 279 ? 0.4820 0.2397 0.3003 -0.0507 0.0098  0.0466  278 TRP A CD1 
2233 C CD2 . TRP A 279 ? 0.4536 0.2391 0.2722 -0.0716 0.0130  0.0378  278 TRP A CD2 
2234 N NE1 . TRP A 279 ? 0.4975 0.2390 0.2968 -0.0552 0.0113  0.0546  278 TRP A NE1 
2235 C CE2 . TRP A 279 ? 0.4862 0.2444 0.2856 -0.0683 0.0135  0.0494  278 TRP A CE2 
2236 C CE3 . TRP A 279 ? 0.4766 0.2832 0.2987 -0.0840 0.0147  0.0304  278 TRP A CE3 
2237 C CZ2 . TRP A 279 ? 0.5737 0.3255 0.3577 -0.0772 0.0156  0.0538  278 TRP A CZ2 
2238 C CZ3 . TRP A 279 ? 0.4816 0.2823 0.2888 -0.0927 0.0168  0.0346  278 TRP A CZ3 
2239 C CH2 . TRP A 279 ? 0.5254 0.2989 0.3138 -0.0894 0.0172  0.0462  278 TRP A CH2 
2240 N N   . TRP A 280 ? 0.4179 0.2370 0.3080 -0.0434 0.0105  0.0092  279 TRP A N   
2241 C CA  . TRP A 280 ? 0.3617 0.1929 0.2675 -0.0479 0.0152  -0.0033 279 TRP A CA  
2242 C C   . TRP A 280 ? 0.4527 0.2574 0.3552 -0.0504 0.0255  -0.0069 279 TRP A C   
2243 O O   . TRP A 280 ? 0.4368 0.2478 0.3485 -0.0585 0.0322  -0.0180 279 TRP A O   
2244 C CB  . TRP A 280 ? 0.3351 0.1891 0.2586 -0.0365 0.0064  -0.0052 279 TRP A CB  
2245 C CG  . TRP A 280 ? 0.3086 0.1956 0.2412 -0.0375 -0.0015 -0.0075 279 TRP A CG  
2246 C CD1 . TRP A 280 ? 0.3252 0.2271 0.2612 -0.0271 -0.0125 -0.0009 279 TRP A CD1 
2247 C CD2 . TRP A 280 ? 0.3087 0.2174 0.2479 -0.0492 0.0009  -0.0172 279 TRP A CD2 
2248 N NE1 . TRP A 280 ? 0.2851 0.2159 0.2291 -0.0319 -0.0169 -0.0058 279 TRP A NE1 
2249 C CE2 . TRP A 280 ? 0.2941 0.2296 0.2402 -0.0451 -0.0090 -0.0157 279 TRP A CE2 
2250 C CE3 . TRP A 280 ? 0.3419 0.2503 0.2819 -0.0627 0.0104  -0.0272 279 TRP A CE3 
2251 C CZ2 . TRP A 280 ? 0.3125 0.2732 0.2654 -0.0536 -0.0097 -0.0237 279 TRP A CZ2 
2252 C CZ3 . TRP A 280 ? 0.3064 0.2407 0.2537 -0.0709 0.0095  -0.0352 279 TRP A CZ3 
2253 C CH2 . TRP A 280 ? 0.2859 0.2458 0.2394 -0.0662 -0.0005 -0.0333 279 TRP A CH2 
2254 N N   . GLY A 281 ? 0.4574 0.2327 0.3469 -0.0433 0.0268  0.0020  280 GLY A N   
2255 C CA  . GLY A 281 ? 0.4734 0.2221 0.3587 -0.0456 0.0366  -0.0011 280 GLY A CA  
2256 C C   . GLY A 281 ? 0.5090 0.2692 0.4129 -0.0418 0.0373  -0.0105 280 GLY A C   
2257 O O   . GLY A 281 ? 0.4264 0.2005 0.3418 -0.0297 0.0290  -0.0089 280 GLY A O   
2258 N N   . ASP A 282 ? 0.4716 0.2276 0.3790 -0.0529 0.0474  -0.0208 281 ASP A N   
2259 C CA  . ASP A 282 ? 0.4649 0.2284 0.3887 -0.0506 0.0498  -0.0302 281 ASP A CA  
2260 C C   . ASP A 282 ? 0.4629 0.2630 0.4053 -0.0543 0.0461  -0.0400 281 ASP A C   
2261 O O   . ASP A 282 ? 0.4205 0.2282 0.3759 -0.0568 0.0502  -0.0501 281 ASP A O   
2262 C CB  . ASP A 282 ? 0.4913 0.2313 0.4095 -0.0603 0.0627  -0.0366 281 ASP A CB  
2263 C CG  . ASP A 282 ? 0.5937 0.3414 0.5097 -0.0779 0.0706  -0.0451 281 ASP A CG  
2264 O OD1 . ASP A 282 ? 0.5717 0.3410 0.4889 -0.0827 0.0662  -0.0454 281 ASP A OD1 
2265 O OD2 . ASP A 282 ? 0.7199 0.4609 0.6354 -0.0842 0.0791  -0.0501 281 ASP A OD2 
2266 N N   . TYR A 283 ? 0.4121 0.2341 0.3554 -0.0548 0.0385  -0.0373 282 TYR A N   
2267 C CA  . TYR A 283 ? 0.3228 0.1791 0.2822 -0.0575 0.0341  -0.0457 282 TYR A CA  
2268 C C   . TYR A 283 ? 0.3749 0.2433 0.3518 -0.0479 0.0304  -0.0504 282 TYR A C   
2269 O O   . TYR A 283 ? 0.3564 0.2180 0.3342 -0.0348 0.0247  -0.0435 282 TYR A O   
2270 C CB  . TYR A 283 ? 0.3634 0.2375 0.3200 -0.0545 0.0243  -0.0388 282 TYR A CB  
2271 C CG  . TYR A 283 ? 0.3264 0.2351 0.2965 -0.0575 0.0191  -0.0460 282 TYR A CG  
2272 C CD1 . TYR A 283 ? 0.3383 0.2599 0.3136 -0.0701 0.0252  -0.0572 282 TYR A CD1 
2273 C CD2 . TYR A 283 ? 0.2676 0.1956 0.2438 -0.0479 0.0081  -0.0412 282 TYR A CD2 
2274 C CE1 . TYR A 283 ? 0.2979 0.2504 0.2841 -0.0725 0.0202  -0.0634 282 TYR A CE1 
2275 C CE2 . TYR A 283 ? 0.2672 0.2255 0.2541 -0.0507 0.0033  -0.0473 282 TYR A CE2 
2276 C CZ  . TYR A 283 ? 0.3263 0.2964 0.3179 -0.0629 0.0094  -0.0583 282 TYR A CZ  
2277 O OH  . TYR A 283 ? 0.2647 0.2643 0.2659 -0.0619 0.0044  -0.0610 282 TYR A OH  
2278 N N   . ILE A 284 ? 0.3370 0.2245 0.3278 -0.0544 0.0335  -0.0625 283 ILE A N   
2279 C CA  . ILE A 284 ? 0.3219 0.2208 0.3296 -0.0471 0.0314  -0.0685 283 ILE A CA  
2280 C C   . ILE A 284 ? 0.2844 0.2025 0.3006 -0.0345 0.0193  -0.0635 283 ILE A C   
2281 O O   . ILE A 284 ? 0.3139 0.2358 0.3416 -0.0253 0.0166  -0.0653 283 ILE A O   
2282 C CB  . ILE A 284 ? 0.3103 0.2284 0.3307 -0.0573 0.0365  -0.0825 283 ILE A CB  
2283 C CG1 . ILE A 284 ? 0.2733 0.2191 0.2926 -0.0616 0.0320  -0.0803 283 ILE A CG1 
2284 C CG2 . ILE A 284 ? 0.3339 0.2389 0.3488 -0.0630 0.0464  -0.0832 283 ILE A CG2 
2285 C CD1 . ILE A 284 ? 0.3165 0.2916 0.3460 -0.0598 0.0328  -0.0809 283 ILE A CD1 
2286 N N   . PHE A 285 ? 0.2858 0.2168 0.2970 -0.0341 0.0122  -0.0576 284 PHE A N   
2287 C CA  . PHE A 285 ? 0.2663 0.2169 0.2853 -0.0231 0.0009  -0.0532 284 PHE A CA  
2288 C C   . PHE A 285 ? 0.2425 0.1803 0.2494 -0.0136 -0.0055 -0.0396 284 PHE A C   
2289 O O   . PHE A 285 ? 0.2496 0.2046 0.2605 -0.0061 -0.0152 -0.0352 284 PHE A O   
2290 C CB  . PHE A 285 ? 0.2489 0.2295 0.2743 -0.0289 -0.0037 -0.0580 284 PHE A CB  
2291 C CG  . PHE A 285 ? 0.2540 0.2506 0.2917 -0.0374 0.0014  -0.0714 284 PHE A CG  
2292 C CD1 . PHE A 285 ? 0.2699 0.2656 0.3196 -0.0344 0.0048  -0.0784 284 PHE A CD1 
2293 C CD2 . PHE A 285 ? 0.2492 0.2621 0.2843 -0.0453 0.0028  -0.0726 284 PHE A CD2 
2294 C CE1 . PHE A 285 ? 0.2492 0.2611 0.3057 -0.0376 0.0095  -0.0821 284 PHE A CE1 
2295 C CE2 . PHE A 285 ? 0.2349 0.2606 0.2745 -0.0430 0.0081  -0.0709 284 PHE A CE2 
2296 C CZ  . PHE A 285 ? 0.2577 0.2840 0.3075 -0.0399 0.0114  -0.0757 284 PHE A CZ  
2297 N N   . SER A 286 ? 0.2762 0.1845 0.2682 -0.0138 -0.0006 -0.0330 285 SER A N   
2298 C CA  . SER A 286 ? 0.3023 0.1991 0.2809 -0.0064 -0.0065 -0.0201 285 SER A CA  
2299 C C   . SER A 286 ? 0.3074 0.2060 0.2920 0.0099  -0.0148 -0.0144 285 SER A C   
2300 O O   . SER A 286 ? 0.3403 0.2235 0.3273 0.0167  -0.0122 -0.0147 285 SER A O   
2301 C CB  . SER A 286 ? 0.2958 0.1593 0.2560 -0.0101 0.0009  -0.0143 285 SER A CB  
2302 O OG  . SER A 286 ? 0.3500 0.2039 0.2983 -0.0014 -0.0057 -0.0018 285 SER A OG  
2303 N N   . MET A 287 ? 0.2681 0.1849 0.2543 0.0159  -0.0247 -0.0089 286 MET A N   
2304 C CA  . MET A 287 ? 0.2936 0.2144 0.2842 0.0312  -0.0337 -0.0026 286 MET A CA  
2305 C C   . MET A 287 ? 0.3469 0.2463 0.3205 0.0385  -0.0368 0.0104  286 MET A C   
2306 O O   . MET A 287 ? 0.3210 0.2250 0.2961 0.0511  -0.0452 0.0170  286 MET A O   
2307 C CB  . MET A 287 ? 0.3013 0.2557 0.3040 0.0331  -0.0426 -0.0050 286 MET A CB  
2308 C CG  . MET A 287 ? 0.2689 0.2349 0.2799 0.0478  -0.0523 -0.0009 286 MET A CG  
2309 S SD  . MET A 287 ? 0.3014 0.2620 0.3256 0.0576  -0.0506 -0.0061 286 MET A SD  
2310 C CE  . MET A 287 ? 0.2783 0.2658 0.3210 0.0485  -0.0479 -0.0206 286 MET A CE  
2311 N N   . GLU A 288 ? 0.3143 0.1903 0.2717 0.0309  -0.0300 0.0141  287 GLU A N   
2312 C CA  . GLU A 288 ? 0.3444 0.2001 0.2844 0.0371  -0.0328 0.0265  287 GLU A CA  
2313 C C   . GLU A 288 ? 0.3769 0.2084 0.3129 0.0493  -0.0323 0.0314  287 GLU A C   
2314 O O   . GLU A 288 ? 0.4016 0.2130 0.3354 0.0461  -0.0236 0.0275  287 GLU A O   
2315 C CB  . GLU A 288 ? 0.3633 0.2015 0.2867 0.0246  -0.0254 0.0287  287 GLU A CB  
2316 C CG  . GLU A 288 ? 0.3824 0.2011 0.2869 0.0299  -0.0286 0.0417  287 GLU A CG  
2317 C CD  . GLU A 288 ? 0.3398 0.1803 0.2441 0.0323  -0.0384 0.0472  287 GLU A CD  
2318 O OE1 . GLU A 288 ? 0.3582 0.2284 0.2774 0.0319  -0.0436 0.0416  287 GLU A OE1 
2319 O OE2 . GLU A 288 ? 0.3777 0.2049 0.2664 0.0345  -0.0407 0.0573  287 GLU A OE2 
2320 N N   . PRO A 289 ? 0.3736 0.2055 0.3077 0.0633  -0.0411 0.0400  288 PRO A N   
2321 C CA  . PRO A 289 ? 0.4031 0.2086 0.3297 0.0753  -0.0405 0.0461  288 PRO A CA  
2322 C C   . PRO A 289 ? 0.5033 0.2748 0.4085 0.0700  -0.0330 0.0522  288 PRO A C   
2323 O O   . PRO A 289 ? 0.4893 0.2591 0.3833 0.0615  -0.0321 0.0559  288 PRO A O   
2324 C CB  . PRO A 289 ? 0.4163 0.2327 0.3434 0.0898  -0.0524 0.0546  288 PRO A CB  
2325 C CG  . PRO A 289 ? 0.3912 0.2427 0.3304 0.0858  -0.0589 0.0509  288 PRO A CG  
2326 C CD  . PRO A 289 ? 0.3847 0.2404 0.3220 0.0686  -0.0518 0.0448  288 PRO A CD  
2327 N N   . ASP A 290 ? 0.5400 0.2836 0.4389 0.0750  -0.0275 0.0533  289 ASP A N   
2328 C CA  . ASP A 290 ? 0.5091 0.2535 0.4207 0.0853  -0.0284 0.0489  289 ASP A CA  
2329 C C   . ASP A 290 ? 0.5840 0.3237 0.5034 0.0757  -0.0183 0.0378  289 ASP A C   
2330 O O   . ASP A 290 ? 0.5968 0.3373 0.5275 0.0827  -0.0180 0.0330  289 ASP A O   
2331 C CB  . ASP A 290 ? 0.6060 0.3213 0.5047 0.0993  -0.0297 0.0581  289 ASP A CB  
2332 C CG  . ASP A 290 ? 0.6702 0.3887 0.5607 0.1102  -0.0398 0.0693  289 ASP A CG  
2333 O OD1 . ASP A 290 ? 0.6221 0.3708 0.5249 0.1142  -0.0487 0.0686  289 ASP A OD1 
2334 O OD2 . ASP A 290 ? 0.9155 0.6076 0.7878 0.1142  -0.0386 0.0784  289 ASP A OD2 
2335 N N   . ASN A 291 ? 0.5225 0.2572 0.4359 0.0598  -0.0099 0.0336  290 ASN A N   
2336 C CA  . ASN A 291 ? 0.5504 0.2737 0.4668 0.0501  0.0011  0.0242  290 ASN A CA  
2337 C C   . ASN A 291 ? 0.4511 0.1994 0.3802 0.0359  0.0046  0.0130  290 ASN A C   
2338 O O   . ASN A 291 ? 0.4743 0.2143 0.4054 0.0263  0.0142  0.0048  290 ASN A O   
2339 C CB  . ASN A 291 ? 0.6069 0.2938 0.5021 0.0438  0.0103  0.0287  290 ASN A CB  
2340 C CG  . ASN A 291 ? 0.7197 0.3781 0.6019 0.0578  0.0084  0.0387  290 ASN A CG  
2341 O OD1 . ASN A 291 ? 0.7520 0.4031 0.6407 0.0673  0.0085  0.0367  290 ASN A OD1 
2342 N ND2 . ASN A 291 ? 0.7155 0.3573 0.5790 0.0594  0.0067  0.0493  290 ASN A ND2 
2343 N N   . GLY A 292 ? 0.4041 0.1822 0.3413 0.0343  -0.0026 0.0122  291 GLY A N   
2344 C CA  . GLY A 292 ? 0.4164 0.2194 0.3668 0.0226  0.0000  0.0010  291 GLY A CA  
2345 C C   . GLY A 292 ? 0.3657 0.1795 0.3343 0.0255  0.0014  -0.0087 291 GLY A C   
2346 O O   . GLY A 292 ? 0.3790 0.1951 0.3551 0.0387  -0.0042 -0.0067 291 GLY A O   
2347 N N   . ILE A 293 ? 0.3759 0.1970 0.3517 0.0132  0.0090  -0.0196 292 ILE A N   
2348 C CA  . ILE A 293 ? 0.3499 0.1782 0.3418 0.0146  0.0119  -0.0295 292 ILE A CA  
2349 C C   . ILE A 293 ? 0.3262 0.1847 0.3354 0.0234  0.0022  -0.0318 292 ILE A C   
2350 O O   . ILE A 293 ? 0.3443 0.2046 0.3645 0.0324  0.0006  -0.0346 292 ILE A O   
2351 C CB  . ILE A 293 ? 0.3937 0.2263 0.3897 -0.0011 0.0216  -0.0410 292 ILE A CB  
2352 C CG1 . ILE A 293 ? 0.4594 0.2594 0.4395 -0.0089 0.0324  -0.0398 292 ILE A CG1 
2353 C CG2 . ILE A 293 ? 0.5753 0.4214 0.5898 0.0003  0.0233  -0.0517 292 ILE A CG2 
2354 C CD1 . ILE A 293 ? 0.6353 0.4396 0.6166 -0.0257 0.0419  -0.0502 292 ILE A CD1 
2355 N N   . ALA A 294 ? 0.2776 0.1604 0.2896 0.0205  -0.0042 -0.0312 293 ALA A N   
2356 C CA  . ALA A 294 ? 0.2434 0.1544 0.2708 0.0285  -0.0134 -0.0332 293 ALA A CA  
2357 C C   . ALA A 294 ? 0.2883 0.1948 0.3129 0.0440  -0.0221 -0.0231 293 ALA A C   
2358 O O   . ALA A 294 ? 0.3046 0.2250 0.3423 0.0537  -0.0277 -0.0250 293 ALA A O   
2359 C CB  . ALA A 294 ? 0.2481 0.1860 0.2787 0.0207  -0.0175 -0.0358 293 ALA A CB  
2360 N N   . TYR A 295 ? 0.2975 0.1849 0.3052 0.0467  -0.0233 -0.0124 294 TYR A N   
2361 C CA  . TYR A 295 ? 0.3032 0.1838 0.3071 0.0620  -0.0310 -0.0027 294 TYR A CA  
2362 C C   . TYR A 295 ? 0.3391 0.2048 0.3480 0.0718  -0.0289 -0.0043 294 TYR A C   
2363 O O   . TYR A 295 ? 0.3490 0.2242 0.3664 0.0847  -0.0362 -0.0024 294 TYR A O   
2364 C CB  . TYR A 295 ? 0.3528 0.2116 0.3361 0.0624  -0.0313 0.0086  294 TYR A CB  
2365 C CG  . TYR A 295 ? 0.3719 0.2239 0.3505 0.0786  -0.0395 0.0188  294 TYR A CG  
2366 C CD1 . TYR A 295 ? 0.3610 0.2360 0.3446 0.0855  -0.0501 0.0228  294 TYR A CD1 
2367 C CD2 . TYR A 295 ? 0.3937 0.2165 0.3630 0.0870  -0.0367 0.0239  294 TYR A CD2 
2368 C CE1 . TYR A 295 ? 0.4124 0.2826 0.3922 0.1004  -0.0578 0.0316  294 TYR A CE1 
2369 C CE2 . TYR A 295 ? 0.4181 0.2353 0.3831 0.1024  -0.0445 0.0328  294 TYR A CE2 
2370 C CZ  . TYR A 295 ? 0.4168 0.2584 0.3875 0.1090  -0.0551 0.0365  294 TYR A CZ  
2371 O OH  . TYR A 295 ? 0.4667 0.3040 0.4334 0.1243  -0.0630 0.0450  294 TYR A OH  
2372 N N   . GLN A 296 ? 0.3255 0.1683 0.3294 0.0658  -0.0187 -0.0080 295 GLN A N   
2373 C CA  . GLN A 296 ? 0.3713 0.1971 0.3785 0.0745  -0.0158 -0.0095 295 GLN A CA  
2374 C C   . GLN A 296 ? 0.3202 0.1673 0.3483 0.0753  -0.0159 -0.0204 295 GLN A C   
2375 O O   . GLN A 296 ? 0.3459 0.1941 0.3821 0.0876  -0.0199 -0.0203 295 GLN A O   
2376 C CB  . GLN A 296 ? 0.4129 0.2061 0.4068 0.0671  -0.0045 -0.0099 295 GLN A CB  
2377 C CG  . GLN A 296 ? 0.5270 0.2917 0.4998 0.0716  -0.0045 0.0019  295 GLN A CG  
2378 C CD  . GLN A 296 ? 0.6918 0.4459 0.6631 0.0894  -0.0107 0.0090  295 GLN A CD  
2379 O OE1 . GLN A 296 ? 0.5624 0.3168 0.5446 0.0965  -0.0104 0.0042  295 GLN A OE1 
2380 N NE2 . GLN A 296 ? 0.6539 0.3993 0.6119 0.0970  -0.0168 0.0204  295 GLN A NE2 
2381 N N   . GLN A 297 ? 0.3137 0.1775 0.3505 0.0625  -0.0116 -0.0301 296 GLN A N   
2382 C CA  . GLN A 297 ? 0.3187 0.1972 0.3734 0.0613  -0.0092 -0.0413 296 GLN A CA  
2383 C C   . GLN A 297 ? 0.3555 0.2699 0.4260 0.0614  -0.0164 -0.0465 296 GLN A C   
2384 O O   . GLN A 297 ? 0.3253 0.2528 0.4111 0.0657  -0.0175 -0.0534 296 GLN A O   
2385 C CB  . GLN A 297 ? 0.3314 0.2004 0.3851 0.0470  0.0024  -0.0501 296 GLN A CB  
2386 C CG  . GLN A 297 ? 0.4184 0.2516 0.4597 0.0474  0.0107  -0.0474 296 GLN A CG  
2387 C CD  . GLN A 297 ? 0.3588 0.1828 0.3994 0.0330  0.0225  -0.0565 296 GLN A CD  
2388 O OE1 . GLN A 297 ? 0.4559 0.2941 0.5110 0.0290  0.0255  -0.0670 296 GLN A OE1 
2389 N NE2 . GLN A 297 ? 0.5367 0.3373 0.5602 0.0252  0.0291  -0.0527 296 GLN A NE2 
2390 N N   . ILE A 298 ? 0.2667 0.1969 0.3336 0.0573  -0.0215 -0.0432 297 ILE A N   
2391 C CA  . ILE A 298 ? 0.2473 0.2108 0.3280 0.0572  -0.0284 -0.0479 297 ILE A CA  
2392 C C   . ILE A 298 ? 0.2619 0.2364 0.3441 0.0703  -0.0394 -0.0401 297 ILE A C   
2393 O O   . ILE A 298 ? 0.2842 0.2805 0.3807 0.0759  -0.0450 -0.0442 297 ILE A O   
2394 C CB  . ILE A 298 ? 0.2320 0.2090 0.3092 0.0438  -0.0270 -0.0507 297 ILE A CB  
2395 C CG1 . ILE A 298 ? 0.2794 0.2514 0.3586 0.0310  -0.0165 -0.0606 297 ILE A CG1 
2396 C CG2 . ILE A 298 ? 0.2090 0.2192 0.2979 0.0447  -0.0351 -0.0539 297 ILE A CG2 
2397 C CD1 . ILE A 298 ? 0.2988 0.2846 0.3957 0.0316  -0.0147 -0.0715 297 ILE A CD1 
2398 N N   . LEU A 299 ? 0.2661 0.2262 0.3339 0.0752  -0.0427 -0.0291 298 LEU A N   
2399 C CA  . LEU A 299 ? 0.2201 0.1919 0.2890 0.0872  -0.0534 -0.0218 298 LEU A CA  
2400 C C   . LEU A 299 ? 0.2622 0.2393 0.3436 0.1002  -0.0574 -0.0237 298 LEU A C   
2401 O O   . LEU A 299 ? 0.2989 0.2992 0.3834 0.0996  -0.0612 -0.0214 298 LEU A O   
2402 C CB  . LEU A 299 ? 0.2893 0.2401 0.3396 0.0915  -0.0554 -0.0095 298 LEU A CB  
2403 C CG  . LEU A 299 ? 0.3194 0.2819 0.3690 0.1034  -0.0665 -0.0012 298 LEU A CG  
2404 C CD1 . LEU A 299 ? 0.3444 0.3383 0.4004 0.0966  -0.0711 -0.0034 298 LEU A CD1 
2405 C CD2 . LEU A 299 ? 0.3760 0.3151 0.4063 0.1072  -0.0675 0.0106  298 LEU A CD2 
2406 N N   . PRO A 300 ? 0.2474 0.2055 0.3302 0.1043  -0.0519 -0.0262 299 PRO A N   
2407 C CA  . PRO A 300 ? 0.3623 0.3301 0.4537 0.1107  -0.0526 -0.0270 299 PRO A CA  
2408 C C   . PRO A 300 ? 0.2939 0.2917 0.3967 0.1018  -0.0518 -0.0341 299 PRO A C   
2409 O O   . PRO A 300 ? 0.3881 0.3985 0.4925 0.1029  -0.0530 -0.0314 299 PRO A O   
2410 C CB  . PRO A 300 ? 0.3596 0.3001 0.4508 0.1147  -0.0459 -0.0304 299 PRO A CB  
2411 C CG  . PRO A 300 ? 0.3436 0.2552 0.4175 0.1117  -0.0418 -0.0247 299 PRO A CG  
2412 C CD  . PRO A 300 ? 0.3601 0.2869 0.4310 0.0992  -0.0421 -0.0254 299 PRO A CD  
2413 N N   . ILE A 301 ? 0.2565 0.2639 0.3658 0.0919  -0.0492 -0.0429 300 ILE A N   
2414 C CA  . ILE A 301 ? 0.3148 0.3458 0.4291 0.0820  -0.0480 -0.0480 300 ILE A CA  
2415 C C   . ILE A 301 ? 0.3405 0.3878 0.4468 0.0753  -0.0512 -0.0433 300 ILE A C   
2416 O O   . ILE A 301 ? 0.3415 0.4005 0.4454 0.0674  -0.0492 -0.0449 300 ILE A O   
2417 C CB  . ILE A 301 ? 0.3307 0.3646 0.4533 0.0725  -0.0423 -0.0592 300 ILE A CB  
2418 C CG1 . ILE A 301 ? 0.2930 0.3331 0.4147 0.0648  -0.0423 -0.0624 300 ILE A CG1 
2419 C CG2 . ILE A 301 ? 0.3629 0.3745 0.4900 0.0769  -0.0359 -0.0635 300 ILE A CG2 
2420 C CD1 . ILE A 301 ? 0.3093 0.3561 0.4375 0.0529  -0.0360 -0.0731 300 ILE A CD1 
2421 N N   . LEU A 302 ? 0.2765 0.3206 0.3757 0.0779  -0.0550 -0.0367 301 LEU A N   
2422 C CA  . LEU A 302 ? 0.2962 0.3524 0.3863 0.0709  -0.0559 -0.0309 301 LEU A CA  
2423 C C   . LEU A 302 ? 0.3772 0.4351 0.4634 0.0754  -0.0574 -0.0222 301 LEU A C   
2424 O O   . LEU A 302 ? 0.2888 0.3551 0.3694 0.0688  -0.0562 -0.0174 301 LEU A O   
2425 C CB  . LEU A 302 ? 0.3043 0.3577 0.3887 0.0696  -0.0587 -0.0280 301 LEU A CB  
2426 C CG  . LEU A 302 ? 0.3221 0.3756 0.4129 0.0641  -0.0570 -0.0376 301 LEU A CG  
2427 C CD1 . LEU A 302 ? 0.2820 0.3339 0.3664 0.0622  -0.0606 -0.0342 301 LEU A CD1 
2428 C CD2 . LEU A 302 ? 0.2921 0.3574 0.3823 0.0517  -0.0507 -0.0440 301 LEU A CD2 
2429 N N   . THR A 303 ? 0.4161 0.4647 0.5057 0.0861  -0.0590 -0.0200 302 THR A N   
2430 C CA  . THR A 303 ? 0.4946 0.5453 0.5828 0.0909  -0.0604 -0.0127 302 THR A CA  
2431 C C   . THR A 303 ? 0.4374 0.5023 0.5254 0.0832  -0.0589 -0.0137 302 THR A C   
2432 O O   . THR A 303 ? 0.3736 0.4421 0.4568 0.0840  -0.0623 -0.0103 302 THR A O   
2433 C CB  . THR A 303 ? 0.4246 0.4636 0.5177 0.1016  -0.0604 -0.0133 302 THR A CB  
2434 O OG1 . THR A 303 ? 0.5001 0.5186 0.5880 0.1105  -0.0622 -0.0093 302 THR A OG1 
2435 C CG2 . THR A 303 ? 0.5700 0.6150 0.6647 0.1050  -0.0612 -0.0084 302 THR A CG2 
2436 N N   . PRO A 304 ? 0.3320 0.4021 0.4226 0.0784  -0.0571 -0.0230 303 PRO A N   
2437 C CA  . PRO A 304 ? 0.4294 0.5077 0.5163 0.0752  -0.0586 -0.0287 303 PRO A CA  
2438 C C   . PRO A 304 ? 0.4124 0.4945 0.4905 0.0691  -0.0584 -0.0293 303 PRO A C   
2439 O O   . PRO A 304 ? 0.4210 0.5080 0.4950 0.0683  -0.0589 -0.0324 303 PRO A O   
2440 C CB  . PRO A 304 ? 0.5006 0.5803 0.5907 0.0710  -0.0559 -0.0384 303 PRO A CB  
2441 C CG  . PRO A 304 ? 0.4224 0.4965 0.5170 0.0693  -0.0529 -0.0386 303 PRO A CG  
2442 C CD  . PRO A 304 ? 0.4020 0.4688 0.4988 0.0770  -0.0533 -0.0286 303 PRO A CD  
2443 N N   . TYR A 305 ? 0.2734 0.3530 0.3484 0.0651  -0.0572 -0.0265 304 TYR A N   
2444 C CA  . TYR A 305 ? 0.3187 0.4009 0.3853 0.0597  -0.0562 -0.0268 304 TYR A CA  
2445 C C   . TYR A 305 ? 0.3265 0.4078 0.3903 0.0625  -0.0594 -0.0175 304 TYR A C   
2446 O O   . TYR A 305 ? 0.4006 0.4831 0.4581 0.0580  -0.0584 -0.0165 304 TYR A O   
2447 C CB  . TYR A 305 ? 0.3001 0.3807 0.3640 0.0525  -0.0522 -0.0310 304 TYR A CB  
2448 C CG  . TYR A 305 ? 0.2688 0.3482 0.3365 0.0502  -0.0494 -0.0394 304 TYR A CG  
2449 C CD1 . TYR A 305 ? 0.2937 0.3749 0.3577 0.0483  -0.0469 -0.0475 304 TYR A CD1 
2450 C CD2 . TYR A 305 ? 0.2264 0.3024 0.3012 0.0505  -0.0488 -0.0392 304 TYR A CD2 
2451 C CE1 . TYR A 305 ? 0.2226 0.3018 0.2892 0.0461  -0.0445 -0.0555 304 TYR A CE1 
2452 C CE2 . TYR A 305 ? 0.2654 0.3402 0.3442 0.0480  -0.0462 -0.0473 304 TYR A CE2 
2453 C CZ  . TYR A 305 ? 0.2729 0.3492 0.3472 0.0456  -0.0444 -0.0554 304 TYR A CZ  
2454 O OH  . TYR A 305 ? 0.2581 0.3324 0.3355 0.0428  -0.0421 -0.0634 304 TYR A OH  
2455 N N   . LEU A 306 ? 0.2713 0.3492 0.3390 0.0701  -0.0627 -0.0108 305 LEU A N   
2456 C CA  . LEU A 306 ? 0.3778 0.4528 0.4418 0.0731  -0.0658 -0.0018 305 LEU A CA  
2457 C C   . LEU A 306 ? 0.5012 0.5796 0.5645 0.0783  -0.0689 0.0001  305 LEU A C   
2458 O O   . LEU A 306 ? 0.4459 0.5286 0.5121 0.0802  -0.0689 -0.0050 305 LEU A O   
2459 C CB  . LEU A 306 ? 0.3574 0.4223 0.4238 0.0788  -0.0664 0.0055  305 LEU A CB  
2460 C CG  . LEU A 306 ? 0.4352 0.4959 0.5019 0.0749  -0.0636 0.0041  305 LEU A CG  
2461 C CD1 . LEU A 306 ? 0.4536 0.4978 0.5201 0.0872  -0.0669 0.0034  305 LEU A CD1 
2462 C CD2 . LEU A 306 ? 0.4458 0.5079 0.5053 0.0682  -0.0639 0.0076  305 LEU A CD2 
2463 O OXT . LEU A 306 ? 0.5350 0.6118 0.5947 0.0805  -0.0717 0.0066  305 LEU A OXT 
2464 N N   . ALA B 2   ? 0.4538 0.6942 0.5241 -0.0356 0.0233  0.0202  1   ALA B N   
2465 C CA  . ALA B 2   ? 0.5557 0.7856 0.6195 -0.0411 0.0251  0.0234  1   ALA B CA  
2466 C C   . ALA B 2   ? 0.4149 0.6292 0.4746 -0.0367 0.0245  0.0227  1   ALA B C   
2467 O O   . ALA B 2   ? 0.4493 0.6588 0.5043 -0.0361 0.0257  0.0249  1   ALA B O   
2468 C CB  . ALA B 2   ? 0.5324 0.7582 0.5949 -0.0498 0.0254  0.0243  1   ALA B CB  
2469 N N   . LYS B 3   ? 0.4572 0.6638 0.5185 -0.0339 0.0226  0.0199  2   LYS B N   
2470 C CA  A LYS B 3   ? 0.3189 0.5119 0.3769 -0.0292 0.0218  0.0191  2   LYS B CA  
2471 C CA  B LYS B 3   ? 0.3190 0.5119 0.3769 -0.0292 0.0219  0.0191  2   LYS B CA  
2472 C C   . LYS B 3   ? 0.2224 0.4198 0.2816 -0.0211 0.0212  0.0185  2   LYS B C   
2473 O O   . LYS B 3   ? 0.3085 0.5180 0.3724 -0.0174 0.0202  0.0171  2   LYS B O   
2474 C CB  A LYS B 3   ? 0.3017 0.4873 0.3616 -0.0278 0.0199  0.0162  2   LYS B CB  
2475 C CB  B LYS B 3   ? 0.3026 0.4879 0.3623 -0.0280 0.0199  0.0163  2   LYS B CB  
2476 C CG  A LYS B 3   ? 0.3539 0.5350 0.4126 -0.0354 0.0202  0.0163  2   LYS B CG  
2477 C CG  B LYS B 3   ? 0.2514 0.4455 0.3177 -0.0231 0.0177  0.0132  2   LYS B CG  
2478 C CD  A LYS B 3   ? 0.3285 0.4935 0.3833 -0.0355 0.0197  0.0154  2   LYS B CD  
2479 C CD  B LYS B 3   ? 0.3609 0.5476 0.4286 -0.0233 0.0159  0.0108  2   LYS B CD  
2480 C CE  A LYS B 3   ? 0.3809 0.5425 0.4349 -0.0425 0.0197  0.0151  2   LYS B CE  
2481 C CE  B LYS B 3   ? 0.3725 0.5681 0.4465 -0.0191 0.0134  0.0079  2   LYS B CE  
2482 N NZ  A LYS B 3   ? 0.2236 0.3964 0.2844 -0.0427 0.0184  0.0130  2   LYS B NZ  
2483 N NZ  B LYS B 3   ? 0.1872 0.3874 0.2625 -0.0116 0.0122  0.0075  2   LYS B NZ  
2484 N N   . VAL B 4   ? 0.2188 0.4059 0.2735 -0.0182 0.0215  0.0195  3   VAL B N   
2485 C CA  . VAL B 4   ? 0.2216 0.4114 0.2767 -0.0107 0.0208  0.0192  3   VAL B CA  
2486 C C   . VAL B 4   ? 0.2682 0.4554 0.3266 -0.0041 0.0181  0.0161  3   VAL B C   
2487 O O   . VAL B 4   ? 0.2143 0.4091 0.2757 0.0018  0.0166  0.0148  3   VAL B O   
2488 C CB  . VAL B 4   ? 0.2083 0.3884 0.2570 -0.0105 0.0223  0.0218  3   VAL B CB  
2489 C CG1 . VAL B 4   ? 0.2260 0.4065 0.2749 -0.0024 0.0212  0.0212  3   VAL B CG1 
2490 C CG2 . VAL B 4   ? 0.2462 0.4318 0.2922 -0.0165 0.0248  0.0250  3   VAL B CG2 
2491 N N   . PHE B 5   ? 0.2099 0.3863 0.2674 -0.0049 0.0171  0.0149  4   PHE B N   
2492 C CA  . PHE B 5   ? 0.1506 0.3233 0.2106 0.0010  0.0145  0.0125  4   PHE B CA  
2493 C C   . PHE B 5   ? 0.2239 0.3995 0.2883 -0.0011 0.0129  0.0101  4   PHE B C   
2494 O O   . PHE B 5   ? 0.2155 0.3921 0.2800 -0.0075 0.0141  0.0105  4   PHE B O   
2495 C CB  . PHE B 5   ? 0.1694 0.3276 0.2250 0.0026  0.0145  0.0130  4   PHE B CB  
2496 C CG  . PHE B 5   ? 0.1735 0.3276 0.2246 0.0050  0.0157  0.0152  4   PHE B CG  
2497 C CD1 . PHE B 5   ? 0.1792 0.3358 0.2312 0.0119  0.0143  0.0149  4   PHE B CD1 
2498 C CD2 . PHE B 5   ? 0.1836 0.3306 0.2292 0.0003  0.0180  0.0177  4   PHE B CD2 
2499 C CE1 . PHE B 5   ? 0.2079 0.3604 0.2556 0.0141  0.0154  0.0170  4   PHE B CE1 
2500 C CE2 . PHE B 5   ? 0.2362 0.3792 0.2775 0.0024  0.0191  0.0199  4   PHE B CE2 
2501 C CZ  . PHE B 5   ? 0.2343 0.3803 0.2769 0.0093  0.0179  0.0195  4   PHE B CZ  
2502 N N   . GLN B 6   ? 0.1737 0.3499 0.2415 0.0041  0.0101  0.0078  5   GLN B N   
2503 C CA  . GLN B 6   ? 0.1749 0.3524 0.2466 0.0024  0.0083  0.0055  5   GLN B CA  
2504 C C   . GLN B 6   ? 0.2445 0.4109 0.3133 -0.0020 0.0093  0.0057  5   GLN B C   
2505 O O   . GLN B 6   ? 0.1869 0.3546 0.2572 -0.0070 0.0095  0.0049  5   GLN B O   
2506 C CB  . GLN B 6   ? 0.1640 0.3425 0.2389 0.0090  0.0049  0.0034  5   GLN B CB  
2507 C CG  . GLN B 6   ? 0.1765 0.3564 0.2555 0.0077  0.0027  0.0011  5   GLN B CG  
2508 C CD  . GLN B 6   ? 0.1909 0.3731 0.2731 0.0139  -0.0011 -0.0007 5   GLN B CD  
2509 O OE1 . GLN B 6   ? 0.2037 0.3858 0.2847 0.0192  -0.0022 -0.0002 5   GLN B OE1 
2510 N NE2 . GLN B 6   ? 0.1991 0.3831 0.2849 0.0130  -0.0034 -0.0027 5   GLN B NE2 
2511 N N   . TRP B 7   ? 0.1467 0.3019 0.2111 0.0000  0.0099  0.0066  6   TRP B N   
2512 C CA  . TRP B 7   ? 0.1378 0.2815 0.1989 -0.0028 0.0105  0.0065  6   TRP B CA  
2513 C C   . TRP B 7   ? 0.1846 0.3188 0.2392 -0.0040 0.0128  0.0089  6   TRP B C   
2514 O O   . TRP B 7   ? 0.2081 0.3413 0.2610 0.0001  0.0129  0.0101  6   TRP B O   
2515 C CB  . TRP B 7   ? 0.1643 0.3027 0.2267 0.0020  0.0083  0.0048  6   TRP B CB  
2516 C CG  . TRP B 7   ? 0.1203 0.2654 0.1883 0.0025  0.0059  0.0024  6   TRP B CG  
2517 C CD1 . TRP B 7   ? 0.1689 0.3169 0.2391 -0.0025 0.0059  0.0012  6   TRP B CD1 
2518 C CD2 . TRP B 7   ? 0.1432 0.2926 0.2151 0.0081  0.0028  0.0010  6   TRP B CD2 
2519 N NE1 . TRP B 7   ? 0.1703 0.3242 0.2456 -0.0002 0.0031  -0.0009 6   TRP B NE1 
2520 C CE2 . TRP B 7   ? 0.1454 0.3002 0.2217 0.0062  0.0010  -0.0010 6   TRP B CE2 
2521 C CE3 . TRP B 7   ? 0.1554 0.3044 0.2272 0.0145  0.0012  0.0013  6   TRP B CE3 
2522 C CZ2 . TRP B 7   ? 0.1399 0.2996 0.2205 0.0102  -0.0024 -0.0027 6   TRP B CZ2 
2523 C CZ3 . TRP B 7   ? 0.1552 0.3088 0.2311 0.0185  -0.0023 -0.0003 6   TRP B CZ3 
2524 C CH2 . TRP B 7   ? 0.1327 0.2915 0.2129 0.0163  -0.0041 -0.0022 6   TRP B CH2 
2525 N N   . PHE B 8   ? 0.1555 0.2823 0.2063 -0.0096 0.0142  0.0096  7   PHE B N   
2526 C CA  . PHE B 8   ? 0.1438 0.2595 0.1877 -0.0108 0.0159  0.0117  7   PHE B CA  
2527 C C   . PHE B 8   ? 0.1978 0.3031 0.2380 -0.0151 0.0163  0.0112  7   PHE B C   
2528 O O   . PHE B 8   ? 0.1776 0.2855 0.2185 -0.0208 0.0167  0.0110  7   PHE B O   
2529 C CB  . PHE B 8   ? 0.1580 0.2780 0.1995 -0.0145 0.0178  0.0145  7   PHE B CB  
2530 C CG  . PHE B 8   ? 0.2271 0.3379 0.2626 -0.0131 0.0189  0.0167  7   PHE B CG  
2531 C CD1 . PHE B 8   ? 0.2191 0.3166 0.2483 -0.0162 0.0197  0.0176  7   PHE B CD1 
2532 C CD2 . PHE B 8   ? 0.2796 0.3944 0.3154 -0.0085 0.0190  0.0178  7   PHE B CD2 
2533 C CE1 . PHE B 8   ? 0.2986 0.3870 0.3220 -0.0148 0.0205  0.0196  7   PHE B CE1 
2534 C CE2 . PHE B 8   ? 0.3374 0.4436 0.3675 -0.0073 0.0200  0.0199  7   PHE B CE2 
2535 C CZ  . PHE B 8   ? 0.2592 0.3521 0.2832 -0.0104 0.0207  0.0208  7   PHE B CZ  
2536 N N   . GLY B 9   ? 0.1595 0.2530 0.1956 -0.0122 0.0162  0.0111  8   GLY B N   
2537 C CA  . GLY B 9   ? 0.1670 0.2507 0.1996 -0.0155 0.0163  0.0101  8   GLY B CA  
2538 C C   . GLY B 9   ? 0.1902 0.2604 0.2172 -0.0121 0.0164  0.0103  8   GLY B C   
2539 O O   . GLY B 9   ? 0.1853 0.2511 0.2088 -0.0099 0.0170  0.0121  8   GLY B O   
2540 N N   . SER B 10  ? 0.1666 0.2302 0.1927 -0.0117 0.0157  0.0083  9   SER B N   
2541 C CA  . SER B 10  ? 0.1744 0.2247 0.1945 -0.0090 0.0159  0.0084  9   SER B CA  
2542 C C   . SER B 10  ? 0.1796 0.2281 0.2019 -0.0049 0.0146  0.0059  9   SER B C   
2543 O O   . SER B 10  ? 0.2038 0.2578 0.2302 -0.0066 0.0138  0.0040  9   SER B O   
2544 C CB  . SER B 10  ? 0.2283 0.2677 0.2410 -0.0149 0.0169  0.0093  9   SER B CB  
2545 O OG  . SER B 10  ? 0.2006 0.2266 0.2070 -0.0118 0.0169  0.0093  9   SER B OG  
2546 N N   . ASN B 11  ? 0.1723 0.2135 0.1920 0.0005  0.0143  0.0059  10  ASN B N   
2547 C CA  . ASN B 11  ? 0.1840 0.2213 0.2040 0.0038  0.0134  0.0038  10  ASN B CA  
2548 C C   . ASN B 11  ? 0.2123 0.2398 0.2267 -0.0003 0.0141  0.0028  10  ASN B C   
2549 O O   . ASN B 11  ? 0.2095 0.2292 0.2177 -0.0043 0.0151  0.0042  10  ASN B O   
2550 C CB  . ASN B 11  ? 0.1755 0.2075 0.1937 0.0106  0.0131  0.0043  10  ASN B CB  
2551 C CG  . ASN B 11  ? 0.1816 0.2235 0.2059 0.0153  0.0118  0.0047  10  ASN B CG  
2552 O OD1 . ASN B 11  ? 0.1637 0.2105 0.1925 0.0185  0.0103  0.0032  10  ASN B OD1 
2553 N ND2 . ASN B 11  ? 0.1795 0.2245 0.2040 0.0156  0.0122  0.0067  10  ASN B ND2 
2554 N N   . GLU B 12  ? 0.1777 0.2057 0.1940 0.0004  0.0133  0.0005  11  GLU B N   
2555 C CA  . GLU B 12  ? 0.1863 0.2053 0.1974 -0.0030 0.0136  -0.0009 11  GLU B CA  
2556 C C   . GLU B 12  ? 0.1976 0.2113 0.2074 0.0027  0.0130  -0.0026 11  GLU B C   
2557 O O   . GLU B 12  ? 0.2062 0.2257 0.2205 0.0040  0.0121  -0.0046 11  GLU B O   
2558 C CB  . GLU B 12  ? 0.1900 0.2161 0.2050 -0.0084 0.0133  -0.0022 11  GLU B CB  
2559 C CG  . GLU B 12  ? 0.2117 0.2412 0.2263 -0.0150 0.0140  -0.0005 11  GLU B CG  
2560 C CD  . GLU B 12  ? 0.2195 0.2367 0.2255 -0.0199 0.0149  0.0006  11  GLU B CD  
2561 O OE1 . GLU B 12  ? 0.2200 0.2260 0.2204 -0.0186 0.0147  -0.0007 11  GLU B OE1 
2562 O OE2 . GLU B 12  ? 0.2183 0.2370 0.2229 -0.0251 0.0155  0.0027  11  GLU B OE2 
2563 N N   . SER B 13  ? 0.1958 0.1988 0.1993 0.0059  0.0135  -0.0019 12  SER B N   
2564 C CA  . SER B 13  ? 0.2029 0.2016 0.2052 0.0127  0.0131  -0.0029 12  SER B CA  
2565 C C   . SER B 13  ? 0.2705 0.2587 0.2666 0.0124  0.0132  -0.0048 12  SER B C   
2566 O O   . SER B 13  ? 0.2528 0.2320 0.2426 0.0077  0.0137  -0.0047 12  SER B O   
2567 C CB  . SER B 13  ? 0.2229 0.2162 0.2219 0.0168  0.0135  -0.0007 12  SER B CB  
2568 O OG  . SER B 13  ? 0.3075 0.2959 0.3045 0.0232  0.0131  -0.0015 12  SER B OG  
2569 N N   . GLY B 14  ? 0.2250 0.2145 0.2228 0.0173  0.0127  -0.0067 13  GLY B N   
2570 C CA  . GLY B 14  ? 0.2220 0.2020 0.2139 0.0181  0.0128  -0.0088 13  GLY B CA  
2571 C C   . GLY B 14  ? 0.2124 0.1987 0.2086 0.0216  0.0121  -0.0110 13  GLY B C   
2572 O O   . GLY B 14  ? 0.2402 0.2200 0.2322 0.0259  0.0121  -0.0124 13  GLY B O   
2573 N N   . ALA B 15  ? 0.1986 0.1978 0.2029 0.0198  0.0113  -0.0113 14  ALA B N   
2574 C CA  . ALA B 15  ? 0.1861 0.1917 0.1945 0.0225  0.0105  -0.0133 14  ALA B CA  
2575 C C   . ALA B 15  ? 0.2340 0.2427 0.2445 0.0298  0.0099  -0.0127 14  ALA B C   
2576 O O   . ALA B 15  ? 0.2048 0.2172 0.2172 0.0329  0.0094  -0.0142 14  ALA B O   
2577 C CB  . ALA B 15  ? 0.1805 0.1987 0.1967 0.0184  0.0095  -0.0137 14  ALA B CB  
2578 N N   . GLU B 16  ? 0.1910 0.1986 0.2012 0.0323  0.0100  -0.0105 15  GLU B N   
2579 C CA  . GLU B 16  ? 0.2045 0.2143 0.2163 0.0391  0.0095  -0.0096 15  GLU B CA  
2580 C C   . GLU B 16  ? 0.2536 0.2510 0.2575 0.0433  0.0104  -0.0094 15  GLU B C   
2581 O O   . GLU B 16  ? 0.2793 0.2775 0.2838 0.0491  0.0100  -0.0084 15  GLU B O   
2582 C CB  . GLU B 16  ? 0.2238 0.2411 0.2408 0.0397  0.0087  -0.0072 15  GLU B CB  
2583 C CG  . GLU B 16  ? 0.1953 0.2054 0.2079 0.0401  0.0096  -0.0050 15  GLU B CG  
2584 C CD  . GLU B 16  ? 0.2118 0.2168 0.2208 0.0337  0.0107  -0.0047 15  GLU B CD  
2585 O OE1 . GLU B 16  ? 0.2232 0.2273 0.2314 0.0290  0.0110  -0.0062 15  GLU B OE1 
2586 O OE2 . GLU B 16  ? 0.2418 0.2439 0.2488 0.0333  0.0112  -0.0026 15  GLU B OE2 
2587 N N   . PHE B 17  ? 0.2570 0.2428 0.2534 0.0405  0.0114  -0.0103 16  PHE B N   
2588 C CA  . PHE B 17  ? 0.2800 0.2527 0.2681 0.0443  0.0120  -0.0102 16  PHE B CA  
2589 C C   . PHE B 17  ? 0.3376 0.3097 0.3246 0.0505  0.0118  -0.0120 16  PHE B C   
2590 O O   . PHE B 17  ? 0.2922 0.2717 0.2832 0.0506  0.0114  -0.0137 16  PHE B O   
2591 C CB  . PHE B 17  ? 0.2786 0.2388 0.2586 0.0394  0.0127  -0.0109 16  PHE B CB  
2592 C CG  . PHE B 17  ? 0.2874 0.2441 0.2655 0.0350  0.0130  -0.0085 16  PHE B CG  
2593 C CD1 . PHE B 17  ? 0.2834 0.2500 0.2680 0.0344  0.0129  -0.0064 16  PHE B CD1 
2594 C CD2 . PHE B 17  ? 0.2697 0.2130 0.2390 0.0316  0.0134  -0.0083 16  PHE B CD2 
2595 C CE1 . PHE B 17  ? 0.2884 0.2525 0.2712 0.0306  0.0134  -0.0042 16  PHE B CE1 
2596 C CE2 . PHE B 17  ? 0.3406 0.2811 0.3080 0.0274  0.0137  -0.0058 16  PHE B CE2 
2597 C CZ  . PHE B 17  ? 0.2656 0.2169 0.2399 0.0269  0.0138  -0.0038 16  PHE B CZ  
2598 N N   . GLY B 18  ? 0.3164 0.2794 0.2975 0.0558  0.0121  -0.0116 17  GLY B N   
2599 C CA  . GLY B 18  ? 0.3396 0.3011 0.3186 0.0621  0.0121  -0.0134 17  GLY B CA  
2600 C C   . GLY B 18  ? 0.3392 0.3151 0.3266 0.0653  0.0113  -0.0133 17  GLY B C   
2601 O O   . GLY B 18  ? 0.3621 0.3413 0.3501 0.0673  0.0112  -0.0154 17  GLY B O   
2602 N N   . SER B 19  ? 0.3606 0.3454 0.3544 0.0658  0.0106  -0.0109 18  SER B N   
2603 C CA  . SER B 19  ? 0.3572 0.3562 0.3595 0.0676  0.0094  -0.0104 18  SER B CA  
2604 C C   . SER B 19  ? 0.3764 0.3778 0.3786 0.0749  0.0091  -0.0105 18  SER B C   
2605 O O   . SER B 19  ? 0.4030 0.4163 0.4118 0.0764  0.0080  -0.0101 18  SER B O   
2606 C CB  . SER B 19  ? 0.3572 0.3633 0.3651 0.0663  0.0085  -0.0078 18  SER B CB  
2607 O OG  . SER B 19  ? 0.5422 0.5417 0.5467 0.0693  0.0089  -0.0058 18  SER B OG  
2608 N N   . GLN B 20  ? 0.3917 0.3825 0.3868 0.0794  0.0100  -0.0109 19  GLN B N   
2609 C CA  . GLN B 20  ? 0.4085 0.4020 0.4033 0.0864  0.0098  -0.0113 19  GLN B CA  
2610 C C   . GLN B 20  ? 0.4539 0.4501 0.4482 0.0868  0.0101  -0.0141 19  GLN B C   
2611 O O   . GLN B 20  ? 0.3947 0.3966 0.3903 0.0922  0.0099  -0.0145 19  GLN B O   
2612 C CB  . GLN B 20  ? 0.4446 0.4258 0.4317 0.0915  0.0106  -0.0109 19  GLN B CB  
2613 C CG  . GLN B 20  ? 0.6098 0.5773 0.5876 0.0915  0.0115  -0.0136 19  GLN B CG  
2614 C CD  . GLN B 20  ? 0.5700 0.5275 0.5433 0.0849  0.0119  -0.0136 19  GLN B CD  
2615 O OE1 . GLN B 20  ? 0.5422 0.5038 0.5198 0.0802  0.0117  -0.0117 19  GLN B OE1 
2616 N NE2 . GLN B 20  ? 0.6528 0.5970 0.6173 0.0846  0.0124  -0.0156 19  GLN B NE2 
2617 N N   . ASN B 21  ? 0.3478 0.3405 0.3402 0.0813  0.0105  -0.0161 20  ASN B N   
2618 C CA  . ASN B 21  ? 0.3327 0.3277 0.3245 0.0810  0.0108  -0.0189 20  ASN B CA  
2619 C C   . ASN B 21  ? 0.3624 0.3695 0.3622 0.0754  0.0098  -0.0188 20  ASN B C   
2620 O O   . ASN B 21  ? 0.3042 0.3093 0.3044 0.0691  0.0099  -0.0190 20  ASN B O   
2621 C CB  . ASN B 21  ? 0.4156 0.3960 0.3981 0.0792  0.0117  -0.0213 20  ASN B CB  
2622 C CG  . ASN B 21  ? 0.5421 0.5112 0.5164 0.0858  0.0123  -0.0220 20  ASN B CG  
2623 O OD1 . ASN B 21  ? 0.5754 0.5302 0.5413 0.0848  0.0127  -0.0230 20  ASN B OD1 
2624 N ND2 . ASN B 21  ? 0.5807 0.5562 0.5572 0.0927  0.0121  -0.0214 20  ASN B ND2 
2625 N N   . LEU B 22  ? 0.3559 0.2832 0.2997 0.0465  0.0427  0.0043  21  LEU B N   
2626 C CA  . LEU B 22  ? 0.3626 0.2999 0.3086 0.0454  0.0399  0.0036  21  LEU B CA  
2627 C C   . LEU B 22  ? 0.5040 0.4407 0.4438 0.0499  0.0415  0.0025  21  LEU B C   
2628 O O   . LEU B 22  ? 0.4764 0.4118 0.4151 0.0557  0.0446  0.0057  21  LEU B O   
2629 C CB  . LEU B 22  ? 0.3517 0.3002 0.3071 0.0463  0.0384  0.0089  21  LEU B CB  
2630 C CG  . LEU B 22  ? 0.2960 0.2463 0.2578 0.0421  0.0366  0.0101  21  LEU B CG  
2631 C CD1 . LEU B 22  ? 0.3335 0.2935 0.3034 0.0435  0.0352  0.0155  21  LEU B CD1 
2632 C CD2 . LEU B 22  ? 0.3499 0.3016 0.3110 0.0361  0.0335  0.0055  21  LEU B CD2 
2633 N N   . PRO B 23  ? 0.3590 0.2969 0.2944 0.0475  0.0395  -0.0018 22  PRO B N   
2634 C CA  . PRO B 23  ? 0.3553 0.2957 0.2917 0.0407  0.0359  -0.0054 22  PRO B CA  
2635 C C   . PRO B 23  ? 0.3070 0.2367 0.2387 0.0362  0.0358  -0.0090 22  PRO B C   
2636 O O   . PRO B 23  ? 0.2956 0.2279 0.2301 0.0305  0.0330  -0.0105 22  PRO B O   
2637 C CB  . PRO B 23  ? 0.3583 0.3017 0.2897 0.0409  0.0347  -0.0084 22  PRO B CB  
2638 C CG  . PRO B 23  ? 0.4008 0.3373 0.3249 0.0467  0.0383  -0.0085 22  PRO B CG  
2639 C CD  . PRO B 23  ? 0.3708 0.3086 0.3000 0.0516  0.0409  -0.0030 22  PRO B CD  
2640 N N   . GLY B 24  ? 0.3261 0.2439 0.2505 0.0387  0.0387  -0.0103 23  GLY B N   
2641 C CA  . GLY B 24  ? 0.3618 0.2685 0.2805 0.0343  0.0383  -0.0140 23  GLY B CA  
2642 C C   . GLY B 24  ? 0.3600 0.2636 0.2712 0.0301  0.0359  -0.0192 23  GLY B C   
2643 O O   . GLY B 24  ? 0.3833 0.2939 0.2941 0.0305  0.0347  -0.0201 23  GLY B O   
2644 N N   . VAL B 25  ? 0.3578 0.2507 0.2628 0.0256  0.0351  -0.0226 24  VAL B N   
2645 C CA  . VAL B 25  ? 0.3776 0.2648 0.2735 0.0215  0.0330  -0.0276 24  VAL B CA  
2646 C C   . VAL B 25  ? 0.3888 0.2764 0.2865 0.0132  0.0293  -0.0291 24  VAL B C   
2647 O O   . VAL B 25  ? 0.3858 0.2674 0.2843 0.0110  0.0295  -0.0285 24  VAL B O   
2648 C CB  . VAL B 25  ? 0.4358 0.3071 0.3193 0.0245  0.0355  -0.0306 24  VAL B CB  
2649 C CG1 . VAL B 25  ? 0.4747 0.3390 0.3479 0.0196  0.0329  -0.0358 24  VAL B CG1 
2650 C CG2 . VAL B 25  ? 0.4990 0.3715 0.3811 0.0331  0.0393  -0.0287 24  VAL B CG2 
2651 N N   . GLU B 26  ? 0.3748 0.2701 0.2733 0.0086  0.0260  -0.0307 25  GLU B N   
2652 C CA  . GLU B 26  ? 0.3909 0.2871 0.2904 0.0006  0.0224  -0.0319 25  GLU B CA  
2653 C C   . GLU B 26  ? 0.3813 0.2618 0.2701 -0.0029 0.0220  -0.0353 25  GLU B C   
2654 O O   . GLU B 26  ? 0.4213 0.2912 0.2996 -0.0008 0.0231  -0.0383 25  GLU B O   
2655 C CB  . GLU B 26  ? 0.3566 0.2630 0.2574 -0.0032 0.0192  -0.0331 25  GLU B CB  
2656 C CG  . GLU B 26  ? 0.3562 0.2674 0.2602 -0.0112 0.0154  -0.0333 25  GLU B CG  
2657 C CD  . GLU B 26  ? 0.3873 0.2865 0.2809 -0.0171 0.0133  -0.0369 25  GLU B CD  
2658 O OE1 . GLU B 26  ? 0.4540 0.3446 0.3376 -0.0161 0.0138  -0.0400 25  GLU B OE1 
2659 O OE2 . GLU B 26  ? 0.4481 0.3462 0.3432 -0.0228 0.0112  -0.0364 25  GLU B OE2 
2660 N N   . GLY B 27  ? 0.3832 0.2618 0.2745 -0.0082 0.0202  -0.0348 26  GLY B N   
2661 C CA  . GLY B 27  ? 0.3792 0.2428 0.2612 -0.0121 0.0193  -0.0374 26  GLY B CA  
2662 C C   . GLY B 27  ? 0.4230 0.2747 0.3019 -0.0072 0.0228  -0.0367 26  GLY B C   
2663 O O   . GLY B 27  ? 0.4848 0.3236 0.3567 -0.0104 0.0220  -0.0385 26  GLY B O   
2664 N N   . LYS B 28  ? 0.3962 0.2516 0.2797 0.0003  0.0265  -0.0341 27  LYS B N   
2665 C CA  A LYS B 28  ? 0.4579 0.3039 0.3400 0.0055  0.0301  -0.0326 27  LYS B CA  
2666 C CA  B LYS B 28  ? 0.4580 0.3040 0.3401 0.0055  0.0301  -0.0326 27  LYS B CA  
2667 C CA  C LYS B 28  ? 0.4582 0.3041 0.3403 0.0055  0.0301  -0.0326 27  LYS B CA  
2668 C C   . LYS B 28  ? 0.4166 0.2721 0.3111 0.0073  0.0314  -0.0278 27  LYS B C   
2669 O O   . LYS B 28  ? 0.4515 0.3025 0.3481 0.0052  0.0315  -0.0265 27  LYS B O   
2670 C CB  A LYS B 28  ? 0.5110 0.3514 0.3861 0.0134  0.0337  -0.0335 27  LYS B CB  
2671 C CB  B LYS B 28  ? 0.5108 0.3510 0.3859 0.0134  0.0338  -0.0335 27  LYS B CB  
2672 C CB  C LYS B 28  ? 0.5104 0.3507 0.3856 0.0133  0.0338  -0.0335 27  LYS B CB  
2673 C CG  A LYS B 28  ? 0.5308 0.3638 0.4054 0.0202  0.0381  -0.0312 27  LYS B CG  
2674 C CG  B LYS B 28  ? 0.5338 0.3647 0.4073 0.0195  0.0379  -0.0316 27  LYS B CG  
2675 C CG  C LYS B 28  ? 0.5344 0.3642 0.4069 0.0192  0.0378  -0.0320 27  LYS B CG  
2676 C CD  A LYS B 28  ? 0.6032 0.4176 0.4664 0.0196  0.0388  -0.0342 27  LYS B CD  
2677 C CD  B LYS B 28  ? 0.5244 0.3476 0.3886 0.0270  0.0414  -0.0331 27  LYS B CD  
2678 C CD  C LYS B 28  ? 0.5241 0.3492 0.3894 0.0272  0.0414  -0.0327 27  LYS B CD  
2679 C CE  A LYS B 28  ? 0.4750 0.2785 0.3242 0.0206  0.0386  -0.0391 27  LYS B CE  
2680 C CE  B LYS B 28  ? 0.5071 0.3438 0.3774 0.0324  0.0431  -0.0303 27  LYS B CE  
2681 C CE  C LYS B 28  ? 0.5170 0.3302 0.3783 0.0329  0.0454  -0.0315 27  LYS B CE  
2682 N NZ  A LYS B 28  ? 0.6071 0.3912 0.4445 0.0198  0.0389  -0.0421 27  LYS B NZ  
2683 N NZ  B LYS B 28  ? 0.4868 0.3174 0.3482 0.0397  0.0464  -0.0316 27  LYS B NZ  
2684 N NZ  C LYS B 28  ? 0.5286 0.3487 0.4014 0.0343  0.0469  -0.0263 27  LYS B NZ  
2685 N N   . ASP B 29  ? 0.3709 0.2395 0.2734 0.0110  0.0322  -0.0249 28  ASP B N   
2686 C CA  . ASP B 29  ? 0.3270 0.2046 0.2407 0.0125  0.0331  -0.0202 28  ASP B CA  
2687 C C   . ASP B 29  ? 0.3437 0.2325 0.2654 0.0066  0.0296  -0.0193 28  ASP B C   
2688 O O   . ASP B 29  ? 0.3715 0.2644 0.3009 0.0058  0.0297  -0.0162 28  ASP B O   
2689 C CB  . ASP B 29  ? 0.3807 0.2664 0.2987 0.0194  0.0355  -0.0172 28  ASP B CB  
2690 C CG  . ASP B 29  ? 0.4599 0.3362 0.3706 0.0261  0.0393  -0.0173 28  ASP B CG  
2691 O OD1 . ASP B 29  ? 0.4992 0.3677 0.4093 0.0284  0.0418  -0.0157 28  ASP B OD1 
2692 O OD2 . ASP B 29  ? 0.4213 0.2982 0.3269 0.0291  0.0398  -0.0190 28  ASP B OD2 
2693 N N   . TYR B 30  ? 0.3156 0.2098 0.2359 0.0026  0.0266  -0.0217 29  TYR B N   
2694 C CA  . TYR B 30  ? 0.3056 0.2117 0.2338 -0.0022 0.0236  -0.0205 29  TYR B CA  
2695 C C   . TYR B 30  ? 0.3304 0.2361 0.2533 -0.0086 0.0202  -0.0240 29  TYR B C   
2696 O O   . TYR B 30  ? 0.3487 0.2460 0.2622 -0.0088 0.0201  -0.0273 29  TYR B O   
2697 C CB  . TYR B 30  ? 0.2732 0.1927 0.2093 0.0015  0.0238  -0.0177 29  TYR B CB  
2698 C CG  . TYR B 30  ? 0.3020 0.2244 0.2344 0.0042  0.0237  -0.0193 29  TYR B CG  
2699 C CD1 . TYR B 30  ? 0.2913 0.2201 0.2229 0.0002  0.0207  -0.0214 29  TYR B CD1 
2700 C CD2 . TYR B 30  ? 0.2804 0.1997 0.2102 0.0109  0.0267  -0.0184 29  TYR B CD2 
2701 C CE1 . TYR B 30  ? 0.2672 0.1989 0.1954 0.0025  0.0206  -0.0228 29  TYR B CE1 
2702 C CE2 . TYR B 30  ? 0.2900 0.2127 0.2165 0.0133  0.0266  -0.0198 29  TYR B CE2 
2703 C CZ  . TYR B 30  ? 0.2635 0.1923 0.1893 0.0090  0.0235  -0.0221 29  TYR B CZ  
2704 O OH  . TYR B 30  ? 0.2870 0.2191 0.2097 0.0113  0.0234  -0.0233 29  TYR B OH  
2705 N N   . ILE B 31  ? 0.2895 0.2044 0.2183 -0.0138 0.0173  -0.0231 30  ILE B N   
2706 C CA  . ILE B 31  ? 0.2630 0.1795 0.1881 -0.0204 0.0137  -0.0255 30  ILE B CA  
2707 C C   . ILE B 31  ? 0.2622 0.1943 0.1965 -0.0229 0.0115  -0.0233 30  ILE B C   
2708 O O   . ILE B 31  ? 0.2811 0.2198 0.2237 -0.0213 0.0122  -0.0203 30  ILE B O   
2709 C CB  . ILE B 31  ? 0.3320 0.2376 0.2514 -0.0262 0.0122  -0.0270 30  ILE B CB  
2710 C CG1 . ILE B 31  ? 0.3761 0.2807 0.2888 -0.0328 0.0086  -0.0298 30  ILE B CG1 
2711 C CG2 . ILE B 31  ? 0.3555 0.2661 0.2830 -0.0287 0.0117  -0.0239 30  ILE B CG2 
2712 C CD1 . ILE B 31  ? 0.5201 0.4122 0.4253 -0.0386 0.0067  -0.0314 30  ILE B CD1 
2713 N N   . TRP B 32  ? 0.2965 0.2345 0.2292 -0.0266 0.0087  -0.0248 31  TRP B N   
2714 C CA  . TRP B 32  ? 0.2559 0.2089 0.1969 -0.0287 0.0067  -0.0228 31  TRP B CA  
2715 C C   . TRP B 32  ? 0.2864 0.2412 0.2284 -0.0358 0.0039  -0.0223 31  TRP B C   
2716 O O   . TRP B 32  ? 0.2851 0.2296 0.2202 -0.0401 0.0029  -0.0240 31  TRP B O   
2717 C CB  . TRP B 32  ? 0.2778 0.2377 0.2174 -0.0285 0.0052  -0.0241 31  TRP B CB  
2718 C CG  . TRP B 32  ? 0.2197 0.1817 0.1611 -0.0213 0.0076  -0.0235 31  TRP B CG  
2719 C CD1 . TRP B 32  ? 0.2693 0.2227 0.2041 -0.0173 0.0097  -0.0252 31  TRP B CD1 
2720 C CD2 . TRP B 32  ? 0.2680 0.2412 0.2181 -0.0172 0.0081  -0.0205 31  TRP B CD2 
2721 N NE1 . TRP B 32  ? 0.2673 0.2266 0.2066 -0.0112 0.0114  -0.0233 31  TRP B NE1 
2722 C CE2 . TRP B 32  ? 0.2396 0.2107 0.1882 -0.0112 0.0103  -0.0205 31  TRP B CE2 
2723 C CE3 . TRP B 32  ? 0.2272 0.2117 0.1859 -0.0179 0.0069  -0.0179 31  TRP B CE3 
2724 C CZ2 . TRP B 32  ? 0.2263 0.2061 0.1816 -0.0064 0.0109  -0.0177 31  TRP B CZ2 
2725 C CZ3 . TRP B 32  ? 0.2121 0.2044 0.1770 -0.0128 0.0076  -0.0155 31  TRP B CZ3 
2726 C CH2 . TRP B 32  ? 0.1834 0.1732 0.1465 -0.0074 0.0094  -0.0154 31  TRP B CH2 
2727 N N   . PRO B 33  ? 0.2505 0.2182 0.2009 -0.0371 0.0026  -0.0197 32  PRO B N   
2728 C CA  . PRO B 33  ? 0.2552 0.2263 0.2075 -0.0437 0.0002  -0.0185 32  PRO B CA  
2729 C C   . PRO B 33  ? 0.2595 0.2290 0.2053 -0.0504 -0.0031 -0.0204 32  PRO B C   
2730 O O   . PRO B 33  ? 0.2983 0.2686 0.2402 -0.0502 -0.0038 -0.0223 32  PRO B O   
2731 C CB  . PRO B 33  ? 0.2526 0.2392 0.2147 -0.0424 -0.0003 -0.0156 32  PRO B CB  
2732 C CG  . PRO B 33  ? 0.2062 0.1936 0.1721 -0.0347 0.0026  -0.0146 32  PRO B CG  
2733 C CD  . PRO B 33  ? 0.2358 0.2148 0.1945 -0.0321 0.0037  -0.0173 32  PRO B CD  
2734 N N   . ASP B 34  ? 0.2684 0.2360 0.2131 -0.0567 -0.0053 -0.0197 33  ASP B N   
2735 C CA  . ASP B 34  ? 0.2769 0.2426 0.2153 -0.0642 -0.0089 -0.0209 33  ASP B CA  
2736 C C   . ASP B 34  ? 0.3566 0.3391 0.3018 -0.0676 -0.0114 -0.0183 33  ASP B C   
2737 O O   . ASP B 34  ? 0.2640 0.2546 0.2160 -0.0692 -0.0119 -0.0154 33  ASP B O   
2738 C CB  . ASP B 34  ? 0.3172 0.2723 0.2510 -0.0695 -0.0103 -0.0209 33  ASP B CB  
2739 C CG  . ASP B 34  ? 0.3156 0.2666 0.2416 -0.0777 -0.0143 -0.0220 33  ASP B CG  
2740 O OD1 . ASP B 34  ? 0.3682 0.3277 0.2942 -0.0802 -0.0164 -0.0220 33  ASP B OD1 
2741 O OD2 . ASP B 34  ? 0.3457 0.2846 0.2653 -0.0818 -0.0156 -0.0228 33  ASP B OD2 
2742 N N   . PRO B 35  ? 0.2983 0.2866 0.2417 -0.0688 -0.0129 -0.0191 34  PRO B N   
2743 C CA  . PRO B 35  ? 0.2888 0.2938 0.2391 -0.0715 -0.0151 -0.0163 34  PRO B CA  
2744 C C   . PRO B 35  ? 0.2987 0.3067 0.2490 -0.0795 -0.0184 -0.0141 34  PRO B C   
2745 O O   . PRO B 35  ? 0.2894 0.3117 0.2472 -0.0809 -0.0194 -0.0108 34  PRO B O   
2746 C CB  . PRO B 35  ? 0.3128 0.3204 0.2593 -0.0719 -0.0163 -0.0181 34  PRO B CB  
2747 C CG  . PRO B 35  ? 0.3362 0.3270 0.2717 -0.0727 -0.0161 -0.0218 34  PRO B CG  
2748 C CD  . PRO B 35  ? 0.2819 0.2623 0.2171 -0.0677 -0.0128 -0.0225 34  PRO B CD  
2749 N N   . ASN B 36  ? 0.3064 0.3013 0.2483 -0.0848 -0.0200 -0.0157 35  ASN B N   
2750 C CA  . ASN B 36  ? 0.3119 0.3094 0.2531 -0.0932 -0.0237 -0.0133 35  ASN B CA  
2751 C C   . ASN B 36  ? 0.3507 0.3522 0.2990 -0.0928 -0.0228 -0.0104 35  ASN B C   
2752 O O   . ASN B 36  ? 0.3126 0.3255 0.2659 -0.0973 -0.0250 -0.0068 35  ASN B O   
2753 C CB  . ASN B 36  ? 0.4208 0.4019 0.3501 -0.0990 -0.0261 -0.0159 35  ASN B CB  
2754 C CG  . ASN B 36  ? 0.5040 0.4822 0.4258 -0.1007 -0.0277 -0.0184 35  ASN B CG  
2755 O OD1 . ASN B 36  ? 0.5797 0.5710 0.5054 -0.1018 -0.0290 -0.0169 35  ASN B OD1 
2756 N ND2 . ASN B 36  ? 0.7103 0.6711 0.6211 -0.1008 -0.0275 -0.0223 35  ASN B ND2 
2757 N N   . THR B 37  ? 0.2920 0.2848 0.2409 -0.0873 -0.0195 -0.0116 36  THR B N   
2758 C CA  . THR B 37  ? 0.2671 0.2641 0.2231 -0.0866 -0.0184 -0.0087 36  THR B CA  
2759 C C   . THR B 37  ? 0.3106 0.3236 0.2770 -0.0815 -0.0166 -0.0062 36  THR B C   
2760 O O   . THR B 37  ? 0.2637 0.2858 0.2366 -0.0828 -0.0170 -0.0030 36  THR B O   
2761 C CB  . THR B 37  ? 0.2922 0.2747 0.2455 -0.0830 -0.0157 -0.0104 36  THR B CB  
2762 O OG1 . THR B 37  ? 0.2809 0.2609 0.2350 -0.0748 -0.0120 -0.0122 36  THR B OG1 
2763 C CG2 . THR B 37  ? 0.3219 0.2874 0.2641 -0.0878 -0.0175 -0.0130 36  THR B CG2 
2764 N N   . ILE B 38  ? 0.2834 0.2999 0.2511 -0.0757 -0.0149 -0.0075 37  ILE B N   
2765 C CA  . ILE B 38  ? 0.2417 0.2737 0.2182 -0.0716 -0.0139 -0.0051 37  ILE B CA  
2766 C C   . ILE B 38  ? 0.2952 0.3411 0.2748 -0.0772 -0.0170 -0.0023 37  ILE B C   
2767 O O   . ILE B 38  ? 0.2731 0.3311 0.2601 -0.0762 -0.0168 0.0009  37  ILE B O   
2768 C CB  . ILE B 38  ? 0.2526 0.2856 0.2292 -0.0652 -0.0121 -0.0070 37  ILE B CB  
2769 C CG1 . ILE B 38  ? 0.2743 0.2972 0.2504 -0.0588 -0.0087 -0.0084 37  ILE B CG1 
2770 C CG2 . ILE B 38  ? 0.2466 0.2961 0.2312 -0.0621 -0.0121 -0.0045 37  ILE B CG2 
2771 C CD1 . ILE B 38  ? 0.2818 0.3039 0.2568 -0.0530 -0.0071 -0.0103 37  ILE B CD1 
2772 N N   . ASP B 39  ? 0.2679 0.3123 0.2417 -0.0829 -0.0200 -0.0031 38  ASP B N   
2773 C CA  . ASP B 39  ? 0.2380 0.2955 0.2144 -0.0889 -0.0232 0.0001  38  ASP B CA  
2774 C C   . ASP B 39  ? 0.3040 0.3657 0.2840 -0.0932 -0.0244 0.0034  38  ASP B C   
2775 O O   . ASP B 39  ? 0.2799 0.3568 0.2665 -0.0942 -0.0253 0.0072  38  ASP B O   
2776 C CB  . ASP B 39  ? 0.2909 0.3431 0.2590 -0.0956 -0.0265 -0.0014 38  ASP B CB  
2777 C CG  . ASP B 39  ? 0.4842 0.5387 0.4507 -0.0926 -0.0261 -0.0034 38  ASP B CG  
2778 O OD1 . ASP B 39  ? 0.5042 0.5657 0.4764 -0.0856 -0.0236 -0.0033 38  ASP B OD1 
2779 O OD2 . ASP B 39  ? 0.5148 0.5636 0.4738 -0.0975 -0.0285 -0.0050 38  ASP B OD2 
2780 N N   . THR B 40  ? 0.2565 0.3048 0.2320 -0.0955 -0.0244 0.0023  39  THR B N   
2781 C CA  . THR B 40  ? 0.2360 0.2874 0.2148 -0.0996 -0.0256 0.0055  39  THR B CA  
2782 C C   . THR B 40  ? 0.3095 0.3713 0.2977 -0.0936 -0.0227 0.0078  39  THR B C   
2783 O O   . THR B 40  ? 0.2543 0.3289 0.2483 -0.0960 -0.0238 0.0117  39  THR B O   
2784 C CB  . THR B 40  ? 0.2561 0.2897 0.2280 -0.1025 -0.0259 0.0034  39  THR B CB  
2785 O OG1 . THR B 40  ? 0.3037 0.3283 0.2663 -0.1089 -0.0292 0.0017  39  THR B OG1 
2786 C CG2 . THR B 40  ? 0.3162 0.3527 0.2920 -0.1063 -0.0269 0.0067  39  THR B CG2 
2787 N N   . LEU B 41  ? 0.2434 0.3000 0.2329 -0.0859 -0.0191 0.0056  40  LEU B N   
2788 C CA  . LEU B 41  ? 0.2000 0.2656 0.1976 -0.0801 -0.0165 0.0077  40  LEU B CA  
2789 C C   . LEU B 41  ? 0.2491 0.3320 0.2526 -0.0781 -0.0169 0.0101  40  LEU B C   
2790 O O   . LEU B 41  ? 0.2285 0.3222 0.2384 -0.0761 -0.0161 0.0130  40  LEU B O   
2791 C CB  . LEU B 41  ? 0.2308 0.2869 0.2280 -0.0726 -0.0130 0.0051  40  LEU B CB  
2792 C CG  . LEU B 41  ? 0.2082 0.2485 0.2011 -0.0735 -0.0120 0.0034  40  LEU B CG  
2793 C CD1 . LEU B 41  ? 0.2295 0.2618 0.2224 -0.0658 -0.0084 0.0015  40  LEU B CD1 
2794 C CD2 . LEU B 41  ? 0.2070 0.2499 0.2037 -0.0767 -0.0124 0.0063  40  LEU B CD2 
2795 N N   . ILE B 42  ? 0.2211 0.3070 0.2222 -0.0784 -0.0180 0.0089  41  ILE B N   
2796 C CA  . ILE B 42  ? 0.2149 0.3174 0.2214 -0.0767 -0.0185 0.0114  41  ILE B CA  
2797 C C   . ILE B 42  ? 0.2249 0.3391 0.2341 -0.0833 -0.0213 0.0156  41  ILE B C   
2798 O O   . ILE B 42  ? 0.2484 0.3773 0.2641 -0.0812 -0.0209 0.0189  41  ILE B O   
2799 C CB  . ILE B 42  ? 0.2150 0.3175 0.2184 -0.0757 -0.0192 0.0093  41  ILE B CB  
2800 C CG1 . ILE B 42  ? 0.1973 0.2921 0.2001 -0.0680 -0.0162 0.0062  41  ILE B CG1 
2801 C CG2 . ILE B 42  ? 0.2113 0.3314 0.2198 -0.0756 -0.0204 0.0123  41  ILE B CG2 
2802 C CD1 . ILE B 42  ? 0.2657 0.3575 0.2642 -0.0674 -0.0168 0.0035  41  ILE B CD1 
2803 N N   . SER B 43  ? 0.2562 0.3642 0.2602 -0.0912 -0.0242 0.0157  42  SER B N   
2804 C CA  A SER B 43  ? 0.2270 0.3459 0.2333 -0.0981 -0.0272 0.0201  42  SER B CA  
2805 C CA  B SER B 43  ? 0.2278 0.3466 0.2341 -0.0982 -0.0272 0.0201  42  SER B CA  
2806 C C   . SER B 43  ? 0.2680 0.3920 0.2800 -0.0971 -0.0260 0.0229  42  SER B C   
2807 O O   . SER B 43  ? 0.2771 0.4152 0.2937 -0.1000 -0.0275 0.0274  42  SER B O   
2808 C CB  A SER B 43  ? 0.2446 0.3537 0.2432 -0.1072 -0.0309 0.0195  42  SER B CB  
2809 C CB  B SER B 43  ? 0.2459 0.3544 0.2444 -0.1072 -0.0309 0.0194  42  SER B CB  
2810 O OG  A SER B 43  ? 0.2706 0.3672 0.2662 -0.1096 -0.0309 0.0186  42  SER B OG  
2811 O OG  B SER B 43  ? 0.2528 0.3577 0.2458 -0.1087 -0.0322 0.0171  42  SER B OG  
2812 N N   . LYS B 44  ? 0.2437 0.3570 0.2555 -0.0928 -0.0233 0.0207  43  LYS B N   
2813 C CA  . LYS B 44  ? 0.2602 0.3781 0.2775 -0.0911 -0.0218 0.0232  43  LYS B CA  
2814 C C   . LYS B 44  ? 0.3568 0.4869 0.3809 -0.0833 -0.0191 0.0246  43  LYS B C   
2815 O O   . LYS B 44  ? 0.2784 0.4146 0.3072 -0.0816 -0.0180 0.0270  43  LYS B O   
2816 C CB  . LYS B 44  ? 0.2611 0.3627 0.2755 -0.0898 -0.0201 0.0205  43  LYS B CB  
2817 C CG  . LYS B 44  ? 0.3238 0.4123 0.3311 -0.0972 -0.0227 0.0193  43  LYS B CG  
2818 C CD  . LYS B 44  ? 0.4396 0.5369 0.4486 -0.1052 -0.0262 0.0236  43  LYS B CD  
2819 C CE  . LYS B 44  ? 0.5396 0.6224 0.5426 -0.1118 -0.0284 0.0228  43  LYS B CE  
2820 N NZ  . LYS B 44  ? 0.5611 0.6521 0.5677 -0.1178 -0.0309 0.0274  43  LYS B NZ  
2821 N N   . GLY B 45  ? 0.2348 0.3682 0.2589 -0.0786 -0.0182 0.0231  44  GLY B N   
2822 C CA  . GLY B 45  ? 0.2371 0.3814 0.2668 -0.0711 -0.0160 0.0243  44  GLY B CA  
2823 C C   . GLY B 45  ? 0.2818 0.4173 0.3109 -0.0633 -0.0130 0.0210  44  GLY B C   
2824 O O   . GLY B 45  ? 0.2462 0.3891 0.2792 -0.0569 -0.0113 0.0218  44  GLY B O   
2825 N N   . MET B 46  ? 0.1996 0.3196 0.2236 -0.0635 -0.0125 0.0175  45  MET B N   
2826 C CA  . MET B 46  ? 0.1979 0.3106 0.2216 -0.0562 -0.0098 0.0150  45  MET B CA  
2827 C C   . MET B 46  ? 0.2337 0.3500 0.2566 -0.0532 -0.0101 0.0136  45  MET B C   
2828 O O   . MET B 46  ? 0.2231 0.3405 0.2430 -0.0576 -0.0122 0.0131  45  MET B O   
2829 C CB  . MET B 46  ? 0.1671 0.2627 0.1859 -0.0570 -0.0089 0.0121  45  MET B CB  
2830 C CG  . MET B 46  ? 0.1935 0.2851 0.2139 -0.0587 -0.0082 0.0135  45  MET B CG  
2831 S SD  . MET B 46  ? 0.2335 0.3052 0.2483 -0.0584 -0.0067 0.0103  45  MET B SD  
2832 C CE  . MET B 46  ? 0.2947 0.3647 0.3132 -0.0587 -0.0054 0.0126  45  MET B CE  
2833 N N   . ASN B 47  ? 0.1883 0.3067 0.2136 -0.0459 -0.0083 0.0132  46  ASN B N   
2834 C CA  . ASN B 47  ? 0.1840 0.3074 0.2093 -0.0427 -0.0087 0.0124  46  ASN B CA  
2835 C C   . ASN B 47  ? 0.1727 0.2873 0.1964 -0.0367 -0.0070 0.0099  46  ASN B C   
2836 O O   . ASN B 47  ? 0.1872 0.3065 0.2118 -0.0327 -0.0071 0.0096  46  ASN B O   
2837 C CB  . ASN B 47  ? 0.2304 0.3695 0.2608 -0.0398 -0.0089 0.0154  46  ASN B CB  
2838 C CG  . ASN B 47  ? 0.2421 0.3822 0.2757 -0.0331 -0.0068 0.0162  46  ASN B CG  
2839 O OD1 . ASN B 47  ? 0.2512 0.3817 0.2838 -0.0319 -0.0053 0.0153  46  ASN B OD1 
2840 N ND2 . ASN B 47  ? 0.2677 0.4189 0.3045 -0.0286 -0.0066 0.0179  46  ASN B ND2 
2841 N N   . ILE B 48  ? 0.1553 0.2577 0.1768 -0.0358 -0.0055 0.0086  47  ILE B N   
2842 C CA  . ILE B 48  ? 0.1791 0.2732 0.1989 -0.0305 -0.0040 0.0067  47  ILE B CA  
2843 C C   . ILE B 48  ? 0.1635 0.2434 0.1789 -0.0325 -0.0031 0.0048  47  ILE B C   
2844 O O   . ILE B 48  ? 0.1860 0.2619 0.2013 -0.0357 -0.0028 0.0054  47  ILE B O   
2845 C CB  . ILE B 48  ? 0.1667 0.2633 0.1903 -0.0241 -0.0025 0.0082  47  ILE B CB  
2846 C CG1 . ILE B 48  ? 0.1804 0.2700 0.2024 -0.0188 -0.0016 0.0068  47  ILE B CG1 
2847 C CG2 . ILE B 48  ? 0.1758 0.2694 0.2010 -0.0250 -0.0014 0.0096  47  ILE B CG2 
2848 C CD1 . ILE B 48  ? 0.1609 0.2534 0.1859 -0.0127 -0.0008 0.0084  47  ILE B CD1 
2849 N N   . PHE B 49  ? 0.1763 0.2489 0.1880 -0.0306 -0.0027 0.0025  48  PHE B N   
2850 C CA  . PHE B 49  ? 0.1711 0.2302 0.1781 -0.0318 -0.0016 0.0006  48  PHE B CA  
2851 C C   . PHE B 49  ? 0.1936 0.2471 0.2000 -0.0258 0.0000  -0.0001 48  PHE B C   
2852 O O   . PHE B 49  ? 0.1874 0.2444 0.1934 -0.0232 -0.0005 -0.0008 48  PHE B O   
2853 C CB  . PHE B 49  ? 0.1727 0.2278 0.1742 -0.0373 -0.0033 -0.0015 48  PHE B CB  
2854 C CG  . PHE B 49  ? 0.1696 0.2304 0.1718 -0.0437 -0.0053 -0.0001 48  PHE B CG  
2855 C CD1 . PHE B 49  ? 0.1860 0.2399 0.1867 -0.0476 -0.0053 0.0002  48  PHE B CD1 
2856 C CD2 . PHE B 49  ? 0.2155 0.2892 0.2206 -0.0456 -0.0072 0.0014  48  PHE B CD2 
2857 C CE1 . PHE B 49  ? 0.1920 0.2517 0.1938 -0.0536 -0.0073 0.0020  48  PHE B CE1 
2858 C CE2 . PHE B 49  ? 0.2188 0.2990 0.2251 -0.0514 -0.0091 0.0034  48  PHE B CE2 
2859 C CZ  . PHE B 49  ? 0.1873 0.2604 0.1918 -0.0556 -0.0093 0.0037  48  PHE B CZ  
2860 N N   . ARG B 50  ? 0.1750 0.2206 0.1815 -0.0235 0.0020  0.0004  49  ARG B N   
2861 C CA  . ARG B 50  ? 0.1557 0.1961 0.1618 -0.0179 0.0036  0.0004  49  ARG B CA  
2862 C C   . ARG B 50  ? 0.1614 0.1904 0.1619 -0.0186 0.0046  -0.0016 49  ARG B C   
2863 O O   . ARG B 50  ? 0.1739 0.1953 0.1720 -0.0216 0.0053  -0.0022 49  ARG B O   
2864 C CB  . ARG B 50  ? 0.1598 0.1989 0.1696 -0.0149 0.0050  0.0028  49  ARG B CB  
2865 C CG  . ARG B 50  ? 0.1365 0.1708 0.1462 -0.0094 0.0064  0.0036  49  ARG B CG  
2866 C CD  . ARG B 50  ? 0.1475 0.1841 0.1612 -0.0064 0.0069  0.0063  49  ARG B CD  
2867 N NE  . ARG B 50  ? 0.1448 0.1764 0.1585 -0.0018 0.0080  0.0077  49  ARG B NE  
2868 C CZ  . ARG B 50  ? 0.1926 0.2164 0.2061 -0.0011 0.0098  0.0090  49  ARG B CZ  
2869 N NH1 . ARG B 50  ? 0.1579 0.1762 0.1702 -0.0046 0.0108  0.0084  49  ARG B NH1 
2870 N NH2 . ARG B 50  ? 0.1656 0.1869 0.1799 0.0030  0.0103  0.0112  49  ARG B NH2 
2871 N N   . VAL B 51  ? 0.1657 0.1933 0.1640 -0.0155 0.0048  -0.0027 50  VAL B N   
2872 C CA  . VAL B 51  ? 0.1904 0.2083 0.1827 -0.0157 0.0058  -0.0050 50  VAL B CA  
2873 C C   . VAL B 51  ? 0.1745 0.1869 0.1667 -0.0101 0.0079  -0.0039 50  VAL B C   
2874 O O   . VAL B 51  ? 0.1845 0.2005 0.1774 -0.0064 0.0077  -0.0035 50  VAL B O   
2875 C CB  . VAL B 51  ? 0.1889 0.2102 0.1779 -0.0173 0.0041  -0.0071 50  VAL B CB  
2876 C CG1 . VAL B 51  ? 0.2055 0.2161 0.1873 -0.0174 0.0051  -0.0096 50  VAL B CG1 
2877 C CG2 . VAL B 51  ? 0.2098 0.2378 0.1994 -0.0231 0.0018  -0.0074 50  VAL B CG2 
2878 N N   . PRO B 52  ? 0.1683 0.1722 0.1597 -0.0094 0.0099  -0.0031 51  PRO B N   
2879 C CA  . PRO B 52  ? 0.1874 0.1859 0.1784 -0.0043 0.0120  -0.0018 51  PRO B CA  
2880 C C   . PRO B 52  ? 0.2267 0.2200 0.2119 -0.0028 0.0128  -0.0039 51  PRO B C   
2881 O O   . PRO B 52  ? 0.2183 0.2067 0.1981 -0.0061 0.0124  -0.0067 51  PRO B O   
2882 C CB  . PRO B 52  ? 0.2003 0.1907 0.1912 -0.0049 0.0139  -0.0007 51  PRO B CB  
2883 C CG  . PRO B 52  ? 0.2385 0.2327 0.2319 -0.0097 0.0125  -0.0006 51  PRO B CG  
2884 C CD  . PRO B 52  ? 0.1533 0.1532 0.1448 -0.0133 0.0102  -0.0029 51  PRO B CD  
2885 N N   . PHE B 53  ? 0.1754 0.1694 0.1613 0.0022  0.0137  -0.0023 52  PHE B N   
2886 C CA  . PHE B 53  ? 0.1571 0.1461 0.1379 0.0047  0.0149  -0.0037 52  PHE B CA  
2887 C C   . PHE B 53  ? 0.1927 0.1811 0.1757 0.0103  0.0166  -0.0004 52  PHE B C   
2888 O O   . PHE B 53  ? 0.1770 0.1698 0.1653 0.0118  0.0162  0.0026  52  PHE B O   
2889 C CB  . PHE B 53  ? 0.1863 0.1817 0.1656 0.0039  0.0129  -0.0057 52  PHE B CB  
2890 C CG  . PHE B 53  ? 0.1931 0.1982 0.1775 0.0068  0.0115  -0.0035 52  PHE B CG  
2891 C CD1 . PHE B 53  ? 0.1762 0.1898 0.1654 0.0051  0.0094  -0.0026 52  PHE B CD1 
2892 C CD2 . PHE B 53  ? 0.1777 0.1835 0.1620 0.0115  0.0122  -0.0019 52  PHE B CD2 
2893 C CE1 . PHE B 53  ? 0.1747 0.1963 0.1682 0.0080  0.0079  -0.0005 52  PHE B CE1 
2894 C CE2 . PHE B 53  ? 0.1798 0.1939 0.1686 0.0140  0.0105  0.0004  52  PHE B CE2 
2895 C CZ  . PHE B 53  ? 0.1633 0.1849 0.1564 0.0123  0.0083  0.0009  52  PHE B CZ  
2896 N N   . MET B 54  ? 0.1689 0.2142 0.1817 -0.0066 -0.0027 -0.0229 53  MET B N   
2897 C CA  A MET B 54  ? 0.1894 0.2393 0.2060 -0.0046 -0.0003 -0.0243 53  MET B CA  
2898 C CA  B MET B 54  ? 0.1890 0.2389 0.2057 -0.0046 -0.0003 -0.0243 53  MET B CA  
2899 C C   . MET B 54  ? 0.1622 0.2161 0.1808 -0.0059 0.0020  -0.0231 53  MET B C   
2900 O O   . MET B 54  ? 0.1902 0.2424 0.2047 -0.0067 0.0022  -0.0226 53  MET B O   
2901 C CB  A MET B 54  ? 0.2025 0.2507 0.2155 -0.0016 0.0000  -0.0271 53  MET B CB  
2902 C CB  B MET B 54  ? 0.2023 0.2505 0.2156 -0.0016 -0.0001 -0.0271 53  MET B CB  
2903 C CG  A MET B 54  ? 0.2205 0.2642 0.2309 0.0003  -0.0021 -0.0287 53  MET B CG  
2904 C CG  B MET B 54  ? 0.2262 0.2694 0.2363 -0.0001 -0.0024 -0.0284 53  MET B CG  
2905 S SD  A MET B 54  ? 0.2122 0.2586 0.2289 0.0010  -0.0025 -0.0288 53  MET B SD  
2906 S SD  B MET B 54  ? 0.1828 0.2251 0.1899 0.0044  -0.0018 -0.0318 53  MET B SD  
2907 C CE  A MET B 54  ? 0.1916 0.2452 0.2136 0.0035  0.0003  -0.0308 53  MET B CE  
2908 C CE  B MET B 54  ? 0.2163 0.2675 0.2322 0.0057  0.0007  -0.0327 53  MET B CE  
2909 N N   . MET B 55  ? 0.1452 0.2040 0.1698 -0.0062 0.0038  -0.0227 54  MET B N   
2910 C CA  . MET B 55  ? 0.1556 0.2179 0.1817 -0.0073 0.0063  -0.0218 54  MET B CA  
2911 C C   . MET B 55  ? 0.1568 0.2193 0.1795 -0.0061 0.0080  -0.0234 54  MET B C   
2912 O O   . MET B 55  ? 0.1651 0.2275 0.1854 -0.0073 0.0093  -0.0224 54  MET B O   
2913 C CB  . MET B 55  ? 0.1392 0.2065 0.1717 -0.0075 0.0081  -0.0218 54  MET B CB  
2914 C CG  . MET B 55  ? 0.1405 0.2078 0.1763 -0.0089 0.0070  -0.0199 54  MET B CG  
2915 S SD  . MET B 55  ? 0.1620 0.2346 0.2045 -0.0091 0.0090  -0.0203 54  MET B SD  
2916 C CE  . MET B 55  ? 0.1476 0.2225 0.1897 -0.0111 0.0121  -0.0191 54  MET B CE  
2917 N N   . GLU B 56  ? 0.1621 0.2249 0.1844 -0.0034 0.0081  -0.0260 55  GLU B N   
2918 C CA  . GLU B 56  ? 0.1666 0.2306 0.1864 -0.0018 0.0102  -0.0278 55  GLU B CA  
2919 C C   . GLU B 56  ? 0.1801 0.2385 0.1923 -0.0018 0.0091  -0.0276 55  GLU B C   
2920 O O   . GLU B 56  ? 0.1756 0.2343 0.1848 -0.0014 0.0111  -0.0282 55  GLU B O   
2921 C CB  . GLU B 56  ? 0.1931 0.2591 0.2146 0.0015  0.0104  -0.0307 55  GLU B CB  
2922 C CG  . GLU B 56  ? 0.1763 0.2483 0.2054 0.0018  0.0114  -0.0314 55  GLU B CG  
2923 C CD  . GLU B 56  ? 0.2017 0.2717 0.2328 0.0018  0.0087  -0.0308 55  GLU B CD  
2924 O OE1 . GLU B 56  ? 0.1812 0.2459 0.2088 0.0006  0.0065  -0.0293 55  GLU B OE1 
2925 O OE2 . GLU B 56  ? 0.2037 0.2776 0.2399 0.0029  0.0090  -0.0319 55  GLU B OE2 
2926 N N   . ARG B 57  ? 0.1596 0.2129 0.1684 -0.0024 0.0061  -0.0268 56  ARG B N   
2927 C CA  . ARG B 57  ? 0.1773 0.2251 0.1788 -0.0030 0.0048  -0.0264 56  ARG B CA  
2928 C C   . ARG B 57  ? 0.1912 0.2390 0.1919 -0.0059 0.0049  -0.0238 56  ARG B C   
2929 O O   . ARG B 57  ? 0.2012 0.2463 0.1965 -0.0063 0.0050  -0.0236 56  ARG B O   
2930 C CB  . ARG B 57  ? 0.2049 0.2470 0.2026 -0.0029 0.0015  -0.0267 56  ARG B CB  
2931 C CG  . ARG B 57  ? 0.2017 0.2421 0.1979 0.0005  0.0012  -0.0295 56  ARG B CG  
2932 C CD  . ARG B 57  ? 0.2221 0.2558 0.2137 0.0004  -0.0020 -0.0298 56  ARG B CD  
2933 N NE  . ARG B 57  ? 0.2254 0.2563 0.2140 0.0040  -0.0023 -0.0325 56  ARG B NE  
2934 C CZ  . ARG B 57  ? 0.2471 0.2739 0.2341 0.0049  -0.0044 -0.0332 56  ARG B CZ  
2935 N NH1 . ARG B 57  ? 0.2221 0.2472 0.2102 0.0023  -0.0063 -0.0315 56  ARG B NH1 
2936 N NH2 . ARG B 57  ? 0.2543 0.2785 0.2382 0.0087  -0.0047 -0.0358 56  ARG B NH2 
2937 N N   . LEU B 58  ? 0.1596 0.2101 0.1652 -0.0078 0.0046  -0.0219 57  LEU B N   
2938 C CA  . LEU B 58  ? 0.1551 0.2055 0.1599 -0.0101 0.0045  -0.0194 57  LEU B CA  
2939 C C   . LEU B 58  ? 0.1756 0.2289 0.1810 -0.0103 0.0077  -0.0191 57  LEU B C   
2940 O O   . LEU B 58  ? 0.1731 0.2247 0.1746 -0.0114 0.0080  -0.0179 57  LEU B O   
2941 C CB  . LEU B 58  ? 0.1624 0.2143 0.1716 -0.0118 0.0031  -0.0174 57  LEU B CB  
2942 C CG  . LEU B 58  ? 0.1507 0.2024 0.1591 -0.0138 0.0025  -0.0147 57  LEU B CG  
2943 C CD1 . LEU B 58  ? 0.1544 0.2019 0.1572 -0.0147 -0.0002 -0.0143 57  LEU B CD1 
2944 C CD2 . LEU B 58  ? 0.1679 0.2220 0.1815 -0.0149 0.0019  -0.0129 57  LEU B CD2 
2945 N N   . VAL B 59  ? 0.1807 0.2385 0.1910 -0.0095 0.0101  -0.0202 58  VAL B N   
2946 C CA  . VAL B 59  ? 0.1704 0.2312 0.1816 -0.0101 0.0135  -0.0200 58  VAL B CA  
2947 C C   . VAL B 59  ? 0.1887 0.2529 0.2021 -0.0081 0.0158  -0.0227 58  VAL B C   
2948 O O   . VAL B 59  ? 0.1863 0.2549 0.2057 -0.0077 0.0167  -0.0235 58  VAL B O   
2949 C CB  . VAL B 59  ? 0.1493 0.2128 0.1653 -0.0120 0.0143  -0.0180 58  VAL B CB  
2950 C CG1 . VAL B 59  ? 0.1915 0.2573 0.2075 -0.0130 0.0179  -0.0178 58  VAL B CG1 
2951 C CG2 . VAL B 59  ? 0.1743 0.2350 0.1889 -0.0135 0.0118  -0.0154 58  VAL B CG2 
2952 N N   . PRO B 60  ? 0.1950 0.2577 0.2038 -0.0065 0.0166  -0.0244 59  PRO B N   
2953 C CA  . PRO B 60  ? 0.1970 0.2630 0.2078 -0.0039 0.0183  -0.0273 59  PRO B CA  
2954 C C   . PRO B 60  ? 0.2415 0.3137 0.2569 -0.0044 0.0221  -0.0279 59  PRO B C   
2955 O O   . PRO B 60  ? 0.1877 0.2602 0.2021 -0.0066 0.0241  -0.0264 59  PRO B O   
2956 C CB  . PRO B 60  ? 0.1826 0.2444 0.1861 -0.0021 0.0182  -0.0286 59  PRO B CB  
2957 C CG  . PRO B 60  ? 0.3000 0.3556 0.2980 -0.0038 0.0153  -0.0266 59  PRO B CG  
2958 C CD  . PRO B 60  ? 0.2245 0.2815 0.2257 -0.0066 0.0152  -0.0238 59  PRO B CD  
2959 N N   . ASN B 61  ? 0.2042 0.2813 0.2244 -0.0025 0.0230  -0.0302 60  ASN B N   
2960 C CA  . ASN B 61  ? 0.1760 0.2599 0.2007 -0.0024 0.0267  -0.0317 60  ASN B CA  
2961 C C   . ASN B 61  ? 0.2256 0.3134 0.2560 -0.0053 0.0280  -0.0302 60  ASN B C   
2962 O O   . ASN B 61  ? 0.2312 0.3245 0.2680 -0.0049 0.0286  -0.0315 60  ASN B O   
2963 C CB  . ASN B 61  ? 0.2251 0.3085 0.2451 -0.0025 0.0296  -0.0321 60  ASN B CB  
2964 C CG  . ASN B 61  ? 0.3104 0.3906 0.3249 0.0008  0.0288  -0.0341 60  ASN B CG  
2965 O OD1 . ASN B 61  ? 0.3153 0.3967 0.3315 0.0038  0.0275  -0.0361 60  ASN B OD1 
2966 N ND2 . ASN B 61  ? 0.3393 0.4148 0.3467 0.0004  0.0294  -0.0333 60  ASN B ND2 
2967 N N   . SER B 62  ? 0.2131 0.2980 0.2410 -0.0081 0.0284  -0.0276 61  SER B N   
2968 C CA  . SER B 62  ? 0.1933 0.2802 0.2251 -0.0110 0.0294  -0.0259 61  SER B CA  
2969 C C   . SER B 62  ? 0.1605 0.2424 0.1904 -0.0122 0.0265  -0.0232 61  SER B C   
2970 O O   . SER B 62  ? 0.2089 0.2859 0.2330 -0.0125 0.0254  -0.0218 61  SER B O   
2971 C CB  . SER B 62  ? 0.2411 0.3292 0.2713 -0.0133 0.0332  -0.0253 61  SER B CB  
2972 O OG  . SER B 62  ? 0.3174 0.4048 0.3489 -0.0162 0.0336  -0.0230 61  SER B OG  
2973 N N   . MET B 63  ? 0.1607 0.2439 0.1954 -0.0129 0.0252  -0.0224 62  MET B N   
2974 C CA  . MET B 63  ? 0.1660 0.2449 0.1991 -0.0138 0.0225  -0.0199 62  MET B CA  
2975 C C   . MET B 63  ? 0.2606 0.3371 0.2907 -0.0161 0.0236  -0.0174 62  MET B C   
2976 O O   . MET B 63  ? 0.1874 0.2605 0.2156 -0.0167 0.0214  -0.0153 62  MET B O   
2977 C CB  . MET B 63  ? 0.1790 0.2595 0.2176 -0.0137 0.0209  -0.0198 62  MET B CB  
2978 C CG  . MET B 63  ? 0.1669 0.2506 0.2097 -0.0157 0.0229  -0.0191 62  MET B CG  
2979 S SD  . MET B 63  ? 0.2121 0.2968 0.2603 -0.0152 0.0207  -0.0191 62  MET B SD  
2980 C CE  . MET B 63  ? 0.2522 0.3412 0.3040 -0.0125 0.0205  -0.0227 62  MET B CE  
2981 N N   . THR B 64  ? 0.2212 0.2994 0.2507 -0.0175 0.0270  -0.0176 63  THR B N   
2982 C CA  . THR B 64  ? 0.2129 0.2881 0.2384 -0.0196 0.0282  -0.0153 63  THR B CA  
2983 C C   . THR B 64  ? 0.2322 0.3038 0.2508 -0.0192 0.0285  -0.0150 63  THR B C   
2984 O O   . THR B 64  ? 0.2453 0.3138 0.2596 -0.0207 0.0296  -0.0132 63  THR B O   
2985 C CB  . THR B 64  ? 0.2353 0.3134 0.2630 -0.0217 0.0319  -0.0154 63  THR B CB  
2986 O OG1 . THR B 64  ? 0.2440 0.3257 0.2719 -0.0214 0.0347  -0.0177 63  THR B OG1 
2987 C CG2 . THR B 64  ? 0.2425 0.3241 0.2769 -0.0223 0.0315  -0.0157 63  THR B CG2 
2988 N N   . GLY B 65  ? 0.2140 0.2853 0.2309 -0.0172 0.0275  -0.0168 64  GLY B N   
2989 C CA  . GLY B 65  ? 0.2099 0.2777 0.2200 -0.0167 0.0278  -0.0169 64  GLY B CA  
2990 C C   . GLY B 65  ? 0.1752 0.2378 0.1807 -0.0165 0.0242  -0.0151 64  GLY B C   
2991 O O   . GLY B 65  ? 0.2125 0.2744 0.2202 -0.0169 0.0217  -0.0136 64  GLY B O   
2992 N N   . SER B 66  ? 0.2414 0.3005 0.2406 -0.0158 0.0240  -0.0155 65  SER B N   
2993 C CA  A SER B 66  ? 0.2558 0.3102 0.2502 -0.0158 0.0206  -0.0141 65  SER B CA  
2994 C CA  B SER B 66  ? 0.2548 0.3092 0.2494 -0.0158 0.0205  -0.0140 65  SER B CA  
2995 C C   . SER B 66  ? 0.2138 0.2677 0.2093 -0.0143 0.0175  -0.0153 65  SER B C   
2996 O O   . SER B 66  ? 0.2381 0.2937 0.2353 -0.0127 0.0182  -0.0176 65  SER B O   
2997 C CB  A SER B 66  ? 0.2583 0.3086 0.2449 -0.0157 0.0214  -0.0141 65  SER B CB  
2998 C CB  B SER B 66  ? 0.2591 0.3094 0.2458 -0.0159 0.0213  -0.0138 65  SER B CB  
2999 O OG  A SER B 66  ? 0.2840 0.3341 0.2687 -0.0171 0.0245  -0.0131 65  SER B OG  
3000 O OG  B SER B 66  ? 0.2650 0.3163 0.2501 -0.0148 0.0240  -0.0161 65  SER B OG  
3001 N N   . PRO B 67  ? 0.2266 0.2779 0.2211 -0.0148 0.0140  -0.0138 66  PRO B N   
3002 C CA  . PRO B 67  ? 0.2102 0.2603 0.2050 -0.0139 0.0111  -0.0149 66  PRO B CA  
3003 C C   . PRO B 67  ? 0.2327 0.2791 0.2211 -0.0127 0.0106  -0.0165 66  PRO B C   
3004 O O   . PRO B 67  ? 0.2464 0.2903 0.2293 -0.0128 0.0116  -0.0163 66  PRO B O   
3005 C CB  . PRO B 67  ? 0.2181 0.2669 0.2132 -0.0152 0.0078  -0.0126 66  PRO B CB  
3006 C CG  . PRO B 67  ? 0.2590 0.3067 0.2512 -0.0164 0.0085  -0.0106 66  PRO B CG  
3007 C CD  . PRO B 67  ? 0.2210 0.2709 0.2144 -0.0163 0.0126  -0.0111 66  PRO B CD  
3008 N N   . ASP B 68  ? 0.1909 0.2363 0.1795 -0.0114 0.0089  -0.0182 67  ASP B N   
3009 C CA  . ASP B 68  ? 0.2124 0.2532 0.1944 -0.0102 0.0078  -0.0197 67  ASP B CA  
3010 C C   . ASP B 68  ? 0.1811 0.2176 0.1585 -0.0119 0.0043  -0.0181 67  ASP B C   
3011 O O   . ASP B 68  ? 0.1889 0.2254 0.1688 -0.0129 0.0018  -0.0173 67  ASP B O   
3012 C CB  . ASP B 68  ? 0.2118 0.2524 0.1951 -0.0082 0.0071  -0.0219 67  ASP B CB  
3013 C CG  . ASP B 68  ? 0.2359 0.2709 0.2116 -0.0068 0.0060  -0.0236 67  ASP B CG  
3014 O OD1 . ASP B 68  ? 0.2681 0.3028 0.2405 -0.0052 0.0084  -0.0250 67  ASP B OD1 
3015 O OD2 . ASP B 68  ? 0.2273 0.2582 0.2000 -0.0074 0.0028  -0.0235 67  ASP B OD2 
3016 N N   . PRO B 69  ? 0.2032 0.2361 0.1740 -0.0124 0.0041  -0.0177 68  PRO B N   
3017 C CA  . PRO B 69  ? 0.1998 0.2295 0.1671 -0.0142 0.0006  -0.0160 68  PRO B CA  
3018 C C   . PRO B 69  ? 0.2169 0.2435 0.1825 -0.0145 -0.0027 -0.0168 68  PRO B C   
3019 O O   . PRO B 69  ? 0.2214 0.2481 0.1883 -0.0164 -0.0055 -0.0154 68  PRO B O   
3020 C CB  . PRO B 69  ? 0.2092 0.2351 0.1688 -0.0141 0.0013  -0.0160 68  PRO B CB  
3021 C CG  . PRO B 69  ? 0.2431 0.2719 0.2045 -0.0132 0.0056  -0.0163 68  PRO B CG  
3022 C CD  . PRO B 69  ? 0.2308 0.2632 0.1977 -0.0116 0.0073  -0.0182 68  PRO B CD  
3023 N N   . ASN B 70  ? 0.1985 0.2222 0.1608 -0.0127 -0.0023 -0.0192 69  ASN B N   
3024 C CA  . ASN B 70  ? 0.1973 0.2166 0.1564 -0.0133 -0.0056 -0.0199 69  ASN B CA  
3025 C C   . ASN B 70  ? 0.1908 0.2128 0.1563 -0.0137 -0.0066 -0.0197 69  ASN B C   
3026 O O   . ASN B 70  ? 0.2097 0.2297 0.1745 -0.0157 -0.0096 -0.0190 69  ASN B O   
3027 C CB  . ASN B 70  ? 0.2207 0.2351 0.1734 -0.0110 -0.0050 -0.0225 69  ASN B CB  
3028 C CG  . ASN B 70  ? 0.2892 0.2991 0.2337 -0.0112 -0.0052 -0.0225 69  ASN B CG  
3029 O OD1 . ASN B 70  ? 0.2811 0.2901 0.2237 -0.0135 -0.0071 -0.0208 69  ASN B OD1 
3030 N ND2 . ASN B 70  ? 0.2970 0.3044 0.2369 -0.0087 -0.0031 -0.0245 69  ASN B ND2 
3031 N N   . TYR B 71  ? 0.1947 0.2207 0.1660 -0.0121 -0.0043 -0.0204 70  TYR B N   
3032 C CA  . TYR B 71  ? 0.1795 0.2079 0.1567 -0.0125 -0.0053 -0.0200 70  TYR B CA  
3033 C C   . TYR B 71  ? 0.1743 0.2062 0.1562 -0.0149 -0.0061 -0.0174 70  TYR B C   
3034 O O   . TYR B 71  ? 0.2040 0.2358 0.1879 -0.0164 -0.0083 -0.0166 70  TYR B O   
3035 C CB  . TYR B 71  ? 0.1756 0.2076 0.1576 -0.0101 -0.0027 -0.0215 70  TYR B CB  
3036 C CG  . TYR B 71  ? 0.1709 0.2040 0.1576 -0.0098 -0.0036 -0.0219 70  TYR B CG  
3037 C CD1 . TYR B 71  ? 0.1744 0.2030 0.1576 -0.0085 -0.0051 -0.0236 70  TYR B CD1 
3038 C CD2 . TYR B 71  ? 0.1637 0.2019 0.1577 -0.0104 -0.0027 -0.0206 70  TYR B CD2 
3039 C CE1 . TYR B 71  ? 0.1858 0.2150 0.1727 -0.0080 -0.0058 -0.0241 70  TYR B CE1 
3040 C CE2 . TYR B 71  ? 0.1780 0.2168 0.1758 -0.0099 -0.0034 -0.0211 70  TYR B CE2 
3041 C CZ  . TYR B 71  ? 0.1770 0.2113 0.1712 -0.0087 -0.0050 -0.0227 70  TYR B CZ  
3042 O OH  . TYR B 71  ? 0.1708 0.2055 0.1685 -0.0081 -0.0056 -0.0232 70  TYR B OH  
3043 N N   . LEU B 72  ? 0.1797 0.2147 0.1633 -0.0151 -0.0043 -0.0161 71  LEU B N   
3044 C CA  . LEU B 72  ? 0.1889 0.2267 0.1759 -0.0170 -0.0053 -0.0136 71  LEU B CA  
3045 C C   . LEU B 72  ? 0.2126 0.2477 0.1960 -0.0190 -0.0087 -0.0126 71  LEU B C   
3046 O O   . LEU B 72  ? 0.1990 0.2363 0.1861 -0.0205 -0.0104 -0.0111 71  LEU B O   
3047 C CB  . LEU B 72  ? 0.2085 0.2483 0.1956 -0.0169 -0.0030 -0.0125 71  LEU B CB  
3048 C CG  . LEU B 72  ? 0.2200 0.2618 0.2091 -0.0184 -0.0041 -0.0099 71  LEU B CG  
3049 C CD1 . LEU B 72  ? 0.1952 0.2408 0.1914 -0.0188 -0.0042 -0.0088 71  LEU B CD1 
3050 C CD2 . LEU B 72  ? 0.2326 0.2746 0.2197 -0.0181 -0.0017 -0.0090 71  LEU B CD2 
3051 N N   . ALA B 73  ? 0.1947 0.2254 0.1711 -0.0192 -0.0098 -0.0134 72  ALA B N   
3052 C CA  . ALA B 73  ? 0.1831 0.2114 0.1558 -0.0213 -0.0132 -0.0125 72  ALA B CA  
3053 C C   . ALA B 73  ? 0.2236 0.2514 0.1982 -0.0227 -0.0155 -0.0127 72  ALA B C   
3054 O O   . ALA B 73  ? 0.2170 0.2464 0.1933 -0.0249 -0.0178 -0.0112 72  ALA B O   
3055 C CB  . ALA B 73  ? 0.2021 0.2248 0.1661 -0.0211 -0.0139 -0.0137 72  ALA B CB  
3056 N N   . ASP B 74  ? 0.1992 0.2248 0.1735 -0.0214 -0.0147 -0.0146 73  ASP B N   
3057 C CA  . ASP B 74  ? 0.2355 0.2597 0.2108 -0.0228 -0.0166 -0.0149 73  ASP B CA  
3058 C C   . ASP B 74  ? 0.2105 0.2399 0.1938 -0.0232 -0.0161 -0.0135 73  ASP B C   
3059 O O   . ASP B 74  ? 0.2061 0.2359 0.1911 -0.0253 -0.0180 -0.0128 73  ASP B O   
3060 C CB  . ASP B 74  ? 0.2288 0.2481 0.2002 -0.0209 -0.0161 -0.0173 73  ASP B CB  
3061 C CG  . ASP B 74  ? 0.3138 0.3264 0.2763 -0.0213 -0.0178 -0.0186 73  ASP B CG  
3062 O OD1 . ASP B 74  ? 0.4103 0.4212 0.3697 -0.0240 -0.0203 -0.0176 73  ASP B OD1 
3063 O OD2 . ASP B 74  ? 0.3033 0.3122 0.2616 -0.0188 -0.0166 -0.0206 73  ASP B OD2 
3064 N N   . LEU B 75  ? 0.1801 0.2136 0.1684 -0.0214 -0.0135 -0.0132 74  LEU B N   
3065 C CA  . LEU B 75  ? 0.1772 0.2155 0.1727 -0.0219 -0.0130 -0.0117 74  LEU B CA  
3066 C C   . LEU B 75  ? 0.2037 0.2447 0.2007 -0.0240 -0.0147 -0.0094 74  LEU B C   
3067 O O   . LEU B 75  ? 0.1892 0.2323 0.1899 -0.0254 -0.0159 -0.0084 74  LEU B O   
3068 C CB  . LEU B 75  ? 0.1805 0.2222 0.1802 -0.0199 -0.0099 -0.0118 74  LEU B CB  
3069 C CG  . LEU B 75  ? 0.1792 0.2253 0.1858 -0.0202 -0.0093 -0.0102 74  LEU B CG  
3070 C CD1 . LEU B 75  ? 0.1704 0.2157 0.1793 -0.0203 -0.0101 -0.0109 74  LEU B CD1 
3071 C CD2 . LEU B 75  ? 0.1827 0.2317 0.1924 -0.0187 -0.0063 -0.0102 74  LEU B CD2 
3072 N N   . ILE B 76  ? 0.1843 0.2255 0.1787 -0.0240 -0.0147 -0.0086 75  ILE B N   
3073 C CA  . ILE B 76  ? 0.1878 0.2316 0.1832 -0.0255 -0.0165 -0.0065 75  ILE B CA  
3074 C C   . ILE B 76  ? 0.2143 0.2568 0.2079 -0.0280 -0.0197 -0.0065 75  ILE B C   
3075 O O   . ILE B 76  ? 0.2314 0.2775 0.2289 -0.0294 -0.0212 -0.0051 75  ILE B O   
3076 C CB  . ILE B 76  ? 0.1934 0.2364 0.1849 -0.0249 -0.0161 -0.0060 75  ILE B CB  
3077 C CG1 . ILE B 76  ? 0.1992 0.2440 0.1930 -0.0230 -0.0127 -0.0057 75  ILE B CG1 
3078 C CG2 . ILE B 76  ? 0.2289 0.2742 0.2207 -0.0263 -0.0186 -0.0040 75  ILE B CG2 
3079 C CD1 . ILE B 76  ? 0.2158 0.2584 0.2042 -0.0224 -0.0118 -0.0055 75  ILE B CD1 
3080 N N   . ALA B 77  ? 0.2094 0.2467 0.1968 -0.0285 -0.0208 -0.0082 76  ALA B N   
3081 C CA  . ALA B 77  ? 0.2176 0.2532 0.2025 -0.0313 -0.0240 -0.0082 76  ALA B CA  
3082 C C   . ALA B 77  ? 0.2004 0.2376 0.1899 -0.0326 -0.0243 -0.0080 76  ALA B C   
3083 O O   . ALA B 77  ? 0.2236 0.2637 0.2156 -0.0350 -0.0263 -0.0069 76  ALA B O   
3084 C CB  . ALA B 77  ? 0.2634 0.2920 0.2401 -0.0316 -0.0249 -0.0102 76  ALA B CB  
3085 N N   . THR B 78  ? 0.2016 0.2374 0.1926 -0.0309 -0.0223 -0.0092 77  THR B N   
3086 C CA  . THR B 78  ? 0.2264 0.2629 0.2210 -0.0319 -0.0225 -0.0092 77  THR B CA  
3087 C C   . THR B 78  ? 0.2008 0.2439 0.2028 -0.0323 -0.0221 -0.0071 77  THR B C   
3088 O O   . THR B 78  ? 0.1848 0.2299 0.1893 -0.0345 -0.0234 -0.0063 77  THR B O   
3089 C CB  . THR B 78  ? 0.2281 0.2617 0.2224 -0.0295 -0.0205 -0.0109 77  THR B CB  
3090 O OG1 . THR B 78  ? 0.2358 0.2629 0.2228 -0.0290 -0.0211 -0.0129 77  THR B OG1 
3091 C CG2 . THR B 78  ? 0.2170 0.2511 0.2150 -0.0303 -0.0206 -0.0107 77  THR B CG2 
3092 N N   . VAL B 79  ? 0.2100 0.2564 0.2154 -0.0301 -0.0201 -0.0063 78  VAL B N   
3093 C CA  . VAL B 79  ? 0.1600 0.2120 0.1718 -0.0299 -0.0195 -0.0043 78  VAL B CA  
3094 C C   . VAL B 79  ? 0.2104 0.2659 0.2231 -0.0319 -0.0218 -0.0027 78  VAL B C   
3095 O O   . VAL B 79  ? 0.2020 0.2611 0.2190 -0.0332 -0.0225 -0.0017 78  VAL B O   
3096 C CB  . VAL B 79  ? 0.1816 0.2354 0.1953 -0.0274 -0.0170 -0.0039 78  VAL B CB  
3097 C CG1 . VAL B 79  ? 0.2510 0.3099 0.2698 -0.0272 -0.0168 -0.0017 78  VAL B CG1 
3098 C CG2 . VAL B 79  ? 0.2007 0.2531 0.2159 -0.0257 -0.0147 -0.0052 78  VAL B CG2 
3099 N N   . ASN B 80  ? 0.1978 0.2523 0.2064 -0.0321 -0.0230 -0.0026 79  ASN B N   
3100 C CA  . ASN B 80  ? 0.1977 0.2562 0.2076 -0.0335 -0.0253 -0.0010 79  ASN B CA  
3101 C C   . ASN B 80  ? 0.2342 0.2928 0.2436 -0.0368 -0.0279 -0.0013 79  ASN B C   
3102 O O   . ASN B 80  ? 0.2480 0.3118 0.2611 -0.0382 -0.0295 0.0001  79  ASN B O   
3103 C CB  . ASN B 80  ? 0.1730 0.2301 0.1783 -0.0327 -0.0260 -0.0007 79  ASN B CB  
3104 C CG  . ASN B 80  ? 0.2257 0.2841 0.2325 -0.0300 -0.0235 0.0002  79  ASN B CG  
3105 O OD1 . ASN B 80  ? 0.2782 0.3388 0.2897 -0.0287 -0.0214 0.0007  79  ASN B OD1 
3106 N ND2 . ASN B 80  ? 0.2754 0.3318 0.2775 -0.0291 -0.0236 0.0003  79  ASN B ND2 
3107 N N   . ALA B 81  ? 0.2092 0.2623 0.2140 -0.0381 -0.0283 -0.0031 80  ALA B N   
3108 C CA  . ALA B 81  ? 0.2238 0.2763 0.2277 -0.0416 -0.0306 -0.0034 80  ALA B CA  
3109 C C   . ALA B 81  ? 0.2579 0.3144 0.2682 -0.0424 -0.0297 -0.0026 80  ALA B C   
3110 O O   . ALA B 81  ? 0.2683 0.3282 0.2809 -0.0452 -0.0314 -0.0019 80  ALA B O   
3111 C CB  . ALA B 81  ? 0.2581 0.3027 0.2549 -0.0425 -0.0310 -0.0055 80  ALA B CB  
3112 N N   . ILE B 82  ? 0.1871 0.2430 0.1999 -0.0400 -0.0271 -0.0028 81  ILE B N   
3113 C CA  . ILE B 82  ? 0.1587 0.2182 0.1775 -0.0403 -0.0261 -0.0020 81  ILE B CA  
3114 C C   . ILE B 82  ? 0.1830 0.2502 0.2077 -0.0400 -0.0264 0.0001  81  ILE B C   
3115 O O   . ILE B 82  ? 0.2217 0.2931 0.2502 -0.0421 -0.0272 0.0010  81  ILE B O   
3116 C CB  . ILE B 82  ? 0.2124 0.2696 0.2323 -0.0375 -0.0234 -0.0027 81  ILE B CB  
3117 C CG1 . ILE B 82  ? 0.2175 0.2675 0.2320 -0.0377 -0.0232 -0.0048 81  ILE B CG1 
3118 C CG2 . ILE B 82  ? 0.2044 0.2658 0.2307 -0.0372 -0.0220 -0.0015 81  ILE B CG2 
3119 C CD1 . ILE B 82  ? 0.1956 0.2433 0.2101 -0.0343 -0.0209 -0.0058 81  ILE B CD1 
3120 N N   . THR B 83  ? 0.1761 0.2450 0.2014 -0.0375 -0.0257 0.0009  82  THR B N   
3121 C CA  . THR B 83  ? 0.1801 0.2556 0.2107 -0.0365 -0.0257 0.0029  82  THR B CA  
3122 C C   . THR B 83  ? 0.1890 0.2685 0.2198 -0.0386 -0.0287 0.0037  82  THR B C   
3123 O O   . THR B 83  ? 0.2145 0.3004 0.2505 -0.0386 -0.0293 0.0052  82  THR B O   
3124 C CB  . THR B 83  ? 0.1601 0.2356 0.1908 -0.0332 -0.0240 0.0036  82  THR B CB  
3125 O OG1 . THR B 83  ? 0.1865 0.2591 0.2118 -0.0329 -0.0249 0.0032  82  THR B OG1 
3126 C CG2 . THR B 83  ? 0.1705 0.2427 0.2016 -0.0314 -0.0211 0.0027  82  THR B CG2 
3127 N N   . GLN B 84  ? 0.1628 0.2390 0.1881 -0.0402 -0.0307 0.0027  83  GLN B N   
3128 C CA  . GLN B 84  ? 0.1933 0.2733 0.2187 -0.0426 -0.0339 0.0033  83  GLN B CA  
3129 C C   . GLN B 84  ? 0.2525 0.3362 0.2817 -0.0459 -0.0348 0.0034  83  GLN B C   
3130 O O   . GLN B 84  ? 0.2466 0.3364 0.2789 -0.0476 -0.0370 0.0043  83  GLN B O   
3131 C CB  . GLN B 84  ? 0.2683 0.3429 0.2861 -0.0440 -0.0358 0.0020  83  GLN B CB  
3132 C CG  . GLN B 84  ? 0.3767 0.4551 0.3942 -0.0464 -0.0393 0.0026  83  GLN B CG  
3133 C CD  . GLN B 84  ? 0.4512 0.5334 0.4698 -0.0439 -0.0401 0.0040  83  GLN B CD  
3134 O OE1 . GLN B 84  ? 0.5191 0.5974 0.5337 -0.0414 -0.0391 0.0039  83  GLN B OE1 
3135 N NE2 . GLN B 84  ? 0.4461 0.5361 0.4699 -0.0445 -0.0420 0.0053  83  GLN B NE2 
3136 N N   . LYS B 85  ? 0.1913 0.2713 0.2201 -0.0469 -0.0332 0.0024  84  LYS B N   
3137 C CA  . LYS B 85  ? 0.2319 0.3148 0.2641 -0.0501 -0.0336 0.0025  84  LYS B CA  
3138 C C   . LYS B 85  ? 0.2467 0.3357 0.2863 -0.0485 -0.0317 0.0039  84  LYS B C   
3139 O O   . LYS B 85  ? 0.2812 0.3734 0.3242 -0.0509 -0.0316 0.0042  84  LYS B O   
3140 C CB  . LYS B 85  ? 0.2269 0.3022 0.2544 -0.0518 -0.0328 0.0008  84  LYS B CB  
3141 C CG  . LYS B 85  ? 0.3015 0.3706 0.3213 -0.0543 -0.0350 -0.0007 84  LYS B CG  
3142 C CD  . LYS B 85  ? 0.3306 0.4022 0.3507 -0.0592 -0.0374 -0.0007 84  LYS B CD  
3143 C CE  . LYS B 85  ? 0.4405 0.5100 0.4612 -0.0616 -0.0361 -0.0012 84  LYS B CE  
3144 N NZ  . LYS B 85  ? 0.3372 0.4117 0.3605 -0.0664 -0.0379 -0.0008 84  LYS B NZ  
3145 N N   . GLY B 86  ? 0.2042 0.3359 0.2542 -0.0329 -0.0069 -0.0218 85  GLY B N   
3146 C CA  . GLY B 86  ? 0.1755 0.3110 0.2306 -0.0306 -0.0067 -0.0229 85  GLY B CA  
3147 C C   . GLY B 86  ? 0.1641 0.2910 0.2153 -0.0310 -0.0043 -0.0205 85  GLY B C   
3148 O O   . GLY B 86  ? 0.2150 0.3444 0.2700 -0.0292 -0.0038 -0.0213 85  GLY B O   
3149 N N   . ALA B 87  ? 0.1884 0.3053 0.2322 -0.0330 -0.0028 -0.0179 86  ALA B N   
3150 C CA  . ALA B 87  ? 0.1941 0.3021 0.2335 -0.0331 -0.0010 -0.0156 86  ALA B CA  
3151 C C   . ALA B 87  ? 0.1758 0.2787 0.2144 -0.0280 -0.0034 -0.0116 86  ALA B C   
3152 O O   . ALA B 87  ? 0.1680 0.2718 0.2071 -0.0253 -0.0060 -0.0102 86  ALA B O   
3153 C CB  . ALA B 87  ? 0.1937 0.2930 0.2250 -0.0376 0.0014  -0.0152 86  ALA B CB  
3154 N N   . TYR B 88  ? 0.1611 0.2584 0.1980 -0.0269 -0.0023 -0.0101 87  TYR B N   
3155 C CA  . TYR B 88  ? 0.1254 0.2174 0.1612 -0.0228 -0.0039 -0.0066 87  TYR B CA  
3156 C C   . TYR B 88  ? 0.1666 0.2498 0.1958 -0.0238 -0.0035 -0.0045 87  TYR B C   
3157 O O   . TYR B 88  ? 0.1605 0.2389 0.1850 -0.0271 -0.0015 -0.0053 87  TYR B O   
3158 C CB  . TYR B 88  ? 0.1398 0.2302 0.1771 -0.0211 -0.0030 -0.0062 87  TYR B CB  
3159 C CG  . TYR B 88  ? 0.1418 0.2402 0.1857 -0.0187 -0.0041 -0.0078 87  TYR B CG  
3160 C CD1 . TYR B 88  ? 0.1845 0.2900 0.2323 -0.0212 -0.0026 -0.0115 87  TYR B CD1 
3161 C CD2 . TYR B 88  ? 0.1365 0.2350 0.1826 -0.0139 -0.0064 -0.0059 87  TYR B CD2 
3162 C CE1 . TYR B 88  ? 0.1456 0.2589 0.1998 -0.0185 -0.0037 -0.0134 87  TYR B CE1 
3163 C CE2 . TYR B 88  ? 0.1780 0.2831 0.2295 -0.0112 -0.0076 -0.0075 87  TYR B CE2 
3164 C CZ  . TYR B 88  ? 0.1896 0.3023 0.2455 -0.0133 -0.0064 -0.0113 87  TYR B CZ  
3165 O OH  . TYR B 88  ? 0.2026 0.3226 0.2645 -0.0103 -0.0077 -0.0134 87  TYR B OH  
3166 N N   . ALA B 89  ? 0.1330 0.2137 0.1614 -0.0207 -0.0054 -0.0021 88  ALA B N   
3167 C CA  . ALA B 89  ? 0.1335 0.2069 0.1566 -0.0210 -0.0053 -0.0004 88  ALA B CA  
3168 C C   . ALA B 89  ? 0.1373 0.2065 0.1603 -0.0178 -0.0057 0.0017  88  ALA B C   
3169 O O   . ALA B 89  ? 0.1541 0.2255 0.1798 -0.0150 -0.0072 0.0028  88  ALA B O   
3170 C CB  . ALA B 89  ? 0.1381 0.2129 0.1604 -0.0208 -0.0068 0.0001  88  ALA B CB  
3171 N N   . VAL B 90  ? 0.1474 0.2102 0.1668 -0.0184 -0.0046 0.0021  89  VAL B N   
3172 C CA  . VAL B 90  ? 0.1440 0.2030 0.1633 -0.0157 -0.0049 0.0036  89  VAL B CA  
3173 C C   . VAL B 90  ? 0.1510 0.2060 0.1673 -0.0150 -0.0055 0.0045  89  VAL B C   
3174 O O   . VAL B 90  ? 0.1770 0.2279 0.1891 -0.0166 -0.0051 0.0039  89  VAL B O   
3175 C CB  . VAL B 90  ? 0.1567 0.2111 0.1739 -0.0163 -0.0036 0.0031  89  VAL B CB  
3176 C CG1 . VAL B 90  ? 0.1712 0.2229 0.1893 -0.0134 -0.0041 0.0045  89  VAL B CG1 
3177 C CG2 . VAL B 90  ? 0.1501 0.2083 0.1698 -0.0178 -0.0024 0.0017  89  VAL B CG2 
3178 N N   . VAL B 91  ? 0.1564 0.2123 0.1746 -0.0127 -0.0065 0.0058  90  VAL B N   
3179 C CA  . VAL B 91  ? 0.1499 0.2030 0.1660 -0.0120 -0.0069 0.0064  90  VAL B CA  
3180 C C   . VAL B 91  ? 0.1861 0.2351 0.2016 -0.0107 -0.0065 0.0064  90  VAL B C   
3181 O O   . VAL B 91  ? 0.1894 0.2389 0.2072 -0.0090 -0.0065 0.0071  90  VAL B O   
3182 C CB  . VAL B 91  ? 0.1490 0.2047 0.1667 -0.0108 -0.0078 0.0075  90  VAL B CB  
3183 C CG1 . VAL B 91  ? 0.2426 0.2955 0.2584 -0.0104 -0.0077 0.0078  90  VAL B CG1 
3184 C CG2 . VAL B 91  ? 0.1930 0.2527 0.2110 -0.0119 -0.0087 0.0071  90  VAL B CG2 
3185 N N   . ASP B 92  ? 0.1338 0.1785 0.1459 -0.0112 -0.0062 0.0055  91  ASP B N   
3186 C CA  . ASP B 92  ? 0.1506 0.1912 0.1617 -0.0098 -0.0062 0.0050  91  ASP B CA  
3187 C C   . ASP B 92  ? 0.1651 0.2039 0.1752 -0.0086 -0.0067 0.0043  91  ASP B C   
3188 O O   . ASP B 92  ? 0.1757 0.2114 0.1822 -0.0092 -0.0070 0.0033  91  ASP B O   
3189 C CB  . ASP B 92  ? 0.1747 0.2110 0.1818 -0.0110 -0.0059 0.0041  91  ASP B CB  
3190 C CG  . ASP B 92  ? 0.2100 0.2406 0.2142 -0.0093 -0.0065 0.0032  91  ASP B CG  
3191 O OD1 . ASP B 92  ? 0.1852 0.2164 0.1920 -0.0072 -0.0069 0.0032  91  ASP B OD1 
3192 O OD2 . ASP B 92  ? 0.2012 0.2263 0.2000 -0.0102 -0.0067 0.0022  91  ASP B OD2 
3193 N N   . PRO B 93  ? 0.1617 0.2020 0.1745 -0.0072 -0.0066 0.0045  92  PRO B N   
3194 C CA  . PRO B 93  ? 0.1665 0.2055 0.1790 -0.0061 -0.0068 0.0030  92  PRO B CA  
3195 C C   . PRO B 93  ? 0.1662 0.2014 0.1772 -0.0046 -0.0075 0.0016  92  PRO B C   
3196 O O   . PRO B 93  ? 0.1810 0.2161 0.1938 -0.0034 -0.0075 0.0017  92  PRO B O   
3197 C CB  . PRO B 93  ? 0.1676 0.2095 0.1833 -0.0056 -0.0062 0.0034  92  PRO B CB  
3198 C CG  . PRO B 93  ? 0.1590 0.2028 0.1763 -0.0058 -0.0060 0.0053  92  PRO B CG  
3199 C CD  . PRO B 93  ? 0.2080 0.2506 0.2241 -0.0063 -0.0063 0.0055  92  PRO B CD  
3200 N N   . HIS B 94  ? 0.1610 0.1923 0.1679 -0.0045 -0.0083 0.0004  93  HIS B N   
3201 C CA  . HIS B 94  ? 0.1793 0.2051 0.1826 -0.0031 -0.0093 -0.0007 93  HIS B CA  
3202 C C   . HIS B 94  ? 0.1930 0.2183 0.1976 -0.0004 -0.0104 -0.0030 93  HIS B C   
3203 O O   . HIS B 94  ? 0.2075 0.2293 0.2089 0.0011  -0.0117 -0.0048 93  HIS B O   
3204 C CB  . HIS B 94  ? 0.2109 0.2318 0.2081 -0.0045 -0.0097 -0.0011 93  HIS B CB  
3205 C CG  . HIS B 94  ? 0.1920 0.2062 0.1839 -0.0044 -0.0103 -0.0014 93  HIS B CG  
3206 N ND1 . HIS B 94  ? 0.1871 0.2010 0.1784 -0.0063 -0.0092 -0.0003 93  HIS B ND1 
3207 C CD2 . HIS B 94  ? 0.2400 0.2470 0.2263 -0.0026 -0.0119 -0.0030 93  HIS B CD2 
3208 C CE1 . HIS B 94  ? 0.1963 0.2027 0.1815 -0.0061 -0.0098 -0.0010 93  HIS B CE1 
3209 N NE2 . HIS B 94  ? 0.2066 0.2083 0.1883 -0.0037 -0.0116 -0.0025 93  HIS B NE2 
3210 N N   . ASN B 95  ? 0.1623 0.1915 0.1718 0.0005  -0.0099 -0.0030 94  ASN B N   
3211 C CA  . ASN B 95  ? 0.1729 0.2045 0.1854 0.0023  -0.0103 -0.0054 94  ASN B CA  
3212 C C   . ASN B 95  ? 0.2054 0.2365 0.2198 0.0045  -0.0112 -0.0069 94  ASN B C   
3213 O O   . ASN B 95  ? 0.1766 0.2104 0.1940 0.0060  -0.0116 -0.0095 94  ASN B O   
3214 C CB  . ASN B 95  ? 0.1570 0.1940 0.1735 0.0007  -0.0086 -0.0048 94  ASN B CB  
3215 C CG  . ASN B 95  ? 0.1949 0.2327 0.2102 -0.0003 -0.0082 -0.0054 94  ASN B CG  
3216 O OD1 . ASN B 95  ? 0.1761 0.2129 0.1888 -0.0019 -0.0080 -0.0037 94  ASN B OD1 
3217 N ND2 . ASN B 95  ? 0.1915 0.2315 0.2087 0.0006  -0.0081 -0.0081 94  ASN B ND2 
3218 N N   . TYR B 96  ? 0.1686 0.1966 0.1814 0.0047  -0.0116 -0.0056 95  TYR B N   
3219 C CA  . TYR B 96  ? 0.1745 0.2010 0.1880 0.0071  -0.0129 -0.0072 95  TYR B CA  
3220 C C   . TYR B 96  ? 0.1694 0.2016 0.1890 0.0073  -0.0119 -0.0081 95  TYR B C   
3221 O O   . TYR B 96  ? 0.1902 0.2229 0.2116 0.0095  -0.0131 -0.0107 95  TYR B O   
3222 C CB  . TYR B 96  ? 0.1940 0.2162 0.2040 0.0099  -0.0154 -0.0101 95  TYR B CB  
3223 C CG  . TYR B 96  ? 0.2414 0.2565 0.2440 0.0094  -0.0162 -0.0092 95  TYR B CG  
3224 C CD1 . TYR B 96  ? 0.2218 0.2306 0.2193 0.0092  -0.0168 -0.0081 95  TYR B CD1 
3225 C CD2 . TYR B 96  ? 0.2527 0.2671 0.2528 0.0087  -0.0162 -0.0095 95  TYR B CD2 
3226 C CE1 . TYR B 96  ? 0.2294 0.2311 0.2193 0.0080  -0.0171 -0.0075 95  TYR B CE1 
3227 C CE2 . TYR B 96  ? 0.2758 0.2833 0.2686 0.0077  -0.0167 -0.0088 95  TYR B CE2 
3228 C CZ  . TYR B 96  ? 0.2560 0.2571 0.2436 0.0073  -0.0171 -0.0078 95  TYR B CZ  
3229 O OH  . TYR B 96  ? 0.2920 0.2855 0.2713 0.0058  -0.0173 -0.0073 95  TYR B OH  
3230 N N   . GLY B 97  ? 0.1735 0.2095 0.1957 0.0050  -0.0099 -0.0063 96  GLY B N   
3231 C CA  . GLY B 97  ? 0.1772 0.2175 0.2038 0.0046  -0.0085 -0.0070 96  GLY B CA  
3232 C C   . GLY B 97  ? 0.1534 0.1974 0.1827 0.0049  -0.0083 -0.0102 96  GLY B C   
3233 O O   . GLY B 97  ? 0.1743 0.2217 0.2072 0.0048  -0.0074 -0.0120 96  GLY B O   
3234 N N   . ARG B 98  ? 0.1575 0.2009 0.1850 0.0052  -0.0089 -0.0112 97  ARG B N   
3235 C CA  . ARG B 98  ? 0.1763 0.2231 0.2063 0.0059  -0.0089 -0.0149 97  ARG B CA  
3236 C C   . ARG B 98  ? 0.1670 0.2148 0.1956 0.0039  -0.0077 -0.0142 97  ARG B C   
3237 O O   . ARG B 98  ? 0.1861 0.2310 0.2112 0.0030  -0.0078 -0.0115 97  ARG B O   
3238 C CB  . ARG B 98  ? 0.1533 0.1977 0.1820 0.0095  -0.0118 -0.0180 97  ARG B CB  
3239 C CG  . ARG B 98  ? 0.1740 0.2184 0.2046 0.0117  -0.0132 -0.0196 97  ARG B CG  
3240 C CD  . ARG B 98  ? 0.2384 0.2771 0.2649 0.0152  -0.0166 -0.0210 97  ARG B CD  
3241 N NE  . ARG B 98  ? 0.1676 0.2072 0.1965 0.0176  -0.0181 -0.0234 97  ARG B NE  
3242 C CZ  . ARG B 98  ? 0.1887 0.2262 0.2171 0.0173  -0.0181 -0.0215 97  ARG B CZ  
3243 N NH1 . ARG B 98  ? 0.1982 0.2330 0.2242 0.0148  -0.0164 -0.0173 97  ARG B NH1 
3244 N NH2 . ARG B 98  ? 0.1862 0.2244 0.2167 0.0197  -0.0198 -0.0241 97  ARG B NH2 
3245 N N   . TYR B 99  ? 0.1794 0.2315 0.2110 0.0032  -0.0064 -0.0170 98  TYR B N   
3246 C CA  . TYR B 99  ? 0.1790 0.2323 0.2096 0.0010  -0.0048 -0.0167 98  TYR B CA  
3247 C C   . TYR B 99  ? 0.1961 0.2527 0.2292 0.0023  -0.0051 -0.0215 98  TYR B C   
3248 O O   . TYR B 99  ? 0.1821 0.2430 0.2195 0.0026  -0.0043 -0.0248 98  TYR B O   
3249 C CB  . TYR B 99  ? 0.1466 0.2017 0.1778 -0.0022 -0.0021 -0.0149 98  TYR B CB  
3250 C CG  . TYR B 99  ? 0.1477 0.2030 0.1768 -0.0048 -0.0005 -0.0141 98  TYR B CG  
3251 C CD1 . TYR B 99  ? 0.1593 0.2115 0.1845 -0.0054 -0.0012 -0.0109 98  TYR B CD1 
3252 C CD2 . TYR B 99  ? 0.1855 0.2439 0.2161 -0.0068 0.0018  -0.0166 98  TYR B CD2 
3253 C CE1 . TYR B 99  ? 0.1868 0.2389 0.2097 -0.0076 0.0001  -0.0101 98  TYR B CE1 
3254 C CE2 . TYR B 99  ? 0.1878 0.2457 0.2157 -0.0093 0.0033  -0.0158 98  TYR B CE2 
3255 C CZ  . TYR B 99  ? 0.1872 0.2418 0.2112 -0.0095 0.0023  -0.0124 98  TYR B CZ  
3256 O OH  . TYR B 99  ? 0.1888 0.2426 0.2098 -0.0119 0.0036  -0.0116 98  TYR B OH  
3257 N N   . TYR B 100 ? 0.1836 0.2382 0.2139 0.0033  -0.0062 -0.0221 99  TYR B N   
3258 C CA  . TYR B 100 ? 0.1728 0.2298 0.2050 0.0057  -0.0073 -0.0268 99  TYR B CA  
3259 C C   . TYR B 100 ? 0.2212 0.2788 0.2559 0.0094  -0.0097 -0.0299 99  TYR B C   
3260 O O   . TYR B 100 ? 0.2172 0.2799 0.2565 0.0109  -0.0099 -0.0347 99  TYR B O   
3261 C CB  . TYR B 100 ? 0.1983 0.2611 0.2341 0.0033  -0.0045 -0.0296 99  TYR B CB  
3262 C CG  . TYR B 100 ? 0.2121 0.2732 0.2443 0.0003  -0.0028 -0.0270 99  TYR B CG  
3263 C CD1 . TYR B 100 ? 0.2071 0.2665 0.2367 0.0014  -0.0038 -0.0280 99  TYR B CD1 
3264 C CD2 . TYR B 100 ? 0.1936 0.2543 0.2245 -0.0033 -0.0004 -0.0237 99  TYR B CD2 
3265 C CE1 . TYR B 100 ? 0.2327 0.2905 0.2589 -0.0014 -0.0024 -0.0257 99  TYR B CE1 
3266 C CE2 . TYR B 100 ? 0.1780 0.2369 0.2053 -0.0058 0.0007  -0.0214 99  TYR B CE2 
3267 C CZ  . TYR B 100 ? 0.2284 0.2861 0.2536 -0.0049 -0.0002 -0.0224 99  TYR B CZ  
3268 O OH  . TYR B 100 ? 0.1966 0.2526 0.2181 -0.0073 0.0008  -0.0204 99  TYR B OH  
3269 N N   . ASN B 101 ? 0.1889 0.2412 0.2203 0.0108  -0.0116 -0.0272 100 ASN B N   
3270 C CA  A ASN B 101 ? 0.2375 0.2880 0.2692 0.0143  -0.0143 -0.0291 100 ASN B CA  
3271 C CA  B ASN B 101 ? 0.2372 0.2879 0.2690 0.0144  -0.0144 -0.0293 100 ASN B CA  
3272 C C   . ASN B 101 ? 0.2781 0.3346 0.3160 0.0142  -0.0134 -0.0316 100 ASN B C   
3273 O O   . ASN B 101 ? 0.2503 0.3073 0.2899 0.0175  -0.0157 -0.0347 100 ASN B O   
3274 C CB  A ASN B 101 ? 0.2491 0.2972 0.2788 0.0186  -0.0176 -0.0328 100 ASN B CB  
3275 C CB  B ASN B 101 ? 0.2442 0.2932 0.2745 0.0185  -0.0174 -0.0333 100 ASN B CB  
3276 C CG  A ASN B 101 ? 0.2807 0.3226 0.3066 0.0222  -0.0211 -0.0330 100 ASN B CG  
3277 C CG  B ASN B 101 ? 0.2806 0.3214 0.3030 0.0192  -0.0190 -0.0309 100 ASN B CG  
3278 O OD1 A ASN B 101 ? 0.2691 0.3058 0.2910 0.0211  -0.0210 -0.0291 100 ASN B OD1 
3279 O OD1 B ASN B 101 ? 0.4215 0.4618 0.4421 0.0195  -0.0192 -0.0321 100 ASN B OD1 
3280 N ND2 A ASN B 101 ? 0.3002 0.3427 0.3273 0.0266  -0.0241 -0.0377 100 ASN B ND2 
3281 N ND2 B ASN B 101 ? 0.3269 0.3612 0.3444 0.0191  -0.0200 -0.0276 100 ASN B ND2 
3282 N N   . SER B 102 ? 0.2034 0.2638 0.2441 0.0104  -0.0100 -0.0302 101 SER B N   
3283 C CA  . SER B 102 ? 0.1960 0.2608 0.2414 0.0094  -0.0087 -0.0317 101 SER B CA  
3284 C C   . SER B 102 ? 0.1935 0.2549 0.2367 0.0074  -0.0076 -0.0269 101 SER B C   
3285 O O   . SER B 102 ? 0.1855 0.2445 0.2257 0.0050  -0.0062 -0.0230 101 SER B O   
3286 C CB  . SER B 102 ? 0.2281 0.2994 0.2777 0.0064  -0.0054 -0.0346 101 SER B CB  
3287 O OG  . SER B 102 ? 0.2839 0.3598 0.3370 0.0086  -0.0065 -0.0402 101 SER B OG  
3288 N N   . ILE B 103 ? 0.1944 0.2562 0.2395 0.0084  -0.0082 -0.0274 102 ILE B N   
3289 C CA  . ILE B 103 ? 0.1584 0.2174 0.2019 0.0066  -0.0071 -0.0232 102 ILE B CA  
3290 C C   . ILE B 103 ? 0.1913 0.2519 0.2348 0.0026  -0.0037 -0.0212 102 ILE B C   
3291 O O   . ILE B 103 ? 0.1980 0.2630 0.2444 0.0007  -0.0016 -0.0239 102 ILE B O   
3292 C CB  . ILE B 103 ? 0.1911 0.2511 0.2372 0.0080  -0.0079 -0.0248 102 ILE B CB  
3293 C CG1 . ILE B 103 ? 0.1951 0.2510 0.2390 0.0120  -0.0116 -0.0255 102 ILE B CG1 
3294 C CG2 . ILE B 103 ? 0.2363 0.2945 0.2815 0.0057  -0.0061 -0.0210 102 ILE B CG2 
3295 C CD1 . ILE B 103 ? 0.2487 0.3062 0.2956 0.0141  -0.0131 -0.0284 102 ILE B CD1 
3296 N N   . ILE B 104 ? 0.1875 0.2443 0.2275 0.0014  -0.0033 -0.0166 103 ILE B N   
3297 C CA  . ILE B 104 ? 0.1747 0.2316 0.2135 -0.0019 -0.0006 -0.0144 103 ILE B CA  
3298 C C   . ILE B 104 ? 0.1830 0.2405 0.2233 -0.0029 0.0007  -0.0144 103 ILE B C   
3299 O O   . ILE B 104 ? 0.2171 0.2720 0.2566 -0.0020 -0.0001 -0.0121 103 ILE B O   
3300 C CB  . ILE B 104 ? 0.1664 0.2194 0.2012 -0.0023 -0.0011 -0.0100 103 ILE B CB  
3301 C CG1 . ILE B 104 ? 0.1884 0.2406 0.2213 -0.0016 -0.0022 -0.0101 103 ILE B CG1 
3302 C CG2 . ILE B 104 ? 0.2195 0.2718 0.2523 -0.0051 0.0011  -0.0076 103 ILE B CG2 
3303 C CD1 . ILE B 104 ? 0.1948 0.2438 0.2243 -0.0017 -0.0031 -0.0065 103 ILE B CD1 
3304 N N   . SER B 105 ? 0.2117 0.2726 0.2542 -0.0051 0.0030  -0.0173 104 SER B N   
3305 C CA  . SER B 105 ? 0.2168 0.2785 0.2607 -0.0064 0.0044  -0.0180 104 SER B CA  
3306 C C   . SER B 105 ? 0.2384 0.2975 0.2787 -0.0099 0.0072  -0.0157 104 SER B C   
3307 O O   . SER B 105 ? 0.2316 0.2902 0.2720 -0.0113 0.0087  -0.0160 104 SER B O   
3308 C CB  . SER B 105 ? 0.2472 0.3147 0.2961 -0.0065 0.0050  -0.0236 104 SER B CB  
3309 O OG  . SER B 105 ? 0.2731 0.3434 0.3224 -0.0089 0.0071  -0.0261 104 SER B OG  
3310 N N   . SER B 106 ? 0.2049 0.2615 0.2414 -0.0112 0.0078  -0.0134 105 SER B N   
3311 C CA  . SER B 106 ? 0.2087 0.2616 0.2404 -0.0142 0.0100  -0.0111 105 SER B CA  
3312 C C   . SER B 106 ? 0.1951 0.2433 0.2230 -0.0128 0.0085  -0.0064 105 SER B C   
3313 O O   . SER B 106 ? 0.1864 0.2338 0.2125 -0.0123 0.0074  -0.0047 105 SER B O   
3314 C CB  . SER B 106 ? 0.1949 0.2484 0.2247 -0.0169 0.0120  -0.0127 105 SER B CB  
3315 O OG  . SER B 106 ? 0.2369 0.2851 0.2604 -0.0194 0.0136  -0.0100 105 SER B OG  
3316 N N   . PRO B 107 ? 0.1922 0.2377 0.2190 -0.0122 0.0082  -0.0043 106 PRO B N   
3317 C CA  . PRO B 107 ? 0.1820 0.2237 0.2054 -0.0108 0.0068  -0.0002 106 PRO B CA  
3318 C C   . PRO B 107 ? 0.1970 0.2353 0.2151 -0.0126 0.0076  0.0014  106 PRO B C   
3319 O O   . PRO B 107 ? 0.2302 0.2674 0.2465 -0.0113 0.0059  0.0038  106 PRO B O   
3320 C CB  . PRO B 107 ? 0.2332 0.2726 0.2562 -0.0104 0.0070  0.0009  106 PRO B CB  
3321 C CG  . PRO B 107 ? 0.2531 0.2961 0.2808 -0.0101 0.0073  -0.0023 106 PRO B CG  
3322 C CD  . PRO B 107 ? 0.2244 0.2707 0.2535 -0.0122 0.0089  -0.0058 106 PRO B CD  
3323 N N   . SER B 108 ? 0.2053 0.2420 0.2204 -0.0158 0.0101  0.0000  107 SER B N   
3324 C CA  A SER B 108 ? 0.2297 0.2618 0.2384 -0.0175 0.0108  0.0017  107 SER B CA  
3325 C CA  B SER B 108 ? 0.2296 0.2617 0.2383 -0.0175 0.0108  0.0016  107 SER B CA  
3326 C C   . SER B 108 ? 0.2270 0.2614 0.2363 -0.0174 0.0100  0.0013  107 SER B C   
3327 O O   . SER B 108 ? 0.2231 0.2546 0.2285 -0.0168 0.0087  0.0038  107 SER B O   
3328 C CB  A SER B 108 ? 0.2696 0.2985 0.2740 -0.0215 0.0141  0.0000  107 SER B CB  
3329 C CB  B SER B 108 ? 0.2698 0.2989 0.2743 -0.0216 0.0142  -0.0001 107 SER B CB  
3330 O OG  A SER B 108 ? 0.3122 0.3457 0.3198 -0.0239 0.0162  -0.0040 107 SER B OG  
3331 O OG  B SER B 108 ? 0.2758 0.2991 0.2728 -0.0233 0.0147  0.0016  107 SER B OG  
3332 N N   . ASP B 109 ? 0.1982 0.2377 0.2122 -0.0177 0.0106  -0.0019 108 ASP B N   
3333 C CA  . ASP B 109 ? 0.1967 0.2380 0.2111 -0.0175 0.0098  -0.0023 108 ASP B CA  
3334 C C   . ASP B 109 ? 0.2106 0.2522 0.2260 -0.0144 0.0067  0.0003  108 ASP B C   
3335 O O   . ASP B 109 ? 0.2088 0.2494 0.2218 -0.0143 0.0058  0.0017  108 ASP B O   
3336 C CB  . ASP B 109 ? 0.1951 0.2419 0.2146 -0.0177 0.0106  -0.0065 108 ASP B CB  
3337 C CG  . ASP B 109 ? 0.2744 0.3222 0.2933 -0.0213 0.0139  -0.0098 108 ASP B CG  
3338 O OD1 . ASP B 109 ? 0.2810 0.3242 0.2943 -0.0242 0.0159  -0.0087 108 ASP B OD1 
3339 O OD2 . ASP B 109 ? 0.2899 0.3428 0.3136 -0.0213 0.0145  -0.0138 108 ASP B OD2 
3340 N N   . PHE B 110 ? 0.1852 0.2281 0.2040 -0.0121 0.0054  0.0006  109 PHE B N   
3341 C CA  . PHE B 110 ? 0.1718 0.2150 0.1915 -0.0097 0.0030  0.0025  109 PHE B CA  
3342 C C   . PHE B 110 ? 0.1897 0.2299 0.2058 -0.0093 0.0020  0.0057  109 PHE B C   
3343 O O   . PHE B 110 ? 0.1742 0.2149 0.1899 -0.0084 0.0005  0.0070  109 PHE B O   
3344 C CB  . PHE B 110 ? 0.1483 0.1928 0.1717 -0.0078 0.0021  0.0020  109 PHE B CB  
3345 C CG  . PHE B 110 ? 0.1383 0.1833 0.1627 -0.0058 0.0000  0.0029  109 PHE B CG  
3346 C CD1 . PHE B 110 ? 0.1474 0.1935 0.1720 -0.0056 -0.0008 0.0019  109 PHE B CD1 
3347 C CD2 . PHE B 110 ? 0.1681 0.2123 0.1933 -0.0043 -0.0009 0.0044  109 PHE B CD2 
3348 C CE1 . PHE B 110 ? 0.1731 0.2187 0.1977 -0.0042 -0.0024 0.0025  109 PHE B CE1 
3349 C CE2 . PHE B 110 ? 0.1569 0.2011 0.1826 -0.0031 -0.0023 0.0048  109 PHE B CE2 
3350 C CZ  . PHE B 110 ? 0.1715 0.2162 0.1967 -0.0031 -0.0030 0.0039  109 PHE B CZ  
3351 N N   . GLN B 111 ? 0.2022 0.2393 0.2156 -0.0100 0.0029  0.0067  110 GLN B N   
3352 C CA  . GLN B 111 ? 0.1964 0.2301 0.2057 -0.0092 0.0017  0.0094  110 GLN B CA  
3353 C C   . GLN B 111 ? 0.2082 0.2404 0.2135 -0.0103 0.0015  0.0100  110 GLN B C   
3354 O O   . GLN B 111 ? 0.2155 0.2476 0.2196 -0.0089 -0.0006 0.0117  110 GLN B O   
3355 C CB  . GLN B 111 ? 0.2132 0.2425 0.2190 -0.0097 0.0028  0.0102  110 GLN B CB  
3356 C CG  . GLN B 111 ? 0.1905 0.2155 0.1913 -0.0083 0.0011  0.0128  110 GLN B CG  
3357 C CD  . GLN B 111 ? 0.2585 0.2786 0.2558 -0.0079 0.0015  0.0138  110 GLN B CD  
3358 O OE1 . GLN B 111 ? 0.2789 0.2995 0.2784 -0.0086 0.0031  0.0127  110 GLN B OE1 
3359 N NE2 . GLN B 111 ? 0.2357 0.2510 0.2274 -0.0065 0.0000  0.0157  110 GLN B NE2 
3360 N N   . THR B 112 ? 0.2011 0.2325 0.2044 -0.0129 0.0035  0.0083  111 THR B N   
3361 C CA  . THR B 112 ? 0.1972 0.2268 0.1964 -0.0142 0.0034  0.0088  111 THR B CA  
3362 C C   . THR B 112 ? 0.1935 0.2271 0.1959 -0.0130 0.0017  0.0087  111 THR B C   
3363 O O   . THR B 112 ? 0.1865 0.2192 0.1863 -0.0125 0.0001  0.0102  111 THR B O   
3364 C CB  . THR B 112 ? 0.2293 0.2576 0.2261 -0.0176 0.0063  0.0066  111 THR B CB  
3365 O OG1 . THR B 112 ? 0.2854 0.3089 0.2778 -0.0192 0.0080  0.0068  111 THR B OG1 
3366 C CG2 . THR B 112 ? 0.2365 0.2628 0.2288 -0.0191 0.0063  0.0069  111 THR B CG2 
3367 N N   . PHE B 113 ? 0.1801 0.2178 0.1875 -0.0126 0.0019  0.0068  112 PHE B N   
3368 C CA  . PHE B 113 ? 0.1783 0.2188 0.1880 -0.0115 0.0004  0.0067  112 PHE B CA  
3369 C C   . PHE B 113 ? 0.1859 0.2265 0.1954 -0.0097 -0.0018 0.0090  112 PHE B C   
3370 O O   . PHE B 113 ? 0.1830 0.2243 0.1914 -0.0097 -0.0031 0.0097  112 PHE B O   
3371 C CB  . PHE B 113 ? 0.1789 0.2223 0.1931 -0.0106 0.0005  0.0046  112 PHE B CB  
3372 C CG  . PHE B 113 ? 0.1555 0.2004 0.1710 -0.0095 -0.0011 0.0046  112 PHE B CG  
3373 C CD1 . PHE B 113 ? 0.1684 0.2139 0.1831 -0.0102 -0.0011 0.0034  112 PHE B CD1 
3374 C CD2 . PHE B 113 ? 0.1437 0.1890 0.1608 -0.0079 -0.0025 0.0057  112 PHE B CD2 
3375 C CE1 . PHE B 113 ? 0.1603 0.2062 0.1751 -0.0095 -0.0025 0.0035  112 PHE B CE1 
3376 C CE2 . PHE B 113 ? 0.1608 0.2067 0.1780 -0.0075 -0.0036 0.0056  112 PHE B CE2 
3377 C CZ  . PHE B 113 ? 0.1904 0.2363 0.2062 -0.0083 -0.0037 0.0045  112 PHE B CZ  
3378 N N   . TRP B 114 ? 0.1751 0.2154 0.1861 -0.0083 -0.0023 0.0099  113 TRP B N   
3379 C CA  . TRP B 114 ? 0.1554 0.1969 0.1673 -0.0065 -0.0042 0.0114  113 TRP B CA  
3380 C C   . TRP B 114 ? 0.1524 0.1918 0.1603 -0.0061 -0.0055 0.0130  113 TRP B C   
3381 O O   . TRP B 114 ? 0.1524 0.1939 0.1610 -0.0050 -0.0073 0.0136  113 TRP B O   
3382 C CB  . TRP B 114 ? 0.1346 0.1765 0.1493 -0.0051 -0.0042 0.0115  113 TRP B CB  
3383 C CG  . TRP B 114 ? 0.1592 0.2036 0.1773 -0.0048 -0.0044 0.0104  113 TRP B CG  
3384 C CD1 . TRP B 114 ? 0.1486 0.1932 0.1688 -0.0047 -0.0036 0.0089  113 TRP B CD1 
3385 C CD2 . TRP B 114 ? 0.1612 0.2077 0.1801 -0.0046 -0.0055 0.0105  113 TRP B CD2 
3386 N NE1 . TRP B 114 ? 0.1522 0.1978 0.1736 -0.0043 -0.0043 0.0083  113 TRP B NE1 
3387 C CE2 . TRP B 114 ? 0.1446 0.1914 0.1652 -0.0046 -0.0052 0.0092  113 TRP B CE2 
3388 C CE3 . TRP B 114 ? 0.1738 0.2218 0.1919 -0.0046 -0.0067 0.0112  113 TRP B CE3 
3389 C CZ2 . TRP B 114 ? 0.1674 0.2151 0.1881 -0.0049 -0.0058 0.0089  113 TRP B CZ2 
3390 C CZ3 . TRP B 114 ? 0.1628 0.2130 0.1821 -0.0051 -0.0072 0.0107  113 TRP B CZ3 
3391 C CH2 . TRP B 114 ? 0.1699 0.2196 0.1901 -0.0054 -0.0066 0.0096  113 TRP B CH2 
3392 N N   . LYS B 115 ? 0.1667 0.2018 0.1702 -0.0068 -0.0047 0.0135  114 LYS B N   
3393 C CA  . LYS B 115 ? 0.1694 0.2014 0.1678 -0.0063 -0.0063 0.0150  114 LYS B CA  
3394 C C   . LYS B 115 ? 0.1635 0.1969 0.1609 -0.0073 -0.0070 0.0147  114 LYS B C   
3395 O O   . LYS B 115 ? 0.1854 0.2197 0.1819 -0.0061 -0.0092 0.0154  114 LYS B O   
3396 C CB  . LYS B 115 ? 0.1791 0.2045 0.1712 -0.0074 -0.0051 0.0155  114 LYS B CB  
3397 C CG  . LYS B 115 ? 0.2114 0.2322 0.1971 -0.0061 -0.0074 0.0171  114 LYS B CG  
3398 C CD  . LYS B 115 ? 0.2450 0.2574 0.2222 -0.0076 -0.0062 0.0178  114 LYS B CD  
3399 C CE  . LYS B 115 ? 0.3440 0.3513 0.3142 -0.0057 -0.0092 0.0193  114 LYS B CE  
3400 N NZ  . LYS B 115 ? 0.3914 0.3891 0.3514 -0.0079 -0.0079 0.0198  114 LYS B NZ  
3401 N N   . THR B 116 ? 0.1848 0.2187 0.1826 -0.0096 -0.0050 0.0133  115 THR B N   
3402 C CA  . THR B 116 ? 0.1783 0.2135 0.1751 -0.0107 -0.0054 0.0128  115 THR B CA  
3403 C C   . THR B 116 ? 0.1940 0.2336 0.1945 -0.0095 -0.0072 0.0128  115 THR B C   
3404 O O   . THR B 116 ? 0.2075 0.2478 0.2064 -0.0093 -0.0089 0.0134  115 THR B O   
3405 C CB  . THR B 116 ? 0.1789 0.2146 0.1766 -0.0129 -0.0030 0.0109  115 THR B CB  
3406 O OG1 . THR B 116 ? 0.2085 0.2400 0.2019 -0.0147 -0.0011 0.0106  115 THR B OG1 
3407 C CG2 . THR B 116 ? 0.2094 0.2465 0.2065 -0.0138 -0.0034 0.0103  115 THR B CG2 
3408 N N   . VAL B 117 ? 0.1650 0.2076 0.1702 -0.0088 -0.0069 0.0121  116 VAL B N   
3409 C CA  . VAL B 117 ? 0.1933 0.2395 0.2013 -0.0084 -0.0080 0.0118  116 VAL B CA  
3410 C C   . VAL B 117 ? 0.1666 0.2147 0.1753 -0.0068 -0.0101 0.0127  116 VAL B C   
3411 O O   . VAL B 117 ? 0.1575 0.2081 0.1664 -0.0069 -0.0114 0.0125  116 VAL B O   
3412 C CB  . VAL B 117 ? 0.1741 0.2217 0.1857 -0.0082 -0.0071 0.0107  116 VAL B CB  
3413 C CG1 . VAL B 117 ? 0.1954 0.2457 0.2089 -0.0082 -0.0081 0.0104  116 VAL B CG1 
3414 C CG2 . VAL B 117 ? 0.2136 0.2600 0.2248 -0.0093 -0.0057 0.0092  116 VAL B CG2 
3415 N N   . ALA B 118 ? 0.1727 0.2197 0.1818 -0.0051 -0.0104 0.0135  117 ALA B N   
3416 C CA  . ALA B 118 ? 0.1451 0.1943 0.1554 -0.0030 -0.0125 0.0139  117 ALA B CA  
3417 C C   . ALA B 118 ? 0.1881 0.2363 0.1947 -0.0024 -0.0145 0.0145  117 ALA B C   
3418 O O   . ALA B 118 ? 0.2024 0.2542 0.2106 -0.0010 -0.0167 0.0141  117 ALA B O   
3419 C CB  . ALA B 118 ? 0.2250 0.2723 0.2357 -0.0012 -0.0124 0.0146  117 ALA B CB  
3420 N N   . SER B 119 ? 0.1843 0.2275 0.1856 -0.0034 -0.0140 0.0152  118 SER B N   
3421 C CA  A SER B 119 ? 0.1713 0.2121 0.1677 -0.0028 -0.0161 0.0158  118 SER B CA  
3422 C CA  B SER B 119 ? 0.1709 0.2119 0.1675 -0.0027 -0.0162 0.0158  118 SER B CA  
3423 C C   . SER B 119 ? 0.2135 0.2586 0.2114 -0.0037 -0.0172 0.0150  118 SER B C   
3424 O O   . SER B 119 ? 0.2649 0.3101 0.2604 -0.0025 -0.0197 0.0152  118 SER B O   
3425 C CB  A SER B 119 ? 0.2233 0.2574 0.2132 -0.0046 -0.0146 0.0165  118 SER B CB  
3426 C CB  B SER B 119 ? 0.2255 0.2595 0.2153 -0.0042 -0.0149 0.0166  118 SER B CB  
3427 O OG  A SER B 119 ? 0.2322 0.2614 0.2191 -0.0038 -0.0140 0.0173  118 SER B OG  
3428 O OG  B SER B 119 ? 0.1870 0.2211 0.1767 -0.0071 -0.0127 0.0158  118 SER B OG  
3429 N N   . GLN B 120 ? 0.1885 0.2366 0.1898 -0.0057 -0.0155 0.0140  119 GLN B N   
3430 C CA  . GLN B 120 ? 0.2037 0.2554 0.2059 -0.0069 -0.0162 0.0131  119 GLN B CA  
3431 C C   . GLN B 120 ? 0.1852 0.2429 0.1919 -0.0058 -0.0178 0.0121  119 GLN B C   
3432 O O   . GLN B 120 ? 0.1898 0.2509 0.1972 -0.0067 -0.0188 0.0112  119 GLN B O   
3433 C CB  . GLN B 120 ? 0.2044 0.2563 0.2076 -0.0093 -0.0139 0.0123  119 GLN B CB  
3434 C CG  . GLN B 120 ? 0.2367 0.2842 0.2374 -0.0104 -0.0118 0.0124  119 GLN B CG  
3435 C CD  . GLN B 120 ? 0.2524 0.2962 0.2477 -0.0113 -0.0120 0.0131  119 GLN B CD  
3436 O OE1 . GLN B 120 ? 0.2383 0.2827 0.2316 -0.0116 -0.0135 0.0131  119 GLN B OE1 
3437 N NE2 . GLN B 120 ? 0.2876 0.3271 0.2801 -0.0118 -0.0105 0.0134  119 GLN B NE2 
3438 N N   . PHE B 121 ? 0.1651 0.2245 0.1751 -0.0041 -0.0179 0.0120  120 PHE B N   
3439 C CA  . PHE B 121 ? 0.1433 0.2088 0.1582 -0.0034 -0.0188 0.0106  120 PHE B CA  
3440 C C   . PHE B 121 ? 0.1767 0.2434 0.1929 -0.0001 -0.0208 0.0107  120 PHE B C   
3441 O O   . PHE B 121 ? 0.1646 0.2365 0.1856 0.0006  -0.0210 0.0093  120 PHE B O   
3442 C CB  . PHE B 121 ? 0.1834 0.2502 0.2014 -0.0052 -0.0164 0.0098  120 PHE B CB  
3443 C CG  . PHE B 121 ? 0.1882 0.2537 0.2046 -0.0080 -0.0148 0.0094  120 PHE B CG  
3444 C CD1 . PHE B 121 ? 0.2026 0.2714 0.2193 -0.0098 -0.0152 0.0082  120 PHE B CD1 
3445 C CD2 . PHE B 121 ? 0.1855 0.2465 0.2000 -0.0088 -0.0130 0.0100  120 PHE B CD2 
3446 C CE1 . PHE B 121 ? 0.2004 0.2672 0.2149 -0.0123 -0.0139 0.0078  120 PHE B CE1 
3447 C CE2 . PHE B 121 ? 0.2059 0.2655 0.2188 -0.0109 -0.0119 0.0094  120 PHE B CE2 
3448 C CZ  . PHE B 121 ? 0.2132 0.2752 0.2256 -0.0127 -0.0123 0.0084  120 PHE B CZ  
3449 N N   . ALA B 122 ? 0.1721 0.2339 0.1838 0.0019  -0.0223 0.0121  121 ALA B N   
3450 C CA  . ALA B 122 ? 0.1987 0.2592 0.2105 0.0051  -0.0235 0.0125  121 ALA B CA  
3451 C C   . ALA B 122 ? 0.2006 0.2673 0.2162 0.0079  -0.0264 0.0108  121 ALA B C   
3452 O O   . ALA B 122 ? 0.2366 0.3045 0.2547 0.0103  -0.0269 0.0104  121 ALA B O   
3453 C CB  . ALA B 122 ? 0.2196 0.2720 0.2241 0.0063  -0.0244 0.0143  121 ALA B CB  
3454 N N   . SER B 123 ? 0.1752 0.2462 0.1917 0.0076  -0.0283 0.0094  122 SER B N   
3455 C CA  A SER B 123 ? 0.2256 0.3036 0.2461 0.0103  -0.0313 0.0071  122 SER B CA  
3456 C CA  B SER B 123 ? 0.2260 0.3040 0.2468 0.0104  -0.0312 0.0071  122 SER B CA  
3457 C C   . SER B 123 ? 0.2454 0.3322 0.2730 0.0079  -0.0298 0.0045  122 SER B C   
3458 O O   . SER B 123 ? 0.2679 0.3622 0.2998 0.0093  -0.0319 0.0018  122 SER B O   
3459 C CB  A SER B 123 ? 0.2738 0.3511 0.2903 0.0117  -0.0347 0.0069  122 SER B CB  
3460 C CB  B SER B 123 ? 0.2689 0.3458 0.2856 0.0127  -0.0350 0.0070  122 SER B CB  
3461 O OG  A SER B 123 ? 0.2471 0.3256 0.2631 0.0081  -0.0335 0.0067  122 SER B OG  
3462 O OG  B SER B 123 ? 0.2306 0.2987 0.2404 0.0155  -0.0365 0.0091  122 SER B OG  
3463 N N   . ASN B 124 ? 0.2053 0.2914 0.2339 0.0043  -0.0262 0.0049  123 ASN B N   
3464 C CA  . ASN B 124 ? 0.1597 0.2525 0.1933 0.0014  -0.0245 0.0024  123 ASN B CA  
3465 C C   . ASN B 124 ? 0.1859 0.2801 0.2232 0.0016  -0.0226 0.0018  123 ASN B C   
3466 O O   . ASN B 124 ? 0.1751 0.2642 0.2106 0.0002  -0.0202 0.0034  123 ASN B O   
3467 C CB  . ASN B 124 ? 0.1834 0.2734 0.2143 -0.0027 -0.0221 0.0031  123 ASN B CB  
3468 C CG  . ASN B 124 ? 0.1899 0.2855 0.2242 -0.0061 -0.0204 0.0005  123 ASN B CG  
3469 O OD1 . ASN B 124 ? 0.1823 0.2833 0.2213 -0.0061 -0.0198 -0.0016 123 ASN B OD1 
3470 N ND2 . ASN B 124 ? 0.1784 0.2727 0.2100 -0.0093 -0.0194 0.0005  123 ASN B ND2 
3471 N N   . PRO B 125 ? 0.1883 0.2895 0.2308 0.0031  -0.0236 -0.0007 124 PRO B N   
3472 C CA  . PRO B 125 ? 0.1769 0.2790 0.2226 0.0035  -0.0218 -0.0013 124 PRO B CA  
3473 C C   . PRO B 125 ? 0.1792 0.2820 0.2261 -0.0009 -0.0182 -0.0022 124 PRO B C   
3474 O O   . PRO B 125 ? 0.1865 0.2885 0.2349 -0.0010 -0.0164 -0.0023 124 PRO B O   
3475 C CB  . PRO B 125 ? 0.2124 0.3227 0.2636 0.0065  -0.0242 -0.0043 124 PRO B CB  
3476 C CG  . PRO B 125 ? 0.2530 0.3688 0.3052 0.0057  -0.0261 -0.0064 124 PRO B CG  
3477 C CD  . PRO B 125 ? 0.1844 0.2932 0.2303 0.0050  -0.0266 -0.0035 124 PRO B CD  
3478 N N   . LEU B 126 ? 0.1747 0.2784 0.2205 -0.0045 -0.0171 -0.0030 125 LEU B N   
3479 C CA  . LEU B 126 ? 0.1710 0.2739 0.2163 -0.0088 -0.0138 -0.0040 125 LEU B CA  
3480 C C   . LEU B 126 ? 0.1584 0.2525 0.1983 -0.0102 -0.0122 -0.0013 125 LEU B C   
3481 O O   . LEU B 126 ? 0.1652 0.2568 0.2033 -0.0134 -0.0098 -0.0018 125 LEU B O   
3482 C CB  . LEU B 126 ? 0.1780 0.2867 0.2247 -0.0123 -0.0133 -0.0069 125 LEU B CB  
3483 C CG  . LEU B 126 ? 0.1680 0.2869 0.2212 -0.0117 -0.0142 -0.0107 125 LEU B CG  
3484 C CD1 . LEU B 126 ? 0.1593 0.2839 0.2136 -0.0155 -0.0137 -0.0137 125 LEU B CD1 
3485 C CD2 . LEU B 126 ? 0.1919 0.3126 0.2482 -0.0125 -0.0118 -0.0123 125 LEU B CD2 
3486 N N   . VAL B 127 ? 0.1376 0.2269 0.1746 -0.0080 -0.0135 0.0013  126 VAL B N   
3487 C CA  . VAL B 127 ? 0.1168 0.1986 0.1496 -0.0088 -0.0121 0.0033  126 VAL B CA  
3488 C C   . VAL B 127 ? 0.1441 0.2232 0.1777 -0.0072 -0.0111 0.0042  126 VAL B C   
3489 O O   . VAL B 127 ? 0.1762 0.2570 0.2121 -0.0045 -0.0123 0.0044  126 VAL B O   
3490 C CB  . VAL B 127 ? 0.1184 0.1966 0.1478 -0.0074 -0.0135 0.0052  126 VAL B CB  
3491 C CG1 . VAL B 127 ? 0.1718 0.2433 0.1979 -0.0078 -0.0121 0.0069  126 VAL B CG1 
3492 C CG2 . VAL B 127 ? 0.1776 0.2580 0.2058 -0.0093 -0.0143 0.0044  126 VAL B CG2 
3493 N N   . ILE B 128 ? 0.1284 0.2029 0.1598 -0.0089 -0.0092 0.0045  127 ILE B N   
3494 C CA  . ILE B 128 ? 0.1284 0.1994 0.1600 -0.0077 -0.0083 0.0054  127 ILE B CA  
3495 C C   . ILE B 128 ? 0.1319 0.1970 0.1601 -0.0074 -0.0080 0.0069  127 ILE B C   
3496 O O   . ILE B 128 ? 0.1619 0.2247 0.1873 -0.0092 -0.0075 0.0067  127 ILE B O   
3497 C CB  . ILE B 128 ? 0.1369 0.2077 0.1687 -0.0098 -0.0064 0.0040  127 ILE B CB  
3498 C CG1 . ILE B 128 ? 0.1256 0.2031 0.1615 -0.0101 -0.0064 0.0019  127 ILE B CG1 
3499 C CG2 . ILE B 128 ? 0.1411 0.2074 0.1722 -0.0085 -0.0056 0.0049  127 ILE B CG2 
3500 C CD1 . ILE B 128 ? 0.1289 0.2061 0.1642 -0.0133 -0.0040 0.0000  127 ILE B CD1 
3501 N N   . PHE B 129 ? 0.1348 0.1977 0.1631 -0.0052 -0.0083 0.0082  128 PHE B N   
3502 C CA  . PHE B 129 ? 0.1537 0.2120 0.1795 -0.0050 -0.0079 0.0092  128 PHE B CA  
3503 C C   . PHE B 129 ? 0.1391 0.1943 0.1648 -0.0050 -0.0068 0.0089  128 PHE B C   
3504 O O   . PHE B 129 ? 0.1767 0.2323 0.2042 -0.0040 -0.0065 0.0090  128 PHE B O   
3505 C CB  . PHE B 129 ? 0.1596 0.2169 0.1849 -0.0032 -0.0087 0.0105  128 PHE B CB  
3506 C CG  . PHE B 129 ? 0.1583 0.2176 0.1828 -0.0028 -0.0102 0.0108  128 PHE B CG  
3507 C CD1 . PHE B 129 ? 0.1498 0.2087 0.1722 -0.0043 -0.0104 0.0107  128 PHE B CD1 
3508 C CD2 . PHE B 129 ? 0.1551 0.2164 0.1808 -0.0007 -0.0117 0.0111  128 PHE B CD2 
3509 C CE1 . PHE B 129 ? 0.1347 0.1951 0.1558 -0.0039 -0.0120 0.0109  128 PHE B CE1 
3510 C CE2 . PHE B 129 ? 0.1530 0.2157 0.1774 0.0000  -0.0136 0.0112  128 PHE B CE2 
3511 C CZ  . PHE B 129 ? 0.1512 0.2135 0.1733 -0.0016 -0.0137 0.0112  128 PHE B CZ  
3512 N N   . ASP B 130 ? 0.1134 0.1654 0.1368 -0.0059 -0.0063 0.0084  129 ASP B N   
3513 C CA  . ASP B 130 ? 0.1284 0.1769 0.1509 -0.0057 -0.0057 0.0078  129 ASP B CA  
3514 C C   . ASP B 130 ? 0.1454 0.1916 0.1676 -0.0046 -0.0057 0.0079  129 ASP B C   
3515 O O   . ASP B 130 ? 0.1604 0.2060 0.1812 -0.0050 -0.0059 0.0075  129 ASP B O   
3516 C CB  . ASP B 130 ? 0.1338 0.1798 0.1531 -0.0075 -0.0054 0.0067  129 ASP B CB  
3517 C CG  . ASP B 130 ? 0.1510 0.1924 0.1682 -0.0073 -0.0051 0.0060  129 ASP B CG  
3518 O OD1 . ASP B 130 ? 0.1752 0.2152 0.1934 -0.0055 -0.0053 0.0062  129 ASP B OD1 
3519 O OD2 . ASP B 130 ? 0.1699 0.2087 0.1840 -0.0090 -0.0046 0.0052  129 ASP B OD2 
3520 N N   . THR B 131 ? 0.1371 0.1826 0.1607 -0.0033 -0.0055 0.0082  130 THR B N   
3521 C CA  . THR B 131 ? 0.1250 0.1698 0.1490 -0.0026 -0.0053 0.0081  130 THR B CA  
3522 C C   . THR B 131 ? 0.1567 0.1998 0.1794 -0.0027 -0.0054 0.0065  130 THR B C   
3523 O O   . THR B 131 ? 0.1561 0.1998 0.1787 -0.0031 -0.0051 0.0060  130 THR B O   
3524 C CB  . THR B 131 ? 0.1379 0.1820 0.1634 -0.0015 -0.0048 0.0085  130 THR B CB  
3525 O OG1 . THR B 131 ? 0.1523 0.1944 0.1778 -0.0009 -0.0049 0.0075  130 THR B OG1 
3526 C CG2 . THR B 131 ? 0.1201 0.1656 0.1466 -0.0009 -0.0049 0.0099  130 THR B CG2 
3527 N N   . ASN B 132 ? 0.1557 0.1962 0.1771 -0.0023 -0.0058 0.0055  131 ASN B N   
3528 C CA  . ASN B 132 ? 0.1364 0.1747 0.1560 -0.0019 -0.0064 0.0038  131 ASN B CA  
3529 C C   . ASN B 132 ? 0.1564 0.1905 0.1730 -0.0016 -0.0071 0.0032  131 ASN B C   
3530 O O   . ASN B 132 ? 0.1692 0.2023 0.1863 -0.0013 -0.0069 0.0037  131 ASN B O   
3531 C CB  . ASN B 132 ? 0.1318 0.1707 0.1534 -0.0006 -0.0064 0.0023  131 ASN B CB  
3532 C CG  . ASN B 132 ? 0.1848 0.2247 0.2062 -0.0008 -0.0064 0.0007  131 ASN B CG  
3533 O OD1 . ASN B 132 ? 0.1658 0.2044 0.1868 0.0005  -0.0074 -0.0015 131 ASN B OD1 
3534 N ND2 . ASN B 132 ? 0.1387 0.1809 0.1605 -0.0022 -0.0056 0.0016  131 ASN B ND2 
3535 N N   . ASN B 133 ? 0.1604 0.1914 0.1735 -0.0017 -0.0078 0.0020  132 ASN B N   
3536 C CA  . ASN B 133 ? 0.1674 0.1927 0.1759 -0.0014 -0.0086 0.0013  132 ASN B CA  
3537 C C   . ASN B 133 ? 0.1809 0.2032 0.1890 0.0011  -0.0099 -0.0002 132 ASN B C   
3538 O O   . ASN B 133 ? 0.1780 0.2007 0.1868 0.0028  -0.0109 -0.0019 132 ASN B O   
3539 C CB  . ASN B 133 ? 0.1723 0.1941 0.1759 -0.0023 -0.0091 0.0006  132 ASN B CB  
3540 C CG  . ASN B 133 ? 0.1735 0.1877 0.1706 -0.0023 -0.0099 -0.0002 132 ASN B CG  
3541 O OD1 . ASN B 133 ? 0.1862 0.1985 0.1810 -0.0042 -0.0089 0.0006  132 ASN B OD1 
3542 N ND2 . ASN B 133 ? 0.1882 0.1977 0.1819 0.0000  -0.0117 -0.0020 132 ASN B ND2 
3543 N N   . GLN B 134 ? 0.1507 0.1705 0.1580 0.0014  -0.0099 0.0002  133 GLN B N   
3544 C CA  A GLN B 134 ? 0.1509 0.1660 0.1558 0.0037  -0.0115 -0.0014 133 GLN B CA  
3545 C CA  B GLN B 134 ? 0.1513 0.1664 0.1562 0.0037  -0.0115 -0.0014 133 GLN B CA  
3546 C C   . GLN B 134 ? 0.1926 0.2111 0.2019 0.0061  -0.0124 -0.0031 133 GLN B C   
3547 O O   . GLN B 134 ? 0.2020 0.2189 0.2101 0.0082  -0.0142 -0.0054 133 GLN B O   
3548 C CB  A GLN B 134 ? 0.1877 0.1953 0.1851 0.0041  -0.0130 -0.0025 133 GLN B CB  
3549 C CB  B GLN B 134 ? 0.1878 0.1955 0.1854 0.0042  -0.0130 -0.0027 133 GLN B CB  
3550 C CG  A GLN B 134 ? 0.1737 0.1769 0.1658 0.0012  -0.0117 -0.0013 133 GLN B CG  
3551 C CG  B GLN B 134 ? 0.1807 0.1827 0.1721 0.0019  -0.0122 -0.0017 133 GLN B CG  
3552 C CD  A GLN B 134 ? 0.2118 0.2064 0.1951 0.0010  -0.0129 -0.0024 133 GLN B CD  
3553 C CD  B GLN B 134 ? 0.2285 0.2207 0.2111 0.0031  -0.0142 -0.0031 133 GLN B CD  
3554 O OE1 A GLN B 134 ? 0.2404 0.2343 0.2223 0.0021  -0.0140 -0.0034 133 GLN B OE1 
3555 O OE1 B GLN B 134 ? 0.2126 0.2030 0.1935 0.0053  -0.0161 -0.0048 133 GLN B OE1 
3556 N NE2 A GLN B 134 ? 0.2349 0.2224 0.2116 -0.0005 -0.0125 -0.0022 133 GLN B NE2 
3557 N NE2 B GLN B 134 ? 0.2532 0.2388 0.2299 0.0017  -0.0137 -0.0027 133 GLN B NE2 
3558 N N   . TYR B 135 ? 0.1769 0.2003 0.1914 0.0057  -0.0111 -0.0023 134 TYR B N   
3559 C CA  . TYR B 135 ? 0.1412 0.1675 0.1596 0.0074  -0.0117 -0.0042 134 TYR B CA  
3560 C C   . TYR B 135 ? 0.1657 0.1872 0.1814 0.0099  -0.0138 -0.0060 134 TYR B C   
3561 O O   . TYR B 135 ? 0.1816 0.1979 0.1932 0.0098  -0.0142 -0.0050 134 TYR B O   
3562 C CB  . TYR B 135 ? 0.1363 0.1663 0.1588 0.0064  -0.0099 -0.0027 134 TYR B CB  
3563 C CG  . TYR B 135 ? 0.1510 0.1847 0.1753 0.0043  -0.0081 -0.0007 134 TYR B CG  
3564 C CD1 . TYR B 135 ? 0.1515 0.1846 0.1746 0.0030  -0.0074 0.0016  134 TYR B CD1 
3565 C CD2 . TYR B 135 ? 0.1617 0.1992 0.1886 0.0037  -0.0073 -0.0015 134 TYR B CD2 
3566 C CE1 . TYR B 135 ? 0.1595 0.1957 0.1840 0.0016  -0.0062 0.0032  134 TYR B CE1 
3567 C CE2 . TYR B 135 ? 0.1675 0.2072 0.1950 0.0020  -0.0059 0.0003  134 TYR B CE2 
3568 C CZ  . TYR B 135 ? 0.1391 0.1781 0.1653 0.0012  -0.0056 0.0027  134 TYR B CZ  
3569 O OH  . TYR B 135 ? 0.1464 0.1874 0.1729 0.0000  -0.0048 0.0043  134 TYR B OH  
3570 N N   . HIS B 136 ? 0.1518 0.1750 0.1697 0.0122  -0.0153 -0.0090 135 HIS B N   
3571 C CA  . HIS B 136 ? 0.1498 0.1687 0.1653 0.0151  -0.0179 -0.0111 135 HIS B CA  
3572 C C   . HIS B 136 ? 0.1608 0.1848 0.1814 0.0172  -0.0189 -0.0147 135 HIS B C   
3573 O O   . HIS B 136 ? 0.1983 0.2278 0.2228 0.0166  -0.0180 -0.0161 135 HIS B O   
3574 C CB  . HIS B 136 ? 0.1893 0.2007 0.1975 0.0166  -0.0202 -0.0119 135 HIS B CB  
3575 C CG  . HIS B 136 ? 0.1851 0.1982 0.1936 0.0178  -0.0211 -0.0141 135 HIS B CG  
3576 N ND1 . HIS B 136 ? 0.1946 0.2081 0.2039 0.0214  -0.0238 -0.0179 135 HIS B ND1 
3577 C CD2 . HIS B 136 ? 0.1867 0.2017 0.1952 0.0160  -0.0198 -0.0132 135 HIS B CD2 
3578 C CE1 . HIS B 136 ? 0.1994 0.2147 0.2090 0.0217  -0.0241 -0.0194 135 HIS B CE1 
3579 N NE2 . HIS B 136 ? 0.2076 0.2236 0.2165 0.0184  -0.0216 -0.0164 135 HIS B NE2 
3580 N N   . ASP B 137 ? 0.1539 0.1758 0.1742 0.0196  -0.0210 -0.0165 136 ASP B N   
3581 C CA  . ASP B 137 ? 0.1634 0.1902 0.1885 0.0221  -0.0226 -0.0208 136 ASP B CA  
3582 C C   . ASP B 137 ? 0.1620 0.1976 0.1943 0.0197  -0.0197 -0.0216 136 ASP B C   
3583 O O   . ASP B 137 ? 0.1923 0.2331 0.2284 0.0202  -0.0197 -0.0248 136 ASP B O   
3584 C CB  . ASP B 137 ? 0.1780 0.2027 0.2007 0.0255  -0.0258 -0.0243 136 ASP B CB  
3585 C CG  . ASP B 137 ? 0.2178 0.2321 0.2317 0.0279  -0.0287 -0.0237 136 ASP B CG  
3586 O OD1 . ASP B 137 ? 0.2551 0.2657 0.2670 0.0298  -0.0306 -0.0244 136 ASP B OD1 
3587 O OD2 . ASP B 137 ? 0.2411 0.2502 0.2493 0.0276  -0.0291 -0.0225 136 ASP B OD2 
3588 N N   . MET B 138 ? 0.1762 0.2131 0.2101 0.0169  -0.0171 -0.0187 137 MET B N   
3589 C CA  . MET B 138 ? 0.1698 0.2133 0.2088 0.0143  -0.0142 -0.0189 137 MET B CA  
3590 C C   . MET B 138 ? 0.1639 0.2070 0.2038 0.0127  -0.0126 -0.0168 137 MET B C   
3591 O O   . MET B 138 ? 0.1857 0.2240 0.2224 0.0134  -0.0134 -0.0148 137 MET B O   
3592 C CB  . MET B 138 ? 0.1743 0.2188 0.2125 0.0118  -0.0121 -0.0168 137 MET B CB  
3593 C CG  . MET B 138 ? 0.1989 0.2387 0.2329 0.0106  -0.0116 -0.0124 137 MET B CG  
3594 S SD  . MET B 138 ? 0.1968 0.2371 0.2290 0.0088  -0.0105 -0.0108 137 MET B SD  
3595 C CE  . MET B 138 ? 0.2046 0.2501 0.2404 0.0058  -0.0073 -0.0101 137 MET B CE  
3596 N N   . ASP B 139 ? 0.1662 0.2142 0.2100 0.0105  -0.0101 -0.0176 138 ASP B N   
3597 C CA  . ASP B 139 ? 0.1442 0.1921 0.1888 0.0091  -0.0086 -0.0162 138 ASP B CA  
3598 C C   . ASP B 139 ? 0.1774 0.2209 0.2184 0.0080  -0.0076 -0.0114 138 ASP B C   
3599 O O   . ASP B 139 ? 0.1759 0.2191 0.2155 0.0067  -0.0066 -0.0093 138 ASP B O   
3600 C CB  . ASP B 139 ? 0.1941 0.2471 0.2422 0.0063  -0.0059 -0.0179 138 ASP B CB  
3601 C CG  . ASP B 139 ? 0.2312 0.2835 0.2795 0.0047  -0.0042 -0.0166 138 ASP B CG  
3602 O OD1 . ASP B 139 ? 0.2444 0.2984 0.2952 0.0054  -0.0049 -0.0193 138 ASP B OD1 
3603 O OD2 . ASP B 139 ? 0.2122 0.2620 0.2581 0.0028  -0.0024 -0.0131 138 ASP B OD2 
3604 N N   . GLN B 140 ? 0.2009 0.1840 0.2074 -0.0137 -0.0300 -0.0078 139 GLN B N   
3605 C CA  . GLN B 140 ? 0.1813 0.1597 0.1815 -0.0111 -0.0279 -0.0067 139 GLN B CA  
3606 C C   . GLN B 140 ? 0.2417 0.2153 0.2380 -0.0115 -0.0256 -0.0075 139 GLN B C   
3607 O O   . GLN B 140 ? 0.2154 0.1877 0.2101 -0.0091 -0.0233 -0.0064 139 GLN B O   
3608 C CB  . GLN B 140 ? 0.2359 0.2106 0.2288 -0.0104 -0.0295 -0.0065 139 GLN B CB  
3609 C CG  . GLN B 140 ? 0.2247 0.1954 0.2118 -0.0075 -0.0272 -0.0056 139 GLN B CG  
3610 C CD  . GLN B 140 ? 0.2511 0.2258 0.2422 -0.0051 -0.0258 -0.0038 139 GLN B CD  
3611 O OE1 . GLN B 140 ? 0.2365 0.2153 0.2323 -0.0052 -0.0273 -0.0028 139 GLN B OE1 
3612 N NE2 . GLN B 140 ? 0.2163 0.1898 0.2053 -0.0030 -0.0229 -0.0033 139 GLN B NE2 
3613 N N   . THR B 141 ? 0.2152 0.1860 0.2092 -0.0146 -0.0263 -0.0095 140 THR B N   
3614 C CA  . THR B 141 ? 0.2176 0.1831 0.2077 -0.0151 -0.0243 -0.0101 140 THR B CA  
3615 C C   . THR B 141 ? 0.2342 0.2036 0.2309 -0.0157 -0.0227 -0.0096 140 THR B C   
3616 O O   . THR B 141 ? 0.2277 0.1945 0.2224 -0.0143 -0.0207 -0.0087 140 THR B O   
3617 C CB  . THR B 141 ? 0.2494 0.2103 0.2346 -0.0190 -0.0253 -0.0125 140 THR B CB  
3618 O OG1 . THR B 141 ? 0.2656 0.2221 0.2436 -0.0187 -0.0263 -0.0130 140 THR B OG1 
3619 C CG2 . THR B 141 ? 0.2559 0.2101 0.2363 -0.0196 -0.0233 -0.0131 140 THR B CG2 
3620 N N   . LEU B 142 ? 0.2106 0.1865 0.2153 -0.0176 -0.0236 -0.0100 141 LEU B N   
3621 C CA  . LEU B 142 ? 0.2316 0.2113 0.2425 -0.0185 -0.0217 -0.0096 141 LEU B CA  
3622 C C   . LEU B 142 ? 0.2054 0.1866 0.2170 -0.0151 -0.0198 -0.0072 141 LEU B C   
3623 O O   . LEU B 142 ? 0.1987 0.1797 0.2107 -0.0153 -0.0178 -0.0065 141 LEU B O   
3624 C CB  . LEU B 142 ? 0.2249 0.2113 0.2446 -0.0207 -0.0226 -0.0106 141 LEU B CB  
3625 C CG  . LEU B 142 ? 0.1882 0.1789 0.2149 -0.0220 -0.0204 -0.0103 141 LEU B CG  
3626 C CD1 . LEU B 142 ? 0.1928 0.1803 0.2174 -0.0254 -0.0189 -0.0115 141 LEU B CD1 
3627 C CD2 . LEU B 142 ? 0.2417 0.2388 0.2771 -0.0233 -0.0212 -0.0114 141 LEU B CD2 
3628 N N   . VAL B 143 ? 0.2020 0.1848 0.2134 -0.0123 -0.0204 -0.0059 142 VAL B N   
3629 C CA  . VAL B 143 ? 0.1780 0.1626 0.1894 -0.0095 -0.0184 -0.0040 142 VAL B CA  
3630 C C   . VAL B 143 ? 0.2038 0.1842 0.2093 -0.0077 -0.0169 -0.0034 142 VAL B C   
3631 O O   . VAL B 143 ? 0.1978 0.1802 0.2046 -0.0070 -0.0149 -0.0022 142 VAL B O   
3632 C CB  . VAL B 143 ? 0.1742 0.1600 0.1847 -0.0073 -0.0193 -0.0030 142 VAL B CB  
3633 C CG1 . VAL B 143 ? 0.1883 0.1753 0.1973 -0.0048 -0.0169 -0.0013 142 VAL B CG1 
3634 C CG2 . VAL B 143 ? 0.2007 0.1909 0.2179 -0.0083 -0.0206 -0.0029 142 VAL B CG2 
3635 N N   . LEU B 144 ? 0.2079 0.1825 0.2068 -0.0069 -0.0178 -0.0043 143 LEU B N   
3636 C CA  . LEU B 144 ? 0.2099 0.1796 0.2031 -0.0048 -0.0164 -0.0039 143 LEU B CA  
3637 C C   . LEU B 144 ? 0.2156 0.1847 0.2103 -0.0065 -0.0155 -0.0038 143 LEU B C   
3638 O O   . LEU B 144 ? 0.2128 0.1828 0.2074 -0.0047 -0.0139 -0.0023 143 LEU B O   
3639 C CB  . LEU B 144 ? 0.2300 0.1924 0.2156 -0.0045 -0.0173 -0.0053 143 LEU B CB  
3640 C CG  . LEU B 144 ? 0.2080 0.1638 0.1874 -0.0022 -0.0158 -0.0052 143 LEU B CG  
3641 C CD1 . LEU B 144 ? 0.2847 0.2424 0.2634 0.0023  -0.0139 -0.0037 143 LEU B CD1 
3642 C CD2 . LEU B 144 ? 0.2574 0.2050 0.2289 -0.0030 -0.0165 -0.0069 143 LEU B CD2 
3643 N N   . ASN B 145 ? 0.2121 0.1801 0.2081 -0.0104 -0.0166 -0.0054 144 ASN B N   
3644 C CA  . ASN B 145 ? 0.2163 0.1823 0.2123 -0.0128 -0.0159 -0.0056 144 ASN B CA  
3645 C C   . ASN B 145 ? 0.2100 0.1825 0.2125 -0.0138 -0.0144 -0.0042 144 ASN B C   
3646 O O   . ASN B 145 ? 0.2267 0.1979 0.2281 -0.0144 -0.0135 -0.0033 144 ASN B O   
3647 C CB  . ASN B 145 ? 0.2345 0.1985 0.2305 -0.0175 -0.0171 -0.0080 144 ASN B CB  
3648 C CG  . ASN B 145 ? 0.2681 0.2245 0.2560 -0.0177 -0.0182 -0.0095 144 ASN B CG  
3649 O OD1 . ASN B 145 ? 0.3127 0.2634 0.2941 -0.0144 -0.0176 -0.0087 144 ASN B OD1 
3650 N ND2 . ASN B 145 ? 0.2570 0.2132 0.2452 -0.0218 -0.0196 -0.0118 144 ASN B ND2 
3651 N N   . LEU B 146 ? 0.1890 0.1678 0.1977 -0.0142 -0.0142 -0.0041 145 LEU B N   
3652 C CA  . LEU B 146 ? 0.1767 0.1612 0.1909 -0.0153 -0.0124 -0.0028 145 LEU B CA  
3653 C C   . LEU B 146 ? 0.1953 0.1813 0.2074 -0.0119 -0.0109 -0.0006 145 LEU B C   
3654 O O   . LEU B 146 ? 0.1808 0.1689 0.1940 -0.0130 -0.0095 0.0006  145 LEU B O   
3655 C CB  . LEU B 146 ? 0.1761 0.1661 0.1968 -0.0161 -0.0122 -0.0032 145 LEU B CB  
3656 C CG  . LEU B 146 ? 0.1862 0.1771 0.2113 -0.0197 -0.0133 -0.0054 145 LEU B CG  
3657 C CD1 . LEU B 146 ? 0.2077 0.2036 0.2391 -0.0193 -0.0132 -0.0054 145 LEU B CD1 
3658 C CD2 . LEU B 146 ? 0.2183 0.2093 0.2454 -0.0240 -0.0120 -0.0064 145 LEU B CD2 
3659 N N   . ASN B 147 ? 0.1877 0.1731 0.1968 -0.0081 -0.0112 0.0000  146 ASN B N   
3660 C CA  . ASN B 147 ? 0.1740 0.1613 0.1811 -0.0048 -0.0097 0.0017  146 ASN B CA  
3661 C C   . ASN B 147 ? 0.1914 0.1747 0.1945 -0.0036 -0.0097 0.0024  146 ASN B C   
3662 O O   . ASN B 147 ? 0.1827 0.1696 0.1868 -0.0028 -0.0085 0.0041  146 ASN B O   
3663 C CB  . ASN B 147 ? 0.1742 0.1606 0.1780 -0.0013 -0.0100 0.0016  146 ASN B CB  
3664 C CG  . ASN B 147 ? 0.1818 0.1732 0.1888 -0.0017 -0.0094 0.0020  146 ASN B CG  
3665 O OD1 . ASN B 147 ? 0.1887 0.1851 0.1973 -0.0012 -0.0074 0.0032  146 ASN B OD1 
3666 N ND2 . ASN B 147 ? 0.2063 0.1965 0.2142 -0.0028 -0.0110 0.0010  146 ASN B ND2 
3667 N N   . GLN B 148 ? 0.1810 0.1570 0.1795 -0.0038 -0.0110 0.0012  147 GLN B N   
3668 C CA  . GLN B 148 ? 0.1777 0.1486 0.1717 -0.0024 -0.0110 0.0020  147 GLN B CA  
3669 C C   . GLN B 148 ? 0.1992 0.1716 0.1957 -0.0061 -0.0108 0.0027  147 GLN B C   
3670 O O   . GLN B 148 ? 0.1977 0.1701 0.1929 -0.0046 -0.0103 0.0046  147 GLN B O   
3671 C CB  . GLN B 148 ? 0.2245 0.1859 0.2118 -0.0023 -0.0121 0.0003  147 GLN B CB  
3672 C CG  . GLN B 148 ? 0.1875 0.1423 0.1690 0.0004  -0.0118 0.0014  147 GLN B CG  
3673 C CD  . GLN B 148 ? 0.2534 0.2101 0.2340 0.0063  -0.0107 0.0030  147 GLN B CD  
3674 O OE1 . GLN B 148 ? 0.2405 0.1962 0.2191 0.0088  -0.0102 0.0021  147 GLN B OE1 
3675 N NE2 . GLN B 148 ? 0.2154 0.1754 0.1975 0.0082  -0.0102 0.0052  147 GLN B NE2 
3676 N N   . ALA B 149 ? 0.1727 0.1461 0.1727 -0.0109 -0.0111 0.0011  148 ALA B N   
3677 C CA  . ALA B 149 ? 0.2031 0.1781 0.2055 -0.0152 -0.0106 0.0015  148 ALA B CA  
3678 C C   . ALA B 149 ? 0.2099 0.1923 0.2162 -0.0148 -0.0090 0.0037  148 ALA B C   
3679 O O   . ALA B 149 ? 0.2028 0.1856 0.2085 -0.0165 -0.0087 0.0052  148 ALA B O   
3680 C CB  . ALA B 149 ? 0.2155 0.1918 0.2222 -0.0203 -0.0107 -0.0009 148 ALA B CB  
3681 N N   . ALA B 150 ? 0.1757 0.1641 0.1857 -0.0132 -0.0080 0.0041  149 ALA B N   
3682 C CA  . ALA B 150 ? 0.1782 0.1740 0.1913 -0.0133 -0.0062 0.0060  149 ALA B CA  
3683 C C   . ALA B 150 ? 0.1826 0.1788 0.1924 -0.0094 -0.0063 0.0082  149 ALA B C   
3684 O O   . ALA B 150 ? 0.1733 0.1732 0.1839 -0.0109 -0.0057 0.0101  149 ALA B O   
3685 C CB  . ALA B 150 ? 0.1847 0.1854 0.2008 -0.0122 -0.0051 0.0058  149 ALA B CB  
3686 N N   . ILE B 151 ? 0.1689 0.1617 0.1749 -0.0045 -0.0070 0.0081  150 ILE B N   
3687 C CA  . ILE B 151 ? 0.1512 0.1441 0.1542 0.0000  -0.0071 0.0100  150 ILE B CA  
3688 C C   . ILE B 151 ? 0.1778 0.1663 0.1783 -0.0012 -0.0082 0.0112  150 ILE B C   
3689 O O   . ILE B 151 ? 0.1945 0.1871 0.1956 -0.0004 -0.0080 0.0136  150 ILE B O   
3690 C CB  . ILE B 151 ? 0.1828 0.1706 0.1816 0.0050  -0.0075 0.0090  150 ILE B CB  
3691 C CG1 . ILE B 151 ? 0.1801 0.1729 0.1810 0.0061  -0.0064 0.0083  150 ILE B CG1 
3692 C CG2 . ILE B 151 ? 0.2083 0.1949 0.2041 0.0101  -0.0075 0.0108  150 ILE B CG2 
3693 C CD1 . ILE B 151 ? 0.1911 0.1781 0.1876 0.0094  -0.0068 0.0067  150 ILE B CD1 
3694 N N   . ASP B 152 ? 0.1800 0.1602 0.1772 -0.0035 -0.0094 0.0096  151 ASP B N   
3695 C CA  . ASP B 152 ? 0.1803 0.1545 0.1735 -0.0049 -0.0105 0.0106  151 ASP B CA  
3696 C C   . ASP B 152 ? 0.2228 0.2027 0.2196 -0.0097 -0.0100 0.0120  151 ASP B C   
3697 O O   . ASP B 152 ? 0.2187 0.1980 0.2134 -0.0094 -0.0107 0.0143  151 ASP B O   
3698 C CB  . ASP B 152 ? 0.1838 0.1484 0.1726 -0.0077 -0.0115 0.0081  151 ASP B CB  
3699 C CG  . ASP B 152 ? 0.2642 0.2216 0.2477 -0.0034 -0.0119 0.0069  151 ASP B CG  
3700 O OD1 . ASP B 152 ? 0.2304 0.1896 0.2135 0.0021  -0.0114 0.0081  151 ASP B OD1 
3701 O OD2 . ASP B 152 ? 0.2547 0.2050 0.2345 -0.0060 -0.0125 0.0047  151 ASP B OD2 
3702 N N   . GLY B 153 ? 0.1858 0.1707 0.1877 -0.0144 -0.0088 0.0106  152 GLY B N   
3703 C CA  . GLY B 153 ? 0.1848 0.1747 0.1898 -0.0196 -0.0079 0.0116  152 GLY B CA  
3704 C C   . GLY B 153 ? 0.1727 0.1709 0.1796 -0.0176 -0.0070 0.0145  152 GLY B C   
3705 O O   . GLY B 153 ? 0.1939 0.1941 0.2002 -0.0198 -0.0073 0.0166  152 GLY B O   
3706 N N   . ILE B 154 ? 0.1637 0.1673 0.1729 -0.0139 -0.0060 0.0145  153 ILE B N   
3707 C CA  . ILE B 154 ? 0.1638 0.1762 0.1748 -0.0120 -0.0051 0.0169  153 ILE B CA  
3708 C C   . ILE B 154 ? 0.1860 0.1973 0.1937 -0.0079 -0.0068 0.0195  153 ILE B C   
3709 O O   . ILE B 154 ? 0.1668 0.1838 0.1754 -0.0093 -0.0069 0.0220  153 ILE B O   
3710 C CB  . ILE B 154 ? 0.1538 0.1706 0.1665 -0.0083 -0.0038 0.0161  153 ILE B CB  
3711 C CG1 . ILE B 154 ? 0.1434 0.1623 0.1595 -0.0124 -0.0020 0.0142  153 ILE B CG1 
3712 C CG2 . ILE B 154 ? 0.1668 0.1926 0.1806 -0.0056 -0.0029 0.0183  153 ILE B CG2 
3713 C CD1 . ILE B 154 ? 0.1600 0.1788 0.1761 -0.0090 -0.0015 0.0128  153 ILE B CD1 
3714 N N   . ARG B 155 ? 0.1738 0.1778 0.1776 -0.0027 -0.0081 0.0191  154 ARG B N   
3715 C CA  . ARG B 155 ? 0.1812 0.1837 0.1819 0.0022  -0.0097 0.0216  154 ARG B CA  
3716 C C   . ARG B 155 ? 0.1901 0.1875 0.1877 -0.0013 -0.0114 0.0232  154 ARG B C   
3717 O O   . ARG B 155 ? 0.2106 0.2106 0.2074 0.0007  -0.0126 0.0263  154 ARG B O   
3718 C CB  . ARG B 155 ? 0.1905 0.1853 0.1873 0.0085  -0.0102 0.0206  154 ARG B CB  
3719 C CG  . ARG B 155 ? 0.1635 0.1631 0.1626 0.0120  -0.0085 0.0190  154 ARG B CG  
3720 C CD  . ARG B 155 ? 0.1656 0.1777 0.1692 0.0135  -0.0073 0.0207  154 ARG B CD  
3721 N NE  . ARG B 155 ? 0.1847 0.1999 0.1893 0.0168  -0.0057 0.0190  154 ARG B NE  
3722 C CZ  . ARG B 155 ? 0.1748 0.2003 0.1829 0.0164  -0.0039 0.0191  154 ARG B CZ  
3723 N NH1 . ARG B 155 ? 0.1779 0.2121 0.1893 0.0128  -0.0034 0.0208  154 ARG B NH1 
3724 N NH2 . ARG B 155 ? 0.1732 0.2002 0.1812 0.0192  -0.0025 0.0174  154 ARG B NH2 
3725 N N   . SER B 156 ? 0.1927 0.1833 0.1886 -0.0068 -0.0115 0.0212  155 SER B N   
3726 C CA  . SER B 156 ? 0.2049 0.1902 0.1971 -0.0110 -0.0129 0.0224  155 SER B CA  
3727 C C   . SER B 156 ? 0.2115 0.2056 0.2070 -0.0156 -0.0125 0.0246  155 SER B C   
3728 O O   . SER B 156 ? 0.2146 0.2058 0.2066 -0.0179 -0.0141 0.0268  155 SER B O   
3729 C CB  . SER B 156 ? 0.2241 0.2014 0.2143 -0.0166 -0.0128 0.0192  155 SER B CB  
3730 O OG  . SER B 156 ? 0.2068 0.1903 0.2024 -0.0227 -0.0109 0.0176  155 SER B OG  
3731 N N   . ALA B 157 ? 0.2119 0.2162 0.2132 -0.0174 -0.0103 0.0242  156 ALA B N   
3732 C CA  . ALA B 157 ? 0.1972 0.2106 0.2013 -0.0220 -0.0095 0.0262  156 ALA B CA  
3733 C C   . ALA B 157 ? 0.2203 0.2411 0.2247 -0.0173 -0.0106 0.0299  156 ALA B C   
3734 O O   . ALA B 157 ? 0.2480 0.2771 0.2542 -0.0210 -0.0101 0.0320  156 ALA B O   
3735 C CB  . ALA B 157 ? 0.2085 0.2292 0.2179 -0.0258 -0.0063 0.0243  156 ALA B CB  
3736 N N   . GLY B 158 ? 0.2262 0.2444 0.2288 -0.0094 -0.0120 0.0307  157 GLY B N   
3737 C CA  . GLY B 158 ? 0.2102 0.2371 0.2145 -0.0042 -0.0127 0.0337  157 GLY B CA  
3738 C C   . GLY B 158 ? 0.2216 0.2596 0.2309 -0.0027 -0.0103 0.0329  157 GLY B C   
3739 O O   . GLY B 158 ? 0.2131 0.2609 0.2247 0.0005  -0.0106 0.0352  157 GLY B O   
3740 N N   . ALA B 159 ? 0.1780 0.2151 0.1890 -0.0049 -0.0081 0.0297  158 ALA B N   
3741 C CA  . ALA B 159 ? 0.1627 0.2087 0.1772 -0.0037 -0.0057 0.0286  158 ALA B CA  
3742 C C   . ALA B 159 ? 0.1725 0.2150 0.1858 0.0040  -0.0060 0.0275  158 ALA B C   
3743 O O   . ALA B 159 ? 0.1665 0.2027 0.1788 0.0046  -0.0054 0.0248  158 ALA B O   
3744 C CB  . ALA B 159 ? 0.1567 0.2021 0.1729 -0.0095 -0.0033 0.0259  158 ALA B CB  
3745 N N   . THR B 160 ? 0.1889 0.2355 0.2023 0.0098  -0.0072 0.0296  159 THR B N   
3746 C CA  . THR B 160 ? 0.1677 0.2100 0.1796 0.0175  -0.0075 0.0288  159 THR B CA  
3747 C C   . THR B 160 ? 0.2019 0.2545 0.2170 0.0210  -0.0055 0.0281  159 THR B C   
3748 O O   . THR B 160 ? 0.2095 0.2588 0.2234 0.0265  -0.0050 0.0265  159 THR B O   
3749 C CB  . THR B 160 ? 0.1981 0.2358 0.2074 0.0228  -0.0100 0.0314  159 THR B CB  
3750 O OG1 . THR B 160 ? 0.2324 0.2812 0.2447 0.0229  -0.0109 0.0347  159 THR B OG1 
3751 C CG2 . THR B 160 ? 0.2472 0.2720 0.2515 0.0197  -0.0119 0.0314  159 THR B CG2 
3752 N N   . SER B 161 ? 0.1840 0.2490 0.2026 0.0177  -0.0042 0.0292  160 SER B N   
3753 C CA  . SER B 161 ? 0.1629 0.2387 0.1843 0.0204  -0.0022 0.0285  160 SER B CA  
3754 C C   . SER B 161 ? 0.1905 0.2659 0.2116 0.0177  0.0004  0.0253  160 SER B C   
3755 O O   . SER B 161 ? 0.1993 0.2807 0.2213 0.0204  0.0022  0.0240  160 SER B O   
3756 C CB  . SER B 161 ? 0.2389 0.3288 0.2637 0.0174  -0.0019 0.0310  160 SER B CB  
3757 O OG  . SER B 161 ? 0.2128 0.3043 0.2376 0.0092  -0.0003 0.0305  160 SER B OG  
3758 N N   . GLN B 162 ? 0.1836 0.2522 0.2033 0.0123  0.0008  0.0241  161 GLN B N   
3759 C CA  . GLN B 162 ? 0.1726 0.2415 0.1921 0.0087  0.0031  0.0217  161 GLN B CA  
3760 C C   . GLN B 162 ? 0.1641 0.2242 0.1811 0.0119  0.0030  0.0192  161 GLN B C   
3761 O O   . GLN B 162 ? 0.1739 0.2243 0.1887 0.0142  0.0012  0.0188  161 GLN B O   
3762 C CB  . GLN B 162 ? 0.1443 0.2103 0.1642 0.0016  0.0036  0.0216  161 GLN B CB  
3763 C CG  . GLN B 162 ? 0.1470 0.2216 0.1688 -0.0034 0.0042  0.0238  161 GLN B CG  
3764 C CD  . GLN B 162 ? 0.2146 0.2867 0.2361 -0.0033 0.0016  0.0262  161 GLN B CD  
3765 O OE1 . GLN B 162 ? 0.1604 0.2246 0.1801 0.0010  -0.0008 0.0264  161 GLN B OE1 
3766 N NE2 . GLN B 162 ? 0.2036 0.2821 0.2262 -0.0086 0.0020  0.0280  161 GLN B NE2 
3767 N N   . TYR B 163 ? 0.1425 0.2056 0.1591 0.0114  0.0051  0.0174  162 TYR B N   
3768 C CA  . TYR B 163 ? 0.1334 0.1879 0.1472 0.0127  0.0050  0.0150  162 TYR B CA  
3769 C C   . TYR B 163 ? 0.1663 0.2134 0.1798 0.0084  0.0042  0.0144  162 TYR B C   
3770 O O   . TYR B 163 ? 0.1734 0.2234 0.1889 0.0034  0.0050  0.0151  162 TYR B O   
3771 C CB  . TYR B 163 ? 0.1638 0.2230 0.1766 0.0126  0.0074  0.0134  162 TYR B CB  
3772 C CG  . TYR B 163 ? 0.1671 0.2327 0.1800 0.0175  0.0083  0.0132  162 TYR B CG  
3773 C CD1 . TYR B 163 ? 0.2001 0.2601 0.2107 0.0225  0.0079  0.0117  162 TYR B CD1 
3774 C CD2 . TYR B 163 ? 0.1992 0.2771 0.2149 0.0169  0.0097  0.0144  162 TYR B CD2 
3775 C CE1 . TYR B 163 ? 0.2091 0.2752 0.2204 0.0272  0.0091  0.0112  162 TYR B CE1 
3776 C CE2 . TYR B 163 ? 0.1980 0.2829 0.2147 0.0216  0.0106  0.0140  162 TYR B CE2 
3777 C CZ  . TYR B 163 ? 0.2591 0.3380 0.2739 0.0269  0.0104  0.0124  162 TYR B CZ  
3778 O OH  . TYR B 163 ? 0.2992 0.3852 0.3155 0.0317  0.0116  0.0117  162 TYR B OH  
3779 N N   . ILE B 164 ? 0.1407 0.1785 0.1517 0.0101  0.0029  0.0128  163 ILE B N   
3780 C CA  . ILE B 164 ? 0.1394 0.1706 0.1505 0.0065  0.0020  0.0118  163 ILE B CA  
3781 C C   . ILE B 164 ? 0.1644 0.1926 0.1733 0.0070  0.0024  0.0100  163 ILE B C   
3782 O O   . ILE B 164 ? 0.1877 0.2120 0.1935 0.0107  0.0018  0.0090  163 ILE B O   
3783 C CB  . ILE B 164 ? 0.1664 0.1892 0.1761 0.0073  -0.0003 0.0117  163 ILE B CB  
3784 C CG1 . ILE B 164 ? 0.1655 0.1909 0.1766 0.0063  -0.0008 0.0138  163 ILE B CG1 
3785 C CG2 . ILE B 164 ? 0.1842 0.2015 0.1944 0.0035  -0.0012 0.0103  163 ILE B CG2 
3786 C CD1 . ILE B 164 ? 0.1848 0.2014 0.1934 0.0069  -0.0030 0.0139  163 ILE B CD1 
3787 N N   . PHE B 165 ? 0.1548 0.1842 0.1650 0.0033  0.0034  0.0096  164 PHE B N   
3788 C CA  . PHE B 165 ? 0.1827 0.2083 0.1906 0.0034  0.0032  0.0081  164 PHE B CA  
3789 C C   . PHE B 165 ? 0.1812 0.1994 0.1895 0.0025  0.0009  0.0073  164 PHE B C   
3790 O O   . PHE B 165 ? 0.1702 0.1882 0.1818 -0.0008 0.0007  0.0075  164 PHE B O   
3791 C CB  . PHE B 165 ? 0.1551 0.1848 0.1636 0.0001  0.0054  0.0082  164 PHE B CB  
3792 C CG  . PHE B 165 ? 0.1491 0.1862 0.1562 0.0006  0.0079  0.0085  164 PHE B CG  
3793 C CD1 . PHE B 165 ? 0.1677 0.2083 0.1740 0.0042  0.0080  0.0086  164 PHE B CD1 
3794 C CD2 . PHE B 165 ? 0.1519 0.1921 0.1581 -0.0027 0.0102  0.0084  164 PHE B CD2 
3795 C CE1 . PHE B 165 ? 0.1533 0.2019 0.1588 0.0043  0.0104  0.0086  164 PHE B CE1 
3796 C CE2 . PHE B 165 ? 0.1853 0.2325 0.1896 -0.0029 0.0127  0.0083  164 PHE B CE2 
3797 C CZ  . PHE B 165 ? 0.1779 0.2300 0.1822 0.0005  0.0128  0.0084  164 PHE B CZ  
3798 N N   . VAL B 166 ? 0.1606 0.1729 0.1656 0.0050  -0.0008 0.0062  165 VAL B N   
3799 C CA  . VAL B 166 ? 0.1845 0.1905 0.1894 0.0039  -0.0030 0.0052  165 VAL B CA  
3800 C C   . VAL B 166 ? 0.1702 0.1750 0.1742 0.0031  -0.0035 0.0046  165 VAL B C   
3801 O O   . VAL B 166 ? 0.1868 0.1930 0.1879 0.0043  -0.0024 0.0045  165 VAL B O   
3802 C CB  . VAL B 166 ? 0.1733 0.1730 0.1745 0.0065  -0.0046 0.0044  165 VAL B CB  
3803 C CG1 . VAL B 166 ? 0.1842 0.1841 0.1857 0.0076  -0.0043 0.0054  165 VAL B CG1 
3804 C CG2 . VAL B 166 ? 0.1672 0.1650 0.1636 0.0096  -0.0042 0.0036  165 VAL B CG2 
3805 N N   . GLU B 167 ? 0.1564 0.1588 0.1629 0.0010  -0.0051 0.0042  166 GLU B N   
3806 C CA  . GLU B 167 ? 0.1441 0.1452 0.1500 0.0005  -0.0060 0.0039  166 GLU B CA  
3807 C C   . GLU B 167 ? 0.1816 0.1777 0.1867 0.0005  -0.0090 0.0029  166 GLU B C   
3808 O O   . GLU B 167 ? 0.1745 0.1690 0.1814 -0.0005 -0.0101 0.0022  166 GLU B O   
3809 C CB  . GLU B 167 ? 0.1705 0.1747 0.1810 -0.0021 -0.0048 0.0045  166 GLU B CB  
3810 C CG  . GLU B 167 ? 0.1868 0.1962 0.1974 -0.0030 -0.0015 0.0055  166 GLU B CG  
3811 C CD  . GLU B 167 ? 0.1927 0.2036 0.2054 -0.0053 0.0003  0.0060  166 GLU B CD  
3812 O OE1 . GLU B 167 ? 0.1950 0.2029 0.2074 -0.0050 -0.0011 0.0059  166 GLU B OE1 
3813 O OE2 . GLU B 167 ? 0.1549 0.1700 0.1694 -0.0075 0.0030  0.0065  166 GLU B OE2 
3814 N N   . GLY B 168 ? 0.1898 0.1834 0.1916 0.0013  -0.0105 0.0027  167 GLY B N   
3815 C CA  . GLY B 168 ? 0.1944 0.1840 0.1949 0.0010  -0.0135 0.0018  167 GLY B CA  
3816 C C   . GLY B 168 ? 0.2088 0.1994 0.2135 -0.0005 -0.0154 0.0020  167 GLY B C   
3817 O O   . GLY B 168 ? 0.1784 0.1720 0.1871 -0.0011 -0.0142 0.0029  167 GLY B O   
3818 N N   . ASN B 169 ? 0.1822 0.1702 0.1860 -0.0009 -0.0184 0.0013  168 ASN B N   
3819 C CA  . ASN B 169 ? 0.1854 0.1745 0.1930 -0.0017 -0.0210 0.0015  168 ASN B CA  
3820 C C   . ASN B 169 ? 0.1914 0.1798 0.1961 -0.0005 -0.0216 0.0029  168 ASN B C   
3821 O O   . ASN B 169 ? 0.2262 0.2133 0.2258 0.0004  -0.0199 0.0033  168 ASN B O   
3822 C CB  . ASN B 169 ? 0.1917 0.1787 0.1980 -0.0028 -0.0240 0.0002  168 ASN B CB  
3823 C CG  . ASN B 169 ? 0.2148 0.2051 0.2281 -0.0043 -0.0261 -0.0003 168 ASN B CG  
3824 O OD1 . ASN B 169 ? 0.2398 0.2332 0.2585 -0.0039 -0.0259 0.0006  168 ASN B OD1 
3825 N ND2 . ASN B 169 ? 0.2071 0.1967 0.2203 -0.0062 -0.0278 -0.0019 168 ASN B ND2 
3826 N N   . SER B 170 ? 0.2031 0.1922 0.2109 -0.0006 -0.0242 0.0035  169 SER B N   
3827 C CA  . SER B 170 ? 0.1910 0.1785 0.1957 0.0005  -0.0253 0.0051  169 SER B CA  
3828 C C   . SER B 170 ? 0.2014 0.1896 0.2057 0.0008  -0.0216 0.0060  169 SER B C   
3829 O O   . SER B 170 ? 0.2288 0.2145 0.2268 0.0013  -0.0209 0.0068  169 SER B O   
3830 C CB  . SER B 170 ? 0.2463 0.2297 0.2424 0.0007  -0.0272 0.0051  169 SER B CB  
3831 O OG  . SER B 170 ? 0.2363 0.2193 0.2327 -0.0001 -0.0312 0.0048  169 SER B OG  
3832 N N   . TRP B 171 ? 0.1841 0.1755 0.1946 0.0001  -0.0192 0.0058  170 TRP B N   
3833 C CA  . TRP B 171 ? 0.1875 0.1799 0.1980 -0.0003 -0.0155 0.0066  170 TRP B CA  
3834 C C   . TRP B 171 ? 0.1790 0.1714 0.1834 -0.0003 -0.0130 0.0063  170 TRP B C   
3835 O O   . TRP B 171 ? 0.2127 0.2050 0.2138 -0.0006 -0.0105 0.0070  170 TRP B O   
3836 C CB  . TRP B 171 ? 0.2152 0.2056 0.2250 0.0004  -0.0160 0.0081  170 TRP B CB  
3837 C CG  . TRP B 171 ? 0.2374 0.2281 0.2532 0.0013  -0.0191 0.0084  170 TRP B CG  
3838 C CD1 . TRP B 171 ? 0.2636 0.2529 0.2785 0.0024  -0.0236 0.0088  170 TRP B CD1 
3839 C CD2 . TRP B 171 ? 0.2456 0.2385 0.2693 0.0011  -0.0179 0.0084  170 TRP B CD2 
3840 N NE1 . TRP B 171 ? 0.2425 0.2340 0.2650 0.0032  -0.0255 0.0091  170 TRP B NE1 
3841 C CE2 . TRP B 171 ? 0.2251 0.2185 0.2531 0.0025  -0.0219 0.0087  170 TRP B CE2 
3842 C CE3 . TRP B 171 ? 0.2481 0.2428 0.2757 -0.0004 -0.0137 0.0080  170 TRP B CE3 
3843 C CZ2 . TRP B 171 ? 0.2179 0.2137 0.2544 0.0030  -0.0216 0.0085  170 TRP B CZ2 
3844 C CZ3 . TRP B 171 ? 0.2721 0.2683 0.3075 -0.0003 -0.0132 0.0078  170 TRP B CZ3 
3845 C CH2 . TRP B 171 ? 0.2164 0.2132 0.2565 0.0016  -0.0171 0.0080  170 TRP B CH2 
3846 N N   . THR B 172 ? 0.1720 0.1643 0.1748 0.0001  -0.0135 0.0053  171 THR B N   
3847 C CA  . THR B 172 ? 0.1565 0.1487 0.1540 0.0008  -0.0116 0.0048  171 THR B CA  
3848 C C   . THR B 172 ? 0.2011 0.1914 0.1919 0.0012  -0.0111 0.0052  171 THR B C   
3849 O O   . THR B 172 ? 0.1940 0.1859 0.1814 0.0014  -0.0084 0.0049  171 THR B O   
3850 C CB  . THR B 172 ? 0.1935 0.1901 0.1942 0.0001  -0.0083 0.0048  171 THR B CB  
3851 O OG1 . THR B 172 ? 0.2007 0.1976 0.1984 0.0015  -0.0075 0.0041  171 THR B OG1 
3852 C CG2 . THR B 172 ? 0.1854 0.1849 0.1859 -0.0010 -0.0052 0.0056  171 THR B CG2 
3853 N N   . GLY B 173 ? 0.2071 0.1938 0.1954 0.0013  -0.0138 0.0058  172 GLY B N   
3854 C CA  . GLY B 173 ? 0.2188 0.2028 0.1998 0.0011  -0.0135 0.0062  172 GLY B CA  
3855 C C   . GLY B 173 ? 0.2241 0.2065 0.1989 0.0016  -0.0130 0.0049  172 GLY B C   
3856 O O   . GLY B 173 ? 0.2142 0.1949 0.1886 0.0021  -0.0148 0.0040  172 GLY B O   
3857 N N   . ALA B 174 ? 0.2213 0.2041 0.1909 0.0011  -0.0103 0.0045  173 ALA B N   
3858 C CA  . ALA B 174 ? 0.1972 0.1784 0.1608 0.0016  -0.0095 0.0029  173 ALA B CA  
3859 C C   . ALA B 174 ? 0.2118 0.1872 0.1697 0.0009  -0.0129 0.0030  173 ALA B C   
3860 O O   . ALA B 174 ? 0.2245 0.1975 0.1798 0.0013  -0.0137 0.0017  173 ALA B O   
3861 C CB  . ALA B 174 ? 0.2533 0.2370 0.2127 0.0009  -0.0058 0.0023  173 ALA B CB  
3862 N N   . TRP B 175 ? 0.1987 0.1714 0.1547 -0.0002 -0.0149 0.0045  174 TRP B N   
3863 C CA  . TRP B 175 ? 0.2023 0.1697 0.1519 -0.0012 -0.0182 0.0048  174 TRP B CA  
3864 C C   . TRP B 175 ? 0.2499 0.2162 0.2024 -0.0008 -0.0219 0.0048  174 TRP B C   
3865 O O   . TRP B 175 ? 0.3049 0.2673 0.2518 -0.0020 -0.0243 0.0046  174 TRP B O   
3866 C CB  . TRP B 175 ? 0.2160 0.1803 0.1625 -0.0021 -0.0198 0.0068  174 TRP B CB  
3867 C CG  . TRP B 175 ? 0.2254 0.1911 0.1791 -0.0011 -0.0215 0.0087  174 TRP B CG  
3868 C CD1 . TRP B 175 ? 0.2668 0.2371 0.2292 -0.0001 -0.0200 0.0087  174 TRP B CD1 
3869 C CD2 . TRP B 175 ? 0.2687 0.2308 0.2213 -0.0010 -0.0249 0.0109  174 TRP B CD2 
3870 N NE1 . TRP B 175 ? 0.2664 0.2363 0.2334 0.0006  -0.0220 0.0104  174 TRP B NE1 
3871 C CE2 . TRP B 175 ? 0.2684 0.2334 0.2297 0.0004  -0.0250 0.0120  174 TRP B CE2 
3872 C CE3 . TRP B 175 ? 0.3190 0.2755 0.2637 -0.0019 -0.0279 0.0122  174 TRP B CE3 
3873 C CZ2 . TRP B 175 ? 0.2955 0.2583 0.2587 0.0015  -0.0279 0.0142  174 TRP B CZ2 
3874 C CZ3 . TRP B 175 ? 0.2804 0.2345 0.2265 -0.0009 -0.0311 0.0148  174 TRP B CZ3 
3875 C CH2 . TRP B 175 ? 0.2945 0.2518 0.2501 0.0010  -0.0311 0.0157  174 TRP B CH2 
3876 N N   . THR B 176 ? 0.2207 0.1906 0.1815 0.0002  -0.0223 0.0050  175 THR B N   
3877 C CA  . THR B 176 ? 0.2478 0.2173 0.2115 0.0001  -0.0254 0.0048  175 THR B CA  
3878 C C   . THR B 176 ? 0.2514 0.2216 0.2163 0.0006  -0.0236 0.0029  175 THR B C   
3879 O O   . THR B 176 ? 0.2436 0.2134 0.2106 0.0001  -0.0257 0.0024  175 THR B O   
3880 C CB  . THR B 176 ? 0.2350 0.2076 0.2069 0.0005  -0.0274 0.0061  175 THR B CB  
3881 O OG1 . THR B 176 ? 0.2625 0.2387 0.2398 0.0012  -0.0239 0.0061  175 THR B OG1 
3882 C CG2 . THR B 176 ? 0.3052 0.2758 0.2754 0.0005  -0.0302 0.0082  175 THR B CG2 
3883 N N   . TRP B 177 ? 0.2147 0.1859 0.1780 0.0015  -0.0198 0.0019  176 TRP B N   
3884 C CA  . TRP B 177 ? 0.2145 0.1867 0.1803 0.0026  -0.0180 0.0006  176 TRP B CA  
3885 C C   . TRP B 177 ? 0.2482 0.2157 0.2093 0.0022  -0.0191 -0.0008 176 TRP B C   
3886 O O   . TRP B 177 ? 0.2628 0.2296 0.2264 0.0021  -0.0199 -0.0014 176 TRP B O   
3887 C CB  . TRP B 177 ? 0.2119 0.1869 0.1771 0.0041  -0.0139 0.0001  176 TRP B CB  
3888 C CG  . TRP B 177 ? 0.2358 0.2119 0.2039 0.0057  -0.0123 -0.0007 176 TRP B CG  
3889 C CD1 . TRP B 177 ? 0.2526 0.2251 0.2169 0.0069  -0.0115 -0.0022 176 TRP B CD1 
3890 C CD2 . TRP B 177 ? 0.1927 0.1729 0.1675 0.0061  -0.0114 0.0000  176 TRP B CD2 
3891 N NE1 . TRP B 177 ? 0.2294 0.2032 0.1976 0.0084  -0.0104 -0.0022 176 TRP B NE1 
3892 C CE2 . TRP B 177 ? 0.2309 0.2098 0.2055 0.0077  -0.0104 -0.0009 176 TRP B CE2 
3893 C CE3 . TRP B 177 ? 0.2209 0.2054 0.2014 0.0052  -0.0112 0.0013  176 TRP B CE3 
3894 C CZ2 . TRP B 177 ? 0.2214 0.2032 0.2012 0.0082  -0.0095 -0.0003 176 TRP B CZ2 
3895 C CZ3 . TRP B 177 ? 0.2125 0.2002 0.1983 0.0053  -0.0100 0.0016  176 TRP B CZ3 
3896 C CH2 . TRP B 177 ? 0.2062 0.1926 0.1915 0.0068  -0.0094 0.0009  176 TRP B CH2 
3897 N N   . THR B 178 ? 0.2291 0.1928 0.1826 0.0016  -0.0189 -0.0016 177 THR B N   
3898 C CA  A THR B 178 ? 0.2553 0.2140 0.2034 0.0013  -0.0185 -0.0034 177 THR B CA  
3899 C CA  B THR B 178 ? 0.2552 0.2139 0.2034 0.0013  -0.0185 -0.0034 177 THR B CA  
3900 C C   . THR B 178 ? 0.2901 0.2464 0.2383 -0.0008 -0.0221 -0.0034 177 THR B C   
3901 O O   . THR B 178 ? 0.3328 0.2864 0.2801 -0.0008 -0.0215 -0.0047 177 THR B O   
3902 C CB  A THR B 178 ? 0.2928 0.2479 0.2326 0.0003  -0.0175 -0.0044 177 THR B CB  
3903 C CB  B THR B 178 ? 0.2932 0.2481 0.2330 0.0004  -0.0173 -0.0045 177 THR B CB  
3904 O OG1 A THR B 178 ? 0.3175 0.2757 0.2577 0.0020  -0.0139 -0.0048 177 THR B OG1 
3905 O OG1 B THR B 178 ? 0.3247 0.2793 0.2619 -0.0016 -0.0199 -0.0032 177 THR B OG1 
3906 C CG2 A THR B 178 ? 0.2932 0.2425 0.2270 -0.0002 -0.0166 -0.0065 177 THR B CG2 
3907 C CG2 B THR B 178 ? 0.3096 0.2669 0.2491 0.0026  -0.0130 -0.0055 177 THR B CG2 
3908 N N   . ASN B 179 ? 0.2881 0.2456 0.2375 -0.0025 -0.0257 -0.0020 178 ASN B N   
3909 C CA  . ASN B 179 ? 0.3343 0.2905 0.2836 -0.0046 -0.0291 -0.0022 178 ASN B CA  
3910 C C   . ASN B 179 ? 0.3173 0.2779 0.2753 -0.0044 -0.0303 -0.0018 178 ASN B C   
3911 O O   . ASN B 179 ? 0.3947 0.3551 0.3533 -0.0064 -0.0327 -0.0024 178 ASN B O   
3912 C CB  . ASN B 179 ? 0.3586 0.3141 0.3045 -0.0068 -0.0331 -0.0009 178 ASN B CB  
3913 C CG  . ASN B 179 ? 0.4373 0.3914 0.3811 -0.0097 -0.0365 -0.0015 178 ASN B CG  
3914 O OD1 . ASN B 179 ? 0.3492 0.3071 0.2977 -0.0106 -0.0403 -0.0003 178 ASN B OD1 
3915 N ND2 . ASN B 179 ? 0.4234 0.3724 0.3603 -0.0114 -0.0350 -0.0036 178 ASN B ND2 
3916 N N   . VAL B 180 ? 0.2238 0.1885 0.1883 -0.0025 -0.0284 -0.0010 179 VAL B N   
3917 C CA  . VAL B 180 ? 0.2397 0.2082 0.2122 -0.0026 -0.0290 -0.0010 179 VAL B CA  
3918 C C   . VAL B 180 ? 0.2658 0.2337 0.2395 -0.0017 -0.0260 -0.0021 179 VAL B C   
3919 O O   . VAL B 180 ? 0.2134 0.1810 0.1893 -0.0030 -0.0267 -0.0031 179 VAL B O   
3920 C CB  . VAL B 180 ? 0.2408 0.2141 0.2199 -0.0017 -0.0292 0.0008  179 VAL B CB  
3921 C CG1 . VAL B 180 ? 0.2456 0.2230 0.2331 -0.0018 -0.0285 0.0005  179 VAL B CG1 
3922 C CG2 . VAL B 180 ? 0.2365 0.2105 0.2158 -0.0024 -0.0331 0.0021  179 VAL B CG2 
3923 N N   . ASN B 181 ? 0.2512 0.2189 0.2232 0.0003  -0.0227 -0.0020 180 ASN B N   
3924 C CA  . ASN B 181 ? 0.2248 0.1936 0.1997 0.0017  -0.0200 -0.0023 180 ASN B CA  
3925 C C   . ASN B 181 ? 0.2220 0.1858 0.1909 0.0032  -0.0180 -0.0036 180 ASN B C   
3926 O O   . ASN B 181 ? 0.2231 0.1879 0.1933 0.0052  -0.0155 -0.0035 180 ASN B O   
3927 C CB  . ASN B 181 ? 0.2192 0.1930 0.1982 0.0031  -0.0178 -0.0011 180 ASN B CB  
3928 C CG  . ASN B 181 ? 0.2088 0.1870 0.1949 0.0018  -0.0189 0.0000  180 ASN B CG  
3929 O OD1 . ASN B 181 ? 0.2262 0.2054 0.2167 0.0006  -0.0198 -0.0004 180 ASN B OD1 
3930 N ND2 . ASN B 181 ? 0.2025 0.1828 0.1892 0.0020  -0.0188 0.0012  180 ASN B ND2 
3931 N N   . ASP B 182 ? 0.2366 0.1949 0.1989 0.0021  -0.0189 -0.0048 181 ASP B N   
3932 C CA  . ASP B 182 ? 0.2433 0.1960 0.1995 0.0037  -0.0165 -0.0062 181 ASP B CA  
3933 C C   . ASP B 182 ? 0.2603 0.2111 0.2182 0.0046  -0.0154 -0.0066 181 ASP B C   
3934 O O   . ASP B 182 ? 0.2716 0.2206 0.2278 0.0075  -0.0127 -0.0068 181 ASP B O   
3935 C CB  . ASP B 182 ? 0.2212 0.1678 0.1697 0.0015  -0.0176 -0.0076 181 ASP B CB  
3936 C CG  . ASP B 182 ? 0.3390 0.2790 0.2807 0.0032  -0.0146 -0.0093 181 ASP B CG  
3937 O OD1 . ASP B 182 ? 0.2852 0.2261 0.2260 0.0059  -0.0119 -0.0094 181 ASP B OD1 
3938 O OD2 . ASP B 182 ? 0.3599 0.2937 0.2972 0.0017  -0.0147 -0.0105 181 ASP B OD2 
3939 N N   . ASN B 183 ? 0.2396 0.1913 0.2010 0.0021  -0.0174 -0.0065 182 ASN B N   
3940 C CA  . ASN B 183 ? 0.2595 0.2081 0.2210 0.0022  -0.0166 -0.0070 182 ASN B CA  
3941 C C   . ASN B 183 ? 0.2407 0.1932 0.2070 0.0049  -0.0146 -0.0057 182 ASN B C   
3942 O O   . ASN B 183 ? 0.2515 0.2006 0.2165 0.0059  -0.0135 -0.0058 182 ASN B O   
3943 C CB  . ASN B 183 ? 0.2487 0.1981 0.2131 -0.0016 -0.0190 -0.0076 182 ASN B CB  
3944 C CG  . ASN B 183 ? 0.2204 0.1776 0.1937 -0.0025 -0.0201 -0.0064 182 ASN B CG  
3945 O OD1 . ASN B 183 ? 0.2584 0.2205 0.2352 -0.0010 -0.0196 -0.0051 182 ASN B OD1 
3946 N ND2 . ASN B 183 ? 0.2544 0.2126 0.2311 -0.0054 -0.0213 -0.0071 182 ASN B ND2 
3947 N N   . MET B 184 ? 0.2140 0.1733 0.1850 0.0059  -0.0141 -0.0044 183 MET B N   
3948 C CA  . MET B 184 ? 0.1887 0.1528 0.1642 0.0079  -0.0122 -0.0030 183 MET B CA  
3949 C C   . MET B 184 ? 0.1967 0.1587 0.1687 0.0117  -0.0098 -0.0031 183 MET B C   
3950 O O   . MET B 184 ? 0.1902 0.1556 0.1652 0.0135  -0.0085 -0.0019 183 MET B O   
3951 C CB  . MET B 184 ? 0.2223 0.1936 0.2025 0.0075  -0.0120 -0.0019 183 MET B CB  
3952 C CG  . MET B 184 ? 0.1968 0.1708 0.1817 0.0044  -0.0141 -0.0016 183 MET B CG  
3953 S SD  . MET B 184 ? 0.2301 0.2084 0.2220 0.0029  -0.0134 -0.0008 183 MET B SD  
3954 C CE  . MET B 184 ? 0.2413 0.2262 0.2357 0.0046  -0.0106 0.0008  183 MET B CE  
3955 N N   . LYS B 185 ? 0.2086 0.1653 0.1742 0.0130  -0.0091 -0.0044 184 LYS B N   
3956 C CA  . LYS B 185 ? 0.2257 0.1801 0.1884 0.0171  -0.0066 -0.0047 184 LYS B CA  
3957 C C   . LYS B 185 ? 0.2387 0.1883 0.2003 0.0185  -0.0063 -0.0044 184 LYS B C   
3958 O O   . LYS B 185 ? 0.2543 0.2037 0.2156 0.0225  -0.0044 -0.0039 184 LYS B O   
3959 C CB  . LYS B 185 ? 0.2617 0.2103 0.2173 0.0176  -0.0056 -0.0065 184 LYS B CB  
3960 C CG  . LYS B 185 ? 0.2582 0.1981 0.2081 0.0150  -0.0070 -0.0079 184 LYS B CG  
3961 C CD  . LYS B 185 ? 0.3140 0.2497 0.2574 0.0138  -0.0066 -0.0095 184 LYS B CD  
3962 C CE  . LYS B 185 ? 0.3644 0.2925 0.3020 0.0102  -0.0081 -0.0109 184 LYS B CE  
3963 N NZ  . LYS B 185 ? 0.3657 0.2900 0.2966 0.0083  -0.0080 -0.0124 184 LYS B NZ  
3964 N N   . SER B 186 ? 0.2141 0.1598 0.1752 0.0152  -0.0081 -0.0047 185 SER B N   
3965 C CA  A SER B 186 ? 0.2445 0.1839 0.2029 0.0161  -0.0078 -0.0045 185 SER B CA  
3966 C CA  B SER B 186 ? 0.2447 0.1841 0.2031 0.0159  -0.0079 -0.0046 185 SER B CA  
3967 C C   . SER B 186 ? 0.2613 0.2060 0.2255 0.0162  -0.0081 -0.0026 185 SER B C   
3968 O O   . SER B 186 ? 0.2838 0.2233 0.2458 0.0167  -0.0081 -0.0022 185 SER B O   
3969 C CB  A SER B 186 ? 0.2672 0.1992 0.2209 0.0121  -0.0094 -0.0061 185 SER B CB  
3970 C CB  B SER B 186 ? 0.2641 0.1971 0.2187 0.0115  -0.0097 -0.0061 185 SER B CB  
3971 O OG  A SER B 186 ? 0.2749 0.2121 0.2337 0.0078  -0.0115 -0.0061 185 SER B OG  
3972 O OG  B SER B 186 ? 0.2775 0.2053 0.2259 0.0106  -0.0096 -0.0078 185 SER B OG  
3973 N N   . LEU B 187 ? 0.2309 0.1850 0.2019 0.0154  -0.0083 -0.0014 186 LEU B N   
3974 C CA  . LEU B 187 ? 0.1999 0.1593 0.1759 0.0153  -0.0082 0.0004  186 LEU B CA  
3975 C C   . LEU B 187 ? 0.2491 0.2075 0.2236 0.0201  -0.0068 0.0017  186 LEU B C   
3976 O O   . LEU B 187 ? 0.2434 0.2019 0.2160 0.0241  -0.0052 0.0014  186 LEU B O   
3977 C CB  . LEU B 187 ? 0.1880 0.1574 0.1704 0.0141  -0.0078 0.0014  186 LEU B CB  
3978 C CG  . LEU B 187 ? 0.1971 0.1679 0.1824 0.0095  -0.0094 0.0006  186 LEU B CG  
3979 C CD1 . LEU B 187 ? 0.1935 0.1724 0.1834 0.0090  -0.0087 0.0014  186 LEU B CD1 
3980 C CD2 . LEU B 187 ? 0.2275 0.1978 0.2155 0.0061  -0.0103 0.0008  186 LEU B CD2 
3981 N N   . THR B 188 ? 0.2308 0.1883 0.2061 0.0197  -0.0073 0.0031  187 THR B N   
3982 C CA  . THR B 188 ? 0.2111 0.1672 0.1851 0.0243  -0.0066 0.0047  187 THR B CA  
3983 C C   . THR B 188 ? 0.2386 0.2037 0.2185 0.0237  -0.0068 0.0071  187 THR B C   
3984 O O   . THR B 188 ? 0.2321 0.2005 0.2154 0.0189  -0.0076 0.0074  187 THR B O   
3985 C CB  . THR B 188 ? 0.2527 0.1969 0.2199 0.0243  -0.0073 0.0044  187 THR B CB  
3986 O OG1 . THR B 188 ? 0.3071 0.2508 0.2757 0.0193  -0.0088 0.0048  187 THR B OG1 
3987 C CG2 . THR B 188 ? 0.3578 0.2931 0.3187 0.0235  -0.0070 0.0018  187 THR B CG2 
3988 N N   . ASP B 189 ? 0.2142 0.1837 0.1955 0.0284  -0.0059 0.0089  188 ASP B N   
3989 C CA  . ASP B 189 ? 0.2325 0.2112 0.2190 0.0279  -0.0061 0.0114  188 ASP B CA  
3990 C C   . ASP B 189 ? 0.2350 0.2134 0.2205 0.0338  -0.0060 0.0134  188 ASP B C   
3991 O O   . ASP B 189 ? 0.2388 0.2191 0.2242 0.0389  -0.0046 0.0129  188 ASP B O   
3992 C CB  . ASP B 189 ? 0.1885 0.1787 0.1803 0.0267  -0.0047 0.0113  188 ASP B CB  
3993 C CG  . ASP B 189 ? 0.1919 0.1923 0.1886 0.0262  -0.0045 0.0137  188 ASP B CG  
3994 O OD1 . ASP B 189 ? 0.2007 0.1999 0.1973 0.0253  -0.0058 0.0157  188 ASP B OD1 
3995 O OD2 . ASP B 189 ? 0.1964 0.2063 0.1965 0.0263  -0.0030 0.0137  188 ASP B OD2 
3996 N N   . PRO B 190 ? 0.2146 0.1906 0.1992 0.0333  -0.0075 0.0156  189 PRO B N   
3997 C CA  . PRO B 190 ? 0.2477 0.2236 0.2316 0.0395  -0.0078 0.0179  189 PRO B CA  
3998 C C   . PRO B 190 ? 0.2351 0.2249 0.2252 0.0427  -0.0068 0.0194  189 PRO B C   
3999 O O   . PRO B 190 ? 0.2756 0.2664 0.2658 0.0492  -0.0064 0.0205  189 PRO B O   
4000 C CB  . PRO B 190 ? 0.2737 0.2450 0.2554 0.0367  -0.0099 0.0201  189 PRO B CB  
4001 C CG  . PRO B 190 ? 0.2676 0.2422 0.2519 0.0290  -0.0103 0.0193  189 PRO B CG  
4002 C CD  . PRO B 190 ? 0.2398 0.2127 0.2239 0.0272  -0.0090 0.0160  189 PRO B CD  
4003 N N   . SER B 191 ? 0.2224 0.2227 0.2175 0.0383  -0.0061 0.0192  190 SER B N   
4004 C CA  . SER B 191 ? 0.2090 0.2229 0.2095 0.0404  -0.0049 0.0202  190 SER B CA  
4005 C C   . SER B 191 ? 0.1805 0.1969 0.1813 0.0431  -0.0026 0.0176  190 SER B C   
4006 O O   . SER B 191 ? 0.2250 0.2523 0.2297 0.0454  -0.0012 0.0180  190 SER B O   
4007 C CB  . SER B 191 ? 0.2474 0.2707 0.2521 0.0340  -0.0047 0.0210  190 SER B CB  
4008 O OG  . SER B 191 ? 0.2566 0.2792 0.2613 0.0314  -0.0066 0.0236  190 SER B OG  
4009 N N   . ASP B 192 ? 0.1998 0.2068 0.1964 0.0424  -0.0021 0.0150  191 ASP B N   
4010 C CA  . ASP B 192 ? 0.2033 0.2113 0.1991 0.0442  0.0000  0.0124  191 ASP B CA  
4011 C C   . ASP B 192 ? 0.2241 0.2438 0.2241 0.0410  0.0014  0.0120  191 ASP B C   
4012 O O   . ASP B 192 ? 0.2380 0.2647 0.2395 0.0436  0.0034  0.0110  191 ASP B O   
4013 C CB  . ASP B 192 ? 0.2371 0.2445 0.2321 0.0516  0.0013  0.0122  191 ASP B CB  
4014 C CG  . ASP B 192 ? 0.3956 0.4014 0.3883 0.0532  0.0036  0.0091  191 ASP B CG  
4015 O OD1 . ASP B 192 ? 0.3462 0.3468 0.3359 0.0491  0.0036  0.0072  191 ASP B OD1 
4016 O OD2 . ASP B 192 ? 0.3958 0.4061 0.3900 0.0585  0.0054  0.0086  191 ASP B OD2 
4017 N N   . LYS B 193 ? 0.1935 0.2149 0.1950 0.0350  0.0007  0.0125  192 LYS B N   
4018 C CA  . LYS B 193 ? 0.1869 0.2179 0.1914 0.0313  0.0021  0.0122  192 LYS B CA  
4019 C C   . LYS B 193 ? 0.1829 0.2095 0.1862 0.0262  0.0019  0.0107  192 LYS B C   
4020 O O   . LYS B 193 ? 0.1987 0.2306 0.2044 0.0217  0.0025  0.0112  192 LYS B O   
4021 C CB  . LYS B 193 ? 0.1919 0.2327 0.2007 0.0293  0.0020  0.0147  192 LYS B CB  
4022 C CG  . LYS B 193 ? 0.1830 0.2326 0.1943 0.0343  0.0027  0.0160  192 LYS B CG  
4023 C CD  . LYS B 193 ? 0.2318 0.2929 0.2472 0.0311  0.0028  0.0183  192 LYS B CD  
4024 C CE  . LYS B 193 ? 0.2463 0.3187 0.2648 0.0357  0.0036  0.0193  192 LYS B CE  
4025 N NZ  . LYS B 193 ? 0.3012 0.3692 0.3194 0.0427  0.0021  0.0205  192 LYS B NZ  
4026 N N   . ILE B 194 ? 0.1789 0.1960 0.1782 0.0269  0.0012  0.0089  193 ILE B N   
4027 C CA  . ILE B 194 ? 0.1956 0.2089 0.1938 0.0227  0.0007  0.0076  193 ILE B CA  
4028 C C   . ILE B 194 ? 0.2084 0.2260 0.2058 0.0225  0.0025  0.0063  193 ILE B C   
4029 O O   . ILE B 194 ? 0.2091 0.2264 0.2041 0.0260  0.0037  0.0051  193 ILE B O   
4030 C CB  . ILE B 194 ? 0.1646 0.1668 0.1586 0.0230  -0.0009 0.0062  193 ILE B CB  
4031 C CG1 . ILE B 194 ? 0.1852 0.1823 0.1792 0.0219  -0.0026 0.0072  193 ILE B CG1 
4032 C CG2 . ILE B 194 ? 0.1690 0.1683 0.1618 0.0195  -0.0015 0.0048  193 ILE B CG2 
4033 C CD1 . ILE B 194 ? 0.2325 0.2185 0.2212 0.0227  -0.0038 0.0058  193 ILE B CD1 
4034 N N   . ILE B 195 ? 0.1765 0.1974 0.1754 0.0183  0.0029  0.0063  194 ILE B N   
4035 C CA  . ILE B 195 ? 0.1937 0.2162 0.1905 0.0173  0.0042  0.0050  194 ILE B CA  
4036 C C   . ILE B 195 ? 0.1761 0.1924 0.1716 0.0143  0.0026  0.0044  194 ILE B C   
4037 O O   . ILE B 195 ? 0.1699 0.1861 0.1683 0.0113  0.0018  0.0053  194 ILE B O   
4038 C CB  . ILE B 195 ? 0.1692 0.2015 0.1682 0.0151  0.0065  0.0057  194 ILE B CB  
4039 C CG1 . ILE B 195 ? 0.1851 0.2253 0.1867 0.0177  0.0076  0.0068  194 ILE B CG1 
4040 C CG2 . ILE B 195 ? 0.1711 0.2041 0.1665 0.0142  0.0081  0.0042  194 ILE B CG2 
4041 C CD1 . ILE B 195 ? 0.1919 0.2332 0.1916 0.0226  0.0087  0.0055  194 ILE B CD1 
4042 N N   . TYR B 196 ? 0.1830 0.1943 0.1741 0.0150  0.0022  0.0029  195 TYR B N   
4043 C CA  . TYR B 196 ? 0.1976 0.2036 0.1874 0.0124  0.0003  0.0025  195 TYR B CA  
4044 C C   . TYR B 196 ? 0.2146 0.2242 0.2047 0.0097  0.0014  0.0029  195 TYR B C   
4045 O O   . TYR B 196 ? 0.2112 0.2220 0.1976 0.0098  0.0028  0.0021  195 TYR B O   
4046 C CB  . TYR B 196 ? 0.1949 0.1938 0.1794 0.0139  -0.0008 0.0010  195 TYR B CB  
4047 C CG  . TYR B 196 ? 0.1904 0.1839 0.1740 0.0158  -0.0019 0.0006  195 TYR B CG  
4048 C CD1 . TYR B 196 ? 0.1979 0.1919 0.1808 0.0194  -0.0004 0.0004  195 TYR B CD1 
4049 C CD2 . TYR B 196 ? 0.1993 0.1874 0.1828 0.0140  -0.0044 0.0004  195 TYR B CD2 
4050 C CE1 . TYR B 196 ? 0.2291 0.2169 0.2103 0.0211  -0.0013 0.0002  195 TYR B CE1 
4051 C CE2 . TYR B 196 ? 0.2270 0.2094 0.2088 0.0151  -0.0052 0.0000  195 TYR B CE2 
4052 C CZ  . TYR B 196 ? 0.2158 0.1975 0.1960 0.0187  -0.0036 -0.0001 195 TYR B CZ  
4053 O OH  . TYR B 196 ? 0.2444 0.2192 0.2219 0.0199  -0.0043 -0.0004 195 TYR B OH  
4054 N N   . GLU B 197 ? 0.1615 0.1723 0.1554 0.0069  0.0009  0.0039  196 GLU B N   
4055 C CA  . GLU B 197 ? 0.1770 0.1902 0.1709 0.0043  0.0023  0.0043  196 GLU B CA  
4056 C C   . GLU B 197 ? 0.1914 0.1988 0.1833 0.0034  0.0001  0.0041  196 GLU B C   
4057 O O   . GLU B 197 ? 0.1948 0.1989 0.1894 0.0029  -0.0021 0.0042  196 GLU B O   
4058 C CB  . GLU B 197 ? 0.1684 0.1857 0.1674 0.0017  0.0034  0.0055  196 GLU B CB  
4059 C CG  . GLU B 197 ? 0.1830 0.2013 0.1816 -0.0012 0.0050  0.0059  196 GLU B CG  
4060 C CD  . GLU B 197 ? 0.2132 0.2347 0.2164 -0.0042 0.0064  0.0067  196 GLU B CD  
4061 O OE1 . GLU B 197 ? 0.2030 0.2260 0.2098 -0.0042 0.0059  0.0071  196 GLU B OE1 
4062 O OE2 . GLU B 197 ? 0.2544 0.2760 0.2574 -0.0067 0.0081  0.0070  196 GLU B OE2 
4063 N N   . MET B 198 ? 0.1797 0.1860 0.1667 0.0031  0.0008  0.0037  197 MET B N   
4064 C CA  . MET B 198 ? 0.1530 0.1539 0.1374 0.0022  -0.0013 0.0038  197 MET B CA  
4065 C C   . MET B 198 ? 0.1947 0.1968 0.1778 0.0000  0.0005  0.0046  197 MET B C   
4066 O O   . MET B 198 ? 0.1894 0.1961 0.1713 -0.0010 0.0036  0.0045  197 MET B O   
4067 C CB  . MET B 198 ? 0.2063 0.2031 0.1843 0.0034  -0.0024 0.0027  197 MET B CB  
4068 C CG  . MET B 198 ? 0.1707 0.1661 0.1488 0.0056  -0.0032 0.0017  197 MET B CG  
4069 S SD  . MET B 198 ? 0.2095 0.1990 0.1796 0.0063  -0.0042 0.0002  197 MET B SD  
4070 C CE  . MET B 198 ? 0.2508 0.2395 0.2212 0.0092  -0.0035 -0.0010 197 MET B CE  
4071 N N   . HIS B 199 ? 0.1876 0.1856 0.1707 -0.0008 -0.0014 0.0054  198 HIS B N   
4072 C CA  . HIS B 199 ? 0.2102 0.2072 0.1911 -0.0026 0.0002  0.0062  198 HIS B CA  
4073 C C   . HIS B 199 ? 0.2500 0.2412 0.2239 -0.0025 -0.0017 0.0063  198 HIS B C   
4074 O O   . HIS B 199 ? 0.2364 0.2240 0.2094 -0.0012 -0.0051 0.0063  198 HIS B O   
4075 C CB  . HIS B 199 ? 0.1802 0.1766 0.1669 -0.0034 -0.0003 0.0072  198 HIS B CB  
4076 C CG  . HIS B 199 ? 0.1854 0.1870 0.1785 -0.0044 0.0016  0.0071  198 HIS B CG  
4077 N ND1 . HIS B 199 ? 0.2388 0.2405 0.2381 -0.0053 0.0015  0.0075  198 HIS B ND1 
4078 C CD2 . HIS B 199 ? 0.1856 0.1924 0.1796 -0.0046 0.0037  0.0067  198 HIS B CD2 
4079 C CE1 . HIS B 199 ? 0.1828 0.1892 0.1859 -0.0066 0.0035  0.0073  198 HIS B CE1 
4080 N NE2 . HIS B 199 ? 0.1739 0.1835 0.1739 -0.0061 0.0046  0.0070  198 HIS B NE2 
4081 N N   . GLN B 200 ? 0.2067 0.1967 0.1750 -0.0043 0.0005  0.0066  199 GLN B N   
4082 C CA  . GLN B 200 ? 0.2156 0.1992 0.1765 -0.0045 -0.0015 0.0069  199 GLN B CA  
4083 C C   . GLN B 200 ? 0.2422 0.2227 0.1994 -0.0065 0.0003  0.0080  199 GLN B C   
4084 O O   . GLN B 200 ? 0.2550 0.2376 0.2082 -0.0087 0.0041  0.0073  199 GLN B O   
4085 C CB  . GLN B 200 ? 0.2385 0.2220 0.1926 -0.0048 -0.0008 0.0054  199 GLN B CB  
4086 C CG  . GLN B 200 ? 0.2149 0.1909 0.1617 -0.0052 -0.0038 0.0058  199 GLN B CG  
4087 C CD  . GLN B 200 ? 0.2114 0.1849 0.1622 -0.0034 -0.0085 0.0068  199 GLN B CD  
4088 O OE1 . GLN B 200 ? 0.2457 0.2207 0.1989 -0.0022 -0.0095 0.0057  199 GLN B OE1 
4089 N NE2 . GLN B 200 ? 0.2290 0.1987 0.1807 -0.0032 -0.0111 0.0087  199 GLN B NE2 
4090 N N   . PHE B 201 ? 0.2273 0.2026 0.1851 -0.0057 -0.0025 0.0097  200 PHE B N   
4091 C CA  . PHE B 201 ? 0.2373 0.2072 0.1898 -0.0071 -0.0014 0.0109  200 PHE B CA  
4092 C C   . PHE B 201 ? 0.2437 0.2067 0.1874 -0.0071 -0.0043 0.0115  200 PHE B C   
4093 O O   . PHE B 201 ? 0.2538 0.2164 0.1967 -0.0061 -0.0075 0.0111  200 PHE B O   
4094 C CB  . PHE B 201 ? 0.2255 0.1940 0.1848 -0.0059 -0.0021 0.0125  200 PHE B CB  
4095 C CG  . PHE B 201 ? 0.2352 0.2097 0.2013 -0.0071 0.0016  0.0118  200 PHE B CG  
4096 C CD1 . PHE B 201 ? 0.2510 0.2259 0.2137 -0.0099 0.0064  0.0115  200 PHE B CD1 
4097 C CD2 . PHE B 201 ? 0.2451 0.2246 0.2201 -0.0058 0.0005  0.0112  200 PHE B CD2 
4098 C CE1 . PHE B 201 ? 0.2354 0.2160 0.2036 -0.0116 0.0099  0.0109  200 PHE B CE1 
4099 C CE2 . PHE B 201 ? 0.2764 0.2612 0.2569 -0.0074 0.0039  0.0106  200 PHE B CE2 
4100 C CZ  . PHE B 201 ? 0.2748 0.2604 0.2521 -0.0103 0.0085  0.0105  200 PHE B CZ  
4101 N N   . LEU B 202 ? 0.2295 0.1867 0.1656 -0.0089 -0.0030 0.0124  201 LEU B N   
4102 C CA  . LEU B 202 ? 0.2591 0.2099 0.1842 -0.0102 -0.0045 0.0126  201 LEU B CA  
4103 C C   . LEU B 202 ? 0.2933 0.2353 0.2146 -0.0092 -0.0079 0.0153  201 LEU B C   
4104 O O   . LEU B 202 ? 0.2987 0.2342 0.2098 -0.0107 -0.0094 0.0158  201 LEU B O   
4105 C CB  . LEU B 202 ? 0.2672 0.2184 0.1839 -0.0139 0.0005  0.0109  201 LEU B CB  
4106 C CG  . LEU B 202 ? 0.2967 0.2574 0.2176 -0.0147 0.0042  0.0085  201 LEU B CG  
4107 C CD1 . LEU B 202 ? 0.3050 0.2669 0.2179 -0.0187 0.0091  0.0069  201 LEU B CD1 
4108 C CD2 . LEU B 202 ? 0.2831 0.2467 0.2057 -0.0131 0.0019  0.0071  201 LEU B CD2 
4109 N N   . ASP B 203 ? 0.2659 0.2076 0.1948 -0.0068 -0.0092 0.0170  202 ASP B N   
4110 C CA  . ASP B 203 ? 0.3209 0.2550 0.2477 -0.0049 -0.0129 0.0198  202 ASP B CA  
4111 C C   . ASP B 203 ? 0.2822 0.2169 0.2125 -0.0024 -0.0191 0.0208  202 ASP B C   
4112 O O   . ASP B 203 ? 0.2743 0.2147 0.2085 -0.0023 -0.0201 0.0192  202 ASP B O   
4113 C CB  . ASP B 203 ? 0.2972 0.2305 0.2306 -0.0032 -0.0112 0.0210  202 ASP B CB  
4114 C CG  . ASP B 203 ? 0.3224 0.2643 0.2691 -0.0017 -0.0104 0.0199  202 ASP B CG  
4115 O OD1 . ASP B 203 ? 0.2843 0.2328 0.2348 -0.0021 -0.0106 0.0182  202 ASP B OD1 
4116 O OD2 . ASP B 203 ? 0.2985 0.2398 0.2514 -0.0002 -0.0095 0.0208  202 ASP B OD2 
4117 N N   . SER B 204 ? 0.3726 0.3009 0.3005 -0.0006 -0.0232 0.0235  203 SER B N   
4118 C CA  . SER B 204 ? 0.4592 0.3872 0.3890 0.0015  -0.0296 0.0251  203 SER B CA  
4119 C C   . SER B 204 ? 0.3747 0.3113 0.3147 0.0026  -0.0312 0.0236  203 SER B C   
4120 O O   . SER B 204 ? 0.4049 0.3430 0.3420 0.0013  -0.0332 0.0225  203 SER B O   
4121 C CB  . SER B 204 ? 0.4981 0.4216 0.4307 0.0049  -0.0329 0.0283  203 SER B CB  
4122 O OG  . SER B 204 ? 0.4837 0.4108 0.4265 0.0068  -0.0299 0.0280  203 SER B OG  
4123 N N   . ASP B 205 ? 0.3185 0.2602 0.2696 0.0046  -0.0301 0.0233  204 ASP B N   
4124 C CA  . ASP B 205 ? 0.3382 0.2874 0.2992 0.0056  -0.0318 0.0220  204 ASP B CA  
4125 C C   . ASP B 205 ? 0.3051 0.2600 0.2699 0.0041  -0.0272 0.0193  204 ASP B C   
4126 O O   . ASP B 205 ? 0.3119 0.2726 0.2853 0.0048  -0.0278 0.0181  204 ASP B O   
4127 C CB  . ASP B 205 ? 0.3657 0.3172 0.3371 0.0088  -0.0340 0.0234  204 ASP B CB  
4128 C CG  . ASP B 205 ? 0.3575 0.3082 0.3327 0.0093  -0.0294 0.0234  204 ASP B CG  
4129 O OD1 . ASP B 205 ? 0.3302 0.2795 0.3003 0.0069  -0.0245 0.0224  204 ASP B OD1 
4130 O OD2 . ASP B 205 ? 0.4047 0.3566 0.3881 0.0119  -0.0305 0.0244  204 ASP B OD2 
4131 N N   . GLY B 206 ? 0.2813 0.2351 0.2400 0.0019  -0.0226 0.0182  205 GLY B N   
4132 C CA  . GLY B 206 ? 0.2804 0.2400 0.2425 0.0006  -0.0184 0.0159  205 GLY B CA  
4133 C C   . GLY B 206 ? 0.2650 0.2288 0.2365 0.0011  -0.0157 0.0156  205 GLY B C   
4134 O O   . GLY B 206 ? 0.2639 0.2331 0.2395 0.0002  -0.0132 0.0140  205 GLY B O   
4135 N N   . SER B 207 ? 0.2438 0.2050 0.2186 0.0024  -0.0162 0.0172  206 SER B N   
4136 C CA  . SER B 207 ? 0.2280 0.1928 0.2119 0.0026  -0.0135 0.0168  206 SER B CA  
4137 C C   . SER B 207 ? 0.2606 0.2254 0.2418 0.0000  -0.0076 0.0161  206 SER B C   
4138 O O   . SER B 207 ? 0.2933 0.2621 0.2814 -0.0008 -0.0047 0.0153  206 SER B O   
4139 C CB  . SER B 207 ? 0.2727 0.2346 0.2614 0.0053  -0.0159 0.0186  206 SER B CB  
4140 O OG  . SER B 207 ? 0.3099 0.2641 0.2907 0.0056  -0.0154 0.0204  206 SER B OG  
4141 N N   . GLY B 208 ? 0.2766 0.2373 0.2476 -0.0018 -0.0056 0.0163  207 GLY B N   
4142 C CA  . GLY B 208 ? 0.2489 0.2099 0.2170 -0.0047 0.0001  0.0157  207 GLY B CA  
4143 C C   . GLY B 208 ? 0.2960 0.2525 0.2658 -0.0045 0.0023  0.0169  207 GLY B C   
4144 O O   . GLY B 208 ? 0.3077 0.2666 0.2801 -0.0068 0.0070  0.0160  207 GLY B O   
4145 N N   . THR B 209 ? 0.2462 0.1961 0.2149 -0.0018 -0.0009 0.0188  208 THR B N   
4146 C CA  . THR B 209 ? 0.2750 0.2197 0.2453 -0.0009 0.0012  0.0200  208 THR B CA  
4147 C C   . THR B 209 ? 0.3153 0.2498 0.2739 -0.0014 0.0020  0.0216  208 THR B C   
4148 O O   . THR B 209 ? 0.3823 0.3114 0.3400 -0.0014 0.0052  0.0224  208 THR B O   
4149 C CB  . THR B 209 ? 0.3444 0.2900 0.3248 0.0033  -0.0029 0.0210  208 THR B CB  
4150 O OG1 . THR B 209 ? 0.3455 0.2887 0.3232 0.0060  -0.0089 0.0225  208 THR B OG1 
4151 C CG2 . THR B 209 ? 0.3006 0.2554 0.2922 0.0031  -0.0029 0.0191  208 THR B CG2 
4152 N N   . SER B 210 ? 0.2900 0.2213 0.2392 -0.0020 -0.0005 0.0221  209 SER B N   
4153 C CA  . SER B 210 ? 0.3407 0.2618 0.2772 -0.0032 0.0003  0.0235  209 SER B CA  
4154 C C   . SER B 210 ? 0.3404 0.2623 0.2670 -0.0082 0.0044  0.0216  209 SER B C   
4155 O O   . SER B 210 ? 0.3068 0.2362 0.2350 -0.0095 0.0042  0.0198  209 SER B O   
4156 C CB  . SER B 210 ? 0.3365 0.2522 0.2687 -0.0004 -0.0061 0.0257  209 SER B CB  
4157 O OG  . SER B 210 ? 0.3868 0.2923 0.3050 -0.0023 -0.0055 0.0269  209 SER B OG  
4158 N N   . ALA B 211 ? 0.3124 0.2265 0.2288 -0.0109 0.0083  0.0220  210 ALA B N   
4159 C CA  . ALA B 211 ? 0.3402 0.2545 0.2460 -0.0160 0.0123  0.0201  210 ALA B CA  
4160 C C   . ALA B 211 ? 0.3207 0.2308 0.2165 -0.0167 0.0088  0.0203  210 ALA B C   
4161 O O   . ALA B 211 ? 0.3570 0.2689 0.2449 -0.0208 0.0117  0.0183  210 ALA B O   
4162 C CB  . ALA B 211 ? 0.3373 0.2440 0.2343 -0.0195 0.0179  0.0202  210 ALA B CB  
4163 N N   . THR B 212 ? 0.3172 0.2224 0.2134 -0.0130 0.0029  0.0226  211 THR B N   
4164 C CA  . THR B 212 ? 0.3407 0.2413 0.2273 -0.0139 -0.0008 0.0230  211 THR B CA  
4165 C C   . THR B 212 ? 0.3403 0.2502 0.2327 -0.0133 -0.0034 0.0213  211 THR B C   
4166 O O   . THR B 212 ? 0.3691 0.2850 0.2731 -0.0099 -0.0061 0.0216  211 THR B O   
4167 C CB  . THR B 212 ? 0.3560 0.2471 0.2399 -0.0104 -0.0062 0.0265  211 THR B CB  
4168 O OG1 . THR B 212 ? 0.4013 0.2827 0.2792 -0.0106 -0.0035 0.0281  211 THR B OG1 
4169 C CG2 . THR B 212 ? 0.4180 0.3040 0.2909 -0.0120 -0.0101 0.0270  211 THR B CG2 
4170 N N   . CYS B 213 ? 0.3471 0.2576 0.2310 -0.0167 -0.0023 0.0194  212 CYS B N   
4171 C CA  . CYS B 213 ? 0.3240 0.2413 0.2112 -0.0164 -0.0046 0.0177  212 CYS B CA  
4172 C C   . CYS B 213 ? 0.3424 0.2531 0.2226 -0.0160 -0.0100 0.0191  212 CYS B C   
4173 O O   . CYS B 213 ? 0.3559 0.2569 0.2250 -0.0177 -0.0108 0.0206  212 CYS B O   
4174 C CB  . CYS B 213 ? 0.3397 0.2630 0.2232 -0.0202 0.0003  0.0143  212 CYS B CB  
4175 S SG  . CYS B 213 ? 0.3318 0.2648 0.2245 -0.0208 0.0061  0.0128  212 CYS B SG  
4176 N N   . VAL B 214 ? 0.3126 0.2281 0.1988 -0.0141 -0.0137 0.0187  213 VAL B N   
4177 C CA  . VAL B 214 ? 0.3313 0.2416 0.2118 -0.0140 -0.0192 0.0201  213 VAL B CA  
4178 C C   . VAL B 214 ? 0.3205 0.2252 0.1867 -0.0186 -0.0177 0.0187  213 VAL B C   
4179 O O   . VAL B 214 ? 0.3349 0.2306 0.1914 -0.0197 -0.0210 0.0207  213 VAL B O   
4180 C CB  . VAL B 214 ? 0.3337 0.2510 0.2226 -0.0121 -0.0222 0.0192  213 VAL B CB  
4181 C CG1 . VAL B 214 ? 0.3425 0.2547 0.2247 -0.0128 -0.0276 0.0204  213 VAL B CG1 
4182 C CG2 . VAL B 214 ? 0.3472 0.2697 0.2496 -0.0080 -0.0238 0.0204  213 VAL B CG2 
4183 N N   . SER B 215 ? 0.2924 0.2026 0.1571 -0.0213 -0.0127 0.0152  214 SER B N   
4184 C CA  . SER B 215 ? 0.3642 0.2709 0.2165 -0.0259 -0.0109 0.0131  214 SER B CA  
4185 C C   . SER B 215 ? 0.3318 0.2463 0.1851 -0.0282 -0.0045 0.0095  214 SER B C   
4186 O O   . SER B 215 ? 0.3376 0.2605 0.2015 -0.0260 -0.0022 0.0087  214 SER B O   
4187 C CB  . SER B 215 ? 0.3461 0.2525 0.1965 -0.0262 -0.0147 0.0125  214 SER B CB  
4188 O OG  . SER B 215 ? 0.3348 0.2507 0.1935 -0.0250 -0.0126 0.0097  214 SER B OG  
4189 N N   . SER B 216 ? 0.3233 0.2353 0.1654 -0.0327 -0.0018 0.0071  215 SER B N   
4190 C CA  A SER B 216 ? 0.3411 0.2609 0.1831 -0.0353 0.0043  0.0034  215 SER B CA  
4191 C CA  B SER B 216 ? 0.3402 0.2602 0.1825 -0.0352 0.0043  0.0034  215 SER B CA  
4192 C C   . SER B 216 ? 0.3053 0.2349 0.1557 -0.0334 0.0050  0.0008  215 SER B C   
4193 O O   . SER B 216 ? 0.3229 0.2608 0.1755 -0.0345 0.0097  -0.0021 215 SER B O   
4194 C CB  A SER B 216 ? 0.3396 0.2538 0.1666 -0.0411 0.0069  0.0013  215 SER B CB  
4195 C CB  B SER B 216 ? 0.3411 0.2554 0.1685 -0.0410 0.0071  0.0014  215 SER B CB  
4196 O OG  A SER B 216 ? 0.3877 0.2937 0.2065 -0.0435 0.0080  0.0031  215 SER B OG  
4197 O OG  B SER B 216 ? 0.3586 0.2663 0.1784 -0.0424 0.0034  0.0015  215 SER B OG  
4198 N N   . THR B 217 ? 0.2962 0.2250 0.1508 -0.0306 0.0005  0.0018  216 THR B N   
4199 C CA  . THR B 217 ? 0.2646 0.2011 0.1261 -0.0287 0.0013  -0.0006 216 THR B CA  
4200 C C   . THR B 217 ? 0.3040 0.2443 0.1778 -0.0239 -0.0017 0.0011  216 THR B C   
4201 O O   . THR B 217 ? 0.2990 0.2437 0.1779 -0.0221 -0.0019 -0.0004 216 THR B O   
4202 C CB  . THR B 217 ? 0.2967 0.2287 0.1501 -0.0310 -0.0001 -0.0023 216 THR B CB  
4203 O OG1 . THR B 217 ? 0.3097 0.2335 0.1599 -0.0306 -0.0059 0.0007  216 THR B OG1 
4204 C CG2 . THR B 217 ? 0.3384 0.2673 0.1795 -0.0363 0.0035  -0.0048 216 THR B CG2 
4205 N N   . ILE B 218 ? 0.2823 0.2400 0.1874 -0.0486 0.0142  0.0399  217 ILE B N   
4206 C CA  . ILE B 218 ? 0.2874 0.2450 0.1962 -0.0472 0.0051  0.0397  217 ILE B CA  
4207 C C   . ILE B 218 ? 0.2430 0.2134 0.1676 -0.0417 0.0081  0.0361  217 ILE B C   
4208 O O   . ILE B 218 ? 0.2618 0.2299 0.1850 -0.0400 0.0036  0.0347  217 ILE B O   
4209 C CB  . ILE B 218 ? 0.2865 0.2467 0.2038 -0.0494 -0.0053 0.0433  217 ILE B CB  
4210 C CG1 . ILE B 218 ? 0.2975 0.2543 0.2144 -0.0488 -0.0154 0.0436  217 ILE B CG1 
4211 C CG2 . ILE B 218 ? 0.2657 0.2438 0.2069 -0.0470 -0.0039 0.0435  217 ILE B CG2 
4212 C CD1 . ILE B 218 ? 0.3910 0.3293 0.2846 -0.0523 -0.0198 0.0447  217 ILE B CD1 
4213 N N   . GLY B 219 ? 0.2513 0.2351 0.1910 -0.0390 0.0155  0.0346  218 GLY B N   
4214 C CA  . GLY B 219 ? 0.2417 0.2379 0.1968 -0.0337 0.0184  0.0312  218 GLY B CA  
4215 C C   . GLY B 219 ? 0.2368 0.2264 0.1801 -0.0317 0.0243  0.0277  218 GLY B C   
4216 O O   . GLY B 219 ? 0.2462 0.2365 0.1915 -0.0292 0.0210  0.0258  218 GLY B O   
4217 N N   . GLN B 220 ? 0.2438 0.2272 0.1747 -0.0328 0.0332  0.0268  219 GLN B N   
4218 C CA  . GLN B 220 ? 0.2607 0.2357 0.1773 -0.0316 0.0389  0.0237  219 GLN B CA  
4219 C C   . GLN B 220 ? 0.3029 0.2644 0.2046 -0.0332 0.0310  0.0242  219 GLN B C   
4220 O O   . GLN B 220 ? 0.3112 0.2718 0.2114 -0.0303 0.0310  0.0215  219 GLN B O   
4221 C CB  . GLN B 220 ? 0.2889 0.2563 0.1912 -0.0339 0.0478  0.0236  219 GLN B CB  
4222 C CG  . GLN B 220 ? 0.2839 0.2405 0.1689 -0.0332 0.0531  0.0207  219 GLN B CG  
4223 C CD  . GLN B 220 ? 0.3001 0.2498 0.1713 -0.0355 0.0622  0.0204  219 GLN B CD  
4224 O OE1 . GLN B 220 ? 0.3088 0.2633 0.1848 -0.0371 0.0657  0.0221  219 GLN B OE1 
4225 N NE2 . GLN B 220 ? 0.3213 0.2598 0.1751 -0.0356 0.0661  0.0184  219 GLN B NE2 
4226 N N   . GLU B 221 ? 0.3257 0.2764 0.2157 -0.0378 0.0242  0.0278  220 GLU B N   
4227 C CA  . GLU B 221 ? 0.3022 0.2393 0.1770 -0.0397 0.0165  0.0285  220 GLU B CA  
4228 C C   . GLU B 221 ? 0.3009 0.2447 0.1877 -0.0366 0.0094  0.0276  220 GLU B C   
4229 O O   . GLU B 221 ? 0.3075 0.2444 0.1855 -0.0355 0.0075  0.0258  220 GLU B O   
4230 C CB  . GLU B 221 ? 0.3150 0.2419 0.1794 -0.0449 0.0091  0.0328  220 GLU B CB  
4231 C CG  . GLU B 221 ? 0.4368 0.3547 0.2867 -0.0488 0.0144  0.0344  220 GLU B CG  
4232 C CD  . GLU B 221 ? 0.4141 0.3237 0.2568 -0.0537 0.0060  0.0388  220 GLU B CD  
4233 O OE1 . GLU B 221 ? 0.6630 0.5642 0.4981 -0.0552 -0.0028 0.0400  220 GLU B OE1 
4234 O OE2 . GLU B 221 ? 0.5289 0.4405 0.3738 -0.0562 0.0080  0.0410  220 GLU B OE2 
4235 N N   . ARG B 222 ? 0.2785 0.2357 0.1855 -0.0352 0.0052  0.0287  221 ARG B N   
4236 C CA  . ARG B 222 ? 0.2685 0.2321 0.1873 -0.0329 -0.0028 0.0283  221 ARG B CA  
4237 C C   . ARG B 222 ? 0.2842 0.2575 0.2138 -0.0277 0.0020  0.0243  221 ARG B C   
4238 O O   . ARG B 222 ? 0.3034 0.2794 0.2389 -0.0258 -0.0042 0.0235  221 ARG B O   
4239 C CB  . ARG B 222 ? 0.2462 0.2208 0.1828 -0.0334 -0.0090 0.0310  221 ARG B CB  
4240 C CG  . ARG B 222 ? 0.2780 0.2422 0.2044 -0.0382 -0.0178 0.0350  221 ARG B CG  
4241 C CD  . ARG B 222 ? 0.2422 0.2169 0.1857 -0.0388 -0.0242 0.0377  221 ARG B CD  
4242 N NE  . ARG B 222 ? 0.2485 0.2125 0.1815 -0.0434 -0.0329 0.0414  221 ARG B NE  
4243 C CZ  . ARG B 222 ? 0.2781 0.2477 0.2218 -0.0449 -0.0396 0.0443  221 ARG B CZ  
4244 N NH1 . ARG B 222 ? 0.2994 0.2852 0.2648 -0.0422 -0.0389 0.0439  221 ARG B NH1 
4245 N NH2 . ARG B 222 ? 0.3206 0.2794 0.2532 -0.0492 -0.0472 0.0476  221 ARG B NH2 
4246 N N   . ILE B 223 ? 0.2365 0.2151 0.1689 -0.0254 0.0126  0.0217  222 ILE B N   
4247 C CA  . ILE B 223 ? 0.2183 0.2054 0.1601 -0.0205 0.0171  0.0178  222 ILE B CA  
4248 C C   . ILE B 223 ? 0.2437 0.2204 0.1686 -0.0197 0.0235  0.0149  222 ILE B C   
4249 O O   . ILE B 223 ? 0.2419 0.2245 0.1730 -0.0156 0.0275  0.0115  222 ILE B O   
4250 C CB  . ILE B 223 ? 0.2181 0.2220 0.1800 -0.0173 0.0242  0.0164  222 ILE B CB  
4251 C CG1 . ILE B 223 ? 0.2126 0.2140 0.1669 -0.0185 0.0343  0.0160  222 ILE B CG1 
4252 C CG2 . ILE B 223 ? 0.2485 0.2631 0.2277 -0.0180 0.0177  0.0191  222 ILE B CG2 
4253 C CD1 . ILE B 223 ? 0.2785 0.2955 0.2505 -0.0148 0.0428  0.0137  222 ILE B CD1 
4254 N N   . THR B 224 ? 0.2523 0.2134 0.1558 -0.0235 0.0241  0.0162  223 THR B N   
4255 C CA  . THR B 224 ? 0.2692 0.2203 0.1561 -0.0229 0.0307  0.0135  223 THR B CA  
4256 C C   . THR B 224 ? 0.2854 0.2323 0.1683 -0.0207 0.0263  0.0114  223 THR B C   
4257 O O   . THR B 224 ? 0.2927 0.2416 0.1758 -0.0173 0.0323  0.0078  223 THR B O   
4258 C CB  . THR B 224 ? 0.2981 0.2335 0.1634 -0.0278 0.0315  0.0156  223 THR B CB  
4259 O OG1 . THR B 224 ? 0.3357 0.2755 0.2041 -0.0291 0.0383  0.0166  223 THR B OG1 
4260 C CG2 . THR B 224 ? 0.3378 0.2605 0.1835 -0.0276 0.0363  0.0131  223 THR B CG2 
4261 N N   . SER B 225 ? 0.2853 0.2264 0.1648 -0.0226 0.0157  0.0137  224 SER B N   
4262 C CA  A SER B 225 ? 0.3073 0.2440 0.1825 -0.0208 0.0110  0.0119  224 SER B CA  
4263 C CA  B SER B 225 ? 0.3074 0.2440 0.1823 -0.0208 0.0114  0.0118  224 SER B CA  
4264 C CA  C SER B 225 ? 0.3074 0.2441 0.1825 -0.0208 0.0111  0.0119  224 SER B CA  
4265 C C   . SER B 225 ? 0.2692 0.2211 0.1644 -0.0158 0.0121  0.0092  224 SER B C   
4266 O O   . SER B 225 ? 0.2739 0.2244 0.1663 -0.0129 0.0142  0.0061  224 SER B O   
4267 C CB  A SER B 225 ? 0.3202 0.2492 0.1898 -0.0240 -0.0010 0.0151  224 SER B CB  
4268 C CB  B SER B 225 ? 0.3256 0.2526 0.1922 -0.0241 -0.0002 0.0149  224 SER B CB  
4269 C CB  C SER B 225 ? 0.3220 0.2505 0.1909 -0.0240 -0.0008 0.0151  224 SER B CB  
4270 O OG  A SER B 225 ? 0.3789 0.3034 0.2441 -0.0223 -0.0057 0.0135  224 SER B OG  
4271 O OG  B SER B 225 ? 0.3226 0.2600 0.2064 -0.0238 -0.0077 0.0169  224 SER B OG  
4272 O OG  C SER B 225 ? 0.3316 0.2445 0.1798 -0.0285 -0.0016 0.0173  224 SER B OG  
4273 N N   . ALA B 226 ? 0.2533 0.2194 0.1686 -0.0147 0.0105  0.0102  225 ALA B N   
4274 C CA  . ALA B 226 ? 0.2487 0.2300 0.1840 -0.0099 0.0117  0.0077  225 ALA B CA  
4275 C C   . ALA B 226 ? 0.2492 0.2354 0.1865 -0.0065 0.0232  0.0039  225 ALA B C   
4276 O O   . ALA B 226 ? 0.2477 0.2395 0.1919 -0.0026 0.0249  0.0008  225 ALA B O   
4277 C CB  . ALA B 226 ? 0.2402 0.2357 0.1962 -0.0097 0.0083  0.0097  225 ALA B CB  
4278 N N   . THR B 227 ? 0.2371 0.2211 0.1683 -0.0079 0.0312  0.0041  226 THR B N   
4279 C CA  . THR B 227 ? 0.2572 0.2449 0.1889 -0.0049 0.0424  0.0005  226 THR B CA  
4280 C C   . THR B 227 ? 0.2888 0.2661 0.2054 -0.0036 0.0444  -0.0024 226 THR B C   
4281 O O   . THR B 227 ? 0.2622 0.2460 0.1856 0.0006  0.0494  -0.0059 226 THR B O   
4282 C CB  . THR B 227 ? 0.2361 0.2210 0.1609 -0.0074 0.0498  0.0016  226 THR B CB  
4283 O OG1 . THR B 227 ? 0.2601 0.2548 0.1992 -0.0086 0.0476  0.0043  226 THR B OG1 
4284 C CG2 . THR B 227 ? 0.2843 0.2736 0.2100 -0.0043 0.0619  -0.0021 226 THR B CG2 
4285 N N   . GLN B 228 ? 0.2692 0.2303 0.1654 -0.0070 0.0403  -0.0009 227 GLN B N   
4286 C CA  A GLN B 228 ? 0.3202 0.2707 0.2013 -0.0060 0.0417  -0.0035 227 GLN B CA  
4287 C CA  B GLN B 228 ? 0.3206 0.2709 0.2015 -0.0061 0.0416  -0.0034 227 GLN B CA  
4288 C C   . GLN B 228 ? 0.3145 0.2697 0.2044 -0.0028 0.0359  -0.0051 227 GLN B C   
4289 O O   . GLN B 228 ? 0.3254 0.2792 0.2120 0.0002  0.0397  -0.0085 227 GLN B O   
4290 C CB  A GLN B 228 ? 0.3348 0.2672 0.1930 -0.0106 0.0376  -0.0012 227 GLN B CB  
4291 C CB  B GLN B 228 ? 0.3345 0.2667 0.1925 -0.0107 0.0372  -0.0011 227 GLN B CB  
4292 C CG  A GLN B 228 ? 0.3304 0.2585 0.1812 -0.0145 0.0410  0.0014  227 GLN B CG  
4293 C CG  B GLN B 228 ? 0.4099 0.3291 0.2481 -0.0105 0.0424  -0.0037 227 GLN B CG  
4294 C CD  A GLN B 228 ? 0.5155 0.4462 0.3648 -0.0131 0.0532  -0.0011 227 GLN B CD  
4295 C CD  B GLN B 228 ? 0.5693 0.4880 0.4078 -0.0071 0.0402  -0.0066 227 GLN B CD  
4296 O OE1 A GLN B 228 ? 0.5777 0.5007 0.4139 -0.0122 0.0589  -0.0037 227 GLN B OE1 
4297 O OE1 B GLN B 228 ? 0.5631 0.4849 0.4028 -0.0036 0.0476  -0.0103 227 GLN B OE1 
4298 N NE2 A GLN B 228 ? 0.4530 0.3949 0.3156 -0.0130 0.0574  -0.0002 227 GLN B NE2 
4299 N NE2 B GLN B 228 ? 0.5329 0.4478 0.3703 -0.0080 0.0299  -0.0050 227 GLN B NE2 
4300 N N   . TRP B 229 ? 0.2835 0.2442 0.1846 -0.0035 0.0265  -0.0027 228 TRP B N   
4301 C CA  . TRP B 229 ? 0.2565 0.2223 0.1667 -0.0006 0.0206  -0.0040 228 TRP B CA  
4302 C C   . TRP B 229 ? 0.2578 0.2386 0.1860 0.0044  0.0268  -0.0074 228 TRP B C   
4303 O O   . TRP B 229 ? 0.2538 0.2352 0.1825 0.0075  0.0274  -0.0103 228 TRP B O   
4304 C CB  . TRP B 229 ? 0.2652 0.2349 0.1850 -0.0024 0.0097  -0.0007 228 TRP B CB  
4305 C CG  . TRP B 229 ? 0.2865 0.2603 0.2143 0.0000  0.0025  -0.0017 228 TRP B CG  
4306 C CD1 . TRP B 229 ? 0.2506 0.2135 0.1663 -0.0013 -0.0049 -0.0012 228 TRP B CD1 
4307 C CD2 . TRP B 229 ? 0.2211 0.2111 0.1710 0.0038  0.0017  -0.0033 228 TRP B CD2 
4308 N NE1 . TRP B 229 ? 0.2567 0.2280 0.1853 0.0015  -0.0101 -0.0024 228 TRP B NE1 
4309 C CE2 . TRP B 229 ? 0.2456 0.2334 0.1952 0.0047  -0.0062 -0.0037 228 TRP B CE2 
4310 C CE3 . TRP B 229 ? 0.2151 0.2212 0.1848 0.0067  0.0071  -0.0044 228 TRP B CE3 
4311 C CZ2 . TRP B 229 ? 0.2010 0.2022 0.1694 0.0082  -0.0090 -0.0051 228 TRP B CZ2 
4312 C CZ3 . TRP B 229 ? 0.2369 0.2564 0.2256 0.0102  0.0043  -0.0058 228 TRP B CZ3 
4313 C CH2 . TRP B 229 ? 0.2198 0.2366 0.2074 0.0109  -0.0037 -0.0062 228 TRP B CH2 
4314 N N   . LEU B 230 ? 0.2298 0.2229 0.1729 0.0052  0.0314  -0.0070 229 LEU B N   
4315 C CA  . LEU B 230 ? 0.2477 0.2552 0.2079 0.0099  0.0380  -0.0102 229 LEU B CA  
4316 C C   . LEU B 230 ? 0.3069 0.3095 0.2569 0.0121  0.0472  -0.0139 229 LEU B C   
4317 O O   . LEU B 230 ? 0.2345 0.2425 0.1912 0.0160  0.0492  -0.0171 229 LEU B O   
4318 C CB  . LEU B 230 ? 0.2238 0.2437 0.1993 0.0099  0.0423  -0.0090 229 LEU B CB  
4319 C CG  . LEU B 230 ? 0.2070 0.2348 0.1965 0.0085  0.0339  -0.0057 229 LEU B CG  
4320 C CD1 . LEU B 230 ? 0.2141 0.2506 0.2135 0.0077  0.0389  -0.0043 229 LEU B CD1 
4321 C CD2 . LEU B 230 ? 0.1859 0.2261 0.1939 0.0121  0.0292  -0.0070 229 LEU B CD2 
4322 N N   . ARG B 231 ? 0.2495 0.2413 0.1826 0.0096  0.0527  -0.0136 230 ARG B N   
4323 C CA  . ARG B 231 ? 0.2613 0.2488 0.1850 0.0118  0.0621  -0.0172 230 ARG B CA  
4324 C C   . ARG B 231 ? 0.3227 0.3003 0.2343 0.0128  0.0587  -0.0191 230 ARG B C   
4325 O O   . ARG B 231 ? 0.3054 0.2863 0.2198 0.0166  0.0634  -0.0228 230 ARG B O   
4326 C CB  . ARG B 231 ? 0.3018 0.2799 0.2099 0.0086  0.0684  -0.0163 230 ARG B CB  
4327 C CG  . ARG B 231 ? 0.3825 0.3561 0.2804 0.0107  0.0783  -0.0201 230 ARG B CG  
4328 C CD  . ARG B 231 ? 0.4203 0.3878 0.3065 0.0080  0.0857  -0.0194 230 ARG B CD  
4329 N NE  . ARG B 231 ? 0.4194 0.3989 0.3205 0.0077  0.0891  -0.0180 230 ARG B NE  
4330 C CZ  . ARG B 231 ? 0.4245 0.4016 0.3231 0.0037  0.0865  -0.0143 230 ARG B CZ  
4331 N NH1 . ARG B 231 ? 0.4565 0.4196 0.3384 -0.0005 0.0806  -0.0116 230 ARG B NH1 
4332 N NH2 . ARG B 231 ? 0.3944 0.3834 0.3077 0.0039  0.0900  -0.0133 230 ARG B NH2 
4333 N N   . ALA B 232 ? 0.3267 0.2920 0.2248 0.0094  0.0504  -0.0167 231 ALA B N   
4334 C CA  . ALA B 232 ? 0.3379 0.2927 0.2231 0.0100  0.0468  -0.0182 231 ALA B CA  
4335 C C   . ALA B 232 ? 0.3788 0.3434 0.2789 0.0140  0.0433  -0.0203 231 ALA B C   
4336 O O   . ALA B 232 ? 0.3375 0.2976 0.2311 0.0163  0.0444  -0.0231 231 ALA B O   
4337 C CB  . ALA B 232 ? 0.3815 0.3226 0.2517 0.0055  0.0376  -0.0148 231 ALA B CB  
4338 N N   . ASN B 233 ? 0.2698 0.2236 0.2122 0.0251  0.0275  -0.0335 232 ASN B N   
4339 C CA  . ASN B 233 ? 0.2844 0.2404 0.2339 0.0310  0.0230  -0.0329 232 ASN B CA  
4340 C C   . ASN B 233 ? 0.3014 0.2681 0.2643 0.0341  0.0239  -0.0353 232 ASN B C   
4341 O O   . ASN B 233 ? 0.2909 0.2603 0.2606 0.0390  0.0201  -0.0348 232 ASN B O   
4342 C CB  . ASN B 233 ? 0.2760 0.2260 0.2215 0.0311  0.0169  -0.0283 232 ASN B CB  
4343 C CG  . ASN B 233 ? 0.3351 0.2749 0.2684 0.0298  0.0152  -0.0260 232 ASN B CG  
4344 O OD1 . ASN B 233 ? 0.3309 0.2686 0.2632 0.0332  0.0142  -0.0267 232 ASN B OD1 
4345 N ND2 . ASN B 233 ? 0.3098 0.2434 0.2340 0.0248  0.0150  -0.0232 232 ASN B ND2 
4346 N N   . GLY B 234 ? 0.2694 0.2423 0.2361 0.0315  0.0288  -0.0380 233 GLY B N   
4347 C CA  . GLY B 234 ? 0.2437 0.2273 0.2231 0.0343  0.0300  -0.0405 233 GLY B CA  
4348 C C   . GLY B 234 ? 0.2754 0.2620 0.2610 0.0354  0.0256  -0.0381 233 GLY B C   
4349 O O   . GLY B 234 ? 0.2580 0.2519 0.2541 0.0398  0.0242  -0.0392 233 GLY B O   
4350 N N   . LYS B 235 ? 0.2551 0.2365 0.2346 0.0315  0.0235  -0.0349 234 LYS B N   
4351 C CA  . LYS B 235 ? 0.1971 0.1800 0.1810 0.0321  0.0191  -0.0323 234 LYS B CA  
4352 C C   . LYS B 235 ? 0.2411 0.2287 0.2277 0.0277  0.0219  -0.0328 234 LYS B C   
4353 O O   . LYS B 235 ? 0.2572 0.2450 0.2400 0.0236  0.0267  -0.0344 234 LYS B O   
4354 C CB  . LYS B 235 ? 0.2218 0.1947 0.1966 0.0311  0.0142  -0.0278 234 LYS B CB  
4355 C CG  . LYS B 235 ? 0.2858 0.2529 0.2564 0.0348  0.0112  -0.0268 234 LYS B CG  
4356 C CD  . LYS B 235 ? 0.2369 0.2100 0.2175 0.0412  0.0093  -0.0285 234 LYS B CD  
4357 C CE  . LYS B 235 ? 0.2777 0.2440 0.2534 0.0446  0.0055  -0.0269 234 LYS B CE  
4358 N NZ  . LYS B 235 ? 0.2724 0.2441 0.2572 0.0508  0.0042  -0.0288 234 LYS B NZ  
4359 N N   . LYS B 236 ? 0.2357 0.2272 0.2289 0.0287  0.0188  -0.0314 235 LYS B N   
4360 C CA  . LYS B 236 ? 0.2429 0.2377 0.2380 0.0245  0.0203  -0.0311 235 LYS B CA  
4361 C C   . LYS B 236 ? 0.2250 0.2124 0.2139 0.0223  0.0161  -0.0267 235 LYS B C   
4362 O O   . LYS B 236 ? 0.2354 0.2194 0.2244 0.0257  0.0110  -0.0242 235 LYS B O   
4363 C CB  . LYS B 236 ? 0.2329 0.2387 0.2409 0.0270  0.0204  -0.0330 235 LYS B CB  
4364 C CG  . LYS B 236 ? 0.3160 0.3304 0.3316 0.0294  0.0247  -0.0373 235 LYS B CG  
4365 C CD  . LYS B 236 ? 0.4050 0.4217 0.4182 0.0246  0.0308  -0.0398 235 LYS B CD  
4366 C CE  . LYS B 236 ? 0.4891 0.5174 0.5133 0.0266  0.0345  -0.0438 235 LYS B CE  
4367 N NZ  . LYS B 236 ? 0.4707 0.5018 0.4932 0.0219  0.0406  -0.0463 235 LYS B NZ  
4368 N N   . GLY B 237 ? 0.2257 0.2109 0.2097 0.0168  0.0182  -0.0257 236 GLY B N   
4369 C CA  . GLY B 237 ? 0.2018 0.1806 0.1806 0.0145  0.0146  -0.0216 236 GLY B CA  
4370 C C   . GLY B 237 ? 0.2018 0.1852 0.1849 0.0112  0.0158  -0.0216 236 GLY B C   
4371 O O   . GLY B 237 ? 0.2157 0.2071 0.2048 0.0099  0.0200  -0.0248 236 GLY B O   
4372 N N   . ILE B 238 ? 0.2198 0.1981 0.1997 0.0098  0.0122  -0.0180 237 ILE B N   
4373 C CA  . ILE B 238 ? 0.2118 0.1922 0.1934 0.0059  0.0132  -0.0173 237 ILE B CA  
4374 C C   . ILE B 238 ? 0.2419 0.2120 0.2133 0.0027  0.0109  -0.0130 237 ILE B C   
4375 O O   . ILE B 238 ? 0.2351 0.1983 0.2016 0.0049  0.0068  -0.0102 237 ILE B O   
4376 C CB  . ILE B 238 ? 0.1840 0.1721 0.1769 0.0089  0.0106  -0.0177 237 ILE B CB  
4377 C CG1 . ILE B 238 ? 0.2104 0.2022 0.2058 0.0045  0.0127  -0.0178 237 ILE B CG1 
4378 C CG2 . ILE B 238 ? 0.2305 0.2139 0.2233 0.0126  0.0043  -0.0143 237 ILE B CG2 
4379 C CD1 . ILE B 238 ? 0.2046 0.2049 0.2116 0.0070  0.0107  -0.0186 237 ILE B CD1 
4380 N N   . ILE B 239 ? 0.2077 0.1767 0.1756 -0.0026 0.0136  -0.0125 238 ILE B N   
4381 C CA  . ILE B 239 ? 0.2141 0.1742 0.1736 -0.0058 0.0114  -0.0083 238 ILE B CA  
4382 C C   . ILE B 239 ? 0.2384 0.2010 0.2042 -0.0048 0.0082  -0.0067 238 ILE B C   
4383 O O   . ILE B 239 ? 0.2442 0.2128 0.2155 -0.0071 0.0105  -0.0082 238 ILE B O   
4384 C CB  . ILE B 239 ? 0.2507 0.2077 0.2027 -0.0120 0.0160  -0.0083 238 ILE B CB  
4385 C CG1 . ILE B 239 ? 0.2569 0.2106 0.2017 -0.0130 0.0189  -0.0096 238 ILE B CG1 
4386 C CG2 . ILE B 239 ? 0.2501 0.1986 0.1945 -0.0152 0.0138  -0.0039 238 ILE B CG2 
4387 C CD1 . ILE B 239 ? 0.2615 0.2051 0.1968 -0.0120 0.0154  -0.0061 238 ILE B CD1 
4388 N N   . GLY B 240 ? 0.2014 0.1597 0.1668 -0.0014 0.0028  -0.0037 239 GLY B N   
4389 C CA  . GLY B 240 ? 0.2125 0.1735 0.1846 0.0001  -0.0006 -0.0024 239 GLY B CA  
4390 C C   . GLY B 240 ? 0.2269 0.1819 0.1937 -0.0039 -0.0015 0.0011  239 GLY B C   
4391 O O   . GLY B 240 ? 0.2247 0.1826 0.1972 -0.0036 -0.0033 0.0017  239 GLY B O   
4392 N N   . GLU B 241 ? 0.2081 0.1546 0.1640 -0.0074 -0.0005 0.0034  240 GLU B N   
4393 C CA  . GLU B 241 ? 0.2025 0.1429 0.1524 -0.0118 -0.0005 0.0065  240 GLU B CA  
4394 C C   . GLU B 241 ? 0.2307 0.1662 0.1710 -0.0165 0.0036  0.0066  240 GLU B C   
4395 O O   . GLU B 241 ? 0.2458 0.1768 0.1799 -0.0157 0.0034  0.0071  240 GLU B O   
4396 C CB  . GLU B 241 ? 0.2127 0.1448 0.1580 -0.0101 -0.0059 0.0112  240 GLU B CB  
4397 C CG  . GLU B 241 ? 0.2161 0.1517 0.1698 -0.0056 -0.0105 0.0118  240 GLU B CG  
4398 C CD  . GLU B 241 ? 0.3075 0.2344 0.2559 -0.0045 -0.0154 0.0166  240 GLU B CD  
4399 O OE1 . GLU B 241 ? 0.2799 0.1985 0.2187 -0.0078 -0.0152 0.0197  240 GLU B OE1 
4400 O OE2 . GLU B 241 ? 0.2564 0.1848 0.2102 -0.0003 -0.0197 0.0174  240 GLU B OE2 
4401 N N   . PHE B 242 ? 0.2319 0.1681 0.1709 -0.0215 0.0072  0.0062  241 PHE B N   
4402 C CA  . PHE B 242 ? 0.2291 0.1591 0.1580 -0.0265 0.0105  0.0073  241 PHE B CA  
4403 C C   . PHE B 242 ? 0.2877 0.2162 0.2153 -0.0310 0.0119  0.0087  241 PHE B C   
4404 O O   . PHE B 242 ? 0.2458 0.1804 0.1814 -0.0309 0.0120  0.0075  241 PHE B O   
4405 C CB  . PHE B 242 ? 0.2729 0.2073 0.2015 -0.0280 0.0155  0.0033  241 PHE B CB  
4406 C CG  . PHE B 242 ? 0.2656 0.2091 0.2016 -0.0303 0.0199  -0.0005 241 PHE B CG  
4407 C CD1 . PHE B 242 ? 0.2534 0.2061 0.2009 -0.0270 0.0191  -0.0031 241 PHE B CD1 
4408 C CD2 . PHE B 242 ? 0.2770 0.2199 0.2084 -0.0359 0.0247  -0.0014 241 PHE B CD2 
4409 C CE1 . PHE B 242 ? 0.2456 0.2072 0.2002 -0.0291 0.0231  -0.0065 241 PHE B CE1 
4410 C CE2 . PHE B 242 ? 0.2615 0.2130 0.1998 -0.0381 0.0288  -0.0050 241 PHE B CE2 
4411 C CZ  . PHE B 242 ? 0.2622 0.2233 0.2122 -0.0347 0.0279  -0.0075 241 PHE B CZ  
4412 N N   . ALA B 243 ? 0.2683 0.1889 0.1858 -0.0352 0.0132  0.0114  242 ALA B N   
4413 C CA  . ALA B 243 ? 0.2690 0.1873 0.1842 -0.0398 0.0149  0.0129  242 ALA B CA  
4414 C C   . ALA B 243 ? 0.2829 0.1933 0.1866 -0.0444 0.0174  0.0149  242 ALA B C   
4415 O O   . ALA B 243 ? 0.2821 0.1876 0.1792 -0.0436 0.0166  0.0161  242 ALA B O   
4416 C CB  . ALA B 243 ? 0.3070 0.2215 0.2235 -0.0383 0.0103  0.0165  242 ALA B CB  
4417 N N   . GLY B 244 ? 0.2702 0.1799 0.1718 -0.0494 0.0206  0.0151  243 GLY B N   
4418 C CA  . GLY B 244 ? 0.2749 0.1762 0.1654 -0.0541 0.0225  0.0178  243 GLY B CA  
4419 C C   . GLY B 244 ? 0.2894 0.1896 0.1799 -0.0581 0.0239  0.0191  243 GLY B C   
4420 O O   . GLY B 244 ? 0.2969 0.2040 0.1959 -0.0579 0.0247  0.0168  243 GLY B O   
4421 N N   . GLY B 245 ? 0.3149 0.2062 0.1957 -0.0617 0.0243  0.0227  244 GLY B N   
4422 C CA  . GLY B 245 ? 0.3562 0.2452 0.2358 -0.0656 0.0258  0.0242  244 GLY B CA  
4423 C C   . GLY B 245 ? 0.3649 0.2601 0.2471 -0.0700 0.0315  0.0204  244 GLY B C   
4424 O O   . GLY B 245 ? 0.3327 0.2322 0.2152 -0.0707 0.0347  0.0171  244 GLY B O   
4425 N N   . ALA B 246 ? 0.3353 0.2309 0.2194 -0.0730 0.0327  0.0208  245 ALA B N   
4426 C CA  . ALA B 246 ? 0.3643 0.2652 0.2504 -0.0776 0.0381  0.0175  245 ALA B CA  
4427 C C   . ALA B 246 ? 0.3657 0.2592 0.2408 -0.0828 0.0414  0.0193  245 ALA B C   
4428 O O   . ALA B 246 ? 0.3857 0.2742 0.2564 -0.0866 0.0424  0.0216  245 ALA B O   
4429 C CB  . ALA B 246 ? 0.3718 0.2761 0.2642 -0.0787 0.0382  0.0171  245 ALA B CB  
4430 N N   . ASN B 247 ? 0.3395 0.2325 0.2100 -0.0831 0.0431  0.0181  246 ASN B N   
4431 C CA  . ASN B 247 ? 0.3571 0.2436 0.2172 -0.0879 0.0462  0.0196  246 ASN B CA  
4432 C C   . ASN B 247 ? 0.3722 0.2630 0.2316 -0.0885 0.0496  0.0159  246 ASN B C   
4433 O O   . ASN B 247 ? 0.3762 0.2739 0.2425 -0.0847 0.0490  0.0128  246 ASN B O   
4434 C CB  . ASN B 247 ? 0.3862 0.2618 0.2368 -0.0873 0.0427  0.0250  246 ASN B CB  
4435 C CG  . ASN B 247 ? 0.3736 0.2486 0.2248 -0.0819 0.0386  0.0257  246 ASN B CG  
4436 O OD1 . ASN B 247 ? 0.4200 0.2973 0.2701 -0.0812 0.0399  0.0234  246 ASN B OD1 
4437 N ND2 . ASN B 247 ? 0.3649 0.2367 0.2177 -0.0782 0.0335  0.0288  246 ASN B ND2 
4438 N N   . ASP B 248 ? 0.3692 0.2136 0.1970 -0.1102 0.0355  0.0180  247 ASP B N   
4439 C CA  . ASP B 248 ? 0.4339 0.2885 0.2608 -0.1095 0.0398  0.0167  247 ASP B CA  
4440 C C   . ASP B 248 ? 0.4370 0.2931 0.2669 -0.0994 0.0366  0.0162  247 ASP B C   
4441 O O   . ASP B 248 ? 0.3751 0.2472 0.2129 -0.0962 0.0384  0.0140  247 ASP B O   
4442 C CB  . ASP B 248 ? 0.4096 0.2532 0.2224 -0.1154 0.0435  0.0184  247 ASP B CB  
4443 C CG  . ASP B 248 ? 0.4884 0.3432 0.3002 -0.1156 0.0483  0.0170  247 ASP B CG  
4444 O OD1 . ASP B 248 ? 0.5514 0.4241 0.3715 -0.1183 0.0521  0.0148  247 ASP B OD1 
4445 O OD2 . ASP B 248 ? 0.5698 0.4155 0.3726 -0.1129 0.0484  0.0182  247 ASP B OD2 
4446 N N   . VAL B 249 ? 0.3720 0.2113 0.1954 -0.0945 0.0319  0.0183  248 VAL B N   
4447 C CA  . VAL B 249 ? 0.3883 0.2275 0.2133 -0.0851 0.0289  0.0180  248 VAL B CA  
4448 C C   . VAL B 249 ? 0.3814 0.2348 0.2211 -0.0789 0.0261  0.0158  248 VAL B C   
4449 O O   . VAL B 249 ? 0.3784 0.2429 0.2237 -0.0732 0.0266  0.0142  248 VAL B O   
4450 C CB  . VAL B 249 ? 0.4307 0.2486 0.2458 -0.0814 0.0242  0.0207  248 VAL B CB  
4451 C CG1 . VAL B 249 ? 0.3615 0.1798 0.1797 -0.0713 0.0205  0.0203  248 VAL B CG1 
4452 C CG2 . VAL B 249 ? 0.4170 0.2225 0.2174 -0.0868 0.0274  0.0226  248 VAL B CG2 
4453 N N   . CYS B 250 ? 0.3592 0.2128 0.2056 -0.0797 0.0233  0.0159  249 CYS B N   
4454 C CA  . CYS B 250 ? 0.3463 0.2128 0.2067 -0.0737 0.0205  0.0140  249 CYS B CA  
4455 C C   . CYS B 250 ? 0.3547 0.2430 0.2247 -0.0758 0.0251  0.0111  249 CYS B C   
4456 O O   . CYS B 250 ? 0.3715 0.2725 0.2510 -0.0694 0.0242  0.0092  249 CYS B O   
4457 C CB  . CYS B 250 ? 0.3904 0.2519 0.2553 -0.0746 0.0167  0.0147  249 CYS B CB  
4458 S SG  . CYS B 250 ? 0.3793 0.2178 0.2370 -0.0696 0.0099  0.0177  249 CYS B SG  
4459 N N   . GLU B 251 ? 0.3528 0.2461 0.2208 -0.0847 0.0300  0.0107  250 GLU B N   
4460 C CA  . GLU B 251 ? 0.3463 0.2603 0.2228 -0.0873 0.0347  0.0081  250 GLU B CA  
4461 C C   . GLU B 251 ? 0.3616 0.2831 0.2370 -0.0835 0.0373  0.0070  250 GLU B C   
4462 O O   . GLU B 251 ? 0.3306 0.2690 0.2162 -0.0797 0.0383  0.0047  250 GLU B O   
4463 C CB  . GLU B 251 ? 0.3372 0.2528 0.2100 -0.0979 0.0394  0.0082  250 GLU B CB  
4464 C CG  . GLU B 251 ? 0.3821 0.2982 0.2613 -0.1010 0.0373  0.0081  250 GLU B CG  
4465 C CD  . GLU B 251 ? 0.4526 0.3645 0.3260 -0.1113 0.0407  0.0089  250 GLU B CD  
4466 O OE1 . GLU B 251 ? 0.4645 0.3775 0.3309 -0.1168 0.0456  0.0090  250 GLU B OE1 
4467 O OE2 . GLU B 251 ? 0.4069 0.3145 0.2827 -0.1139 0.0384  0.0095  250 GLU B OE2 
4468 N N   . THR B 252 ? 0.3296 0.2386 0.1926 -0.0840 0.0383  0.0087  251 THR B N   
4469 C CA  . THR B 252 ? 0.3378 0.2529 0.1993 -0.0799 0.0405  0.0078  251 THR B CA  
4470 C C   . THR B 252 ? 0.3887 0.3063 0.2570 -0.0695 0.0360  0.0070  251 THR B C   
4471 O O   . THR B 252 ? 0.3213 0.2531 0.1960 -0.0654 0.0376  0.0050  251 THR B O   
4472 C CB  . THR B 252 ? 0.3348 0.2345 0.1812 -0.0825 0.0421  0.0099  251 THR B CB  
4473 O OG1 . THR B 252 ? 0.3761 0.2730 0.2163 -0.0923 0.0461  0.0107  251 THR B OG1 
4474 C CG2 . THR B 252 ? 0.3811 0.2882 0.2256 -0.0792 0.0451  0.0088  251 THR B CG2 
4475 N N   . ALA B 253 ? 0.3365 0.2405 0.2034 -0.0650 0.0302  0.0086  252 ALA B N   
4476 C CA  . ALA B 253 ? 0.3175 0.2230 0.1910 -0.0551 0.0255  0.0081  252 ALA B CA  
4477 C C   . ALA B 253 ? 0.3001 0.2243 0.1890 -0.0523 0.0251  0.0055  252 ALA B C   
4478 O O   . ALA B 253 ? 0.2982 0.2319 0.1940 -0.0452 0.0241  0.0040  252 ALA B O   
4479 C CB  . ALA B 253 ? 0.2960 0.1830 0.1650 -0.0517 0.0195  0.0104  252 ALA B CB  
4480 N N   . ILE B 254 ? 0.3127 0.2420 0.2070 -0.0578 0.0259  0.0051  253 ILE B N   
4481 C CA  . ILE B 254 ? 0.2709 0.2180 0.1798 -0.0555 0.0256  0.0027  253 ILE B CA  
4482 C C   . ILE B 254 ? 0.2972 0.2632 0.2112 -0.0563 0.0308  0.0003  253 ILE B C   
4483 O O   . ILE B 254 ? 0.2786 0.2574 0.2023 -0.0500 0.0300  -0.0016 253 ILE B O   
4484 C CB  . ILE B 254 ? 0.2620 0.2099 0.1748 -0.0618 0.0255  0.0028  253 ILE B CB  
4485 C CG1 . ILE B 254 ? 0.2937 0.2256 0.2046 -0.0590 0.0194  0.0049  253 ILE B CG1 
4486 C CG2 . ILE B 254 ? 0.2832 0.2520 0.2105 -0.0612 0.0268  0.0001  253 ILE B CG2 
4487 C CD1 . ILE B 254 ? 0.3064 0.2347 0.2178 -0.0658 0.0192  0.0055  253 ILE B CD1 
4488 N N   . THR B 255 ? 0.2846 0.2523 0.1920 -0.0640 0.0362  0.0003  254 THR B N   
4489 C CA  . THR B 255 ? 0.2977 0.2824 0.2087 -0.0653 0.0416  -0.0018 254 THR B CA  
4490 C C   . THR B 255 ? 0.2928 0.2785 0.2023 -0.0576 0.0410  -0.0022 254 THR B C   
4491 O O   . THR B 255 ? 0.2876 0.2895 0.2059 -0.0537 0.0424  -0.0044 254 THR B O   
4492 C CB  . THR B 255 ? 0.3407 0.3238 0.2428 -0.0749 0.0471  -0.0012 254 THR B CB  
4493 O OG1 . THR B 255 ? 0.3433 0.3300 0.2493 -0.0820 0.0482  -0.0014 254 THR B OG1 
4494 C CG2 . THR B 255 ? 0.4192 0.4175 0.3229 -0.0758 0.0526  -0.0030 254 THR B CG2 
4495 N N   . GLY B 256 ? 0.2938 0.2621 0.1926 -0.0550 0.0386  -0.0001 255 GLY B N   
4496 C CA  . GLY B 256 ? 0.2889 0.2571 0.1857 -0.0478 0.0379  -0.0004 255 GLY B CA  
4497 C C   . GLY B 256 ? 0.3005 0.2751 0.2080 -0.0385 0.0334  -0.0016 255 GLY B C   
4498 O O   . GLY B 256 ? 0.2887 0.2741 0.2008 -0.0332 0.0344  -0.0033 255 GLY B O   
4499 N N   . MET B 257 ? 0.2871 0.2552 0.1987 -0.0363 0.0285  -0.0008 256 MET B N   
4500 C CA  . MET B 257 ? 0.2738 0.2475 0.1957 -0.0275 0.0240  -0.0019 256 MET B CA  
4501 C C   . MET B 257 ? 0.2535 0.2494 0.1889 -0.0268 0.0264  -0.0047 256 MET B C   
4502 O O   . MET B 257 ? 0.2404 0.2460 0.1828 -0.0197 0.0255  -0.0063 256 MET B O   
4503 C CB  . MET B 257 ? 0.2760 0.2374 0.1989 -0.0259 0.0183  -0.0003 256 MET B CB  
4504 C CG  . MET B 257 ? 0.2558 0.2210 0.1885 -0.0166 0.0133  -0.0011 256 MET B CG  
4505 S SD  . MET B 257 ? 0.3071 0.2592 0.2418 -0.0149 0.0069  0.0007  256 MET B SD  
4506 C CE  . MET B 257 ? 0.3497 0.3182 0.2964 -0.0203 0.0090  -0.0012 256 MET B CE  
4507 N N   . LEU B 258 ? 0.2547 0.2590 0.1938 -0.0343 0.0296  -0.0055 257 LEU B N   
4508 C CA  . LEU B 258 ? 0.2596 0.2853 0.2117 -0.0340 0.0319  -0.0082 257 LEU B CA  
4509 C C   . LEU B 258 ? 0.2484 0.2871 0.2004 -0.0343 0.0372  -0.0098 257 LEU B C   
4510 O O   . LEU B 258 ? 0.2627 0.3174 0.2248 -0.0297 0.0379  -0.0120 257 LEU B O   
4511 C CB  . LEU B 258 ? 0.2737 0.3042 0.2297 -0.0418 0.0336  -0.0084 257 LEU B CB  
4512 C CG  . LEU B 258 ? 0.2441 0.2634 0.2015 -0.0415 0.0285  -0.0070 257 LEU B CG  
4513 C CD1 . LEU B 258 ? 0.2560 0.2780 0.2146 -0.0504 0.0308  -0.0070 257 LEU B CD1 
4514 C CD2 . LEU B 258 ? 0.2243 0.2502 0.1934 -0.0331 0.0239  -0.0081 257 LEU B CD2 
4515 N N   . ASP B 259 ? 0.2628 0.2951 0.2036 -0.0397 0.0410  -0.0088 258 ASP B N   
4516 C CA  . ASP B 259 ? 0.2523 0.2954 0.1920 -0.0394 0.0457  -0.0102 258 ASP B CA  
4517 C C   . ASP B 259 ? 0.3111 0.3542 0.2523 -0.0296 0.0431  -0.0106 258 ASP B C   
4518 O O   . ASP B 259 ? 0.2936 0.3521 0.2416 -0.0261 0.0453  -0.0127 258 ASP B O   
4519 C CB  . ASP B 259 ? 0.2806 0.3142 0.2069 -0.0463 0.0497  -0.0087 258 ASP B CB  
4520 C CG  . ASP B 259 ? 0.2929 0.3327 0.2192 -0.0562 0.0542  -0.0090 258 ASP B CG  
4521 O OD1 . ASP B 259 ? 0.3113 0.3653 0.2486 -0.0577 0.0550  -0.0107 258 ASP B OD1 
4522 O OD2 . ASP B 259 ? 0.3298 0.3604 0.2452 -0.0627 0.0571  -0.0075 258 ASP B OD2 
4523 N N   . TYR B 260 ? 0.2835 0.3095 0.2184 -0.0249 0.0382  -0.0087 259 TYR B N   
4524 C CA  . TYR B 260 ? 0.2631 0.2882 0.1996 -0.0154 0.0351  -0.0091 259 TYR B CA  
4525 C C   . TYR B 260 ? 0.2725 0.3119 0.2236 -0.0092 0.0328  -0.0112 259 TYR B C   
4526 O O   . TYR B 260 ? 0.2916 0.3419 0.2478 -0.0035 0.0336  -0.0128 259 TYR B O   
4527 C CB  . TYR B 260 ? 0.3045 0.3082 0.2320 -0.0121 0.0301  -0.0066 259 TYR B CB  
4528 C CG  . TYR B 260 ? 0.2402 0.2416 0.1693 -0.0021 0.0263  -0.0069 259 TYR B CG  
4529 C CD1 . TYR B 260 ? 0.2663 0.2657 0.1884 0.0007  0.0281  -0.0069 259 TYR B CD1 
4530 C CD2 . TYR B 260 ? 0.2935 0.2950 0.2312 0.0045  0.0210  -0.0071 259 TYR B CD2 
4531 C CE1 . TYR B 260 ? 0.2954 0.2928 0.2191 0.0098  0.0246  -0.0072 259 TYR B CE1 
4532 C CE2 . TYR B 260 ? 0.3316 0.3312 0.2710 0.0135  0.0176  -0.0074 259 TYR B CE2 
4533 C CZ  . TYR B 260 ? 0.3666 0.3641 0.2991 0.0161  0.0193  -0.0074 259 TYR B CZ  
4534 O OH  . TYR B 260 ? 0.4019 0.3975 0.3364 0.0252  0.0157  -0.0077 259 TYR B OH  
4535 N N   . MET B 261 ? 0.2586 0.2980 0.2164 -0.0102 0.0299  -0.0110 260 MET B N   
4536 C CA  . MET B 261 ? 0.2187 0.2718 0.1907 -0.0047 0.0276  -0.0129 260 MET B CA  
4537 C C   . MET B 261 ? 0.2753 0.3501 0.2556 -0.0063 0.0327  -0.0155 260 MET B C   
4538 O O   . MET B 261 ? 0.2253 0.3127 0.2152 0.0001  0.0320  -0.0174 260 MET B O   
4539 C CB  . MET B 261 ? 0.2344 0.2838 0.2114 -0.0066 0.0242  -0.0123 260 MET B CB  
4540 C CG  . MET B 261 ? 0.2046 0.2341 0.1757 -0.0031 0.0184  -0.0099 260 MET B CG  
4541 S SD  . MET B 261 ? 0.2311 0.2544 0.2063 -0.0064 0.0147  -0.0088 260 MET B SD  
4542 C CE  . MET B 261 ? 0.1983 0.2405 0.1911 0.0001  0.0127  -0.0113 260 MET B CE  
4543 N N   . ALA B 262 ? 0.2377 0.3173 0.2145 -0.0149 0.0380  -0.0157 261 ALA B N   
4544 C CA  . ALA B 262 ? 0.2561 0.3564 0.2405 -0.0171 0.0430  -0.0182 261 ALA B CA  
4545 C C   . ALA B 262 ? 0.2233 0.3303 0.2062 -0.0125 0.0455  -0.0193 261 ALA B C   
4546 O O   . ALA B 262 ? 0.2505 0.3758 0.2421 -0.0111 0.0485  -0.0215 261 ALA B O   
4547 C CB  . ALA B 262 ? 0.2684 0.3712 0.2487 -0.0276 0.0480  -0.0180 261 ALA B CB  
4548 N N   . GLN B 263 ? 0.2516 0.3445 0.2238 -0.0100 0.0444  -0.0177 262 GLN B N   
4549 C CA  A GLN B 263 ? 0.2849 0.3827 0.2556 -0.0046 0.0460  -0.0186 262 GLN B CA  
4550 C CA  B GLN B 263 ? 0.2849 0.3827 0.2556 -0.0046 0.0460  -0.0186 262 GLN B CA  
4551 C C   . GLN B 263 ? 0.2488 0.3479 0.2264 0.0056  0.0413  -0.0193 262 GLN B C   
4552 O O   . GLN B 263 ? 0.2671 0.3703 0.2443 0.0111  0.0421  -0.0202 262 GLN B O   
4553 C CB  A GLN B 263 ? 0.2939 0.3759 0.2497 -0.0065 0.0471  -0.0167 262 GLN B CB  
4554 C CB  B GLN B 263 ? 0.2943 0.3764 0.2503 -0.0063 0.0470  -0.0167 262 GLN B CB  
4555 C CG  A GLN B 263 ? 0.3556 0.4291 0.3022 -0.0164 0.0500  -0.0151 262 GLN B CG  
4556 C CG  B GLN B 263 ? 0.3358 0.4149 0.2837 -0.0163 0.0516  -0.0158 262 GLN B CG  
4557 C CD  A GLN B 263 ? 0.3116 0.4015 0.2627 -0.0237 0.0558  -0.0167 262 GLN B CD  
4558 C CD  B GLN B 263 ? 0.3924 0.4516 0.3256 -0.0180 0.0508  -0.0133 262 GLN B CD  
4559 O OE1 A GLN B 263 ? 0.3459 0.4499 0.3003 -0.0227 0.0597  -0.0184 262 GLN B OE1 
4560 O OE1 B GLN B 263 ? 0.4858 0.5403 0.4131 -0.0136 0.0508  -0.0131 262 GLN B OE1 
4561 N NE2 A GLN B 263 ? 0.2560 0.3440 0.2073 -0.0311 0.0565  -0.0160 262 GLN B NE2 
4562 N NE2 B GLN B 263 ? 0.4503 0.4974 0.3776 -0.0242 0.0500  -0.0115 262 GLN B NE2 
4563 N N   . ASN B 264 ? 0.2433 0.3392 0.2274 0.0083  0.0365  -0.0190 263 ASN B N   
4564 C CA  . ASN B 264 ? 0.2308 0.3252 0.2207 0.0179  0.0313  -0.0193 263 ASN B CA  
4565 C C   . ASN B 264 ? 0.2495 0.3553 0.2530 0.0198  0.0292  -0.0206 263 ASN B C   
4566 O O   . ASN B 264 ? 0.2690 0.3679 0.2762 0.0247  0.0238  -0.0199 263 ASN B O   
4567 C CB  . ASN B 264 ? 0.2403 0.3128 0.2211 0.0204  0.0263  -0.0167 263 ASN B CB  
4568 C CG  . ASN B 264 ? 0.2581 0.3199 0.2262 0.0203  0.0279  -0.0156 263 ASN B CG  
4569 O OD1 . ASN B 264 ? 0.2996 0.3629 0.2674 0.0268  0.0273  -0.0162 263 ASN B OD1 
4570 N ND2 . ASN B 264 ? 0.2975 0.3486 0.2549 0.0128  0.0300  -0.0139 263 ASN B ND2 
4571 N N   . THR B 265 ? 0.2300 0.3418 0.2633 -0.0022 0.0231  0.0174  264 THR B N   
4572 C CA  . THR B 265 ? 0.2271 0.3386 0.2603 -0.0005 0.0212  0.0169  264 THR B CA  
4573 C C   . THR B 265 ? 0.2290 0.3403 0.2621 0.0067  0.0218  0.0162  264 THR B C   
4574 O O   . THR B 265 ? 0.2438 0.3540 0.2766 0.0086  0.0203  0.0159  264 THR B O   
4575 C CB  . THR B 265 ? 0.2255 0.3483 0.2618 -0.0038 0.0196  0.0175  264 THR B CB  
4576 O OG1 . THR B 265 ? 0.2277 0.3636 0.2680 -0.0018 0.0209  0.0180  264 THR B OG1 
4577 C CG2 . THR B 265 ? 0.2091 0.3300 0.2445 -0.0114 0.0184  0.0182  264 THR B CG2 
4578 N N   . ASP B 266 ? 0.2616 0.3733 0.2945 0.0107  0.0238  0.0160  265 ASP B N   
4579 C CA  . ASP B 266 ? 0.2159 0.3242 0.2475 0.0173  0.0240  0.0154  265 ASP B CA  
4580 C C   . ASP B 266 ? 0.2423 0.3374 0.2700 0.0180  0.0232  0.0154  265 ASP B C   
4581 O O   . ASP B 266 ? 0.2613 0.3533 0.2880 0.0225  0.0225  0.0152  265 ASP B O   
4582 C CB  . ASP B 266 ? 0.3065 0.4164 0.3375 0.0213  0.0262  0.0151  265 ASP B CB  
4583 C CG  . ASP B 266 ? 0.3144 0.4164 0.3427 0.0189  0.0274  0.0153  265 ASP B CG  
4584 O OD1 . ASP B 266 ? 0.3003 0.3997 0.3285 0.0133  0.0271  0.0160  265 ASP B OD1 
4585 O OD2 . ASP B 266 ? 0.4277 0.5257 0.4536 0.0227  0.0287  0.0149  265 ASP B OD2 
4586 N N   . VAL B 267 ? 0.2289 0.3166 0.2547 0.0135  0.0232  0.0160  266 VAL B N   
4587 C CA  . VAL B 267 ? 0.1996 0.2758 0.2220 0.0141  0.0224  0.0164  266 VAL B CA  
4588 C C   . VAL B 267 ? 0.2329 0.3061 0.2546 0.0098  0.0210  0.0166  266 VAL B C   
4589 O O   . VAL B 267 ? 0.2236 0.2902 0.2431 0.0111  0.0201  0.0168  266 VAL B O   
4590 C CB  . VAL B 267 ? 0.2446 0.3122 0.2643 0.0141  0.0237  0.0172  266 VAL B CB  
4591 C CG1 . VAL B 267 ? 0.2404 0.3088 0.2595 0.0189  0.0248  0.0168  266 VAL B CG1 
4592 C CG2 . VAL B 267 ? 0.2244 0.2920 0.2443 0.0087  0.0246  0.0177  266 VAL B CG2 
4593 N N   . TRP B 268 ? 0.1940 0.2712 0.2169 0.0046  0.0208  0.0167  267 TRP B N   
4594 C CA  . TRP B 268 ? 0.1794 0.2518 0.2003 0.0004  0.0193  0.0168  267 TRP B CA  
4595 C C   . TRP B 268 ? 0.1728 0.2520 0.1951 -0.0004 0.0174  0.0162  267 TRP B C   
4596 O O   . TRP B 268 ? 0.2178 0.3072 0.2433 -0.0025 0.0171  0.0162  267 TRP B O   
4597 C CB  . TRP B 268 ? 0.2017 0.2726 0.2222 -0.0053 0.0197  0.0174  267 TRP B CB  
4598 C CG  . TRP B 268 ? 0.2187 0.2811 0.2371 -0.0052 0.0212  0.0182  267 TRP B CG  
4599 C CD1 . TRP B 268 ? 0.2011 0.2651 0.2204 -0.0062 0.0228  0.0188  267 TRP B CD1 
4600 C CD2 . TRP B 268 ? 0.1856 0.2371 0.2006 -0.0040 0.0212  0.0189  267 TRP B CD2 
4601 N NE1 . TRP B 268 ? 0.1634 0.2179 0.1801 -0.0060 0.0237  0.0198  267 TRP B NE1 
4602 C CE2 . TRP B 268 ? 0.1870 0.2341 0.2012 -0.0046 0.0227  0.0200  267 TRP B CE2 
4603 C CE3 . TRP B 268 ? 0.1818 0.2273 0.1943 -0.0024 0.0201  0.0188  267 TRP B CE3 
4604 C CZ2 . TRP B 268 ? 0.2149 0.2523 0.2263 -0.0037 0.0232  0.0213  267 TRP B CZ2 
4605 C CZ3 . TRP B 268 ? 0.2122 0.2482 0.2217 -0.0013 0.0207  0.0200  267 TRP B CZ3 
4606 C CH2 . TRP B 268 ? 0.1912 0.2234 0.2004 -0.0019 0.0222  0.0213  267 TRP B CH2 
4607 N N   . THR B 269 ? 0.1647 0.2386 0.1847 0.0010  0.0161  0.0158  268 THR B N   
4608 C CA  . THR B 269 ? 0.1824 0.2611 0.2028 -0.0001 0.0140  0.0152  268 THR B CA  
4609 C C   . THR B 269 ? 0.2331 0.3092 0.2513 -0.0062 0.0124  0.0151  268 THR B C   
4610 O O   . THR B 269 ? 0.2051 0.2861 0.2235 -0.0083 0.0105  0.0148  268 THR B O   
4611 C CB  . THR B 269 ? 0.1938 0.2678 0.2122 0.0043  0.0132  0.0149  268 THR B CB  
4612 O OG1 . THR B 269 ? 0.2011 0.2636 0.2152 0.0037  0.0132  0.0151  268 THR B OG1 
4613 C CG2 . THR B 269 ? 0.1970 0.2724 0.2170 0.0103  0.0144  0.0151  268 THR B CG2 
4614 N N   . GLY B 270 ? 0.1723 0.2408 0.1880 -0.0092 0.0131  0.0155  269 GLY B N   
4615 C CA  . GLY B 270 ? 0.2069 0.2721 0.2199 -0.0151 0.0115  0.0154  269 GLY B CA  
4616 C C   . GLY B 270 ? 0.1520 0.2044 0.1602 -0.0161 0.0119  0.0156  269 GLY B C   
4617 O O   . GLY B 270 ? 0.1759 0.2233 0.1838 -0.0132 0.0138  0.0163  269 GLY B O   
4618 N N   . ALA B 271 ? 0.1851 0.2319 0.1892 -0.0199 0.0101  0.0151  270 ALA B N   
4619 C CA  . ALA B 271 ? 0.1707 0.2058 0.1702 -0.0216 0.0105  0.0154  270 ALA B CA  
4620 C C   . ALA B 271 ? 0.2688 0.2968 0.2626 -0.0234 0.0083  0.0144  270 ALA B C   
4621 O O   . ALA B 271 ? 0.2070 0.2398 0.2006 -0.0263 0.0060  0.0137  270 ALA B O   
4622 C CB  . ALA B 271 ? 0.1999 0.2358 0.2004 -0.0266 0.0109  0.0163  270 ALA B CB  
4623 N N   . ILE B 272 ? 0.2029 0.2194 0.1918 -0.0218 0.0090  0.0145  271 ILE B N   
4624 C CA  . ILE B 272 ? 0.1893 0.1972 0.1717 -0.0222 0.0073  0.0134  271 ILE B CA  
4625 C C   . ILE B 272 ? 0.2152 0.2118 0.1926 -0.0242 0.0077  0.0138  271 ILE B C   
4626 O O   . ILE B 272 ? 0.2172 0.2088 0.1945 -0.0211 0.0099  0.0150  271 ILE B O   
4627 C CB  . ILE B 272 ? 0.1996 0.2050 0.1805 -0.0162 0.0078  0.0130  271 ILE B CB  
4628 C CG1 . ILE B 272 ? 0.1923 0.2086 0.1784 -0.0135 0.0076  0.0128  271 ILE B CG1 
4629 C CG2 . ILE B 272 ? 0.2191 0.2158 0.1926 -0.0167 0.0060  0.0117  271 ILE B CG2 
4630 C CD1 . ILE B 272 ? 0.1841 0.1982 0.1685 -0.0080 0.0078  0.0126  271 ILE B CD1 
4631 N N   . TRP B 273 ? 0.2100 0.2026 0.1834 -0.0296 0.0055  0.0131  272 TRP B N   
4632 C CA  . TRP B 273 ? 0.1883 0.1698 0.1566 -0.0319 0.0056  0.0135  272 TRP B CA  
4633 C C   . TRP B 273 ? 0.2304 0.2002 0.1922 -0.0274 0.0063  0.0131  272 TRP B C   
4634 O O   . TRP B 273 ? 0.2353 0.2037 0.1940 -0.0249 0.0054  0.0118  272 TRP B O   
4635 C CB  . TRP B 273 ? 0.2308 0.2107 0.1956 -0.0390 0.0025  0.0128  272 TRP B CB  
4636 C CG  . TRP B 273 ? 0.2245 0.1930 0.1838 -0.0419 0.0022  0.0132  272 TRP B CG  
4637 C CD1 . TRP B 273 ? 0.2318 0.1869 0.1824 -0.0418 0.0011  0.0122  272 TRP B CD1 
4638 C CD2 . TRP B 273 ? 0.2396 0.2086 0.2015 -0.0455 0.0030  0.0148  272 TRP B CD2 
4639 N NE1 . TRP B 273 ? 0.2389 0.1861 0.1866 -0.0448 0.0011  0.0131  272 TRP B NE1 
4640 C CE2 . TRP B 273 ? 0.2355 0.1912 0.1901 -0.0473 0.0022  0.0148  272 TRP B CE2 
4641 C CE3 . TRP B 273 ? 0.2670 0.2462 0.2362 -0.0470 0.0043  0.0163  272 TRP B CE3 
4642 C CZ2 . TRP B 273 ? 0.2552 0.2078 0.2101 -0.0509 0.0027  0.0163  272 TRP B CZ2 
4643 C CZ3 . TRP B 273 ? 0.2500 0.2264 0.2194 -0.0507 0.0048  0.0177  272 TRP B CZ3 
4644 C CH2 . TRP B 273 ? 0.2323 0.1956 0.1948 -0.0527 0.0039  0.0178  272 TRP B CH2 
4645 N N   . TRP B 274 ? 0.2155 0.1771 0.1750 -0.0264 0.0080  0.0142  273 TRP B N   
4646 C CA  . TRP B 274 ? 0.2344 0.1840 0.1869 -0.0227 0.0087  0.0140  273 TRP B CA  
4647 C C   . TRP B 274 ? 0.2552 0.1946 0.2011 -0.0272 0.0071  0.0136  273 TRP B C   
4648 O O   . TRP B 274 ? 0.2591 0.1970 0.2065 -0.0298 0.0079  0.0150  273 TRP B O   
4649 C CB  . TRP B 274 ? 0.2301 0.1782 0.1848 -0.0175 0.0119  0.0162  273 TRP B CB  
4650 C CG  . TRP B 274 ? 0.2311 0.1678 0.1787 -0.0134 0.0128  0.0163  273 TRP B CG  
4651 C CD1 . TRP B 274 ? 0.2522 0.1785 0.1946 -0.0140 0.0132  0.0169  273 TRP B CD1 
4652 C CD2 . TRP B 274 ? 0.2419 0.1767 0.1866 -0.0078 0.0133  0.0158  273 TRP B CD2 
4653 N NE1 . TRP B 274 ? 0.2771 0.1951 0.2133 -0.0088 0.0141  0.0168  273 TRP B NE1 
4654 C CE2 . TRP B 274 ? 0.2441 0.1674 0.1817 -0.0051 0.0142  0.0162  273 TRP B CE2 
4655 C CE3 . TRP B 274 ? 0.2235 0.1654 0.1709 -0.0048 0.0131  0.0153  273 TRP B CE3 
4656 C CZ2 . TRP B 274 ? 0.2893 0.2084 0.2223 0.0006  0.0150  0.0159  273 TRP B CZ2 
4657 C CZ3 . TRP B 274 ? 0.2436 0.1811 0.1866 0.0005  0.0138  0.0151  273 TRP B CZ3 
4658 C CH2 . TRP B 274 ? 0.2666 0.1931 0.2025 0.0032  0.0148  0.0154  273 TRP B CH2 
4659 N N   . ALA B 275 ? 0.2370 0.1687 0.1753 -0.0283 0.0048  0.0117  274 ALA B N   
4660 C CA  . ALA B 275 ? 0.2277 0.1599 0.1631 -0.0256 0.0037  0.0099  274 ALA B CA  
4661 C C   . ALA B 275 ? 0.2365 0.1614 0.1639 -0.0304 0.0001  0.0079  274 ALA B C   
4662 O O   . ALA B 275 ? 0.2721 0.1877 0.1941 -0.0340 -0.0010 0.0078  274 ALA B O   
4663 C CB  . ALA B 275 ? 0.2666 0.1924 0.1985 -0.0182 0.0061  0.0102  274 ALA B CB  
4664 N N   . ALA B 276 ? 0.2469 0.1755 0.1731 -0.0306 -0.0019 0.0063  275 ALA B N   
4665 C CA  . ALA B 276 ? 0.2895 0.2095 0.2065 -0.0339 -0.0052 0.0042  275 ALA B CA  
4666 C C   . ALA B 276 ? 0.2907 0.2016 0.2004 -0.0276 -0.0042 0.0029  275 ALA B C   
4667 O O   . ALA B 276 ? 0.2637 0.1754 0.1759 -0.0211 -0.0010 0.0040  275 ALA B O   
4668 C CB  . ALA B 276 ? 0.2862 0.2165 0.2062 -0.0387 -0.0083 0.0035  275 ALA B CB  
4669 N N   . GLY B 277 ? 0.2684 0.1708 0.1688 -0.0295 -0.0071 0.0007  276 GLY B N   
4670 C CA  . GLY B 277 ? 0.2798 0.1722 0.1718 -0.0237 -0.0064 -0.0007 276 GLY B CA  
4671 C C   . GLY B 277 ? 0.3188 0.1948 0.1983 -0.0263 -0.0086 -0.0025 276 GLY B C   
4672 O O   . GLY B 277 ? 0.3523 0.2234 0.2302 -0.0314 -0.0100 -0.0021 276 GLY B O   
4673 N N   . PRO B 278 ? 0.3177 0.1843 0.1876 -0.0227 -0.0092 -0.0045 277 PRO B N   
4674 C CA  . PRO B 278 ? 0.3578 0.2085 0.2147 -0.0259 -0.0121 -0.0066 277 PRO B CA  
4675 C C   . PRO B 278 ? 0.3678 0.2036 0.2170 -0.0219 -0.0101 -0.0066 277 PRO B C   
4676 O O   . PRO B 278 ? 0.4150 0.2368 0.2534 -0.0251 -0.0127 -0.0082 277 PRO B O   
4677 C CB  . PRO B 278 ? 0.3948 0.2428 0.2447 -0.0235 -0.0136 -0.0090 277 PRO B CB  
4678 C CG  . PRO B 278 ? 0.3793 0.2372 0.2365 -0.0163 -0.0101 -0.0078 277 PRO B CG  
4679 C CD  . PRO B 278 ? 0.2986 0.1699 0.1692 -0.0166 -0.0078 -0.0050 277 PRO B CD  
4680 N N   . TRP B 279 ? 0.3639 0.2021 0.2179 -0.0152 -0.0057 -0.0046 278 TRP B N   
4681 C CA  . TRP B 279 ? 0.3757 0.2006 0.2225 -0.0105 -0.0035 -0.0042 278 TRP B CA  
4682 C C   . TRP B 279 ? 0.4644 0.2917 0.3181 -0.0117 -0.0015 -0.0015 278 TRP B C   
4683 O O   . TRP B 279 ? 0.4117 0.2345 0.2646 -0.0059 0.0018  0.0001  278 TRP B O   
4684 C CB  . TRP B 279 ? 0.3519 0.1755 0.1965 -0.0010 0.0000  -0.0040 278 TRP B CB  
4685 C CG  . TRP B 279 ? 0.4077 0.2211 0.2401 0.0014  -0.0016 -0.0070 278 TRP B CG  
4686 C CD1 . TRP B 279 ? 0.4268 0.2326 0.2506 -0.0043 -0.0060 -0.0098 278 TRP B CD1 
4687 C CD2 . TRP B 279 ? 0.3940 0.2038 0.2213 0.0101  0.0011  -0.0073 278 TRP B CD2 
4688 N NE1 . TRP B 279 ? 0.4604 0.2574 0.2735 0.0003  -0.0062 -0.0122 278 TRP B NE1 
4689 C CE2 . TRP B 279 ? 0.4061 0.2057 0.2213 0.0093  -0.0018 -0.0107 278 TRP B CE2 
4690 C CE3 . TRP B 279 ? 0.4583 0.2728 0.2898 0.0182  0.0055  -0.0049 278 TRP B CE3 
4691 C CZ2 . TRP B 279 ? 0.4858 0.2798 0.2930 0.0167  -0.0001 -0.0118 278 TRP B CZ2 
4692 C CZ3 . TRP B 279 ? 0.4640 0.2736 0.2881 0.0254  0.0071  -0.0057 278 TRP B CZ3 
4693 C CH2 . TRP B 279 ? 0.4423 0.2418 0.2544 0.0248  0.0044  -0.0093 278 TRP B CH2 
4694 N N   . TRP B 280 ? 0.3890 0.2239 0.2494 -0.0191 -0.0035 -0.0007 279 TRP B N   
4695 C CA  . TRP B 280 ? 0.3793 0.2170 0.2463 -0.0207 -0.0018 0.0019  279 TRP B CA  
4696 C C   . TRP B 280 ? 0.4095 0.2336 0.2687 -0.0248 -0.0036 0.0016  279 TRP B C   
4697 O O   . TRP B 280 ? 0.4116 0.2343 0.2738 -0.0242 -0.0016 0.0038  279 TRP B O   
4698 C CB  . TRP B 280 ? 0.3472 0.2011 0.2262 -0.0259 -0.0025 0.0032  279 TRP B CB  
4699 C CG  . TRP B 280 ? 0.3219 0.1897 0.2109 -0.0212 0.0004  0.0045  279 TRP B CG  
4700 C CD1 . TRP B 280 ? 0.3121 0.1920 0.2068 -0.0223 -0.0007 0.0039  279 TRP B CD1 
4701 C CD2 . TRP B 280 ? 0.3112 0.1821 0.2053 -0.0150 0.0044  0.0068  279 TRP B CD2 
4702 N NE1 . TRP B 280 ? 0.3380 0.2274 0.2407 -0.0170 0.0025  0.0056  279 TRP B NE1 
4703 C CE2 . TRP B 280 ? 0.3113 0.1956 0.2138 -0.0128 0.0055  0.0075  279 TRP B CE2 
4704 C CE3 . TRP B 280 ? 0.3347 0.1984 0.2269 -0.0112 0.0071  0.0087  279 TRP B CE3 
4705 C CZ2 . TRP B 280 ? 0.3159 0.2060 0.2246 -0.0072 0.0090  0.0099  279 TRP B CZ2 
4706 C CZ3 . TRP B 280 ? 0.3141 0.1846 0.2131 -0.0057 0.0107  0.0113  279 TRP B CZ3 
4707 C CH2 . TRP B 280 ? 0.2897 0.1730 0.1966 -0.0040 0.0114  0.0118  279 TRP B CH2 
4708 N N   . GLY B 281 ? 0.4267 0.2404 0.2759 -0.0293 -0.0076 -0.0008 280 GLY B N   
4709 C CA  . GLY B 281 ? 0.4729 0.2733 0.3145 -0.0340 -0.0098 -0.0010 280 GLY B CA  
4710 C C   . GLY B 281 ? 0.4519 0.2605 0.3024 -0.0403 -0.0102 0.0015  280 GLY B C   
4711 O O   . GLY B 281 ? 0.4700 0.2921 0.3289 -0.0456 -0.0116 0.0021  280 GLY B O   
4712 N N   . ASP B 282 ? 0.4371 0.2381 0.2862 -0.0395 -0.0087 0.0031  281 ASP B N   
4713 C CA  . ASP B 282 ? 0.4246 0.2321 0.2813 -0.0455 -0.0091 0.0055  281 ASP B CA  
4714 C C   . ASP B 282 ? 0.4262 0.2481 0.2957 -0.0420 -0.0049 0.0082  281 ASP B C   
4715 O O   . ASP B 282 ? 0.4224 0.2468 0.2968 -0.0448 -0.0042 0.0105  281 ASP B O   
4716 C CB  . ASP B 282 ? 0.4747 0.2668 0.3234 -0.0473 -0.0100 0.0061  281 ASP B CB  
4717 C CG  . ASP B 282 ? 0.5994 0.3793 0.4371 -0.0543 -0.0153 0.0041  281 ASP B CG  
4718 O OD1 . ASP B 282 ? 0.5165 0.3034 0.3557 -0.0603 -0.0186 0.0031  281 ASP B OD1 
4719 O OD2 . ASP B 282 ? 0.6339 0.3967 0.4610 -0.0539 -0.0163 0.0036  281 ASP B OD2 
4720 N N   . TYR B 283 ? 0.3824 0.2132 0.2568 -0.0362 -0.0025 0.0080  282 TYR B N   
4721 C CA  . TYR B 283 ? 0.3562 0.2004 0.2422 -0.0331 0.0011  0.0104  282 TYR B CA  
4722 C C   . TYR B 283 ? 0.3311 0.1863 0.2260 -0.0398 0.0002  0.0120  282 TYR B C   
4723 O O   . TYR B 283 ? 0.3615 0.2217 0.2575 -0.0463 -0.0030 0.0110  282 TYR B O   
4724 C CB  . TYR B 283 ? 0.3177 0.1717 0.2079 -0.0288 0.0021  0.0096  282 TYR B CB  
4725 C CG  . TYR B 283 ? 0.3466 0.2131 0.2473 -0.0246 0.0056  0.0118  282 TYR B CG  
4726 C CD1 . TYR B 283 ? 0.3553 0.2197 0.2579 -0.0198 0.0090  0.0143  282 TYR B CD1 
4727 C CD2 . TYR B 283 ? 0.2965 0.1767 0.2048 -0.0251 0.0054  0.0115  282 TYR B CD2 
4728 C CE1 . TYR B 283 ? 0.3437 0.2192 0.2553 -0.0162 0.0119  0.0165  282 TYR B CE1 
4729 C CE2 . TYR B 283 ? 0.2812 0.1718 0.1982 -0.0212 0.0084  0.0134  282 TYR B CE2 
4730 C CZ  . TYR B 283 ? 0.2877 0.1758 0.2062 -0.0170 0.0114  0.0159  282 TYR B CZ  
4731 O OH  . TYR B 283 ? 0.3039 0.2017 0.2304 -0.0135 0.0140  0.0179  282 TYR B OH  
4732 N N   . ILE B 284 ? 0.3297 0.1895 0.2313 -0.0383 0.0031  0.0147  283 ILE B N   
4733 C CA  . ILE B 284 ? 0.3127 0.1822 0.2223 -0.0443 0.0026  0.0163  283 ILE B CA  
4734 C C   . ILE B 284 ? 0.3321 0.2172 0.2499 -0.0465 0.0021  0.0159  283 ILE B C   
4735 O O   . ILE B 284 ? 0.3144 0.2075 0.2373 -0.0526 0.0007  0.0167  283 ILE B O   
4736 C CB  . ILE B 284 ? 0.3341 0.2053 0.2489 -0.0415 0.0061  0.0193  283 ILE B CB  
4737 C CG1 . ILE B 284 ? 0.3186 0.1949 0.2375 -0.0337 0.0096  0.0202  283 ILE B CG1 
4738 C CG2 . ILE B 284 ? 0.3762 0.2329 0.2837 -0.0416 0.0060  0.0202  283 ILE B CG2 
4739 C CD1 . ILE B 284 ? 0.3810 0.2617 0.3064 -0.0318 0.0126  0.0234  283 ILE B CD1 
4740 N N   . PHE B 285 ? 0.3019 0.1919 0.2212 -0.0415 0.0031  0.0148  284 PHE B N   
4741 C CA  . PHE B 285 ? 0.2879 0.1927 0.2151 -0.0428 0.0027  0.0145  284 PHE B CA  
4742 C C   . PHE B 285 ? 0.2764 0.1816 0.1996 -0.0442 -0.0002 0.0120  284 PHE B C   
4743 O O   . PHE B 285 ? 0.2853 0.2020 0.2142 -0.0433 -0.0001 0.0117  284 PHE B O   
4744 C CB  . PHE B 285 ? 0.2614 0.1741 0.1953 -0.0364 0.0062  0.0157  284 PHE B CB  
4745 C CG  . PHE B 285 ? 0.2756 0.1892 0.2140 -0.0350 0.0090  0.0183  284 PHE B CG  
4746 C CD1 . PHE B 285 ? 0.3037 0.2196 0.2450 -0.0405 0.0085  0.0196  284 PHE B CD1 
4747 C CD2 . PHE B 285 ? 0.2765 0.1893 0.2161 -0.0283 0.0120  0.0197  284 PHE B CD2 
4748 C CE1 . PHE B 285 ? 0.3324 0.2492 0.2777 -0.0393 0.0111  0.0221  284 PHE B CE1 
4749 C CE2 . PHE B 285 ? 0.2891 0.2029 0.2327 -0.0271 0.0145  0.0223  284 PHE B CE2 
4750 C CZ  . PHE B 285 ? 0.2825 0.1982 0.2289 -0.0327 0.0140  0.0234  284 PHE B CZ  
4751 N N   . SER B 286 ? 0.2788 0.1718 0.1921 -0.0463 -0.0028 0.0104  285 SER B N   
4752 C CA  . SER B 286 ? 0.2676 0.1599 0.1763 -0.0463 -0.0052 0.0081  285 SER B CA  
4753 C C   . SER B 286 ? 0.2991 0.2030 0.2125 -0.0529 -0.0081 0.0079  285 SER B C   
4754 O O   . SER B 286 ? 0.3112 0.2142 0.2233 -0.0601 -0.0109 0.0083  285 SER B O   
4755 C CB  . SER B 286 ? 0.3403 0.2158 0.2363 -0.0469 -0.0074 0.0062  285 SER B CB  
4756 O OG  . SER B 286 ? 0.3363 0.2126 0.2285 -0.0479 -0.0101 0.0041  285 SER B OG  
4757 N N   . MET B 287 ? 0.2831 0.1981 0.2019 -0.0504 -0.0077 0.0074  286 MET B N   
4758 C CA  . MET B 287 ? 0.3095 0.2362 0.2326 -0.0555 -0.0103 0.0073  286 MET B CA  
4759 C C   . MET B 287 ? 0.2982 0.2194 0.2133 -0.0574 -0.0139 0.0052  286 MET B C   
4760 O O   . MET B 287 ? 0.3034 0.2347 0.2218 -0.0608 -0.0161 0.0051  286 MET B O   
4761 C CB  . MET B 287 ? 0.2912 0.2331 0.2246 -0.0514 -0.0078 0.0082  286 MET B CB  
4762 C CG  . MET B 287 ? 0.3002 0.2571 0.2402 -0.0556 -0.0097 0.0085  286 MET B CG  
4763 S SD  . MET B 287 ? 0.3008 0.2639 0.2443 -0.0645 -0.0117 0.0104  286 MET B SD  
4764 C CE  . MET B 287 ? 0.3323 0.2993 0.2832 -0.0608 -0.0072 0.0122  286 MET B CE  
4765 N N   . GLU B 288 ? 0.3015 0.2070 0.2060 -0.0555 -0.0145 0.0036  287 GLU B N   
4766 C CA  . GLU B 288 ? 0.3088 0.2083 0.2050 -0.0566 -0.0176 0.0014  287 GLU B CA  
4767 C C   . GLU B 288 ? 0.3234 0.2203 0.2149 -0.0660 -0.0225 0.0013  287 GLU B C   
4768 O O   . GLU B 288 ? 0.3713 0.2572 0.2569 -0.0696 -0.0238 0.0015  287 GLU B O   
4769 C CB  . GLU B 288 ? 0.3262 0.2094 0.2118 -0.0510 -0.0166 -0.0003 287 GLU B CB  
4770 C CG  . GLU B 288 ? 0.3448 0.2212 0.2210 -0.0511 -0.0195 -0.0029 287 GLU B CG  
4771 C CD  . GLU B 288 ? 0.3429 0.2304 0.2245 -0.0464 -0.0183 -0.0032 287 GLU B CD  
4772 O OE1 . GLU B 288 ? 0.3295 0.2309 0.2224 -0.0442 -0.0158 -0.0015 287 GLU B OE1 
4773 O OE2 . GLU B 288 ? 0.3350 0.2171 0.2092 -0.0450 -0.0199 -0.0052 287 GLU B OE2 
4774 N N   . PRO B 289 ? 0.3073 0.2137 0.2010 -0.0702 -0.0254 0.0011  288 PRO B N   
4775 C CA  . PRO B 289 ? 0.3074 0.2105 0.1954 -0.0794 -0.0306 0.0011  288 PRO B CA  
4776 C C   . PRO B 289 ? 0.4178 0.3010 0.2911 -0.0795 -0.0330 -0.0013 288 PRO B C   
4777 O O   . PRO B 289 ? 0.3888 0.2650 0.2570 -0.0728 -0.0313 -0.0032 288 PRO B O   
4778 C CB  . PRO B 289 ? 0.3811 0.2988 0.2744 -0.0818 -0.0326 0.0014  288 PRO B CB  
4779 C CG  . PRO B 289 ? 0.3799 0.3110 0.2841 -0.0745 -0.0283 0.0021  288 PRO B CG  
4780 C CD  . PRO B 289 ? 0.3055 0.2258 0.2065 -0.0666 -0.0243 0.0011  288 PRO B CD  
4781 N N   . ASP B 290 ? 0.4001 0.2739 0.2659 -0.0873 -0.0370 -0.0012 289 ASP B N   
4782 C CA  . ASP B 290 ? 0.3712 0.2531 0.2421 -0.0959 -0.0395 0.0013  289 ASP B CA  
4783 C C   . ASP B 290 ? 0.4865 0.3608 0.3571 -0.0964 -0.0379 0.0025  289 ASP B C   
4784 O O   . ASP B 290 ? 0.4395 0.3198 0.3144 -0.1032 -0.0394 0.0048  289 ASP B O   
4785 C CB  . ASP B 290 ? 0.3740 0.2502 0.2363 -0.1052 -0.0457 0.0010  289 ASP B CB  
4786 C CG  . ASP B 290 ? 0.5165 0.4022 0.3801 -0.1062 -0.0479 0.0004  289 ASP B CG  
4787 O OD1 . ASP B 290 ? 0.4290 0.3316 0.3038 -0.1027 -0.0453 0.0014  289 ASP B OD1 
4788 O OD2 . ASP B 290 ? 0.5876 0.4638 0.4407 -0.1107 -0.0524 -0.0009 289 ASP B OD2 
4789 N N   . ASN B 291 ? 0.4071 0.2689 0.2727 -0.0893 -0.0347 0.0012  290 ASN B N   
4790 C CA  . ASN B 291 ? 0.4021 0.2533 0.2646 -0.0900 -0.0338 0.0022  290 ASN B CA  
4791 C C   . ASN B 291 ? 0.4723 0.3274 0.3425 -0.0827 -0.0282 0.0033  290 ASN B C   
4792 O O   . ASN B 291 ? 0.4218 0.2683 0.2897 -0.0828 -0.0273 0.0043  290 ASN B O   
4793 C CB  . ASN B 291 ? 0.4965 0.3252 0.3433 -0.0896 -0.0361 -0.0001 290 ASN B CB  
4794 C CG  . ASN B 291 ? 0.5328 0.3559 0.3709 -0.0982 -0.0423 -0.0010 290 ASN B CG  
4795 O OD1 . ASN B 291 ? 0.5490 0.3796 0.3908 -0.1069 -0.0455 0.0009  290 ASN B OD1 
4796 N ND2 . ASN B 291 ? 0.5609 0.3712 0.3874 -0.0958 -0.0439 -0.0039 290 ASN B ND2 
4797 N N   . GLY B 292 ? 0.3526 0.2201 0.2314 -0.0766 -0.0248 0.0035  291 GLY B N   
4798 C CA  . GLY B 292 ? 0.3414 0.2138 0.2280 -0.0708 -0.0199 0.0050  291 GLY B CA  
4799 C C   . GLY B 292 ? 0.3560 0.2365 0.2502 -0.0762 -0.0198 0.0076  291 GLY B C   
4800 O O   . GLY B 292 ? 0.3541 0.2449 0.2527 -0.0830 -0.0224 0.0086  291 GLY B O   
4801 N N   . ILE B 293 ? 0.3118 0.1879 0.2074 -0.0733 -0.0168 0.0089  292 ILE B N   
4802 C CA  . ILE B 293 ? 0.3532 0.2352 0.2548 -0.0787 -0.0169 0.0114  292 ILE B CA  
4803 C C   . ILE B 293 ? 0.3427 0.2445 0.2569 -0.0789 -0.0151 0.0128  292 ILE B C   
4804 O O   . ILE B 293 ? 0.3492 0.2600 0.2684 -0.0854 -0.0166 0.0144  292 ILE B O   
4805 C CB  . ILE B 293 ? 0.3501 0.2226 0.2500 -0.0754 -0.0141 0.0126  292 ILE B CB  
4806 C CG1 . ILE B 293 ? 0.3723 0.2480 0.2759 -0.0824 -0.0152 0.0150  292 ILE B CG1 
4807 C CG2 . ILE B 293 ? 0.3405 0.2191 0.2473 -0.0671 -0.0092 0.0134  292 ILE B CG2 
4808 C CD1 . ILE B 293 ? 0.3385 0.2053 0.2407 -0.0798 -0.0127 0.0165  292 ILE B CD1 
4809 N N   . ALA B 294 ? 0.3159 0.2247 0.2350 -0.0719 -0.0121 0.0122  293 ALA B N   
4810 C CA  . ALA B 294 ? 0.2861 0.2128 0.2162 -0.0718 -0.0106 0.0133  293 ALA B CA  
4811 C C   . ALA B 294 ? 0.3131 0.2488 0.2444 -0.0763 -0.0139 0.0127  293 ALA B C   
4812 O O   . ALA B 294 ? 0.2958 0.2458 0.2350 -0.0796 -0.0141 0.0141  293 ALA B O   
4813 C CB  . ALA B 294 ? 0.2887 0.2197 0.2235 -0.0632 -0.0066 0.0131  293 ALA B CB  
4814 N N   . TYR B 295 ? 0.2978 0.2254 0.2210 -0.0766 -0.0165 0.0107  294 TYR B N   
4815 C CA  . TYR B 295 ? 0.3142 0.2495 0.2377 -0.0816 -0.0201 0.0103  294 TYR B CA  
4816 C C   . TYR B 295 ? 0.3161 0.2545 0.2400 -0.0911 -0.0235 0.0121  294 TYR B C   
4817 O O   . TYR B 295 ? 0.3413 0.2937 0.2711 -0.0954 -0.0251 0.0133  294 TYR B O   
4818 C CB  . TYR B 295 ? 0.3062 0.2301 0.2195 -0.0807 -0.0226 0.0079  294 TYR B CB  
4819 C CG  . TYR B 295 ? 0.3232 0.2553 0.2367 -0.0863 -0.0266 0.0078  294 TYR B CG  
4820 C CD1 . TYR B 295 ? 0.3062 0.2533 0.2275 -0.0837 -0.0256 0.0080  294 TYR B CD1 
4821 C CD2 . TYR B 295 ? 0.3519 0.2767 0.2576 -0.0943 -0.0315 0.0077  294 TYR B CD2 
4822 C CE1 . TYR B 295 ? 0.3252 0.2808 0.2472 -0.0887 -0.0292 0.0082  294 TYR B CE1 
4823 C CE2 . TYR B 295 ? 0.3595 0.2926 0.2656 -0.0998 -0.0353 0.0080  294 TYR B CE2 
4824 C CZ  . TYR B 295 ? 0.3336 0.2826 0.2483 -0.0969 -0.0340 0.0084  294 TYR B CZ  
4825 O OH  . TYR B 295 ? 0.4135 0.3715 0.3290 -0.1024 -0.0378 0.0091  294 TYR B OH  
4826 N N   . GLN B 296 ? 0.3201 0.2461 0.2379 -0.0942 -0.0244 0.0125  295 GLN B N   
4827 C CA  . GLN B 296 ? 0.3322 0.2598 0.2493 -0.1037 -0.0281 0.0143  295 GLN B CA  
4828 C C   . GLN B 296 ? 0.3603 0.2999 0.2871 -0.1057 -0.0260 0.0170  295 GLN B C   
4829 O O   . GLN B 296 ? 0.4130 0.3639 0.3443 -0.1124 -0.0282 0.0189  295 GLN B O   
4830 C CB  . GLN B 296 ? 0.3686 0.2763 0.2737 -0.1070 -0.0308 0.0136  295 GLN B CB  
4831 C CG  . GLN B 296 ? 0.4346 0.3296 0.3290 -0.1054 -0.0332 0.0109  295 GLN B CG  
4832 C CD  . GLN B 296 ? 0.5626 0.4423 0.4452 -0.1127 -0.0382 0.0105  295 GLN B CD  
4833 O OE1 . GLN B 296 ? 0.5319 0.4013 0.4048 -0.1133 -0.0411 0.0084  295 GLN B OE1 
4834 N NE2 . GLN B 296 ? 0.5050 0.3827 0.3880 -0.1185 -0.0394 0.0126  295 GLN B NE2 
4835 N N   . GLN B 297 ? 0.3449 0.2827 0.2750 -0.0999 -0.0217 0.0173  296 GLN B N   
4836 C CA  . GLN B 297 ? 0.3362 0.2831 0.2741 -0.1019 -0.0198 0.0197  296 GLN B CA  
4837 C C   . GLN B 297 ? 0.3139 0.2760 0.2622 -0.0965 -0.0158 0.0202  296 GLN B C   
4838 O O   . GLN B 297 ? 0.3535 0.3270 0.3090 -0.0992 -0.0148 0.0222  296 GLN B O   
4839 C CB  . GLN B 297 ? 0.3122 0.2458 0.2459 -0.1007 -0.0182 0.0203  296 GLN B CB  
4840 C CG  . GLN B 297 ? 0.3664 0.2860 0.2906 -0.1074 -0.0224 0.0204  296 GLN B CG  
4841 C CD  . GLN B 297 ? 0.3458 0.2529 0.2663 -0.1061 -0.0208 0.0213  296 GLN B CD  
4842 O OE1 . GLN B 297 ? 0.4360 0.3263 0.3471 -0.1040 -0.0215 0.0199  296 GLN B OE1 
4843 N NE2 . GLN B 297 ? 0.3199 0.2352 0.2479 -0.1070 -0.0185 0.0235  296 GLN B NE2 
4844 N N   . ILE B 298 ? 0.2931 0.2554 0.2422 -0.0890 -0.0135 0.0186  297 ILE B N   
4845 C CA  . ILE B 298 ? 0.2355 0.2110 0.1937 -0.0837 -0.0099 0.0189  297 ILE B CA  
4846 C C   . ILE B 298 ? 0.3206 0.3096 0.2833 -0.0842 -0.0112 0.0186  297 ILE B C   
4847 O O   . ILE B 298 ? 0.3158 0.3192 0.2867 -0.0837 -0.0096 0.0198  297 ILE B O   
4848 C CB  . ILE B 298 ? 0.2750 0.2433 0.2321 -0.0750 -0.0065 0.0178  297 ILE B CB  
4849 C CG1 . ILE B 298 ? 0.2739 0.2304 0.2275 -0.0741 -0.0049 0.0187  297 ILE B CG1 
4850 C CG2 . ILE B 298 ? 0.3017 0.2830 0.2675 -0.0698 -0.0033 0.0182  297 ILE B CG2 
4851 C CD1 . ILE B 298 ? 0.3119 0.2757 0.2720 -0.0765 -0.0031 0.0209  297 ILE B CD1 
4852 N N   . LEU B 299 ? 0.2922 0.2770 0.2495 -0.0850 -0.0140 0.0171  298 LEU B N   
4853 C CA  . LEU B 299 ? 0.2993 0.2975 0.2610 -0.0857 -0.0154 0.0171  298 LEU B CA  
4854 C C   . LEU B 299 ? 0.3013 0.3142 0.2695 -0.0920 -0.0166 0.0195  298 LEU B C   
4855 O O   . LEU B 299 ? 0.3335 0.3613 0.3094 -0.0897 -0.0152 0.0201  298 LEU B O   
4856 C CB  . LEU B 299 ? 0.3016 0.2921 0.2554 -0.0876 -0.0190 0.0154  298 LEU B CB  
4857 C CG  . LEU B 299 ? 0.3627 0.3664 0.3207 -0.0876 -0.0203 0.0154  298 LEU B CG  
4858 C CD1 . LEU B 299 ? 0.3247 0.3354 0.2888 -0.0790 -0.0165 0.0147  298 LEU B CD1 
4859 C CD2 . LEU B 299 ? 0.4172 0.4125 0.3667 -0.0901 -0.0242 0.0138  298 LEU B CD2 
4860 N N   . PRO B 300 ? 0.3383 0.3484 0.3042 -0.0994 -0.0189 0.0210  299 PRO B N   
4861 C CA  . PRO B 300 ? 0.4132 0.4390 0.3860 -0.1051 -0.0198 0.0237  299 PRO B CA  
4862 C C   . PRO B 300 ? 0.3846 0.4226 0.3666 -0.1008 -0.0156 0.0247  299 PRO B C   
4863 O O   . PRO B 300 ? 0.3739 0.4281 0.3628 -0.1027 -0.0155 0.0264  299 PRO B O   
4864 C CB  . PRO B 300 ? 0.4306 0.4478 0.3982 -0.1131 -0.0227 0.0251  299 PRO B CB  
4865 C CG  . PRO B 300 ? 0.4085 0.4072 0.3652 -0.1133 -0.0251 0.0229  299 PRO B CG  
4866 C CD  . PRO B 300 ? 0.3608 0.3537 0.3172 -0.1035 -0.0214 0.0206  299 PRO B CD  
4867 N N   . ILE B 301 ? 0.3408 0.3717 0.3228 -0.0950 -0.0120 0.0238  300 ILE B N   
4868 C CA  . ILE B 301 ? 0.3562 0.3979 0.3461 -0.0908 -0.0081 0.0247  300 ILE B CA  
4869 C C   . ILE B 301 ? 0.3818 0.4289 0.3752 -0.0828 -0.0057 0.0232  300 ILE B C   
4870 O O   . ILE B 301 ? 0.3401 0.3966 0.3398 -0.0790 -0.0027 0.0237  300 ILE B O   
4871 C CB  . ILE B 301 ? 0.3742 0.4077 0.3634 -0.0895 -0.0055 0.0251  300 ILE B CB  
4872 C CG1 . ILE B 301 ? 0.3569 0.3773 0.3420 -0.0827 -0.0035 0.0233  300 ILE B CG1 
4873 C CG2 . ILE B 301 ? 0.3947 0.4211 0.3796 -0.0972 -0.0081 0.0266  300 ILE B CG2 
4874 C CD1 . ILE B 301 ? 0.3377 0.3525 0.3235 -0.0807 -0.0005 0.0243  300 ILE B CD1 
4875 N N   . LEU B 302 ? 0.2885 0.3299 0.2778 -0.0804 -0.0071 0.0214  301 LEU B N   
4876 C CA  . LEU B 302 ? 0.2759 0.3235 0.2686 -0.0736 -0.0054 0.0203  301 LEU B CA  
4877 C C   . LEU B 302 ? 0.2982 0.3599 0.2949 -0.0758 -0.0074 0.0209  301 LEU B C   
4878 O O   . LEU B 302 ? 0.2979 0.3699 0.3000 -0.0709 -0.0057 0.0208  301 LEU B O   
4879 C CB  . LEU B 302 ? 0.3027 0.3371 0.2891 -0.0691 -0.0055 0.0181  301 LEU B CB  
4880 C CG  . LEU B 302 ? 0.2971 0.3168 0.2787 -0.0667 -0.0038 0.0177  301 LEU B CG  
4881 C CD1 . LEU B 302 ? 0.3213 0.3300 0.2970 -0.0618 -0.0038 0.0158  301 LEU B CD1 
4882 C CD2 . LEU B 302 ? 0.3425 0.3658 0.3295 -0.0625 0.0001  0.0186  301 LEU B CD2 
4883 N N   . THR B 303 ? 0.3584 0.4204 0.3521 -0.0832 -0.0112 0.0218  302 THR B N   
4884 C CA  . THR B 303 ? 0.3827 0.4587 0.3800 -0.0865 -0.0136 0.0230  302 THR B CA  
4885 C C   . THR B 303 ? 0.3413 0.4355 0.3480 -0.0845 -0.0113 0.0247  302 THR B C   
4886 O O   . THR B 303 ? 0.3654 0.4707 0.3758 -0.0825 -0.0118 0.0250  302 THR B O   
4887 C CB  . THR B 303 ? 0.3789 0.4521 0.3718 -0.0962 -0.0180 0.0244  302 THR B CB  
4888 O OG1 . THR B 303 ? 0.4287 0.4877 0.4128 -0.0972 -0.0208 0.0225  302 THR B OG1 
4889 C CG2 . THR B 303 ? 0.5733 0.6641 0.5717 -0.1011 -0.0202 0.0270  302 THR B CG2 
4890 N N   . PRO B 304 ? 0.3468 0.4447 0.3572 -0.0845 -0.0088 0.0259  303 PRO B N   
4891 C CA  . PRO B 304 ? 0.3022 0.4174 0.3209 -0.0818 -0.0064 0.0273  303 PRO B CA  
4892 C C   . PRO B 304 ? 0.3922 0.5111 0.4140 -0.0730 -0.0037 0.0258  303 PRO B C   
4893 O O   . PRO B 304 ? 0.4091 0.5428 0.4371 -0.0706 -0.0024 0.0268  303 PRO B O   
4894 C CB  . PRO B 304 ? 0.3683 0.4824 0.3884 -0.0828 -0.0040 0.0282  303 PRO B CB  
4895 C CG  . PRO B 304 ? 0.3271 0.4290 0.3411 -0.0895 -0.0067 0.0286  303 PRO B CG  
4896 C CD  . PRO B 304 ? 0.3731 0.4613 0.3804 -0.0880 -0.0085 0.0264  303 PRO B CD  
4897 N N   . TYR B 305 ? 0.2887 0.3952 0.3064 -0.0680 -0.0029 0.0235  304 TYR B N   
4898 C CA  . TYR B 305 ? 0.3165 0.4257 0.3369 -0.0597 -0.0005 0.0223  304 TYR B CA  
4899 C C   . TYR B 305 ? 0.3454 0.4565 0.3648 -0.0582 -0.0026 0.0215  304 TYR B C   
4900 O O   . TYR B 305 ? 0.3239 0.4393 0.3460 -0.0518 -0.0010 0.0207  304 TYR B O   
4901 C CB  . TYR B 305 ? 0.2504 0.3461 0.2675 -0.0548 0.0020  0.0207  304 TYR B CB  
4902 C CG  . TYR B 305 ? 0.2568 0.3495 0.2743 -0.0569 0.0037  0.0216  304 TYR B CG  
4903 C CD1 . TYR B 305 ? 0.2837 0.3860 0.3064 -0.0549 0.0063  0.0226  304 TYR B CD1 
4904 C CD2 . TYR B 305 ? 0.2620 0.3424 0.2742 -0.0612 0.0026  0.0217  304 TYR B CD2 
4905 C CE1 . TYR B 305 ? 0.2467 0.3466 0.2696 -0.0572 0.0078  0.0235  304 TYR B CE1 
4906 C CE2 . TYR B 305 ? 0.3307 0.4087 0.3433 -0.0635 0.0040  0.0227  304 TYR B CE2 
4907 C CZ  . TYR B 305 ? 0.2933 0.3813 0.3114 -0.0617 0.0066  0.0237  304 TYR B CZ  
4908 O OH  . TYR B 305 ? 0.2897 0.3753 0.3079 -0.0642 0.0079  0.0248  304 TYR B OH  
4909 N N   . LEU B 306 ? 0.3269 0.4350 0.3423 -0.0642 -0.0063 0.0217  305 LEU B N   
4910 C CA  . LEU B 306 ? 0.3563 0.4635 0.3692 -0.0634 -0.0086 0.0207  305 LEU B CA  
4911 C C   . LEU B 306 ? 0.3589 0.4826 0.3767 -0.0659 -0.0105 0.0226  305 LEU B C   
4912 O O   . LEU B 306 ? 0.3807 0.5067 0.3979 -0.0646 -0.0122 0.0221  305 LEU B O   
4913 C CB  . LEU B 306 ? 0.3041 0.3967 0.3084 -0.0683 -0.0117 0.0197  305 LEU B CB  
4914 C CG  . LEU B 306 ? 0.3433 0.4192 0.3422 -0.0655 -0.0098 0.0181  305 LEU B CG  
4915 C CD1 . LEU B 306 ? 0.3656 0.4271 0.3555 -0.0702 -0.0129 0.0171  305 LEU B CD1 
4916 C CD2 . LEU B 306 ? 0.3338 0.4060 0.3332 -0.0568 -0.0071 0.0165  305 LEU B CD2 
4917 O OXT . LEU B 306 ? 0.3981 0.5338 0.4208 -0.0692 -0.0104 0.0248  305 LEU B OXT 
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